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CRYST1  143.714  143.714  143.714  90.00  90.00  90.00 I 2 3         1
ATOM      1  N   ALA A 694      15.538 216.263  50.657  1.00 50.95           N  
ATOM      2  CA  ALA A 694      14.386 216.765  51.468  1.00 43.81           C  
ATOM      3  C   ALA A 694      13.036 216.837  50.734  1.00 37.00           C  
ATOM      4  O   ALA A 694      12.042 216.989  51.404  1.00 36.14           O  
ATOM      5  CB  ALA A 694      14.722 218.100  52.080  1.00 48.10           C  
ATOM      6  N   MET A 695      12.978 216.706  49.406  1.00 32.42           N  
ATOM      7  CA AMET A 695      11.693 216.695  48.683  0.50 36.73           C  
ATOM      8  CA BMET A 695      11.682 216.737  48.705  0.50 35.93           C  
ATOM      9  C   MET A 695      10.919 215.459  49.073  1.00 36.84           C  
ATOM     10  O   MET A 695      11.504 214.390  49.171  1.00 35.90           O  
ATOM     11  CB AMET A 695      11.889 216.627  47.177  0.50 38.17           C  
ATOM     12  CB BMET A 695      11.849 216.870  47.180  0.50 36.17           C  
ATOM     13  CG AMET A 695      12.440 217.886  46.569  0.50 39.56           C  
ATOM     14  CG BMET A 695      10.594 217.315  46.419  0.50 36.90           C  
ATOM     15  SD AMET A 695      12.243 217.905  44.784  0.50 45.90           S  
ATOM     16  SD BMET A 695      10.744 217.033  44.624  0.50 40.27           S  
ATOM     17  CE AMET A 695      10.450 217.994  44.658  0.50 45.78           C  
ATOM     18  CE BMET A 695      11.129 218.658  43.971  0.50 42.14           C  
ATOM     19  N   GLY A 696       9.622 215.598  49.307  1.00 33.11           N  
ATOM     20  CA  GLY A 696       8.770 214.429  49.624  1.00 33.61           C  
ATOM     21  C   GLY A 696       8.095 213.879  48.365  1.00 33.73           C  
ATOM     22  O   GLY A 696       8.479 214.269  47.219  1.00 32.91           O  
ATOM     23  N   GLU A 697       7.002 213.124  48.562  1.00 47.33           N  
ANISOU   23  N   GLU A 697     5517   8762   3702   -622    629  -1453       N  
ATOM     24  CA  GLU A 697       6.294 212.516  47.438  1.00 44.89           C  
ANISOU   24  CA  GLU A 697     5260   8189   3608   -524    633  -1273       C  
ATOM     25  C   GLU A 697       4.857 212.985  47.385  1.00 39.35           C  
ANISOU   25  C   GLU A 697     4566   7374   3011   -493    751  -1373       C  
ATOM     26  O   GLU A 697       4.221 213.099  48.397  1.00 40.36           O  
ANISOU   26  O   GLU A 697     4655   7684   2994   -523    829  -1457       O  
ATOM     27  CB  GLU A 697       6.307 210.995  47.635  1.00 46.21           C  
ANISOU   27  CB  GLU A 697     5419   8467   3669   -483    586   -977       C  
ATOM     28  CG  GLU A 697       7.689 210.419  47.917  1.00 47.09           C  
ANISOU   28  CG  GLU A 697     5501   8750   3638   -492    479   -846       C  
ATOM     29  CD  GLU A 697       8.493 210.372  46.669  1.00 47.13           C  
ANISOU   29  CD  GLU A 697     5546   8530   3829   -449    405   -782       C  
ATOM     30  OE1 GLU A 697       7.909 210.496  45.575  1.00 44.48           O  
ANISOU   30  OE1 GLU A 697     5268   7915   3715   -404    430   -781       O  
ATOM     31  OE2 GLU A 697       9.722 210.197  46.794  1.00 54.59           O1-
ANISOU   31  OE2 GLU A 697     6454   9600   4685   -458    320   -727       O1-
ATOM     32  N   ALA A 698       4.331 213.173  46.194  1.00 35.81           N  
ANISOU   32  N   ALA A 698     4156   6647   2803   -425    764  -1343       N  
ATOM     33  CA  ALA A 698       2.936 213.627  46.020  1.00 37.07           C  
ANISOU   33  CA  ALA A 698     4304   6700   3081   -375    873  -1416       C  
ATOM     34  C   ALA A 698       2.010 212.403  45.710  1.00 34.92           C  
ANISOU   34  C   ALA A 698     4019   6421   2828   -334    873  -1185       C  
ATOM     35  O   ALA A 698       2.464 211.406  45.114  1.00 31.85           O  
ANISOU   35  O   ALA A 698     3660   5978   2462   -323    789   -985       O  
ATOM     36  CB  ALA A 698       2.883 214.570  44.828  1.00 37.71           C  
ANISOU   36  CB  ALA A 698     4420   6493   3414   -319    885  -1498       C  
ATOM     37  N   PRO A 699       0.721 212.527  45.987  1.00 35.14           N  
ANISOU   37  N   PRO A 699     4002   6476   2871   -310    972  -1223       N  
ATOM     38  CA  PRO A 699      -0.204 211.404  45.712  1.00 35.07           C  
ANISOU   38  CA  PRO A 699     3972   6470   2882   -297    981  -1022       C  
ATOM     39  C   PRO A 699      -0.332 211.101  44.254  1.00 35.33           C  
ANISOU   39  C   PRO A 699     4034   6270   3120   -251    923   -909       C  
ATOM     40  O   PRO A 699      -0.152 211.988  43.419  1.00 34.54           O  
ANISOU   40  O   PRO A 699     3950   5998   3175   -203    909  -1000       O  
ATOM     41  CB  PRO A 699      -1.529 211.848  46.289  1.00 36.90           C  
ANISOU   41  CB  PRO A 699     4131   6788   3099   -281   1107  -1125       C  
ATOM     42  CG  PRO A 699      -1.335 213.217  46.784  1.00 38.80           C  
ANISOU   42  CG  PRO A 699     4368   7040   3334   -271   1174  -1383       C  
ATOM     43  CD  PRO A 699       0.086 213.642  46.678  1.00 36.86           C  
ANISOU   43  CD  PRO A 699     4182   6748   3072   -305   1091  -1455       C  
ATOM     44  N   ASN A 700      -0.556 209.824  43.928  1.00 34.25           N  
ANISOU   44  N   ASN A 700     3909   6125   2979   -273    890   -706       N  
ATOM     45  CA  ASN A 700      -0.839 209.419  42.585  1.00 32.23           C  
ANISOU   45  CA  ASN A 700     3671   5680   2893   -249    845   -607       C  
ATOM     46  C   ASN A 700      -2.345 209.180  42.503  1.00 34.61           C  
ANISOU   46  C   ASN A 700     3898   6014   3238   -255    920   -581       C  
ATOM     47  O   ASN A 700      -2.876 208.189  43.041  1.00 34.29           O  
ANISOU   47  O   ASN A 700     3839   6080   3109   -315    956   -467       O  
ATOM     48  CB  ASN A 700      -0.087 208.144  42.226  1.00 33.44           C  
ANISOU   48  CB  ASN A 700     3892   5786   3026   -280    773   -420       C  
ATOM     49  CG  ASN A 700      -0.304 207.740  40.773  1.00 32.11           C  
ANISOU   49  CG  ASN A 700     3749   5423   3025   -268    728   -346       C  
ATOM     50  ND2 ASN A 700       0.514 206.818  40.272  1.00 31.30           N  
ANISOU   50  ND2 ASN A 700     3719   5236   2937   -279    669   -219       N  
ATOM     51  OD1 ASN A 700      -1.218 208.254  40.106  1.00 32.93           O  
ANISOU   51  OD1 ASN A 700     3803   5469   3240   -245    751   -402       O  
ATOM     52  N   GLN A 701      -3.071 210.098  41.888  1.00 33.67           N  
ANISOU   52  N   GLN A 701     3725   5817   3250   -193    951   -677       N  
ATOM     53  CA  GLN A 701      -4.521 210.001  41.934  1.00 35.06           C  
ANISOU   53  CA  GLN A 701     3801   6068   3453   -192   1028   -666       C  
ATOM     54  C   GLN A 701      -5.083 209.420  40.637  1.00 33.70           C  
ANISOU   54  C   GLN A 701     3603   5792   3407   -202    979   -554       C  
ATOM     55  O   GLN A 701      -6.280 209.550  40.393  1.00 35.51           O  
ANISOU   55  O   GLN A 701     3728   6073   3691   -186   1027   -556       O  
ATOM     56  CB  GLN A 701      -5.176 211.350  42.251  1.00 36.00           C  
ANISOU   56  CB  GLN A 701     3846   6211   3621   -105   1120   -837       C  
ATOM     57  CG  GLN A 701      -4.969 211.837  43.673  1.00 38.91           C  
ANISOU   57  CG  GLN A 701     4215   6730   3838   -120   1200   -973       C  
ATOM     58  CD  GLN A 701      -5.495 213.250  43.867  1.00 39.12           C  
ANISOU   58  CD  GLN A 701     4190   6727   3944    -25   1303  -1165       C  
ATOM     59  NE2 GLN A 701      -6.535 213.358  44.540  1.00 40.32           N  
ANISOU   59  NE2 GLN A 701     4253   7017   4048    -10   1410  -1211       N  
ATOM     60  OE1 GLN A 701      -4.948 214.212  43.337  1.00 42.74           O  
ANISOU   60  OE1 GLN A 701     4693   7023   4522     36   1290  -1261       O  
ATOM     61  N   ALA A 702      -4.269 208.704  39.888  1.00 34.48           N  
ANISOU   61  N   ALA A 702     3787   5777   3536   -236    890   -458       N  
ATOM     62  CA  ALA A 702      -4.743 208.003  38.677  1.00 33.35           C  
ANISOU   62  CA  ALA A 702     3629   5552   3488   -273    844   -363       C  
ATOM     63  C   ALA A 702      -5.914 207.122  39.020  1.00 35.60           C  
ANISOU   63  C   ALA A 702     3839   5954   3731   -363    905   -294       C  
ATOM     64  O   ALA A 702      -6.024 206.629  40.146  1.00 32.98           O  
ANISOU   64  O   ALA A 702     3512   5735   3284   -415    965   -262       O  
ATOM     65  CB  ALA A 702      -3.634 207.195  38.042  1.00 33.28           C  
ANISOU   65  CB  ALA A 702     3735   5416   3493   -309    762   -277       C  
ATOM     66  N   LEU A 703      -6.843 206.990  38.069  1.00 35.34           N  
ANISOU   66  N   LEU A 703     3724   5918   3785   -384    893   -272       N  
ATOM     67  CA  LEU A 703      -8.025 206.159  38.253  1.00 37.30           C  
ANISOU   67  CA  LEU A 703     3883   6281   4006   -490    949   -214       C  
ATOM     68  C   LEU A 703      -7.805 204.869  37.498  1.00 36.03           C  
ANISOU   68  C   LEU A 703     3796   6022   3872   -613    904   -118       C  
ATOM     69  O   LEU A 703      -7.456 204.884  36.335  1.00 38.47           O  
ANISOU   69  O   LEU A 703     4135   6222   4257   -603    828   -121       O  
ATOM     70  CB  LEU A 703      -9.289 206.839  37.733  1.00 39.59           C  
ANISOU   70  CB  LEU A 703     4006   6669   4364   -445    970   -258       C  
ATOM     71  CG  LEU A 703      -9.793 208.095  38.420  1.00 43.00           C  
ANISOU   71  CG  LEU A 703     4344   7197   4796   -317   1045   -356       C  
ATOM     72  CD1 LEU A 703     -11.132 208.481  37.765  1.00 45.37           C  
ANISOU   72  CD1 LEU A 703     4461   7605   5170   -279   1064   -354       C  
ATOM     73  CD2 LEU A 703      -9.992 207.919  39.938  1.00 42.93           C  
ANISOU   73  CD2 LEU A 703     4329   7323   4659   -352   1147   -379       C  
ATOM     74  N   LEU A 704      -7.977 203.744  38.170  1.00 38.00           N  
ANISOU   74  N   LEU A 704     4080   6301   4057   -731    961    -32       N  
ATOM     75  CA  LEU A 704      -7.821 202.435  37.548  1.00 37.39           C  
ANISOU   75  CA  LEU A 704     4084   6105   4017   -859    948     52       C  
ATOM     76  C   LEU A 704      -9.184 201.958  37.129  1.00 37.98           C  
ANISOU   76  C   LEU A 704     4036   6270   4122   -989    985     53       C  
ATOM     77  O   LEU A 704     -10.050 201.751  37.968  1.00 35.69           O  
ANISOU   77  O   LEU A 704     3662   6119   3778  -1050   1070     77       O  
ATOM     78  CB  LEU A 704      -7.251 201.457  38.537  1.00 40.30           C  
ANISOU   78  CB  LEU A 704     4562   6440   4311   -913   1005    164       C  
ATOM     79  CG  LEU A 704      -6.973 200.043  38.018  1.00 41.34           C  
ANISOU   79  CG  LEU A 704     4804   6407   4496  -1034   1019    260       C  
ATOM     80  CD1 LEU A 704      -6.034 200.066  36.849  1.00 39.73           C  
ANISOU   80  CD1 LEU A 704     4690   6031   4372   -987    930    228       C  
ATOM     81  CD2 LEU A 704      -6.401 199.246  39.179  1.00 44.34           C  
ANISOU   81  CD2 LEU A 704     5279   6771   4794  -1046   1088    399       C  
ATOM     82  N   ARG A 705      -9.405 201.813  35.831  1.00 36.80           N  
ANISOU   82  N   ARG A 705     3861   6069   4049  -1036    922     21       N  
ATOM     83  CA  ARG A 705     -10.761 201.476  35.381  1.00 40.30           C  
ANISOU   83  CA  ARG A 705     4155   6643   4510  -1165    946      5       C  
ATOM     84  C   ARG A 705     -10.882 199.963  35.197  1.00 38.73           C  
ANISOU   84  C   ARG A 705     4035   6350   4328  -1374    991     59       C  
ATOM     85  O   ARG A 705      -9.994 199.341  34.626  1.00 38.26           O  
ANISOU   85  O   ARG A 705     4123   6104   4309  -1402    960     73       O  
ATOM     86  CB  ARG A 705     -11.074 202.196  34.066  1.00 43.09           C  
ANISOU   86  CB  ARG A 705     4409   7042   4920  -1112    853    -59       C  
ATOM     87  CG  ARG A 705     -12.580 202.181  33.786  1.00 47.84           C  
ANISOU   87  CG  ARG A 705     4800   7858   5518  -1204    874    -77       C  
ATOM     88  CD  ARG A 705     -12.876 202.773  32.412  1.00 50.89           C  
ANISOU   88  CD  ARG A 705     5080   8311   5942  -1158    774   -116       C  
ATOM     89  NE  ARG A 705     -14.309 202.695  32.092  1.00 52.55           N  
ANISOU   89  NE  ARG A 705     5068   8758   6138  -1253    784   -125       N  
ATOM     90  CZ  ARG A 705     -14.908 203.408  31.139  1.00 57.29           C  
ANISOU   90  CZ  ARG A 705     5504   9513   6751  -1184    712   -137       C  
ATOM     91  NH1 ARG A 705     -14.217 204.287  30.419  1.00 60.86           N1+
ANISOU   91  NH1 ARG A 705     5996   9890   7236  -1015    633   -136       N1+
ATOM     92  NH2 ARG A 705     -16.205 203.254  30.893  1.00 61.57           N  
ANISOU   92  NH2 ARG A 705     5826  10296   7268  -1281    720   -137       N  
ATOM     93  N   ILE A 706     -11.941 199.406  35.732  1.00 40.04           N  
ANISOU   93  N   ILE A 706     4107   6637   4470  -1513   1077     88       N  
ATOM     94  CA  ILE A 706     -12.188 197.983  35.698  1.00 42.91           C  
ANISOU   94  CA  ILE A 706     4538   6906   4857  -1730   1149    139       C  
ATOM     95  C   ILE A 706     -13.216 197.754  34.597  1.00 43.76           C  
ANISOU   95  C   ILE A 706     4508   7115   5004  -1886   1117     58       C  
ATOM     96  O   ILE A 706     -14.341 198.206  34.737  1.00 43.74           O  
ANISOU   96  O   ILE A 706     4308   7338   4972  -1909   1131     33       O  
ATOM     97  CB  ILE A 706     -12.814 197.457  36.998  1.00 45.50           C  
ANISOU   97  CB  ILE A 706     4834   7324   5130  -1818   1276    228       C  
ATOM     98  CG1 ILE A 706     -11.969 197.776  38.238  1.00 46.00           C  
ANISOU   98  CG1 ILE A 706     4991   7368   5115  -1667   1310    309       C  
ATOM     99  CG2 ILE A 706     -13.080 195.956  36.886  1.00 48.05           C  
ANISOU   99  CG2 ILE A 706     5238   7516   5503  -2057   1365    286       C  
ATOM    100  CD1 ILE A 706     -10.518 197.460  38.112  1.00 45.87           C  
ANISOU  100  CD1 ILE A 706     5176   7132   5121  -1584   1269    359       C  
ATOM    101  N   LEU A 707     -12.834 197.056  33.535  1.00 41.90           N  
ANISOU  101  N   LEU A 707     4366   6730   4823  -1992   1079     15       N  
ATOM    102  CA  LEU A 707     -13.752 196.767  32.440  1.00 45.55           C  
ANISOU  102  CA  LEU A 707     4699   7306   5302  -2166   1043    -75       C  
ATOM    103  C   LEU A 707     -14.389 195.408  32.599  1.00 48.59           C  
ANISOU  103  C   LEU A 707     5105   7640   5714  -2445   1153    -68       C  
ATOM    104  O   LEU A 707     -13.726 194.473  32.995  1.00 49.61           O  
ANISOU  104  O   LEU A 707     5426   7535   5887  -2505   1234     -8       O  
ATOM    105  CB  LEU A 707     -12.985 196.822  31.129  1.00 45.86           C  
ANISOU  105  CB  LEU A 707     4822   7229   5370  -2135    943   -149       C  
ATOM    106  CG  LEU A 707     -12.234 198.131  30.947  1.00 47.53           C  
ANISOU  106  CG  LEU A 707     5035   7454   5568  -1868    845   -145       C  
ATOM    107  CD1 LEU A 707     -11.630 198.139  29.571  1.00 48.87           C  
ANISOU  107  CD1 LEU A 707     5263   7547   5756  -1864    752   -215       C  
ATOM    108  CD2 LEU A 707     -13.137 199.347  31.156  1.00 48.81           C  
ANISOU  108  CD2 LEU A 707     4976   7875   5693  -1745    811   -146       C  
ATOM    109  N   LYS A 708     -15.675 195.312  32.301  1.00 51.25           N  
ANISOU  109  N   LYS A 708     5241   8199   6031  -2611   1160   -123       N  
ATOM    110  CA  LYS A 708     -16.390 194.037  32.264  1.00 56.68           C  
ANISOU  110  CA  LYS A 708     5927   8855   6752  -2919   1262   -146       C  
ATOM    111  C   LYS A 708     -16.042 193.268  31.009  1.00 57.75           C  
ANISOU  111  C   LYS A 708     6167   8837   6936  -3082   1230   -260       C  
ATOM    112  O   LYS A 708     -15.934 193.863  29.936  1.00 53.61           O  
ANISOU  112  O   LYS A 708     5576   8409   6383  -3018   1105   -348       O  
ATOM    113  CB  LYS A 708     -17.885 194.284  32.274  1.00 61.82           C  
ANISOU  113  CB  LYS A 708     6297   9835   7355  -3046   1267   -181       C  
ATOM    114  CG  LYS A 708     -18.344 195.061  33.482  1.00 65.82           C  
ANISOU  114  CG  LYS A 708     6680  10517   7809  -2890   1312    -87       C  
ATOM    115  CD  LYS A 708     -19.804 195.460  33.399  1.00 71.23           C  
ANISOU  115  CD  LYS A 708     7060  11556   8447  -2972   1308   -122       C  
ATOM    116  CE  LYS A 708     -20.079 196.528  34.455  1.00 74.36           C  
ANISOU  116  CE  LYS A 708     7341  12118   8793  -2740   1337    -51       C  
ATOM    117  NZ  LYS A 708     -21.526 196.594  34.819  1.00 79.18           N1+
ANISOU  117  NZ  LYS A 708     7677  13043   9363  -2851   1398    -48       N1+
ATOM    118  N   GLU A 709     -15.878 191.952  31.118  1.00 63.63           N  
ANISOU  118  N   GLU A 709     7074   9345   7754  -3292   1350   -259       N  
ATOM    119  CA  GLU A 709     -15.532 191.144  29.934  1.00 69.42           C  
ANISOU  119  CA  GLU A 709     7925   9908   8541  -3463   1343   -392       C  
ATOM    120  C   GLU A 709     -16.617 191.215  28.842  1.00 66.61           C  
ANISOU  120  C   GLU A 709     7350   9829   8130  -3669   1267   -553       C  
ATOM    121  O   GLU A 709     -16.307 191.174  27.659  1.00 67.41           O  
ANISOU  121  O   GLU A 709     7477   9917   8217  -3711   1188   -680       O  
ATOM    122  CB  GLU A 709     -15.193 189.674  30.268  1.00 76.31           C  
ANISOU  122  CB  GLU A 709     9023  10445   9526  -3656   1512   -365       C  
ATOM    123  CG  GLU A 709     -14.669 188.926  29.019  1.00 83.38           C  
ANISOU  123  CG  GLU A 709    10063  11134  10481  -3794   1512   -524       C  
ATOM    124  CD  GLU A 709     -13.537 187.930  29.272  1.00 85.54           C  
ANISOU  124  CD  GLU A 709    10636  10985  10877  -3769   1640   -459       C  
ATOM    125  OE1 GLU A 709     -12.407 188.167  28.757  1.00 86.63           O  
ANISOU  125  OE1 GLU A 709    10907  10980  11028  -3584   1580   -474       O  
ATOM    126  OE2 GLU A 709     -13.783 186.910  29.963  1.00 85.08           O1-
ANISOU  126  OE2 GLU A 709    10676  10742  10907  -3931   1807   -385       O1-
ATOM    127  N   THR A 710     -17.864 191.393  29.244  1.00 65.20           N  
ANISOU  127  N   THR A 710     6940   9927   7904  -3781   1284   -541       N  
ATOM    128  CA  THR A 710     -18.950 191.560  28.288  1.00 66.31           C  
ANISOU  128  CA  THR A 710     6829  10391   7972  -3958   1201   -672       C  
ATOM    129  C   THR A 710     -18.818 192.795  27.367  1.00 64.25           C  
ANISOU  129  C   THR A 710     6429  10356   7625  -3738   1018   -705       C  
ATOM    130  O   THR A 710     -19.439 192.817  26.316  1.00 62.15           O  
ANISOU  130  O   THR A 710     6000  10322   7292  -3880    934   -822       O  
ATOM    131  CB  THR A 710     -20.315 191.610  29.002  1.00 68.34           C  
ANISOU  131  CB  THR A 710     6838  10932   8194  -4087   1257   -629       C  
ATOM    132  CG2 THR A 710     -20.657 190.253  29.600  1.00 72.19           C  
ANISOU  132  CG2 THR A 710     7430  11236   8762  -4392   1437   -627       C  
ATOM    133  OG1 THR A 710     -20.284 192.614  30.026  1.00 68.16           O  
ANISOU  133  OG1 THR A 710     6750  11003   8144  -3800   1251   -483       O  
ATOM    134  N   GLU A 711     -18.014 193.802  27.746  1.00 60.48           N  
ANISOU  134  N   GLU A 711     6015   9817   7146  -3403    962   -601       N  
ATOM    135  CA  GLU A 711     -17.934 195.051  26.998  1.00 60.36           C  
ANISOU  135  CA  GLU A 711     5865  10004   7064  -3178    810   -602       C  
ATOM    136  C   GLU A 711     -17.009 194.962  25.792  1.00 61.39           C  
ANISOU  136  C   GLU A 711     6133  10005   7187  -3159    726   -689       C  
ATOM    137  O   GLU A 711     -17.004 195.871  24.965  1.00 59.89           O  
ANISOU  137  O   GLU A 711     5825   9997   6932  -3017    600   -695       O  
ATOM    138  CB  GLU A 711     -17.351 196.175  27.852  1.00 61.32           C  
ANISOU  138  CB  GLU A 711     6021  10077   7199  -2840    796   -473       C  
ATOM    139  CG  GLU A 711     -18.151 196.740  29.015  1.00 62.68           C  
ANISOU  139  CG  GLU A 711     6035  10422   7358  -2750    855   -382       C  
ATOM    140  CD  GLU A 711     -17.314 197.812  29.726  1.00 61.95           C  
ANISOU  140  CD  GLU A 711     6028  10227   7280  -2425    841   -294       C  
ATOM    141  OE1 GLU A 711     -16.843 197.624  30.874  1.00 61.91           O  
ANISOU  141  OE1 GLU A 711     6159  10065   7298  -2370    932   -225       O  
ATOM    142  OE2 GLU A 711     -17.051 198.846  29.105  1.00 60.84           O1-
ANISOU  142  OE2 GLU A 711     5831  10158   7126  -2226    738   -293       O1-
ATOM    143  N   PHE A 712     -16.165 193.940  25.694  1.00 61.90           N  
ANISOU  143  N   PHE A 712     6450   9751   7318  -3272    802   -741       N  
ATOM    144  CA  PHE A 712     -15.209 193.913  24.589  1.00 62.71           C  
ANISOU  144  CA  PHE A 712     6687   9728   7410  -3227    732   -823       C  
ATOM    145  C   PHE A 712     -15.160 192.533  23.950  1.00 69.07           C  
ANISOU  145  C   PHE A 712     7624  10369   8249  -3533    811   -977       C  
ATOM    146  O   PHE A 712     -15.385 191.525  24.626  1.00 72.76           O  
ANISOU  146  O   PHE A 712     8185  10665   8796  -3717    951   -978       O  
ATOM    147  CB  PHE A 712     -13.804 194.461  24.994  1.00 63.10           C  
ANISOU  147  CB  PHE A 712     6935   9529   7509  -2930    721   -720       C  
ATOM    148  CG  PHE A 712     -13.173 193.726  26.118  1.00 61.18           C  
ANISOU  148  CG  PHE A 712     6900   8982   7360  -2921    855   -638       C  
ATOM    149  CD1 PHE A 712     -13.491 194.044  27.411  1.00 61.44           C  
ANISOU  149  CD1 PHE A 712     6886   9054   7404  -2831    910   -513       C  
ATOM    150  CD2 PHE A 712     -12.278 192.694  25.875  1.00 65.39           C  
ANISOU  150  CD2 PHE A 712     7673   9203   7968  -3002    935   -682       C  
ATOM    151  CE1 PHE A 712     -12.931 193.341  28.451  1.00 63.95           C  
ANISOU  151  CE1 PHE A 712     7385   9123   7790  -2825   1032   -418       C  
ATOM    152  CE2 PHE A 712     -11.703 191.974  26.911  1.00 63.87           C  
ANISOU  152  CE2 PHE A 712     7665   8736   7864  -2982   1064   -579       C  
ATOM    153  CZ  PHE A 712     -12.029 192.298  28.202  1.00 65.25           C  
ANISOU  153  CZ  PHE A 712     7784   8972   8033  -2896   1108   -439       C  
ATOM    154  N   LYS A 713     -14.974 192.521  22.625  1.00 67.47           N  
ANISOU  154  N   LYS A 713     7407  10247   7979  -3600    726  -1111       N  
ATOM    155  CA  LYS A 713     -14.951 191.306  21.821  1.00 71.66           C  
ANISOU  155  CA  LYS A 713     8049  10654   8524  -3898    793  -1301       C  
ATOM    156  C   LYS A 713     -13.527 191.112  21.312  1.00 71.80           C  
ANISOU  156  C   LYS A 713     8319  10375   8586  -3769    804  -1334       C  
ATOM    157  O   LYS A 713     -12.939 192.036  20.725  1.00 71.12           O  
ANISOU  157  O   LYS A 713     8207  10382   8434  -3549    684  -1300       O  
ATOM    158  CB  LYS A 713     -15.937 191.420  20.648  1.00 71.13           C  
ANISOU  158  CB  LYS A 713     7740  10970   8313  -4103    686  -1452       C  
ATOM    159  N   LYS A 714     -12.943 189.941  21.564  1.00 71.85           N  
ANISOU  159  N   LYS A 714     8569  10017   8713  -3887    957  -1383       N  
ATOM    160  CA  LYS A 714     -11.689 189.573  20.900  1.00 71.03           C  
ANISOU  160  CA  LYS A 714     8691   9647   8650  -3813    985  -1453       C  
ATOM    161  C   LYS A 714     -11.971 189.344  19.424  1.00 72.12           C  
ANISOU  161  C   LYS A 714     8763   9958   8678  -4017    924  -1681       C  
ATOM    162  O   LYS A 714     -13.115 189.132  19.048  1.00 73.87           O  
ANISOU  162  O   LYS A 714     8806  10435   8822  -4271    900  -1796       O  
ATOM    163  CB  LYS A 714     -11.078 188.333  21.522  1.00 73.37           C  
ANISOU  163  CB  LYS A 714     9252   9512   9111  -3888   1179  -1443       C  
ATOM    164  CG  LYS A 714     -10.049 188.642  22.577  1.00 75.18           C  
ANISOU  164  CG  LYS A 714     9622   9517   9426  -3584   1212  -1224       C  
ATOM    165  CD  LYS A 714      -9.565 187.388  23.291  1.00 79.22           C  
ANISOU  165  CD  LYS A 714    10371   9626  10101  -3650   1413  -1173       C  
ATOM    166  CE  LYS A 714     -10.133 187.233  24.696  1.00 80.24           C  
ANISOU  166  CE  LYS A 714    10468   9738  10281  -3661   1494   -996       C  
ATOM    167  NZ  LYS A 714      -9.014 187.009  25.660  1.00 78.55           N1+
ANISOU  167  NZ  LYS A 714    10446   9234  10164  -3429   1579   -797       N1+
ATOM    168  N   ILE A 715     -10.944 189.423  18.593  1.00 69.59           N  
ANISOU  168  N   ILE A 715     8571   9532   8336  -3906    895  -1745       N  
ATOM    169  CA  ILE A 715     -11.103 189.179  17.156  1.00 75.30           C  
ANISOU  169  CA  ILE A 715     9248  10423   8938  -4095    844  -1971       C  
ATOM    170  C   ILE A 715     -10.057 188.229  16.625  1.00 75.01           C  
ANISOU  170  C   ILE A 715     9480  10037   8980  -4145    969  -2113       C  
ATOM    171  O   ILE A 715     -10.387 187.298  15.915  1.00 78.14           O  
ANISOU  171  O   ILE A 715     9922  10403   9363  -4439   1046  -2345       O  
ATOM    172  CB  ILE A 715     -11.010 190.455  16.278  1.00 75.07           C  
ANISOU  172  CB  ILE A 715     9044  10739   8738  -3909    649  -1931       C  
ATOM    173  CG1 ILE A 715     -11.839 191.614  16.855  1.00 73.28           C  
ANISOU  173  CG1 ILE A 715     8566  10823   8454  -3761    528  -1747       C  
ATOM    174  CG2 ILE A 715     -11.444 190.128  14.844  1.00 78.24           C  
ANISOU  174  CG2 ILE A 715     9355  11392   8980  -4159    595  -2169       C  
ATOM    175  CD1 ILE A 715     -13.327 191.352  17.020  1.00 75.40           C  
ANISOU  175  CD1 ILE A 715     8613  11363   8670  -4017    521  -1803       C  
ATOM    176  N   LYS A 716      -8.801 188.502  16.938  1.00 72.66           N  
ANISOU  176  N   LYS A 716     9348   9496   8762  -3859    989  -1984       N  
ATOM    177  CA  LYS A 716      -7.713 187.708  16.437  1.00 74.89           C  
ANISOU  177  CA  LYS A 716     9873   9457   9122  -3853   1106  -2096       C  
ATOM    178  C   LYS A 716      -6.539 187.841  17.390  1.00 73.41           C  
ANISOU  178  C   LYS A 716     9853   8963   9073  -3547   1165  -1881       C  
ATOM    179  O   LYS A 716      -6.441 188.806  18.148  1.00 71.78           O  
ANISOU  179  O   LYS A 716     9558   8861   8854  -3319   1072  -1674       O  
ATOM    180  CB  LYS A 716      -7.330 188.184  15.031  1.00 75.34           C  
ANISOU  180  CB  LYS A 716     9880   9724   9019  -3830    997  -2232       C  
ATOM    181  N   VAL A 717      -5.643 186.869  17.349  1.00 73.82           N  
ANISOU  181  N   VAL A 717    10145   8646   9255  -3543   1324  -1936       N  
ATOM    182  CA  VAL A 717      -4.412 186.919  18.126  1.00 72.69           C  
ANISOU  182  CA  VAL A 717    10157   8227   9232  -3250   1381  -1741       C  
ATOM    183  C   VAL A 717      -3.396 187.749  17.369  1.00 71.09           C  
ANISOU  183  C   VAL A 717     9948   8117   8944  -3023   1273  -1732       C  
ATOM    184  O   VAL A 717      -3.437 187.800  16.150  1.00 74.15           O  
ANISOU  184  O   VAL A 717    10301   8649   9222  -3125   1227  -1917       O  
ATOM    185  CB  VAL A 717      -3.859 185.496  18.360  1.00 75.05           C  
ANISOU  185  CB  VAL A 717    10711   8084   9718  -3323   1612  -1789       C  
ATOM    186  CG1 VAL A 717      -2.548 185.530  19.135  1.00 72.50           C  
ANISOU  186  CG1 VAL A 717    10530   7506   9508  -3004   1666  -1571       C  
ATOM    187  CG2 VAL A 717      -4.895 184.646  19.075  1.00 76.29           C  
ANISOU  187  CG2 VAL A 717    10878   8138   9967  -3571   1734  -1795       C  
ATOM    188  N   LEU A 718      -2.508 188.416  18.101  1.00 71.26           N  
ANISOU  188  N   LEU A 718     9993   8077   9003  -2727   1231  -1518       N  
ATOM    189  CA  LEU A 718      -1.405 189.185  17.534  1.00 72.73           C  
ANISOU  189  CA  LEU A 718    10186   8313   9133  -2496   1147  -1481       C  
ATOM    190  C   LEU A 718      -0.012 188.616  17.921  1.00 80.88           C  
ANISOU  190  C   LEU A 718    11420   9007  10302  -2303   1271  -1394       C  
ATOM    191  O   LEU A 718       1.004 189.036  17.358  1.00 90.15           O  
ANISOU  191  O   LEU A 718    12622  10184  11444  -2135   1233  -1389       O  
ATOM    192  CB  LEU A 718      -1.500 190.661  17.981  1.00 67.87           C  
ANISOU  192  CB  LEU A 718     9396   7960   8430  -2303    974  -1308       C  
ATOM    193  CG  LEU A 718      -2.668 191.536  17.500  1.00 66.08           C  
ANISOU  193  CG  LEU A 718     8943   8105   8057  -2401    827  -1350       C  
ATOM    194  CD1 LEU A 718      -2.857 192.756  18.393  1.00 62.38           C  
ANISOU  194  CD1 LEU A 718     8339   7791   7569  -2212    718  -1155       C  
ATOM    195  CD2 LEU A 718      -2.427 191.985  16.068  1.00 66.51           C  
ANISOU  195  CD2 LEU A 718     8944   8347   7979  -2409    739  -1471       C  
ATOM    196  N   GLY A 719       0.051 187.708  18.901  1.00 85.90           N  
ANISOU  196  N   GLY A 719    12181   9369  11085  -2312   1416  -1303       N  
ATOM    197  CA  GLY A 719       1.306 187.009  19.242  1.00 89.35           C  
ANISOU  197  CA  GLY A 719    12806   9479  11662  -2136   1554  -1213       C  
ATOM    198  C   GLY A 719       1.228 186.322  20.600  1.00 90.29           C  
ANISOU  198  C   GLY A 719    13009   9377  11918  -2106   1674  -1028       C  
ATOM    199  O   GLY A 719       0.987 186.993  21.591  1.00 84.89           O  
ANISOU  199  O   GLY A 719    12224   8832  11198  -2011   1589   -851       O  
ATOM    200  N   SER A 720       1.417 184.992  20.644  1.00 94.17           N  
ANISOU  200  N   SER A 720    13686   9527  12565  -2186   1879  -1068       N  
ATOM    201  CA  SER A 720       1.297 184.187  21.886  1.00 90.03           C  
ANISOU  201  CA  SER A 720    13258   8766  12182  -2174   2022   -880       C  
ATOM    202  C   SER A 720       2.660 183.819  22.472  1.00 87.73           C  
ANISOU  202  C   SER A 720    13097   8231  12004  -1887   2115   -676       C  
ATOM    203  O   SER A 720       3.564 184.655  22.527  1.00 84.46           O  
ANISOU  203  O   SER A 720    12619   7950  11521  -1648   1999   -576       O  
ATOM    204  CB  SER A 720       0.496 182.910  21.630  1.00 90.03           C  
ANISOU  204  CB  SER A 720    13380   8528  12300  -2470   2209  -1038       C  
ATOM    205  N   GLY A 724       2.637 185.406  28.263  1.00 95.02           N  
ANISOU  205  N   GLY A 724    13736   9587  12778  -1341   1934    393       N  
ATOM    206  CA  GLY A 724       2.270 186.564  27.461  1.00 94.06           C  
ANISOU  206  CA  GLY A 724    13469   9739  12528  -1395   1756    203       C  
ATOM    207  C   GLY A 724       1.615 186.206  26.130  1.00 94.04           C  
ANISOU  207  C   GLY A 724    13493   9683  12553  -1627   1784    -65       C  
ATOM    208  O   GLY A 724       2.282 185.680  25.235  1.00 99.03           O  
ANISOU  208  O   GLY A 724    14237  10131  13255  -1608   1854   -171       O  
ATOM    209  N   THR A 725       0.304 186.470  26.018  1.00 89.24           N  
ANISOU  209  N   THR A 725    12775   9251  11881  -1846   1735   -176       N  
ATOM    210  CA  THR A 725      -0.418 186.552  24.719  1.00 82.04           C  
ANISOU  210  CA  THR A 725    11809   8436  10923  -2061   1691   -441       C  
ATOM    211  C   THR A 725      -1.159 187.933  24.542  1.00 74.21           C  
ANISOU  211  C   THR A 725    10596   7832   9769  -2073   1491   -491       C  
ATOM    212  O   THR A 725      -1.670 188.503  25.515  1.00 65.98           O  
ANISOU  212  O   THR A 725     9445   6950   8675  -2036   1437   -366       O  
ATOM    213  CB  THR A 725      -1.364 185.342  24.496  1.00 84.55           C  
ANISOU  213  CB  THR A 725    12209   8578  11337  -2360   1850   -565       C  
ATOM    214  CG2 THR A 725      -2.250 185.099  25.684  1.00 89.91           C  
ANISOU  214  CG2 THR A 725    12844   9281  12036  -2454   1905   -421       C  
ATOM    215  OG1 THR A 725      -2.186 185.560  23.342  1.00 84.67           O  
ANISOU  215  OG1 THR A 725    12128   8774  11268  -2582   1778   -817       O  
ATOM    216  N   VAL A 726      -1.170 188.466  23.312  1.00 65.32           N  
ANISOU  216  N   VAL A 726     9404   6851   8563  -2110   1391   -665       N  
ATOM    217  CA  VAL A 726      -1.781 189.772  22.992  1.00 58.80           C  
ANISOU  217  CA  VAL A 726     8375   6371   7595  -2097   1211   -702       C  
ATOM    218  C   VAL A 726      -2.790 189.600  21.872  1.00 58.36           C  
ANISOU  218  C   VAL A 726     8237   6460   7475  -2349   1185   -917       C  
ATOM    219  O   VAL A 726      -2.478 189.012  20.832  1.00 61.65           O  
ANISOU  219  O   VAL A 726     8742   6777   7903  -2442   1233  -1077       O  
ATOM    220  CB  VAL A 726      -0.728 190.824  22.581  1.00 58.16           C  
ANISOU  220  CB  VAL A 726     8264   6381   7453  -1860   1091   -665       C  
ATOM    221  CG1 VAL A 726      -1.373 192.158  22.181  1.00 54.82           C  
ANISOU  221  CG1 VAL A 726     7642   6285   6901  -1841    924   -695       C  
ATOM    222  CG2 VAL A 726       0.264 191.060  23.713  1.00 57.63           C  
ANISOU  222  CG2 VAL A 726     8252   6216   7428  -1624   1103   -461       C  
ATOM    223  N   TYR A 727      -4.009 190.077  22.097  1.00 55.39           N  
ANISOU  223  N   TYR A 727     7686   6331   7026  -2464   1115   -924       N  
ATOM    224  CA  TYR A 727      -5.113 189.947  21.138  1.00 56.53           C  
ANISOU  224  CA  TYR A 727     7711   6675   7092  -2716   1077  -1112       C  
ATOM    225  C   TYR A 727      -5.532 191.316  20.621  1.00 55.66           C  
ANISOU  225  C   TYR A 727     7388   6920   6838  -2628    893  -1108       C  
ATOM    226  O   TYR A 727      -5.436 192.318  21.324  1.00 48.16           O  
ANISOU  226  O   TYR A 727     6353   6076   5868  -2431    816   -957       O  
ATOM    227  CB  TYR A 727      -6.345 189.345  21.782  1.00 60.52           C  
ANISOU  227  CB  TYR A 727     8153   7213   7627  -2944   1152  -1119       C  
ATOM    228  CG  TYR A 727      -6.161 187.995  22.453  1.00 67.92           C  
ANISOU  228  CG  TYR A 727     9285   7802   8718  -3052   1350  -1091       C  
ATOM    229  CD1 TYR A 727      -5.625 187.902  23.743  1.00 70.31           C  
ANISOU  229  CD1 TYR A 727     9676   7934   9103  -2877   1419   -873       C  
ATOM    230  CD2 TYR A 727      -6.561 186.815  21.815  1.00 74.31           C  
ANISOU  230  CD2 TYR A 727    10186   8461   9587  -3336   1476  -1278       C  
ATOM    231  CE1 TYR A 727      -5.473 186.671  24.369  1.00 76.79           C  
ANISOU  231  CE1 TYR A 727    10671   8437  10066  -2961   1607   -813       C  
ATOM    232  CE2 TYR A 727      -6.422 185.571  22.433  1.00 79.54           C  
ANISOU  232  CE2 TYR A 727    11035   8775  10411  -3435   1677  -1240       C  
ATOM    233  CZ  TYR A 727      -5.872 185.503  23.709  1.00 80.74           C  
ANISOU  233  CZ  TYR A 727    11272   8755  10647  -3236   1743   -992       C  
ATOM    234  OH  TYR A 727      -5.719 184.289  24.345  1.00 83.97           O  
ANISOU  234  OH  TYR A 727    11865   8820  11219  -3311   1947   -918       O  
ATOM    235  N   LYS A 728      -6.038 191.347  19.405  1.00 54.79           N  
ANISOU  235  N   LYS A 728     7187   7002   6629  -2781    831  -1274       N  
ATOM    236  CA  LYS A 728      -6.695 192.528  18.911  1.00 55.48           C  
ANISOU  236  CA  LYS A 728     7048   7450   6581  -2731    670  -1257       C  
ATOM    237  C   LYS A 728      -8.179 192.323  19.212  1.00 51.90           C  
ANISOU  237  C   LYS A 728     6424   7199   6094  -2946    671  -1293       C  
ATOM    238  O   LYS A 728      -8.649 191.202  19.192  1.00 54.69           O  
ANISOU  238  O   LYS A 728     6836   7450   6491  -3198    778  -1411       O  
ATOM    239  CB  LYS A 728      -6.392 192.703  17.420  1.00 57.27           C  
ANISOU  239  CB  LYS A 728     7253   7809   6695  -2764    596  -1395       C  
ATOM    240  CG  LYS A 728      -7.542 193.188  16.574  1.00 62.35           C  
ANISOU  240  CG  LYS A 728     7661   8844   7184  -2900    477  -1471       C  
ATOM    241  CD  LYS A 728      -7.181 193.056  15.106  1.00 68.55           C  
ANISOU  241  CD  LYS A 728     8462   9732   7852  -2977    435  -1629       C  
ATOM    242  CE  LYS A 728      -8.415 193.171  14.227  1.00 77.32           C  
ANISOU  242  CE  LYS A 728     9344  11237   8796  -3187    340  -1742       C  
ATOM    243  NZ  LYS A 728      -8.726 194.599  13.933  1.00 78.21           N1+
ANISOU  243  NZ  LYS A 728     9242  11676   8796  -2989    177  -1588       N1+
ATOM    244  N   GLY A 729      -8.894 193.410  19.509  1.00 48.13           N  
ANISOU  244  N   GLY A 729     5738   6999   5550  -2842    563  -1188       N  
ATOM    245  CA  GLY A 729     -10.328 193.399  19.828  1.00 47.62           C  
ANISOU  245  CA  GLY A 729     5471   7178   5444  -3009    551  -1198       C  
ATOM    246  C   GLY A 729     -11.073 194.727  19.682  1.00 46.48           C  
ANISOU  246  C   GLY A 729     5068   7394   5199  -2874    410  -1109       C  
ATOM    247  O   GLY A 729     -10.559 195.730  19.160  1.00 46.10           O  
ANISOU  247  O   GLY A 729     4982   7434   5098  -2664    308  -1047       O  
ATOM    248  N   LEU A 730     -12.306 194.740  20.138  1.00 48.74           N  
ANISOU  248  N   LEU A 730     5169   7887   5462  -2991    412  -1094       N  
ATOM    249  CA  LEU A 730     -13.156 195.924  20.054  1.00 48.65           C  
ANISOU  249  CA  LEU A 730     4892   8224   5366  -2866    298  -1004       C  
ATOM    250  C   LEU A 730     -13.811 196.165  21.402  1.00 46.99           C  
ANISOU  250  C   LEU A 730     4600   8034   5218  -2812    357   -890       C  
ATOM    251  O   LEU A 730     -14.378 195.259  21.983  1.00 46.79           O  
ANISOU  251  O   LEU A 730     4586   7957   5233  -3020    456   -932       O  
ATOM    252  CB  LEU A 730     -14.222 195.711  18.982  1.00 52.48           C  
ANISOU  252  CB  LEU A 730     5162   9056   5720  -3094    224  -1125       C  
ATOM    253  CG  LEU A 730     -14.793 196.917  18.230  1.00 54.24           C  
ANISOU  253  CG  LEU A 730     5127   9663   5819  -2949     73  -1049       C  
ATOM    254  CD1 LEU A 730     -13.694 197.615  17.453  1.00 52.23           C  
ANISOU  254  CD1 LEU A 730     4972   9338   5533  -2735     -1  -1006       C  
ATOM    255  CD2 LEU A 730     -15.959 196.491  17.318  1.00 57.94           C  
ANISOU  255  CD2 LEU A 730     5365  10503   6145  -3223     11  -1174       C  
ATOM    256  N   TRP A 731     -13.758 197.386  21.897  1.00 44.72           N  
ANISOU  256  N   TRP A 731     4229   7824   4937  -2541    307   -751       N  
ATOM    257  CA  TRP A 731     -14.336 197.678  23.188  1.00 45.38           C  
ANISOU  257  CA  TRP A 731     4236   7936   5068  -2475    370   -654       C  
ATOM    258  C   TRP A 731     -15.548 198.582  22.969  1.00 47.55           C  
ANISOU  258  C   TRP A 731     4207   8587   5272  -2418    293   -608       C  
ATOM    259  O   TRP A 731     -15.473 199.569  22.241  1.00 46.73           O  
ANISOU  259  O   TRP A 731     4002   8631   5121  -2245    190   -561       O  
ATOM    260  CB  TRP A 731     -13.302 198.316  24.080  1.00 43.61           C  
ANISOU  260  CB  TRP A 731     4167   7484   4916  -2214    399   -547       C  
ATOM    261  CG  TRP A 731     -13.859 198.771  25.386  1.00 43.01           C  
ANISOU  261  CG  TRP A 731     4007   7465   4870  -2122    459   -456       C  
ATOM    262  CD1 TRP A 731     -14.762 198.147  26.137  1.00 45.52           C  
ANISOU  262  CD1 TRP A 731     4248   7853   5191  -2285    545   -457       C  
ATOM    263  CD2 TRP A 731     -13.512 199.967  26.074  1.00 42.24           C  
ANISOU  263  CD2 TRP A 731     3897   7356   4797  -1849    447   -361       C  
ATOM    264  CE2 TRP A 731     -14.276 200.016  27.237  1.00 43.63           C  
ANISOU  264  CE2 TRP A 731     3980   7614   4980  -1855    528   -316       C  
ATOM    265  CE3 TRP A 731     -12.661 201.018  25.791  1.00 41.47           C  
ANISOU  265  CE3 TRP A 731     3849   7191   4713  -1611    383   -319       C  
ATOM    266  NE1 TRP A 731     -15.031 198.883  27.273  1.00 45.35           N  
ANISOU  266  NE1 TRP A 731     4160   7884   5185  -2123    587   -366       N  
ATOM    267  CZ2 TRP A 731     -14.181 201.059  28.145  1.00 44.59           C  
ANISOU  267  CZ2 TRP A 731     4072   7747   5121  -1631    549   -246       C  
ATOM    268  CZ3 TRP A 731     -12.555 202.035  26.682  1.00 41.63           C  
ANISOU  268  CZ3 TRP A 731     3845   7204   4765  -1400    405   -249       C  
ATOM    269  CH2 TRP A 731     -13.302 202.057  27.845  1.00 41.12           C  
ANISOU  269  CH2 TRP A 731     3698   7219   4704  -1409    488   -221       C  
ATOM    270  N   ILE A 732     -16.675 198.206  23.549  1.00 47.99           N  
ANISOU  270  N   ILE A 732     4109   8803   5320  -2571    349   -613       N  
ATOM    271  CA  ILE A 732     -17.908 198.913  23.337  1.00 53.47           C  
ANISOU  271  CA  ILE A 732     4494   9876   5946  -2540    287   -572       C  
ATOM    272  C   ILE A 732     -18.454 199.230  24.701  1.00 56.70           C  
ANISOU  272  C   ILE A 732     4831  10303   6408  -2453    379   -485       C  
ATOM    273  O   ILE A 732     -19.148 198.428  25.274  1.00 56.96           O  
ANISOU  273  O   ILE A 732     4818  10376   6448  -2663    464   -518       O  
ATOM    274  CB  ILE A 732     -18.895 198.063  22.548  1.00 57.17           C  
ANISOU  274  CB  ILE A 732     4797  10596   6328  -2860    262   -690       C  
ATOM    275  CG1 ILE A 732     -18.272 197.658  21.201  1.00 58.77           C  
ANISOU  275  CG1 ILE A 732     5096  10768   6465  -2966    184   -804       C  
ATOM    276  CG2 ILE A 732     -20.162 198.858  22.315  1.00 60.68           C  
ANISOU  276  CG2 ILE A 732     4891  11470   6694  -2801    189   -626       C  
ATOM    277  CD1 ILE A 732     -19.067 196.628  20.417  1.00 63.64           C  
ANISOU  277  CD1 ILE A 732     5603  11583   6995  -3333    175   -968       C  
ATOM    278  N   PRO A 733     -18.079 200.387  25.250  1.00 57.70           N  
ANISOU  278  N   PRO A 733     4965  10382   6575  -2148    373   -381       N  
ATOM    279  CA  PRO A 733     -18.420 200.665  26.646  1.00 60.38           C  
ANISOU  279  CA  PRO A 733     5278  10701   6960  -2059    477   -316       C  
ATOM    280  C   PRO A 733     -19.888 200.959  26.926  1.00 67.78           C  
ANISOU  280  C   PRO A 733     5911  11978   7861  -2089    497   -286       C  
ATOM    281  O   PRO A 733     -20.695 201.134  25.992  1.00 62.04           O  
ANISOU  281  O   PRO A 733     4957  11544   7070  -2141    412   -295       O  
ATOM    282  CB  PRO A 733     -17.542 201.868  27.000  1.00 58.11           C  
ANISOU  282  CB  PRO A 733     5089  10266   6723  -1735    461   -243       C  
ATOM    283  CG  PRO A 733     -17.135 202.463  25.702  1.00 56.93           C  
ANISOU  283  CG  PRO A 733     4920  10161   6549  -1631    339   -238       C  
ATOM    284  CD  PRO A 733     -17.189 201.394  24.663  1.00 54.56           C  
ANISOU  284  CD  PRO A 733     4638   9903   6188  -1894    290   -332       C  
ATOM    285  N   GLU A 734     -20.199 200.930  28.231  1.00 73.48           N  
ANISOU  285  N   GLU A 734     6632  12672   8615  -2068    613   -248       N  
ATOM    286  CA  GLU A 734     -21.434 201.459  28.824  1.00 74.83           C  
ANISOU  286  CA  GLU A 734     6533  13128   8768  -2012    661   -200       C  
ATOM    287  C   GLU A 734     -22.584 201.491  27.835  1.00 78.82           C  
ANISOU  287  C   GLU A 734     6738  14000   9207  -2115    580   -212       C  
ATOM    288  O   GLU A 734     -22.874 200.481  27.190  1.00 83.41           O  
ANISOU  288  O   GLU A 734     7298  14650   9744  -2403    553   -291       O  
ATOM    289  CB  GLU A 734     -21.163 202.856  29.408  1.00 72.61           C  
ANISOU  289  CB  GLU A 734     6241  12814   8531  -1662    679   -129       C  
ATOM    290  N   GLY A 735     -23.253 202.637  27.737  1.00 81.63           N  
ANISOU  290  N   GLY A 735     6858  14597   9558  -1882    549   -135       N  
ATOM    291  CA  GLY A 735     -24.309 202.843  26.743  1.00 85.93           C  
ANISOU  291  CA  GLY A 735     7088  15530  10029  -1926    455   -115       C  
ATOM    292  C   GLY A 735     -23.889 204.046  25.925  1.00 85.73           C  
ANISOU  292  C   GLY A 735     7033  15524  10014  -1625    353    -32       C  
ATOM    293  O   GLY A 735     -24.583 205.062  25.892  1.00 87.18           O  
ANISOU  293  O   GLY A 735     6985  15930  10209  -1396    345     67       O  
ATOM    294  N   GLU A 736     -22.743 203.926  25.259  1.00 78.78           N  
ANISOU  294  N   GLU A 736     6388  14405   9137  -1620    286    -65       N  
ATOM    295  CA  GLU A 736     -22.094 205.082  24.687  1.00 75.52           C  
ANISOU  295  CA  GLU A 736     6016  13918   8758  -1323    218     20       C  
ATOM    296  C   GLU A 736     -22.130 205.250  23.155  1.00 74.45           C  
ANISOU  296  C   GLU A 736     5769  13985   8533  -1329     70     51       C  
ATOM    297  O   GLU A 736     -21.727 206.298  22.667  1.00 77.14           O  
ANISOU  297  O   GLU A 736     6108  14298   8902  -1067     21    152       O  
ATOM    298  CB  GLU A 736     -20.631 205.092  25.136  1.00 20.00           C  
ATOM    299  N   LYS A 737     -22.582 204.251  22.400  1.00 71.67           N  
ANISOU  299  N   LYS A 737     5327  13832   8070  -1628      7    -37       N  
ATOM    300  CA  LYS A 737     -22.560 204.312  20.925  1.00 70.92           C  
ANISOU  300  CA  LYS A 737     5136  13948   7860  -1666   -135    -28       C  
ATOM    301  C   LYS A 737     -21.162 204.661  20.381  1.00 67.93           C  
ANISOU  301  C   LYS A 737     5025  13272   7510  -1528   -177    -17       C  
ATOM    302  O   LYS A 737     -20.994 205.497  19.488  1.00 72.61           O  
ANISOU  302  O   LYS A 737     5543  13980   8064  -1340   -267     88       O  
ATOM    303  CB  LYS A 737     -23.647 205.271  20.375  1.00 74.08           C  
ANISOU  303  CB  LYS A 737     5172  14776   8199  -1482   -210    121       C  
ATOM    304  N   VAL A 738     -20.151 204.012  20.937  1.00 62.22           N  
ANISOU  304  N   VAL A 738     4609  12173   6857  -1618   -106   -114       N  
ATOM    305  CA  VAL A 738     -18.810 204.044  20.366  1.00 60.45           C  
ANISOU  305  CA  VAL A 738     4641  11681   6646  -1562   -142   -136       C  
ATOM    306  C   VAL A 738     -18.204 202.650  20.390  1.00 56.83           C  
ANISOU  306  C   VAL A 738     4409  11002   6179  -1851   -100   -300       C  
ATOM    307  O   VAL A 738     -18.522 201.850  21.272  1.00 56.57           O  
ANISOU  307  O   VAL A 738     4419  10886   6187  -2020     -6   -366       O  
ATOM    308  CB  VAL A 738     -17.860 205.000  21.118  1.00 60.23           C  
ANISOU  308  CB  VAL A 738     4794  11342   6748  -1269    -85    -51       C  
ATOM    309  CG1 VAL A 738     -18.401 206.416  21.090  1.00 62.70           C  
ANISOU  309  CG1 VAL A 738     4908  11820   7095   -968   -103    107       C  
ATOM    310  CG2 VAL A 738     -17.650 204.548  22.550  1.00 59.59           C  
ANISOU  310  CG2 VAL A 738     4864  11019   6758  -1315     40   -102       C  
ATOM    311  N   LYS A 739     -17.314 202.386  19.441  1.00 53.15           N  
ANISOU  311  N   LYS A 739     4092  10432   5667  -1895   -157   -357       N  
ATOM    312  CA  LYS A 739     -16.556 201.145  19.360  1.00 52.10           C  
ANISOU  312  CA  LYS A 739     4204  10046   5544  -2125   -108   -507       C  
ATOM    313  C   LYS A 739     -15.085 201.481  19.210  1.00 48.35           C  
ANISOU  313  C   LYS A 739     3981   9262   5126  -1952   -109   -482       C  
ATOM    314  O   LYS A 739     -14.708 202.109  18.256  1.00 49.09           O  
ANISOU  314  O   LYS A 739     4048   9440   5161  -1834   -195   -437       O  
ATOM    315  CB  LYS A 739     -16.972 200.323  18.152  1.00 54.02           C  
ANISOU  315  CB  LYS A 739     4362  10512   5651  -2401   -173   -643       C  
ATOM    316  CG  LYS A 739     -18.452 200.124  17.996  1.00 60.20           C  
ANISOU  316  CG  LYS A 739     4842  11688   6342  -2577   -206   -666       C  
ATOM    317  CD  LYS A 739     -18.688 199.156  16.840  1.00 63.33           C  
ANISOU  317  CD  LYS A 739     5201  12261   6600  -2896   -258   -845       C  
ATOM    318  CE  LYS A 739     -20.082 198.571  16.867  1.00 70.44           C  
ANISOU  318  CE  LYS A 739     5846  13491   7426  -3170   -258   -922       C  
ATOM    319  NZ  LYS A 739     -21.091 199.574  16.426  1.00 72.64           N1+
ANISOU  319  NZ  LYS A 739     5770  14233   7596  -3026   -374   -784       N1+
ATOM    320  N   ILE A 740     -14.263 201.038  20.149  1.00 45.16           N  
ANISOU  320  N   ILE A 740     3812   8517   4829  -1943    -11   -504       N  
ATOM    321  CA  ILE A 740     -12.905 201.456  20.238  1.00 44.46           C  
ANISOU  321  CA  ILE A 740     3937   8149   4805  -1758     -4   -463       C  
ATOM    322  C   ILE A 740     -12.016 200.250  19.976  1.00 44.18           C  
ANISOU  322  C   ILE A 740     4134   7868   4781  -1932     44   -585       C  
ATOM    323  O   ILE A 740     -12.106 199.262  20.714  1.00 44.74           O  
ANISOU  323  O   ILE A 740     4302   7791   4905  -2090    140   -642       O  
ATOM    324  CB  ILE A 740     -12.634 202.016  21.660  1.00 44.16           C  
ANISOU  324  CB  ILE A 740     3967   7934   4877  -1577     72   -375       C  
ATOM    325  CG1 ILE A 740     -13.476 203.276  21.876  1.00 46.31           C  
ANISOU  325  CG1 ILE A 740     4017   8426   5152  -1382     41   -264       C  
ATOM    326  CG2 ILE A 740     -11.167 202.351  21.846  1.00 41.96           C  
ANISOU  326  CG2 ILE A 740     3912   7365   4663  -1414     85   -346       C  
ATOM    327  CD1 ILE A 740     -14.202 203.276  23.171  1.00 51.32           C  
ANISOU  327  CD1 ILE A 740     4581   9083   5833  -1381    129   -242       C  
ATOM    328  N   PRO A 741     -11.156 200.321  18.959  1.00 43.22           N  
ANISOU  328  N   PRO A 741     4106   7695   4618  -1896     -8   -616       N  
ATOM    329  CA  PRO A 741     -10.191 199.251  18.698  1.00 41.82           C  
ANISOU  329  CA  PRO A 741     4161   7262   4467  -2021     50   -728       C  
ATOM    330  C   PRO A 741      -9.148 199.138  19.794  1.00 38.90           C  
ANISOU  330  C   PRO A 741     4002   6557   4220  -1897    136   -673       C  
ATOM    331  O   PRO A 741      -8.477 200.136  20.199  1.00 35.74           O  
ANISOU  331  O   PRO A 741     3634   6080   3864  -1658    114   -563       O  
ATOM    332  CB  PRO A 741      -9.549 199.684  17.353  1.00 42.81           C  
ANISOU  332  CB  PRO A 741     4295   7464   4504  -1954    -37   -744       C  
ATOM    333  CG  PRO A 741     -10.586 200.551  16.726  1.00 44.48           C  
ANISOU  333  CG  PRO A 741     4241   8046   4610  -1911   -143   -678       C  
ATOM    334  CD  PRO A 741     -11.077 201.348  17.897  1.00 44.35           C  
ANISOU  334  CD  PRO A 741     4135   8033   4681  -1746   -120   -547       C  
ATOM    335  N   VAL A 742      -9.024 197.931  20.328  1.00 39.39           N  
ANISOU  335  N   VAL A 742     4204   6422   4341  -2060    241   -741       N  
ATOM    336  CA  VAL A 742      -8.092 197.712  21.450  1.00 37.96           C  
ANISOU  336  CA  VAL A 742     4208   5948   4264  -1950    327   -671       C  
ATOM    337  C   VAL A 742      -7.115 196.538  21.259  1.00 37.29           C  
ANISOU  337  C   VAL A 742     4352   5580   4235  -2038    413   -744       C  
ATOM    338  O   VAL A 742      -7.343 195.662  20.465  1.00 39.35           O  
ANISOU  338  O   VAL A 742     4643   5836   4471  -2237    441   -875       O  
ATOM    339  CB  VAL A 742      -8.855 197.462  22.757  1.00 37.56           C  
ANISOU  339  CB  VAL A 742     4112   5900   4259  -2001    403   -615       C  
ATOM    340  CG1 VAL A 742      -9.660 198.691  23.184  1.00 37.05           C  
ANISOU  340  CG1 VAL A 742     3841   6071   4163  -1862    344   -529       C  
ATOM    341  CG2 VAL A 742      -9.732 196.259  22.642  1.00 40.47           C  
ANISOU  341  CG2 VAL A 742     4460   6293   4624  -2288    473   -715       C  
ATOM    342  N   ALA A 743      -6.033 196.567  22.020  1.00 36.30           N  
ANISOU  342  N   ALA A 743     4379   5227   4183  -1881    460   -658       N  
ATOM    343  CA  ALA A 743      -5.195 195.404  22.200  1.00 37.97           C  
ANISOU  343  CA  ALA A 743     4800   5153   4473  -1937    569   -685       C  
ATOM    344  C   ALA A 743      -5.428 194.941  23.640  1.00 39.82           C  
ANISOU  344  C   ALA A 743     5077   5278   4775  -1949    664   -586       C  
ATOM    345  O   ALA A 743      -5.665 195.742  24.546  1.00 36.91           O  
ANISOU  345  O   ALA A 743     4623   5008   4393  -1827    635   -484       O  
ATOM    346  CB  ALA A 743      -3.739 195.729  21.952  1.00 35.89           C  
ANISOU  346  CB  ALA A 743     4663   4740   4233  -1745    550   -645       C  
ATOM    347  N   ILE A 744      -5.358 193.645  23.834  1.00 40.73           N  
ANISOU  347  N   ILE A 744     5328   5186   4960  -2095    787   -617       N  
ATOM    348  CA  ILE A 744      -5.744 192.991  25.106  1.00 44.62           C  
ANISOU  348  CA  ILE A 744     5860   5579   5512  -2155    898   -522       C  
ATOM    349  C   ILE A 744      -4.633 192.026  25.499  1.00 47.83           C  
ANISOU  349  C   ILE A 744     6488   5666   6018  -2103   1014   -457       C  
ATOM    350  O   ILE A 744      -4.452 191.017  24.826  1.00 50.26           O  
ANISOU  350  O   ILE A 744     6914   5795   6385  -2237   1098   -556       O  
ATOM    351  CB  ILE A 744      -7.032 192.185  24.918  1.00 45.21           C  
ANISOU  351  CB  ILE A 744     5866   5720   5590  -2442    961   -620       C  
ATOM    352  CG1 ILE A 744      -8.188 193.100  24.538  1.00 45.38           C  
ANISOU  352  CG1 ILE A 744     5644   6088   5510  -2488    847   -668       C  
ATOM    353  CG2 ILE A 744      -7.395 191.420  26.188  1.00 47.79           C  
ANISOU  353  CG2 ILE A 744     6248   5925   5984  -2518   1093   -510       C  
ATOM    354  CD1 ILE A 744      -9.339 192.418  23.842  1.00 47.43           C  
ANISOU  354  CD1 ILE A 744     5805   6473   5740  -2784    869   -815       C  
ATOM    355  N   LYS A 745      -3.865 192.348  26.537  1.00 48.31           N  
ANISOU  355  N   LYS A 745     6599   5663   6093  -1905   1022   -298       N  
ATOM    356  CA  LYS A 745      -2.706 191.548  26.927  1.00 51.58           C  
ANISOU  356  CA  LYS A 745     7201   5804   6591  -1809   1119   -204       C  
ATOM    357  C   LYS A 745      -2.974 190.690  28.167  1.00 57.22           C  
ANISOU  357  C   LYS A 745     7981   6396   7362  -1859   1250    -62       C  
ATOM    358  O   LYS A 745      -3.477 191.194  29.179  1.00 51.29           O  
ANISOU  358  O   LYS A 745     7133   5798   6554  -1824   1230     34       O  
ATOM    359  CB  LYS A 745      -1.487 192.448  27.180  1.00 53.26           C  
ANISOU  359  CB  LYS A 745     7423   6041   6771  -1547   1034   -114       C  
ATOM    360  CG  LYS A 745      -0.297 191.754  27.848  1.00 55.62           C  
ANISOU  360  CG  LYS A 745     7875   6117   7137  -1410   1123     28       C  
ATOM    361  CD  LYS A 745       0.952 192.565  27.601  1.00 57.77           C  
ANISOU  361  CD  LYS A 745     8151   6419   7379  -1197   1032     54       C  
ATOM    362  CE  LYS A 745       2.024 192.319  28.641  1.00 59.49           C  
ANISOU  362  CE  LYS A 745     8443   6545   7616  -1022   1075    237       C  
ATOM    363  NZ  LYS A 745       3.204 193.172  28.324  1.00 58.81           N1+
ANISOU  363  NZ  LYS A 745     8337   6514   7494   -838    979    242       N1+
ATOM    364  N   GLU A 746      -2.622 189.401  28.076  1.00 62.50           N  
ANISOU  364  N   GLU A 746     8819   6784   8143  -1935   1395    -48       N  
ATOM    365  CA  GLU A 746      -2.559 188.497  29.242  1.00 68.17           C  
ANISOU  365  CA  GLU A 746     9638   7331   8933  -1935   1538    132       C  
ATOM    366  C   GLU A 746      -1.306 187.601  29.193  1.00 69.35           C  
ANISOU  366  C   GLU A 746     9983   7171   9194  -1812   1647    220       C  
ATOM    367  O   GLU A 746      -1.131 186.702  30.020  1.00 76.63           O  
ANISOU  367  O   GLU A 746    11012   7904  10197  -1799   1786    385       O  
ATOM    368  CB  GLU A 746      -3.829 187.659  29.336  1.00 70.66           C  
ANISOU  368  CB  GLU A 746     9943   7606   9296  -2213   1650     80       C  
ATOM    369  CG  GLU A 746      -4.125 186.812  28.110  1.00 75.39           C  
ANISOU  369  CG  GLU A 746    10621   8045   9978  -2433   1722   -125       C  
ATOM    370  CD  GLU A 746      -5.504 186.166  28.162  1.00 80.59           C  
ANISOU  370  CD  GLU A 746    11227   8729  10663  -2740   1810   -204       C  
ATOM    371  OE1 GLU A 746      -6.464 186.846  28.559  1.00 81.72           O  
ANISOU  371  OE1 GLU A 746    11188   9150  10711  -2797   1732   -197       O  
ATOM    372  OE2 GLU A 746      -5.642 184.980  27.794  1.00 86.75           O1-
ANISOU  372  OE2 GLU A 746    12143   9250  11564  -2930   1965   -282       O1-
ATOM    373  N   SER A 752       2.694 180.815  39.133  1.00119.02           N  
ANISOU  373  N   SER A 752    17022  12364  15836   -739   2772   2872       N  
ATOM    374  CA  SER A 752       1.610 181.484  38.428  1.00118.77           C  
ANISOU  374  CA  SER A 752    16906  12453  15765   -994   2680   2540       C  
ATOM    375  C   SER A 752       1.068 182.689  39.226  1.00123.73           C  
ANISOU  375  C   SER A 752    17334  13527  16148  -1011   2511   2520       C  
ATOM    376  O   SER A 752       0.915 183.772  38.647  1.00124.21           O  
ANISOU  376  O   SER A 752    17279  13797  16117  -1041   2340   2274       O  
ATOM    377  CB  SER A 752       0.503 180.481  38.071  1.00118.92           C  
ANISOU  377  CB  SER A 752    17038  12188  15958  -1283   2870   2462       C  
ATOM    378  OG  SER A 752      -0.659 181.135  37.592  1.00111.91           O  
ANISOU  378  OG  SER A 752    16032  11486  15002  -1531   2777   2184       O  
ATOM    379  N   PRO A 753       0.775 182.518  40.548  1.00127.66           N  
ANISOU  379  N   PRO A 753    17791  14172  16541   -988   2565   2779       N  
ATOM    380  CA  PRO A 753       0.506 183.706  41.395  1.00123.70           C  
ANISOU  380  CA  PRO A 753    17102  14109  15789   -953   2407   2770       C  
ATOM    381  C   PRO A 753       1.653 184.752  41.425  1.00123.78           C  
ANISOU  381  C   PRO A 753    17018  14354  15656   -718   2216   2740       C  
ATOM    382  O   PRO A 753       1.386 185.957  41.539  1.00115.62           O  
ANISOU  382  O   PRO A 753    15840  13625  14465   -733   2061   2576       O  
ATOM    383  CB  PRO A 753       0.274 183.102  42.791  1.00122.45           C  
ANISOU  383  CB  PRO A 753    16950  14022  15554   -931   2528   3101       C  
ATOM    384  CG  PRO A 753      -0.228 181.724  42.533  1.00124.66           C  
ANISOU  384  CG  PRO A 753    17395  13910  16059  -1082   2756   3194       C  
ATOM    385  CD  PRO A 753       0.443 181.263  41.262  1.00127.74           C  
ANISOU  385  CD  PRO A 753    17920  13957  16656  -1044   2787   3053       C  
ATOM    386  N   LYS A 754       2.905 184.291  41.312  1.00122.41           N  
ANISOU  386  N   LYS A 754    16927  14035  15547   -508   2238   2892       N  
ATOM    387  CA  LYS A 754       4.075 185.177  41.247  1.00113.66           C  
ANISOU  387  CA  LYS A 754    15734  13126  14325   -297   2071   2863       C  
ATOM    388  C   LYS A 754       4.058 186.100  40.020  1.00107.11           C  
ANISOU  388  C   LYS A 754    14858  12318  13520   -358   1934   2520       C  
ATOM    389  O   LYS A 754       4.687 187.156  40.047  1.00105.75           O  
ANISOU  389  O   LYS A 754    14576  12383  13218   -248   1774   2440       O  
ATOM    390  CB  LYS A 754       5.371 184.352  41.269  1.00112.78           C  
ANISOU  390  CB  LYS A 754    15718  12827  14306    -65   2145   3103       C  
ATOM    391  N   ALA A 755       3.330 185.707  38.964  1.00103.27           N  
ANISOU  391  N   ALA A 755    14449  11594  13192   -542   2000   2322       N  
ATOM    392  CA  ALA A 755       3.252 186.470  37.697  1.00 97.05           C  
ANISOU  392  CA  ALA A 755    13626  10815  12433   -609   1884   2011       C  
ATOM    393  C   ALA A 755       2.141 187.538  37.618  1.00 90.20           C  
ANISOU  393  C   ALA A 755    12617  10199  11455   -768   1772   1799       C  
ATOM    394  O   ALA A 755       2.327 188.550  36.933  1.00 77.04           O  
ANISOU  394  O   ALA A 755    10872   8656   9741   -744   1631   1605       O  
ATOM    395  CB  ALA A 755       3.123 185.510  36.518  1.00 98.15           C  
ANISOU  395  CB  ALA A 755    13913  10595  12782   -719   2007   1893       C  
ATOM    396  N   ASN A 756       0.994 187.310  38.281  1.00 91.90           N  
ANISOU  396  N   ASN A 756    12797  10480  11637   -926   1842   1841       N  
ATOM    397  CA  ASN A 756      -0.093 188.330  38.379  1.00 88.10           C  
ANISOU  397  CA  ASN A 756    12163  10266  11043  -1052   1749   1671       C  
ATOM    398  C   ASN A 756       0.345 189.636  39.076  1.00 82.95           C  
ANISOU  398  C   ASN A 756    11376   9937  10203   -903   1600   1665       C  
ATOM    399  O   ASN A 756      -0.220 190.702  38.818  1.00 78.28           O  
ANISOU  399  O   ASN A 756    10666   9530   9544   -951   1497   1478       O  
ATOM    400  CB  ASN A 756      -1.341 187.758  39.076  1.00 87.41           C  
ANISOU  400  CB  ASN A 756    12058  10200  10953  -1238   1871   1747       C  
ATOM    401  N   LYS A 757       1.346 189.527  39.959  1.00 82.52           N  
ANISOU  401  N   LYS A 757    11337   9948  10066   -726   1597   1871       N  
ATOM    402  CA  LYS A 757       1.976 190.675  40.632  1.00 77.41           C  
ANISOU  402  CA  LYS A 757    10575   9596   9240   -585   1462   1865       C  
ATOM    403  C   LYS A 757       2.725 191.530  39.642  1.00 69.49           C  
ANISOU  403  C   LYS A 757     9549   8590   8264   -504   1332   1681       C  
ATOM    404  O   LYS A 757       2.682 192.742  39.748  1.00 66.45           O  
ANISOU  404  O   LYS A 757     9054   8418   7773   -485   1218   1542       O  
ATOM    405  CB  LYS A 757       2.943 190.225  41.749  1.00 77.26           C  
ANISOU  405  CB  LYS A 757    10574   9659   9121   -419   1491   2144       C  
ATOM    406  N   GLU A 758       3.413 190.906  38.679  1.00 67.99           N  
ANISOU  406  N   GLU A 758     9464   8151   8217   -459   1359   1677       N  
ATOM    407  CA  GLU A 758       4.152 191.665  37.641  1.00 62.57           C  
ANISOU  407  CA  GLU A 758     8758   7452   7560   -388   1245   1508       C  
ATOM    408  C   GLU A 758       3.187 192.364  36.664  1.00 60.07           C  
ANISOU  408  C   GLU A 758     8391   7152   7281   -533   1189   1254       C  
ATOM    409  O   GLU A 758       3.433 193.509  36.248  1.00 48.61           O  
ANISOU  409  O   GLU A 758     6860   5829   5781   -489   1068   1111       O  
ATOM    410  CB  GLU A 758       5.166 190.782  36.878  1.00 61.83           C  
ANISOU  410  CB  GLU A 758     8788   7100   7603   -292   1302   1572       C  
ATOM    411  N   ILE A 759       2.075 191.700  36.318  1.00 60.21           N  
ANISOU  411  N   ILE A 759     8445   7052   7380   -707   1277   1206       N  
ATOM    412  CA  ILE A 759       1.116 192.319  35.385  1.00 58.11           C  
ANISOU  412  CA  ILE A 759     8109   6834   7136   -843   1221    983       C  
ATOM    413  C   ILE A 759       0.376 193.481  36.077  1.00 52.10           C  
ANISOU  413  C   ILE A 759     7196   6352   6246   -856   1146    924       C  
ATOM    414  O   ILE A 759       0.102 194.469  35.420  1.00 41.46           O  
ANISOU  414  O   ILE A 759     5765   5100   4884   -862   1052    763       O  
ATOM    415  CB  ILE A 759       0.156 191.317  34.683  1.00 59.94           C  
ANISOU  415  CB  ILE A 759     8404   6883   7486  -1046   1327    917       C  
ATOM    416  CG1 ILE A 759      -0.090 191.761  33.230  1.00 62.26           C  
ANISOU  416  CG1 ILE A 759     8670   7161   7826  -1119   1251    694       C  
ATOM    417  CG2 ILE A 759      -1.165 191.197  35.405  1.00 62.69           C  
ANISOU  417  CG2 ILE A 759     8678   7347   7793  -1199   1385    939       C  
ATOM    418  CD1 ILE A 759      -0.909 190.783  32.404  1.00 63.85           C  
ANISOU  418  CD1 ILE A 759     8931   7197   8132  -1331   1345    596       C  
ATOM    419  N   LEU A 760       0.098 193.376  37.387  1.00 50.47           N  
ANISOU  419  N   LEU A 760     6957   6274   5946   -848   1195   1060       N  
ATOM    420  CA  LEU A 760      -0.443 194.544  38.112  1.00 48.74           C  
ANISOU  420  CA  LEU A 760     6598   6324   5595   -834   1132    993       C  
ATOM    421  C   LEU A 760       0.554 195.685  38.356  1.00 44.68           C  
ANISOU  421  C   LEU A 760     6035   5949   4990   -676   1019    950       C  
ATOM    422  O   LEU A 760       0.136 196.833  38.398  1.00 41.09           O  
ANISOU  422  O   LEU A 760     5478   5652   4481   -670    954    815       O  
ATOM    423  CB  LEU A 760      -1.141 194.150  39.389  1.00 50.70           C  
ANISOU  423  CB  LEU A 760     6814   6695   5756   -892   1223   1124       C  
ATOM    424  CG  LEU A 760      -2.465 193.383  39.124  1.00 54.76           C  
ANISOU  424  CG  LEU A 760     7324   7131   6349  -1090   1325   1108       C  
ATOM    425  CD1 LEU A 760      -3.152 193.079  40.421  1.00 57.55           C  
ANISOU  425  CD1 LEU A 760     7633   7629   6604  -1146   1418   1242       C  
ATOM    426  CD2 LEU A 760      -3.451 194.113  38.227  1.00 55.68           C  
ANISOU  426  CD2 LEU A 760     7334   7319   6501  -1187   1267    897       C  
ATOM    427  N   ASP A 761       1.855 195.408  38.458  1.00 42.85           N  
ANISOU  427  N   ASP A 761     5870   5657   4752   -551    998   1053       N  
ATOM    428  CA  ASP A 761       2.838 196.508  38.498  1.00 42.35           C  
ANISOU  428  CA  ASP A 761     5755   5716   4618   -426    886    985       C  
ATOM    429  C   ASP A 761       2.844 197.240  37.176  1.00 40.13           C  
ANISOU  429  C   ASP A 761     5459   5360   4427   -435    810    801       C  
ATOM    430  O   ASP A 761       2.954 198.488  37.120  1.00 37.64           O  
ANISOU  430  O   ASP A 761     5067   5167   4068   -396    729    676       O  
ATOM    431  CB  ASP A 761       4.269 196.015  38.796  1.00 45.91           C  
ANISOU  431  CB  ASP A 761     6262   6134   5046   -290    876   1140       C  
ATOM    432  CG  ASP A 761       4.451 195.528  40.246  1.00 50.68           C  
ANISOU  432  CG  ASP A 761     6853   6884   5516   -246    927   1343       C  
ATOM    433  OD1 ASP A 761       3.791 196.014  41.187  1.00 50.96           O  
ANISOU  433  OD1 ASP A 761     6811   7123   5426   -292    932   1326       O  
ATOM    434  OD2 ASP A 761       5.280 194.627  40.450  1.00 59.51           O1-
ANISOU  434  OD2 ASP A 761     8037   7921   6652   -157    968   1532       O1-
ATOM    435  N   GLU A 762       2.771 196.464  36.089  1.00 37.35           N  
ANISOU  435  N   GLU A 762     5187   4802   4202   -486    844    785       N  
ATOM    436  CA  GLU A 762       2.669 197.020  34.745  1.00 36.38           C  
ANISOU  436  CA  GLU A 762     5050   4616   4154   -511    781    624       C  
ATOM    437  C   GLU A 762       1.396 197.857  34.569  1.00 34.25           C  
ANISOU  437  C   GLU A 762     4673   4471   3868   -597    754    492       C  
ATOM    438  O   GLU A 762       1.452 198.939  34.022  1.00 32.84           O  
ANISOU  438  O   GLU A 762     4432   4354   3689   -555    675    381       O  
ATOM    439  CB  GLU A 762       2.726 195.871  33.716  1.00 39.05           C  
ANISOU  439  CB  GLU A 762     5497   4725   4612   -573    843    627       C  
ATOM    440  CG  GLU A 762       2.806 196.318  32.282  1.00 39.18           C  
ANISOU  440  CG  GLU A 762     5509   4688   4688   -590    780    477       C  
ATOM    441  CD  GLU A 762       3.078 195.148  31.323  1.00 41.21           C  
ANISOU  441  CD  GLU A 762     5885   4721   5049   -641    851    469       C  
ATOM    442  OE1 GLU A 762       3.441 194.065  31.803  1.00 43.90           O  
ANISOU  442  OE1 GLU A 762     6322   4923   5433   -626    948    594       O  
ATOM    443  OE2 GLU A 762       2.936 195.299  30.089  1.00 42.30           O1-
ANISOU  443  OE2 GLU A 762     6024   4820   5227   -693    818    339       O1-
ATOM    444  N   ALA A 763       0.254 197.370  35.050  1.00 32.75           N  
ANISOU  444  N   ALA A 763     4454   4321   3668   -710    825    518       N  
ATOM    445  CA  ALA A 763      -0.974 198.142  34.948  1.00 33.47           C  
ANISOU  445  CA  ALA A 763     4424   4552   3741   -778    806    408       C  
ATOM    446  C   ALA A 763      -0.862 199.442  35.724  1.00 35.92           C  
ANISOU  446  C   ALA A 763     4645   5040   3963   -677    757    364       C  
ATOM    447  O   ALA A 763      -1.326 200.478  35.230  1.00 35.17           O  
ANISOU  447  O   ALA A 763     4463   5016   3882   -657    706    248       O  
ATOM    448  CB  ALA A 763      -2.149 197.367  35.468  1.00 33.39           C  
ANISOU  448  CB  ALA A 763     4387   4574   3725   -917    901    455       C  
ATOM    449  N   TYR A 764      -0.224 199.396  36.913  1.00 35.57           N  
ANISOU  449  N   TYR A 764     4621   5067   3825   -613    777    455       N  
ATOM    450  CA  TYR A 764      -0.001 200.591  37.713  1.00 35.68           C  
ANISOU  450  CA  TYR A 764     4562   5249   3744   -532    738    393       C  
ATOM    451  C   TYR A 764       0.729 201.663  36.925  1.00 35.06           C  
ANISOU  451  C   TYR A 764     4473   5136   3709   -448    649    280       C  
ATOM    452  O   TYR A 764       0.305 202.832  36.865  1.00 32.80           O  
ANISOU  452  O   TYR A 764     4109   4927   3424   -421    624    161       O  
ATOM    453  CB  TYR A 764       0.777 200.272  39.019  1.00 38.29           C  
ANISOU  453  CB  TYR A 764     4920   5679   3949   -481    761    514       C  
ATOM    454  CG  TYR A 764       0.955 201.485  39.920  1.00 39.04           C  
ANISOU  454  CG  TYR A 764     4936   5968   3926   -426    732    421       C  
ATOM    455  CD1 TYR A 764       2.011 202.386  39.727  1.00 38.84           C  
ANISOU  455  CD1 TYR A 764     4910   5954   3893   -345    653    339       C  
ATOM    456  CD2 TYR A 764       0.082 201.720  40.966  1.00 40.92           C  
ANISOU  456  CD2 TYR A 764     5103   6380   4062   -465    793    405       C  
ATOM    457  CE1 TYR A 764       2.159 203.505  40.529  1.00 37.26           C  
ANISOU  457  CE1 TYR A 764     4645   5916   3593   -316    638    227       C  
ATOM    458  CE2 TYR A 764       0.237 202.836  41.791  1.00 42.50           C  
ANISOU  458  CE2 TYR A 764     5239   6754   4153   -423    779    292       C  
ATOM    459  CZ  TYR A 764       1.288 203.736  41.539  1.00 39.03           C  
ANISOU  459  CZ  TYR A 764     4807   6304   3719   -353    702    195       C  
ATOM    460  OH  TYR A 764       1.433 204.848  42.348  1.00 37.91           O  
ANISOU  460  OH  TYR A 764     4607   6319   3475   -332    701     58       O  
ATOM    461  N   VAL A 765       1.869 201.308  36.354  1.00 34.00           N  
ANISOU  461  N   VAL A 765     4418   4885   3614   -398    609    324       N  
ATOM    462  CA  VAL A 765       2.623 202.276  35.556  1.00 35.87           C  
ANISOU  462  CA  VAL A 765     4647   5084   3895   -328    531    231       C  
ATOM    463  C   VAL A 765       1.805 202.819  34.382  1.00 33.75           C  
ANISOU  463  C   VAL A 765     4336   4770   3717   -359    507    129       C  
ATOM    464  O   VAL A 765       1.731 204.047  34.121  1.00 34.99           O  
ANISOU  464  O   VAL A 765     4434   4966   3893   -312    468     32       O  
ATOM    465  CB  VAL A 765       3.926 201.643  35.042  1.00 36.68           C  
ANISOU  465  CB  VAL A 765     4836   5068   4031   -275    505    305       C  
ATOM    466  CG1 VAL A 765       4.625 202.560  34.063  1.00 36.14           C  
ANISOU  466  CG1 VAL A 765     4759   4953   4018   -221    433    215       C  
ATOM    467  CG2 VAL A 765       4.815 201.287  36.224  1.00 38.69           C  
ANISOU  467  CG2 VAL A 765     5106   5410   4184   -220    514    417       C  
ATOM    468  N   MET A 766       1.222 201.906  33.641  1.00 33.73           N  
ANISOU  468  N   MET A 766     4361   4682   3771   -438    533    154       N  
ATOM    469  CA  MET A 766       0.500 202.288  32.408  1.00 33.50           C  
ANISOU  469  CA  MET A 766     4283   4635   3809   -474    500     72       C  
ATOM    470  C   MET A 766      -0.730 203.123  32.729  1.00 34.28           C  
ANISOU  470  C   MET A 766     4260   4871   3893   -485    511     12       C  
ATOM    471  O   MET A 766      -1.133 203.955  31.924  1.00 36.77           O  
ANISOU  471  O   MET A 766     4508   5212   4250   -455    470    -50       O  
ATOM    472  CB  MET A 766       0.030 201.065  31.659  1.00 36.00           C  
ANISOU  472  CB  MET A 766     4646   4861   4171   -587    534     93       C  
ATOM    473  CG  MET A 766       0.987 200.522  30.649  1.00 38.57           C  
ANISOU  473  CG  MET A 766     5068   5040   4545   -574    514     96       C  
ATOM    474  SD  MET A 766       0.229 199.218  29.649  1.00 41.09           S  
ANISOU  474  SD  MET A 766     5432   5262   4918   -738    564     65       S  
ATOM    475  CE  MET A 766      -0.007 199.974  28.047  1.00 41.70           C  
ANISOU  475  CE  MET A 766     5443   5389   5010   -744    478    -44       C  
ATOM    476  N   ALA A 767      -1.312 202.963  33.924  1.00 34.13           N  
ANISOU  476  N   ALA A 767     4204   4949   3811   -514    571     39       N  
ATOM    477  CA  ALA A 767      -2.428 203.831  34.325  1.00 34.82           C  
ANISOU  477  CA  ALA A 767     4168   5177   3883   -504    595    -23       C  
ATOM    478  C   ALA A 767      -1.973 205.218  34.771  1.00 35.69           C  
ANISOU  478  C   ALA A 767     4249   5331   3980   -388    575    -99       C  
ATOM    479  O   ALA A 767      -2.800 206.114  34.935  1.00 39.28           O  
ANISOU  479  O   ALA A 767     4606   5871   4447   -350    599   -164       O  
ATOM    480  CB  ALA A 767      -3.264 203.189  35.424  1.00 34.82           C  
ANISOU  480  CB  ALA A 767     4133   5279   3816   -583    678     24       C  
ATOM    481  N   SER A 768      -0.685 205.395  35.004  1.00 32.53           N  
ANISOU  481  N   SER A 768     3925   4876   3557   -334    543    -93       N  
ATOM    482  CA  SER A 768      -0.179 206.623  35.580  1.00 35.55           C  
ANISOU  482  CA  SER A 768     4288   5301   3917   -255    537   -179       C  
ATOM    483  C   SER A 768       0.477 207.527  34.528  1.00 35.96           C  
ANISOU  483  C   SER A 768     4355   5248   4059   -188    478   -231       C  
ATOM    484  O   SER A 768       1.020 208.573  34.863  1.00 38.37           O  
ANISOU  484  O   SER A 768     4657   5553   4367   -133    475   -309       O  
ATOM    485  CB  SER A 768       0.893 206.276  36.635  1.00 35.44           C  
ANISOU  485  CB  SER A 768     4333   5333   3798   -252    537   -141       C  
ATOM    486  OG  SER A 768       0.352 205.491  37.678  1.00 36.55           O  
ANISOU  486  OG  SER A 768     4462   5582   3843   -306    597    -74       O  
ATOM    487  N   VAL A 769       0.509 207.083  33.284  1.00 33.78           N  
ANISOU  487  N   VAL A 769     4101   4883   3849   -202    436   -188       N  
ATOM    488  CA  VAL A 769       1.170 207.846  32.224  1.00 33.44           C  
ANISOU  488  CA  VAL A 769     4074   4748   3881   -143    382   -213       C  
ATOM    489  C   VAL A 769       0.124 208.379  31.268  1.00 35.77           C  
ANISOU  489  C   VAL A 769     4289   5055   4246   -122    376   -226       C  
ATOM    490  O   VAL A 769      -0.861 207.718  31.006  1.00 36.49           O  
ANISOU  490  O   VAL A 769     4333   5202   4329   -181    386   -198       O  
ATOM    491  CB  VAL A 769       2.207 207.006  31.445  1.00 33.92           C  
ANISOU  491  CB  VAL A 769     4223   4714   3950   -161    337   -153       C  
ATOM    492  CG1 VAL A 769       3.361 206.596  32.342  1.00 35.82           C  
ANISOU  492  CG1 VAL A 769     4526   4958   4126   -153    338   -122       C  
ATOM    493  CG2 VAL A 769       1.588 205.794  30.816  1.00 35.07           C  
ANISOU  493  CG2 VAL A 769     4384   4839   4101   -240    344   -103       C  
ATOM    494  N   ASN A 771       0.691 210.681  27.813  1.00 27.42           N  
ANISOU  494  N   ASN A 771     3185   3837   3396     60    265   -188       N  
ATOM    495  CA  ASN A 771       1.491 211.495  26.869  1.00 26.73           C  
ANISOU  495  CA  ASN A 771     3124   3663   3368    123    236   -163       C  
ATOM    496  C   ASN A 771       1.256 210.918  25.482  1.00 26.59           C  
ANISOU  496  C   ASN A 771     3087   3685   3328     94    181    -99       C  
ATOM    497  O   ASN A 771       1.099 209.681  25.335  1.00 27.84           O  
ANISOU  497  O   ASN A 771     3268   3884   3424      2    164    -99       O  
ATOM    498  CB  ASN A 771       2.977 211.417  27.259  1.00 25.58           C  
ANISOU  498  CB  ASN A 771     3077   3432   3210    105    228   -191       C  
ATOM    499  CG  ASN A 771       3.880 212.235  26.368  1.00 28.24           C  
ANISOU  499  CG  ASN A 771     3440   3681   3608    153    209   -168       C  
ATOM    500  ND2 ASN A 771       4.022 213.500  26.671  1.00 28.45           N  
ANISOU  500  ND2 ASN A 771     3456   3642   3710    211    249   -203       N  
ATOM    501  OD1 ASN A 771       4.433 211.726  25.415  1.00 28.45           O  
ANISOU  501  OD1 ASN A 771     3499   3693   3616    134    167   -121       O  
ATOM    502  N   PRO A 772       1.267 211.783  24.443  1.00 26.41           N  
ANISOU  502  N   PRO A 772     3028   3650   3354    167    161    -45       N  
ATOM    503  CA  PRO A 772       1.012 211.285  23.067  1.00 28.61           C  
ANISOU  503  CA  PRO A 772     3277   4006   3587    136    105     12       C  
ATOM    504  C   PRO A 772       2.027 210.237  22.562  1.00 27.13           C  
ANISOU  504  C   PRO A 772     3188   3776   3344     55     75     -4       C  
ATOM    505  O   PRO A 772       1.756 209.583  21.570  1.00 29.48           O  
ANISOU  505  O   PRO A 772     3468   4146   3583     -1     39      8       O  
ATOM    506  CB  PRO A 772       1.124 212.551  22.219  1.00 30.42           C  
ANISOU  506  CB  PRO A 772     3466   4211   3881    247    100     90       C  
ATOM    507  CG  PRO A 772       0.675 213.643  23.163  1.00 32.38           C  
ANISOU  507  CG  PRO A 772     3675   4407   4220    339    165     73       C  
ATOM    508  CD  PRO A 772       1.247 213.252  24.515  1.00 29.20           C  
ANISOU  508  CD  PRO A 772     3351   3938   3804    280    200    -30       C  
ATOM    509  N   HIS A 773       3.171 210.079  23.230  1.00 26.64           N  
ANISOU  509  N   HIS A 773     3218   3608   3293     50     94    -37       N  
ATOM    510  CA  HIS A 773       4.204 209.150  22.793  1.00 26.23           C  
ANISOU  510  CA  HIS A 773     3255   3508   3204      0     79    -44       C  
ATOM    511  C   HIS A 773       4.481 208.025  23.793  1.00 26.58           C  
ANISOU  511  C   HIS A 773     3363   3518   3216    -58    107    -78       C  
ATOM    512  O   HIS A 773       5.521 207.383  23.747  1.00 26.68           O  
ANISOU  512  O   HIS A 773     3452   3468   3216    -68    111    -76       O  
ATOM    513  CB  HIS A 773       5.470 209.902  22.400  1.00 25.24           C  
ANISOU  513  CB  HIS A 773     3168   3305   3115     58     73    -23       C  
ATOM    514  CG  HIS A 773       5.245 210.856  21.273  1.00 26.10           C  
ANISOU  514  CG  HIS A 773     3225   3441   3250    113     53     37       C  
ATOM    515  CD2 HIS A 773       5.198 212.210  21.236  1.00 27.79           C  
ANISOU  515  CD2 HIS A 773     3400   3617   3540    193     70     76       C  
ATOM    516  ND1 HIS A 773       4.890 210.431  20.014  1.00 27.06           N  
ANISOU  516  ND1 HIS A 773     3320   3646   3313     86     19     70       N  
ATOM    517  CE1 HIS A 773       4.723 211.489  19.231  1.00 27.32           C  
ANISOU  517  CE1 HIS A 773     3298   3706   3374    157      8    148       C  
ATOM    518  NE2 HIS A 773       4.891 212.566  19.948  1.00 27.63           N  
ANISOU  518  NE2 HIS A 773     3333   3657   3506    226     44    158       N  
ATOM    519  N   VAL A 774       3.516 207.766  24.665  1.00 25.84           N  
ANISOU  519  N   VAL A 774     3233   3475   3110    -91    132    -95       N  
ATOM    520  CA  VAL A 774       3.552 206.631  25.565  1.00 26.36           C  
ANISOU  520  CA  VAL A 774     3350   3521   3141   -153    167   -102       C  
ATOM    521  C   VAL A 774       2.198 205.946  25.489  1.00 26.74           C  
ANISOU  521  C   VAL A 774     3348   3644   3166   -240    182   -112       C  
ATOM    522  O   VAL A 774       1.177 206.646  25.403  1.00 27.55           O  
ANISOU  522  O   VAL A 774     3351   3839   3277   -224    174   -116       O  
ATOM    523  CB  VAL A 774       3.834 207.152  27.006  1.00 30.01           C  
ANISOU  523  CB  VAL A 774     3811   3989   3601   -112    193   -112       C  
ATOM    524  CG1 VAL A 774       3.610 206.041  27.977  1.00 37.04           C  
ANISOU  524  CG1 VAL A 774     4734   4891   4445   -171    234    -94       C  
ATOM    525  CG2 VAL A 774       5.265 207.675  27.093  1.00 29.82           C  
ANISOU  525  CG2 VAL A 774     3831   3906   3590    -55    177   -112       C  
ATOM    526  N   CYS A 775       2.159 204.606  25.520  1.00 26.69           N  
ANISOU  526  N   CYS A 775     3404   3598   3137   -332    212   -113       N  
ATOM    527  CA  CYS A 775       0.882 203.885  25.538  1.00 30.23           C  
ANISOU  527  CA  CYS A 775     3805   4115   3566   -444    237   -132       C  
ATOM    528  C   CYS A 775       0.257 203.883  26.948  1.00 32.88           C  
ANISOU  528  C   CYS A 775     4106   4497   3890   -453    284   -114       C  
ATOM    529  O   CYS A 775       0.915 203.498  27.901  1.00 37.87           O  
ANISOU  529  O   CYS A 775     4807   5068   4512   -434    319    -81       O  
ATOM    530  CB  CYS A 775       1.099 202.445  25.133  1.00 32.42           C  
ANISOU  530  CB  CYS A 775     4176   4301   3839   -550    275   -147       C  
ATOM    531  SG  CYS A 775       1.592 202.379  23.384  1.00 39.25           S  
ANISOU  531  SG  CYS A 775     5066   5151   4693   -564    230   -195       S  
ATOM    532  N   ARG A 776      -1.001 204.232  27.082  1.00 34.73           N  
ANISOU  532  N   ARG A 776     4226   4853   4115   -483    289   -129       N  
ATOM    533  CA  ARG A 776      -1.612 204.187  28.391  1.00 39.39           C  
ANISOU  533  CA  ARG A 776     4779   5500   4685   -497    343   -117       C  
ATOM    534  C   ARG A 776      -2.692 203.147  28.481  1.00 36.02           C  
ANISOU  534  C   ARG A 776     4317   5127   4239   -641    387   -117       C  
ATOM    535  O   ARG A 776      -3.196 202.668  27.490  1.00 32.02           O  
ANISOU  535  O   ARG A 776     3782   4648   3734   -734    367   -146       O  
ATOM    536  CB  ARG A 776      -2.191 205.531  28.781  1.00 46.74           C  
ANISOU  536  CB  ARG A 776     5600   6531   5628   -399    339   -135       C  
ATOM    537  CG  ARG A 776      -3.461 205.951  28.022  1.00 55.33           C  
ANISOU  537  CG  ARG A 776     6544   7750   6726   -410    318   -144       C  
ATOM    538  CD  ARG A 776      -4.231 207.026  28.794  1.00 62.66           C  
ANISOU  538  CD  ARG A 776     7361   8774   7671   -318    354   -155       C  
ATOM    539  NE  ARG A 776      -3.668 207.185  30.133  1.00 69.13           N  
ANISOU  539  NE  ARG A 776     8247   9546   8472   -283    406   -174       N  
ATOM    540  CZ  ARG A 776      -4.245 207.839  31.126  1.00 75.34           C  
ANISOU  540  CZ  ARG A 776     8965  10407   9251   -232    464   -204       C  
ATOM    541  NH1 ARG A 776      -5.397 208.470  30.938  1.00 83.47           N1+
ANISOU  541  NH1 ARG A 776     9855  11547  10310   -186    483   -210       N1+
ATOM    542  NH2 ARG A 776      -3.622 207.900  32.301  1.00 74.91           N  
ANISOU  542  NH2 ARG A 776     8976  10329   9155   -218    504   -230       N  
ATOM    543  N   LEU A 777      -3.052 202.826  29.707  1.00 35.98           N  
ANISOU  543  N   LEU A 777     4308   5153   4209   -670    450    -89       N  
ATOM    544  CA  LEU A 777      -3.994 201.766  29.959  1.00 36.37           C  
ANISOU  544  CA  LEU A 777     4336   5237   4245   -821    510    -78       C  
ATOM    545  C   LEU A 777      -5.391 202.329  29.771  1.00 37.61           C  
ANISOU  545  C   LEU A 777     4320   5577   4392   -851    502   -112       C  
ATOM    546  O   LEU A 777      -5.670 203.402  30.294  1.00 36.93           O  
ANISOU  546  O   LEU A 777     4149   5581   4299   -740    500   -117       O  
ATOM    547  CB  LEU A 777      -3.830 201.294  31.411  1.00 36.28           C  
ANISOU  547  CB  LEU A 777     4376   5209   4198   -826    586    -12       C  
ATOM    548  CG  LEU A 777      -4.548 200.002  31.735  1.00 37.14           C  
ANISOU  548  CG  LEU A 777     4503   5301   4306   -990    668     25       C  
ATOM    549  CD1 LEU A 777      -3.846 198.849  31.042  1.00 38.73           C  
ANISOU  549  CD1 LEU A 777     4845   5313   4556  -1062    686     39       C  
ATOM    550  CD2 LEU A 777      -4.611 199.769  33.227  1.00 39.92           C  
ANISOU  550  CD2 LEU A 777     4868   5694   4605   -983    743    105       C  
ATOM    551  N   LEU A 778      -6.263 201.634  29.040  1.00 34.80           N  
ANISOU  551  N   LEU A 778     3905   5282   4035   -998    502   -141       N  
ATOM    552  CA  LEU A 778      -7.661 201.977  29.053  1.00 35.72           C  
ANISOU  552  CA  LEU A 778     3839   5600   4132  -1043    507   -157       C  
ATOM    553  C   LEU A 778      -8.349 201.381  30.324  1.00 35.67           C  
ANISOU  553  C   LEU A 778     3808   5641   4102  -1132    605   -124       C  
ATOM    554  O   LEU A 778      -9.218 202.022  30.954  1.00 35.91           O  
ANISOU  554  O   LEU A 778     3701   5830   4113  -1089    632   -119       O  
ATOM    555  CB  LEU A 778      -8.350 201.482  27.798  1.00 38.35           C  
ANISOU  555  CB  LEU A 778     4095   6021   4453  -1183    464   -207       C  
ATOM    556  CG  LEU A 778      -7.913 202.138  26.483  1.00 41.80           C  
ANISOU  556  CG  LEU A 778     4516   6476   4889  -1101    367   -229       C  
ATOM    557  CD1 LEU A 778      -8.587 201.473  25.306  1.00 42.70           C  
ANISOU  557  CD1 LEU A 778     4558   6702   4964  -1273    330   -290       C  
ATOM    558  CD2 LEU A 778      -8.238 203.632  26.534  1.00 44.53           C  
ANISOU  558  CD2 LEU A 778     4730   6945   5244   -912    328   -192       C  
ATOM    559  N   GLY A 779      -7.980 200.154  30.675  1.00 33.46           N  
ANISOU  559  N   GLY A 779     3659   5225   3829  -1253    667    -95       N  
ATOM    560  CA  GLY A 779      -8.468 199.553  31.908  1.00 36.00           C  
ANISOU  560  CA  GLY A 779     3978   5572   4125  -1330    767    -37       C  
ATOM    561  C   GLY A 779      -8.005 198.116  32.048  1.00 37.04           C  
ANISOU  561  C   GLY A 779     4269   5516   4287  -1463    840     10       C  
ATOM    562  O   GLY A 779      -7.225 197.634  31.219  1.00 36.60           O  
ANISOU  562  O   GLY A 779     4331   5300   4273  -1478    815    -12       O  
ATOM    563  N   ILE A 780      -8.446 197.439  33.093  1.00 35.88           N  
ANISOU  563  N   ILE A 780     4131   5378   4121  -1550    941     84       N  
ATOM    564  CA  ILE A 780      -8.080 196.032  33.243  1.00 37.97           C  
ANISOU  564  CA  ILE A 780     4551   5444   4433  -1676   1032    149       C  
ATOM    565  C   ILE A 780      -9.351 195.246  33.363  1.00 38.32           C  
ANISOU  565  C   ILE A 780     4516   5556   4489  -1899   1118    142       C  
ATOM    566  O   ILE A 780     -10.374 195.788  33.751  1.00 37.12           O  
ANISOU  566  O   ILE A 780     4196   5620   4288  -1921   1121    126       O  
ATOM    567  CB  ILE A 780      -7.183 195.736  34.474  1.00 39.30           C  
ANISOU  567  CB  ILE A 780     4841   5518   4572  -1573   1093    291       C  
ATOM    568  CG1 ILE A 780      -7.865 196.178  35.756  1.00 41.42           C  
ANISOU  568  CG1 ILE A 780     5003   5980   4754  -1551   1141    348       C  
ATOM    569  CG2 ILE A 780      -5.835 196.398  34.324  1.00 40.10           C  
ANISOU  569  CG2 ILE A 780     5021   5549   4664  -1376   1010    294       C  
ATOM    570  CD1 ILE A 780      -7.171 195.650  37.008  1.00 43.54           C  
ANISOU  570  CD1 ILE A 780     5379   6189   4973  -1496   1217    506       C  
ATOM    571  N   CYS A 781      -9.286 193.967  33.011  1.00 40.17           N  
ANISOU  571  N   CYS A 781     4868   5599   4794  -2067   1197    148       N  
ATOM    572  CA ACYS A 781     -10.400 193.068  33.173  0.70 42.90           C  
ANISOU  572  CA ACYS A 781     5163   5971   5164  -2310   1300    145       C  
ATOM    573  CA BCYS A 781     -10.406 193.050  33.184  0.30 44.11           C  
ANISOU  573  CA BCYS A 781     5317   6123   5318  -2313   1302    147       C  
ATOM    574  C   CYS A 781      -9.944 191.935  34.086  1.00 44.56           C  
ANISOU  574  C   CYS A 781     5543   5965   5421  -2356   1441    295       C  
ATOM    575  O   CYS A 781      -8.865 191.378  33.867  1.00 45.74           O  
ANISOU  575  O   CYS A 781     5872   5872   5632  -2293   1464    337       O  
ATOM    576  CB ACYS A 781     -10.832 192.489  31.826  0.70 44.07           C  
ANISOU  576  CB ACYS A 781     5301   6075   5366  -2511   1285     -2       C  
ATOM    577  CB BCYS A 781     -10.854 192.452  31.856  0.30 46.48           C  
ANISOU  577  CB BCYS A 781     5608   6378   5673  -2517   1290      0       C  
ATOM    578  SG ACYS A 781     -12.254 191.414  31.988  0.70 46.71           S  
ANISOU  578  SG ACYS A 781     5554   6459   5732  -2846   1412    -29       S  
ATOM    579  SG BCYS A 781     -11.479 193.690  30.721  0.30 49.23           S  
ANISOU  579  SG BCYS A 781     5737   7011   5954  -2473   1126   -145       S  
ATOM    580  N   LEU A 782     -10.737 191.650  35.091  1.00 45.26           N  
ANISOU  580  N   LEU A 782     5567   6151   5479  -2446   1537    386       N  
ATOM    581  CA  LEU A 782     -10.399 190.659  36.107  1.00 50.01           C  
ANISOU  581  CA  LEU A 782     6309   6584   6108  -2475   1679    567       C  
ATOM    582  C   LEU A 782     -11.080 189.357  35.745  1.00 54.93           C  
ANISOU  582  C   LEU A 782     6987   7045   6837  -2758   1810    547       C  
ATOM    583  O   LEU A 782     -12.190 189.101  36.153  1.00 59.25           O  
ANISOU  583  O   LEU A 782     7423   7719   7369  -2933   1885    557       O  
ATOM    584  CB  LEU A 782     -10.884 191.109  37.476  1.00 49.59           C  
ANISOU  584  CB  LEU A 782     6150   6746   5942  -2417   1720    686       C  
ATOM    585  CG  LEU A 782     -10.336 192.450  37.943  1.00 49.15           C  
ANISOU  585  CG  LEU A 782     6028   6869   5775  -2163   1607    680       C  
ATOM    586  CD1 LEU A 782     -10.939 192.741  39.305  1.00 53.27           C  
ANISOU  586  CD1 LEU A 782     6449   7607   6182  -2146   1676    779       C  
ATOM    587  CD2 LEU A 782      -8.825 192.460  37.988  1.00 47.87           C  
ANISOU  587  CD2 LEU A 782     6030   6537   5620  -1973   1563    752       C  
ATOM    588  N   THR A 783     -10.381 188.549  34.968  1.00 62.72           N  
ANISOU  588  N   THR A 783     8146   7747   7935  -2801   1845    511       N  
ATOM    589  CA  THR A 783     -10.853 187.212  34.583  1.00 71.51           C  
ANISOU  589  CA  THR A 783     9356   8639   9175  -3074   1992    477       C  
ATOM    590  C   THR A 783      -9.984 186.202  35.316  1.00 77.27           C  
ANISOU  590  C   THR A 783    10306   9060   9993  -3010   2140    685       C  
ATOM    591  O   THR A 783      -9.186 186.603  36.176  1.00 80.10           O  
ANISOU  591  O   THR A 783    10700   9448  10284  -2771   2113    853       O  
ATOM    592  CB  THR A 783     -10.726 187.015  33.051  1.00 72.46           C  
ANISOU  592  CB  THR A 783     9513   8655   9360  -3182   1937    255       C  
ATOM    593  CG2 THR A 783     -11.950 187.565  32.364  1.00 74.15           C  
ANISOU  593  CG2 THR A 783     9501   9164   9507  -3352   1848     73       C  
ATOM    594  OG1 THR A 783      -9.572 187.719  32.565  1.00 67.10           O  
ANISOU  594  OG1 THR A 783     8891   7948   8654  -2931   1812    231       O  
ATOM    595  N   SER A 784     -10.139 184.913  34.989  1.00 80.86           N  
ANISOU  595  N   SER A 784    10902   9225  10594  -3221   2299    675       N  
ATOM    596  CA  SER A 784      -9.215 183.868  35.433  1.00 81.95           C  
ANISOU  596  CA  SER A 784    11273   9010  10853  -3146   2451    863       C  
ATOM    597  C   SER A 784      -7.798 184.422  35.509  1.00 80.32           C  
ANISOU  597  C   SER A 784    11141   8770  10605  -2815   2350    950       C  
ATOM    598  O   SER A 784      -7.140 184.288  36.540  1.00 80.96           O  
ANISOU  598  O   SER A 784    11288   8812  10659  -2636   2397   1191       O  
ATOM    599  CB  SER A 784      -9.265 182.669  34.472  1.00 84.86           C  
ANISOU  599  CB  SER A 784    11801   9035  11404  -3372   2588    731       C  
ATOM    600  N   THR A 785      -7.357 185.038  34.403  1.00 76.18           N  
ANISOU  600  N   THR A 785    10595   8281  10066  -2746   2212    756       N  
ATOM    601  CA  THR A 785      -6.117 185.808  34.320  1.00 72.59           C  
ANISOU  601  CA  THR A 785    10164   7862   9552  -2452   2084    791       C  
ATOM    602  C   THR A 785      -6.479 187.301  34.145  1.00 68.91           C  
ANISOU  602  C   THR A 785     9491   7756   8934  -2375   1889    669       C  
ATOM    603  O   THR A 785      -7.465 187.641  33.478  1.00 69.00           O  
ANISOU  603  O   THR A 785     9371   7924   8920  -2541   1835    493       O  
ATOM    604  CB  THR A 785      -5.248 185.370  33.120  1.00 68.62           C  
ANISOU  604  CB  THR A 785     9806   7106   9160  -2423   2090    666       C  
ATOM    605  N   VAL A 786      -5.687 188.182  34.753  1.00 62.68           N  
ANISOU  605  N   VAL A 786     8668   7100   8046  -2124   1791    768       N  
ATOM    606  CA  VAL A 786      -5.849 189.615  34.569  1.00 56.84           C  
ANISOU  606  CA  VAL A 786     7762   6647   7186  -2023   1622    658       C  
ATOM    607  C   VAL A 786      -5.472 190.040  33.131  1.00 55.85           C  
ANISOU  607  C   VAL A 786     7638   6492   7091  -2004   1514    466       C  
ATOM    608  O   VAL A 786      -4.405 189.670  32.634  1.00 58.44           O  
ANISOU  608  O   VAL A 786     8101   6619   7483  -1911   1522    474       O  
ATOM    609  CB  VAL A 786      -4.984 190.388  35.571  1.00 55.98           C  
ANISOU  609  CB  VAL A 786     7638   6659   6972  -1776   1559    796       C  
ATOM    610  CG1 VAL A 786      -4.957 191.881  35.242  1.00 54.72           C  
ANISOU  610  CG1 VAL A 786     7338   6733   6720  -1657   1396    666       C  
ATOM    611  CG2 VAL A 786      -5.471 190.124  36.998  1.00 59.26           C  
ANISOU  611  CG2 VAL A 786     8021   7176   7318  -1797   1652    973       C  
ATOM    612  N   GLN A 787      -6.343 190.840  32.500  1.00 51.61           N  
ANISOU  612  N   GLN A 787     6938   6170   6499  -2080   1417    311       N  
ATOM    613  CA  GLN A 787      -6.120 191.380  31.156  1.00 48.74           C  
ANISOU  613  CA  GLN A 787     6543   5839   6135  -2062   1304    143       C  
ATOM    614  C   GLN A 787      -5.885 192.875  31.246  1.00 46.42           C  
ANISOU  614  C   GLN A 787     6125   5764   5746  -1865   1160    131       C  
ATOM    615  O   GLN A 787      -6.628 193.564  31.964  1.00 43.82           O  
ANISOU  615  O   GLN A 787     5658   5643   5348  -1848   1139    159       O  
ATOM    616  CB  GLN A 787      -7.355 191.146  30.292  1.00 53.36           C  
ANISOU  616  CB  GLN A 787     7021   6527   6726  -2306   1302    -16       C  
ATOM    617  CG  GLN A 787      -7.602 189.700  29.911  1.00 56.17           C  
ANISOU  617  CG  GLN A 787     7503   6651   7188  -2541   1443    -66       C  
ATOM    618  CD  GLN A 787      -8.988 189.461  29.354  1.00 60.52           C  
ANISOU  618  CD  GLN A 787     7914   7356   7723  -2816   1451   -210       C  
ATOM    619  NE2 GLN A 787      -9.053 188.910  28.158  1.00 62.95           N  
ANISOU  619  NE2 GLN A 787     8267   7583   8068  -2980   1458   -382       N  
ATOM    620  OE1 GLN A 787      -9.988 189.717  30.009  1.00 68.56           O  
ANISOU  620  OE1 GLN A 787     8785   8570   8693  -2889   1459   -170       O  
ATOM    621  N   LEU A 788      -4.835 193.353  30.568  1.00 43.61           N  
ANISOU  621  N   LEU A 788     5825   5348   5394  -1717   1079     95       N  
ATOM    622  CA  LEU A 788      -4.621 194.773  30.330  1.00 41.72           C  
ANISOU  622  CA  LEU A 788     5476   5286   5087  -1559    946     53       C  
ATOM    623  C   LEU A 788      -5.186 195.158  28.948  1.00 41.84           C  
ANISOU  623  C   LEU A 788     5398   5403   5093  -1641    864    -97       C  
ATOM    624  O   LEU A 788      -4.937 194.443  27.981  1.00 40.92           O  
ANISOU  624  O   LEU A 788     5365   5162   5020  -1735    883   -176       O  
ATOM    625  CB  LEU A 788      -3.148 195.101  30.385  1.00 42.60           C  
ANISOU  625  CB  LEU A 788     5690   5292   5203  -1361    906    109       C  
ATOM    626  CG  LEU A 788      -2.253 194.626  31.513  1.00 46.28           C  
ANISOU  626  CG  LEU A 788     6263   5647   5671  -1257    971    265       C  
ATOM    627  CD1 LEU A 788      -0.878 195.275  31.431  1.00 45.12           C  
ANISOU  627  CD1 LEU A 788     6159   5475   5507  -1059    897    292       C  
ATOM    628  CD2 LEU A 788      -2.890 194.910  32.848  1.00 50.91           C  
ANISOU  628  CD2 LEU A 788     6769   6386   6188  -1254   1002    352       C  
ATOM    629  N   ILE A 789      -5.949 196.261  28.871  1.00 38.64           N  
ANISOU  629  N   ILE A 789     4819   5232   4629  -1601    783   -133       N  
ATOM    630  CA  ILE A 789      -6.658 196.686  27.652  1.00 38.35           C  
ANISOU  630  CA  ILE A 789     4655   5350   4564  -1673    703   -245       C  
ATOM    631  C   ILE A 789      -6.097 198.061  27.315  1.00 36.09           C  
ANISOU  631  C   ILE A 789     4315   5145   4249  -1463    595   -238       C  
ATOM    632  O   ILE A 789      -5.941 198.904  28.200  1.00 34.91           O  
ANISOU  632  O   ILE A 789     4130   5046   4086  -1318    585   -175       O  
ATOM    633  CB  ILE A 789      -8.192 196.718  27.831  1.00 41.17           C  
ANISOU  633  CB  ILE A 789     4831   5923   4888  -1815    716   -273       C  
ATOM    634  CG1 ILE A 789      -8.794 195.292  27.885  1.00 45.29           C  
ANISOU  634  CG1 ILE A 789     5403   6358   5447  -2071    825   -307       C  
ATOM    635  CG2 ILE A 789      -8.882 197.388  26.646  1.00 40.39           C  
ANISOU  635  CG2 ILE A 789     4566   6039   4740  -1839    613   -359       C  
ATOM    636  CD1 ILE A 789      -8.769 194.680  29.249  1.00 48.45           C  
ANISOU  636  CD1 ILE A 789     5880   6649   5877  -2087    941   -192       C  
ATOM    637  N   THR A 790      -5.662 198.243  26.068  1.00 35.03           N  
ANISOU  637  N   THR A 790     4198   5003   4109  -1449    527   -303       N  
ATOM    638  CA  THR A 790      -4.991 199.478  25.651  1.00 32.27           C  
ANISOU  638  CA  THR A 790     3820   4695   3744  -1258    437   -286       C  
ATOM    639  C   THR A 790      -5.400 199.747  24.205  1.00 32.29           C  
ANISOU  639  C   THR A 790     3732   4832   3704  -1309    358   -359       C  
ATOM    640  O   THR A 790      -5.951 198.894  23.550  1.00 30.83           O  
ANISOU  640  O   THR A 790     3535   4681   3498  -1490    374   -438       O  
ATOM    641  CB  THR A 790      -3.467 199.362  25.780  1.00 32.85           C  
ANISOU  641  CB  THR A 790     4060   4566   3852  -1141    448   -249       C  
ATOM    642  CG2 THR A 790      -2.869 198.371  24.757  1.00 32.76           C  
ANISOU  642  CG2 THR A 790     4170   4416   3860  -1232    469   -315       C  
ATOM    643  OG1 THR A 790      -2.865 200.669  25.653  1.00 35.10           O  
ANISOU  643  OG1 THR A 790     4309   4895   4129   -961    374   -222       O  
ATOM    644  N   GLN A 791      -5.144 200.947  23.732  1.00 30.72           N  
ANISOU  644  N   GLN A 791     3465   4717   3488  -1154    279   -330       N  
ATOM    645  CA  GLN A 791      -5.476 201.351  22.369  1.00 32.47           C  
ANISOU  645  CA  GLN A 791     3588   5094   3653  -1170    197   -367       C  
ATOM    646  C   GLN A 791      -4.766 200.433  21.394  1.00 31.62           C  
ANISOU  646  C   GLN A 791     3606   4879   3527  -1273    203   -448       C  
ATOM    647  O   GLN A 791      -3.582 200.192  21.573  1.00 31.97           O  
ANISOU  647  O   GLN A 791     3805   4724   3615  -1204    236   -435       O  
ATOM    648  CB  GLN A 791      -4.931 202.778  22.170  1.00 33.94           C  
ANISOU  648  CB  GLN A 791     3738   5304   3851   -954    135   -293       C  
ATOM    649  CG  GLN A 791      -4.919 203.311  20.732  1.00 38.73           C  
ANISOU  649  CG  GLN A 791     4273   6042   4399   -924     51   -293       C  
ATOM    650  CD  GLN A 791      -4.234 204.681  20.642  1.00 40.48           C  
ANISOU  650  CD  GLN A 791     4490   6231   4657   -711     14   -205       C  
ATOM    651  NE2 GLN A 791      -4.757 205.547  19.791  1.00 40.94           N  
ANISOU  651  NE2 GLN A 791     4411   6465   4678   -639    -48   -149       N  
ATOM    652  OE1 GLN A 791      -3.258 204.953  21.349  1.00 39.73           O  
ANISOU  652  OE1 GLN A 791     4508   5961   4624   -615     48   -183       O  
ATOM    653  N   LEU A 792      -5.431 200.018  20.339  1.00 32.89           N  
ANISOU  653  N   LEU A 792     3691   5186   3616  -1423    170   -532       N  
ATOM    654  CA  LEU A 792      -4.793 199.229  19.286  1.00 35.54           C  
ANISOU  654  CA  LEU A 792     4138   5444   3921  -1523    179   -633       C  
ATOM    655  C   LEU A 792      -3.857 200.123  18.468  1.00 36.50           C  
ANISOU  655  C   LEU A 792     4276   5578   4012  -1358    111   -591       C  
ATOM    656  O   LEU A 792      -4.231 201.209  18.059  1.00 34.98           O  
ANISOU  656  O   LEU A 792     3946   5571   3774  -1256     29   -522       O  
ATOM    657  CB  LEU A 792      -5.846 198.566  18.401  1.00 38.02           C  
ANISOU  657  CB  LEU A 792     4349   5948   4147  -1754    162   -755       C  
ATOM    658  CG  LEU A 792      -5.337 197.689  17.261  1.00 40.43           C  
ANISOU  658  CG  LEU A 792     4761   6197   4404  -1892    183   -899       C  
ATOM    659  CD1 LEU A 792      -4.592 196.445  17.770  1.00 40.46           C  
ANISOU  659  CD1 LEU A 792     4984   5875   4511  -1967    316   -960       C  
ATOM    660  CD2 LEU A 792      -6.524 197.315  16.419  1.00 43.15           C  
ANISOU  660  CD2 LEU A 792     4954   6807   4635  -2116    142  -1016       C  
ATOM    661  N   MET A 793      -2.626 199.671  18.305  1.00 33.24           N  
ANISOU  661  N   MET A 793     4032   4959   3636  -1320    154   -616       N  
ATOM    662  CA  MET A 793      -1.649 200.333  17.498  1.00 33.33           C  
ANISOU  662  CA  MET A 793     4075   4968   3620  -1191    107   -587       C  
ATOM    663  C   MET A 793      -1.556 199.538  16.206  1.00 35.85           C  
ANISOU  663  C   MET A 793     4432   5332   3855  -1337    113   -720       C  
ATOM    664  O   MET A 793      -0.799 198.580  16.119  1.00 37.13           O  
ANISOU  664  O   MET A 793     4749   5302   4056  -1389    193   -799       O  
ATOM    665  CB  MET A 793      -0.341 200.358  18.255  1.00 32.55           C  
ANISOU  665  CB  MET A 793     4120   4632   3612  -1053    158   -527       C  
ATOM    666  CG  MET A 793      -0.482 201.113  19.568  1.00 32.77           C  
ANISOU  666  CG  MET A 793     4107   4639   3702   -934    156   -421       C  
ATOM    667  SD  MET A 793      -0.700 202.896  19.383  1.00 34.58           S  
ANISOU  667  SD  MET A 793     4192   5029   3918   -764     66   -321       S  
ATOM    668  CE  MET A 793       0.985 203.334  19.238  1.00 35.00           C  
ANISOU  668  CE  MET A 793     4364   4922   4010   -623     69   -280       C  
ATOM    669  N   PRO A 794      -2.347 199.923  15.194  1.00 39.96           N  
ANISOU  669  N   PRO A 794     4806   6120   4256  -1402     32   -748       N  
ATOM    670  CA  PRO A 794      -2.590 198.970  14.105  1.00 41.48           C  
ANISOU  670  CA  PRO A 794     5014   6395   4349  -1606     46   -914       C  
ATOM    671  C   PRO A 794      -1.394 198.481  13.313  1.00 38.99           C  
ANISOU  671  C   PRO A 794     4851   5945   4017  -1600     93   -998       C  
ATOM    672  O   PRO A 794      -1.470 197.400  12.754  1.00 41.16           O  
ANISOU  672  O   PRO A 794     5198   6185   4256  -1783    154  -1166       O  
ATOM    673  CB  PRO A 794      -3.557 199.714  13.178  1.00 44.41           C  
ANISOU  673  CB  PRO A 794     5173   7126   4573  -1635    -68   -890       C  
ATOM    674  CG  PRO A 794      -4.083 200.858  13.967  1.00 44.09           C  
ANISOU  674  CG  PRO A 794     5002   7163   4584  -1470   -120   -718       C  
ATOM    675  CD  PRO A 794      -3.088 201.187  15.010  1.00 40.56           C  
ANISOU  675  CD  PRO A 794     4690   6439   4278  -1298    -66   -631       C  
ATOM    676  N   PHE A 795      -0.339 199.267  13.225  1.00 37.83           N  
ANISOU  676  N   PHE A 795     4747   5731   3894  -1404     72   -893       N  
ATOM    677  CA  PHE A 795       0.851 198.896  12.428  1.00 37.78           C  
ANISOU  677  CA  PHE A 795     4868   5620   3865  -1378    117   -961       C  
ATOM    678  C   PHE A 795       1.838 198.066  13.234  1.00 39.24           C  
ANISOU  678  C   PHE A 795     5238   5480   4190  -1335    235   -979       C  
ATOM    679  O   PHE A 795       2.845 197.622  12.721  1.00 40.32           O  
ANISOU  679  O   PHE A 795     5487   5498   4332  -1307    295  -1038       O  
ATOM    680  CB  PHE A 795       1.540 200.146  11.829  1.00 37.67           C  
ANISOU  680  CB  PHE A 795     4798   5712   3801  -1199     43   -833       C  
ATOM    681  CG  PHE A 795       0.710 200.851  10.790  1.00 39.26           C  
ANISOU  681  CG  PHE A 795     4828   6241   3846  -1233    -60   -806       C  
ATOM    682  CD1 PHE A 795      -0.272 201.763  11.175  1.00 40.14           C  
ANISOU  682  CD1 PHE A 795     4778   6516   3955  -1175   -139   -681       C  
ATOM    683  CD2 PHE A 795       0.839 200.531   9.437  1.00 44.27           C  
ANISOU  683  CD2 PHE A 795     5454   7039   4326  -1329    -73   -910       C  
ATOM    684  CE1 PHE A 795      -1.091 202.370  10.233  1.00 43.18           C  
ANISOU  684  CE1 PHE A 795     4989   7221   4194  -1195   -233   -634       C  
ATOM    685  CE2 PHE A 795       0.053 201.145   8.476  1.00 45.46           C  
ANISOU  685  CE2 PHE A 795     5433   7527   4312  -1361   -174   -871       C  
ATOM    686  CZ  PHE A 795      -0.933 202.061   8.876  1.00 46.57           C  
ANISOU  686  CZ  PHE A 795     5405   7832   4458  -1289   -257   -722       C  
ATOM    687  N   GLY A 796       1.579 197.872  14.518  1.00 37.77           N  
ANISOU  687  N   GLY A 796     5076   5159   4115  -1316    271   -916       N  
ATOM    688  CA  GLY A 796       2.399 196.949  15.309  1.00 36.23           C  
ANISOU  688  CA  GLY A 796     5047   4673   4045  -1285    388   -919       C  
ATOM    689  C   GLY A 796       3.696 197.567  15.765  1.00 33.94           C  
ANISOU  689  C   GLY A 796     4808   4272   3817  -1068    384   -792       C  
ATOM    690  O   GLY A 796       3.796 198.782  15.942  1.00 34.05           O  
ANISOU  690  O   GLY A 796     4729   4395   3813   -944    299   -682       O  
ATOM    691  N   LEU A 798       7.593 198.789  15.943  1.00 30.84           N  
ANISOU  691  N   LEU A 798     4539   3653   3524   -590    401   -569       N  
ATOM    692  CA  LEU A 798       8.413 199.552  15.034  1.00 31.65           C  
ANISOU  692  CA  LEU A 798     4609   3841   3573   -509    363   -550       C  
ATOM    693  C   LEU A 798       9.530 198.709  14.450  1.00 32.35           C  
ANISOU  693  C   LEU A 798     4803   3809   3678   -475    457   -613       C  
ATOM    694  O   LEU A 798       9.854 198.866  13.258  1.00 30.90           O  
ANISOU  694  O   LEU A 798     4610   3717   3413   -489    453   -672       O  
ATOM    695  CB  LEU A 798       8.943 200.798  15.726  1.00 31.47           C  
ANISOU  695  CB  LEU A 798     4520   3850   3586   -372    299   -413       C  
ATOM    696  CG  LEU A 798       9.726 201.797  14.871  1.00 29.56           C  
ANISOU  696  CG  LEU A 798     4230   3700   3299   -294    257   -368       C  
ATOM    697  CD1 LEU A 798       8.968 202.257  13.631  1.00 31.04           C  
ANISOU  697  CD1 LEU A 798     4346   4070   3377   -364    203   -401       C  
ATOM    698  CD2 LEU A 798      10.114 202.967  15.764  1.00 31.97           C  
ANISOU  698  CD2 LEU A 798     4478   4006   3661   -189    208   -251       C  
ATOM    699  N   LEU A 799      10.050 197.751  15.224  1.00 32.08           N  
ANISOU  699  N   LEU A 799     4867   3580   3742   -435    550   -602       N  
ATOM    700  CA  LEU A 799      11.080 196.860  14.707  1.00 33.53           C  
ANISOU  700  CA  LEU A 799     5152   3629   3958   -388    660   -660       C  
ATOM    701  C   LEU A 799      10.609 196.090  13.462  1.00 33.53           C  
ANISOU  701  C   LEU A 799     5205   3642   3890   -534    719   -846       C  
ATOM    702  O   LEU A 799      11.248 196.110  12.428  1.00 33.55           O  
ANISOU  702  O   LEU A 799     5220   3693   3833   -514    744   -912       O  
ATOM    703  CB  LEU A 799      11.566 195.882  15.787  1.00 33.03           C  
ANISOU  703  CB  LEU A 799     5183   3347   4019   -315    760   -599       C  
ATOM    704  CG  LEU A 799      12.672 194.922  15.303  1.00 34.30           C  
ANISOU  704  CG  LEU A 799     5448   3348   4235   -236    893   -645       C  
ATOM    705  CD1 LEU A 799      13.907 195.680  14.824  1.00 34.93           C  
ANISOU  705  CD1 LEU A 799     5469   3520   4280    -97    861   -590       C  
ATOM    706  CD2 LEU A 799      13.021 193.977  16.434  1.00 37.90           C  
ANISOU  706  CD2 LEU A 799     5987   3594   4818   -153    992   -551       C  
ATOM    707  N   ASP A 800       9.480 195.406  13.572  1.00 36.29           N  
ANISOU  707  N   ASP A 800     5584   3962   4243   -694    744   -938       N  
ATOM    708  CA  ASP A 800       8.879 194.715  12.433  1.00 39.61           C  
ANISOU  708  CA  ASP A 800     6039   4426   4582   -872    791  -1138       C  
ATOM    709  C   ASP A 800       8.504 195.652  11.313  1.00 38.83           C  
ANISOU  709  C   ASP A 800     5822   4611   4319   -923    679  -1174       C  
ATOM    710  O   ASP A 800       8.617 195.283  10.120  1.00 37.16           O  
ANISOU  710  O   ASP A 800     5636   4471   4009  -1006    718  -1323       O  
ATOM    711  CB  ASP A 800       7.609 193.945  12.855  1.00 45.81           C  
ANISOU  711  CB  ASP A 800     6848   5159   5397  -1058    823  -1221       C  
ATOM    712  CG  ASP A 800       7.923 192.648  13.629  1.00 52.65           C  
ANISOU  712  CG  ASP A 800     7869   5712   6422  -1053    982  -1231       C  
ATOM    713  OD1 ASP A 800       9.114 192.317  13.817  1.00 53.83           O  
ANISOU  713  OD1 ASP A 800     8102   5694   6656   -893   1066  -1174       O  
ATOM    714  OD2 ASP A 800       6.975 191.940  14.028  1.00 58.15           O1-
ANISOU  714  OD2 ASP A 800     8599   6331   7162  -1208   1031  -1291       O1-
ATOM    715  N   TYR A 801       7.983 196.814  11.673  1.00 35.74           N  
ANISOU  715  N   TYR A 801     5302   4386   3891   -883    549  -1043       N  
ATOM    716  CA  TYR A 801       7.585 197.793  10.657  1.00 35.97           C  
ANISOU  716  CA  TYR A 801     5207   4689   3770   -908    441  -1034       C  
ATOM    717  C   TYR A 801       8.801 198.204   9.818  1.00 35.88           C  
ANISOU  717  C   TYR A 801     5209   4713   3709   -797    455  -1012       C  
ATOM    718  O   TYR A 801       8.718 198.210   8.583  1.00 37.64           O  
ANISOU  718  O   TYR A 801     5406   5104   3792   -871    446  -1104       O  
ATOM    719  CB  TYR A 801       6.924 199.030  11.304  1.00 34.70           C  
ANISOU  719  CB  TYR A 801     4913   4656   3613   -846    321   -873       C  
ATOM    720  CG  TYR A 801       6.382 199.992  10.307  1.00 34.34           C  
ANISOU  720  CG  TYR A 801     4735   4885   3425   -864    218   -839       C  
ATOM    721  CD1 TYR A 801       5.124 199.800   9.743  1.00 39.09           C  
ANISOU  721  CD1 TYR A 801     5250   5685   3913  -1021    170   -921       C  
ATOM    722  CD2 TYR A 801       7.143 201.044   9.880  1.00 36.56           C  
ANISOU  722  CD2 TYR A 801     4972   5238   3679   -730    175   -720       C  
ATOM    723  CE1 TYR A 801       4.643 200.654   8.764  1.00 39.58           C  
ANISOU  723  CE1 TYR A 801     5180   6030   3830  -1025     74   -870       C  
ATOM    724  CE2 TYR A 801       6.699 201.902   8.906  1.00 37.51           C  
ANISOU  724  CE2 TYR A 801     4976   5607   3666   -734     92   -665       C  
ATOM    725  CZ  TYR A 801       5.441 201.709   8.372  1.00 39.15           C  
ANISOU  725  CZ  TYR A 801     5093   6023   3757   -872     39   -731       C  
ATOM    726  OH  TYR A 801       5.007 202.579   7.451  1.00 38.34           O  
ANISOU  726  OH  TYR A 801     4862   6184   3519   -857    -45   -646       O  
ATOM    727  N   VAL A 802       9.931 198.508  10.456  1.00 35.01           N  
ANISOU  727  N   VAL A 802     5133   4468   3701   -632    481   -897       N  
ATOM    728  CA  VAL A 802      11.136 198.921   9.667  1.00 36.77           C  
ANISOU  728  CA  VAL A 802     5357   4734   3880   -529    501   -870       C  
ATOM    729  C   VAL A 802      11.701 197.780   8.830  1.00 39.03           C  
ANISOU  729  C   VAL A 802     5748   4944   4136   -575    626  -1038       C  
ATOM    730  O   VAL A 802      12.172 198.038   7.715  1.00 38.03           O  
ANISOU  730  O   VAL A 802     5599   4951   3896   -571    632  -1078       O  
ATOM    731  CB  VAL A 802      12.279 199.617  10.444  1.00 37.54           C  
ANISOU  731  CB  VAL A 802     5439   4745   4077   -353    493   -711       C  
ATOM    732  CG1 VAL A 802      11.771 200.878  11.135  1.00 38.18           C  
ANISOU  732  CG1 VAL A 802     5418   4910   4179   -313    380   -566       C  
ATOM    733  CG2 VAL A 802      12.988 198.712  11.430  1.00 39.97           C  
ANISOU  733  CG2 VAL A 802     5841   4821   4521   -277    588   -703       C  
ATOM    734  N   ARG A 803      11.583 196.533   9.312  1.00 38.51           N  
ANISOU  734  N   ARG A 803     5797   4670   4165   -626    733  -1141       N  
ATOM    735  CA  ARG A 803      12.016 195.390   8.521  1.00 40.83           C  
ANISOU  735  CA  ARG A 803     6204   4862   4445   -680    874  -1326       C  
ATOM    736  C   ARG A 803      11.103 195.172   7.309  1.00 41.99           C  
ANISOU  736  C   ARG A 803     6329   5203   4422   -880    856  -1512       C  
ATOM    737  O   ARG A 803      11.603 194.960   6.208  1.00 41.92           O  
ANISOU  737  O   ARG A 803     6344   5272   4310   -901    913  -1631       O  
ATOM    738  CB  ARG A 803      12.109 194.114   9.371  1.00 41.80           C  
ANISOU  738  CB  ARG A 803     6464   4683   4734   -678   1010  -1374       C  
ATOM    739  CG  ARG A 803      13.173 194.164  10.448  1.00 41.14           C  
ANISOU  739  CG  ARG A 803     6403   4431   4797   -469   1044  -1197       C  
ATOM    740  CD  ARG A 803      13.066 192.981  11.424  1.00 41.93           C  
ANISOU  740  CD  ARG A 803     6623   4250   5058   -465   1164  -1197       C  
ATOM    741  NE  ARG A 803      14.220 192.936  12.323  1.00 41.89           N  
ANISOU  741  NE  ARG A 803     6631   4112   5172   -250   1206  -1027       N  
ATOM    742  CZ  ARG A 803      14.410 192.056  13.313  1.00 43.29           C  
ANISOU  742  CZ  ARG A 803     6894   4059   5494   -180   1305   -953       C  
ATOM    743  NH1 ARG A 803      13.520 191.117  13.564  1.00 43.39           N1+
ANISOU  743  NH1 ARG A 803     7002   3915   5569   -315   1385  -1037       N1+
ATOM    744  NH2 ARG A 803      15.510 192.119  14.051  1.00 43.73           N  
ANISOU  744  NH2 ARG A 803     6932   4052   5629     23   1325   -785       N  
ATOM    745  N   GLU A 804       9.781 195.216   7.523  1.00 41.12           N  
ANISOU  745  N   GLU A 804     6161   5189   4272  -1029    780  -1540       N  
ATOM    746  CA  GLU A 804       8.784 195.040   6.468  1.00 43.59           C  
ANISOU  746  CA  GLU A 804     6423   5729   4409  -1237    744  -1709       C  
ATOM    747  C   GLU A 804       8.824 196.158   5.409  1.00 44.21           C  
ANISOU  747  C   GLU A 804     6368   6134   4296  -1209    630  -1644       C  
ATOM    748  O   GLU A 804       8.533 195.899   4.260  1.00 49.46           O  
ANISOU  748  O   GLU A 804     7014   6990   4789  -1343    635  -1800       O  
ATOM    749  CB  GLU A 804       7.364 194.920   7.066  1.00 43.85           C  
ANISOU  749  CB  GLU A 804     6396   5810   4453  -1387    680  -1721       C  
ATOM    750  N   HIS A 805       9.202 197.378   5.766  1.00 41.56           N  
ANISOU  750  N   HIS A 805     5944   5861   3983  -1044    536  -1418       N  
ATOM    751  CA  HIS A 805       9.145 198.506   4.820  1.00 43.20           C  
ANISOU  751  CA  HIS A 805     6022   6367   4023  -1013    431  -1320       C  
ATOM    752  C   HIS A 805      10.496 199.115   4.546  1.00 42.87           C  
ANISOU  752  C   HIS A 805     5991   6299   3995   -844    459  -1209       C  
ATOM    753  O   HIS A 805      10.584 200.285   4.218  1.00 44.64           O  
ANISOU  753  O   HIS A 805     6113   6691   4156   -766    372  -1045       O  
ATOM    754  CB  HIS A 805       8.217 199.573   5.367  1.00 42.54           C  
ANISOU  754  CB  HIS A 805     5803   6412   3946   -982    294  -1142       C  
ATOM    755  CG  HIS A 805       6.822 199.085   5.522  1.00 47.02           C  
ANISOU  755  CG  HIS A 805     6324   7068   4473  -1154    255  -1240       C  
ATOM    756  CD2 HIS A 805       5.821 198.943   4.622  1.00 48.01           C  
ANISOU  756  CD2 HIS A 805     6356   7468   4415  -1320    198  -1343       C  
ATOM    757  ND1 HIS A 805       6.367 198.525   6.691  1.00 44.48           N  
ANISOU  757  ND1 HIS A 805     6052   6544   4301  -1188    287  -1259       N  
ATOM    758  CE1 HIS A 805       5.120 198.126   6.532  1.00 46.44           C  
ANISOU  758  CE1 HIS A 805     6237   6934   4474  -1366    251  -1361       C  
ATOM    759  NE2 HIS A 805       4.757 198.392   5.294  1.00 48.64           N  
ANISOU  759  NE2 HIS A 805     6420   7511   4549  -1449    191  -1413       N  
ATOM    760  N   LYS A 806      11.528 198.304   4.711  1.00 44.18           N  
ANISOU  760  N   LYS A 806     6281   6247   4258   -788    588  -1290       N  
ATOM    761  CA  LYS A 806      12.953 198.663   4.622  1.00 48.41           C  
ANISOU  761  CA  LYS A 806     6836   6716   4839   -624    641  -1199       C  
ATOM    762  C   LYS A 806      13.268 199.481   3.387  1.00 50.93           C  
ANISOU  762  C   LYS A 806     7071   7299   4981   -613    600  -1152       C  
ATOM    763  O   LYS A 806      14.044 200.404   3.424  1.00 52.15           O  
ANISOU  763  O   LYS A 806     7174   7481   5160   -487    574   -986       O  
ATOM    764  CB  LYS A 806      13.684 197.331   4.450  1.00 59.11           C  
ANISOU  764  CB  LYS A 806     8330   7876   6250   -628    808  -1380       C  
ATOM    765  CG  LYS A 806      15.079 197.219   4.993  1.00 65.82           C  
ANISOU  765  CG  LYS A 806     9230   8535   7243   -445    895  -1297       C  
ATOM    766  CD  LYS A 806      15.350 195.793   5.501  1.00 71.91           C  
ANISOU  766  CD  LYS A 806    10146   9021   8156   -438   1048  -1427       C  
ATOM    767  CE  LYS A 806      14.884 194.703   4.550  1.00 75.51           C  
ANISOU  767  CE  LYS A 806    10694   9473   8523   -601   1155  -1693       C  
ATOM    768  NZ  LYS A 806      15.866 194.487   3.459  1.00 84.20           N1+
ANISOU  768  NZ  LYS A 806    11820  10635   9536   -554   1261  -1796       N1+
ATOM    769  N   ASP A 807      12.676 199.066   2.277  1.00 48.76           N  
ANISOU  769  N   ASP A 807     6785   7220   4519   -759    605  -1309       N  
ATOM    770  CA  ASP A 807      12.899 199.670   0.977  1.00 54.33           C  
ANISOU  770  CA  ASP A 807     7414   8210   5017   -770    578  -1285       C  
ATOM    771  C   ASP A 807      12.154 200.976   0.758  1.00 52.59           C  
ANISOU  771  C   ASP A 807     7044   8236   4701   -757    426  -1082       C  
ATOM    772  O   ASP A 807      12.411 201.658  -0.205  1.00 53.82           O  
ANISOU  772  O   ASP A 807     7126   8619   4702   -735    398   -998       O  
ATOM    773  CB  ASP A 807      12.490 198.676  -0.122  1.00 58.24           C  
ANISOU  773  CB  ASP A 807     7950   8849   5327   -949    642  -1551       C  
ATOM    774  CG  ASP A 807      13.373 197.433  -0.146  1.00 62.08           C  
ANISOU  774  CG  ASP A 807     8592   9096   5898   -943    823  -1757       C  
ATOM    775  OD1 ASP A 807      14.565 197.518   0.244  1.00 62.61           O  
ANISOU  775  OD1 ASP A 807     8702   8989   6097   -777    897  -1670       O  
ATOM    776  OD2 ASP A 807      12.875 196.364  -0.565  1.00 69.57           O1-
ANISOU  776  OD2 ASP A 807     9615  10033   6784  -1107    899  -2011       O1-
ATOM    777  N   ASN A 808      11.235 201.315   1.640  1.00 50.98           N  
ANISOU  777  N   ASN A 808     6793   7988   4589   -764    338   -995       N  
ATOM    778  CA  ASN A 808      10.443 202.519   1.500  1.00 54.03           C  
ANISOU  778  CA  ASN A 808     7036   8586   4906   -736    206   -799       C  
ATOM    779  C   ASN A 808      10.563 203.522   2.616  1.00 50.69           C  
ANISOU  779  C   ASN A 808     6581   8006   4670   -593    157   -586       C  
ATOM    780  O   ASN A 808       9.787 204.464   2.664  1.00 58.12           O  
ANISOU  780  O   ASN A 808     7413   9078   5589   -563     62   -431       O  
ATOM    781  CB  ASN A 808       8.972 202.156   1.409  1.00 59.84           C  
ANISOU  781  CB  ASN A 808     7705   9485   5546   -888    133   -888       C  
ATOM    782  CG  ASN A 808       8.465 202.327   0.023  1.00 69.30           C  
ANISOU  782  CG  ASN A 808     8800  11054   6476   -983     78   -915       C  
ATOM    783  ND2 ASN A 808       8.753 201.351  -0.832  1.00 72.14           N  
ANISOU  783  ND2 ASN A 808     9226  11484   6697  -1108    158  -1144       N  
ATOM    784  OD1 ASN A 808       7.905 203.371  -0.312  1.00 79.13           O  
ANISOU  784  OD1 ASN A 808     9906  12524   7633   -931    -26   -720       O  
ATOM    785  N   ILE A 809      11.469 203.303   3.548  1.00 42.66           N  
ANISOU  785  N   ILE A 809     5655   6717   3835   -507    225   -582       N  
ATOM    786  CA  ILE A 809      11.572 204.201   4.659  1.00 41.82           C  
ANISOU  786  CA  ILE A 809     5522   6472   3897   -394    183   -412       C  
ATOM    787  C   ILE A 809      12.638 205.226   4.302  1.00 39.13           C  
ANISOU  787  C   ILE A 809     5149   6151   3566   -280    194   -255       C  
ATOM    788  O   ILE A 809      13.766 204.870   3.998  1.00 40.18           O  
ANISOU  788  O   ILE A 809     5337   6228   3701   -247    275   -300       O  
ATOM    789  CB  ILE A 809      11.866 203.456   5.973  1.00 41.36           C  
ANISOU  789  CB  ILE A 809     5557   6138   4017   -372    238   -480       C  
ATOM    790  CG1 ILE A 809      10.588 202.699   6.400  1.00 42.67           C  
ANISOU  790  CG1 ILE A 809     5731   6298   4182   -491    214   -590       C  
ATOM    791  CG2 ILE A 809      12.282 204.431   7.062  1.00 40.52           C  
ANISOU  791  CG2 ILE A 809     5425   5903   4067   -251    208   -316       C  
ATOM    792  CD1 ILE A 809      10.794 201.726   7.531  1.00 40.75           C  
ANISOU  792  CD1 ILE A 809     5592   5801   4089   -492    285   -670       C  
ATOM    793  N   GLY A 810      12.227 206.486   4.381  1.00 36.77           N  
ANISOU  793  N   GLY A 810     4761   5924   3286   -221    121    -69       N  
ATOM    794  CA  GLY A 810      13.063 207.633   4.138  1.00 36.81           C  
ANISOU  794  CA  GLY A 810     4729   5933   3324   -124    129    104       C  
ATOM    795  C   GLY A 810      13.572 208.335   5.383  1.00 32.75           C  
ANISOU  795  C   GLY A 810     4228   5200   3014    -38    134    196       C  
ATOM    796  O   GLY A 810      13.214 208.010   6.517  1.00 30.86           O  
ANISOU  796  O   GLY A 810     4020   4816   2888    -40    123    142       O  
ATOM    797  N   SER A 811      14.410 209.331   5.147  1.00 32.36           N  
ANISOU  797  N   SER A 811     4151   5140   3003     26    155    336       N  
ATOM    798  CA  SER A 811      15.131 209.984   6.224  1.00 31.61           C  
ANISOU  798  CA  SER A 811     4069   4852   3087     86    174    399       C  
ATOM    799  C   SER A 811      14.199 210.774   7.142  1.00 30.76           C  
ANISOU  799  C   SER A 811     3929   4667   3091    113    120    472       C  
ATOM    800  O   SER A 811      14.436 210.836   8.355  1.00 29.77           O  
ANISOU  800  O   SER A 811     3831   4378   3101    131    127    441       O  
ATOM    801  CB  SER A 811      16.257 210.889   5.668  1.00 31.70           C  
ANISOU  801  CB  SER A 811     4053   4879   3112    126    221    525       C  
ATOM    802  OG  SER A 811      15.785 211.773   4.644  1.00 29.47           O  
ANISOU  802  OG  SER A 811     3707   4749   2737    139    199    678       O  
ATOM    803  N   GLN A 812      13.127 211.316   6.575  1.00 29.90           N  
ANISOU  803  N   GLN A 812     3755   4690   2914    119     70    564       N  
ATOM    804  CA  GLN A 812      12.159 212.082   7.340  1.00 36.11           C  
ANISOU  804  CA  GLN A 812     4500   5417   3801    160     29    639       C  
ATOM    805  C   GLN A 812      11.470 211.220   8.394  1.00 32.84           C  
ANISOU  805  C   GLN A 812     4116   4930   3431    119      6    499       C  
ATOM    806  O   GLN A 812      11.405 211.598   9.559  1.00 31.21           O  
ANISOU  806  O   GLN A 812     3923   4574   3361    150     11    498       O  
ATOM    807  CB  GLN A 812      11.113 212.734   6.419  1.00 40.53           C  
ANISOU  807  CB  GLN A 812     4967   6168   4263    190    -18    780       C  
ATOM    808  CG  GLN A 812      10.174 213.688   7.139  1.00 49.92           C  
ANISOU  808  CG  GLN A 812     6104   7290   5574    263    -42    885       C  
ATOM    809  CD  GLN A 812      10.942 214.816   7.857  1.00 59.14           C  
ANISOU  809  CD  GLN A 812     7304   8236   6930    328     15    969       C  
ATOM    810  NE2 GLN A 812      11.409 215.775   7.234  1.00 65.38           N  
ANISOU  810  NE2 GLN A 812     8140   8848   7850    318     30    864       N  
ATOM    811  OE1 GLN A 812      11.060 214.699   9.179  1.00 60.32           O  
ANISOU  811  OE1 GLN A 812     7436   8380   7102    377     50   1124       O  
ATOM    812  N   TYR A 813      11.055 210.030   7.995  1.00 30.11           N  
ANISOU  812  N   TYR A 813     3788   4682   2970     41     -5    372       N  
ATOM    813  CA  TYR A 813      10.457 209.104   8.954  1.00 32.59           C  
ANISOU  813  CA  TYR A 813     4139   4916   3325    -11    -11    241       C  
ATOM    814  C   TYR A 813      11.413 208.695  10.062  1.00 30.27           C  
ANISOU  814  C   TYR A 813     3927   4419   3154      7     37    177       C  
ATOM    815  O   TYR A 813      11.056 208.742  11.247  1.00 29.01           O  
ANISOU  815  O   TYR A 813     3775   4153   3092     19     29    163       O  
ATOM    816  CB  TYR A 813       9.902 207.878   8.232  1.00 36.82           C  
ANISOU  816  CB  TYR A 813     4688   5581   3720   -119    -16    105       C  
ATOM    817  CG  TYR A 813       8.600 208.136   7.545  1.00 43.70           C  
ANISOU  817  CG  TYR A 813     5456   6673   4475   -158    -85    147       C  
ATOM    818  CD1 TYR A 813       7.431 208.156   8.259  1.00 49.54           C  
ANISOU  818  CD1 TYR A 813     6142   7424   5256   -176   -127    144       C  
ATOM    819  CD2 TYR A 813       8.535 208.329   6.177  1.00 55.12           C  
ANISOU  819  CD2 TYR A 813     6844   8341   5756   -177   -108    192       C  
ATOM    820  CE1 TYR A 813       6.219 208.365   7.647  1.00 55.27           C  
ANISOU  820  CE1 TYR A 813     6751   8378   5871   -208   -193    188       C  
ATOM    821  CE2 TYR A 813       7.326 208.547   5.549  1.00 61.92           C  
ANISOU  821  CE2 TYR A 813     7590   9443   6493   -210   -180    241       C  
ATOM    822  CZ  TYR A 813       6.166 208.564   6.302  1.00 58.56           C  
ANISOU  822  CZ  TYR A 813     7104   9025   6121   -223   -224    240       C  
ATOM    823  OH  TYR A 813       4.944 208.772   5.726  1.00 64.52           O  
ANISOU  823  OH  TYR A 813     7721  10038   6753   -251   -298    295       O  
ATOM    824  N   LEU A 814      12.629 208.286   9.704  1.00 28.55           N  
ANISOU  824  N   LEU A 814     3760   4164   2922     15     89    142       N  
ATOM    825  CA  LEU A 814      13.601 207.812  10.693  1.00 27.52           C  
ANISOU  825  CA  LEU A 814     3690   3873   2890     43    135     94       C  
ATOM    826  C   LEU A 814      13.886 208.890  11.711  1.00 27.02           C  
ANISOU  826  C   LEU A 814     3597   3716   2950     98    120    178       C  
ATOM    827  O   LEU A 814      13.890 208.657  12.937  1.00 25.75           O  
ANISOU  827  O   LEU A 814     3459   3454   2868    105    121    143       O  
ATOM    828  CB  LEU A 814      14.897 207.350  10.028  1.00 28.40           C  
ANISOU  828  CB  LEU A 814     3836   3986   2965     62    198     65       C  
ATOM    829  CG  LEU A 814      14.780 206.042   9.268  1.00 30.18           C  
ANISOU  829  CG  LEU A 814     4118   4255   3092      6    241    -64       C  
ATOM    830  CD1 LEU A 814      15.912 205.869   8.269  1.00 31.75           C  
ANISOU  830  CD1 LEU A 814     4327   4509   3225     30    305    -77       C  
ATOM    831  CD2 LEU A 814      14.729 204.848  10.224  1.00 29.76           C  
ANISOU  831  CD2 LEU A 814     4141   4057   3110     -4    280   -165       C  
ATOM    832  N   LEU A 815      14.122 210.108  11.249  1.00 27.03           N  
ANISOU  832  N   LEU A 815     3550   3749   2969    130    113    289       N  
ATOM    833  CA  LEU A 815      14.455 211.170  12.210  1.00 28.09           C  
ANISOU  833  CA  LEU A 815     3665   3775   3230    165    115    346       C  
ATOM    834  C   LEU A 815      13.274 211.584  13.072  1.00 27.63           C  
ANISOU  834  C   LEU A 815     3586   3679   3230    171     82    348       C  
ATOM    835  O   LEU A 815      13.444 211.839  14.280  1.00 26.99           O  
ANISOU  835  O   LEU A 815     3516   3500   3240    178     88    316       O  
ATOM    836  CB  LEU A 815      15.076 212.386  11.500  1.00 29.27           C  
ANISOU  836  CB  LEU A 815     3778   3936   3404    190    138    466       C  
ATOM    837  CG  LEU A 815      16.405 212.050  10.840  1.00 30.21           C  
ANISOU  837  CG  LEU A 815     3908   4090   3480    184    182    462       C  
ATOM    838  CD1 LEU A 815      16.742 213.070   9.746  1.00 31.50           C  
ANISOU  838  CD1 LEU A 815     4032   4313   3622    196    206    596       C  
ATOM    839  CD2 LEU A 815      17.560 211.883  11.821  1.00 31.53           C  
ANISOU  839  CD2 LEU A 815     4086   4167   3726    184    209    410       C  
ATOM    840  N   ASN A 816      12.083 211.635  12.486  1.00 28.06           N  
ANISOU  840  N   ASN A 816     3603   3831   3226    169     48    380       N  
ATOM    841  CA  ASN A 816      10.888 211.920  13.271  1.00 30.54           C  
ANISOU  841  CA  ASN A 816     3885   4128   3589    180     22    378       C  
ATOM    842  C   ASN A 816      10.657 210.818  14.296  1.00 27.54           C  
ANISOU  842  C   ASN A 816     3548   3702   3213    134     21    258       C  
ATOM    843  O   ASN A 816      10.265 211.105  15.377  1.00 28.08           O  
ANISOU  843  O   ASN A 816     3609   3705   3352    147     22    241       O  
ATOM    844  CB  ASN A 816       9.647 212.054  12.400  1.00 35.89           C  
ANISOU  844  CB  ASN A 816     4492   4958   4185    185    -18    438       C  
ATOM    845  CG  ASN A 816       9.572 213.402  11.669  1.00 50.44           C  
ANISOU  845  CG  ASN A 816     6278   6832   6055    261    -14    601       C  
ATOM    846  ND2 ASN A 816       9.006 213.492  10.580  1.00 55.85           N  
ANISOU  846  ND2 ASN A 816     6978   7366   6875    310     28    652       N  
ATOM    847  OD1 ASN A 816      10.112 214.451  12.277  1.00 60.84           O  
ANISOU  847  OD1 ASN A 816     7534   8311   7268    271    -44    682       O  
ATOM    848  N   TRP A 817      10.905 209.555  13.970  1.00 28.03           N  
ANISOU  848  N   TRP A 817     3657   3791   3201     83     30    178       N  
ATOM    849  CA  TRP A 817      10.716 208.521  15.013  1.00 27.91           C  
ANISOU  849  CA  TRP A 817     3690   3706   3207     46     43     89       C  
ATOM    850  C   TRP A 817      11.661 208.731  16.172  1.00 27.20           C  
ANISOU  850  C   TRP A 817     3627   3506   3200     85     66     88       C  
ATOM    851  O   TRP A 817      11.276 208.534  17.328  1.00 27.24           O  
ANISOU  851  O   TRP A 817     3639   3467   3243     78     66     60       O  
ATOM    852  CB  TRP A 817      10.883 207.103  14.457  1.00 28.46           C  
ANISOU  852  CB  TRP A 817     3820   3787   3204    -11     72      1       C  
ATOM    853  CG  TRP A 817       9.854 206.715  13.491  1.00 28.96           C  
ANISOU  853  CG  TRP A 817     3855   3977   3170    -82     48    -34       C  
ATOM    854  CD1 TRP A 817       8.583 207.157  13.452  1.00 29.53           C  
ANISOU  854  CD1 TRP A 817     3851   4149   3220   -104      1     -6       C  
ATOM    855  CD2 TRP A 817       9.990 205.782  12.409  1.00 29.36           C  
ANISOU  855  CD2 TRP A 817     3943   4089   3123   -147     73   -116       C  
ATOM    856  CE2 TRP A 817       8.756 205.732  11.745  1.00 30.23           C  
ANISOU  856  CE2 TRP A 817     3989   4354   3140   -222     29   -138       C  
ATOM    857  CE3 TRP A 817      11.053 205.042  11.897  1.00 29.56           C  
ANISOU  857  CE3 TRP A 817     4040   4065   3124   -145    133   -175       C  
ATOM    858  NE1 TRP A 817       7.917 206.598  12.382  1.00 31.32           N  
ANISOU  858  NE1 TRP A 817     4051   4520   3328   -186    -17    -58       N  
ATOM    859  CZ2 TRP A 817       8.545 204.937  10.607  1.00 33.76           C  
ANISOU  859  CZ2 TRP A 817     4448   4915   3461   -316     39   -235       C  
ATOM    860  CZ3 TRP A 817      10.853 204.272  10.762  1.00 30.10           C  
ANISOU  860  CZ3 TRP A 817     4131   4224   3080   -226    155   -273       C  
ATOM    861  CH2 TRP A 817       9.608 204.220  10.126  1.00 31.16           C  
ANISOU  861  CH2 TRP A 817     4206   4520   3113   -320    107   -310       C  
ATOM    862  N   CYS A 818      12.919 209.096  15.887  1.00 26.75           N  
ANISOU  862  N   CYS A 818     3576   3425   3160    117     86    119       N  
ATOM    863  CA  CYS A 818      13.860 209.369  16.961  1.00 25.61           C  
ANISOU  863  CA  CYS A 818     3436   3213   3081    142    100    117       C  
ATOM    864  C   CYS A 818      13.398 210.527  17.843  1.00 25.90           C  
ANISOU  864  C   CYS A 818     3435   3216   3189    149     85    132       C  
ATOM    865  O   CYS A 818      13.579 210.513  19.083  1.00 25.31           O  
ANISOU  865  O   CYS A 818     3361   3108   3145    146     87     96       O  
ATOM    866  CB  CYS A 818      15.277 209.686  16.434  1.00 24.03           C  
ANISOU  866  CB  CYS A 818     3227   3016   2888    164    124    150       C  
ATOM    867  SG  CYS A 818      16.043 208.391  15.471  1.00 29.22           S  
ANISOU  867  SG  CYS A 818     3927   3702   3473    175    165    121       S  
ATOM    868  N   VAL A 819      12.877 211.571  17.229  1.00 25.34           N  
ANISOU  868  N   VAL A 819     3328   3155   3144    163     80    188       N  
ATOM    869  CA  VAL A 819      12.300 212.650  18.010  1.00 26.97           C  
ANISOU  869  CA  VAL A 819     3505   3310   3430    180     84    193       C  
ATOM    870  C   VAL A 819      11.175 212.169  18.940  1.00 25.67           C  
ANISOU  870  C   VAL A 819     3337   3159   3257    170     72    140       C  
ATOM    871  O   VAL A 819      11.136 212.490  20.146  1.00 26.74           O  
ANISOU  871  O   VAL A 819     3471   3253   3435    166     85     92       O  
ATOM    872  CB  VAL A 819      11.759 213.793  17.110  1.00 26.04           C  
ANISOU  872  CB  VAL A 819     3348   3193   3350    220     92    288       C  
ATOM    873  CG1 VAL A 819      11.026 214.859  17.931  1.00 26.61           C  
ANISOU  873  CG1 VAL A 819     3396   3192   3522    252    116    287       C  
ATOM    874  CG2 VAL A 819      12.882 214.426  16.291  1.00 27.74           C  
ANISOU  874  CG2 VAL A 819     3567   3386   3587    223    117    354       C  
ATOM    875  N   GLN A 820      10.248 211.414  18.381  1.00 25.57           N  
ANISOU  875  N   GLN A 820     3317   3218   3181    154     50    143       N  
ATOM    876  CA  GLN A 820       9.055 211.026  19.140  1.00 25.34           C  
ANISOU  876  CA  GLN A 820     3268   3216   3144    136     43    104       C  
ATOM    877  C   GLN A 820       9.410 210.062  20.263  1.00 26.04           C  
ANISOU  877  C   GLN A 820     3404   3272   3217    102     56     40       C  
ATOM    878  O   GLN A 820       8.868 210.145  21.345  1.00 23.35           O  
ANISOU  878  O   GLN A 820     3050   2927   2895     98     65     10       O  
ATOM    879  CB  GLN A 820       8.036 210.372  18.212  1.00 26.24           C  
ANISOU  879  CB  GLN A 820     3352   3433   3183    103     16    113       C  
ATOM    880  CG  GLN A 820       7.433 211.376  17.239  1.00 28.47           C  
ANISOU  880  CG  GLN A 820     3563   3785   3467    153     -2    202       C  
ATOM    881  CD  GLN A 820       6.438 210.738  16.312  1.00 33.94           C  
ANISOU  881  CD  GLN A 820     4206   4626   4062    108    -39    206       C  
ATOM    882  NE2 GLN A 820       6.165 211.420  15.236  1.00 38.79           N  
ANISOU  882  NE2 GLN A 820     4758   5334   4644    150    -62    300       N  
ATOM    883  OE1 GLN A 820       5.912 209.655  16.554  1.00 32.61           O  
ANISOU  883  OE1 GLN A 820     4049   4495   3844     31    -44    131       O  
ATOM    884  N   ILE A 821      10.328 209.136  20.005  1.00 23.59           N  
ANISOU  884  N   ILE A 821     3145   2944   2870     86     64     29       N  
ATOM    885  CA  ILE A 821      10.771 208.256  21.067  1.00 25.54           C  
ANISOU  885  CA  ILE A 821     3434   3161   3109     76     82      1       C  
ATOM    886  C   ILE A 821      11.443 209.035  22.209  1.00 25.98           C  
ANISOU  886  C   ILE A 821     3469   3201   3199    100     84     -4       C  
ATOM    887  O   ILE A 821      11.241 208.723  23.439  1.00 26.26           O  
ANISOU  887  O   ILE A 821     3506   3249   3221     90     91    -25       O  
ATOM    888  CB  ILE A 821      11.704 207.170  20.500  1.00 25.10           C  
ANISOU  888  CB  ILE A 821     3433   3079   3023     79    104      3       C  
ATOM    889  CG1 ILE A 821      10.936 206.220  19.591  1.00 25.37           C  
ANISOU  889  CG1 ILE A 821     3498   3124   3015     28    115    -27       C  
ATOM    890  CG2 ILE A 821      12.304 206.351  21.613  1.00 26.64           C  
ANISOU  890  CG2 ILE A 821     3662   3241   3218     96    128      8       C  
ATOM    891  CD1 ILE A 821      11.855 205.409  18.654  1.00 27.22           C  
ANISOU  891  CD1 ILE A 821     3786   3331   3224     36    149    -41       C  
ATOM    892  N   ALA A 822      12.252 210.029  21.847  1.00 24.90           N  
ANISOU  892  N   ALA A 822     3311   3050   3100    119     81      8       N  
ATOM    893  CA  ALA A 822      12.910 210.879  22.840  1.00 24.82           C  
ANISOU  893  CA  ALA A 822     3275   3032   3122    116     86    -20       C  
ATOM    894  C   ALA A 822      11.880 211.716  23.624  1.00 26.55           C  
ANISOU  894  C   ALA A 822     3469   3241   3377    110     97    -63       C  
ATOM    895  O   ALA A 822      12.035 211.892  24.846  1.00 25.26           O  
ANISOU  895  O   ALA A 822     3295   3100   3201     91    104   -117       O  
ATOM    896  CB  ALA A 822      13.995 211.764  22.204  1.00 25.76           C  
ANISOU  896  CB  ALA A 822     3377   3128   3283    118     92     -1       C  
ATOM    897  N   LYS A 823      10.828 212.199  22.957  1.00 25.81           N  
ANISOU  897  N   LYS A 823     3358   3130   3317    130    102    -39       N  
ATOM    898  CA  LYS A 823       9.730 212.850  23.645  1.00 24.55           C  
ANISOU  898  CA  LYS A 823     3167   2965   3193    143    123    -73       C  
ATOM    899  C   LYS A 823       9.056 211.968  24.682  1.00 24.34           C  
ANISOU  899  C   LYS A 823     3142   2997   3109    117    124   -112       C  
ATOM    900  O   LYS A 823       8.844 212.375  25.832  1.00 25.50           O  
ANISOU  900  O   LYS A 823     3274   3154   3258    110    148   -172       O  
ATOM    901  CB  LYS A 823       8.678 213.380  22.675  1.00 26.61           C  
ANISOU  901  CB  LYS A 823     3390   3226   3492    187    125    -14       C  
ATOM    902  CG  LYS A 823       9.129 214.661  21.985  1.00 27.41           C  
ANISOU  902  CG  LYS A 823     3484   3250   3680    226    150     31       C  
ATOM    903  CD  LYS A 823       8.074 215.118  21.011  1.00 28.77           C  
ANISOU  903  CD  LYS A 823     3607   3447   3875    288    148    121       C  
ATOM    904  CE  LYS A 823       8.544 216.420  20.405  1.00 32.88           C  
ANISOU  904  CE  LYS A 823     4127   3870   4493    335    188    189       C  
ATOM    905  NZ  LYS A 823       7.582 217.015  19.478  1.00 33.61           N1+
ANISOU  905  NZ  LYS A 823     4164   3990   4616    418    192    308       N1+
ATOM    906  N   GLY A 824       8.715 210.756  24.293  1.00 23.07           N  
ANISOU  906  N   GLY A 824     2999   2873   2891     96    106    -82       N  
ATOM    907  CA  GLY A 824       8.106 209.851  25.226  1.00 24.42           C  
ANISOU  907  CA  GLY A 824     3177   3087   3012     64    117   -100       C  
ATOM    908  C   GLY A 824       9.003 209.549  26.391  1.00 25.22           C  
ANISOU  908  C   GLY A 824     3302   3204   3075     55    124   -119       C  
ATOM    909  O   GLY A 824       8.531 209.453  27.505  1.00 25.17           O  
ANISOU  909  O   GLY A 824     3281   3244   3035     40    142   -146       O  
ATOM    910  N   MET A 825      10.295 209.342  26.131  1.00 27.05           N  
ANISOU  910  N   MET A 825     3559   3418   3299     67    109    -96       N  
ATOM    911  CA  MET A 825      11.240 209.011  27.166  1.00 24.85           C  
ANISOU  911  CA  MET A 825     3283   3186   2970     67    107    -95       C  
ATOM    912  C   MET A 825      11.464 210.170  28.092  1.00 26.29           C  
ANISOU  912  C   MET A 825     3424   3409   3155     51    110   -167       C  
ATOM    913  O   MET A 825      11.559 209.975  29.313  1.00 25.87           O  
ANISOU  913  O   MET A 825     3355   3439   3034     35    113   -188       O  
ATOM    914  CB  MET A 825      12.572 208.515  26.569  1.00 27.50           C  
ANISOU  914  CB  MET A 825     3637   3508   3301     94     94    -46       C  
ATOM    915  CG  MET A 825      12.490 207.131  25.944  1.00 27.14           C  
ANISOU  915  CG  MET A 825     3646   3420   3244    109    111      9       C  
ATOM    916  SD  MET A 825      11.857 205.845  27.042  1.00 29.07           S  
ANISOU  916  SD  MET A 825     3925   3680   3439     99    142     52       S  
ATOM    917  CE  MET A 825      13.069 205.952  28.330  1.00 30.50           C  
ANISOU  917  CE  MET A 825     4064   3964   3558    137    126     88       C  
ATOM    918  N   ASN A 826      11.533 211.405  27.554  1.00 25.92           N  
ANISOU  918  N   ASN A 826     3359   3305   3182     51    117   -209       N  
ATOM    919  CA  ASN A 826      11.597 212.573  28.397  1.00 25.04           C  
ANISOU  919  CA  ASN A 826     3220   3201   3093     23    141   -304       C  
ATOM    920  C   ASN A 826      10.406 212.699  29.332  1.00 26.07           C  
ANISOU  920  C   ASN A 826     3336   3366   3201     19    173   -359       C  
ATOM    921  O   ASN A 826      10.547 213.099  30.497  1.00 25.69           O  
ANISOU  921  O   ASN A 826     3269   3384   3108    -15    191   -445       O  
ATOM    922  CB  ASN A 826      11.735 213.852  27.550  1.00 26.66           C  
ANISOU  922  CB  ASN A 826     3422   3298   3408     29    164   -324       C  
ATOM    923  CG  ASN A 826      11.832 215.087  28.391  1.00 28.76           C  
ANISOU  923  CG  ASN A 826     3673   3538   3717     -9    209   -441       C  
ATOM    924  ND2 ASN A 826      10.794 215.881  28.402  1.00 29.90           N  
ANISOU  924  ND2 ASN A 826     3815   3608   3938     21    260   -476       N  
ATOM    925  OD1 ASN A 826      12.866 215.362  28.969  1.00 28.68           O  
ANISOU  925  OD1 ASN A 826     3647   3572   3675    -67    202   -503       O  
ATOM    926  N   TYR A 827       9.218 212.393  28.830  1.00 26.75           N  
ANISOU  926  N   TYR A 827     3421   3427   3312     48    183   -318       N  
ATOM    927  CA  TYR A 827       8.029 212.399  29.643  1.00 26.56           C  
ANISOU  927  CA  TYR A 827     3372   3451   3266     47    218   -357       C  
ATOM    928  C   TYR A 827       8.150 211.397  30.782  1.00 26.30           C  
ANISOU  928  C   TYR A 827     3345   3528   3118     13    213   -350       C  
ATOM    929  O   TYR A 827       7.879 211.716  31.962  1.00 27.00           O  
ANISOU  929  O   TYR A 827     3410   3693   3154     -7    244   -422       O  
ATOM    930  CB  TYR A 827       6.773 212.131  28.797  1.00 28.18           C  
ANISOU  930  CB  TYR A 827     3557   3640   3510     76    221   -301       C  
ATOM    931  CG  TYR A 827       5.561 211.866  29.655  1.00 27.76           C  
ANISOU  931  CG  TYR A 827     3466   3662   3418     67    257   -326       C  
ATOM    932  CD1 TYR A 827       4.856 212.927  30.212  1.00 30.11           C  
ANISOU  932  CD1 TYR A 827     3721   3958   3760     99    312   -401       C  
ATOM    933  CD2 TYR A 827       5.167 210.562  29.960  1.00 28.18           C  
ANISOU  933  CD2 TYR A 827     3529   3780   3395     25    249   -278       C  
ATOM    934  CE1 TYR A 827       3.767 212.719  31.030  1.00 31.04           C  
ANISOU  934  CE1 TYR A 827     3794   4159   3839     94    354   -428       C  
ATOM    935  CE2 TYR A 827       4.075 210.322  30.786  1.00 30.08           C  
ANISOU  935  CE2 TYR A 827     3729   4100   3597      6    289   -297       C  
ATOM    936  CZ  TYR A 827       3.379 211.405  31.311  1.00 31.94           C  
ANISOU  936  CZ  TYR A 827     3910   4355   3867     42    338   -372       C  
ATOM    937  OH  TYR A 827       2.297 211.177  32.088  1.00 31.85           O  
ANISOU  937  OH  TYR A 827     3849   4435   3815     27    384   -390       O  
ATOM    938  N   LEU A 828       8.581 210.199  30.449  1.00 26.30           N  
ANISOU  938  N   LEU A 828     3377   3536   3077      9    183   -261       N  
ATOM    939  CA  LEU A 828       8.766 209.180  31.496  1.00 27.94           C  
ANISOU  939  CA  LEU A 828     3595   3837   3183     -8    186   -218       C  
ATOM    940  C   LEU A 828       9.760 209.679  32.534  1.00 28.58           C  
ANISOU  940  C   LEU A 828     3650   4016   3193    -22    174   -268       C  
ATOM    941  O   LEU A 828       9.514 209.552  33.742  1.00 27.69           O  
ANISOU  941  O   LEU A 828     3514   4018   2986    -44    192   -290       O  
ATOM    942  CB  LEU A 828       9.230 207.850  30.916  1.00 27.71           C  
ANISOU  942  CB  LEU A 828     3614   3768   3144      4    171   -110       C  
ATOM    943  CG  LEU A 828       8.248 207.126  30.009  1.00 29.25           C  
ANISOU  943  CG  LEU A 828     3837   3891   3384    -11    187    -74       C  
ATOM    944  CD1 LEU A 828       8.858 205.808  29.553  1.00 30.64           C  
ANISOU  944  CD1 LEU A 828     4075   4010   3556     -2    192      9       C  
ATOM    945  CD2 LEU A 828       6.935 206.875  30.765  1.00 28.47           C  
ANISOU  945  CD2 LEU A 828     3714   3849   3254    -49    225    -83       C  
ATOM    946  N   GLU A 829      10.848 210.298  32.087  1.00 26.69           N  
ANISOU  946  N   GLU A 829     3404   3749   2988    -20    147   -296       N  
ATOM    947  CA  GLU A 829      11.820 210.885  33.025  1.00 27.99           C  
ANISOU  947  CA  GLU A 829     3528   4025   3082    -57    132   -366       C  
ATOM    948  C   GLU A 829      11.180 211.951  33.927  1.00 29.73           C  
ANISOU  948  C   GLU A 829     3722   4286   3288   -102    175   -510       C  
ATOM    949  O   GLU A 829      11.435 211.997  35.145  1.00 27.98           O  
ANISOU  949  O   GLU A 829     3465   4216   2948   -143    176   -566       O  
ATOM    950  CB  GLU A 829      13.060 211.431  32.276  1.00 28.96           C  
ANISOU  950  CB  GLU A 829     3640   4105   3259    -64    103   -377       C  
ATOM    951  CG  GLU A 829      14.069 212.125  33.181  1.00 31.18           C  
ANISOU  951  CG  GLU A 829     3863   4513   3468   -128     86   -470       C  
ATOM    952  CD  GLU A 829      15.412 212.432  32.528  1.00 33.73           C  
ANISOU  952  CD  GLU A 829     4158   4830   3826   -144     55   -459       C  
ATOM    953  OE1 GLU A 829      16.307 212.873  33.280  1.00 36.73           O  
ANISOU  953  OE1 GLU A 829     4477   5346   4133   -209     33   -530       O  
ATOM    954  OE2 GLU A 829      15.580 212.255  31.305  1.00 33.80           O1-
ANISOU  954  OE2 GLU A 829     4198   4720   3923   -101     52   -387       O1-
ATOM    955  N   ASP A 830      10.349 212.822  33.362  1.00 29.15           N  
ANISOU  955  N   ASP A 830     3660   4087   3328    -89    217   -572       N  
ATOM    956  CA  ASP A 830       9.654 213.802  34.176  1.00 30.87           C  
ANISOU  956  CA  ASP A 830     3859   4318   3552   -114    279   -712       C  
ATOM    957  C   ASP A 830       8.791 213.096  35.234  1.00 31.65           C  
ANISOU  957  C   ASP A 830     3939   4550   3536   -118    301   -702       C  
ATOM    958  O   ASP A 830       8.548 213.654  36.304  1.00 32.91           O  
ANISOU  958  O   ASP A 830     4074   4798   3631   -155    345   -823       O  
ATOM    959  CB  ASP A 830       8.692 214.703  33.359  1.00 35.10           C  
ANISOU  959  CB  ASP A 830     4403   4692   4239    -65    333   -740       C  
ATOM    960  CG  ASP A 830       9.405 215.802  32.557  1.00 39.18           C  
ANISOU  960  CG  ASP A 830     4937   5067   4879    -69    345   -779       C  
ATOM    961  OD1 ASP A 830      10.528 216.195  32.882  1.00 39.69           O  
ANISOU  961  OD1 ASP A 830     4999   5159   4920   -134    333   -847       O  
ATOM    962  OD2 ASP A 830       8.791 216.281  31.582  1.00 47.14           O1-
ANISOU  962  OD2 ASP A 830     5954   5946   6010     -8    371   -733       O1-
ATOM    963  N   ARG A 831       8.259 211.927  34.913  1.00 31.30           N  
ANISOU  963  N   ARG A 831     3908   4511   3472    -87    284   -569       N  
ATOM    964  CA  ARG A 831       7.440 211.171  35.878  1.00 33.84           C  
ANISOU  964  CA  ARG A 831     4213   4953   3689    -99    312   -537       C  
ATOM    965  C   ARG A 831       8.269 210.287  36.843  1.00 32.79           C  
ANISOU  965  C   ARG A 831     4076   4981   3402   -123    280   -466       C  
ATOM    966  O   ARG A 831       7.709 209.494  37.625  1.00 31.16           O  
ANISOU  966  O   ARG A 831     3860   4877   3099   -131    304   -401       O  
ATOM    967  CB  ARG A 831       6.432 210.325  35.132  1.00 33.77           C  
ANISOU  967  CB  ARG A 831     4219   4876   3735    -75    320   -432       C  
ATOM    968  CG  ARG A 831       5.512 211.188  34.262  1.00 38.20           C  
ANISOU  968  CG  ARG A 831     4759   5327   4424    -41    348   -483       C  
ATOM    969  CD  ARG A 831       4.575 212.028  35.114  1.00 45.90           C  
ANISOU  969  CD  ARG A 831     5688   6357   5394    -36    420   -594       C  
ATOM    970  NE  ARG A 831       3.677 211.023  35.684  1.00 57.35           N  
ANISOU  970  NE  ARG A 831     7116   7910   6763    -61    443   -530       N  
ATOM    971  CZ  ARG A 831       3.431 210.802  36.965  1.00 62.05           C  
ANISOU  971  CZ  ARG A 831     7689   8646   7238    -94    483   -560       C  
ATOM    972  NH1 ARG A 831       3.919 211.602  37.924  1.00 71.85           N1+
ANISOU  972  NH1 ARG A 831     8920   9965   8412   -110    509   -684       N1+
ATOM    973  NH2 ARG A 831       2.619 209.796  37.272  1.00 59.45           N  
ANISOU  973  NH2 ARG A 831     7345   8388   6855   -122    506   -472       N  
ATOM    974  N   ARG A 832       9.586 210.413  36.742  1.00 32.22           N  
ANISOU  974  N   ARG A 832     3999   4934   3309   -128    229   -462       N  
ATOM    975  CA  ARG A 832      10.558 209.633  37.528  1.00 33.02           C  
ANISOU  975  CA  ARG A 832     4077   5200   3267   -130    188   -373       C  
ATOM    976  C   ARG A 832      10.496 208.125  37.260  1.00 30.81           C  
ANISOU  976  C   ARG A 832     3835   4891   2979    -77    183   -177       C  
ATOM    977  O   ARG A 832      10.855 207.327  38.115  1.00 30.39           O  
ANISOU  977  O   ARG A 832     3765   4978   2803    -63    175    -70       O  
ATOM    978  CB  ARG A 832      10.392 209.894  39.001  1.00 34.81           C  
ANISOU  978  CB  ARG A 832     4254   5637   3333   -179    209   -447       C  
ATOM    979  CG  ARG A 832      10.408 211.351  39.367  1.00 39.20           C  
ANISOU  979  CG  ARG A 832     4782   6213   3897   -243    236   -667       C  
ATOM    980  CD  ARG A 832      10.380 211.446  40.871  1.00 44.02           C  
ANISOU  980  CD  ARG A 832     5340   7071   4313   -299    253   -740       C  
ATOM    981  NE  ARG A 832      10.133 212.812  41.288  1.00 51.85           N  
ANISOU  981  NE  ARG A 832     6317   8061   5319   -366    308   -978       N  
ATOM    982  CZ  ARG A 832       9.198 213.219  42.151  1.00 60.82           C  
ANISOU  982  CZ  ARG A 832     7440   9275   6392   -393    384  -1097       C  
ATOM    983  NH1 ARG A 832       8.357 212.358  42.759  1.00 63.31           N1+
ANISOU  983  NH1 ARG A 832     7746   9699   6607   -367    411   -992       N1+
ATOM    984  NH2 ARG A 832       9.135 214.528  42.448  1.00 63.83           N  
ANISOU  984  NH2 ARG A 832     7819   9624   6809   -453    445  -1331       N  
ATOM    985  N   LEU A 833      10.128 207.742  36.047  1.00 30.53           N  
ANISOU  985  N   LEU A 833     3851   4674   3073    -49    189   -127       N  
ATOM    986  CA  LEU A 833      10.064 206.332  35.671  1.00 30.59           C  
ANISOU  986  CA  LEU A 833     3910   4614   3097    -12    201     31       C  
ATOM    987  C   LEU A 833      11.285 205.972  34.843  1.00 30.90           C  
ANISOU  987  C   LEU A 833     3969   4586   3183     39    164     97       C  
ATOM    988  O   LEU A 833      11.598 206.684  33.881  1.00 29.62           O  
ANISOU  988  O   LEU A 833     3808   4336   3107     38    141     26       O  
ATOM    989  CB  LEU A 833       8.822 206.078  34.834  1.00 31.41           C  
ANISOU  989  CB  LEU A 833     4052   4578   3301    -31    237     23       C  
ATOM    990  CG  LEU A 833       7.508 206.099  35.589  1.00 34.38           C  
ANISOU  990  CG  LEU A 833     4406   5020   3637    -75    287     -5       C  
ATOM    991  CD1 LEU A 833       6.330 206.237  34.641  1.00 33.21           C  
ANISOU  991  CD1 LEU A 833     4261   4764   3593    -98    309    -47       C  
ATOM    992  CD2 LEU A 833       7.317 204.862  36.464  1.00 37.12           C  
ANISOU  992  CD2 LEU A 833     4772   5434   3896    -83    326    129       C  
ATOM    993  N   VAL A 834      11.976 204.893  35.223  1.00 28.33           N  
ANISOU  993  N   VAL A 834     3654   4306   2802     91    165    243       N  
ATOM    994  CA  VAL A 834      12.998 204.279  34.405  1.00 27.10           C  
ANISOU  994  CA  VAL A 834     3524   4070   2703    159    152    329       C  
ATOM    995  C   VAL A 834      12.345 203.121  33.686  1.00 26.81           C  
ANISOU  995  C   VAL A 834     3577   3858   2752    173    210    407       C  
ATOM    996  O   VAL A 834      11.790 202.201  34.319  1.00 26.88           O  
ANISOU  996  O   VAL A 834     3619   3866   2729    173    259    504       O  
ATOM    997  CB  VAL A 834      14.209 203.823  35.231  1.00 29.01           C  
ANISOU  997  CB  VAL A 834     3711   4470   2840    226    126    448       C  
ATOM    998  CG1 VAL A 834      15.297 203.265  34.339  1.00 32.35           C  
ANISOU  998  CG1 VAL A 834     4147   4811   3331    310    122    530       C  
ATOM    999  CG2 VAL A 834      14.776 204.996  36.012  1.00 31.17           C  
ANISOU  999  CG2 VAL A 834     3886   4945   3010    177     69    341       C  
ATOM   1000  N   HIS A 835      12.427 203.125  32.358  1.00 26.12           N  
ANISOU 1000  N   HIS A 835     3530   3624   2769    177    212    365       N  
ATOM   1001  CA  HIS A 835      11.695 202.163  31.565  1.00 26.97           C  
ANISOU 1001  CA  HIS A 835     3720   3569   2955    158    267    391       C  
ATOM   1002  C   HIS A 835      12.315 200.785  31.682  1.00 28.76           C  
ANISOU 1002  C   HIS A 835     4006   3724   3196    230    322    537       C  
ATOM   1003  O   HIS A 835      11.614 199.753  31.903  1.00 28.20           O  
ANISOU 1003  O   HIS A 835     4000   3567   3148    207    392    605       O  
ATOM   1004  CB  HIS A 835      11.644 202.615  30.110  1.00 27.51           C  
ANISOU 1004  CB  HIS A 835     3807   3536   3107    138    251    299       C  
ATOM   1005  CG  HIS A 835      10.804 201.734  29.250  1.00 27.79           C  
ANISOU 1005  CG  HIS A 835     3916   3434   3206     90    302    289       C  
ATOM   1006  CD2 HIS A 835       9.599 201.935  28.665  1.00 27.86           C  
ANISOU 1006  CD2 HIS A 835     3926   3416   3244      8    304    211       C  
ATOM   1007  ND1 HIS A 835      11.188 200.467  28.897  1.00 28.78           N  
ANISOU 1007  ND1 HIS A 835     4119   3440   3373    122    363    360       N  
ATOM   1008  CE1 HIS A 835      10.255 199.918  28.149  1.00 29.73           C  
ANISOU 1008  CE1 HIS A 835     4294   3460   3542     41    404    308       C  
ATOM   1009  NE2 HIS A 835       9.277 200.788  27.996  1.00 28.39           N  
ANISOU 1009  NE2 HIS A 835     4069   3361   3357    -29    362    222       N  
ATOM   1010  N   ARG A 836      13.654 200.761  31.554  1.00 27.54           N  
ANISOU 1010  N   ARG A 836     3825   3604   3035    321    300    591       N  
ATOM   1011  CA  ARG A 836      14.489 199.546  31.676  1.00 30.15           C  
ANISOU 1011  CA  ARG A 836     4193   3877   3384    429    355    747       C  
ATOM   1012  C   ARG A 836      14.357 198.518  30.570  1.00 31.69           C  
ANISOU 1012  C   ARG A 836     4497   3847   3696    443    438    752       C  
ATOM   1013  O   ARG A 836      15.021 197.484  30.622  1.00 31.25           O  
ANISOU 1013  O   ARG A 836     4485   3710   3679    543    504    878       O  
ATOM   1014  CB  ARG A 836      14.273 198.832  33.017  1.00 31.78           C  
ANISOU 1014  CB  ARG A 836     4398   4158   3518    460    390    897       C  
ATOM   1015  CG  ARG A 836      14.655 199.707  34.189  1.00 33.70           C  
ANISOU 1015  CG  ARG A 836     4526   4659   3619    460    314    902       C  
ATOM   1016  CD  ARG A 836      14.499 199.042  35.529  1.00 35.58           C  
ANISOU 1016  CD  ARG A 836     4749   5012   3755    494    343   1063       C  
ATOM   1017  NE  ARG A 836      15.331 197.886  35.704  1.00 38.54           N  
ANISOU 1017  NE  ARG A 836     5145   5348   4147    630    395   1270       N  
ATOM   1018  CZ  ARG A 836      14.917 196.657  36.056  1.00 38.73           C  
ANISOU 1018  CZ  ARG A 836     5250   5254   4209    670    493   1434       C  
ATOM   1019  NH1 ARG A 836      13.642 196.352  36.287  1.00 37.11           N1+
ANISOU 1019  NH1 ARG A 836     5112   4965   4022    568    550   1414       N1+
ATOM   1020  NH2 ARG A 836      15.831 195.718  36.205  1.00 39.80           N  
ANISOU 1020  NH2 ARG A 836     5395   5358   4368    820    542   1632       N  
ATOM   1021  N   ASP A 837      13.537 198.775  29.557  1.00 30.68           N  
ANISOU 1021  N   ASP A 837     4410   3621   3623    347    441    616       N  
ATOM   1022  CA  ASP A 837      13.429 197.824  28.432  1.00 30.28           C  
ANISOU 1022  CA  ASP A 837     4461   3374   3670    338    520    588       C  
ATOM   1023  C   ASP A 837      13.153 198.552  27.114  1.00 29.60           C  
ANISOU 1023  C   ASP A 837     4368   3271   3605    269    480    434       C  
ATOM   1024  O   ASP A 837      12.410 198.069  26.250  1.00 32.26           O  
ANISOU 1024  O   ASP A 837     4770   3498   3988    187    523    354       O  
ATOM   1025  CB  ASP A 837      12.375 196.738  28.713  1.00 31.31           C  
ANISOU 1025  CB  ASP A 837     4680   3373   3842    266    611    620       C  
ATOM   1026  CG  ASP A 837      12.537 195.484  27.810  1.00 34.32           C  
ANISOU 1026  CG  ASP A 837     5182   3528   4329    276    724    615       C  
ATOM   1027  OD1 ASP A 837      13.495 195.372  27.003  1.00 34.23           O  
ANISOU 1027  OD1 ASP A 837     5186   3463   4354    357    740    596       O  
ATOM   1028  OD2 ASP A 837      11.687 194.603  27.919  1.00 37.15           O1-
ANISOU 1028  OD2 ASP A 837     5619   3758   4735    195    808    621       O1-
ATOM   1029  N   LEU A 838      13.755 199.721  26.945  1.00 27.42           N  
ANISOU 1029  N   LEU A 838     4009   3115   3293    293    400    394       N  
ATOM   1030  CA  LEU A 838      13.575 200.411  25.701  1.00 27.03           C  
ANISOU 1030  CA  LEU A 838     3951   3057   3262    243    368    282       C  
ATOM   1031  C   LEU A 838      14.322 199.660  24.567  1.00 28.32           C  
ANISOU 1031  C   LEU A 838     4175   3111   3473    290    426    270       C  
ATOM   1032  O   LEU A 838      15.500 199.267  24.719  1.00 27.52           O  
ANISOU 1032  O   LEU A 838     4070   3002   3385    400    454    347       O  
ATOM   1033  CB  LEU A 838      14.023 201.844  25.853  1.00 27.70           C  
ANISOU 1033  CB  LEU A 838     3940   3272   3309    252    285    252       C  
ATOM   1034  CG  LEU A 838      13.893 202.710  24.593  1.00 29.39           C  
ANISOU 1034  CG  LEU A 838     4137   3487   3541    213    252    165       C  
ATOM   1035  CD1 LEU A 838      12.427 202.783  24.194  1.00 32.74           C  
ANISOU 1035  CD1 LEU A 838     4577   3891   3969    121    250    100       C  
ATOM   1036  CD2 LEU A 838      14.490 204.100  24.828  1.00 28.83           C  
ANISOU 1036  CD2 LEU A 838     3982   3516   3455    224    191    149       C  
ATOM   1037  N   ALA A 839      13.623 199.489  23.448  1.00 26.21           N  
ANISOU 1037  N   ALA A 839     3954   2780   3223    209    446    171       N  
ATOM   1038  CA  ALA A 839      14.108 198.802  22.274  1.00 26.36           C  
ANISOU 1038  CA  ALA A 839     4037   2703   3274    225    510    122       C  
ATOM   1039  C   ALA A 839      13.088 199.038  21.175  1.00 27.21           C  
ANISOU 1039  C   ALA A 839     4155   2825   3358    103    491      0       C  
ATOM   1040  O   ALA A 839      11.926 199.440  21.452  1.00 29.08           O  
ANISOU 1040  O   ALA A 839     4359   3118   3571     13    448    -28       O  
ATOM   1041  CB  ALA A 839      14.259 197.304  22.536  1.00 28.48           C  
ANISOU 1041  CB  ALA A 839     4408   2806   3606    262    626    166       C  
ATOM   1042  N   ALA A 840      13.471 198.793  19.930  1.00 26.86           N  
ANISOU 1042  N   ALA A 840     4143   2751   3308     97    525    -73       N  
ATOM   1043  CA  ALA A 840      12.506 199.044  18.814  1.00 27.54           C  
ANISOU 1043  CA  ALA A 840     4222   2895   3343    -23    498   -186       C  
ATOM   1044  C   ALA A 840      11.290 198.133  18.901  1.00 28.36           C  
ANISOU 1044  C   ALA A 840     4383   2931   3459   -150    544   -254       C  
ATOM   1045  O   ALA A 840      10.194 198.510  18.466  1.00 28.12           O  
ANISOU 1045  O   ALA A 840     4306   2997   3378   -259    493   -317       O  
ATOM   1046  CB  ALA A 840      13.197 198.905  17.457  1.00 27.08           C  
ANISOU 1046  CB  ALA A 840     4189   2842   3258    -10    532   -257       C  
ATOM   1047  N   ARG A 841      11.462 196.924  19.472  1.00 30.79           N  
ANISOU 1047  N   ARG A 841     4784   3076   3836   -136    644   -231       N  
ATOM   1048  CA  ARG A 841      10.321 196.007  19.661  1.00 32.39           C  
ANISOU 1048  CA  ARG A 841     5047   3193   4065   -272    704   -289       C  
ATOM   1049  C   ARG A 841       9.284 196.540  20.656  1.00 32.34           C  
ANISOU 1049  C   ARG A 841     4967   3280   4038   -327    638   -236       C  
ATOM   1050  O   ARG A 841       8.167 196.025  20.688  1.00 31.76           O  
ANISOU 1050  O   ARG A 841     4909   3189   3967   -464    666   -294       O  
ATOM   1051  CB  ARG A 841      10.773 194.581  20.091  1.00 35.58           C  
ANISOU 1051  CB  ARG A 841     5580   3369   4569   -236    847   -256       C  
ATOM   1052  CG  ARG A 841      11.407 194.591  21.477  1.00 37.11           C  
ANISOU 1052  CG  ARG A 841     5759   3538   4800    -96    849    -75       C  
ATOM   1053  CD  ARG A 841      11.943 193.262  21.985  1.00 39.55           C  
ANISOU 1053  CD  ARG A 841     6182   3631   5212    -20    992      8       C  
ATOM   1054  NE  ARG A 841      12.650 193.561  23.236  1.00 43.89           N  
ANISOU 1054  NE  ARG A 841     6675   4243   5756    129    956    194       N  
ATOM   1055  CZ  ARG A 841      13.948 193.889  23.333  1.00 44.40           C  
ANISOU 1055  CZ  ARG A 841     6693   4362   5813    293    934    280       C  
ATOM   1056  NH1 ARG A 841      14.420 194.205  24.524  1.00 47.83           N1+
ANISOU 1056  NH1 ARG A 841     7059   4895   6217    395    888    435       N1+
ATOM   1057  NH2 ARG A 841      14.790 193.909  22.278  1.00 39.57           N  
ANISOU 1057  NH2 ARG A 841     6091   3730   5213    351    957    212       N  
ATOM   1058  N   ASN A 842       9.683 197.504  21.485  1.00 29.12           N  
ANISOU 1058  N   ASN A 842     4483   2968   3612   -226    565   -134       N  
ATOM   1059  CA  ASN A 842       8.834 198.098  22.495  1.00 30.61           C  
ANISOU 1059  CA  ASN A 842     4599   3250   3778   -255    512    -87       C  
ATOM   1060  C   ASN A 842       8.407 199.494  22.149  1.00 29.61           C  
ANISOU 1060  C   ASN A 842     4364   3288   3599   -261    409   -116       C  
ATOM   1061  O   ASN A 842       8.013 200.247  23.029  1.00 30.22           O  
ANISOU 1061  O   ASN A 842     4372   3447   3660   -243    364    -73       O  
ATOM   1062  CB  ASN A 842       9.495 198.051  23.902  1.00 27.72           C  
ANISOU 1062  CB  ASN A 842     4234   2870   3428   -149    524     44       C  
ATOM   1063  CG  ASN A 842       9.569 196.655  24.446  1.00 31.54           C  
ANISOU 1063  CG  ASN A 842     4818   3195   3968   -149    635    107       C  
ATOM   1064  ND2 ASN A 842      10.553 196.392  25.312  1.00 33.38           N  
ANISOU 1064  ND2 ASN A 842     5064   3401   4215    -20    660    237       N  
ATOM   1065  OD1 ASN A 842       8.769 195.795  24.061  1.00 30.24           O  
ANISOU 1065  OD1 ASN A 842     4717   2932   3838   -266    704     43       O  
ATOM   1066  N   VAL A 843       8.477 199.840  20.862  1.00 28.18           N  
ANISOU 1066  N   VAL A 843     4166   3154   3388   -282    379   -186       N  
ATOM   1067  CA  VAL A 843       7.866 201.047  20.343  1.00 28.71           C  
ANISOU 1067  CA  VAL A 843     4132   3368   3409   -297    295   -204       C  
ATOM   1068  C   VAL A 843       6.770 200.585  19.374  1.00 30.44           C  
ANISOU 1068  C   VAL A 843     4337   3644   3582   -432    296   -298       C  
ATOM   1069  O   VAL A 843       6.986 199.665  18.588  1.00 31.31           O  
ANISOU 1069  O   VAL A 843     4520   3691   3685   -491    349   -373       O  
ATOM   1070  CB  VAL A 843       8.906 201.914  19.640  1.00 28.95           C  
ANISOU 1070  CB  VAL A 843     4138   3433   3426   -208    257   -182       C  
ATOM   1071  CG1 VAL A 843       8.222 203.168  19.104  1.00 30.25           C  
ANISOU 1071  CG1 VAL A 843     4203   3733   3555   -213    182   -176       C  
ATOM   1072  CG2 VAL A 843      10.028 202.248  20.604  1.00 27.40           C  
ANISOU 1072  CG2 VAL A 843     3947   3194   3267    -99    259   -105       C  
ATOM   1073  N   LEU A 844       5.567 201.166  19.466  1.00 29.17           N  
ANISOU 1073  N   LEU A 844     4080   3610   3392   -487    244   -301       N  
ATOM   1074  CA  LEU A 844       4.466 200.720  18.639  1.00 28.84           C  
ANISOU 1074  CA  LEU A 844     4000   3661   3294   -627    237   -387       C  
ATOM   1075  C   LEU A 844       4.096 201.831  17.641  1.00 28.66           C  
ANISOU 1075  C   LEU A 844     3865   3822   3202   -603    151   -374       C  
ATOM   1076  O   LEU A 844       4.269 202.996  17.927  1.00 29.45           O  
ANISOU 1076  O   LEU A 844     3904   3965   3321   -492    105   -291       O  
ATOM   1077  CB  LEU A 844       3.236 200.391  19.486  1.00 31.36           C  
ANISOU 1077  CB  LEU A 844     4273   4014   3625   -719    252   -391       C  
ATOM   1078  CG  LEU A 844       3.401 199.211  20.444  1.00 34.07           C  
ANISOU 1078  CG  LEU A 844     4724   4186   4033   -762    346   -386       C  
ATOM   1079  CD1 LEU A 844       2.104 198.860  21.142  1.00 35.17           C  
ANISOU 1079  CD1 LEU A 844     4811   4378   4175   -877    367   -394       C  
ATOM   1080  CD2 LEU A 844       3.922 197.986  19.738  1.00 36.12           C  
ANISOU 1080  CD2 LEU A 844     5107   4305   4310   -832    427   -469       C  
ATOM   1081  N   VAL A 845       3.559 201.432  16.507  1.00 29.45           N  
ANISOU 1081  N   VAL A 845     3937   4030   3221   -713    137   -457       N  
ATOM   1082  CA  VAL A 845       3.195 202.322  15.417  1.00 30.03           C  
ANISOU 1082  CA  VAL A 845     3901   4302   3205   -697     59   -434       C  
ATOM   1083  C   VAL A 845       1.677 202.525  15.287  1.00 28.89           C  
ANISOU 1083  C   VAL A 845     3616   4358   3002   -784      6   -440       C  
ATOM   1084  O   VAL A 845       0.966 201.643  14.913  1.00 30.00           O  
ANISOU 1084  O   VAL A 845     3744   4565   3087   -942     20   -543       O  
ATOM   1085  CB  VAL A 845       3.746 201.759  14.094  1.00 30.72           C  
ANISOU 1085  CB  VAL A 845     4042   4422   3209   -758     75   -523       C  
ATOM   1086  CG1 VAL A 845       3.513 202.737  12.945  1.00 30.99           C  
ANISOU 1086  CG1 VAL A 845     3961   4678   3135   -723     -5   -469       C  
ATOM   1087  CG2 VAL A 845       5.232 201.483  14.263  1.00 30.13           C  
ANISOU 1087  CG2 VAL A 845     4094   4155   3199   -666    138   -516       C  
ATOM   1088  N   LYS A 846       1.204 203.715  15.629  1.00 28.39           N  
ANISOU 1088  N   LYS A 846     3440   4387   2958   -677    -46   -329       N  
ATOM   1089  CA  LYS A 846      -0.226 204.057  15.508  1.00 30.03           C  
ANISOU 1089  CA  LYS A 846     3487   4807   3114   -723    -97   -308       C  
ATOM   1090  C   LYS A 846      -0.489 204.386  14.038  1.00 29.88           C  
ANISOU 1090  C   LYS A 846     3374   5012   2966   -745   -165   -298       C  
ATOM   1091  O   LYS A 846      -1.422 203.903  13.432  1.00 32.05           O  
ANISOU 1091  O   LYS A 846     3557   5479   3140   -879   -197   -362       O  
ATOM   1092  CB  LYS A 846      -0.563 205.277  16.388  1.00 29.77           C  
ANISOU 1092  CB  LYS A 846     3373   4776   3161   -573   -112   -188       C  
ATOM   1093  CG  LYS A 846      -2.056 205.596  16.326  1.00 34.08           C  
ANISOU 1093  CG  LYS A 846     3740   5544   3662   -603   -155   -158       C  
ATOM   1094  CD  LYS A 846      -2.407 206.917  17.017  1.00 36.33           C  
ANISOU 1094  CD  LYS A 846     3938   5837   4029   -431   -159    -39       C  
ATOM   1095  CE  LYS A 846      -3.762 207.378  16.526  1.00 41.54           C  
ANISOU 1095  CE  LYS A 846     4396   6759   4628   -424   -212     21       C  
ATOM   1096  NZ  LYS A 846      -4.241 208.678  17.069  1.00 43.95           N1+
ANISOU 1096  NZ  LYS A 846     4600   7081   5017   -244   -203    140       N1+
ATOM   1097  N   THR A 847       0.370 205.230  13.476  1.00 31.41           N  
ANISOU 1097  N   THR A 847     3585   5191   3157   -616   -186   -211       N  
ATOM   1098  CA  THR A 847       0.464 205.467  12.039  1.00 33.28           C  
ANISOU 1098  CA  THR A 847     3767   5614   3262   -626   -236   -192       C  
ATOM   1099  C   THR A 847       1.954 205.625  11.774  1.00 32.81           C  
ANISOU 1099  C   THR A 847     3836   5392   3236   -546   -199   -176       C  
ATOM   1100  O   THR A 847       2.739 205.815  12.714  1.00 31.24           O  
ANISOU 1100  O   THR A 847     3727   4978   3162   -462   -153   -150       O  
ATOM   1101  CB  THR A 847      -0.214 206.781  11.623  1.00 35.28           C  
ANISOU 1101  CB  THR A 847     3855   6063   3485   -502   -306    -24       C  
ATOM   1102  CG2 THR A 847      -1.606 206.867  12.157  1.00 37.11           C  
ANISOU 1102  CG2 THR A 847     3946   6431   3722   -528   -333     -6       C  
ATOM   1103  OG1 THR A 847       0.565 207.870  12.121  1.00 35.43           O  
ANISOU 1103  OG1 THR A 847     3919   5914   3626   -326   -282     98       O  
ATOM   1104  N   PRO A 848       2.376 205.579  10.498  1.00 33.38           N  
ANISOU 1104  N   PRO A 848     3906   5587   3188   -570   -217   -188       N  
ATOM   1105  CA  PRO A 848       3.798 205.780  10.218  1.00 32.63           C  
ANISOU 1105  CA  PRO A 848     3917   5356   3122   -490   -177   -164       C  
ATOM   1106  C   PRO A 848       4.342 207.085  10.747  1.00 31.97           C  
ANISOU 1106  C   PRO A 848     3823   5168   3154   -319   -179     -4       C  
ATOM   1107  O   PRO A 848       5.536 207.194  10.968  1.00 32.66           O  
ANISOU 1107  O   PRO A 848     4004   5095   3310   -260   -134      4       O  
ATOM   1108  CB  PRO A 848       3.856 205.736   8.667  1.00 35.09           C  
ANISOU 1108  CB  PRO A 848     4183   5893   3256   -540   -209   -177       C  
ATOM   1109  CG  PRO A 848       2.699 204.894   8.309  1.00 37.10           C  
ANISOU 1109  CG  PRO A 848     4370   6329   3396   -708   -239   -300       C  
ATOM   1110  CD  PRO A 848       1.619 205.308   9.283  1.00 36.36           C  
ANISOU 1110  CD  PRO A 848     4181   6248   3385   -680   -273   -231       C  
ATOM   1111  N   GLN A 849       3.482 208.066  11.012  1.00 31.81           N  
ANISOU 1111  N   GLN A 849     3688   5229   3166   -241   -221    115       N  
ATOM   1112  CA  GLN A 849       3.946 209.355  11.510  1.00 32.77           C  
ANISOU 1112  CA  GLN A 849     3806   5231   3411    -89   -207    252       C  
ATOM   1113  C   GLN A 849       3.791 209.470  13.034  1.00 31.14           C  
ANISOU 1113  C   GLN A 849     3632   4852   3346    -56   -173    226       C  
ATOM   1114  O   GLN A 849       4.046 210.520  13.572  1.00 32.38           O  
ANISOU 1114  O   GLN A 849     3784   4907   3610     52   -154    311       O  
ATOM   1115  CB  GLN A 849       3.127 210.507  10.886  1.00 37.17           C  
ANISOU 1115  CB  GLN A 849     4221   5961   3938      7   -254    420       C  
ATOM   1116  CG  GLN A 849       3.225 210.657   9.357  1.00 43.15           C  
ANISOU 1116  CG  GLN A 849     4922   6932   4540      1   -294    494       C  
ATOM   1117  CD  GLN A 849       2.354 209.644   8.620  1.00 51.22           C  
ANISOU 1117  CD  GLN A 849     5873   8202   5384   -143   -347    391       C  
ATOM   1118  NE2 GLN A 849       1.223 209.294   9.052  1.00 56.66           N  
ANISOU 1118  NE2 GLN A 849     6589   9010   5927   -217   -353    340       N  
ATOM   1119  OE1 GLN A 849       2.874 209.151   7.504  1.00 52.63           O  
ANISOU 1119  OE1 GLN A 849     5969   8473   5551   -201   -376    345       O  
ATOM   1120  N   HIS A 850       3.313 208.443  13.714  1.00 30.76           N  
ANISOU 1120  N   HIS A 850     3610   4779   3296   -155   -160    111       N  
ATOM   1121  CA  HIS A 850       3.012 208.589  15.167  1.00 29.32           C  
ANISOU 1121  CA  HIS A 850     3438   4475   3225   -125   -130     98       C  
ATOM   1122  C   HIS A 850       3.297 207.256  15.856  1.00 28.09           C  
ANISOU 1122  C   HIS A 850     3385   4211   3075   -229    -88    -23       C  
ATOM   1123  O   HIS A 850       2.529 206.292  15.703  1.00 30.26           O  
ANISOU 1123  O   HIS A 850     3644   4563   3290   -350    -90   -101       O  
ATOM   1124  CB  HIS A 850       1.558 208.995  15.387  1.00 30.66           C  
ANISOU 1124  CB  HIS A 850     3472   4786   3390   -113   -158    141       C  
ATOM   1125  CG  HIS A 850       1.227 209.332  16.812  1.00 32.70           C  
ANISOU 1125  CG  HIS A 850     3729   4940   3755    -66   -119    135       C  
ATOM   1126  CD2 HIS A 850       1.955 209.226  17.948  1.00 32.86           C  
ANISOU 1126  CD2 HIS A 850     3847   4784   3853    -52    -71     90       C  
ATOM   1127  ND1 HIS A 850       0.014 209.856  17.195  1.00 35.76           N  
ANISOU 1127  ND1 HIS A 850     3994   5430   4164    -24   -126    178       N  
ATOM   1128  CE1 HIS A 850       0.001 210.050  18.504  1.00 34.94           C  
ANISOU 1128  CE1 HIS A 850     3920   5208   4146      7    -77    148       C  
ATOM   1129  NE2 HIS A 850       1.175 209.685  18.978  1.00 32.76           N  
ANISOU 1129  NE2 HIS A 850     3777   4771   3899    -12    -48     96       N  
ATOM   1130  N   VAL A 851       4.374 207.236  16.637  1.00 27.87           N  
ANISOU 1130  N   VAL A 851     3455   4011   3123   -183    -47    -31       N  
ATOM   1131  CA  VAL A 851       4.786 206.055  17.418  1.00 25.86           C  
ANISOU 1131  CA  VAL A 851     3299   3634   2889   -247      1   -109       C  
ATOM   1132  C   VAL A 851       4.684 206.315  18.924  1.00 26.36           C  
ANISOU 1132  C   VAL A 851     3368   3617   3029   -206     25    -92       C  
ATOM   1133  O   VAL A 851       4.711 207.470  19.365  1.00 25.52           O  
ANISOU 1133  O   VAL A 851     3216   3506   2972   -119     14    -40       O  
ATOM   1134  CB  VAL A 851       6.191 205.589  17.042  1.00 26.72           C  
ANISOU 1134  CB  VAL A 851     3510   3641   3000   -228     33   -129       C  
ATOM   1135  CG1 VAL A 851       6.201 205.256  15.538  1.00 28.86           C  
ANISOU 1135  CG1 VAL A 851     3776   4011   3176   -282     19   -165       C  
ATOM   1136  CG2 VAL A 851       7.309 206.567  17.404  1.00 27.91           C  
ANISOU 1136  CG2 VAL A 851     3674   3718   3213   -118     34    -62       C  
ATOM   1137  N   LYS A 852       4.596 205.245  19.697  1.00 26.44           N  
ANISOU 1137  N   LYS A 852     3437   3561   3046   -271     66   -138       N  
ATOM   1138  CA  LYS A 852       4.483 205.351  21.148  1.00 26.17           C  
ANISOU 1138  CA  LYS A 852     3407   3478   3057   -244     93   -122       C  
ATOM   1139  C   LYS A 852       5.267 204.226  21.847  1.00 27.49           C  
ANISOU 1139  C   LYS A 852     3680   3525   3237   -265    146   -133       C  
ATOM   1140  O   LYS A 852       5.291 203.100  21.398  1.00 28.72           O  
ANISOU 1140  O   LYS A 852     3898   3633   3379   -337    180   -170       O  
ATOM   1141  CB  LYS A 852       3.019 205.258  21.614  1.00 27.20           C  
ANISOU 1141  CB  LYS A 852     3457   3700   3175   -306     95   -136       C  
ATOM   1142  CG  LYS A 852       2.050 206.285  21.035  1.00 27.81           C  
ANISOU 1142  CG  LYS A 852     3408   3916   3242   -272     50   -108       C  
ATOM   1143  CD  LYS A 852       0.655 206.131  21.685  1.00 30.70           C  
ANISOU 1143  CD  LYS A 852     3683   4380   3600   -326     63   -119       C  
ATOM   1144  CE  LYS A 852      -0.330 207.003  20.939  1.00 34.69           C  
ANISOU 1144  CE  LYS A 852     4046   5044   4087   -286     18    -79       C  
ATOM   1145  NZ  LYS A 852      -1.634 207.229  21.631  1.00 36.58           N1+
ANISOU 1145  NZ  LYS A 852     4168   5394   4334   -292     33    -72       N1+
ATOM   1146  N   ILE A 853       5.805 204.542  23.012  1.00 27.15           N  
ANISOU 1146  N   ILE A 853     3650   3442   3220   -204    159    -98       N  
ATOM   1147  CA  ILE A 853       6.553 203.585  23.807  1.00 27.24           C  
ANISOU 1147  CA  ILE A 853     3743   3366   3238   -197    205    -74       C  
ATOM   1148  C   ILE A 853       5.571 202.739  24.640  1.00 28.44           C  
ANISOU 1148  C   ILE A 853     3903   3519   3383   -275    250    -71       C  
ATOM   1149  O   ILE A 853       4.620 203.268  25.196  1.00 26.19           O  
ANISOU 1149  O   ILE A 853     3546   3316   3088   -294    240    -77       O  
ATOM   1150  CB  ILE A 853       7.493 204.331  24.734  1.00 27.80           C  
ANISOU 1150  CB  ILE A 853     3804   3441   3317   -110    192    -36       C  
ATOM   1151  CG1 ILE A 853       8.541 205.075  23.892  1.00 30.41           C  
ANISOU 1151  CG1 ILE A 853     4130   3761   3663    -51    160    -36       C  
ATOM   1152  CG2 ILE A 853       8.172 203.391  25.735  1.00 29.39           C  
ANISOU 1152  CG2 ILE A 853     4063   3594   3507    -90    234     16       C  
ATOM   1153  CD1 ILE A 853       9.141 206.196  24.663  1.00 31.91           C  
ANISOU 1153  CD1 ILE A 853     4278   3981   3864      3    138    -29       C  
ATOM   1154  N   THR A 854       5.847 201.435  24.732  1.00 28.50           N  
ANISOU 1154  N   THR A 854     3998   3425   3403   -314    310    -56       N  
ATOM   1155  CA  THR A 854       5.030 200.530  25.522  1.00 30.81           C  
ANISOU 1155  CA  THR A 854     4313   3695   3698   -394    369    -37       C  
ATOM   1156  C   THR A 854       5.920 199.570  26.327  1.00 30.53           C  
ANISOU 1156  C   THR A 854     4370   3547   3683   -346    434     48       C  
ATOM   1157  O   THR A 854       7.157 199.757  26.409  1.00 29.86           O  
ANISOU 1157  O   THR A 854     4307   3435   3600   -239    421     92       O  
ATOM   1158  CB  THR A 854       4.062 199.762  24.588  1.00 32.65           C  
ANISOU 1158  CB  THR A 854     4556   3912   3935   -534    396   -114       C  
ATOM   1159  CG2 THR A 854       4.800 198.693  23.789  1.00 32.27           C  
ANISOU 1159  CG2 THR A 854     4621   3718   3920   -555    453   -144       C  
ATOM   1160  OG1 THR A 854       2.994 199.191  25.349  1.00 35.28           O  
ANISOU 1160  OG1 THR A 854     4873   4263   4269   -633    444   -103       O  
ATOM   1161  N   ASP A 855       5.260 198.546  26.881  1.00 31.34           N  
ANISOU 1161  N   ASP A 855     4515   3590   3800   -426    509     79       N  
ATOM   1162  CA AASP A 855       5.877 197.452  27.668  0.50 31.90           C  
ANISOU 1162  CA AASP A 855     4678   3541   3900   -388    592    188       C  
ATOM   1163  CA BASP A 855       5.908 197.469  27.610  0.50 31.46           C  
ANISOU 1163  CA BASP A 855     4622   3483   3845   -386    590    184       C  
ATOM   1164  C   ASP A 855       6.680 197.916  28.845  1.00 31.49           C  
ANISOU 1164  C   ASP A 855     4596   3566   3801   -266    566    294       C  
ATOM   1165  O   ASP A 855       7.938 197.992  28.840  1.00 31.13           O  
ANISOU 1165  O   ASP A 855     4567   3502   3756   -151    550    346       O  
ATOM   1166  CB AASP A 855       6.701 196.453  26.871  0.50 33.87           C  
ANISOU 1166  CB AASP A 855     5039   3613   4216   -364    658    187       C  
ATOM   1167  CB BASP A 855       6.750 196.625  26.655  0.50 32.53           C  
ANISOU 1167  CB BASP A 855     4860   3456   4043   -361    643    166       C  
ATOM   1168  CG AASP A 855       6.920 195.127  27.650  0.50 34.99           C  
ANISOU 1168  CG AASP A 855     5281   3600   4411   -350    776    307       C  
ATOM   1169  CG BASP A 855       5.969 195.435  26.131  0.50 33.41           C  
ANISOU 1169  CG BASP A 855     5053   3430   4211   -504    737    106       C  
ATOM   1170  OD1AASP A 855       6.596 195.033  28.883  0.50 32.38           O  
ANISOU 1170  OD1AASP A 855     4929   3323   4049   -343    795    415       O  
ATOM   1171  OD1BASP A 855       5.531 194.624  26.976  0.50 34.27           O  
ANISOU 1171  OD1BASP A 855     5206   3466   4349   -551    818    183       O  
ATOM   1172  OD2AASP A 855       7.401 194.168  27.002  0.50 38.26           O1-
ANISOU 1172  OD2AASP A 855     5800   3835   4901   -345    860    296       O1-
ATOM   1173  OD2BASP A 855       5.769 195.329  24.912  0.50 31.49           O1-
ANISOU 1173  OD2BASP A 855     4824   3161   3977   -580    734    -17       O1-
ATOM   1174  N   PHE A 856       5.912 198.171  29.884  1.00 30.52           N  
ANISOU 1174  N   PHE A 856     4418   3547   3628   -301    568    326       N  
ATOM   1175  CA  PHE A 856       6.391 198.695  31.104  1.00 31.73           C  
ANISOU 1175  CA  PHE A 856     4524   3822   3708   -220    541    401       C  
ATOM   1176  C   PHE A 856       6.597 197.627  32.126  1.00 33.15           C  
ANISOU 1176  C   PHE A 856     4759   3963   3872   -197    619    553       C  
ATOM   1177  O   PHE A 856       6.663 197.937  33.289  1.00 30.32           O  
ANISOU 1177  O   PHE A 856     4351   3740   3428   -162    608    620       O  
ATOM   1178  CB  PHE A 856       5.371 199.707  31.615  1.00 32.03           C  
ANISOU 1178  CB  PHE A 856     4463   4012   3692   -269    504    331       C  
ATOM   1179  CG  PHE A 856       5.331 200.928  30.775  1.00 32.42           C  
ANISOU 1179  CG  PHE A 856     4452   4109   3757   -254    429    215       C  
ATOM   1180  CD1 PHE A 856       6.353 201.876  30.867  1.00 32.35           C  
ANISOU 1180  CD1 PHE A 856     4414   4151   3726   -164    371    198       C  
ATOM   1181  CD2 PHE A 856       4.319 201.104  29.849  1.00 32.87           C  
ANISOU 1181  CD2 PHE A 856     4477   4161   3851   -331    420    132       C  
ATOM   1182  CE1 PHE A 856       6.330 202.990  30.051  1.00 34.81           C  
ANISOU 1182  CE1 PHE A 856     4679   4480   4066   -150    316    108       C  
ATOM   1183  CE2 PHE A 856       4.285 202.220  29.052  1.00 33.32           C  
ANISOU 1183  CE2 PHE A 856     4475   4260   3922   -302    357     55       C  
ATOM   1184  CZ  PHE A 856       5.300 203.151  29.141  1.00 33.92           C  
ANISOU 1184  CZ  PHE A 856     4538   4357   3991   -209    311     48       C  
ATOM   1185  N   GLY A 857       6.732 196.381  31.691  1.00 33.53           N  
ANISOU 1185  N   GLY A 857     4910   3828   4002   -213    704    609       N  
ATOM   1186  CA  GLY A 857       6.954 195.264  32.606  1.00 36.22           C  
ANISOU 1186  CA  GLY A 857     5315   4097   4348   -177    798    784       C  
ATOM   1187  C   GLY A 857       8.173 195.332  33.505  1.00 36.32           C  
ANISOU 1187  C   GLY A 857     5304   4203   4293    -21    774    934       C  
ATOM   1188  O   GLY A 857       8.173 194.718  34.585  1.00 37.15           O  
ANISOU 1188  O   GLY A 857     5422   4339   4354     10    830   1097       O  
ATOM   1189  N   LEU A 858       9.208 196.041  33.068  1.00 33.70           N  
ANISOU 1189  N   LEU A 858     4931   3927   3945     70    695    889       N  
ATOM   1190  CA  LEU A 858      10.421 196.178  33.845  1.00 34.50           C  
ANISOU 1190  CA  LEU A 858     4984   4151   3970    209    659   1016       C  
ATOM   1191  C   LEU A 858      10.533 197.578  34.492  1.00 33.62           C  
ANISOU 1191  C   LEU A 858     4751   4288   3734    204    550    938       C  
ATOM   1192  O   LEU A 858      11.506 197.834  35.194  1.00 33.35           O  
ANISOU 1192  O   LEU A 858     4654   4404   3612    294    506   1018       O  
ATOM   1193  CB  LEU A 858      11.640 195.897  32.961  1.00 34.89           C  
ANISOU 1193  CB  LEU A 858     5066   4097   4092    318    662   1031       C  
ATOM   1194  CG  LEU A 858      11.797 194.437  32.424  1.00 37.68           C  
ANISOU 1194  CG  LEU A 858     5548   4191   4574    356    791   1120       C  
ATOM   1195  CD1 LEU A 858      13.132 194.274  31.753  1.00 37.21           C  
ANISOU 1195  CD1 LEU A 858     5494   4077   4564    494    792   1148       C  
ATOM   1196  CD2 LEU A 858      11.659 193.413  33.521  1.00 42.08           C  
ANISOU 1196  CD2 LEU A 858     6148   4713   5125    400    883   1329       C  
ATOM   1197  N   ALA A 859       9.560 198.465  34.272  1.00 30.91           N  
ANISOU 1197  N   ALA A 859     4369   3991   3382    101    514    782       N  
ATOM   1198  CA  ALA A 859       9.758 199.874  34.637  1.00 29.02           C  
ANISOU 1198  CA  ALA A 859     4031   3933   3060     99    426    675       C  
ATOM   1199  C   ALA A 859       9.683 200.095  36.149  1.00 31.18           C  
ANISOU 1199  C   ALA A 859     4242   4413   3192    103    420    736       C  
ATOM   1200  O   ALA A 859       8.982 199.366  36.841  1.00 31.51           O  
ANISOU 1200  O   ALA A 859     4307   4462   3201     72    483    830       O  
ATOM   1201  CB  ALA A 859       8.750 200.746  33.963  1.00 29.75           C  
ANISOU 1201  CB  ALA A 859     4101   4003   3198     12    403    510       C  
ATOM   1202  N   LYS A 860      10.428 201.087  36.649  1.00 30.76           N  
ANISOU 1202  N   LYS A 860     4107   4532   3048    130    348    679       N  
ATOM   1203  CA  LYS A 860      10.532 201.333  38.087  1.00 32.77           C  
ANISOU 1203  CA  LYS A 860     4291   5019   3139    131    335    722       C  
ATOM   1204  C   LYS A 860      10.386 202.813  38.321  1.00 33.57           C  
ANISOU 1204  C   LYS A 860     4320   5245   3190     73    284    526       C  
ATOM   1205  O   LYS A 860      10.950 203.641  37.569  1.00 31.26           O  
ANISOU 1205  O   LYS A 860     4010   4907   2959     76    235    414       O  
ATOM   1206  CB  LYS A 860      11.870 200.888  38.631  1.00 34.23           C  
ANISOU 1206  CB  LYS A 860     4439   5328   3239    230    305    871       C  
ATOM   1207  CG  LYS A 860      12.148 199.385  38.541  1.00 36.79           C  
ANISOU 1207  CG  LYS A 860     4836   5526   3616    318    374   1094       C  
ATOM   1208  CD  LYS A 860      11.202 198.557  39.383  1.00 39.29           C  
ANISOU 1208  CD  LYS A 860     5190   5851   3887    287    455   1221       C  
ATOM   1209  CE  LYS A 860      11.387 197.085  39.041  1.00 41.85           C  
ANISOU 1209  CE  LYS A 860     5614   5968   4319    362    546   1419       C  
ATOM   1210  NZ  LYS A 860      10.468 196.320  39.880  1.00 45.21           N1+
ANISOU 1210  NZ  LYS A 860     6075   6397   4704    319    634   1550       N1+
ATOM   1211  N   LEU A 861       9.674 203.131  39.392  1.00 34.81           N  
ANISOU 1211  N   LEU A 861     4435   5555   3234     23    306    490       N  
ATOM   1212  CA  LEU A 861       9.476 204.516  39.850  1.00 34.92           C  
ANISOU 1212  CA  LEU A 861     4383   5696   3188    -32    281    296       C  
ATOM   1213  C   LEU A 861      10.561 204.925  40.807  1.00 35.14           C  
ANISOU 1213  C   LEU A 861     4335   5959   3055    -24    229    288       C  
ATOM   1214  O   LEU A 861      10.794 204.267  41.827  1.00 37.52           O  
ANISOU 1214  O   LEU A 861     4606   6439   3208     -2    234    423       O  
ATOM   1215  CB  LEU A 861       8.101 204.653  40.514  1.00 36.59           C  
ANISOU 1215  CB  LEU A 861     4582   5964   3355    -92    345    243       C  
ATOM   1216  CG  LEU A 861       7.773 206.047  41.073  1.00 39.78           C  
ANISOU 1216  CG  LEU A 861     4925   6485   3702   -142    347     33       C  
ATOM   1217  CD1 LEU A 861       7.635 207.095  39.972  1.00 37.16           C  
ANISOU 1217  CD1 LEU A 861     4604   5984   3530   -146    333   -122       C  
ATOM   1218  CD2 LEU A 861       6.512 205.996  41.938  1.00 42.13           C  
ANISOU 1218  CD2 LEU A 861     5198   6883   3924   -186    422     11       C  
ATOM   1219  N   LEU A 862      11.256 206.001  40.495  1.00 33.34           N  
ANISOU 1219  N   LEU A 862     4070   5747   2849    -46    178    138       N  
ATOM   1220  CA  LEU A 862      12.287 206.515  41.379  1.00 34.25           C  
ANISOU 1220  CA  LEU A 862     4099   6107   2807    -68    125     93       C  
ATOM   1221  C   LEU A 862      11.694 207.455  42.433  1.00 34.85           C  
ANISOU 1221  C   LEU A 862     4128   6352   2760   -157    151    -85       C  
ATOM   1222  O   LEU A 862      10.771 208.218  42.149  1.00 34.35           O  
ANISOU 1222  O   LEU A 862     4093   6169   2789   -198    199   -238       O  
ATOM   1223  CB  LEU A 862      13.359 207.230  40.576  1.00 34.74           C  
ANISOU 1223  CB  LEU A 862     4138   6110   2950    -73     68      7       C  
ATOM   1224  CG  LEU A 862      14.258 206.385  39.673  1.00 36.71           C  
ANISOU 1224  CG  LEU A 862     4409   6255   3284     17     38    170       C  
ATOM   1225  CD1 LEU A 862      15.284 207.279  38.980  1.00 36.21           C  
ANISOU 1225  CD1 LEU A 862     4306   6167   3283     -7    -10     60       C  
ATOM   1226  CD2 LEU A 862      14.945 205.258  40.405  1.00 39.86           C  
ANISOU 1226  CD2 LEU A 862     4766   6822   3553     98     20    388       C  
ATOM   1227  N   GLY A 863      12.176 207.339  43.651  1.00 35.88           N  
ANISOU 1227  N   GLY A 863     4184   6770   2678   -178    127    -54       N  
ATOM   1228  CA  GLY A 863      11.870 208.305  44.694  1.00 41.18           C  
ANISOU 1228  CA  GLY A 863     4801   7641   3205   -274    148   -254       C  
ATOM   1229  C   GLY A 863      12.281 209.706  44.265  1.00 41.71           C  
ANISOU 1229  C   GLY A 863     4855   7633   3356   -350    135   -507       C  
ATOM   1230  O   GLY A 863      13.094 209.897  43.349  1.00 40.35           O  
ANISOU 1230  O   GLY A 863     4690   7336   3303   -333     89   -502       O  
ATOM   1231  N   ALA A 864      11.677 210.688  44.916  1.00 44.49           N  
ANISOU 1231  N   ALA A 864     5194   8050   3657   -434    190   -728       N  
ATOM   1232  CA  ALA A 864      11.831 212.074  44.526  1.00 46.84           C  
ANISOU 1232  CA  ALA A 864     5502   8226   4068   -508    213   -980       C  
ATOM   1233  C   ALA A 864      13.306 212.464  44.558  1.00 50.66           C  
ANISOU 1233  C   ALA A 864     5920   8838   4489   -571    133  -1034       C  
ATOM   1234  O   ALA A 864      13.756 213.160  43.681  1.00 51.55           O  
ANISOU 1234  O   ALA A 864     6055   8768   4761   -593    127  -1120       O  
ATOM   1235  CB  ALA A 864      11.023 212.981  45.439  1.00 49.92           C  
ANISOU 1235  CB  ALA A 864     5883   8701   4384   -586    300  -1213       C  
ATOM   1236  N   GLU A 865      14.071 212.003  45.525  1.00 53.10           N  
ANISOU 1236  N   GLU A 865     6138   9468   4566   -599     71   -969       N  
ATOM   1237  CA  GLU A 865      15.497 212.312  45.464  1.00 63.62           C  
ANISOU 1237  CA  GLU A 865     7389  10938   5844   -656    -11  -1003       C  
ATOM   1238  C   GLU A 865      16.319 211.024  45.400  1.00 66.50           C  
ANISOU 1238  C   GLU A 865     7700  11438   6129   -546    -95   -706       C  
ATOM   1239  O   GLU A 865      17.134 210.736  46.279  1.00 72.71           O  
ANISOU 1239  O   GLU A 865     8372  12559   6693   -569   -161   -647       O  
ATOM   1240  CB  GLU A 865      15.895 213.286  46.604  1.00 64.26           C  
ANISOU 1240  CB  GLU A 865     7385  11300   5728   -821    -12  -1261       C  
ATOM   1241  CG  GLU A 865      15.895 214.742  46.089  1.00 65.43           C  
ANISOU 1241  CG  GLU A 865     7580  11228   6052   -935     48  -1554       C  
ATOM   1242  CD  GLU A 865      15.604 215.808  47.138  1.00 63.94           C  
ANISOU 1242  CD  GLU A 865     7371  11183   5739  -1090    116  -1867       C  
ATOM   1243  OE1 GLU A 865      15.625 217.012  46.799  1.00 62.62           O  
ANISOU 1243  OE1 GLU A 865     7247  10826   5719  -1188    183  -2113       O  
ATOM   1244  OE2 GLU A 865      15.339 215.453  48.287  1.00 63.46           O1-
ANISOU 1244  OE2 GLU A 865     7256  11415   5439  -1114    115  -1870       O1-
ATOM   1245  N   GLU A 866      16.057 210.246  44.351  1.00 57.92           N  
ANISOU 1245  N   GLU A 866     6693  10090   5224   -423    -83   -520       N  
ATOM   1246  CA  GLU A 866      16.739 208.974  44.113  1.00 55.07           C  
ANISOU 1246  CA  GLU A 866     6308   9776   4841   -295   -134   -234       C  
ATOM   1247  C   GLU A 866      17.229 209.049  42.703  1.00 50.22           C  
ANISOU 1247  C   GLU A 866     5738   8898   4444   -250   -146   -214       C  
ATOM   1248  O   GLU A 866      16.476 209.404  41.790  1.00 48.48           O  
ANISOU 1248  O   GLU A 866     5616   8388   4414   -250    -93   -290       O  
ATOM   1249  CB  GLU A 866      15.794 207.790  44.247  1.00 57.26           C  
ANISOU 1249  CB  GLU A 866     6657   9975   5124   -192    -83    -25       C  
ATOM   1250  CG  GLU A 866      15.997 206.891  45.433  1.00 63.09           C  
ANISOU 1250  CG  GLU A 866     7325  11013   5633   -144   -102    169       C  
ATOM   1251  CD  GLU A 866      14.887 205.846  45.546  1.00 68.66           C  
ANISOU 1251  CD  GLU A 866     8118  11597   6371    -71    -26    348       C  
ATOM   1252  OE1 GLU A 866      14.219 205.537  44.535  1.00 63.36           O  
ANISOU 1252  OE1 GLU A 866     7554  10608   5910    -33     23    372       O  
ATOM   1253  OE2 GLU A 866      14.657 205.331  46.661  1.00 75.53           O1-
ANISOU 1253  OE2 GLU A 866     8946  12703   7047    -62    -13    465       O1-
ATOM   1254  N   LYS A 867      18.505 208.746  42.526  1.00 46.98           N  
ANISOU 1254  N   LYS A 867     5244   8610   3996   -211   -214   -111       N  
ATOM   1255  CA  LYS A 867      19.125 208.707  41.220  1.00 46.96           C  
ANISOU 1255  CA  LYS A 867     5267   8397   4176   -158   -224    -69       C  
ATOM   1256  C   LYS A 867      18.969 207.332  40.568  1.00 45.47           C  
ANISOU 1256  C   LYS A 867     5150   8044   4081      2   -199    181       C  
ATOM   1257  O   LYS A 867      18.868 207.221  39.339  1.00 45.09           O  
ANISOU 1257  O   LYS A 867     5181   7731   4218     46   -171    194       O  
ATOM   1258  CB  LYS A 867      20.636 209.018  41.352  1.00 49.54           C  
ANISOU 1258  CB  LYS A 867     5452   8957   4414   -193   -303    -78       C  
ATOM   1259  N   GLU A 868      18.988 206.281  41.382  1.00 41.97           N  
ANISOU 1259  N   GLU A 868     4678   7761   3506     89   -202    382       N  
ATOM   1260  CA  GLU A 868      19.217 204.932  40.859  1.00 42.59           C  
ANISOU 1260  CA  GLU A 868     4802   7715   3662    250   -176    636       C  
ATOM   1261  C   GLU A 868      18.180 203.926  41.320  1.00 41.79           C  
ANISOU 1261  C   GLU A 868     4787   7545   3547    307   -108    786       C  
ATOM   1262  O   GLU A 868      17.719 204.001  42.460  1.00 38.30           O  
ANISOU 1262  O   GLU A 868     4309   7302   2942    260   -108    784       O  
ATOM   1263  CB  GLU A 868      20.569 204.428  41.381  1.00 45.21           C  
ANISOU 1263  CB  GLU A 868     4995   8323   3860    340   -238    809       C  
ATOM   1264  CG  GLU A 868      21.724 205.271  40.911  1.00 48.48           C  
ANISOU 1264  CG  GLU A 868     5305   8827   4287    286   -303    691       C  
ATOM   1265  CD  GLU A 868      23.055 204.850  41.502  1.00 51.51           C  
ANISOU 1265  CD  GLU A 868     5518   9535   4515    367   -373    856       C  
ATOM   1266  OE1 GLU A 868      23.098 204.054  42.460  1.00 52.88           O  
ANISOU 1266  OE1 GLU A 868     5639   9915   4536    454   -382   1051       O  
ATOM   1267  OE2 GLU A 868      24.056 205.365  40.990  1.00 55.39           O1-
ANISOU 1267  OE2 GLU A 868     5921  10086   5038    340   -418    791       O1-
ATOM   1268  N   TYR A 869      17.874 202.960  40.460  1.00 37.66           N  
ANISOU 1268  N   TYR A 869     4371   6754   3183    401    -46    916       N  
ATOM   1269  CA  TYR A 869      17.207 201.732  40.867  1.00 39.81           C  
ANISOU 1269  CA  TYR A 869     4715   6959   3451    475     25   1118       C  
ATOM   1270  C   TYR A 869      18.267 200.610  40.873  1.00 40.64           C  
ANISOU 1270  C   TYR A 869     4788   7102   3552    644     31   1381       C  
ATOM   1271  O   TYR A 869      18.978 200.432  39.889  1.00 39.38           O  
ANISOU 1271  O   TYR A 869     4639   6803   3517    713     32   1396       O  
ATOM   1272  CB  TYR A 869      16.025 201.371  39.948  1.00 38.98           C  
ANISOU 1272  CB  TYR A 869     4757   6522   3531    447    106   1072       C  
ATOM   1273  CG  TYR A 869      15.459 199.988  40.235  1.00 41.77           C  
ANISOU 1273  CG  TYR A 869     5192   6767   3908    517    195   1289       C  
ATOM   1274  CD1 TYR A 869      14.662 199.750  41.362  1.00 45.48           C  
ANISOU 1274  CD1 TYR A 869     5657   7369   4254    478    228   1356       C  
ATOM   1275  CD2 TYR A 869      15.768 198.901  39.427  1.00 43.64           C  
ANISOU 1275  CD2 TYR A 869     5512   6775   4291    621    258   1432       C  
ATOM   1276  CE1 TYR A 869      14.195 198.461  41.672  1.00 48.45           C  
ANISOU 1276  CE1 TYR A 869     6108   7644   4656    537    321   1576       C  
ATOM   1277  CE2 TYR A 869      15.279 197.615  39.712  1.00 45.37           C  
ANISOU 1277  CE2 TYR A 869     5816   6869   4550    678    357   1633       C  
ATOM   1278  CZ  TYR A 869      14.507 197.400  40.831  1.00 48.13           C  
ANISOU 1278  CZ  TYR A 869     6159   7347   4781    635    387   1713       C  
ATOM   1279  OH  TYR A 869      14.044 196.130  41.091  1.00 50.01           O  
ANISOU 1279  OH  TYR A 869     6485   7445   5070    683    497   1922       O  
ATOM   1280  N   HIS A 870      18.390 199.880  41.975  1.00 42.35           N  
ANISOU 1280  N   HIS A 870     4956   7512   3621    718     41   1593       N  
ATOM   1281  CA  HIS A 870      19.326 198.745  42.043  1.00 46.60           C  
ANISOU 1281  CA  HIS A 870     5463   8076   4164    905     64   1879       C  
ATOM   1282  C   HIS A 870      18.579 197.418  41.934  1.00 46.06           C  
ANISOU 1282  C   HIS A 870     5539   7746   4215    987    190   2076       C  
ATOM   1283  O   HIS A 870      17.823 197.083  42.812  1.00 45.01           O  
ANISOU 1283  O   HIS A 870     5428   7684   3990    957    229   2166       O  
ATOM   1284  CB  HIS A 870      20.139 198.731  43.340  1.00 52.15           C  
ANISOU 1284  CB  HIS A 870     5997   9196   4618    962     -7   2036       C  
ATOM   1285  CG  HIS A 870      21.233 197.707  43.311  1.00 60.33           C  
ANISOU 1285  CG  HIS A 870     6976  10275   5670   1174      7   2328       C  
ATOM   1286  CD2 HIS A 870      22.403 197.677  42.625  1.00 61.25           C  
ANISOU 1286  CD2 HIS A 870     7020  10394   5856   1277    -23   2362       C  
ATOM   1287  ND1 HIS A 870      21.139 196.491  43.959  1.00 66.03           N  
ANISOU 1287  ND1 HIS A 870     7724  11003   6359   1321     82   2642       N  
ATOM   1288  CE1 HIS A 870      22.227 195.781  43.727  1.00 65.97           C  
ANISOU 1288  CE1 HIS A 870     7656  11012   6397   1517     94   2861       C  
ATOM   1289  NE2 HIS A 870      23.008 196.476  42.918  1.00 69.31           N  
ANISOU 1289  NE2 HIS A 870     8014  11441   6879   1493     29   2691       N  
ATOM   1290  N   ALA A 871      18.792 196.658  40.867  1.00 43.75           N  
ANISOU 1290  N   ALA A 871     5345   7151   4126   1080    264   2139       N  
ATOM   1291  CA  ALA A 871      17.933 195.498  40.627  1.00 46.30           C  
ANISOU 1291  CA  ALA A 871     5827   7174   4590   1110    399   2263       C  
ATOM   1292  C   ALA A 871      18.451 194.285  41.438  1.00 50.54           C  
ANISOU 1292  C   ALA A 871     6347   7774   5079   1292    465   2613       C  
ATOM   1293  O   ALA A 871      19.595 194.305  41.902  1.00 50.73           O  
ANISOU 1293  O   ALA A 871     6235   8049   4991   1419    402   2754       O  
ATOM   1294  CB  ALA A 871      17.888 195.197  39.133  1.00 44.40           C  
ANISOU 1294  CB  ALA A 871     5707   6581   4582   1116    462   2156       C  
ATOM   1295  N   GLU A 872      17.607 193.276  41.658  1.00 54.04           N  
ANISOU 1295  N   GLU A 872     6917   8016   5600   1300    590   2759       N  
ATOM   1296  CA  GLU A 872      18.084 191.979  42.140  1.00 60.21           C  
ANISOU 1296  CA  GLU A 872     7722   8747   6408   1494    690   3107       C  
ATOM   1297  C   GLU A 872      18.434 191.138  40.895  1.00 64.19           C  
ANISOU 1297  C   GLU A 872     8353   8864   7171   1597    802   3126       C  
ATOM   1298  O   GLU A 872      18.849 191.672  39.876  1.00 62.93           O  
ANISOU 1298  O   GLU A 872     8187   8627   7094   1574    757   2926       O  
ATOM   1299  CB  GLU A 872      17.051 191.303  43.062  1.00 63.76           C  
ANISOU 1299  CB  GLU A 872     8242   9173   6809   1448    783   3273       C  
ATOM   1300  N   GLY A 873      18.296 189.820  40.972  1.00 72.19           N  
ANISOU 1300  N   GLY A 873     9483   9630   8313   1710    959   3366       N  
ATOM   1301  CA  GLY A 873      18.345 188.991  39.770  1.00 71.26           C  
ANISOU 1301  CA  GLY A 873     9523   9095   8458   1762   1095   3332       C  
ATOM   1302  C   GLY A 873      17.103 189.191  38.911  1.00 71.08           C  
ANISOU 1302  C   GLY A 873     9637   8813   8554   1533   1133   3046       C  
ATOM   1303  O   GLY A 873      16.163 189.903  39.284  1.00 75.33           O  
ANISOU 1303  O   GLY A 873    10153   9480   8988   1352   1066   2903       O  
ATOM   1304  N   GLY A 874      17.089 188.557  37.751  1.00 70.56           N  
ANISOU 1304  N   GLY A 874     9709   8396   8703   1542   1245   2960       N  
ATOM   1305  CA  GLY A 874      16.011 188.766  36.794  1.00 67.29           C  
ANISOU 1305  CA  GLY A 874     9406   7766   8393   1327   1269   2677       C  
ATOM   1306  C   GLY A 874      16.610 188.993  35.429  1.00 66.97           C  
ANISOU 1306  C   GLY A 874     9389   7593   8463   1349   1259   2485       C  
ATOM   1307  O   GLY A 874      17.624 189.708  35.302  1.00 66.11           O  
ANISOU 1307  O   GLY A 874     9154   7687   8275   1442   1150   2462       O  
ATOM   1308  N   LYS A 875      15.986 188.346  34.436  1.00 67.77           N  
ANISOU 1308  N   LYS A 875     9649   7362   8739   1254   1380   2350       N  
ATOM   1309  CA  LYS A 875      16.335 188.453  33.023  1.00 63.14           C  
ANISOU 1309  CA  LYS A 875     9109   6619   8259   1240   1394   2140       C  
ATOM   1310  C   LYS A 875      16.144 189.877  32.579  1.00 59.88           C  
ANISOU 1310  C   LYS A 875     8591   6427   7731   1110   1222   1903       C  
ATOM   1311  O   LYS A 875      15.123 190.506  32.864  1.00 54.03           O  
ANISOU 1311  O   LYS A 875     7827   5786   6913    941   1153   1795       O  
ATOM   1312  CB  LYS A 875      15.446 187.536  32.173  1.00 64.95           C  
ANISOU 1312  CB  LYS A 875     9525   6489   8664   1108   1550   2015       C  
ATOM   1313  N   VAL A 876      17.131 190.389  31.862  1.00 57.46           N  
ANISOU 1313  N   VAL A 876     8220   6189   7422   1194   1164   1827       N  
ATOM   1314  CA  VAL A 876      17.043 191.719  31.307  1.00 55.81           C  
ANISOU 1314  CA  VAL A 876     7922   6152   7128   1081   1020   1610       C  
ATOM   1315  C   VAL A 876      17.742 191.644  29.955  1.00 51.65           C  
ANISOU 1315  C   VAL A 876     7430   5499   6695   1130   1056   1490       C  
ATOM   1316  O   VAL A 876      18.764 190.984  29.849  1.00 52.11           O  
ANISOU 1316  O   VAL A 876     7491   5489   6816   1308   1131   1616       O  
ATOM   1317  CB  VAL A 876      17.673 192.750  32.273  1.00 55.47           C  
ANISOU 1317  CB  VAL A 876     7705   6453   6916   1131    873   1681       C  
ATOM   1318  CG1 VAL A 876      16.716 193.071  33.424  1.00 55.53           C  
ANISOU 1318  CG1 VAL A 876     7683   6603   6811   1026    828   1715       C  
ATOM   1319  CG2 VAL A 876      18.984 192.215  32.821  1.00 59.05           C  
ANISOU 1319  CG2 VAL A 876     8087   6993   7354   1354    898   1914       C  
ATOM   1320  N   PRO A 877      17.165 192.258  28.904  1.00 48.31           N  
ANISOU 1320  N   PRO A 877     7031   5040   6281    979   1015   1256       N  
ATOM   1321  CA  PRO A 877      17.777 192.127  27.569  1.00 45.38           C  
ANISOU 1321  CA  PRO A 877     6699   4554   5987   1015   1061   1137       C  
ATOM   1322  C   PRO A 877      19.172 192.779  27.476  1.00 41.29           C  
ANISOU 1322  C   PRO A 877     6050   4221   5417   1157    988   1186       C  
ATOM   1323  O   PRO A 877      19.288 193.969  27.316  1.00 37.79           O  
ANISOU 1323  O   PRO A 877     5505   3965   4885   1092    863   1091       O  
ATOM   1324  CB  PRO A 877      16.773 192.818  26.643  1.00 47.61           C  
ANISOU 1324  CB  PRO A 877     7006   4834   6249    814   1005    902       C  
ATOM   1325  CG  PRO A 877      15.483 192.633  27.320  1.00 50.44           C  
ANISOU 1325  CG  PRO A 877     7406   5165   6595    681   1011    906       C  
ATOM   1326  CD  PRO A 877      15.785 192.751  28.814  1.00 51.47           C  
ANISOU 1326  CD  PRO A 877     7455   5451   6648    773    969   1106       C  
ATOM   1327  N   ILE A 878      20.206 191.960  27.569  1.00 41.44           N  
ANISOU 1327  N   ILE A 878     6070   4174   5498   1351   1079   1337       N  
ATOM   1328  CA  ILE A 878      21.588 192.416  27.731  1.00 44.03           C  
ANISOU 1328  CA  ILE A 878     6250   4707   5773   1506   1018   1434       C  
ATOM   1329  C   ILE A 878      22.109 193.357  26.630  1.00 40.37           C  
ANISOU 1329  C   ILE A 878     5721   4335   5283   1459    951   1262       C  
ATOM   1330  O   ILE A 878      22.851 194.305  26.905  1.00 39.51           O  
ANISOU 1330  O   ILE A 878     5460   4470   5081   1479    838   1280       O  
ATOM   1331  CB  ILE A 878      22.517 191.194  27.808  1.00 47.10           C  
ANISOU 1331  CB  ILE A 878     6668   4962   6266   1737   1161   1622       C  
ATOM   1332  CG1 ILE A 878      22.230 190.368  29.080  1.00 56.76           C  
ANISOU 1332  CG1 ILE A 878     7920   6148   7495   1819   1216   1857       C  
ATOM   1333  CG2 ILE A 878      23.981 191.595  27.790  1.00 50.04           C  
ANISOU 1333  CG2 ILE A 878     6874   5546   6591   1902   1111   1710       C  
ATOM   1334  CD1 ILE A 878      22.777 190.959  30.370  1.00 59.57           C  
ANISOU 1334  CD1 ILE A 878     8098   6840   7696   1891   1087   2036       C  
ATOM   1335  N   LYS A 879      21.722 193.090  25.393  1.00 38.33           N  
ANISOU 1335  N   LYS A 879     5574   3888   5100   1386   1025   1096       N  
ATOM   1336  CA  LYS A 879      22.245 193.860  24.255  1.00 38.11           C  
ANISOU 1336  CA  LYS A 879     5493   3935   5048   1354    984    951       C  
ATOM   1337  C   LYS A 879      21.726 195.293  24.166  1.00 35.75           C  
ANISOU 1337  C   LYS A 879     5119   3815   4649   1187    833    830       C  
ATOM   1338  O   LYS A 879      22.212 196.073  23.325  1.00 33.95           O  
ANISOU 1338  O   LYS A 879     4832   3675   4393   1160    789    738       O  
ATOM   1339  CB  LYS A 879      22.004 193.086  22.957  1.00 38.06           C  
ANISOU 1339  CB  LYS A 879     5628   3695   5136   1329   1117    810       C  
ATOM   1340  CG  LYS A 879      22.849 191.851  22.933  1.00 40.80           C  
ANISOU 1340  CG  LYS A 879     6028   3880   5595   1528   1276    924       C  
ATOM   1341  CD  LYS A 879      22.645 191.013  21.707  1.00 42.44           C  
ANISOU 1341  CD  LYS A 879     6384   3841   5898   1502   1428    767       C  
ATOM   1342  CE  LYS A 879      23.616 189.872  21.720  1.00 46.25           C  
ANISOU 1342  CE  LYS A 879     6907   4163   6502   1730   1597    889       C  
ATOM   1343  NZ  LYS A 879      23.436 189.066  20.491  1.00 49.65           N1+
ANISOU 1343  NZ  LYS A 879     7490   4347   7025   1694   1761    703       N1+
ATOM   1344  N   TRP A 880      20.733 195.642  24.996  1.00 32.84           N  
ANISOU 1344  N   TRP A 880     4754   3490   4232   1079    766    832       N  
ATOM   1345  CA  TRP A 880      20.217 197.001  25.084  1.00 32.47           C  
ANISOU 1345  CA  TRP A 880     4635   3600   4102    941    637    734       C  
ATOM   1346  C   TRP A 880      20.598 197.742  26.373  1.00 33.11           C  
ANISOU 1346  C   TRP A 880     4588   3901   4091    960    536    828       C  
ATOM   1347  O   TRP A 880      20.258 198.921  26.541  1.00 31.89           O  
ANISOU 1347  O   TRP A 880     4370   3869   3874    854    440    744       O  
ATOM   1348  CB  TRP A 880      18.677 197.001  24.959  1.00 33.37           C  
ANISOU 1348  CB  TRP A 880     4838   3618   4222    784    635    630       C  
ATOM   1349  CG  TRP A 880      18.201 196.828  23.564  1.00 31.94           C  
ANISOU 1349  CG  TRP A 880     4740   3313   4083    704    682    482       C  
ATOM   1350  CD1 TRP A 880      17.764 197.805  22.736  1.00 30.86           C  
ANISOU 1350  CD1 TRP A 880     4574   3244   3907    598    613    357       C  
ATOM   1351  CD2 TRP A 880      18.138 195.598  22.808  1.00 33.76           C  
ANISOU 1351  CD2 TRP A 880     5093   3339   4395    723    813    443       C  
ATOM   1352  CE2 TRP A 880      17.661 195.927  21.523  1.00 32.39           C  
ANISOU 1352  CE2 TRP A 880     4950   3151   4206    612    806    278       C  
ATOM   1353  CE3 TRP A 880      18.468 194.271  23.084  1.00 37.05           C  
ANISOU 1353  CE3 TRP A 880     5597   3582   4898    825    944    532       C  
ATOM   1354  NE1 TRP A 880      17.446 197.274  21.507  1.00 30.72           N  
ANISOU 1354  NE1 TRP A 880     4640   3111   3920    547    681    245       N  
ATOM   1355  CZ2 TRP A 880      17.492 194.971  20.525  1.00 35.26           C  
ANISOU 1355  CZ2 TRP A 880     5426   3349   4623    582    920    175       C  
ATOM   1356  CZ3 TRP A 880      18.275 193.324  22.123  1.00 39.68           C  
ANISOU 1356  CZ3 TRP A 880     6053   3714   5308    800   1069    431       C  
ATOM   1357  CH2 TRP A 880      17.784 193.681  20.847  1.00 38.73           C  
ANISOU 1357  CH2 TRP A 880     5960   3599   5156    669   1055    239       C  
ATOM   1358  N   MET A 881      21.312 197.076  27.267  1.00 34.71           N  
ANISOU 1358  N   MET A 881     4748   4159   4281   1097    563    999       N  
ATOM   1359  CA  MET A 881      21.575 197.573  28.607  1.00 36.09           C  
ANISOU 1359  CA  MET A 881     4806   4558   4347   1109    477   1095       C  
ATOM   1360  C   MET A 881      22.869 198.378  28.675  1.00 35.68           C  
ANISOU 1360  C   MET A 881     4594   4730   4232   1157    400   1110       C  
ATOM   1361  O   MET A 881      23.887 198.042  28.026  1.00 34.04           O  
ANISOU 1361  O   MET A 881     4352   4512   4070   1269    443   1153       O  
ATOM   1362  CB  MET A 881      21.710 196.392  29.584  1.00 37.66           C  
ANISOU 1362  CB  MET A 881     5025   4735   4548   1241    545   1303       C  
ATOM   1363  CG  MET A 881      20.387 195.742  30.027  1.00 39.24           C  
ANISOU 1363  CG  MET A 881     5350   4783   4775   1167    602   1319       C  
ATOM   1364  SD  MET A 881      20.696 194.131  30.787  1.00 43.56           S  
ANISOU 1364  SD  MET A 881     5955   5216   5378   1351    732   1586       S  
ATOM   1365  CE  MET A 881      21.623 194.540  32.271  1.00 45.18           C  
ANISOU 1365  CE  MET A 881     5970   5781   5415   1458    628   1781       C  
ATOM   1366  N   ALA A 882      22.844 199.415  29.505  1.00 34.10           N  
ANISOU 1366  N   ALA A 882     4291   4739   3924   1068    294   1073       N  
ATOM   1367  CA  ALA A 882      24.061 200.147  29.781  1.00 34.78           C  
ANISOU 1367  CA  ALA A 882     4212   5065   3936   1090    219   1091       C  
ATOM   1368  C   ALA A 882      25.066 199.283  30.482  1.00 36.41           C  
ANISOU 1368  C   ALA A 882     4328   5404   4103   1267    238   1299       C  
ATOM   1369  O   ALA A 882      24.713 198.373  31.229  1.00 37.12           O  
ANISOU 1369  O   ALA A 882     4461   5461   4179   1348    281   1442       O  
ATOM   1370  CB  ALA A 882      23.760 201.362  30.595  1.00 34.67           C  
ANISOU 1370  CB  ALA A 882     4120   5233   3817    946    118    991       C  
ATOM   1371  N   LEU A 883      26.346 199.562  30.259  1.00 36.82           N  
ANISOU 1371  N   LEU A 883     4240   5617   4133   1333    210   1333       N  
ATOM   1372  CA  LEU A 883      27.384 198.762  30.862  1.00 39.31           C  
ANISOU 1372  CA  LEU A 883     4441   6084   4408   1523    227   1548       C  
ATOM   1373  C   LEU A 883      27.271 198.703  32.382  1.00 38.56           C  
ANISOU 1373  C   LEU A 883     4264   6217   4169   1531    161   1672       C  
ATOM   1374  O   LEU A 883      27.418 197.620  32.974  1.00 38.65           O  
ANISOU 1374  O   LEU A 883     4279   6230   4176   1696    216   1887       O  
ATOM   1375  CB  LEU A 883      28.768 199.277  30.469  1.00 42.30           C  
ANISOU 1375  CB  LEU A 883     4646   6661   4763   1563    188   1548       C  
ATOM   1376  CG  LEU A 883      29.937 198.443  30.956  1.00 44.84           C  
ANISOU 1376  CG  LEU A 883     4826   7157   5052   1784    210   1781       C  
ATOM   1377  CD1 LEU A 883      29.819 196.968  30.561  1.00 45.92           C  
ANISOU 1377  CD1 LEU A 883     5094   7028   5323   1990    360   1932       C  
ATOM   1378  CD2 LEU A 883      31.223 199.017  30.417  1.00 49.13           C  
ANISOU 1378  CD2 LEU A 883     5194   7889   5581   1800    177   1754       C  
ATOM   1379  N   GLU A 884      26.966 199.834  33.027  1.00 37.58           N  
ANISOU 1379  N   GLU A 884     4073   6276   3927   1355     56   1541       N  
ATOM   1380  CA  GLU A 884      26.807 199.847  34.487  1.00 38.38           C  
ANISOU 1380  CA  GLU A 884     4094   6622   3864   1341     -7   1633       C  
ATOM   1381  C   GLU A 884      25.618 199.002  34.973  1.00 39.06           C  
ANISOU 1381  C   GLU A 884     4332   6535   3971   1366     60   1719       C  
ATOM   1382  O   GLU A 884      25.592 198.546  36.120  1.00 37.72           O  
ANISOU 1382  O   GLU A 884     4110   6537   3683   1427     44   1882       O  
ATOM   1383  CB  GLU A 884      26.705 201.276  35.083  1.00 39.21           C  
ANISOU 1383  CB  GLU A 884     4105   6953   3839   1132   -120   1441       C  
ATOM   1384  CG  GLU A 884      25.419 202.082  34.804  1.00 37.13           C  
ANISOU 1384  CG  GLU A 884     3978   6501   3626    948   -116   1220       C  
ATOM   1385  CD  GLU A 884      25.417 202.765  33.428  1.00 36.19           C  
ANISOU 1385  CD  GLU A 884     3919   6183   3647    872    -95   1052       C  
ATOM   1386  OE1 GLU A 884      24.462 203.515  33.120  1.00 35.10           O  
ANISOU 1386  OE1 GLU A 884     3872   5907   3555    735    -95    883       O  
ATOM   1387  OE2 GLU A 884      26.381 202.556  32.637  1.00 37.24           O1-
ANISOU 1387  OE2 GLU A 884     4000   6305   3842    956    -75   1099       O1-
ATOM   1388  N   SER A 885      24.648 198.795  34.099  1.00 35.64           N  
ANISOU 1388  N   SER A 885     4078   5782   3680   1312    135   1614       N  
ATOM   1389  CA  SER A 885      23.499 197.982  34.469  1.00 36.64           C  
ANISOU 1389  CA  SER A 885     4348   5731   3841   1315    209   1683       C  
ATOM   1390  C   SER A 885      23.884 196.526  34.393  1.00 38.12           C  
ANISOU 1390  C   SER A 885     4589   5777   4116   1520    322   1914       C  
ATOM   1391  O   SER A 885      23.475 195.756  35.242  1.00 40.67           O  
ANISOU 1391  O   SER A 885     4949   6098   4406   1580    366   2083       O  
ATOM   1392  CB  SER A 885      22.322 198.244  33.531  1.00 34.13           C  
ANISOU 1392  CB  SER A 885     4186   5140   3639   1178    250   1488       C  
ATOM   1393  OG  SER A 885      21.956 199.601  33.553  1.00 33.05           O  
ANISOU 1393  OG  SER A 885     4005   5106   3444   1010    161   1287       O  
ATOM   1394  N   ILE A 886      24.711 196.166  33.407  1.00 38.04           N  
ANISOU 1394  N   ILE A 886     4579   5656   4217   1632    376   1929       N  
ATOM   1395  CA  ILE A 886      25.224 194.806  33.280  1.00 40.16           C  
ANISOU 1395  CA  ILE A 886     4892   5778   4586   1850    500   2146       C  
ATOM   1396  C   ILE A 886      26.116 194.482  34.452  1.00 43.30           C  
ANISOU 1396  C   ILE A 886     5127   6466   4859   2011    461   2403       C  
ATOM   1397  O   ILE A 886      25.934 193.470  35.090  1.00 45.41           O  
ANISOU 1397  O   ILE A 886     5442   6668   5141   2138    540   2621       O  
ATOM   1398  CB  ILE A 886      26.025 194.577  31.987  1.00 41.30           C  
ANISOU 1398  CB  ILE A 886     5050   5778   4863   1944    569   2093       C  
ATOM   1399  CG1 ILE A 886      25.132 194.803  30.770  1.00 40.09           C  
ANISOU 1399  CG1 ILE A 886     5058   5351   4821   1791    613   1853       C  
ATOM   1400  CG2 ILE A 886      26.578 193.157  31.926  1.00 44.17           C  
ANISOU 1400  CG2 ILE A 886     5460   5980   5342   2189    716   2320       C  
ATOM   1401  CD1 ILE A 886      25.892 194.829  29.464  1.00 41.32           C  
ANISOU 1401  CD1 ILE A 886     5213   5416   5070   1845    663   1762       C  
ATOM   1402  N   LEU A 887      27.077 195.338  34.750  1.00 44.39           N  
ANISOU 1402  N   LEU A 887     5064   6934   4866   2002    340   2384       N  
ATOM   1403  CA  LEU A 887      28.080 195.025  35.783  1.00 45.75           C  
ANISOU 1403  CA  LEU A 887     5046   7434   4903   2167    293   2637       C  
ATOM   1404  C   LEU A 887      27.573 195.209  37.210  1.00 45.79           C  
ANISOU 1404  C   LEU A 887     4993   7687   4716   2100    216   2722       C  
ATOM   1405  O   LEU A 887      28.006 194.515  38.127  1.00 47.45           O  
ANISOU 1405  O   LEU A 887     5113   8077   4836   2264    223   2994       O  
ATOM   1406  CB  LEU A 887      29.299 195.926  35.600  1.00 46.36           C  
ANISOU 1406  CB  LEU A 887     4907   7812   4893   2150    186   2566       C  
ATOM   1407  CG  LEU A 887      30.053 195.822  34.287  1.00 47.71           C  
ANISOU 1407  CG  LEU A 887     5080   7829   5216   2231    251   2506       C  
ATOM   1408  CD1 LEU A 887      31.104 196.924  34.234  1.00 48.51           C  
ANISOU 1408  CD1 LEU A 887     4962   8260   5209   2151    129   2407       C  
ATOM   1409  CD2 LEU A 887      30.699 194.453  34.160  1.00 50.80           C  
ANISOU 1409  CD2 LEU A 887     5477   8108   5715   2524    382   2774       C  
ATOM   1410  N   HIS A 888      26.669 196.163  37.426  1.00 44.16           N  
ANISOU 1410  N   HIS A 888     4830   7508   4438   1866    145   2497       N  
ATOM   1411  CA  HIS A 888      26.291 196.533  38.791  1.00 46.32           C  
ANISOU 1411  CA  HIS A 888     5024   8074   4501   1782     62   2536       C  
ATOM   1412  C   HIS A 888      24.798 196.540  39.081  1.00 45.82           C  
ANISOU 1412  C   HIS A 888     5124   7834   4449   1642    102   2444       C  
ATOM   1413  O   HIS A 888      24.390 196.789  40.215  1.00 46.83           O  
ANISOU 1413  O   HIS A 888     5200   8191   4402   1573     50   2474       O  
ATOM   1414  CB  HIS A 888      26.894 197.898  39.144  1.00 47.33           C  
ANISOU 1414  CB  HIS A 888     4967   8555   4461   1628    -86   2355       C  
ATOM   1415  CG  HIS A 888      28.388 197.929  39.064  1.00 50.38           C  
ANISOU 1415  CG  HIS A 888     5150   9196   4796   1748   -139   2459       C  
ATOM   1416  CD2 HIS A 888      29.326 197.211  39.714  1.00 53.93           C  
ANISOU 1416  CD2 HIS A 888     5443   9900   5148   1950   -152   2742       C  
ATOM   1417  ND1 HIS A 888      29.073 198.740  38.181  1.00 51.47           N  
ANISOU 1417  ND1 HIS A 888     5220   9342   4993   1672   -179   2277       N  
ATOM   1418  CE1 HIS A 888      30.373 198.543  38.317  1.00 52.54           C  
ANISOU 1418  CE1 HIS A 888     5156   9740   5063   1808   -218   2430       C  
ATOM   1419  NE2 HIS A 888      30.550 197.616  39.237  1.00 55.96           N  
ANISOU 1419  NE2 HIS A 888     5529  10331   5401   1985   -205   2716       N  
ATOM   1420  N   ARG A 889      23.986 196.258  38.069  1.00 44.53           N  
ANISOU 1420  N   ARG A 889     5150   7288   4481   1597    195   2330       N  
ATOM   1421  CA  ARG A 889      22.552 196.183  38.229  1.00 43.95           C  
ANISOU 1421  CA  ARG A 889     5227   7035   4438   1469    243   2248       C  
ATOM   1422  C   ARG A 889      21.994 197.539  38.601  1.00 41.71           C  
ANISOU 1422  C   ARG A 889     4893   6921   4033   1259    141   2006       C  
ATOM   1423  O   ARG A 889      20.966 197.627  39.229  1.00 42.14           O  
ANISOU 1423  O   ARG A 889     5000   6981   4028   1162    151   1972       O  
ATOM   1424  CB  ARG A 889      22.177 195.077  39.245  1.00 47.88           C  
ANISOU 1424  CB  ARG A 889     5760   7546   4884   1575    317   2521       C  
ATOM   1425  CG  ARG A 889      22.810 193.748  38.862  1.00 52.65           C  
ANISOU 1425  CG  ARG A 889     6417   7956   5630   1803    437   2769       C  
ATOM   1426  CD  ARG A 889      22.117 192.520  39.456  1.00 59.30           C  
ANISOU 1426  CD  ARG A 889     7379   8632   6519   1881    565   3006       C  
ATOM   1427  NE  ARG A 889      21.946 192.639  40.894  1.00 64.51           N  
ANISOU 1427  NE  ARG A 889     7938   9615   6958   1871    505   3156       N  
ATOM   1428  CZ  ARG A 889      22.582 191.934  41.834  1.00 75.62           C  
ANISOU 1428  CZ  ARG A 889     9251  11219   8260   2055    520   3480       C  
ATOM   1429  NH1 ARG A 889      23.480 191.001  41.518  1.00 75.88           N1+
ANISOU 1429  NH1 ARG A 889     9277  11144   8407   2291    603   3712       N1+
ATOM   1430  NH2 ARG A 889      22.298 192.164  43.123  1.00 76.68           N  
ANISOU 1430  NH2 ARG A 889     9294  11673   8165   2009    457   3580       N  
ATOM   1431  N   ILE A 890      22.655 198.596  38.145  1.00 42.00           N  
ANISOU 1431  N   ILE A 890     4836   7071   4052   1186     56   1830       N  
ATOM   1432  CA  ILE A 890      22.213 199.973  38.373  1.00 41.63           C  
ANISOU 1432  CA  ILE A 890     4749   7146   3922    988    -24   1579       C  
ATOM   1433  C   ILE A 890      21.487 200.510  37.138  1.00 40.06           C  
ANISOU 1433  C   ILE A 890     4675   6653   3892    882      7   1363       C  
ATOM   1434  O   ILE A 890      21.985 200.428  36.003  1.00 38.81           O  
ANISOU 1434  O   ILE A 890     4545   6336   3863    927     31   1335       O  
ATOM   1435  CB  ILE A 890      23.428 200.860  38.718  1.00 45.81           C  
ANISOU 1435  CB  ILE A 890     5087   7998   4320    956   -132   1521       C  
ATOM   1436  CG1 ILE A 890      23.962 200.503  40.117  1.00 51.12           C  
ANISOU 1436  CG1 ILE A 890     5615   9035   4773   1025   -184   1710       C  
ATOM   1437  CG2 ILE A 890      23.069 202.327  38.698  1.00 44.88           C  
ANISOU 1437  CG2 ILE A 890     4951   7933   4169    749   -192   1235       C  
ATOM   1438  CD1 ILE A 890      25.407 200.912  40.317  1.00 56.08           C  
ANISOU 1438  CD1 ILE A 890     6036   9980   5289   1055   -276   1738       C  
ATOM   1439  N   TYR A 891      20.289 201.049  37.368  1.00 38.18           N  
ANISOU 1439  N   TYR A 891     4505   6357   3643    747     12   1220       N  
ATOM   1440  CA  TYR A 891      19.495 201.657  36.319  1.00 35.64           C  
ANISOU 1440  CA  TYR A 891     4281   5801   3458    645     33   1026       C  
ATOM   1441  C   TYR A 891      19.111 203.086  36.691  1.00 34.46           C  
ANISOU 1441  C   TYR A 891     4082   5769   3240    491    -25    811       C  
ATOM   1442  O   TYR A 891      18.759 203.391  37.857  1.00 33.83           O  
ANISOU 1442  O   TYR A 891     3953   5880   3020    434    -48    791       O  
ATOM   1443  CB  TYR A 891      18.236 200.835  36.108  1.00 36.48           C  
ANISOU 1443  CB  TYR A 891     4529   5679   3651    640    120   1065       C  
ATOM   1444  CG  TYR A 891      18.513 199.408  35.676  1.00 36.69           C  
ANISOU 1444  CG  TYR A 891     4633   5534   3773    777    204   1254       C  
ATOM   1445  CD1 TYR A 891      18.841 198.447  36.599  1.00 37.86           C  
ANISOU 1445  CD1 TYR A 891     4759   5775   3851    890    237   1479       C  
ATOM   1446  CD2 TYR A 891      18.427 199.037  34.339  1.00 34.27           C  
ANISOU 1446  CD2 TYR A 891     4424   4970   3627    793    261   1203       C  
ATOM   1447  CE1 TYR A 891      19.100 197.135  36.221  1.00 39.92           C  
ANISOU 1447  CE1 TYR A 891     5100   5847   4220   1026    335   1657       C  
ATOM   1448  CE2 TYR A 891      18.665 197.734  33.949  1.00 36.35           C  
ANISOU 1448  CE2 TYR A 891     4769   5054   3987    911    357   1350       C  
ATOM   1449  CZ  TYR A 891      19.002 196.797  34.876  1.00 39.67           C  
ANISOU 1449  CZ  TYR A 891     5174   5538   4359   1031    399   1575       C  
ATOM   1450  OH  TYR A 891      19.229 195.516  34.456  1.00 41.72           O  
ANISOU 1450  OH  TYR A 891     5528   5584   4741   1155    514   1719       O  
ATOM   1451  N   THR A 892      19.141 203.940  35.679  1.00 32.77           N  
ANISOU 1451  N   THR A 892     3888   5431   3132    426    -36    654       N  
ATOM   1452  CA  THR A 892      18.861 205.339  35.829  1.00 31.57           C  
ANISOU 1452  CA  THR A 892     3701   5332   2958    292    -72    448       C  
ATOM   1453  C   THR A 892      18.241 205.825  34.530  1.00 30.21           C  
ANISOU 1453  C   THR A 892     3618   4910   2948    252    -40    337       C  
ATOM   1454  O   THR A 892      18.151 205.100  33.519  1.00 29.17           O  
ANISOU 1454  O   THR A 892     3561   4599   2923    317     -2    405       O  
ATOM   1455  CB  THR A 892      20.165 206.164  36.021  1.00 33.62           C  
ANISOU 1455  CB  THR A 892     3831   5791   3151    252   -138    385       C  
ATOM   1456  CG2 THR A 892      20.976 205.738  37.225  1.00 35.06           C  
ANISOU 1456  CG2 THR A 892     3891   6275   3153    293   -186    502       C  
ATOM   1457  OG1 THR A 892      20.949 206.031  34.841  1.00 33.19           O  
ANISOU 1457  OG1 THR A 892     3778   5623   3208    307   -133    420       O  
ATOM   1458  N   HIS A 893      17.856 207.091  34.516  1.00 29.55           N  
ANISOU 1458  N   HIS A 893     3524   4818   2883    147    -52    162       N  
ATOM   1459  CA  HIS A 893      17.418 207.698  33.251  1.00 27.71           C  
ANISOU 1459  CA  HIS A 893     3354   4377   2796    118    -29     75       C  
ATOM   1460  C   HIS A 893      18.509 207.631  32.229  1.00 27.45           C  
ANISOU 1460  C   HIS A 893     3302   4300   2827    160    -41    116       C  
ATOM   1461  O   HIS A 893      18.250 207.441  31.032  1.00 27.09           O  
ANISOU 1461  O   HIS A 893     3322   4083   2886    188    -13    128       O  
ATOM   1462  CB  HIS A 893      16.945 209.140  33.495  1.00 29.71           C  
ANISOU 1462  CB  HIS A 893     3591   4627   3066     12    -27   -104       C  
ATOM   1463  CG  HIS A 893      15.798 209.220  34.446  1.00 30.04           C  
ANISOU 1463  CG  HIS A 893     3652   4711   3051    -21     -2   -156       C  
ATOM   1464  CD2 HIS A 893      15.690 209.786  35.673  1.00 31.43           C  
ANISOU 1464  CD2 HIS A 893     3776   5048   3115    -87     -5   -251       C  
ATOM   1465  ND1 HIS A 893      14.599 208.568  34.217  1.00 30.45           N  
ANISOU 1465  ND1 HIS A 893     3773   4651   3143     10     37   -104       N  
ATOM   1466  CE1 HIS A 893      13.799 208.762  35.250  1.00 28.41           C  
ANISOU 1466  CE1 HIS A 893     3504   4481   2809    -28     59   -158       C  
ATOM   1467  NE2 HIS A 893      14.425 209.509  36.127  1.00 29.71           N  
ANISOU 1467  NE2 HIS A 893     3600   4806   2881    -84     36   -252       N  
ATOM   1468  N   GLN A 894      19.756 207.765  32.683  1.00 28.75           N  
ANISOU 1468  N   GLN A 894     3364   4640   2917    164    -82    139       N  
ATOM   1469  CA  GLN A 894      20.910 207.720  31.771  1.00 29.81           C  
ANISOU 1469  CA  GLN A 894     3457   4763   3103    205    -90    182       C  
ATOM   1470  C   GLN A 894      21.223 206.306  31.246  1.00 30.68           C  
ANISOU 1470  C   GLN A 894     3606   4808   3243    345    -58    347       C  
ATOM   1471  O   GLN A 894      21.767 206.157  30.147  1.00 30.28           O  
ANISOU 1471  O   GLN A 894     3567   4667   3270    388    -36    369       O  
ATOM   1472  CB  GLN A 894      22.114 208.410  32.432  1.00 32.83           C  
ANISOU 1472  CB  GLN A 894     3700   5375   3398    145   -145    139       C  
ATOM   1473  CG  GLN A 894      21.843 209.906  32.717  1.00 33.13           C  
ANISOU 1473  CG  GLN A 894     3722   5420   3446    -10   -153    -56       C  
ATOM   1474  CD  GLN A 894      21.341 210.636  31.458  1.00 33.27           C  
ANISOU 1474  CD  GLN A 894     3825   5195   3620    -44   -109   -128       C  
ATOM   1475  NE2 GLN A 894      22.228 210.839  30.510  1.00 32.76           N  
ANISOU 1475  NE2 GLN A 894     3728   5098   3618    -39   -106   -105       N  
ATOM   1476  OE1 GLN A 894      20.146 210.952  31.319  1.00 32.88           O  
ANISOU 1476  OE1 GLN A 894     3862   5002   3629    -62    -75   -186       O  
ATOM   1477  N   SER A 895      20.872 205.255  31.988  1.00 29.65           N  
ANISOU 1477  N   SER A 895     3500   4707   3056    418    -40    464       N  
ATOM   1478  CA  SER A 895      20.908 203.916  31.391  1.00 29.63           C  
ANISOU 1478  CA  SER A 895     3572   4568   3118    542     20    599       C  
ATOM   1479  C   SER A 895      19.837 203.729  30.319  1.00 30.84           C  
ANISOU 1479  C   SER A 895     3856   4478   3383    512     73    536       C  
ATOM   1480  O   SER A 895      20.058 203.037  29.332  1.00 30.24           O  
ANISOU 1480  O   SER A 895     3837   4267   3385    576    122    574       O  
ATOM   1481  CB  SER A 895      20.924 202.811  32.458  1.00 32.99           C  
ANISOU 1481  CB  SER A 895     3989   5078   3466    636     38    766       C  
ATOM   1482  OG  SER A 895      19.749 202.759  33.204  1.00 33.27           O  
ANISOU 1482  OG  SER A 895     4079   5102   3461    575     48    747       O  
ATOM   1483  N   ASP A 896      18.674 204.350  30.495  1.00 30.87           N  
ANISOU 1483  N   ASP A 896     3899   4438   3390    414     65    433       N  
ATOM   1484  CA  ASP A 896      17.664 204.355  29.460  1.00 29.33           C  
ANISOU 1484  CA  ASP A 896     3798   4061   3285    373    100    366       C  
ATOM   1485  C   ASP A 896      18.200 205.056  28.192  1.00 28.08           C  
ANISOU 1485  C   ASP A 896     3629   3846   3193    359     91    300       C  
ATOM   1486  O   ASP A 896      17.853 204.651  27.096  1.00 24.86           O  
ANISOU 1486  O   ASP A 896     3290   3307   2847    368    126    291       O  
ATOM   1487  CB  ASP A 896      16.359 205.054  29.914  1.00 27.99           C  
ANISOU 1487  CB  ASP A 896     3644   3886   3104    281     90    272       C  
ATOM   1488  CG  ASP A 896      15.370 204.121  30.671  1.00 30.79           C  
ANISOU 1488  CG  ASP A 896     4048   4221   3426    281    128    334       C  
ATOM   1489  OD1 ASP A 896      15.592 202.868  30.778  1.00 28.96           O  
ANISOU 1489  OD1 ASP A 896     3859   3944   3197    349    172    454       O  
ATOM   1490  OD2 ASP A 896      14.361 204.697  31.153  1.00 29.80           O1-
ANISOU 1490  OD2 ASP A 896     3919   4122   3282    213    125    261       O1-
ATOM   1491  N   VAL A 897      19.019 206.110  28.351  1.00 27.13           N  
ANISOU 1491  N   VAL A 897     3422   3833   3051    324     47    252       N  
ATOM   1492  CA  VAL A 897      19.610 206.785  27.196  1.00 26.16           C  
ANISOU 1492  CA  VAL A 897     3284   3666   2989    307     47    209       C  
ATOM   1493  C   VAL A 897      20.541 205.824  26.410  1.00 26.28           C  
ANISOU 1493  C   VAL A 897     3304   3656   3025    405     82    296       C  
ATOM   1494  O   VAL A 897      20.561 205.843  25.178  1.00 25.49           O  
ANISOU 1494  O   VAL A 897     3243   3462   2979    409    110    275       O  
ATOM   1495  CB  VAL A 897      20.367 208.072  27.634  1.00 26.42           C  
ANISOU 1495  CB  VAL A 897     3219   3817   3000    233      5    139       C  
ATOM   1496  CG1 VAL A 897      21.239 208.598  26.508  1.00 27.56           C  
ANISOU 1496  CG1 VAL A 897     3334   3936   3201    225     14    131       C  
ATOM   1497  CG2 VAL A 897      19.396 209.142  28.057  1.00 26.89           C  
ANISOU 1497  CG2 VAL A 897     3295   3844   3075    140     -1     29       C  
ATOM   1498  N   TRP A 898      21.294 204.985  27.102  1.00 27.19           N  
ANISOU 1498  N   TRP A 898     3376   3858   3094    491     86    396       N  
ATOM   1499  CA  TRP A 898      22.062 203.908  26.397  1.00 27.92           C  
ANISOU 1499  CA  TRP A 898     3487   3899   3222    610    143    485       C  
ATOM   1500  C   TRP A 898      21.147 203.055  25.540  1.00 28.50           C  
ANISOU 1500  C   TRP A 898     3694   3776   3359    623    210    469       C  
ATOM   1501  O   TRP A 898      21.386 202.871  24.358  1.00 29.14           O  
ANISOU 1501  O   TRP A 898     3811   3776   3485    642    252    441       O  
ATOM   1502  CB  TRP A 898      22.818 203.044  27.375  1.00 28.88           C  
ANISOU 1502  CB  TRP A 898     3547   4132   3291    722    148    621       C  
ATOM   1503  CG  TRP A 898      23.684 202.006  26.757  1.00 29.11           C  
ANISOU 1503  CG  TRP A 898     3582   4110   3367    865    218    719       C  
ATOM   1504  CD1 TRP A 898      23.294 200.982  25.931  1.00 29.57           C  
ANISOU 1504  CD1 TRP A 898     3763   3968   3504    924    310    729       C  
ATOM   1505  CD2 TRP A 898      25.104 201.866  26.906  1.00 29.50           C  
ANISOU 1505  CD2 TRP A 898     3504   4313   3389    968    212    813       C  
ATOM   1506  CE2 TRP A 898      25.489 200.753  26.139  1.00 31.34           C  
ANISOU 1506  CE2 TRP A 898     3796   4414   3697   1104    311    881       C  
ATOM   1507  CE3 TRP A 898      26.079 202.563  27.627  1.00 29.24           C  
ANISOU 1507  CE3 TRP A 898     3306   4528   3274    954    137    839       C  
ATOM   1508  NE1 TRP A 898      24.363 200.259  25.537  1.00 30.63           N  
ANISOU 1508  NE1 TRP A 898     3865   4102   3671   1063    370    814       N  
ATOM   1509  CZ2 TRP A 898      26.830 200.328  26.050  1.00 31.45           C  
ANISOU 1509  CZ2 TRP A 898     3703   4533   3713   1248    340    989       C  
ATOM   1510  CZ3 TRP A 898      27.395 202.138  27.564  1.00 30.84           C  
ANISOU 1510  CZ3 TRP A 898     3391   4859   3467   1082    153    950       C  
ATOM   1511  CH2 TRP A 898      27.766 201.040  26.780  1.00 32.23           C  
ANISOU 1511  CH2 TRP A 898     3622   4897   3724   1238    255   1031       C  
ATOM   1512  N   SER A 899      20.061 202.547  26.123  1.00 27.95           N  
ANISOU 1512  N   SER A 899     3695   3641   3284    598    224    477       N  
ATOM   1513  CA  SER A 899      19.080 201.769  25.360  1.00 27.97           C  
ANISOU 1513  CA  SER A 899     3818   3468   3341    576    286    442       C  
ATOM   1514  C   SER A 899      18.505 202.534  24.163  1.00 25.60           C  
ANISOU 1514  C   SER A 899     3542   3120   3065    489    271    327       C  
ATOM   1515  O   SER A 899      18.260 201.955  23.102  1.00 26.51           O  
ANISOU 1515  O   SER A 899     3728   3130   3214    485    322    289       O  
ATOM   1516  CB  SER A 899      17.944 201.357  26.289  1.00 27.81           C  
ANISOU 1516  CB  SER A 899     3845   3419   3303    533    293    460       C  
ATOM   1517  OG  SER A 899      18.456 200.670  27.431  1.00 28.70           O  
ANISOU 1517  OG  SER A 899     3931   3594   3379    618    308    591       O  
ATOM   1518  N   TYR A 900      18.286 203.843  24.345  1.00 26.92           N  
ANISOU 1518  N   TYR A 900     3648   3368   3212    418    205    272       N  
ATOM   1519  CA  TYR A 900      17.809 204.703  23.279  1.00 27.17           C  
ANISOU 1519  CA  TYR A 900     3686   3369   3265    353    189    196       C  
ATOM   1520  C   TYR A 900      18.768 204.719  22.097  1.00 26.28           C  
ANISOU 1520  C   TYR A 900     3564   3252   3169    389    214    198       C  
ATOM   1521  O   TYR A 900      18.337 204.602  20.929  1.00 26.87           O  
ANISOU 1521  O   TYR A 900     3686   3272   3252    364    237    157       O  
ATOM   1522  CB  TYR A 900      17.590 206.134  23.805  1.00 26.74           C  
ANISOU 1522  CB  TYR A 900     3568   3385   3207    291    133    152       C  
ATOM   1523  CG  TYR A 900      17.187 207.121  22.753  1.00 26.99           C  
ANISOU 1523  CG  TYR A 900     3598   3385   3271    243    123    106       C  
ATOM   1524  CD1 TYR A 900      15.857 207.299  22.418  1.00 25.13           C  
ANISOU 1524  CD1 TYR A 900     3395   3105   3045    202    119     73       C  
ATOM   1525  CD2 TYR A 900      18.143 207.893  22.079  1.00 28.33           C  
ANISOU 1525  CD2 TYR A 900     3723   3581   3459    243    120    111       C  
ATOM   1526  CE1 TYR A 900      15.476 208.231  21.469  1.00 27.35           C  
ANISOU 1526  CE1 TYR A 900     3663   3374   3352    176    109     59       C  
ATOM   1527  CE2 TYR A 900      17.769 208.799  21.111  1.00 26.94           C  
ANISOU 1527  CE2 TYR A 900     3546   3375   3312    208    118     96       C  
ATOM   1528  CZ  TYR A 900      16.449 208.973  20.806  1.00 27.77           C  
ANISOU 1528  CZ  TYR A 900     3683   3441   3425    183    111     77       C  
ATOM   1529  OH  TYR A 900      16.084 209.894  19.838  1.00 25.26           O  
ANISOU 1529  OH  TYR A 900     3354   3109   3132    166    109     89       O  
ATOM   1530  N   GLY A 901      20.067 204.872  22.372  1.00 25.14           N  
ANISOU 1530  N   GLY A 901     3347   3188   3017    443    209    244       N  
ATOM   1531  CA  GLY A 901      21.036 204.785  21.317  1.00 24.42           C  
ANISOU 1531  CA  GLY A 901     3237   3104   2936    486    244    254       C  
ATOM   1532  C   GLY A 901      20.971 203.449  20.595  1.00 24.94           C  
ANISOU 1532  C   GLY A 901     3389   3069   3017    549    323    256       C  
ATOM   1533  O   GLY A 901      21.076 203.394  19.362  1.00 25.24           O  
ANISOU 1533  O   GLY A 901     3455   3077   3055    542    360    215       O  
ATOM   1534  N   VAL A 902      20.800 202.349  21.324  1.00 27.74           N  
ANISOU 1534  N   VAL A 902     3790   3364   3383    606    360    302       N  
ATOM   1535  CA  VAL A 902      20.718 201.034  20.638  1.00 26.83           C  
ANISOU 1535  CA  VAL A 902     3774   3116   3302    658    458    289       C  
ATOM   1536  C   VAL A 902      19.452 201.014  19.772  1.00 28.16           C  
ANISOU 1536  C   VAL A 902     4026   3207   3465    547    464    183       C  
ATOM   1537  O   VAL A 902      19.459 200.520  18.657  1.00 28.60           O  
ANISOU 1537  O   VAL A 902     4137   3205   3521    541    524    118       O  
ATOM   1538  CB  VAL A 902      20.747 199.853  21.640  1.00 29.97           C  
ANISOU 1538  CB  VAL A 902     4215   3441   3731    742    511    378       C  
ATOM   1539  CG1 VAL A 902      20.644 198.530  20.880  1.00 29.52           C  
ANISOU 1539  CG1 VAL A 902     4275   3210   3731    785    633    346       C  
ATOM   1540  CG2 VAL A 902      22.012 199.881  22.478  1.00 29.08           C  
ANISOU 1540  CG2 VAL A 902     3996   3447   3605    861    496    499       C  
ATOM   1541  N   THR A 903      18.370 201.551  20.304  1.00 26.55           N  
ANISOU 1541  N   THR A 903     3820   3023   3245    460    404    163       N  
ATOM   1542  CA  THR A 903      17.108 201.631  19.576  1.00 28.04           C  
ANISOU 1542  CA  THR A 903     4056   3179   3417    355    395     76       C  
ATOM   1543  C   THR A 903      17.245 202.440  18.280  1.00 27.04           C  
ANISOU 1543  C   THR A 903     3898   3117   3256    321    372     28       C  
ATOM   1544  O   THR A 903      16.815 202.005  17.203  1.00 26.23           O  
ANISOU 1544  O   THR A 903     3846   2993   3127    275    406    -42       O  
ATOM   1545  CB  THR A 903      16.021 202.237  20.484  1.00 26.71           C  
ANISOU 1545  CB  THR A 903     3862   3047   3239    288    332     78       C  
ATOM   1546  CG2 THR A 903      14.703 202.302  19.746  1.00 27.03           C  
ANISOU 1546  CG2 THR A 903     3928   3082   3259    187    319      2       C  
ATOM   1547  OG1 THR A 903      15.881 201.405  21.639  1.00 26.45           O  
ANISOU 1547  OG1 THR A 903     3859   2964   3224    315    361    132       O  
ATOM   1548  N   VAL A 904      17.900 203.601  18.363  1.00 25.95           N  
ANISOU 1548  N   VAL A 904     3678   3066   3114    339    322     68       N  
ATOM   1549  CA  VAL A 904      18.213 204.376  17.150  1.00 25.13           C  
ANISOU 1549  CA  VAL A 904     3542   3023   2982    319    314     54       C  
ATOM   1550  C   VAL A 904      19.033 203.578  16.127  1.00 27.00           C  
ANISOU 1550  C   VAL A 904     3811   3246   3199    366    389     29       C  
ATOM   1551  O   VAL A 904      18.787 203.643  14.890  1.00 26.83           O  
ANISOU 1551  O   VAL A 904     3807   3259   3127    326    405    -17       O  
ATOM   1552  CB  VAL A 904      18.897 205.703  17.537  1.00 26.07           C  
ANISOU 1552  CB  VAL A 904     3572   3213   3121    324    266    106       C  
ATOM   1553  CG1 VAL A 904      19.418 206.447  16.295  1.00 28.42           C  
ANISOU 1553  CG1 VAL A 904     3835   3565   3396    312    274    118       C  
ATOM   1554  CG2 VAL A 904      17.899 206.550  18.299  1.00 25.44           C  
ANISOU 1554  CG2 VAL A 904     3473   3133   3057    270    208    102       C  
ATOM   1555  N   TRP A 905      20.029 202.827  16.609  1.00 27.14           N  
ANISOU 1555  N   TRP A 905     3830   3231   3251    457    441     64       N  
ATOM   1556  CA  TRP A 905      20.819 201.958  15.743  1.00 28.14           C  
ANISOU 1556  CA  TRP A 905     3991   3326   3373    522    534     36       C  
ATOM   1557  C   TRP A 905      19.979 200.918  15.027  1.00 28.82           C  
ANISOU 1557  C   TRP A 905     4188   3318   3444    474    599    -66       C  
ATOM   1558  O   TRP A 905      20.193 200.671  13.846  1.00 28.90           O  
ANISOU 1558  O   TRP A 905     4224   3346   3411    463    654   -136       O  
ATOM   1559  CB  TRP A 905      21.916 201.259  16.556  1.00 28.50           C  
ANISOU 1559  CB  TRP A 905     4012   3345   3471    649    583    111       C  
ATOM   1560  CG  TRP A 905      22.901 200.517  15.768  1.00 30.10           C  
ANISOU 1560  CG  TRP A 905     4226   3525   3682    742    686     97       C  
ATOM   1561  CD1 TRP A 905      24.092 200.983  15.277  1.00 32.06           C  
ANISOU 1561  CD1 TRP A 905     4385   3879   3915    799    702    131       C  
ATOM   1562  CD2 TRP A 905      22.818 199.156  15.388  1.00 31.56           C  
ANISOU 1562  CD2 TRP A 905     4518   3569   3901    793    803     40       C  
ATOM   1563  CE2 TRP A 905      23.997 198.842  14.708  1.00 33.08           C  
ANISOU 1563  CE2 TRP A 905     4680   3786   4099    896    889     43       C  
ATOM   1564  CE3 TRP A 905      21.887 198.146  15.627  1.00 32.20           C  
ANISOU 1564  CE3 TRP A 905     4719   3495   4021    759    854    -10       C  
ATOM   1565  NE1 TRP A 905      24.732 199.993  14.615  1.00 34.47           N  
ANISOU 1565  NE1 TRP A 905     4731   4127   4238    892    820    100       N  
ATOM   1566  CZ2 TRP A 905      24.218 197.597  14.151  1.00 36.09           C  
ANISOU 1566  CZ2 TRP A 905     5156   4034   4521    968   1030    -22       C  
ATOM   1567  CZ3 TRP A 905      22.111 196.908  15.114  1.00 33.62           C  
ANISOU 1567  CZ3 TRP A 905     4995   3531   4246    817    993    -73       C  
ATOM   1568  CH2 TRP A 905      23.281 196.624  14.386  1.00 36.83           C  
ANISOU 1568  CH2 TRP A 905     5378   3954   4660    928   1084    -82       C  
ATOM   1569  N   GLU A 906      19.053 200.271  15.742  1.00 28.10           N  
ANISOU 1569  N   GLU A 906     4159   3132   3383    436    602    -83       N  
ATOM   1570  CA  GLU A 906      18.167 199.324  15.108  1.00 28.91           C  
ANISOU 1570  CA  GLU A 906     4362   3146   3473    357    663   -196       C  
ATOM   1571  C   GLU A 906      17.377 200.020  13.990  1.00 28.92           C  
ANISOU 1571  C   GLU A 906     4341   3263   3381    243    609   -273       C  
ATOM   1572  O   GLU A 906      17.146 199.433  12.965  1.00 30.94           O  
ANISOU 1572  O   GLU A 906     4652   3515   3589    187    665   -382       O  
ATOM   1573  CB  GLU A 906      17.134 198.781  16.070  1.00 30.07           C  
ANISOU 1573  CB  GLU A 906     4559   3202   3661    303    658   -192       C  
ATOM   1574  CG  GLU A 906      17.670 198.010  17.283  1.00 30.83           C  
ANISOU 1574  CG  GLU A 906     4684   3189   3840    408    711    -94       C  
ATOM   1575  CD  GLU A 906      16.503 197.579  18.156  1.00 29.83           C  
ANISOU 1575  CD  GLU A 906     4602   2991   3738    331    704    -89       C  
ATOM   1576  OE1 GLU A 906      15.910 196.516  17.849  1.00 31.42           O  
ANISOU 1576  OE1 GLU A 906     4905   3059   3972    268    792   -167       O  
ATOM   1577  OE2 GLU A 906      16.161 198.288  19.124  1.00 28.02           O1-
ANISOU 1577  OE2 GLU A 906     4308   2839   3496    322    621    -17       O1-
ATOM   1578  N   LEU A 907      16.957 201.248  14.210  1.00 28.48           N  
ANISOU 1578  N   LEU A 907     4204   3314   3300    211    506   -214       N  
ATOM   1579  CA  LEU A 907      16.178 201.950  13.189  1.00 29.49           C  
ANISOU 1579  CA  LEU A 907     4299   3565   3341    123    452   -251       C  
ATOM   1580  C   LEU A 907      17.030 202.244  11.984  1.00 27.10           C  
ANISOU 1580  C   LEU A 907     3974   3348   2975    149    482   -260       C  
ATOM   1581  O   LEU A 907      16.608 202.075  10.841  1.00 29.13           O  
ANISOU 1581  O   LEU A 907     4244   3685   3137     82    495   -337       O  
ATOM   1582  CB  LEU A 907      15.601 203.265  13.760  1.00 29.17           C  
ANISOU 1582  CB  LEU A 907     4176   3594   3310    109    352   -167       C  
ATOM   1583  CG  LEU A 907      14.609 203.101  14.937  1.00 30.66           C  
ANISOU 1583  CG  LEU A 907     4373   3728   3545     75    320   -161       C  
ATOM   1584  CD1 LEU A 907      13.950 204.412  15.281  1.00 30.97           C  
ANISOU 1584  CD1 LEU A 907     4335   3842   3590     62    238   -100       C  
ATOM   1585  CD2 LEU A 907      13.561 202.055  14.678  1.00 32.79           C  
ANISOU 1585  CD2 LEU A 907     4703   3966   3787    -17    351   -258       C  
ATOM   1586  N   MET A 908      18.224 202.737  12.248  1.00 27.96           N  
ANISOU 1586  N   MET A 908     4034   3464   3123    239    490   -179       N  
ATOM   1587  CA  MET A 908      19.090 203.262  11.192  1.00 28.73           C  
ANISOU 1587  CA  MET A 908     4088   3663   3164    263    512   -159       C  
ATOM   1588  C   MET A 908      19.691 202.107  10.368  1.00 29.08           C  
ANISOU 1588  C   MET A 908     4197   3678   3174    292    625   -258       C  
ATOM   1589  O   MET A 908      20.173 202.334   9.242  1.00 29.48           O  
ANISOU 1589  O   MET A 908     4225   3832   3144    289    658   -276       O  
ATOM   1590  CB  MET A 908      20.221 204.090  11.788  1.00 29.55           C  
ANISOU 1590  CB  MET A 908     4113   3786   3328    335    495    -52       C  
ATOM   1591  CG  MET A 908      19.846 205.363  12.474  1.00 29.89           C  
ANISOU 1591  CG  MET A 908     4094   3854   3408    305    407     28       C  
ATOM   1592  SD  MET A 908      18.861 206.465  11.436  1.00 33.88           S  
ANISOU 1592  SD  MET A 908     4570   4461   3841    230    352     59       S  
ATOM   1593  CE  MET A 908      18.216 207.598  12.687  1.00 32.14           C  
ANISOU 1593  CE  MET A 908     4307   4193   3710    215    274    125       C  
ATOM   1594  N   THR A 909      19.703 200.887  10.924  1.00 30.08           N  
ANISOU 1594  N   THR A 909     4403   3660   3365    325    695   -316       N  
ATOM   1595  CA  THR A 909      20.068 199.684  10.133  1.00 31.46           C  
ANISOU 1595  CA  THR A 909     4661   3770   3522    342    823   -438       C  
ATOM   1596  C   THR A 909      18.854 198.983   9.581  1.00 32.10           C  
ANISOU 1596  C   THR A 909     4826   3826   3545    211    842   -584       C  
ATOM   1597  O   THR A 909      18.929 197.833   9.135  1.00 33.02           O  
ANISOU 1597  O   THR A 909     5036   3840   3668    200    959   -714       O  
ATOM   1598  CB  THR A 909      20.828 198.667  11.010  1.00 35.14           C  
ANISOU 1598  CB  THR A 909     5175   4068   4109    465    916   -411       C  
ATOM   1599  CG2 THR A 909      22.133 199.265  11.500  1.00 35.25           C  
ANISOU 1599  CG2 THR A 909     5086   4141   4163    593    902   -276       C  
ATOM   1600  OG1 THR A 909      20.028 198.302  12.165  1.00 33.19           O  
ANISOU 1600  OG1 THR A 909     4968   3708   3934    441    883   -381       O  
ATOM   1601  N   PHE A 910      17.694 199.629   9.684  1.00 32.82           N  
ANISOU 1601  N   PHE A 910     4881   3999   3589    108    735   -569       N  
ATOM   1602  CA  PHE A 910      16.443 199.045   9.200  1.00 35.04           C  
ANISOU 1602  CA  PHE A 910     5214   4295   3803    -36    735   -703       C  
ATOM   1603  C   PHE A 910      16.155 197.697   9.863  1.00 35.89           C  
ANISOU 1603  C   PHE A 910     5434   4191   4010    -56    829   -788       C  
ATOM   1604  O   PHE A 910      15.725 196.764   9.221  1.00 35.01           O  
ANISOU 1604  O   PHE A 910     5403   4034   3864   -154    908   -950       O  
ATOM   1605  CB  PHE A 910      16.461 198.920   7.656  1.00 39.81           C  
ANISOU 1605  CB  PHE A 910     5823   5044   4259   -108    773   -826       C  
ATOM   1606  CG  PHE A 910      16.644 200.236   6.963  1.00 38.97           C  
ANISOU 1606  CG  PHE A 910     5608   5149   4049    -93    687   -720       C  
ATOM   1607  CD1 PHE A 910      15.572 201.109   6.841  1.00 39.58           C  
ANISOU 1607  CD1 PHE A 910     5608   5372   4056   -167    569   -660       C  
ATOM   1608  CD2 PHE A 910      17.876 200.609   6.469  1.00 40.90           C  
ANISOU 1608  CD2 PHE A 910     5821   5442   4277      0    731   -666       C  
ATOM   1609  CE1 PHE A 910      15.731 202.341   6.240  1.00 40.23           C  
ANISOU 1609  CE1 PHE A 910     5596   5625   4061   -141    502   -536       C  
ATOM   1610  CE2 PHE A 910      18.040 201.850   5.883  1.00 41.51           C  
ANISOU 1610  CE2 PHE A 910     5802   5696   4274      8    662   -549       C  
ATOM   1611  CZ  PHE A 910      16.964 202.707   5.767  1.00 39.71           C  
ANISOU 1611  CZ  PHE A 910     5510   5591   3984    -59    550   -480       C  
ATOM   1612  N   GLY A 911      16.384 197.624  11.167  1.00 35.21           N  
ANISOU 1612  N   GLY A 911     5351   3980   4044     28    822   -676       N  
ATOM   1613  CA  GLY A 911      16.041 196.465  11.937  1.00 34.68           C  
ANISOU 1613  CA  GLY A 911     5383   3714   4079     15    904   -712       C  
ATOM   1614  C   GLY A 911      17.066 195.379  12.071  1.00 35.69           C  
ANISOU 1614  C   GLY A 911     5599   3654   4305    134   1053   -723       C  
ATOM   1615  O   GLY A 911      16.694 194.235  12.266  1.00 36.41           O  
ANISOU 1615  O   GLY A 911     5801   3563   4469     93   1158   -800       O  
ATOM   1616  N   SER A 912      18.349 195.694  11.996  1.00 34.70           N  
ANISOU 1616  N   SER A 912     5425   3563   4195    283   1073   -641       N  
ATOM   1617  CA  SER A 912      19.379 194.683  12.255  1.00 36.51           C  
ANISOU 1617  CA  SER A 912     5719   3620   4532    432   1217   -618       C  
ATOM   1618  C   SER A 912      19.409 194.350  13.731  1.00 35.69           C  
ANISOU 1618  C   SER A 912     5622   3397   4541    518   1213   -469       C  
ATOM   1619  O   SER A 912      18.980 195.151  14.561  1.00 33.69           O  
ANISOU 1619  O   SER A 912     5293   3236   4268    490   1087   -368       O  
ATOM   1620  CB  SER A 912      20.764 195.169  11.848  1.00 36.68           C  
ANISOU 1620  CB  SER A 912     5656   3744   4534    573   1232   -553       C  
ATOM   1621  OG  SER A 912      20.788 195.344  10.442  1.00 39.41           O  
ANISOU 1621  OG  SER A 912     6006   4197   4770    500   1258   -690       O  
ATOM   1622  N   LYS A 913      19.916 193.159  14.019  1.00 37.78           N  
ANISOU 1622  N   LYS A 913     5978   3458   4919    625   1361   -455       N  
ATOM   1623  CA  LYS A 913      20.098 192.679  15.362  1.00 39.32           C  
ANISOU 1623  CA  LYS A 913     6182   3537   5218    735   1383   -291       C  
ATOM   1624  C   LYS A 913      21.400 193.252  15.888  1.00 39.70           C  
ANISOU 1624  C   LYS A 913     6102   3710   5269    919   1338   -120       C  
ATOM   1625  O   LYS A 913      22.438 193.087  15.256  1.00 36.03           O  
ANISOU 1625  O   LYS A 913     5616   3257   4815   1033   1414   -131       O  
ATOM   1626  CB  LYS A 913      20.185 191.138  15.353  1.00 42.15           C  
ANISOU 1626  CB  LYS A 913     6693   3611   5708    793   1583   -332       C  
ATOM   1627  CG  LYS A 913      18.873 190.493  14.979  1.00 45.92           C  
ANISOU 1627  CG  LYS A 913     7297   3954   6194    588   1635   -504       C  
ATOM   1628  CD  LYS A 913      18.933 188.983  14.985  1.00 52.88           C  
ANISOU 1628  CD  LYS A 913     8344   4523   7225    627   1850   -555       C  
ATOM   1629  CE  LYS A 913      17.669 188.426  14.373  1.00 56.80           C  
ANISOU 1629  CE  LYS A 913     8954   4916   7708    382   1902   -776       C  
ATOM   1630  NZ  LYS A 913      17.802 186.959  14.165  1.00 64.04           N1+
ANISOU 1630  NZ  LYS A 913    10049   5504   8779    403   2139   -869       N1+
ATOM   1631  N   PRO A 914      21.380 193.840  17.091  1.00 37.98           N  
ANISOU 1631  N   PRO A 914     5797   3588   5043    950   1227     34       N  
ATOM   1632  CA  PRO A 914      22.681 194.318  17.576  1.00 37.85           C  
ANISOU 1632  CA  PRO A 914     5649   3709   5023   1113   1190    183       C  
ATOM   1633  C   PRO A 914      23.614 193.197  17.982  1.00 39.48           C  
ANISOU 1633  C   PRO A 914     5881   3784   5334   1317   1327    298       C  
ATOM   1634  O   PRO A 914      23.164 192.166  18.539  1.00 39.73           O  
ANISOU 1634  O   PRO A 914     6021   3621   5454   1347   1420    343       O  
ATOM   1635  CB  PRO A 914      22.344 195.193  18.792  1.00 36.69           C  
ANISOU 1635  CB  PRO A 914     5408   3703   4829   1073   1042    295       C  
ATOM   1636  CG  PRO A 914      20.871 195.131  18.949  1.00 38.37           C  
ANISOU 1636  CG  PRO A 914     5705   3841   5031    910   1012    217       C  
ATOM   1637  CD  PRO A 914      20.288 194.108  18.044  1.00 38.00           C  
ANISOU 1637  CD  PRO A 914     5803   3602   5031    844   1137     75       C  
ATOM   1638  N   TYR A 915      24.899 193.432  17.721  1.00 39.01           N  
ANISOU 1638  N   TYR A 915     5715   3838   5268   1458   1343    359       N  
ATOM   1639  CA  TYR A 915      25.972 192.508  18.009  1.00 42.82           C  
ANISOU 1639  CA  TYR A 915     6184   4242   5843   1685   1471    486       C  
ATOM   1640  C   TYR A 915      25.580 191.144  17.446  1.00 47.01           C  
ANISOU 1640  C   TYR A 915     6902   4471   6486   1708   1664    387       C  
ATOM   1641  O   TYR A 915      25.600 190.173  18.167  1.00 48.99           O  
ANISOU 1641  O   TYR A 915     7219   4550   6842   1825   1763    505       O  
ATOM   1642  CB  TYR A 915      26.223 192.415  19.533  1.00 42.03           C  
ANISOU 1642  CB  TYR A 915     6004   4206   5759   1797   1414    713       C  
ATOM   1643  CG  TYR A 915      26.285 193.748  20.256  1.00 38.88           C  
ANISOU 1643  CG  TYR A 915     5447   4081   5243   1718   1219    774       C  
ATOM   1644  CD1 TYR A 915      27.458 194.521  20.263  1.00 38.99           C  
ANISOU 1644  CD1 TYR A 915     5283   4330   5201   1791   1152    838       C  
ATOM   1645  CD2 TYR A 915      25.177 194.233  20.899  1.00 36.99           C  
ANISOU 1645  CD2 TYR A 915     5236   3863   4955   1562   1115    752       C  
ATOM   1646  CE1 TYR A 915      27.512 195.747  20.909  1.00 36.54           C  
ANISOU 1646  CE1 TYR A 915     4838   4253   4793   1696    988    868       C  
ATOM   1647  CE2 TYR A 915      25.199 195.474  21.573  1.00 37.35           C  
ANISOU 1647  CE2 TYR A 915     5148   4141   4901   1483    951    785       C  
ATOM   1648  CZ  TYR A 915      26.374 196.226  21.580  1.00 36.41           C  
ANISOU 1648  CZ  TYR A 915     4864   4237   4731   1545    891    837       C  
ATOM   1649  OH  TYR A 915      26.367 197.430  22.250  1.00 33.31           O  
ANISOU 1649  OH  TYR A 915     4354   4052   4251   1446    745    846       O  
ATOM   1650  N   ASP A 916      25.189 191.087  16.173  1.00 50.16           N  
ANISOU 1650  N   ASP A 916     7389   4811   6859   1587   1721    170       N  
ATOM   1651  CA  ASP A 916      24.505 189.888  15.638  1.00 54.71           C  
ANISOU 1651  CA  ASP A 916     8160   5100   7525   1530   1890     21       C  
ATOM   1652  C   ASP A 916      25.391 188.633  15.728  1.00 56.84           C  
ANISOU 1652  C   ASP A 916     8497   5150   7950   1762   2102     97       C  
ATOM   1653  O   ASP A 916      26.557 188.640  15.299  1.00 56.48           O  
ANISOU 1653  O   ASP A 916     8371   5174   7913   1929   2163    129       O  
ATOM   1654  CB  ASP A 916      24.019 190.102  14.189  1.00 57.65           C  
ANISOU 1654  CB  ASP A 916     8593   5500   7811   1354   1908   -237       C  
ATOM   1655  CG  ASP A 916      23.428 188.826  13.573  1.00 61.30           C  
ANISOU 1655  CG  ASP A 916     9253   5676   8361   1283   2099   -424       C  
ATOM   1656  OD1 ASP A 916      22.478 188.258  14.142  1.00 61.18           O  
ANISOU 1656  OD1 ASP A 916     9341   5493   8410   1187   2123   -429       O  
ATOM   1657  OD2 ASP A 916      23.943 188.355  12.532  1.00 71.94           O1-
ANISOU 1657  OD2 ASP A 916    10655   6961   9719   1322   2239   -571       O1-
ATOM   1658  N   GLY A 917      24.845 187.575  16.325  1.00 56.83           N  
ANISOU 1658  N   GLY A 917     8633   4883   8075   1779   2217    141       N  
ATOM   1659  CA  GLY A 917      25.579 186.347  16.469  1.00 62.08           C  
ANISOU 1659  CA  GLY A 917     9378   5300   8910   2005   2433    230       C  
ATOM   1660  C   GLY A 917      26.586 186.322  17.603  1.00 64.14           C  
ANISOU 1660  C   GLY A 917     9502   5654   9215   2268   2410    541       C  
ATOM   1661  O   GLY A 917      27.247 185.318  17.785  1.00 67.76           O  
ANISOU 1661  O   GLY A 917    10008   5917   9819   2489   2591    655       O  
ATOM   1662  N   ILE A 918      26.708 187.391  18.387  1.00 62.68           N  
ANISOU 1662  N   ILE A 918     9143   5764   8905   2249   2198    682       N  
ATOM   1663  CA  ILE A 918      27.564 187.347  19.584  1.00 63.84           C  
ANISOU 1663  CA  ILE A 918     9151   6033   9071   2475   2161    981       C  
ATOM   1664  C   ILE A 918      26.737 186.886  20.782  1.00 62.60           C  
ANISOU 1664  C   ILE A 918     9066   5764   8956   2446   2149   1131       C  
ATOM   1665  O   ILE A 918      25.679 187.444  21.002  1.00 62.98           O  
ANISOU 1665  O   ILE A 918     9141   5866   8922   2224   2027   1046       O  
ATOM   1666  CB  ILE A 918      28.205 188.711  19.862  1.00 62.90           C  
ANISOU 1666  CB  ILE A 918     8802   6303   8794   2462   1950   1048       C  
ATOM   1667  CG1 ILE A 918      29.248 188.997  18.779  1.00 67.52           C  
ANISOU 1667  CG1 ILE A 918     9301   6992   9360   2543   1996    957       C  
ATOM   1668  CG2 ILE A 918      28.845 188.716  21.239  1.00 63.34           C  
ANISOU 1668  CG2 ILE A 918     8710   6521   8834   2640   1883   1341       C  
ATOM   1669  CD1 ILE A 918      29.778 190.410  18.773  1.00 67.18           C  
ANISOU 1669  CD1 ILE A 918     9054   7303   9166   2472   1805    964       C  
ATOM   1670  N   PRO A 919      27.199 185.865  21.550  1.00 64.70           N  
ANISOU 1670  N   PRO A 919     9357   5876   9347   2676   2283   1365       N  
ATOM   1671  CA  PRO A 919      26.413 185.428  22.716  1.00 64.77           C  
ANISOU 1671  CA  PRO A 919     9431   5791   9385   2647   2276   1529       C  
ATOM   1672  C   PRO A 919      26.272 186.538  23.738  1.00 62.98           C  
ANISOU 1672  C   PRO A 919     9032   5914   8982   2572   2037   1645       C  
ATOM   1673  O   PRO A 919      27.221 187.295  23.946  1.00 63.51           O  
ANISOU 1673  O   PRO A 919     8902   6278   8948   2669   1918   1732       O  
ATOM   1674  CB  PRO A 919      27.244 184.287  23.314  1.00 69.70           C  
ANISOU 1674  CB  PRO A 919    10067   6254  10160   2960   2452   1804       C  
ATOM   1675  CG  PRO A 919      28.123 183.803  22.212  1.00 71.02           C  
ANISOU 1675  CG  PRO A 919    10264   6286  10434   3111   2620   1701       C  
ATOM   1676  CD  PRO A 919      28.398 185.018  21.355  1.00 68.97           C  
ANISOU 1676  CD  PRO A 919     9878   6307  10017   2975   2463   1493       C  
ATOM   1677  N   ALA A 920      25.102 186.633  24.371  1.00 60.78           N  
ANISOU 1677  N   ALA A 920     8822   5604   8665   2394   1974   1637       N  
ATOM   1678  CA  ALA A 920      24.835 187.685  25.349  1.00 59.49           C  
ANISOU 1678  CA  ALA A 920     8513   5754   8333   2301   1761   1716       C  
ATOM   1679  C   ALA A 920      25.888 187.683  26.466  1.00 58.36           C  
ANISOU 1679  C   ALA A 920     8197   5838   8138   2534   1712   2016       C  
ATOM   1680  O   ALA A 920      26.304 188.737  26.949  1.00 56.87           O  
ANISOU 1680  O   ALA A 920     7826   5987   7795   2509   1534   2048       O  
ATOM   1681  CB  ALA A 920      23.434 187.528  25.935  1.00 60.18           C  
ANISOU 1681  CB  ALA A 920     8714   5737   8414   2112   1746   1693       C  
ATOM   1682  N   SER A 921      26.355 186.508  26.838  1.00 59.54           N  
ANISOU 1682  N   SER A 921     8397   5808   8415   2761   1876   2232       N  
ATOM   1683  CA  SER A 921      27.336 186.397  27.903  1.00 61.77           C  
ANISOU 1683  CA  SER A 921     8507   6316   8643   3001   1838   2545       C  
ATOM   1684  C   SER A 921      28.690 186.995  27.525  1.00 61.83           C  
ANISOU 1684  C   SER A 921     8312   6591   8588   3140   1770   2560       C  
ATOM   1685  O   SER A 921      29.543 187.110  28.375  1.00 62.77           O  
ANISOU 1685  O   SER A 921     8245   6978   8625   3310   1701   2795       O  
ATOM   1686  CB  SER A 921      27.535 184.924  28.301  1.00 64.99           C  
ANISOU 1686  CB  SER A 921     9026   6437   9227   3240   2056   2795       C  
ATOM   1687  OG  SER A 921      28.058 184.176  27.223  1.00 65.27           O  
ANISOU 1687  OG  SER A 921     9162   6198   9440   3370   2250   2710       O  
ATOM   1688  N   GLU A 922      28.908 187.350  26.262  1.00 61.15           N  
ANISOU 1688  N   GLU A 922     8249   6451   8532   3069   1791   2319       N  
ATOM   1689  CA  GLU A 922      30.174 187.992  25.870  1.00 60.08           C  
ANISOU 1689  CA  GLU A 922     7911   6584   8331   3176   1725   2323       C  
ATOM   1690  C   GLU A 922      30.073 189.501  25.746  1.00 55.47           C  
ANISOU 1690  C   GLU A 922     7199   6301   7574   2950   1511   2154       C  
ATOM   1691  O   GLU A 922      31.070 190.175  25.568  1.00 51.94           O  
ANISOU 1691  O   GLU A 922     6566   6112   7053   3001   1434   2162       O  
ATOM   1692  CB  GLU A 922      30.657 187.450  24.545  1.00 62.59           C  
ANISOU 1692  CB  GLU A 922     8313   6682   8784   3266   1898   2185       C  
ATOM   1693  CG  GLU A 922      30.985 185.977  24.575  1.00 67.07           C  
ANISOU 1693  CG  GLU A 922     8993   6943   9545   3526   2137   2349       C  
ATOM   1694  CD  GLU A 922      31.443 185.498  23.228  1.00 70.82           C  
ANISOU 1694  CD  GLU A 922     9555   7207  10145   3599   2316   2174       C  
ATOM   1695  OE1 GLU A 922      31.271 184.296  22.931  1.00 77.35           O  
ANISOU 1695  OE1 GLU A 922    10566   7665  11157   3712   2543   2181       O  
ATOM   1696  OE2 GLU A 922      31.981 186.327  22.463  1.00 71.71           O1-
ANISOU 1696  OE2 GLU A 922     9554   7521  10172   3539   2238   2026       O1-
ATOM   1697  N   ILE A 923      28.876 190.041  25.859  1.00 53.09           N  
ANISOU 1697  N   ILE A 923     6992   5965   7214   2703   1422   2006       N  
ATOM   1698  CA  ILE A 923      28.678 191.462  25.594  1.00 51.13           C  
ANISOU 1698  CA  ILE A 923     6654   5940   6832   2485   1247   1825       C  
ATOM   1699  C   ILE A 923      29.351 192.414  26.589  1.00 52.42           C  
ANISOU 1699  C   ILE A 923     6587   6491   6839   2489   1073   1940       C  
ATOM   1700  O   ILE A 923      29.975 193.396  26.182  1.00 48.73           O  
ANISOU 1700  O   ILE A 923     5985   6230   6299   2425    980   1848       O  
ATOM   1701  CB  ILE A 923      27.189 191.794  25.500  1.00 48.42           C  
ANISOU 1701  CB  ILE A 923     6459   5467   6472   2236   1202   1651       C  
ATOM   1702  CG1 ILE A 923      26.592 191.174  24.231  1.00 48.83           C  
ANISOU 1702  CG1 ILE A 923     6704   5205   6642   2170   1343   1461       C  
ATOM   1703  CG2 ILE A 923      26.981 193.280  25.540  1.00 45.31           C  
ANISOU 1703  CG2 ILE A 923     5958   5317   5941   2043   1020   1521       C  
ATOM   1704  CD1 ILE A 923      27.159 191.686  22.917  1.00 48.81           C  
ANISOU 1704  CD1 ILE A 923     6669   5242   6634   2142   1351   1290       C  
ATOM   1705  N   SER A 924      29.206 192.128  27.880  1.00 52.10           N  
ANISOU 1705  N   SER A 924     6501   6551   6740   2550   1033   2135       N  
ATOM   1706  CA  SER A 924      29.922 192.840  28.923  1.00 52.19           C  
ANISOU 1706  CA  SER A 924     6286   6948   6592   2574    884   2263       C  
ATOM   1707  C   SER A 924      31.426 193.051  28.597  1.00 52.77           C  
ANISOU 1707  C   SER A 924     6156   7245   6646   2724    872   2332       C  
ATOM   1708  O   SER A 924      31.914 194.175  28.618  1.00 50.15           O  
ANISOU 1708  O   SER A 924     5666   7186   6203   2609    739   2244       O  
ATOM   1709  CB  SER A 924      29.757 192.067  30.233  1.00 54.93           C  
ANISOU 1709  CB  SER A 924     6624   7341   6905   2701    900   2523       C  
ATOM   1710  OG  SER A 924      30.475 192.684  31.259  1.00 57.94           O  
ANISOU 1710  OG  SER A 924     6776   8124   7112   2727    758   2650       O  
ATOM   1711  N   SER A 925      32.142 191.989  28.250  1.00 54.02           N  
ANISOU 1711  N   SER A 925     6322   7278   6924   2973   1021   2479       N  
ATOM   1712  CA  SER A 925      33.607 192.086  28.062  1.00 56.99           C  
ANISOU 1712  CA  SER A 925     6479   7894   7280   3148   1018   2582       C  
ATOM   1713  C   SER A 925      34.004 192.869  26.790  1.00 56.55           C  
ANISOU 1713  C   SER A 925     6394   7851   7239   3033   1010   2351       C  
ATOM   1714  O   SER A 925      34.996 193.614  26.819  1.00 54.45           O  
ANISOU 1714  O   SER A 925     5908   7897   6883   3032    919   2363       O  
ATOM   1715  CB  SER A 925      34.268 190.700  28.100  1.00 64.86           C  
ANISOU 1715  CB  SER A 925     7483   8749   8409   3477   1195   2825       C  
ATOM   1716  OG  SER A 925      34.049 190.029  26.871  1.00 71.24           O  
ANISOU 1716  OG  SER A 925     8486   9188   9395   3517   1377   2687       O  
ATOM   1717  N   ILE A 926      33.175 192.741  25.724  1.00 54.77           N  
ANISOU 1717  N   ILE A 926     6386   7309   7112   2916   1098   2140       N  
ATOM   1718  CA  ILE A 926      33.240 193.570  24.507  1.00 51.91           C  
ANISOU 1718  CA  ILE A 926     6033   6943   6746   2760   1081   1904       C  
ATOM   1719  C   ILE A 926      33.120 195.048  24.840  1.00 47.58           C  
ANISOU 1719  C   ILE A 926     5365   6657   6053   2527    889   1800       C  
ATOM   1720  O   ILE A 926      33.948 195.841  24.429  1.00 44.73           O  
ANISOU 1720  O   ILE A 926     4851   6499   5642   2486    836   1749       O  
ATOM   1721  CB  ILE A 926      32.154 193.110  23.492  1.00 53.62           C  
ANISOU 1721  CB  ILE A 926     6511   6795   7066   2659   1195   1712       C  
ATOM   1722  CG1 ILE A 926      32.644 191.819  22.821  1.00 58.06           C  
ANISOU 1722  CG1 ILE A 926     7159   7120   7778   2886   1408   1762       C  
ATOM   1723  CG2 ILE A 926      31.822 194.150  22.432  1.00 53.23           C  
ANISOU 1723  CG2 ILE A 926     6489   6763   6972   2438   1136   1471       C  
ATOM   1724  CD1 ILE A 926      31.570 191.100  22.039  1.00 59.65           C  
ANISOU 1724  CD1 ILE A 926     7624   6952   8086   2803   1540   1595       C  
ATOM   1725  N   LEU A 927      32.092 195.418  25.588  1.00 45.21           N  
ANISOU 1725  N   LEU A 927     5136   6346   5693   2372    797   1765       N  
ATOM   1726  CA  LEU A 927      31.840 196.823  25.910  1.00 43.54           C  
ANISOU 1726  CA  LEU A 927     4842   6338   5364   2143    635   1643       C  
ATOM   1727  C   LEU A 927      32.949 197.371  26.799  1.00 45.27           C  
ANISOU 1727  C   LEU A 927     4804   6931   5463   2182    526   1762       C  
ATOM   1728  O   LEU A 927      33.349 198.522  26.675  1.00 43.41           O  
ANISOU 1728  O   LEU A 927     4447   6887   5157   2033    431   1656       O  
ATOM   1729  CB  LEU A 927      30.496 196.973  26.619  1.00 42.36           C  
ANISOU 1729  CB  LEU A 927     4818   6095   5179   1999    579   1594       C  
ATOM   1730  CG  LEU A 927      29.274 196.647  25.772  1.00 41.50           C  
ANISOU 1730  CG  LEU A 927     4941   5663   5164   1905    658   1447       C  
ATOM   1731  CD1 LEU A 927      27.987 196.766  26.600  1.00 41.78           C  
ANISOU 1731  CD1 LEU A 927     5072   5642   5159   1776    603   1423       C  
ATOM   1732  CD2 LEU A 927      29.213 197.549  24.543  1.00 40.12           C  
ANISOU 1732  CD2 LEU A 927     4784   5459   4998   1761    640   1248       C  
ATOM   1733  N   GLU A 928      33.432 196.538  27.711  1.00 48.53           N  
ANISOU 1733  N   GLU A 928     5133   7453   5853   2378    544   1988       N  
ATOM   1734  CA  GLU A 928      34.491 196.953  28.606  1.00 51.54           C  
ANISOU 1734  CA  GLU A 928     5251   8228   6102   2424    438   2118       C  
ATOM   1735  C   GLU A 928      35.766 197.272  27.833  1.00 52.32           C  
ANISOU 1735  C   GLU A 928     5178   8485   6215   2482    454   2105       C  
ATOM   1736  O   GLU A 928      36.463 198.197  28.188  1.00 55.20           O  
ANISOU 1736  O   GLU A 928     5340   9165   6467   2377    339   2078       O  
ATOM   1737  CB  GLU A 928      34.778 195.877  29.671  1.00 55.26           C  
ANISOU 1737  CB  GLU A 928     5661   8790   6545   2658    467   2401       C  
ATOM   1738  CG  GLU A 928      33.693 195.755  30.710  1.00 55.40           C  
ANISOU 1738  CG  GLU A 928     5781   8769   6495   2580    419   2438       C  
ATOM   1739  CD  GLU A 928      34.067 194.795  31.829  1.00 62.12           C  
ANISOU 1739  CD  GLU A 928     6543   9765   7294   2808    437   2746       C  
ATOM   1740  OE1 GLU A 928      33.806 193.568  31.696  1.00 63.14           O  
ANISOU 1740  OE1 GLU A 928     6814   9619   7556   2999    585   2895       O  
ATOM   1741  OE2 GLU A 928      34.608 195.295  32.845  1.00 60.26           O1-
ANISOU 1741  OE2 GLU A 928     6095   9922   6879   2786    305   2836       O1-
ATOM   1742  N   LYS A 929      36.065 196.532  26.772  1.00 51.57           N  
ANISOU 1742  N   LYS A 929     5161   8177   6256   2633    603   2112       N  
ATOM   1743  CA  LYS A 929      37.207 196.871  25.912  1.00 54.70           C  
ANISOU 1743  CA  LYS A 929     5404   8709   6669   2674    633   2079       C  
ATOM   1744  C   LYS A 929      37.004 198.136  25.035  1.00 52.54           C  
ANISOU 1744  C   LYS A 929     5154   8429   6376   2410    578   1835       C  
ATOM   1745  O   LYS A 929      37.948 198.586  24.375  1.00 52.72           O  
ANISOU 1745  O   LYS A 929     5035   8598   6396   2405    590   1802       O  
ATOM   1746  CB  LYS A 929      37.578 195.684  25.028  1.00 57.73           C  
ANISOU 1746  CB  LYS A 929     5870   8863   7200   2921    825   2147       C  
ATOM   1747  CG  LYS A 929      38.075 194.482  25.811  1.00 64.34           C  
ANISOU 1747  CG  LYS A 929     6641   9732   8073   3221    899   2423       C  
ATOM   1748  CD  LYS A 929      38.850 193.526  24.913  1.00 70.29           C  
ANISOU 1748  CD  LYS A 929     7397  10344   8966   3480   1090   2490       C  
ATOM   1749  CE  LYS A 929      39.345 192.306  25.672  1.00 77.53           C  
ANISOU 1749  CE  LYS A 929     8252  11264   9938   3806   1182   2788       C  
ATOM   1750  NZ  LYS A 929      38.176 191.612  26.286  1.00 80.66           N1+
ANISOU 1750  NZ  LYS A 929     8874  11386  10384   3803   1218   2841       N1+
ATOM   1751  N   GLY A 930      35.797 198.699  25.017  1.00 47.42           N  
ANISOU 1751  N   GLY A 930     4677   7619   5721   2201    527   1678       N  
ATOM   1752  CA  GLY A 930      35.542 199.984  24.327  1.00 45.82           C  
ANISOU 1752  CA  GLY A 930     4491   7420   5499   1953    468   1475       C  
ATOM   1753  C   GLY A 930      34.892 199.827  22.966  1.00 44.43           C  
ANISOU 1753  C   GLY A 930     4515   6947   5419   1916    571   1337       C  
ATOM   1754  O   GLY A 930      34.729 200.788  22.238  1.00 42.67           O  
ANISOU 1754  O   GLY A 930     4310   6713   5188   1744    544   1196       O  
ATOM   1755  N   GLU A 931      34.551 198.599  22.608  1.00 46.44           N  
ANISOU 1755  N   GLU A 931     4916   6967   5762   2077    697   1381       N  
ATOM   1756  CA  GLU A 931      33.885 198.337  21.352  1.00 43.53           C  
ANISOU 1756  CA  GLU A 931     4739   6332   5468   2036    798   1239       C  
ATOM   1757  C   GLU A 931      32.422 198.727  21.469  1.00 39.04           C  
ANISOU 1757  C   GLU A 931     4341   5603   4887   1849    738   1119       C  
ATOM   1758  O   GLU A 931      31.830 198.628  22.536  1.00 35.39           O  
ANISOU 1758  O   GLU A 931     3903   5145   4398   1827    675   1176       O  
ATOM   1759  CB  GLU A 931      34.026 196.867  20.988  1.00 47.72           C  
ANISOU 1759  CB  GLU A 931     5370   6659   6102   2261    965   1309       C  
ATOM   1760  CG  GLU A 931      33.201 196.429  19.802  1.00 49.02           C  
ANISOU 1760  CG  GLU A 931     5751   6539   6333   2207   1076   1146       C  
ATOM   1761  CD  GLU A 931      33.453 194.984  19.403  1.00 56.40           C  
ANISOU 1761  CD  GLU A 931     6784   7262   7382   2424   1265   1191       C  
ATOM   1762  OE1 GLU A 931      32.591 194.474  18.632  1.00 56.59           O  
ANISOU 1762  OE1 GLU A 931     7009   7033   7459   2363   1356   1050       O  
ATOM   1763  OE2 GLU A 931      34.493 194.375  19.841  1.00 53.70           O1-
ANISOU 1763  OE2 GLU A 931     6317   7009   7077   2651   1325   1363       O1-
ATOM   1764  N   ARG A 932      31.854 199.204  20.359  1.00 35.16           N  
ANISOU 1764  N   ARG A 932     3954   4995   4408   1715    757    961       N  
ATOM   1765  CA  ARG A 932      30.467 199.588  20.303  1.00 33.55           C  
ANISOU 1765  CA  ARG A 932     3900   4651   4196   1547    709    848       C  
ATOM   1766  C   ARG A 932      29.876 199.167  18.970  1.00 34.08           C  
ANISOU 1766  C   ARG A 932     4124   4519   4305   1519    807    722       C  
ATOM   1767  O   ARG A 932      30.581 198.718  18.108  1.00 33.54           O  
ANISOU 1767  O   ARG A 932     4045   4433   4263   1614    908    710       O  
ATOM   1768  CB  ARG A 932      30.317 201.117  20.431  1.00 33.81           C  
ANISOU 1768  CB  ARG A 932     3854   4826   4164   1354    583    778       C  
ATOM   1769  CG  ARG A 932      30.845 201.701  21.743  1.00 33.48           C  
ANISOU 1769  CG  ARG A 932     3654   5006   4062   1332    476    858       C  
ATOM   1770  CD  ARG A 932      29.991 201.278  22.900  1.00 33.87           C  
ANISOU 1770  CD  ARG A 932     3768   5007   4093   1337    436    904       C  
ATOM   1771  NE  ARG A 932      30.370 201.906  24.148  1.00 32.94           N  
ANISOU 1771  NE  ARG A 932     3506   5118   3892   1290    329    955       N  
ATOM   1772  CZ  ARG A 932      31.306 201.471  24.994  1.00 34.79           C  
ANISOU 1772  CZ  ARG A 932     3593   5545   4078   1415    311   1098       C  
ATOM   1773  NH1 ARG A 932      31.523 202.129  26.133  1.00 35.08           N1+
ANISOU 1773  NH1 ARG A 932     3501   5810   4016   1337    204   1117       N1+
ATOM   1774  NH2 ARG A 932      31.965 200.356  24.767  1.00 36.55           N  
ANISOU 1774  NH2 ARG A 932     3799   5739   4348   1621    403   1224       N  
ATOM   1775  N   LEU A 933      28.570 199.360  18.802  1.00 31.95           N  
ANISOU 1775  N   LEU A 933     3988   4122   4028   1380    776    622       N  
ATOM   1776  CA  LEU A 933      27.915 199.034  17.557  1.00 33.24           C  
ANISOU 1776  CA  LEU A 933     4288   4135   4206   1324    852    491       C  
ATOM   1777  C   LEU A 933      28.463 199.931  16.449  1.00 33.92           C  
ANISOU 1777  C   LEU A 933     4305   4337   4245   1262    845    431       C  
ATOM   1778  O   LEU A 933      28.745 201.117  16.693  1.00 33.63           O  
ANISOU 1778  O   LEU A 933     4158   4449   4168   1177    749    454       O  
ATOM   1779  CB  LEU A 933      26.404 199.236  17.683  1.00 31.37           C  
ANISOU 1779  CB  LEU A 933     4169   3796   3955   1175    795    410       C  
ATOM   1780  CG  LEU A 933      25.670 198.221  18.605  1.00 31.53           C  
ANISOU 1780  CG  LEU A 933     4287   3669   4024   1214    826    454       C  
ATOM   1781  CD1 LEU A 933      24.345 198.743  19.067  1.00 30.90           C  
ANISOU 1781  CD1 LEU A 933     4257   3567   3914   1063    737    406       C  
ATOM   1782  CD2 LEU A 933      25.534 196.879  17.905  1.00 33.11           C  
ANISOU 1782  CD2 LEU A 933     4622   3666   4290   1284    978    398       C  
ATOM   1783  N   PRO A 934      28.553 199.397  15.244  1.00 35.14           N  
ANISOU 1783  N   PRO A 934     4530   4419   4402   1289    953    346       N  
ATOM   1784  CA  PRO A 934      29.198 200.127  14.179  1.00 35.29           C  
ANISOU 1784  CA  PRO A 934     4476   4562   4369   1251    966    310       C  
ATOM   1785  C   PRO A 934      28.299 201.198  13.556  1.00 34.32           C  
ANISOU 1785  C   PRO A 934     4388   4470   4182   1069    885    237       C  
ATOM   1786  O   PRO A 934      27.076 201.225  13.786  1.00 33.90           O  
ANISOU 1786  O   PRO A 934     4428   4327   4124    978    833    190       O  
ATOM   1787  CB  PRO A 934      29.575 199.024  13.176  1.00 39.23           C  
ANISOU 1787  CB  PRO A 934     5048   4969   4886   1357   1125    239       C  
ATOM   1788  CG  PRO A 934      28.493 198.000  13.349  1.00 39.73           C  
ANISOU 1788  CG  PRO A 934     5282   4821   4992   1347   1173    168       C  
ATOM   1789  CD  PRO A 934      28.147 198.036  14.819  1.00 38.77           C  
ANISOU 1789  CD  PRO A 934     5139   4680   4912   1358   1084    278       C  
ATOM   1790  N   GLN A 935      28.928 202.100  12.827  1.00 32.57           N  
ANISOU 1790  N   GLN A 935     4076   4382   3915   1024    877    245       N  
ATOM   1791  CA  GLN A 935      28.239 203.154  12.107  1.00 31.87           C  
ANISOU 1791  CA  GLN A 935     4007   4333   3769    876    818    207       C  
ATOM   1792  C   GLN A 935      27.352 202.605  11.004  1.00 31.97           C  
ANISOU 1792  C   GLN A 935     4147   4274   3724    834    872     97       C  
ATOM   1793  O   GLN A 935      27.842 202.013  10.058  1.00 32.07           O  
ANISOU 1793  O   GLN A 935     4179   4303   3702    886    976     42       O  
ATOM   1794  CB  GLN A 935      29.271 204.134  11.537  1.00 32.91           C  
ANISOU 1794  CB  GLN A 935     4011   4621   3872    850    823    260       C  
ATOM   1795  CG  GLN A 935      28.658 205.434  11.012  1.00 33.32           C  
ANISOU 1795  CG  GLN A 935     4062   4712   3884    705    756    268       C  
ATOM   1796  CD  GLN A 935      29.693 206.530  10.743  1.00 34.42           C  
ANISOU 1796  CD  GLN A 935     4069   4986   4021    660    756    341       C  
ATOM   1797  NE2 GLN A 935      29.391 207.564  10.119  1.00 35.36           N  
ANISOU 1797  NE2 GLN A 935     4076   5188   4170    734    788    383       N  
ATOM   1798  OE1 GLN A 935      30.898 206.303  11.174  1.00 36.25           O  
ANISOU 1798  OE1 GLN A 935     4298   5248   4227    559    734    368       O  
ATOM   1799  N   PRO A 936      26.016 202.784  11.111  1.00 29.84           N  
ANISOU 1799  N   PRO A 936     3959   3940   3437    734    805     54       N  
ATOM   1800  CA  PRO A 936      25.192 202.287  10.022  1.00 31.56           C  
ANISOU 1800  CA  PRO A 936     4277   4131   3581    675    848    -58       C  
ATOM   1801  C   PRO A 936      25.533 203.002   8.686  1.00 33.31           C  
ANISOU 1801  C   PRO A 936     4454   4498   3703    628    868    -60       C  
ATOM   1802  O   PRO A 936      25.865 204.187   8.689  1.00 35.38           O  
ANISOU 1802  O   PRO A 936     4627   4854   3960    592    811     33       O  
ATOM   1803  CB  PRO A 936      23.774 202.623  10.473  1.00 30.69           C  
ANISOU 1803  CB  PRO A 936     4217   3973   3468    572    752    -72       C  
ATOM   1804  CG  PRO A 936      23.867 202.713  11.966  1.00 32.29           C  
ANISOU 1804  CG  PRO A 936     4388   4117   3762    612    698      4       C  
ATOM   1805  CD  PRO A 936      25.213 203.322  12.221  1.00 31.47           C  
ANISOU 1805  CD  PRO A 936     4166   4107   3684    675    698     94       C  
ATOM   1806  N   PRO A 937      25.486 202.295   7.579  1.00 36.00           N  
ANISOU 1806  N   PRO A 937     4855   4858   3964    625    958   -167       N  
ATOM   1807  CA  PRO A 937      25.795 202.916   6.284  1.00 36.01           C  
ANISOU 1807  CA  PRO A 937     4812   5020   3847    582    983   -164       C  
ATOM   1808  C   PRO A 937      25.102 204.249   5.948  1.00 34.57           C  
ANISOU 1808  C   PRO A 937     4586   4943   3603    476    877    -78       C  
ATOM   1809  O   PRO A 937      25.713 205.111   5.325  1.00 34.41           O  
ANISOU 1809  O   PRO A 937     4489   5046   3537    464    884      4       O  
ATOM   1810  CB  PRO A 937      25.355 201.830   5.284  1.00 39.42           C  
ANISOU 1810  CB  PRO A 937     5347   5444   4187    558   1076   -333       C  
ATOM   1811  CG  PRO A 937      25.594 200.539   6.019  1.00 40.50           C  
ANISOU 1811  CG  PRO A 937     5557   5396   4435    653   1160   -403       C  
ATOM   1812  CD  PRO A 937      25.339 200.827   7.468  1.00 38.44           C  
ANISOU 1812  CD  PRO A 937     5273   5039   4292    673   1064   -297       C  
ATOM   1813  N   ILE A 938      23.826 204.400   6.278  1.00 32.69           N  
ANISOU 1813  N   ILE A 938     4394   4660   3363    404    792    -91       N  
ATOM   1814  CA  ILE A 938      23.136 205.617   5.944  1.00 32.72           C  
ANISOU 1814  CA  ILE A 938     4357   4756   3320    328    704      1       C  
ATOM   1815  C   ILE A 938      23.514 206.819   6.810  1.00 31.78           C  
ANISOU 1815  C   ILE A 938     4161   4605   3307    335    643    138       C  
ATOM   1816  O   ILE A 938      23.113 207.921   6.493  1.00 32.95           O  
ANISOU 1816  O   ILE A 938     4273   4810   3437    287    594    233       O  
ATOM   1817  CB  ILE A 938      21.589 205.452   5.990  1.00 29.62           C  
ANISOU 1817  CB  ILE A 938     4019   4347   2887    252    633    -51       C  
ATOM   1818  CG1 ILE A 938      21.109 205.145   7.403  1.00 29.12           C  
ANISOU 1818  CG1 ILE A 938     3988   4127   2948    266    587    -63       C  
ATOM   1819  CG2 ILE A 938      21.147 204.403   4.974  1.00 30.76           C  
ANISOU 1819  CG2 ILE A 938     4230   4554   2902    206    691   -202       C  
ATOM   1820  CD1 ILE A 938      19.592 205.220   7.567  1.00 29.06           C  
ANISOU 1820  CD1 ILE A 938     4006   4119   2915    189    509    -86       C  
ATOM   1821  N   CYS A 939      24.196 206.597   7.921  1.00 30.65           N  
ANISOU 1821  N   CYS A 939     3997   4374   3275    390    647    147       N  
ATOM   1822  CA  CYS A 939      24.378 207.627   8.936  1.00 30.25           C  
ANISOU 1822  CA  CYS A 939     3884   4285   3323    373    583    237       C  
ATOM   1823  C   CYS A 939      25.614 208.453   8.642  1.00 30.73           C  
ANISOU 1823  C   CYS A 939     3848   4426   3399    373    618    321       C  
ATOM   1824  O   CYS A 939      26.730 207.918   8.592  1.00 32.92           O  
ANISOU 1824  O   CYS A 939     4081   4746   3680    433    682    309       O  
ATOM   1825  CB  CYS A 939      24.576 207.023  10.329  1.00 31.61           C  
ANISOU 1825  CB  CYS A 939     4061   4362   3585    423    565    211       C  
ATOM   1826  SG  CYS A 939      23.076 206.244  10.933  1.00 32.99           S  
ANISOU 1826  SG  CYS A 939     4339   4428   3767    403    521    134       S  
ATOM   1827  N   THR A 940      25.426 209.760   8.631  1.00 28.02           N  
ANISOU 1827  N   THR A 940     3467   4090   3087    307    577    410       N  
ATOM   1828  CA  THR A 940      26.545 210.684   8.670  1.00 27.65           C  
ANISOU 1828  CA  THR A 940     3326   4089   3090    277    603    490       C  
ATOM   1829  C   THR A 940      27.228 210.598  10.013  1.00 27.47           C  
ANISOU 1829  C   THR A 940     3248   4029   3159    291    580    468       C  
ATOM   1830  O   THR A 940      26.648 210.069  10.954  1.00 26.18           O  
ANISOU 1830  O   THR A 940     3127   3791   3026    316    533    414       O  
ATOM   1831  CB  THR A 940      26.050 212.121   8.428  1.00 28.04           C  
ANISOU 1831  CB  THR A 940     3366   4111   3175    199    577    589       C  
ATOM   1832  CG2 THR A 940      25.500 212.225   6.980  1.00 28.84           C  
ANISOU 1832  CG2 THR A 940     3498   4299   3160    195    602    643       C  
ATOM   1833  OG1 THR A 940      25.036 212.464   9.395  1.00 27.18           O  
ANISOU 1833  OG1 THR A 940     3299   3888   3139    178    505    570       O  
ATOM   1834  N   ILE A 941      28.433 211.152  10.118  1.00 27.79           N  
ANISOU 1834  N   ILE A 941     3184   4138   3235    265    610    514       N  
ATOM   1835  CA  ILE A 941      29.096 211.252  11.406  1.00 29.19           C  
ANISOU 1835  CA  ILE A 941     3285   4320   3484    256    576    498       C  
ATOM   1836  C   ILE A 941      28.268 211.982  12.475  1.00 29.24           C  
ANISOU 1836  C   ILE A 941     3323   4225   3561    186    500    478       C  
ATOM   1837  O   ILE A 941      28.327 211.672  13.695  1.00 27.22           O  
ANISOU 1837  O   ILE A 941     3045   3962   3333    199    453    436       O  
ATOM   1838  CB  ILE A 941      30.521 211.828  11.265  1.00 29.34           C  
ANISOU 1838  CB  ILE A 941     3168   4456   3523    213    621    547       C  
ATOM   1839  CG1 ILE A 941      31.208 211.930  12.617  1.00 30.67           C  
ANISOU 1839  CG1 ILE A 941     3237   4670   3744    190    575    524       C  
ATOM   1840  CG2 ILE A 941      30.517 213.190  10.569  1.00 31.27           C  
ANISOU 1840  CG2 ILE A 941     3400   4685   3796     97    646    618       C  
ATOM   1841  CD1 ILE A 941      32.700 211.989  12.490  1.00 34.24           C  
ANISOU 1841  CD1 ILE A 941     3535   5281   4190    186    622    560       C  
ATOM   1842  N   ASP A 942      27.491 212.957  12.049  1.00 29.38           N  
ANISOU 1842  N   ASP A 942     3388   4170   3605    119    492    514       N  
ATOM   1843  CA  ASP A 942      26.679 213.711  12.990  1.00 30.30           C  
ANISOU 1843  CA  ASP A 942     3536   4178   3795     61    439    490       C  
ATOM   1844  C   ASP A 942      25.702 212.790  13.705  1.00 30.15           C  
ANISOU 1844  C   ASP A 942     3588   4112   3753    122    386    424       C  
ATOM   1845  O   ASP A 942      25.517 212.896  14.928  1.00 29.86           O  
ANISOU 1845  O   ASP A 942     3544   4043   3758    100    343    375       O  
ATOM   1846  CB  ASP A 942      25.875 214.783  12.258  1.00 31.41           C  
ANISOU 1846  CB  ASP A 942     3726   4239   3969     15    453    560       C  
ATOM   1847  CG  ASP A 942      26.725 215.741  11.508  1.00 32.91           C  
ANISOU 1847  CG  ASP A 942     3859   4455   4189    -50    517    645       C  
ATOM   1848  OD1 ASP A 942      27.319 215.421  10.442  1.00 33.54           O  
ANISOU 1848  OD1 ASP A 942     3911   4635   4195    -25    566    698       O  
ATOM   1849  OD2 ASP A 942      26.787 216.866  11.960  1.00 34.70           O1-
ANISOU 1849  OD2 ASP A 942     4072   4595   4517   -136    528    659       O1-
ATOM   1850  N   VAL A 943      25.038 211.903  12.956  1.00 31.47           N  
ANISOU 1850  N   VAL A 943     3825   4281   3850    186    395    417       N  
ATOM   1851  CA  VAL A 943      24.090 210.964  13.582  1.00 28.30           C  
ANISOU 1851  CA  VAL A 943     3493   3828   3431    230    357    355       C  
ATOM   1852  C   VAL A 943      24.794 209.882  14.387  1.00 30.79           C  
ANISOU 1852  C   VAL A 943     3786   4172   3740    295    362    320       C  
ATOM   1853  O   VAL A 943      24.371 209.555  15.517  1.00 29.85           O  
ANISOU 1853  O   VAL A 943     3683   4015   3642    305    322    289       O  
ATOM   1854  CB  VAL A 943      23.116 210.341  12.568  1.00 30.19           C  
ANISOU 1854  CB  VAL A 943     3809   4063   3596    253    366    341       C  
ATOM   1855  CG1 VAL A 943      22.213 209.320  13.243  1.00 29.89           C  
ANISOU 1855  CG1 VAL A 943     3839   3968   3549    281    339    272       C  
ATOM   1856  CG2 VAL A 943      22.276 211.429  11.896  1.00 28.80           C  
ANISOU 1856  CG2 VAL A 943     3643   3877   3421    206    349    402       C  
ATOM   1857  N   TYR A 944      25.867 209.327  13.859  1.00 27.39           N  
ANISOU 1857  N   TYR A 944     3311   3814   3280    349    417    335       N  
ATOM   1858  CA  TYR A 944      26.602 208.343  14.634  1.00 28.18           C  
ANISOU 1858  CA  TYR A 944     3375   3946   3384    434    429    328       C  
ATOM   1859  C   TYR A 944      27.163 208.891  15.924  1.00 29.57           C  
ANISOU 1859  C   TYR A 944     3459   4177   3598    401    378    344       C  
ATOM   1860  O   TYR A 944      27.189 208.181  16.939  1.00 31.18           O  
ANISOU 1860  O   TYR A 944     3656   4388   3801    458    355    344       O  
ATOM   1861  CB  TYR A 944      27.709 207.734  13.823  1.00 29.66           C  
ANISOU 1861  CB  TYR A 944     3516   4210   3542    510    508    347       C  
ATOM   1862  CG  TYR A 944      28.355 206.514  14.440  1.00 30.48           C  
ANISOU 1862  CG  TYR A 944     3597   4328   3654    635    542    356       C  
ATOM   1863  CD1 TYR A 944      27.601 205.428  14.912  1.00 29.08           C  
ANISOU 1863  CD1 TYR A 944     3518   4045   3485    698    548    326       C  
ATOM   1864  CD2 TYR A 944      29.736 206.429  14.535  1.00 31.64           C  
ANISOU 1864  CD2 TYR A 944     3618   4598   3805    697    577    406       C  
ATOM   1865  CE1 TYR A 944      28.217 204.323  15.484  1.00 30.69           C  
ANISOU 1865  CE1 TYR A 944     3703   4247   3709    829    592    360       C  
ATOM   1866  CE2 TYR A 944      30.357 205.318  15.039  1.00 32.13           C  
ANISOU 1866  CE2 TYR A 944     3649   4680   3879    837    617    438       C  
ATOM   1867  CZ  TYR A 944      29.607 204.276  15.550  1.00 30.34           C  
ANISOU 1867  CZ  TYR A 944     3528   4330   3669    908    626    423       C  
ATOM   1868  OH  TYR A 944      30.302 203.203  16.065  1.00 31.55           O  
ANISOU 1868  OH  TYR A 944     3645   4496   3847   1064    678    482       O  
ATOM   1869  N   MET A 945      27.642 210.127  15.902  1.00 27.38           N  
ANISOU 1869  N   MET A 945     3108   3945   3350    305    365    359       N  
ATOM   1870  CA  MET A 945      28.179 210.745  17.105  1.00 32.97           C  
ANISOU 1870  CA  MET A 945     3723   4720   4084    242    317    346       C  
ATOM   1871  C   MET A 945      27.153 210.789  18.238  1.00 32.60           C  
ANISOU 1871  C   MET A 945     3733   4606   4046    218    257    299       C  
ATOM   1872  O   MET A 945      27.499 210.521  19.391  1.00 32.23           O  
ANISOU 1872  O   MET A 945     3627   4638   3978    229    219    290       O  
ATOM   1873  CB  MET A 945      28.658 212.158  16.820  1.00 37.14           C  
ANISOU 1873  CB  MET A 945     4188   5264   4658    113    328    349       C  
ATOM   1874  CG  MET A 945      29.360 212.807  17.996  1.00 43.19           C  
ANISOU 1874  CG  MET A 945     4844   6122   5442     21    288    311       C  
ATOM   1875  SD  MET A 945      31.003 212.073  18.315  1.00 54.86           S  
ANISOU 1875  SD  MET A 945     6149   7827   6866     85    293    353       S  
ATOM   1876  CE  MET A 945      31.814 212.562  16.783  1.00 50.80           C  
ANISOU 1876  CE  MET A 945     5591   7338   6371     53    378    407       C  
ATOM   1877  N   ILE A 946      25.897 211.085  17.910  1.00 30.95           N  
ANISOU 1877  N   ILE A 946     3628   4273   3857    192    251    277       N  
ATOM   1878  CA  ILE A 946      24.854 211.023  18.904  1.00 30.52           C  
ANISOU 1878  CA  ILE A 946     3628   4161   3808    181    206    233       C  
ATOM   1879  C   ILE A 946      24.740 209.631  19.524  1.00 29.48           C  
ANISOU 1879  C   ILE A 946     3521   4049   3630    279    198    244       C  
ATOM   1880  O   ILE A 946      24.661 209.483  20.733  1.00 29.60           O  
ANISOU 1880  O   ILE A 946     3511   4105   3628    277    160    230       O  
ATOM   1881  CB  ILE A 946      23.483 211.456  18.354  1.00 32.77           C  
ANISOU 1881  CB  ILE A 946     4006   4325   4117    156    206    221       C  
ATOM   1882  CG1 ILE A 946      23.549 212.913  17.935  1.00 36.65           C  
ANISOU 1882  CG1 ILE A 946     4477   4776   4672     70    222    230       C  
ATOM   1883  CG2 ILE A 946      22.412 211.256  19.432  1.00 32.05           C  
ANISOU 1883  CG2 ILE A 946     3960   4190   4025    154    166    175       C  
ATOM   1884  CD1 ILE A 946      22.300 213.309  17.155  1.00 39.23           C  
ANISOU 1884  CD1 ILE A 946     4878   5009   5016     75    229    256       C  
ATOM   1885  N   MET A 947      24.739 208.618  18.685  1.00 29.49           N  
ANISOU 1885  N   MET A 947     3571   4020   3610    361    243    268       N  
ATOM   1886  CA  MET A 947      24.669 207.259  19.155  1.00 30.93           C  
ANISOU 1886  CA  MET A 947     3792   4187   3772    458    259    287       C  
ATOM   1887  C   MET A 947      25.810 206.945  20.066  1.00 30.73           C  
ANISOU 1887  C   MET A 947     3661   4282   3730    517    249    339       C  
ATOM   1888  O   MET A 947      25.587 206.383  21.138  1.00 29.40           O  
ANISOU 1888  O   MET A 947     3496   4130   3544    556    225    363       O  
ATOM   1889  CB  MET A 947      24.745 206.285  17.998  1.00 32.82           C  
ANISOU 1889  CB  MET A 947     4093   4373   4002    531    332    289       C  
ATOM   1890  CG  MET A 947      23.392 205.947  17.420  1.00 37.87           C  
ANISOU 1890  CG  MET A 947     4850   4903   4633    498    341    237       C  
ATOM   1891  SD  MET A 947      23.582 204.951  15.902  1.00 41.19           S  
ANISOU 1891  SD  MET A 947     5337   5286   5024    551    435    202       S  
ATOM   1892  CE  MET A 947      23.305 206.304  14.879  1.00 33.45           C  
ANISOU 1892  CE  MET A 947     4331   4360   4017    456    405    199       C  
ATOM   1893  N   VAL A 948      27.037 207.247  19.602  1.00 29.74           N  
ANISOU 1893  N   VAL A 948     3435   4259   3603    529    271    367       N  
ATOM   1894  CA  VAL A 948      28.222 207.013  20.387  1.00 30.51           C  
ANISOU 1894  CA  VAL A 948     3402   4514   3677    584    257    425       C  
ATOM   1895  C   VAL A 948      28.139 207.714  21.739  1.00 29.25           C  
ANISOU 1895  C   VAL A 948     3176   4448   3489    498    176    402       C  
ATOM   1896  O   VAL A 948      28.530 207.146  22.763  1.00 31.06           O  
ANISOU 1896  O   VAL A 948     3339   4789   3673    562    149    457       O  
ATOM   1897  CB  VAL A 948      29.522 207.428  19.625  1.00 33.98           C  
ANISOU 1897  CB  VAL A 948     3723   5067   4118    582    292    450       C  
ATOM   1898  CG1 VAL A 948      30.729 207.431  20.550  1.00 35.72           C  
ANISOU 1898  CG1 VAL A 948     3771   5495   4303    609    258    504       C  
ATOM   1899  CG2 VAL A 948      29.805 206.446  18.485  1.00 36.09           C  
ANISOU 1899  CG2 VAL A 948     4038   5279   4393    704    384    477       C  
ATOM   1900  N   LYS A 949      27.660 208.955  21.776  1.00 28.30           N  
ANISOU 1900  N   LYS A 949     3068   4293   3391    356    145    325       N  
ATOM   1901  CA  LYS A 949      27.554 209.643  23.045  1.00 29.77           C  
ANISOU 1901  CA  LYS A 949     3200   4562   3549    262     82    274       C  
ATOM   1902  C   LYS A 949      26.592 208.945  24.043  1.00 29.77           C  
ANISOU 1902  C   LYS A 949     3268   4531   3509    309     54    279       C  
ATOM   1903  O   LYS A 949      26.812 208.996  25.268  1.00 28.46           O  
ANISOU 1903  O   LYS A 949     3030   4504   3280    286      5    274       O  
ATOM   1904  CB  LYS A 949      27.100 211.074  22.831  1.00 32.69           C  
ANISOU 1904  CB  LYS A 949     3595   4851   3974    112     79    182       C  
ATOM   1905  CG  LYS A 949      28.184 211.980  22.292  1.00 38.05           C  
ANISOU 1905  CG  LYS A 949     4175   5597   4683     24     99    172       C  
ATOM   1906  CD  LYS A 949      27.522 213.315  21.989  1.00 43.61           C  
ANISOU 1906  CD  LYS A 949     4942   6160   5467   -103    119    100       C  
ATOM   1907  CE  LYS A 949      28.518 214.315  21.457  1.00 52.71           C  
ANISOU 1907  CE  LYS A 949     6010   7349   6667   -215    153     91       C  
ATOM   1908  NZ  LYS A 949      27.801 215.603  21.313  1.00 57.97           N1+
ANISOU 1908  NZ  LYS A 949     6749   7850   7425   -328    183     29       N1+
ATOM   1909  N   CYS A 950      25.538 208.325  23.509  1.00 29.25           N  
ANISOU 1909  N   CYS A 950     3335   4303   3474    360     87    286       N  
ATOM   1910  CA  CYS A 950      24.644 207.529  24.316  1.00 30.13           C  
ANISOU 1910  CA  CYS A 950     3514   4375   3557    406     77    305       C  
ATOM   1911  C   CYS A 950      25.314 206.319  24.992  1.00 31.10           C  
ANISOU 1911  C   CYS A 950     3591   4593   3632    534     85    415       C  
ATOM   1912  O   CYS A 950      24.744 205.768  25.916  1.00 29.31           O  
ANISOU 1912  O   CYS A 950     3394   4373   3367    562     72    448       O  
ATOM   1913  CB  CYS A 950      23.448 207.061  23.502  1.00 27.76           C  
ANISOU 1913  CB  CYS A 950     3352   3894   3299    421    116    287       C  
ATOM   1914  SG  CYS A 950      22.355 208.365  22.974  1.00 28.05           S  
ANISOU 1914  SG  CYS A 950     3441   3832   3383    301    102    193       S  
ATOM   1915  N   TRP A 951      26.492 205.907  24.495  1.00 31.07           N  
ANISOU 1915  N   TRP A 951     3512   4660   3632    620    114    481       N  
ATOM   1916  CA  TRP A 951      27.192 204.726  24.927  1.00 31.88           C  
ANISOU 1916  CA  TRP A 951     3568   4833   3709    773    141    607       C  
ATOM   1917  C   TRP A 951      28.537 205.008  25.608  1.00 32.39           C  
ANISOU 1917  C   TRP A 951     3444   5153   3709    795     94    668       C  
ATOM   1918  O   TRP A 951      29.422 204.141  25.691  1.00 34.49           O  
ANISOU 1918  O   TRP A 951     3634   5504   3963    944    125    789       O  
ATOM   1919  CB  TRP A 951      27.415 203.777  23.737  1.00 31.76           C  
ANISOU 1919  CB  TRP A 951     3624   4681   3759    890    237    643       C  
ATOM   1920  CG  TRP A 951      26.186 203.424  22.954  1.00 29.04           C  
ANISOU 1920  CG  TRP A 951     3450   4117   3466    859    284    574       C  
ATOM   1921  CD1 TRP A 951      24.933 203.234  23.429  1.00 28.07           C  
ANISOU 1921  CD1 TRP A 951     3428   3893   3343    810    271    544       C  
ATOM   1922  CD2 TRP A 951      26.115 203.183  21.547  1.00 29.08           C  
ANISOU 1922  CD2 TRP A 951     3530   4002   3514    870    355    523       C  
ATOM   1923  CE2 TRP A 951      24.775 202.873  21.237  1.00 28.52           C  
ANISOU 1923  CE2 TRP A 951     3600   3772   3464    816    372    459       C  
ATOM   1924  CE3 TRP A 951      27.038 203.212  20.523  1.00 31.10           C  
ANISOU 1924  CE3 TRP A 951     3741   4291   3784    913    405    522       C  
ATOM   1925  NE1 TRP A 951      24.074 202.905  22.405  1.00 29.08           N  
ANISOU 1925  NE1 TRP A 951     3681   3852   3514    782    322    477       N  
ATOM   1926  CZ2 TRP A 951      24.356 202.587  19.954  1.00 29.90           C  
ANISOU 1926  CZ2 TRP A 951     3865   3832   3660    798    431    390       C  
ATOM   1927  CZ3 TRP A 951      26.623 202.909  19.246  1.00 32.80           C  
ANISOU 1927  CZ3 TRP A 951     4057   4383   4022    904    472    455       C  
ATOM   1928  CH2 TRP A 951      25.277 202.620  18.970  1.00 30.18           C  
ANISOU 1928  CH2 TRP A 951     3861   3906   3698    841    480    385       C  
ATOM   1929  N   MET A 952      28.658 206.198  26.160  1.00 33.03           N  
ANISOU 1929  N   MET A 952     3442   5360   3744    646     24    583       N  
ATOM   1930  CA  MET A 952      29.768 206.579  26.958  1.00 35.06           C  
ANISOU 1930  CA  MET A 952     3514   5887   3919    621    -34    610       C  
ATOM   1931  C   MET A 952      29.697 205.843  28.286  1.00 37.33           C  
ANISOU 1931  C   MET A 952     3758   6316   4109    702    -74    711       C  
ATOM   1932  O   MET A 952      28.617 205.600  28.792  1.00 32.01           O  
ANISOU 1932  O   MET A 952     3196   5541   3426    692    -76    697       O  
ATOM   1933  CB  MET A 952      29.702 208.047  27.283  1.00 39.43           C  
ANISOU 1933  CB  MET A 952     4021   6506   4455    413    -88    462       C  
ATOM   1934  CG  MET A 952      29.632 208.929  26.083  1.00 43.85           C  
ANISOU 1934  CG  MET A 952     4634   6916   5111    316    -47    373       C  
ATOM   1935  SD  MET A 952      31.249 209.497  25.680  1.00 50.27           S  
ANISOU 1935  SD  MET A 952     5255   7927   5916    264    -49    382       S  
ATOM   1936  CE  MET A 952      30.787 211.222  25.735  1.00 50.18           C  
ANISOU 1936  CE  MET A 952     5276   7837   5953     17    -63    205       C  
ATOM   1937  N   ILE A 953      30.856 205.550  28.850  1.00 36.88           N  
ANISOU 1937  N   ILE A 953     3524   6515   3973    777   -107    816       N  
ATOM   1938  CA  ILE A 953      30.938 204.906  30.133  1.00 41.07           C  
ANISOU 1938  CA  ILE A 953     3981   7233   4389    861   -152    938       C  
ATOM   1939  C   ILE A 953      30.433 205.793  31.265  1.00 42.06           C  
ANISOU 1939  C   ILE A 953     4077   7499   4405    687   -234    822       C  
ATOM   1940  O   ILE A 953      29.826 205.292  32.204  1.00 41.77           O  
ANISOU 1940  O   ILE A 953     4076   7502   4293    727   -251    886       O  
ATOM   1941  CB  ILE A 953      32.365 204.398  30.387  1.00 44.57           C  
ANISOU 1941  CB  ILE A 953     4218   7946   4768    997   -168   1095       C  
ATOM   1942  CG1 ILE A 953      32.569 203.129  29.570  1.00 49.47           C  
ANISOU 1942  CG1 ILE A 953     4909   8389   5495   1227    -61   1244       C  
ATOM   1943  CG2 ILE A 953      32.613 204.089  31.853  1.00 48.95           C  
ANISOU 1943  CG2 ILE A 953     4641   8794   5161   1039   -244   1211       C  
ATOM   1944  CD1 ILE A 953      33.951 202.546  29.666  1.00 55.15           C  
ANISOU 1944  CD1 ILE A 953     5431   9341   6179   1401    -54   1415       C  
ATOM   1945  N   ASP A 954      30.705 207.098  31.216  1.00 42.34           N  
ANISOU 1945  N   ASP A 954     4046   7613   4427    491   -276    653       N  
ATOM   1946  CA  ASP A 954      30.250 207.957  32.278  1.00 43.69           C  
ANISOU 1946  CA  ASP A 954     4194   7906   4499    322   -338    518       C  
ATOM   1947  C   ASP A 954      28.805 208.301  31.974  1.00 39.37           C  
ANISOU 1947  C   ASP A 954     3851   7063   4043    256   -294    405       C  
ATOM   1948  O   ASP A 954      28.520 209.013  31.019  1.00 35.02           O  
ANISOU 1948  O   ASP A 954     3381   6313   3612    176   -255    299       O  
ATOM   1949  CB  ASP A 954      31.068 209.224  32.403  1.00 48.75           C  
ANISOU 1949  CB  ASP A 954     4692   8726   5102    124   -384    365       C  
ATOM   1950  CG  ASP A 954      30.518 210.129  33.503  1.00 55.30           C  
ANISOU 1950  CG  ASP A 954     5518   9657   5834    -61   -430    192       C  
ATOM   1951  OD1 ASP A 954      30.131 209.591  34.546  1.00 64.70           O  
ANISOU 1951  OD1 ASP A 954     6699  10984   6900    -10   -465    252       O  
ATOM   1952  OD2 ASP A 954      30.407 211.354  33.328  1.00 58.44           O1-
ANISOU 1952  OD2 ASP A 954     5935   9981   6285   -253   -418     -1       O1-
ATOM   1953  N   ALA A 955      27.881 207.774  32.759  1.00 35.85           N  
ANISOU 1953  N   ALA A 955     3482   6596   3541    298   -296    442       N  
ATOM   1954  CA  ALA A 955      26.468 207.924  32.457  1.00 35.85           C  
ANISOU 1954  CA  ALA A 955     3663   6329   3626    262   -250    361       C  
ATOM   1955  C   ALA A 955      26.019 209.401  32.370  1.00 34.98           C  
ANISOU 1955  C   ALA A 955     3584   6146   3561     69   -252    145       C  
ATOM   1956  O   ALA A 955      25.159 209.762  31.577  1.00 33.51           O  
ANISOU 1956  O   ALA A 955     3525   5713   3494     43   -205     79       O  
ATOM   1957  CB  ALA A 955      25.641 207.218  33.527  1.00 36.69           C  
ANISOU 1957  CB  ALA A 955     3815   6484   3641    313   -256    431       C  
ATOM   1958  N   ASP A 956      26.600 210.232  33.212  1.00 39.06           N  
ANISOU 1958  N   ASP A 956     3979   6883   3979    -63   -302     37       N  
ATOM   1959  CA  ASP A 956      26.248 211.625  33.255  1.00 43.34           C  
ANISOU 1959  CA  ASP A 956     4547   7351   4567   -247   -288   -173       C  
ATOM   1960  C   ASP A 956      26.800 212.377  32.061  1.00 43.60           C  
ANISOU 1960  C   ASP A 956     4581   7247   4737   -308   -254   -223       C  
ATOM   1961  O   ASP A 956      26.404 213.506  31.860  1.00 43.00           O  
ANISOU 1961  O   ASP A 956     4559   7034   4744   -439   -219   -375       O  
ATOM   1962  CB  ASP A 956      26.739 212.266  34.543  1.00 47.07           C  
ANISOU 1962  CB  ASP A 956     4889   8108   4884   -391   -344   -296       C  
ATOM   1963  CG  ASP A 956      25.947 211.813  35.739  1.00 49.16           C  
ANISOU 1963  CG  ASP A 956     5177   8487   5015   -364   -363   -286       C  
ATOM   1964  OD1 ASP A 956      24.721 211.548  35.606  1.00 54.32           O  
ANISOU 1964  OD1 ASP A 956     5973   8932   5731   -308   -316   -275       O  
ATOM   1965  OD2 ASP A 956      26.563 211.683  36.790  1.00 62.33           O1-
ANISOU 1965  OD2 ASP A 956     6708  10469   6504   -399   -425   -277       O1-
ATOM   1966  N   SER A 957      27.726 211.774  31.318  1.00 40.48           N  
ANISOU 1966  N   SER A 957     4122   6893   4364   -213   -256    -94       N  
ATOM   1967  CA  SER A 957      28.192 212.332  30.035  1.00 39.63           C  
ANISOU 1967  CA  SER A 957     4025   6644   4385   -249   -211   -110       C  
ATOM   1968  C   SER A 957      27.299 212.075  28.866  1.00 36.90           C  
ANISOU 1968  C   SER A 957     3840   6011   4166   -164   -149    -65       C  
ATOM   1969  O   SER A 957      27.515 212.627  27.806  1.00 35.82           O  
ANISOU 1969  O   SER A 957     3727   5752   4129   -200   -108    -80       O  
ATOM   1970  CB  SER A 957      29.552 211.749  29.648  1.00 39.30           C  
ANISOU 1970  CB  SER A 957     3843   6777   4312   -170   -227     11       C  
ATOM   1971  OG  SER A 957      30.463 212.284  30.543  1.00 44.27           O  
ANISOU 1971  OG  SER A 957     4301   7683   4834   -293   -284    -56       O  
ATOM   1972  N   ARG A 958      26.346 211.181  29.008  1.00 34.57           N  
ANISOU 1972  N   ARG A 958     3646   5626   3860    -51   -142      1       N  
ATOM   1973  CA AARG A 958      25.516 210.830  27.878  0.50 34.07           C  
ANISOU 1973  CA AARG A 958     3721   5324   3899     22    -89     41       C  
ATOM   1974  CA BARG A 958      25.442 210.813  27.914  0.50 30.46           C  
ANISOU 1974  CA BARG A 958     3269   4862   3440     23    -89     40       C  
ATOM   1975  C   ARG A 958      24.488 211.963  27.678  1.00 31.36           C  
ANISOU 1975  C   ARG A 958     3467   4810   3636    -84    -64    -80       C  
ATOM   1976  O   ARG A 958      24.220 212.724  28.578  1.00 30.55           O  
ANISOU 1976  O   ARG A 958     3347   4753   3506   -185    -78   -190       O  
ATOM   1977  CB AARG A 958      24.907 209.448  28.126  0.50 35.84           C  
ANISOU 1977  CB AARG A 958     4012   5516   4085    162    -83    150       C  
ATOM   1978  CB BARG A 958      24.628 209.561  28.271  0.50 26.99           C  
ANISOU 1978  CB BARG A 958     2909   4380   2964    145    -84    130       C  
ATOM   1979  CG AARG A 958      25.935 208.554  28.817  0.50 38.82           C  
ANISOU 1979  CG AARG A 958     4277   6104   4368    257   -112    267       C  
ATOM   1980  CG BARG A 958      25.491 208.322  28.272  0.50 25.07           C  
ANISOU 1980  CG BARG A 958     2610   4236   2677    288    -82    277       C  
ATOM   1981  CD AARG A 958      25.941 207.104  28.394  0.50 40.89           C  
ANISOU 1981  CD AARG A 958     4593   6291   4649    431    -68    414       C  
ATOM   1982  CD BARG A 958      24.857 207.085  28.848  0.50 22.20           C  
ANISOU 1982  CD BARG A 958     2311   3848   2275    399    -69    378       C  
ATOM   1983  NE AARG A 958      24.940 206.348  29.098  0.50 40.07           N  
ANISOU 1983  NE AARG A 958     4575   6134   4515    478    -60    459       N  
ATOM   1984  NE BARG A 958      25.904 206.127  29.270  0.50 21.81           N  
ANISOU 1984  NE BARG A 958     2164   3957   2164    529    -74    526       N  
ATOM   1985  CZ AARG A 958      25.175 205.454  30.061  0.50 41.37           C  
ANISOU 1985  CZ AARG A 958     4695   6424   4597    573    -71    583       C  
ATOM   1986  CZ BARG A 958      25.732 205.226  30.238  0.50 22.74           C  
ANISOU 1986  CZ BARG A 958     2277   4152   2209    617    -80    639       C  
ATOM   1987  NH1AARG A 958      26.403 205.144  30.466  0.50 43.09           N1+
ANISOU 1987  NH1AARG A 958     4773   6850   4748    649    -98    686       N1+
ATOM   1988  NH1BARG A 958      26.713 204.381  30.589  0.50 23.17           N1+
ANISOU 1988  NH1BARG A 958     2234   4353   2215    755    -79    797       N1+
ATOM   1989  NH2AARG A 958      24.141 204.859  30.620  0.50 39.77           N  
ANISOU 1989  NH2AARG A 958     4585   6147   4379    594    -52    617       N  
ATOM   1990  NH2BARG A 958      24.566 205.190  30.863  0.50 21.83           N  
ANISOU 1990  NH2BARG A 958     2247   3974   2070    571    -80    605       N  
ATOM   1991  N   PRO A 959      23.967 212.102  26.471  1.00 30.94           N  
ANISOU 1991  N   PRO A 959     3503   4572   3679    -59    -20    -61       N  
ATOM   1992  CA  PRO A 959      22.959 213.135  26.304  1.00 31.47           C  
ANISOU 1992  CA  PRO A 959     3645   4485   3825   -132      7   -149       C  
ATOM   1993  C   PRO A 959      21.739 212.879  27.203  1.00 31.99           C  
ANISOU 1993  C   PRO A 959     3770   4529   3855   -117     -1   -187       C  
ATOM   1994  O   PRO A 959      21.466 211.745  27.598  1.00 28.87           O  
ANISOU 1994  O   PRO A 959     3390   4184   3393    -35    -19   -118       O  
ATOM   1995  CB  PRO A 959      22.565 213.002  24.829  1.00 32.18           C  
ANISOU 1995  CB  PRO A 959     3810   4424   3991    -73     45    -80       C  
ATOM   1996  CG  PRO A 959      23.633 212.186  24.195  1.00 31.91           C  
ANISOU 1996  CG  PRO A 959     3728   4469   3927     -5     46      7       C  
ATOM   1997  CD  PRO A 959      24.122 211.281  25.268  1.00 31.62           C  
ANISOU 1997  CD  PRO A 959     3629   4587   3796     45      8     39       C  
ATOM   1998  N   LYS A 960      21.003 213.935  27.475  1.00 30.12           N  
ANISOU 1998  N   LYS A 960     3566   4202   3673   -192     23   -289       N  
ATOM   1999  CA  LYS A 960      19.694 213.856  28.094  1.00 30.02           C  
ANISOU 1999  CA  LYS A 960     3613   4141   3649   -175     32   -329       C  
ATOM   2000  C   LYS A 960      18.597 213.745  27.039  1.00 29.06           C  
ANISOU 2000  C   LYS A 960     3576   3857   3608   -110     61   -273       C  
ATOM   2001  O   LYS A 960      18.723 214.244  25.932  1.00 26.13           O  
ANISOU 2001  O   LYS A 960     3223   3388   3317   -107     85   -242       O  
ATOM   2002  CB  LYS A 960      19.439 215.099  28.951  1.00 33.87           C  
ANISOU 2002  CB  LYS A 960     4089   4617   4160   -281     58   -481       C  
ATOM   2003  CG  LYS A 960      20.463 215.359  30.071  1.00 38.51           C  
ANISOU 2003  CG  LYS A 960     4582   5397   4650   -380     27   -571       C  
ATOM   2004  CD  LYS A 960      20.485 214.283  31.176  1.00 44.63           C  
ANISOU 2004  CD  LYS A 960     5315   6373   5268   -337    -24   -529       C  
ATOM   2005  CE  LYS A 960      19.184 214.186  32.037  1.00 52.31           C  
ANISOU 2005  CE  LYS A 960     6339   7334   6199   -324     -5   -581       C  
ATOM   2006  NZ  LYS A 960      18.890 212.859  32.754  1.00 50.97           N1+
ANISOU 2006  NZ  LYS A 960     6163   7298   5904   -242    -39   -472       N1+
ATOM   2007  N   PHE A 961      17.498 213.086  27.374  1.00 26.61           N  
ANISOU 2007  N   PHE A 961     3308   3533   3266    -62     59   -256       N  
ATOM   2008  CA  PHE A 961      16.424 212.929  26.415  1.00 27.19           C  
ANISOU 2008  CA  PHE A 961     3441   3491   3397    -12     78   -208       C  
ATOM   2009  C   PHE A 961      15.951 214.266  25.852  1.00 29.44           C  
ANISOU 2009  C   PHE A 961     3739   3656   3790    -36    117   -246       C  
ATOM   2010  O   PHE A 961      15.649 214.385  24.656  1.00 27.32           O  
ANISOU 2010  O   PHE A 961     3494   3312   3573      0    128   -179       O  
ATOM   2011  CB  PHE A 961      15.254 212.154  27.036  1.00 27.79           C  
ANISOU 2011  CB  PHE A 961     3547   3586   3426     15     77   -203       C  
ATOM   2012  CG  PHE A 961      15.523 210.664  27.162  1.00 24.21           C  
ANISOU 2012  CG  PHE A 961     3107   3191   2897     61     58   -122       C  
ATOM   2013  CD1 PHE A 961      15.745 209.900  26.039  1.00 25.84           C  
ANISOU 2013  CD1 PHE A 961     3348   3350   3120    104     62    -51       C  
ATOM   2014  CD2 PHE A 961      15.555 210.042  28.410  1.00 26.44           C  
ANISOU 2014  CD2 PHE A 961     3374   3577   3095     61     48   -116       C  
ATOM   2015  CE1 PHE A 961      16.016 208.542  26.134  1.00 25.74           C  
ANISOU 2015  CE1 PHE A 961     3359   3357   3061    152     66     16       C  
ATOM   2016  CE2 PHE A 961      15.805 208.687  28.522  1.00 27.17           C  
ANISOU 2016  CE2 PHE A 961     3486   3698   3137    115     47    -22       C  
ATOM   2017  CZ  PHE A 961      16.058 207.930  27.390  1.00 27.82           C  
ANISOU 2017  CZ  PHE A 961     3610   3702   3257    163     61     41       C  
ATOM   2018  N   ARG A 962      15.965 215.291  26.674  1.00 25.89           N  
ANISOU 2018  N   ARG A 962     3272   3191   3373    -96    145   -349       N  
ATOM   2019  CA  ARG A 962      15.503 216.593  26.221  1.00 29.88           C  
ANISOU 2019  CA  ARG A 962     3796   3552   4001   -107    202   -380       C  
ATOM   2020  C   ARG A 962      16.466 217.180  25.181  1.00 30.57           C  
ANISOU 2020  C   ARG A 962     3878   3578   4158   -132    219   -329       C  
ATOM   2021  O   ARG A 962      16.029 217.850  24.278  1.00 29.88           O  
ANISOU 2021  O   ARG A 962     3814   3373   4163    -99    257   -271       O  
ATOM   2022  CB  ARG A 962      15.268 217.536  27.392  1.00 34.21           C  
ANISOU 2022  CB  ARG A 962     4339   4079   4577   -171    248   -526       C  
ATOM   2023  CG  ARG A 962      16.486 217.871  28.238  1.00 40.04           C  
ANISOU 2023  CG  ARG A 962     5034   4909   5270   -282    240   -633       C  
ATOM   2024  CD  ARG A 962      16.202 218.958  29.291  1.00 47.14           C  
ANISOU 2024  CD  ARG A 962     5937   5768   6206   -363    304   -808       C  
ATOM   2025  NE  ARG A 962      15.722 220.187  28.612  1.00 56.14           N  
ANISOU 2025  NE  ARG A 962     7124   6684   7520   -351    393   -820       N  
ATOM   2026  CZ  ARG A 962      16.470 221.029  27.875  1.00 58.44           C  
ANISOU 2026  CZ  ARG A 962     7424   6857   7922   -403    435   -806       C  
ATOM   2027  NH1 ARG A 962      17.784 220.846  27.733  1.00 57.52           N1+
ANISOU 2027  NH1 ARG A 962     7261   6835   7758   -485    395   -801       N1+
ATOM   2028  NH2 ARG A 962      15.897 222.091  27.290  1.00 60.99           N  
ANISOU 2028  NH2 ARG A 962     7796   6967   8409   -369    527   -789       N  
ATOM   2029  N   GLU A 963      17.772 216.917  25.318  1.00 29.41           N  
ANISOU 2029  N   GLU A 963     3688   3525   3961   -185    192   -337       N  
ATOM   2030  CA  GLU A 963      18.754 217.266  24.293  1.00 29.80           C  
ANISOU 2030  CA  GLU A 963     3719   3545   4057   -208    206   -274       C  
ATOM   2031  C   GLU A 963      18.596 216.488  23.002  1.00 28.19           C  
ANISOU 2031  C   GLU A 963     3537   3339   3831   -121    189   -142       C  
ATOM   2032  O   GLU A 963      18.742 217.038  21.901  1.00 27.93           O  
ANISOU 2032  O   GLU A 963     3515   3235   3861   -114    221    -71       O  
ATOM   2033  CB  GLU A 963      20.183 217.067  24.838  1.00 30.35           C  
ANISOU 2033  CB  GLU A 963     3714   3753   4062   -283    177   -316       C  
ATOM   2034  CG  GLU A 963      20.430 217.944  26.070  1.00 34.95           C  
ANISOU 2034  CG  GLU A 963     4265   4361   4652   -400    195   -471       C  
ATOM   2035  CD  GLU A 963      21.718 217.610  26.811  1.00 37.52           C  
ANISOU 2035  CD  GLU A 963     4493   4887   4877   -474    148   -515       C  
ATOM   2036  OE1 GLU A 963      22.242 216.503  26.676  1.00 36.07           O  
ANISOU 2036  OE1 GLU A 963     4268   4831   4604   -404     97   -423       O  
ATOM   2037  OE2 GLU A 963      22.198 218.478  27.511  1.00 38.86           O1-
ANISOU 2037  OE2 GLU A 963     4622   5083   5058   -602    168   -644       O1-
ATOM   2038  N   LEU A 964      18.304 215.207  23.130  1.00 28.62           N  
ANISOU 2038  N   LEU A 964     3602   3476   3796    -60    146   -112       N  
ATOM   2039  CA  LEU A 964      18.081 214.351  21.989  1.00 27.76           C  
ANISOU 2039  CA  LEU A 964     3521   3371   3655      8    136    -19       C  
ATOM   2040  C   LEU A 964      16.875 214.812  21.159  1.00 30.11           C  
ANISOU 2040  C   LEU A 964     3855   3584   4001     43    154     25       C  
ATOM   2041  O   LEU A 964      16.929 214.781  19.909  1.00 28.24           O  
ANISOU 2041  O   LEU A 964     3627   3341   3762     71    162    104       O  
ATOM   2042  CB  LEU A 964      17.963 212.882  22.425  1.00 26.62           C  
ANISOU 2042  CB  LEU A 964     3390   3303   3420     54    104    -10       C  
ATOM   2043  CG  LEU A 964      19.254 212.323  23.038  1.00 29.38           C  
ANISOU 2043  CG  LEU A 964     3689   3756   3716     51     88    -11       C  
ATOM   2044  CD1 LEU A 964      18.927 211.087  23.849  1.00 30.02           C  
ANISOU 2044  CD1 LEU A 964     3787   3890   3726     98     68      0       C  
ATOM   2045  CD2 LEU A 964      20.311 212.023  21.985  1.00 28.62           C  
ANISOU 2045  CD2 LEU A 964     3571   3687   3616     78    103     49       C  
ATOM   2046  N   ILE A 965      15.827 215.292  21.831  1.00 26.62           N  
ANISOU 2046  N   ILE A 965     3424   3093   3595     46    164    -18       N  
ATOM   2047  CA  ILE A 965      14.692 215.884  21.148  1.00 26.08           C  
ANISOU 2047  CA  ILE A 965     3369   2958   3582     91    184     34       C  
ATOM   2048  C   ILE A 965      15.163 217.075  20.299  1.00 28.52           C  
ANISOU 2048  C   ILE A 965     3673   3180   3982     85    231     97       C  
ATOM   2049  O   ILE A 965      14.773 217.200  19.128  1.00 26.05           O  
ANISOU 2049  O   ILE A 965     3360   2865   3671    132    234    203       O  
ATOM   2050  CB  ILE A 965      13.585 216.379  22.127  1.00 27.08           C  
ANISOU 2050  CB  ILE A 965     3495   3042   3752    102    205    -31       C  
ATOM   2051  CG1 ILE A 965      13.012 215.197  22.898  1.00 25.74           C  
ANISOU 2051  CG1 ILE A 965     3328   2961   3490    105    167    -71       C  
ATOM   2052  CG2 ILE A 965      12.493 217.139  21.382  1.00 27.77           C  
ANISOU 2052  CG2 ILE A 965     3576   3062   3911    167    235     44       C  
ATOM   2053  CD1 ILE A 965      12.223 215.613  24.127  1.00 27.52           C  
ANISOU 2053  CD1 ILE A 965     3546   3175   3736     98    193   -159       C  
ATOM   2054  N   ILE A 966      15.989 217.943  20.882  1.00 27.59           N  
ANISOU 2054  N   ILE A 966     3548   3001   3934     18    269     34       N  
ATOM   2055  CA  ILE A 966      16.464 219.166  20.196  1.00 28.24           C  
ANISOU 2055  CA  ILE A 966     3632   2969   4125     -5    333     90       C  
ATOM   2056  C   ILE A 966      17.321 218.764  19.007  1.00 29.50           C  
ANISOU 2056  C   ILE A 966     3777   3195   4234     -3    319    191       C  
ATOM   2057  O   ILE A 966      17.091 219.212  17.873  1.00 30.05           O  
ANISOU 2057  O   ILE A 966     3853   3230   4334     37    346    314       O  
ATOM   2058  CB  ILE A 966      17.212 220.088  21.152  1.00 31.77           C  
ANISOU 2058  CB  ILE A 966     4074   3342   4653   -108    382    -27       C  
ATOM   2059  CG1 ILE A 966      16.204 220.679  22.149  1.00 32.17           C  
ANISOU 2059  CG1 ILE A 966     4149   3306   4768    -97    420   -125       C  
ATOM   2060  CG2 ILE A 966      17.915 221.221  20.402  1.00 35.99           C  
ANISOU 2060  CG2 ILE A 966     4613   3758   5302   -157    456     33       C  
ATOM   2061  CD1 ILE A 966      16.869 221.308  23.370  1.00 35.97           C  
ANISOU 2061  CD1 ILE A 966     4622   3761   5283   -218    456   -296       C  
ATOM   2062  N   GLU A 967      18.253 217.844  19.238  1.00 28.06           N  
ANISOU 2062  N   GLU A 967     3570   3127   3964    -34    279    152       N  
ATOM   2063  CA  GLU A 967      19.223 217.507  18.194  1.00 30.66           C  
ANISOU 2063  CA  GLU A 967     3877   3522   4249    -36    282    229       C  
ATOM   2064  C   GLU A 967      18.556 216.808  17.018  1.00 29.13           C  
ANISOU 2064  C   GLU A 967     3705   3381   3981     41    262    322       C  
ATOM   2065  O   GLU A 967      18.830 217.146  15.843  1.00 29.90           O  
ANISOU 2065  O   GLU A 967     3797   3488   4076     52    290    422       O  
ATOM   2066  CB  GLU A 967      20.397 216.691  18.781  1.00 36.17           C  
ANISOU 2066  CB  GLU A 967     4530   4334   4877    -71    253    168       C  
ATOM   2067  CG  GLU A 967      21.218 217.435  19.843  1.00 45.10           C  
ANISOU 2067  CG  GLU A 967     5616   5459   6058   -172    267     74       C  
ATOM   2068  CD  GLU A 967      21.762 218.799  19.360  1.00 53.56           C  
ANISOU 2068  CD  GLU A 967     6676   6430   7241   -254    337     98       C  
ATOM   2069  OE1 GLU A 967      21.560 219.834  20.050  1.00 58.76           O  
ANISOU 2069  OE1 GLU A 967     7348   6980   7994   -326    377     19       O  
ATOM   2070  OE2 GLU A 967      22.357 218.854  18.261  1.00 57.11           O1-
ANISOU 2070  OE2 GLU A 967     7109   6898   7689   -249    363    194       O1-
ATOM   2071  N   PHE A 968      17.649 215.853  17.297  1.00 27.70           N  
ANISOU 2071  N   PHE A 968     3546   3244   3733     86    218    289       N  
ATOM   2072  CA  PHE A 968      17.002 215.136  16.200  1.00 28.56           C  
ANISOU 2072  CA  PHE A 968     3670   3421   3759    135    198    350       C  
ATOM   2073  C   PHE A 968      15.971 216.034  15.501  1.00 28.60           C  
ANISOU 2073  C   PHE A 968     3671   3391   3803    172    210    443       C  
ATOM   2074  O   PHE A 968      15.756 215.897  14.278  1.00 28.14           O  
ANISOU 2074  O   PHE A 968     3605   3408   3679    200    206    530       O  
ATOM   2075  CB  PHE A 968      16.428 213.790  16.675  1.00 27.10           C  
ANISOU 2075  CB  PHE A 968     3509   3289   3497    151    158    282       C  
ATOM   2076  CG  PHE A 968      17.440 212.691  16.767  1.00 27.83           C  
ANISOU 2076  CG  PHE A 968     3608   3434   3531    150    158    244       C  
ATOM   2077  CD1 PHE A 968      17.960 212.129  15.612  1.00 31.33           C  
ANISOU 2077  CD1 PHE A 968     4057   3936   3910    166    176    277       C  
ATOM   2078  CD2 PHE A 968      17.882 212.193  17.987  1.00 27.57           C  
ANISOU 2078  CD2 PHE A 968     3571   3403   3501    143    147    183       C  
ATOM   2079  CE1 PHE A 968      18.918 211.117  15.674  1.00 29.81           C  
ANISOU 2079  CE1 PHE A 968     3868   3779   3677    185    193    246       C  
ATOM   2080  CE2 PHE A 968      18.818 211.190  18.051  1.00 26.19           C  
ANISOU 2080  CE2 PHE A 968     3393   3275   3281    167    155    174       C  
ATOM   2081  CZ  PHE A 968      19.319 210.624  16.905  1.00 27.50           C  
ANISOU 2081  CZ  PHE A 968     3569   3476   3401    193    182    203       C  
ATOM   2082  N   SER A 969      15.347 216.966  16.243  1.00 28.72           N  
ANISOU 2082  N   SER A 969     3685   3306   3919    180    231    431       N  
ATOM   2083  CA  SER A 969      14.445 217.937  15.632  1.00 30.87           C  
ANISOU 2083  CA  SER A 969     3946   3531   4253    237    257    541       C  
ATOM   2084  C   SER A 969      15.149 218.777  14.613  1.00 30.81           C  
ANISOU 2084  C   SER A 969     3931   3490   4283    237    306    665       C  
ATOM   2085  O   SER A 969      14.584 219.091  13.572  1.00 30.71           O  
ANISOU 2085  O   SER A 969     3900   3523   4246    296    309    801       O  
ATOM   2086  CB  SER A 969      13.805 218.907  16.668  1.00 31.98           C  
ANISOU 2086  CB  SER A 969     4093   3535   4523    253    299    497       C  
ATOM   2087  OG  SER A 969      12.993 218.078  17.448  1.00 40.66           O  
ANISOU 2087  OG  SER A 969     5189   4695   5566    261    253    408       O  
ATOM   2088  N   LYS A 970      16.349 219.227  14.959  1.00 31.47           N  
ANISOU 2088  N   LYS A 970     4023   3503   4431    167    348    625       N  
ATOM   2089  CA  LYS A 970      17.161 219.999  14.041  1.00 33.72           C  
ANISOU 2089  CA  LYS A 970     4300   3755   4756    146    405    739       C  
ATOM   2090  C   LYS A 970      17.522 219.216  12.785  1.00 31.34           C  
ANISOU 2090  C   LYS A 970     3979   3614   4313    164    378    818       C  
ATOM   2091  O   LYS A 970      17.416 219.752  11.670  1.00 31.13           O  
ANISOU 2091  O   LYS A 970     3942   3612   4275    198    407    971       O  
ATOM   2092  CB  LYS A 970      18.396 220.578  14.731  1.00 38.15           C  
ANISOU 2092  CB  LYS A 970     4859   4227   5409     43    454    660       C  
ATOM   2093  CG  LYS A 970      17.960 221.526  15.861  1.00 45.58           C  
ANISOU 2093  CG  LYS A 970     5824   4999   6492     17    500    575       C  
ATOM   2094  CD  LYS A 970      18.991 222.557  16.311  1.00 50.39           C  
ANISOU 2094  CD  LYS A 970     6435   5480   7227    -98    578    521       C  
ATOM   2095  CE  LYS A 970      20.119 221.968  17.144  1.00 51.35           C  
ANISOU 2095  CE  LYS A 970     6519   5703   7289   -203    540    375       C  
ATOM   2096  NZ  LYS A 970      20.694 223.045  18.010  1.00 51.49           N1+
ANISOU 2096  NZ  LYS A 970     6538   5590   7435   -329    610    261       N1+
ATOM   2097  N   MET A 971      17.878 217.962  12.949  1.00 27.93           N  
ANISOU 2097  N   MET A 971     3547   3292   3773    148    329    721       N  
ATOM   2098  CA  MET A 971      18.240 217.128  11.815  1.00 28.64           C  
ANISOU 2098  CA  MET A 971     3626   3527   3726    161    317    761       C  
ATOM   2099  C   MET A 971      17.029 216.845  10.938  1.00 31.09           C  
ANISOU 2099  C   MET A 971     3934   3936   3941    218    280    831       C  
ATOM   2100  O   MET A 971      17.151 216.808   9.692  1.00 32.36           O  
ANISOU 2100  O   MET A 971     4076   4210   4006    231    291    926       O  
ATOM   2101  CB  MET A 971      18.890 215.859  12.265  1.00 28.70           C  
ANISOU 2101  CB  MET A 971     3640   3599   3664    142    291    637       C  
ATOM   2102  CG  MET A 971      20.242 216.097  12.932  1.00 30.71           C  
ANISOU 2102  CG  MET A 971     3868   3817   3982     88    322    590       C  
ATOM   2103  SD  MET A 971      20.928 214.542  13.469  1.00 33.94           S  
ANISOU 2103  SD  MET A 971     4274   4310   4310    103    296    478       S  
ATOM   2104  CE  MET A 971      22.538 215.072  14.003  1.00 39.87           C  
ANISOU 2104  CE  MET A 971     4956   5068   5123     42    330    464       C  
ATOM   2105  N   ALA A 972      15.855 216.722  11.542  1.00 30.66           N  
ANISOU 2105  N   ALA A 972     3884   3859   3904    247    241    793       N  
ATOM   2106  CA  ALA A 972      14.634 216.477  10.751  1.00 33.41           C  
ANISOU 2106  CA  ALA A 972     4208   4330   4157    292    199    858       C  
ATOM   2107  C   ALA A 972      14.243 217.599   9.846  1.00 36.92           C  
ANISOU 2107  C   ALA A 972     4614   4791   4621    349    225   1046       C  
ATOM   2108  O   ALA A 972      13.423 217.389   8.955  1.00 38.89           O  
ANISOU 2108  O   ALA A 972     4823   5195   4756    384    187   1123       O  
ATOM   2109  CB  ALA A 972      13.457 216.129  11.644  1.00 34.79           C  
ANISOU 2109  CB  ALA A 972     4379   4486   4351    307    157    781       C  
ATOM   2110  N   ARG A 973      14.740 218.810  10.102  1.00 35.92           N  
ANISOU 2110  N   ARG A 973     4497   4509   4641    357    291   1123       N  
ATOM   2111  CA  ARG A 973      14.496 219.920   9.229  1.00 40.46           C  
ANISOU 2111  CA  ARG A 973     5044   5072   5254    419    336   1329       C  
ATOM   2112  C   ARG A 973      15.357 219.906   7.968  1.00 36.79           C  
ANISOU 2112  C   ARG A 973     4566   4724   4686    397    361   1437       C  
ATOM   2113  O   ARG A 973      15.043 220.632   7.033  1.00 34.75           O  
ANISOU 2113  O   ARG A 973     4276   4517   4410    456    386   1634       O  
ATOM   2114  CB  ARG A 973      14.623 221.247   9.996  1.00 47.26           C  
ANISOU 2114  CB  ARG A 973     5933   5690   6332    432    417   1366       C  
ATOM   2115  CG  ARG A 973      13.531 221.332  11.088  1.00 54.71           C  
ANISOU 2115  CG  ARG A 973     6878   6550   7358    476    400   1280       C  
ATOM   2116  CD  ARG A 973      13.301 222.726  11.660  1.00 62.30           C  
ANISOU 2116  CD  ARG A 973     7863   7278   8530    520    494   1335       C  
ATOM   2117  NE  ARG A 973      14.546 223.317  12.153  1.00 70.57           N  
ANISOU 2117  NE  ARG A 973     8958   8158   9696    420    568   1265       N  
ATOM   2118  CZ  ARG A 973      15.050 223.175  13.390  1.00 76.24           C  
ANISOU 2118  CZ  ARG A 973     9707   8788  10472    331    574   1066       C  
ATOM   2119  NH1 ARG A 973      16.219 223.772  13.676  1.00 74.58           N1+
ANISOU 2119  NH1 ARG A 973     9521   8458  10355    227    640   1018       N1+
ATOM   2120  NH2 ARG A 973      14.418 222.452  14.343  1.00 76.37           N  
ANISOU 2120  NH2 ARG A 973     9721   8851  10444    335    514    919       N  
ATOM   2121  N   ASP A 974      16.415 219.093   7.928  1.00 31.97           N  
ANISOU 2121  N   ASP A 974     3973   4167   4005    324    359   1324       N  
ATOM   2122  CA  ASP A 974      17.289 218.976   6.718  1.00 32.32           C  
ANISOU 2122  CA  ASP A 974     3999   4345   3935    301    391   1408       C  
ATOM   2123  C   ASP A 974      17.726 217.494   6.645  1.00 30.52           C  
ANISOU 2123  C   ASP A 974     3783   4245   3566    259    354   1237       C  
ATOM   2124  O   ASP A 974      18.912 217.152   6.809  1.00 28.98           O  
ANISOU 2124  O   ASP A 974     3596   4033   3380    212    389   1163       O  
ATOM   2125  CB  ASP A 974      18.499 219.951   6.776  1.00 33.82           C  
ANISOU 2125  CB  ASP A 974     4196   4401   4254    253    482   1478       C  
ATOM   2126  CG  ASP A 974      19.297 220.012   5.471  1.00 36.41           C  
ANISOU 2126  CG  ASP A 974     4495   4870   4469    237    528   1601       C  
ATOM   2127  OD1 ASP A 974      18.880 219.354   4.494  1.00 40.50           O  
ANISOU 2127  OD1 ASP A 974     4991   5595   4802    267    490   1633       O  
ATOM   2128  OD2 ASP A 974      20.363 220.701   5.398  1.00 37.74           O1-
ANISOU 2128  OD2 ASP A 974     4657   4958   4722    182    607   1659       O1-
ATOM   2129  N   PRO A 975      16.745 216.605   6.461  1.00 29.13           N  
ANISOU 2129  N   PRO A 975     3605   4190   3272    275    288   1170       N  
ATOM   2130  CA  PRO A 975      16.971 215.220   6.688  1.00 28.63           C  
ANISOU 2130  CA  PRO A 975     3571   4180   3125    237    264    989       C  
ATOM   2131  C   PRO A 975      18.064 214.596   5.823  1.00 28.50           C  
ANISOU 2131  C   PRO A 975     3558   4273   2996    210    309    957       C  
ATOM   2132  O   PRO A 975      18.801 213.770   6.341  1.00 29.39           O  
ANISOU 2132  O   PRO A 975     3698   4341   3124    191    327    826       O  
ATOM   2133  CB  PRO A 975      15.604 214.574   6.456  1.00 30.28           C  
ANISOU 2133  CB  PRO A 975     3770   4507   3228    244    197    948       C  
ATOM   2134  CG  PRO A 975      14.794 215.543   5.697  1.00 32.87           C  
ANISOU 2134  CG  PRO A 975     4040   4925   3524    294    180   1134       C  
ATOM   2135  CD  PRO A 975      15.349 216.898   6.044  1.00 33.33           C  
ANISOU 2135  CD  PRO A 975     4098   4813   3751    328    239   1269       C  
ATOM   2136  N   GLN A 976      18.196 215.010   4.562  1.00 28.47           N  
ANISOU 2136  N   GLN A 976     3519   4413   2883    216    334   1086       N  
ATOM   2137  CA  GLN A 976      19.152 214.417   3.669  1.00 31.21           C  
ANISOU 2137  CA  GLN A 976     3865   4888   3106    193    385   1051       C  
ATOM   2138  C   GLN A 976      20.575 214.951   3.923  1.00 33.83           C  
ANISOU 2138  C   GLN A 976     4183   5125   3544    179    458   1089       C  
ATOM   2139  O   GLN A 976      21.524 214.429   3.359  1.00 33.19           O  
ANISOU 2139  O   GLN A 976     4092   5132   3383    166    511   1047       O  
ATOM   2140  CB  GLN A 976      18.730 214.622   2.201  1.00 32.72           C  
ANISOU 2140  CB  GLN A 976     4015   5306   3110    198    383   1172       C  
ATOM   2141  CG  GLN A 976      17.369 213.983   1.895  1.00 33.87           C  
ANISOU 2141  CG  GLN A 976     4153   5592   3124    191    306   1112       C  
ATOM   2142  CD  GLN A 976      17.123 213.737   0.395  1.00 36.56           C  
ANISOU 2142  CD  GLN A 976     4452   6220   3219    171    303   1158       C  
ATOM   2143  NE2 GLN A 976      15.903 213.917  -0.018  1.00 38.28           N  
ANISOU 2143  NE2 GLN A 976     4618   6586   3338    181    232   1231       N  
ATOM   2144  OE1 GLN A 976      18.007 213.384  -0.364  1.00 38.69           O  
ANISOU 2144  OE1 GLN A 976     4726   6592   3382    148    364   1126       O  
ATOM   2145  N   ARG A 977      20.713 215.977   4.770  1.00 32.51           N  
ANISOU 2145  N   ARG A 977     4011   4786   3555    175    467   1157       N  
ATOM   2146  CA  ARG A 977      22.031 216.355   5.265  1.00 32.93           C  
ANISOU 2146  CA  ARG A 977     4046   4748   3719    137    526   1148       C  
ATOM   2147  C   ARG A 977      22.545 215.344   6.287  1.00 30.35           C  
ANISOU 2147  C   ARG A 977     3733   4372   3426    131    508    967       C  
ATOM   2148  O   ARG A 977      23.757 215.238   6.487  1.00 30.10           O  
ANISOU 2148  O   ARG A 977     3667   4343   3426    108    553    936       O  
ATOM   2149  CB  ARG A 977      22.030 217.741   5.893  1.00 34.43           C  
ANISOU 2149  CB  ARG A 977     4229   4763   4088    113    549   1248       C  
ATOM   2150  CG  ARG A 977      23.401 218.169   6.431  1.00 36.72           C  
ANISOU 2150  CG  ARG A 977     4487   4976   4489     43    609   1223       C  
ATOM   2151  CD  ARG A 977      23.328 219.532   7.110  1.00 38.34           C  
ANISOU 2151  CD  ARG A 977     4698   4986   4880     -1    642   1288       C  
ATOM   2152  NE  ARG A 977      24.643 219.987   7.549  1.00 38.92           N  
ANISOU 2152  NE  ARG A 977     4729   5009   5048    -95    700   1258       N  
ATOM   2153  CZ  ARG A 977      24.856 221.163   8.139  1.00 40.55           C  
ANISOU 2153  CZ  ARG A 977     4939   5045   5423   -170    750   1284       C  
ATOM   2154  NH1 ARG A 977      23.824 221.987   8.414  1.00 37.14           N1+
ANISOU 2154  NH1 ARG A 977     4559   4455   5097   -141    755   1340       N1+
ATOM   2155  NH2 ARG A 977      26.087 221.486   8.498  1.00 40.05           N  
ANISOU 2155  NH2 ARG A 977     4821   4969   5426   -275    798   1241       N  
ATOM   2156  N   TYR A 978      21.647 214.620   6.941  1.00 26.69           N  
ANISOU 2156  N   TYR A 978     3311   3873   2957    154    447    861       N  
ATOM   2157  CA  TYR A 978      22.037 213.765   8.066  1.00 26.86           C  
ANISOU 2157  CA  TYR A 978     3348   3828   3029    158    431    720       C  
ATOM   2158  C   TYR A 978      21.962 212.252   7.824  1.00 26.75           C  
ANISOU 2158  C   TYR A 978     3371   3884   2908    188    430    598       C  
ATOM   2159  O   TYR A 978      22.698 211.500   8.469  1.00 26.80           O  
ANISOU 2159  O   TYR A 978     3378   3860   2945    208    448    515       O  
ATOM   2160  CB  TYR A 978      21.234 214.184   9.312  1.00 26.52           C  
ANISOU 2160  CB  TYR A 978     3325   3651   3100    152    379    691       C  
ATOM   2161  CG  TYR A 978      21.580 215.583   9.692  1.00 26.23           C  
ANISOU 2161  CG  TYR A 978     3258   3514   3191    113    405    772       C  
ATOM   2162  CD1 TYR A 978      22.832 215.867  10.260  1.00 28.16           C  
ANISOU 2162  CD1 TYR A 978     3461   3729   3507     66    439    745       C  
ATOM   2163  CD2 TYR A 978      20.749 216.624   9.417  1.00 27.45           C  
ANISOU 2163  CD2 TYR A 978     3420   3612   3396    121    406    880       C  
ATOM   2164  CE1 TYR A 978      23.187 217.176  10.573  1.00 29.21           C  
ANISOU 2164  CE1 TYR A 978     3572   3762   3764      4    476    802       C  
ATOM   2165  CE2 TYR A 978      21.101 217.946   9.736  1.00 29.15           C  
ANISOU 2165  CE2 TYR A 978     3622   3701   3750     80    454    951       C  
ATOM   2166  CZ  TYR A 978      22.321 218.186  10.352  1.00 30.53           C  
ANISOU 2166  CZ  TYR A 978     3766   3834   3998     10    488    895       C  
ATOM   2167  OH  TYR A 978      22.717 219.463  10.667  1.00 30.74           O  
ANISOU 2167  OH  TYR A 978     3782   3731   4165    -56    545    941       O  
ATOM   2168  N   LEU A 979      21.124 211.838   6.862  1.00 27.46           N  
ANISOU 2168  N   LEU A 979     3486   4072   2873    189    418    592       N  
ATOM   2169  CA  LEU A 979      21.029 210.443   6.443  1.00 27.75           C  
ANISOU 2169  CA  LEU A 979     3568   4172   2804    197    437    462       C  
ATOM   2170  C   LEU A 979      21.028 210.386   4.943  1.00 28.62           C  
ANISOU 2170  C   LEU A 979     3666   4454   2753    182    471    490       C  
ATOM   2171  O   LEU A 979      20.301 211.136   4.296  1.00 29.40           O  
ANISOU 2171  O   LEU A 979     3739   4640   2791    165    436    595       O  
ATOM   2172  CB  LEU A 979      19.751 209.828   7.027  1.00 29.10           C  
ANISOU 2172  CB  LEU A 979     3787   4291   2977    183    378    378       C  
ATOM   2173  CG  LEU A 979      19.533 209.777   8.552  1.00 27.92           C  
ANISOU 2173  CG  LEU A 979     3655   3991   2962    194    342    343       C  
ATOM   2174  CD1 LEU A 979      18.151 209.220   8.876  1.00 29.43           C  
ANISOU 2174  CD1 LEU A 979     3884   4167   3130    168    292    276       C  
ATOM   2175  CD2 LEU A 979      20.584 208.917   9.207  1.00 27.91           C  
ANISOU 2175  CD2 LEU A 979     3670   3926   3008    231    388    271       C  
ATOM   2176  N   VAL A 980      21.873 209.532   4.375  1.00 28.93           N  
ANISOU 2176  N   VAL A 980     3717   4554   2719    196    544    406       N  
ATOM   2177  CA  VAL A 980      22.059 209.422   2.950  1.00 30.32           C  
ANISOU 2177  CA  VAL A 980     3879   4912   2727    179    592    414       C  
ATOM   2178  C   VAL A 980      21.494 208.047   2.517  1.00 32.53           C  
ANISOU 2178  C   VAL A 980     4226   5241   2891    155    611    229       C  
ATOM   2179  O   VAL A 980      22.160 207.003   2.678  1.00 30.35           O  
ANISOU 2179  O   VAL A 980     3992   4902   2634    186    685     99       O  
ATOM   2180  CB  VAL A 980      23.578 209.495   2.678  1.00 31.50           C  
ANISOU 2180  CB  VAL A 980     3985   5089   2891    212    684    441       C  
ATOM   2181  CG1 VAL A 980      23.840 209.468   1.197  1.00 34.34           C  
ANISOU 2181  CG1 VAL A 980     4324   5654   3069    194    744    459       C  
ATOM   2182  CG2 VAL A 980      24.146 210.752   3.331  1.00 31.24           C  
ANISOU 2182  CG2 VAL A 980     3892   4977   3001    211    669    589       C  
ATOM   2183  N   ILE A 981      20.260 208.059   2.035  1.00 31.31           N  
ANISOU 2183  N   ILE A 981     4077   5187   2629    100    549    219       N  
ATOM   2184  CA  ILE A 981      19.453 206.845   1.871  1.00 33.97           C  
ANISOU 2184  CA  ILE A 981     4477   5543   2884     44    548     33       C  
ATOM   2185  C   ILE A 981      19.009 206.718   0.411  1.00 39.18           C  
ANISOU 2185  C   ILE A 981     5117   6458   3312    -21    553     -1       C  
ATOM   2186  O   ILE A 981      18.469 207.645  -0.158  1.00 39.69           O  
ANISOU 2186  O   ILE A 981     5113   6680   3289    -34    492    144       O  
ATOM   2187  CB  ILE A 981      18.182 206.873   2.708  1.00 35.44           C  
ANISOU 2187  CB  ILE A 981     4675   5653   3137     12    456     27       C  
ATOM   2188  CG1 ILE A 981      18.478 207.040   4.178  1.00 32.94           C  
ANISOU 2188  CG1 ILE A 981     4373   5114   3025     67    442     61       C  
ATOM   2189  CG2 ILE A 981      17.370 205.566   2.526  1.00 38.26           C  
ANISOU 2189  CG2 ILE A 981     5097   6026   3414    -69    466   -176       C  
ATOM   2190  CD1 ILE A 981      17.220 207.141   5.009  1.00 33.71           C  
ANISOU 2190  CD1 ILE A 981     4473   5149   3183     39    359     63       C  
ATOM   2191  N   GLN A 982      19.220 205.544  -0.158  1.00 40.67           N  
ANISOU 2191  N   GLN A 982     5364   6686   3401    -60    632   -198       N  
ATOM   2192  CA  GLN A 982      18.818 205.227  -1.524  1.00 45.16           C  
ANISOU 2192  CA  GLN A 982     5920   7510   3727   -144    648   -284       C  
ATOM   2193  C   GLN A 982      17.328 205.382  -1.668  1.00 45.40           C  
ANISOU 2193  C   GLN A 982     5914   7673   3662   -230    535   -278       C  
ATOM   2194  O   GLN A 982      16.601 204.933  -0.815  1.00 46.35           O  
ANISOU 2194  O   GLN A 982     6071   7654   3884   -259    495   -352       O  
ATOM   2195  CB  GLN A 982      19.187 203.772  -1.831  1.00 50.49           C  
ANISOU 2195  CB  GLN A 982     6690   8136   4358   -181    765   -547       C  
ATOM   2196  CG  GLN A 982      18.915 203.332  -3.269  1.00 56.35           C  
ANISOU 2196  CG  GLN A 982     7427   9150   4834   -282    803   -685       C  
ATOM   2197  CD  GLN A 982      19.208 201.859  -3.432  1.00 59.86           C  
ANISOU 2197  CD  GLN A 982     7983   9489   5270   -323    934   -971       C  
ATOM   2198  NE2 GLN A 982      20.149 201.550  -4.274  1.00 62.28           N  
ANISOU 2198  NE2 GLN A 982     8302   9883   5478   -298   1054  -1051       N  
ATOM   2199  OE1 GLN A 982      18.604 201.010  -2.766  1.00 68.51           O  
ANISOU 2199  OE1 GLN A 982     9157  10410   6463   -373    939  -1114       O  
ATOM   2200  N   GLY A 983      16.892 206.073  -2.717  1.00 48.55           N  
ANISOU 2200  N   GLY A 983     6228   8351   3867   -262    484   -166       N  
ATOM   2201  CA  GLY A 983      15.476 206.229  -3.018  1.00 52.99           C  
ANISOU 2201  CA  GLY A 983     6727   9104   4302   -339    374   -147       C  
ATOM   2202  C   GLY A 983      14.697 207.079  -2.033  1.00 55.97           C  
ANISOU 2202  C   GLY A 983     7056   9368   4839   -285    274     24       C  
ATOM   2203  O   GLY A 983      13.480 206.930  -1.926  1.00 64.99           O  
ANISOU 2203  O   GLY A 983     8159  10600   5932   -348    192     -7       O  
ATOM   2204  N   ASP A 984      15.390 207.938  -1.277  1.00 53.69           N  
ANISOU 2204  N   ASP A 984     6769   8884   4744   -177    287    188       N  
ATOM   2205  CA  ASP A 984      14.760 208.813  -0.273  1.00 45.75           C  
ANISOU 2205  CA  ASP A 984     5728   7744   3910   -118    212    340       C  
ATOM   2206  C   ASP A 984      13.801 209.755  -0.982  1.00 45.48           C  
ANISOU 2206  C   ASP A 984     5582   7944   3751   -105    129    532       C  
ATOM   2207  O   ASP A 984      14.136 210.200  -2.101  1.00 43.19           O  
ANISOU 2207  O   ASP A 984     5243   7863   3303    -96    146    643       O  
ATOM   2208  CB  ASP A 984      15.834 209.674   0.389  1.00 42.47           C  
ANISOU 2208  CB  ASP A 984     5325   7125   3684    -23    257    479       C  
ATOM   2209  CG  ASP A 984      15.495 210.054   1.825  1.00 38.82           C  
ANISOU 2209  CG  ASP A 984     4879   6426   3443     18    219    511       C  
ATOM   2210  OD1 ASP A 984      14.388 209.742   2.276  1.00 37.19           O  
ANISOU 2210  OD1 ASP A 984     4666   6219   3244    -12    157    455       O  
ATOM   2211  OD2 ASP A 984      16.363 210.637   2.502  1.00 35.63           O1-
ANISOU 2211  OD2 ASP A 984     4489   5850   3197     73    255    582       O1-
ATOM   2212  N   MET A1007     -18.878 200.796  11.286  1.00 87.50           N  
ANISOU 2212  N   MET A1007     7691  16626   8928  -2820   -803   -781       N  
ATOM   2213  CA  MET A1007     -17.739 201.703  11.363  1.00 86.02           C  
ANISOU 2213  CA  MET A1007     7691  16150   8840  -2490   -792   -625       C  
ATOM   2214  C   MET A1007     -18.081 203.180  11.623  1.00 81.93           C  
ANISOU 2214  C   MET A1007     6995  15760   8374  -2119   -838   -340       C  
ATOM   2215  O   MET A1007     -17.186 203.958  11.952  1.00 78.77           O  
ANISOU 2215  O   MET A1007     6760  15068   8100  -1849   -802   -214       O  
ATOM   2216  CB  MET A1007     -16.884 201.590  10.100  1.00 88.50           C  
ANISOU 2216  CB  MET A1007     8113  16497   9014  -2526   -854   -690       C  
ATOM   2217  CG  MET A1007     -15.771 200.562  10.207  1.00 90.23           C  
ANISOU 2217  CG  MET A1007     8671  16301   9309  -2687   -751   -898       C  
ATOM   2218  SD  MET A1007     -14.217 201.160   9.508  1.00 97.74           S  
ANISOU 2218  SD  MET A1007     9848  17030  10259  -2456   -765   -822       S  
ATOM   2219  CE  MET A1007     -13.383 201.883  10.925  1.00 89.22           C  
ANISOU 2219  CE  MET A1007     8970  15475   9454  -2144   -665   -658       C  
ATOM   2220  N   ASP A1008     -19.354 203.563  11.466  1.00 83.81           N  
ANISOU 2220  N   ASP A1008     6895  16426   8520  -2106   -908   -242       N  
ATOM   2221  CA  ASP A1008     -19.843 204.916  11.834  1.00 82.70           C  
ANISOU 2221  CA  ASP A1008     6565  16400   8453  -1752   -925     26       C  
ATOM   2222  C   ASP A1008     -19.352 205.378  13.200  1.00 76.78           C  
ANISOU 2222  C   ASP A1008     6006  15216   7948  -1543   -797     87       C  
ATOM   2223  O   ASP A1008     -18.826 206.488  13.351  1.00 74.31           O  
ANISOU 2223  O   ASP A1008     5753  14742   7738  -1225   -781    263       O  
ATOM   2224  CB  ASP A1008     -21.385 204.956  11.882  1.00 84.31           C  
ANISOU 2224  CB  ASP A1008     6394  17069   8570  -1818   -975     79       C  
ATOM   2225  CG  ASP A1008     -22.011 205.459  10.595  1.00 88.61           C  
ANISOU 2225  CG  ASP A1008     6634  18139   8895  -1768  -1127    211       C  
ATOM   2226  OD1 ASP A1008     -21.267 205.812   9.660  1.00 87.73           O  
ANISOU 2226  OD1 ASP A1008     6604  18032   8695  -1675  -1191    271       O  
ATOM   2227  OD2 ASP A1008     -23.263 205.508  10.532  1.00 93.62           O1-
ANISOU 2227  OD2 ASP A1008     6932  19201   9437  -1817  -1181    265       O1-
ATOM   2228  N   ASP A1009     -19.565 204.509  14.186  1.00 73.25           N  
ANISOU 2228  N   ASP A1009     5646  14599   7587  -1738   -701    -60       N  
ATOM   2229  CA  ASP A1009     -19.335 204.817  15.583  1.00 69.22           C  
ANISOU 2229  CA  ASP A1009     5268  13756   7275  -1586   -579    -20       C  
ATOM   2230  C   ASP A1009     -17.971 204.381  16.056  1.00 63.13           C  
ANISOU 2230  C   ASP A1009     4863  12507   6613  -1605   -498   -117       C  
ATOM   2231  O   ASP A1009     -17.736 204.381  17.263  1.00 62.73           O  
ANISOU 2231  O   ASP A1009     4944  12185   6706  -1544   -393   -121       O  
ATOM   2232  CB  ASP A1009     -20.419 204.147  16.422  1.00 72.07           C  
ANISOU 2232  CB  ASP A1009     5487  14244   7653  -1779   -517    -98       C  
ATOM   2233  CG  ASP A1009     -21.794 204.594  16.014  1.00 77.46           C  
ANISOU 2233  CG  ASP A1009     5779  15422   8228  -1751   -593      5       C  
ATOM   2234  OD1 ASP A1009     -21.865 205.509  15.175  1.00 82.41           O  
ANISOU 2234  OD1 ASP A1009     6261  16265   8785  -1540   -687    163       O  
ATOM   2235  OD2 ASP A1009     -22.800 204.048  16.500  1.00 82.35           O1-
ANISOU 2235  OD2 ASP A1009     6227  16231   8830  -1932   -560    -55       O1-
ATOM   2236  N   VAL A1010     -17.064 204.026  15.138  1.00 58.70           N  
ANISOU 2236  N   VAL A1010     4462  11857   5982  -1680   -543   -190       N  
ATOM   2237  CA  VAL A1010     -15.680 203.697  15.549  1.00 57.69           C  
ANISOU 2237  CA  VAL A1010     4673  11283   5964  -1661   -467   -260       C  
ATOM   2238  C   VAL A1010     -14.950 204.954  16.038  1.00 55.31           C  
ANISOU 2238  C   VAL A1010     4462  10762   5791  -1319   -442    -95       C  
ATOM   2239  O   VAL A1010     -14.942 205.982  15.370  1.00 58.58           O  
ANISOU 2239  O   VAL A1010     4769  11315   6173  -1115   -508     52       O  
ATOM   2240  CB  VAL A1010     -14.836 203.042  14.435  1.00 57.05           C  
ANISOU 2240  CB  VAL A1010     4740  11154   5780  -1808   -509   -382       C  
ATOM   2241  CG1 VAL A1010     -13.386 202.897  14.871  1.00 56.39           C  
ANISOU 2241  CG1 VAL A1010     4975  10630   5819  -1727   -432   -413       C  
ATOM   2242  CG2 VAL A1010     -15.407 201.674  14.080  1.00 61.85           C  
ANISOU 2242  CG2 VAL A1010     5318  11893   6289  -2177   -501   -591       C  
ATOM   2243  N   VAL A1011     -14.323 204.866  17.198  1.00 49.83           N  
ANISOU 2243  N   VAL A1011     3964   9728   5240  -1266   -341   -119       N  
ATOM   2244  CA  VAL A1011     -13.595 205.990  17.732  1.00 48.44           C  
ANISOU 2244  CA  VAL A1011     3885   9333   5186   -980   -306      1       C  
ATOM   2245  C   VAL A1011     -12.238 205.443  18.143  1.00 44.93           C  
ANISOU 2245  C   VAL A1011     3741   8518   4813  -1020   -247    -86       C  
ATOM   2246  O   VAL A1011     -12.168 204.450  18.857  1.00 45.74           O  
ANISOU 2246  O   VAL A1011     3954   8480   4946  -1187   -178   -193       O  
ATOM   2247  CB  VAL A1011     -14.328 206.609  18.944  1.00 48.52           C  
ANISOU 2247  CB  VAL A1011     3789   9346   5297   -844   -234     71       C  
ATOM   2248  CG1 VAL A1011     -13.601 207.844  19.447  1.00 48.62           C  
ANISOU 2248  CG1 VAL A1011     3898   9138   5436   -557   -191    176       C  
ATOM   2249  CG2 VAL A1011     -15.762 206.963  18.591  1.00 52.96           C  
ANISOU 2249  CG2 VAL A1011     4034  10299   5789   -826   -283    150       C  
ATOM   2250  N   ASP A1012     -11.183 206.088  17.691  1.00 43.39           N  
ANISOU 2250  N   ASP A1012     3665   8175   4643   -866   -269    -28       N  
ATOM   2251  CA  ASP A1012      -9.850 205.820  18.176  1.00 41.43           C  
ANISOU 2251  CA  ASP A1012     3676   7588   4475   -848   -212    -79       C  
ATOM   2252  C   ASP A1012      -9.745 206.231  19.642  1.00 40.68           C  
ANISOU 2252  C   ASP A1012     3641   7307   4506   -734   -126    -52       C  
ATOM   2253  O   ASP A1012     -10.374 207.213  20.085  1.00 40.95           O  
ANISOU 2253  O   ASP A1012     3544   7425   4589   -573   -113     37       O  
ATOM   2254  CB  ASP A1012      -8.813 206.590  17.384  1.00 42.55           C  
ANISOU 2254  CB  ASP A1012     3900   7645   4620   -695   -252     -6       C  
ATOM   2255  CG  ASP A1012      -7.405 206.269  17.823  1.00 45.03           C  
ANISOU 2255  CG  ASP A1012     4462   7639   5006   -685   -199    -61       C  
ATOM   2256  OD1 ASP A1012      -6.882 205.206  17.404  1.00 49.12           O  
ANISOU 2256  OD1 ASP A1012     5098   8086   5476   -845   -193   -169       O  
ATOM   2257  OD2 ASP A1012      -6.798 207.052  18.612  1.00 45.42           O1-
ANISOU 2257  OD2 ASP A1012     4588   7505   5162   -522   -156     -4       O1-
ATOM   2258  N   ALA A1013      -8.968 205.473  20.401  1.00 38.24           N  
ANISOU 2258  N   ALA A1013     3525   6758   4245   -812    -61   -129       N  
ATOM   2259  CA  ALA A1013      -8.849 205.740  21.826  1.00 38.39           C  
ANISOU 2259  CA  ALA A1013     3602   6629   4354   -730     19   -115       C  
ATOM   2260  C   ALA A1013      -8.241 207.130  22.107  1.00 37.52           C  
ANISOU 2260  C   ALA A1013     3517   6414   4323   -486     25    -33       C  
ATOM   2261  O   ALA A1013      -8.552 207.706  23.106  1.00 38.35           O  
ANISOU 2261  O   ALA A1013     3587   6496   4486   -391     81    -12       O  
ATOM   2262  CB  ALA A1013      -8.059 204.639  22.528  1.00 36.49           C  
ANISOU 2262  CB  ALA A1013     3560   6166   4137   -850     82   -189       C  
ATOM   2263  N   ASP A1014      -7.468 207.702  21.194  1.00 38.93           N  
ANISOU 2263  N   ASP A1014     3742   6546   4502   -393    -24     11       N  
ATOM   2264  CA  ASP A1014      -7.031 209.105  21.385  1.00 40.78           C  
ANISOU 2264  CA  ASP A1014     3981   6687   4823   -173     -9     94       C  
ATOM   2265  C   ASP A1014      -8.196 210.136  21.343  1.00 41.72           C  
ANISOU 2265  C   ASP A1014     3895   6983   4971    -30     -6    188       C  
ATOM   2266  O   ASP A1014      -8.009 211.275  21.790  1.00 45.04           O  
ANISOU 2266  O   ASP A1014     4321   7301   5490    148     40    240       O  
ATOM   2267  CB  ASP A1014      -5.904 209.476  20.400  1.00 40.56           C  
ANISOU 2267  CB  ASP A1014     4051   6564   4793   -114    -53    132       C  
ATOM   2268  CG  ASP A1014      -4.568 208.786  20.742  1.00 40.41           C  
ANISOU 2268  CG  ASP A1014     4240   6325   4787   -184    -29     55       C  
ATOM   2269  OD1 ASP A1014      -4.394 208.437  21.913  1.00 42.15           O  
ANISOU 2269  OD1 ASP A1014     4533   6437   5045   -213     27      2       O  
ATOM   2270  OD2 ASP A1014      -3.725 208.536  19.848  1.00 38.95           O1-
ANISOU 2270  OD2 ASP A1014     4137   6096   4566   -212    -65     51       O1-
ATOM   2271  N   GLU A1015      -9.370 209.757  20.822  1.00 40.07           N  
ANISOU 2271  N   GLU A1015     3506   7036   4683   -107    -49    207       N  
ATOM   2272  CA  GLU A1015     -10.557 210.634  20.856  1.00 40.81           C  
ANISOU 2272  CA  GLU A1015     3380   7322   4801     33    -41    306       C  
ATOM   2273  C   GLU A1015     -11.628 210.141  21.851  1.00 41.05           C  
ANISOU 2273  C   GLU A1015     3301   7467   4826    -50     13    250       C  
ATOM   2274  O   GLU A1015     -12.759 210.624  21.855  1.00 44.12           O  
ANISOU 2274  O   GLU A1015     3480   8064   5216     32     19    319       O  
ATOM   2275  CB  GLU A1015     -11.143 210.812  19.452  1.00 44.03           C  
ANISOU 2275  CB  GLU A1015     3616   7998   5115     48   -137    406       C  
ATOM   2276  CG  GLU A1015     -10.320 211.776  18.567  1.00 45.33           C  
ANISOU 2276  CG  GLU A1015     3837   8077   5310    215   -169    522       C  
ATOM   2277  CD  GLU A1015      -9.049 211.148  18.024  1.00 45.41           C  
ANISOU 2277  CD  GLU A1015     4045   7934   5272     99   -202    449       C  
ATOM   2278  OE1 GLU A1015      -7.935 211.682  18.199  1.00 44.96           O  
ANISOU 2278  OE1 GLU A1015     4149   7634   5300    191   -167    461       O  
ATOM   2279  OE2 GLU A1015      -9.160 210.083  17.394  1.00 48.32           O1-
ANISOU 2279  OE2 GLU A1015     4407   8433   5518    -94   -259    371       O1-
ATOM   2280  N   TYR A1016     -11.261 209.172  22.690  1.00 40.45           N  
ANISOU 2280  N   TYR A1016     3363   7261   4743   -207     59    138       N  
ATOM   2281  CA  TYR A1016     -12.141 208.619  23.715  1.00 42.97           C  
ANISOU 2281  CA  TYR A1016     3607   7662   5055   -305    124     86       C  
ATOM   2282  C   TYR A1016     -11.549 208.982  25.093  1.00 44.56           C  
ANISOU 2282  C   TYR A1016     3946   7646   5337   -219    221     49       C  
ATOM   2283  O   TYR A1016     -10.676 208.272  25.647  1.00 40.49           O  
ANISOU 2283  O   TYR A1016     3616   6951   4817   -316    247    -15       O  
ATOM   2284  CB  TYR A1016     -12.308 207.098  23.607  1.00 43.48           C  
ANISOU 2284  CB  TYR A1016     3710   7770   5037   -580    112     -3       C  
ATOM   2285  CG  TYR A1016     -13.301 206.628  24.603  1.00 45.23           C  
ANISOU 2285  CG  TYR A1016     3832   8098   5254   -676    185    -32       C  
ATOM   2286  CD1 TYR A1016     -14.650 206.777  24.359  1.00 49.42           C  
ANISOU 2286  CD1 TYR A1016     4110   8922   5745   -694    169      2       C  
ATOM   2287  CD2 TYR A1016     -12.900 206.088  25.827  1.00 46.34           C  
ANISOU 2287  CD2 TYR A1016     4117   8066   5423   -737    272    -82       C  
ATOM   2288  CE1 TYR A1016     -15.601 206.384  25.294  1.00 50.98           C  
ANISOU 2288  CE1 TYR A1016     4198   9234   5937   -781    245    -19       C  
ATOM   2289  CE2 TYR A1016     -13.831 205.710  26.791  1.00 46.98           C  
ANISOU 2289  CE2 TYR A1016     4100   8256   5494   -819    350    -96       C  
ATOM   2290  CZ  TYR A1016     -15.170 205.856  26.520  1.00 50.83           C  
ANISOU 2290  CZ  TYR A1016     4338   9025   5947   -844    339    -70       C  
ATOM   2291  OH  TYR A1016     -16.102 205.465  27.440  1.00 53.71           O  
ANISOU 2291  OH  TYR A1016     4596   9512   6300   -934    421    -82       O  
ATOM   2292  N   LEU A1017     -12.015 210.096  25.650  1.00 44.95           N  
ANISOU 2292  N   LEU A1017     3902   7720   5457    -31    280     90       N  
ATOM   2293  CA  LEU A1017     -11.365 210.606  26.843  1.00 45.13           C  
ANISOU 2293  CA  LEU A1017     4055   7544   5546     58    368     40       C  
ATOM   2294  C   LEU A1017     -12.143 210.207  28.079  1.00 45.30           C  
ANISOU 2294  C   LEU A1017     4015   7651   5545     -5    456    -10       C  
ATOM   2295  O   LEU A1017     -13.342 210.313  28.135  1.00 44.23           O  
ANISOU 2295  O   LEU A1017     3687   7719   5399      9    480     18       O  
ATOM   2296  CB  LEU A1017     -11.116 212.102  26.728  1.00 45.80           C  
ANISOU 2296  CB  LEU A1017     4130   7535   5736    296    398     89       C  
ATOM   2297  CG  LEU A1017      -9.811 212.193  25.924  1.00 46.39           C  
ANISOU 2297  CG  LEU A1017     4367   7436   5823    300    332    104       C  
ATOM   2298  CD1 LEU A1017     -10.002 213.020  24.673  1.00 50.35           C  
ANISOU 2298  CD1 LEU A1017     4770   8002   6356    436    278    224       C  
ATOM   2299  CD2 LEU A1017      -8.587 212.608  26.739  1.00 45.24           C  
ANISOU 2299  CD2 LEU A1017     4412   7043   5732    342    384     33       C  
ATOM   2300  N   ILE A1018     -11.406 209.685  29.045  1.00 48.74           N  
ANISOU 2300  N   ILE A1018     4613   7943   5961    -84    501    -76       N  
ATOM   2301  CA  ILE A1018     -11.951 209.166  30.285  1.00 57.40           C  
ANISOU 2301  CA  ILE A1018     5686   9106   7017   -166    588   -118       C  
ATOM   2302  C   ILE A1018     -11.570 210.219  31.345  1.00 59.87           C  
ANISOU 2302  C   ILE A1018     6052   9318   7376     -7    675   -168       C  
ATOM   2303  O   ILE A1018     -10.365 210.539  31.487  1.00 52.57           O  
ANISOU 2303  O   ILE A1018     5292   8208   6475     36    663   -200       O  
ATOM   2304  CB  ILE A1018     -11.337 207.764  30.592  1.00 59.79           C  
ANISOU 2304  CB  ILE A1018     6140   9322   7254   -369    580   -141       C  
ATOM   2305  CG1 ILE A1018     -11.898 206.713  29.603  1.00 64.00           C  
ANISOU 2305  CG1 ILE A1018     6607   9961   7745   -550    520   -122       C  
ATOM   2306  CG2 ILE A1018     -11.611 207.335  32.033  1.00 60.85           C  
ANISOU 2306  CG2 ILE A1018     6290   9488   7342   -431    681   -167       C  
ATOM   2307  CD1 ILE A1018     -11.070 205.442  29.485  1.00 62.82           C  
ANISOU 2307  CD1 ILE A1018     6637   9664   7566   -720    505   -140       C  
ATOM   2308  N   PRO A1019     -12.573 210.766  32.069  1.00 48.37           N  
ATOM   2309  CA  PRO A1019     -12.279 211.753  33.141  1.00 55.44           C  
ATOM   2310  C   PRO A1019     -11.187 211.259  34.107  1.00 61.19           C  
ATOM   2311  O   PRO A1019     -11.017 210.030  34.270  1.00 52.68           O  
ATOM   2312  CB  PRO A1019     -13.625 211.918  33.880  1.00 56.92           C  
ATOM   2313  CG  PRO A1019     -14.669 211.449  32.910  1.00 57.14           C  
ATOM   2314  CD  PRO A1019     -14.011 210.411  32.022  1.00 54.14           C  
ATOM   2315  N   GLN A1020     -10.467 212.214  34.713  1.00 68.27           N  
ATOM   2316  CA  GLN A1020      -9.331 211.941  35.613  1.00 75.22           C  
ATOM   2317  C   GLN A1020      -9.464 212.641  36.960  1.00 73.95           C  
ATOM   2318  O   GLN A1020     -10.566 213.010  37.368  1.00 81.40           O  
ATOM   2319  CB  GLN A1020      -8.041 212.380  34.944  1.00 75.04           C  
ATOM   2320  CG  GLN A1020      -7.706 211.552  33.712  1.00 80.06           C  
ATOM   2321  CD  GLN A1020      -6.462 212.039  32.983  1.00 85.03           C  
ATOM   2322  NE2 GLN A1020      -6.082 211.496  31.944  1.00 90.54           N  
ATOM   2323  OE1 GLN A1020      -5.819 213.069  33.527  1.00 83.36           O  
TER   
END