CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 21051011392454930

Job options:

ID        	=	 21051011392454930
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


ATOM      1  N   ALA A   8      -0.385  32.320 -28.009  1.00102.34      A    N  
ANISOU    1  N   ALA A   8    11520  14122  13241    154    206   1923  A    N  
ATOM      2  CA  ALA A   8      -0.699  31.750 -29.311  1.00100.38      A    C  
ANISOU    2  CA  ALA A   8    11256  14000  12884    206    250   1935  A    C  
ATOM      3  C   ALA A   8      -1.382  30.388 -29.209  1.00100.18      A    C  
ANISOU    3  C   ALA A   8    11314  13979  12769    248    264   1794  A    C  
ATOM      4  O   ALA A   8      -2.478  30.212 -29.719  1.00 99.62      A    O  
ANISOU    4  O   ALA A   8    11287  13872  12688    246    256   1748  A    O  
ATOM      5  CB  ALA A   8       0.550  31.678 -30.185  1.00 94.99      A    C  
ANISOU    5  CB  ALA A   8    10486  13456  12148    240    287   2034  A    C  
ATOM      6  N   VAL A   9      -0.744  29.423 -28.553  1.00101.83      A    N  
ANISOU    6  N   VAL A   9    11544  14226  12919    280    277   1731  A    N  
ATOM      7  CA  VAL A   9      -1.394  28.143 -28.293  1.00 98.70      A    C  
ANISOU    7  CA  VAL A   9    11226  13823  12449    315    281   1598  A    C  
ATOM      8  C   VAL A   9      -1.734  27.967 -26.803  1.00102.25      A    C  
ANISOU    8  C   VAL A   9    11754  14140  12954    276    247   1502  A    C  
ATOM      9  O   VAL A   9      -2.551  27.141 -26.434  1.00 96.27      A    O  
ANISOU    9  O   VAL A   9    11063  13355  12160    289    243   1405  A    O  
ATOM     10  CB  VAL A   9      -0.589  26.963 -28.837  1.00 94.60      A    C  
ANISOU   10  CB  VAL A   9    10695  13414  11833    377    306   1567  A    C  
ATOM     11  CG1 VAL A   9      -1.474  25.751 -29.007  1.00 88.89      A    C  
ANISOU   11  CG1 VAL A   9    10044  12694  11035    418    303   1444  A    C  
ATOM     12  CG2 VAL A   9       0.037  27.336 -30.161  1.00 91.32      A    C  
ANISOU   12  CG2 VAL A   9    10195  13142  11360    420    340   1668  A    C  
ATOM     13  N   ALA A  10      -1.116  28.779 -25.966  1.00 90.17      A    N  
ANISOU   13  N   ALA A  10    10213  12531  11515    231    222   1532  A    N  
ATOM     14  CA  ALA A  10      -1.587  29.007 -24.630  1.00 75.68      A    C  
ANISOU   14  CA  ALA A  10     8441  10570   9745    192    186   1462  A    C  
ATOM     15  C   ALA A  10      -2.601  30.161 -24.660  1.00 96.00      A    C  
ANISOU   15  C   ALA A  10    11017  13074  12382    159    163   1487  A    C  
ATOM     16  O   ALA A  10      -2.456  31.141 -23.938  1.00102.16      A    O  
ANISOU   16  O   ALA A  10    11801  13762  13251    121    126   1495  A    O  
ATOM     17  CB  ALA A  10      -0.432  29.361 -23.736  1.00 69.59      A    C  
ANISOU   17  CB  ALA A  10     7655   9741   9043    163    161   1479  A    C  
ATOM     18  N   SER A  11      -3.615  30.052 -25.508  1.00 88.55      A    N  
ANISOU   18  N   SER A  11    10072  12174  11396    177    179   1495  A    N  
ATOM     19  CA  SER A  11      -4.574  31.131 -25.694  1.00 87.24      A    C  
ANISOU   19  CA  SER A  11     9899  11953  11293    150    157   1531  A    C  
ATOM     20  C   SER A  11      -5.557  31.284 -24.549  1.00 87.55      A    C  
ANISOU   20  C   SER A  11    10009  11893  11364    132    130   1441  A    C  
ATOM     21  O   SER A  11      -6.422  32.137 -24.603  1.00 80.40      A    O  
ANISOU   21  O   SER A  11     9103  10954  10490    119    114   1454  A    O  
ATOM     22  CB  SER A  11      -5.365  30.955 -26.990  1.00 89.96      A    C  
ANISOU   22  CB  SER A  11    10210  12385  11583    176    184   1584  A    C  
ATOM     23  OG  SER A  11      -5.028  29.769 -27.665  1.00 79.45      A    O  
ANISOU   23  OG  SER A  11     8914  11121  10151    219    213   1514  A    O  
ATOM     24  N   GLY A  12      -5.435  30.453 -23.526  1.00 83.25      A    N  
ANISOU   24  N   GLY A  12     9518  11307  10805    132    124   1353  A    N  
ATOM     25  CA  GLY A  12      -6.346  30.500 -22.404  1.00 77.82      A    C  
ANISOU   25  CA  GLY A  12     8893  10538  10134    119    102   1267  A    C  
ATOM     26  C   GLY A  12      -7.801  30.441 -22.818  1.00 81.82      A    C  
ANISOU   26  C   GLY A  12     9426  11059  10601    132    114   1233  A    C  
ATOM     27  O   GLY A  12      -8.178  29.593 -23.600  1.00 82.14      A    O  
ANISOU   27  O   GLY A  12     9472  11170  10565    161    143   1216  A    O  
ATOM     28  N   SER A  13      -8.611  31.351 -22.302  1.00 71.74      A    N  
ANISOU   28  N   SER A  13     8162   9716   9377    115     86   1222  A    N  
ATOM     29  CA  SER A  13     -10.046  31.319 -22.535  1.00 79.74      A    C  
ANISOU   29  CA  SER A  13     9200  10735  10360    125     95   1186  A    C  
ATOM     30  C   SER A  13     -10.492  31.854 -23.894  1.00 87.67      A    C  
ANISOU   30  C   SER A  13    10162  11796  11351    135    108   1255  A    C  
ATOM     31  O   SER A  13     -11.657  31.746 -24.256  1.00 83.71      A    O  
ANISOU   31  O   SER A  13     9678  11307  10819    146    116   1229  A    O  
ATOM     32  CB  SER A  13     -10.763  32.079 -21.431  1.00 77.31      A    C  
ANISOU   32  CB  SER A  13     8924  10341  10108    109     59   1138  A    C  
ATOM     33  OG  SER A  13     -10.965  31.253 -20.311  1.00 71.80      A    O  
ANISOU   33  OG  SER A  13     8275   9610   9394    109     57   1059  A    O  
ATOM     34  N   GLY A  14      -9.570  32.431 -24.642  1.00 80.58      A    N  
ANISOU   34  N   GLY A  14     9205  10935  10474    131    111   1348  A    N  
ATOM     35  CA  GLY A  14      -9.908  32.983 -25.927  1.00 78.98      A    C  
ANISOU   35  CA  GLY A  14     8955  10789  10264    140    122   1428  A    C  
ATOM     36  C   GLY A  14     -10.475  34.373 -25.799  1.00 77.98      A    C  
ANISOU   36  C   GLY A  14     8810  10597  10223    114     85   1471  A    C  
ATOM     37  O   GLY A  14     -10.610  34.915 -24.716  1.00 72.43      A    O  
ANISOU   37  O   GLY A  14     8132   9802   9585     94     47   1432  A    O  
ATOM     38  N   GLU A  15     -10.798  34.962 -26.930  1.00 84.14      A    N  
ANISOU   38  N   GLU A  15     9543  11425  10999    119     92   1551  A    N  
ATOM     39  CA  GLU A  15     -11.397  36.263 -26.923  1.00 90.32      A    C  
ANISOU   39  CA  GLU A  15    10313  12154  11852    101     57   1587  A    C  
ATOM     40  C   GLU A  15     -12.827  36.071 -26.487  1.00 80.86      A    C  
ANISOU   40  C   GLU A  15     9175  10910  10636    109     50   1484  A    C  
ATOM     41  O   GLU A  15     -13.509  35.203 -26.993  1.00 76.39      A    O  
ANISOU   41  O   GLU A  15     8637  10399   9988    135     84   1435  A    O  
ATOM     42  CB  GLU A  15     -11.313  36.870 -28.311  1.00 99.39      A    C  
ANISOU   42  CB  GLU A  15    11408  13382  12973    113     76   1681  A    C  
ATOM     43  CG  GLU A  15      -9.942  37.411 -28.634  1.00104.97      A    C  
ANISOU   43  CG  GLU A  15    12040  14132  13709    101     79   1805  A    C  
ATOM     44  CD  GLU A  15      -9.764  38.837 -28.169  1.00115.39      A    C  
ANISOU   44  CD  GLU A  15    13332  15351  15158     58     20   1858  A    C  
ATOM     45  OE1 GLU A  15     -10.273  39.745 -28.857  1.00117.38      A    O  
ANISOU   45  OE1 GLU A  15    13558  15570  15472     42    -11   1916  A    O  
ATOM     46  OE2 GLU A  15      -9.120  39.052 -27.117  1.00114.66      A    O1-
ANISOU   46  OE2 GLU A  15    13247  15208  15107     41      2   1837  A    O1-
ATOM     47  N   PRO A  16     -13.269  36.860 -25.529  1.00 71.04      A    N  
ANISOU   47  N   PRO A  16     7950   9570   9470     90      5   1452  A    N  
ATOM     48  CA  PRO A  16     -14.666  36.757 -25.036  1.00 77.11      A    C  
ANISOU   48  CA  PRO A  16     8767  10307  10221    101      1   1366  A    C  
ATOM     49  C   PRO A  16     -15.677  36.694 -26.198  1.00 78.77      A    C  
ANISOU   49  C   PRO A  16     8968  10578  10381    119     24   1385  A    C  
ATOM     50  O   PRO A  16     -15.555  37.427 -27.189  1.00 76.33      A    O  
ANISOU   50  O   PRO A  16     8612  10295  10094    115     19   1473  A    O  
ATOM     51  CB  PRO A  16     -14.867  38.048 -24.233  1.00 72.85      A    C  
ANISOU   51  CB  PRO A  16     8225   9670   9784     84    -59   1364  A    C  
ATOM     52  CG  PRO A  16     -13.481  38.550 -23.935  1.00 71.77      A    C  
ANISOU   52  CG  PRO A  16     8054   9498   9715     62    -89   1422  A    C  
ATOM     53  CD  PRO A  16     -12.576  38.051 -25.022  1.00 72.73      A    C  
ANISOU   53  CD  PRO A  16     8133   9707   9793     63    -47   1502  A    C  
ATOM     54  N   ARG A  17     -16.643  35.804 -26.117  1.00 81.68      A    N  
ANISOU   54  N   ARG A  17     9378  10972  10684    138     48   1309  A    N  
ATOM     55  CA  ARG A  17     -17.698  35.771 -27.138  1.00 87.88      A    C  
ANISOU   55  CA  ARG A  17    10158  11804  11426    156     64   1319  A    C  
ATOM     56  C   ARG A  17     -18.606  37.002 -26.993  1.00 78.51      A    C  
ANISOU   56  C   ARG A  17     8966  10559  10305    147     27   1326  A    C  
ATOM     57  O   ARG A  17     -18.748  37.574 -25.903  1.00 75.34      A    O  
ANISOU   57  O   ARG A  17     8582  10081   9964    135     -8   1288  A    O  
ATOM     58  CB  ARG A  17     -18.523  34.488 -27.032  1.00 88.46      A    C  
ANISOU   58  CB  ARG A  17    10277  11912  11422    177     93   1234  A    C  
ATOM     59  CG  ARG A  17     -17.691  33.222 -27.174  1.00 88.67      A    C  
ANISOU   59  CG  ARG A  17    10313  11992  11384    190    123   1218  A    C  
ATOM     60  CD  ARG A  17     -18.366  32.055 -26.477  1.00 94.09      A    C  
ANISOU   60  CD  ARG A  17    11051  12672  12028    196    133   1124  A    C  
ATOM     61  NE  ARG A  17     -18.592  32.249 -25.021  1.00 96.50      A    N  
ANISOU   61  NE  ARG A  17    11387  12902  12376    177    113   1070  A    N  
ATOM     62  CZ  ARG A  17     -17.865  31.717 -24.013  1.00100.21      A    C  
ANISOU   62  CZ  ARG A  17    11879  13346  12850    168    111   1035  A    C  
ATOM     63  NH1 ARG A  17     -16.817  30.921 -24.246  1.00 84.98      A    N1+
ANISOU   63  NH1 ARG A  17     9946  11452  10889    173    126   1046  A    N1+
ATOM     64  NH2 ARG A  17     -18.203  31.974 -22.739  1.00 95.81      A    N  
ANISOU   64  NH2 ARG A  17    11348  12729  12326    157     92    987  A    N  
ATOM     65  N   GLU A  18     -19.191  37.399 -28.113  1.00 71.27      A    N  
ANISOU   65  N   GLU A  18     8023   9681   9373    157     32   1376  A    N  
ATOM     66  CA  GLU A  18     -20.092  38.532 -28.182  1.00 70.09      A    C  
ANISOU   66  CA  GLU A  18     7865   9484   9281    152     -2   1389  A    C  
ATOM     67  C   GLU A  18     -21.512  38.033 -27.966  1.00 67.38      A    C  
ANISOU   67  C   GLU A  18     7561   9143   8895    169      8   1304  A    C  
ATOM     68  O   GLU A  18     -21.969  37.174 -28.676  1.00 61.77      A    O  
ANISOU   68  O   GLU A  18     6860   8498   8111    188     42   1290  A    O  
ATOM     69  CB  GLU A  18     -20.034  39.181 -29.585  1.00 75.05      A    C  
ANISOU   69  CB  GLU A  18     8442  10162   9913    154     -1   1492  A    C  
ATOM     70  CG  GLU A  18     -18.737  39.889 -29.961  1.00 74.11      A    C  
ANISOU   70  CG  GLU A  18     8267  10043   9845    133    -16   1601  A    C  
ATOM     71  CD  GLU A  18     -18.620  41.276 -29.365  1.00 73.92      A    C  
ANISOU   71  CD  GLU A  18     8224   9920   9941    106    -79   1635  A    C  
ATOM     72  OE1 GLU A  18     -19.462  41.689 -28.546  1.00 77.18      A    O  
ANISOU   72  OE1 GLU A  18     8669  10261  10393    106   -113   1564  A    O  
ATOM     73  OE2 GLU A  18     -17.653  41.955 -29.704  1.00 84.38      A    O1-
ANISOU   73  OE2 GLU A  18     9498  11238  11322     84   -100   1733  A    O1-
ATOM     74  N   GLU A  19     -22.240  38.616 -27.031  1.00 62.94      A    N  
ANISOU   74  N   GLU A  19     7018   8513   8380    166    -24   1250  A    N  
ATOM     75  CA  GLU A  19     -23.640  38.229 -26.842  1.00 57.86      A    C  
ANISOU   75  CA  GLU A  19     6406   7877   7700    183    -13   1178  A    C  
ATOM     76  C   GLU A  19     -24.476  38.628 -28.081  1.00 56.15      A    C  
ANISOU   76  C   GLU A  19     6167   7696   7469    194    -11   1220  A    C  
ATOM     77  O   GLU A  19     -24.214  39.640 -28.776  1.00 56.51      A    O  
ANISOU   77  O   GLU A  19     6176   7733   7562    187    -35   1298  A    O  
ATOM     78  CB  GLU A  19     -24.291  38.878 -25.596  1.00 55.98      A    C  
ANISOU   78  CB  GLU A  19     6189   7567   7514    184    -50   1114  A    C  
ATOM     79  CG  GLU A  19     -23.449  39.210 -24.384  1.00 68.03      A    C  
ANISOU   79  CG  GLU A  19     7724   9032   9091    175    -80   1091  A    C  
ATOM     80  CD  GLU A  19     -24.238  39.964 -23.297  1.00 86.40      A    C  
ANISOU   80  CD  GLU A  19    10066  11297  11463    189   -121   1025  A    C  
ATOM     81  OE1 GLU A  19     -25.498  39.755 -23.129  1.00 91.29      A    O  
ANISOU   81  OE1 GLU A  19    10702  11934  12050    206   -110    971  A    O  
ATOM     82  OE2 GLU A  19     -23.567  40.791 -22.613  1.00 84.37      A    O1-
ANISOU   82  OE2 GLU A  19     9802  10976  11276    184   -169   1028  A    O1-
ATOM     83  N   ALA A  20     -25.504  37.847 -28.318  1.00 50.99      A    N  
ANISOU   83  N   ALA A  20     5535   7079   6756    210     13   1170  A    N  
ATOM     84  CA  ALA A  20     -26.436  38.090 -29.371  1.00 57.49      A    C  
ANISOU   84  CA  ALA A  20     6345   7937   7560    225     14   1192  A    C  
ATOM     85  C   ALA A  20     -27.119  39.510 -29.230  1.00 57.88      A    C  
ANISOU   85  C   ALA A  20     6380   7927   7685    221    -29   1206  A    C  
ATOM     86  O   ALA A  20     -27.351  40.004 -28.095  1.00 49.30      A    O  
ANISOU   86  O   ALA A  20     5308   6776   6646    218    -58   1157  A    O  
ATOM     87  CB  ALA A  20     -27.477  36.979 -29.373  1.00 57.34      A    C  
ANISOU   87  CB  ALA A  20     6355   7952   7475    241     41   1120  A    C  
ATOM     88  N   GLY A  21     -27.466  40.100 -30.388  1.00 53.96      A    N  
ANISOU   88  N   GLY A  21     5854   7455   7192    228    -36   1268  A    N  
ATOM     89  CA  GLY A  21     -28.134  41.390 -30.460  1.00 49.49      A    C  
ANISOU   89  CA  GLY A  21     5270   6837   6693    227    -81   1289  A    C  
ATOM     90  C   GLY A  21     -27.228  42.552 -30.067  1.00 52.99      A    C  
ANISOU   90  C   GLY A  21     5689   7213   7230    206   -128   1344  A    C  
ATOM     91  O   GLY A  21     -27.709  43.570 -29.586  1.00 47.25      A    O  
ANISOU   91  O   GLY A  21     4959   6418   6573    207   -178   1329  A    O  
ATOM     92  N   ALA A  22     -25.913  42.363 -30.270  1.00 55.85      A    N  
ANISOU   92  N   ALA A  22     6030   7594   7592    191   -117   1404  A    N  
ATOM     93  CA  ALA A  22     -24.868  43.360 -30.110  1.00 54.42      A    C  
ANISOU   93  CA  ALA A  22     5816   7359   7499    166   -159   1478  A    C  
ATOM     94  C   ALA A  22     -24.840  43.928 -28.697  1.00 56.09      A    C  
ANISOU   94  C   ALA A  22     6049   7476   7784    161   -209   1413  A    C  
ATOM     95  O   ALA A  22     -24.627  45.126 -28.502  1.00 53.50      A    O  
ANISOU   95  O   ALA A  22     5697   7075   7552    149   -270   1451  A    O  
ATOM     96  CB  ALA A  22     -25.059  44.449 -31.144  1.00 51.88      A    C  
ANISOU   96  CB  ALA A  22     5451   7035   7226    161   -190   1575  A    C  
ATOM     97  N   LEU A  23     -25.030  43.053 -27.708  1.00 58.22      A    N  
ANISOU   97  N   LEU A  23     6361   7747   8010    172   -185   1318  A    N  
ATOM     98  CA  LEU A  23     -25.045  43.468 -26.312  1.00 58.34      A    C  
ANISOU   98  CA  LEU A  23     6398   7687   8079    176   -226   1246  A    C  
ATOM     99  C   LEU A  23     -23.639  43.477 -25.708  1.00 59.83      A    C  
ANISOU   99  C   LEU A  23     6581   7844   8307    157   -241   1269  A    C  
ATOM    100  O   LEU A  23     -23.486  43.603 -24.509  1.00 66.44      A    O  
ANISOU  100  O   LEU A  23     7441   8629   9174    163   -269   1205  A    O  
ATOM    101  CB  LEU A  23     -25.982  42.585 -25.511  1.00 61.13      A    C  
ANISOU  101  CB  LEU A  23     6796   8061   8367    198   -196   1140  A    C  
ATOM    102  CG  LEU A  23     -27.454  42.639 -25.941  1.00 64.66      A    C  
ANISOU  102  CG  LEU A  23     7248   8532   8786    218   -188   1108  A    C  
ATOM    103  CD1 LEU A  23     -28.257  41.556 -25.243  1.00 68.32      A    C  
ANISOU  103  CD1 LEU A  23     7748   9031   9177    233   -148   1019  A    C  
ATOM    104  CD2 LEU A  23     -28.077  43.988 -25.659  1.00 68.29      A    C  
ANISOU  104  CD2 LEU A  23     7697   8924   9325    229   -252   1097  A    C  
ATOM    105  N   GLY A  24     -22.611  43.416 -26.549  1.00 62.60      A    N  
ANISOU  105  N   GLY A  24     6897   8227   8659    137   -226   1363  A    N  
ATOM    106  CA  GLY A  24     -21.227  43.613 -26.104  1.00 58.31      A    C  
ANISOU  106  CA  GLY A  24     6336   7648   8168    114   -248   1402  A    C  
ATOM    107  C   GLY A  24     -20.571  42.318 -25.630  1.00 62.13      A    C  
ANISOU  107  C   GLY A  24     6847   8178   8580    117   -197   1359  A    C  
ATOM    108  O   GLY A  24     -21.223  41.269 -25.508  1.00 52.57      A    O  
ANISOU  108  O   GLY A  24     5672   7015   7285    133   -150   1293  A    O  
ATOM    109  N   PRO A  25     -19.270  42.378 -25.333  1.00 59.21      A    N  
ANISOU  109  N   PRO A  25     6460   7787   8248     97   -209   1399  A    N  
ATOM    110  CA  PRO A  25     -18.633  41.143 -24.878  1.00 57.97      A    C  
ANISOU  110  CA  PRO A  25     6330   7672   8025    100   -163   1358  A    C  
ATOM    111  C   PRO A  25     -19.238  40.641 -23.591  1.00 57.14      A    C  
ANISOU  111  C   PRO A  25     6277   7537   7895    117   -164   1240  A    C  
ATOM    112  O   PRO A  25     -19.522  41.414 -22.701  1.00 51.83      A    O  
ANISOU  112  O   PRO A  25     5616   6793   7283    122   -215   1198  A    O  
ATOM    113  CB  PRO A  25     -17.154  41.544 -24.691  1.00 55.66      A    C  
ANISOU  113  CB  PRO A  25     6003   7347   7796     76   -190   1422  A    C  
ATOM    114  CG  PRO A  25     -17.159  43.047 -24.655  1.00 58.71      A    C  
ANISOU  114  CG  PRO A  25     6356   7650   8298     61   -264   1472  A    C  
ATOM    115  CD  PRO A  25     -18.303  43.468 -25.545  1.00 57.65      A    C  
ANISOU  115  CD  PRO A  25     6212   7539   8150     71   -261   1493  A    C  
ATOM    116  N   ALA A  26     -19.456  39.348 -23.498  1.00 59.79      A    N  
ANISOU  116  N   ALA A  26     6645   7930   8142    127   -111   1190  A    N  
ATOM    117  CA  ALA A  26     -20.062  38.826 -22.308  1.00 69.76      A    C  
ANISOU  117  CA  ALA A  26     7953   9173   9377    142   -107   1091  A    C  
ATOM    118  C   ALA A  26     -19.232  39.167 -20.985  1.00 63.39      A    C  
ANISOU  118  C   ALA A  26     7158   8301   8626    139   -148   1056  A    C  
ATOM    119  O   ALA A  26     -19.768  39.415 -19.901  1.00 71.78      A    O  
ANISOU  119  O   ALA A  26     8247   9324   9702    156   -174    983  A    O  
ATOM    120  CB  ALA A  26     -20.284  37.337 -22.535  1.00 66.72      A    C  
ANISOU  120  CB  ALA A  26     7593   8861   8896    149    -48   1059  A    C  
ATOM    121  N   TRP A  27     -17.923  39.257 -21.115  1.00 56.09      A    N  
ANISOU  121  N   TRP A  27     6212   7366   7734    119   -157   1111  A    N  
ATOM    122  CA  TRP A  27     -17.045  39.619 -19.988  1.00 58.13      A    C  
ANISOU  122  CA  TRP A  27     6476   7559   8051    116   -199   1087  A    C  
ATOM    123  C   TRP A  27     -15.736  40.138 -20.592  1.00 56.91      A    C  
ANISOU  123  C   TRP A  27     6275   7391   7957     89   -219   1184  A    C  
ATOM    124  O   TRP A  27     -15.551  40.127 -21.825  1.00 55.88      A    O  
ANISOU  124  O   TRP A  27     6108   7310   7812     78   -194   1266  A    O  
ATOM    125  CB  TRP A  27     -16.761  38.367 -19.115  1.00 54.31      A    C  
ANISOU  125  CB  TRP A  27     6033   7102   7499    122   -163   1020  A    C  
ATOM    126  CG  TRP A  27     -16.433  37.189 -19.967  1.00 52.16      A    C  
ANISOU  126  CG  TRP A  27     5759   6908   7151    116   -102   1050  A    C  
ATOM    127  CD1 TRP A  27     -17.326  36.348 -20.565  1.00 56.54      A    C  
ANISOU  127  CD1 TRP A  27     6328   7524   7629    125    -56   1032  A    C  
ATOM    128  CD2 TRP A  27     -15.159  36.773 -20.413  1.00 49.37      A    C  
ANISOU  128  CD2 TRP A  27     5383   6580   6792    101    -86   1105  A    C  
ATOM    129  CE2 TRP A  27     -15.345  35.646 -21.259  1.00 51.08      A    C  
ANISOU  129  CE2 TRP A  27     5605   6877   6923    108    -30   1111  A    C  
ATOM    130  CE3 TRP A  27     -13.872  37.202 -20.155  1.00 52.16      A    C  
ANISOU  130  CE3 TRP A  27     5712   6898   7205     84   -114   1147  A    C  
ATOM    131  NE1 TRP A  27     -16.674  35.405 -21.345  1.00 53.47      A    N  
ANISOU  131  NE1 TRP A  27     5932   7198   7187    122    -16   1066  A    N  
ATOM    132  CZ2 TRP A  27     -14.308  34.971 -21.839  1.00 54.36      A    C  
ANISOU  132  CZ2 TRP A  27     6003   7343   7308    105     -2   1153  A    C  
ATOM    133  CZ3 TRP A  27     -12.834  36.499 -20.718  1.00 52.97      A    C  
ANISOU  133  CZ3 TRP A  27     5797   7053   7276     76    -80   1193  A    C  
ATOM    134  CH2 TRP A  27     -13.062  35.402 -21.548  1.00 54.22      A    C  
ANISOU  134  CH2 TRP A  27     5960   7294   7344     89    -25   1194  A    C  
ATOM    135  N   ASP A  28     -14.808  40.564 -19.756  1.00 54.87      A    N  
ANISOU  135  N   ASP A  28     6012   7070   7764     81   -265   1180  A    N  
ATOM    136  CA  ASP A  28     -13.488  40.850 -20.300  1.00 59.33      A    C  
ANISOU  136  CA  ASP A  28     6531   7633   8380     53   -276   1275  A    C  
ATOM    137  C   ASP A  28     -12.362  40.416 -19.388  1.00 62.90      A    C  
ANISOU  137  C   ASP A  28     6995   8061   8843     49   -284   1249  A    C  
ATOM    138  O   ASP A  28     -12.567  40.112 -18.195  1.00 49.42      A    O  
ANISOU  138  O   ASP A  28     5333   6323   7122     66   -296   1155  A    O  
ATOM    139  CB  ASP A  28     -13.313  42.341 -20.651  1.00 66.30      A    C  
ANISOU  139  CB  ASP A  28     7364   8447   9377     36   -346   1349  A    C  
ATOM    140  CG  ASP A  28     -13.005  43.170 -19.453  1.00 66.07      A    C  
ANISOU  140  CG  ASP A  28     7345   8314   9442     40   -426   1303  A    C  
ATOM    141  OD1 ASP A  28     -13.964  43.534 -18.781  1.00 84.43      A    O  
ANISOU  141  OD1 ASP A  28     9702  10600  11774     67   -457   1223  A    O  
ATOM    142  OD2 ASP A  28     -11.834  43.417 -19.138  1.00 64.70      A    O1-
ANISOU  142  OD2 ASP A  28     7149   8101   9331     21   -459   1339  A    O1-
ATOM    143  N   GLU A  29     -11.158  40.499 -19.963  1.00 61.64      A    N  
ANISOU  143  N   GLU A  29     6790   7916   8715     24   -282   1337  A    N  
ATOM    144  CA  GLU A  29     -10.026  39.855 -19.412  1.00 63.98      A    C  
ANISOU  144  CA  GLU A  29     7091   8215   9003     17   -272   1328  A    C  
ATOM    145  C   GLU A  29      -9.741  40.404 -18.036  1.00 59.92      A    C  
ANISOU  145  C   GLU A  29     6600   7605   8560     21   -340   1264  A    C  
ATOM    146  O   GLU A  29      -9.373  39.660 -17.165  1.00 54.63      A    O  
ANISOU  146  O   GLU A  29     5966   6935   7855     32   -328   1201  A    O  
ATOM    147  CB  GLU A  29      -8.840  39.966 -20.319  1.00 74.69      A    C  
ANISOU  147  CB  GLU A  29     8386   9606  10384     -7   -262   1441  A    C  
ATOM    148  CG  GLU A  29      -8.016  38.696 -20.238  1.00 89.38      A    C  
ANISOU  148  CG  GLU A  29    10260  11529  12171     -2   -209   1425  A    C  
ATOM    149  CD  GLU A  29      -6.547  38.971 -20.367  1.00101.66      A    C  
ANISOU  149  CD  GLU A  29    11762  13077  13785    -26   -227   1506  A    C  
ATOM    150  OE1 GLU A  29      -6.218  40.076 -20.845  1.00114.51      A    O  
ANISOU  150  OE1 GLU A  29    13334  14672  15501    -49   -269   1598  A    O  
ATOM    151  OE2 GLU A  29      -5.743  38.097 -19.970  1.00108.71      A    O1-
ANISOU  151  OE2 GLU A  29    12669  13994  14639    -22   -203   1480  A    O1-
ATOM    152  N   SER A  30     -10.017  41.670 -17.791  1.00 54.86      A    N  
ANISOU  152  N   SER A  30     5943   6884   8015     20   -412   1273  A    N  
ATOM    153  CA  SER A  30      -9.812  42.230 -16.435  1.00 55.90      A    C  
ANISOU  153  CA  SER A  30     6098   6923   8215     34   -486   1199  A    C  
ATOM    154  C   SER A  30     -10.591  41.554 -15.299  1.00 52.18      A    C  
ANISOU  154  C   SER A  30     5694   6461   7671     73   -469   1072  A    C  
ATOM    155  O   SER A  30     -10.265  41.732 -14.148  1.00 49.29      A    O  
ANISOU  155  O   SER A  30     5350   6040   7336     90   -515   1007  A    O  
ATOM    156  CB  SER A  30     -10.131  43.730 -16.415  1.00 51.37      A    C  
ANISOU  156  CB  SER A  30     5497   6260   7759     33   -575   1221  A    C  
ATOM    157  OG  SER A  30     -11.525  43.925 -16.463  1.00 52.22      A    O  
ANISOU  157  OG  SER A  30     5631   6378   7832     60   -570   1168  A    O  
ATOM    158  N   GLN A  31     -11.636  40.818 -15.636  1.00 49.61      A    N  
ANISOU  158  N   GLN A  31     5394   6204   7250     87   -407   1040  A    N  
ATOM    159  CA  GLN A  31     -12.432  40.081 -14.642  1.00 54.69      A    C  
ANISOU  159  CA  GLN A  31     6094   6870   7816    119   -382    933  A    C  
ATOM    160  C   GLN A  31     -11.853  38.710 -14.152  1.00 50.43      A    C  
ANISOU  160  C   GLN A  31     5585   6377   7197    118   -329    901  A    C  
ATOM    161  O   GLN A  31     -12.481  38.039 -13.337  1.00 48.18      A    O  
ANISOU  161  O   GLN A  31     5342   6114   6847    142   -307    823  A    O  
ATOM    162  CB  GLN A  31     -13.838  39.859 -15.229  1.00 49.98      A    C  
ANISOU  162  CB  GLN A  31     5509   6324   7157    132   -341    918  A    C  
ATOM    163  CG  GLN A  31     -14.522  41.146 -15.610  1.00 55.74      A    C  
ANISOU  163  CG  GLN A  31     6213   7006   7956    137   -394    938  A    C  
ATOM    164  CD  GLN A  31     -15.880  40.892 -16.166  1.00 53.57      A    C  
ANISOU  164  CD  GLN A  31     5949   6784   7620    150   -353    922  A    C  
ATOM    165  NE2 GLN A  31     -16.832  40.736 -15.275  1.00 47.79      A    N  
ANISOU  165  NE2 GLN A  31     5253   6056   6849    183   -353    832  A    N  
ATOM    166  OE1 GLN A  31     -16.067  40.773 -17.380  1.00 53.26      A    O  
ANISOU  166  OE1 GLN A  31     5886   6789   7562    132   -317    989  A    O  
ATOM    167  N   LEU A  32     -10.684  38.326 -14.674  1.00 50.08      A    N  
ANISOU  167  N   LEU A  32     5515   6351   7160     92   -310    964  A    N  
ATOM    168  CA  LEU A  32     -10.069  37.022 -14.462  1.00 49.84      A    C  
ANISOU  168  CA  LEU A  32     5507   6370   7057     88   -261    948  A    C  
ATOM    169  C   LEU A  32      -8.906  37.202 -13.521  1.00 51.37      A    C  
ANISOU  169  C   LEU A  32     5703   6509   7305     86   -304    933  A    C  
ATOM    170  O   LEU A  32      -8.106  38.067 -13.746  1.00 56.92      A    O  
ANISOU  170  O   LEU A  32     6367   7165   8095     68   -351    989  A    O  
ATOM    171  CB  LEU A  32      -9.533  36.516 -15.786  1.00 48.07      A    C  
ANISOU  171  CB  LEU A  32     5248   6211   6805     67   -213   1030  A    C  
ATOM    172  CG  LEU A  32     -10.562  36.302 -16.888  1.00 54.63      A    C  
ANISOU  172  CG  LEU A  32     6072   7101   7582     71   -170   1054  A    C  
ATOM    173  CD1 LEU A  32     -10.004  35.594 -18.110  1.00 58.77      A    C  
ANISOU  173  CD1 LEU A  32     6568   7703   8058     61   -118   1121  A    C  
ATOM    174  CD2 LEU A  32     -11.763  35.524 -16.388  1.00 57.85      A    C  
ANISOU  174  CD2 LEU A  32     6529   7535   7913     93   -139    971  A    C  
ATOM    175  N   ARG A  33      -8.809  36.410 -12.464  1.00 51.65      A    N  
ANISOU  175  N   ARG A  33     5782   6549   7292    102   -294    859  A    N  
ATOM    176  CA  ARG A  33      -7.628  36.453 -11.621  1.00 49.05      A    C  
ANISOU  176  CA  ARG A  33     5454   6174   7006    100   -331    846  A    C  
ATOM    177  C   ARG A  33      -6.354  36.034 -12.396  1.00 47.66      A    C  
ANISOU  177  C   ARG A  33     5243   6025   6840     71   -308    924  A    C  
ATOM    178  O   ARG A  33      -6.392  35.473 -13.506  1.00 45.76      A    O  
ANISOU  178  O   ARG A  33     4983   5851   6553     58   -253    976  A    O  
ATOM    179  CB  ARG A  33      -7.845  35.648 -10.382  1.00 46.87      A    C  
ANISOU  179  CB  ARG A  33     5232   5908   6668    126   -320    757  A    C  
ATOM    180  CG  ARG A  33      -8.945  36.233  -9.569  1.00 48.96      A    C  
ANISOU  180  CG  ARG A  33     5521   6147   6932    160   -352    686  A    C  
ATOM    181  CD  ARG A  33      -9.377  35.267  -8.504  1.00 49.49      A    C  
ANISOU  181  CD  ARG A  33     5636   6249   6916    185   -324    610  A    C  
ATOM    182  NE  ARG A  33     -10.449  35.801  -7.693  1.00 48.22      A    N  
ANISOU  182  NE  ARG A  33     5496   6078   6746    224   -351    541  A    N  
ATOM    183  CZ  ARG A  33     -10.311  36.642  -6.659  1.00 50.49      A    C  
ANISOU  183  CZ  ARG A  33     5791   6310   7080    258   -419    487  A    C  
ATOM    184  NH1 ARG A  33      -9.141  37.066  -6.287  1.00 48.35      A    N1+
ANISOU  184  NH1 ARG A  33     5511   5982   6878    253   -471    493  A    N1+
ATOM    185  NH2 ARG A  33     -11.378  37.048  -5.959  1.00 47.03      A    N  
ANISOU  185  NH2 ARG A  33     5370   5879   6619    301   -437    422  A    N  
ATOM    186  N   SER A  34      -5.195  36.387 -11.881  1.00 50.12      A    N  
ANISOU  186  N   SER A  34     5539   6286   7217     61   -352    936  A    N  
ATOM    187  CA  SER A  34      -3.971  36.016 -12.636  1.00 50.07      A    C  
ANISOU  187  CA  SER A  34     5492   6312   7221     36   -328   1015  A    C  
ATOM    188  C   SER A  34      -3.114  35.046 -11.837  1.00 46.55      A    C  
ANISOU  188  C   SER A  34     5074   5872   6737     41   -316    972  A    C  
ATOM    189  O   SER A  34      -2.972  35.137 -10.625  1.00 45.40      A    O  
ANISOU  189  O   SER A  34     4961   5676   6611     56   -356    905  A    O  
ATOM    190  CB  SER A  34      -3.167  37.225 -13.067  1.00 62.38      A    C  
ANISOU  190  CB  SER A  34     6988   7817   8894     11   -385   1101  A    C  
ATOM    191  OG  SER A  34      -2.803  37.904 -11.907  1.00 66.37      A    O  
ANISOU  191  OG  SER A  34     7507   8234   9475     19   -460   1053  A    O  
ATOM    192  N   TYR A  35      -2.608  34.069 -12.554  1.00 44.65      A    N  
ANISOU  192  N   TYR A  35     4822   5702   6438     33   -260   1007  A    N  
ATOM    193  CA  TYR A  35      -2.006  32.905 -11.965  1.00 48.61      A    C  
ANISOU  193  CA  TYR A  35     5357   6228   6885     40   -236    962  A    C  
ATOM    194  C   TYR A  35      -0.674  32.741 -12.639  1.00 49.21      A    C  
ANISOU  194  C   TYR A  35     5384   6330   6982     23   -225   1036  A    C  
ATOM    195  O   TYR A  35      -0.389  33.440 -13.576  1.00 47.38      A    O  
ANISOU  195  O   TYR A  35     5096   6109   6796      7   -230   1120  A    O  
ATOM    196  CB  TYR A  35      -2.922  31.656 -12.124  1.00 42.22      A    C  
ANISOU  196  CB  TYR A  35     4591   5484   5965     56   -176    914  A    C  
ATOM    197  CG  TYR A  35      -4.169  31.820 -11.277  1.00 38.99      A    C  
ANISOU  197  CG  TYR A  35     4227   5049   5536     74   -189    842  A    C  
ATOM    198  CD1 TYR A  35      -4.063  32.002  -9.940  1.00 37.98      A    C  
ANISOU  198  CD1 TYR A  35     4131   4869   5429     87   -228    780  A    C  
ATOM    199  CD2 TYR A  35      -5.463  31.882 -11.851  1.00 41.52      A    C  
ANISOU  199  CD2 TYR A  35     4553   5400   5821     80   -163    838  A    C  
ATOM    200  CE1 TYR A  35      -5.195  32.200  -9.137  1.00 40.58      A    C  
ANISOU  200  CE1 TYR A  35     4497   5186   5736    111   -240    715  A    C  
ATOM    201  CE2 TYR A  35      -6.629  32.105 -11.051  1.00 43.76      A    C  
ANISOU  201  CE2 TYR A  35     4873   5665   6089     99   -175    775  A    C  
ATOM    202  CZ  TYR A  35      -6.469  32.260  -9.698  1.00 41.22      A    C  
ANISOU  202  CZ  TYR A  35     4580   5299   5782    116   -213    713  A    C  
ATOM    203  OH  TYR A  35      -7.501  32.454  -8.842  1.00 44.47      A    O  
ANISOU  203  OH  TYR A  35     5022   5700   6172    141   -224    650  A    O  
ATOM    204  N   SER A  36       0.100  31.782 -12.156  1.00 47.76      A    N  
ANISOU  204  N   SER A  36     5221   6161   6763     28   -211   1005  A    N  
ATOM    205  CA  SER A  36       1.501  31.622 -12.474  1.00 47.96      A    C  
ANISOU  205  CA  SER A  36     5203   6203   6814     16   -212   1060  A    C  
ATOM    206  C   SER A  36       1.699  30.637 -13.579  1.00 47.83      A    C  
ANISOU  206  C   SER A  36     5169   6283   6721     23   -149   1095  A    C  
ATOM    207  O   SER A  36       2.799  30.438 -14.004  1.00 56.19      A    O  
ANISOU  207  O   SER A  36     6188   7374   7789     18   -140   1144  A    O  
ATOM    208  CB  SER A  36       2.216  31.116 -11.212  1.00 51.27      A    C  
ANISOU  208  CB  SER A  36     5661   6581   7239     23   -236    997  A    C  
ATOM    209  OG  SER A  36       1.857  29.785 -10.877  1.00 46.48      A    O  
ANISOU  209  OG  SER A  36     5107   6015   6536     41   -196    930  A    O  
ATOM    210  N   PHE A  37       0.660  29.995 -14.077  1.00 43.11      A    N  
ANISOU  210  N   PHE A  37     4598   5736   6044     38   -107   1067  A    N  
ATOM    211  CA  PHE A  37       0.859  28.858 -14.977  1.00 41.36      A    C  
ANISOU  211  CA  PHE A  37     4370   5603   5740     55    -55   1076  A    C  
ATOM    212  C   PHE A  37       0.193  29.211 -16.246  1.00 41.68      A    C  
ANISOU  212  C   PHE A  37     4377   5699   5760     58    -28   1131  A    C  
ATOM    213  O   PHE A  37      -0.602  30.088 -16.253  1.00 42.72      A    O  
ANISOU  213  O   PHE A  37     4506   5796   5927     49    -45   1142  A    O  
ATOM    214  CB  PHE A  37       0.281  27.562 -14.428  1.00 41.34      A    C  
ANISOU  214  CB  PHE A  37     4434   5615   5658     73    -35    990  A    C  
ATOM    215  CG  PHE A  37      -1.167  27.718 -13.925  1.00 39.14      A    C  
ANISOU  215  CG  PHE A  37     4200   5305   5364     75    -39    936  A    C  
ATOM    216  CD1 PHE A  37      -2.209  27.740 -14.807  1.00 39.33      A    C  
ANISOU  216  CD1 PHE A  37     4219   5368   5353     81    -13    949  A    C  
ATOM    217  CD2 PHE A  37      -1.437  27.931 -12.572  1.00 39.28      A    C  
ANISOU  217  CD2 PHE A  37     4261   5257   5408     72    -72    878  A    C  
ATOM    218  CE1 PHE A  37      -3.527  27.916 -14.376  1.00 37.73      A    C  
ANISOU  218  CE1 PHE A  37     4053   5142   5139     83    -17    905  A    C  
ATOM    219  CE2 PHE A  37      -2.750  28.133 -12.133  1.00 38.94      A    C  
ANISOU  219  CE2 PHE A  37     4250   5194   5348     77    -75    835  A    C  
ATOM    220  CZ  PHE A  37      -3.775  28.161 -13.043  1.00 36.92      A    C  
ANISOU  220  CZ  PHE A  37     3987   4978   5061     81    -47    850  A    C  
ATOM    221  N   PRO A  38       0.559  28.570 -17.346  1.00 43.34      A    N  
ANISOU  221  N   PRO A  38     4555   5997   5911     76     11   1169  A    N  
ATOM    222  CA  PRO A  38      -0.148  28.823 -18.587  1.00 48.64      A    C  
ANISOU  222  CA  PRO A  38     5198   6730   6551     85     38   1217  A    C  
ATOM    223  C   PRO A  38      -1.324  27.894 -18.797  1.00 49.51      A    C  
ANISOU  223  C   PRO A  38     5359   6872   6581    108     65   1149  A    C  
ATOM    224  O   PRO A  38      -1.397  26.863 -18.146  1.00 46.11      A    O  
ANISOU  224  O   PRO A  38     4978   6432   6109    118     68   1076  A    O  
ATOM    225  CB  PRO A  38       0.890  28.464 -19.633  1.00 50.69      A    C  
ANISOU  225  CB  PRO A  38     5400   7081   6779    103     68   1283  A    C  
ATOM    226  CG  PRO A  38       1.650  27.335 -18.989  1.00 51.05      A    C  
ANISOU  226  CG  PRO A  38     5476   7128   6789    117     70   1223  A    C  
ATOM    227  CD  PRO A  38       1.764  27.778 -17.555  1.00 48.12      A    C  
ANISOU  227  CD  PRO A  38     5141   6653   6489     90     27   1181  A    C  
ATOM    228  N   THR A  39      -2.170  28.229 -19.772  1.00 42.63      A    N  
ANISOU  228  N   THR A  39     4469   6041   5687    116     83   1182  A    N  
ATOM    229  CA  THR A  39      -3.380  27.471 -20.101  1.00 46.00      A    C  
ANISOU  229  CA  THR A  39     4936   6496   6044    136    104   1126  A    C  
ATOM    230  C   THR A  39      -3.687  27.568 -21.557  1.00 47.87      A    C  
ANISOU  230  C   THR A  39     5132   6817   6239    158    132   1181  A    C  
ATOM    231  O   THR A  39      -3.254  28.481 -22.221  1.00 43.35      A    O  
ANISOU  231  O   THR A  39     4501   6266   5701    150    132   1266  A    O  
ATOM    232  CB  THR A  39      -4.618  28.044 -19.418  1.00 44.73      A    C  
ANISOU  232  CB  THR A  39     4812   6269   5912    120     85   1088  A    C  
ATOM    233  CG2 THR A  39      -4.416  28.081 -17.890  1.00 44.16      A    C  
ANISOU  233  CG2 THR A  39     4780   6115   5881    103     53   1033  A    C  
ATOM    234  OG1 THR A  39      -4.825  29.366 -19.910  1.00 44.03      A    O  
ANISOU  234  OG1 THR A  39     4680   6167   5881    105     71   1156  A    O  
ATOM    235  N   ARG A  40      -4.401  26.572 -22.026  1.00 46.36      A    N  
ANISOU  235  N   ARG A  40     4970   6670   5973    186    152   1132  A    N  
ATOM    236  CA  ARG A  40      -4.868  26.481 -23.367  1.00 53.44      A    C  
ANISOU  236  CA  ARG A  40     5839   7648   6816    214    175   1163  A    C  
ATOM    237  C   ARG A  40      -6.446  26.377 -23.297  1.00 46.99      A    C  
ANISOU  237  C   ARG A  40     5066   6805   5982    214    173   1111  A    C  
ATOM    238  O   ARG A  40      -6.963  26.038 -22.276  1.00 43.57      A    O  
ANISOU  238  O   ARG A  40     4682   6310   5560    198    158   1047  A    O  
ATOM    239  CB  ARG A  40      -4.247  25.222 -23.966  1.00 66.49      A    C  
ANISOU  239  CB  ARG A  40     7490   9380   8393    258    193   1137  A    C  
ATOM    240  CG  ARG A  40      -4.230  25.264 -25.489  1.00107.70      A    C  
ANISOU  240  CG  ARG A  40    12659  14706  13556    298    219   1191  A    C  
ATOM    241  CD  ARG A  40      -3.200  24.393 -26.216  1.00131.79      A    C  
ANISOU  241  CD  ARG A  40    15680  17852  16541    347    236   1196  A    C  
ATOM    242  NE  ARG A  40      -3.491  22.965 -26.082  1.00138.40      A    N  
ANISOU  242  NE  ARG A  40    16569  18695  17318    379    228   1098  A    N  
ATOM    243  CZ  ARG A  40      -4.428  22.308 -26.758  1.00129.72      A    C  
ANISOU  243  CZ  ARG A  40    15493  17632  16162    413    227   1052  A    C  
ATOM    244  NH1 ARG A  40      -4.592  21.012 -26.528  1.00120.73      A    N1+
ANISOU  244  NH1 ARG A  40    14399  16485  14985    439    209    966  A    N1+
ATOM    245  NH2 ARG A  40      -5.196  22.932 -27.650  1.00129.67      A    N  
ANISOU  245  NH2 ARG A  40    15463  17664  16141    423    239   1092  A    N  
ATOM    246  N   PRO A  41      -7.176  26.663 -24.380  1.00 49.66      A    N  
ANISOU  246  N   PRO A  41     5382   7193   6292    230    186   1142  A    N  
ATOM    247  CA  PRO A  41      -8.658  26.620 -24.317  1.00 45.62      A    C  
ANISOU  247  CA  PRO A  41     4908   6656   5771    228    182   1096  A    C  
ATOM    248  C   PRO A  41      -9.257  25.261 -24.300  1.00 46.00      A    C  
ANISOU  248  C   PRO A  41     5000   6718   5757    251    185   1017  A    C  
ATOM    249  O   PRO A  41      -8.797  24.371 -25.001  1.00 43.49      A    O  
ANISOU  249  O   PRO A  41     4675   6466   5383    286    194   1006  A    O  
ATOM    250  CB  PRO A  41      -9.130  27.345 -25.609  1.00 46.64      A    C  
ANISOU  250  CB  PRO A  41     4993   6842   5886    243    195   1161  A    C  
ATOM    251  CG  PRO A  41      -7.940  27.363 -26.523  1.00 52.62      A    C  
ANISOU  251  CG  PRO A  41     5694   7680   6617    266    214   1230  A    C  
ATOM    252  CD  PRO A  41      -6.691  27.261 -25.653  1.00 48.28      A    C  
ANISOU  252  CD  PRO A  41     5142   7097   6104    248    205   1231  A    C  
ATOM    253  N   ILE A  42     -10.320  25.105 -23.511  1.00 41.25      A    N  
ANISOU  253  N   ILE A  42     4443   6059   5169    232    172    963  A    N  
ATOM    254  CA  ILE A  42     -11.164  23.938 -23.660  1.00 38.21      A    C  
ANISOU  254  CA  ILE A  42     4093   5689   4734    250    171    899  A    C  
ATOM    255  C   ILE A  42     -12.045  24.188 -24.886  1.00 38.64      A    C  
ANISOU  255  C   ILE A  42     4128   5794   4759    273    180    920  A    C  
ATOM    256  O   ILE A  42     -12.589  25.312 -25.030  1.00 42.23      A    O  
ANISOU  256  O   ILE A  42     4565   6234   5248    257    182    960  A    O  
ATOM    257  CB  ILE A  42     -12.050  23.766 -22.438  1.00 38.71      A    C  
ANISOU  257  CB  ILE A  42     4202   5682   4823    221    157    848  A    C  
ATOM    258  CG1 ILE A  42     -11.188  23.409 -21.225  1.00 37.14      A    C  
ANISOU  258  CG1 ILE A  42     4026   5439   4646    204    147    823  A    C  
ATOM    259  CG2 ILE A  42     -13.120  22.712 -22.748  1.00 38.85      A    C  
ANISOU  259  CG2 ILE A  42     4246   5714   4798    236    152    797  A    C  
ATOM    260  CD1 ILE A  42     -11.837  23.648 -19.901  1.00 34.67      A    C  
ANISOU  260  CD1 ILE A  42     3744   5060   4366    175    135    792  A    C  
ATOM    261  N   PRO A  43     -12.212  23.158 -25.733  1.00 36.27      A    N  
ANISOU  261  N   PRO A  43     3833   5550   4397    312    180    890  A    N  
ATOM    262  CA  PRO A  43     -13.049  23.277 -26.902  1.00 43.20      A    C  
ANISOU  262  CA  PRO A  43     4695   6478   5241    339    184    902  A    C  
ATOM    263  C   PRO A  43     -14.495  23.578 -26.543  1.00 46.88      A    C  
ANISOU  263  C   PRO A  43     5184   6895   5731    315    177    878  A    C  
ATOM    264  O   PRO A  43     -15.084  22.959 -25.641  1.00 41.80      A    O  
ANISOU  264  O   PRO A  43     4580   6201   5099    295    163    825  A    O  
ATOM    265  CB  PRO A  43     -12.991  21.895 -27.555  1.00 42.42      A    C  
ANISOU  265  CB  PRO A  43     4609   6429   5077    386    173    850  A    C  
ATOM    266  CG  PRO A  43     -11.838  21.188 -26.932  1.00 44.56      A    C  
ANISOU  266  CG  PRO A  43     4891   6691   5347    387    167    827  A    C  
ATOM    267  CD  PRO A  43     -11.574  21.824 -25.618  1.00 38.61      A    C  
ANISOU  267  CD  PRO A  43     4150   5861   4657    335    168    840  A    C  
ATOM    268  N   ARG A  44     -15.080  24.489 -27.293  1.00 44.10      A    N  
ANISOU  268  N   ARG A  44     4806   6566   5383    319    185    922  A    N  
ATOM    269  CA  ARG A  44     -16.456  24.885 -27.075  1.00 50.38      A    C  
ANISOU  269  CA  ARG A  44     5618   7324   6201    301    179    904  A    C  
ATOM    270  C   ARG A  44     -17.226  24.458 -28.334  1.00 51.84      A    C  
ANISOU  270  C   ARG A  44     5795   7567   6333    338    177    895  A    C  
ATOM    271  O   ARG A  44     -16.962  24.956 -29.430  1.00 45.19      A    O  
ANISOU  271  O   ARG A  44     4916   6787   5467    366    189    945  A    O  
ATOM    272  CB  ARG A  44     -16.444  26.374 -26.721  1.00 50.91      A    C  
ANISOU  272  CB  ARG A  44     5662   7353   6327    271    182    959  A    C  
ATOM    273  CG  ARG A  44     -17.751  27.055 -26.801  1.00 62.69      A    C  
ANISOU  273  CG  ARG A  44     7156   8822   7840    261    177    958  A    C  
ATOM    274  CD  ARG A  44     -17.646  28.577 -26.584  1.00 62.36      A    C  
ANISOU  274  CD  ARG A  44     7088   8745   7860    238    171   1014  A    C  
ATOM    275  NE  ARG A  44     -19.023  29.130 -26.556  1.00 65.29      A    N  
ANISOU  275  NE  ARG A  44     7467   9090   8249    231    163   1000  A    N  
ATOM    276  CZ  ARG A  44     -19.776  29.201 -25.435  1.00 66.62      A    C  
ANISOU  276  CZ  ARG A  44     7664   9202   8446    211    152    952  A    C  
ATOM    277  NH1 ARG A  44     -19.264  28.815 -24.220  1.00 52.13      A    N1+
ANISOU  277  NH1 ARG A  44     5854   7327   6626    195    148    917  A    N1+
ATOM    278  NH2 ARG A  44     -21.020  29.704 -25.491  1.00 59.23      A    N  
ANISOU  278  NH2 ARG A  44     6730   8251   7522    209    146    941  A    N  
ATOM    279  N   LEU A  45     -18.131  23.485 -28.179  1.00 44.24      A    N  
ANISOU  279  N   LEU A  45     4866   6588   5355    343    160    832  A    N  
ATOM    280  CA  LEU A  45     -18.722  22.801 -29.307  1.00 40.76      A    C  
ANISOU  280  CA  LEU A  45     4422   6199   4863    386    148    807  A    C  
ATOM    281  C   LEU A  45     -20.224  22.627 -29.194  1.00 45.79      A    C  
ANISOU  281  C   LEU A  45     5080   6803   5513    372    133    772  A    C  
ATOM    282  O   LEU A  45     -20.828  22.736 -28.113  1.00 39.69      A    O  
ANISOU  282  O   LEU A  45     4328   5969   4783    331    130    756  A    O  
ATOM    283  CB  LEU A  45     -18.146  21.428 -29.471  1.00 40.85      A    C  
ANISOU  283  CB  LEU A  45     4451   6234   4835    417    130    758  A    C  
ATOM    284  CG  LEU A  45     -16.621  21.327 -29.686  1.00 46.41      A    C  
ANISOU  284  CG  LEU A  45     5134   6982   5514    440    142    782  A    C  
ATOM    285  CD1 LEU A  45     -16.152  19.869 -29.646  1.00 43.26      A    C  
ANISOU  285  CD1 LEU A  45     4760   6593   5084    471    115    719  A    C  
ATOM    286  CD2 LEU A  45     -16.296  21.972 -31.031  1.00 49.34      A    C  
ANISOU  286  CD2 LEU A  45     5459   7443   5844    484    161    837  A    C  
ATOM    287  N   SER A  46     -20.800  22.249 -30.327  1.00 44.12      A    N  
ANISOU  287  N   SER A  46     4861   6639   5261    412    121    758  A    N  
ATOM    288  CA  SER A  46     -22.167  21.859 -30.326  1.00 45.39      A    C  
ANISOU  288  CA  SER A  46     5041   6774   5431    405    100    719  A    C  
ATOM    289  C   SER A  46     -22.267  20.443 -29.896  1.00 43.67      A    C  
ANISOU  289  C   SER A  46     4852   6529   5210    406     69    657  A    C  
ATOM    290  O   SER A  46     -21.481  19.577 -30.279  1.00 40.13      A    O  
ANISOU  290  O   SER A  46     4408   6110   4727    441     53    632  A    O  
ATOM    291  CB  SER A  46     -22.856  21.988 -31.708  1.00 42.94      A    C  
ANISOU  291  CB  SER A  46     4711   6519   5083    449     92    724  A    C  
ATOM    292  OG  SER A  46     -24.146  21.278 -31.639  1.00 42.33      A    O  
ANISOU  292  OG  SER A  46     4655   6410   5015    442     62    673  A    O  
ATOM    293  N   GLN A  47     -23.314  20.228 -29.131  1.00 44.29      A    N  
ANISOU  293  N   GLN A  47     4948   6551   5326    369     57    635  A    N  
ATOM    294  CA  GLN A  47     -23.856  18.962 -28.753  1.00 45.18      A    C  
ANISOU  294  CA  GLN A  47     5086   6630   5448    361     20    584  A    C  
ATOM    295  C   GLN A  47     -23.950  17.990 -29.914  1.00 45.06      A    C  
ANISOU  295  C   GLN A  47     5072   6653   5395    413    -17    544  A    C  
ATOM    296  O   GLN A  47     -23.686  16.829 -29.752  1.00 46.09      A    O  
ANISOU  296  O   GLN A  47     5220   6767   5522    424    -54    502  A    O  
ATOM    297  CB  GLN A  47     -25.227  19.261 -28.167  1.00 55.88      A    C  
ANISOU  297  CB  GLN A  47     6442   7948   6842    322     25    589  A    C  
ATOM    298  CG  GLN A  47     -26.118  18.100 -27.903  1.00 58.16      A    C  
ANISOU  298  CG  GLN A  47     6742   8200   7152    304     -9    555  A    C  
ATOM    299  CD  GLN A  47     -26.815  17.651 -29.130  1.00 56.34      A    C  
ANISOU  299  CD  GLN A  47     6510   7996   6901    344    -47    525  A    C  
ATOM    300  NE2 GLN A  47     -26.882  16.362 -29.315  1.00 52.15      A    N  
ANISOU  300  NE2 GLN A  47     5994   7447   6371    355    -92    483  A    N  
ATOM    301  OE1 GLN A  47     -27.279  18.451 -29.907  1.00 57.27      A    O  
ANISOU  301  OE1 GLN A  47     6612   8147   7003    367    -40    537  A    O  
ATOM    302  N   SER A  48     -24.299  18.479 -31.095  1.00 49.13      A    N  
ANISOU  302  N   SER A  48     5567   7221   5877    453    -14    556  A    N  
ATOM    303  CA  SER A  48     -24.394  17.604 -32.317  1.00 50.75      A    C  
ANISOU  303  CA  SER A  48     5772   7472   6038    516    -56    512  A    C  
ATOM    304  C   SER A  48     -23.072  17.225 -32.929  1.00 55.10      A    C  
ANISOU  304  C   SER A  48     6316   8082   6537    570    -58    504  A    C  
ATOM    305  O   SER A  48     -23.027  16.406 -33.861  1.00 48.67      A    O  
ANISOU  305  O   SER A  48     5502   7308   5681    629    -96    459  A    O  
ATOM    306  CB  SER A  48     -25.201  18.304 -33.407  1.00 51.13      A    C  
ANISOU  306  CB  SER A  48     5799   7564   6062    545    -51    529  A    C  
ATOM    307  OG  SER A  48     -24.625  19.595 -33.649  1.00 51.59      A    O  
ANISOU  307  OG  SER A  48     5831   7664   6106    544     -1    594  A    O  
ATOM    308  N   ASP A  49     -21.986  17.833 -32.439  1.00 55.73      A    N  
ANISOU  308  N   ASP A  49     6385   8171   6616    553    -17    547  A    N  
ATOM    309  CA  ASP A  49     -20.675  17.694 -33.088  1.00 50.59      A    C  
ANISOU  309  CA  ASP A  49     5717   7591   5912    605     -8    554  A    C  
ATOM    310  C   ASP A  49     -19.990  16.415 -32.669  1.00 53.10      A    C  
ANISOU  310  C   ASP A  49     6059   7889   6227    619    -44    498  A    C  
ATOM    311  O   ASP A  49     -19.694  16.245 -31.497  1.00 51.64      A    O  
ANISOU  311  O   ASP A  49     5892   7642   6085    569    -40    499  A    O  
ATOM    312  CB  ASP A  49     -19.836  18.917 -32.709  1.00 49.27      A    C  
ANISOU  312  CB  ASP A  49     5526   7437   5757    575     44    628  A    C  
ATOM    313  CG  ASP A  49     -18.555  19.005 -33.497  1.00 52.98      A    C  
ANISOU  313  CG  ASP A  49     5964   7992   6171    628     61    656  A    C  
ATOM    314  OD1 ASP A  49     -18.106  17.952 -33.938  1.00 48.85      A    O  
ANISOU  314  OD1 ASP A  49     5448   7504   5606    679     32    605  A    O  
ATOM    315  OD2 ASP A  49     -17.992  20.116 -33.609  1.00 53.01      A    O1-
ANISOU  315  OD2 ASP A  49     5936   8027   6177    616    102    729  A    O1-
ATOM    316  N   PRO A  50     -19.687  15.517 -33.622  1.00 54.54      A    N  
ANISOU  316  N   PRO A  50     6239   8123   6356    690    -82    449  A    N  
ATOM    317  CA  PRO A  50     -18.979  14.285 -33.309  1.00 54.31      A    C  
ANISOU  317  CA  PRO A  50     6232   8077   6325    711   -122    392  A    C  
ATOM    318  C   PRO A  50     -17.719  14.462 -32.459  1.00 53.42      A    C  
ANISOU  318  C   PRO A  50     6117   7956   6223    685    -90    421  A    C  
ATOM    319  O   PRO A  50     -17.399  13.575 -31.680  1.00 55.01      A    O  
ANISOU  319  O   PRO A  50     6346   8103   6451    668   -120    383  A    O  
ATOM    320  CB  PRO A  50     -18.594  13.732 -34.694  1.00 56.94      A    C  
ANISOU  320  CB  PRO A  50     6549   8502   6582    808   -152    351  A    C  
ATOM    321  CG  PRO A  50     -19.647  14.292 -35.603  1.00 55.53      A    C  
ANISOU  321  CG  PRO A  50     6356   8358   6385    828   -151    364  A    C  
ATOM    322  CD  PRO A  50     -19.921  15.656 -35.063  1.00 54.14      A    C  
ANISOU  322  CD  PRO A  50     6166   8160   6245    761    -89    444  A    C  
ATOM    323  N   ARG A  51     -17.032  15.582 -32.579  1.00 50.95      A    N  
ANISOU  323  N   ARG A  51     5773   7689   5895    679    -34    489  A    N  
ATOM    324  CA  ARG A  51     -15.826  15.770 -31.814  1.00 51.08      A    C  
ANISOU  324  CA  ARG A  51     5785   7696   5924    656     -8    517  A    C  
ATOM    325  C   ARG A  51     -16.187  15.852 -30.389  1.00 53.53      A    C  
ANISOU  325  C   ARG A  51     6125   7908   6303    578     -6    520  A    C  
ATOM    326  O   ARG A  51     -15.428  15.405 -29.543  1.00 48.07      A    O  
ANISOU  326  O   ARG A  51     5449   7183   5632    559    -10    508  A    O  
ATOM    327  CB  ARG A  51     -15.029  17.005 -32.253  1.00 53.92      A    C  
ANISOU  327  CB  ARG A  51     6101   8124   6262    662     45    597  A    C  
ATOM    328  CG  ARG A  51     -14.573  16.791 -33.718  1.00 66.50      A    C  
ANISOU  328  CG  ARG A  51     7660   9834   7772    750     43    594  A    C  
ATOM    329  CD  ARG A  51     -14.103  18.031 -34.474  1.00 63.24      A    C  
ANISOU  329  CD  ARG A  51     7192   9504   7330    764     92    684  A    C  
ATOM    330  NE  ARG A  51     -15.226  18.961 -34.743  1.00 69.32      A    N  
ANISOU  330  NE  ARG A  51     7956  10258   8122    736    106    722  A    N  
ATOM    331  CZ  ARG A  51     -15.077  20.276 -34.920  1.00 67.97      A    C  
ANISOU  331  CZ  ARG A  51     7747  10111   7965    711    147    811  A    C  
ATOM    332  NH1 ARG A  51     -13.885  20.835 -34.869  1.00 70.09      A    N1+
ANISOU  332  NH1 ARG A  51     7979  10417   8232    708    178    875  A    N1+
ATOM    333  NH2 ARG A  51     -16.119  21.038 -35.153  1.00 73.65      A    N  
ANISOU  333  NH2 ARG A  51     8464  10812   8705    689    152    838  A    N  
ATOM    334  N   ALA A  52     -17.345  16.446 -30.109  1.00 54.05      A    N  
ANISOU  334  N   ALA A  52     6195   7933   6405    537      3    537  A    N  
ATOM    335  CA  ALA A  52     -17.767  16.596 -28.748  1.00 44.81      A    C  
ANISOU  335  CA  ALA A  52     5049   6681   5295    469      9    543  A    C  
ATOM    336  C   ALA A  52     -17.934  15.238 -28.144  1.00 46.72      A    C  
ANISOU  336  C   ALA A  52     5325   6870   5555    460    -38    485  A    C  
ATOM    337  O   ALA A  52     -17.440  14.962 -27.052  1.00 48.96      A    O  
ANISOU  337  O   ALA A  52     5627   7108   5867    425    -37    482  A    O  
ATOM    338  CB  ALA A  52     -19.061  17.337 -28.683  1.00 45.11      A    C  
ANISOU  338  CB  ALA A  52     5084   6693   5359    438     19    563  A    C  
ATOM    339  N   GLU A  53     -18.596  14.364 -28.879  1.00 49.26      A    N  
ANISOU  339  N   GLU A  53     5654   7201   5861    495    -83    438  A    N  
ATOM    340  CA  GLU A  53     -18.879  13.033 -28.416  1.00 50.12      A    C  
ANISOU  340  CA  GLU A  53     5792   7254   5994    487   -139    385  A    C  
ATOM    341  C   GLU A  53     -17.581  12.265 -28.219  1.00 52.61      A    C  
ANISOU  341  C   GLU A  53     6117   7577   6295    513   -157    358  A    C  
ATOM    342  O   GLU A  53     -17.434  11.489 -27.271  1.00 51.00      A    O  
ANISOU  342  O   GLU A  53     5936   7313   6125    481   -183    339  A    O  
ATOM    343  CB  GLU A  53     -19.789  12.312 -29.397  1.00 57.44      A    C  
ANISOU  343  CB  GLU A  53     6721   8192   6910    527   -192    339  A    C  
ATOM    344  CG  GLU A  53     -20.633  11.243 -28.763  1.00 67.35      A    C  
ANISOU  344  CG  GLU A  53     8001   9371   8218    494   -248    305  A    C  
ATOM    345  CD  GLU A  53     -21.916  11.753 -28.045  1.00 68.03      A    C  
ANISOU  345  CD  GLU A  53     8085   9410   8352    429   -229    340  A    C  
ATOM    346  OE1 GLU A  53     -22.107  12.952 -27.695  1.00 56.02      A    O  
ANISOU  346  OE1 GLU A  53     6551   7899   6833    398   -171    389  A    O  
ATOM    347  OE2 GLU A  53     -22.752  10.886 -27.778  1.00 68.78      A    O1-
ANISOU  347  OE2 GLU A  53     8191   9454   8486    407   -279    318  A    O1-
ATOM    348  N   GLU A  54     -16.630  12.522 -29.110  1.00 50.61      A    N  
ANISOU  348  N   GLU A  54     5842   7400   5987    570   -141    363  A    N  
ATOM    349  CA  GLU A  54     -15.332  11.918 -29.057  1.00 51.01      A    C  
ANISOU  349  CA  GLU A  54     5894   7472   6015    602   -153    339  A    C  
ATOM    350  C   GLU A  54     -14.610  12.361 -27.754  1.00 50.23      A    C  
ANISOU  350  C   GLU A  54     5803   7329   5953    543   -116    378  A    C  
ATOM    351  O   GLU A  54     -14.077  11.559 -27.041  1.00 42.85      A    O  
ANISOU  351  O   GLU A  54     4889   6354   5036    532   -142    350  A    O  
ATOM    352  CB  GLU A  54     -14.516  12.391 -30.269  1.00 61.89      A    C  
ANISOU  352  CB  GLU A  54     7235   8956   7324    672   -127    356  A    C  
ATOM    353  CG  GLU A  54     -13.424  11.458 -30.745  1.00 71.54      A    C  
ANISOU  353  CG  GLU A  54     8454  10225   8501    740   -158    307  A    C  
ATOM    354  CD  GLU A  54     -12.436  12.152 -31.672  1.00 74.44      A    C  
ANISOU  354  CD  GLU A  54     8776  10704   8803    796   -115    347  A    C  
ATOM    355  OE1 GLU A  54     -11.250  11.787 -31.639  1.00 77.91      A    O  
ANISOU  355  OE1 GLU A  54     9205  11177   9217    827   -115    336  A    O  
ATOM    356  OE2 GLU A  54     -12.830  13.084 -32.421  1.00 77.24      A    O1-
ANISOU  356  OE2 GLU A  54     9100  11114   9131    807    -80    394  A    O1-
ATOM    357  N   LEU A  55     -14.615  13.647 -27.457  1.00 42.44      A    N  
ANISOU  357  N   LEU A  55     4797   6348   4978    507    -61    439  A    N  
ATOM    358  CA  LEU A  55     -14.049  14.125 -26.223  1.00 45.58      A    C  
ANISOU  358  CA  LEU A  55     5203   6701   5414    455    -34    470  A    C  
ATOM    359  C   LEU A  55     -14.624  13.460 -24.938  1.00 44.68      A    C  
ANISOU  359  C   LEU A  55     5125   6502   5349    402    -59    448  A    C  
ATOM    360  O   LEU A  55     -13.875  13.066 -24.057  1.00 45.62      A    O  
ANISOU  360  O   LEU A  55     5260   6588   5484    383    -64    441  A    O  
ATOM    361  CB  LEU A  55     -14.174  15.656 -26.156  1.00 42.11      A    C  
ANISOU  361  CB  LEU A  55     4738   6272   4987    427     17    537  A    C  
ATOM    362  CG  LEU A  55     -13.267  16.382 -27.162  1.00 45.88      A    C  
ANISOU  362  CG  LEU A  55     5173   6833   5426    469     47    578  A    C  
ATOM    363  CD1 LEU A  55     -13.660  17.839 -27.308  1.00 41.45      A    C  
ANISOU  363  CD1 LEU A  55     4585   6279   4883    443     85    643  A    C  
ATOM    364  CD2 LEU A  55     -11.808  16.308 -26.750  1.00 46.46      A    C  
ANISOU  364  CD2 LEU A  55     5239   6916   5497    472     57    590  A    C  
ATOM    365  N   ILE A  56     -15.941  13.373 -24.813  1.00 43.33      A    N  
ANISOU  365  N   ILE A  56     4963   6298   5200    376    -72    443  A    N  
ATOM    366  CA  ILE A  56     -16.570  12.815 -23.606  1.00 43.34      A    C  
ANISOU  366  CA  ILE A  56     4991   6229   5246    324    -91    434  A    C  
ATOM    367  C   ILE A  56     -16.187  11.337 -23.476  1.00 48.17      A    C  
ANISOU  367  C   ILE A  56     5625   6812   5862    339   -148    386  A    C  
ATOM    368  O   ILE A  56     -15.886  10.842 -22.403  1.00 51.65      A    O  
ANISOU  368  O   ILE A  56     6085   7207   6330    305   -159    385  A    O  
ATOM    369  CB  ILE A  56     -18.083  12.961 -23.734  1.00 41.42      A    C  
ANISOU  369  CB  ILE A  56     4746   5970   5022    303    -97    439  A    C  
ATOM    370  CG1 ILE A  56     -18.463  14.477 -23.727  1.00 36.72      A    C  
ANISOU  370  CG1 ILE A  56     4129   5394   4427    287    -43    485  A    C  
ATOM    371  CG2 ILE A  56     -18.782  12.353 -22.589  1.00 42.38      A    C  
ANISOU  371  CG2 ILE A  56     4886   6031   5185    253   -116    438  A    C  
ATOM    372  CD1 ILE A  56     -19.857  14.746 -24.236  1.00 38.72      A    C  
ANISOU  372  CD1 ILE A  56     4373   5650   4687    283    -47    489  A    C  
ATOM    373  N   GLU A  57     -16.200  10.670 -24.621  1.00 45.34      A    N  
ANISOU  373  N   GLU A  57     5262   6485   5477    393   -188    346  A    N  
ATOM    374  CA  GLU A  57     -15.879   9.253 -24.751  1.00 54.85      A    C  
ANISOU  374  CA  GLU A  57     6487   7667   6686    421   -254    291  A    C  
ATOM    375  C   GLU A  57     -14.473   9.002 -24.233  1.00 50.13      A    C  
ANISOU  375  C   GLU A  57     5896   7071   6079    429   -249    285  A    C  
ATOM    376  O   GLU A  57     -14.255   8.045 -23.503  1.00 50.24      A    O  
ANISOU  376  O   GLU A  57     5933   7032   6122    411   -290    263  A    O  
ATOM    377  CB  GLU A  57     -16.019   8.797 -26.228  1.00 55.98      A    C  
ANISOU  377  CB  GLU A  57     6618   7860   6789    494   -294    246  A    C  
ATOM    378  CG  GLU A  57     -15.726   7.332 -26.509  1.00 60.69      A    C  
ANISOU  378  CG  GLU A  57     7233   8434   7390    536   -375    177  A    C  
ATOM    379  CD  GLU A  57     -16.496   6.350 -25.633  1.00 70.92      A    C  
ANISOU  379  CD  GLU A  57     8554   9638   8753    484   -432    166  A    C  
ATOM    380  OE1 GLU A  57     -17.340   6.769 -24.771  1.00 71.64      A    O  
ANISOU  380  OE1 GLU A  57     8647   9689   8884    416   -404    212  A    O  
ATOM    381  OE2 GLU A  57     -16.237   5.127 -25.825  1.00 74.06      A    O1-
ANISOU  381  OE2 GLU A  57     8967  10008   9164    516   -508    111  A    O1-
ATOM    382  N   ASN A  58     -13.554   9.899 -24.552  1.00 48.10      A    N  
ANISOU  382  N   ASN A  58     5617   6871   5787    451   -199    313  A    N  
ATOM    383  CA  ASN A  58     -12.176   9.807 -24.082  1.00 49.25      A    C  
ANISOU  383  CA  ASN A  58     5763   7023   5924    458   -188    314  A    C  
ATOM    384  C   ASN A  58     -11.952  10.447 -22.751  1.00 43.91      A    C  
ANISOU  384  C   ASN A  58     5097   6303   5284    395   -151    355  A    C  
ATOM    385  O   ASN A  58     -10.835  10.686 -22.370  1.00 38.02      A    O  
ANISOU  385  O   ASN A  58     4345   5565   4532    397   -131    368  A    O  
ATOM    386  CB  ASN A  58     -11.283  10.521 -25.069  1.00 59.70      A    C  
ANISOU  386  CB  ASN A  58     7053   8433   7196    510   -152    331  A    C  
ATOM    387  CG  ASN A  58     -11.098   9.734 -26.307  1.00 72.20      A    C  
ANISOU  387  CG  ASN A  58     8627  10073   8731    588   -192    280  A    C  
ATOM    388  ND2 ASN A  58     -10.293   8.697 -26.198  1.00 90.17      A    N  
ANISOU  388  ND2 ASN A  58    10917  12341  11001    619   -235    233  A    N  
ATOM    389  OD1 ASN A  58     -11.687  10.016 -27.340  1.00 81.02      A    O  
ANISOU  389  OD1 ASN A  58     9726  11239   9818    623   -190    279  A    O  
ATOM    390  N   GLU A  59     -13.004  10.826 -22.073  1.00 39.88      A    N  
ANISOU  390  N   GLU A  59     4595   5748   4806    344   -139    379  A    N  
ATOM    391  CA  GLU A  59     -12.859  11.498 -20.813  1.00 42.66      A    C  
ANISOU  391  CA  GLU A  59     4954   6067   5186    293   -104    415  A    C  
ATOM    392  C   GLU A  59     -11.953  12.707 -20.822  1.00 40.21      A    C  
ANISOU  392  C   GLU A  59     4620   5791   4865    298    -54    453  A    C  
ATOM    393  O   GLU A  59     -11.108  12.867 -19.995  1.00 40.36      A    O  
ANISOU  393  O   GLU A  59     4644   5791   4898    278    -42    465  A    O  
ATOM    394  CB  GLU A  59     -12.449  10.498 -19.767  1.00 47.28      A    C  
ANISOU  394  CB  GLU A  59     5567   6602   5794    274   -140    392  A    C  
ATOM    395  CG  GLU A  59     -13.634   9.690 -19.331  1.00 47.56      A    C  
ANISOU  395  CG  GLU A  59     5618   6591   5859    241   -173    385  A    C  
ATOM    396  CD  GLU A  59     -13.268   8.537 -18.496  1.00 54.36      A    C  
ANISOU  396  CD  GLU A  59     6505   7401   6745    219   -215    370  A    C  
ATOM    397  OE1 GLU A  59     -12.905   7.514 -19.061  1.00 61.84      A    O  
ANISOU  397  OE1 GLU A  59     7460   8345   7689    254   -265    329  A    O  
ATOM    398  OE2 GLU A  59     -13.355   8.665 -17.287  1.00 52.92      A    O1-
ANISOU  398  OE2 GLU A  59     6333   7187   6585    173   -198    398  A    O1-
ATOM    399  N   GLU A  60     -12.190  13.562 -21.780  1.00 40.53      A    N  
ANISOU  399  N   GLU A  60     4633   5878   4886    318    -30    476  A    N  
ATOM    400  CA  GLU A  60     -11.613  14.877 -21.887  1.00 42.00      A    C  
ANISOU  400  CA  GLU A  60     4790   6092   5073    315     13    525  A    C  
ATOM    401  C   GLU A  60     -12.665  15.990 -21.864  1.00 40.37      A    C  
ANISOU  401  C   GLU A  60     4574   5879   4885    288     39    558  A    C  
ATOM    402  O   GLU A  60     -13.754  15.804 -22.332  1.00 38.65      A    O  
ANISOU  402  O   GLU A  60     4358   5665   4662    291     29    546  A    O  
ATOM    403  CB  GLU A  60     -10.846  14.953 -23.215  1.00 45.14      A    C  
ANISOU  403  CB  GLU A  60     5156   6567   5426    371     20    532  A    C  
ATOM    404  CG  GLU A  60      -9.595  14.071 -23.209  1.00 52.00      A    C  
ANISOU  404  CG  GLU A  60     6029   7452   6276    401      1    503  A    C  
ATOM    405  CD  GLU A  60      -8.924  14.104 -24.535  1.00 54.07      A    C  
ANISOU  405  CD  GLU A  60     6255   7802   6487    464      9    510  A    C  
ATOM    406  OE1 GLU A  60      -8.920  13.093 -25.218  1.00 64.92      A    O  
ANISOU  406  OE1 GLU A  60     7635   9204   7826    512    -25    461  A    O  
ATOM    407  OE2 GLU A  60      -8.523  15.184 -24.932  1.00 57.40      A    O1-
ANISOU  407  OE2 GLU A  60     6639   8266   6903    466     46    566  A    O1-
ATOM    408  N   PRO A  61     -12.328  17.143 -21.314  1.00 35.70      A    N  
ANISOU  408  N   PRO A  61     3969   5275   4319    264     68    598  A    N  
ATOM    409  CA  PRO A  61     -13.298  18.158 -21.088  1.00 36.26      A    C  
ANISOU  409  CA  PRO A  61     4034   5328   4414    238     85    622  A    C  
ATOM    410  C   PRO A  61     -13.753  18.821 -22.384  1.00 38.83      A    C  
ANISOU  410  C   PRO A  61     4328   5703   4719    263     99    650  A    C  
ATOM    411  O   PRO A  61     -13.055  18.782 -23.403  1.00 36.70      A    O  
ANISOU  411  O   PRO A  61     4035   5489   4420    299    104    663  A    O  
ATOM    412  CB  PRO A  61     -12.598  19.099 -20.144  1.00 37.78      A    C  
ANISOU  412  CB  PRO A  61     4222   5491   4640    213    101    648  A    C  
ATOM    413  CG  PRO A  61     -11.067  18.925 -20.493  1.00 34.72      A    C  
ANISOU  413  CG  PRO A  61     3818   5132   4242    235    102    661  A    C  
ATOM    414  CD  PRO A  61     -10.998  17.471 -20.771  1.00 37.19      A    C  
ANISOU  414  CD  PRO A  61     4152   5458   4522    258     78    615  A    C  
ATOM    415  N   VAL A  62     -14.991  19.286 -22.380  1.00 34.83      A    N  
ANISOU  415  N   VAL A  62     3824   5183   4226    248    102    653  A    N  
ATOM    416  CA  VAL A  62     -15.628  19.958 -23.569  1.00 35.28      A    C  
ANISOU  416  CA  VAL A  62     3854   5283   4268    268    114    678  A    C  
ATOM    417  C   VAL A  62     -16.716  20.811 -23.004  1.00 37.55      A    C  
ANISOU  417  C   VAL A  62     4143   5534   4589    237    122    690  A    C  
ATOM    418  O   VAL A  62     -17.377  20.459 -22.013  1.00 38.94      A    O  
ANISOU  418  O   VAL A  62     4343   5669   4783    211    114    663  A    O  
ATOM    419  CB  VAL A  62     -16.161  18.938 -24.602  1.00 38.10      A    C  
ANISOU  419  CB  VAL A  62     4214   5676   4584    305     92    645  A    C  
ATOM    420  CG1 VAL A  62     -17.187  17.945 -24.021  1.00 36.75      A    C  
ANISOU  420  CG1 VAL A  62     4075   5463   4426    285     64    600  A    C  
ATOM    421  CG2 VAL A  62     -16.719  19.609 -25.847  1.00 37.07      A    C  
ANISOU  421  CG2 VAL A  62     4055   5595   4432    331    103    672  A    C  
ATOM    422  N   VAL A  63     -16.803  22.015 -23.493  1.00 35.74      A    N  
ANISOU  422  N   VAL A  63     3887   5320   4372    239    138    732  A    N  
ATOM    423  CA  VAL A  63     -17.925  22.860 -23.189  1.00 36.92      A    C  
ANISOU  423  CA  VAL A  63     4034   5443   4549    219    142    740  A    C  
ATOM    424  C   VAL A  63     -18.928  22.656 -24.342  1.00 40.71      A    C  
ANISOU  424  C   VAL A  63     4505   5960   5000    242    138    735  A    C  
ATOM    425  O   VAL A  63     -18.586  22.845 -25.502  1.00 40.38      A    O  
ANISOU  425  O   VAL A  63     4440   5970   4933    272    144    761  A    O  
ATOM    426  CB  VAL A  63     -17.551  24.334 -23.175  1.00 38.12      A    C  
ANISOU  426  CB  VAL A  63     4160   5586   4737    211    153    789  A    C  
ATOM    427  CG1 VAL A  63     -18.791  25.199 -23.113  1.00 40.28      A    C  
ANISOU  427  CG1 VAL A  63     4429   5841   5034    200    153    794  A    C  
ATOM    428  CG2 VAL A  63     -16.696  24.693 -21.994  1.00 38.17      A    C  
ANISOU  428  CG2 VAL A  63     4174   5548   4779    189    149    791  A    C  
ATOM    429  N   LEU A  64     -20.143  22.269 -23.989  1.00 39.73      A    N  
ANISOU  429  N   LEU A  64     4398   5814   4882    229    129    706  A    N  
ATOM    430  CA  LEU A  64     -21.224  22.105 -24.911  1.00 40.72      A    C  
ANISOU  430  CA  LEU A  64     4517   5965   4989    245    123    698  A    C  
ATOM    431  C   LEU A  64     -22.141  23.305 -24.839  1.00 35.24      A    C  
ANISOU  431  C   LEU A  64     3808   5257   4321    232    133    721  A    C  
ATOM    432  O   LEU A  64     -22.601  23.732 -23.777  1.00 37.95      A    O  
ANISOU  432  O   LEU A  64     4160   5562   4695    205    137    714  A    O  
ATOM    433  CB  LEU A  64     -22.013  20.845 -24.606  1.00 43.90      A    C  
ANISOU  433  CB  LEU A  64     4943   6350   5386    238     98    652  A    C  
ATOM    434  CG  LEU A  64     -21.154  19.596 -24.654  1.00 46.79      A    C  
ANISOU  434  CG  LEU A  64     5325   6721   5731    253     79    624  A    C  
ATOM    435  CD1 LEU A  64     -21.724  18.585 -23.769  1.00 52.91      A    C  
ANISOU  435  CD1 LEU A  64     6123   7456   6523    227     57    592  A    C  
ATOM    436  CD2 LEU A  64     -21.042  18.982 -25.999  1.00 53.70      A    C  
ANISOU  436  CD2 LEU A  64     6192   7644   6567    298     60    608  A    C  
ATOM    437  N   THR A  65     -22.440  23.875 -25.977  1.00 34.75      A    N  
ANISOU  437  N   THR A  65     3724   5231   4246    254    137    746  A    N  
ATOM    438  CA  THR A  65     -23.122  25.169 -25.937  1.00 39.56      A    C  
ANISOU  438  CA  THR A  65     4316   5826   4886    243    145    774  A    C  
ATOM    439  C   THR A  65     -24.644  25.060 -26.158  1.00 36.63      A    C  
ANISOU  439  C   THR A  65     3948   5453   4514    242    137    752  A    C  
ATOM    440  O   THR A  65     -25.356  26.037 -26.007  1.00 37.99      A    O  
ANISOU  440  O   THR A  65     4110   5611   4713    233    141    765  A    O  
ATOM    441  CB  THR A  65     -22.641  26.048 -27.110  1.00 42.68      A    C  
ANISOU  441  CB  THR A  65     4679   6262   5272    264    153    828  A    C  
ATOM    442  CG2 THR A  65     -21.153  26.188 -27.089  1.00 47.28      A    C  
ANISOU  442  CG2 THR A  65     5249   6857   5855    268    161    860  A    C  
ATOM    443  OG1 THR A  65     -22.996  25.357 -28.289  1.00 42.17      A    O  
ANISOU  443  OG1 THR A  65     4610   6248   5161    298    147    817  A    O  
ATOM    444  N   ASP A  66     -25.171  23.925 -26.551  1.00 39.13      A    N  
ANISOU  444  N   ASP A  66     4277   5785   4805    253    122    718  A    N  
ATOM    445  CA  ASP A  66     -26.585  23.952 -26.959  1.00 41.46      A    C  
ANISOU  445  CA  ASP A  66     4567   6082   5102    255    113    706  A    C  
ATOM    446  C   ASP A  66     -27.332  22.704 -26.516  1.00 44.42      A    C  
ANISOU  446  C   ASP A  66     4959   6439   5477    243     93    664  A    C  
ATOM    447  O   ASP A  66     -28.109  22.144 -27.290  1.00 42.43      A    O  
ANISOU  447  O   ASP A  66     4705   6203   5212    258     73    646  A    O  
ATOM    448  CB  ASP A  66     -26.596  24.065 -28.481  1.00 45.62      A    C  
ANISOU  448  CB  ASP A  66     5077   6661   5596    294    108    722  A    C  
ATOM    449  CG  ASP A  66     -25.819  22.958 -29.130  1.00 49.55      A    C  
ANISOU  449  CG  ASP A  66     5581   7191   6053    324     93    701  A    C  
ATOM    450  OD1 ASP A  66     -25.093  22.246 -28.385  1.00 44.91      A    O  
ANISOU  450  OD1 ASP A  66     5011   6584   5468    312     90    683  A    O  
ATOM    451  OD2 ASP A  66     -25.932  22.786 -30.354  1.00 48.33      A    O1-
ANISOU  451  OD2 ASP A  66     5415   7085   5861    364     83    701  A    O1-
ATOM    452  N   THR A  67     -27.071  22.212 -25.293  1.00 41.12      A    N  
ANISOU  452  N   THR A  67     4558   5990   5075    215     94    650  A    N  
ATOM    453  CA  THR A  67     -27.663  20.963 -24.855  1.00 34.15      A    C  
ANISOU  453  CA  THR A  67     3688   5089   4197    199     72    620  A    C  
ATOM    454  C   THR A  67     -29.100  21.203 -24.358  1.00 37.06      A    C  
ANISOU  454  C   THR A  67     4046   5445   4588    177     73    621  A    C  
ATOM    455  O   THR A  67     -29.888  20.294 -24.381  1.00 42.66      A    O  
ANISOU  455  O   THR A  67     4756   6148   5305    168     51    605  A    O  
ATOM    456  CB  THR A  67     -26.946  20.357 -23.631  1.00 37.20      A    C  
ANISOU  456  CB  THR A  67     4093   5448   4594    175     73    614  A    C  
ATOM    457  CG2 THR A  67     -25.523  20.108 -23.878  1.00 39.63      A    C  
ANISOU  457  CG2 THR A  67     4410   5763   4883    192     72    613  A    C  
ATOM    458  OG1 THR A  67     -27.067  21.263 -22.519  1.00 32.86      A    O  
ANISOU  458  OG1 THR A  67     3541   4882   4063    154     98    628  A    O  
ATOM    459  N   ASN A  68     -29.390  22.386 -23.812  1.00 39.20      A    N  
ANISOU  459  N   ASN A  68     4306   5712   4874    170     98    637  A    N  
ATOM    460  CA  ASN A  68     -30.697  22.720 -23.222  1.00 39.84      A    C  
ANISOU  460  CA  ASN A  68     4375   5789   4973    153    104    636  A    C  
ATOM    461  C   ASN A  68     -30.860  21.908 -21.970  1.00 39.41      A    C  
ANISOU  461  C   ASN A  68     4327   5718   4926    126    103    629  A    C  
ATOM    462  O   ASN A  68     -31.997  21.588 -21.552  1.00 33.66      A    O  
ANISOU  462  O   ASN A  68     3585   4993   4209    109    101    629  A    O  
ATOM    463  CB  ASN A  68     -31.897  22.475 -24.180  1.00 37.56      A    C  
ANISOU  463  CB  ASN A  68     4071   5514   4685    162     86    630  A    C  
ATOM    464  CG  ASN A  68     -31.914  23.478 -25.309  1.00 43.46      A    C  
ANISOU  464  CG  ASN A  68     4807   6281   5424    190     91    644  A    C  
ATOM    465  ND2 ASN A  68     -31.748  23.020 -26.543  1.00 38.41      A    N  
ANISOU  465  ND2 ASN A  68     4169   5661   4763    215     73    639  A    N  
ATOM    466  OD1 ASN A  68     -32.094  24.645 -25.065  1.00 39.30      A    O  
ANISOU  466  OD1 ASN A  68     4269   5751   4909    191    107    657  A    O  
ATOM    467  N   LEU A  69     -29.721  21.561 -21.361  1.00 36.80      A    N  
ANISOU  467  N   LEU A  69     4015   5375   4591    120    106    627  A    N  
ATOM    468  CA  LEU A  69     -29.753  20.712 -20.159  1.00 35.47      A    C  
ANISOU  468  CA  LEU A  69     3854   5194   4428     93    104    625  A    C  
ATOM    469  C   LEU A  69     -30.576  21.309 -19.117  1.00 32.59      A    C  
ANISOU  469  C   LEU A  69     3474   4838   4069     82    124    632  A    C  
ATOM    470  O   LEU A  69     -31.413  20.609 -18.563  1.00 37.88      A    O  
ANISOU  470  O   LEU A  69     4134   5514   4745     61    120    639  A    O  
ATOM    471  CB  LEU A  69     -28.365  20.459 -19.642  1.00 36.86      A    C  
ANISOU  471  CB  LEU A  69     4051   5355   4596     92    106    623  A    C  
ATOM    472  CG  LEU A  69     -28.300  19.483 -18.467  1.00 37.64      A    C  
ANISOU  472  CG  LEU A  69     4159   5442   4699     65    101    623  A    C  
ATOM    473  CD1 LEU A  69     -29.027  18.155 -18.755  1.00 41.71      A    C  
ANISOU  473  CD1 LEU A  69     4671   5952   5225     48     70    623  A    C  
ATOM    474  CD2 LEU A  69     -26.827  19.272 -18.067  1.00 38.43      A    C  
ANISOU  474  CD2 LEU A  69     4281   5527   4792     67    101    617  A    C  
ATOM    475  N   VAL A  70     -30.352  22.598 -18.809  1.00 34.99      A    N  
ANISOU  475  N   VAL A  70     3775   5144   4375     97    144    632  A    N  
ATOM    476  CA  VAL A  70     -31.120  23.238 -17.748  1.00 36.82      A    C  
ANISOU  476  CA  VAL A  70     3993   5389   4609     96    160    630  A    C  
ATOM    477  C   VAL A  70     -31.918  24.429 -18.252  1.00 36.16      A    C  
ANISOU  477  C   VAL A  70     3890   5315   4534    116    164    628  A    C  
ATOM    478  O   VAL A  70     -32.022  25.468 -17.575  1.00 34.57      A    O  
ANISOU  478  O   VAL A  70     3682   5115   4337    132    173    619  A    O  
ATOM    479  CB  VAL A  70     -30.280  23.602 -16.547  1.00 39.38      A    C  
ANISOU  479  CB  VAL A  70     4330   5705   4928    100    170    623  A    C  
ATOM    480  CG1 VAL A  70     -29.739  22.339 -15.898  1.00 43.03      A    C  
ANISOU  480  CG1 VAL A  70     4807   6163   5380     77    165    629  A    C  
ATOM    481  CG2 VAL A  70     -29.170  24.603 -16.900  1.00 35.10      A    C  
ANISOU  481  CG2 VAL A  70     3798   5139   4396    118    167    619  A    C  
ATOM    482  N   TYR A  71     -32.474  24.265 -19.457  1.00 38.65      A    N  
ANISOU  482  N   TYR A  71     4196   5635   4853    119    154    633  A    N  
ATOM    483  CA  TYR A  71     -33.236  25.361 -20.084  1.00 40.19      A    C  
ANISOU  483  CA  TYR A  71     4374   5838   5059    138    154    633  A    C  
ATOM    484  C   TYR A  71     -34.217  26.042 -19.114  1.00 41.21      A    C  
ANISOU  484  C   TYR A  71     4483   5982   5191    144    166    625  A    C  
ATOM    485  O   TYR A  71     -34.214  27.254 -19.013  1.00 44.45      A    O  
ANISOU  485  O   TYR A  71     4889   6387   5613    164    167    617  A    O  
ATOM    486  CB  TYR A  71     -33.894  24.914 -21.392  1.00 44.02      A    C  
ANISOU  486  CB  TYR A  71     4850   6331   5542    140    140    638  A    C  
ATOM    487  CG  TYR A  71     -34.943  25.879 -21.915  1.00 43.62      A    C  
ANISOU  487  CG  TYR A  71     4778   6291   5502    155    140    638  A    C  
ATOM    488  CD1 TYR A  71     -34.595  27.042 -22.575  1.00 45.77      A    C  
ANISOU  488  CD1 TYR A  71     5050   6558   5784    176    138    647  A    C  
ATOM    489  CD2 TYR A  71     -36.308  25.637 -21.653  1.00 45.18      A    C  
ANISOU  489  CD2 TYR A  71     4954   6507   5705    148    141    635  A    C  
ATOM    490  CE1 TYR A  71     -35.607  27.929 -23.050  1.00 48.65      A    C  
ANISOU  490  CE1 TYR A  71     5395   6930   6160    191    135    647  A    C  
ATOM    491  CE2 TYR A  71     -37.315  26.523 -22.074  1.00 49.46      A    C  
ANISOU  491  CE2 TYR A  71     5476   7060   6257    164    140    633  A    C  
ATOM    492  CZ  TYR A  71     -36.981  27.657 -22.781  1.00 47.02      A    C  
ANISOU  492  CZ  TYR A  71     5168   6740   5955    186    137    637  A    C  
ATOM    493  OH  TYR A  71     -38.017  28.514 -23.151  1.00 58.67      A    O  
ANISOU  493  OH  TYR A  71     6623   8224   7442    201    132    634  A    O  
ATOM    494  N   PRO A  72     -34.995  25.280 -18.332  1.00 40.49      A    N  
ANISOU  494  N   PRO A  72     4379   5912   5090    128    174    626  A    N  
ATOM    495  CA  PRO A  72     -36.006  25.943 -17.460  1.00 40.50      A    C  
ANISOU  495  CA  PRO A  72     4355   5943   5088    142    188    618  A    C  
ATOM    496  C   PRO A  72     -35.400  26.669 -16.323  1.00 46.29      A    C  
ANISOU  496  C   PRO A  72     5095   6676   5813    160    196    601  A    C  
ATOM    497  O   PRO A  72     -36.044  27.545 -15.776  1.00 41.40      A    O  
ANISOU  497  O   PRO A  72     4460   6078   5192    185    201    586  A    O  
ATOM    498  CB  PRO A  72     -36.817  24.760 -16.894  1.00 46.14      A    C  
ANISOU  498  CB  PRO A  72     5051   6687   5793    115    194    636  A    C  
ATOM    499  CG  PRO A  72     -36.707  23.684 -17.974  1.00 45.79      A    C  
ANISOU  499  CG  PRO A  72     5016   6621   5761     92    173    650  A    C  
ATOM    500  CD  PRO A  72     -35.250  23.839 -18.452  1.00 44.33      A    C  
ANISOU  500  CD  PRO A  72     4865   6402   5575    100    165    640  A    C  
ATOM    501  N   ALA A  73     -34.133  26.337 -15.962  1.00 43.05      A    N  
ANISOU  501  N   ALA A  73     4713   6244   5400    153    195    602  A    N  
ATOM    502  CA  ALA A  73     -33.464  27.048 -14.871  1.00 41.71      A    C  
ANISOU  502  CA  ALA A  73     4551   6069   5224    172    196    582  A    C  
ATOM    503  C   ALA A  73     -32.901  28.361 -15.332  1.00 39.55      A    C  
ANISOU  503  C   ALA A  73     4286   5763   4977    196    179    568  A    C  
ATOM    504  O   ALA A  73     -32.507  29.212 -14.518  1.00 41.21      A    O  
ANISOU  504  O   ALA A  73     4500   5963   5193    221    171    546  A    O  
ATOM    505  CB  ALA A  73     -32.371  26.207 -14.254  1.00 44.56      A    C  
ANISOU  505  CB  ALA A  73     4937   6419   5574    156    199    587  A    C  
ATOM    506  N   LEU A  74     -32.829  28.574 -16.643  1.00 43.10      A    N  
ANISOU  506  N   LEU A  74     4735   6193   5445    191    170    584  A    N  
ATOM    507  CA  LEU A  74     -32.252  29.821 -17.092  1.00 45.10      A    C  
ANISOU  507  CA  LEU A  74     4991   6414   5729    210    151    583  A    C  
ATOM    508  C   LEU A  74     -32.923  31.071 -16.590  1.00 48.80      A    C  
ANISOU  508  C   LEU A  74     5444   6881   6215    241    138    559  A    C  
ATOM    509  O   LEU A  74     -32.246  32.095 -16.437  1.00 49.76      A    O  
ANISOU  509  O   LEU A  74     5571   6968   6367    258    116    551  A    O  
ATOM    510  CB  LEU A  74     -32.091  29.850 -18.589  1.00 47.17      A    C  
ANISOU  510  CB  LEU A  74     5251   6666   6004    202    145    611  A    C  
ATOM    511  CG  LEU A  74     -31.197  28.704 -19.091  1.00 44.75      A    C  
ANISOU  511  CG  LEU A  74     4961   6359   5681    181    150    628  A    C  
ATOM    512  CD1 LEU A  74     -30.995  28.854 -20.603  1.00 44.89      A    C  
ANISOU  512  CD1 LEU A  74     4974   6377   5704    184    143    654  A    C  
ATOM    513  CD2 LEU A  74     -29.863  28.685 -18.419  1.00 45.96      A    C  
ANISOU  513  CD2 LEU A  74     5132   6489   5838    178    148    628  A    C  
ATOM    514  N   LYS A  75     -34.229  31.008 -16.292  1.00 46.62      A    N  
ANISOU  514  N   LYS A  75     5147   6641   5921    251    149    545  A    N  
ATOM    515  CA  LYS A  75     -34.934  32.156 -15.676  1.00 50.43      A    C  
ANISOU  515  CA  LYS A  75     5614   7131   6414    289    136    513  A    C  
ATOM    516  C   LYS A  75     -34.700  32.322 -14.188  1.00 53.32      A    C  
ANISOU  516  C   LYS A  75     5984   7513   6762    315    136    479  A    C  
ATOM    517  O   LYS A  75     -35.127  33.286 -13.625  1.00 51.82      A    O  
ANISOU  517  O   LYS A  75     5781   7327   6578    354    118    445  A    O  
ATOM    518  CB  LYS A  75     -36.454  32.024 -15.889  1.00 49.01      A    C  
ANISOU  518  CB  LYS A  75     5406   6993   6220    295    148    511  A    C  
ATOM    519  CG  LYS A  75     -36.981  30.670 -15.475  1.00 48.54      A    C  
ANISOU  519  CG  LYS A  75     5337   6979   6123    270    177    526  A    C  
ATOM    520  CD  LYS A  75     -38.502  30.565 -15.655  1.00 49.74      A    C  
ANISOU  520  CD  LYS A  75     5456   7175   6267    275    189    529  A    C  
ATOM    521  CE  LYS A  75     -39.068  29.605 -14.662  1.00 45.93      A    C  
ANISOU  521  CE  LYS A  75     4955   6747   5750    265    214    538  A    C  
ATOM    522  NZ  LYS A  75     -38.992  28.255 -15.224  1.00 45.37      A    N1+
ANISOU  522  NZ  LYS A  75     4887   6670   5678    219    220    574  A    N1+
ATOM    523  N   TRP A  76     -34.073  31.362 -13.526  1.00 54.76      A    N  
ANISOU  523  N   TRP A  76     6179   7707   6917    296    152    487  A    N  
ATOM    524  CA  TRP A  76     -33.788  31.469 -12.077  1.00 53.92      A    C  
ANISOU  524  CA  TRP A  76     6078   7620   6788    323    152    456  A    C  
ATOM    525  C   TRP A  76     -32.958  32.688 -11.707  1.00 58.32      A    C  
ANISOU  525  C   TRP A  76     6648   8132   7379    355    115    423  A    C  
ATOM    526  O   TRP A  76     -31.970  33.023 -12.367  1.00 59.66      A    O  
ANISOU  526  O   TRP A  76     6834   8247   7588    340     94    439  A    O  
ATOM    527  CB  TRP A  76     -33.002  30.258 -11.572  1.00 51.42      A    C  
ANISOU  527  CB  TRP A  76     5779   7311   6446    293    171    476  A    C  
ATOM    528  CG  TRP A  76     -33.760  29.010 -11.601  1.00 50.33      A    C  
ANISOU  528  CG  TRP A  76     5627   7216   6279    263    200    506  A    C  
ATOM    529  CD1 TRP A  76     -35.044  28.818 -12.089  1.00 47.21      A    C  
ANISOU  529  CD1 TRP A  76     5203   6854   5878    257    212    520  A    C  
ATOM    530  CD2 TRP A  76     -33.317  27.744 -11.171  1.00 44.77      A    C  
ANISOU  530  CD2 TRP A  76     4933   6524   5553    232    215    530  A    C  
ATOM    531  CE2 TRP A  76     -34.371  26.834 -11.402  1.00 46.99      A    C  
ANISOU  531  CE2 TRP A  76     5190   6842   5821    207    232    559  A    C  
ATOM    532  CE3 TRP A  76     -32.130  27.279 -10.622  1.00 45.92      A    C  
ANISOU  532  CE3 TRP A  76     5104   6650   5692    222    211    530  A    C  
ATOM    533  NE1 TRP A  76     -35.410  27.522 -11.954  1.00 44.34      A    N  
ANISOU  533  NE1 TRP A  76     4830   6519   5495    224    231    552  A    N  
ATOM    534  CZ2 TRP A  76     -34.278  25.515 -11.090  1.00 47.30      A    C  
ANISOU  534  CZ2 TRP A  76     5230   6896   5846    173    243    591  A    C  
ATOM    535  CZ3 TRP A  76     -32.041  25.956 -10.313  1.00 44.70      A    C  
ANISOU  535  CZ3 TRP A  76     4952   6512   5518    189    225    559  A    C  
ATOM    536  CH2 TRP A  76     -33.096  25.089 -10.533  1.00 45.26      A    C  
ANISOU  536  CH2 TRP A  76     4999   6617   5580    165    240    590  A    C  
ATOM    537  N   ASP A  77     -33.363  33.319 -10.615  1.00 52.99      A    N  
ANISOU  537  N   ASP A  77     5964   7484   6687    403    103    379  A    N  
ATOM    538  CA  ASP A  77     -32.617  34.367  -9.963  1.00 54.15      A    C  
ANISOU  538  CA  ASP A  77     6122   7590   6860    442     61    338  A    C  
ATOM    539  C   ASP A  77     -33.049  34.336  -8.512  1.00 53.81      A    C  
ANISOU  539  C   ASP A  77     6069   7608   6766    488     67    294  A    C  
ATOM    540  O   ASP A  77     -33.863  33.499  -8.121  1.00 53.80      A    O  
ANISOU  540  O   ASP A  77     6051   7677   6713    484    107    309  A    O  
ATOM    541  CB  ASP A  77     -32.837  35.741 -10.614  1.00 58.26      A    C  
ANISOU  541  CB  ASP A  77     6634   8063   7438    466     16    321  A    C  
ATOM    542  CG  ASP A  77     -34.312  36.211 -10.600  1.00 54.61      A    C  
ANISOU  542  CG  ASP A  77     6143   7646   6958    501     19    296  A    C  
ATOM    543  OD1 ASP A  77     -35.227  35.610 -10.008  1.00 61.44      A    O  
ANISOU  543  OD1 ASP A  77     6990   8584   7769    514     53    289  A    O  
ATOM    544  OD2 ASP A  77     -34.549  37.221 -11.234  1.00 62.68      A    O1-
ANISOU  544  OD2 ASP A  77     7157   8628   8028    516    -15    288  A    O1-
ATOM    545  N   LEU A  78     -32.511  35.217  -7.687  1.00 57.92      A    N  
ANISOU  545  N   LEU A  78     6600   8106   7301    536     27    245  A    N  
ATOM    546  CA  LEU A  78     -32.799  35.092  -6.259  1.00 54.01      A    C  
ANISOU  546  CA  LEU A  78     6097   7677   6745    586     34    204  A    C  
ATOM    547  C   LEU A  78     -34.298  35.226  -5.969  1.00 53.81      A    C  
ANISOU  547  C   LEU A  78     6036   7731   6676    624     54    186  A    C  
ATOM    548  O   LEU A  78     -34.851  34.413  -5.225  1.00 51.51      A    O  
ANISOU  548  O   LEU A  78     5728   7523   6320    629     96    198  A    O  
ATOM    549  CB  LEU A  78     -31.962  36.073  -5.464  1.00 58.16      A    C  
ANISOU  549  CB  LEU A  78     6640   8161   7296    637    -21    145  A    C  
ATOM    550  CG  LEU A  78     -30.457  35.862  -5.595  1.00 58.46      A    C  
ANISOU  550  CG  LEU A  78     6709   8128   7372    601    -39    164  A    C  
ATOM    551  CD1 LEU A  78     -29.732  36.918  -4.774  1.00 58.86      A    C  
ANISOU  551  CD1 LEU A  78     6772   8135   7455    657   -105    102  A    C  
ATOM    552  CD2 LEU A  78     -30.025  34.475  -5.120  1.00 58.09      A    C  
ANISOU  552  CD2 LEU A  78     6674   8123   7273    565      8    198  A    C  
ATOM    553  N   GLU A  79     -34.979  36.149  -6.648  1.00 53.16      A    N  
ANISOU  553  N   GLU A  79     5940   7627   6631    643     29    169  A    N  
ATOM    554  CA  GLU A  79     -36.391  36.360  -6.348  1.00 58.93      A    C  
ANISOU  554  CA  GLU A  79     6634   8435   7320    685     45    148  A    C  
ATOM    555  C   GLU A  79     -37.205  35.094  -6.668  1.00 55.07      A    C  
ANISOU  555  C   GLU A  79     6123   8011   6791    636    108    209  A    C  
ATOM    556  O   GLU A  79     -37.933  34.522  -5.803  1.00 55.33      A    O  
ANISOU  556  O   GLU A  79     6127   8136   6759    656    144    213  A    O  
ATOM    557  CB  GLU A  79     -36.935  37.576  -7.128  1.00 70.22      A    C  
ANISOU  557  CB  GLU A  79     8054   9820   8806    709      3    121  A    C  
ATOM    558  CG  GLU A  79     -38.233  38.142  -6.527  1.00 74.48      A    C  
ANISOU  558  CG  GLU A  79     8556  10434   9305    780      1     73  A    C  
ATOM    559  CD  GLU A  79     -39.141  38.861  -7.537  1.00 83.72      A    C  
ANISOU  559  CD  GLU A  79     9709  11582  10517    782    -17     72  A    C  
ATOM    560  OE1 GLU A  79     -38.603  39.501  -8.480  1.00 68.50      A    O  
ANISOU  560  OE1 GLU A  79     7801   9564   8662    759    -56     82  A    O  
ATOM    561  OE2 GLU A  79     -40.400  38.803  -7.367  1.00 80.59      A    O1-
ANISOU  561  OE2 GLU A  79     9276  11263  10080    810      8     64  A    O1-
ATOM    562  N   TYR A  80     -37.048  34.623  -7.907  1.00 53.14      A    N  
ANISOU  562  N   TYR A  80     5887   7717   6584    572    119    260  A    N  
ATOM    563  CA  TYR A  80     -37.746  33.433  -8.340  1.00 49.99      A    C  
ANISOU  563  CA  TYR A  80     5470   7362   6161    523    166    317  A    C  
ATOM    564  C   TYR A  80     -37.436  32.275  -7.429  1.00 50.40      A    C  
ANISOU  564  C   TYR A  80     5523   7463   6163    504    199    342  A    C  
ATOM    565  O   TYR A  80     -38.327  31.525  -7.029  1.00 54.89      A    O  
ANISOU  565  O   TYR A  80     6058   8106   6689    496    235    371  A    O  
ATOM    566  CB  TYR A  80     -37.429  33.095  -9.783  1.00 51.44      A    C  
ANISOU  566  CB  TYR A  80     5671   7483   6391    463    165    359  A    C  
ATOM    567  CG  TYR A  80     -38.129  31.867 -10.267  1.00 54.37      A    C  
ANISOU  567  CG  TYR A  80     6023   7891   6744    415    201    411  A    C  
ATOM    568  CD1 TYR A  80     -39.442  31.905 -10.766  1.00 56.56      A    C  
ANISOU  568  CD1 TYR A  80     6267   8203   7019    417    212    421  A    C  
ATOM    569  CD2 TYR A  80     -37.508  30.650 -10.194  1.00 50.42      A    C  
ANISOU  569  CD2 TYR A  80     5538   7387   6232    370    221    449  A    C  
ATOM    570  CE1 TYR A  80     -40.076  30.745 -11.215  1.00 54.13      A    C  
ANISOU  570  CE1 TYR A  80     5941   7921   6703    371    240    469  A    C  
ATOM    571  CE2 TYR A  80     -38.133  29.502 -10.626  1.00 48.02      A    C  
ANISOU  571  CE2 TYR A  80     5218   7109   5920    325    245    495  A    C  
ATOM    572  CZ  TYR A  80     -39.400  29.528 -11.145  1.00 51.14      A    C  
ANISOU  572  CZ  TYR A  80     5579   7533   6316    324    253    507  A    C  
ATOM    573  OH  TYR A  80     -39.933  28.321 -11.569  1.00 47.36      A    O  
ANISOU  573  OH  TYR A  80     5084   7070   5838    278    269    554  A    O  
ATOM    574  N   LEU A  81     -36.206  32.167  -6.975  1.00 49.35      A    N  
ANISOU  574  N   LEU A  81     5421   7294   6034    500    186    333  A    N  
ATOM    575  CA  LEU A  81     -35.890  31.023  -6.097  1.00 49.39      A    C  
ANISOU  575  CA  LEU A  81     5428   7346   5992    480    216    362  A    C  
ATOM    576  C   LEU A  81     -36.358  31.253  -4.666  1.00 51.53      A    C  
ANISOU  576  C   LEU A  81     5675   7702   6201    543    227    330  A    C  
ATOM    577  O   LEU A  81     -36.702  30.301  -3.927  1.00 47.59      A    O  
ANISOU  577  O   LEU A  81     5154   7276   5650    532    262    367  A    O  
ATOM    578  CB  LEU A  81     -34.366  30.672  -6.093  1.00 48.05      A    C  
ANISOU  578  CB  LEU A  81     5301   7110   5845    452    202    368  A    C  
ATOM    579  CG  LEU A  81     -33.724  30.180  -7.403  1.00 48.03      A    C  
ANISOU  579  CG  LEU A  81     5321   7037   5890    391    198    406  A    C  
ATOM    580  CD1 LEU A  81     -32.197  30.190  -7.307  1.00 49.40      A    C  
ANISOU  580  CD1 LEU A  81     5532   7149   6088    380    177    398  A    C  
ATOM    581  CD2 LEU A  81     -34.227  28.799  -7.819  1.00 43.82      A    C  
ANISOU  581  CD2 LEU A  81     4775   6530   5342    337    231    463  A    C  
ATOM    582  N   GLN A  82     -36.246  32.471  -4.181  1.00 54.96      A    N  
ANISOU  582  N   GLN A  82     6114   8131   6638    609    191    264  A    N  
ATOM    583  CA  GLN A  82     -36.751  32.681  -2.819  1.00 58.80      A    C  
ANISOU  583  CA  GLN A  82     6574   8711   7056    679    200    229  A    C  
ATOM    584  C   GLN A  82     -38.231  32.313  -2.779  1.00 59.02      A    C  
ANISOU  584  C   GLN A  82     6549   8834   7042    684    241    260  A    C  
ATOM    585  O   GLN A  82     -38.682  31.674  -1.876  1.00 56.40      A    O  
ANISOU  585  O   GLN A  82     6187   8595   6646    697    275    284  A    O  
ATOM    586  CB  GLN A  82     -36.612  34.111  -2.419  1.00 68.70      A    C  
ANISOU  586  CB  GLN A  82     7834   9944   8322    757    147    146  A    C  
ATOM    587  CG  GLN A  82     -37.068  34.294  -0.998  1.00 71.93      A    C  
ANISOU  587  CG  GLN A  82     8218  10459   8653    838    154    104  A    C  
ATOM    588  CD  GLN A  82     -36.565  35.580  -0.406  1.00 71.90      A    C  
ANISOU  588  CD  GLN A  82     8232  10423   8663    920     89     14  A    C  
ATOM    589  NE2 GLN A  82     -37.366  36.162   0.440  1.00 84.88      A    N  
ANISOU  589  NE2 GLN A  82     9845  12152  10251   1006     83    -40  A    N  
ATOM    590  OE1 GLN A  82     -35.487  36.041  -0.699  1.00 73.05      A    O  
ANISOU  590  OE1 GLN A  82     8417  10469   8868    908     44     -8  A    O  
ATOM    591  N   GLU A  83     -38.925  32.677  -3.840  1.00 60.33      A    N  
ANISOU  591  N   GLU A  83     6704   8970   7248    666    234    266  A    N  
ATOM    592  CA  GLU A  83     -40.341  32.462  -3.975  1.00 65.29      A    C  
ANISOU  592  CA  GLU A  83     7281   9674   7850    670    266    292  A    C  
ATOM    593  C   GLU A  83     -40.697  30.964  -4.093  1.00 66.24      A    C  
ANISOU  593  C   GLU A  83     7380   9833   7953    600    313    378  A    C  
ATOM    594  O   GLU A  83     -41.719  30.517  -3.601  1.00 62.58      A    O  
ANISOU  594  O   GLU A  83     6867   9466   7444    608    348    411  A    O  
ATOM    595  CB  GLU A  83     -40.795  33.235  -5.232  1.00 63.81      A    C  
ANISOU  595  CB  GLU A  83     7097   9424   7724    662    241    277  A    C  
ATOM    596  CG  GLU A  83     -42.269  33.271  -5.472  1.00 77.54      A    C  
ANISOU  596  CG  GLU A  83     8785  11230   9445    674    262    291  A    C  
ATOM    597  CD  GLU A  83     -42.947  34.093  -4.406  1.00 82.87      A    C  
ANISOU  597  CD  GLU A  83     9427  11993  10067    765    257    233  A    C  
ATOM    598  OE1 GLU A  83     -42.374  35.145  -4.038  1.00 83.17      A    O  
ANISOU  598  OE1 GLU A  83     9488  11994  10115    824    212    162  A    O  
ATOM    599  OE2 GLU A  83     -44.010  33.660  -3.924  1.00 86.75      A    O1-
ANISOU  599  OE2 GLU A  83     9865  12587  10506    780    296    260  A    O1-
ATOM    600  N   ASN A  84     -39.848  30.165  -4.715  1.00 61.32      A    N  
ANISOU  600  N   ASN A  84     6791   9140   7367    531    313    417  A    N  
ATOM    601  CA  ASN A  84     -40.258  28.803  -5.089  1.00 58.14      A    C  
ANISOU  601  CA  ASN A  84     6369   8754   6965    462    343    494  A    C  
ATOM    602  C   ASN A  84     -39.484  27.647  -4.518  1.00 57.48      A    C  
ANISOU  602  C   ASN A  84     6300   8674   6865    422    357    538  A    C  
ATOM    603  O   ASN A  84     -39.964  26.498  -4.628  1.00 55.59      A    O  
ANISOU  603  O   ASN A  84     6035   8460   6625    369    379    605  A    O  
ATOM    604  CB  ASN A  84     -40.262  28.667  -6.611  1.00 61.61      A    C  
ANISOU  604  CB  ASN A  84     6827   9112   7470    410    327    512  A    C  
ATOM    605  CG  ASN A  84     -41.347  29.489  -7.240  1.00 69.23      A    C  
ANISOU  605  CG  ASN A  84     7764  10088   8450    435    321    491  A    C  
ATOM    606  ND2 ASN A  84     -40.986  30.628  -7.825  1.00 70.67      A    N  
ANISOU  606  ND2 ASN A  84     7973  10209   8668    463    287    441  A    N  
ATOM    607  OD1 ASN A  84     -42.510  29.108  -7.172  1.00 66.68      A    O  
ANISOU  607  OD1 ASN A  84     7396   9831   8109    430    344    523  A    O  
ATOM    608  N   ILE A  85     -38.334  27.914  -3.887  1.00 56.07      A    N  
ANISOU  608  N   ILE A  85     6157   8469   6675    444    342    504  A    N  
ATOM    609  CA  ILE A  85     -37.382  26.837  -3.559  1.00 58.60      A    C  
ANISOU  609  CA  ILE A  85     6503   8768   6993    400    347    543  A    C  
ATOM    610  C   ILE A  85     -37.783  26.084  -2.271  1.00 68.59      A    C  
ANISOU  610  C   ILE A  85     7732  10134   8193    409    379    584  A    C  
ATOM    611  O   ILE A  85     -37.177  25.070  -1.874  1.00 69.49      A    O  
ANISOU  611  O   ILE A  85     7857  10246   8299    371    387    626  A    O  
ATOM    612  CB  ILE A  85     -35.913  27.357  -3.607  1.00 50.49      A    C  
ANISOU  612  CB  ILE A  85     5531   7659   5992    411    315    495  A    C  
ATOM    613  CG1 ILE A  85     -34.958  26.190  -3.861  1.00 59.05      A    C  
ANISOU  613  CG1 ILE A  85     6645   8693   7096    348    315    537  A    C  
ATOM    614  CG2 ILE A  85     -35.506  28.140  -2.374  1.00 53.74      A    C  
ANISOU  614  CG2 ILE A  85     5949   8107   6360    482    303    440  A    C  
ATOM    615  CD1 ILE A  85     -33.517  26.612  -4.154  1.00 58.76      A    C  
ANISOU  615  CD1 ILE A  85     6660   8571   7096    347    283    501  A    C  
ATOM    616  N   GLY A  86     -38.828  26.551  -1.618  1.00 69.53      A    N  
ANISOU  616  N   GLY A  86     7803  10349   8264    460    400    576  A    N  
ATOM    617  CA  GLY A  86     -39.308  25.871  -0.436  1.00 63.68      A    C  
ANISOU  617  CA  GLY A  86     7017   9722   7454    477    435    622  A    C  
ATOM    618  C   GLY A  86     -38.680  26.340   0.848  1.00 61.78      A    C  
ANISOU  618  C   GLY A  86     6791   9528   7154    543    430    577  A    C  
ATOM    619  O   GLY A  86     -38.012  27.346   0.884  1.00 55.69      A    O  
ANISOU  619  O   GLY A  86     6060   8703   6394    588    397    500  A    O  
ATOM    620  N   ASN A  87     -38.907  25.594   1.913  1.00 63.77      A    N  
ANISOU  620  N   ASN A  87     7008   9877   7345    545    463    632  A    N  
ATOM    621  CA  ASN A  87     -38.383  25.991   3.195  1.00 71.12      A    C  
ANISOU  621  CA  ASN A  87     7941  10874   8206    614    464    597  A    C  
ATOM    622  C   ASN A  87     -37.438  25.022   3.845  1.00 68.95      A    C  
ANISOU  622  C   ASN A  87     7692  10586   7919    578    467    639  A    C  
ATOM    623  O   ASN A  87     -37.338  24.975   5.044  1.00 72.78      A    O  
ANISOU  623  O   ASN A  87     8166  11152   8334    629    478    633  A    O  
ATOM    624  CB  ASN A  87     -39.499  26.334   4.152  1.00 79.28      A    C  
ANISOU  624  CB  ASN A  87     8905  12060   9156    675    500    615  A    C  
ATOM    625  CG  ASN A  87     -39.280  27.660   4.812  1.00 89.21      A    C  
ANISOU  625  CG  ASN A  87    10170  13372  10353    785    483    522  A    C  
ATOM    626  ND2 ASN A  87     -39.048  28.676   4.010  1.00 98.42      A    N  
ANISOU  626  ND2 ASN A  87    11381  14446  11565    818    436    430  A    N  
ATOM    627  OD1 ASN A  87     -39.339  27.776   6.041  1.00 88.77      A    O  
ANISOU  627  OD1 ASN A  87    10080  13437  10212    841    506    533  A    O  
ATOM    628  N   GLY A  88     -36.718  24.272   3.045  1.00 68.44      A    N  
ANISOU  628  N   GLY A  88     7664  10418   7921    497    453    672  A    N  
ATOM    629  CA  GLY A  88     -35.673  23.439   3.568  1.00 62.35      A    C  
ANISOU  629  CA  GLY A  88     6928   9611   7148    467    445    693  A    C  
ATOM    630  C   GLY A  88     -34.547  24.313   4.033  1.00 61.01      A    C  
ANISOU  630  C   GLY A  88     6804   9412   6963    530    415    606  A    C  
ATOM    631  O   GLY A  88     -34.523  25.487   3.756  1.00 59.23      A    O  
ANISOU  631  O   GLY A  88     6594   9160   6751    583    390    528  A    O  
ATOM    632  N   ASP A  89     -33.617  23.719   4.755  1.00 63.96      A    N  
ANISOU  632  N   ASP A  89     7201   9789   7312    524    413    622  A    N  
ATOM    633  CA  ASP A  89     -32.326  24.366   5.099  1.00 65.41      A    C  
ANISOU  633  CA  ASP A  89     7439   9911   7501    563    376    547  A    C  
ATOM    634  C   ASP A  89     -31.316  24.334   3.951  1.00 59.34      A    C  
ANISOU  634  C   ASP A  89     6723   9002   6820    506    344    529  A    C  
ATOM    635  O   ASP A  89     -31.146  23.306   3.299  1.00 54.99      A    O  
ANISOU  635  O   ASP A  89     6179   8406   6308    431    351    589  A    O  
ATOM    636  CB  ASP A  89     -31.664  23.631   6.215  1.00 59.43      A    C  
ANISOU  636  CB  ASP A  89     6688   9198   6694    568    384    575  A    C  
ATOM    637  CG  ASP A  89     -32.287  23.901   7.549  1.00 63.39      A    C  
ANISOU  637  CG  ASP A  89     7147   9840   7097    646    407    570  A    C  
ATOM    638  OD1 ASP A  89     -33.021  24.880   7.706  1.00 63.89      A    O  
ANISOU  638  OD1 ASP A  89     7186   9957   7129    715    407    519  A    O  
ATOM    639  OD2 ASP A  89     -31.983  23.114   8.448  1.00 59.96      A    O1-
ANISOU  639  OD2 ASP A  89     6707   9460   6614    643    422    617  A    O1-
ATOM    640  N   PHE A  90     -30.599  25.425   3.773  1.00 55.84      A    N  
ANISOU  640  N   PHE A  90     6315   8495   6406    546    306    450  A    N  
ATOM    641  CA  PHE A  90     -29.509  25.493   2.764  1.00 53.76      A    C  
ANISOU  641  CA  PHE A  90     6098   8106   6220    501    276    434  A    C  
ATOM    642  C   PHE A  90     -28.170  25.688   3.417  1.00 57.66      A    C  
ANISOU  642  C   PHE A  90     6632   8560   6714    524    245    394  A    C  
ATOM    643  O   PHE A  90     -28.016  26.628   4.225  1.00 56.34      A    O  
ANISOU  643  O   PHE A  90     6468   8418   6519    598    222    329  A    O  
ATOM    644  CB  PHE A  90     -29.762  26.623   1.815  1.00 49.36      A    C  
ANISOU  644  CB  PHE A  90     5545   7495   5715    516    251    389  A    C  
ATOM    645  CG  PHE A  90     -30.890  26.360   0.909  1.00 50.79      A    C  
ANISOU  645  CG  PHE A  90     5694   7690   5912    481    275    430  A    C  
ATOM    646  CD1 PHE A  90     -32.220  26.529   1.361  1.00 54.24      A    C  
ANISOU  646  CD1 PHE A  90     6082   8225   6299    517    301    438  A    C  
ATOM    647  CD2 PHE A  90     -30.664  25.932  -0.389  1.00 50.23      A    C  
ANISOU  647  CD2 PHE A  90     5639   7542   5903    415    272    461  A    C  
ATOM    648  CE1 PHE A  90     -33.287  26.262   0.510  1.00 54.15      A    C  
ANISOU  648  CE1 PHE A  90     6041   8226   6307    481    323    479  A    C  
ATOM    649  CE2 PHE A  90     -31.730  25.662  -1.231  1.00 53.22      A    C  
ANISOU  649  CE2 PHE A  90     5988   7934   6296    385    290    497  A    C  
ATOM    650  CZ  PHE A  90     -33.040  25.838  -0.778  1.00 56.77      A    C  
ANISOU  650  CZ  PHE A  90     6391   8474   6703    416    315    506  A    C  
ATOM    651  N   SER A  91     -27.206  24.832   3.062  1.00 52.65      A    N  
ANISOU  651  N   SER A  91     6028   7863   6114    465    240    426  A    N  
ATOM    652  CA  SER A  91     -25.818  25.067   3.508  1.00 55.84      A    C  
ANISOU  652  CA  SER A  91     6473   8212   6531    481    207    386  A    C  
ATOM    653  C   SER A  91     -25.236  26.260   2.813  1.00 48.91      A    C  
ANISOU  653  C   SER A  91     5616   7249   5716    500    166    327  A    C  
ATOM    654  O   SER A  91     -25.126  26.307   1.584  1.00 46.49      A    O  
ANISOU  654  O   SER A  91     5316   6876   5468    455    162    343  A    O  
ATOM    655  CB  SER A  91     -24.906  23.856   3.335  1.00 51.18      A    C  
ANISOU  655  CB  SER A  91     5907   7578   5960    419    211    433  A    C  
ATOM    656  OG  SER A  91     -25.484  22.698   3.937  1.00 56.28      A    O  
ANISOU  656  OG  SER A  91     6529   8296   6556    395    244    497  A    O  
ATOM    657  N   VAL A  92     -24.880  27.240   3.626  1.00 48.12      A    N  
ANISOU  657  N   VAL A  92     5525   7154   5603    568    133    261  A    N  
ATOM    658  CA  VAL A  92     -24.265  28.459   3.180  1.00 51.46      A    C  
ANISOU  658  CA  VAL A  92     5967   7496   6090    593     83    204  A    C  
ATOM    659  C   VAL A  92     -22.935  28.598   3.904  1.00 58.17      A    C  
ANISOU  659  C   VAL A  92     6848   8304   6948    614     44    167  A    C  
ATOM    660  O   VAL A  92     -22.898  28.624   5.149  1.00 61.53      A    O  
ANISOU  660  O   VAL A  92     7275   8789   7315    669     38    136  A    O  
ATOM    661  CB  VAL A  92     -25.126  29.686   3.519  1.00 50.51      A    C  
ANISOU  661  CB  VAL A  92     5825   7411   5955    668     60    144  A    C  
ATOM    662  CG1 VAL A  92     -24.411  30.946   3.088  1.00 54.77      A    C  
ANISOU  662  CG1 VAL A  92     6383   7856   6571    691     -1     88  A    C  
ATOM    663  CG2 VAL A  92     -26.465  29.619   2.821  1.00 48.92      A    C  
ANISOU  663  CG2 VAL A  92     5589   7252   5745    652     95    176  A    C  
ATOM    664  N   TYR A  93     -21.861  28.695   3.105  1.00 57.00      A    N  
ANISOU  664  N   TYR A  93     6724   8059   6873    571     19    174  A    N  
ATOM    665  CA  TYR A  93     -20.480  28.900   3.585  1.00 50.13      A    C  
ANISOU  665  CA  TYR A  93     5884   7131   6030    582    -21    143  A    C  
ATOM    666  C   TYR A  93     -20.191  30.383   3.621  1.00 52.97      A    C  
ANISOU  666  C   TYR A  93     6247   7436   6443    635    -83     77  A    C  
ATOM    667  O   TYR A  93     -20.545  31.147   2.713  1.00 47.67      A    O  
ANISOU  667  O   TYR A  93     5562   6723   5824    627    -98     75  A    O  
ATOM    668  CB  TYR A  93     -19.447  28.164   2.680  1.00 51.81      A    C  
ANISOU  668  CB  TYR A  93     6116   7274   6294    509    -14    190  A    C  
ATOM    669  CG  TYR A  93     -19.561  26.671   2.831  1.00 48.60      A    C  
ANISOU  669  CG  TYR A  93     5711   6913   5841    464     31    247  A    C  
ATOM    670  CD1 TYR A  93     -18.840  25.959   3.851  1.00 47.36      A    C  
ANISOU  670  CD1 TYR A  93     5572   6774   5644    470     30    246  A    C  
ATOM    671  CD2 TYR A  93     -20.477  25.987   2.071  1.00 45.80      A    C  
ANISOU  671  CD2 TYR A  93     5338   6587   5476    422     72    297  A    C  
ATOM    672  CE1 TYR A  93     -19.037  24.592   4.032  1.00 45.02      A    C  
ANISOU  672  CE1 TYR A  93     5275   6520   5308    431     69    303  A    C  
ATOM    673  CE2 TYR A  93     -20.692  24.643   2.239  1.00 50.14      A    C  
ANISOU  673  CE2 TYR A  93     5886   7176   5988    384    107    350  A    C  
ATOM    674  CZ  TYR A  93     -19.966  23.951   3.215  1.00 49.76      A    C  
ANISOU  674  CZ  TYR A  93     5856   7143   5907    387    105    354  A    C  
ATOM    675  OH  TYR A  93     -20.223  22.642   3.282  1.00 57.00      A    O  
ANISOU  675  OH  TYR A  93     6768   8091   6798    343    133    412  A    O  
ATOM    676  N   SER A  94     -19.489  30.767   4.663  1.00 56.87      A    N  
ANISOU  676  N   SER A  94     6757   7924   6928    686   -125     24  A    N  
ATOM    677  CA  SER A  94     -19.154  32.127   4.928  1.00 60.95      A    C  
ANISOU  677  CA  SER A  94     7277   8387   7493    743   -196    -46  A    C  
ATOM    678  C   SER A  94     -17.644  32.240   4.984  1.00 55.59      A    C  
ANISOU  678  C   SER A  94     6623   7622   6875    726   -241    -55  A    C  
ATOM    679  O   SER A  94     -17.016  31.448   5.651  1.00 62.61      A    O  
ANISOU  679  O   SER A  94     7529   8532   7726    720   -229    -47  A    O  
ATOM    680  CB  SER A  94     -19.727  32.462   6.311  1.00 68.24      A    C  
ANISOU  680  CB  SER A  94     8194   9393   8339    835   -212   -111  A    C  
ATOM    681  OG  SER A  94     -19.713  33.849   6.506  1.00 66.99      A    O  
ANISOU  681  OG  SER A  94     8034   9191   8226    901   -285   -187  A    O  
ATOM    682  N   ALA A  95     -17.037  33.205   4.325  1.00 57.69      A    N  
ANISOU  682  N   ALA A  95     6888   7794   7235    718   -296    -68  A    N  
ATOM    683  CA  ALA A  95     -15.602  33.455   4.573  1.00 56.58      A    C  
ANISOU  683  CA  ALA A  95     6767   7575   7155    713   -350    -84  A    C  
ATOM    684  C   ALA A  95     -15.175  34.909   4.413  1.00 58.66      A    C  
ANISOU  684  C   ALA A  95     7024   7749   7514    745   -437   -130  A    C  
ATOM    685  O   ALA A  95     -15.828  35.676   3.739  1.00 61.16      A    O  
ANISOU  685  O   ALA A  95     7321   8045   7870    747   -451   -130  A    O  
ATOM    686  CB  ALA A  95     -14.760  32.596   3.661  1.00 56.37      A    C  
ANISOU  686  CB  ALA A  95     6746   7510   7160    629   -314    -12  A    C  
ATOM    687  N   SER A  96     -14.050  35.262   5.031  1.00 59.94      A    N  
ANISOU  687  N   SER A  96     7201   7854   7719    765   -498   -167  A    N  
ATOM    688  CA  SER A  96     -13.429  36.537   4.789  1.00 66.51      A    C  
ANISOU  688  CA  SER A  96     8026   8583   8660    780   -587   -195  A    C  
ATOM    689  C   SER A  96     -12.270  36.460   3.791  1.00 66.13      A    C  
ANISOU  689  C   SER A  96     7972   8453   8703    703   -594   -126  A    C  
ATOM    690  O   SER A  96     -11.532  37.406   3.704  1.00 79.82      A    O  
ANISOU  690  O   SER A  96     9698  10097  10532    709   -671   -141  A    O  
ATOM    691  CB  SER A  96     -12.948  37.144   6.110  1.00 71.30      A    C  
ANISOU  691  CB  SER A  96     8648   9172   9267    861   -667   -286  A    C  
ATOM    692  OG  SER A  96     -12.045  36.249   6.741  1.00 80.04      A    O  
ANISOU  692  OG  SER A  96     9778  10295  10338    848   -648   -278  A    O  
ATOM    693  N   THR A  97     -12.145  35.382   3.023  1.00 63.52      A    N  
ANISOU  693  N   THR A  97     7641   8149   8343    634   -518    -52  A    N  
ATOM    694  CA  THR A  97     -11.223  35.306   1.890  1.00 55.46      A    C  
ANISOU  694  CA  THR A  97     6606   7066   7399    561   -513     20  A    C  
ATOM    695  C   THR A  97     -12.013  34.904   0.665  1.00 53.40      A    C  
ANISOU  695  C   THR A  97     6328   6842   7120    515   -447     83  A    C  
ATOM    696  O   THR A  97     -13.060  34.355   0.806  1.00 56.17      A    O  
ANISOU  696  O   THR A  97     6684   7267   7390    526   -395     76  A    O  
ATOM    697  CB  THR A  97     -10.136  34.245   2.093  1.00 58.70      A    C  
ANISOU  697  CB  THR A  97     7033   7480   7788    524   -484     51  A    C  
ATOM    698  CG2 THR A  97     -10.714  32.898   2.000  1.00 59.43      A    C  
ANISOU  698  CG2 THR A  97     7147   7666   7769    524   -411     52  A    C  
ATOM    699  OG1 THR A  97      -9.156  34.358   1.068  1.00 52.58      A    O  
ANISOU  699  OG1 THR A  97     6240   6674   7063    456   -458    128  A    O  
ATOM    700  N   HIS A  98     -11.512  35.157  -0.533  1.00 52.57      A    N  
ANISOU  700  N   HIS A  98     6201   6687   7083    463   -448    145  A    N  
ATOM    701  CA  HIS A  98     -12.230  34.740  -1.762  1.00 51.80      A    C  
ANISOU  701  CA  HIS A  98     6088   6626   6966    421   -386    205  A    C  
ATOM    702  C   HIS A  98     -12.233  33.201  -1.939  1.00 51.46      A    C  
ANISOU  702  C   HIS A  98     6059   6647   6844    385   -310    239  A    C  
ATOM    703  O   HIS A  98     -13.085  32.646  -2.629  1.00 49.40      A    O  
ANISOU  703  O   HIS A  98     5794   6434   6541    363   -256    270  A    O  
ATOM    704  CB  HIS A  98     -11.665  35.424  -3.001  1.00 55.91      A    C  
ANISOU  704  CB  HIS A  98     6578   7087   7578    380   -409    268  A    C  
ATOM    705  CG  HIS A  98     -10.193  35.231  -3.182  1.00 60.42      A    C  
ANISOU  705  CG  HIS A  98     7143   7615   8198    346   -425    305  A    C  
ATOM    706  CD2 HIS A  98      -9.497  34.481  -4.066  1.00 59.30      A    C  
ANISOU  706  CD2 HIS A  98     6991   7486   8054    296   -381    371  A    C  
ATOM    707  ND1 HIS A  98      -9.253  35.885  -2.407  1.00 60.11      A    N  
ANISOU  707  ND1 HIS A  98     7105   7513   8220    367   -496    273  A    N  
ATOM    708  CE1 HIS A  98      -8.042  35.543  -2.815  1.00 60.42      A    C  
ANISOU  708  CE1 HIS A  98     7135   7527   8295    327   -493    323  A    C  
ATOM    709  NE2 HIS A  98      -8.164  34.655  -3.784  1.00 58.23      A    N  
ANISOU  709  NE2 HIS A  98     6850   7299   7974    288   -421    380  A    N  
ATOM    710  N   LYS A  99     -11.335  32.508  -1.251  1.00 50.89      A    N  
ANISOU  710  N   LYS A  99     6008   6575   6752    382   -308    230  A    N  
ATOM    711  CA  LYS A  99     -11.161  31.061  -1.473  1.00 51.71      A    C  
ANISOU  711  CA  LYS A  99     6125   6725   6796    345   -246    265  A    C  
ATOM    712  C   LYS A  99     -11.978  30.215  -0.562  1.00 52.98      A    C  
ANISOU  712  C   LYS A  99     6306   6956   6867    367   -211    237  A    C  
ATOM    713  O   LYS A  99     -11.690  30.157   0.612  1.00 54.31      A    O  
ANISOU  713  O   LYS A  99     6491   7131   7010    401   -232    194  A    O  
ATOM    714  CB  LYS A  99      -9.694  30.642  -1.313  1.00 50.73      A    C  
ANISOU  714  CB  LYS A  99     6009   6566   6699    325   -262    278  A    C  
ATOM    715  CG  LYS A  99      -8.832  31.143  -2.475  1.00 58.94      A    C  
ANISOU  715  CG  LYS A  99     7021   7554   7818    288   -278    332  A    C  
ATOM    716  CD  LYS A  99      -7.376  30.734  -2.341  1.00 64.39      A    C  
ANISOU  716  CD  LYS A  99     7714   8214   8534    269   -291    348  A    C  
ATOM    717  CE  LYS A  99      -6.659  31.447  -1.222  1.00 70.61      A    C  
ANISOU  717  CE  LYS A  99     8511   8950   9365    303   -358    299  A    C  
ATOM    718  NZ  LYS A  99      -5.813  32.566  -1.745  1.00 82.52      A    N1+
ANISOU  718  NZ  LYS A  99     9987  10386  10979    290   -414    328  A    N1+
ATOM    719  N   PHE A 100     -12.929  29.468  -1.144  1.00 50.05      A    N  
ANISOU  719  N   PHE A 100     5931   6636   6449    343   -157    268  A    N  
ATOM    720  CA  PHE A 100     -13.762  28.510  -0.408  1.00 46.67      A    C  
ANISOU  720  CA  PHE A 100     5515   6280   5937    353   -117    260  A    C  
ATOM    721  C   PHE A 100     -13.224  27.086  -0.567  1.00 43.57      A    C  
ANISOU  721  C   PHE A 100     5137   5903   5515    311    -83    297  A    C  
ATOM    722  O   PHE A 100     -13.787  26.244  -1.285  1.00 43.86      A    O  
ANISOU  722  O   PHE A 100     5167   5969   5527    278    -43    335  A    O  
ATOM    723  CB  PHE A 100     -15.200  28.612  -0.927  1.00 50.17      A    C  
ANISOU  723  CB  PHE A 100     5938   6767   6354    354    -87    272  A    C  
ATOM    724  CG  PHE A 100     -15.886  29.833  -0.459  1.00 53.80      A    C  
ANISOU  724  CG  PHE A 100     6387   7227   6824    407   -120    225  A    C  
ATOM    725  CD1 PHE A 100     -15.689  31.049  -1.113  1.00 53.04      A    C  
ANISOU  725  CD1 PHE A 100     6277   7073   6802    413   -161    218  A    C  
ATOM    726  CD2 PHE A 100     -16.662  29.800   0.692  1.00 54.07      A    C  
ANISOU  726  CD2 PHE A 100     6424   7323   6795    454   -115    186  A    C  
ATOM    727  CE1 PHE A 100     -16.283  32.207  -0.674  1.00 51.20      A    C  
ANISOU  727  CE1 PHE A 100     6034   6832   6585    465   -202    170  A    C  
ATOM    728  CE2 PHE A 100     -17.269  30.963   1.148  1.00 57.78      A    C  
ANISOU  728  CE2 PHE A 100     6884   7797   7273    512   -151    133  A    C  
ATOM    729  CZ  PHE A 100     -17.066  32.172   0.489  1.00 58.14      A    C  
ANISOU  729  CZ  PHE A 100     6918   7773   7397    518   -198    121  A    C  
ATOM    730  N   LEU A 101     -12.079  26.852   0.013  1.00 45.45      A    N  
ANISOU  730  N   LEU A 101     5391   6113   5763    313   -105    285  A    N  
ATOM    731  CA  LEU A 101     -11.537  25.485   0.173  1.00 44.86      A    C  
ANISOU  731  CA  LEU A 101     5335   6054   5655    284    -81    310  A    C  
ATOM    732  C   LEU A 101     -12.538  24.508   0.765  1.00 40.13      A    C  
ANISOU  732  C   LEU A 101     4741   5523   4982    283    -44    318  A    C  
ATOM    733  O   LEU A 101     -13.007  24.684   1.884  1.00 45.24      A    O  
ANISOU  733  O   LEU A 101     5393   6208   5588    321    -48    290  A    O  
ATOM    734  CB  LEU A 101     -10.325  25.493   1.103  1.00 37.91      A    C  
ANISOU  734  CB  LEU A 101     4474   5145   4785    299   -114    282  A    C  
ATOM    735  CG  LEU A 101      -9.444  24.234   1.157  1.00 43.21      A    C  
ANISOU  735  CG  LEU A 101     5163   5812   5440    268   -101    305  A    C  
ATOM    736  CD1 LEU A 101      -8.877  23.865  -0.232  1.00 43.50      A    C  
ANISOU  736  CD1 LEU A 101     5188   5822   5516    225    -88    347  A    C  
ATOM    737  CD2 LEU A 101      -8.279  24.419   2.151  1.00 43.04      A    C  
ANISOU  737  CD2 LEU A 101     5159   5759   5433    291   -141    272  A    C  
ATOM    738  N   TYR A 102     -12.874  23.466   0.004  1.00 42.91      A    N  
ANISOU  738  N   TYR A 102     5091   5892   5320    242    -10    362  A    N  
ATOM    739  CA  TYR A 102     -13.737  22.397   0.508  1.00 49.96      A    C  
ANISOU  739  CA  TYR A 102     5985   6842   6154    232     19    383  A    C  
ATOM    740  C   TYR A 102     -13.026  21.624   1.618  1.00 51.75      A    C  
ANISOU  740  C   TYR A 102     6234   7077   6349    236     11    379  A    C  
ATOM    741  O   TYR A 102     -11.863  21.242   1.458  1.00 44.09      A    O  
ANISOU  741  O   TYR A 102     5280   6066   5406    220     -3    380  A    O  
ATOM    742  CB  TYR A 102     -14.142  21.411  -0.595  1.00 50.36      A    C  
ANISOU  742  CB  TYR A 102     6029   6898   6208    186     44    427  A    C  
ATOM    743  CG  TYR A 102     -15.126  20.411  -0.073  1.00 52.16      A    C  
ANISOU  743  CG  TYR A 102     6252   7179   6386    174     68    454  A    C  
ATOM    744  CD1 TYR A 102     -16.484  20.768   0.078  1.00 56.07      A    C  
ANISOU  744  CD1 TYR A 102     6724   7724   6855    189     87    460  A    C  
ATOM    745  CD2 TYR A 102     -14.715  19.142   0.347  1.00 52.13      A    C  
ANISOU  745  CD2 TYR A 102     6263   7179   6364    150     68    479  A    C  
ATOM    746  CE1 TYR A 102     -17.404  19.885   0.601  1.00 54.78      A    C  
ANISOU  746  CE1 TYR A 102     6550   7615   6648    176    110    493  A    C  
ATOM    747  CE2 TYR A 102     -15.632  18.232   0.874  1.00 51.00      A    C  
ANISOU  747  CE2 TYR A 102     6111   7085   6180    135     87    514  A    C  
ATOM    748  CZ  TYR A 102     -16.976  18.609   0.987  1.00 59.54      A    C  
ANISOU  748  CZ  TYR A 102     7165   8218   7237    147    108    524  A    C  
ATOM    749  OH  TYR A 102     -17.912  17.733   1.470  1.00 60.70      A    O  
ANISOU  749  OH  TYR A 102     7296   8417   7350    130    126    568  A    O  
ATOM    750  N   TYR A 103     -13.747  21.351   2.699  1.00 46.90      A    N  
ANISOU  750  N   TYR A 103     5618   6522   5679    258     23    377  A    N  
ATOM    751  CA  TYR A 103     -13.301  20.381   3.704  1.00 49.74      A    C  
ANISOU  751  CA  TYR A 103     5995   6903   6000    255     23    389  A    C  
ATOM    752  C   TYR A 103     -14.384  19.396   4.193  1.00 53.83      A    C  
ANISOU  752  C   TYR A 103     6499   7490   6463    242     54    434  A    C  
ATOM    753  O   TYR A 103     -15.570  19.735   4.247  1.00 49.06      A    O  
ANISOU  753  O   TYR A 103     5872   6937   5832    256     74    441  A    O  
ATOM    754  CB  TYR A 103     -12.692  21.110   4.889  1.00 57.06      A    C  
ANISOU  754  CB  TYR A 103     6935   7833   6912    308     -5    341  A    C  
ATOM    755  CG  TYR A 103     -13.603  22.095   5.492  1.00 56.14      A    C  
ANISOU  755  CG  TYR A 103     6802   7764   6763    361     -5    308  A    C  
ATOM    756  CD1 TYR A 103     -13.700  23.376   4.982  1.00 55.86      A    C  
ANISOU  756  CD1 TYR A 103     6758   7695   6770    385    -26    271  A    C  
ATOM    757  CD2 TYR A 103     -14.367  21.753   6.583  1.00 61.84      A    C  
ANISOU  757  CD2 TYR A 103     7516   8568   7412    390     12    315  A    C  
ATOM    758  CE1 TYR A 103     -14.548  24.309   5.545  1.00 66.00      A    C  
ANISOU  758  CE1 TYR A 103     8027   9023   8027    441    -33    233  A    C  
ATOM    759  CE2 TYR A 103     -15.233  22.670   7.164  1.00 67.69      A    C  
ANISOU  759  CE2 TYR A 103     8238   9363   8116    448     12    280  A    C  
ATOM    760  CZ  TYR A 103     -15.323  23.944   6.657  1.00 72.72      A    C  
ANISOU  760  CZ  TYR A 103     8869   9962   8797    476    -12    235  A    C  
ATOM    761  OH  TYR A 103     -16.193  24.837   7.253  1.00 83.24      A    O  
ANISOU  761  OH  TYR A 103    10184  11349  10094    539    -19    195  A    O  
ATOM    762  N   ASP A 104     -13.969  18.157   4.489  1.00 48.75      A    N  
ANISOU  762  N   ASP A 104     5869   6846   5806    210     54    469  A    N  
ATOM    763  CA  ASP A 104     -14.870  17.107   4.976  1.00 49.96      A    C  
ANISOU  763  CA  ASP A 104     6007   7058   5917    189     77    524  A    C  
ATOM    764  C   ASP A 104     -14.904  17.107   6.522  1.00 50.46      A    C  
ANISOU  764  C   ASP A 104     6071   7185   5917    229     79    521  A    C  
ATOM    765  O   ASP A 104     -13.937  16.697   7.231  1.00 46.67      A    O  
ANISOU  765  O   ASP A 104     5615   6691   5427    234     61    514  A    O  
ATOM    766  CB  ASP A 104     -14.416  15.757   4.421  1.00 47.35      A    C  
ANISOU  766  CB  ASP A 104     5688   6688   5613    134     69    564  A    C  
ATOM    767  CG  ASP A 104     -15.297  14.575   4.866  1.00 55.16      A    C  
ANISOU  767  CG  ASP A 104     6659   7725   6572    103     84    630  A    C  
ATOM    768  OD1 ASP A 104     -16.125  14.740   5.789  1.00 55.37      A    O  
ANISOU  768  OD1 ASP A 104     6663   7825   6547    126    104    650  A    O  
ATOM    769  OD2 ASP A 104     -15.142  13.466   4.268  1.00 49.94      A    O1-
ANISOU  769  OD2 ASP A 104     6002   7028   5942     57     70    665  A    O1-
ATOM    770  N   GLU A 105     -16.050  17.525   7.041  1.00 49.28      A    N  
ANISOU  770  N   GLU A 105     5893   7112   5720    260    103    528  A    N  
ATOM    771  CA  GLU A 105     -16.232  17.707   8.488  1.00 47.41      A    C  
ANISOU  771  CA  GLU A 105     5649   6952   5411    312    108    521  A    C  
ATOM    772  C   GLU A 105     -16.067  16.400   9.217  1.00 43.62      A    C  
ANISOU  772  C   GLU A 105     5171   6503   4899    283    112    581  A    C  
ATOM    773  O   GLU A 105     -15.595  16.396  10.318  1.00 49.11      A    O  
ANISOU  773  O   GLU A 105     5877   7232   5550    319    104    569  A    O  
ATOM    774  CB  GLU A 105     -17.587  18.379   8.783  1.00 51.96      A    C  
ANISOU  774  CB  GLU A 105     6188   7613   5941    352    134    520  A    C  
ATOM    775  CG  GLU A 105     -17.589  19.854   8.392  1.00 56.80      A    C  
ANISOU  775  CG  GLU A 105     6804   8198   6579    398    116    446  A    C  
ATOM    776  CD  GLU A 105     -18.950  20.493   8.387  1.00 62.84      A    C  
ANISOU  776  CD  GLU A 105     7531   9031   7312    430    140    443  A    C  
ATOM    777  OE1 GLU A 105     -19.786  20.109   9.218  1.00 67.84      A    O  
ANISOU  777  OE1 GLU A 105     8137   9762   7877    450    167    479  A    O  
ATOM    778  OE2 GLU A 105     -19.185  21.400   7.575  1.00 54.95      A    O1-
ANISOU  778  OE2 GLU A 105     6529   7993   6354    439    131    408  A    O1-
ATOM    779  N   LYS A 106     -16.354  15.267   8.589  1.00 50.57      A    N  
ANISOU  779  N   LYS A 106     6043   7363   5807    219    121    645  A    N  
ATOM    780  CA  LYS A 106     -16.216  13.982   9.308  1.00 51.49      A    C  
ANISOU  780  CA  LYS A 106     6159   7504   5899    189    120    710  A    C  
ATOM    781  C   LYS A 106     -14.770  13.641   9.513  1.00 51.91      A    C  
ANISOU  781  C   LYS A 106     6253   7494   5975    184     87    683  A    C  
ATOM    782  O   LYS A 106     -14.469  12.897  10.388  1.00 54.11      A    O  
ANISOU  782  O   LYS A 106     6537   7799   6223    180     81    718  A    O  
ATOM    783  CB  LYS A 106     -16.920  12.846   8.599  1.00 54.83      A    C  
ANISOU  783  CB  LYS A 106     6561   7916   6356    122    125    784  A    C  
ATOM    784  CG  LYS A 106     -18.422  13.149   8.397  1.00 66.72      A    C  
ANISOU  784  CG  LYS A 106     8020   9488   7841    124    158    816  A    C  
ATOM    785  CD  LYS A 106     -19.194  12.102   7.595  1.00 75.73      A    C  
ANISOU  785  CD  LYS A 106     9137  10610   9024     57    158    886  A    C  
ATOM    786  CE  LYS A 106     -18.797  12.107   6.116  1.00 89.12      A    C  
ANISOU  786  CE  LYS A 106    10856  12211  10794     27    136    850  A    C  
ATOM    787  NZ  LYS A 106     -19.084  10.831   5.383  1.00 97.87      A    N1+
ANISOU  787  NZ  LYS A 106    11955  13275  11952    -36    115    907  A    N1+
ATOM    788  N   LYS A 107     -13.869  14.214   8.726  1.00 49.37      A    N  
ANISOU  788  N   LYS A 107     5958   7092   5705    186     65    625  A    N  
ATOM    789  CA  LYS A 107     -12.450  13.949   8.895  1.00 48.42      A    C  
ANISOU  789  CA  LYS A 107     5875   6911   5609    184     33    598  A    C  
ATOM    790  C   LYS A 107     -11.738  14.910   9.871  1.00 45.89      A    C  
ANISOU  790  C   LYS A 107     5571   6604   5259    247     18    536  A    C  
ATOM    791  O   LYS A 107     -10.519  14.777  10.102  1.00 51.22      A    O  
ANISOU  791  O   LYS A 107     6276   7231   5954    250    -10    509  A    O  
ATOM    792  CB  LYS A 107     -11.762  13.938   7.512  1.00 42.40      A    C  
ANISOU  792  CB  LYS A 107     5128   6061   4921    150     16    575  A    C  
ATOM    793  CG  LYS A 107     -12.047  12.661   6.713  1.00 43.98      A    C  
ANISOU  793  CG  LYS A 107     5322   6235   5152     91     14    629  A    C  
ATOM    794  CD  LYS A 107     -11.593  12.762   5.278  1.00 41.55      A    C  
ANISOU  794  CD  LYS A 107     5022   5859   4904     69      3    604  A    C  
ATOM    795  CE  LYS A 107     -11.760  11.464   4.559  1.00 43.23      A    C  
ANISOU  795  CE  LYS A 107     5233   6042   5146     20    -10    646  A    C  
ATOM    796  NZ  LYS A 107     -11.376  11.582   3.109  1.00 48.59      A    N1+
ANISOU  796  NZ  LYS A 107     5917   6668   5876      8    -19    619  A    N1+
ATOM    797  N   MET A 108     -12.444  15.903  10.393  1.00 52.37      A    N  
ANISOU  797  N   MET A 108     6375   7485   6039    300     30    507  A    N  
ATOM    798  CA  MET A 108     -11.770  16.944  11.210  1.00 57.59      A    C  
ANISOU  798  CA  MET A 108     7053   8148   6681    366      5    437  A    C  
ATOM    799  C   MET A 108     -11.358  16.445  12.603  1.00 64.65      A    C  
ANISOU  799  C   MET A 108     7958   9092   7512    396     -3    445  A    C  
ATOM    800  O   MET A 108     -10.384  16.914  13.184  1.00 62.85      A    O  
ANISOU  800  O   MET A 108     7755   8838   7286    435    -36    391  A    O  
ATOM    801  CB  MET A 108     -12.681  18.148  11.380  1.00 63.54      A    C  
ANISOU  801  CB  MET A 108     7784   8952   7407    423     13    397  A    C  
ATOM    802  CG  MET A 108     -12.878  18.946  10.104  1.00 63.33      A    C  
ANISOU  802  CG  MET A 108     7750   8866   7446    407     10    372  A    C  
ATOM    803  SD  MET A 108     -14.021  20.306  10.375  1.00 64.98      A    S  
ANISOU  803  SD  MET A 108     7930   9136   7620    475     16    327  A    S  
ATOM    804  CE  MET A 108     -13.082  21.449  11.403  1.00 63.97      A    C  
ANISOU  804  CE  MET A 108     7826   8993   7485    557    -36    235  A    C  
ATOM    805  N   ALA A 109     -12.105  15.487  13.133  1.00 68.42      A    N  
ANISOU  805  N   ALA A 109     8414   9641   7939    378     23    517  A    N  
ATOM    806  CA  ALA A 109     -11.751  14.878  14.409  1.00 71.51      A    C  
ANISOU  806  CA  ALA A 109     8813  10085   8269    400     18    539  A    C  
ATOM    807  C   ALA A 109     -10.320  14.370  14.417  1.00 69.53      A    C  
ANISOU  807  C   ALA A 109     8602   9755   8059    378    -16    523  A    C  
ATOM    808  O   ALA A 109      -9.596  14.597  15.384  1.00 71.75      A    O  
ANISOU  808  O   ALA A 109     8903  10049   8308    423    -39    488  A    O  
ATOM    809  CB  ALA A 109     -12.715  13.745  14.731  1.00 71.67      A    C  
ANISOU  809  CB  ALA A 109     8801  10181   8248    363     51    639  A    C  
ATOM    810  N   ASN A 110      -9.903  13.713  13.333  1.00 69.18      A    N  
ANISOU  810  N   ASN A 110     8569   9628   8086    313    -25    545  A    N  
ATOM    811  CA  ASN A 110      -8.487  13.255  13.174  1.00 67.38      A    C  
ANISOU  811  CA  ASN A 110     8377   9318   7905    291    -60    525  A    C  
ATOM    812  C   ASN A 110      -7.406  14.293  12.881  1.00 61.14      A    C  
ANISOU  812  C   ASN A 110     7610   8459   7160    321    -91    443  A    C  
ATOM    813  O   ASN A 110      -6.213  13.971  12.853  1.00 56.59      A    O  
ANISOU  813  O   ASN A 110     7060   7823   6618    309   -120    426  A    O  
ATOM    814  CB  ASN A 110      -8.406  12.223  12.057  1.00 63.97      A    C  
ANISOU  814  CB  ASN A 110     7947   8825   7531    218    -61    569  A    C  
ATOM    815  CG  ASN A 110      -9.156  10.959  12.403  1.00 71.88      A    C  
ANISOU  815  CG  ASN A 110     8930   9872   8506    179    -47    656  A    C  
ATOM    816  ND2 ASN A 110      -9.830  10.393  11.431  1.00 64.41      A    N  
ANISOU  816  ND2 ASN A 110     7968   8907   7597    129    -37    697  A    N  
ATOM    817  OD1 ASN A 110      -9.126  10.494  13.547  1.00 77.83      A    O  
ANISOU  817  OD1 ASN A 110     9685  10679   9208    194    -48    688  A    O  
ATOM    818  N   PHE A 111      -7.817  15.511  12.569  1.00 58.80      A    N  
ANISOU  818  N   PHE A 111     7301   8166   6872    354    -88    398  A    N  
ATOM    819  CA  PHE A 111      -6.854  16.555  12.289  1.00 62.67      A    C  
ANISOU  819  CA  PHE A 111     7807   8588   7414    380   -123    328  A    C  
ATOM    820  C   PHE A 111      -7.264  17.775  13.076  1.00 59.53      A    C  
ANISOU  820  C   PHE A 111     7402   8237   6979    454   -134    273  A    C  
ATOM    821  O   PHE A 111      -7.682  18.782  12.525  1.00 58.46      A    O  
ANISOU  821  O   PHE A 111     7252   8087   6871    470   -135    242  A    O  
ATOM    822  CB  PHE A 111      -6.757  16.833  10.763  1.00 56.19      A    C  
ANISOU  822  CB  PHE A 111     6979   7701   6670    339   -118    328  A    C  
ATOM    823  CG  PHE A 111      -6.066  15.750  10.011  1.00 51.02      A    C  
ANISOU  823  CG  PHE A 111     6336   6994   6055    280   -121    363  A    C  
ATOM    824  CD1 PHE A 111      -6.694  14.528   9.801  1.00 51.77      A    C  
ANISOU  824  CD1 PHE A 111     6423   7112   6132    237    -98    425  A    C  
ATOM    825  CD2 PHE A 111      -4.765  15.936   9.509  1.00 46.31      A    C  
ANISOU  825  CD2 PHE A 111     5754   6323   5517    271   -150    334  A    C  
ATOM    826  CE1 PHE A 111      -6.027  13.502   9.125  1.00 52.78      A    C  
ANISOU  826  CE1 PHE A 111     6563   7190   6298    190   -109    449  A    C  
ATOM    827  CE2 PHE A 111      -4.111  14.927   8.848  1.00 44.05      A    C  
ANISOU  827  CE2 PHE A 111     5477   5995   5262    226   -154    360  A    C  
ATOM    828  CZ  PHE A 111      -4.728  13.707   8.661  1.00 47.92      A    C  
ANISOU  828  CZ  PHE A 111     5964   6508   5733    188   -136    413  A    C  
ATOM    829  N   GLN A 112      -7.103  17.649  14.383  1.00 65.03      A    N  
ANISOU  829  N   GLN A 112     8107   8986   7612    500   -145    261  A    N  
ATOM    830  CA  GLN A 112      -7.418  18.692  15.374  1.00 67.82      A    C  
ANISOU  830  CA  GLN A 112     8458   9397   7915    585   -163    202  A    C  
ATOM    831  C   GLN A 112      -6.837  20.049  15.024  1.00 63.99      A    C  
ANISOU  831  C   GLN A 112     7979   8839   7493    619   -208    123  A    C  
ATOM    832  O   GLN A 112      -7.448  21.089  15.314  1.00 68.69      A    O  
ANISOU  832  O   GLN A 112     8561   9468   8070    678   -221     75  A    O  
ATOM    833  CB  GLN A 112      -6.867  18.259  16.742  1.00 83.25      A    C  
ANISOU  833  CB  GLN A 112    10429  11395   9805    626   -180    194  A    C  
ATOM    834  CG  GLN A 112      -7.878  18.272  17.884  1.00 99.48      A    C  
ANISOU  834  CG  GLN A 112    12464  13579  11754    687   -157    205  A    C  
ATOM    835  CD  GLN A 112      -9.030  17.306  17.663  1.00 98.86      A    C  
ANISOU  835  CD  GLN A 112    12355  13570  11636    640   -100    298  A    C  
ATOM    836  NE2 GLN A 112     -10.249  17.785  17.872  1.00106.70      A    N  
ANISOU  836  NE2 GLN A 112    13314  14650  12575    678    -71    303  A    N  
ATOM    837  OE1 GLN A 112      -8.828  16.151  17.307  1.00 91.41      A    O  
ANISOU  837  OE1 GLN A 112    11415  12601  10714    571    -84    367  A    O  
ATOM    838  N   ASN A 113      -5.649  20.065  14.420  1.00 64.69      A    N  
ANISOU  838  N   ASN A 113     8086   8831   7660    584   -238    110  A    N  
ATOM    839  CA  ASN A 113      -5.032  21.335  14.038  1.00 70.80      A    C  
ANISOU  839  CA  ASN A 113     8861   9530   8507    609   -287     47  A    C  
ATOM    840  C   ASN A 113      -5.482  21.934  12.694  1.00 66.99      A    C  
ANISOU  840  C   ASN A 113     8358   9005   8090    574   -274     57  A    C  
ATOM    841  O   ASN A 113      -4.902  22.918  12.272  1.00 63.09      A    O  
ANISOU  841  O   ASN A 113     7861   8441   7667    584   -314     18  A    O  
ATOM    842  CB  ASN A 113      -3.503  21.228  14.097  1.00 76.49      A    C  
ANISOU  842  CB  ASN A 113     9605  10171   9283    596   -330     26  A    C  
ATOM    843  CG  ASN A 113      -2.976  21.148  15.531  1.00 84.65      A    C  
ANISOU  843  CG  ASN A 113    10661  11238  10264    654   -363    -12  A    C  
ATOM    844  ND2 ASN A 113      -1.673  20.936  15.655  1.00 83.43      A    N  
ANISOU  844  ND2 ASN A 113    10526  11018  10152    642   -399    -27  A    N  
ATOM    845  OD1 ASN A 113      -3.722  21.291  16.514  1.00 82.89      A    O  
ANISOU  845  OD1 ASN A 113    10435  11097   9959    713   -357    -30  A    O  
ATOM    846  N   PHE A 114      -6.508  21.369  12.041  1.00 61.21      A    N  
ANISOU  846  N   PHE A 114     7607   8313   7335    535   -221    112  A    N  
ATOM    847  CA  PHE A 114      -7.041  21.951  10.809  1.00 57.19      A    C  
ANISOU  847  CA  PHE A 114     7077   7773   6878    508   -209    122  A    C  
ATOM    848  C   PHE A 114      -8.044  23.038  11.159  1.00 61.73      A    C  
ANISOU  848  C   PHE A 114     7634   8391   7428    567   -215     82  A    C  
ATOM    849  O   PHE A 114      -9.067  22.757  11.816  1.00 58.66      A    O  
ANISOU  849  O   PHE A 114     7235   8092   6961    595   -186     93  A    O  
ATOM    850  CB  PHE A 114      -7.767  20.926   9.939  1.00 55.52      A    C  
ANISOU  850  CB  PHE A 114     6853   7585   6656    446   -156    193  A    C  
ATOM    851  CG  PHE A 114      -8.406  21.552   8.691  1.00 58.70      A    C  
ANISOU  851  CG  PHE A 114     7232   7963   7105    424   -141    201  A    C  
ATOM    852  CD1 PHE A 114      -7.610  22.176   7.725  1.00 54.64      A    C  
ANISOU  852  CD1 PHE A 114     6717   7370   6672    403   -166    190  A    C  
ATOM    853  CD2 PHE A 114      -9.796  21.565   8.504  1.00 61.45      A    C  
ANISOU  853  CD2 PHE A 114     7558   8372   7416    425   -105    224  A    C  
ATOM    854  CE1 PHE A 114      -8.163  22.768   6.592  1.00 55.67      A    C  
ANISOU  854  CE1 PHE A 114     6825   7481   6842    385   -154    202  A    C  
ATOM    855  CE2 PHE A 114     -10.360  22.152   7.353  1.00 59.88      A    C  
ANISOU  855  CE2 PHE A 114     7341   8150   7260    407    -95    230  A    C  
ATOM    856  CZ  PHE A 114      -9.546  22.766   6.411  1.00 58.27      A    C  
ANISOU  856  CZ  PHE A 114     7137   7868   7135    388   -120    219  A    C  
ATOM    857  N   LYS A 115      -7.774  24.271  10.726  1.00 66.32      A    N  
ANISOU  857  N   LYS A 115     8210   8912   8075    588   -256     36  A    N  
ATOM    858  CA  LYS A 115      -8.668  25.382  11.059  1.00 63.83      A    C  
ANISOU  858  CA  LYS A 115     7879   8628   7743    650   -274    -11  A    C  
ATOM    859  C   LYS A 115      -9.263  25.958   9.821  1.00 64.66      A    C  
ANISOU  859  C   LYS A 115     7961   8702   7902    620   -263      6  A    C  
ATOM    860  O   LYS A 115      -8.634  26.781   9.158  1.00 63.63      A    O  
ANISOU  860  O   LYS A 115     7828   8491   7855    609   -302    -10  A    O  
ATOM    861  CB  LYS A 115      -7.970  26.466  11.890  1.00 71.15      A    C  
ANISOU  861  CB  LYS A 115     8818   9519   8694    720   -348    -92  A    C  
ATOM    862  CG  LYS A 115      -7.850  26.047  13.349  1.00 87.85      A    C  
ANISOU  862  CG  LYS A 115    10950  11703  10725    776   -356   -122  A    C  
ATOM    863  CD  LYS A 115      -9.218  25.670  13.972  1.00 98.29      A    C  
ANISOU  863  CD  LYS A 115    12255  13148  11940    812   -307   -106  A    C  
ATOM    864  CE  LYS A 115      -9.141  24.498  14.960  1.00 99.57      A    C  
ANISOU  864  CE  LYS A 115    12429  13388  12014    816   -275    -72  A    C  
ATOM    865  NZ  LYS A 115      -8.141  24.786  16.026  1.00104.35      A    N1+
ANISOU  865  NZ  LYS A 115    13059  13979  12610    873   -333   -132  A    N1+
ATOM    866  N   PRO A 116     -10.507  25.555   9.517  1.00 64.30      A    N  
ANISOU  866  N   PRO A 116     7898   8723   7809    605   -209     43  A    N  
ATOM    867  CA  PRO A 116     -11.112  25.935   8.226  1.00 64.28      A    C  
ANISOU  867  CA  PRO A 116     7874   8694   7855    569   -192     69  A    C  
ATOM    868  C   PRO A 116     -11.208  27.429   8.094  1.00 57.08      A    C  
ANISOU  868  C   PRO A 116     6953   7741   6995    614   -243     14  A    C  
ATOM    869  O   PRO A 116     -11.580  28.084   9.034  1.00 61.91      A    O  
ANISOU  869  O   PRO A 116     7563   8387   7571    684   -271    -43  A    O  
ATOM    870  CB  PRO A 116     -12.503  25.304   8.273  1.00 70.72      A    C  
ANISOU  870  CB  PRO A 116     8672   9600   8599    563   -135    107  A    C  
ATOM    871  CG  PRO A 116     -12.668  24.678   9.629  1.00 69.22      A    C  
ANISOU  871  CG  PRO A 116     8488   9490   8322    602   -123    104  A    C  
ATOM    872  CD  PRO A 116     -11.483  24.991  10.474  1.00 72.60      A    C  
ANISOU  872  CD  PRO A 116     8942   9882   8760    639   -174     53  A    C  
ATOM    873  N   ARG A 117     -10.863  27.982   6.950  1.00 61.46      A    N  
ANISOU  873  N   ARG A 117     7498   8221   7634    577   -258     28  A    N  
ATOM    874  CA  ARG A 117     -11.100  29.425   6.735  1.00 62.64      A    C  
ANISOU  874  CA  ARG A 117     7633   8329   7839    616   -309    -17  A    C  
ATOM    875  C   ARG A 117     -12.572  29.782   6.396  1.00 61.80      A    C  
ANISOU  875  C   ARG A 117     7504   8275   7702    632   -280    -15  A    C  
ATOM    876  O   ARG A 117     -12.908  30.949   6.328  1.00 62.93      A    O  
ANISOU  876  O   ARG A 117     7634   8392   7883    672   -324    -57  A    O  
ATOM    877  CB  ARG A 117     -10.167  29.962   5.656  1.00 70.30      A    C  
ANISOU  877  CB  ARG A 117     8595   9202   8913    571   -339      5  A    C  
ATOM    878  CG  ARG A 117      -8.662  29.834   5.992  1.00 78.16      A    C  
ANISOU  878  CG  ARG A 117     9607  10137   9952    561   -378     -1  A    C  
ATOM    879  CD  ARG A 117      -7.944  31.157   5.757  1.00 89.18      A    C  
ANISOU  879  CD  ARG A 117    10991  11443  11451    576   -455    -29  A    C  
ATOM    880  NE  ARG A 117      -8.508  32.190   6.650  1.00 94.23      A    N  
ANISOU  880  NE  ARG A 117    11631  12088  12083    654   -510   -105  A    N  
ATOM    881  CZ  ARG A 117      -8.694  33.472   6.336  1.00 95.43      A    C  
ANISOU  881  CZ  ARG A 117    11766  12185  12308    677   -568   -133  A    C  
ATOM    882  NH1 ARG A 117      -9.206  34.309   7.239  1.00 95.52      A    N1+
ANISOU  882  NH1 ARG A 117    11780  12208  12304    757   -621   -211  A    N1+
ATOM    883  NH2 ARG A 117      -8.372  33.929   5.128  1.00 92.15      A    N  
ANISOU  883  NH2 ARG A 117    11326  11704  11979    626   -577    -82  A    N  
ATOM    884  N   SER A 118     -13.438  28.796   6.158  1.00 54.11      A    N  
ANISOU  884  N   SER A 118     6521   7370   6666    601   -213     33  A    N  
ATOM    885  CA  SER A 118     -14.803  29.075   5.767  1.00 58.59      A    C  
ANISOU  885  CA  SER A 118     7065   7985   7209    611   -185     40  A    C  
ATOM    886  C   SER A 118     -15.687  28.299   6.759  1.00 61.00      A    C  
ANISOU  886  C   SER A 118     7365   8400   7410    640   -142     46  A    C  
ATOM    887  O   SER A 118     -15.240  27.275   7.297  1.00 55.04      A    O  
ANISOU  887  O   SER A 118     6625   7670   6615    621   -121     72  A    O  
ATOM    888  CB  SER A 118     -15.031  28.679   4.299  1.00 51.74      A    C  
ANISOU  888  CB  SER A 118     6186   7091   6381    539   -148    104  A    C  
ATOM    889  OG  SER A 118     -15.194  27.282   4.211  1.00 57.87      A    O  
ANISOU  889  OG  SER A 118     6965   7910   7110    493    -95    158  A    O  
ATOM    890  N   ASN A 119     -16.888  28.832   7.037  1.00 61.71      A    N  
ANISOU  890  N   ASN A 119     7434   8553   7460    687   -135     24  A    N  
ATOM    891  CA  ASN A 119     -17.820  28.281   8.055  1.00 64.80      A    C  
ANISOU  891  CA  ASN A 119     7810   9060   7749    727    -96     28  A    C  
ATOM    892  C   ASN A 119     -19.112  28.005   7.391  1.00 53.27      A    C  
ANISOU  892  C   ASN A 119     6320   7650   6267    700    -47     72  A    C  
ATOM    893  O   ASN A 119     -19.529  28.798   6.581  1.00 62.49      A    O  
ANISOU  893  O   ASN A 119     7477   8783   7484    700    -60     58  A    O  
ATOM    894  CB  ASN A 119     -18.112  29.289   9.161  1.00 66.28      A    C  
ANISOU  894  CB  ASN A 119     7992   9293   7895    828   -138    -54  A    C  
ATOM    895  CG  ASN A 119     -16.867  29.946   9.640  1.00 86.35      A    C  
ANISOU  895  CG  ASN A 119    10562  11762  10483    863   -207   -115  A    C  
ATOM    896  ND2 ASN A 119     -16.628  31.192   9.199  1.00 91.01      A    N  
ANISOU  896  ND2 ASN A 119    11153  12273  11153    886   -269   -168  A    N  
ATOM    897  OD1 ASN A 119     -16.085  29.321  10.361  1.00 87.96      A    O  
ANISOU  897  OD1 ASN A 119    10786  11974  10659    863   -209   -112  A    O  
ATOM    898  N   ARG A 120     -19.745  26.913   7.764  1.00 53.04      A    N  
ANISOU  898  N   ARG A 120     6276   7705   6171    681      6    127  A    N  
ATOM    899  CA  ARG A 120     -21.038  26.523   7.226  1.00 58.24      A    C  
ANISOU  899  CA  ARG A 120     6901   8419   6805    653     54    177  A    C  
ATOM    900  C   ARG A 120     -22.113  26.926   8.197  1.00 62.34      A    C  
ANISOU  900  C   ARG A 120     7389   9050   7244    729     66    151  A    C  
ATOM    901  O   ARG A 120     -22.003  26.619   9.370  1.00 66.12      A    O  
ANISOU  901  O   ARG A 120     7869   9599   7654    771     71    143  A    O  
ATOM    902  CB  ARG A 120     -21.089  25.020   7.050  1.00 58.14      A    C  
ANISOU  902  CB  ARG A 120     6887   8429   6774    582     99    260  A    C  
ATOM    903  CG  ARG A 120     -22.390  24.468   6.488  1.00 58.40      A    C  
ANISOU  903  CG  ARG A 120     6884   8515   6790    546    145    320  A    C  
ATOM    904  CD  ARG A 120     -22.274  22.981   6.247  1.00 57.08      A    C  
ANISOU  904  CD  ARG A 120     6718   8347   6622    473    175    400  A    C  
ATOM    905  NE  ARG A 120     -21.895  22.276   7.469  1.00 59.01      A    N  
ANISOU  905  NE  ARG A 120     6967   8645   6808    487    181    419  A    N  
ATOM    906  CZ  ARG A 120     -22.754  21.858   8.397  1.00 67.62      A    C  
ANISOU  906  CZ  ARG A 120     8024   9845   7822    512    211    456  A    C  
ATOM    907  NH1 ARG A 120     -24.079  22.054   8.268  1.00 72.73      A    N1+
ANISOU  907  NH1 ARG A 120     8629  10563   8443    524    240    476  A    N1+
ATOM    908  NH2 ARG A 120     -22.298  21.248   9.473  1.00 65.72      A    N  
ANISOU  908  NH2 ARG A 120     7789   9650   7530    526    214    474  A    N  
ATOM    909  N   GLU A 121     -23.124  27.624   7.696  1.00 62.66      A    N  
ANISOU  909  N   GLU A 121     7405   9109   7294    748     71    136  A    N  
ATOM    910  CA  GLU A 121     -24.305  27.981   8.439  1.00 60.35      A    C  
ANISOU  910  CA  GLU A 121     7076   8929   6925    817     89    118  A    C  
ATOM    911  C   GLU A 121     -25.519  27.433   7.688  1.00 65.09      A    C  
ANISOU  911  C   GLU A 121     7639   9571   7519    767    141    185  A    C  
ATOM    912  O   GLU A 121     -25.683  27.669   6.478  1.00 53.82      A    O  
ANISOU  912  O   GLU A 121     6214   8074   6160    722    138    196  A    O  
ATOM    913  CB  GLU A 121     -24.397  29.491   8.534  1.00 68.02      A    C  
ANISOU  913  CB  GLU A 121     8049   9875   7919    896     34     25  A    C  
ATOM    914  CG  GLU A 121     -25.604  29.956   9.353  1.00 79.96      A    C  
ANISOU  914  CG  GLU A 121     9521  11512   9348    982     47     -8  A    C  
ATOM    915  CD  GLU A 121     -25.568  31.422   9.748  1.00 78.01      A    C  
ANISOU  915  CD  GLU A 121     9280  11247   9112   1079    -19   -116  A    C  
ATOM    916  OE1 GLU A 121     -24.622  32.160   9.365  1.00 81.76      A    O  
ANISOU  916  OE1 GLU A 121     9788  11606   9671   1077    -81   -164  A    O  
ATOM    917  OE2 GLU A 121     -26.518  31.821  10.431  1.00 74.98      A    O1-
ANISOU  917  OE2 GLU A 121     8863  10967   8656   1158    -12   -150  A    O1-
ATOM    918  N   GLU A 122     -26.358  26.665   8.382  1.00 61.24      A    N  
ANISOU  918  N   GLU A 122     7116   9198   6952    775    189    238  A    N  
ATOM    919  CA  GLU A 122     -27.609  26.226   7.798  1.00 57.26      A    C  
ANISOU  919  CA  GLU A 122     6570   8744   6439    738    233    298  A    C  
ATOM    920  C   GLU A 122     -28.632  27.339   7.927  1.00 63.66      A    C  
ANISOU  920  C   GLU A 122     7350   9613   7225    812    227    244  A    C  
ATOM    921  O   GLU A 122     -28.731  28.005   8.965  1.00 63.89      A    O  
ANISOU  921  O   GLU A 122     7369   9711   7192    903    210    185  A    O  
ATOM    922  CB  GLU A 122     -28.125  24.962   8.460  1.00 61.00      A    C  
ANISOU  922  CB  GLU A 122     7012   9316   6848    710    283    386  A    C  
ATOM    923  CG  GLU A 122     -27.138  23.796   8.404  1.00 59.04      A    C  
ANISOU  923  CG  GLU A 122     6793   9013   6625    639    285    440  A    C  
ATOM    924  CD  GLU A 122     -26.861  23.341   7.005  1.00 62.01      A    C  
ANISOU  924  CD  GLU A 122     7189   9280   7089    552    280    472  A    C  
ATOM    925  OE1 GLU A 122     -27.842  22.909   6.378  1.00 61.87      A    O  
ANISOU  925  OE1 GLU A 122     7140   9285   7082    511    308    525  A    O  
ATOM    926  OE2 GLU A 122     -25.675  23.401   6.546  1.00 62.25      A    O1-
ANISOU  926  OE2 GLU A 122     7265   9209   7176    527    248    445  A    O1-
ATOM    927  N   MET A 123     -29.376  27.583   6.864  1.00 61.55      A    N  
ANISOU  927  N   MET A 123     7067   9316   7002    780    236    258  A    N  
ATOM    928  CA  MET A 123     -30.291  28.689   6.897  1.00 63.38      A    C  
ANISOU  928  CA  MET A 123     7271   9590   7219    851    224    201  A    C  
ATOM    929  C   MET A 123     -31.252  28.541   5.744  1.00 65.37      A    C  
ANISOU  929  C   MET A 123     7498   9829   7511    796    250    247  A    C  
ATOM    930  O   MET A 123     -30.972  27.817   4.778  1.00 55.65      A    O  
ANISOU  930  O   MET A 123     6280   8525   6334    711    261    302  A    O  
ATOM    931  CB  MET A 123     -29.524  30.018   6.831  1.00 62.17      A    C  
ANISOU  931  CB  MET A 123     7153   9352   7114    906    156    103  A    C  
ATOM    932  CG  MET A 123     -29.055  30.378   5.423  1.00 63.91      A    C  
ANISOU  932  CG  MET A 123     7401   9440   7442    843    129    105  A    C  
ATOM    933  SD  MET A 123     -28.004  31.858   5.340  1.00 65.19      A    S  
ANISOU  933  SD  MET A 123     7603   9489   7677    893     42      7  A    S  
ATOM    934  CE  MET A 123     -26.701  31.450   6.489  1.00 67.34      A    C  
ANISOU  934  CE  MET A 123     7906   9758   7918    915     23    -13  A    C  
ATOM    935  N   LYS A 124     -32.385  29.229   5.873  1.00 59.36      A    N  
ANISOU  935  N   LYS A 124     6697   9139   6716    854    257    220  A    N  
ATOM    936  CA  LYS A 124     -33.421  29.252   4.861  1.00 55.24      A    C  
ANISOU  936  CA  LYS A 124     6148   8614   6228    817    277    252  A    C  
ATOM    937  C   LYS A 124     -33.047  30.166   3.713  1.00 52.62      A    C  
ANISOU  937  C   LYS A 124     5847   8161   5986    803    232    207  A    C  
ATOM    938  O   LYS A 124     -32.309  31.144   3.872  1.00 51.05      A    O  
ANISOU  938  O   LYS A 124     5679   7903   5816    849    181    133  A    O  
ATOM    939  CB  LYS A 124     -34.754  29.804   5.453  1.00 61.80      A    C  
ANISOU  939  CB  LYS A 124     6922   9568   6989    895    296    230  A    C  
ATOM    940  CG  LYS A 124     -35.209  29.149   6.757  1.00 64.22      A    C  
ANISOU  940  CG  LYS A 124     7187  10020   7192    933    338    267  A    C  
ATOM    941  CD  LYS A 124     -35.461  27.673   6.512  1.00 67.60      A    C  
ANISOU  941  CD  LYS A 124     7595  10470   7620    839    388    383  A    C  
ATOM    942  CE  LYS A 124     -35.738  26.858   7.769  1.00 69.70      A    C  
ANISOU  942  CE  LYS A 124     7820  10870   7792    861    429    442  A    C  
ATOM    943  NZ  LYS A 124     -35.843  25.429   7.318  1.00 68.57      A    N1+
ANISOU  943  NZ  LYS A 124     7663  10710   7678    754    462    556  A    N1+
ATOM    944  N   PHE A 125     -33.647  29.924   2.552  1.00 49.99      A    N  
ANISOU  944  N   PHE A 125     5502   7793   5698    744    250    250  A    N  
ATOM    945  CA  PHE A 125     -33.157  30.614   1.354  1.00 54.85      A    C  
ANISOU  945  CA  PHE A 125     6149   8289   6401    716    211    224  A    C  
ATOM    946  C   PHE A 125     -33.339  32.104   1.563  1.00 59.15      A    C  
ANISOU  946  C   PHE A 125     6692   8823   6957    798    164    138  A    C  
ATOM    947  O   PHE A 125     -32.458  32.889   1.244  1.00 54.35      A    O  
ANISOU  947  O   PHE A 125     6118   8122   6409    807    112     94  A    O  
ATOM    948  CB  PHE A 125     -33.843  30.104   0.102  1.00 54.72      A    C  
ANISOU  948  CB  PHE A 125     6117   8248   6424    647    237    283  A    C  
ATOM    949  CG  PHE A 125     -33.143  30.504  -1.163  1.00 56.21      A    C  
ANISOU  949  CG  PHE A 125     6340   8319   6697    604    206    277  A    C  
ATOM    950  CD1 PHE A 125     -33.437  31.702  -1.784  1.00 57.69      A    C  
ANISOU  950  CD1 PHE A 125     6526   8466   6928    635    171    232  A    C  
ATOM    951  CD2 PHE A 125     -32.131  29.700  -1.714  1.00 54.81      A    C  
ANISOU  951  CD2 PHE A 125     6194   8075   6554    539    207    317  A    C  
ATOM    952  CE1 PHE A 125     -32.784  32.082  -2.960  1.00 58.90      A    C  
ANISOU  952  CE1 PHE A 125     6704   8515   7156    596    143    237  A    C  
ATOM    953  CE2 PHE A 125     -31.476  30.078  -2.875  1.00 51.30      A    C  
ANISOU  953  CE2 PHE A 125     5775   7535   6181    505    180    316  A    C  
ATOM    954  CZ  PHE A 125     -31.796  31.263  -3.506  1.00 53.39      A    C  
ANISOU  954  CZ  PHE A 125     6036   7762   6487    531    150    280  A    C  
ATOM    955  N   HIS A 126     -34.476  32.485   2.184  1.00 64.98      A    N  
ANISOU  955  N   HIS A 126     7389   9663   7636    864    177    112  A    N  
ATOM    956  CA  HIS A 126     -34.809  33.899   2.383  1.00 58.79      A    C  
ANISOU  956  CA  HIS A 126     6599   8876   6861    950    127     26  A    C  
ATOM    957  C   HIS A 126     -33.765  34.568   3.276  1.00 57.09      A    C  
ANISOU  957  C   HIS A 126     6416   8631   6645   1013     72    -49  A    C  
ATOM    958  O   HIS A 126     -33.380  35.717   3.035  1.00 56.19      A    O  
ANISOU  958  O   HIS A 126     6322   8438   6589   1050      8   -115  A    O  
ATOM    959  CB  HIS A 126     -36.296  34.096   2.889  1.00 63.81      A    C  
ANISOU  959  CB  HIS A 126     7178   9640   7425   1012    157     15  A    C  
ATOM    960  CG  HIS A 126     -36.482  33.935   4.373  1.00 64.38      A    C  
ANISOU  960  CG  HIS A 126     7226   9838   7397   1090    172     -8  A    C  
ATOM    961  CD2 HIS A 126     -36.772  32.847   5.127  1.00 60.98      A    C  
ANISOU  961  CD2 HIS A 126     6767   9515   6888   1077    231     55  A    C  
ATOM    962  ND1 HIS A 126     -36.360  34.990   5.256  1.00 65.88      A    N  
ANISOU  962  ND1 HIS A 126     7419  10055   7556   1198    122   -106  A    N  
ATOM    963  CE1 HIS A 126     -36.529  34.547   6.488  1.00 65.27      A    C  
ANISOU  963  CE1 HIS A 126     7318  10101   7381   1251    151   -104  A    C  
ATOM    964  NE2 HIS A 126     -36.780  33.250   6.434  1.00 62.22      A    N  
ANISOU  964  NE2 HIS A 126     6910   9766   6964   1177    219     -2  A    N  
ATOM    965  N   GLU A 127     -33.288  33.832   4.283  1.00 57.78      A    N  
ANISOU  965  N   GLU A 127     6508   8775   6669   1022     94    -34  A    N  
ATOM    966  CA  GLU A 127     -32.181  34.298   5.130  1.00 62.92      A    C  
ANISOU  966  CA  GLU A 127     7192   9393   7319   1075     42    -98  A    C  
ATOM    967  C   GLU A 127     -30.886  34.499   4.350  1.00 61.88      A    C  
ANISOU  967  C   GLU A 127     7109   9116   7286   1016      1    -98  A    C  
ATOM    968  O   GLU A 127     -30.086  35.422   4.633  1.00 64.27      A    O  
ANISOU  968  O   GLU A 127     7437   9351   7630   1062    -68   -169  A    O  
ATOM    969  CB  GLU A 127     -31.942  33.309   6.292  1.00 65.86      A    C  
ANISOU  969  CB  GLU A 127     7560   9862   7604   1085     82    -69  A    C  
ATOM    970  CG  GLU A 127     -33.197  33.061   7.128  1.00 70.51      A    C  
ANISOU  970  CG  GLU A 127     8093  10609   8087   1143    129    -57  A    C  
ATOM    971  CD  GLU A 127     -33.013  32.064   8.263  1.00 75.20      A    C  
ANISOU  971  CD  GLU A 127     8675  11305   8591   1153    171    -15  A    C  
ATOM    972  OE1 GLU A 127     -33.127  32.485   9.410  1.00 81.98      A    O  
ANISOU  972  OE1 GLU A 127     9520  12255   9373   1251    157    -71  A    O  
ATOM    973  OE2 GLU A 127     -32.757  30.868   8.041  1.00 74.57      A    O1-
ANISOU  973  OE2 GLU A 127     8598  11219   8514   1067    213     72  A    O1-
ATOM    974  N   PHE A 128     -30.668  33.626   3.372  1.00 59.22      A    N  
ANISOU  974  N   PHE A 128     6781   8733   6988    918     37    -19  A    N  
ATOM    975  CA  PHE A 128     -29.468  33.721   2.545  1.00 55.23      A    C  
ANISOU  975  CA  PHE A 128     6314   8100   6570    860      6     -7  A    C  
ATOM    976  C   PHE A 128     -29.534  35.009   1.734  1.00 58.49      A    C  
ANISOU  976  C   PHE A 128     6729   8431   7062    876    -50    -49  A    C  
ATOM    977  O   PHE A 128     -28.566  35.783   1.691  1.00 54.05      A    O  
ANISOU  977  O   PHE A 128     6192   7779   6562    890   -112    -88  A    O  
ATOM    978  CB  PHE A 128     -29.323  32.474   1.624  1.00 55.17      A    C  
ANISOU  978  CB  PHE A 128     6311   8071   6578    758     57     84  A    C  
ATOM    979  CG  PHE A 128     -28.370  32.677   0.473  1.00 55.72      A    C  
ANISOU  979  CG  PHE A 128     6409   8024   6738    700     30    101  A    C  
ATOM    980  CD1 PHE A 128     -27.021  32.903   0.711  1.00 56.47      A    C  
ANISOU  980  CD1 PHE A 128     6536   8048   6870    700    -10     79  A    C  
ATOM    981  CD2 PHE A 128     -28.814  32.630  -0.843  1.00 53.78      A    C  
ANISOU  981  CD2 PHE A 128     6154   7741   6536    648     45    142  A    C  
ATOM    982  CE1 PHE A 128     -26.138  33.070  -0.340  1.00 59.84      A    C  
ANISOU  982  CE1 PHE A 128     6982   8376   7376    647    -31    103  A    C  
ATOM    983  CE2 PHE A 128     -27.931  32.797  -1.889  1.00 56.29      A    C  
ANISOU  983  CE2 PHE A 128     6494   7964   6929    599     22    164  A    C  
ATOM    984  CZ  PHE A 128     -26.592  33.021  -1.640  1.00 59.99      A    C  
ANISOU  984  CZ  PHE A 128     6991   8369   7434    598    -13    147  A    C  
ATOM    985  N   VAL A 129     -30.695  35.263   1.131  1.00 59.40      A    N  
ANISOU  985  N   VAL A 129     6815   8575   7176    878    -32    -38  A    N  
ATOM    986  CA  VAL A 129     -30.858  36.494   0.364  1.00 62.88      A    C  
ANISOU  986  CA  VAL A 129     7256   8942   7691    895    -86    -76  A    C  
ATOM    987  C   VAL A 129     -30.768  37.739   1.238  1.00 63.17      A    C  
ANISOU  987  C   VAL A 129     7294   8971   7733    994   -158   -173  A    C  
ATOM    988  O   VAL A 129     -30.139  38.708   0.851  1.00 61.41      A    O  
ANISOU  988  O   VAL A 129     7089   8649   7595   1002   -227   -205  A    O  
ATOM    989  CB  VAL A 129     -32.188  36.547  -0.393  1.00 62.80      A    C  
ANISOU  989  CB  VAL A 129     7213   8971   7675    885    -54    -50  A    C  
ATOM    990  CG1 VAL A 129     -32.149  37.722  -1.356  1.00 67.64      A    C  
ANISOU  990  CG1 VAL A 129     7831   9490   8379    886   -112    -73  A    C  
ATOM    991  CG2 VAL A 129     -32.422  35.248  -1.154  1.00 68.50      A    C  
ANISOU  991  CG2 VAL A 129     7929   9712   8385    797     14     38  A    C  
ATOM    992  N   GLU A 130     -31.385  37.704   2.413  1.00 68.93      A    N  
ANISOU  992  N   GLU A 130     8005   9807   8376   1071   -147   -216  A    N  
ATOM    993  CA  GLU A 130     -31.242  38.808   3.419  1.00 71.65      A    C  
ANISOU  993  CA  GLU A 130     8353  10157   8713   1178   -221   -321  A    C  
ATOM    994  C   GLU A 130     -29.792  39.053   3.757  1.00 62.48      A    C  
ANISOU  994  C   GLU A 130     7229   8906   7603   1178   -278   -349  A    C  
ATOM    995  O   GLU A 130     -29.324  40.165   3.721  1.00 67.88      A    O  
ANISOU  995  O   GLU A 130     7927   9504   8359   1216   -362   -409  A    O  
ATOM    996  CB  GLU A 130     -32.010  38.484   4.738  1.00 73.79      A    C  
ANISOU  996  CB  GLU A 130     8596  10578   8863   1261   -188   -354  A    C  
ATOM    997  CG  GLU A 130     -33.459  38.974   4.793  1.00 76.53      A    C  
ANISOU  997  CG  GLU A 130     8899  11012   9166   1323   -177   -384  A    C  
ATOM    998  CD  GLU A 130     -34.454  37.945   5.337  1.00 78.08      A    C  
ANISOU  998  CD  GLU A 130     9053  11361   9250   1327    -88   -331  A    C  
ATOM    999  OE1 GLU A 130     -34.198  37.308   6.388  1.00 82.23      A    O  
ANISOU  999  OE1 GLU A 130     9576  11971   9697   1353    -61   -326  A    O  
ATOM   1000  OE2 GLU A 130     -35.525  37.781   4.693  1.00 80.66      A    O1-
ANISOU 1000  OE2 GLU A 130     9348  11727   9572   1300    -48   -291  A    O1-
ATOM   1001  N   LYS A 131     -29.073  37.992   4.074  1.00 63.03      A    N  
ANISOU 1001  N   LYS A 131     7315   8991   7639   1131   -236   -301  A    N  
ATOM   1002  CA  LYS A 131     -27.677  38.135   4.553  1.00 65.54      A    C  
ANISOU 1002  CA  LYS A 131     7669   9236   7994   1135   -287   -329  A    C  
ATOM   1003  C   LYS A 131     -26.827  38.733   3.454  1.00 64.20      A    C  
ANISOU 1003  C   LYS A 131     7519   8926   7947   1078   -337   -310  A    C  
ATOM   1004  O   LYS A 131     -25.913  39.551   3.672  1.00 59.14      A    O  
ANISOU 1004  O   LYS A 131     6897   8198   7373   1104   -417   -359  A    O  
ATOM   1005  CB  LYS A 131     -27.144  36.776   4.953  1.00 62.34      A    C  
ANISOU 1005  CB  LYS A 131     7276   8877   7532   1085   -224   -269  A    C  
ATOM   1006  CG  LYS A 131     -25.885  36.795   5.797  1.00 69.70      A    C  
ANISOU 1006  CG  LYS A 131     8239   9773   8471   1109   -268   -306  A    C  
ATOM   1007  CD  LYS A 131     -25.721  35.431   6.450  1.00 72.24      A    C  
ANISOU 1007  CD  LYS A 131     8564  10178   8706   1082   -200   -255  A    C  
ATOM   1008  CE  LYS A 131     -24.356  35.266   7.109  1.00 81.63      A    C  
ANISOU 1008  CE  LYS A 131     9787  11320   9909   1086   -236   -275  A    C  
ATOM   1009  NZ  LYS A 131     -24.441  35.711   8.518  1.00 91.30      A    N1+
ANISOU 1009  NZ  LYS A 131    11008  12616  11062   1195   -272   -358  A    N1+
ATOM   1010  N   LEU A 132     -27.170  38.315   2.245  1.00 64.60      A    N  
ANISOU 1010  N   LEU A 132     7560   8956   8027    998   -291   -236  A    N  
ATOM   1011  CA  LEU A 132     -26.465  38.744   1.078  1.00 67.64      A    C  
ANISOU 1011  CA  LEU A 132     7957   9225   8518    936   -322   -199  A    C  
ATOM   1012  C   LEU A 132     -26.733  40.221   0.879  1.00 74.05      A    C  
ANISOU 1012  C   LEU A 132     8760   9974   9401    989   -405   -259  A    C  
ATOM   1013  O   LEU A 132     -25.814  41.007   0.656  1.00 66.37      A    O  
ANISOU 1013  O   LEU A 132     7800   8898   8519    985   -477   -275  A    O  
ATOM   1014  CB  LEU A 132     -26.991  37.951  -0.088  1.00 70.21      A    C  
ANISOU 1014  CB  LEU A 132     8270   9566   8839    856   -252   -114  A    C  
ATOM   1015  CG  LEU A 132     -26.200  38.069  -1.356  1.00 74.71      A    C  
ANISOU 1015  CG  LEU A 132     8850  10037   9499    782   -265    -57  A    C  
ATOM   1016  CD1 LEU A 132     -24.750  37.711  -1.067  1.00 79.93      A    C  
ANISOU 1016  CD1 LEU A 132     9536  10646  10184    755   -281    -46  A    C  
ATOM   1017  CD2 LEU A 132     -26.804  37.100  -2.356  1.00 73.69      A    C  
ANISOU 1017  CD2 LEU A 132     8709   9943   9344    713   -190     17  A    C  
ATOM   1018  N   GLN A 133     -28.016  40.579   0.983  1.00 72.52      A    N  
ANISOU 1018  N   GLN A 133     8542   9846   9167   1039   -396   -291  A    N  
ATOM   1019  CA  GLN A 133     -28.461  41.975   0.894  1.00 75.55      A    C  
ANISOU 1019  CA  GLN A 133     8913  10182   9608   1101   -477   -357  A    C  
ATOM   1020  C   GLN A 133     -27.842  42.835   1.932  1.00 73.68      A    C  
ANISOU 1020  C   GLN A 133     8690   9909   9393   1185   -567   -450  A    C  
ATOM   1021  O   GLN A 133     -27.384  43.922   1.614  1.00 72.39      A    O  
ANISOU 1021  O   GLN A 133     8532   9641   9331   1197   -655   -479  A    O  
ATOM   1022  CB  GLN A 133     -29.962  42.079   1.040  1.00 73.71      A    C  
ANISOU 1022  CB  GLN A 133     8650  10047   9309   1153   -446   -383  A    C  
ATOM   1023  CG  GLN A 133     -30.619  41.708  -0.260  1.00 85.64      A    C  
ANISOU 1023  CG  GLN A 133    10145  11554  10838   1077   -391   -305  A    C  
ATOM   1024  CD  GLN A 133     -32.116  41.615  -0.148  1.00 91.39      A    C  
ANISOU 1024  CD  GLN A 133    10840  12387  11496   1116   -349   -318  A    C  
ATOM   1025  NE2 GLN A 133     -32.758  41.224  -1.242  1.00 88.41      A    N  
ANISOU 1025  NE2 GLN A 133    10448  12013  11129   1052   -299   -251  A    N  
ATOM   1026  OE1 GLN A 133     -32.693  41.885   0.907  1.00 98.25      A    O  
ANISOU 1026  OE1 GLN A 133    11693  13336  12299   1205   -360   -387  A    O  
ATOM   1027  N   ASP A 134     -27.839  42.369   3.176  1.00 70.53      A    N  
ANISOU 1027  N   ASP A 134     8295   9598   8902   1243   -550   -494  A    N  
ATOM   1028  CA  ASP A 134     -27.209  43.140   4.212  1.00 75.67      A    C  
ANISOU 1028  CA  ASP A 134     8961  10218   9570   1328   -640   -588  A    C  
ATOM   1029  C   ASP A 134     -25.761  43.484   3.799  1.00 75.91      A    C  
ANISOU 1029  C   ASP A 134     9018  10109   9714   1275   -703   -568  A    C  
ATOM   1030  O   ASP A 134     -25.412  44.651   3.701  1.00 76.55      A    O  
ANISOU 1030  O   ASP A 134     9100  10093   9891   1308   -803   -617  A    O  
ATOM   1031  CB  ASP A 134     -27.245  42.410   5.539  1.00 80.35      A    C  
ANISOU 1031  CB  ASP A 134     9557  10927  10042   1385   -601   -621  A    C  
ATOM   1032  CG  ASP A 134     -26.238  42.968   6.493  1.00 93.05      A    C  
ANISOU 1032  CG  ASP A 134    11189  12487  11676   1450   -689   -700  A    C  
ATOM   1033  OD1 ASP A 134     -26.430  44.111   6.963  1.00 97.24      A    O  
ANISOU 1033  OD1 ASP A 134    11718  12993  12236   1544   -782   -799  A    O  
ATOM   1034  OD2 ASP A 134     -25.211  42.298   6.726  1.00102.39      A    O1-
ANISOU 1034  OD2 ASP A 134    12395  13647  12859   1406   -673   -668  A    O1-
ATOM   1035  N   ILE A 135     -24.940  42.469   3.513  1.00 79.30      A    N  
ANISOU 1035  N   ILE A 135     9463  10528  10139   1192   -645   -491  A    N  
ATOM   1036  CA  ILE A 135     -23.554  42.680   3.103  1.00 74.81      A    C  
ANISOU 1036  CA  ILE A 135     8913   9840   9671   1137   -693   -461  A    C  
ATOM   1037  C   ILE A 135     -23.383  43.794   2.093  1.00 76.65      A    C  
ANISOU 1037  C   ILE A 135     9134   9955  10031   1112   -765   -447  A    C  
ATOM   1038  O   ILE A 135     -22.547  44.672   2.288  1.00 66.58      A    O  
ANISOU 1038  O   ILE A 135     7867   8582   8847   1134   -862   -484  A    O  
ATOM   1039  CB  ILE A 135     -22.943  41.404   2.464  1.00 78.91      A    C  
ANISOU 1039  CB  ILE A 135     9442  10366  10173   1034   -607   -359  A    C  
ATOM   1040  CG1 ILE A 135     -22.414  40.479   3.567  1.00 79.20      A    C  
ANISOU 1040  CG1 ILE A 135     9497  10466  10128   1051   -574   -373  A    C  
ATOM   1041  CG2 ILE A 135     -21.804  41.742   1.484  1.00 71.43      A    C  
ANISOU 1041  CG2 ILE A 135     8499   9296   9344    960   -645   -302  A    C  
ATOM   1042  CD1 ILE A 135     -22.305  39.027   3.155  1.00 83.63      A    C  
ANISOU 1042  CD1 ILE A 135    10062  11077  10634    969   -474   -285  A    C  
ATOM   1043  N   GLN A 136     -24.119  43.719   0.989  1.00 76.14      A    N  
ANISOU 1043  N   GLN A 136     9052   9898   9979   1062   -720   -387  A    N  
ATOM   1044  CA  GLN A 136     -23.877  44.642  -0.108  1.00 86.65      A    C  
ANISOU 1044  CA  GLN A 136    10372  11120  11431   1022   -777   -351  A    C  
ATOM   1045  C   GLN A 136     -24.184  46.056   0.368  1.00 88.16      A    C  
ANISOU 1045  C   GLN A 136    10556  11257  11683   1110   -890   -444  A    C  
ATOM   1046  O   GLN A 136     -23.349  46.938   0.200  1.00 80.93      A    O  
ANISOU 1046  O   GLN A 136     9641  10227  10882   1106   -984   -450  A    O  
ATOM   1047  CB  GLN A 136     -24.645  44.254  -1.384  1.00 95.74      A    C  
ANISOU 1047  CB  GLN A 136    11505  12296  12574    957   -704   -270  A    C  
ATOM   1048  CG  GLN A 136     -26.052  44.809  -1.519  1.00110.32      A    C  
ANISOU 1048  CG  GLN A 136    13332  14185  14398   1005   -709   -307  A    C  
ATOM   1049  CD  GLN A 136     -27.001  43.868  -2.239  1.00121.26      A    C  
ANISOU 1049  CD  GLN A 136    14705  15655  15712    958   -604   -245  A    C  
ATOM   1050  NE2 GLN A 136     -28.299  44.110  -2.059  1.00119.66      A    N  
ANISOU 1050  NE2 GLN A 136    14485  15520  15461   1010   -593   -286  A    N  
ATOM   1051  OE1 GLN A 136     -26.583  42.927  -2.937  1.00118.56      A    O  
ANISOU 1051  OE1 GLN A 136    14368  15319  15358    877   -538   -163  A    O  
ATOM   1052  N   GLN A 137     -25.326  46.229   1.047  1.00 93.75      A    N  
ANISOU 1052  N   GLN A 137    11256  12049  12314   1193   -886   -519  A    N  
ATOM   1053  CA  GLN A 137     -25.786  47.527   1.572  1.00 98.44      A    C  
ANISOU 1053  CA  GLN A 137    11843  12610  12951   1292   -994   -622  A    C  
ATOM   1054  C   GLN A 137     -24.818  48.160   2.559  1.00 95.23      A    C  
ANISOU 1054  C   GLN A 137    11453  12137  12592   1354  -1099   -701  A    C  
ATOM   1055  O   GLN A 137     -24.508  49.332   2.438  1.00106.85      A    O  
ANISOU 1055  O   GLN A 137    12921  13499  14177   1381  -1214   -740  A    O  
ATOM   1056  CB  GLN A 137     -27.118  47.387   2.304  1.00103.04      A    C  
ANISOU 1056  CB  GLN A 137    12411  13322  13415   1379   -957   -690  A    C  
ATOM   1057  CG  GLN A 137     -28.311  47.045   1.436  1.00108.97      A    C  
ANISOU 1057  CG  GLN A 137    13139  14136  14127   1342   -877   -635  A    C  
ATOM   1058  CD  GLN A 137     -29.527  46.710   2.280  1.00114.95      A    C  
ANISOU 1058  CD  GLN A 137    13879  15039  14755   1423   -828   -692  A    C  
ATOM   1059  NE2 GLN A 137     -30.412  45.868   1.739  1.00117.65      A    N  
ANISOU 1059  NE2 GLN A 137    14224  15413  15064   1536   -894   -802  A    N  
ATOM   1060  OE1 GLN A 137     -29.678  47.207   3.397  1.00113.86      A    O  
ANISOU 1060  OE1 GLN A 137    13724  14987  14548   1386   -733   -636  A    O  
ATOM   1061  N   ARG A 138     -24.366  47.409   3.553  1.00 83.99      A    N  
ANISOU 1061  N   ARG A 138    10047  10778  11086   1380  -1067   -729  A    N  
ATOM   1062  CA  ARG A 138     -23.337  47.934   4.446  1.00 89.84      A    C  
ANISOU 1062  CA  ARG A 138    10806  11451  11876   1432  -1165   -799  A    C  
ATOM   1063  C   ARG A 138     -21.945  47.810   3.794  1.00 85.04      A    C  
ANISOU 1063  C   ARG A 138    10209  10729  11372   1335  -1182   -717  A    C  
ATOM   1064  O   ARG A 138     -20.934  48.031   4.441  1.00 77.70      A    O  
ANISOU 1064  O   ARG A 138     9294   9742  10484   1356  -1251   -755  A    O  
ATOM   1065  CB  ARG A 138     -23.388  47.266   5.826  1.00 88.26      A    C  
ANISOU 1065  CB  ARG A 138    10620  11366  11545   1508  -1133   -865  A    C  
ATOM   1066  CG  ARG A 138     -22.831  45.863   5.860  1.00 98.42      A    C  
ANISOU 1066  CG  ARG A 138    11921  12711  12761   1432  -1026   -785  A    C  
ATOM   1067  CD  ARG A 138     -23.145  45.138   7.159  1.00101.96      A    C  
ANISOU 1067  CD  ARG A 138    12377  13296  13068   1506   -979   -838  A    C  
ATOM   1068  NE  ARG A 138     -22.934  43.707   6.969  1.00101.64      A    N  
ANISOU 1068  NE  ARG A 138    12342  13320  12955   1422   -862   -742  A    N  
ATOM   1069  CZ  ARG A 138     -21.745  43.123   6.924  1.00108.07      A    C  
ANISOU 1069  CZ  ARG A 138    13178  14084  13799   1359   -851   -696  A    C  
ATOM   1070  NH1 ARG A 138     -20.640  43.835   7.070  1.00111.84      A    N1+
ANISOU 1070  NH1 ARG A 138    13670  14447  14376   1368   -949   -730  A    N1+
ATOM   1071  NH2 ARG A 138     -21.654  41.814   6.720  1.00112.58      A    N  
ANISOU 1071  NH2 ARG A 138    13753  14716  14306   1286   -748   -613  A    N  
ATOM   1072  N   GLY A 139     -21.913  47.466   2.508  1.00 84.68      A    N  
ANISOU 1072  N   GLY A 139    10151  10657  11366   1231  -1122   -607  A    N  
ATOM   1073  CA  GLY A 139     -20.662  47.367   1.751  1.00 91.22      A    C  
ANISOU 1073  CA  GLY A 139    10980  11388  12290   1138  -1133   -519  A    C  
ATOM   1074  C   GLY A 139     -19.594  46.447   2.324  1.00 86.48      A    C  
ANISOU 1074  C   GLY A 139    10401  10804  11651   1111  -1097   -502  A    C  
ATOM   1075  O   GLY A 139     -18.411  46.711   2.177  1.00 77.99      A    O  
ANISOU 1075  O   GLY A 139     9328   9635  10669   1074  -1151   -474  A    O  
ATOM   1076  N   GLY A 140     -19.998  45.359   2.969  1.00 88.80      A    N  
ANISOU 1076  N   GLY A 140    10709  11218  11813   1127  -1007   -513  A    N  
ATOM   1077  CA  GLY A 140     -19.049  44.525   3.718  1.00 84.86      A    C  
ANISOU 1077  CA  GLY A 140    10232  10741  11267   1120   -982   -513  A    C  
ATOM   1078  C   GLY A 140     -18.062  43.749   2.860  1.00 78.62      A    C  
ANISOU 1078  C   GLY A 140     9445   9913  10513   1011   -928   -406  A    C  
ATOM   1079  O   GLY A 140     -18.156  43.740   1.649  1.00 78.61      A    O  
ANISOU 1079  O   GLY A 140     9427   9882  10559    940   -897   -325  A    O  
ATOM   1080  N   GLU A 141     -17.116  43.097   3.507  1.00 78.14      A    N  
ANISOU 1080  N   GLU A 141     9404   9858  10427   1003   -919   -408  A    N  
ATOM   1081  CA  GLU A 141     -16.124  42.299   2.818  1.00 74.20      A    C  
ANISOU 1081  CA  GLU A 141     8907   9331   9953    910   -868   -316  A    C  
ATOM   1082  C   GLU A 141     -16.436  40.793   2.913  1.00 73.84      A    C  
ANISOU 1082  C   GLU A 141     8875   9396   9785    877   -751   -274  A    C  
ATOM   1083  O   GLU A 141     -15.877  40.028   2.145  1.00 67.69      A    O  
ANISOU 1083  O   GLU A 141     8095   8608   9014    798   -695   -193  A    O  
ATOM   1084  CB  GLU A 141     -14.731  42.603   3.383  1.00 81.11      A    C  
ANISOU 1084  CB  GLU A 141     9794  10124  10900    915   -946   -338  A    C  
ATOM   1085  CG  GLU A 141     -13.639  42.740   2.329  1.00 89.88      A    C  
ANISOU 1085  CG  GLU A 141    10889  11141  12121    829   -960   -249  A    C  
ATOM   1086  CD  GLU A 141     -14.006  43.722   1.226  1.00 94.93      A    C  
ANISOU 1086  CD  GLU A 141    11497  11715  12856    802   -999   -207  A    C  
ATOM   1087  OE1 GLU A 141     -14.107  44.933   1.496  1.00 90.85      A    O  
ANISOU 1087  OE1 GLU A 141    10971  11126  12418    852  -1102   -262  A    O  
ATOM   1088  OE2 GLU A 141     -14.202  43.285   0.078  1.00 95.82      A    O1-
ANISOU 1088  OE2 GLU A 141    11594  11847  12965    733   -929   -118  A    O1-
ATOM   1089  N   GLU A 142     -17.316  40.335   3.813  1.00 67.31      A    N  
ANISOU 1089  N   GLU A 142     8054   8671   8846    935   -712   -324  A    N  
ATOM   1090  CA  GLU A 142     -17.518  38.892   3.902  1.00 65.85      A    C  
ANISOU 1090  CA  GLU A 142     7879   8579   8559    896   -608   -276  A    C  
ATOM   1091  C   GLU A 142     -18.141  38.389   2.609  1.00 64.32      A    C  
ANISOU 1091  C   GLU A 142     7669   8404   8365    824   -535   -192  A    C  
ATOM   1092  O   GLU A 142     -18.760  39.152   1.797  1.00 62.19      A    O  
ANISOU 1092  O   GLU A 142     7380   8104   8144    818   -554   -182  A    O  
ATOM   1093  CB  GLU A 142     -18.252  38.401   5.173  1.00 66.27      A    C  
ANISOU 1093  CB  GLU A 142     7939   8749   8491    969   -579   -331  A    C  
ATOM   1094  CG  GLU A 142     -19.760  38.276   5.089  1.00 70.76      A    C  
ANISOU 1094  CG  GLU A 142     8488   9411   8985    994   -525   -333  A    C  
ATOM   1095  CD  GLU A 142     -20.426  37.567   6.287  1.00 72.64      A    C  
ANISOU 1095  CD  GLU A 142     8725   9778   9093   1052   -479   -362  A    C  
ATOM   1096  OE1 GLU A 142     -21.188  38.210   7.026  1.00 77.44      A    O  
ANISOU 1096  OE1 GLU A 142     9323  10442   9660   1142   -509   -436  A    O  
ATOM   1097  OE2 GLU A 142     -20.267  36.355   6.485  1.00 65.68      A    O1-
ANISOU 1097  OE2 GLU A 142     7851   8953   8149   1012   -411   -311  A    O1-
ATOM   1098  N   ARG A 143     -17.881  37.102   2.406  1.00 57.91      A    N  
ANISOU 1098  N   ARG A 143     6866   7635   7501    766   -459   -131  A    N  
ATOM   1099  CA  ARG A 143     -18.396  36.375   1.275  1.00 57.07      A    C  
ANISOU 1099  CA  ARG A 143     6749   7554   7380    698   -386    -55  A    C  
ATOM   1100  C   ARG A 143     -19.197  35.180   1.670  1.00 51.72      A    C  
ANISOU 1100  C   ARG A 143     6072   6983   6595    694   -308    -37  A    C  
ATOM   1101  O   ARG A 143     -18.877  34.526   2.650  1.00 55.73      A    O  
ANISOU 1101  O   ARG A 143     6596   7534   7045    714   -295    -54  A    O  
ATOM   1102  CB  ARG A 143     -17.256  35.892   0.398  1.00 55.85      A    C  
ANISOU 1102  CB  ARG A 143     6598   7342   7278    623   -373     12  A    C  
ATOM   1103  CG  ARG A 143     -16.632  36.989  -0.418  1.00 54.36      A    C  
ANISOU 1103  CG  ARG A 143     6395   7054   7202    605   -435     29  A    C  
ATOM   1104  CD  ARG A 143     -15.252  36.547  -0.818  1.00 57.19      A    C  
ANISOU 1104  CD  ARG A 143     6759   7364   7605    550   -435     79  A    C  
ATOM   1105  NE  ARG A 143     -14.529  37.527  -1.597  1.00 51.36      A    N  
ANISOU 1105  NE  ARG A 143     6000   6534   6977    526   -492    110  A    N  
ATOM   1106  CZ  ARG A 143     -14.811  37.867  -2.829  1.00 54.74      A    C  
ANISOU 1106  CZ  ARG A 143     6405   6945   7448    488   -481    166  A    C  
ATOM   1107  NH1 ARG A 143     -15.845  37.315  -3.507  1.00 60.76      A    N1+
ANISOU 1107  NH1 ARG A 143     7162   7770   8155    469   -416    196  A    N1+
ATOM   1108  NH2 ARG A 143     -14.034  38.762  -3.396  1.00 57.85      A    N  
ANISOU 1108  NH2 ARG A 143     6778   7256   7945    468   -539    199  A    N  
ATOM   1109  N   LEU A 144     -20.195  34.878   0.842  1.00 49.80      A    N  
ANISOU 1109  N   LEU A 144     5811   6776   6333    664   -258      4  A    N  
ATOM   1110  CA  LEU A 144     -20.992  33.727   1.029  1.00 49.58      A    C  
ANISOU 1110  CA  LEU A 144     5779   6840   6218    649   -186     34  A    C  
ATOM   1111  C   LEU A 144     -20.984  32.893  -0.225  1.00 45.52      A    C  
ANISOU 1111  C   LEU A 144     5262   6314   5720    569   -136    112  A    C  
ATOM   1112  O   LEU A 144     -20.980  33.424  -1.319  1.00 46.87      A    O  
ANISOU 1112  O   LEU A 144     5422   6434   5951    541   -149    135  A    O  
ATOM   1113  CB  LEU A 144     -22.438  34.117   1.321  1.00 51.13      A    C  
ANISOU 1113  CB  LEU A 144     5952   7108   6367    699   -174      5  A    C  
ATOM   1114  CG  LEU A 144     -22.654  35.136   2.423  1.00 57.24      A    C  
ANISOU 1114  CG  LEU A 144     6724   7898   7126    792   -230    -82  A    C  
ATOM   1115  CD1 LEU A 144     -24.116  35.518   2.426  1.00 61.96      A    C  
ANISOU 1115  CD1 LEU A 144     7293   8563   7683    833   -214   -102  A    C  
ATOM   1116  CD2 LEU A 144     -22.237  34.591   3.775  1.00 56.96      A    C  
ANISOU 1116  CD2 LEU A 144     6702   7917   7019    831   -226   -112  A    C  
ATOM   1117  N   TYR A 145     -21.110  31.598  -0.049  1.00 44.01      A    N  
ANISOU 1117  N   TYR A 145     5075   6177   5468    537    -81    149  A    N  
ATOM   1118  CA  TYR A 145     -21.291  30.670  -1.131  1.00 49.76      A    C  
ANISOU 1118  CA  TYR A 145     5799   6907   6199    469    -34    216  A    C  
ATOM   1119  C   TYR A 145     -22.303  29.648  -0.685  1.00 52.83      A    C  
ANISOU 1119  C   TYR A 145     6177   7385   6511    466     16    238  A    C  
ATOM   1120  O   TYR A 145     -22.052  28.907   0.222  1.00 54.53      A    O  
ANISOU 1120  O   TYR A 145     6402   7638   6677    471     30    239  A    O  
ATOM   1121  CB  TYR A 145     -19.968  29.978  -1.443  1.00 48.79      A    C  
ANISOU 1121  CB  TYR A 145     5696   6734   6104    423    -35    247  A    C  
ATOM   1122  CG  TYR A 145     -19.763  29.573  -2.869  1.00 43.91      A    C  
ANISOU 1122  CG  TYR A 145     5074   6084   5523    364    -16    302  A    C  
ATOM   1123  CD1 TYR A 145     -20.688  28.835  -3.526  1.00 43.79      A    C  
ANISOU 1123  CD1 TYR A 145     5042   6098   5498    345     13    330  A    C  
ATOM   1124  CD2 TYR A 145     -18.632  29.935  -3.551  1.00 43.63      A    C  
ANISOU 1124  CD2 TYR A 145     5050   5995   5529    332    -28    324  A    C  
ATOM   1125  CE1 TYR A 145     -20.513  28.471  -4.822  1.00 48.12      A    C  
ANISOU 1125  CE1 TYR A 145     5586   6622   6074    301     29    374  A    C  
ATOM   1126  CE2 TYR A 145     -18.444  29.570  -4.849  1.00 43.95      A    C  
ANISOU 1126  CE2 TYR A 145     5083   6017   5597    288    -10    372  A    C  
ATOM   1127  CZ  TYR A 145     -19.390  28.829  -5.475  1.00 44.66      A    C  
ANISOU 1127  CZ  TYR A 145     5158   6137   5671    273     18    395  A    C  
ATOM   1128  OH  TYR A 145     -19.234  28.455  -6.760  1.00 42.34      A    O  
ANISOU 1128  OH  TYR A 145     4856   5833   5394    236     35    439  A    O  
ATOM   1129  N   LEU A 146     -23.454  29.610  -1.323  1.00 45.67      A    N  
ANISOU 1129  N   LEU A 146     5248   6510   5595    455     43    259  A    N  
ATOM   1130  CA  LEU A 146     -24.470  28.615  -1.007  1.00 48.47      A    C  
ANISOU 1130  CA  LEU A 146     5584   6946   5886    444     91    291  A    C  
ATOM   1131  C   LEU A 146     -24.202  27.393  -1.853  1.00 45.33      A    C  
ANISOU 1131  C   LEU A 146     5194   6530   5499    374    119    352  A    C  
ATOM   1132  O   LEU A 146     -24.003  27.523  -3.095  1.00 44.09      A    O  
ANISOU 1132  O   LEU A 146     5039   6322   5391    341    115    371  A    O  
ATOM   1133  CB  LEU A 146     -25.879  29.163  -1.292  1.00 50.72      A    C  
ANISOU 1133  CB  LEU A 146     5837   7273   6158    467    103    284  A    C  
ATOM   1134  CG  LEU A 146     -27.055  28.201  -1.153  1.00 51.34      A    C  
ANISOU 1134  CG  LEU A 146     5889   7434   6183    448    151    328  A    C  
ATOM   1135  CD1 LEU A 146     -28.360  28.981  -0.818  1.00 54.43      A    C  
ANISOU 1135  CD1 LEU A 146     6246   7889   6544    503    156    299  A    C  
ATOM   1136  CD2 LEU A 146     -27.216  27.333  -2.383  1.00 53.04      A    C  
ANISOU 1136  CD2 LEU A 146     6102   7623   6427    380    174    385  A    C  
ATOM   1137  N   GLN A 147     -24.179  26.222  -1.203  1.00 43.20      A    N  
ANISOU 1137  N   GLN A 147     4926   6303   5185    354    145    381  A    N  
ATOM   1138  CA  GLN A 147     -23.904  24.963  -1.881  1.00 44.81      A    C  
ANISOU 1138  CA  GLN A 147     5138   6487   5399    292    163    433  A    C  
ATOM   1139  C   GLN A 147     -24.737  23.904  -1.262  1.00 43.04      A    C  
ANISOU 1139  C   GLN A 147     4895   6333   5123    278    193    473  A    C  
ATOM   1140  O   GLN A 147     -24.462  23.445  -0.155  1.00 47.05      A    O  
ANISOU 1140  O   GLN A 147     5407   6876   5590    291    198    476  A    O  
ATOM   1141  CB  GLN A 147     -22.414  24.585  -1.774  1.00 44.25      A    C  
ANISOU 1141  CB  GLN A 147     5100   6364   5349    276    143    430  A    C  
ATOM   1142  CG  GLN A 147     -21.434  25.705  -2.045  1.00 44.85      A    C  
ANISOU 1142  CG  GLN A 147     5190   6375   5473    296    107    392  A    C  
ATOM   1143  CD  GLN A 147     -19.933  25.234  -2.027  1.00 46.80      A    C  
ANISOU 1143  CD  GLN A 147     5466   6572   5743    275     91    395  A    C  
ATOM   1144  NE2 GLN A 147     -19.073  26.111  -2.433  1.00 42.85      A    N  
ANISOU 1144  NE2 GLN A 147     4971   6014   5293    283     60    376  A    N  
ATOM   1145  OE1 GLN A 147     -19.593  24.108  -1.656  1.00 46.21      A    O  
ANISOU 1145  OE1 GLN A 147     5403   6511   5644    251    103    418  A    O  
ATOM   1146  N   GLN A 148     -25.805  23.576  -1.940  1.00 45.51      A    N  
ANISOU 1146  N   GLN A 148     5183   6669   5438    255    214    505  A    N  
ATOM   1147  CA  GLN A 148     -26.807  22.678  -1.394  1.00 46.49      A    C  
ANISOU 1147  CA  GLN A 148     5278   6864   5520    241    242    550  A    C  
ATOM   1148  C   GLN A 148     -27.320  21.699  -2.423  1.00 47.50      A    C  
ANISOU 1148  C   GLN A 148     5396   6976   5676    184    250    600  A    C  
ATOM   1149  O   GLN A 148     -27.672  22.113  -3.535  1.00 45.38      A    O  
ANISOU 1149  O   GLN A 148     5123   6677   5442    175    245    593  A    O  
ATOM   1150  CB  GLN A 148     -27.987  23.543  -0.955  1.00 54.63      A    C  
ANISOU 1150  CB  GLN A 148     6274   7962   6518    288    255    531  A    C  
ATOM   1151  CG  GLN A 148     -29.159  22.757  -0.437  1.00 51.91      A    C  
ANISOU 1151  CG  GLN A 148     5889   7702   6131    277    288    584  A    C  
ATOM   1152  CD  GLN A 148     -28.765  21.846   0.680  1.00 52.38      A    C  
ANISOU 1152  CD  GLN A 148     5949   7802   6149    270    297    618  A    C  
ATOM   1153  NE2 GLN A 148     -28.997  20.542   0.499  1.00 52.85      A    N  
ANISOU 1153  NE2 GLN A 148     5998   7865   6217    212    307    685  A    N  
ATOM   1154  OE1 GLN A 148     -28.175  22.285   1.637  1.00 47.92      A    O  
ANISOU 1154  OE1 GLN A 148     5398   7257   5550    315    289    582  A    O  
ATOM   1155  N   THR A 149     -27.372  20.410  -2.092  1.00 46.62      A    N  
ANISOU 1155  N   THR A 149     5279   6882   5553    145    256    650  A    N  
ATOM   1156  CA  THR A 149     -27.933  19.455  -3.041  1.00 48.43      A    C  
ANISOU 1156  CA  THR A 149     5496   7092   5814     94    255    694  A    C  
ATOM   1157  C   THR A 149     -29.430  19.702  -3.116  1.00 52.35      A    C  
ANISOU 1157  C   THR A 149     5947   7645   6295    100    275    715  A    C  
ATOM   1158  O   THR A 149     -30.070  20.013  -2.125  1.00 53.67      A    O  
ANISOU 1158  O   THR A 149     6087   7886   6419    130    297    722  A    O  
ATOM   1159  CB  THR A 149     -27.643  17.998  -2.639  1.00 49.01      A    C  
ANISOU 1159  CB  THR A 149     5572   7163   5887     51    248    746  A    C  
ATOM   1160  CG2 THR A 149     -26.243  17.579  -3.036  1.00 55.92      A    C  
ANISOU 1160  CG2 THR A 149     6490   7966   6790     35    222    727  A    C  
ATOM   1161  OG1 THR A 149     -27.661  17.912  -1.248  1.00 56.52      A    O  
ANISOU 1161  OG1 THR A 149     6512   8174   6789     71    264    761  A    O  
ATOM   1162  N   LEU A 150     -29.961  19.610  -4.319  1.00 53.87      A    N  
ANISOU 1162  N   LEU A 150     6133   7808   6527     77    269    723  A    N  
ATOM   1163  CA  LEU A 150     -31.351  19.744  -4.579  1.00 46.99      A    C  
ANISOU 1163  CA  LEU A 150     5218   6980   5652     75    284    744  A    C  
ATOM   1164  C   LEU A 150     -32.031  18.487  -4.056  1.00 54.83      A    C  
ANISOU 1164  C   LEU A 150     6179   8015   6638     36    291    814  A    C  
ATOM   1165  O   LEU A 150     -31.555  17.343  -4.285  1.00 48.38      A    O  
ANISOU 1165  O   LEU A 150     5376   7156   5847     -8    270    846  A    O  
ATOM   1166  CB  LEU A 150     -31.619  19.862  -6.074  1.00 49.46      A    C  
ANISOU 1166  CB  LEU A 150     5537   7244   6011     58    269    735  A    C  
ATOM   1167  CG  LEU A 150     -31.120  21.178  -6.706  1.00 57.13      A    C  
ANISOU 1167  CG  LEU A 150     6531   8179   6996     94    261    677  A    C  
ATOM   1168  CD1 LEU A 150     -31.321  21.207  -8.230  1.00 57.43      A    C  
ANISOU 1168  CD1 LEU A 150     6573   8172   7074     75    247    674  A    C  
ATOM   1169  CD2 LEU A 150     -31.704  22.433  -6.065  1.00 58.58      A    C  
ANISOU 1169  CD2 LEU A 150     6694   8409   7151    145    275    646  A    C  
ATOM   1170  N   ASN A 151     -33.127  18.673  -3.326  1.00 52.26      A    N  
ANISOU 1170  N   ASN A 151     5807   7772   6276     53    317    842  A    N  
ATOM   1171  CA  ASN A 151     -33.887  17.497  -2.809  1.00 59.52      A    C  
ANISOU 1171  CA  ASN A 151     6684   8738   7191     12    325    922  A    C  
ATOM   1172  C   ASN A 151     -35.383  17.726  -2.774  1.00 57.15      A    C  
ANISOU 1172  C   ASN A 151     6326   8509   6879     19    348    954  A    C  
ATOM   1173  O   ASN A 151     -35.892  18.803  -3.089  1.00 54.15      A    O  
ANISOU 1173  O   ASN A 151     5937   8147   6488     58    359    911  A    O  
ATOM   1174  CB  ASN A 151     -33.428  17.183  -1.386  1.00 57.96      A    C  
ANISOU 1174  CB  ASN A 151     6483   8595   6943     26    340    947  A    C  
ATOM   1175  CG  ASN A 151     -33.572  18.402  -0.480  1.00 64.35      A    C  
ANISOU 1175  CG  ASN A 151     7283   9477   7689     98    367    902  A    C  
ATOM   1176  ND2 ASN A 151     -32.494  18.710   0.211  1.00 67.66      A    N  
ANISOU 1176  ND2 ASN A 151     7737   9886   8081    129    361    864  A    N  
ATOM   1177  OD1 ASN A 151     -34.645  19.071  -0.405  1.00 60.85      A    O  
ANISOU 1177  OD1 ASN A 151     6800   9097   7223    130    389    898  A    O  
ATOM   1178  N   ASP A 152     -36.095  16.718  -2.308  1.00 68.12      A    N  
ANISOU 1178  N   ASP A 152     7669   9944   8268    -19    354   1035  A    N  
ATOM   1179  CA  ASP A 152     -37.563  16.769  -2.319  1.00 65.16      A    C  
ANISOU 1179  CA  ASP A 152     7230   9637   7888    -22    374   1079  A    C  
ATOM   1180  C   ASP A 152     -38.206  17.852  -1.437  1.00 64.81      A    C  
ANISOU 1180  C   ASP A 152     7151   9698   7774     44    415   1058  A    C  
ATOM   1181  O   ASP A 152     -39.410  17.999  -1.494  1.00 65.21      A    O  
ANISOU 1181  O   ASP A 152     7148   9807   7818     48    433   1088  A    O  
ATOM   1182  CB  ASP A 152     -38.131  15.415  -1.922  1.00 71.71      A    C  
ANISOU 1182  CB  ASP A 152     8013  10494   8738    -80    369   1181  A    C  
ATOM   1183  CG  ASP A 152     -37.694  15.000  -0.536  1.00 72.98      A    C  
ANISOU 1183  CG  ASP A 152     8162  10718   8845    -73    387   1224  A    C  
ATOM   1184  OD1 ASP A 152     -37.317  15.883   0.272  1.00 85.89      A    O  
ANISOU 1184  OD1 ASP A 152     9810  12407  10416    -12    414   1179  A    O  
ATOM   1185  OD2 ASP A 152     -37.683  13.794  -0.273  1.00 76.82      A    O1-
ANISOU 1185  OD2 ASP A 152     8632  11196   9361   -127    370   1303  A    O1-
ATOM   1186  N   THR A 153     -37.481  18.624  -0.630  1.00 63.05      A    N  
ANISOU 1186  N   THR A 153     6954   9501   7498    101    427   1005  A    N  
ATOM   1187  CA  THR A 153     -38.198  19.734   0.029  1.00 61.82      A    C  
ANISOU 1187  CA  THR A 153     6766   9440   7282    173    457    971  A    C  
ATOM   1188  C   THR A 153     -38.456  20.952  -0.904  1.00 64.52      A    C  
ANISOU 1188  C   THR A 153     7125   9742   7647    208    446    894  A    C  
ATOM   1189  O   THR A 153     -39.108  21.910  -0.512  1.00 62.47      A    O  
ANISOU 1189  O   THR A 153     6839   9551   7347    269    463    860  A    O  
ATOM   1190  CB  THR A 153     -37.497  20.239   1.297  1.00 67.86      A    C  
ANISOU 1190  CB  THR A 153     7544  10260   7977    235    468    935  A    C  
ATOM   1191  CG2 THR A 153     -36.875  19.084   2.056  1.00 70.40      A    C  
ANISOU 1191  CG2 THR A 153     7871  10592   8286    197    470    999  A    C  
ATOM   1192  OG1 THR A 153     -36.527  21.237   0.944  1.00 70.52      A    O  
ANISOU 1192  OG1 THR A 153     7942  10524   8329    273    443    841  A    O  
ATOM   1193  N   VAL A 154     -37.961  20.947  -2.128  1.00 53.73      A    N  
ANISOU 1193  N   VAL A 154     5799   8269   6343    175    417    867  A    N  
ATOM   1194  CA  VAL A 154     -38.058  22.177  -2.913  1.00 56.93      A    C  
ANISOU 1194  CA  VAL A 154     6224   8638   6768    212    405    796  A    C  
ATOM   1195  C   VAL A 154     -39.517  22.373  -3.377  1.00 59.06      A    C  
ANISOU 1195  C   VAL A 154     6442   8954   7045    213    418    817  A    C  
ATOM   1196  O   VAL A 154     -40.242  21.394  -3.609  1.00 61.38      A    O  
ANISOU 1196  O   VAL A 154     6700   9263   7358    162    424    887  A    O  
ATOM   1197  CB  VAL A 154     -37.076  22.198  -4.160  1.00 52.19      A    C  
ANISOU 1197  CB  VAL A 154     5681   7917   6229    181    371    764  A    C  
ATOM   1198  CG1 VAL A 154     -35.638  22.034  -3.723  1.00 56.80      A    C  
ANISOU 1198  CG1 VAL A 154     6313   8458   6809    182    357    743  A    C  
ATOM   1199  CG2 VAL A 154     -37.441  21.111  -5.155  1.00 52.49      A    C  
ANISOU 1199  CG2 VAL A 154     5711   7913   6317    115    358    815  A    C  
ATOM   1200  N   GLY A 155     -39.929  23.620  -3.581  1.00 57.48      A    N  
ANISOU 1200  N   GLY A 155     6238   8766   6835    267    418    759  A    N  
ATOM   1201  CA  GLY A 155     -41.285  23.891  -4.000  1.00 60.97      A    C  
ANISOU 1201  CA  GLY A 155     6631   9251   7281    273    430    773  A    C  
ATOM   1202  C   GLY A 155     -41.614  23.370  -5.391  1.00 69.03      A    C  
ANISOU 1202  C   GLY A 155     7657  10201   8369    214    411    797  A    C  
ATOM   1203  O   GLY A 155     -40.771  22.777  -6.090  1.00 58.35      A    O  
ANISOU 1203  O   GLY A 155     6346   8765   7057    170    387    802  A    O  
ATOM   1204  N   ARG A 156     -42.849  23.615  -5.815  1.00 64.48      A    N  
ANISOU 1204  N   ARG A 156     7037   9662   7801    218    419    809  A    N  
ATOM   1205  CA  ARG A 156     -43.399  22.850  -6.933  1.00 71.86      A    C  
ANISOU 1205  CA  ARG A 156     7960  10550   8792    159    403    850  A    C  
ATOM   1206  C   ARG A 156     -42.943  23.304  -8.300  1.00 57.95      A    C  
ANISOU 1206  C   ARG A 156     6246   8693   7080    152    372    803  A    C  
ATOM   1207  O   ARG A 156     -42.812  22.475  -9.184  1.00 58.35      A    O  
ANISOU 1207  O   ARG A 156     6309   8684   7174    102    348    828  A    O  
ATOM   1208  CB  ARG A 156     -44.942  22.807  -6.894  1.00 80.34      A    C  
ANISOU 1208  CB  ARG A 156     8963  11699   9860    160    421    889  A    C  
ATOM   1209  CG  ARG A 156     -45.411  21.548  -6.191  1.00102.92      A    C  
ANISOU 1209  CG  ARG A 156    11773  14616  12715    115    436    980  A    C  
ATOM   1210  CD  ARG A 156     -46.863  21.629  -5.784  1.00114.49      A    C  
ANISOU 1210  CD  ARG A 156    13159  16184  14159    128    464   1023  A    C  
ATOM   1211  NE  ARG A 156     -47.109  20.717  -4.677  1.00114.16      A    N  
ANISOU 1211  NE  ARG A 156    13066  16222  14084    106    488   1107  A    N  
ATOM   1212  CZ  ARG A 156     -48.311  20.465  -4.186  1.00123.28      A    C  
ANISOU 1212  CZ  ARG A 156    14141  17476  15221    104    515   1173  A    C  
ATOM   1213  NH1 ARG A 156     -48.441  19.620  -3.167  1.00134.44      A    N1+
ANISOU 1213  NH1 ARG A 156    15507  18964  16606     82    536   1258  A    N1+
ATOM   1214  NH2 ARG A 156     -49.382  21.046  -4.717  1.00115.87      A    N  
ANISOU 1214  NH2 ARG A 156    13166  16564  14294    123    520   1159  A    N  
ATOM   1215  N   LYS A 157     -42.814  24.609  -8.473  1.00 46.26      A    N  
ANISOU 1215  N   LYS A 157     4784   7203   5591    204    367    739  A    N  
ATOM   1216  CA  LYS A 157     -42.259  25.167  -9.671  1.00 57.30      A    C  
ANISOU 1216  CA  LYS A 157     6224   8516   7028    203    339    698  A    C  
ATOM   1217  C   LYS A 157     -40.806  24.705  -9.848  1.00 52.50      A    C  
ANISOU 1217  C   LYS A 157     5670   7839   6436    179    322    693  A    C  
ATOM   1218  O   LYS A 157     -40.411  24.442 -10.965  1.00 54.39      A    O  
ANISOU 1218  O   LYS A 157     5938   8014   6713    151    301    693  A    O  
ATOM   1219  CB  LYS A 157     -42.377  26.692  -9.642  1.00 57.33      A    C  
ANISOU 1219  CB  LYS A 157     6234   8525   7023    266    335    636  A    C  
ATOM   1220  CG  LYS A 157     -43.863  27.058  -9.763  1.00 67.42      A    C  
ANISOU 1220  CG  LYS A 157     7460   9861   8295    284    347    642  A    C  
ATOM   1221  CD  LYS A 157     -44.143  28.495 -10.134  1.00 74.75      A    C  
ANISOU 1221  CD  LYS A 157     8391  10777   9230    338    330    583  A    C  
ATOM   1222  CE  LYS A 157     -45.452  28.524 -10.923  1.00 88.03      A    C  
ANISOU 1222  CE  LYS A 157    10035  12478  10933    329    331    599  A    C  
ATOM   1223  NZ  LYS A 157     -46.242  29.748 -10.659  1.00 98.85      A    N1+
ANISOU 1223  NZ  LYS A 157    11380  13891  12287    392    330    554  A    N1+
ATOM   1224  N   ILE A 158     -40.065  24.541  -8.762  1.00 51.28      A    N  
ANISOU 1224  N   ILE A 158     5528   7705   6249    190    332    693  A    N  
ATOM   1225  CA  ILE A 158     -38.667  24.081  -8.896  1.00 50.27      A    C  
ANISOU 1225  CA  ILE A 158     5451   7514   6136    167    317    688  A    C  
ATOM   1226  C   ILE A 158     -38.745  22.625  -9.321  1.00 53.34      A    C  
ANISOU 1226  C   ILE A 158     5834   7883   6549    106    308    742  A    C  
ATOM   1227  O   ILE A 158     -38.068  22.160 -10.236  1.00 44.32      A    O  
ANISOU 1227  O   ILE A 158     4724   6674   5441     79    285    740  A    O  
ATOM   1228  CB  ILE A 158     -37.839  24.248  -7.606  1.00 51.97      A    C  
ANISOU 1228  CB  ILE A 158     5680   7753   6312    194    326    672  A    C  
ATOM   1229  CG1 ILE A 158     -37.687  25.707  -7.173  1.00 46.86      A    C  
ANISOU 1229  CG1 ILE A 158     5040   7117   5646    259    322    611  A    C  
ATOM   1230  CG2 ILE A 158     -36.395  23.724  -7.817  1.00 60.33      A    C  
ANISOU 1230  CG2 ILE A 158     6787   8743   7389    167    307    669  A    C  
ATOM   1231  CD1 ILE A 158     -37.316  26.656  -8.272  1.00 49.46      A    C  
ANISOU 1231  CD1 ILE A 158     5397   7377   6019    270    295    571  A    C  
ATOM   1232  N   VAL A 159     -39.656  21.893  -8.725  1.00 59.83      A    N  
ANISOU 1232  N   VAL A 159     6611   8763   7359     87    324    793  A    N  
ATOM   1233  CA  VAL A 159     -39.821  20.532  -9.168  1.00 56.70      A    C  
ANISOU 1233  CA  VAL A 159     6206   8339   6997     28    306    845  A    C  
ATOM   1234  C   VAL A 159     -40.132  20.538 -10.683  1.00 53.32      A    C  
ANISOU 1234  C   VAL A 159     5788   7855   6616     13    279    830  A    C  
ATOM   1235  O   VAL A 159     -39.569  19.744 -11.460  1.00 46.88      A    O  
ANISOU 1235  O   VAL A 159     4999   6978   5834    -18    248    835  A    O  
ATOM   1236  CB  VAL A 159     -40.914  19.846  -8.333  1.00 62.95      A    C  
ANISOU 1236  CB  VAL A 159     6936   9206   7775      9    325    911  A    C  
ATOM   1237  CG1 VAL A 159     -41.485  18.647  -9.056  1.00 62.65      A    C  
ANISOU 1237  CG1 VAL A 159     6876   9136   7789    -48    296    963  A    C  
ATOM   1238  CG2 VAL A 159     -40.375  19.442  -6.969  1.00 62.94      A    C  
ANISOU 1238  CG2 VAL A 159     6931   9250   7732     11    343    938  A    C  
ATOM   1239  N   MET A 160     -41.005  21.440 -11.119  1.00 55.81      A    N  
ANISOU 1239  N   MET A 160     6082   8192   6931     40    287    810  A    N  
ATOM   1240  CA  MET A 160     -41.439  21.424 -12.526  1.00 54.04      A    C  
ANISOU 1240  CA  MET A 160     5861   7923   6746     28    262    799  A    C  
ATOM   1241  C   MET A 160     -40.263  21.853 -13.418  1.00 52.74      A    C  
ANISOU 1241  C   MET A 160     5751   7691   6593     40    242    755  A    C  
ATOM   1242  O   MET A 160     -40.118  21.368 -14.496  1.00 45.13      A    O  
ANISOU 1242  O   MET A 160     4804   6683   5659     21    216    754  A    O  
ATOM   1243  CB  MET A 160     -42.599  22.387 -12.813  1.00 61.42      A    C  
ANISOU 1243  CB  MET A 160     6762   8895   7678     57    273    784  A    C  
ATOM   1244  CG  MET A 160     -43.921  22.047 -12.134  1.00 76.38      A    C  
ANISOU 1244  CG  MET A 160     8594  10863   9564     48    292    830  A    C  
ATOM   1245  SD  MET A 160     -44.701  20.585 -12.850  1.00 84.17      A    S  
ANISOU 1245  SD  MET A 160     9551  11826  10604    -14    262    890  A    S  
ATOM   1246  CE  MET A 160     -45.380  21.377 -14.321  1.00 76.84      A    C  
ANISOU 1246  CE  MET A 160     8624  10865   9702      4    243    849  A    C  
ATOM   1247  N   ASP A 161     -39.468  22.792 -12.953  1.00 51.40      A    N  
ANISOU 1247  N   ASP A 161     5607   7520   6401     74    255    721  A    N  
ATOM   1248  CA  ASP A 161     -38.244  23.168 -13.646  1.00 54.20      A    C  
ANISOU 1248  CA  ASP A 161     6008   7818   6767     83    238    690  A    C  
ATOM   1249  C   ASP A 161     -37.254  21.987 -13.875  1.00 46.19      A    C  
ANISOU 1249  C   ASP A 161     5024   6763   5765     49    220    704  A    C  
ATOM   1250  O   ASP A 161     -36.863  21.678 -15.004  1.00 48.61      A    O  
ANISOU 1250  O   ASP A 161     5348   7027   6091     40    197    698  A    O  
ATOM   1251  CB  ASP A 161     -37.631  24.320 -12.873  1.00 53.55      A    C  
ANISOU 1251  CB  ASP A 161     5939   7743   6663    123    251    655  A    C  
ATOM   1252  CG  ASP A 161     -38.412  25.633 -13.055  1.00 52.00      A    C  
ANISOU 1252  CG  ASP A 161     5724   7565   6466    163    254    627  A    C  
ATOM   1253  OD1 ASP A 161     -39.289  25.707 -13.982  1.00 48.95      A    O  
ANISOU 1253  OD1 ASP A 161     5321   7178   6100    157    247    634  A    O  
ATOM   1254  OD2 ASP A 161     -38.068  26.619 -12.338  1.00 51.34      A    O1-
ANISOU 1254  OD2 ASP A 161     5647   7491   6369    201    257    596  A    O1-
ATOM   1255  N   PHE A 162     -36.930  21.304 -12.794  1.00 45.47      A    N  
ANISOU 1255  N   PHE A 162     4931   6689   5658     34    228    726  A    N  
ATOM   1256  CA  PHE A 162     -36.027  20.196 -12.741  1.00 46.75      A    C  
ANISOU 1256  CA  PHE A 162     5117   6818   5828      5    210    740  A    C  
ATOM   1257  C   PHE A 162     -36.483  19.140 -13.714  1.00 47.36      A    C  
ANISOU 1257  C   PHE A 162     5187   6866   5940    -26    180    761  A    C  
ATOM   1258  O   PHE A 162     -35.686  18.521 -14.445  1.00 43.72      A    O  
ANISOU 1258  O   PHE A 162     4755   6359   5496    -36    152    750  A    O  
ATOM   1259  CB  PHE A 162     -36.047  19.665 -11.279  1.00 51.23      A    C  
ANISOU 1259  CB  PHE A 162     5668   7425   6371     -7    228    772  A    C  
ATOM   1260  CG  PHE A 162     -35.124  18.517 -11.005  1.00 54.01      A    C  
ANISOU 1260  CG  PHE A 162     6043   7745   6731    -36    209    790  A    C  
ATOM   1261  CD1 PHE A 162     -33.771  18.732 -10.714  1.00 55.33      A    C  
ANISOU 1261  CD1 PHE A 162     6250   7885   6886    -22    208    763  A    C  
ATOM   1262  CD2 PHE A 162     -35.600  17.199 -11.021  1.00 57.77      A    C  
ANISOU 1262  CD2 PHE A 162     6500   8216   7233    -79    187    837  A    C  
ATOM   1263  CE1 PHE A 162     -32.945  17.649 -10.421  1.00 57.25      A    C  
ANISOU 1263  CE1 PHE A 162     6514   8101   7137    -48    191    780  A    C  
ATOM   1264  CE2 PHE A 162     -34.788  16.124 -10.731  1.00 55.36      A    C  
ANISOU 1264  CE2 PHE A 162     6215   7878   6940   -106    164    855  A    C  
ATOM   1265  CZ  PHE A 162     -33.447  16.347 -10.432  1.00 59.14      A    C  
ANISOU 1265  CZ  PHE A 162     6735   8334   7400    -89    168    824  A    C  
ATOM   1266  N   LEU A 163     -37.781  18.905 -13.714  1.00 45.99      A    N  
ANISOU 1266  N   LEU A 163     4971   6722   5777    -40    181    789  A    N  
ATOM   1267  CA  LEU A 163     -38.335  17.864 -14.531  1.00 42.93      A    C  
ANISOU 1267  CA  LEU A 163     4573   6308   5430    -72    144    810  A    C  
ATOM   1268  C   LEU A 163     -38.226  18.245 -16.028  1.00 39.55      A    C  
ANISOU 1268  C   LEU A 163     4166   5845   5017    -53    122    771  A    C  
ATOM   1269  O   LEU A 163     -38.316  17.375 -16.891  1.00 36.81      A    O  
ANISOU 1269  O   LEU A 163     3822   5462   4698    -68     81    773  A    O  
ATOM   1270  CB  LEU A 163     -39.837  17.718 -14.247  1.00 46.36      A    C  
ANISOU 1270  CB  LEU A 163     4951   6786   5875    -88    151    849  A    C  
ATOM   1271  CG  LEU A 163     -40.270  16.916 -13.037  1.00 47.87      A    C  
ANISOU 1271  CG  LEU A 163     5105   7016   6064   -120    161    908  A    C  
ATOM   1272  CD1 LEU A 163     -41.781  17.098 -12.900  1.00 53.97      A    C  
ANISOU 1272  CD1 LEU A 163     5819   7841   6844   -125    174    942  A    C  
ATOM   1273  CD2 LEU A 163     -39.853  15.441 -13.209  1.00 48.66      A    C  
ANISOU 1273  CD2 LEU A 163     5215   7065   6206   -163    114    938  A    C  
ATOM   1274  N   GLY A 164     -38.187  19.545 -16.291  1.00 36.69      A    N  
ANISOU 1274  N   GLY A 164     3809   5494   4634    -17    144    742  A    N  
ATOM   1275  CA  GLY A 164     -37.990  20.073 -17.600  1.00 36.14      A    C  
ANISOU 1275  CA  GLY A 164     3758   5400   4572      4    130    712  A    C  
ATOM   1276  C   GLY A 164     -36.529  20.031 -18.094  1.00 36.46      A    C  
ANISOU 1276  C   GLY A 164     3842   5406   4605     16    119    689  A    C  
ATOM   1277  O   GLY A 164     -36.275  20.354 -19.248  1.00 41.46      A    O  
ANISOU 1277  O   GLY A 164     4489   6024   5240     35    107    671  A    O  
ATOM   1278  N   PHE A 165     -35.597  19.593 -17.269  1.00 36.09      A    N  
ANISOU 1278  N   PHE A 165     3813   5350   4548      6    124    693  A    N  
ATOM   1279  CA  PHE A 165     -34.188  19.478 -17.691  1.00 37.41      A    C  
ANISOU 1279  CA  PHE A 165     4017   5487   4708     16    113    675  A    C  
ATOM   1280  C   PHE A 165     -34.097  18.508 -18.855  1.00 38.15      A    C  
ANISOU 1280  C   PHE A 165     4121   5556   4818     12     74    667  A    C  
ATOM   1281  O   PHE A 165     -35.053  17.707 -19.043  1.00 40.18      A    O  
ANISOU 1281  O   PHE A 165     4357   5810   5098     -6     49    680  A    O  
ATOM   1282  CB  PHE A 165     -33.310  19.002 -16.510  1.00 34.44      A    C  
ANISOU 1282  CB  PHE A 165     3656   5105   4322      2    121    683  A    C  
ATOM   1283  CG  PHE A 165     -33.090  20.045 -15.454  1.00 37.32      A    C  
ANISOU 1283  CG  PHE A 165     4020   5493   4667     18    155    678  A    C  
ATOM   1284  CD1 PHE A 165     -33.622  21.303 -15.561  1.00 42.16      A    C  
ANISOU 1284  CD1 PHE A 165     4619   6125   5274     43    172    667  A    C  
ATOM   1285  CD2 PHE A 165     -32.314  19.757 -14.334  1.00 37.93      A    C  
ANISOU 1285  CD2 PHE A 165     4110   5570   4730     11    163    682  A    C  
ATOM   1286  CE1 PHE A 165     -33.426  22.261 -14.577  1.00 40.07      A    C  
ANISOU 1286  CE1 PHE A 165     4353   5876   4993     64    194    654  A    C  
ATOM   1287  CE2 PHE A 165     -32.107  20.715 -13.376  1.00 37.53      A    C  
ANISOU 1287  CE2 PHE A 165     4059   5539   4659     32    187    672  A    C  
ATOM   1288  CZ  PHE A 165     -32.644  21.950 -13.487  1.00 39.44      A    C  
ANISOU 1288  CZ  PHE A 165     4288   5798   4898     60    200    656  A    C  
ATOM   1289  N   ASN A 166     -33.011  18.567 -19.647  1.00 36.13      A    N  
ANISOU 1289  N   ASN A 166     3890   5283   4551     34     63    646  A    N  
ATOM   1290  CA  ASN A 166     -32.932  17.665 -20.805  1.00 37.48      A    C  
ANISOU 1290  CA  ASN A 166     4070   5438   4731     42     22    630  A    C  
ATOM   1291  C   ASN A 166     -32.441  16.240 -20.441  1.00 43.49      A    C  
ANISOU 1291  C   ASN A 166     4845   6172   5507     21    -13    630  A    C  
ATOM   1292  O   ASN A 166     -31.303  15.787 -20.826  1.00 45.18      A    O  
ANISOU 1292  O   ASN A 166     5083   6371   5709     36    -30    610  A    O  
ATOM   1293  CB  ASN A 166     -32.135  18.268 -21.969  1.00 36.67      A    C  
ANISOU 1293  CB  ASN A 166     3982   5343   4607     80     22    611  A    C  
ATOM   1294  CG  ASN A 166     -32.276  17.446 -23.209  1.00 39.39      A    C  
ANISOU 1294  CG  ASN A 166     4329   5682   4952     98    -20    589  A    C  
ATOM   1295  ND2 ASN A 166     -31.778  17.951 -24.329  1.00 40.32      A    N  
ANISOU 1295  ND2 ASN A 166     4454   5820   5047    135    -19    577  A    N  
ATOM   1296  OD1 ASN A 166     -32.873  16.362 -23.170  1.00 37.90      A    O  
ANISOU 1296  OD1 ASN A 166     4136   5475   4788     81    -57    586  A    O  
ATOM   1297  N   TRP A 167     -33.289  15.526 -19.698  1.00 42.75      A    N  
ANISOU 1297  N   TRP A 167     4732   6072   5439    -13    -25    655  A    N  
ATOM   1298  CA  TRP A 167     -33.034  14.134 -19.271  1.00 41.22      A    C  
ANISOU 1298  CA  TRP A 167     4545   5847   5271    -41    -65    664  A    C  
ATOM   1299  C   TRP A 167     -32.828  13.213 -20.470  1.00 42.72      A    C  
ANISOU 1299  C   TRP A 167     4748   6006   5478    -23   -125    633  A    C  
ATOM   1300  O   TRP A 167     -32.037  12.254 -20.452  1.00 41.15      A    O  
ANISOU 1300  O   TRP A 167     4568   5777   5286    -24   -162    620  A    O  
ATOM   1301  CB  TRP A 167     -34.190  13.624 -18.385  1.00 38.95      A    C  
ANISOU 1301  CB  TRP A 167     4222   5563   5012    -83    -69    709  A    C  
ATOM   1302  CG  TRP A 167     -34.281  14.449 -17.139  1.00 40.12      A    C  
ANISOU 1302  CG  TRP A 167     4359   5750   5136    -90    -13    735  A    C  
ATOM   1303  CD1 TRP A 167     -35.246  15.321 -16.807  1.00 38.94      A    C  
ANISOU 1303  CD1 TRP A 167     4179   5638   4975    -87     21    750  A    C  
ATOM   1304  CD2 TRP A 167     -33.306  14.514 -16.108  1.00 42.37      A    C  
ANISOU 1304  CD2 TRP A 167     4662   6038   5399    -93      9    739  A    C  
ATOM   1305  CE2 TRP A 167     -33.748  15.474 -15.179  1.00 39.05      A    C  
ANISOU 1305  CE2 TRP A 167     4221   5661   4953    -89     58    755  A    C  
ATOM   1306  CE3 TRP A 167     -32.085  13.871 -15.899  1.00 41.00      A    C  
ANISOU 1306  CE3 TRP A 167     4519   5835   5222    -95     -7    729  A    C  
ATOM   1307  NE1 TRP A 167     -34.956  15.940 -15.625  1.00 42.95      A    N  
ANISOU 1307  NE1 TRP A 167     4686   6178   5455    -85     64    762  A    N  
ATOM   1308  CZ2 TRP A 167     -33.053  15.800 -14.081  1.00 42.43      A    C  
ANISOU 1308  CZ2 TRP A 167     4662   6105   5355    -85     86    759  A    C  
ATOM   1309  CZ3 TRP A 167     -31.351  14.222 -14.773  1.00 41.25      A    C  
ANISOU 1309  CZ3 TRP A 167     4562   5881   5229    -95     24    736  A    C  
ATOM   1310  CH2 TRP A 167     -31.815  15.183 -13.898  1.00 42.26      A    C  
ANISOU 1310  CH2 TRP A 167     4672   6051   5332    -89     70    750  A    C  
ATOM   1311  N   ASN A 168     -33.487  13.530 -21.554  1.00 42.72      A    N  
ANISOU 1311  N   ASN A 168     4738   6015   5477     -1   -137    616  A    N  
ATOM   1312  CA  ASN A 168     -33.336  12.698 -22.720  1.00 44.08      A    C  
ANISOU 1312  CA  ASN A 168     4921   6165   5660     23   -197    579  A    C  
ATOM   1313  C   ASN A 168     -31.854  12.671 -23.086  1.00 44.72      A    C  
ANISOU 1313  C   ASN A 168     5035   6249   5707     58   -197    548  A    C  
ATOM   1314  O   ASN A 168     -31.300  11.606 -23.270  1.00 41.02      A    O  
ANISOU 1314  O   ASN A 168     4582   5752   5250     66   -245    526  A    O  
ATOM   1315  CB  ASN A 168     -34.156  13.203 -23.886  1.00 45.13      A    C  
ANISOU 1315  CB  ASN A 168     5041   6317   5788     51   -206    563  A    C  
ATOM   1316  CG  ASN A 168     -33.981  12.339 -25.113  1.00 47.44      A    C  
ANISOU 1316  CG  ASN A 168     5346   6592   6085     88   -272    518  A    C  
ATOM   1317  ND2 ASN A 168     -33.629  12.950 -26.237  1.00 50.84      A    N  
ANISOU 1317  ND2 ASN A 168     5785   7055   6476    139   -263    489  A    N  
ATOM   1318  OD1 ASN A 168     -34.110  11.125 -25.034  1.00 55.97      A    O  
ANISOU 1318  OD1 ASN A 168     6428   7632   7205     73   -333    510  A    O  
ATOM   1319  N   TRP A 169     -31.233  13.840 -23.141  1.00 42.53      A    N  
ANISOU 1319  N   TRP A 169     4763   6004   5390     80   -143    550  A    N  
ATOM   1320  CA  TRP A 169     -29.860  14.000 -23.663  1.00 43.94      A    C  
ANISOU 1320  CA  TRP A 169     4965   6197   5533    118   -137    526  A    C  
ATOM   1321  C   TRP A 169     -28.849  13.421 -22.652  1.00 44.47      A    C  
ANISOU 1321  C   TRP A 169     5050   6242   5604     98   -137    531  A    C  
ATOM   1322  O   TRP A 169     -28.003  12.632 -23.001  1.00 45.16      A    O  
ANISOU 1322  O   TRP A 169     5155   6318   5687    118   -171    504  A    O  
ATOM   1323  CB  TRP A 169     -29.536  15.517 -23.971  1.00 44.42      A    C  
ANISOU 1323  CB  TRP A 169     5020   6297   5560    139    -81    539  A    C  
ATOM   1324  CG  TRP A 169     -28.089  15.673 -24.347  1.00 42.30      A    C  
ANISOU 1324  CG  TRP A 169     4767   6044   5260    171    -72    527  A    C  
ATOM   1325  CD1 TRP A 169     -27.545  15.395 -25.556  1.00 39.03      A    C  
ANISOU 1325  CD1 TRP A 169     4357   5654   4818    217    -94    502  A    C  
ATOM   1326  CD2 TRP A 169     -27.007  15.993 -23.471  1.00 38.47      A    C  
ANISOU 1326  CD2 TRP A 169     4292   5554   4767    159    -42    540  A    C  
ATOM   1327  CE2 TRP A 169     -25.826  15.909 -24.243  1.00 43.91      A    C  
ANISOU 1327  CE2 TRP A 169     4991   6266   5427    197    -47    525  A    C  
ATOM   1328  CE3 TRP A 169     -26.911  16.290 -22.110  1.00 41.58      A    C  
ANISOU 1328  CE3 TRP A 169     4691   5931   5177    124    -15    561  A    C  
ATOM   1329  NE1 TRP A 169     -26.212  15.574 -25.513  1.00 41.62      A    N  
ANISOU 1329  NE1 TRP A 169     4694   5996   5120    234    -77    503  A    N  
ATOM   1330  CZ2 TRP A 169     -24.560  16.153 -23.710  1.00 39.42      A    C  
ANISOU 1330  CZ2 TRP A 169     4431   5696   4847    198    -25    533  A    C  
ATOM   1331  CZ3 TRP A 169     -25.679  16.525 -21.574  1.00 41.73      A    C  
ANISOU 1331  CZ3 TRP A 169     4722   5947   5185    125      3    564  A    C  
ATOM   1332  CH2 TRP A 169     -24.497  16.483 -22.383  1.00 42.21      A    C  
ANISOU 1332  CH2 TRP A 169     4791   6026   5221    160     -1    552  A    C  
ATOM   1333  N   ILE A 170     -29.010  13.785 -21.391  1.00 41.89      A    N  
ANISOU 1333  N   ILE A 170     4718   5910   5286     61   -102    563  A    N  
ATOM   1334  CA  ILE A 170     -28.075  13.379 -20.382  1.00 42.43      A    C  
ANISOU 1334  CA  ILE A 170     4804   5962   5356     44    -97    569  A    C  
ATOM   1335  C   ILE A 170     -28.249  11.888 -20.026  1.00 43.37      A    C  
ANISOU 1335  C   ILE A 170     4926   6041   5510     19   -152    569  A    C  
ATOM   1336  O   ILE A 170     -27.288  11.221 -19.749  1.00 46.01      A    O  
ANISOU 1336  O   ILE A 170     5280   6356   5843     20   -172    558  A    O  
ATOM   1337  CB  ILE A 170     -28.128  14.341 -19.184  1.00 45.32      A    C  
ANISOU 1337  CB  ILE A 170     5162   6343   5713     23    -43    598  A    C  
ATOM   1338  CG1 ILE A 170     -26.827  14.226 -18.369  1.00 44.71      A    C  
ANISOU 1338  CG1 ILE A 170     5108   6255   5625     20    -32    596  A    C  
ATOM   1339  CG2 ILE A 170     -29.325  14.091 -18.294  1.00 41.05      A    C  
ANISOU 1339  CG2 ILE A 170     4599   5801   5195    -14    -40    630  A    C  
ATOM   1340  CD1 ILE A 170     -26.736  15.228 -17.224  1.00 45.75      A    C  
ANISOU 1340  CD1 ILE A 170     5235   6402   5745     10     14    616  A    C  
ATOM   1341  N   ASN A 171     -29.454  11.346 -20.038  1.00 41.21      A    N  
ANISOU 1341  N   ASN A 171     4632   5753   5271     -5   -182    585  A    N  
ATOM   1342  CA  ASN A 171     -29.618   9.884 -19.833  1.00 41.33      A    C  
ANISOU 1342  CA  ASN A 171     4649   5723   5332    -30   -247    589  A    C  
ATOM   1343  C   ASN A 171     -28.957   9.111 -20.994  1.00 42.46      A    C  
ANISOU 1343  C   ASN A 171     4813   5845   5474     11   -307    535  A    C  
ATOM   1344  O   ASN A 171     -28.429   8.044 -20.768  1.00 43.03      A    O  
ANISOU 1344  O   ASN A 171     4898   5879   5569      5   -357    524  A    O  
ATOM   1345  CB  ASN A 171     -31.115   9.383 -19.685  1.00 42.64      A    C  
ANISOU 1345  CB  ASN A 171     4781   5874   5545    -68   -277    622  A    C  
ATOM   1346  CG  ASN A 171     -31.863  10.021 -18.531  1.00 45.22      A    C  
ANISOU 1346  CG  ASN A 171     5081   6230   5869   -104   -222    677  A    C  
ATOM   1347  ND2 ASN A 171     -33.138   9.912 -18.611  1.00 45.57      A    N  
ANISOU 1347  ND2 ASN A 171     5092   6278   5943   -126   -233    703  A    N  
ATOM   1348  OD1 ASN A 171     -31.312  10.573 -17.561  1.00 41.66      A    O  
ANISOU 1348  OD1 ASN A 171     4636   5802   5389   -110   -172    693  A    O  
ATOM   1349  N   LYS A 172     -29.013   9.589 -22.227  1.00 43.23      A    N  
ANISOU 1349  N   LYS A 172     4911   5969   5546     57   -309    501  A    N  
ATOM   1350  CA  LYS A 172     -28.327   8.890 -23.273  1.00 47.35      A    C  
ANISOU 1350  CA  LYS A 172     5450   6483   6058    105   -363    447  A    C  
ATOM   1351  C   LYS A 172     -26.774   8.939 -23.034  1.00 51.05      A    C  
ANISOU 1351  C   LYS A 172     5943   6963   6491    127   -342    431  A    C  
ATOM   1352  O   LYS A 172     -26.059   7.981 -23.386  1.00 47.70      A    O  
ANISOU 1352  O   LYS A 172     5536   6518   6070    154   -396    393  A    O  
ATOM   1353  CB  LYS A 172     -28.585   9.480 -24.656  1.00 52.09      A    C  
ANISOU 1353  CB  LYS A 172     6045   7123   6625    157   -361    417  A    C  
ATOM   1354  CG  LYS A 172     -29.933   9.117 -25.298  1.00 65.01      A    C  
ANISOU 1354  CG  LYS A 172     7662   8742   8295    155   -408    409  A    C  
ATOM   1355  CD  LYS A 172     -30.148   9.628 -26.746  1.00 66.62      A    C  
ANISOU 1355  CD  LYS A 172     7862   8988   8461    213   -414    375  A    C  
ATOM   1356  CE  LYS A 172     -29.933  11.133 -26.841  1.00 79.73      A    C  
ANISOU 1356  CE  LYS A 172     9515  10703  10073    223   -331    401  A    C  
ATOM   1357  NZ  LYS A 172     -30.569  11.745 -28.036  1.00 81.82      A    N1+
ANISOU 1357  NZ  LYS A 172     9767  11005  10313    263   -330    387  A    N1+
ATOM   1358  N   GLN A 173     -26.268  10.069 -22.534  1.00 43.74      A    N  
ANISOU 1358  N   GLN A 173     5016   6068   5531    123   -271    456  A    N  
ATOM   1359  CA  GLN A 173     -24.847  10.178 -22.140  1.00 47.28      A    C  
ANISOU 1359  CA  GLN A 173     5484   6525   5954    134   -248    450  A    C  
ATOM   1360  C   GLN A 173     -24.492   9.148 -21.088  1.00 48.11      A    C  
ANISOU 1360  C   GLN A 173     5603   6584   6091    100   -279    457  A    C  
ATOM   1361  O   GLN A 173     -23.531   8.390 -21.262  1.00 46.44      A    O  
ANISOU 1361  O   GLN A 173     5409   6358   5875    123   -315    427  A    O  
ATOM   1362  CB  GLN A 173     -24.499  11.553 -21.625  1.00 42.77      A    C  
ANISOU 1362  CB  GLN A 173     4908   5985   5357    126   -174    481  A    C  
ATOM   1363  CG  GLN A 173     -24.444  12.610 -22.707  1.00 43.97      A    C  
ANISOU 1363  CG  GLN A 173     5047   6184   5474    165   -144    476  A    C  
ATOM   1364  CD  GLN A 173     -23.405  12.334 -23.802  1.00 45.99      A    C  
ANISOU 1364  CD  GLN A 173     5310   6467   5693    221   -163    442  A    C  
ATOM   1365  NE2 GLN A 173     -23.790  12.599 -25.042  1.00 43.55      A    N  
ANISOU 1365  NE2 GLN A 173     4989   6195   5363    261   -171    428  A    N  
ATOM   1366  OE1 GLN A 173     -22.294  11.940 -23.549  1.00 45.57      A    O  
ANISOU 1366  OE1 GLN A 173     5270   6412   5632    232   -168    430  A    O  
ATOM   1367  N   GLN A 174     -25.267   9.124 -20.004  1.00 41.27      A    N  
ANISOU 1367  N   GLN A 174     4726   5699   5254     48   -266    500  A    N  
ATOM   1368  CA  GLN A 174     -25.027   8.187 -18.929  1.00 42.31      A    C  
ANISOU 1368  CA  GLN A 174     4866   5791   5417     11   -292    519  A    C  
ATOM   1369  C   GLN A 174     -24.964   6.759 -19.493  1.00 48.63      A    C  
ANISOU 1369  C   GLN A 174     5675   6546   6253     21   -380    487  A    C  
ATOM   1370  O   GLN A 174     -24.052   6.023 -19.211  1.00 42.38      A    O  
ANISOU 1370  O   GLN A 174     4904   5729   5468     26   -412    470  A    O  
ATOM   1371  CB  GLN A 174     -26.153   8.305 -17.939  1.00 41.91      A    C  
ANISOU 1371  CB  GLN A 174     4793   5739   5392    -39   -273    574  A    C  
ATOM   1372  CG  GLN A 174     -26.181   7.234 -16.874  1.00 45.46      A    C  
ANISOU 1372  CG  GLN A 174     5241   6149   5879    -84   -307    607  A    C  
ATOM   1373  CD  GLN A 174     -27.424   7.338 -16.072  1.00 49.66      A    C  
ANISOU 1373  CD  GLN A 174     5741   6693   6433   -130   -288    665  A    C  
ATOM   1374  NE2 GLN A 174     -27.331   7.021 -14.795  1.00 50.71      A    N  
ANISOU 1374  NE2 GLN A 174     5869   6822   6573   -166   -277    709  A    N  
ATOM   1375  OE1 GLN A 174     -28.473   7.754 -16.592  1.00 50.76      A    O  
ANISOU 1375  OE1 GLN A 174     5857   6849   6579   -129   -281    671  A    O  
ATOM   1376  N   GLY A 175     -25.926   6.412 -20.350  1.00 48.88      A    N  
ANISOU 1376  N   GLY A 175     5694   6568   6310     30   -424    473  A    N  
ATOM   1377  CA  GLY A 175     -25.956   5.100 -20.997  1.00 47.61      A    C  
ANISOU 1377  CA  GLY A 175     5540   6360   6188     48   -519    435  A    C  
ATOM   1378  C   GLY A 175     -24.792   4.850 -21.905  1.00 51.76      A    C  
ANISOU 1378  C   GLY A 175     6088   6897   6678    113   -545    370  A    C  
ATOM   1379  O   GLY A 175     -24.141   3.838 -21.803  1.00 51.36      A    O  
ANISOU 1379  O   GLY A 175     6054   6809   6648    122   -604    343  A    O  
ATOM   1380  N   LYS A 176     -24.506   5.787 -22.797  1.00 51.66      A    N  
ANISOU 1380  N   LYS A 176     6074   6942   6609    161   -502    347  A    N  
ATOM   1381  CA  LYS A 176     -23.468   5.562 -23.763  1.00 51.68      A    C  
ANISOU 1381  CA  LYS A 176     6092   6972   6572    229   -525    289  A    C  
ATOM   1382  C   LYS A 176     -22.157   5.355 -23.056  1.00 53.08      A    C  
ANISOU 1382  C   LYS A 176     6287   7143   6735    229   -512    287  A    C  
ATOM   1383  O   LYS A 176     -21.409   4.534 -23.485  1.00 52.52      A    O  
ANISOU 1383  O   LYS A 176     6231   7062   6661    269   -565    239  A    O  
ATOM   1384  CB  LYS A 176     -23.277   6.751 -24.703  1.00 56.95      A    C  
ANISOU 1384  CB  LYS A 176     6748   7711   7176    275   -467    283  A    C  
ATOM   1385  CG  LYS A 176     -24.162   6.868 -25.945  1.00 60.21      A    C  
ANISOU 1385  CG  LYS A 176     7149   8149   7580    313   -493    256  A    C  
ATOM   1386  CD  LYS A 176     -24.560   8.338 -26.083  1.00 71.03      A    C  
ANISOU 1386  CD  LYS A 176     8500   9568   8916    305   -412    297  A    C  
ATOM   1387  CE  LYS A 176     -25.019   8.787 -27.445  1.00 82.04      A    C  
ANISOU 1387  CE  LYS A 176     9882  11013  10276    358   -415    274  A    C  
ATOM   1388  NZ  LYS A 176     -25.506  10.187 -27.308  1.00 77.21      A    N1+
ANISOU 1388  NZ  LYS A 176     9252  10432   9649    334   -340    323  A    N1+
ATOM   1389  N   ARG A 177     -21.865   6.125 -22.004  1.00 52.66      A    N  
ANISOU 1389  N   ARG A 177     6234   7099   6674    187   -443    335  A    N  
ATOM   1390  CA  ARG A 177     -20.603   6.019 -21.305  1.00 53.04      A    C  
ANISOU 1390  CA  ARG A 177     6299   7144   6709    186   -427    335  A    C  
ATOM   1391  C   ARG A 177     -20.515   4.857 -20.315  1.00 53.39      A    C  
ANISOU 1391  C   ARG A 177     6357   7124   6802    146   -479    344  A    C  
ATOM   1392  O   ARG A 177     -19.451   4.589 -19.781  1.00 46.72      A    O  
ANISOU 1392  O   ARG A 177     5529   6270   5950    150   -478    337  A    O  
ATOM   1393  CB  ARG A 177     -20.301   7.300 -20.490  1.00 56.01      A    C  
ANISOU 1393  CB  ARG A 177     6670   7549   7059    159   -339    381  A    C  
ATOM   1394  CG  ARG A 177     -20.237   8.610 -21.233  1.00 51.38      A    C  
ANISOU 1394  CG  ARG A 177     6068   7022   6429    188   -281    386  A    C  
ATOM   1395  CD  ARG A 177     -19.516   8.537 -22.556  1.00 53.74      A    C  
ANISOU 1395  CD  ARG A 177     6366   7363   6689    256   -298    344  A    C  
ATOM   1396  NE  ARG A 177     -20.221   9.400 -23.493  1.00 57.36      A    N  
ANISOU 1396  NE  ARG A 177     6804   7864   7124    277   -271    351  A    N  
ATOM   1397  CZ  ARG A 177     -20.102   9.338 -24.810  1.00 60.79      A    C  
ANISOU 1397  CZ  ARG A 177     7231   8342   7524    336   -291    318  A    C  
ATOM   1398  NH1 ARG A 177     -19.290   8.448 -25.355  1.00 63.76      A    N1+
ANISOU 1398  NH1 ARG A 177     7616   8726   7881    385   -337    270  A    N1+
ATOM   1399  NH2 ARG A 177     -20.819  10.160 -25.575  1.00 65.52      A    N  
ANISOU 1399  NH2 ARG A 177     7812   8978   8105    350   -265    332  A    N  
ATOM   1400  N   GLY A 178     -21.632   4.251 -19.969  1.00 48.92      A    N  
ANISOU 1400  N   GLY A 178     5781   6514   6288    105   -518    369  A    N  
ATOM   1401  CA  GLY A 178     -21.607   3.132 -19.020  1.00 46.31      A    C  
ANISOU 1401  CA  GLY A 178     5459   6123   6011     62   -571    389  A    C  
ATOM   1402  C   GLY A 178     -21.456   3.617 -17.595  1.00 45.75      A    C  
ANISOU 1402  C   GLY A 178     5387   6058   5935     12   -509    448  A    C  
ATOM   1403  O   GLY A 178     -21.118   2.866 -16.697  1.00 47.49      A    O  
ANISOU 1403  O   GLY A 178     5617   6241   6185    -19   -537    468  A    O  
ATOM   1404  N   TRP A 179     -21.734   4.882 -17.374  1.00 46.45      A    N  
ANISOU 1404  N   TRP A 179     5464   6194   5989      5   -430    474  A    N  
ATOM   1405  CA  TRP A 179     -21.702   5.433 -16.033  1.00 47.22      A    C  
ANISOU 1405  CA  TRP A 179     5558   6303   6078    -36   -373    525  A    C  
ATOM   1406  C   TRP A 179     -22.735   4.824 -15.048  1.00 51.08      A    C  
ANISOU 1406  C   TRP A 179     6028   6766   6611    -96   -391    584  A    C  
ATOM   1407  O   TRP A 179     -23.738   4.304 -15.429  1.00 49.06      A    O  
ANISOU 1407  O   TRP A 179     5754   6490   6394   -112   -432    595  A    O  
ATOM   1408  CB  TRP A 179     -21.928   6.943 -16.065  1.00 42.50      A    C  
ANISOU 1408  CB  TRP A 179     4948   5759   5439    -28   -294    538  A    C  
ATOM   1409  CG  TRP A 179     -20.906   7.753 -16.773  1.00 42.50      A    C  
ANISOU 1409  CG  TRP A 179     4959   5793   5395     18   -262    501  A    C  
ATOM   1410  CD1 TRP A 179     -19.650   7.334 -17.215  1.00 44.89      A    C  
ANISOU 1410  CD1 TRP A 179     5281   6090   5683     55   -285    462  A    C  
ATOM   1411  CD2 TRP A 179     -20.982   9.145 -17.086  1.00 38.64      A    C  
ANISOU 1411  CD2 TRP A 179     4459   5347   4873     35   -200    508  A    C  
ATOM   1412  CE2 TRP A 179     -19.778   9.489 -17.770  1.00 42.01      A    C  
ANISOU 1412  CE2 TRP A 179     4896   5796   5269     78   -190    478  A    C  
ATOM   1413  CE3 TRP A 179     -21.959  10.126 -16.906  1.00 43.42      A    C  
ANISOU 1413  CE3 TRP A 179     5043   5977   5474     20   -158    536  A    C  
ATOM   1414  NE1 TRP A 179     -19.003   8.370 -17.820  1.00 40.93      A    N  
ANISOU 1414  NE1 TRP A 179     4776   5632   5141     91   -240    449  A    N  
ATOM   1415  CZ2 TRP A 179     -19.519  10.774 -18.251  1.00 41.79      A    C  
ANISOU 1415  CZ2 TRP A 179     4857   5809   5212    101   -141    481  A    C  
ATOM   1416  CZ3 TRP A 179     -21.710  11.419 -17.406  1.00 39.01      A    C  
ANISOU 1416  CZ3 TRP A 179     4479   5455   4886     45   -110    532  A    C  
ATOM   1417  CH2 TRP A 179     -20.484  11.731 -18.051  1.00 42.30      A    C  
ANISOU 1417  CH2 TRP A 179     4903   5889   5278     83   -103    509  A    C  
ATOM   1418  N   GLY A 180     -22.497   4.990 -13.751  1.00 50.71      A    N  
ANISOU 1418  N   GLY A 180     5983   6727   6556   -126   -356    625  A    N  
ATOM   1419  CA  GLY A 180     -23.498   4.646 -12.768  1.00 48.96      A    C  
ANISOU 1419  CA  GLY A 180     5736   6502   6364   -179   -357    692  A    C  
ATOM   1420  C   GLY A 180     -24.585   5.693 -12.607  1.00 49.43      A    C  
ANISOU 1420  C   GLY A 180     5766   6611   6403   -189   -297    722  A    C  
ATOM   1421  O   GLY A 180     -24.805   6.585 -13.445  1.00 50.80      A    O  
ANISOU 1421  O   GLY A 180     5937   6812   6552   -159   -268    692  A    O  
ATOM   1422  N   GLN A 181     -25.219   5.615 -11.462  1.00 49.45      A    N  
ANISOU 1422  N   GLN A 181     5745   6631   6410   -228   -277    785  A    N  
ATOM   1423  CA  GLN A 181     -26.387   6.395 -11.175  1.00 57.60      A    C  
ANISOU 1423  CA  GLN A 181     6743   7711   7429   -241   -229    820  A    C  
ATOM   1424  C   GLN A 181     -25.988   7.860 -10.997  1.00 53.78      A    C  
ANISOU 1424  C   GLN A 181     6269   7276   6887   -207   -157    795  A    C  
ATOM   1425  O   GLN A 181     -24.856   8.161 -10.562  1.00 43.86      A    O  
ANISOU 1425  O   GLN A 181     5040   6021   5603   -190   -138    774  A    O  
ATOM   1426  CB  GLN A 181     -27.048   5.859  -9.905  1.00 60.20      A    C  
ANISOU 1426  CB  GLN A 181     7042   8056   7773   -289   -227    899  A    C  
ATOM   1427  CG  GLN A 181     -26.280   6.264  -8.645  1.00 74.70      A    C  
ANISOU 1427  CG  GLN A 181     8892   9924   9565   -285   -181    913  A    C  
ATOM   1428  CD  GLN A 181     -26.789   5.602  -7.372  1.00 84.73      A    C  
ANISOU 1428  CD  GLN A 181    10132  11214  10845   -328   -183    994  A    C  
ATOM   1429  NE2 GLN A 181     -28.125   5.493  -7.223  1.00 84.16      A    N  
ANISOU 1429  NE2 GLN A 181    10081  11133  10763   -335   -189   1006  A    N  
ATOM   1430  OE1 GLN A 181     -25.991   5.204  -6.528  1.00 96.63      A    O  
ANISOU 1430  OE1 GLN A 181    11596  12747  12370   -356   -180   1049  A    O  
ATOM   1431  N   LEU A 182     -26.917   8.743 -11.366  1.00 43.68      A    N  
ANISOU 1431  N   LEU A 182     4967   6032   5595   -198   -123    796  A    N  
ATOM   1432  CA  LEU A 182     -26.894  10.113 -10.935  1.00 44.33      A    C  
ANISOU 1432  CA  LEU A 182     5047   6162   5632   -175    -59    788  A    C  
ATOM   1433  C   LEU A 182     -26.938  10.124  -9.417  1.00 43.83      A    C  
ANISOU 1433  C   LEU A 182     4972   6131   5548   -192    -31    831  A    C  
ATOM   1434  O   LEU A 182     -27.878   9.622  -8.875  1.00 47.77      A    O  
ANISOU 1434  O   LEU A 182     5439   6648   6060   -223    -34    884  A    O  
ATOM   1435  CB  LEU A 182     -28.126  10.836 -11.429  1.00 45.68      A    C  
ANISOU 1435  CB  LEU A 182     5188   6365   5803   -169    -37    795  A    C  
ATOM   1436  CG  LEU A 182     -28.249  12.341 -11.074  1.00 47.25      A    C  
ANISOU 1436  CG  LEU A 182     5381   6611   5960   -141     21    781  A    C  
ATOM   1437  CD1 LEU A 182     -27.193  13.133 -11.806  1.00 43.92      A    C  
ANISOU 1437  CD1 LEU A 182     4989   6174   5521   -104     31    731  A    C  
ATOM   1438  CD2 LEU A 182     -29.615  12.934 -11.445  1.00 47.16      A    C  
ANISOU 1438  CD2 LEU A 182     5336   6633   5951   -140     39    794  A    C  
ATOM   1439  N   THR A 183     -25.978  10.723  -8.725  1.00 41.84      A    N  
ANISOU 1439  N   THR A 183     4743   5892   5261   -172     -2    813  A    N  
ATOM   1440  CA  THR A 183     -26.035  10.774  -7.270  1.00 41.71      A    C  
ANISOU 1440  CA  THR A 183     4715   5914   5217   -182     24    850  A    C  
ATOM   1441  C   THR A 183     -26.540  12.053  -6.688  1.00 43.50      A    C  
ANISOU 1441  C   THR A 183     4924   6199   5402   -154     76    846  A    C  
ATOM   1442  O   THR A 183     -27.100  12.050  -5.581  1.00 48.22      A    O  
ANISOU 1442  O   THR A 183     5497   6847   5975   -161     99    886  A    O  
ATOM   1443  CB  THR A 183     -24.642  10.513  -6.624  1.00 42.57      A    C  
ANISOU 1443  CB  THR A 183     4859   6000   5312   -174     16    834  A    C  
ATOM   1444  CG2 THR A 183     -24.064   9.207  -7.089  1.00 38.97      A    C  
ANISOU 1444  CG2 THR A 183     4421   5486   4896   -197    -38    835  A    C  
ATOM   1445  OG1 THR A 183     -23.765  11.627  -6.932  1.00 40.79      A    O  
ANISOU 1445  OG1 THR A 183     4659   5773   5065   -135     40    780  A    O  
ATOM   1446  N   SER A 184     -26.301  13.183  -7.322  1.00 40.89      A    N  
ANISOU 1446  N   SER A 184     4606   5869   5062   -121     95    798  A    N  
ATOM   1447  CA  SER A 184     -26.668  14.462  -6.693  1.00 40.34      A    C  
ANISOU 1447  CA  SER A 184     4523   5848   4955    -89    137    786  A    C  
ATOM   1448  C   SER A 184     -26.649  15.532  -7.767  1.00 42.18      A    C  
ANISOU 1448  C   SER A 184     4763   6068   5195    -62    144    744  A    C  
ATOM   1449  O   SER A 184     -26.061  15.322  -8.819  1.00 37.00      A    O  
ANISOU 1449  O   SER A 184     4125   5369   4562    -63    123    723  A    O  
ATOM   1450  CB  SER A 184     -25.672  14.822  -5.597  1.00 48.16      A    C  
ANISOU 1450  CB  SER A 184     5535   6847   5914    -69    150    771  A    C  
ATOM   1451  OG  SER A 184     -24.327  14.432  -5.953  1.00 48.85      A    O  
ANISOU 1451  OG  SER A 184     5660   6882   6019    -71    125    746  A    O  
ATOM   1452  N   ASN A 185     -27.382  16.610  -7.530  1.00 42.09      A    N  
ANISOU 1452  N   ASN A 185     4730   6095   5165    -38    172    736  A    N  
ATOM   1453  CA  ASN A 185     -27.335  17.820  -8.292  1.00 41.17      A    C  
ANISOU 1453  CA  ASN A 185     4619   5972   5054     -8    180    699  A    C  
ATOM   1454  C   ASN A 185     -27.062  18.905  -7.250  1.00 45.39      A    C  
ANISOU 1454  C   ASN A 185     5155   6532   5558     27    200    675  A    C  
ATOM   1455  O   ASN A 185     -27.940  19.311  -6.510  1.00 48.09      A    O  
ANISOU 1455  O   ASN A 185     5472   6925   5875     43    219    683  A    O  
ATOM   1456  CB  ASN A 185     -28.673  18.116  -8.952  1.00 41.19      A    C  
ANISOU 1456  CB  ASN A 185     4590   5996   5064     -9    187    708  A    C  
ATOM   1457  CG  ASN A 185     -28.993  17.190 -10.116  1.00 47.58      A    C  
ANISOU 1457  CG  ASN A 185     5397   6776   5905    -36    161    723  A    C  
ATOM   1458  ND2 ASN A 185     -28.293  17.368 -11.217  1.00 43.78      A    N  
ANISOU 1458  ND2 ASN A 185     4937   6257   5439    -27    146    695  A    N  
ATOM   1459  OD1 ASN A 185     -29.857  16.304 -10.022  1.00 50.80      A    O  
ANISOU 1459  OD1 ASN A 185     5781   7195   6324    -65    151    758  A    O  
ATOM   1460  N   LEU A 186     -25.852  19.392  -7.201  1.00 42.58      A    N  
ANISOU 1460  N   LEU A 186     4826   6144   5206     44    192    645  A    N  
ATOM   1461  CA  LEU A 186     -25.528  20.554  -6.375  1.00 42.28      A    C  
ANISOU 1461  CA  LEU A 186     4793   6120   5151     83    199    613  A    C  
ATOM   1462  C   LEU A 186     -25.885  21.867  -7.016  1.00 44.23      A    C  
ANISOU 1462  C   LEU A 186     5030   6360   5414    110    200    587  A    C  
ATOM   1463  O   LEU A 186     -25.506  22.125  -8.179  1.00 42.14      A    O  
ANISOU 1463  O   LEU A 186     4774   6057   5180    105    189    582  A    O  
ATOM   1464  CB  LEU A 186     -24.001  20.557  -6.088  1.00 42.66      A    C  
ANISOU 1464  CB  LEU A 186     4873   6127   5206     88    184    593  A    C  
ATOM   1465  CG  LEU A 186     -23.470  21.361  -4.871  1.00 42.10      A    C  
ANISOU 1465  CG  LEU A 186     4812   6068   5116    125    182    564  A    C  
ATOM   1466  CD1 LEU A 186     -23.975  20.771  -3.555  1.00 42.87      A    C  
ANISOU 1466  CD1 LEU A 186     4899   6222   5169    128    197    581  A    C  
ATOM   1467  CD2 LEU A 186     -21.941  21.399  -4.903  1.00 41.89      A    C  
ANISOU 1467  CD2 LEU A 186     4814   5990   5109    125    162    546  A    C  
ATOM   1468  N   LEU A 187     -26.539  22.716  -6.223  1.00 43.10      A    N  
ANISOU 1468  N   LEU A 187     4870   6255   5249    145    210    569  A    N  
ATOM   1469  CA  LEU A 187     -26.914  24.072  -6.582  1.00 40.85      A    C  
ANISOU 1469  CA  LEU A 187     4574   5965   4978    179    205    538  A    C  
ATOM   1470  C   LEU A 187     -25.914  24.937  -5.907  1.00 41.96      A    C  
ANISOU 1470  C   LEU A 187     4735   6082   5125    211    186    501  A    C  
ATOM   1471  O   LEU A 187     -25.715  24.823  -4.683  1.00 40.28      A    O  
ANISOU 1471  O   LEU A 187     4526   5897   4878    231    188    489  A    O  
ATOM   1472  CB  LEU A 187     -28.290  24.408  -5.997  1.00 45.19      A    C  
ANISOU 1472  CB  LEU A 187     5092   6580   5498    203    223    538  A    C  
ATOM   1473  CG  LEU A 187     -28.695  25.890  -6.057  1.00 47.06      A    C  
ANISOU 1473  CG  LEU A 187     5319   6817   5745    249    211    497  A    C  
ATOM   1474  CD1 LEU A 187     -28.840  26.392  -7.458  1.00 45.02      A    C  
ANISOU 1474  CD1 LEU A 187     5059   6517   5530    236    201    499  A    C  
ATOM   1475  CD2 LEU A 187     -30.042  26.125  -5.399  1.00 50.20      A    C  
ANISOU 1475  CD2 LEU A 187     5680   7287   6104    278    230    494  A    C  
ATOM   1476  N   LEU A 188     -25.263  25.764  -6.690  1.00 39.54      A    N  
ANISOU 1476  N   LEU A 188     4439   5724   4860    216    165    486  A    N  
ATOM   1477  CA  LEU A 188     -24.204  26.593  -6.216  1.00 42.16      A    C  
ANISOU 1477  CA  LEU A 188     4787   6018   5213    241    138    455  A    C  
ATOM   1478  C   LEU A 188     -24.563  28.013  -6.496  1.00 40.34      A    C  
ANISOU 1478  C   LEU A 188     4543   5770   5012    274    117    429  A    C  
ATOM   1479  O   LEU A 188     -24.837  28.367  -7.607  1.00 44.09      A    O  
ANISOU 1479  O   LEU A 188     5008   6225   5519    261    115    444  A    O  
ATOM   1480  CB  LEU A 188     -22.914  26.233  -6.939  1.00 39.29      A    C  
ANISOU 1480  CB  LEU A 188     4443   5602   4884    210    127    473  A    C  
ATOM   1481  CG  LEU A 188     -22.365  24.849  -6.692  1.00 42.85      A    C  
ANISOU 1481  CG  LEU A 188     4910   6060   5311    180    140    495  A    C  
ATOM   1482  CD1 LEU A 188     -22.088  24.098  -7.964  1.00 48.50      A    C  
ANISOU 1482  CD1 LEU A 188     5630   6755   6043    144    143    525  A    C  
ATOM   1483  CD2 LEU A 188     -21.123  24.934  -5.864  1.00 39.88      A    C  
ANISOU 1483  CD2 LEU A 188     4555   5658   4938    193    122    475  A    C  
ATOM   1484  N   ILE A 189     -24.531  28.844  -5.488  1.00 38.52      A    N  
ANISOU 1484  N   ILE A 189     4312   5546   4775    319     97    386  A    N  
ATOM   1485  CA  ILE A 189     -24.847  30.246  -5.717  1.00 40.91      A    C  
ANISOU 1485  CA  ILE A 189     4603   5824   5114    355     65    355  A    C  
ATOM   1486  C   ILE A 189     -23.783  31.079  -5.032  1.00 45.73      A    C  
ANISOU 1486  C   ILE A 189     5229   6388   5756    385     20    316  A    C  
ATOM   1487  O   ILE A 189     -23.549  30.923  -3.822  1.00 42.41      A    O  
ANISOU 1487  O   ILE A 189     4819   5993   5301    415     15    286  A    O  
ATOM   1488  CB  ILE A 189     -26.259  30.649  -5.190  1.00 39.57      A    C  
ANISOU 1488  CB  ILE A 189     4409   5714   4908    395     75    329  A    C  
ATOM   1489  CG1 ILE A 189     -27.325  29.789  -5.786  1.00 42.06      A    C  
ANISOU 1489  CG1 ILE A 189     4707   6075   5196    363    116    369  A    C  
ATOM   1490  CG2 ILE A 189     -26.540  32.064  -5.641  1.00 45.28      A    C  
ANISOU 1490  CG2 ILE A 189     5122   6400   5679    426     36    300  A    C  
ATOM   1491  CD1 ILE A 189     -28.755  30.090  -5.327  1.00 46.11      A    C  
ANISOU 1491  CD1 ILE A 189     5190   6655   5672    399    131    353  A    C  
ATOM   1492  N   GLY A 190     -23.126  31.951  -5.794  1.00 46.95      A    N  
ANISOU 1492  N   GLY A 190     5384   6476   5978    378    -14    321  A    N  
ATOM   1493  CA  GLY A 190     -21.862  32.529  -5.313  1.00 47.39      A    C  
ANISOU 1493  CA  GLY A 190     5454   6475   6076    392    -59    300  A    C  
ATOM   1494  C   GLY A 190     -21.839  33.973  -5.648  1.00 46.51      A    C  
ANISOU 1494  C   GLY A 190     5329   6309   6032    416   -111    281  A    C  
ATOM   1495  O   GLY A 190     -22.594  34.427  -6.508  1.00 48.88      A    O  
ANISOU 1495  O   GLY A 190     5613   6609   6352    411   -109    297  A    O  
ATOM   1496  N   MET A 191     -20.978  34.672  -4.938  1.00 42.28      A    N  
ANISOU 1496  N   MET A 191     4803   5726   5535    444   -165    246  A    N  
ATOM   1497  CA  MET A 191     -20.812  36.052  -5.067  1.00 46.58      A    C  
ANISOU 1497  CA  MET A 191     5337   6209   6153    470   -229    223  A    C  
ATOM   1498  C   MET A 191     -19.653  36.207  -5.981  1.00 52.26      A    C  
ANISOU 1498  C   MET A 191     6050   6862   6940    423   -245    278  A    C  
ATOM   1499  O   MET A 191     -18.734  35.355  -6.052  1.00 52.91      A    O  
ANISOU 1499  O   MET A 191     6145   6947   7012    389   -221    309  A    O  
ATOM   1500  CB  MET A 191     -20.495  36.701  -3.689  1.00 53.76      A    C  
ANISOU 1500  CB  MET A 191     6258   7101   7067    532   -286    149  A    C  
ATOM   1501  CG  MET A 191     -21.680  36.699  -2.703  1.00 59.73      A    C  
ANISOU 1501  CG  MET A 191     7011   7931   7749    593   -274     90  A    C  
ATOM   1502  SD  MET A 191     -21.255  37.291  -1.026  1.00 61.60      A    S  
ANISOU 1502  SD  MET A 191     7264   8167   7974    674   -338     -2  A    S  
ATOM   1503  CE  MET A 191     -20.395  38.803  -1.426  1.00 63.23      A    C  
ANISOU 1503  CE  MET A 191     7464   8248   8309    684   -438    -19  A    C  
ATOM   1504  N   GLU A 192     -19.687  37.303  -6.697  1.00 50.11      A    N  
ANISOU 1504  N   GLU A 192     5758   6538   6742    423   -288    294  A    N  
ATOM   1505  CA  GLU A 192     -18.663  37.587  -7.690  1.00 52.31      A    C  
ANISOU 1505  CA  GLU A 192     6022   6762   7091    378   -304    359  A    C  
ATOM   1506  C   GLU A 192     -17.302  37.528  -7.047  1.00 48.22      A    C  
ANISOU 1506  C   GLU A 192     5516   6202   6604    374   -335    353  A    C  
ATOM   1507  O   GLU A 192     -17.156  37.999  -5.956  1.00 46.82      A    O  
ANISOU 1507  O   GLU A 192     5349   6001   6437    417   -383    292  A    O  
ATOM   1508  CB  GLU A 192     -18.923  38.987  -8.250  1.00 51.16      A    C  
ANISOU 1508  CB  GLU A 192     5851   6557   7028    389   -364    368  A    C  
ATOM   1509  CG  GLU A 192     -18.943  40.079  -7.203  1.00 52.59      A    C  
ANISOU 1509  CG  GLU A 192     6035   6687   7256    445   -445    296  A    C  
ATOM   1510  CD  GLU A 192     -19.394  41.443  -7.766  1.00 55.77      A    C  
ANISOU 1510  CD  GLU A 192     6414   7033   7743    458   -508    302  A    C  
ATOM   1511  OE1 GLU A 192     -19.662  41.602  -9.004  1.00 49.76      A    O  
ANISOU 1511  OE1 GLU A 192     5630   6269   7005    422   -489    368  A    O  
ATOM   1512  OE2 GLU A 192     -19.472  42.344  -6.901  1.00 51.20      A    O1-
ANISOU 1512  OE2 GLU A 192     5838   6412   7203    511   -581    235  A    O1-
ATOM   1513  N   GLY A 193     -16.315  36.942  -7.717  1.00 53.45      A    N  
ANISOU 1513  N   GLY A 193     6172   6858   7277    328   -310    413  A    N  
ATOM   1514  CA  GLY A 193     -14.959  36.856  -7.184  1.00 55.45      A    C  
ANISOU 1514  CA  GLY A 193     6433   7072   7563    321   -339    413  A    C  
ATOM   1515  C   GLY A 193     -14.744  35.641  -6.271  1.00 53.89      A    C  
ANISOU 1515  C   GLY A 193     6267   6921   7287    327   -300    380  A    C  
ATOM   1516  O   GLY A 193     -13.648  35.388  -5.850  1.00 51.84      A    O  
ANISOU 1516  O   GLY A 193     6015   6636   7042    318   -314    381  A    O  
ATOM   1517  N   ASN A 194     -15.785  34.879  -5.975  1.00 47.03      A    N  
ANISOU 1517  N   ASN A 194     5413   6119   6335    338   -251    355  A    N  
ATOM   1518  CA  ASN A 194     -15.604  33.658  -5.202  1.00 47.99      A    C  
ANISOU 1518  CA  ASN A 194     5560   6287   6386    338   -212    337  A    C  
ATOM   1519  C   ASN A 194     -14.778  32.639  -6.010  1.00 45.31      A    C  
ANISOU 1519  C   ASN A 194     5221   5955   6038    287   -173    395  A    C  
ATOM   1520  O   ASN A 194     -15.007  32.458  -7.199  1.00 44.30      A    O  
ANISOU 1520  O   ASN A 194     5076   5840   5913    259   -145    444  A    O  
ATOM   1521  CB  ASN A 194     -16.958  33.005  -4.887  1.00 48.09      A    C  
ANISOU 1521  CB  ASN A 194     5580   6374   6319    352   -166    317  A    C  
ATOM   1522  CG  ASN A 194     -17.670  33.625  -3.686  1.00 51.06      A    C  
ANISOU 1522  CG  ASN A 194     5961   6767   6671    413   -195    249  A    C  
ATOM   1523  ND2 ASN A 194     -18.705  32.931  -3.214  1.00 54.56      A    N  
ANISOU 1523  ND2 ASN A 194     6408   7284   7037    427   -152    236  A    N  
ATOM   1524  OD1 ASN A 194     -17.295  34.690  -3.173  1.00 52.05      A    O  
ANISOU 1524  OD1 ASN A 194     6086   6844   6847    449   -257    209  A    O  
ATOM   1525  N   VAL A 195     -13.923  31.880  -5.310  1.00 47.19      A    N  
ANISOU 1525  N   VAL A 195     5480   6196   6252    283   -168    384  A    N  
ATOM   1526  CA  VAL A 195     -13.117  30.830  -5.918  1.00 42.13      A    C  
ANISOU 1526  CA  VAL A 195     4842   5566   5597    243   -134    428  A    C  
ATOM   1527  C   VAL A 195     -13.278  29.543  -5.175  1.00 39.63      A    C  
ANISOU 1527  C   VAL A 195     4553   5296   5208    243   -101    409  A    C  
ATOM   1528  O   VAL A 195     -13.269  29.530  -3.933  1.00 37.59      A    O  
ANISOU 1528  O   VAL A 195     4313   5043   4926    272   -116    365  A    O  
ATOM   1529  CB  VAL A 195     -11.613  31.252  -5.895  1.00 47.38      A    C  
ANISOU 1529  CB  VAL A 195     5500   6175   6326    234   -173    443  A    C  
ATOM   1530  CG1 VAL A 195     -10.722  30.113  -6.332  1.00 44.58      A    C  
ANISOU 1530  CG1 VAL A 195     5151   5837   5948    202   -141    477  A    C  
ATOM   1531  CG2 VAL A 195     -11.413  32.537  -6.722  1.00 49.46      A    C  
ANISOU 1531  CG2 VAL A 195     5730   6390   6672    228   -211    477  A    C  
ATOM   1532  N   THR A 196     -13.398  28.458  -5.903  1.00 36.93      A    N  
ANISOU 1532  N   THR A 196     4212   4988   4830    212    -57    443  A    N  
ATOM   1533  CA  THR A 196     -13.305  27.137  -5.347  1.00 37.01      A    C  
ANISOU 1533  CA  THR A 196     4246   5031   4782    203    -30    437  A    C  
ATOM   1534  C   THR A 196     -11.979  26.606  -5.830  1.00 38.76      A    C  
ANISOU 1534  C   THR A 196     4469   5229   5026    179    -33    464  A    C  
ATOM   1535  O   THR A 196     -11.825  26.361  -6.988  1.00 37.58      A    O  
ANISOU 1535  O   THR A 196     4304   5083   4890    158    -17    502  A    O  
ATOM   1536  CB  THR A 196     -14.414  26.212  -5.857  1.00 40.99      A    C  
ANISOU 1536  CB  THR A 196     4750   5585   5239    186     10    455  A    C  
ATOM   1537  CG2 THR A 196     -14.167  24.812  -5.464  1.00 41.30      A    C  
ANISOU 1537  CG2 THR A 196     4809   5647   5236    170     28    459  A    C  
ATOM   1538  OG1 THR A 196     -15.665  26.608  -5.338  1.00 41.21      A    O  
ANISOU 1538  OG1 THR A 196     4771   5643   5243    208     16    435  A    O  
ATOM   1539  N   PRO A 197     -11.039  26.427  -4.921  1.00 36.37      A    N  
ANISOU 1539  N   PRO A 197     4183   4905   4729    186    -54    443  A    N  
ATOM   1540  CA  PRO A 197      -9.657  26.010  -5.255  1.00 40.79      A    C  
ANISOU 1540  CA  PRO A 197     4743   5442   5313    168    -60    464  A    C  
ATOM   1541  C   PRO A 197      -9.631  24.593  -5.789  1.00 39.01      A    C  
ANISOU 1541  C   PRO A 197     4528   5250   5044    145    -27    484  A    C  
ATOM   1542  O   PRO A 197     -10.549  23.833  -5.536  1.00 38.80      A    O  
ANISOU 1542  O   PRO A 197     4514   5258   4971    142     -5    476  A    O  
ATOM   1543  CB  PRO A 197      -8.940  25.998  -3.914  1.00 41.51      A    C  
ANISOU 1543  CB  PRO A 197     4856   5511   5403    186    -89    427  A    C  
ATOM   1544  CG  PRO A 197      -9.746  26.854  -3.025  1.00 43.45      A    C  
ANISOU 1544  CG  PRO A 197     5105   5757   5645    220   -109    388  A    C  
ATOM   1545  CD  PRO A 197     -11.186  26.667  -3.471  1.00 38.70      A    C  
ANISOU 1545  CD  PRO A 197     4496   5200   5004    218    -75    396  A    C  
ATOM   1546  N   ALA A 198      -8.575  24.309  -6.514  1.00 36.06      A    N  
ANISOU 1546  N   ALA A 198     4144   4865   4690    131    -27    508  A    N  
ATOM   1547  CA  ALA A 198      -8.426  23.149  -7.333  1.00 35.66      A    C  
ANISOU 1547  CA  ALA A 198     4094   4843   4611    114     -4    530  A    C  
ATOM   1548  C   ALA A 198      -8.568  21.866  -6.570  1.00 37.84      A    C  
ANISOU 1548  C   ALA A 198     4401   5133   4842    110      3    508  A    C  
ATOM   1549  O   ALA A 198      -8.000  21.707  -5.541  1.00 33.13      A    O  
ANISOU 1549  O   ALA A 198     3824   4519   4244    117    -14    486  A    O  
ATOM   1550  CB  ALA A 198      -7.085  23.200  -8.012  1.00 38.54      A    C  
ANISOU 1550  CB  ALA A 198     4441   5193   5007    110    -13    553  A    C  
ATOM   1551  N   HIS A 199      -9.332  20.958  -7.133  1.00 35.71      A    N  
ANISOU 1551  N   HIS A 199     4135   4893   4539    100     21    516  A    N  
ATOM   1552  CA  HIS A 199      -9.599  19.663  -6.570  1.00 33.78      A    C  
ANISOU 1552  CA  HIS A 199     3914   4661   4258     90     24    507  A    C  
ATOM   1553  C   HIS A 199     -10.047  18.786  -7.680  1.00 31.81      A    C  
ANISOU 1553  C   HIS A 199     3660   4432   3993     79     34    521  A    C  
ATOM   1554  O   HIS A 199     -10.291  19.275  -8.801  1.00 32.24      A    O  
ANISOU 1554  O   HIS A 199     3692   4498   4057     83     44    536  A    O  
ATOM   1555  CB  HIS A 199     -10.695  19.696  -5.502  1.00 36.43      A    C  
ANISOU 1555  CB  HIS A 199     4261   5012   4568     93     30    495  A    C  
ATOM   1556  CG  HIS A 199     -11.990  20.207  -6.030  1.00 36.74      A    C  
ANISOU 1556  CG  HIS A 199     4283   5074   4603     95     47    504  A    C  
ATOM   1557  CD2 HIS A 199     -13.071  19.570  -6.529  1.00 39.07      A    C  
ANISOU 1557  CD2 HIS A 199     4572   5395   4877     81     61    518  A    C  
ATOM   1558  ND1 HIS A 199     -12.221  21.548  -6.209  1.00 36.45      A    N  
ANISOU 1558  ND1 HIS A 199     4228   5029   4590    110     44    500  A    N  
ATOM   1559  CE1 HIS A 199     -13.364  21.719  -6.808  1.00 39.21      A    C  
ANISOU 1559  CE1 HIS A 199     4563   5401   4932    108     59    510  A    C  
ATOM   1560  NE2 HIS A 199     -13.930  20.540  -6.969  1.00 39.38      A    N  
ANISOU 1560  NE2 HIS A 199     4591   5444   4925     91     71    520  A    N  
ATOM   1561  N   TYR A 200     -10.096  17.487  -7.398  1.00 33.46      A    N  
ANISOU 1561  N   TYR A 200     3888   4645   4179     69     28    517  A    N  
ATOM   1562  CA  TYR A 200     -10.697  16.502  -8.275  1.00 35.95      A    C  
ANISOU 1562  CA  TYR A 200     4201   4975   4481     59     28    525  A    C  
ATOM   1563  C   TYR A 200     -11.808  15.748  -7.536  1.00 37.55      A    C  
ANISOU 1563  C   TYR A 200     4415   5186   4665     43     27    530  A    C  
ATOM   1564  O   TYR A 200     -11.882  15.743  -6.287  1.00 32.98      A    O  
ANISOU 1564  O   TYR A 200     3848   4606   4075     39     27    528  A    O  
ATOM   1565  CB  TYR A 200      -9.690  15.530  -8.837  1.00 36.67      A    C  
ANISOU 1565  CB  TYR A 200     4301   5059   4572     63     10    518  A    C  
ATOM   1566  CG  TYR A 200      -9.053  14.609  -7.827  1.00 36.36      A    C  
ANISOU 1566  CG  TYR A 200     4287   4999   4528     55     -9    506  A    C  
ATOM   1567  CD1 TYR A 200      -7.881  14.945  -7.136  1.00 33.78      A    C  
ANISOU 1567  CD1 TYR A 200     3968   4655   4211     61    -15    497  A    C  
ATOM   1568  CD2 TYR A 200      -9.531  13.335  -7.675  1.00 34.81      A    C  
ANISOU 1568  CD2 TYR A 200     4104   4799   4321     40    -27    507  A    C  
ATOM   1569  CE1 TYR A 200      -7.332  14.035  -6.188  1.00 36.46      A    C  
ANISOU 1569  CE1 TYR A 200     4333   4976   4545     53    -36    488  A    C  
ATOM   1570  CE2 TYR A 200      -8.997  12.453  -6.765  1.00 35.51      A    C  
ANISOU 1570  CE2 TYR A 200     4216   4868   4407     30    -48    502  A    C  
ATOM   1571  CZ  TYR A 200      -7.861  12.823  -6.042  1.00 35.29      A    C  
ANISOU 1571  CZ  TYR A 200     4197   4825   4383     39    -51    491  A    C  
ATOM   1572  OH  TYR A 200      -7.388  11.943  -5.211  1.00 35.07      A    O  
ANISOU 1572  OH  TYR A 200     4192   4780   4352     30    -73    488  A    O  
ATOM   1573  N   GLU A 201     -12.674  15.129  -8.332  1.00 31.87      A    N  
ANISOU 1573  N   GLU A 201     3688   4479   3940     34     26    538  A    N  
ATOM   1574  CA  GLU A 201     -13.871  14.390  -7.842  1.00 35.50      A    C  
ANISOU 1574  CA  GLU A 201     4149   4950   4390     13     23    554  A    C  
ATOM   1575  C   GLU A 201     -13.741  12.946  -8.297  1.00 34.69      A    C  
ANISOU 1575  C   GLU A 201     4056   4831   4291      0     -7    553  A    C  
ATOM   1576  O   GLU A 201     -13.152  12.645  -9.338  1.00 36.76      A    O  
ANISOU 1576  O   GLU A 201     4318   5086   4561     15    -22    539  A    O  
ATOM   1577  CB  GLU A 201     -15.192  15.024  -8.444  1.00 34.93      A    C  
ANISOU 1577  CB  GLU A 201     4053   4901   4315     14     42    564  A    C  
ATOM   1578  CG  GLU A 201     -16.017  15.734  -7.446  1.00 34.29      A    C  
ANISOU 1578  CG  GLU A 201     3964   4841   4222     13     62    572  A    C  
ATOM   1579  CD  GLU A 201     -15.699  17.202  -7.300  1.00 33.47      A    C  
ANISOU 1579  CD  GLU A 201     3853   4738   4124     37     77    557  A    C  
ATOM   1580  OE1 GLU A 201     -15.390  17.929  -8.284  1.00 29.34      A    O  
ANISOU 1580  OE1 GLU A 201     3320   4208   3619     49     79    553  A    O  
ATOM   1581  OE2 GLU A 201     -15.817  17.637  -6.140  1.00 34.82      A    O1-
ANISOU 1581  OE2 GLU A 201     4028   4919   4281     46     83    552  A    O1-
ATOM   1582  N   GLU A 202     -14.215  12.033  -7.486  1.00 35.14      A    N  
ANISOU 1582  N   GLU A 202     4121   4884   4347    -21    -21    571  A    N  
ATOM   1583  CA  GLU A 202     -14.311  10.631  -7.915  1.00 39.02      A    C  
ANISOU 1583  CA  GLU A 202     4619   5352   4853    -36    -60    574  A    C  
ATOM   1584  C   GLU A 202     -15.696  10.292  -8.540  1.00 43.10      A    C  
ANISOU 1584  C   GLU A 202     5116   5877   5380    -51    -68    591  A    C  
ATOM   1585  O   GLU A 202     -16.190   9.151  -8.377  1.00 42.53      A    O  
ANISOU 1585  O   GLU A 202     5044   5788   5324    -75   -101    610  A    O  
ATOM   1586  CB  GLU A 202     -14.190   9.702  -6.686  1.00 42.80      A    C  
ANISOU 1586  CB  GLU A 202     5112   5817   5333    -60    -81    596  A    C  
ATOM   1587  CG  GLU A 202     -12.822   9.500  -6.152  1.00 49.86      A    C  
ANISOU 1587  CG  GLU A 202     6029   6691   6225    -51    -93    577  A    C  
ATOM   1588  CD  GLU A 202     -12.824   8.465  -5.007  1.00 50.09      A    C  
ANISOU 1588  CD  GLU A 202     6069   6705   6256    -76   -117    605  A    C  
ATOM   1589  OE1 GLU A 202     -13.674   8.578  -4.071  1.00 40.33      A    O  
ANISOU 1589  OE1 GLU A 202     4822   5494   5006    -93    -99    641  A    O  
ATOM   1590  OE2 GLU A 202     -11.971   7.582  -5.070  1.00 43.28      A    O1-
ANISOU 1590  OE2 GLU A 202     5225   5811   5408    -77   -153    592  A    O1-
ATOM   1591  N   GLN A 203     -16.337  11.271  -9.169  1.00 40.40      A    N  
ANISOU 1591  N   GLN A 203     4756   5561   5032    -38    -40    589  A    N  
ATOM   1592  CA  GLN A 203     -17.486  11.058 -10.048  1.00 36.48      A    C  
ANISOU 1592  CA  GLN A 203     4242   5072   4547    -44    -48    597  A    C  
ATOM   1593  C   GLN A 203     -17.317  11.906 -11.338  1.00 36.65      A    C  
ANISOU 1593  C   GLN A 203     4255   5108   4562    -13    -34    573  A    C  
ATOM   1594  O   GLN A 203     -16.534  12.854 -11.319  1.00 39.41      A    O  
ANISOU 1594  O   GLN A 203     4606   5465   4901      4    -10    564  A    O  
ATOM   1595  CB  GLN A 203     -18.737  11.514  -9.345  1.00 36.98      A    C  
ANISOU 1595  CB  GLN A 203     4285   5162   4603    -61    -22    628  A    C  
ATOM   1596  CG  GLN A 203     -19.179  10.630  -8.169  1.00 40.34      A    C  
ANISOU 1596  CG  GLN A 203     4708   5586   5032    -94    -35    665  A    C  
ATOM   1597  CD  GLN A 203     -20.575  10.915  -7.608  1.00 43.68      A    C  
ANISOU 1597  CD  GLN A 203     5102   6046   5447   -110    -11    703  A    C  
ATOM   1598  NE2 GLN A 203     -20.657  10.951  -6.268  1.00 43.87      A    N  
ANISOU 1598  NE2 GLN A 203     5122   6095   5450   -119      6    731  A    N  
ATOM   1599  OE1 GLN A 203     -21.595  10.977  -8.343  1.00 40.03      A    O  
ANISOU 1599  OE1 GLN A 203     4619   5592   4997   -116    -12    710  A    O  
ATOM   1600  N   GLN A 204     -18.092  11.583 -12.366  1.00 36.63      A    N  
ANISOU 1600  N   GLN A 204     4240   5109   4568    -10    -51    570  A    N  
ATOM   1601  CA  GLN A 204     -18.247  12.382 -13.551  1.00 36.02      A    C  
ANISOU 1601  CA  GLN A 204     4149   5053   4482     16    -35    558  A    C  
ATOM   1602  C   GLN A 204     -19.146  13.542 -13.326  1.00 36.38      A    C  
ANISOU 1602  C   GLN A 204     4176   5122   4522     11      0    575  A    C  
ATOM   1603  O   GLN A 204     -20.121  13.481 -12.486  1.00 37.56      A    O  
ANISOU 1603  O   GLN A 204     4318   5276   4676    -12      9    597  A    O  
ATOM   1604  CB  GLN A 204     -18.774  11.517 -14.686  1.00 40.25      A    C  
ANISOU 1604  CB  GLN A 204     4680   5583   5028     25    -74    542  A    C  
ATOM   1605  CG  GLN A 204     -18.035  10.184 -14.839  1.00 41.00      A    C  
ANISOU 1605  CG  GLN A 204     4794   5650   5132     30   -125    520  A    C  
ATOM   1606  CD  GLN A 204     -16.787  10.324 -15.699  1.00 39.88      A    C  
ANISOU 1606  CD  GLN A 204     4657   5522   4970     72   -127    490  A    C  
ATOM   1607  NE2 GLN A 204     -16.186   9.202 -16.092  1.00 36.13      A    N  
ANISOU 1607  NE2 GLN A 204     4196   5030   4500     90   -175    460  A    N  
ATOM   1608  OE1 GLN A 204     -16.381  11.442 -15.983  1.00 35.88      A    O  
ANISOU 1608  OE1 GLN A 204     4141   5045   4446     89    -87    495  A    O  
ATOM   1609  N   ASN A 205     -18.909  14.622 -14.073  1.00 34.59      A    N  
ANISOU 1609  N   ASN A 205     3939   4912   4288     35     23    569  A    N  
ATOM   1610  CA  ASN A 205     -19.660  15.872 -13.806  1.00 34.59      A    C  
ANISOU 1610  CA  ASN A 205     3923   4931   4287     34     55    583  A    C  
ATOM   1611  C   ASN A 205     -20.023  16.615 -15.100  1.00 38.57      A    C  
ANISOU 1611  C   ASN A 205     4409   5454   4790     56     64    582  A    C  
ATOM   1612  O   ASN A 205     -19.164  16.866 -15.942  1.00 38.50      A    O  
ANISOU 1612  O   ASN A 205     4399   5451   4776     78     63    577  A    O  
ATOM   1613  CB  ASN A 205     -18.894  16.723 -12.822  1.00 36.33      A    C  
ANISOU 1613  CB  ASN A 205     4149   5146   4506     38     75    583  A    C  
ATOM   1614  CG  ASN A 205     -19.567  18.049 -12.481  1.00 37.96      A    C  
ANISOU 1614  CG  ASN A 205     4342   5366   4715     44     99    588  A    C  
ATOM   1615  ND2 ASN A 205     -18.940  18.745 -11.572  1.00 35.63      A    N  
ANISOU 1615  ND2 ASN A 205     4052   5062   4421     51    108    583  A    N  
ATOM   1616  OD1 ASN A 205     -20.633  18.446 -12.991  1.00 39.22      A    O  
ANISOU 1616  OD1 ASN A 205     4483   5541   4875     46    108    595  A    O  
ATOM   1617  N   PHE A 206     -21.321  16.802 -15.313  1.00 39.32      A    N  
ANISOU 1617  N   PHE A 206     4489   5561   4889     49     69    591  A    N  
ATOM   1618  CA  PHE A 206     -21.803  17.829 -16.222  1.00 38.59      A    C  
ANISOU 1618  CA  PHE A 206     4377   5487   4795     66     84    595  A    C  
ATOM   1619  C   PHE A 206     -22.240  19.020 -15.398  1.00 39.09      A    C  
ANISOU 1619  C   PHE A 206     4432   5556   4865     63    109    603  A    C  
ATOM   1620  O   PHE A 206     -23.185  18.938 -14.569  1.00 41.15      A    O  
ANISOU 1620  O   PHE A 206     4687   5822   5124     49    116    608  A    O  
ATOM   1621  CB  PHE A 206     -22.910  17.373 -17.074  1.00 37.88      A    C  
ANISOU 1621  CB  PHE A 206     4277   5408   4708     66     70    594  A    C  
ATOM   1622  CG  PHE A 206     -22.523  16.426 -18.132  1.00 36.07      A    C  
ANISOU 1622  CG  PHE A 206     4054   5179   4472     82     40    577  A    C  
ATOM   1623  CD1 PHE A 206     -21.818  16.845 -19.213  1.00 37.96      A    C  
ANISOU 1623  CD1 PHE A 206     4288   5439   4696    114     43    573  A    C  
ATOM   1624  CD2 PHE A 206     -22.993  15.143 -18.111  1.00 35.82      A    C  
ANISOU 1624  CD2 PHE A 206     4027   5131   4449     69      5    568  A    C  
ATOM   1625  CE1 PHE A 206     -21.537  15.970 -20.240  1.00 35.42      A    C  
ANISOU 1625  CE1 PHE A 206     3970   5126   4361    137     13    552  A    C  
ATOM   1626  CE2 PHE A 206     -22.711  14.245 -19.115  1.00 36.83      A    C  
ANISOU 1626  CE2 PHE A 206     4162   5258   4573     90    -31    545  A    C  
ATOM   1627  CZ  PHE A 206     -21.976  14.655 -20.187  1.00 39.06      A    C  
ANISOU 1627  CZ  PHE A 206     4442   5566   4833    128    -26    533  A    C  
ATOM   1628  N   PHE A 207     -21.490  20.102 -15.609  1.00 32.42      A    N  
ANISOU 1628  N   PHE A 207     3583   4708   4026     80    121    606  A    N  
ATOM   1629  CA  PHE A 207     -21.526  21.317 -14.874  1.00 32.98      A    C  
ANISOU 1629  CA  PHE A 207     3649   4774   4109     85    133    607  A    C  
ATOM   1630  C   PHE A 207     -22.298  22.378 -15.648  1.00 35.58      A    C  
ANISOU 1630  C   PHE A 207     3955   5113   4447     98    140    616  A    C  
ATOM   1631  O   PHE A 207     -21.797  22.864 -16.653  1.00 35.60      A    O  
ANISOU 1631  O   PHE A 207     3949   5119   4458    110    139    629  A    O  
ATOM   1632  CB  PHE A 207     -20.095  21.707 -14.692  1.00 34.59      A    C  
ANISOU 1632  CB  PHE A 207     3859   4959   4322     92    130    608  A    C  
ATOM   1633  CG  PHE A 207     -19.873  22.929 -13.846  1.00 33.14      A    C  
ANISOU 1633  CG  PHE A 207     3673   4759   4159    100    131    604  A    C  
ATOM   1634  CD1 PHE A 207     -19.747  24.159 -14.420  1.00 39.06      A    C  
ANISOU 1634  CD1 PHE A 207     4405   5501   4933    112    130    616  A    C  
ATOM   1635  CD2 PHE A 207     -19.665  22.814 -12.528  1.00 38.36      A    C  
ANISOU 1635  CD2 PHE A 207     4348   5410   4814     98    129    588  A    C  
ATOM   1636  CE1 PHE A 207     -19.471  25.260 -13.653  1.00 38.47      A    C  
ANISOU 1636  CE1 PHE A 207     4327   5402   4884    122    120    609  A    C  
ATOM   1637  CE2 PHE A 207     -19.368  23.896 -11.759  1.00 37.47      A    C  
ANISOU 1637  CE2 PHE A 207     4235   5280   4720    111    123    577  A    C  
ATOM   1638  CZ  PHE A 207     -19.267  25.114 -12.320  1.00 39.56      A    C  
ANISOU 1638  CZ  PHE A 207     4482   5531   5016    123    115    584  A    C  
ATOM   1639  N   ALA A 208     -23.557  22.622 -15.246  1.00 34.81      A    N  
ANISOU 1639  N   ALA A 208     3849   5029   4348     95    147    612  A    N  
ATOM   1640  CA  ALA A 208     -24.506  23.429 -16.008  1.00 37.33      A    C  
ANISOU 1640  CA  ALA A 208     4148   5359   4675    105    152    619  A    C  
ATOM   1641  C   ALA A 208     -24.661  24.836 -15.465  1.00 36.87      A    C  
ANISOU 1641  C   ALA A 208     4079   5293   4636    120    153    613  A    C  
ATOM   1642  O   ALA A 208     -25.270  25.088 -14.396  1.00 38.07      A    O  
ANISOU 1642  O   ALA A 208     4229   5452   4783    125    158    598  A    O  
ATOM   1643  CB  ALA A 208     -25.827  22.730 -16.041  1.00 39.95      A    C  
ANISOU 1643  CB  ALA A 208     4471   5711   4996     94    153    618  A    C  
ATOM   1644  N   GLN A 209     -24.107  25.773 -16.221  1.00 37.65      A    N  
ANISOU 1644  N   GLN A 209     4169   5377   4757    131    147    627  A    N  
ATOM   1645  CA  GLN A 209     -24.119  27.180 -15.816  1.00 38.97      A    C  
ANISOU 1645  CA  GLN A 209     4327   5525   4954    146    137    623  A    C  
ATOM   1646  C   GLN A 209     -25.486  27.823 -16.177  1.00 41.49      A    C  
ANISOU 1646  C   GLN A 209     4627   5859   5277    157    138    620  A    C  
ATOM   1647  O   GLN A 209     -26.053  27.580 -17.312  1.00 35.56      A    O  
ANISOU 1647  O   GLN A 209     3866   5126   4519    154    144    637  A    O  
ATOM   1648  CB  GLN A 209     -22.999  27.876 -16.535  1.00 38.47      A    C  
ANISOU 1648  CB  GLN A 209     4255   5440   4919    150    126    650  A    C  
ATOM   1649  CG  GLN A 209     -22.678  29.271 -16.048  1.00 38.04      A    C  
ANISOU 1649  CG  GLN A 209     4193   5351   4909    163    104    647  A    C  
ATOM   1650  CD  GLN A 209     -22.297  29.333 -14.576  1.00 37.01      A    C  
ANISOU 1650  CD  GLN A 209     4078   5201   4781    169     93    614  A    C  
ATOM   1651  NE2 GLN A 209     -22.299  30.537 -14.052  1.00 41.78      A    N  
ANISOU 1651  NE2 GLN A 209     4676   5776   5423    188     67    600  A    N  
ATOM   1652  OE1 GLN A 209     -22.008  28.334 -13.912  1.00 36.04      A    O  
ANISOU 1652  OE1 GLN A 209     3974   5089   4629    161    105    600  A    O  
ATOM   1653  N   ILE A 210     -25.975  28.645 -15.242  1.00 40.91      A    N  
ANISOU 1653  N   ILE A 210     4549   5779   5214    173    132    597  A    N  
ATOM   1654  CA  ILE A 210     -27.380  29.135 -15.296  1.00 41.65      A    C  
ANISOU 1654  CA  ILE A 210     4626   5893   5307    187    135    585  A    C  
ATOM   1655  C   ILE A 210     -27.354  30.641 -15.275  1.00 42.38      A    C  
ANISOU 1655  C   ILE A 210     4706   5955   5439    211    109    578  A    C  
ATOM   1656  O   ILE A 210     -27.867  31.264 -16.191  1.00 42.15      A    O  
ANISOU 1656  O   ILE A 210     4662   5924   5428    215    103    594  A    O  
ATOM   1657  CB  ILE A 210     -28.173  28.593 -14.090  1.00 42.38      A    C  
ANISOU 1657  CB  ILE A 210     4718   6016   5366    192    148    561  A    C  
ATOM   1658  CG1 ILE A 210     -28.592  27.171 -14.369  1.00 40.75      A    C  
ANISOU 1658  CG1 ILE A 210     4514   5837   5132    165    166    577  A    C  
ATOM   1659  CG2 ILE A 210     -29.421  29.409 -13.719  1.00 45.12      A    C  
ANISOU 1659  CG2 ILE A 210     5045   6384   5713    217    146    540  A    C  
ATOM   1660  CD1 ILE A 210     -28.804  26.393 -13.086  1.00 42.15      A    C  
ANISOU 1660  CD1 ILE A 210     4694   6039   5279    160    178    568  A    C  
ATOM   1661  N   LYS A 211     -26.705  31.222 -14.268  1.00 42.00      A    N  
ANISOU 1661  N   LYS A 211     4666   5882   5407    225     90    555  A    N  
ATOM   1662  CA  LYS A 211     -26.568  32.649 -14.212  1.00 40.39      A    C  
ANISOU 1662  CA  LYS A 211     4452   5640   5252    248     54    545  A    C  
ATOM   1663  C   LYS A 211     -25.149  33.106 -13.990  1.00 42.61      A    C  
ANISOU 1663  C   LYS A 211     4742   5874   5572    246     28    554  A    C  
ATOM   1664  O   LYS A 211     -24.454  32.629 -13.074  1.00 43.92      A    O  
ANISOU 1664  O   LYS A 211     4924   6037   5723    246     29    535  A    O  
ATOM   1665  CB  LYS A 211     -27.404  33.226 -13.092  1.00 41.86      A    C  
ANISOU 1665  CB  LYS A 211     4635   5838   5430    284     42    497  A    C  
ATOM   1666  CG  LYS A 211     -27.350  34.751 -13.010  1.00 47.40      A    C  
ANISOU 1666  CG  LYS A 211     5325   6494   6188    315     -6    479  A    C  
ATOM   1667  CD  LYS A 211     -28.152  35.173 -11.777  1.00 52.96      A    C  
ANISOU 1667  CD  LYS A 211     6028   7221   6871    360    -18    419  A    C  
ATOM   1668  CE  LYS A 211     -28.197  36.697 -11.599  1.00 58.19      A    C  
ANISOU 1668  CE  LYS A 211     6681   7835   7592    398    -76    388  A    C  
ATOM   1669  NZ  LYS A 211     -28.871  37.329 -12.765  1.00 60.01      A    N1+
ANISOU 1669  NZ  LYS A 211     6892   8053   7856    391    -85    415  A    N1+
ATOM   1670  N   GLY A 212     -24.759  34.166 -14.703  1.00 40.29      A    N  
ANISOU 1670  N   GLY A 212     4433   5541   5334    246     -2    581  A    N  
ATOM   1671  CA  GLY A 212     -23.400  34.697 -14.509  1.00 43.28      A    C  
ANISOU 1671  CA  GLY A 212     4812   5871   5760    241    -33    596  A    C  
ATOM   1672  C   GLY A 212     -22.311  33.897 -15.227  1.00 40.31      A    C  
ANISOU 1672  C   GLY A 212     4437   5503   5374    211    -11    643  A    C  
ATOM   1673  O   GLY A 212     -22.585  32.931 -15.978  1.00 38.35      A    O  
ANISOU 1673  O   GLY A 212     4192   5298   5083    196     24    662  A    O  
ATOM   1674  N   TYR A 213     -21.045  34.263 -14.983  1.00 46.01      A    N  
ANISOU 1674  N   TYR A 213     5158   6186   6137    205    -36    658  A    N  
ATOM   1675  CA  TYR A 213     -19.935  33.650 -15.685  1.00 38.73      A    C  
ANISOU 1675  CA  TYR A 213     4230   5273   5210    180    -19    706  A    C  
ATOM   1676  C   TYR A 213     -18.974  33.003 -14.707  1.00 43.19      A    C  
ANISOU 1676  C   TYR A 213     4816   5828   5762    177    -18    681  A    C  
ATOM   1677  O   TYR A 213     -18.624  33.597 -13.686  1.00 40.44      A    O  
ANISOU 1677  O   TYR A 213     4476   5440   5447    191    -52    649  A    O  
ATOM   1678  CB  TYR A 213     -19.244  34.660 -16.599  1.00 42.13      A    C  
ANISOU 1678  CB  TYR A 213     4628   5674   5702    170    -45    767  A    C  
ATOM   1679  CG  TYR A 213     -20.187  35.059 -17.726  1.00 47.87      A    C  
ANISOU 1679  CG  TYR A 213     5335   6424   6428    172    -37    798  A    C  
ATOM   1680  CD1 TYR A 213     -21.171  36.092 -17.552  1.00 51.32      A    C  
ANISOU 1680  CD1 TYR A 213     5765   6834   6900    189    -67    778  A    C  
ATOM   1681  CD2 TYR A 213     -20.165  34.387 -18.917  1.00 46.45      A    C  
ANISOU 1681  CD2 TYR A 213     5145   6294   6209    161     -3    839  A    C  
ATOM   1682  CE1 TYR A 213     -22.078  36.416 -18.553  1.00 51.22      A    C  
ANISOU 1682  CE1 TYR A 213     5735   6842   6883    191    -60    804  A    C  
ATOM   1683  CE2 TYR A 213     -21.097  34.678 -19.904  1.00 51.15      A    C  
ANISOU 1683  CE2 TYR A 213     5724   6912   6795    166      6    862  A    C  
ATOM   1684  CZ  TYR A 213     -22.023  35.701 -19.734  1.00 56.76      A    C  
ANISOU 1684  CZ  TYR A 213     6428   7595   7544    179    -23    847  A    C  
ATOM   1685  OH  TYR A 213     -22.861  35.959 -20.789  1.00 57.86      A    O  
ANISOU 1685  OH  TYR A 213     6550   7759   7675    181    -15    874  A    O  
ATOM   1686  N   LYS A 214     -18.524  31.791 -15.035  1.00 40.52      A    N  
ANISOU 1686  N   LYS A 214     4490   5526   5380    163     14    693  A    N  
ATOM   1687  CA  LYS A 214     -17.443  31.167 -14.259  1.00 39.78      A    C  
ANISOU 1687  CA  LYS A 214     4414   5421   5279    157     13    679  A    C  
ATOM   1688  C   LYS A 214     -16.277  30.792 -15.161  1.00 39.32      A    C  
ANISOU 1688  C   LYS A 214     4340   5373   5224    141     24    729  A    C  
ATOM   1689  O   LYS A 214     -16.493  30.240 -16.256  1.00 42.61      A    O  
ANISOU 1689  O   LYS A 214     4747   5831   5610    136     49    756  A    O  
ATOM   1690  CB  LYS A 214     -17.917  29.907 -13.554  1.00 39.43      A    C  
ANISOU 1690  CB  LYS A 214     4398   5409   5174    157     40    640  A    C  
ATOM   1691  CG  LYS A 214     -18.582  30.187 -12.241  1.00 40.29      A    C  
ANISOU 1691  CG  LYS A 214     4522   5509   5275    176     27    590  A    C  
ATOM   1692  CD  LYS A 214     -19.185  28.946 -11.617  1.00 40.57      A    C  
ANISOU 1692  CD  LYS A 214     4578   5584   5251    173     56    564  A    C  
ATOM   1693  CE  LYS A 214     -19.781  29.272 -10.242  1.00 43.68      A    C  
ANISOU 1693  CE  LYS A 214     4982   5983   5631    199     45    519  A    C  
ATOM   1694  NZ  LYS A 214     -20.241  28.037  -9.586  1.00 42.00      A    N1+
ANISOU 1694  NZ  LYS A 214     4784   5810   5362    191     72    507  A    N1+
ATOM   1695  N   ARG A 215     -15.053  31.085 -14.697  1.00 35.58      A    N  
ANISOU 1695  N   ARG A 215     3863   4865   4788    135      2    738  A    N  
ATOM   1696  CA  ARG A 215     -13.820  30.597 -15.391  1.00 33.49      A    C  
ANISOU 1696  CA  ARG A 215     3584   4619   4522    123     12    782  A    C  
ATOM   1697  C   ARG A 215     -13.428  29.296 -14.741  1.00 33.10      A    C  
ANISOU 1697  C   ARG A 215     3565   4585   4425    121     30    745  A    C  
ATOM   1698  O   ARG A 215     -13.287  29.210 -13.495  1.00 37.67      A    O  
ANISOU 1698  O   ARG A 215     4169   5137   5007    126     15    704  A    O  
ATOM   1699  CB  ARG A 215     -12.747  31.604 -15.170  1.00 40.28      A    C  
ANISOU 1699  CB  ARG A 215     4421   5430   5453    116    -24    812  A    C  
ATOM   1700  CG  ARG A 215     -11.450  31.358 -15.848  1.00 44.96      A    C  
ANISOU 1700  CG  ARG A 215     4987   6040   6055    105    -16    866  A    C  
ATOM   1701  CD  ARG A 215     -10.397  31.961 -14.963  1.00 48.39      A    C  
ANISOU 1701  CD  ARG A 215     5417   6416   6551     99    -56    865  A    C  
ATOM   1702  NE  ARG A 215      -9.150  32.017 -15.699  1.00 47.45      A    N  
ANISOU 1702  NE  ARG A 215     5260   6311   6455     85    -53    931  A    N  
ATOM   1703  CZ  ARG A 215      -8.077  32.650 -15.253  1.00 53.84      A    C  
ANISOU 1703  CZ  ARG A 215     6051   7075   7332     75    -90    954  A    C  
ATOM   1704  NH1 ARG A 215      -8.071  33.314 -14.076  1.00 47.58      A    N1+
ANISOU 1704  NH1 ARG A 215     5275   6213   6590     80   -138    911  A    N1+
ATOM   1705  NH2 ARG A 215      -6.985  32.606 -16.011  1.00 54.96      A    N  
ANISOU 1705  NH2 ARG A 215     6151   7241   7487     63    -82   1021  A    N  
ATOM   1706  N   CYS A 216     -13.301  28.265 -15.562  1.00 34.37      A    N  
ANISOU 1706  N   CYS A 216     3727   4792   4539    120     59    759  A    N  
ATOM   1707  CA  CYS A 216     -13.022  26.954 -15.063  1.00 32.84      A    C  
ANISOU 1707  CA  CYS A 216     3561   4613   4301    118     71    726  A    C  
ATOM   1708  C   CYS A 216     -11.661  26.607 -15.605  1.00 39.21      A    C  
ANISOU 1708  C   CYS A 216     4353   5433   5110    117     74    757  A    C  
ATOM   1709  O   CYS A 216     -11.451  26.581 -16.858  1.00 36.56      A    O  
ANISOU 1709  O   CYS A 216     3989   5137   4762    123     88    798  A    O  
ATOM   1710  CB  CYS A 216     -14.024  26.003 -15.600  1.00 36.10      A    C  
ANISOU 1710  CB  CYS A 216     3986   5066   4664    121     93    712  A    C  
ATOM   1711  SG  CYS A 216     -15.752  26.445 -15.158  1.00 39.47      A    S  
ANISOU 1711  SG  CYS A 216     4421   5488   5086    123     94    685  A    S  
ATOM   1712  N   ILE A 217     -10.730  26.388 -14.681  1.00 38.45      A    N  
ANISOU 1712  N   ILE A 217     4271   5310   5027    113     61    740  A    N  
ATOM   1713  CA  ILE A 217      -9.376  25.901 -15.073  1.00 40.15      A    C  
ANISOU 1713  CA  ILE A 217     4473   5542   5240    113     64    763  A    C  
ATOM   1714  C   ILE A 217      -9.181  24.440 -14.688  1.00 36.30      A    C  
ANISOU 1714  C   ILE A 217     4018   5070   4704    116     72    724  A    C  
ATOM   1715  O   ILE A 217      -9.210  24.110 -13.528  1.00 36.94      A    O  
ANISOU 1715  O   ILE A 217     4129   5121   4784    112     62    687  A    O  
ATOM   1716  CB  ILE A 217      -8.277  26.735 -14.459  1.00 35.82      A    C  
ANISOU 1716  CB  ILE A 217     3909   4950   4750    105     37    781  A    C  
ATOM   1717  CG1 ILE A 217      -8.420  28.208 -14.828  1.00 38.93      A    C  
ANISOU 1717  CG1 ILE A 217     4267   5318   5203    100     18    823  A    C  
ATOM   1718  CG2 ILE A 217      -6.940  26.235 -15.003  1.00 38.90      A    C  
ANISOU 1718  CG2 ILE A 217     4278   5365   5134    107     44    811  A    C  
ATOM   1719  CD1 ILE A 217      -7.709  29.179 -13.901  1.00 41.15      A    C  
ANISOU 1719  CD1 ILE A 217     4542   5535   5555     93    -22    824  A    C  
ATOM   1720  N   LEU A 218      -8.947  23.585 -15.673  1.00 32.37      A    N  
ANISOU 1720  N   LEU A 218     3512   4618   4168    128     87    734  A    N  
ATOM   1721  CA  LEU A 218      -8.826  22.167 -15.458  1.00 32.94      A    C  
ANISOU 1721  CA  LEU A 218     3614   4703   4199    132     88    696  A    C  
ATOM   1722  C   LEU A 218      -7.415  21.683 -15.662  1.00 34.67      A    C  
ANISOU 1722  C   LEU A 218     3822   4936   4413    143     85    706  A    C  
ATOM   1723  O   LEU A 218      -6.697  22.224 -16.490  1.00 36.48      A    O  
ANISOU 1723  O   LEU A 218     4014   5193   4654    151     93    748  A    O  
ATOM   1724  CB  LEU A 218      -9.721  21.441 -16.482  1.00 32.58      A    C  
ANISOU 1724  CB  LEU A 218     3568   4699   4110    146     99    689  A    C  
ATOM   1725  CG  LEU A 218     -11.150  21.198 -15.992  1.00 30.67      A    C  
ANISOU 1725  CG  LEU A 218     3351   4441   3859    135     99    661  A    C  
ATOM   1726  CD1 LEU A 218     -11.843  22.527 -15.649  1.00 29.77      A    C  
ANISOU 1726  CD1 LEU A 218     3226   4307   3778    125    101    676  A    C  
ATOM   1727  CD2 LEU A 218     -11.943  20.418 -16.988  1.00 32.58      A    C  
ANISOU 1727  CD2 LEU A 218     3593   4720   4065    148    102    653  A    C  
ATOM   1728  N   PHE A 219      -7.051  20.629 -14.966  1.00 35.47      A    N  
ANISOU 1728  N   PHE A 219     3955   5024   4497    142     75    669  A    N  
ATOM   1729  CA  PHE A 219      -5.790  19.915 -15.215  1.00 37.59      A    C  
ANISOU 1729  CA  PHE A 219     4215   5311   4752    156     71    667  A    C  
ATOM   1730  C   PHE A 219      -6.006  18.402 -15.246  1.00 36.10      A    C  
ANISOU 1730  C   PHE A 219     4058   5134   4523    167     60    625  A    C  
ATOM   1731  O   PHE A 219      -6.741  17.846 -14.448  1.00 35.96      A    O  
ANISOU 1731  O   PHE A 219     4074   5088   4501    152     50    594  A    O  
ATOM   1732  CB  PHE A 219      -4.738  20.266 -14.112  1.00 35.83      A    C  
ANISOU 1732  CB  PHE A 219     3999   5047   4568    143     55    666  A    C  
ATOM   1733  CG  PHE A 219      -4.700  21.737 -13.751  1.00 36.11      A    C  
ANISOU 1733  CG  PHE A 219     4014   5050   4656    129     51    696  A    C  
ATOM   1734  CD1 PHE A 219      -5.611  22.255 -12.890  1.00 36.47      A    C  
ANISOU 1734  CD1 PHE A 219     4080   5058   4716    116     43    677  A    C  
ATOM   1735  CD2 PHE A 219      -3.714  22.597 -14.283  1.00 35.84      A    C  
ANISOU 1735  CD2 PHE A 219     3934   5024   4658    130     51    747  A    C  
ATOM   1736  CE1 PHE A 219      -5.573  23.560 -12.506  1.00 35.99      A    C  
ANISOU 1736  CE1 PHE A 219     4003   4963   4707    109     29    695  A    C  
ATOM   1737  CE2 PHE A 219      -3.685  23.925 -13.924  1.00 35.15      A    C  
ANISOU 1737  CE2 PHE A 219     3828   4897   4628    115     35    773  A    C  
ATOM   1738  CZ  PHE A 219      -4.631  24.420 -13.058  1.00 42.42      A    C  
ANISOU 1738  CZ  PHE A 219     4775   5776   5565    107     22    744  A    C  
ATOM   1739  N   PRO A 220      -5.419  17.749 -16.226  1.00 39.86      A    N  
ANISOU 1739  N   PRO A 220     4519   5656   4969    196     60    623  A    N  
ATOM   1740  CA  PRO A 220      -5.536  16.329 -16.313  1.00 35.09      A    C  
ANISOU 1740  CA  PRO A 220     3941   5056   4333    210     40    580  A    C  
ATOM   1741  C   PRO A 220      -4.992  15.536 -15.162  1.00 33.29      A    C  
ANISOU 1741  C   PRO A 220     3747   4787   4115    197     18    550  A    C  
ATOM   1742  O   PRO A 220      -4.135  16.010 -14.341  1.00 36.19      A    O  
ANISOU 1742  O   PRO A 220     4114   5127   4507    184     18    559  A    O  
ATOM   1743  CB  PRO A 220      -4.769  15.951 -17.565  1.00 38.71      A    C  
ANISOU 1743  CB  PRO A 220     4369   5577   4758    253     42    584  A    C  
ATOM   1744  CG  PRO A 220      -4.247  17.190 -18.119  1.00 43.87      A    C  
ANISOU 1744  CG  PRO A 220     4978   6264   5426    256     68    640  A    C  
ATOM   1745  CD  PRO A 220      -4.453  18.309 -17.180  1.00 41.73      A    C  
ANISOU 1745  CD  PRO A 220     4709   5941   5204    217     74    665  A    C  
ATOM   1746  N   PRO A 221      -5.489  14.297 -15.061  1.00 36.17      A    N  
ANISOU 1746  N   PRO A 221     4141   5140   4461    200     -6    513  A    N  
ATOM   1747  CA  PRO A 221      -5.135  13.475 -13.903  1.00 34.83      A    C  
ANISOU 1747  CA  PRO A 221     4005   4926   4301    183    -29    487  A    C  
ATOM   1748  C   PRO A 221      -3.608  13.246 -13.836  1.00 33.91      A    C  
ANISOU 1748  C   PRO A 221     3882   4816   4186    201    -38    481  A    C  
ATOM   1749  O   PRO A 221      -3.055  13.038 -12.763  1.00 34.10      A    O  
ANISOU 1749  O   PRO A 221     3926   4802   4225    185    -50    472  A    O  
ATOM   1750  CB  PRO A 221      -5.828  12.160 -14.196  1.00 35.25      A    C  
ANISOU 1750  CB  PRO A 221     4079   4974   4337    190    -60    455  A    C  
ATOM   1751  CG  PRO A 221      -7.032  12.561 -15.023  1.00 35.97      A    C  
ANISOU 1751  CG  PRO A 221     4157   5090   4420    192    -47    466  A    C  
ATOM   1752  CD  PRO A 221      -6.603  13.724 -15.846  1.00 35.28      A    C  
ANISOU 1752  CD  PRO A 221     4031   5044   4327    210    -14    498  A    C  
ATOM   1753  N   ASP A 222      -2.967  13.220 -14.998  1.00 37.73      A    N  
ANISOU 1753  N   ASP A 222     4336   5352   4648    238    -33    485  A    N  
ATOM   1754  CA  ASP A 222      -1.529  13.101 -15.018  1.00 33.75      A    C  
ANISOU 1754  CA  ASP A 222     3815   4863   4143    258    -36    485  A    C  
ATOM   1755  C   ASP A 222      -0.745  14.267 -14.429  1.00 37.96      A    C  
ANISOU 1755  C   ASP A 222     4328   5381   4711    237    -16    523  A    C  
ATOM   1756  O   ASP A 222       0.433  14.223 -14.524  1.00 38.77      A    O  
ANISOU 1756  O   ASP A 222     4412   5502   4816    253    -18    529  A    O  
ATOM   1757  CB  ASP A 222      -1.041  12.722 -16.385  1.00 37.65      A    C  
ANISOU 1757  CB  ASP A 222     4278   5427   4600    308    -36    481  A    C  
ATOM   1758  CG  ASP A 222      -0.914  13.903 -17.324  1.00 42.81      A    C  
ANISOU 1758  CG  ASP A 222     4881   6135   5249    320      2    533  A    C  
ATOM   1759  OD1 ASP A 222      -1.205  15.051 -16.974  1.00 46.25      A    O  
ANISOU 1759  OD1 ASP A 222     5306   6550   5716    288     22    573  A    O  
ATOM   1760  OD2 ASP A 222      -0.527  13.661 -18.451  1.00 47.04      A    O1-
ANISOU 1760  OD2 ASP A 222     5387   6739   5747    365      6    535  A    O1-
ATOM   1761  N   GLN A 223      -1.362  15.324 -13.914  1.00 35.67      A    N  
ANISOU 1761  N   GLN A 223     4037   5064   4450    207     -1    549  A    N  
ATOM   1762  CA  GLN A 223      -0.657  16.402 -13.222  1.00 35.89      A    C  
ANISOU 1762  CA  GLN A 223     4050   5065   4521    189      4    577  A    C  
ATOM   1763  C   GLN A 223      -0.674  16.216 -11.728  1.00 36.06      A    C  
ANISOU 1763  C   GLN A 223     4112   5026   4561    165    -15    550  A    C  
ATOM   1764  O   GLN A 223      -0.364  17.147 -10.957  1.00 31.62      A    O  
ANISOU 1764  O   GLN A 223     3546   4430   4036    148    -17    564  A    O  
ATOM   1765  CB  GLN A 223      -1.333  17.700 -13.474  1.00 40.56      A    C  
ANISOU 1765  CB  GLN A 223     4619   5655   5135    175     21    615  A    C  
ATOM   1766  CG  GLN A 223      -1.620  17.953 -14.914  1.00 57.25      A    C  
ANISOU 1766  CG  GLN A 223     6695   7829   7227    196     42    645  A    C  
ATOM   1767  CD  GLN A 223      -0.628  18.870 -15.514  1.00 57.08      A    C  
ANISOU 1767  CD  GLN A 223     6621   7837   7229    203     53    699  A    C  
ATOM   1768  NE2 GLN A 223       0.245  18.302 -16.266  1.00 67.47      A    N  
ANISOU 1768  NE2 GLN A 223     7912   9206   8516    232     58    705  A    N  
ATOM   1769  OE1 GLN A 223      -0.635  20.084 -15.274  1.00 57.59      A    O  
ANISOU 1769  OE1 GLN A 223     6664   7876   7339    182     56    738  A    O  
ATOM   1770  N   PHE A 224      -1.076  15.041 -11.294  1.00 32.19      A    N  
ANISOU 1770  N   PHE A 224     3660   4522   4048    164    -32    514  A    N  
ATOM   1771  CA  PHE A 224      -1.043  14.746  -9.862  1.00 34.80      A    C  
ANISOU 1771  CA  PHE A 224     4027   4804   4389    143    -50    492  A    C  
ATOM   1772  C   PHE A 224       0.244  15.235  -9.167  1.00 35.41      A    C  
ANISOU 1772  C   PHE A 224     4098   4859   4497    143    -59    497  A    C  
ATOM   1773  O   PHE A 224       0.211  15.879  -8.103  1.00 33.17      A    O  
ANISOU 1773  O   PHE A 224     3826   4538   4235    127    -64    495  A    O  
ATOM   1774  CB  PHE A 224      -1.230  13.216  -9.658  1.00 35.06      A    C  
ANISOU 1774  CB  PHE A 224     4093   4828   4396    146    -74    459  A    C  
ATOM   1775  CG  PHE A 224      -1.313  12.813  -8.209  1.00 33.79      A    C  
ANISOU 1775  CG  PHE A 224     3970   4627   4243    125    -92    445  A    C  
ATOM   1776  CD1 PHE A 224      -0.152  12.599  -7.463  1.00 34.72      A    C  
ANISOU 1776  CD1 PHE A 224     4098   4722   4372    127   -108    433  A    C  
ATOM   1777  CD2 PHE A 224      -2.525  12.588  -7.610  1.00 34.35      A    C  
ANISOU 1777  CD2 PHE A 224     4061   4685   4304    105    -91    445  A    C  
ATOM   1778  CE1 PHE A 224      -0.216  12.210  -6.136  1.00 35.37      A    C  
ANISOU 1778  CE1 PHE A 224     4213   4770   4454    111   -125    421  A    C  
ATOM   1779  CE2 PHE A 224      -2.601  12.160  -6.283  1.00 34.39      A    C  
ANISOU 1779  CE2 PHE A 224     4096   4662   4308     88   -106    438  A    C  
ATOM   1780  CZ  PHE A 224      -1.449  11.994  -5.534  1.00 34.17      A    C  
ANISOU 1780  CZ  PHE A 224     4081   4613   4289     92   -123    426  A    C  
ATOM   1781  N   GLU A 225       1.379  14.949  -9.789  1.00 39.11      A    N  
ANISOU 1781  N   GLU A 225     4545   5351   4964    162    -62    500  A    N  
ATOM   1782  CA  GLU A 225       2.680  15.318  -9.197  1.00 42.23      A    C  
ANISOU 1782  CA  GLU A 225     4929   5725   5391    161    -74    506  A    C  
ATOM   1783  C   GLU A 225       2.885  16.802  -9.108  1.00 40.63      A    C  
ANISOU 1783  C   GLU A 225     4695   5509   5232    150    -66    543  A    C  
ATOM   1784  O   GLU A 225       3.730  17.227  -8.342  1.00 38.10      A    O  
ANISOU 1784  O   GLU A 225     4372   5155   4945    143    -83    543  A    O  
ATOM   1785  CB  GLU A 225       3.822  14.816 -10.033  1.00 47.16      A    C  
ANISOU 1785  CB  GLU A 225     5525   6388   6004    188    -75    510  A    C  
ATOM   1786  CG  GLU A 225       3.937  13.337 -10.068  1.00 58.14      A    C  
ANISOU 1786  CG  GLU A 225     6944   7784   7359    205    -95    469  A    C  
ATOM   1787  CD  GLU A 225       5.386  12.915 -10.020  1.00 63.16      A    C  
ANISOU 1787  CD  GLU A 225     7567   8429   8001    224   -110    460  A    C  
ATOM   1788  OE1 GLU A 225       5.893  12.570  -8.902  1.00 69.66      A    O  
ANISOU 1788  OE1 GLU A 225     8421   9207   8840    212   -134    438  A    O  
ATOM   1789  OE2 GLU A 225       6.021  13.051 -11.085  1.00 70.12      A    O1-
ANISOU 1789  OE2 GLU A 225     8405   9365   8872    252    -97    479  A    O1-
ATOM   1790  N   CYS A 226       2.197  17.593  -9.931  1.00 35.04      A    N  
ANISOU 1790  N   CYS A 226     3959   4825   4528    148    -45    574  A    N  
ATOM   1791  CA  CYS A 226       2.326  19.068  -9.821  1.00 36.04      A    C  
ANISOU 1791  CA  CYS A 226     4055   4930   4707    135    -46    610  A    C  
ATOM   1792  C   CYS A 226       1.367  19.758  -8.841  1.00 34.97      A    C  
ANISOU 1792  C   CYS A 226     3947   4750   4590    120    -57    594  A    C  
ATOM   1793  O   CYS A 226       1.497  20.951  -8.639  1.00 36.19      A    O  
ANISOU 1793  O   CYS A 226     4079   4876   4792    112    -67    616  A    O  
ATOM   1794  CB  CYS A 226       2.192  19.729 -11.187  1.00 34.33      A    C  
ANISOU 1794  CB  CYS A 226     3789   4761   4494    142    -23    662  A    C  
ATOM   1795  SG  CYS A 226       3.160  18.881 -12.494  1.00 39.09      A    S  
ANISOU 1795  SG  CYS A 226     4353   5440   5057    173     -6    681  A    S  
ATOM   1796  N   LEU A 227       0.352  19.028  -8.301  1.00 38.70      A    N  
ANISOU 1796  N   LEU A 227     4461   5217   5023    118    -54    558  A    N  
ATOM   1797  CA  LEU A 227      -0.765  19.688  -7.599  1.00 36.17      A    C  
ANISOU 1797  CA  LEU A 227     4159   4875   4709    109    -55    546  A    C  
ATOM   1798  C   LEU A 227      -0.931  19.280  -6.132  1.00 35.96      A    C  
ANISOU 1798  C   LEU A 227     4174   4818   4669    108    -72    507  A    C  
ATOM   1799  O   LEU A 227      -1.726  19.886  -5.406  1.00 36.05      A    O  
ANISOU 1799  O   LEU A 227     4197   4815   4682    108    -76    494  A    O  
ATOM   1800  CB  LEU A 227      -2.040  19.372  -8.357  1.00 34.41      A    C  
ANISOU 1800  CB  LEU A 227     3937   4685   4451    109    -32    550  A    C  
ATOM   1801  CG  LEU A 227      -2.086  20.208  -9.648  1.00 36.85      A    C  
ANISOU 1801  CG  LEU A 227     4202   5020   4778    113    -16    592  A    C  
ATOM   1802  CD1 LEU A 227      -3.107  19.692 -10.600  1.00 36.67      A    C  
ANISOU 1802  CD1 LEU A 227     4177   5036   4716    117      4    595  A    C  
ATOM   1803  CD2 LEU A 227      -2.427  21.669  -9.322  1.00 37.79      A    C  
ANISOU 1803  CD2 LEU A 227     4305   5110   4944    106    -25    608  A    C  
ATOM   1804  N   TYR A 228      -0.218  18.247  -5.723  1.00 36.21      A    N  
ANISOU 1804  N   TYR A 228     4227   4846   4684    109    -83    489  A    N  
ATOM   1805  CA  TYR A 228       0.050  18.054  -4.321  1.00 35.49      A    C  
ANISOU 1805  CA  TYR A 228     4168   4725   4591    109   -104    460  A    C  
ATOM   1806  C   TYR A 228      -1.250  18.005  -3.469  1.00 34.52      A    C  
ANISOU 1806  C   TYR A 228     4071   4606   4438    108    -99    444  A    C  
ATOM   1807  O   TYR A 228      -1.418  18.785  -2.530  1.00 34.98      A    O  
ANISOU 1807  O   TYR A 228     4138   4647   4507    117   -112    428  A    O  
ATOM   1808  CB  TYR A 228       0.992  19.116  -3.826  1.00 35.03      A    C  
ANISOU 1808  CB  TYR A 228     4094   4632   4582    115   -129    461  A    C  
ATOM   1809  CG  TYR A 228       2.368  19.114  -4.539  1.00 33.28      A    C  
ANISOU 1809  CG  TYR A 228     3842   4410   4391    115   -135    483  A    C  
ATOM   1810  CD1 TYR A 228       3.374  18.233  -4.165  1.00 33.53      A    C  
ANISOU 1810  CD1 TYR A 228     3888   4436   4416    120   -149    467  A    C  
ATOM   1811  CD2 TYR A 228       2.638  19.989  -5.555  1.00 34.41      A    C  
ANISOU 1811  CD2 TYR A 228     3940   4564   4571    114   -126    522  A    C  
ATOM   1812  CE1 TYR A 228       4.630  18.213  -4.798  1.00 32.98      A    C  
ANISOU 1812  CE1 TYR A 228     3787   4373   4372    123   -152    488  A    C  
ATOM   1813  CE2 TYR A 228       3.868  20.014  -6.190  1.00 35.23      A    C  
ANISOU 1813  CE2 TYR A 228     4007   4676   4700    115   -129    551  A    C  
ATOM   1814  CZ  TYR A 228       4.861  19.151  -5.799  1.00 36.52      A    C  
ANISOU 1814  CZ  TYR A 228     4184   4836   4855    121   -141    532  A    C  
ATOM   1815  OH  TYR A 228       6.068  19.177  -6.503  1.00 39.59      A    O  
ANISOU 1815  OH  TYR A 228     4532   5244   5266    125   -141    563  A    O  
ATOM   1816  N   PRO A 229      -2.103  17.010  -3.750  1.00 34.66      A    N  
ANISOU 1816  N   PRO A 229     4102   4648   4417     99    -84    446  A    N  
ATOM   1817  CA  PRO A 229      -3.329  16.834  -2.924  1.00 34.19      A    C  
ANISOU 1817  CA  PRO A 229     4063   4601   4327     96    -77    439  A    C  
ATOM   1818  C   PRO A 229      -2.939  16.595  -1.463  1.00 35.72      A    C  
ANISOU 1818  C   PRO A 229     4284   4780   4508    102    -96    418  A    C  
ATOM   1819  O   PRO A 229      -1.925  15.993  -1.201  1.00 39.98      A    O  
ANISOU 1819  O   PRO A 229     4836   5302   5052    102   -113    411  A    O  
ATOM   1820  CB  PRO A 229      -3.958  15.601  -3.497  1.00 33.15      A    C  
ANISOU 1820  CB  PRO A 229     3939   4489   4167     82    -69    449  A    C  
ATOM   1821  CG  PRO A 229      -2.874  14.901  -4.309  1.00 33.42      A    C  
ANISOU 1821  CG  PRO A 229     3968   4517   4211     84    -80    448  A    C  
ATOM   1822  CD  PRO A 229      -2.050  16.031  -4.848  1.00 35.37      A    C  
ANISOU 1822  CD  PRO A 229     4186   4759   4492     95    -77    455  A    C  
ATOM   1823  N   TYR A 230      -3.761  17.050  -0.551  1.00 34.71      A    N  
ANISOU 1823  N   TYR A 230     4163   4664   4359    111    -93    409  A    N  
ATOM   1824  CA  TYR A 230      -3.717  16.691   0.843  1.00 31.13      A    C  
ANISOU 1824  CA  TYR A 230     3735   4213   3878    121   -106    395  A    C  
ATOM   1825  C   TYR A 230      -3.740  15.192   1.049  1.00 33.89      A    C  
ANISOU 1825  C   TYR A 230     4104   4572   4199    102   -107    409  A    C  
ATOM   1826  O   TYR A 230      -4.162  14.383   0.160  1.00 31.64      A    O  
ANISOU 1826  O   TYR A 230     3813   4294   3911     81    -98    429  A    O  
ATOM   1827  CB  TYR A 230      -4.890  17.315   1.645  1.00 32.97      A    C  
ANISOU 1827  CB  TYR A 230     3967   4477   4081    138    -95    387  A    C  
ATOM   1828  CG  TYR A 230      -4.813  18.786   1.859  1.00 32.43      A    C  
ANISOU 1828  CG  TYR A 230     3887   4394   4038    166   -109    362  A    C  
ATOM   1829  CD1 TYR A 230      -5.321  19.657   0.916  1.00 32.06      A    C  
ANISOU 1829  CD1 TYR A 230     3816   4346   4020    165    -98    369  A    C  
ATOM   1830  CD2 TYR A 230      -4.247  19.321   3.029  1.00 35.35      A    C  
ANISOU 1830  CD2 TYR A 230     4270   4752   4409    196   -137    329  A    C  
ATOM   1831  CE1 TYR A 230      -5.251  20.990   1.089  1.00 35.32      A    C  
ANISOU 1831  CE1 TYR A 230     4216   4738   4464    189   -119    348  A    C  
ATOM   1832  CE2 TYR A 230      -4.202  20.675   3.215  1.00 35.54      A    C  
ANISOU 1832  CE2 TYR A 230     4283   4756   4463    224   -159    301  A    C  
ATOM   1833  CZ  TYR A 230      -4.688  21.488   2.227  1.00 33.02      A    C  
ANISOU 1833  CZ  TYR A 230     3938   4428   4177    219   -151    313  A    C  
ATOM   1834  OH  TYR A 230      -4.641  22.830   2.342  1.00 37.02      A    O  
ANISOU 1834  OH  TYR A 230     4430   4908   4724    245   -180    288  A    O  
ATOM   1835  N   PRO A 231      -3.203  14.766   2.197  1.00 34.65      A    N  
ANISOU 1835  N   PRO A 231     4222   4661   4278    108   -125    399  A    N  
ATOM   1836  CA  PRO A 231      -3.366  13.328   2.509  1.00 36.93      A    C  
ANISOU 1836  CA  PRO A 231     4529   4959   4543     88   -131    419  A    C  
ATOM   1837  C   PRO A 231      -4.843  12.891   2.482  1.00 36.92      A    C  
ANISOU 1837  C   PRO A 231     4519   4994   4511     72   -109    450  A    C  
ATOM   1838  O   PRO A 231      -5.728  13.680   2.833  1.00 36.65      A    O  
ANISOU 1838  O   PRO A 231     4474   4991   4459     85    -91    451  A    O  
ATOM   1839  CB  PRO A 231      -2.842  13.261   3.930  1.00 36.16      A    C  
ANISOU 1839  CB  PRO A 231     4453   4861   4423    105   -148    406  A    C  
ATOM   1840  CG  PRO A 231      -1.703  14.250   3.889  1.00 38.24      A    C  
ANISOU 1840  CG  PRO A 231     4714   5092   4722    126   -165    372  A    C  
ATOM   1841  CD  PRO A 231      -2.322  15.438   3.166  1.00 37.38      A    C  
ANISOU 1841  CD  PRO A 231     4580   4989   4633    134   -148    369  A    C  
ATOM   1842  N   VAL A 232      -5.090  11.644   2.104  1.00 36.65      A    N  
ANISOU 1842  N   VAL A 232     4490   4956   4477     45   -117    475  A    N  
ATOM   1843  CA  VAL A 232      -6.434  11.173   1.962  1.00 35.94      A    C  
ANISOU 1843  CA  VAL A 232     4388   4896   4371     26   -103    509  A    C  
ATOM   1844  C   VAL A 232      -7.283  11.274   3.219  1.00 38.72      A    C  
ANISOU 1844  C   VAL A 232     4737   5292   4681     30    -89    531  A    C  
ATOM   1845  O   VAL A 232      -8.495  11.518   3.130  1.00 37.31      A    O  
ANISOU 1845  O   VAL A 232     4539   5149   4486     27    -66    553  A    O  
ATOM   1846  CB  VAL A 232      -6.398   9.743   1.464  1.00 40.87      A    C  
ANISOU 1846  CB  VAL A 232     5019   5498   5010     -1   -127    529  A    C  
ATOM   1847  CG1 VAL A 232      -7.640   8.979   1.861  1.00 42.16      A    C  
ANISOU 1847  CG1 VAL A 232     5173   5686   5156    -27   -125    576  A    C  
ATOM   1848  CG2 VAL A 232      -6.189   9.747  -0.016  1.00 43.16      A    C  
ANISOU 1848  CG2 VAL A 232     5300   5769   5331     -1   -131    513  A    C  
ATOM   1849  N   HIS A 233      -6.664  11.155   4.406  1.00 38.70      A    N  
ANISOU 1849  N   HIS A 233     4753   5293   4656     45   -102    526  A    N  
ATOM   1850  CA  HIS A 233      -7.420  11.254   5.658  1.00 39.94      A    C  
ANISOU 1850  CA  HIS A 233     4905   5505   4764     57    -88    549  A    C  
ATOM   1851  C   HIS A 233      -7.590  12.651   6.179  1.00 39.12      A    C  
ANISOU 1851  C   HIS A 233     4794   5430   4638    100    -72    513  A    C  
ATOM   1852  O   HIS A 233      -8.329  12.893   7.128  1.00 41.48      A    O  
ANISOU 1852  O   HIS A 233     5084   5786   4890    122    -58    525  A    O  
ATOM   1853  CB  HIS A 233      -6.767  10.428   6.729  1.00 39.59      A    C  
ANISOU 1853  CB  HIS A 233     4881   5461   4700     56   -109    563  A    C  
ATOM   1854  CG  HIS A 233      -6.808   8.981   6.424  1.00 39.82      A    C  
ANISOU 1854  CG  HIS A 233     4915   5466   4748     14   -130    604  A    C  
ATOM   1855  CD2 HIS A 233      -7.753   8.043   6.665  1.00 41.57      A    C  
ANISOU 1855  CD2 HIS A 233     5122   5714   4958    -16   -129    664  A    C  
ATOM   1856  ND1 HIS A 233      -5.755   8.317   5.822  1.00 42.65      A    N  
ANISOU 1856  ND1 HIS A 233     5292   5767   5146      2   -161    587  A    N  
ATOM   1857  CE1 HIS A 233      -6.032   7.033   5.717  1.00 38.83      A    C  
ANISOU 1857  CE1 HIS A 233     4809   5269   4675    -34   -183    628  A    C  
ATOM   1858  NE2 HIS A 233      -7.251   6.837   6.208  1.00 44.35      A    N  
ANISOU 1858  NE2 HIS A 233     5487   6015   5347    -48   -166    679  A    N  
ATOM   1859  N   HIS A 234      -6.900  13.578   5.569  1.00 36.98      A    N  
ANISOU 1859  N   HIS A 234     4524   5121   4402    117    -80    471  A    N  
ATOM   1860  CA  HIS A 234      -7.111  15.002   5.847  1.00 42.93      A    C  
ANISOU 1860  CA  HIS A 234     5269   5890   5151    157    -74    434  A    C  
ATOM   1861  C   HIS A 234      -8.505  15.469   5.389  1.00 41.53      A    C  
ANISOU 1861  C   HIS A 234     5065   5751   4960    157    -45    449  A    C  
ATOM   1862  O   HIS A 234      -9.049  14.921   4.423  1.00 41.92      A    O  
ANISOU 1862  O   HIS A 234     5103   5796   5026    123    -32    478  A    O  
ATOM   1863  CB  HIS A 234      -6.035  15.801   5.157  1.00 41.57      A    C  
ANISOU 1863  CB  HIS A 234     5100   5661   5031    165    -94    397  A    C  
ATOM   1864  CG  HIS A 234      -5.923  17.195   5.634  1.00 44.61      A    C  
ANISOU 1864  CG  HIS A 234     5481   6045   5424    208   -107    356  A    C  
ATOM   1865  CD2 HIS A 234      -5.117  17.750   6.560  1.00 44.18      A    C  
ANISOU 1865  CD2 HIS A 234     5440   5974   5370    243   -136    317  A    C  
ATOM   1866  ND1 HIS A 234      -6.706  18.209   5.141  1.00 45.86      A    N  
ANISOU 1866  ND1 HIS A 234     5617   6212   5593    222    -95    345  A    N  
ATOM   1867  CE1 HIS A 234      -6.368  19.339   5.727  1.00 44.87      A    C  
ANISOU 1867  CE1 HIS A 234     5494   6075   5480    262   -121    303  A    C  
ATOM   1868  NE2 HIS A 234      -5.428  19.079   6.610  1.00 46.76      A    N  
ANISOU 1868  NE2 HIS A 234     5753   6299   5711    277   -145    283  A    N  
ATOM   1869  N   PRO A 235      -9.072  16.472   6.080  1.00 41.74      A    N  
ANISOU 1869  N   PRO A 235     5082   5816   4959    199    -39    425  A    N  
ATOM   1870  CA  PRO A 235     -10.354  17.067   5.688  1.00 45.85      A    C  
ANISOU 1870  CA  PRO A 235     5576   6374   5468    206    -14    432  A    C  
ATOM   1871  C   PRO A 235     -10.361  17.562   4.251  1.00 41.32      A    C  
ANISOU 1871  C   PRO A 235     4991   5757   4948    186    -11    427  A    C  
ATOM   1872  O   PRO A 235     -11.402  17.514   3.612  1.00 38.65      A    O  
ANISOU 1872  O   PRO A 235     4635   5442   4608    171      9    451  A    O  
ATOM   1873  CB  PRO A 235     -10.488  18.240   6.653  1.00 50.01      A    C  
ANISOU 1873  CB  PRO A 235     6102   6930   5968    265    -25    386  A    C  
ATOM   1874  CG  PRO A 235      -9.940  17.648   7.910  1.00 50.79      A    C  
ANISOU 1874  CG  PRO A 235     6219   7053   6025    282    -36    387  A    C  
ATOM   1875  CD  PRO A 235      -8.685  16.927   7.422  1.00 48.94      A    C  
ANISOU 1875  CD  PRO A 235     6007   6752   5836    245    -56    393  A    C  
ATOM   1876  N   CYS A 236      -9.180  17.873   3.714  1.00 40.18      A    N  
ANISOU 1876  N   CYS A 236     4858   5554   4851    183    -34    405  A    N  
ATOM   1877  CA  CYS A 236      -9.091  18.446   2.393  1.00 36.42      A    C  
ANISOU 1877  CA  CYS A 236     4368   5045   4424    170    -32    404  A    C  
ATOM   1878  C   CYS A 236      -8.618  17.484   1.323  1.00 36.69      A    C  
ANISOU 1878  C   CYS A 236     4406   5053   4483    132    -30    429  A    C  
ATOM   1879  O   CYS A 236      -8.063  17.906   0.239  1.00 39.08      A    O  
ANISOU 1879  O   CYS A 236     4697   5322   4826    125    -34    427  A    O  
ATOM   1880  CB  CYS A 236      -8.244  19.682   2.396  1.00 37.61      A    C  
ANISOU 1880  CB  CYS A 236     4518   5155   4617    197    -59    367  A    C  
ATOM   1881  SG  CYS A 236      -8.965  20.973   3.433  1.00 42.90      A    S  
ANISOU 1881  SG  CYS A 236     5181   5853   5265    251    -71    327  A    S  
ATOM   1882  N   ASP A 237      -8.877  16.207   1.600  1.00 34.86      A    N  
ANISOU 1882  N   ASP A 237     4183   4837   4225    109    -25    456  A    N  
ATOM   1883  CA  ASP A 237      -8.735  15.120   0.621  1.00 34.13      A    C  
ANISOU 1883  CA  ASP A 237     4091   4727   4148     76    -28    480  A    C  
ATOM   1884  C   ASP A 237      -9.342  15.551  -0.715  1.00 35.26      A    C  
ANISOU 1884  C   ASP A 237     4212   4871   4312     69    -13    485  A    C  
ATOM   1885  O   ASP A 237     -10.453  16.132  -0.755  1.00 35.79      A    O  
ANISOU 1885  O   ASP A 237     4262   4965   4367     75      5    491  A    O  
ATOM   1886  CB  ASP A 237      -9.397  13.875   1.160  1.00 34.98      A    C  
ANISOU 1886  CB  ASP A 237     4204   4859   4228     53    -27    513  A    C  
ATOM   1887  CG  ASP A 237      -9.321  12.666   0.244  1.00 39.35      A    C  
ANISOU 1887  CG  ASP A 237     4759   5389   4801     22    -41    532  A    C  
ATOM   1888  OD1 ASP A 237      -8.307  12.424  -0.490  1.00 34.96      A    O  
ANISOU 1888  OD1 ASP A 237     4213   4798   4272     21    -57    515  A    O  
ATOM   1889  OD2 ASP A 237     -10.338  11.906   0.271  1.00 38.02      A    O1-
ANISOU 1889  OD2 ASP A 237     4583   5241   4621      1    -36    567  A    O1-
ATOM   1890  N   ARG A 238      -8.562  15.308  -1.746  1.00 36.20      A    N  
ANISOU 1890  N   ARG A 238     4331   4962   4461     61    -22    482  A    N  
ATOM   1891  CA  ARG A 238      -8.882  15.599  -3.113  1.00 37.63      A    C  
ANISOU 1891  CA  ARG A 238     4492   5143   4660     57    -12    488  A    C  
ATOM   1892  C   ARG A 238      -8.604  17.039  -3.507  1.00 35.83      A    C  
ANISOU 1892  C   ARG A 238     4248   4908   4458     76     -6    477  A    C  
ATOM   1893  O   ARG A 238      -8.685  17.353  -4.654  1.00 36.93      A    O  
ANISOU 1893  O   ARG A 238     4367   5050   4614     74      2    487  A    O  
ATOM   1894  CB  ARG A 238     -10.318  15.189  -3.452  1.00 33.41      A    C  
ANISOU 1894  CB  ARG A 238     3946   4636   4109     41      2    511  A    C  
ATOM   1895  CG  ARG A 238     -10.545  13.700  -3.518  1.00 35.81      A    C  
ANISOU 1895  CG  ARG A 238     4262   4940   4402     18    -11    529  A    C  
ATOM   1896  CD  ARG A 238     -11.985  13.348  -3.810  1.00 36.46      A    C  
ANISOU 1896  CD  ARG A 238     4328   5049   4476      1     -2    555  A    C  
ATOM   1897  NE  ARG A 238     -12.832  13.934  -2.815  1.00 35.40      A    N  
ANISOU 1897  NE  ARG A 238     4183   4947   4318      9     21    564  A    N  
ATOM   1898  CZ  ARG A 238     -13.490  15.065  -2.954  1.00 42.59      A    C  
ANISOU 1898  CZ  ARG A 238     5077   5878   5227     25     41    555  A    C  
ATOM   1899  NH1 ARG A 238     -13.460  15.744  -4.074  1.00 34.90      A    N1+
ANISOU 1899  NH1 ARG A 238     4092   4892   4275     32     44    545  A    N1+
ATOM   1900  NH2 ARG A 238     -14.195  15.516  -1.955  1.00 45.80      A    N  
ANISOU 1900  NH2 ARG A 238     5475   6318   5606     40     55    558  A    N  
ATOM   1901  N   GLN A 239      -8.259  17.887  -2.555  1.00 33.19      A    N  
ANISOU 1901  N   GLN A 239     3917   4563   4127     95    -15    459  A    N  
ATOM   1902  CA  GLN A 239      -8.020  19.304  -2.824  1.00 34.64      A    C  
ANISOU 1902  CA  GLN A 239     4084   4732   4345    112    -20    450  A    C  
ATOM   1903  C   GLN A 239      -6.500  19.519  -2.877  1.00 35.99      A    C  
ANISOU 1903  C   GLN A 239     4256   4866   4551    116    -42    443  A    C  
ATOM   1904  O   GLN A 239      -5.756  18.844  -2.169  1.00 37.05      A    O  
ANISOU 1904  O   GLN A 239     4411   4990   4676    115    -55    433  A    O  
ATOM   1905  CB  GLN A 239      -8.614  20.277  -1.807  1.00 36.28      A    C  
ANISOU 1905  CB  GLN A 239     4293   4947   4545    137    -25    427  A    C  
ATOM   1906  CG  GLN A 239      -9.918  19.923  -1.082  1.00 38.09      A    C  
ANISOU 1906  CG  GLN A 239     4525   5220   4726    142     -7    428  A    C  
ATOM   1907  CD  GLN A 239     -11.072  19.763  -2.028  1.00 39.90      A    C  
ANISOU 1907  CD  GLN A 239     4736   5474   4948    126     15    452  A    C  
ATOM   1908  NE2 GLN A 239     -11.541  18.557  -2.139  1.00 41.71      A    N  
ANISOU 1908  NE2 GLN A 239     4970   5722   5153    102     27    474  A    N  
ATOM   1909  OE1 GLN A 239     -11.522  20.715  -2.680  1.00 38.55      A    O  
ANISOU 1909  OE1 GLN A 239     4546   5300   4798    134     20    451  A    O  
ATOM   1910  N   SER A 240      -6.069  20.471  -3.692  1.00 35.95      A    N  
ANISOU 1910  N   SER A 240     4227   4844   4588    119    -46    453  A    N  
ATOM   1911  CA  SER A 240      -4.662  20.825  -3.843  1.00 38.15      A    C  
ANISOU 1911  CA  SER A 240     4494   5091   4906    120    -67    456  A    C  
ATOM   1912  C   SER A 240      -4.236  21.595  -2.632  1.00 35.07      A    C  
ANISOU 1912  C   SER A 240     4115   4672   4537    139    -97    428  A    C  
ATOM   1913  O   SER A 240      -4.916  22.519  -2.256  1.00 37.63      A    O  
ANISOU 1913  O   SER A 240     4435   4992   4870    154   -105    413  A    O  
ATOM   1914  CB  SER A 240      -4.431  21.731  -5.070  1.00 37.53      A    C  
ANISOU 1914  CB  SER A 240     4379   5009   4871    117    -64    487  A    C  
ATOM   1915  OG  SER A 240      -3.048  22.092  -5.258  1.00 34.21      A    O  
ANISOU 1915  OG  SER A 240     3941   4563   4494    116    -84    500  A    O  
ATOM   1916  N   GLN A 241      -3.020  21.308  -2.147  1.00 36.97      A    N  
ANISOU 1916  N   GLN A 241     4366   4888   4793    140   -118    418  A    N  
ATOM   1917  CA  GLN A 241      -2.337  22.076  -1.052  1.00 37.30      A    C  
ANISOU 1917  CA  GLN A 241     4414   4893   4864    160   -157    389  A    C  
ATOM   1918  C   GLN A 241      -1.767  23.386  -1.513  1.00 36.66      A    C  
ANISOU 1918  C   GLN A 241     4301   4772   4853    164   -184    401  A    C  
ATOM   1919  O   GLN A 241      -1.455  24.211  -0.714  1.00 41.04      A    O  
ANISOU 1919  O   GLN A 241     4858   5294   5440    183   -221    374  A    O  
ATOM   1920  CB  GLN A 241      -1.167  21.282  -0.464  1.00 35.08      A    C  
ANISOU 1920  CB  GLN A 241     4152   4595   4580    158   -173    377  A    C  
ATOM   1921  CG  GLN A 241      -1.617  20.185   0.480  1.00 39.44      A    C  
ANISOU 1921  CG  GLN A 241     4740   5174   5071    162   -163    360  A    C  
ATOM   1922  CD  GLN A 241      -0.465  19.289   0.844  1.00 38.75      A    C  
ANISOU 1922  CD  GLN A 241     4669   5072   4980    156   -177    354  A    C  
ATOM   1923  NE2 GLN A 241      -0.093  18.455  -0.057  1.00 38.85      A    N  
ANISOU 1923  NE2 GLN A 241     4674   5092   4991    137   -163    377  A    N  
ATOM   1924  OE1 GLN A 241       0.089  19.378   1.905  1.00 38.88      A    O  
ANISOU 1924  OE1 GLN A 241     4704   5071   4998    172   -204    329  A    O  
ATOM   1925  N   VAL A 242      -1.609  23.543  -2.814  1.00 39.75      A    N  
ANISOU 1925  N   VAL A 242     4661   5172   5270    145   -166    443  A    N  
ATOM   1926  CA  VAL A 242      -0.973  24.693  -3.342  1.00 37.60      A    C  
ANISOU 1926  CA  VAL A 242     4351   4865   5067    142   -192    469  A    C  
ATOM   1927  C   VAL A 242      -1.874  25.921  -3.269  1.00 39.61      A    C  
ANISOU 1927  C   VAL A 242     4595   5102   5351    154   -210    462  A    C  
ATOM   1928  O   VAL A 242      -2.973  25.874  -3.731  1.00 45.45      A    O  
ANISOU 1928  O   VAL A 242     5334   5872   6059    153   -182    467  A    O  
ATOM   1929  CB  VAL A 242      -0.576  24.433  -4.823  1.00 34.81      A    C  
ANISOU 1929  CB  VAL A 242     3963   4539   4723    121   -164    524  A    C  
ATOM   1930  CG1 VAL A 242       0.102  25.631  -5.395  1.00 40.58      A    C  
ANISOU 1930  CG1 VAL A 242     4648   5239   5530    114   -188    565  A    C  
ATOM   1931  CG2 VAL A 242       0.311  23.268  -4.996  1.00 36.17      A    C  
ANISOU 1931  CG2 VAL A 242     4143   4730   4868    115   -150    528  A    C  
ATOM   1932  N   ASP A 243      -1.382  27.048  -2.744  1.00 40.82      A    N  
ANISOU 1932  N   ASP A 243     4737   5203   5569    167   -261    450  A    N  
ATOM   1933  CA  ASP A 243      -2.123  28.328  -2.802  1.00 40.79      A    C  
ANISOU 1933  CA  ASP A 243     4717   5174   5607    179   -288    445  A    C  
ATOM   1934  C   ASP A 243      -1.837  28.948  -4.131  1.00 43.10      A    C  
ANISOU 1934  C   ASP A 243     4962   5458   5956    155   -285    510  A    C  
ATOM   1935  O   ASP A 243      -0.716  29.403  -4.397  1.00 42.51      A    O  
ANISOU 1935  O   ASP A 243     4857   5347   5946    141   -314    544  A    O  
ATOM   1936  CB  ASP A 243      -1.619  29.244  -1.732  1.00 47.44      A    C  
ANISOU 1936  CB  ASP A 243     5564   5956   6503    206   -354    403  A    C  
ATOM   1937  CG  ASP A 243      -2.367  30.574  -1.666  1.00 50.75      A    C  
ANISOU 1937  CG  ASP A 243     5968   6342   6969    227   -395    386  A    C  
ATOM   1938  OD1 ASP A 243      -3.089  30.985  -2.591  1.00 45.30      A    O  
ANISOU 1938  OD1 ASP A 243     5256   5665   6289    215   -377    420  A    O  
ATOM   1939  OD2 ASP A 243      -2.154  31.230  -0.635  1.00 52.30      A    O1-
ANISOU 1939  OD2 ASP A 243     6177   6496   7196    260   -453    336  A    O1-
ATOM   1940  N   PHE A 244      -2.806  28.899  -5.017  1.00 40.80      A    N  
ANISOU 1940  N   PHE A 244     4660   5204   5635    147   -248    534  A    N  
ATOM   1941  CA  PHE A 244      -2.584  29.351  -6.374  1.00 39.66      A    C  
ANISOU 1941  CA  PHE A 244     4471   5068   5530    124   -237    603  A    C  
ATOM   1942  C   PHE A 244      -2.235  30.858  -6.378  1.00 44.91      A    C  
ANISOU 1942  C   PHE A 244     5100   5667   6293    123   -296    624  A    C  
ATOM   1943  O   PHE A 244      -1.664  31.341  -7.322  1.00 41.44      A    O  
ANISOU 1943  O   PHE A 244     4615   5223   5905    102   -299    691  A    O  
ATOM   1944  CB  PHE A 244      -3.856  29.148  -7.204  1.00 44.99      A    C  
ANISOU 1944  CB  PHE A 244     5145   5790   6158    122   -194    615  A    C  
ATOM   1945  CG  PHE A 244      -3.964  27.810  -7.879  1.00 42.66      A    C  
ANISOU 1945  CG  PHE A 244     4860   5556   5792    113   -140    628  A    C  
ATOM   1946  CD1 PHE A 244      -3.524  26.662  -7.289  1.00 39.00      A    C  
ANISOU 1946  CD1 PHE A 244     4427   5108   5283    114   -127    599  A    C  
ATOM   1947  CD2 PHE A 244      -4.618  27.707  -9.082  1.00 38.67      A    C  
ANISOU 1947  CD2 PHE A 244     4335   5093   5264    105   -105    665  A    C  
ATOM   1948  CE1 PHE A 244      -3.659  25.421  -7.928  1.00 37.59      A    C  
ANISOU 1948  CE1 PHE A 244     4256   4978   5044    108    -86    606  A    C  
ATOM   1949  CE2 PHE A 244      -4.751  26.491  -9.721  1.00 39.28      A    C  
ANISOU 1949  CE2 PHE A 244     4422   5224   5279    101    -64    669  A    C  
ATOM   1950  CZ  PHE A 244      -4.278  25.346  -9.144  1.00 37.48      A    C  
ANISOU 1950  CZ  PHE A 244     4223   5005   5013    103    -57    639  A    C  
ATOM   1951  N   ASP A 245      -2.660  31.601  -5.362  1.00 45.15      A    N  
ANISOU 1951  N   ASP A 245     5150   5653   6348    149   -343    570  A    N  
ATOM   1952  CA  ASP A 245      -2.356  33.052  -5.283  1.00 44.63      A    C  
ANISOU 1952  CA  ASP A 245     5053   5515   6386    152   -414    583  A    C  
ATOM   1953  C   ASP A 245      -0.943  33.311  -4.725  1.00 50.83      A    C  
ANISOU 1953  C   ASP A 245     5827   6246   7239    148   -465    586  A    C  
ATOM   1954  O   ASP A 245      -0.410  34.382  -4.921  1.00 45.68      A    O  
ANISOU 1954  O   ASP A 245     5137   5534   6684    137   -522    620  A    O  
ATOM   1955  CB  ASP A 245      -3.383  33.759  -4.427  1.00 45.67      A    C  
ANISOU 1955  CB  ASP A 245     5210   5623   6519    191   -451    515  A    C  
ATOM   1956  CG  ASP A 245      -4.796  33.637  -5.001  1.00 46.00      A    C  
ANISOU 1956  CG  ASP A 245     5257   5715   6504    195   -406    516  A    C  
ATOM   1957  OD1 ASP A 245      -4.914  33.666  -6.238  1.00 51.17      A    O  
ANISOU 1957  OD1 ASP A 245     5881   6393   7167    166   -374    581  A    O  
ATOM   1958  OD2 ASP A 245      -5.772  33.574  -4.223  1.00 51.22      A    O1-
ANISOU 1958  OD2 ASP A 245     5949   6395   7116    229   -404    454  A    O1-
ATOM   1959  N   ASN A 246      -0.339  32.328  -4.062  1.00 48.57      A    N  
ANISOU 1959  N   ASN A 246     5570   5978   6906    152   -448    555  A    N  
ATOM   1960  CA  ASN A 246       1.040  32.467  -3.523  1.00 49.81      A    C  
ANISOU 1960  CA  ASN A 246     5716   6086   7122    149   -495    557  A    C  
ATOM   1961  C   ASN A 246       1.676  31.092  -3.466  1.00 46.37      A    C  
ANISOU 1961  C   ASN A 246     5300   5698   6619    139   -446    556  A    C  
ATOM   1962  O   ASN A 246       1.727  30.462  -2.403  1.00 46.85      A    O  
ANISOU 1962  O   ASN A 246     5403   5761   6634    161   -450    495  A    O  
ATOM   1963  CB  ASN A 246       1.034  33.123  -2.135  1.00 53.43      A    C  
ANISOU 1963  CB  ASN A 246     6202   6484   7612    186   -568    479  A    C  
ATOM   1964  CG  ASN A 246       2.460  33.490  -1.652  1.00 62.08      A    C  
ANISOU 1964  CG  ASN A 246     7280   7515   8791    181   -631    484  A    C  
ATOM   1965  ND2 ASN A 246       2.632  33.569  -0.354  1.00 66.98      A    N  
ANISOU 1965  ND2 ASN A 246     7936   8102   9410    218   -679    409  A    N  
ATOM   1966  OD1 ASN A 246       3.387  33.671  -2.444  1.00 67.07      A    O  
ANISOU 1966  OD1 ASN A 246     7866   8133   9484    146   -633    558  A    O  
ATOM   1967  N   PRO A 247       2.096  30.574  -4.625  1.00 39.62      A    N  
ANISOU 1967  N   PRO A 247     4413   4886   5752    110   -400    623  A    N  
ATOM   1968  CA  PRO A 247       2.582  29.204  -4.631  1.00 41.27      A    C  
ANISOU 1968  CA  PRO A 247     4643   5143   5892    106   -354    616  A    C  
ATOM   1969  C   PRO A 247       3.928  29.074  -3.955  1.00 45.65      A    C  
ANISOU 1969  C   PRO A 247     5195   5662   6485    106   -390    607  A    C  
ATOM   1970  O   PRO A 247       4.845  29.826  -4.249  1.00 46.32      A    O  
ANISOU 1970  O   PRO A 247     5235   5709   6652     90   -426    654  A    O  
ATOM   1971  CB  PRO A 247       2.694  28.837  -6.102  1.00 44.62      A    C  
ANISOU 1971  CB  PRO A 247     5028   5625   6298     84   -303    687  A    C  
ATOM   1972  CG  PRO A 247       2.409  30.063  -6.874  1.00 46.87      A    C  
ANISOU 1972  CG  PRO A 247     5267   5891   6650     72   -322    742  A    C  
ATOM   1973  CD  PRO A 247       1.992  31.171  -5.947  1.00 46.00      A    C  
ANISOU 1973  CD  PRO A 247     5171   5710   6598     87   -385    701  A    C  
ATOM   1974  N   ASP A 248       4.016  28.092  -3.073  1.00 39.29      A    N  
ANISOU 1974  N   ASP A 248     4437   4871   5620    120   -380    553  A    N  
ATOM   1975  CA  ASP A 248       5.248  27.753  -2.402  1.00 43.86      A    C  
ANISOU 1975  CA  ASP A 248     5022   5422   6220    122   -408    538  A    C  
ATOM   1976  C   ASP A 248       6.060  26.720  -3.167  1.00 43.28      A    C  
ANISOU 1976  C   ASP A 248     4931   5395   6116    105   -365    577  A    C  
ATOM   1977  O   ASP A 248       5.925  25.497  -2.972  1.00 42.98      A    O  
ANISOU 1977  O   ASP A 248     4929   5397   6003    112   -331    549  A    O  
ATOM   1978  CB  ASP A 248       4.959  27.212  -1.009  1.00 41.00      A    C  
ANISOU 1978  CB  ASP A 248     4718   5052   5807    150   -421    460  A    C  
ATOM   1979  CG  ASP A 248       6.215  27.191  -0.178  1.00 47.87      A    C  
ANISOU 1979  CG  ASP A 248     5592   5879   6716    157   -467    439  A    C  
ATOM   1980  OD1 ASP A 248       7.306  27.096  -0.803  1.00 45.08      A    O  
ANISOU 1980  OD1 ASP A 248     5202   5522   6403    135   -467    487  A    O  
ATOM   1981  OD2 ASP A 248       6.120  27.167   1.063  1.00 50.86      A    O1-
ANISOU 1981  OD2 ASP A 248     6011   6236   7078    185   -499    377  A    O1-
ATOM   1982  N   TYR A 249       6.955  27.227  -3.991  1.00 46.39      A    N  
ANISOU 1982  N   TYR A 249     5268   5786   6572     86   -374    642  A    N  
ATOM   1983  CA  TYR A 249       7.795  26.428  -4.877  1.00 45.39      A    C  
ANISOU 1983  CA  TYR A 249     5110   5711   6422     75   -335    687  A    C  
ATOM   1984  C   TYR A 249       8.827  25.560  -4.174  1.00 46.25      A    C  
ANISOU 1984  C   TYR A 249     5240   5813   6517     82   -345    655  A    C  
ATOM   1985  O   TYR A 249       9.335  24.601  -4.755  1.00 43.33      A    O  
ANISOU 1985  O   TYR A 249     4862   5495   6104     82   -310    671  A    O  
ATOM   1986  CB  TYR A 249       8.488  27.351  -5.888  1.00 45.04      A    C  
ANISOU 1986  CB  TYR A 249     4990   5667   6454     53   -344    775  A    C  
ATOM   1987  CG  TYR A 249       7.506  28.022  -6.818  1.00 44.45      A    C  
ANISOU 1987  CG  TYR A 249     4891   5613   6383     46   -324    817  A    C  
ATOM   1988  CD1 TYR A 249       6.514  27.285  -7.485  1.00 45.56      A    C  
ANISOU 1988  CD1 TYR A 249     5053   5819   6438     54   -269    808  A    C  
ATOM   1989  CD2 TYR A 249       7.540  29.385  -7.041  1.00 45.70      A    C  
ANISOU 1989  CD2 TYR A 249     5005   5725   6632     30   -365    866  A    C  
ATOM   1990  CE1 TYR A 249       5.611  27.917  -8.338  1.00 41.93      A    C  
ANISOU 1990  CE1 TYR A 249     4570   5378   5981     48   -252    846  A    C  
ATOM   1991  CE2 TYR A 249       6.637  29.985  -7.862  1.00 48.36      A    C  
ANISOU 1991  CE2 TYR A 249     5321   6079   6972     24   -350    903  A    C  
ATOM   1992  CZ  TYR A 249       5.653  29.257  -8.492  1.00 45.24      A    C  
ANISOU 1992  CZ  TYR A 249     4949   5751   6489     33   -292    891  A    C  
ATOM   1993  OH  TYR A 249       4.795  29.900  -9.388  1.00 45.26      A    O  
ANISOU 1993  OH  TYR A 249     4926   5773   6497     27   -276    935  A    O  
ATOM   1994  N   GLU A 250       9.073  25.830  -2.909  1.00 42.60      A    N  
ANISOU 1994  N   GLU A 250     4810   5293   6083     93   -394    605  A    N  
ATOM   1995  CA  GLU A 250       9.995  25.033  -2.167  1.00 48.10      A    C  
ANISOU 1995  CA  GLU A 250     5529   5980   6764    101   -407    571  A    C  
ATOM   1996  C   GLU A 250       9.307  23.761  -1.698  1.00 45.89      A    C  
ANISOU 1996  C   GLU A 250     5310   5736   6388    116   -373    518  A    C  
ATOM   1997  O   GLU A 250       9.844  22.682  -1.858  1.00 51.20      A    O  
ANISOU 1997  O   GLU A 250     5992   6441   7021    116   -352    515  A    O  
ATOM   1998  CB  GLU A 250      10.485  25.807  -0.983  1.00 54.02      A    C  
ANISOU 1998  CB  GLU A 250     6289   6654   7578    111   -476    535  A    C  
ATOM   1999  CG  GLU A 250      11.352  26.962  -1.420  1.00 71.10      A    C  
ANISOU 1999  CG  GLU A 250     8387   8775   9849     92   -518    594  A    C  
ATOM   2000  CD  GLU A 250      12.040  27.596  -0.234  1.00 83.05      A    C  
ANISOU 2000  CD  GLU A 250     9912  10210  11433    103   -595    554  A    C  
ATOM   2001  OE1 GLU A 250      12.477  26.837   0.675  1.00 82.32      A    O  
ANISOU 2001  OE1 GLU A 250     9859  10112  11305    121   -604    501  A    O  
ATOM   2002  OE2 GLU A 250      12.116  28.839  -0.209  1.00 77.37      A    O1-
ANISOU 2002  OE2 GLU A 250     9159   9433  10805     98   -650    573  A    O1-
ATOM   2003  N   ARG A 251       8.095  23.895  -1.170  1.00 47.39      A    N  
ANISOU 2003  N   ARG A 251     5538   5924   6543    127   -370    480  A    N  
ATOM   2004  CA  ARG A 251       7.304  22.750  -0.823  1.00 41.70      A    C  
ANISOU 2004  CA  ARG A 251     4867   5240   5736    136   -338    444  A    C  
ATOM   2005  C   ARG A 251       6.723  22.076  -2.059  1.00 40.07      A    C  
ANISOU 2005  C   ARG A 251     4647   5093   5482    125   -284    477  A    C  
ATOM   2006  O   ARG A 251       6.620  20.859  -2.058  1.00 36.34      A    O  
ANISOU 2006  O   ARG A 251     4203   4652   4952    127   -260    460  A    O  
ATOM   2007  CB  ARG A 251       6.164  23.147   0.103  1.00 52.17      A    C  
ANISOU 2007  CB  ARG A 251     6229   6555   7038    154   -349    400  A    C  
ATOM   2008  CG  ARG A 251       6.603  23.785   1.426  1.00 57.48      A    C  
ANISOU 2008  CG  ARG A 251     6920   7174   7744    177   -407    355  A    C  
ATOM   2009  CD  ARG A 251       5.422  24.363   2.219  1.00 57.20      A    C  
ANISOU 2009  CD  ARG A 251     6910   7136   7685    203   -420    313  A    C  
ATOM   2010  NE  ARG A 251       4.603  23.266   2.693  1.00 61.72      A    N  
ANISOU 2010  NE  ARG A 251     7525   7756   8168    210   -383    291  A    N  
ATOM   2011  CZ  ARG A 251       3.321  23.318   3.039  1.00 55.08      A    C  
ANISOU 2011  CZ  ARG A 251     6703   6945   7277    226   -366    270  A    C  
ATOM   2012  NH1 ARG A 251       2.626  24.405   2.987  1.00 50.61      A    N1+
ANISOU 2012  NH1 ARG A 251     6122   6368   6737    240   -381    262  A    N1+
ATOM   2013  NH2 ARG A 251       2.741  22.226   3.449  1.00 55.17      A    N  
ANISOU 2013  NH2 ARG A 251     6746   7001   7215    227   -334    262  A    N  
ATOM   2014  N   PHE A 252       6.362  22.868  -3.100  1.00 39.54      A    N  
ANISOU 2014  N   PHE A 252     4540   5039   5444    115   -269    523  A    N  
ATOM   2015  CA  PHE A 252       5.649  22.358  -4.254  1.00 38.98      A    C  
ANISOU 2015  CA  PHE A 252     4458   5024   5327    110   -223    549  A    C  
ATOM   2016  C   PHE A 252       6.352  22.616  -5.553  1.00 37.64      A    C  
ANISOU 2016  C   PHE A 252     4229   4886   5184    101   -206    611  A    C  
ATOM   2017  O   PHE A 252       5.786  23.234  -6.456  1.00 41.16      A    O  
ANISOU 2017  O   PHE A 252     4644   5353   5640     96   -189    650  A    O  
ATOM   2018  CB  PHE A 252       4.218  22.835  -4.279  1.00 32.09      A    C  
ANISOU 2018  CB  PHE A 252     3599   4157   4437    112   -211    540  A    C  
ATOM   2019  CG  PHE A 252       3.523  22.772  -2.911  1.00 32.82      A    C  
ANISOU 2019  CG  PHE A 252     3740   4224   4504    125   -228    483  A    C  
ATOM   2020  CD1 PHE A 252       3.437  21.568  -2.204  1.00 36.75      A    C  
ANISOU 2020  CD1 PHE A 252     4281   4736   4945    131   -221    448  A    C  
ATOM   2021  CD2 PHE A 252       3.044  23.913  -2.312  1.00 34.37      A    C  
ANISOU 2021  CD2 PHE A 252     3937   4385   4737    135   -259    467  A    C  
ATOM   2022  CE1 PHE A 252       2.784  21.531  -0.971  1.00 36.53      A    C  
ANISOU 2022  CE1 PHE A 252     4292   4698   4888    145   -233    405  A    C  
ATOM   2023  CE2 PHE A 252       2.348  23.883  -1.074  1.00 36.89      A    C  
ANISOU 2023  CE2 PHE A 252     4297   4695   5023    155   -274    414  A    C  
ATOM   2024  CZ  PHE A 252       2.253  22.704  -0.407  1.00 33.84      A    C  
ANISOU 2024  CZ  PHE A 252     3950   4332   4575    160   -259    387  A    C  
ATOM   2025  N   PRO A 253       7.572  22.063  -5.694  1.00 40.87      A    N  
ANISOU 2025  N   PRO A 253     4621   5307   5598    103   -209    621  A    N  
ATOM   2026  CA  PRO A 253       8.398  22.448  -6.861  1.00 39.09      A    C  
ANISOU 2026  CA  PRO A 253     4329   5116   5404     99   -196    688  A    C  
ATOM   2027  C   PRO A 253       7.738  22.177  -8.211  1.00 39.37      A    C  
ANISOU 2027  C   PRO A 253     4342   5222   5393    105   -152    722  A    C  
ATOM   2028  O   PRO A 253       7.879  22.958  -9.169  1.00 35.86      A    O  
ANISOU 2028  O   PRO A 253     3841   4803   4978     97   -141    786  A    O  
ATOM   2029  CB  PRO A 253       9.705  21.663  -6.653  1.00 40.16      A    C  
ANISOU 2029  CB  PRO A 253     4460   5261   5536    106   -204    681  A    C  
ATOM   2030  CG  PRO A 253       9.301  20.478  -5.818  1.00 38.73      A    C  
ANISOU 2030  CG  PRO A 253     4347   5072   5296    118   -204    611  A    C  
ATOM   2031  CD  PRO A 253       8.281  21.098  -4.825  1.00 40.68      A    C  
ANISOU 2031  CD  PRO A 253     4634   5270   5553    113   -223    577  A    C  
ATOM   2032  N   ASN A 254       6.954  21.124  -8.294  1.00 41.39      A    N  
ANISOU 2032  N   ASN A 254     4641   5507   5578    117   -129    681  A    N  
ATOM   2033  CA  ASN A 254       6.434  20.735  -9.572  1.00 38.52      A    C  
ANISOU 2033  CA  ASN A 254     4257   5210   5167    128    -92    704  A    C  
ATOM   2034  C   ASN A 254       5.192  21.576  -9.958  1.00 36.41      A    C  
ANISOU 2034  C   ASN A 254     3984   4941   4906    118    -80    723  A    C  
ATOM   2035  O   ASN A 254       4.716  21.481 -11.034  1.00 38.75      A    O  
ANISOU 2035  O   ASN A 254     4259   5289   5172    127    -53    748  A    O  
ATOM   2036  CB  ASN A 254       6.196  19.232  -9.647  1.00 39.60      A    C  
ANISOU 2036  CB  ASN A 254     4433   5377   5235    147    -79    655  A    C  
ATOM   2037  CG  ASN A 254       7.485  18.391  -9.846  1.00 43.27      A    C  
ANISOU 2037  CG  ASN A 254     4884   5871   5685    166    -84    650  A    C  
ATOM   2038  ND2 ASN A 254       8.196  18.579 -10.977  1.00 38.03      A    N  
ANISOU 2038  ND2 ASN A 254     4161   5269   5021    181    -64    700  A    N  
ATOM   2039  OD1 ASN A 254       7.790  17.543  -9.015  1.00 49.43      A    O  
ANISOU 2039  OD1 ASN A 254     5705   6624   6452    169   -102    604  A    O  
ATOM   2040  N   PHE A 255       4.749  22.472  -9.120  1.00 37.74      A    N  
ANISOU 2040  N   PHE A 255     4168   5052   5119    104   -104    713  A    N  
ATOM   2041  CA  PHE A 255       3.708  23.384  -9.540  1.00 40.26      A    C  
ANISOU 2041  CA  PHE A 255     4475   5369   5453     96    -98    736  A    C  
ATOM   2042  C   PHE A 255       4.235  24.357 -10.567  1.00 39.20      A    C  
ANISOU 2042  C   PHE A 255     4272   5254   5366     88    -95    813  A    C  
ATOM   2043  O   PHE A 255       3.458  25.049 -11.233  1.00 36.06      A    O  
ANISOU 2043  O   PHE A 255     3855   4868   4977     84    -84    846  A    O  
ATOM   2044  CB  PHE A 255       3.154  24.161  -8.345  1.00 38.75      A    C  
ANISOU 2044  CB  PHE A 255     4313   5109   5298     90   -131    701  A    C  
ATOM   2045  CG  PHE A 255       1.902  24.929  -8.637  1.00 36.59      A    C  
ANISOU 2045  CG  PHE A 255     4038   4834   5030     87   -126    708  A    C  
ATOM   2046  CD1 PHE A 255       0.685  24.270  -8.785  1.00 37.97      A    C  
ANISOU 2046  CD1 PHE A 255     4244   5040   5141     94    -97    679  A    C  
ATOM   2047  CD2 PHE A 255       1.922  26.297  -8.708  1.00 39.20      A    C  
ANISOU 2047  CD2 PHE A 255     4335   5126   5431     79   -154    742  A    C  
ATOM   2048  CE1 PHE A 255      -0.459  24.980  -9.036  1.00 40.51      A    C  
ANISOU 2048  CE1 PHE A 255     4562   5359   5467     93    -93    685  A    C  
ATOM   2049  CE2 PHE A 255       0.768  27.013  -8.961  1.00 41.76      A    C  
ANISOU 2049  CE2 PHE A 255     4658   5446   5761     78   -153    746  A    C  
ATOM   2050  CZ  PHE A 255      -0.417  26.355  -9.125  1.00 41.46      A    C  
ANISOU 2050  CZ  PHE A 255     4651   5444   5656     86   -120    717  A    C  
ATOM   2051  N   GLN A 256       5.554  24.440 -10.687  1.00 37.81      A    N  
ANISOU 2051  N   GLN A 256     4058   5082   5224     86   -105    849  A    N  
ATOM   2052  CA  GLN A 256       6.214  25.171 -11.778  1.00 35.90      A    C  
ANISOU 2052  CA  GLN A 256     3741   4877   5020     79    -96    936  A    C  
ATOM   2053  C   GLN A 256       6.021  24.553 -13.138  1.00 34.42      A    C  
ANISOU 2053  C   GLN A 256     3528   4783   4765    100    -50    966  A    C  
ATOM   2054  O   GLN A 256       6.281  25.218 -14.167  1.00 39.40      A    O  
ANISOU 2054  O   GLN A 256     4095   5458   5416     96    -36   1044  A    O  
ATOM   2055  CB  GLN A 256       7.758  25.352 -11.510  1.00 41.15      A    C  
ANISOU 2055  CB  GLN A 256     4367   5528   5740     72   -120    968  A    C  
ATOM   2056  CG  GLN A 256       7.975  26.416 -10.437  1.00 41.96      A    C  
ANISOU 2056  CG  GLN A 256     4474   5536   5933     51   -177    962  A    C  
ATOM   2057  CD  GLN A 256       9.358  26.390  -9.842  1.00 47.83      A    C  
ANISOU 2057  CD  GLN A 256     5199   6248   6725     44   -208    969  A    C  
ATOM   2058  NE2 GLN A 256       9.791  25.259  -9.296  1.00 44.67      A    N  
ANISOU 2058  NE2 GLN A 256     4837   5859   6275     61   -201    913  A    N  
ATOM   2059  OE1 GLN A 256      10.039  27.398  -9.911  1.00 47.86      A    O  
ANISOU 2059  OE1 GLN A 256     5150   6220   6815     25   -241   1028  A    O  
ATOM   2060  N   ASN A 257       5.639  23.285 -13.177  1.00 35.85      A    N  
ANISOU 2060  N   ASN A 257     3753   4999   4869    122    -29    908  A    N  
ATOM   2061  CA  ASN A 257       5.423  22.573 -14.419  1.00 35.28      A    C  
ANISOU 2061  CA  ASN A 257     3662   5013   4727    149      8    921  A    C  
ATOM   2062  C   ASN A 257       3.925  22.405 -14.775  1.00 36.28      A    C  
ANISOU 2062  C   ASN A 257     3821   5151   4810    154     24    893  A    C  
ATOM   2063  O   ASN A 257       3.575  21.768 -15.770  1.00 42.29      A    O  
ANISOU 2063  O   ASN A 257     4575   5979   5511    180     49    892  A    O  
ATOM   2064  CB  ASN A 257       6.025  21.220 -14.357  1.00 33.28      A    C  
ANISOU 2064  CB  ASN A 257     3432   4793   4420    176     12    874  A    C  
ATOM   2065  CG  ASN A 257       7.465  21.247 -13.928  1.00 40.58      A    C  
ANISOU 2065  CG  ASN A 257     4329   5706   5381    174     -3    890  A    C  
ATOM   2066  ND2 ASN A 257       8.289  21.739 -14.831  1.00 34.41      A    N  
ANISOU 2066  ND2 ASN A 257     3476   4982   4615    180     11    964  A    N  
ATOM   2067  OD1 ASN A 257       7.853  20.791 -12.768  1.00 41.85      A    O  
ANISOU 2067  OD1 ASN A 257     4532   5811   5556    166    -30    838  A    O  
ATOM   2068  N   VAL A 258       3.045  23.030 -14.022  1.00 40.33      A    N  
ANISOU 2068  N   VAL A 258     4365   5601   5357    133      7    874  A    N  
ATOM   2069  CA  VAL A 258       1.665  22.733 -14.203  1.00 39.17      A    C  
ANISOU 2069  CA  VAL A 258     4252   5461   5168    136     21    841  A    C  
ATOM   2070  C   VAL A 258       1.122  23.487 -15.426  1.00 42.10      A    C  
ANISOU 2070  C   VAL A 258     4580   5877   5538    140     41    899  A    C  
ATOM   2071  O   VAL A 258       1.534  24.634 -15.692  1.00 37.99      A    O  
ANISOU 2071  O   VAL A 258     4011   5347   5075    125     34    964  A    O  
ATOM   2072  CB  VAL A 258       0.885  23.104 -12.975  1.00 42.92      A    C  
ANISOU 2072  CB  VAL A 258     4772   5863   5669    118     -1    798  A    C  
ATOM   2073  CG1 VAL A 258       0.489  24.568 -12.991  1.00 40.83      A    C  
ANISOU 2073  CG1 VAL A 258     4481   5565   5465    102    -14    837  A    C  
ATOM   2074  CG2 VAL A 258      -0.290  22.208 -12.900  1.00 53.15      A    C  
ANISOU 2074  CG2 VAL A 258     6113   7171   6907    126     12    748  A    C  
ATOM   2075  N   VAL A 259       0.310  22.806 -16.212  1.00 40.47      A    N  
ANISOU 2075  N   VAL A 259     4384   5720   5270    160     64    882  A    N  
ATOM   2076  CA  VAL A 259      -0.301  23.446 -17.361  1.00 42.76      A    C  
ANISOU 2076  CA  VAL A 259     4637   6056   5553    166     84    932  A    C  
ATOM   2077  C   VAL A 259      -1.838  23.150 -17.425  1.00 42.75      A    C  
ANISOU 2077  C   VAL A 259     4676   6048   5516    168     90    890  A    C  
ATOM   2078  O   VAL A 259      -2.228  22.019 -17.496  1.00 44.35      A    O  
ANISOU 2078  O   VAL A 259     4912   6272   5667    186     95    841  A    O  
ATOM   2079  CB  VAL A 259       0.287  22.924 -18.667  1.00 43.73      A    C  
ANISOU 2079  CB  VAL A 259     4718   6274   5623    201    109    966  A    C  
ATOM   2080  CG1 VAL A 259      -0.281  23.781 -19.786  1.00 51.73      A    C  
ANISOU 2080  CG1 VAL A 259     5687   7332   6635    205    128   1029  A    C  
ATOM   2081  CG2 VAL A 259       1.822  22.952 -18.689  1.00 44.85      A    C  
ANISOU 2081  CG2 VAL A 259     4817   6439   5783    206    108   1004  A    C  
ATOM   2082  N   GLY A 260      -2.651  24.185 -17.506  1.00 42.99      A    N  
ANISOU 2082  N   GLY A 260     4697   6056   5580    152     88    916  A    N  
ATOM   2083  CA  GLY A 260      -4.118  24.079 -17.452  1.00 46.38      A    C  
ANISOU 2083  CA  GLY A 260     5161   6474   5987    151     92    879  A    C  
ATOM   2084  C   GLY A 260      -4.874  24.111 -18.809  1.00 50.63      A    C  
ANISOU 2084  C   GLY A 260     5675   7073   6486    170    114    906  A    C  
ATOM   2085  O   GLY A 260      -4.300  24.406 -19.898  1.00 42.32      A    O  
ANISOU 2085  O   GLY A 260     4574   6082   5425    185    130    964  A    O  
ATOM   2086  N   TYR A 261      -6.163  23.784 -18.718  1.00 42.87      A    N  
ANISOU 2086  N   TYR A 261     4726   6082   5479    169    116    866  A    N  
ATOM   2087  CA  TYR A 261      -7.073  23.888 -19.801  1.00 42.10      A    C  
ANISOU 2087  CA  TYR A 261     4615   6029   5353    185    131    882  A    C  
ATOM   2088  C   TYR A 261      -8.164  24.827 -19.259  1.00 46.25      A    C  
ANISOU 2088  C   TYR A 261     5151   6503   5915    161    123    879  A    C  
ATOM   2089  O   TYR A 261      -8.705  24.630 -18.122  1.00 38.65      A    O  
ANISOU 2089  O   TYR A 261     4230   5491   4964    148    111    830  A    O  
ATOM   2090  CB  TYR A 261      -7.676  22.537 -20.110  1.00 45.19      A    C  
ANISOU 2090  CB  TYR A 261     5037   6450   5682    207    135    828  A    C  
ATOM   2091  CG  TYR A 261      -6.834  21.529 -20.836  1.00 50.26      A    C  
ANISOU 2091  CG  TYR A 261     5668   7149   6275    240    139    820  A    C  
ATOM   2092  CD1 TYR A 261      -5.902  20.756 -20.182  1.00 57.04      A    C  
ANISOU 2092  CD1 TYR A 261     6544   7994   7132    242    128    791  A    C  
ATOM   2093  CD2 TYR A 261      -7.020  21.303 -22.203  1.00 76.58      A    C  
ANISOU 2093  CD2 TYR A 261     8976  10558   9562    278    152    836  A    C  
ATOM   2094  CE1 TYR A 261      -5.162  19.819 -20.859  1.00 65.66      A    C  
ANISOU 2094  CE1 TYR A 261     7627   9142   8178    280    127    777  A    C  
ATOM   2095  CE2 TYR A 261      -6.272  20.370 -22.891  1.00 76.79      A    C  
ANISOU 2095  CE2 TYR A 261     8992  10645   9538    319    152    822  A    C  
ATOM   2096  CZ  TYR A 261      -5.368  19.614 -22.197  1.00 75.04      A    C  
ANISOU 2096  CZ  TYR A 261     8788  10405   9318    319    139    789  A    C  
ATOM   2097  OH  TYR A 261      -4.619  18.691 -22.852  1.00 83.90      A    O  
ANISOU 2097  OH  TYR A 261     9899  11587  10392    365    135    770  A    O  
ATOM   2098  N   GLU A 262      -8.510  25.875 -20.003  1.00 40.60      A    N  
ANISOU 2098  N   GLU A 262     4401   5801   5223    160    127    930  A    N  
ATOM   2099  CA  GLU A 262      -9.446  26.797 -19.383  1.00 38.94      A    C  
ANISOU 2099  CA  GLU A 262     4202   5536   5056    142    112    922  A    C  
ATOM   2100  C   GLU A 262     -10.595  27.218 -20.264  1.00 38.88      A    C  
ANISOU 2100  C   GLU A 262     4182   5554   5035    149    122    939  A    C  
ATOM   2101  O   GLU A 262     -10.522  27.098 -21.464  1.00 38.67      A    O  
ANISOU 2101  O   GLU A 262     4128   5587   4977    166    138    975  A    O  
ATOM   2102  CB  GLU A 262      -8.761  27.975 -18.742  1.00 40.49      A    C  
ANISOU 2102  CB  GLU A 262     4378   5677   5326    122     86    954  A    C  
ATOM   2103  CG  GLU A 262      -8.408  29.140 -19.588  1.00 43.17      A    C  
ANISOU 2103  CG  GLU A 262     4664   6026   5711    116     79   1034  A    C  
ATOM   2104  CD  GLU A 262      -7.965  30.342 -18.790  1.00 45.40      A    C  
ANISOU 2104  CD  GLU A 262     4933   6236   6080     95     40   1054  A    C  
ATOM   2105  OE1 GLU A 262      -6.775  30.408 -18.577  1.00 48.79      A    O  
ANISOU 2105  OE1 GLU A 262     5343   6656   6539     88     30   1080  A    O  
ATOM   2106  OE2 GLU A 262      -8.755  31.198 -18.354  1.00 49.07      A    O1-
ANISOU 2106  OE2 GLU A 262     5405   6652   6585     89     15   1041  A    O1-
ATOM   2107  N   THR A 263     -11.640  27.678 -19.628  1.00 39.12      A    N  
ANISOU 2107  N   THR A 263     4233   5542   5085    139    111    910  A    N  
ATOM   2108  CA  THR A 263     -12.781  28.179 -20.355  1.00 43.97      A    C  
ANISOU 2108  CA  THR A 263     4837   6172   5695    144    116    924  A    C  
ATOM   2109  C   THR A 263     -13.581  29.087 -19.449  1.00 41.89      A    C  
ANISOU 2109  C   THR A 263     4587   5851   5478    132     94    901  A    C  
ATOM   2110  O   THR A 263     -13.425  29.113 -18.199  1.00 39.76      A    O  
ANISOU 2110  O   THR A 263     4342   5535   5228    124     78    862  A    O  
ATOM   2111  CB  THR A 263     -13.660  27.047 -20.918  1.00 43.45      A    C  
ANISOU 2111  CB  THR A 263     4792   6151   5564    160    134    889  A    C  
ATOM   2112  CG2 THR A 263     -14.485  26.526 -19.841  1.00 43.28      A    C  
ANISOU 2112  CG2 THR A 263     4811   6096   5536    151    129    828  A    C  
ATOM   2113  OG1 THR A 263     -14.510  27.566 -21.950  1.00 38.85      A    O  
ANISOU 2113  OG1 THR A 263     4187   5598   4973    170    141    917  A    O  
ATOM   2114  N   VAL A 264     -14.375  29.930 -20.101  1.00 39.80      A    N  
ANISOU 2114  N   VAL A 264     4302   5589   5229    134     91    929  A    N  
ATOM   2115  CA  VAL A 264     -15.404  30.674 -19.330  1.00 40.70      A    C  
ANISOU 2115  CA  VAL A 264     4431   5657   5375    131     71    896  A    C  
ATOM   2116  C   VAL A 264     -16.770  30.272 -19.776  1.00 43.42      A    C  
ANISOU 2116  C   VAL A 264     4786   6033   5678    140     88    872  A    C  
ATOM   2117  O   VAL A 264     -17.107  30.338 -21.000  1.00 40.14      A    O  
ANISOU 2117  O   VAL A 264     4349   5657   5243    148    101    908  A    O  
ATOM   2118  CB  VAL A 264     -15.318  32.166 -19.413  1.00 45.46      A    C  
ANISOU 2118  CB  VAL A 264     5003   6219   6049    125     39    937  A    C  
ATOM   2119  CG1 VAL A 264     -16.430  32.777 -18.536  1.00 44.25      A    C  
ANISOU 2119  CG1 VAL A 264     4870   6025   5918    131     16    887  A    C  
ATOM   2120  CG2 VAL A 264     -13.940  32.610 -18.942  1.00 40.80      A    C  
ANISOU 2120  CG2 VAL A 264     4398   5593   5511    113     15    964  A    C  
ATOM   2121  N   VAL A 265     -17.520  29.751 -18.807  1.00 41.98      A    N  
ANISOU 2121  N   VAL A 265     4637   5838   5476    141     90    814  A    N  
ATOM   2122  CA  VAL A 265     -18.871  29.276 -19.074  1.00 41.92      A    C  
ANISOU 2122  CA  VAL A 265     4639   5855   5431    147    104    788  A    C  
ATOM   2123  C   VAL A 265     -19.888  30.305 -18.648  1.00 41.05      A    C  
ANISOU 2123  C   VAL A 265     4525   5718   5352    151     88    774  A    C  
ATOM   2124  O   VAL A 265     -19.757  30.898 -17.610  1.00 39.86      A    O  
ANISOU 2124  O   VAL A 265     4381   5529   5232    153     68    751  A    O  
ATOM   2125  CB  VAL A 265     -19.262  27.940 -18.383  1.00 37.68      A    C  
ANISOU 2125  CB  VAL A 265     4135   5331   4851    144    118    741  A    C  
ATOM   2126  CG1 VAL A 265     -18.646  26.755 -19.053  1.00 43.68      A    C  
ANISOU 2126  CG1 VAL A 265     4899   6124   5572    145    130    746  A    C  
ATOM   2127  CG2 VAL A 265     -19.027  27.925 -16.897  1.00 41.75      A    C  
ANISOU 2127  CG2 VAL A 265     4671   5814   5377    139    107    705  A    C  
ATOM   2128  N   GLY A 266     -20.899  30.505 -19.488  1.00 41.17      A    N  
ANISOU 2128  N   GLY A 266     4528   5756   5356    157     96    784  A    N  
ATOM   2129  CA  GLY A 266     -22.062  31.300 -19.072  1.00 43.06      A    C  
ANISOU 2129  CA  GLY A 266     4765   5977   5616    165     82    762  A    C  
ATOM   2130  C   GLY A 266     -23.406  30.590 -19.242  1.00 38.52      A    C  
ANISOU 2130  C   GLY A 266     4200   5437   5000    170    101    734  A    C  
ATOM   2131  O   GLY A 266     -23.487  29.350 -19.528  1.00 43.20      A    O  
ANISOU 2131  O   GLY A 266     4804   6060   5549    164    121    726  A    O  
ATOM   2132  N   PRO A 267     -24.492  31.360 -19.083  1.00 42.84      A    N  
ANISOU 2132  N   PRO A 267     4738   5976   5563    180     91    720  A    N  
ATOM   2133  CA  PRO A 267     -25.843  30.779 -19.106  1.00 39.30      A    C  
ANISOU 2133  CA  PRO A 267     4292   5557   5080    182    107    694  A    C  
ATOM   2134  C   PRO A 267     -26.051  29.877 -20.296  1.00 38.22      A    C  
ANISOU 2134  C   PRO A 267     4154   5457   4910    178    123    713  A    C  
ATOM   2135  O   PRO A 267     -25.824  30.268 -21.439  1.00 37.93      A    O  
ANISOU 2135  O   PRO A 267     4101   5430   4879    183    121    749  A    O  
ATOM   2136  CB  PRO A 267     -26.728  32.042 -19.185  1.00 49.36      A    C  
ANISOU 2136  CB  PRO A 267     5550   6816   6389    199     89    691  A    C  
ATOM   2137  CG  PRO A 267     -25.968  33.055 -18.394  1.00 48.54      A    C  
ANISOU 2137  CG  PRO A 267     5446   6668   6331    206     59    686  A    C  
ATOM   2138  CD  PRO A 267     -24.539  32.825 -18.864  1.00 41.91      A    C  
ANISOU 2138  CD  PRO A 267     4605   5818   5500    191     60    725  A    C  
ATOM   2139  N   GLY A 268     -26.403  28.636 -20.050  1.00 37.93      A    N  
ANISOU 2139  N   GLY A 268     4132   5441   4838    169    137    692  A    N  
ATOM   2140  CA  GLY A 268     -26.651  27.697 -21.156  1.00 37.78      A    C  
ANISOU 2140  CA  GLY A 268     4111   5454   4789    169    143    700  A    C  
ATOM   2141  C   GLY A 268     -25.548  26.739 -21.497  1.00 39.14      A    C  
ANISOU 2141  C   GLY A 268     4295   5636   4940    167    145    706  A    C  
ATOM   2142  O   GLY A 268     -25.755  25.639 -22.124  1.00 38.03      A    O  
ANISOU 2142  O   GLY A 268     4160   5518   4770    170    143    697  A    O  
ATOM   2143  N   ASP A 269     -24.351  27.121 -21.080  1.00 40.74      A    N  
ANISOU 2143  N   ASP A 269     4501   5820   5158    165    143    718  A    N  
ATOM   2144  CA  ASP A 269     -23.184  26.239 -21.316  1.00 39.40      A    C  
ANISOU 2144  CA  ASP A 269     4340   5660   4967    165    145    723  A    C  
ATOM   2145  C   ASP A 269     -23.194  25.059 -20.338  1.00 41.02      A    C  
ANISOU 2145  C   ASP A 269     4570   5856   5157    151    145    689  A    C  
ATOM   2146  O   ASP A 269     -23.625  25.177 -19.196  1.00 35.92      A    O  
ANISOU 2146  O   ASP A 269     3933   5191   4521    140    146    671  A    O  
ATOM   2147  CB  ASP A 269     -21.890  27.015 -21.171  1.00 37.06      A    C  
ANISOU 2147  CB  ASP A 269     4034   5347   4697    164    142    751  A    C  
ATOM   2148  CG  ASP A 269     -21.738  28.149 -22.214  1.00 37.24      A    C  
ANISOU 2148  CG  ASP A 269     4027   5381   4740    176    139    800  A    C  
ATOM   2149  OD1 ASP A 269     -22.320  28.075 -23.333  1.00 35.84      A    O  
ANISOU 2149  OD1 ASP A 269     3837   5238   4542    188    145    814  A    O  
ATOM   2150  OD2 ASP A 269     -21.006  29.118 -21.903  1.00 41.73      A    O1-
ANISOU 2150  OD2 ASP A 269     4582   5921   5349    170    129    826  A    O1-
ATOM   2151  N   VAL A 270     -22.700  23.909 -20.810  1.00 36.62      A    N  
ANISOU 2151  N   VAL A 270     4023   5316   4573    155    141    682  A    N  
ATOM   2152  CA  VAL A 270     -22.490  22.784 -19.905  1.00 35.55      A    C  
ANISOU 2152  CA  VAL A 270     3910   5167   4429    140    134    656  A    C  
ATOM   2153  C   VAL A 270     -20.978  22.346 -20.151  1.00 34.78      A    C  
ANISOU 2153  C   VAL A 270     3819   5073   4321    150    131    661  A    C  
ATOM   2154  O   VAL A 270     -20.521  22.252 -21.315  1.00 37.70      A    O  
ANISOU 2154  O   VAL A 270     4177   5472   4673    171    130    675  A    O  
ATOM   2155  CB  VAL A 270     -23.440  21.686 -20.258  1.00 36.74      A    C  
ANISOU 2155  CB  VAL A 270     4067   5329   4564    138    123    639  A    C  
ATOM   2156  CG1 VAL A 270     -23.116  20.440 -19.459  1.00 41.67      A    C  
ANISOU 2156  CG1 VAL A 270     4712   5936   5183    122    110    620  A    C  
ATOM   2157  CG2 VAL A 270     -24.910  22.087 -20.025  1.00 39.40      A    C  
ANISOU 2157  CG2 VAL A 270     4392   5667   4910    128    128    638  A    C  
ATOM   2158  N   LEU A 271     -20.220  22.278 -19.077  1.00 34.97      A    N  
ANISOU 2158  N   LEU A 271     3857   5072   4356    138    131    655  A    N  
ATOM   2159  CA  LEU A 271     -18.834  21.800 -19.071  1.00 32.21      A    C  
ANISOU 2159  CA  LEU A 271     3515   4722   4000    143    126    656  A    C  
ATOM   2160  C   LEU A 271     -18.767  20.348 -18.558  1.00 31.72      A    C  
ANISOU 2160  C   LEU A 271     3477   4650   3922    134    112    627  A    C  
ATOM   2161  O   LEU A 271     -19.257  20.004 -17.467  1.00 32.78      A    O  
ANISOU 2161  O   LEU A 271     3626   4764   4062    113    109    613  A    O  
ATOM   2162  CB  LEU A 271     -17.964  22.732 -18.213  1.00 34.03      A    C  
ANISOU 2162  CB  LEU A 271     3744   4925   4259    135    130    667  A    C  
ATOM   2163  CG  LEU A 271     -16.513  22.262 -18.021  1.00 34.79      A    C  
ANISOU 2163  CG  LEU A 271     3847   5017   4353    138    125    668  A    C  
ATOM   2164  CD1 LEU A 271     -15.736  22.199 -19.322  1.00 35.01      A    C  
ANISOU 2164  CD1 LEU A 271     3853   5083   4364    160    129    693  A    C  
ATOM   2165  CD2 LEU A 271     -15.783  23.160 -17.034  1.00 41.70      A    C  
ANISOU 2165  CD2 LEU A 271     4722   5858   5261    128    123    676  A    C  
ATOM   2166  N   TYR A 272     -18.307  19.434 -19.409  1.00 28.88      A    N  
ANISOU 2166  N   TYR A 272     3120   4311   3540    151     98    617  A    N  
ATOM   2167  CA  TYR A 272     -17.976  18.133 -18.953  1.00 30.57      A    C  
ANISOU 2167  CA  TYR A 272     3356   4510   3746    146     77    591  A    C  
ATOM   2168  C   TYR A 272     -16.667  18.237 -18.232  1.00 33.89      A    C  
ANISOU 2168  C   TYR A 272     3786   4916   4174    142     81    594  A    C  
ATOM   2169  O   TYR A 272     -15.605  18.528 -18.871  1.00 35.73      A    O  
ANISOU 2169  O   TYR A 272     4005   5170   4399    164     86    606  A    O  
ATOM   2170  CB  TYR A 272     -17.929  17.134 -20.070  1.00 33.18      A    C  
ANISOU 2170  CB  TYR A 272     3687   4864   4054    172     53    571  A    C  
ATOM   2171  CG  TYR A 272     -17.484  15.755 -19.705  1.00 34.95      A    C  
ANISOU 2171  CG  TYR A 272     3935   5069   4277    171     22    543  A    C  
ATOM   2172  CD1 TYR A 272     -17.994  15.103 -18.590  1.00 36.84      A    C  
ANISOU 2172  CD1 TYR A 272     4191   5271   4534    138      8    536  A    C  
ATOM   2173  CD2 TYR A 272     -16.452  15.149 -20.405  1.00 33.86      A    C  
ANISOU 2173  CD2 TYR A 272     3796   4951   4116    204      4    526  A    C  
ATOM   2174  CE1 TYR A 272     -17.524  13.856 -18.225  1.00 38.61      A    C  
ANISOU 2174  CE1 TYR A 272     4436   5473   4762    134    -24    516  A    C  
ATOM   2175  CE2 TYR A 272     -15.986  13.885 -20.033  1.00 38.37      A    C  
ANISOU 2175  CE2 TYR A 272     4390   5499   4690    204    -30    496  A    C  
ATOM   2176  CZ  TYR A 272     -16.508  13.248 -18.944  1.00 38.22      A    C  
ANISOU 2176  CZ  TYR A 272     4389   5435   4695    167    -46    492  A    C  
ATOM   2177  OH  TYR A 272     -16.043  11.989 -18.556  1.00 38.77      A    O  
ANISOU 2177  OH  TYR A 272     4480   5477   4772    165    -85    467  A    O  
ATOM   2178  N   ILE A 273     -16.740  17.969 -16.921  1.00 35.86      A    N  
ANISOU 2178  N   ILE A 273     4054   5133   4435    117     78    585  A    N  
ATOM   2179  CA  ILE A 273     -15.575  17.786 -16.040  1.00 32.74      A    C  
ANISOU 2179  CA  ILE A 273     3674   4718   4047    111     75    580  A    C  
ATOM   2180  C   ILE A 273     -15.414  16.251 -15.792  1.00 34.03      A    C  
ANISOU 2180  C   ILE A 273     3860   4869   4201    106     47    557  A    C  
ATOM   2181  O   ILE A 273     -16.115  15.639 -14.988  1.00 35.54      A    O  
ANISOU 2181  O   ILE A 273     4063   5041   4396     85     37    553  A    O  
ATOM   2182  CB  ILE A 273     -15.763  18.529 -14.776  1.00 32.56      A    C  
ANISOU 2182  CB  ILE A 273     3656   4674   4041     94     87    584  A    C  
ATOM   2183  CG1 ILE A 273     -16.005  20.020 -15.059  1.00 31.88      A    C  
ANISOU 2183  CG1 ILE A 273     3547   4592   3971    102    103    603  A    C  
ATOM   2184  CG2 ILE A 273     -14.517  18.496 -13.884  1.00 37.13      A    C  
ANISOU 2184  CG2 ILE A 273     4248   5231   4627     92     82    580  A    C  
ATOM   2185  CD1 ILE A 273     -16.246  20.780 -13.727  1.00 32.26      A    C  
ANISOU 2185  CD1 ILE A 273     3602   4619   4036     93    107    598  A    C  
ATOM   2186  N   PRO A 274     -14.499  15.619 -16.516  1.00 30.25      A    N  
ANISOU 2186  N   PRO A 274     3381   4402   3710    129     32    545  A    N  
ATOM   2187  CA  PRO A 274     -14.318  14.194 -16.419  1.00 30.44      A    C  
ANISOU 2187  CA  PRO A 274     3426   4411   3730    129     -2    519  A    C  
ATOM   2188  C   PRO A 274     -13.784  13.824 -15.024  1.00 35.95      A    C  
ANISOU 2188  C   PRO A 274     4145   5074   4440    106     -8    517  A    C  
ATOM   2189  O   PRO A 274     -13.149  14.670 -14.387  1.00 35.52      A    O  
ANISOU 2189  O   PRO A 274     4088   5015   4390    101     12    529  A    O  
ATOM   2190  CB  PRO A 274     -13.253  13.895 -17.474  1.00 31.94      A    C  
ANISOU 2190  CB  PRO A 274     3606   4630   3898    169    -13    505  A    C  
ATOM   2191  CG  PRO A 274     -13.061  15.111 -18.324  1.00 32.29      A    C  
ANISOU 2191  CG  PRO A 274     3622   4712   3933    189     17    530  A    C  
ATOM   2192  CD  PRO A 274     -13.482  16.251 -17.396  1.00 32.57      A    C  
ANISOU 2192  CD  PRO A 274     3654   4726   3993    158     44    556  A    C  
ATOM   2193  N   MET A 275     -14.156  12.622 -14.553  1.00 34.16      A    N  
ANISOU 2193  N   MET A 275     3936   4823   4219     89    -40    506  A    N  
ATOM   2194  CA  MET A 275     -13.795  12.124 -13.224  1.00 37.56      A    C  
ANISOU 2194  CA  MET A 275     4387   5224   4660     64    -49    509  A    C  
ATOM   2195  C   MET A 275     -12.262  12.159 -13.127  1.00 35.13      A    C  
ANISOU 2195  C   MET A 275     4086   4912   4346     82    -51    496  A    C  
ATOM   2196  O   MET A 275     -11.546  11.894 -14.120  1.00 33.35      A    O  
ANISOU 2196  O   MET A 275     3855   4704   4111    112    -63    479  A    O  
ATOM   2197  CB  MET A 275     -14.266  10.679 -13.115  1.00 39.75      A    C  
ANISOU 2197  CB  MET A 275     4677   5476   4949     49    -94    501  A    C  
ATOM   2198  CG  MET A 275     -14.094  10.075 -11.751  1.00 41.89      A    C  
ANISOU 2198  CG  MET A 275     4966   5720   5230     21   -105    514  A    C  
ATOM   2199  SD  MET A 275     -15.030   8.565 -11.597  1.00 48.40      A    S  
ANISOU 2199  SD  MET A 275     5795   6513   6080     -7   -158    524  A    S  
ATOM   2200  CE  MET A 275     -14.433   7.698 -13.078  1.00 49.08      A    C  
ANISOU 2200  CE  MET A 275     5886   6591   6171     32   -209    477  A    C  
ATOM   2201  N   TYR A 276     -11.789  12.573 -11.959  1.00 35.05      A    N  
ANISOU 2201  N   TYR A 276     4086   4888   4342     67    -37    505  A    N  
ATOM   2202  CA  TYR A 276     -10.336  12.667 -11.601  1.00 36.13      A    C  
ANISOU 2202  CA  TYR A 276     4231   5016   4481     79    -39    495  A    C  
ATOM   2203  C   TYR A 276      -9.669  13.908 -12.187  1.00 36.63      A    C  
ANISOU 2203  C   TYR A 276     4271   5100   4545     98    -12    506  A    C  
ATOM   2204  O   TYR A 276      -8.505  14.119 -11.944  1.00 33.28      A    O  
ANISOU 2204  O   TYR A 276     3847   4670   4127    106    -12    504  A    O  
ATOM   2205  CB  TYR A 276      -9.497  11.449 -12.010  1.00 37.37      A    C  
ANISOU 2205  CB  TYR A 276     4400   5165   4634     95    -75    471  A    C  
ATOM   2206  CG  TYR A 276      -9.811  10.195 -11.258  1.00 40.83      A    C  
ANISOU 2206  CG  TYR A 276     4861   5570   5080     73   -110    465  A    C  
ATOM   2207  CD1 TYR A 276      -9.386   9.994  -9.964  1.00 41.65      A    C  
ANISOU 2207  CD1 TYR A 276     4983   5649   5190     53   -114    472  A    C  
ATOM   2208  CD2 TYR A 276     -10.524   9.180 -11.867  1.00 43.97      A    C  
ANISOU 2208  CD2 TYR A 276     5261   5960   5484     73   -145    456  A    C  
ATOM   2209  CE1 TYR A 276      -9.709   8.841  -9.255  1.00 39.06      A    C  
ANISOU 2209  CE1 TYR A 276     4673   5293   4872     30   -147    476  A    C  
ATOM   2210  CE2 TYR A 276     -10.835   8.012 -11.185  1.00 43.67      A    C  
ANISOU 2210  CE2 TYR A 276     5242   5888   5463     49   -185    458  A    C  
ATOM   2211  CZ  TYR A 276     -10.439   7.834  -9.898  1.00 45.48      A    C  
ANISOU 2211  CZ  TYR A 276     5486   6095   5697     26   -184    472  A    C  
ATOM   2212  OH  TYR A 276     -10.826   6.621  -9.327  1.00 39.84      A    O  
ANISOU 2212  OH  TYR A 276     4786   5348   5004      2   -227    483  A    O  
ATOM   2213  N   TRP A 277     -10.352  14.672 -13.023  1.00 32.91      A    N  
ANISOU 2213  N   TRP A 277     3778   4653   4072    106      6    520  A    N  
ATOM   2214  CA  TRP A 277      -9.711  15.894 -13.551  1.00 32.84      A    C  
ANISOU 2214  CA  TRP A 277     3743   4661   4070    120     27    539  A    C  
ATOM   2215  C   TRP A 277      -9.790  16.956 -12.502  1.00 33.01      A    C  
ANISOU 2215  C   TRP A 277     3766   4662   4115    104     40    550  A    C  
ATOM   2216  O   TRP A 277     -10.803  17.210 -11.922  1.00 31.52      A    O  
ANISOU 2216  O   TRP A 277     3584   4465   3927     91     47    550  A    O  
ATOM   2217  CB  TRP A 277     -10.291  16.387 -14.868  1.00 32.25      A    C  
ANISOU 2217  CB  TRP A 277     3641   4623   3986    136     41    554  A    C  
ATOM   2218  CG  TRP A 277      -9.869  15.667 -16.065  1.00 32.09      A    C  
ANISOU 2218  CG  TRP A 277     3612   4639   3943    168     29    544  A    C  
ATOM   2219  CD1 TRP A 277     -10.021  14.340 -16.325  1.00 34.30      A    C  
ANISOU 2219  CD1 TRP A 277     3909   4917   4205    178      2    513  A    C  
ATOM   2220  CD2 TRP A 277      -9.191  16.218 -17.193  1.00 33.24      A    C  
ANISOU 2220  CD2 TRP A 277     3724   4828   4075    196     44    565  A    C  
ATOM   2221  CE2 TRP A 277      -8.932  15.149 -18.084  1.00 33.18      A    C  
ANISOU 2221  CE2 TRP A 277     3716   4851   4036    230     24    539  A    C  
ATOM   2222  CE3 TRP A 277      -8.718  17.492 -17.512  1.00 36.64      A    C  
ANISOU 2222  CE3 TRP A 277     4124   5276   4521    198     67    606  A    C  
ATOM   2223  NE1 TRP A 277      -9.446  14.007 -17.515  1.00 33.68      A    N  
ANISOU 2223  NE1 TRP A 277     3814   4881   4102    217     -5    504  A    N  
ATOM   2224  CZ2 TRP A 277      -8.330  15.332 -19.300  1.00 35.54      A    C  
ANISOU 2224  CZ2 TRP A 277     3985   5210   4309    269     33    552  A    C  
ATOM   2225  CZ3 TRP A 277      -8.130  17.683 -18.765  1.00 34.30      A    C  
ANISOU 2225  CZ3 TRP A 277     3793   5036   4203    231     78    629  A    C  
ATOM   2226  CH2 TRP A 277      -7.978  16.634 -19.656  1.00 34.23      A    C  
ANISOU 2226  CH2 TRP A 277     3782   5068   4152    268     64    602  A    C  
ATOM   2227  N   TRP A 278      -8.655  17.559 -12.231  1.00 32.93      A    N  
ANISOU 2227  N   TRP A 278     3747   4640   4122    109     41    558  A    N  
ATOM   2228  CA  TRP A 278      -8.557  18.704 -11.367  1.00 32.48      A    C  
ANISOU 2228  CA  TRP A 278     3689   4559   4092    101     44    564  A    C  
ATOM   2229  C   TRP A 278      -9.297  19.880 -11.958  1.00 30.96      A    C  
ANISOU 2229  C   TRP A 278     3471   4377   3915    103     58    586  A    C  
ATOM   2230  O   TRP A 278      -9.256  20.093 -13.118  1.00 30.72      A    O  
ANISOU 2230  O   TRP A 278     3415   4373   3883    114     68    609  A    O  
ATOM   2231  CB  TRP A 278      -7.105  19.115 -11.202  1.00 32.86      A    C  
ANISOU 2231  CB  TRP A 278     3725   4592   4164    106     36    573  A    C  
ATOM   2232  CG  TRP A 278      -6.257  18.132 -10.532  1.00 35.17      A    C  
ANISOU 2232  CG  TRP A 278     4042   4872   4448    106     20    551  A    C  
ATOM   2233  CD1 TRP A 278      -5.634  17.115 -11.100  1.00 35.04      A    C  
ANISOU 2233  CD1 TRP A 278     4028   4871   4414    117     12    544  A    C  
ATOM   2234  CD2 TRP A 278      -5.958  18.070  -9.155  1.00 34.65      A    C  
ANISOU 2234  CD2 TRP A 278     4002   4773   4390     97      6    532  A    C  
ATOM   2235  CE2 TRP A 278      -5.140  16.976  -8.968  1.00 33.63      A    C  
ANISOU 2235  CE2 TRP A 278     3889   4638   4249     98     -7    517  A    C  
ATOM   2236  CE3 TRP A 278      -6.313  18.828  -8.058  1.00 36.76      A    C  
ANISOU 2236  CE3 TRP A 278     4277   5018   4671     93      3    525  A    C  
ATOM   2237  NE1 TRP A 278      -4.955  16.413 -10.187  1.00 35.42      A    N  
ANISOU 2237  NE1 TRP A 278     4101   4894   4460    111     -5    522  A    N  
ATOM   2238  CZ2 TRP A 278      -4.655  16.623  -7.745  1.00 33.46      A    C  
ANISOU 2238  CZ2 TRP A 278     3894   4590   4229     93    -23    499  A    C  
ATOM   2239  CZ3 TRP A 278      -5.834  18.480  -6.849  1.00 38.12      A    C  
ANISOU 2239  CZ3 TRP A 278     4475   5167   4839     92    -12    503  A    C  
ATOM   2240  CH2 TRP A 278      -5.017  17.386  -6.695  1.00 35.32      A    C  
ANISOU 2240  CH2 TRP A 278     4138   4807   4475     90    -24    493  A    C  
ATOM   2241  N   HIS A 279      -9.959  20.647 -11.122  1.00 33.48      A    N  
ANISOU 2241  N   HIS A 279     3794   4676   4248     98     58    580  A    N  
ATOM   2242  CA  HIS A 279     -10.569  21.876 -11.549  1.00 35.44      A    C  
ANISOU 2242  CA  HIS A 279     4019   4926   4520    101     63    599  A    C  
ATOM   2243  C   HIS A 279     -10.551  22.970 -10.517  1.00 35.16      A    C  
ANISOU 2243  C   HIS A 279     3987   4858   4515    104     50    588  A    C  
ATOM   2244  O   HIS A 279     -10.739  22.738  -9.364  1.00 35.79      A    O  
ANISOU 2244  O   HIS A 279     4090   4927   4581    105     44    560  A    O  
ATOM   2245  CB  HIS A 279     -11.981  21.634 -12.072  1.00 40.23      A    C  
ANISOU 2245  CB  HIS A 279     4624   5557   5102    100     78    598  A    C  
ATOM   2246  CG  HIS A 279     -12.820  20.769 -11.198  1.00 38.26      A    C  
ANISOU 2246  CG  HIS A 279     4400   5311   4825     91     79    575  A    C  
ATOM   2247  CD2 HIS A 279     -13.825  21.069 -10.358  1.00 40.68      A    C  
ANISOU 2247  CD2 HIS A 279     4712   5620   5123     88     84    564  A    C  
ATOM   2248  ND1 HIS A 279     -12.686  19.410 -11.156  1.00 41.65      A    N  
ANISOU 2248  ND1 HIS A 279     4847   5744   5231     84     73    564  A    N  
ATOM   2249  CE1 HIS A 279     -13.564  18.911 -10.318  1.00 41.35      A    C  
ANISOU 2249  CE1 HIS A 279     4823   5708   5176     72     73    556  A    C  
ATOM   2250  NE2 HIS A 279     -14.262  19.897  -9.805  1.00 37.14      A    N  
ANISOU 2250  NE2 HIS A 279     4283   5179   4649     76     82    555  A    N  
ATOM   2251  N   HIS A 280     -10.284  24.173 -10.977  1.00 35.34      A    N  
ANISOU 2251  N   HIS A 280     3981   4867   4579    108     42    612  A    N  
ATOM   2252  CA  HIS A 280     -10.326  25.385 -10.179  1.00 33.86      A    C  
ANISOU 2252  CA  HIS A 280     3790   4643   4431    116     18    601  A    C  
ATOM   2253  C   HIS A 280     -11.457  26.211 -10.782  1.00 32.59      A    C  
ANISOU 2253  C   HIS A 280     3611   4490   4280    120     24    613  A    C  
ATOM   2254  O   HIS A 280     -11.473  26.399 -12.019  1.00 38.86      A    O  
ANISOU 2254  O   HIS A 280     4380   5304   5081    115     34    650  A    O  
ATOM   2255  CB  HIS A 280      -9.000  26.100 -10.406  1.00 35.03      A    C  
ANISOU 2255  CB  HIS A 280     3916   4762   4632    113     -2    628  A    C  
ATOM   2256  CG  HIS A 280      -8.972  27.556 -10.037  1.00 36.33      A    C  
ANISOU 2256  CG  HIS A 280     4064   4882   4857    120    -37    631  A    C  
ATOM   2257  CD2 HIS A 280      -9.502  28.648 -10.643  1.00 38.62      A    C  
ANISOU 2257  CD2 HIS A 280     4327   5161   5183    122    -47    655  A    C  
ATOM   2258  ND1 HIS A 280      -8.271  28.025  -8.950  1.00 41.86      A    N  
ANISOU 2258  ND1 HIS A 280     4773   5539   5593    127    -73    605  A    N  
ATOM   2259  CE1 HIS A 280      -8.372  29.339  -8.895  1.00 42.08      A    C  
ANISOU 2259  CE1 HIS A 280     4782   5527   5680    135   -107    612  A    C  
ATOM   2260  NE2 HIS A 280      -9.123  29.740  -9.903  1.00 41.42      A    N  
ANISOU 2260  NE2 HIS A 280     4676   5463   5598    130    -92    643  A    N  
ATOM   2261  N   ILE A 281     -12.343  26.744  -9.966  1.00 35.10      A    N  
ANISOU 2261  N   ILE A 281     3939   4799   4599    132     14    582  A    N  
ATOM   2262  CA  ILE A 281     -13.579  27.413 -10.458  1.00 39.74      A    C  
ANISOU 2262  CA  ILE A 281     4512   5398   5188    139     19    586  A    C  
ATOM   2263  C   ILE A 281     -13.723  28.799  -9.838  1.00 38.92      A    C  
ANISOU 2263  C   ILE A 281     4401   5256   5132    158    -15    569  A    C  
ATOM   2264  O   ILE A 281     -13.759  28.964  -8.606  1.00 37.67      A    O  
ANISOU 2264  O   ILE A 281     4259   5084   4970    176    -33    528  A    O  
ATOM   2265  CB  ILE A 281     -14.876  26.609 -10.203  1.00 38.51      A    C  
ANISOU 2265  CB  ILE A 281     4370   5280   4979    140     45    566  A    C  
ATOM   2266  CG1 ILE A 281     -14.815  25.154 -10.666  1.00 42.87      A    C  
ANISOU 2266  CG1 ILE A 281     4935   5862   5489    123     68    576  A    C  
ATOM   2267  CG2 ILE A 281     -16.063  27.226 -10.878  1.00 42.71      A    C  
ANISOU 2267  CG2 ILE A 281     4885   5828   5514    145     52    574  A    C  
ATOM   2268  CD1 ILE A 281     -14.836  24.955 -12.140  1.00 49.65      A    C  
ANISOU 2268  CD1 ILE A 281     5776   6742   6346    116     81    607  A    C  
ATOM   2269  N   GLU A 282     -13.773  29.815 -10.679  1.00 35.83      A    N  
ANISOU 2269  N   GLU A 282     3979   4846   4786    156    -30    600  A    N  
ATOM   2270  CA  GLU A 282     -13.950  31.157 -10.100  1.00 40.92      A    C  
ANISOU 2270  CA  GLU A 282     4616   5446   5483    176    -74    580  A    C  
ATOM   2271  C   GLU A 282     -15.081  31.905 -10.768  1.00 39.28      A    C  
ANISOU 2271  C   GLU A 282     4390   5245   5287    183    -75    589  A    C  
ATOM   2272  O   GLU A 282     -15.241  31.848 -12.010  1.00 43.59      A    O  
ANISOU 2272  O   GLU A 282     4916   5811   5832    167    -54    636  A    O  
ATOM   2273  CB  GLU A 282     -12.649  31.981 -10.138  1.00 41.60      A    C  
ANISOU 2273  CB  GLU A 282     4682   5478   5642    170   -116    606  A    C  
ATOM   2274  CG  GLU A 282     -12.111  32.218 -11.512  1.00 48.04      A    C  
ANISOU 2274  CG  GLU A 282     5464   6298   6489    146   -107    677  A    C  
ATOM   2275  CD  GLU A 282     -10.712  32.840 -11.488  1.00 49.87      A    C  
ANISOU 2275  CD  GLU A 282     5673   6482   6790    135   -145    712  A    C  
ATOM   2276  OE1 GLU A 282      -9.896  32.426 -10.660  1.00 50.74      A    O  
ANISOU 2276  OE1 GLU A 282     5800   6578   6900    137   -155    686  A    O  
ATOM   2277  OE2 GLU A 282     -10.452  33.751 -12.292  1.00 42.59      A    O1-
ANISOU 2277  OE2 GLU A 282     4713   5539   5928    123   -167    767  A    O1-
ATOM   2278  N   SER A 283     -15.882  32.554  -9.929  1.00 42.99      A    N  
ANISOU 2278  N   SER A 283     4867   5705   5761    213    -98    543  A    N  
ATOM   2279  CA  SER A 283     -16.985  33.439 -10.396  1.00 44.32      A    C  
ANISOU 2279  CA  SER A 283     5018   5871   5947    226   -108    543  A    C  
ATOM   2280  C   SER A 283     -16.346  34.791 -10.763  1.00 45.00      A    C  
ANISOU 2280  C   SER A 283     5079   5894   6123    225   -163    569  A    C  
ATOM   2281  O   SER A 283     -15.653  35.347  -9.940  1.00 40.83      A    O  
ANISOU 2281  O   SER A 283     4555   5319   5638    240   -208    545  A    O  
ATOM   2282  CB  SER A 283     -18.008  33.646  -9.272  1.00 41.80      A    C  
ANISOU 2282  CB  SER A 283     4714   5568   5599    264   -117    478  A    C  
ATOM   2283  OG  SER A 283     -18.802  32.473  -9.078  1.00 45.26      A    O  
ANISOU 2283  OG  SER A 283     5166   6068   5960    259    -67    468  A    O  
ATOM   2284  N   LEU A 284     -16.538  35.249 -12.009  1.00 43.77      A    N  
ANISOU 2284  N   LEU A 284     4896   5737   5996    209   -159    625  A    N  
ATOM   2285  CA  LEU A 284     -15.804  36.391 -12.548  1.00 47.33      A    C  
ANISOU 2285  CA  LEU A 284     5313   6132   6534    197   -207    673  A    C  
ATOM   2286  C   LEU A 284     -15.852  37.632 -11.638  1.00 45.86      A    C  
ANISOU 2286  C   LEU A 284     5126   5878   6417    226   -280    629  A    C  
ATOM   2287  O   LEU A 284     -16.875  37.944 -11.038  1.00 45.25      A    O  
ANISOU 2287  O   LEU A 284     5063   5806   6322    260   -292    572  A    O  
ATOM   2288  CB  LEU A 284     -16.338  36.726 -13.932  1.00 47.51      A    C  
ANISOU 2288  CB  LEU A 284     5308   6175   6567    182   -191    732  A    C  
ATOM   2289  CG  LEU A 284     -15.466  36.259 -15.080  1.00 49.92      A    C  
ANISOU 2289  CG  LEU A 284     5590   6509   6867    151   -160    810  A    C  
ATOM   2290  CD1 LEU A 284     -15.210  34.767 -14.993  1.00 48.68      A    C  
ANISOU 2290  CD1 LEU A 284     5458   6407   6631    144   -106    793  A    C  
ATOM   2291  CD2 LEU A 284     -16.124  36.646 -16.418  1.00 51.35      A    C  
ANISOU 2291  CD2 LEU A 284     5742   6717   7051    143   -146    865  A    C  
ATOM   2292  N   LEU A 285     -14.711  38.270 -11.453  1.00 44.92      A    N  
ANISOU 2292  N   LEU A 285     4992   5700   6372    218   -330    652  A    N  
ATOM   2293  CA  LEU A 285     -14.663  39.545 -10.704  1.00 51.26      A    C  
ANISOU 2293  CA  LEU A 285     5791   6427   7257    246   -414    613  A    C  
ATOM   2294  C   LEU A 285     -15.629  40.550 -11.310  1.00 49.55      A    C  
ANISOU 2294  C   LEU A 285     5553   6190   7081    256   -443    624  A    C  
ATOM   2295  O   LEU A 285     -15.757  40.653 -12.522  1.00 52.17      A    O  
ANISOU 2295  O   LEU A 285     5858   6537   7424    227   -421    697  A    O  
ATOM   2296  CB  LEU A 285     -13.285  40.153 -10.750  1.00 53.97      A    C  
ANISOU 2296  CB  LEU A 285     6109   6703   7692    224   -468    659  A    C  
ATOM   2297  CG  LEU A 285     -12.128  39.257 -10.344  1.00 55.91      A    C  
ANISOU 2297  CG  LEU A 285     6367   6962   7913    208   -445    663  A    C  
ATOM   2298  CD1 LEU A 285     -10.805  39.795 -10.885  1.00 55.35      A    C  
ANISOU 2298  CD1 LEU A 285     6256   6841   7933    173   -481    743  A    C  
ATOM   2299  CD2 LEU A 285     -12.074  39.109  -8.841  1.00 55.81      A    C  
ANISOU 2299  CD2 LEU A 285     6391   6932   7880    247   -472    572  A    C  
ATOM   2300  N   ASN A 286     -16.365  41.224 -10.442  1.00 58.08      A    N  
ANISOU 2300  N   ASN A 286     6647   7244   8175    302   -491    550  A    N  
ATOM   2301  CA  ASN A 286     -17.383  42.208 -10.791  1.00 59.52      A    C  
ANISOU 2301  CA  ASN A 286     6815   7406   8394    322   -527    540  A    C  
ATOM   2302  C   ASN A 286     -18.393  41.682 -11.757  1.00 61.66      A    C  
ANISOU 2302  C   ASN A 286     7082   7744   8602    308   -459    572  A    C  
ATOM   2303  O   ASN A 286     -18.909  42.434 -12.598  1.00 55.40      A    O  
ANISOU 2303  O   ASN A 286     6264   6931   7851    301   -479    609  A    O  
ATOM   2304  CB  ASN A 286     -16.758  43.491 -11.353  1.00 66.21      A    C  
ANISOU 2304  CB  ASN A 286     7625   8165   9366    305   -606    598  A    C  
ATOM   2305  CG  ASN A 286     -15.878  44.170 -10.347  1.00 75.64      A    C  
ANISOU 2305  CG  ASN A 286     8822   9279  10636    326   -691    557  A    C  
ATOM   2306  ND2 ASN A 286     -14.568  44.230 -10.621  1.00 75.68      A    N  
ANISOU 2306  ND2 ASN A 286     8805   9244  10703    287   -710    623  A    N  
ATOM   2307  OD1 ASN A 286     -16.360  44.592  -9.298  1.00 88.81      A    O  
ANISOU 2307  OD1 ASN A 286    10511  10927  12305    380   -738    465  A    O  
ATOM   2308  N   GLY A 287     -18.705  40.399 -11.637  1.00 52.03      A    N  
ANISOU 2308  N   GLY A 287     5884   6599   7283    302   -383    557  A    N  
ATOM   2309  CA  GLY A 287     -19.614  39.795 -12.559  1.00 46.77      A    C  
ANISOU 2309  CA  GLY A 287     5214   5996   6558    288   -321    585  A    C  
ATOM   2310  C   GLY A 287     -21.008  39.635 -11.968  1.00 49.56      A    C  
ANISOU 2310  C   GLY A 287     5583   6391   6852    325   -304    517  A    C  
ATOM   2311  O   GLY A 287     -21.878  39.109 -12.630  1.00 44.24      A    O  
ANISOU 2311  O   GLY A 287     4908   5770   6128    315   -256    533  A    O  
ATOM   2312  N   GLY A 288     -21.206  40.018 -10.709  1.00 48.63      A    N  
ANISOU 2312  N   GLY A 288     5482   6260   6736    371   -342    441  A    N  
ATOM   2313  CA  GLY A 288     -22.450  39.712 -10.018  1.00 55.05      A    C  
ANISOU 2313  CA  GLY A 288     6307   7129   7478    409   -317    378  A    C  
ATOM   2314  C   GLY A 288     -22.512  38.264  -9.617  1.00 54.83      A    C  
ANISOU 2314  C   GLY A 288     6299   7172   7360    397   -248    374  A    C  
ATOM   2315  O   GLY A 288     -21.551  37.517  -9.773  1.00 46.93      A    O  
ANISOU 2315  O   GLY A 288     5307   6170   6351    362   -224    408  A    O  
ATOM   2316  N   ILE A 289     -23.670  37.844  -9.156  1.00 51.29      A    N  
ANISOU 2316  N   ILE A 289     5854   6786   6846    421   -215    336  A    N  
ATOM   2317  CA  ILE A 289     -23.807  36.488  -8.645  1.00 51.35      A    C  
ANISOU 2317  CA  ILE A 289     5878   6859   6771    411   -156    333  A    C  
ATOM   2318  C   ILE A 289     -23.888  35.456  -9.750  1.00 47.58      A    C  
ANISOU 2318  C   ILE A 289     5399   6412   6267    359   -100    394  A    C  
ATOM   2319  O   ILE A 289     -24.283  35.749 -10.925  1.00 43.45      A    O  
ANISOU 2319  O   ILE A 289     4858   5881   5767    340    -95    431  A    O  
ATOM   2320  CB  ILE A 289     -25.006  36.310  -7.690  1.00 52.42      A    C  
ANISOU 2320  CB  ILE A 289     6014   7060   6843    455   -139    280  A    C  
ATOM   2321  CG1 ILE A 289     -26.300  36.276  -8.445  1.00 59.88      A    C  
ANISOU 2321  CG1 ILE A 289     6939   8042   7768    450   -110    296  A    C  
ATOM   2322  CG2 ILE A 289     -24.965  37.399  -6.599  1.00 54.16      A    C  
ANISOU 2322  CG2 ILE A 289     6236   7256   7086    519   -201    209  A    C  
ATOM   2323  CD1 ILE A 289     -27.393  35.703  -7.570  1.00 68.70      A    C  
ANISOU 2323  CD1 ILE A 289     8051   9240   8809    479    -75    262  A    C  
ATOM   2324  N   THR A 290     -23.530  34.235  -9.354  1.00 43.93      A    N  
ANISOU 2324  N   THR A 290     4953   5984   5754    340    -61    400  A    N  
ATOM   2325  CA  THR A 290     -23.500  33.130 -10.273  1.00 41.94      A    C  
ANISOU 2325  CA  THR A 290     4702   5758   5473    296    -16    448  A    C  
ATOM   2326  C   THR A 290     -24.359  32.037  -9.739  1.00 37.38      A    C  
ANISOU 2326  C   THR A 290     4130   5244   4827    296     25    437  A    C  
ATOM   2327  O   THR A 290     -24.402  31.862  -8.557  1.00 40.00      A    O  
ANISOU 2327  O   THR A 290     4471   5597   5129    319     24    403  A    O  
ATOM   2328  CB  THR A 290     -22.069  32.573 -10.434  1.00 43.26      A    C  
ANISOU 2328  CB  THR A 290     4883   5900   5654    267    -15    476  A    C  
ATOM   2329  CG2 THR A 290     -21.204  33.622 -11.008  1.00 48.42      A    C  
ANISOU 2329  CG2 THR A 290     5522   6494   6378    264    -55    500  A    C  
ATOM   2330  OG1 THR A 290     -21.497  32.232  -9.158  1.00 40.70      A    O  
ANISOU 2330  OG1 THR A 290     4577   5575   5308    283    -21    442  A    O  
ATOM   2331  N   ILE A 291     -24.923  31.253 -10.640  1.00 37.87      A    N  
ANISOU 2331  N   ILE A 291     4185   5334   4867    267     58    470  A    N  
ATOM   2332  CA  ILE A 291     -25.671  30.118 -10.310  1.00 40.70      A    C  
ANISOU 2332  CA  ILE A 291     4546   5746   5172    256     93    472  A    C  
ATOM   2333  C   ILE A 291     -25.282  29.032 -11.247  1.00 37.21      A    C  
ANISOU 2333  C   ILE A 291     4110   5305   4723    217    114    512  A    C  
ATOM   2334  O   ILE A 291     -25.199  29.227 -12.496  1.00 40.28      A    O  
ANISOU 2334  O   ILE A 291     4490   5678   5135    204    112    538  A    O  
ATOM   2335  CB  ILE A 291     -27.194  30.399 -10.493  1.00 39.79      A    C  
ANISOU 2335  CB  ILE A 291     4408   5668   5042    271    105    465  A    C  
ATOM   2336  CG1 ILE A 291     -27.601  31.579  -9.619  1.00 40.90      A    C  
ANISOU 2336  CG1 ILE A 291     4540   5809   5191    320     78    419  A    C  
ATOM   2337  CG2 ILE A 291     -27.975  29.171 -10.177  1.00 38.41      A    C  
ANISOU 2337  CG2 ILE A 291     4228   5547   4818    254    139    477  A    C  
ATOM   2338  CD1 ILE A 291     -29.103  31.879  -9.633  1.00 40.32      A    C  
ANISOU 2338  CD1 ILE A 291     4441   5780   5096    342     90    406  A    C  
ATOM   2339  N   THR A 292     -25.119  27.863 -10.660  1.00 37.22      A    N  
ANISOU 2339  N   THR A 292     4124   5328   4689    201    132    514  A    N  
ATOM   2340  CA  THR A 292     -24.761  26.686 -11.419  1.00 36.13      A    C  
ANISOU 2340  CA  THR A 292     3993   5191   4540    168    145    543  A    C  
ATOM   2341  C   THR A 292     -25.455  25.553 -10.794  1.00 34.53      A    C  
ANISOU 2341  C   THR A 292     3791   5027   4301    154    163    548  A    C  
ATOM   2342  O   THR A 292     -25.659  25.526  -9.598  1.00 40.70      A    O  
ANISOU 2342  O   THR A 292     4573   5830   5060    167    168    532  A    O  
ATOM   2343  CB  THR A 292     -23.195  26.424 -11.295  1.00 37.75      A    C  
ANISOU 2343  CB  THR A 292     4219   5363   4759    158    133    547  A    C  
ATOM   2344  CG2 THR A 292     -22.796  25.320 -12.237  1.00 40.36      A    C  
ANISOU 2344  CG2 THR A 292     4556   5696   5082    133    141    571  A    C  
ATOM   2345  OG1 THR A 292     -22.490  27.655 -11.601  1.00 33.63      A    O  
ANISOU 2345  OG1 THR A 292     3693   4804   4280    173    111    545  A    O  
ATOM   2346  N   VAL A 293     -25.818  24.576 -11.588  1.00 36.06      A    N  
ANISOU 2346  N   VAL A 293     3981   5229   4487    129    171    570  A    N  
ATOM   2347  CA  VAL A 293     -26.218  23.293 -11.039  1.00 36.99      A    C  
ANISOU 2347  CA  VAL A 293     4102   5371   4581    107    181    584  A    C  
ATOM   2348  C   VAL A 293     -25.405  22.200 -11.706  1.00 36.66      A    C  
ANISOU 2348  C   VAL A 293     4076   5306   4544     83    171    597  A    C  
ATOM   2349  O   VAL A 293     -25.319  22.173 -12.976  1.00 34.87      A    O  
ANISOU 2349  O   VAL A 293     3849   5069   4332     81    164    602  A    O  
ATOM   2350  CB  VAL A 293     -27.706  22.963 -11.347  1.00 40.69      A    C  
ANISOU 2350  CB  VAL A 293     4544   5873   5042     98    191    598  A    C  
ATOM   2351  CG1 VAL A 293     -28.010  21.604 -10.888  1.00 38.53      A    C  
ANISOU 2351  CG1 VAL A 293     4268   5616   4753     70    194    622  A    C  
ATOM   2352  CG2 VAL A 293     -28.647  23.912 -10.641  1.00 45.02      A    C  
ANISOU 2352  CG2 VAL A 293     5071   6454   5578    125    202    584  A    C  
ATOM   2353  N   ASN A 294     -24.883  21.271 -10.902  1.00 34.11      A    N  
ANISOU 2353  N   ASN A 294     3768   4982   4208     68    168    601  A    N  
ATOM   2354  CA  ASN A 294     -24.020  20.206 -11.422  1.00 33.36      A    C  
ANISOU 2354  CA  ASN A 294     3691   4863   4119     50    153    608  A    C  
ATOM   2355  C   ASN A 294     -24.758  18.929 -11.426  1.00 36.38      A    C  
ANISOU 2355  C   ASN A 294     4067   5256   4498     24    145    627  A    C  
ATOM   2356  O   ASN A 294     -25.884  18.888 -10.958  1.00 34.57      A    O  
ANISOU 2356  O   ASN A 294     3818   5056   4260     18    156    641  A    O  
ATOM   2357  CB  ASN A 294     -22.688  20.181 -10.680  1.00 35.11      A    C  
ANISOU 2357  CB  ASN A 294     3935   5065   4338     54    147    597  A    C  
ATOM   2358  CG  ASN A 294     -22.740  19.433  -9.388  1.00 39.85      A    C  
ANISOU 2358  CG  ASN A 294     4542   5679   4919     43    149    604  A    C  
ATOM   2359  ND2 ASN A 294     -21.631  19.511  -8.628  1.00 39.81      A    N  
ANISOU 2359  ND2 ASN A 294     4557   5658   4911     51    144    592  A    N  
ATOM   2360  OD1 ASN A 294     -23.745  18.817  -9.042  1.00 40.87      A    O  
ANISOU 2360  OD1 ASN A 294     4657   5834   5037     28    154    624  A    O  
ATOM   2361  N   PHE A 295     -24.202  17.920 -12.061  1.00 36.36      A    N  
ANISOU 2361  N   PHE A 295     4079   5232   4504     12    124    628  A    N  
ATOM   2362  CA  PHE A 295     -24.868  16.593 -12.239  1.00 37.25      A    C  
ANISOU 2362  CA  PHE A 295     4186   5342   4625    -13    102    647  A    C  
ATOM   2363  C   PHE A 295     -23.762  15.577 -12.028  1.00 41.24      A    C  
ANISOU 2363  C   PHE A 295     4715   5819   5134    -24     79    642  A    C  
ATOM   2364  O   PHE A 295     -22.842  15.474 -12.889  1.00 37.59      A    O  
ANISOU 2364  O   PHE A 295     4268   5338   4675     -9     64    623  A    O  
ATOM   2365  CB  PHE A 295     -25.407  16.388 -13.666  1.00 41.00      A    C  
ANISOU 2365  CB  PHE A 295     4651   5811   5114    -10     85    642  A    C  
ATOM   2366  CG  PHE A 295     -26.631  17.217 -14.022  1.00 39.42      A    C  
ANISOU 2366  CG  PHE A 295     4426   5636   4914     -4    103    647  A    C  
ATOM   2367  CD1 PHE A 295     -26.554  18.596 -14.091  1.00 41.00      A    C  
ANISOU 2367  CD1 PHE A 295     4621   5848   5107     20    126    636  A    C  
ATOM   2368  CD2 PHE A 295     -27.847  16.605 -14.349  1.00 44.97      A    C  
ANISOU 2368  CD2 PHE A 295     5108   6347   5631    -20     88    663  A    C  
ATOM   2369  CE1 PHE A 295     -27.637  19.361 -14.484  1.00 45.62      A    C  
ANISOU 2369  CE1 PHE A 295     5184   6454   5695     29    138    638  A    C  
ATOM   2370  CE2 PHE A 295     -28.949  17.368 -14.758  1.00 40.66      A    C  
ANISOU 2370  CE2 PHE A 295     4537   5823   5085    -12    104    666  A    C  
ATOM   2371  CZ  PHE A 295     -28.849  18.750 -14.779  1.00 43.92      A    C  
ANISOU 2371  CZ  PHE A 295     4948   6250   5487     13    129    653  A    C  
ATOM   2372  N   TRP A 296     -23.802  14.863 -10.894  1.00 39.26      A    N  
ANISOU 2372  N   TRP A 296     4466   5570   4879    -45     74    663  A    N  
ATOM   2373  CA  TRP A 296     -22.714  13.976 -10.509  1.00 38.10      A    C  
ANISOU 2373  CA  TRP A 296     4344   5396   4736    -54     52    660  A    C  
ATOM   2374  C   TRP A 296     -23.126  12.506 -10.661  1.00 43.75      A    C  
ANISOU 2374  C   TRP A 296     5057   6090   5475    -83     12    680  A    C  
ATOM   2375  O   TRP A 296     -24.070  12.071 -10.023  1.00 46.67      A    O  
ANISOU 2375  O   TRP A 296     5406   6475   5849   -109     11    716  A    O  
ATOM   2376  CB  TRP A 296     -22.277  14.251  -9.084  1.00 37.72      A    C  
ANISOU 2376  CB  TRP A 296     4302   5361   4666    -54     71    668  A    C  
ATOM   2377  CG  TRP A 296     -21.182  15.242  -8.873  1.00 41.20      A    C  
ANISOU 2377  CG  TRP A 296     4760   5796   5098    -27     86    640  A    C  
ATOM   2378  CD1 TRP A 296     -20.014  15.388  -9.619  1.00 42.09      A    C  
ANISOU 2378  CD1 TRP A 296     4890   5882   5219    -12     76    615  A    C  
ATOM   2379  CD2 TRP A 296     -21.037  16.121  -7.778  1.00 38.48      A    C  
ANISOU 2379  CD2 TRP A 296     4416   5472   4733    -11    109    634  A    C  
ATOM   2380  CE2 TRP A 296     -19.798  16.818  -7.946  1.00 38.89      A    C  
ANISOU 2380  CE2 TRP A 296     4485   5499   4790      9    106    607  A    C  
ATOM   2381  CE3 TRP A 296     -21.840  16.438  -6.682  1.00 41.82      A    C  
ANISOU 2381  CE3 TRP A 296     4822   5932   5132     -8    128    648  A    C  
ATOM   2382  NE1 TRP A 296     -19.218  16.366  -9.080  1.00 37.42      A    N  
ANISOU 2382  NE1 TRP A 296     4307   5289   4622      6     89    600  A    N  
ATOM   2383  CZ2 TRP A 296     -19.370  17.816  -7.077  1.00 41.26      A    C  
ANISOU 2383  CZ2 TRP A 296     4790   5805   5082     32    118    590  A    C  
ATOM   2384  CZ3 TRP A 296     -21.393  17.438  -5.776  1.00 41.94      A    C  
ANISOU 2384  CZ3 TRP A 296     4844   5960   5128     21    141    626  A    C  
ATOM   2385  CH2 TRP A 296     -20.137  18.083  -5.979  1.00 41.52      A    C  
ANISOU 2385  CH2 TRP A 296     4811   5873   5089     39    132    596  A    C  
ATOM   2386  N   TYR A 297     -22.450  11.802 -11.572  1.00 38.91      A    N  
ANISOU 2386  N   TYR A 297     4459   5445   4877    -76    -23    656  A    N  
ATOM   2387  CA  TYR A 297     -22.613  10.384 -11.842  1.00 38.51      A    C  
ANISOU 2387  CA  TYR A 297     4412   5362   4857    -96    -75    664  A    C  
ATOM   2388  C   TYR A 297     -21.429   9.569 -11.332  1.00 44.78      A    C  
ANISOU 2388  C   TYR A 297     5232   6127   5654    -99   -101    655  A    C  
ATOM   2389  O   TYR A 297     -20.264   9.964 -11.510  1.00 41.06      A    O  
ANISOU 2389  O   TYR A 297     4781   5652   5167    -74    -92    625  A    O  
ATOM   2390  CB  TYR A 297     -22.734  10.127 -13.340  1.00 36.41      A    C  
ANISOU 2390  CB  TYR A 297     4146   5083   4602    -74   -106    632  A    C  
ATOM   2391  CG  TYR A 297     -24.012  10.749 -13.959  1.00 39.07      A    C  
ANISOU 2391  CG  TYR A 297     4458   5445   4943    -73    -90    640  A    C  
ATOM   2392  CD1 TYR A 297     -24.061  12.104 -14.286  1.00 41.35      A    C  
ANISOU 2392  CD1 TYR A 297     4739   5764   5206    -49    -46    631  A    C  
ATOM   2393  CD2 TYR A 297     -25.171   9.998 -14.154  1.00 39.67      A    C  
ANISOU 2393  CD2 TYR A 297     4512   5508   5050    -97   -124    662  A    C  
ATOM   2394  CE1 TYR A 297     -25.225  12.690 -14.743  1.00 42.68      A    C  
ANISOU 2394  CE1 TYR A 297     4884   5955   5377    -48    -31    639  A    C  
ATOM   2395  CE2 TYR A 297     -26.354  10.573 -14.632  1.00 42.47      A    C  
ANISOU 2395  CE2 TYR A 297     4841   5887   5406    -98   -108    672  A    C  
ATOM   2396  CZ  TYR A 297     -26.358  11.930 -14.948  1.00 44.85      A    C  
ANISOU 2396  CZ  TYR A 297     5139   6221   5678    -71    -61    658  A    C  
ATOM   2397  OH  TYR A 297     -27.484  12.581 -15.433  1.00 38.60      A    O  
ANISOU 2397  OH  TYR A 297     4324   5454   4888    -67    -45    664  A    O  
ATOM   2398  N   LYS A 298     -21.725   8.435 -10.708  1.00 44.72      A    N  
ANISOU 2398  N   LYS A 298     5221   6096   5671   -132   -137    686  A    N  
ATOM   2399  CA  LYS A 298     -20.707   7.446 -10.451  1.00 43.13      A    C  
ANISOU 2399  CA  LYS A 298     5044   5856   5484   -136   -178    675  A    C  
ATOM   2400  C   LYS A 298     -20.112   7.076 -11.771  1.00 39.66      A    C  
ANISOU 2400  C   LYS A 298     4620   5394   5055   -104   -216    625  A    C  
ATOM   2401  O   LYS A 298     -20.814   6.938 -12.754  1.00 40.74      A    O  
ANISOU 2401  O   LYS A 298     4745   5528   5207    -96   -237    613  A    O  
ATOM   2402  CB  LYS A 298     -21.330   6.185  -9.832  1.00 50.19      A    C  
ANISOU 2402  CB  LYS A 298     5927   6724   6417   -179   -223    722  A    C  
ATOM   2403  CG  LYS A 298     -21.747   6.275  -8.380  1.00 57.53      A    C  
ANISOU 2403  CG  LYS A 298     6841   7681   7335   -210   -192    780  A    C  
ATOM   2404  CD  LYS A 298     -21.587   4.872  -7.764  1.00 67.00      A    C  
ANISOU 2404  CD  LYS A 298     8044   8840   8572   -245   -248    817  A    C  
ATOM   2405  CE  LYS A 298     -22.374   4.620  -6.479  1.00 73.45      A    C  
ANISOU 2405  CE  LYS A 298     8830   9687   9387   -286   -232    895  A    C  
ATOM   2406  NZ  LYS A 298     -22.400   5.841  -5.654  1.00 69.57      A    N1+
ANISOU 2406  NZ  LYS A 298     8334   9260   8837   -267   -159    899  A    N1+
ATOM   2407  N   GLY A 299     -18.818   6.834 -11.811  1.00 40.89      A    N  
ANISOU 2407  N   GLY A 299     4801   5534   5202    -83   -229    594  A    N  
ATOM   2408  CA  GLY A 299     -18.187   6.333 -13.027  1.00 43.95      A    C  
ANISOU 2408  CA  GLY A 299     5199   5904   5593    -47   -271    545  A    C  
ATOM   2409  C   GLY A 299     -18.494   4.856 -13.333  1.00 44.89      A    C  
ANISOU 2409  C   GLY A 299     5321   5976   5757    -56   -351    537  A    C  
ATOM   2410  O   GLY A 299     -19.078   4.180 -12.558  1.00 43.90      A    O  
ANISOU 2410  O   GLY A 299     5190   5825   5664    -98   -375    577  A    O  
ATOM   2411  N   ALA A 300     -18.087   4.419 -14.507  1.00 49.41      A    N  
ANISOU 2411  N   ALA A 300     5901   6539   6330    -16   -394    485  A    N  
ATOM   2412  CA  ALA A 300     -18.215   3.035 -14.988  1.00 53.77      A    C  
ANISOU 2412  CA  ALA A 300     6461   7042   6927    -11   -482    462  A    C  
ATOM   2413  C   ALA A 300     -17.543   2.085 -14.036  1.00 55.69      A    C  
ANISOU 2413  C   ALA A 300     6721   7241   7198    -35   -522    473  A    C  
ATOM   2414  O   ALA A 300     -16.578   2.475 -13.376  1.00 54.81      A    O  
ANISOU 2414  O   ALA A 300     6624   7143   7058    -32   -484    475  A    O  
ATOM   2415  CB  ALA A 300     -17.544   2.937 -16.355  1.00 51.39      A    C  
ANISOU 2415  CB  ALA A 300     6168   6756   6602     54   -509    393  A    C  
ATOM   2416  N   PRO A 301     -18.009   0.821 -13.972  1.00 66.85      A    N  
ANISOU 2416  N   PRO A 301     8134   8597   8669    -57   -603    481  A    N  
ATOM   2417  CA  PRO A 301     -17.234  -0.160 -13.156  1.00 63.96      A    C  
ANISOU 2417  CA  PRO A 301     7787   8184   8331    -74   -650    488  A    C  
ATOM   2418  C   PRO A 301     -15.858  -0.356 -13.790  1.00 61.65      A    C  
ANISOU 2418  C   PRO A 301     7520   7893   8012    -16   -671    416  A    C  
ATOM   2419  O   PRO A 301     -15.684  -0.166 -14.997  1.00 64.48      A    O  
ANISOU 2419  O   PRO A 301     7877   8274   8348     37   -680    361  A    O  
ATOM   2420  CB  PRO A 301     -18.085  -1.423 -13.189  1.00 60.23      A    C  
ANISOU 2420  CB  PRO A 301     7304   7646   7934   -106   -742    508  A    C  
ATOM   2421  CG  PRO A 301     -18.997  -1.247 -14.368  1.00 65.95      A    C  
ANISOU 2421  CG  PRO A 301     8012   8380   8666    -83   -759    482  A    C  
ATOM   2422  CD  PRO A 301     -18.928   0.160 -14.907  1.00 63.37      A    C  
ANISOU 2422  CD  PRO A 301     7681   8127   8270    -50   -671    463  A    C  
ATOM   2423  N   THR A 302     -14.852  -0.614 -12.986  1.00 71.72      A    N  
ANISOU 2423  N   THR A 302     8813   9154   9282    -21   -670    419  A    N  
ATOM   2424  CA  THR A 302     -13.517  -0.866 -13.554  1.00 82.20      A    C  
ANISOU 2424  CA  THR A 302    10161  10483  10587     35   -694    353  A    C  
ATOM   2425  C   THR A 302     -13.541  -2.226 -14.253  1.00 80.10      A    C  
ANISOU 2425  C   THR A 302     9903  10162  10369     61   -804    306  A    C  
ATOM   2426  O   THR A 302     -14.295  -3.115 -13.817  1.00 80.14      A    O  
ANISOU 2426  O   THR A 302     9903  10108  10436     17   -866    339  A    O  
ATOM   2427  CB  THR A 302     -12.450  -0.939 -12.456  1.00 84.50      A    C  
ANISOU 2427  CB  THR A 302    10470  10765  10869     20   -676    367  A    C  
ATOM   2428  CG2 THR A 302     -12.383   0.343 -11.669  1.00 89.15      A    C  
ANISOU 2428  CG2 THR A 302    11053  11401  11417     -1   -580    409  A    C  
ATOM   2429  OG1 THR A 302     -12.808  -1.993 -11.569  1.00 86.15      A    O  
ANISOU 2429  OG1 THR A 302    10684  10914  11135    -27   -735    407  A    O  
ATOM   2430  N   PRO A 303     -12.719  -2.406 -15.307  1.00 82.74      A    N  
ANISOU 2430  N   PRO A 303    10246  10514  10677    132   -832    230  A    N  
ATOM   2431  CA  PRO A 303     -12.642  -3.743 -15.906  1.00 92.44      A    C  
ANISOU 2431  CA  PRO A 303    11484  11685  11951    164   -947    175  A    C  
ATOM   2432  C   PRO A 303     -12.369  -4.829 -14.842  1.00 94.85      A    C  
ANISOU 2432  C   PRO A 303    11806  11915  12317    121  -1011    201  A    C  
ATOM   2433  O   PRO A 303     -11.600  -4.587 -13.903  1.00 98.18      A    O  
ANISOU 2433  O   PRO A 303    12238  12344  12721    100   -969    228  A    O  
ATOM   2434  CB  PRO A 303     -11.483  -3.613 -16.917  1.00 94.67      A    C  
ANISOU 2434  CB  PRO A 303    11773  12018  12178    251   -947     94  A    C  
ATOM   2435  CG  PRO A 303     -11.424  -2.153 -17.253  1.00 92.59      A    C  
ANISOU 2435  CG  PRO A 303    11494  11839  11847    263   -839    112  A    C  
ATOM   2436  CD  PRO A 303     -11.814  -1.447 -15.975  1.00 88.68      A    C  
ANISOU 2436  CD  PRO A 303    10995  11339  11358    188   -768    194  A    C  
ATOM   2437  N   LYS A 304     -13.028  -5.990 -14.954  1.00114.69      A    N  
ANISOU 2437  N   LYS A 304    14318  14354  14905    105  -1115    198  A    N  
ATOM   2438  CA  LYS A 304     -12.794  -7.104 -14.008  1.00113.97      A    C  
ANISOU 2438  CA  LYS A 304    14239  14184  14879     63  -1189    227  A    C  
ATOM   2439  C   LYS A 304     -11.327  -7.507 -14.105  1.00114.03      A    C  
ANISOU 2439  C   LYS A 304    14273  14189  14864    119  -1217    161  A    C  
ATOM   2440  O   LYS A 304     -10.755  -7.983 -13.128  1.00 94.18      A    O  
ANISOU 2440  O   LYS A 304    11772  11639  12374     87  -1234    189  A    O  
ATOM   2441  CB  LYS A 304     -13.729  -8.312 -14.241  1.00115.63      A    C  
ANISOU 2441  CB  LYS A 304    14440  14308  15184     41  -1310    232  A    C  
ATOM   2442  CG  LYS A 304     -14.986  -8.333 -13.362  1.00118.09      A    C  
ANISOU 2442  CG  LYS A 304    14726  14595  15547    -48  -1298    339  A    C  
ATOM   2443  CD  LYS A 304     -15.302  -9.734 -12.837  1.00121.05      A    C  
ANISOU 2443  CD  LYS A 304    15099  14868  16026    -94  -1417    375  A    C  
ATOM   2444  CE  LYS A 304     -16.733  -9.869 -12.340  1.00117.47      A    C  
ANISOU 2444  CE  LYS A 304    14609  14390  15633   -172  -1425    473  A    C  
ATOM   2445  NZ  LYS A 304     -17.655 -10.137 -13.478  1.00116.98      A    N1+
ANISOU 2445  NZ  LYS A 304    14531  14302  15613   -150  -1491    435  A    N1+
ATOM   2446  N   ARG A 305     -10.726  -7.288 -15.283  1.00126.01      A    N  
ANISOU 2446  N   ARG A 305    15793  15753  16332    202  -1219     76  A    N  
ATOM   2447  CA  ARG A 305      -9.267  -7.227 -15.382  1.00123.80      A    C  
ANISOU 2447  CA  ARG A 305    15528  15505  16003    258  -1205     23  A    C  
ATOM   2448  C   ARG A 305      -8.622  -6.056 -16.187  1.00117.38      A    C  
ANISOU 2448  C   ARG A 305    14705  14796  15098    318  -1114    -13  A    C  
ATOM   2449  O   ARG A 305      -9.085  -5.591 -17.252  1.00112.64      A    O  
ANISOU 2449  O   ARG A 305    14089  14244  14465    359  -1096    -40  A    O  
ATOM   2450  CB  ARG A 305      -8.703  -8.590 -15.770  1.00128.45      A    C  
ANISOU 2450  CB  ARG A 305    16134  16032  16637    307  -1331    -50  A    C  
ATOM   2451  CG  ARG A 305      -8.841  -9.591 -14.626  1.00129.78      A    C  
ANISOU 2451  CG  ARG A 305    16315  16104  16888    240  -1402     -1  A    C  
ATOM   2452  CD  ARG A 305      -7.815 -10.697 -14.669  1.00127.82      A    C  
ANISOU 2452  CD  ARG A 305    16090  15806  16670    286  -1500    -66  A    C  
ATOM   2453  NE  ARG A 305      -7.644 -11.193 -16.024  1.00133.53      A    N  
ANISOU 2453  NE  ARG A 305    16814  16537  17385    378  -1578   -171  A    N  
ATOM   2454  CZ  ARG A 305      -6.799 -12.157 -16.355  1.00128.76      A    C  
ANISOU 2454  CZ  ARG A 305    16226  15896  16799    440  -1675   -251  A    C  
ATOM   2455  NH1 ARG A 305      -6.059 -12.752 -15.428  1.00121.77      A    N1+
ANISOU 2455  NH1 ARG A 305    15359  14959  15947    416  -1709   -235  A    N1+
ATOM   2456  NH2 ARG A 305      -6.711 -12.537 -17.621  1.00134.17      A    N  
ANISOU 2456  NH2 ARG A 305    16909  16599  17469    533  -1743   -349  A    N  
ATOM   2457  N   ILE A 306      -7.500  -5.646 -15.606  1.00107.50      A    N  
ANISOU 2457  N   ILE A 306    13460  13572  13810    321  -1060     -6  A    N  
ATOM   2458  CA  ILE A 306      -6.756  -4.442 -15.901  1.00 97.24      A    C  
ANISOU 2458  CA  ILE A 306    12149  12361  12436    352   -961     -7  A    C  
ATOM   2459  C   ILE A 306      -5.823  -4.617 -17.068  1.00 91.72      A    C  
ANISOU 2459  C   ILE A 306    11444  11714  11690    447   -986    -90  A    C  
ATOM   2460  O   ILE A 306      -5.061  -5.575 -17.118  1.00 92.45      A    O  
ANISOU 2460  O   ILE A 306    11551  11777  11798    486  -1058   -142  A    O  
ATOM   2461  CB  ILE A 306      -5.881  -4.094 -14.651  1.00 99.79      A    C  
ANISOU 2461  CB  ILE A 306    12484  12680  12752    313   -910     33  A    C  
ATOM   2462  CG1 ILE A 306      -6.761  -3.935 -13.395  1.00106.44      A    C  
ANISOU 2462  CG1 ILE A 306    13321  13517  13603    233   -841    119  A    C  
ATOM   2463  CG2 ILE A 306      -4.935  -2.912 -14.889  1.00 92.78      A    C  
ANISOU 2463  CG2 ILE A 306    11588  11861  11803    368   -857      2  A    C  
ATOM   2464  CD1 ILE A 306      -7.851  -2.855 -13.463  1.00106.63      A    C  
ANISOU 2464  CD1 ILE A 306    13324  13578  13613    221   -793    145  A    C  
ATOM   2465  N   GLU A 307      -5.796  -3.631 -17.946  1.00 81.04      A    N  
ANISOU 2465  N   GLU A 307    10068  10446  10276    486   -919    -95  A    N  
ATOM   2466  CA  GLU A 307      -4.913  -3.660 -19.083  1.00 80.65      A    C  
ANISOU 2466  CA  GLU A 307    10004  10467  10170    581   -927   -163  A    C  
ATOM   2467  C   GLU A 307      -3.775  -2.659 -18.941  1.00 75.71      A    C  
ANISOU 2467  C   GLU A 307     9362   9914   9489    593   -837   -140  A    C  
ATOM   2468  O   GLU A 307      -3.913  -1.595 -18.351  1.00 85.51      A    O  
ANISOU 2468  O   GLU A 307    10595  11172  10722    540   -754    -74  A    O  
ATOM   2469  CB  GLU A 307      -5.751  -3.384 -20.312  1.00 99.77      A    C  
ANISOU 2469  CB  GLU A 307    12407  12934  12563    622   -929   -186  A    C  
ATOM   2470  CG  GLU A 307      -7.054  -4.188 -20.229  1.00114.73      A    C  
ANISOU 2470  CG  GLU A 307    14316  14747  14527    587  -1008   -187  A    C  
ATOM   2471  CD  GLU A 307      -7.972  -4.011 -21.419  1.00122.37      A    C  
ANISOU 2471  CD  GLU A 307    15266  15750  15475    627  -1022   -213  A    C  
ATOM   2472  OE1 GLU A 307      -7.863  -2.994 -22.133  1.00128.88      A    O  
ANISOU 2472  OE1 GLU A 307    16069  16665  16235    660   -947   -205  A    O  
ATOM   2473  OE2 GLU A 307      -8.823  -4.893 -21.625  1.00119.26      A    O1-
ANISOU 2473  OE2 GLU A 307    14882  15293  15137    624  -1111   -240  A    O1-
ATOM   2474  N   TYR A 308      -2.626  -3.016 -19.452  1.00 66.30      A    N  
ANISOU 2474  N   TYR A 308     8163   8764   8261    665   -858   -195  A    N  
ATOM   2475  CA  TYR A 308      -1.457  -2.170 -19.318  1.00 76.58      A    C  
ANISOU 2475  CA  TYR A 308     9445  10132   9517    678   -782   -172  A    C  
ATOM   2476  C   TYR A 308      -1.236  -1.540 -20.666  1.00 83.63      A    C  
ANISOU 2476  C   TYR A 308    10301  11134  10339    753   -744   -191  A    C  
ATOM   2477  O   TYR A 308      -1.644  -2.104 -21.670  1.00 94.97      A    O  
ANISOU 2477  O   TYR A 308    11733  12591  11759    814   -799   -247  A    O  
ATOM   2478  CB  TYR A 308      -0.247  -2.998 -18.859  1.00 73.42      A    C  
ANISOU 2478  CB  TYR A 308     9059   9708   9126    705   -829   -213  A    C  
ATOM   2479  CG  TYR A 308      -0.549  -3.594 -17.512  1.00 72.30      A    C  
ANISOU 2479  CG  TYR A 308     8955   9462   9055    628   -866   -186  A    C  
ATOM   2480  CD1 TYR A 308      -0.356  -2.854 -16.369  1.00 74.08      A    C  
ANISOU 2480  CD1 TYR A 308     9185   9670   9293    559   -801   -119  A    C  
ATOM   2481  CD2 TYR A 308      -1.141  -4.843 -17.388  1.00 75.28      A    C  
ANISOU 2481  CD2 TYR A 308     9359   9757   9488    623   -968   -219  A    C  
ATOM   2482  CE1 TYR A 308      -0.688  -3.352 -15.127  1.00 72.14      A    C  
ANISOU 2482  CE1 TYR A 308     8968   9337   9103    489   -829    -86  A    C  
ATOM   2483  CE2 TYR A 308      -1.486  -5.344 -16.145  1.00 82.38      A    C  
ANISOU 2483  CE2 TYR A 308    10284  10564  10451    546   -997   -179  A    C  
ATOM   2484  CZ  TYR A 308      -1.243  -4.580 -15.017  1.00 77.56      A    C  
ANISOU 2484  CZ  TYR A 308     9677   9949   9840    483   -924   -111  A    C  
ATOM   2485  OH  TYR A 308      -1.546  -5.021 -13.762  1.00 87.57      A    O  
ANISOU 2485  OH  TYR A 308    10969  11141  11161    412   -947    -67  A    O  
ATOM   2486  N   PRO A 309      -0.620  -0.359 -20.705  1.00 83.11      A    N  
ANISOU 2486  N   PRO A 309    10205  11139  10235    748   -654   -142  A    N  
ATOM   2487  CA  PRO A 309      -0.097   0.350 -19.559  1.00 77.24      A    C  
ANISOU 2487  CA  PRO A 309     9464  10371   9511    683   -595    -81  A    C  
ATOM   2488  C   PRO A 309      -1.266   0.968 -18.774  1.00 63.86      A    C  
ANISOU 2488  C   PRO A 309     7785   8621   7857    596   -562    -20  A    C  
ATOM   2489  O   PRO A 309      -2.340   1.218 -19.343  1.00 60.77      A    O  
ANISOU 2489  O   PRO A 309     7387   8239   7461    593   -557    -13  A    O  
ATOM   2490  CB  PRO A 309       0.764   1.435 -20.205  1.00 75.67      A    C  
ANISOU 2490  CB  PRO A 309     9218  10274   9256    720   -521    -52  A    C  
ATOM   2491  CG  PRO A 309      -0.015   1.796 -21.446  1.00 75.87      A    C  
ANISOU 2491  CG  PRO A 309     9220  10365   9242    760   -508    -57  A    C  
ATOM   2492  CD  PRO A 309      -0.716   0.526 -21.889  1.00 76.62      A    C  
ANISOU 2492  CD  PRO A 309     9341  10419   9351    796   -600   -129  A    C  
ATOM   2493  N   LEU A 310      -1.089   1.128 -17.467  1.00 57.94      A    N  
ANISOU 2493  N   LEU A 310     7054   7815   7144    531   -544     16  A    N  
ATOM   2494  CA  LEU A 310      -2.169   1.703 -16.617  1.00 59.23      A    C  
ANISOU 2494  CA  LEU A 310     7230   7932   7340    453   -512     74  A    C  
ATOM   2495  C   LEU A 310      -2.338   3.169 -16.918  1.00 53.22      A    C  
ANISOU 2495  C   LEU A 310     6439   7229   6553    442   -429    122  A    C  
ATOM   2496  O   LEU A 310      -1.366   3.842 -17.161  1.00 52.90      A    O  
ANISOU 2496  O   LEU A 310     6373   7239   6484    466   -387    134  A    O  
ATOM   2497  CB  LEU A 310      -1.806   1.601 -15.129  1.00 55.55      A    C  
ANISOU 2497  CB  LEU A 310     6790   7405   6910    396   -509    102  A    C  
ATOM   2498  CG  LEU A 310      -2.058   0.272 -14.424  1.00 53.37      A    C  
ANISOU 2498  CG  LEU A 310     6548   7051   6680    373   -587     82  A    C  
ATOM   2499  CD1 LEU A 310      -1.852   0.536 -12.949  1.00 57.69      A    C  
ANISOU 2499  CD1 LEU A 310     7113   7555   7250    312   -561    127  A    C  
ATOM   2500  CD2 LEU A 310      -3.438  -0.350 -14.644  1.00 51.20      A    C  
ANISOU 2500  CD2 LEU A 310     6282   6735   6435    352   -633     81  A    C  
ATOM   2501  N   LYS A 311      -3.542   3.686 -16.841  1.00 50.47      A    N  
ANISOU 2501  N   LYS A 311     6091   6867   6216    404   -406    156  A    N  
ATOM   2502  CA  LYS A 311      -3.738   5.133 -17.037  1.00 48.52      A    C  
ANISOU 2502  CA  LYS A 311     5818   6666   5952    389   -332    205  A    C  
ATOM   2503  C   LYS A 311      -3.481   5.944 -15.765  1.00 44.40      A    C  
ANISOU 2503  C   LYS A 311     5302   6115   5453    333   -288    251  A    C  
ATOM   2504  O   LYS A 311      -3.408   5.367 -14.676  1.00 48.86      A    O  
ANISOU 2504  O   LYS A 311     5896   6623   6046    300   -313    250  A    O  
ATOM   2505  CB  LYS A 311      -5.153   5.339 -17.550  1.00 55.41      A    C  
ANISOU 2505  CB  LYS A 311     6685   7539   6826    377   -329    215  A    C  
ATOM   2506  CG  LYS A 311      -5.311   4.842 -19.004  1.00 65.26      A    C  
ANISOU 2506  CG  LYS A 311     7918   8836   8042    443   -362    170  A    C  
ATOM   2507  CD  LYS A 311      -6.744   4.453 -19.350  1.00 73.12      A    C  
ANISOU 2507  CD  LYS A 311     8923   9804   9055    431   -394    162  A    C  
ATOM   2508  CE  LYS A 311      -7.730   5.600 -19.190  1.00 88.58      A    C  
ANISOU 2508  CE  LYS A 311    10869  11769  11019    387   -337    216  A    C  
ATOM   2509  NZ  LYS A 311      -9.171   5.183 -19.245  1.00 94.88      A    N1+
ANISOU 2509  NZ  LYS A 311    11676  12529  11843    362   -368    214  A    N1+
ATOM   2510  N   ALA A 312      -3.426   7.276 -15.876  1.00 41.74      A    N  
ANISOU 2510  N   ALA A 312     4939   5812   5106    324   -228    293  A    N  
ATOM   2511  CA  ALA A 312      -3.026   8.105 -14.777  1.00 43.66      A    C  
ANISOU 2511  CA  ALA A 312     5186   6033   5370    284   -194    328  A    C  
ATOM   2512  C   ALA A 312      -4.063   7.974 -13.705  1.00 39.19      A    C  
ANISOU 2512  C   ALA A 312     4647   5411   4830    232   -200    342  A    C  
ATOM   2513  O   ALA A 312      -3.744   7.854 -12.535  1.00 38.67      A    O  
ANISOU 2513  O   ALA A 312     4602   5307   4783    204   -205    349  A    O  
ATOM   2514  CB  ALA A 312      -2.861   9.566 -15.206  1.00 49.11      A    C  
ANISOU 2514  CB  ALA A 312     5840   6766   6053    285   -139    369  A    C  
ATOM   2515  N   HIS A 313      -5.316   7.959 -14.094  1.00 39.25      A    N  
ANISOU 2515  N   HIS A 313     4654   5420   4839    223   -201    347  A    N  
ATOM   2516  CA  HIS A 313      -6.367   7.979 -13.087  1.00 36.82      A    C  
ANISOU 2516  CA  HIS A 313     4363   5072   4552    174   -199    371  A    C  
ATOM   2517  C   HIS A 313      -6.369   6.643 -12.329  1.00 37.95      A    C  
ANISOU 2517  C   HIS A 313     4536   5167   4716    156   -252    355  A    C  
ATOM   2518  O   HIS A 313      -6.723   6.597 -11.191  1.00 39.60      A    O  
ANISOU 2518  O   HIS A 313     4761   5345   4940    118   -249    377  A    O  
ATOM   2519  CB  HIS A 313      -7.717   8.341 -13.687  1.00 41.93      A    C  
ANISOU 2519  CB  HIS A 313     4999   5735   5198    166   -187    384  A    C  
ATOM   2520  CG  HIS A 313      -8.342   7.236 -14.449  1.00 47.85      A    C  
ANISOU 2520  CG  HIS A 313     5753   6477   5950    183   -235    356  A    C  
ATOM   2521  CD2 HIS A 313      -8.286   6.919 -15.764  1.00 46.70      A    C  
ANISOU 2521  CD2 HIS A 313     5595   6364   5784    229   -256    326  A    C  
ATOM   2522  ND1 HIS A 313      -9.073   6.231 -13.837  1.00 49.76      A    N  
ANISOU 2522  ND1 HIS A 313     6015   6673   6219    152   -278    356  A    N  
ATOM   2523  CE1 HIS A 313      -9.428   5.338 -14.740  1.00 50.46      A    C  
ANISOU 2523  CE1 HIS A 313     6103   6756   6312    177   -328    324  A    C  
ATOM   2524  NE2 HIS A 313      -8.958   5.729 -15.912  1.00 48.20      A    N  
ANISOU 2524  NE2 HIS A 313     5799   6519   5994    227   -316    301  A    N  
ATOM   2525  N   GLN A 314      -5.909   5.569 -12.942  1.00 40.14      A    N  
ANISOU 2525  N   GLN A 314     4820   5437   4992    187   -301    315  A    N  
ATOM   2526  CA  GLN A 314      -5.817   4.273 -12.241  1.00 38.67      A    C  
ANISOU 2526  CA  GLN A 314     4660   5197   4832    171   -359    302  A    C  
ATOM   2527  C   GLN A 314      -4.692   4.256 -11.219  1.00 36.07      A    C  
ANISOU 2527  C   GLN A 314     4347   4850   4506    162   -356    305  A    C  
ATOM   2528  O   GLN A 314      -4.838   3.624 -10.167  1.00 39.45      A    O  
ANISOU 2528  O   GLN A 314     4796   5234   4957    128   -381    319  A    O  
ATOM   2529  CB  GLN A 314      -5.619   3.132 -13.242  1.00 42.38      A    C  
ANISOU 2529  CB  GLN A 314     5134   5663   5304    216   -424    251  A    C  
ATOM   2530  CG  GLN A 314      -6.739   3.081 -14.279  1.00 45.22      A    C  
ANISOU 2530  CG  GLN A 314     5480   6038   5661    229   -437    243  A    C  
ATOM   2531  CD  GLN A 314      -6.437   2.073 -15.339  1.00 46.51      A    C  
ANISOU 2531  CD  GLN A 314     5644   6204   5820    285   -501    183  A    C  
ATOM   2532  NE2 GLN A 314      -7.154   0.993 -15.291  1.00 52.41      A    N  
ANISOU 2532  NE2 GLN A 314     6406   6900   6606    273   -569    169  A    N  
ATOM   2533  OE1 GLN A 314      -5.497   2.223 -16.140  1.00 55.10      A    O  
ANISOU 2533  OE1 GLN A 314     6720   7341   6872    342   -495    150  A    O  
ATOM   2534  N   LYS A 315      -3.612   4.987 -11.488  1.00 35.67      A    N  
ANISOU 2534  N   LYS A 315     4282   4834   4436    190   -323    297  A    N  
ATOM   2535  CA  LYS A 315      -2.537   5.182 -10.497  1.00 37.72      A    C  
ANISOU 2535  CA  LYS A 315     4553   5078   4701    180   -313    304  A    C  
ATOM   2536  C   LYS A 315      -2.995   6.044  -9.356  1.00 38.67      A    C  
ANISOU 2536  C   LYS A 315     4677   5186   4828    137   -274    344  A    C  
ATOM   2537  O   LYS A 315      -2.693   5.778  -8.202  1.00 37.61      A    O  
ANISOU 2537  O   LYS A 315     4563   5020   4704    115   -285    352  A    O  
ATOM   2538  CB  LYS A 315      -1.277   5.712 -11.139  1.00 37.28      A    C  
ANISOU 2538  CB  LYS A 315     4473   5064   4626    220   -293    289  A    C  
ATOM   2539  CG  LYS A 315      -0.658   4.697 -12.129  1.00 46.99      A    C  
ANISOU 2539  CG  LYS A 315     5700   6310   5842    272   -338    241  A    C  
ATOM   2540  CD  LYS A 315       0.469   5.330 -12.942  1.00 51.28      A    C  
ANISOU 2540  CD  LYS A 315     6208   6915   6359    317   -308    236  A    C  
ATOM   2541  CE  LYS A 315       1.237   4.305 -13.750  1.00 64.98      A    C  
ANISOU 2541  CE  LYS A 315     7940   8673   8075    376   -354    185  A    C  
ATOM   2542  NZ  LYS A 315       2.123   4.954 -14.781  1.00 69.83      A    N1+
ANISOU 2542  NZ  LYS A 315     8509   9367   8655    425   -320    188  A    N1+
ATOM   2543  N   VAL A 316      -3.768   7.052  -9.662  1.00 37.58      A    N  
ANISOU 2543  N   VAL A 316     4521   5074   4682    130   -234    367  A    N  
ATOM   2544  CA  VAL A 316      -4.361   7.831  -8.595  1.00 38.27      A    C  
ANISOU 2544  CA  VAL A 316     4613   5152   4775     96   -203    398  A    C  
ATOM   2545  C   VAL A 316      -5.266   6.932  -7.730  1.00 38.47      A    C  
ANISOU 2545  C   VAL A 316     4659   5146   4810     62   -230    413  A    C  
ATOM   2546  O   VAL A 316      -5.173   6.948  -6.477  1.00 35.21      A    O  
ANISOU 2546  O   VAL A 316     4262   4716   4398     40   -226    429  A    O  
ATOM   2547  CB  VAL A 316      -5.208   8.949  -9.092  1.00 35.97      A    C  
ANISOU 2547  CB  VAL A 316     4300   4890   4477     94   -163    418  A    C  
ATOM   2548  CG1 VAL A 316      -5.852   9.716  -7.935  1.00 40.13      A    C  
ANISOU 2548  CG1 VAL A 316     4831   5410   5006     65   -136    444  A    C  
ATOM   2549  CG2 VAL A 316      -4.408   9.866  -9.979  1.00 34.73      A    C  
ANISOU 2549  CG2 VAL A 316     4116   4765   4313    123   -137    416  A    C  
ATOM   2550  N   ALA A 317      -6.070   6.108  -8.361  1.00 38.23      A    N  
ANISOU 2550  N   ALA A 317     4628   5108   4788     59   -260    409  A    N  
ATOM   2551  CA  ALA A 317      -6.942   5.228  -7.541  1.00 40.90      A    C  
ANISOU 2551  CA  ALA A 317     4980   5416   5142     22   -289    434  A    C  
ATOM   2552  C   ALA A 317      -6.111   4.310  -6.613  1.00 41.86      A    C  
ANISOU 2552  C   ALA A 317     5126   5502   5277     13   -326    432  A    C  
ATOM   2553  O   ALA A 317      -6.446   4.150  -5.424  1.00 37.52      A    O  
ANISOU 2553  O   ALA A 317     4585   4940   4728    -17   -324    466  A    O  
ATOM   2554  CB  ALA A 317      -7.823   4.381  -8.424  1.00 38.00      A    C  
ANISOU 2554  CB  ALA A 317     4606   5037   4791     22   -328    428  A    C  
ATOM   2555  N   ILE A 318      -5.025   3.772  -7.182  1.00 39.79      A    N  
ANISOU 2555  N   ILE A 318     4870   5228   5017     44   -358    392  A    N  
ATOM   2556  CA  ILE A 318      -4.083   2.942  -6.438  1.00 41.23      A    C  
ANISOU 2556  CA  ILE A 318     5076   5376   5212     42   -396    382  A    C  
ATOM   2557  C   ILE A 318      -3.504   3.698  -5.224  1.00 36.50      A    C  
ANISOU 2557  C   ILE A 318     4484   4782   4599     30   -360    401  A    C  
ATOM   2558  O   ILE A 318      -3.552   3.206  -4.064  1.00 40.35      A    O  
ANISOU 2558  O   ILE A 318     4989   5246   5093      4   -375    425  A    O  
ATOM   2559  CB  ILE A 318      -3.002   2.367  -7.361  1.00 37.21      A    C  
ANISOU 2559  CB  ILE A 318     4568   4865   4705     87   -432    330  A    C  
ATOM   2560  CG1 ILE A 318      -3.569   1.261  -8.217  1.00 37.67      A    C  
ANISOU 2560  CG1 ILE A 318     4628   4901   4783     99   -492    307  A    C  
ATOM   2561  CG2 ILE A 318      -1.839   1.803  -6.582  1.00 37.30      A    C  
ANISOU 2561  CG2 ILE A 318     4601   4848   4724     90   -461    316  A    C  
ATOM   2562  CD1 ILE A 318      -2.750   1.011  -9.494  1.00 40.71      A    C  
ANISOU 2562  CD1 ILE A 318     5003   5309   5153    158   -515    250  A    C  
ATOM   2563  N   MET A 319      -3.041   4.907  -5.464  1.00 38.84      A    N  
ANISOU 2563  N   MET A 319     4768   5111   4880     48   -313    393  A    N  
ATOM   2564  CA  MET A 319      -2.448   5.693  -4.404  1.00 38.55      A    C  
ANISOU 2564  CA  MET A 319     4737   5076   4835     43   -285    403  A    C  
ATOM   2565  C   MET A 319      -3.473   5.923  -3.335  1.00 37.34      A    C  
ANISOU 2565  C   MET A 319     4587   4925   4672     11   -268    440  A    C  
ATOM   2566  O   MET A 319      -3.188   5.730  -2.199  1.00 37.36      A    O  
ANISOU 2566  O   MET A 319     4607   4916   4671      1   -275    452  A    O  
ATOM   2567  CB  MET A 319      -1.855   6.992  -4.949  1.00 40.81      A    C  
ANISOU 2567  CB  MET A 319     5001   5391   5114     66   -246    393  A    C  
ATOM   2568  CG  MET A 319      -0.598   6.735  -5.780  1.00 40.36      A    C  
ANISOU 2568  CG  MET A 319     4936   5338   5060    100   -262    362  A    C  
ATOM   2569  SD  MET A 319       0.256   8.248  -6.183  1.00 41.52      A    S  
ANISOU 2569  SD  MET A 319     5051   5515   5207    119   -219    366  A    S  
ATOM   2570  CE  MET A 319      -0.856   8.950  -7.389  1.00 38.80      A    C  
ANISOU 2570  CE  MET A 319     4679   5208   4854    124   -188    382  A    C  
ATOM   2571  N   ARG A 320      -4.694   6.299  -3.697  1.00 35.76      A    N  
ANISOU 2571  N   ARG A 320     4372   4746   4467      2   -246    460  A    N  
ATOM   2572  CA  ARG A 320      -5.718   6.467  -2.659  1.00 34.98      A    C  
ANISOU 2572  CA  ARG A 320     4273   4660   4356    -25   -228    498  A    C  
ATOM   2573  C   ARG A 320      -5.937   5.187  -1.871  1.00 40.15      A    C  
ANISOU 2573  C   ARG A 320     4944   5291   5021    -51   -268    525  A    C  
ATOM   2574  O   ARG A 320      -6.041   5.231  -0.625  1.00 36.71      A    O  
ANISOU 2574  O   ARG A 320     4515   4864   4568    -64   -260    552  A    O  
ATOM   2575  CB  ARG A 320      -7.059   6.992  -3.205  1.00 33.38      A    C  
ANISOU 2575  CB  ARG A 320     4048   4485   4150    -33   -202    516  A    C  
ATOM   2576  CG  ARG A 320      -6.996   8.314  -4.008  1.00 37.72      A    C  
ANISOU 2576  CG  ARG A 320     4580   5059   4692    -10   -164    498  A    C  
ATOM   2577  CD  ARG A 320      -8.363   8.870  -4.556  1.00 34.85      A    C  
ANISOU 2577  CD  ARG A 320     4193   4721   4324    -16   -138    516  A    C  
ATOM   2578  NE  ARG A 320      -9.313   8.967  -3.479  1.00 36.27      A    N  
ANISOU 2578  NE  ARG A 320     4371   4920   4489    -36   -123    548  A    N  
ATOM   2579  CZ  ARG A 320      -9.336   9.923  -2.581  1.00 37.32      A    C  
ANISOU 2579  CZ  ARG A 320     4502   5073   4603    -28    -95    550  A    C  
ATOM   2580  NH1 ARG A 320      -8.430  10.927  -2.626  1.00 39.09      A    N1+
ANISOU 2580  NH1 ARG A 320     4728   5293   4829     -3    -82    523  A    N1+
ATOM   2581  NH2 ARG A 320     -10.187   9.813  -1.573  1.00 34.98      A    N  
ANISOU 2581  NH2 ARG A 320     4203   4801   4287    -41    -85    581  A    N  
ATOM   2582  N   ASN A 321      -6.011   4.042  -2.566  1.00 39.87      A    N  
ANISOU 2582  N   ASN A 321     4911   5226   5011    -58   -314    519  A    N  
ATOM   2583  CA  ASN A 321      -6.278   2.787  -1.818  1.00 39.78      A    C  
ANISOU 2583  CA  ASN A 321     4911   5185   5018    -89   -360    554  A    C  
ATOM   2584  C   ASN A 321      -5.123   2.437  -0.909  1.00 41.29      A    C  
ANISOU 2584  C   ASN A 321     5126   5356   5207    -84   -379    545  A    C  
ATOM   2585  O   ASN A 321      -5.378   2.076   0.260  1.00 42.19      A    O  
ANISOU 2585  O   ASN A 321     5246   5471   5314   -109   -384    588  A    O  
ATOM   2586  CB  ASN A 321      -6.638   1.640  -2.720  1.00 35.51      A    C  
ANISOU 2586  CB  ASN A 321     4368   4607   4514    -95   -417    547  A    C  
ATOM   2587  CG  ASN A 321      -8.040   1.762  -3.263  1.00 38.66      A    C  
ANISOU 2587  CG  ASN A 321     4743   5022   4920   -112   -407    573  A    C  
ATOM   2588  ND2 ASN A 321      -8.210   1.412  -4.513  1.00 39.04      A    N  
ANISOU 2588  ND2 ASN A 321     4786   5057   4989    -96   -436    541  A    N  
ATOM   2589  OD1 ASN A 321      -8.946   2.189  -2.576  1.00 39.50      A    O  
ANISOU 2589  OD1 ASN A 321     4836   5159   5012   -136   -373    619  A    O  
ATOM   2590  N   ILE A 322      -3.881   2.636  -1.369  1.00 37.37      A    N  
ANISOU 2590  N   ILE A 322     4639   4848   4710    -52   -384    497  A    N  
ATOM   2591  CA  ILE A 322      -2.747   2.444  -0.412  1.00 38.33      A    C  
ANISOU 2591  CA  ILE A 322     4783   4952   4827    -48   -398    488  A    C  
ATOM   2592  C   ILE A 322      -2.880   3.348   0.822  1.00 36.58      A    C  
ANISOU 2592  C   ILE A 322     4562   4762   4575    -53   -356    513  A    C  
ATOM   2593  O   ILE A 322      -2.664   2.877   1.925  1.00 37.05      A    O  
ANISOU 2593  O   ILE A 322     4637   4813   4627    -65   -371    536  A    O  
ATOM   2594  CB  ILE A 322      -1.359   2.675  -1.002  1.00 37.91      A    C  
ANISOU 2594  CB  ILE A 322     4734   4891   4778    -11   -403    436  A    C  
ATOM   2595  CG1 ILE A 322      -1.036   1.712  -2.140  1.00 41.48      A    C  
ANISOU 2595  CG1 ILE A 322     5187   5319   5253      7   -451    402  A    C  
ATOM   2596  CG2 ILE A 322      -0.247   2.567   0.076  1.00 40.03      A    C  
ANISOU 2596  CG2 ILE A 322     5024   5142   5041     -7   -415    429  A    C  
ATOM   2597  CD1 ILE A 322      -1.174   0.242  -1.855  1.00 48.54      A    C  
ANISOU 2597  CD1 ILE A 322     6097   6166   6176    -12   -518    413  A    C  
ATOM   2598  N   GLU A 323      -3.192   4.640   0.659  1.00 35.85      A    N  
ANISOU 2598  N   GLU A 323     4453   4703   4462    -39   -306    507  A    N  
ATOM   2599  CA  GLU A 323      -3.295   5.448   1.871  1.00 33.36      A    C  
ANISOU 2599  CA  GLU A 323     4142   4416   4118    -36   -275    521  A    C  
ATOM   2600  C   GLU A 323      -4.380   5.004   2.805  1.00 38.28      A    C  
ANISOU 2600  C   GLU A 323     4760   5061   4721    -62   -273    574  A    C  
ATOM   2601  O   GLU A 323      -4.217   5.063   4.034  1.00 38.14      A    O  
ANISOU 2601  O   GLU A 323     4752   5059   4677    -60   -269    591  A    O  
ATOM   2602  CB  GLU A 323      -3.524   6.930   1.489  1.00 35.68      A    C  
ANISOU 2602  CB  GLU A 323     4417   4739   4400    -15   -231    503  A    C  
ATOM   2603  CG  GLU A 323      -2.349   7.510   0.726  1.00 35.31      A    C  
ANISOU 2603  CG  GLU A 323     4367   4675   4371      9   -231    461  A    C  
ATOM   2604  CD  GLU A 323      -2.553   8.900   0.110  1.00 34.98      A    C  
ANISOU 2604  CD  GLU A 323     4304   4655   4332     24   -194    450  A    C  
ATOM   2605  OE1 GLU A 323      -2.800   9.885   0.816  1.00 36.17      A    O  
ANISOU 2605  OE1 GLU A 323     4451   4822   4469     34   -174    451  A    O  
ATOM   2606  OE2 GLU A 323      -2.340   9.011  -1.111  1.00 37.16      A    O1-
ANISOU 2606  OE2 GLU A 323     4565   4930   4624     33   -192    437  A    O1-
ATOM   2607  N   LYS A 324      -5.545   4.652   2.231  1.00 36.11      A    N  
ANISOU 2607  N   LYS A 324     4467   4795   4456    -83   -272    604  A    N  
ATOM   2608  CA  LYS A 324      -6.687   4.166   3.002  1.00 40.21      A    C  
ANISOU 2608  CA  LYS A 324     4973   5341   4962   -112   -269    665  A    C  
ATOM   2609  C   LYS A 324      -6.396   2.876   3.794  1.00 38.17      A    C  
ANISOU 2609  C   LYS A 324     4730   5058   4716   -136   -315    702  A    C  
ATOM   2610  O   LYS A 324      -6.674   2.802   4.973  1.00 42.68      A    O  
ANISOU 2610  O   LYS A 324     5297   5660   5256   -145   -304    745  A    O  
ATOM   2611  CB  LYS A 324      -7.856   3.914   2.060  1.00 43.45      A    C  
ANISOU 2611  CB  LYS A 324     5362   5754   5394   -133   -270    685  A    C  
ATOM   2612  CG  LYS A 324      -8.557   5.174   1.540  1.00 40.61      A    C  
ANISOU 2612  CG  LYS A 324     4981   5433   5014   -115   -221    670  A    C  
ATOM   2613  CD  LYS A 324      -9.779   4.731   0.731  1.00 45.44      A    C  
ANISOU 2613  CD  LYS A 324     5570   6045   5649   -139   -228    699  A    C  
ATOM   2614  CE  LYS A 324     -10.272   5.811  -0.181  1.00 46.69      A    C  
ANISOU 2614  CE  LYS A 324     5711   6226   5801   -121   -192    672  A    C  
ATOM   2615  NZ  LYS A 324     -11.558   5.407  -0.812  1.00 46.22      A    N1+
ANISOU 2615  NZ  LYS A 324     5627   6171   5760   -145   -198    703  A    N1+
ATOM   2616  N   MET A 325      -5.746   1.933   3.163  1.00 37.58      A    N  
ANISOU 2616  N   MET A 325     4670   4929   4680   -143   -365    682  A    N  
ATOM   2617  CA  MET A 325      -5.412   0.653   3.787  1.00 41.11      A    C  
ANISOU 2617  CA  MET A 325     5131   5340   5150   -166   -418    715  A    C  
ATOM   2618  C   MET A 325      -4.375   0.820   4.915  1.00 41.39      A    C  
ANISOU 2618  C   MET A 325     5187   5379   5157   -150   -415    706  A    C  
ATOM   2619  O   MET A 325      -4.465   0.176   5.966  1.00 39.19      A    O  
ANISOU 2619  O   MET A 325     4912   5105   4870   -170   -433    756  A    O  
ATOM   2620  CB  MET A 325      -4.788  -0.247   2.719  1.00 43.26      A    C  
ANISOU 2620  CB  MET A 325     5415   5550   5470   -163   -476    675  A    C  
ATOM   2621  CG  MET A 325      -5.795  -0.739   1.688  1.00 48.70      A    C  
ANISOU 2621  CG  MET A 325     6085   6223   6195   -180   -499    685  A    C  
ATOM   2622  SD  MET A 325      -5.039  -1.634   0.279  1.00 62.19      A    S  
ANISOU 2622  SD  MET A 325     7807   7870   7951   -157   -568    619  A    S  
ATOM   2623  CE  MET A 325      -4.400  -3.012   1.195  1.00 66.36      A    C  
ANISOU 2623  CE  MET A 325     8357   8343   8511   -179   -640    646  A    C  
ATOM   2624  N   LEU A 326      -3.394   1.678   4.670  1.00 40.47      A    N  
ANISOU 2624  N   LEU A 326     5083   5262   5029   -114   -395    646  A    N  
ATOM   2625  CA  LEU A 326      -2.412   2.019   5.698  1.00 42.53      A    C  
ANISOU 2625  CA  LEU A 326     5365   5530   5265    -94   -391    630  A    C  
ATOM   2626  C   LEU A 326      -3.044   2.660   6.909  1.00 42.42      A    C  
ANISOU 2626  C   LEU A 326     5342   5572   5200    -90   -353    666  A    C  
ATOM   2627  O   LEU A 326      -2.720   2.317   8.044  1.00 40.00      A    O  
ANISOU 2627  O   LEU A 326     5048   5276   4872    -91   -364    690  A    O  
ATOM   2628  CB  LEU A 326      -1.263   2.878   5.149  1.00 42.45      A    C  
ANISOU 2628  CB  LEU A 326     5362   5504   5259    -59   -378    562  A    C  
ATOM   2629  CG  LEU A 326      -0.319   2.147   4.187  1.00 48.71      A    C  
ANISOU 2629  CG  LEU A 326     6167   6249   6092    -51   -421    523  A    C  
ATOM   2630  CD1 LEU A 326       0.784   3.031   3.630  1.00 47.40      A    C  
ANISOU 2630  CD1 LEU A 326     5999   6079   5929    -17   -405    468  A    C  
ATOM   2631  CD2 LEU A 326       0.331   0.953   4.874  1.00 53.48      A    C  
ANISOU 2631  CD2 LEU A 326     6793   6816   6710    -63   -473    535  A    C  
ATOM   2632  N   GLY A 327      -3.920   3.613   6.679  1.00 42.77      A    N  
ANISOU 2632  N   GLY A 327     5366   5660   5224    -83   -309    667  A    N  
ATOM   2633  CA  GLY A 327      -4.663   4.250   7.778  1.00 46.67      A    C  
ANISOU 2633  CA  GLY A 327     5846   6219   5665    -72   -272    699  A    C  
ATOM   2634  C   GLY A 327      -5.462   3.271   8.665  1.00 47.23      A    C  
ANISOU 2634  C   GLY A 327     5906   6319   5719   -102   -283    779  A    C  
ATOM   2635  O   GLY A 327      -5.387   3.288   9.888  1.00 46.53      A    O  
ANISOU 2635  O   GLY A 327     5819   6270   5586    -90   -276    804  A    O  
ATOM   2636  N   GLU A 328      -6.169   2.395   8.008  1.00 46.57      A    N  
ANISOU 2636  N   GLU A 328     5806   6213   5672   -141   -304    819  A    N  
ATOM   2637  CA  GLU A 328      -6.832   1.286   8.652  1.00 54.96      A    C  
ANISOU 2637  CA  GLU A 328     6854   7287   6739   -180   -327    902  A    C  
ATOM   2638  C   GLU A 328      -5.943   0.283   9.345  1.00 48.53      A    C  
ANISOU 2638  C   GLU A 328     6063   6436   5936   -191   -374    922  A    C  
ATOM   2639  O   GLU A 328      -6.162   0.027  10.537  1.00 44.41      A    O  
ANISOU 2639  O   GLU A 328     5534   5960   5378   -197   -370    980  A    O  
ATOM   2640  CB  GLU A 328      -7.708   0.535   7.670  1.00 62.03      A    C  
ANISOU 2640  CB  GLU A 328     7730   8152   7687   -220   -353    935  A    C  
ATOM   2641  CG  GLU A 328      -9.093   0.466   8.265  1.00 80.28      A    C  
ANISOU 2641  CG  GLU A 328    10001  10527   9973   -244   -326   1019  A    C  
ATOM   2642  CD  GLU A 328      -9.891  -0.602   7.628  1.00 92.51      A    C  
ANISOU 2642  CD  GLU A 328    11528  12038  11582   -292   -369   1073  A    C  
ATOM   2643  OE1 GLU A 328     -10.086  -0.463   6.391  1.00 92.91      A    O  
ANISOU 2643  OE1 GLU A 328    11579  12053  11669   -292   -376   1029  A    O  
ATOM   2644  OE2 GLU A 328     -10.285  -1.551   8.364  1.00 93.87      A    O1-
ANISOU 2644  OE2 GLU A 328    11683  12218  11765   -329   -396   1158  A    O1-
ATOM   2645  N   ALA A 329      -4.901  -0.218   8.657  1.00 44.92      A    N  
ANISOU 2645  N   ALA A 329     5634   5907   5526   -190   -419    871  A    N  
ATOM   2646  CA  ALA A 329      -4.014  -1.178   9.305  1.00 42.65      A    C  
ANISOU 2646  CA  ALA A 329     5369   5580   5254   -199   -468    885  A    C  
ATOM   2647  C   ALA A 329      -3.228  -0.597  10.462  1.00 43.53      A    C  
ANISOU 2647  C   ALA A 329     5500   5726   5313   -166   -448    868  A    C  
ATOM   2648  O   ALA A 329      -3.001  -1.264  11.433  1.00 49.47      A    O  
ANISOU 2648  O   ALA A 329     6259   6483   6053   -177   -471    914  A    O  
ATOM   2649  CB  ALA A 329      -3.113  -1.850   8.301  1.00 44.11      A    C  
ANISOU 2649  CB  ALA A 329     5576   5685   5497   -199   -523    832  A    C  
ATOM   2650  N   LEU A 330      -2.790   0.657  10.392  1.00 44.20      A    N  
ANISOU 2650  N   LEU A 330     5592   5834   5368   -124   -409    805  A    N  
ATOM   2651  CA  LEU A 330      -1.980   1.216  11.470  1.00 44.40      A    C  
ANISOU 2651  CA  LEU A 330     5636   5883   5349    -89   -398    781  A    C  
ATOM   2652  C   LEU A 330      -2.854   1.675  12.641  1.00 48.59      A    C  
ANISOU 2652  C   LEU A 330     6147   6501   5812    -76   -360    830  A    C  
ATOM   2653  O   LEU A 330      -2.372   1.997  13.739  1.00 53.53      A    O  
ANISOU 2653  O   LEU A 330     6786   7161   6391    -45   -355    824  A    O  
ATOM   2654  CB  LEU A 330      -1.148   2.405  10.984  1.00 46.50      A    C  
ANISOU 2654  CB  LEU A 330     5914   6136   5616    -48   -379    696  A    C  
ATOM   2655  CG  LEU A 330      -0.119   1.972   9.961  1.00 47.28      A    C  
ANISOU 2655  CG  LEU A 330     6029   6162   5771    -51   -414    647  A    C  
ATOM   2656  CD1 LEU A 330       0.401   3.235   9.338  1.00 46.16      A    C  
ANISOU 2656  CD1 LEU A 330     5885   6019   5634    -18   -387    581  A    C  
ATOM   2657  CD2 LEU A 330       0.987   1.110  10.594  1.00 46.64      A    C  
ANISOU 2657  CD2 LEU A 330     5975   6042   5701    -52   -462    644  A    C  
ATOM   2658  N   GLY A 331      -4.144   1.726  12.387  1.00 49.44      A    N  
ANISOU 2658  N   GLY A 331     6223   6649   5912    -96   -333    878  A    N  
ATOM   2659  CA  GLY A 331      -5.084   2.074  13.413  1.00 53.30      A    C  
ANISOU 2659  CA  GLY A 331     6686   7229   6336    -83   -296    931  A    C  
ATOM   2660  C   GLY A 331      -5.134   3.557  13.606  1.00 52.55      A    C  
ANISOU 2660  C   GLY A 331     6590   7183   6194    -29   -252    871  A    C  
ATOM   2661  O   GLY A 331      -5.823   4.022  14.469  1.00 54.01      A    O  
ANISOU 2661  O   GLY A 331     6754   7449   6315     -4   -220    898  A    O  
ATOM   2662  N   ASN A 332      -4.416   4.336  12.830  1.00 50.66      A    N  
ANISOU 2662  N   ASN A 332     6369   6896   5984     -7   -253    790  A    N  
ATOM   2663  CA  ASN A 332      -4.477   5.770  13.034  1.00 51.83      A    C  
ANISOU 2663  CA  ASN A 332     6513   7084   6096     41   -220    736  A    C  
ATOM   2664  C   ASN A 332      -3.915   6.517  11.836  1.00 51.28      A    C  
ANISOU 2664  C   ASN A 332     6452   6954   6077     49   -221    665  A    C  
ATOM   2665  O   ASN A 332      -2.818   6.264  11.438  1.00 47.65      A    O  
ANISOU 2665  O   ASN A 332     6016   6433   5654     47   -251    628  A    O  
ATOM   2666  CB  ASN A 332      -3.784   6.100  14.356  1.00 57.83      A    C  
ANISOU 2666  CB  ASN A 332     7291   7876   6805     86   -227    714  A    C  
ATOM   2667  CG  ASN A 332      -3.189   7.477  14.409  1.00 61.60      A    C  
ANISOU 2667  CG  ASN A 332     7781   8343   7280    138   -224    630  A    C  
ATOM   2668  ND2 ASN A 332      -1.984   7.550  14.879  1.00 70.05      A    N  
ANISOU 2668  ND2 ASN A 332     8879   9376   8357    157   -254    589  A    N  
ATOM   2669  OD1 ASN A 332      -3.797   8.452  14.024  1.00 65.21      A    O  
ANISOU 2669  OD1 ASN A 332     8222   8821   7733    159   -198    600  A    O  
ATOM   2670  N   PRO A 333      -4.665   7.446  11.276  1.00 48.46      A    N  
ANISOU 2670  N   PRO A 333     6074   6619   5718     61   -191    646  A    N  
ATOM   2671  CA  PRO A 333      -4.235   8.006  10.019  1.00 51.57      A    C  
ANISOU 2671  CA  PRO A 333     6471   6959   6163     59   -192    598  A    C  
ATOM   2672  C   PRO A 333      -2.956   8.776  10.112  1.00 46.33      A    C  
ANISOU 2672  C   PRO A 333     5826   6259   5515     92   -208    532  A    C  
ATOM   2673  O   PRO A 333      -2.242   8.916   9.120  1.00 42.64      A    O  
ANISOU 2673  O   PRO A 333     5363   5739   5096     85   -219    500  A    O  
ATOM   2674  CB  PRO A 333      -5.414   8.905   9.601  1.00 49.11      A    C  
ANISOU 2674  CB  PRO A 333     6131   6690   5838     69   -154    598  A    C  
ATOM   2675  CG  PRO A 333      -6.124   9.183  10.879  1.00 51.01      A    C  
ANISOU 2675  CG  PRO A 333     6360   7008   6012     96   -135    622  A    C  
ATOM   2676  CD  PRO A 333      -5.968   7.948  11.685  1.00 44.27      A    C  
ANISOU 2676  CD  PRO A 333     5515   6166   5140     74   -154    677  A    C  
ATOM   2677  N   GLN A 334      -2.634   9.259  11.288  1.00 53.02      A    N  
ANISOU 2677  N   GLN A 334     6685   7136   6323    130   -213    514  A    N  
ATOM   2678  CA  GLN A 334      -1.429  10.096  11.423  1.00 56.64      A    C  
ANISOU 2678  CA  GLN A 334     7159   7555   6802    163   -234    451  A    C  
ATOM   2679  C   GLN A 334      -0.128   9.372  11.369  1.00 49.55      A    C  
ANISOU 2679  C   GLN A 334     6285   6602   5938    150   -269    438  A    C  
ATOM   2680  O   GLN A 334       0.912   9.994  11.164  1.00 51.27      A    O  
ANISOU 2680  O   GLN A 334     6511   6778   6189    168   -287    391  A    O  
ATOM   2681  CB  GLN A 334      -1.543  10.965  12.667  1.00 69.03      A    C  
ANISOU 2681  CB  GLN A 334     8732   9174   8321    217   -233    424  A    C  
ATOM   2682  CG  GLN A 334      -2.790  11.839  12.507  1.00 82.87      A    C  
ANISOU 2682  CG  GLN A 334    10458  10976  10049    235   -201    424  A    C  
ATOM   2683  CD  GLN A 334      -2.804  13.113  13.309  1.00 88.59      A    C  
ANISOU 2683  CD  GLN A 334    11183  11731  10743    298   -206    371  A    C  
ATOM   2684  NE2 GLN A 334      -2.000  13.146  14.370  1.00 88.79      A    N  
ANISOU 2684  NE2 GLN A 334    11188  11776  10772    314   -188    354  A    N  
ATOM   2685  OE1 GLN A 334      -3.506  14.063  12.978  1.00 94.30      A    O  
ANISOU 2685  OE1 GLN A 334    11925  12461  11443    333   -231    343  A    O  
ATOM   2686  N   GLU A 335      -0.171   8.065  11.516  1.00 46.62      A    N  
ANISOU 2686  N   GLU A 335     5923   6227   5563    119   -281    484  A    N  
ATOM   2687  CA  GLU A 335       0.995   7.238  11.281  1.00 49.51      A    C  
ANISOU 2687  CA  GLU A 335     6309   6535   5965    103   -317    473  A    C  
ATOM   2688  C   GLU A 335       1.270   6.901   9.808  1.00 43.03      A    C  
ANISOU 2688  C   GLU A 335     5481   5667   5201     76   -322    463  A    C  
ATOM   2689  O   GLU A 335       2.278   6.304   9.504  1.00 40.02      A    O  
ANISOU 2689  O   GLU A 335     5112   5240   4850     70   -353    447  A    O  
ATOM   2690  CB  GLU A 335       0.855   5.926  12.015  1.00 52.90      A    C  
ANISOU 2690  CB  GLU A 335     6749   6974   6374     80   -337    525  A    C  
ATOM   2691  CG  GLU A 335       1.186   6.039  13.498  1.00 61.37      A    C  
ANISOU 2691  CG  GLU A 335     7838   8081   7397    111   -346    526  A    C  
ATOM   2692  CD  GLU A 335       1.217   4.671  14.069  1.00 68.29      A    C  
ANISOU 2692  CD  GLU A 335     8726   8956   8265     82   -372    582  A    C  
ATOM   2693  OE1 GLU A 335       0.269   4.360  14.800  1.00 73.05      A    O  
ANISOU 2693  OE1 GLU A 335     9315   9618   8822     77   -355    640  A    O  
ATOM   2694  OE2 GLU A 335       2.129   3.887  13.685  1.00 79.02      A    O1-
ANISOU 2694  OE2 GLU A 335    10102  10254   9667     64   -408    571  A    O1-
ATOM   2695  N   VAL A 336       0.410   7.328   8.896  1.00 39.75      A    N  
ANISOU 2695  N   VAL A 336     5043   5263   4795     68   -296    469  A    N  
ATOM   2696  CA  VAL A 336       0.557   6.896   7.519  1.00 34.65      A    C  
ANISOU 2696  CA  VAL A 336     4389   4583   4193     47   -302    464  A    C  
ATOM   2697  C   VAL A 336       1.854   7.462   6.911  1.00 35.24      A    C  
ANISOU 2697  C   VAL A 336     4465   4621   4304     66   -313    415  A    C  
ATOM   2698  O   VAL A 336       2.638   6.757   6.296  1.00 35.69      A    O  
ANISOU 2698  O   VAL A 336     4526   4644   4388     59   -337    403  A    O  
ATOM   2699  CB  VAL A 336      -0.656   7.281   6.693  1.00 39.83      A    C  
ANISOU 2699  CB  VAL A 336     5020   5264   4848     35   -270    481  A    C  
ATOM   2700  CG1 VAL A 336      -0.348   7.126   5.203  1.00 41.21      A    C  
ANISOU 2700  CG1 VAL A 336     5184   5407   5064     27   -275    462  A    C  
ATOM   2701  CG2 VAL A 336      -1.817   6.383   7.085  1.00 40.79      A    C  
ANISOU 2701  CG2 VAL A 336     5135   5412   4947      8   -269    537  A    C  
ATOM   2702  N   GLY A 337       2.106   8.712   7.157  1.00 35.98      A    N  
ANISOU 2702  N   GLY A 337     4551   4722   4396     92   -299    387  A    N  
ATOM   2703  CA  GLY A 337       3.264   9.356   6.604  1.00 39.64      A    C  
ANISOU 2703  CA  GLY A 337     5008   5154   4898    107   -308    351  A    C  
ATOM   2704  C   GLY A 337       4.582   8.797   7.097  1.00 40.59      A    C  
ANISOU 2704  C   GLY A 337     5148   5241   5032    114   -344    332  A    C  
ATOM   2705  O   GLY A 337       5.504   8.576   6.276  1.00 36.31      A    O  
ANISOU 2705  O   GLY A 337     4599   4673   4524    112   -356    317  A    O  
ATOM   2706  N   PRO A 338       4.702   8.636   8.454  1.00 41.86      A    N  
ANISOU 2706  N   PRO A 338     5332   5409   5163    125   -359    333  A    N  
ATOM   2707  CA  PRO A 338       5.963   8.056   8.988  1.00 40.82      A    C  
ANISOU 2707  CA  PRO A 338     5220   5244   5042    131   -396    314  A    C  
ATOM   2708  C   PRO A 338       6.256   6.683   8.395  1.00 39.68      A    C  
ANISOU 2708  C   PRO A 338     5084   5078   4914    108   -417    328  A    C  
ATOM   2709  O   PRO A 338       7.369   6.426   7.965  1.00 38.31      A    O  
ANISOU 2709  O   PRO A 338     4910   4873   4770    114   -438    305  A    O  
ATOM   2710  CB  PRO A 338       5.715   7.970  10.505  1.00 40.19      A    C  
ANISOU 2710  CB  PRO A 338     5163   5190   4917    147   -405    323  A    C  
ATOM   2711  CG  PRO A 338       4.828   9.221  10.756  1.00 45.90      A    C  
ANISOU 2711  CG  PRO A 338     5870   5951   5616    168   -376    315  A    C  
ATOM   2712  CD  PRO A 338       3.924   9.325   9.513  1.00 41.59      A    C  
ANISOU 2712  CD  PRO A 338     5301   5415   5086    145   -345    336  A    C  
ATOM   2713  N   LEU A 339       5.253   5.850   8.307  1.00 38.28      A    N  
ANISOU 2713  N   LEU A 339     4908   4915   4718     84   -413    366  A    N  
ATOM   2714  CA  LEU A 339       5.426   4.586   7.649  1.00 37.30      A    C  
ANISOU 2714  CA  LEU A 339     4790   4765   4616     64   -440    376  A    C  
ATOM   2715  C   LEU A 339       5.838   4.715   6.207  1.00 38.50      A    C  
ANISOU 2715  C   LEU A 339     4922   4903   4803     69   -437    350  A    C  
ATOM   2716  O   LEU A 339       6.742   4.069   5.778  1.00 37.96      A    O  
ANISOU 2716  O   LEU A 339     4858   4805   4757     75   -465    327  A    O  
ATOM   2717  CB  LEU A 339       4.180   3.756   7.729  1.00 41.36      A    C  
ANISOU 2717  CB  LEU A 339     5304   5295   5115     35   -439    425  A    C  
ATOM   2718  CG  LEU A 339       4.558   2.340   7.387  1.00 46.70      A    C  
ANISOU 2718  CG  LEU A 339     5992   5931   5819     18   -486    430  A    C  
ATOM   2719  CD1 LEU A 339       4.050   1.342   8.373  1.00 53.24      A    C  
ANISOU 2719  CD1 LEU A 339     6836   6758   6635     -6   -513    480  A    C  
ATOM   2720  CD2 LEU A 339       4.102   2.015   6.003  1.00 53.12      A    C  
ANISOU 2720  CD2 LEU A 339     6788   6739   6656      9   -484    429  A    C  
ATOM   2721  N   LEU A 340       5.165   5.552   5.448  1.00 37.36      A    N  
ANISOU 2721  N   LEU A 340     4754   4782   4659     71   -400    352  A    N  
ATOM   2722  CA  LEU A 340       5.554   5.689   4.014  1.00 37.45      A    C  
ANISOU 2722  CA  LEU A 340     4742   4789   4696     79   -395    331  A    C  
ATOM   2723  C   LEU A 340       7.000   6.175   3.895  1.00 38.94      A    C  
ANISOU 2723  C   LEU A 340     4923   4963   4909    101   -404    300  A    C  
ATOM   2724  O   LEU A 340       7.756   5.750   3.008  1.00 35.50      A    O  
ANISOU 2724  O   LEU A 340     4476   4520   4492    113   -417    281  A    O  
ATOM   2725  CB  LEU A 340       4.630   6.598   3.273  1.00 34.46      A    C  
ANISOU 2725  CB  LEU A 340     4337   4439   4314     77   -355    342  A    C  
ATOM   2726  CG  LEU A 340       3.233   6.037   2.975  1.00 37.63      A    C  
ANISOU 2726  CG  LEU A 340     4738   4857   4702     55   -348    372  A    C  
ATOM   2727  CD1 LEU A 340       2.343   7.194   2.483  1.00 41.81      A    C  
ANISOU 2727  CD1 LEU A 340     5244   5416   5225     57   -305    380  A    C  
ATOM   2728  CD2 LEU A 340       3.278   4.906   1.920  1.00 36.73      A    C  
ANISOU 2728  CD2 LEU A 340     4622   4727   4605     52   -374    365  A    C  
ATOM   2729  N   ASN A 341       7.377   7.099   4.760  1.00 38.53      A    N  
ANISOU 2729  N   ASN A 341     4873   4908   4856    112   -398    292  A    N  
ATOM   2730  CA  ASN A 341       8.730   7.626   4.668  1.00 41.25      A    C  
ANISOU 2730  CA  ASN A 341     5206   5235   5229    130   -409    266  A    C  
ATOM   2731  C   ASN A 341       9.771   6.568   4.975  1.00 36.66      A    C  
ANISOU 2731  C   ASN A 341     4644   4629   4656    135   -448    249  A    C  
ATOM   2732  O   ASN A 341      10.777   6.475   4.332  1.00 35.49      A    O  
ANISOU 2732  O   ASN A 341     4478   4472   4531    149   -458    232  A    O  
ATOM   2733  CB  ASN A 341       8.864   8.834   5.644  1.00 43.01      A    C  
ANISOU 2733  CB  ASN A 341     5430   5454   5456    142   -406    258  A    C  
ATOM   2734  CG  ASN A 341       8.357  10.122   5.041  1.00 44.37      A    C  
ANISOU 2734  CG  ASN A 341     5571   5642   5642    145   -375    264  A    C  
ATOM   2735  ND2 ASN A 341       7.315  10.660   5.602  1.00 46.84      A    N  
ANISOU 2735  ND2 ASN A 341     5891   5973   5931    145   -360    271  A    N  
ATOM   2736  OD1 ASN A 341       8.919  10.632   4.089  1.00 57.54      A    O  
ANISOU 2736  OD1 ASN A 341     7209   7309   7343    149   -368    263  A    O  
ATOM   2737  N   THR A 342       9.550   5.814   6.040  1.00 37.36      A    N  
ANISOU 2737  N   THR A 342     4766   4705   4722    127   -470    257  A    N  
ATOM   2738  CA  THR A 342      10.391   4.680   6.361  1.00 38.56      A    C  
ANISOU 2738  CA  THR A 342     4939   4830   4881    129   -511    245  A    C  
ATOM   2739  C   THR A 342      10.485   3.690   5.226  1.00 36.32      A    C  
ANISOU 2739  C   THR A 342     4647   4540   4611    129   -527    239  A    C  
ATOM   2740  O   THR A 342      11.554   3.221   4.910  1.00 37.16      A    O  
ANISOU 2740  O   THR A 342     4752   4630   4736    144   -554    213  A    O  
ATOM   2741  CB  THR A 342       9.816   3.968   7.560  1.00 45.53      A    C  
ANISOU 2741  CB  THR A 342     5853   5708   5735    114   -529    269  A    C  
ATOM   2742  CG2 THR A 342      10.598   2.734   7.883  1.00 44.57      A    C  
ANISOU 2742  CG2 THR A 342     5755   5554   5623    114   -577    262  A    C  
ATOM   2743  OG1 THR A 342       9.820   4.869   8.677  1.00 44.08      A    O  
ANISOU 2743  OG1 THR A 342     5678   5537   5532    126   -519    268  A    O  
ATOM   2744  N   MET A 343       9.372   3.435   4.570  1.00 39.08      A    N  
ANISOU 2744  N   MET A 343     4990   4905   4952    114   -515    258  A    N  
ATOM   2745  CA  MET A 343       9.373   2.647   3.362  1.00 37.76      A    C  
ANISOU 2745  CA  MET A 343     4811   4736   4796    122   -531    244  A    C  
ATOM   2746  C   MET A 343      10.323   3.194   2.341  1.00 33.54      A    C  
ANISOU 2746  C   MET A 343     4245   4219   4277    149   -516    218  A    C  
ATOM   2747  O   MET A 343      11.027   2.429   1.747  1.00 31.27      A    O  
ANISOU 2747  O   MET A 343     3953   3926   3999    170   -547    191  A    O  
ATOM   2748  CB  MET A 343       8.010   2.577   2.708  1.00 37.95      A    C  
ANISOU 2748  CB  MET A 343     4827   4778   4813    106   -515    266  A    C  
ATOM   2749  CG  MET A 343       7.101   1.467   3.153  1.00 51.11      A    C  
ANISOU 2749  CG  MET A 343     6514   6420   6483     87   -556    281  A    C  
ATOM   2750  SD  MET A 343       5.698   1.162   2.089  1.00 46.39      A    S  
ANISOU 2750  SD  MET A 343     5903   5838   5885     69   -547    305  A    S  
ATOM   2751  CE  MET A 343       6.437  -0.043   1.098  1.00 50.61      A    C  
ANISOU 2751  CE  MET A 343     6434   6403   6393     50   -494    341  A    C  
ATOM   2752  N   ILE A 344      10.341   4.505   2.117  1.00 34.72      A    N  
ANISOU 2752  N   ILE A 344     4368   4392   4429    153   -476    225  A    N  
ATOM   2753  CA  ILE A 344      11.100   4.926   0.929  1.00 36.95      A    C  
ANISOU 2753  CA  ILE A 344     4612   4701   4726    178   -461    212  A    C  
ATOM   2754  C   ILE A 344      12.527   5.365   1.143  1.00 34.59      A    C  
ANISOU 2754  C   ILE A 344     4298   4396   4449    195   -469    197  A    C  
ATOM   2755  O   ILE A 344      13.352   5.279   0.230  1.00 39.44      A    O  
ANISOU 2755  O   ILE A 344     4882   5032   5072    220   -470    184  A    O  
ATOM   2756  CB  ILE A 344      10.359   5.978  -0.019  1.00 45.00      A    C  
ANISOU 2756  CB  ILE A 344     5597   5758   5743    176   -415    232  A    C  
ATOM   2757  CG1 ILE A 344      10.541   7.410   0.438  1.00 54.00      A    C  
ANISOU 2757  CG1 ILE A 344     6719   6897   6898    170   -390    248  A    C  
ATOM   2758  CG2 ILE A 344       8.919   5.615  -0.225  1.00 46.28      A    C  
ANISOU 2758  CG2 ILE A 344     5773   5927   5885    159   -407    248  A    C  
ATOM   2759  CD1 ILE A 344      10.169   8.416  -0.644  1.00 66.81      A    C  
ANISOU 2759  CD1 ILE A 344     8300   8555   8528    174   -352    269  A    C  
ATOM   2760  N   LYS A 345      12.808   5.970   2.301  1.00 38.11      A    N  
ANISOU 2760  N   LYS A 345     4758   4818   4905    186   -473    200  A    N  
ATOM   2761  CA  LYS A 345      14.098   6.633   2.475  1.00 39.55      A    C  
ANISOU 2761  CA  LYS A 345     4918   4992   5115    200   -479    190  A    C  
ATOM   2762  C   LYS A 345      15.207   5.675   2.400  1.00 38.09      A    C  
ANISOU 2762  C   LYS A 345     4736   4797   4937    218   -512    166  A    C  
ATOM   2763  O   LYS A 345      15.256   4.694   3.146  1.00 36.89      A    O  
ANISOU 2763  O   LYS A 345     4623   4617   4775    216   -547    151  A    O  
ATOM   2764  CB  LYS A 345      14.201   7.291   3.853  1.00 42.07      A    C  
ANISOU 2764  CB  LYS A 345     5259   5281   5442    192   -489    189  A    C  
ATOM   2765  CG  LYS A 345      13.531   8.633   3.832  1.00 45.59      A    C  
ANISOU 2765  CG  LYS A 345     5686   5737   5897    184   -459    208  A    C  
ATOM   2766  CD  LYS A 345      12.902   9.014   5.139  1.00 55.17      A    C  
ANISOU 2766  CD  LYS A 345     6931   6935   7094    179   -466    206  A    C  
ATOM   2767  CE  LYS A 345      13.921   9.495   6.116  1.00 61.64      A    C  
ANISOU 2767  CE  LYS A 345     7758   7724   7937    190   -495    185  A    C  
ATOM   2768  NZ  LYS A 345      13.150  10.470   6.953  1.00 75.20      A    N1+
ANISOU 2768  NZ  LYS A 345     9486   9440   9645    193   -490    184  A    N1+
ATOM   2769  N   GLY A 346      16.121   5.963   1.500  1.00 34.72      A    N  
ANISOU 2769  N   GLY A 346     4266   4396   4528    239   -504    163  A    N  
ATOM   2770  CA  GLY A 346      17.309   5.161   1.324  1.00 33.86      A    C  
ANISOU 2770  CA  GLY A 346     4152   4286   4426    264   -534    136  A    C  
ATOM   2771  C   GLY A 346      16.964   3.862   0.551  1.00 37.63      A    C  
ANISOU 2771  C   GLY A 346     4640   4777   4877    281   -553    115  A    C  
ATOM   2772  O   GLY A 346      17.801   3.029   0.428  1.00 36.15      A    O  
ANISOU 2772  O   GLY A 346     4454   4587   4691    306   -585     87  A    O  
ATOM   2773  N   ARG A 347      15.730   3.686   0.061  1.00 34.81      A    N  
ANISOU 2773  N   ARG A 347     4292   4433   4499    271   -538    125  A    N  
ATOM   2774  CA  ARG A 347      15.345   2.440  -0.524  1.00 36.94      A    C  
ANISOU 2774  CA  ARG A 347     4576   4704   4753    286   -568    102  A    C  
ATOM   2775  C   ARG A 347      14.747   2.675  -1.899  1.00 39.17      A    C  
ANISOU 2775  C   ARG A 347     4826   5038   5019    302   -538    108  A    C  
ATOM   2776  O   ARG A 347      15.007   1.926  -2.827  1.00 38.61      A    O  
ANISOU 2776  O   ARG A 347     4742   4993   4934    338   -557     80  A    O  
ATOM   2777  CB  ARG A 347      14.286   1.748   0.356  1.00 38.94      A    C  
ANISOU 2777  CB  ARG A 347     4879   4914   4999    253   -592    111  A    C  
ATOM   2778  CG  ARG A 347      14.798   1.351   1.760  1.00 36.96      A    C  
ANISOU 2778  CG  ARG A 347     4666   4617   4759    239   -625    108  A    C  
ATOM   2779  CD  ARG A 347      13.769   0.550   2.514  1.00 35.47      A    C  
ANISOU 2779  CD  ARG A 347     4519   4396   4563    209   -650    125  A    C  
ATOM   2780  NE  ARG A 347      13.494  -0.765   1.938  1.00 37.12      A    N  
ANISOU 2780  NE  ARG A 347     4740   4588   4775    219   -696    108  A    N  
ATOM   2781  CZ  ARG A 347      12.292  -1.250   1.574  1.00 35.37      A    C  
ANISOU 2781  CZ  ARG A 347     4526   4363   4549    201   -703    124  A    C  
ATOM   2782  NH1 ARG A 347      11.190  -0.559   1.775  1.00 35.53      A    N1+
ANISOU 2782  NH1 ARG A 347     4542   4398   4556    173   -663    162  A    N1+
ATOM   2783  NH2 ARG A 347      12.192  -2.510   1.080  1.00 37.25      A    N  
ANISOU 2783  NH2 ARG A 347     4774   4576   4799    213   -759    101  A    N  
ATOM   2784  N   TYR A 348      13.903   3.682  -2.032  1.00 38.69      A    N  
ANISOU 2784  N   TYR A 348     4752   4993   4955    280   -495    142  A    N  
ATOM   2785  CA  TYR A 348      13.339   4.022  -3.321  1.00 38.59      A    C  
ANISOU 2785  CA  TYR A 348     4705   5031   4925    295   -464    152  A    C  
ATOM   2786  C   TYR A 348      13.521   5.519  -3.748  1.00 40.85      A    C  
ANISOU 2786  C   TYR A 348     4945   5354   5221    292   -413    188  A    C  
ATOM   2787  O   TYR A 348      12.985   5.895  -4.765  1.00 39.64      A    O  
ANISOU 2787  O   TYR A 348     4763   5244   5054    301   -385    204  A    O  
ATOM   2788  CB  TYR A 348      11.821   3.705  -3.332  1.00 37.97      A    C  
ANISOU 2788  CB  TYR A 348     4654   4939   4832    271   -464    161  A    C  
ATOM   2789  CG  TYR A 348      11.419   2.229  -3.230  1.00 40.83      A    C  
ANISOU 2789  CG  TYR A 348     5053   5268   5191    275   -517    134  A    C  
ATOM   2790  CD1 TYR A 348      11.357   1.444  -4.350  1.00 39.44      A    C  
ANISOU 2790  CD1 TYR A 348     4866   5117   5002    310   -541    103  A    C  
ATOM   2791  CD2 TYR A 348      11.031   1.640  -2.004  1.00 39.01      A    C  
ANISOU 2791  CD2 TYR A 348     4866   4985   4970    242   -547    140  A    C  
ATOM   2792  CE1 TYR A 348      10.948   0.123  -4.274  1.00 41.73      A    C  
ANISOU 2792  CE1 TYR A 348     5188   5369   5298    312   -599     78  A    C  
ATOM   2793  CE2 TYR A 348      10.596   0.314  -1.947  1.00 37.72      A    C  
ANISOU 2793  CE2 TYR A 348     4731   4787   4811    239   -600    125  A    C  
ATOM   2794  CZ  TYR A 348      10.604  -0.441  -3.087  1.00 39.23      A    C  
ANISOU 2794  CZ  TYR A 348     4912   4995   4999    275   -629     91  A    C  
ATOM   2795  OH  TYR A 348      10.183  -1.742  -3.123  1.00 37.93      A    O  
ANISOU 2795  OH  TYR A 348     4772   4790   4847    275   -692     72  A    O  
ATOM   2796  N   ASN A 349      14.221   6.356  -2.996  1.00 42.06      A    N  
ANISOU 2796  N   ASN A 349     5089   5488   5402    278   -407    204  A    N  
ATOM   2797  CA  ASN A 349      14.343   7.808  -3.382  1.00 49.41      A    C  
ANISOU 2797  CA  ASN A 349     5973   6445   6355    269   -367    245  A    C  
ATOM   2798  C   ASN A 349      15.741   8.299  -3.748  1.00 46.24      A    C  
ANISOU 2798  C   ASN A 349     5520   6068   5977    289   -363    259  A    C  
ATOM   2799  O   ASN A 349      16.681   7.546  -3.509  1.00 55.03      A    O  
ANISOU 2799  O   ASN A 349     6640   7175   7091    308   -391    231  A    O  
ATOM   2800  CB  ASN A 349      13.809   8.670  -2.279  1.00 41.11      A    C  
ANISOU 2800  CB  ASN A 349     4945   5349   5325    236   -363    260  A    C  
ATOM   2801  CG  ASN A 349      14.626   8.592  -1.028  1.00 41.41      A    C  
ANISOU 2801  CG  ASN A 349     5007   5341   5384    230   -394    244  A    C  
ATOM   2802  ND2 ASN A 349      14.192   9.366  -0.074  1.00 50.57      A    N  
ANISOU 2802  ND2 ASN A 349     6186   6468   6557    209   -393    252  A    N  
ATOM   2803  OD1 ASN A 349      15.611   7.822  -0.875  1.00 41.76      A    O  
ANISOU 2803  OD1 ASN A 349     5056   5378   5430    247   -421    220  A    O  
TER   
END


A second structure was input as follows:


HEADER    TRANSCRIPTION ACTIVATOR/INHIBITOR       12-AUG-02   1H2K              
TITLE     FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT    
TITLE    2 PEPTIDE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FACTOR INHIBITING HIF1;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HYPOXIA-INDUCIBLE FACTOR 1 ALPHA;                          
COMPND   7 CHAIN: S;                                                            
COMPND   8 FRAGMENT: C-TERMINAL TRANSACTIVATION DOMAIN FRAGMENT, RESIDUES 786-  
COMPND   9 826;                                                                 
COMPND  10 SYNONYM: HIF-1 ALPHA, ARNT INTERACTING PROTEIN, MEMBER OF PAS PROTEIN
COMPND  11 1;                                                                   
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28A(+);                                
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PGEX-GP-1                                 
KEYWDS    TRANSCRIPTION ACTIVATOR-INHIBITOR COMPLEX, FIH, HIF, DSBH, OXYGENASE, 
KEYWDS   2 TRANSCRIPTION, HYPOXIA, 2- OXOGLUTARATE, ASPARAGINYL HYDROXYLASE,    
KEYWDS   3 PHOSPHORYLATION                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.ELKINS,K.S.HEWITSON,L.A.MCNEILL,I.SCHLEMMINGER,J.F.SEIBEL,        
AUTHOR   2 C.J.SCHOFIELD                                                        
REVDAT   6   21-FEB-18 1H2K    1       JRNL                                     
REVDAT   5   13-JUL-11 1H2K    1       VERSN                                    
REVDAT   4   21-JUL-09 1H2K    1       HETNAM                                   
REVDAT   3   24-FEB-09 1H2K    1       VERSN                                    
REVDAT   2   30-JAN-03 1H2K    1       JRNL                                     
REVDAT   1   28-NOV-02 1H2K    0                                                
JRNL        AUTH   J.M.ELKINS,K.S.HEWITSON,L.A.MCNEILL,J.F.SEIBEL,              
JRNL        AUTH 2 I.SCHLEMMINGER,C.PUGH,P.RATCLIFFE,C.J.SCHOFIELD              
JRNL        TITL   STRUCTURE OF FACTOR-INHIBITING HYPOXIA-INDUCIBLE FACTOR      
JRNL        TITL 2 (HIF) REVEALS MECHANISM OF OXIDATIVE MODIFICATION OF         
JRNL        TITL 3 HIF-1ALPHA                                                   
JRNL        REF    J.BIOL.CHEM.                  V. 278  1802 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12446723                                                     
JRNL        DOI    10.1074/JBC.C200644200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 28171                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2340                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.21                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1906                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2220                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 152                          
REMARK   3   BIN FREE R VALUE                    : 0.2570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2875                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 194                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.27000                                             
REMARK   3    B22 (A**2) : -0.27000                                             
REMARK   3    B33 (A**2) : 0.55000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.174         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.156         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.147         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.588         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2973 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2561 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4044 ; 1.374 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5979 ; 0.722 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   352 ; 4.018 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   515 ;17.698 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   416 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3333 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   604 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   714 ; 0.218 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2499 ; 0.204 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   259 ; 0.152 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     4 ; 0.087 ; 0.500       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    18 ; 0.245 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    72 ; 0.248 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.255 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):     1 ; 0.052 ; 0.500       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    15        A   349                          
REMARK   3    RESIDUE RANGE :   S   795        S   823                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.6620  27.4620  28.2370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1474 T22:   0.0149                                     
REMARK   3      T33:   0.0919 T12:  -0.0099                                     
REMARK   3      T13:  -0.0455 T23:   0.0363                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0098 L22:   2.2577                                     
REMARK   3      L33:   1.2037 L12:   0.6963                                     
REMARK   3      L13:   0.4840 L23:   1.0420                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0288 S12:  -0.1525 S13:  -0.0400                       
REMARK   3      S21:   0.1459 S22:   0.0002 S23:   0.1021                       
REMARK   3      S31:   0.1876 S32:  -0.0468 S33:  -0.0290                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1H2K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-AUG-02.                  
REMARK 100 THE DEPOSITION ID IS D_1290011170.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30574                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.170                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M AMMONIUM SULPHATE, 4% PEG400,       
REMARK 280  0.1M HEPES PH7.5, ARGON ATMOSPHERE, 11MG/ML PROTEIN WITH 1MM        
REMARK 280  FE(II), 2.5MM NOG AND 2.5MM PEPTIDE, PH 7.50                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.32800            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       43.08050            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.08050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       36.66400            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.08050            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.08050            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      109.99200            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.08050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.08050            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       36.66400            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.08050            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.08050            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      109.99200            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       73.32800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE PROTEIN IS A DIMERIC   FORMED BY CHAIN                   
REMARK 300   A.A HETERODIMERIC ASSOCIATION OF CHAIN A WITH                      
REMARK 300  CHAIN SPRODUCES A TETRAMER.THE BURIED SURFACE AREA                  
REMARK 300   SHOWN BELOW IS AN AVERAGECALCULATED FOR THE                        
REMARK 300  HETEROTETRAMER AND DOES NOTCORRESPOND TO THE BURIED                 
REMARK 300   SURFACE AREA FOR THEHOMODIMER OF CHAIN A                           
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, S                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000       86.16100            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       86.16100            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       73.32800            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     LYS A   304                                                      
REMARK 465     ARG A   305                                                      
REMARK 465     ILE A   306                                                      
REMARK 465     SER S   786                                                      
REMARK 465     MET S   787                                                      
REMARK 465     ASP S   788                                                      
REMARK 465     GLU S   789                                                      
REMARK 465     SER S   790                                                      
REMARK 465     GLY S   791                                                      
REMARK 465     LEU S   792                                                      
REMARK 465     PRO S   793                                                      
REMARK 465     GLN S   794                                                      
REMARK 465     GLN S   807                                                      
REMARK 465     GLY S   808                                                      
REMARK 465     SER S   809                                                      
REMARK 465     ARG S   810                                                      
REMARK 465     ASN S   811                                                      
REMARK 465     GLN S   824                                                      
REMARK 465     VAL S   825                                                      
REMARK 465     ASN S   826                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  15    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  29    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  87    CG   OD1  ND2                                       
REMARK 470     LYS A 106    CD   CE   NZ                                        
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     ARG A 117    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 133    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 136    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 137    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 156    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 157    CD   CE   NZ                                        
REMARK 470     LYS A 311    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 347   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ARG A 347   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP S 823   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 100       75.43   -100.76                                   
REMARK 500    ARG A 238      -10.72     79.28                                   
REMARK 500    ASN A 246       73.96   -153.19                                   
REMARK 500    TYR A 276       -8.71     73.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A1350  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 199   NE2                                                    
REMARK 620 2 ASP A 201   OD2 104.0                                              
REMARK 620 3 HIS A 279   NE2  85.8  88.0                                        
REMARK 620 4 OGA A1351   O2  163.5  92.4  96.8                                  
REMARK 620 5 OGA A1351   O2'  86.4 168.8  97.0  77.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 1350                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1352                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1353                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OGA A 1351                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1D7G   RELATED DB: PDB                                   
REMARK 900 A MODEL FOR THE COMPLEX BETWEEN THE HYPOXIA-INDUCIBLE FACTOR-1 (HIF- 
REMARK 900 1) AND ITS CONSENSUS DEOXYRIBONUCLEIC ACID SEQUENCE                  
REMARK 900 RELATED ID: 1H2L   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT   
REMARK 900 PEPTIDE                                                              
REMARK 900 RELATED ID: 1H2M   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT   
REMARK 900 PEPTIDE                                                              
REMARK 900 RELATED ID: 1H2N   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA FRAGMENT   
REMARK 900 PEPTIDE                                                              
REMARK 900 RELATED ID: 1L8C   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL BASIS FOR HIF-1ALPHA/CBP RECOGNITION IN THECELLULAR       
REMARK 900 HYPOXIC RESPONSE                                                     
REMARK 900 RELATED ID: 1LM8   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF A HIF-1A-PVHL-ELONGINB- ELONGINC COMPLEX                
REMARK 900 RELATED ID: 1LQB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A HYDROXYLATED HIF-1 ALPHA PEPTIDEBOUND TO THE  
REMARK 900 PVHL/ELONGIN-C/ ELONGIN-B COMPLEX                                    
DBREF  1H2K A    1   349  UNP    Q969Q7   Q969Q7           1    349             
DBREF  1H2K S  786   826  UNP    Q16665   HIFA_HUMAN     786    826             
SEQRES   1 A  349  MET ALA ALA THR ALA ALA GLU ALA VAL ALA SER GLY SER          
SEQRES   2 A  349  GLY GLU PRO ARG GLU GLU ALA GLY ALA LEU GLY PRO ALA          
SEQRES   3 A  349  TRP ASP GLU SER GLN LEU ARG SER TYR SER PHE PRO THR          
SEQRES   4 A  349  ARG PRO ILE PRO ARG LEU SER GLN SER ASP PRO ARG ALA          
SEQRES   5 A  349  GLU GLU LEU ILE GLU ASN GLU GLU PRO VAL VAL LEU THR          
SEQRES   6 A  349  ASP THR ASN LEU VAL TYR PRO ALA LEU LYS TRP ASP LEU          
SEQRES   7 A  349  GLU TYR LEU GLN GLU ASN ILE GLY ASN GLY ASP PHE SER          
SEQRES   8 A  349  VAL TYR SER ALA SER THR HIS LYS PHE LEU TYR TYR ASP          
SEQRES   9 A  349  GLU LYS LYS MET ALA ASN PHE GLN ASN PHE LYS PRO ARG          
SEQRES  10 A  349  SER ASN ARG GLU GLU MET LYS PHE HIS GLU PHE VAL GLU          
SEQRES  11 A  349  LYS LEU GLN ASP ILE GLN GLN ARG GLY GLY GLU GLU ARG          
SEQRES  12 A  349  LEU TYR LEU GLN GLN THR LEU ASN ASP THR VAL GLY ARG          
SEQRES  13 A  349  LYS ILE VAL MET ASP PHE LEU GLY PHE ASN TRP ASN TRP          
SEQRES  14 A  349  ILE ASN LYS GLN GLN GLY LYS ARG GLY TRP GLY GLN LEU          
SEQRES  15 A  349  THR SER ASN LEU LEU LEU ILE GLY MET GLU GLY ASN VAL          
SEQRES  16 A  349  THR PRO ALA HIS TYR ASP GLU GLN GLN ASN PHE PHE ALA          
SEQRES  17 A  349  GLN ILE LYS GLY TYR LYS ARG CYS ILE LEU PHE PRO PRO          
SEQRES  18 A  349  ASP GLN PHE GLU CYS LEU TYR PRO TYR PRO VAL HIS HIS          
SEQRES  19 A  349  PRO CYS ASP ARG GLN SER GLN VAL ASP PHE ASP ASN PRO          
SEQRES  20 A  349  ASP TYR GLU ARG PHE PRO ASN PHE GLN ASN VAL VAL GLY          
SEQRES  21 A  349  TYR GLU THR VAL VAL GLY PRO GLY ASP VAL LEU TYR ILE          
SEQRES  22 A  349  PRO MET TYR TRP TRP HIS HIS ILE GLU SER LEU LEU ASN          
SEQRES  23 A  349  GLY GLY ILE THR ILE THR VAL ASN PHE TRP TYR LYS GLY          
SEQRES  24 A  349  ALA PRO THR PRO LYS ARG ILE GLU TYR PRO LEU LYS ALA          
SEQRES  25 A  349  HIS GLN LYS VAL ALA ILE MET ARG ASN ILE GLU LYS MET          
SEQRES  26 A  349  LEU GLY GLU ALA LEU GLY ASN PRO GLN GLU VAL GLY PRO          
SEQRES  27 A  349  LEU LEU ASN THR MET ILE LYS GLY ARG TYR ASN                  
SEQRES   1 S   41  SER MET ASP GLU SER GLY LEU PRO GLN LEU THR SER TYR          
SEQRES   2 S   41  ASP CYS GLU VAL ASN ALA PRO ILE GLN GLY SER ARG ASN          
SEQRES   3 S   41  LEU LEU GLN GLY GLU GLU LEU LEU ARG ALA LEU ASP GLN          
SEQRES   4 S   41  VAL ASN                                                      
HET    FE2  A1350       1                                                       
HET    OGA  A1351      10                                                       
HET    SO4  A1352       5                                                       
HET    SO4  A1353       5                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM     OGA N-OXALYLGLYCINE                                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  FE2    FE 2+                                                        
FORMUL   4  OGA    C4 H5 N O5                                                   
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   7  HOH   *194(H2 O)                                                    
HELIX    1   1 ASP A   28  LEU A   32  5                                   5    
HELIX    2   2 ASP A   49  ASN A   58  1                                  10    
HELIX    3   3 VAL A   70  TRP A   76  5                                   7    
HELIX    4   4 ASP A   77  ILE A   85  1                                   9    
HELIX    5   5 ASP A  104  GLN A  112  5                                   9    
HELIX    6   6 LYS A  124  ARG A  138  1                                  15    
HELIX    7   7 GLY A  155  GLY A  164  1                                  10    
HELIX    8   8 ASN A  166  GLY A  178  1                                  13    
HELIX    9   9 PRO A  220  ASP A  222  5                                   3    
HELIX   10  10 GLN A  223  TYR A  228  1                                   6    
HELIX   11  11 PHE A  252  VAL A  258  5                                   7    
HELIX   12  12 LYS A  311  GLY A  331  1                                  21    
HELIX   13  13 ASN A  332  GLN A  334  5                                   3    
HELIX   14  14 GLU A  335  LYS A  345  1                                  11    
HELIX   15  15 GLN S  814  ASP S  823  1                                  10    
SHEET    1  AA 5 THR A  39  PRO A  41  0                                        
SHEET    2  AA 5 GLY A 260  VAL A 265  1  O  GLY A 260   N  ARG A  40           
SHEET    3  AA 5 LYS A 214  PHE A 219 -1  O  LYS A 214   N  VAL A 265           
SHEET    4  AA 5 TRP A 278  SER A 283 -1  O  TRP A 278   N  PHE A 219           
SHEET    5  AA 5 VAL A 195  HIS A 199 -1  O  THR A 196   N  ILE A 281           
SHEET    1  AB 6 ARG A  44  LEU A  45  0                                        
SHEET    2  AB 6 VAL A  62  LEU A  64  1  O  VAL A  63   N  LEU A  45           
SHEET    3  AB 6 VAL A 270  ILE A 273 -1  O  VAL A 270   N  LEU A  64           
SHEET    4  AB 6 GLN A 203  LYS A 211 -1  O  ASN A 205   N  ILE A 273           
SHEET    5  AB 6 THR A 290  LYS A 298 -1  O  ILE A 291   N  ILE A 210           
SHEET    6  AB 6 LEU A 182  SER A 184 -1  N  THR A 183   O  TRP A 296           
SHEET    1  AC 9 ARG A  44  LEU A  45  0                                        
SHEET    2  AC 9 VAL A  62  LEU A  64  1  O  VAL A  63   N  LEU A  45           
SHEET    3  AC 9 VAL A 270  ILE A 273 -1  O  VAL A 270   N  LEU A  64           
SHEET    4  AC 9 GLN A 203  LYS A 211 -1  O  ASN A 205   N  ILE A 273           
SHEET    5  AC 9 THR A 290  LYS A 298 -1  O  ILE A 291   N  ILE A 210           
SHEET    6  AC 9 LEU A 186  GLY A 190 -1  O  LEU A 186   N  ASN A 294           
SHEET    7  AC 9 ARG A 143  THR A 149 -1  O  LEU A 146   N  ILE A 189           
SHEET    8  AC 9 PHE A  90  ALA A  95 -1  O  SER A  91   N  GLN A 147           
SHEET    9  AC 9 SER A 118  MET A 123 -1  O  ASN A 119   N  SER A  94           
LINK        FE   FE2 A1350                 NE2 HIS A 199     1555   1555  2.12  
LINK        FE   FE2 A1350                 OD2 ASP A 201     1555   1555  2.05  
LINK        FE   FE2 A1350                 NE2 HIS A 279     1555   1555  2.08  
LINK        FE   FE2 A1350                 O2  OGA A1351     1555   1555  2.13  
LINK        FE   FE2 A1350                 O2' OGA A1351     1555   1555  2.17  
CISPEP   1 TYR A  308    PRO A  309          0        -1.09                     
SITE     1 AC1  4 HIS A 199  ASP A 201  HIS A 279  OGA A1351                    
SITE     1 AC2  4 ARG A 138  GLY A 140  GLU A 141  GLU A 142                    
SITE     1 AC3  5 ARG A 143  GLU A 192  GLY A 193  LEU A 285                    
SITE     2 AC3  5 ASN A 286                                                     
SITE     1 AC4 12 TYR A 145  THR A 196  HIS A 199  ASP A 201                    
SITE     2 AC4 12 ASN A 205  PHE A 207  LYS A 214  HIS A 279                    
SITE     3 AC4 12 ILE A 281  ASN A 294  TRP A 296  FE2 A1350                    
CRYST1   86.161   86.161  146.656  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011606  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011606  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006819        0.00000                         
ATOM      1  N   GLU A  15       8.429  32.653   9.844  1.00 50.99           N  
ATOM      2  CA  GLU A  15       7.077  32.034   9.723  1.00 51.05           C  
ATOM      3  C   GLU A  15       7.166  30.582  10.163  1.00 50.79           C  
ATOM      4  O   GLU A  15       8.052  29.857   9.730  1.00 51.18           O  
ATOM      5  CB  GLU A  15       6.570  32.124   8.296  1.00 51.20           C  
ATOM      6  N   PRO A  16       6.254  30.150  11.022  1.00 50.50           N  
ATOM      7  CA  PRO A  16       6.301  28.781  11.549  1.00 50.12           C  
ATOM      8  C   PRO A  16       6.265  27.737  10.438  1.00 49.56           C  
ATOM      9  O   PRO A  16       5.471  27.827   9.503  1.00 49.32           O  
ATOM     10  CB  PRO A  16       5.049  28.701  12.429  1.00 50.27           C  
ATOM     11  CG  PRO A  16       4.734  30.135  12.770  1.00 50.58           C  
ATOM     12  CD  PRO A  16       5.108  30.911  11.548  1.00 50.56           C  
ATOM     13  N   ARG A  17       7.133  26.746  10.550  1.00 48.83           N  
ATOM     14  CA  ARG A  17       7.219  25.695   9.550  1.00 48.33           C  
ATOM     15  C   ARG A  17       5.967  24.832   9.561  1.00 47.48           C  
ATOM     16  O   ARG A  17       5.245  24.782  10.557  1.00 47.64           O  
ATOM     17  CB  ARG A  17       8.421  24.798   9.835  1.00 48.61           C  
ATOM     18  CG  ARG A  17       9.776  25.511   9.835  1.00 49.21           C  
ATOM     19  CD  ARG A  17      10.944  24.577  10.196  1.00 49.84           C  
ATOM     20  NE  ARG A  17      10.918  24.137  11.596  1.00 50.12           N  
ATOM     21  CZ  ARG A  17      11.455  24.809  12.623  1.00 50.99           C  
ATOM     22  NH1 ARG A  17      12.065  25.979  12.431  1.00 50.40           N  
ATOM     23  NH2 ARG A  17      11.381  24.310  13.857  1.00 50.81           N  
ATOM     24  N   GLU A  18       5.723  24.153   8.446  1.00 46.05           N  
ATOM     25  CA  GLU A  18       4.603  23.246   8.329  1.00 45.06           C  
ATOM     26  C   GLU A  18       5.096  21.830   8.607  1.00 44.00           C  
ATOM     27  O   GLU A  18       6.101  21.405   8.044  1.00 43.89           O  
ATOM     28  CB  GLU A  18       4.013  23.324   6.923  1.00 45.21           C  
ATOM     29  CG  GLU A  18       3.323  24.648   6.621  1.00 45.56           C  
ATOM     30  CD  GLU A  18       1.951  24.780   7.265  1.00 45.64           C  
ATOM     31  OE1 GLU A  18       1.342  23.749   7.641  1.00 44.14           O  
ATOM     32  OE2 GLU A  18       1.480  25.932   7.388  1.00 45.83           O  
ATOM     33  N   GLU A  19       4.396  21.113   9.484  1.00 42.49           N  
ATOM     34  CA  GLU A  19       4.734  19.728   9.795  1.00 41.55           C  
ATOM     35  C   GLU A  19       4.357  18.817   8.635  1.00 39.79           C  
ATOM     36  O   GLU A  19       3.266  18.933   8.066  1.00 39.13           O  
ATOM     37  CB  GLU A  19       4.010  19.256  11.052  1.00 41.88           C  
ATOM     38  CG  GLU A  19       4.420  19.997  12.311  1.00 44.80           C  
ATOM     39  CD  GLU A  19       4.276  19.155  13.574  1.00 49.28           C  
ATOM     40  OE1 GLU A  19       3.759  18.008  13.497  1.00 51.52           O  
ATOM     41  OE2 GLU A  19       4.695  19.643  14.656  1.00 52.76           O  
ATOM     42  N   ALA A  20       5.270  17.910   8.311  1.00 38.00           N  
ATOM     43  CA  ALA A  20       5.099  16.952   7.227  1.00 36.77           C  
ATOM     44  C   ALA A  20       3.803  16.168   7.373  1.00 35.56           C  
ATOM     45  O   ALA A  20       3.445  15.734   8.460  1.00 35.74           O  
ATOM     46  CB  ALA A  20       6.283  15.999   7.180  1.00 36.63           C  
ATOM     47  N   GLY A  21       3.082  16.020   6.279  1.00 34.05           N  
ATOM     48  CA  GLY A  21       1.860  15.242   6.307  1.00 33.24           C  
ATOM     49  C   GLY A  21       0.666  16.137   6.551  1.00 32.36           C  
ATOM     50  O   GLY A  21      -0.393  15.673   6.951  1.00 30.93           O  
ATOM     51  N   ALA A  22       0.867  17.432   6.323  1.00 32.41           N  
ATOM     52  CA  ALA A  22      -0.184  18.425   6.459  1.00 32.78           C  
ATOM     53  C   ALA A  22      -0.723  18.441   7.873  1.00 33.14           C  
ATOM     54  O   ALA A  22      -1.915  18.605   8.088  1.00 32.74           O  
ATOM     55  CB  ALA A  22      -1.304  18.139   5.462  1.00 32.61           C  
ATOM     56  N   LEU A  23       0.151  18.253   8.849  1.00 34.01           N  
ATOM     57  CA  LEU A  23      -0.297  18.275  10.232  1.00 34.91           C  
ATOM     58  C   LEU A  23      -0.342  19.694  10.757  1.00 35.27           C  
ATOM     59  O   LEU A  23      -0.528  19.918  11.943  1.00 35.72           O  
ATOM     60  CB  LEU A  23       0.565  17.366  11.097  1.00 35.27           C  
ATOM     61  CG  LEU A  23       0.384  15.910  10.653  1.00 36.36           C  
ATOM     62  CD1 LEU A  23       1.211  14.947  11.491  1.00 37.75           C  
ATOM     63  CD2 LEU A  23      -1.077  15.523  10.719  1.00 37.98           C  
ATOM     64  N   GLY A  24      -0.177  20.656   9.855  1.00 35.73           N  
ATOM     65  CA  GLY A  24      -0.332  22.053  10.194  1.00 35.66           C  
ATOM     66  C   GLY A  24       0.901  22.655  10.804  1.00 36.08           C  
ATOM     67  O   GLY A  24       1.945  22.001  10.913  1.00 36.05           O  
ATOM     68  N   PRO A  25       0.764  23.894  11.253  1.00 35.96           N  
ATOM     69  CA  PRO A  25       1.896  24.628  11.804  1.00 36.12           C  
ATOM     70  C   PRO A  25       2.327  23.980  13.108  1.00 36.32           C  
ATOM     71  O   PRO A  25       1.488  23.577  13.914  1.00 36.08           O  
ATOM     72  CB  PRO A  25       1.341  26.047  12.043  1.00 36.15           C  
ATOM     73  CG  PRO A  25      -0.162  25.942  11.982  1.00 35.84           C  
ATOM     74  CD  PRO A  25      -0.504  24.638  11.350  1.00 36.22           C  
ATOM     75  N   ALA A  26       3.632  23.848  13.285  1.00 36.64           N  
ATOM     76  CA  ALA A  26       4.178  23.274  14.499  1.00 37.19           C  
ATOM     77  C   ALA A  26       3.860  24.172  15.706  1.00 36.77           C  
ATOM     78  O   ALA A  26       3.595  23.678  16.808  1.00 37.19           O  
ATOM     79  CB  ALA A  26       5.672  23.099  14.347  1.00 37.52           C  
ATOM     80  N   TRP A  27       3.848  25.479  15.484  1.00 35.62           N  
ATOM     81  CA  TRP A  27       3.520  26.420  16.543  1.00 35.04           C  
ATOM     82  C   TRP A  27       3.029  27.729  15.933  1.00 34.20           C  
ATOM     83  O   TRP A  27       2.992  27.883  14.723  1.00 33.57           O  
ATOM     84  CB  TRP A  27       4.774  26.672  17.382  1.00 35.28           C  
ATOM     85  CG  TRP A  27       5.951  26.889  16.511  1.00 34.67           C  
ATOM     86  CD1 TRP A  27       6.761  25.930  15.955  1.00 35.52           C  
ATOM     87  CD2 TRP A  27       6.426  28.135  16.033  1.00 34.40           C  
ATOM     88  NE1 TRP A  27       7.723  26.522  15.172  1.00 35.09           N  
ATOM     89  CE2 TRP A  27       7.541  27.877  15.209  1.00 34.23           C  
ATOM     90  CE3 TRP A  27       6.038  29.452  16.232  1.00 34.31           C  
ATOM     91  CZ2 TRP A  27       8.255  28.879  14.592  1.00 35.79           C  
ATOM     92  CZ3 TRP A  27       6.750  30.442  15.629  1.00 36.35           C  
ATOM     93  CH2 TRP A  27       7.847  30.154  14.808  1.00 36.47           C  
ATOM     94  N   ASP A  28       2.638  28.672  16.766  1.00 33.77           N  
ATOM     95  CA  ASP A  28       2.259  29.970  16.249  1.00 33.48           C  
ATOM     96  C   ASP A  28       2.759  31.050  17.165  1.00 32.26           C  
ATOM     97  O   ASP A  28       3.210  30.791  18.276  1.00 32.05           O  
ATOM     98  CB  ASP A  28       0.749  30.080  16.037  1.00 34.30           C  
ATOM     99  CG  ASP A  28      -0.026  29.986  17.317  1.00 36.29           C  
ATOM    100  OD1 ASP A  28      -0.184  31.027  18.002  1.00 39.59           O  
ATOM    101  OD2 ASP A  28      -0.517  28.906  17.712  1.00 39.78           O  
ATOM    102  N   GLU A  29       2.691  32.268  16.654  1.00 31.30           N  
ATOM    103  CA  GLU A  29       3.181  33.465  17.326  1.00 30.15           C  
ATOM    104  C   GLU A  29       2.674  33.625  18.752  1.00 28.85           C  
ATOM    105  O   GLU A  29       3.407  34.036  19.621  1.00 28.58           O  
ATOM    106  CB  GLU A  29       2.791  34.682  16.503  1.00 30.32           C  
ATOM    107  N   SER A  30       1.414  33.313  18.992  1.00 27.95           N  
ATOM    108  CA  SER A  30       0.845  33.501  20.320  1.00 27.46           C  
ATOM    109  C   SER A  30       1.537  32.671  21.389  1.00 26.93           C  
ATOM    110  O   SER A  30       1.312  32.907  22.567  1.00 26.79           O  
ATOM    111  CB  SER A  30      -0.651  33.168  20.322  1.00 27.23           C  
ATOM    112  OG  SER A  30      -0.857  31.764  20.306  1.00 27.69           O  
ATOM    113  N   GLN A  31       2.360  31.703  20.984  1.00 26.55           N  
ATOM    114  CA  GLN A  31       3.071  30.837  21.926  1.00 26.63           C  
ATOM    115  C   GLN A  31       4.419  31.409  22.334  1.00 26.66           C  
ATOM    116  O   GLN A  31       5.078  30.855  23.205  1.00 26.45           O  
ATOM    117  CB  GLN A  31       3.282  29.426  21.349  1.00 26.41           C  
ATOM    118  CG  GLN A  31       1.998  28.637  21.131  1.00 26.28           C  
ATOM    119  CD  GLN A  31       2.245  27.287  20.489  1.00 26.25           C  
ATOM    120  OE1 GLN A  31       2.258  27.183  19.271  1.00 27.92           O  
ATOM    121  NE2 GLN A  31       2.465  26.258  21.305  1.00 24.36           N  
ATOM    122  N   LEU A  32       4.824  32.508  21.703  1.00 26.89           N  
ATOM    123  CA  LEU A  32       6.083  33.176  22.029  1.00 27.24           C  
ATOM    124  C   LEU A  32       5.852  34.321  23.006  1.00 26.92           C  
ATOM    125  O   LEU A  32       4.888  35.047  22.868  1.00 26.42           O  
ATOM    126  CB  LEU A  32       6.717  33.746  20.760  1.00 27.46           C  
ATOM    127  CG  LEU A  32       6.964  32.728  19.640  1.00 28.65           C  
ATOM    128  CD1 LEU A  32       7.630  33.391  18.452  1.00 29.44           C  
ATOM    129  CD2 LEU A  32       7.792  31.573  20.127  1.00 27.98           C  
ATOM    130  N   ARG A  33       6.728  34.472  23.995  1.00 26.71           N  
ATOM    131  CA  ARG A  33       6.627  35.596  24.923  1.00 26.77           C  
ATOM    132  C   ARG A  33       7.040  36.880  24.209  1.00 26.57           C  
ATOM    133  O   ARG A  33       7.719  36.844  23.203  1.00 26.30           O  
ATOM    134  CB  ARG A  33       7.492  35.357  26.163  1.00 26.67           C  
ATOM    135  CG  ARG A  33       7.052  34.141  26.983  1.00 26.29           C  
ATOM    136  CD  ARG A  33       7.937  33.837  28.181  1.00 25.85           C  
ATOM    137  NE  ARG A  33       7.381  32.778  29.018  1.00 25.80           N  
ATOM    138  CZ  ARG A  33       6.451  32.946  29.945  1.00 24.68           C  
ATOM    139  NH1 ARG A  33       5.937  34.140  30.189  1.00 23.50           N  
ATOM    140  NH2 ARG A  33       6.029  31.901  30.637  1.00 25.35           N  
ATOM    141  N   SER A  34       6.633  38.020  24.732  1.00 26.80           N  
ATOM    142  CA  SER A  34       6.903  39.280  24.061  1.00 27.15           C  
ATOM    143  C   SER A  34       7.990  40.048  24.791  1.00 26.39           C  
ATOM    144  O   SER A  34       7.964  40.140  26.005  1.00 25.87           O  
ATOM    145  CB  SER A  34       5.628  40.104  24.030  1.00 27.68           C  
ATOM    146  OG  SER A  34       5.494  40.737  25.285  1.00 32.47           O  
ATOM    147  N   TYR A  35       8.944  40.589  24.042  1.00 25.89           N  
ATOM    148  CA  TYR A  35      10.110  41.223  24.637  1.00 26.28           C  
ATOM    149  C   TYR A  35      10.353  42.558  23.970  1.00 26.85           C  
ATOM    150  O   TYR A  35       9.722  42.856  22.967  1.00 26.92           O  
ATOM    151  CB  TYR A  35      11.326  40.308  24.510  1.00 25.90           C  
ATOM    152  CG  TYR A  35      11.169  39.032  25.309  1.00 25.33           C  
ATOM    153  CD1 TYR A  35      10.975  39.073  26.685  1.00 24.99           C  
ATOM    154  CD2 TYR A  35      11.198  37.787  24.692  1.00 23.82           C  
ATOM    155  CE1 TYR A  35      10.823  37.898  27.429  1.00 24.56           C  
ATOM    156  CE2 TYR A  35      11.046  36.620  25.426  1.00 24.42           C  
ATOM    157  CZ  TYR A  35      10.862  36.682  26.793  1.00 23.48           C  
ATOM    158  OH  TYR A  35      10.696  35.524  27.513  1.00 24.75           O  
ATOM    159  N   SER A  36      11.304  43.327  24.496  1.00 27.27           N  
ATOM    160  CA  SER A  36      11.525  44.704  24.052  1.00 27.55           C  
ATOM    161  C   SER A  36      12.513  44.912  22.917  1.00 27.06           C  
ATOM    162  O   SER A  36      12.734  46.049  22.504  1.00 27.94           O  
ATOM    163  CB  SER A  36      12.082  45.498  25.226  1.00 27.88           C  
ATOM    164  OG  SER A  36      13.350  44.976  25.590  1.00 28.36           O  
ATOM    165  N   PHE A  37      13.128  43.851  22.429  1.00 25.35           N  
ATOM    166  CA  PHE A  37      14.202  44.014  21.461  1.00 24.62           C  
ATOM    167  C   PHE A  37      13.899  43.272  20.159  1.00 24.75           C  
ATOM    168  O   PHE A  37      13.130  42.335  20.135  1.00 24.25           O  
ATOM    169  CB  PHE A  37      15.487  43.462  22.071  1.00 23.87           C  
ATOM    170  CG  PHE A  37      15.318  42.069  22.635  1.00 22.53           C  
ATOM    171  CD1 PHE A  37      15.348  40.972  21.802  1.00 21.11           C  
ATOM    172  CD2 PHE A  37      15.069  41.872  23.988  1.00 21.63           C  
ATOM    173  CE1 PHE A  37      15.158  39.687  22.314  1.00 22.41           C  
ATOM    174  CE2 PHE A  37      14.900  40.612  24.505  1.00 22.29           C  
ATOM    175  CZ  PHE A  37      14.936  39.509  23.675  1.00 21.45           C  
ATOM    176  N   PRO A  38      14.489  43.715  19.067  1.00 24.94           N  
ATOM    177  CA  PRO A  38      14.322  43.017  17.793  1.00 24.67           C  
ATOM    178  C   PRO A  38      15.267  41.823  17.678  1.00 24.41           C  
ATOM    179  O   PRO A  38      16.249  41.745  18.427  1.00 23.73           O  
ATOM    180  CB  PRO A  38      14.725  44.072  16.783  1.00 24.75           C  
ATOM    181  CG  PRO A  38      15.791  44.872  17.530  1.00 26.09           C  
ATOM    182  CD  PRO A  38      15.287  44.950  18.941  1.00 25.27           C  
ATOM    183  N   THR A  39      14.981  40.927  16.734  1.00 23.30           N  
ATOM    184  CA  THR A  39      15.859  39.816  16.444  1.00 23.42           C  
ATOM    185  C   THR A  39      15.857  39.534  14.955  1.00 24.29           C  
ATOM    186  O   THR A  39      14.958  39.964  14.239  1.00 24.61           O  
ATOM    187  CB  THR A  39      15.368  38.538  17.135  1.00 23.09           C  
ATOM    188  OG1 THR A  39      14.044  38.232  16.680  1.00 19.92           O  
ATOM    189  CG2 THR A  39      15.213  38.731  18.641  1.00 23.03           C  
ATOM    190  N   ARG A  40      16.854  38.773  14.525  1.00 24.43           N  
ATOM    191  CA  ARG A  40      16.982  38.273  13.170  1.00 24.91           C  
ATOM    192  C   ARG A  40      17.061  36.751  13.268  1.00 24.49           C  
ATOM    193  O   ARG A  40      17.434  36.225  14.301  1.00 23.58           O  
ATOM    194  CB  ARG A  40      18.253  38.805  12.536  1.00 25.36           C  
ATOM    195  CG  ARG A  40      18.208  40.281  12.248  1.00 30.74           C  
ATOM    196  CD  ARG A  40      16.823  40.775  11.890  1.00 34.86           C  
ATOM    197  NE  ARG A  40      16.604  40.989  10.477  1.00 39.38           N  
ATOM    198  CZ  ARG A  40      15.403  41.229   9.971  1.00 43.86           C  
ATOM    199  NH1 ARG A  40      14.345  41.254  10.782  1.00 45.88           N  
ATOM    200  NH2 ARG A  40      15.252  41.457   8.674  1.00 44.96           N  
ATOM    201  N   PRO A  41      16.687  36.031  12.221  1.00 25.08           N  
ATOM    202  CA  PRO A  41      16.715  34.565  12.290  1.00 25.39           C  
ATOM    203  C   PRO A  41      18.095  33.913  12.282  1.00 25.10           C  
ATOM    204  O   PRO A  41      19.007  34.370  11.636  1.00 25.16           O  
ATOM    205  CB  PRO A  41      15.953  34.130  11.023  1.00 25.76           C  
ATOM    206  CG  PRO A  41      15.286  35.392  10.504  1.00 26.54           C  
ATOM    207  CD  PRO A  41      16.151  36.524  10.939  1.00 24.85           C  
ATOM    208  N   ILE A  42      18.225  32.823  13.020  1.00 25.28           N  
ATOM    209  CA  ILE A  42      19.388  31.974  12.919  1.00 24.31           C  
ATOM    210  C   ILE A  42      19.147  31.116  11.677  1.00 24.68           C  
ATOM    211  O   ILE A  42      18.043  30.614  11.466  1.00 24.72           O  
ATOM    212  CB  ILE A  42      19.481  31.104  14.163  1.00 24.80           C  
ATOM    213  CG1 ILE A  42      19.763  31.993  15.384  1.00 24.24           C  
ATOM    214  CG2 ILE A  42      20.530  30.004  13.961  1.00 23.81           C  
ATOM    215  CD1 ILE A  42      19.531  31.325  16.729  1.00 23.59           C  
ATOM    216  N   PRO A  43      20.146  30.953  10.826  1.00 24.48           N  
ATOM    217  CA  PRO A  43      19.963  30.108   9.651  1.00 24.60           C  
ATOM    218  C   PRO A  43      19.611  28.650  10.001  1.00 24.85           C  
ATOM    219  O   PRO A  43      20.148  28.130  10.989  1.00 24.38           O  
ATOM    220  CB  PRO A  43      21.320  30.192   8.937  1.00 24.87           C  
ATOM    221  CG  PRO A  43      22.040  31.372   9.541  1.00 25.04           C  
ATOM    222  CD  PRO A  43      21.475  31.583  10.886  1.00 24.37           C  
ATOM    223  N   ARG A  44      18.686  28.032   9.248  1.00 24.70           N  
ATOM    224  CA  ARG A  44      18.367  26.608   9.391  1.00 25.53           C  
ATOM    225  C   ARG A  44      18.910  25.943   8.152  1.00 25.00           C  
ATOM    226  O   ARG A  44      18.505  26.265   7.030  1.00 24.62           O  
ATOM    227  CB  ARG A  44      16.873  26.287   9.452  1.00 26.51           C  
ATOM    228  CG  ARG A  44      16.044  27.133  10.378  1.00 29.49           C  
ATOM    229  CD  ARG A  44      14.683  26.485  10.813  1.00 31.03           C  
ATOM    230  NE  ARG A  44      14.401  25.120  10.323  1.00 32.36           N  
ATOM    231  CZ  ARG A  44      14.174  24.057  11.126  1.00 33.85           C  
ATOM    232  NH1 ARG A  44      14.239  24.170  12.451  1.00 30.71           N  
ATOM    233  NH2 ARG A  44      13.898  22.863  10.613  1.00 35.56           N  
ATOM    234  N   LEU A  45      19.815  25.006   8.337  1.00 23.91           N  
ATOM    235  CA  LEU A  45      20.500  24.444   7.202  1.00 23.40           C  
ATOM    236  C   LEU A  45      20.684  22.967   7.352  1.00 23.52           C  
ATOM    237  O   LEU A  45      20.559  22.423   8.446  1.00 22.50           O  
ATOM    238  CB  LEU A  45      21.888  25.064   7.093  1.00 22.62           C  
ATOM    239  CG  LEU A  45      21.911  26.563   6.819  1.00 23.96           C  
ATOM    240  CD1 LEU A  45      23.317  27.111   6.947  1.00 24.52           C  
ATOM    241  CD2 LEU A  45      21.366  26.845   5.423  1.00 24.63           C  
ATOM    242  N   SER A  46      21.018  22.347   6.227  1.00 23.57           N  
ATOM    243  CA  SER A  46      21.382  20.975   6.221  1.00 24.12           C  
ATOM    244  C   SER A  46      22.820  20.888   6.668  1.00 24.81           C  
ATOM    245  O   SER A  46      23.640  21.757   6.398  1.00 23.76           O  
ATOM    246  CB  SER A  46      21.236  20.354   4.830  1.00 23.80           C  
ATOM    247  OG  SER A  46      21.744  19.020   4.830  1.00 24.09           O  
ATOM    248  N   GLN A  47      23.089  19.804   7.366  1.00 25.92           N  
ATOM    249  CA  GLN A  47      24.399  19.444   7.844  1.00 27.25           C  
ATOM    250  C   GLN A  47      25.379  19.326   6.674  1.00 27.54           C  
ATOM    251  O   GLN A  47      26.563  19.564   6.836  1.00 27.97           O  
ATOM    252  CB  GLN A  47      24.245  18.088   8.554  1.00 28.46           C  
ATOM    253  CG  GLN A  47      25.487  17.279   8.705  1.00 31.10           C  
ATOM    254  CD  GLN A  47      25.776  16.372   7.570  1.00 33.17           C  
ATOM    255  OE1 GLN A  47      24.881  15.970   6.803  1.00 36.23           O  
ATOM    256  NE2 GLN A  47      27.041  16.000   7.458  1.00 36.17           N  
ATOM    257  N   SER A  48      24.884  18.951   5.498  1.00 27.72           N  
ATOM    258  CA  SER A  48      25.736  18.809   4.323  1.00 28.35           C  
ATOM    259  C   SER A  48      26.016  20.150   3.629  1.00 28.86           C  
ATOM    260  O   SER A  48      26.825  20.235   2.711  1.00 28.96           O  
ATOM    261  CB  SER A  48      25.092  17.839   3.324  1.00 28.65           C  
ATOM    262  OG  SER A  48      23.798  18.276   2.918  1.00 28.51           O  
ATOM    263  N   ASP A  49      25.347  21.203   4.065  1.00 29.16           N  
ATOM    264  CA  ASP A  49      25.515  22.496   3.442  1.00 29.28           C  
ATOM    265  C   ASP A  49      26.800  23.163   3.913  1.00 29.71           C  
ATOM    266  O   ASP A  49      26.981  23.398   5.101  1.00 29.02           O  
ATOM    267  CB  ASP A  49      24.325  23.369   3.783  1.00 29.35           C  
ATOM    268  CG  ASP A  49      24.316  24.667   3.010  1.00 29.93           C  
ATOM    269  OD1 ASP A  49      25.398  25.183   2.666  1.00 28.14           O  
ATOM    270  OD2 ASP A  49      23.259  25.247   2.731  1.00 30.49           O  
ATOM    271  N   PRO A  50      27.693  23.483   2.976  1.00 30.34           N  
ATOM    272  CA  PRO A  50      28.964  24.134   3.315  1.00 30.54           C  
ATOM    273  C   PRO A  50      28.783  25.354   4.186  1.00 30.38           C  
ATOM    274  O   PRO A  50      29.661  25.651   4.990  1.00 30.53           O  
ATOM    275  CB  PRO A  50      29.520  24.573   1.952  1.00 30.39           C  
ATOM    276  CG  PRO A  50      28.926  23.667   0.988  1.00 30.96           C  
ATOM    277  CD  PRO A  50      27.574  23.243   1.531  1.00 30.51           C  
ATOM    278  N   ARG A  51      27.683  26.072   4.008  1.00 30.50           N  
ATOM    279  CA  ARG A  51      27.439  27.253   4.817  1.00 30.94           C  
ATOM    280  C   ARG A  51      27.341  26.875   6.299  1.00 30.49           C  
ATOM    281  O   ARG A  51      27.744  27.646   7.161  1.00 29.74           O  
ATOM    282  CB  ARG A  51      26.171  27.979   4.370  1.00 30.97           C  
ATOM    283  CG  ARG A  51      26.337  28.781   3.099  1.00 33.47           C  
ATOM    284  CD  ARG A  51      25.029  29.321   2.521  1.00 34.80           C  
ATOM    285  NE  ARG A  51      24.071  28.252   2.221  1.00 36.68           N  
ATOM    286  CZ  ARG A  51      22.766  28.448   2.081  1.00 37.94           C  
ATOM    287  NH1 ARG A  51      22.260  29.677   2.208  1.00 39.10           N  
ATOM    288  NH2 ARG A  51      21.967  27.436   1.794  1.00 36.51           N  
ATOM    289  N   ALA A  52      26.831  25.684   6.596  1.00 30.03           N  
ATOM    290  CA  ALA A  52      26.697  25.288   7.993  1.00 29.96           C  
ATOM    291  C   ALA A  52      28.079  25.101   8.593  1.00 30.07           C  
ATOM    292  O   ALA A  52      28.345  25.518   9.710  1.00 29.00           O  
ATOM    293  CB  ALA A  52      25.901  24.028   8.119  1.00 29.81           C  
ATOM    294  N   GLU A  53      28.958  24.455   7.845  1.00 30.12           N  
ATOM    295  CA  GLU A  53      30.290  24.213   8.347  1.00 31.08           C  
ATOM    296  C   GLU A  53      30.999  25.550   8.579  1.00 30.37           C  
ATOM    297  O   GLU A  53      31.683  25.730   9.580  1.00 29.89           O  
ATOM    298  CB  GLU A  53      31.086  23.362   7.379  1.00 31.41           C  
ATOM    299  CG  GLU A  53      32.189  22.603   8.081  1.00 35.02           C  
ATOM    300  CD  GLU A  53      31.785  21.185   8.507  1.00 37.87           C  
ATOM    301  OE1 GLU A  53      30.614  20.929   8.887  1.00 39.16           O  
ATOM    302  OE2 GLU A  53      32.674  20.313   8.463  1.00 40.43           O  
ATOM    303  N   GLU A  54      30.811  26.479   7.652  1.00 29.84           N  
ATOM    304  CA  GLU A  54      31.413  27.796   7.757  1.00 30.22           C  
ATOM    305  C   GLU A  54      30.975  28.486   9.045  1.00 29.05           C  
ATOM    306  O   GLU A  54      31.780  29.102   9.719  1.00 28.03           O  
ATOM    307  CB  GLU A  54      31.026  28.680   6.573  1.00 30.53           C  
ATOM    308  CG  GLU A  54      31.635  28.276   5.243  1.00 34.66           C  
ATOM    309  CD  GLU A  54      30.993  29.002   4.058  1.00 38.49           C  
ATOM    310  OE1 GLU A  54      30.651  30.208   4.214  1.00 42.20           O  
ATOM    311  OE2 GLU A  54      30.829  28.368   2.975  1.00 41.54           O  
ATOM    312  N   LEU A  55      29.696  28.366   9.387  1.00 28.24           N  
ATOM    313  CA  LEU A  55      29.177  29.029  10.571  1.00 27.28           C  
ATOM    314  C   LEU A  55      29.774  28.448  11.827  1.00 26.43           C  
ATOM    315  O   LEU A  55      30.212  29.199  12.695  1.00 25.20           O  
ATOM    316  CB  LEU A  55      27.655  28.975  10.597  1.00 27.25           C  
ATOM    317  CG  LEU A  55      27.027  29.829   9.502  1.00 27.43           C  
ATOM    318  CD1 LEU A  55      25.568  29.452   9.322  1.00 28.83           C  
ATOM    319  CD2 LEU A  55      27.173  31.318   9.821  1.00 26.98           C  
ATOM    320  N   ILE A  56      29.829  27.116  11.915  1.00 25.75           N  
ATOM    321  CA  ILE A  56      30.382  26.473  13.107  1.00 25.50           C  
ATOM    322  C   ILE A  56      31.874  26.815  13.254  1.00 26.26           C  
ATOM    323  O   ILE A  56      32.346  27.134  14.349  1.00 25.55           O  
ATOM    324  CB  ILE A  56      30.192  24.955  13.059  1.00 25.63           C  
ATOM    325  CG1 ILE A  56      28.698  24.574  13.034  1.00 24.00           C  
ATOM    326  CG2 ILE A  56      30.848  24.321  14.263  1.00 25.48           C  
ATOM    327  CD1 ILE A  56      28.439  23.170  12.531  1.00 24.10           C  
ATOM    328  N   GLU A  57      32.597  26.781  12.135  1.00 27.04           N  
ATOM    329  CA  GLU A  57      34.023  27.082  12.107  1.00 28.01           C  
ATOM    330  C   GLU A  57      34.232  28.491  12.625  1.00 28.49           C  
ATOM    331  O   GLU A  57      35.183  28.770  13.344  1.00 28.92           O  
ATOM    332  CB  GLU A  57      34.561  26.977  10.676  1.00 28.61           C  
ATOM    333  CG  GLU A  57      36.053  27.224  10.509  1.00 30.77           C  
ATOM    334  CD  GLU A  57      36.902  26.322  11.394  1.00 35.15           C  
ATOM    335  OE1 GLU A  57      36.556  25.127  11.591  1.00 37.11           O  
ATOM    336  OE2 GLU A  57      37.924  26.818  11.909  1.00 40.88           O  
ATOM    337  N   ASN A  58      33.321  29.378  12.270  1.00 28.34           N  
ATOM    338  CA  ASN A  58      33.424  30.758  12.701  1.00 28.81           C  
ATOM    339  C   ASN A  58      32.770  31.079  14.025  1.00 27.23           C  
ATOM    340  O   ASN A  58      32.630  32.233  14.374  1.00 26.07           O  
ATOM    341  CB  ASN A  58      32.792  31.641  11.656  1.00 29.66           C  
ATOM    342  CG  ASN A  58      33.789  32.386  10.913  1.00 33.61           C  
ATOM    343  OD1 ASN A  58      34.280  31.901   9.893  1.00 38.81           O  
ATOM    344  ND2 ASN A  58      34.160  33.582  11.429  1.00 36.72           N  
ATOM    345  N   GLU A  59      32.343  30.053  14.735  1.00 26.39           N  
ATOM    346  CA  GLU A  59      31.712  30.241  16.030  1.00 26.36           C  
ATOM    347  C   GLU A  59      30.495  31.144  15.926  1.00 25.39           C  
ATOM    348  O   GLU A  59      30.325  32.100  16.668  1.00 24.14           O  
ATOM    349  CB  GLU A  59      32.753  30.697  17.059  1.00 26.80           C  
ATOM    350  CG  GLU A  59      33.717  29.537  17.316  1.00 29.10           C  
ATOM    351  CD  GLU A  59      34.722  29.791  18.407  1.00 32.85           C  
ATOM    352  OE1 GLU A  59      35.790  30.330  18.080  1.00 37.47           O  
ATOM    353  OE2 GLU A  59      34.466  29.432  19.572  1.00 34.14           O  
ATOM    354  N   GLU A  60      29.641  30.799  14.970  1.00 24.88           N  
ATOM    355  CA  GLU A  60      28.366  31.465  14.801  1.00 25.20           C  
ATOM    356  C   GLU A  60      27.262  30.414  14.822  1.00 24.07           C  
ATOM    357  O   GLU A  60      27.420  29.320  14.293  1.00 22.49           O  
ATOM    358  CB  GLU A  60      28.343  32.249  13.505  1.00 25.69           C  
ATOM    359  CG  GLU A  60      29.354  33.363  13.536  1.00 30.40           C  
ATOM    360  CD  GLU A  60      28.962  34.516  12.657  1.00 37.91           C  
ATOM    361  OE1 GLU A  60      29.009  34.377  11.414  1.00 38.24           O  
ATOM    362  OE2 GLU A  60      28.595  35.566  13.236  1.00 46.50           O  
ATOM    363  N   PRO A  61      26.124  30.779  15.386  1.00 22.90           N  
ATOM    364  CA  PRO A  61      25.045  29.816  15.571  1.00 22.19           C  
ATOM    365  C   PRO A  61      24.448  29.371  14.267  1.00 21.47           C  
ATOM    366  O   PRO A  61      24.419  30.104  13.266  1.00 20.48           O  
ATOM    367  CB  PRO A  61      23.996  30.583  16.368  1.00 22.29           C  
ATOM    368  CG  PRO A  61      24.315  32.053  16.148  1.00 22.67           C  
ATOM    369  CD  PRO A  61      25.764  32.140  15.798  1.00 22.92           C  
ATOM    370  N   VAL A  62      23.957  28.142  14.283  1.00 20.87           N  
ATOM    371  CA  VAL A  62      23.248  27.591  13.146  1.00 20.94           C  
ATOM    372  C   VAL A  62      22.353  26.475  13.655  1.00 21.15           C  
ATOM    373  O   VAL A  62      22.714  25.761  14.605  1.00 21.21           O  
ATOM    374  CB  VAL A  62      24.214  27.052  12.073  1.00 21.30           C  
ATOM    375  CG1 VAL A  62      25.061  25.912  12.608  1.00 22.10           C  
ATOM    376  CG2 VAL A  62      23.440  26.587  10.825  1.00 21.19           C  
ATOM    377  N   VAL A  63      21.158  26.366  13.084  1.00 21.48           N  
ATOM    378  CA  VAL A  63      20.302  25.231  13.374  1.00 21.87           C  
ATOM    379  C   VAL A  63      20.526  24.212  12.270  1.00 22.00           C  
ATOM    380  O   VAL A  63      20.366  24.528  11.109  1.00 22.54           O  
ATOM    381  CB  VAL A  63      18.793  25.574  13.421  1.00 22.02           C  
ATOM    382  CG1 VAL A  63      17.955  24.277  13.612  1.00 21.90           C  
ATOM    383  CG2 VAL A  63      18.494  26.522  14.546  1.00 21.22           C  
ATOM    384  N   LEU A  64      20.911  23.002  12.643  1.00 22.48           N  
ATOM    385  CA  LEU A  64      21.067  21.902  11.710  1.00 23.08           C  
ATOM    386  C   LEU A  64      19.826  21.014  11.775  1.00 22.19           C  
ATOM    387  O   LEU A  64      19.423  20.558  12.843  1.00 21.85           O  
ATOM    388  CB  LEU A  64      22.327  21.107  12.032  1.00 24.00           C  
ATOM    389  CG  LEU A  64      23.614  21.930  11.984  1.00 27.02           C  
ATOM    390  CD1 LEU A  64      24.791  21.080  12.303  1.00 31.61           C  
ATOM    391  CD2 LEU A  64      23.827  22.540  10.640  1.00 29.86           C  
ATOM    392  N   THR A  65      19.222  20.757  10.628  1.00 21.50           N  
ATOM    393  CA  THR A  65      17.943  20.056  10.613  1.00 21.95           C  
ATOM    394  C   THR A  65      18.022  18.561  10.389  1.00 21.35           C  
ATOM    395  O   THR A  65      17.028  17.870  10.581  1.00 21.37           O  
ATOM    396  CB  THR A  65      17.062  20.592   9.478  1.00 22.08           C  
ATOM    397  OG1 THR A  65      17.725  20.351   8.230  1.00 22.38           O  
ATOM    398  CG2 THR A  65      16.919  22.099   9.553  1.00 24.00           C  
ATOM    399  N   ASP A  66      19.168  18.062   9.961  1.00 21.50           N  
ATOM    400  CA  ASP A  66      19.259  16.650   9.604  1.00 21.86           C  
ATOM    401  C   ASP A  66      20.513  15.899  10.069  1.00 21.61           C  
ATOM    402  O   ASP A  66      21.070  15.088   9.316  1.00 21.82           O  
ATOM    403  CB  ASP A  66      19.152  16.553   8.084  1.00 22.20           C  
ATOM    404  CG  ASP A  66      20.199  17.355   7.390  1.00 21.49           C  
ATOM    405  OD1 ASP A  66      21.065  17.936   8.070  1.00 21.14           O  
ATOM    406  OD2 ASP A  66      20.240  17.477   6.159  1.00 25.40           O  
ATOM    407  N   THR A  67      20.967  16.158  11.287  1.00 21.05           N  
ATOM    408  CA  THR A  67      22.154  15.491  11.768  1.00 20.85           C  
ATOM    409  C   THR A  67      21.858  14.084  12.231  1.00 20.12           C  
ATOM    410  O   THR A  67      22.757  13.281  12.283  1.00 20.45           O  
ATOM    411  CB  THR A  67      22.747  16.207  12.977  1.00 20.77           C  
ATOM    412  OG1 THR A  67      21.782  16.210  14.039  1.00 20.61           O  
ATOM    413  CG2 THR A  67      23.054  17.671  12.682  1.00 22.44           C  
ATOM    414  N   ASN A  68      20.614  13.815  12.618  1.00 19.51           N  
ATOM    415  CA  ASN A  68      20.269  12.555  13.267  1.00 19.09           C  
ATOM    416  C   ASN A  68      21.116  12.349  14.517  1.00 18.40           C  
ATOM    417  O   ASN A  68      21.383  11.212  14.928  1.00 17.67           O  
ATOM    418  CB  ASN A  68      20.455  11.362  12.325  1.00 19.63           C  
ATOM    419  CG  ASN A  68      19.453  11.344  11.209  1.00 19.93           C  
ATOM    420  OD1 ASN A  68      18.253  11.236  11.442  1.00 19.76           O  
ATOM    421  ND2 ASN A  68      19.941  11.423   9.987  1.00 19.96           N  
ATOM    422  N   LEU A  69      21.532  13.448  15.134  1.00 18.28           N  
ATOM    423  CA  LEU A  69      22.378  13.382  16.326  1.00 17.98           C  
ATOM    424  C   LEU A  69      21.773  12.542  17.447  1.00 17.59           C  
ATOM    425  O   LEU A  69      22.478  11.725  18.039  1.00 17.61           O  
ATOM    426  CB  LEU A  69      22.693  14.772  16.844  1.00 18.38           C  
ATOM    427  CG  LEU A  69      23.636  14.859  18.035  1.00 18.31           C  
ATOM    428  CD1 LEU A  69      24.936  14.144  17.744  1.00 20.68           C  
ATOM    429  CD2 LEU A  69      23.907  16.299  18.399  1.00 19.25           C  
ATOM    430  N   VAL A  70      20.489  12.741  17.740  1.00 17.27           N  
ATOM    431  CA  VAL A  70      19.811  11.989  18.794  1.00 17.72           C  
ATOM    432  C   VAL A  70      18.588  11.253  18.257  1.00 18.11           C  
ATOM    433  O   VAL A  70      17.557  11.148  18.927  1.00 17.23           O  
ATOM    434  CB  VAL A  70      19.395  12.866  19.999  1.00 17.54           C  
ATOM    435  CG1 VAL A  70      20.624  13.402  20.704  1.00 19.07           C  
ATOM    436  CG2 VAL A  70      18.451  13.994  19.599  1.00 17.50           C  
ATOM    437  N   TYR A  71      18.715  10.764  17.028  1.00 19.22           N  
ATOM    438  CA  TYR A  71      17.615  10.071  16.367  1.00 19.79           C  
ATOM    439  C   TYR A  71      16.934   9.072  17.306  1.00 19.62           C  
ATOM    440  O   TYR A  71      15.726   9.120  17.457  1.00 18.64           O  
ATOM    441  CB  TYR A  71      18.082   9.406  15.055  1.00 20.19           C  
ATOM    442  CG  TYR A  71      17.156   8.320  14.554  1.00 22.29           C  
ATOM    443  CD1 TYR A  71      15.938   8.619  13.948  1.00 25.33           C  
ATOM    444  CD2 TYR A  71      17.503   6.986  14.691  1.00 23.31           C  
ATOM    445  CE1 TYR A  71      15.080   7.555  13.480  1.00 24.74           C  
ATOM    446  CE2 TYR A  71      16.684   5.968  14.252  1.00 23.57           C  
ATOM    447  CZ  TYR A  71      15.479   6.244  13.650  1.00 24.07           C  
ATOM    448  OH  TYR A  71      14.686   5.159  13.266  1.00 27.86           O  
ATOM    449  N   PRO A  72      17.688   8.200  17.960  1.00 20.27           N  
ATOM    450  CA  PRO A  72      17.074   7.196  18.840  1.00 21.30           C  
ATOM    451  C   PRO A  72      16.307   7.794  20.008  1.00 21.82           C  
ATOM    452  O   PRO A  72      15.463   7.120  20.535  1.00 21.13           O  
ATOM    453  CB  PRO A  72      18.267   6.377  19.351  1.00 21.33           C  
ATOM    454  CG  PRO A  72      19.362   6.650  18.386  1.00 21.75           C  
ATOM    455  CD  PRO A  72      19.151   8.065  17.905  1.00 20.71           C  
ATOM    456  N   ALA A  73      16.588   9.038  20.391  1.00 22.47           N  
ATOM    457  CA  ALA A  73      15.892   9.658  21.522  1.00 23.20           C  
ATOM    458  C   ALA A  73      14.567  10.293  21.103  1.00 23.47           C  
ATOM    459  O   ALA A  73      13.801  10.765  21.938  1.00 23.46           O  
ATOM    460  CB  ALA A  73      16.783  10.718  22.173  1.00 23.27           C  
ATOM    461  N   LEU A  74      14.297  10.322  19.808  1.00 23.79           N  
ATOM    462  CA  LEU A  74      13.086  10.967  19.329  1.00 24.10           C  
ATOM    463  C   LEU A  74      11.797  10.301  19.801  1.00 24.55           C  
ATOM    464  O   LEU A  74      10.732  10.903  19.746  1.00 23.83           O  
ATOM    465  CB  LEU A  74      13.114  11.076  17.810  1.00 24.16           C  
ATOM    466  CG  LEU A  74      14.185  12.061  17.296  1.00 24.67           C  
ATOM    467  CD1 LEU A  74      13.988  12.320  15.820  1.00 26.73           C  
ATOM    468  CD2 LEU A  74      14.225  13.371  18.077  1.00 23.39           C  
ATOM    469  N   LYS A  75      11.897   9.053  20.244  1.00 24.97           N  
ATOM    470  CA  LYS A  75      10.741   8.317  20.738  1.00 25.16           C  
ATOM    471  C   LYS A  75      10.589   8.519  22.245  1.00 25.37           C  
ATOM    472  O   LYS A  75       9.612   8.082  22.822  1.00 25.23           O  
ATOM    473  CB  LYS A  75      10.885   6.819  20.428  1.00 25.16           C  
ATOM    474  CG  LYS A  75      12.079   6.163  21.097  1.00 25.17           C  
ATOM    475  CD  LYS A  75      12.178   4.653  20.765  1.00 27.19           C  
ATOM    476  CE  LYS A  75      13.646   4.220  20.609  1.00 26.95           C  
ATOM    477  NZ  LYS A  75      14.348   4.123  21.868  1.00 26.22           N  
ATOM    478  N   TRP A  76      11.552   9.179  22.882  1.00 25.25           N  
ATOM    479  CA  TRP A  76      11.486   9.389  24.319  1.00 25.56           C  
ATOM    480  C   TRP A  76      10.268  10.201  24.749  1.00 26.35           C  
ATOM    481  O   TRP A  76       9.920  11.198  24.130  1.00 26.71           O  
ATOM    482  CB  TRP A  76      12.719  10.139  24.816  1.00 25.19           C  
ATOM    483  CG  TRP A  76      13.975   9.338  24.816  1.00 24.32           C  
ATOM    484  CD1 TRP A  76      14.129   8.059  24.393  1.00 22.72           C  
ATOM    485  CD2 TRP A  76      15.258   9.762  25.271  1.00 22.34           C  
ATOM    486  NE1 TRP A  76      15.431   7.658  24.552  1.00 20.61           N  
ATOM    487  CE2 TRP A  76      16.145   8.685  25.096  1.00 20.28           C  
ATOM    488  CE3 TRP A  76      15.750  10.944  25.817  1.00 22.65           C  
ATOM    489  CZ2 TRP A  76      17.481   8.756  25.437  1.00 20.18           C  
ATOM    490  CZ3 TRP A  76      17.088  11.012  26.163  1.00 21.43           C  
ATOM    491  CH2 TRP A  76      17.932   9.934  25.970  1.00 21.94           C  
ATOM    492  N   ASP A  77       9.643   9.772  25.836  1.00 26.46           N  
ATOM    493  CA  ASP A  77       8.583  10.530  26.467  1.00 26.47           C  
ATOM    494  C   ASP A  77       8.618  10.116  27.931  1.00 26.16           C  
ATOM    495  O   ASP A  77       9.405   9.264  28.291  1.00 26.44           O  
ATOM    496  CB  ASP A  77       7.230  10.276  25.810  1.00 26.51           C  
ATOM    497  CG  ASP A  77       6.795   8.835  25.885  1.00 27.32           C  
ATOM    498  OD1 ASP A  77       7.388   8.015  26.638  1.00 26.02           O  
ATOM    499  OD2 ASP A  77       5.832   8.439  25.211  1.00 29.97           O  
ATOM    500  N   LEU A  78       7.790  10.705  28.775  1.00 25.96           N  
ATOM    501  CA  LEU A  78       7.893  10.441  30.201  1.00 26.27           C  
ATOM    502  C   LEU A  78       7.716   8.965  30.539  1.00 26.14           C  
ATOM    503  O   LEU A  78       8.446   8.438  31.374  1.00 25.51           O  
ATOM    504  CB  LEU A  78       6.905  11.301  30.979  1.00 26.32           C  
ATOM    505  CG  LEU A  78       7.155  12.802  30.860  1.00 27.35           C  
ATOM    506  CD1 LEU A  78       6.098  13.579  31.623  1.00 28.05           C  
ATOM    507  CD2 LEU A  78       8.536  13.165  31.379  1.00 28.39           C  
ATOM    508  N   GLU A  79       6.775   8.297  29.874  1.00 26.56           N  
ATOM    509  CA  GLU A  79       6.526   6.876  30.123  1.00 27.00           C  
ATOM    510  C   GLU A  79       7.754   6.029  29.780  1.00 26.63           C  
ATOM    511  O   GLU A  79       8.220   5.231  30.583  1.00 25.94           O  
ATOM    512  CB  GLU A  79       5.302   6.371  29.333  1.00 27.39           C  
ATOM    513  CG  GLU A  79       4.963   4.919  29.657  1.00 29.75           C  
ATOM    514  CD  GLU A  79       3.803   4.347  28.854  1.00 33.15           C  
ATOM    515  OE1 GLU A  79       3.361   4.976  27.863  1.00 35.39           O  
ATOM    516  OE2 GLU A  79       3.338   3.245  29.224  1.00 35.44           O  
ATOM    517  N   TYR A  80       8.279   6.205  28.575  1.00 26.53           N  
ATOM    518  CA  TYR A  80       9.466   5.465  28.169  1.00 26.29           C  
ATOM    519  C   TYR A  80      10.669   5.763  29.072  1.00 25.83           C  
ATOM    520  O   TYR A  80      11.418   4.863  29.435  1.00 25.75           O  
ATOM    521  CB  TYR A  80       9.812   5.802  26.728  1.00 26.53           C  
ATOM    522  CG  TYR A  80      11.047   5.106  26.210  1.00 26.94           C  
ATOM    523  CD1 TYR A  80      10.971   3.836  25.637  1.00 26.53           C  
ATOM    524  CD2 TYR A  80      12.287   5.721  26.291  1.00 25.32           C  
ATOM    525  CE1 TYR A  80      12.113   3.208  25.142  1.00 26.28           C  
ATOM    526  CE2 TYR A  80      13.416   5.109  25.823  1.00 25.73           C  
ATOM    527  CZ  TYR A  80      13.331   3.861  25.240  1.00 25.94           C  
ATOM    528  OH  TYR A  80      14.478   3.294  24.758  1.00 25.55           O  
ATOM    529  N   LEU A  81      10.859   7.016  29.448  1.00 25.62           N  
ATOM    530  CA  LEU A  81      12.000   7.350  30.309  1.00 25.87           C  
ATOM    531  C   LEU A  81      11.821   6.794  31.733  1.00 26.06           C  
ATOM    532  O   LEU A  81      12.763   6.263  32.327  1.00 26.00           O  
ATOM    533  CB  LEU A  81      12.250   8.863  30.340  1.00 25.81           C  
ATOM    534  CG  LEU A  81      12.748   9.501  29.030  1.00 25.65           C  
ATOM    535  CD1 LEU A  81      12.828  11.010  29.174  1.00 26.40           C  
ATOM    536  CD2 LEU A  81      14.102   8.959  28.592  1.00 25.79           C  
ATOM    537  N   GLN A  82      10.617   6.913  32.274  1.00 26.27           N  
ATOM    538  CA  GLN A  82      10.338   6.388  33.602  1.00 26.77           C  
ATOM    539  C   GLN A  82      10.640   4.897  33.623  1.00 26.51           C  
ATOM    540  O   GLN A  82      11.232   4.384  34.552  1.00 26.60           O  
ATOM    541  CB  GLN A  82       8.877   6.611  33.974  1.00 26.90           C  
ATOM    542  CG  GLN A  82       8.466   5.856  35.236  1.00 28.41           C  
ATOM    543  CD  GLN A  82       7.315   6.501  35.987  1.00 30.63           C  
ATOM    544  OE1 GLN A  82       6.755   7.501  35.551  1.00 32.13           O  
ATOM    545  NE2 GLN A  82       6.944   5.907  37.116  1.00 34.12           N  
ATOM    546  N   GLU A  83      10.252   4.216  32.561  1.00 26.68           N  
ATOM    547  CA  GLU A  83      10.429   2.773  32.456  1.00 26.90           C  
ATOM    548  C   GLU A  83      11.893   2.359  32.295  1.00 26.42           C  
ATOM    549  O   GLU A  83      12.285   1.294  32.764  1.00 25.50           O  
ATOM    550  CB  GLU A  83       9.604   2.257  31.273  1.00 26.84           C  
ATOM    551  CG  GLU A  83       9.607   0.753  31.080  1.00 29.20           C  
ATOM    552  CD  GLU A  83       8.902   0.014  32.205  1.00 31.92           C  
ATOM    553  OE1 GLU A  83       8.258   0.666  33.060  1.00 34.06           O  
ATOM    554  OE2 GLU A  83       9.008  -1.221  32.243  1.00 33.78           O  
ATOM    555  N   ASN A  84      12.711   3.223  31.700  1.00 25.79           N  
ATOM    556  CA  ASN A  84      14.063   2.824  31.312  1.00 25.87           C  
ATOM    557  C   ASN A  84      15.273   3.607  31.810  1.00 26.08           C  
ATOM    558  O   ASN A  84      16.392   3.138  31.628  1.00 26.05           O  
ATOM    559  CB  ASN A  84      14.137   2.844  29.784  1.00 25.74           C  
ATOM    560  CG  ASN A  84      13.262   1.799  29.152  1.00 25.67           C  
ATOM    561  OD1 ASN A  84      13.402   0.608  29.439  1.00 24.26           O  
ATOM    562  ND2 ASN A  84      12.354   2.231  28.288  1.00 22.66           N  
ATOM    563  N   ILE A  85      15.087   4.773  32.422  1.00 26.02           N  
ATOM    564  CA  ILE A  85      16.240   5.599  32.763  1.00 26.74           C  
ATOM    565  C   ILE A  85      16.930   5.307  34.099  1.00 26.89           C  
ATOM    566  O   ILE A  85      17.820   6.054  34.519  1.00 26.93           O  
ATOM    567  CB  ILE A  85      15.846   7.076  32.688  1.00 26.70           C  
ATOM    568  CG1 ILE A  85      17.049   7.923  32.270  1.00 27.99           C  
ATOM    569  CG2 ILE A  85      15.232   7.535  33.988  1.00 26.50           C  
ATOM    570  CD1 ILE A  85      16.696   9.389  32.000  1.00 28.77           C  
ATOM    571  N   GLY A  86      16.503   4.253  34.773  1.00 27.27           N  
ATOM    572  CA  GLY A  86      17.130   3.834  36.018  1.00 27.51           C  
ATOM    573  C   GLY A  86      16.573   4.453  37.289  1.00 27.73           C  
ATOM    574  O   GLY A  86      15.563   5.163  37.268  1.00 27.80           O  
ATOM    575  N   ASN A  87      17.273   4.186  38.392  1.00 27.70           N  
ATOM    576  CA  ASN A  87      16.864   4.603  39.726  1.00 27.53           C  
ATOM    577  C   ASN A  87      17.849   5.602  40.320  1.00 27.33           C  
ATOM    578  O   ASN A  87      17.932   5.762  41.539  1.00 26.97           O  
ATOM    579  CB  ASN A  87      16.726   3.367  40.644  1.00 27.60           C  
ATOM    580  N   GLY A  88      18.601   6.273  39.455  1.00 27.41           N  
ATOM    581  CA  GLY A  88      19.528   7.307  39.888  1.00 27.29           C  
ATOM    582  C   GLY A  88      18.762   8.549  40.288  1.00 27.18           C  
ATOM    583  O   GLY A  88      17.570   8.654  40.001  1.00 27.43           O  
ATOM    584  N   ASP A  89      19.437   9.489  40.945  1.00 27.04           N  
ATOM    585  CA  ASP A  89      18.808  10.739  41.366  1.00 26.88           C  
ATOM    586  C   ASP A  89      18.761  11.755  40.227  1.00 26.69           C  
ATOM    587  O   ASP A  89      19.697  11.848  39.446  1.00 26.91           O  
ATOM    588  CB  ASP A  89      19.596  11.372  42.504  1.00 26.95           C  
ATOM    589  CG  ASP A  89      19.375  10.688  43.834  1.00 27.28           C  
ATOM    590  OD1 ASP A  89      18.499   9.811  43.939  1.00 29.31           O  
ATOM    591  OD2 ASP A  89      20.040  10.983  44.839  1.00 27.32           O  
ATOM    592  N   PHE A  90      17.687  12.531  40.152  1.00 26.24           N  
ATOM    593  CA  PHE A  90      17.598  13.594  39.165  1.00 26.10           C  
ATOM    594  C   PHE A  90      17.407  14.931  39.866  1.00 26.23           C  
ATOM    595  O   PHE A  90      16.629  15.037  40.811  1.00 26.48           O  
ATOM    596  CB  PHE A  90      16.460  13.322  38.184  1.00 25.91           C  
ATOM    597  CG  PHE A  90      16.747  12.201  37.241  1.00 25.26           C  
ATOM    598  CD1 PHE A  90      16.601  10.886  37.640  1.00 25.32           C  
ATOM    599  CD2 PHE A  90      17.190  12.459  35.958  1.00 26.02           C  
ATOM    600  CE1 PHE A  90      16.872   9.856  36.777  1.00 24.09           C  
ATOM    601  CE2 PHE A  90      17.460  11.427  35.091  1.00 25.07           C  
ATOM    602  CZ  PHE A  90      17.308  10.117  35.512  1.00 24.67           C  
ATOM    603  N   SER A  91      18.149  15.941  39.430  1.00 26.33           N  
ATOM    604  CA  SER A  91      17.985  17.280  39.973  1.00 26.48           C  
ATOM    605  C   SER A  91      16.777  17.923  39.310  1.00 26.71           C  
ATOM    606  O   SER A  91      16.696  18.029  38.077  1.00 26.09           O  
ATOM    607  CB  SER A  91      19.226  18.152  39.763  1.00 26.25           C  
ATOM    608  OG  SER A  91      20.364  17.543  40.326  1.00 26.61           O  
ATOM    609  N   VAL A  92      15.835  18.327  40.150  1.00 27.06           N  
ATOM    610  CA  VAL A  92      14.629  18.971  39.695  1.00 27.44           C  
ATOM    611  C   VAL A  92      14.468  20.295  40.405  1.00 27.57           C  
ATOM    612  O   VAL A  92      14.475  20.376  41.642  1.00 26.69           O  
ATOM    613  CB  VAL A  92      13.407  18.132  40.004  1.00 27.60           C  
ATOM    614  CG1 VAL A  92      12.164  18.800  39.432  1.00 28.15           C  
ATOM    615  CG2 VAL A  92      13.584  16.731  39.457  1.00 27.84           C  
ATOM    616  N   TYR A  93      14.312  21.334  39.598  1.00 27.77           N  
ATOM    617  CA  TYR A  93      14.120  22.661  40.108  1.00 27.91           C  
ATOM    618  C   TYR A  93      12.654  22.940  40.172  1.00 28.16           C  
ATOM    619  O   TYR A  93      11.894  22.525  39.303  1.00 28.02           O  
ATOM    620  CB  TYR A  93      14.810  23.673  39.216  1.00 27.94           C  
ATOM    621  CG  TYR A  93      16.291  23.593  39.368  1.00 29.53           C  
ATOM    622  CD1 TYR A  93      16.929  24.258  40.395  1.00 29.48           C  
ATOM    623  CD2 TYR A  93      17.046  22.815  38.522  1.00 30.95           C  
ATOM    624  CE1 TYR A  93      18.266  24.169  40.553  1.00 29.93           C  
ATOM    625  CE2 TYR A  93      18.386  22.726  38.679  1.00 31.90           C  
ATOM    626  CZ  TYR A  93      18.985  23.402  39.704  1.00 31.56           C  
ATOM    627  OH  TYR A  93      20.327  23.306  39.878  1.00 35.47           O  
ATOM    628  N   SER A  94      12.282  23.669  41.208  1.00 28.70           N  
ATOM    629  CA  SER A  94      10.913  24.037  41.459  1.00 29.47           C  
ATOM    630  C   SER A  94      10.856  25.547  41.554  1.00 29.69           C  
ATOM    631  O   SER A  94      11.705  26.167  42.187  1.00 29.50           O  
ATOM    632  CB  SER A  94      10.456  23.411  42.774  1.00 29.32           C  
ATOM    633  OG  SER A  94       9.093  23.701  43.009  1.00 30.85           O  
ATOM    634  N   ALA A  95       9.858  26.146  40.928  1.00 30.39           N  
ATOM    635  CA  ALA A  95       9.760  27.591  40.929  1.00 31.04           C  
ATOM    636  C   ALA A  95       8.330  28.064  40.932  1.00 31.76           C  
ATOM    637  O   ALA A  95       7.425  27.386  40.452  1.00 31.87           O  
ATOM    638  CB  ALA A  95      10.480  28.165  39.716  1.00 31.12           C  
ATOM    639  N   SER A  96       8.147  29.258  41.467  1.00 32.54           N  
ATOM    640  CA  SER A  96       6.848  29.891  41.489  1.00 33.42           C  
ATOM    641  C   SER A  96       6.708  30.869  40.326  1.00 33.15           C  
ATOM    642  O   SER A  96       5.662  31.487  40.163  1.00 34.35           O  
ATOM    643  CB  SER A  96       6.673  30.661  42.787  1.00 33.88           C  
ATOM    644  OG  SER A  96       5.380  31.217  42.815  1.00 35.79           O  
ATOM    645  N   THR A  97       7.775  31.031  39.554  1.00 32.09           N  
ATOM    646  CA  THR A  97       7.797  31.920  38.397  1.00 31.44           C  
ATOM    647  C   THR A  97       8.185  31.095  37.191  1.00 30.26           C  
ATOM    648  O   THR A  97       8.693  30.003  37.348  1.00 29.72           O  
ATOM    649  CB  THR A  97       8.857  33.031  38.582  1.00 31.64           C  
ATOM    650  OG1 THR A  97       9.147  33.656  37.323  1.00 32.17           O  
ATOM    651  CG2 THR A  97      10.227  32.455  38.978  1.00 31.73           C  
ATOM    652  N   HIS A  98       7.974  31.623  35.996  1.00 29.35           N  
ATOM    653  CA  HIS A  98       8.379  30.915  34.780  1.00 28.83           C  
ATOM    654  C   HIS A  98       9.899  30.969  34.589  1.00 28.37           C  
ATOM    655  O   HIS A  98      10.467  30.189  33.824  1.00 27.53           O  
ATOM    656  CB  HIS A  98       7.671  31.490  33.548  1.00 28.76           C  
ATOM    657  CG  HIS A  98       7.936  32.942  33.309  1.00 28.53           C  
ATOM    658  ND1 HIS A  98       7.271  33.944  33.984  1.00 29.18           N  
ATOM    659  CD2 HIS A  98       8.793  33.566  32.463  1.00 29.68           C  
ATOM    660  CE1 HIS A  98       7.708  35.120  33.568  1.00 29.42           C  
ATOM    661  NE2 HIS A  98       8.638  34.919  32.650  1.00 29.10           N  
ATOM    662  N   LYS A  99      10.562  31.874  35.299  1.00 27.85           N  
ATOM    663  CA  LYS A  99      11.997  32.041  35.124  1.00 28.24           C  
ATOM    664  C   LYS A  99      12.878  31.143  35.997  1.00 27.69           C  
ATOM    665  O   LYS A  99      12.892  31.278  37.216  1.00 29.10           O  
ATOM    666  CB  LYS A  99      12.366  33.498  35.349  1.00 28.47           C  
ATOM    667  CG  LYS A  99      11.836  34.410  34.255  1.00 30.42           C  
ATOM    668  CD  LYS A  99      12.431  35.791  34.347  1.00 32.66           C  
ATOM    669  CE  LYS A  99      11.757  36.624  35.421  1.00 34.45           C  
ATOM    670  NZ  LYS A  99      10.569  37.347  34.884  1.00 35.39           N  
ATOM    671  N   PHE A 100      13.621  30.237  35.376  1.00 26.40           N  
ATOM    672  CA  PHE A 100      14.551  29.397  36.127  1.00 25.95           C  
ATOM    673  C   PHE A 100      15.978  29.920  35.995  1.00 25.87           C  
ATOM    674  O   PHE A 100      16.809  29.386  35.247  1.00 25.86           O  
ATOM    675  CB  PHE A 100      14.469  27.945  35.686  1.00 25.48           C  
ATOM    676  CG  PHE A 100      13.211  27.267  36.109  1.00 25.06           C  
ATOM    677  CD1 PHE A 100      12.047  27.436  35.388  1.00 24.80           C  
ATOM    678  CD2 PHE A 100      13.191  26.472  37.238  1.00 25.18           C  
ATOM    679  CE1 PHE A 100      10.886  26.805  35.772  1.00 25.96           C  
ATOM    680  CE2 PHE A 100      12.030  25.835  37.631  1.00 25.79           C  
ATOM    681  CZ  PHE A 100      10.878  26.004  36.898  1.00 26.05           C  
ATOM    682  N   LEU A 101      16.237  30.997  36.709  1.00 25.77           N  
ATOM    683  CA  LEU A 101      17.549  31.589  36.747  1.00 25.85           C  
ATOM    684  C   LEU A 101      18.527  30.605  37.381  1.00 25.87           C  
ATOM    685  O   LEU A 101      18.319  30.136  38.503  1.00 24.99           O  
ATOM    686  CB  LEU A 101      17.488  32.876  37.559  1.00 25.84           C  
ATOM    687  CG  LEU A 101      18.795  33.656  37.708  1.00 26.07           C  
ATOM    688  CD1 LEU A 101      19.244  34.200  36.377  1.00 25.11           C  
ATOM    689  CD2 LEU A 101      18.609  34.800  38.710  1.00 27.75           C  
ATOM    690  N   TYR A 102      19.582  30.274  36.644  1.00 26.56           N  
ATOM    691  CA  TYR A 102      20.611  29.380  37.159  1.00 26.99           C  
ATOM    692  C   TYR A 102      21.430  30.072  38.260  1.00 27.10           C  
ATOM    693  O   TYR A 102      21.711  31.264  38.174  1.00 27.00           O  
ATOM    694  CB  TYR A 102      21.562  28.939  36.053  1.00 27.26           C  
ATOM    695  CG  TYR A 102      22.667  28.088  36.620  1.00 28.93           C  
ATOM    696  CD1 TYR A 102      22.457  26.750  36.914  1.00 29.52           C  
ATOM    697  CD2 TYR A 102      23.906  28.636  36.909  1.00 31.11           C  
ATOM    698  CE1 TYR A 102      23.463  25.979  37.480  1.00 32.23           C  
ATOM    699  CE2 TYR A 102      24.913  27.872  37.470  1.00 32.52           C  
ATOM    700  CZ  TYR A 102      24.693  26.549  37.750  1.00 33.88           C  
ATOM    701  OH  TYR A 102      25.727  25.794  38.314  1.00 38.68           O  
ATOM    702  N   TYR A 103      21.793  29.322  39.296  1.00 26.83           N  
ATOM    703  CA  TYR A 103      22.667  29.840  40.343  1.00 27.22           C  
ATOM    704  C   TYR A 103      23.613  28.750  40.834  1.00 26.77           C  
ATOM    705  O   TYR A 103      23.287  27.556  40.853  1.00 25.60           O  
ATOM    706  CB  TYR A 103      21.880  30.440  41.517  1.00 27.38           C  
ATOM    707  CG  TYR A 103      20.909  29.493  42.154  1.00 29.11           C  
ATOM    708  CD1 TYR A 103      19.639  29.340  41.639  1.00 30.58           C  
ATOM    709  CD2 TYR A 103      21.257  28.759  43.279  1.00 32.13           C  
ATOM    710  CE1 TYR A 103      18.734  28.469  42.212  1.00 32.78           C  
ATOM    711  CE2 TYR A 103      20.357  27.887  43.877  1.00 33.15           C  
ATOM    712  CZ  TYR A 103      19.096  27.745  43.329  1.00 34.41           C  
ATOM    713  OH  TYR A 103      18.187  26.888  43.892  1.00 37.44           O  
ATOM    714  N   ASP A 104      24.798  29.182  41.225  1.00 26.36           N  
ATOM    715  CA  ASP A 104      25.832  28.273  41.673  1.00 26.28           C  
ATOM    716  C   ASP A 104      25.802  28.239  43.184  1.00 26.21           C  
ATOM    717  O   ASP A 104      26.163  29.212  43.845  1.00 25.45           O  
ATOM    718  CB  ASP A 104      27.174  28.765  41.154  1.00 25.92           C  
ATOM    719  CG  ASP A 104      28.330  27.889  41.575  1.00 27.39           C  
ATOM    720  OD1 ASP A 104      28.161  26.973  42.437  1.00 27.13           O  
ATOM    721  OD2 ASP A 104      29.459  28.068  41.075  1.00 27.68           O  
ATOM    722  N   GLU A 105      25.358  27.114  43.724  1.00 26.46           N  
ATOM    723  CA  GLU A 105      25.218  26.962  45.162  1.00 27.02           C  
ATOM    724  C   GLU A 105      26.540  27.199  45.916  1.00 26.91           C  
ATOM    725  O   GLU A 105      26.523  27.718  47.026  1.00 26.51           O  
ATOM    726  CB  GLU A 105      24.602  25.587  45.481  1.00 27.45           C  
ATOM    727  CG  GLU A 105      23.088  25.556  45.254  1.00 29.46           C  
ATOM    728  CD  GLU A 105      22.527  24.158  45.025  1.00 32.85           C  
ATOM    729  OE1 GLU A 105      22.908  23.234  45.765  1.00 32.90           O  
ATOM    730  OE2 GLU A 105      21.703  23.980  44.085  1.00 35.16           O  
ATOM    731  N   LYS A 106      27.680  26.874  45.305  1.00 27.12           N  
ATOM    732  CA  LYS A 106      28.979  27.041  45.983  1.00 27.54           C  
ATOM    733  C   LYS A 106      29.331  28.493  46.258  1.00 27.70           C  
ATOM    734  O   LYS A 106      30.164  28.769  47.099  1.00 27.61           O  
ATOM    735  CB  LYS A 106      30.127  26.441  45.163  1.00 27.58           C  
ATOM    736  CG  LYS A 106      30.038  24.928  44.918  1.00 28.61           C  
ATOM    737  N   LYS A 107      28.713  29.420  45.537  1.00 27.99           N  
ATOM    738  CA  LYS A 107      29.020  30.826  45.694  1.00 28.30           C  
ATOM    739  C   LYS A 107      28.034  31.513  46.631  1.00 29.21           C  
ATOM    740  O   LYS A 107      28.175  32.701  46.917  1.00 29.08           O  
ATOM    741  CB  LYS A 107      29.040  31.524  44.324  1.00 28.30           C  
ATOM    742  CG  LYS A 107      30.344  31.291  43.516  1.00 28.07           C  
ATOM    743  CD  LYS A 107      30.242  31.737  42.034  1.00 27.29           C  
ATOM    744  CE  LYS A 107      31.584  31.518  41.315  1.00 26.86           C  
ATOM    745  NZ  LYS A 107      31.642  31.889  39.870  1.00 24.80           N  
ATOM    746  N   MET A 108      27.041  30.781  47.125  1.00 30.08           N  
ATOM    747  CA  MET A 108      26.031  31.405  47.982  1.00 31.53           C  
ATOM    748  C   MET A 108      26.581  31.952  49.309  1.00 32.44           C  
ATOM    749  O   MET A 108      26.102  32.972  49.812  1.00 32.47           O  
ATOM    750  CB  MET A 108      24.862  30.452  48.218  1.00 31.81           C  
ATOM    751  CG  MET A 108      24.072  30.193  46.932  1.00 33.07           C  
ATOM    752  SD  MET A 108      22.625  29.140  47.064  1.00 35.76           S  
ATOM    753  CE  MET A 108      21.540  30.140  48.050  1.00 35.99           C  
ATOM    754  N   ALA A 109      27.603  31.315  49.860  1.00 33.56           N  
ATOM    755  CA  ALA A 109      28.154  31.769  51.138  1.00 34.94           C  
ATOM    756  C   ALA A 109      28.651  33.212  51.060  1.00 35.81           C  
ATOM    757  O   ALA A 109      28.483  33.989  51.991  1.00 36.23           O  
ATOM    758  CB  ALA A 109      29.279  30.838  51.606  1.00 34.82           C  
ATOM    759  N   ASN A 110      29.236  33.575  49.929  1.00 37.05           N  
ATOM    760  CA  ASN A 110      29.774  34.918  49.748  1.00 37.94           C  
ATOM    761  C   ASN A 110      28.731  35.992  49.413  1.00 38.13           C  
ATOM    762  O   ASN A 110      29.064  37.167  49.293  1.00 37.92           O  
ATOM    763  CB  ASN A 110      30.855  34.878  48.669  1.00 38.16           C  
ATOM    764  CG  ASN A 110      32.050  34.035  49.079  1.00 39.37           C  
ATOM    765  OD1 ASN A 110      32.407  33.964  50.265  1.00 40.12           O  
ATOM    766  ND2 ASN A 110      32.670  33.377  48.103  1.00 39.46           N  
ATOM    767  N   PHE A 111      27.480  35.588  49.234  1.00 38.71           N  
ATOM    768  CA  PHE A 111      26.408  36.539  48.966  1.00 39.02           C  
ATOM    769  C   PHE A 111      25.180  36.135  49.773  1.00 39.71           C  
ATOM    770  O   PHE A 111      24.143  35.747  49.232  1.00 39.45           O  
ATOM    771  CB  PHE A 111      26.091  36.603  47.471  1.00 38.97           C  
ATOM    772  CG  PHE A 111      27.110  37.362  46.672  1.00 38.04           C  
ATOM    773  CD1 PHE A 111      28.329  36.791  46.363  1.00 37.99           C  
ATOM    774  CD2 PHE A 111      26.851  38.642  46.235  1.00 36.83           C  
ATOM    775  CE1 PHE A 111      29.269  37.493  45.635  1.00 37.68           C  
ATOM    776  CE2 PHE A 111      27.788  39.339  45.500  1.00 36.08           C  
ATOM    777  CZ  PHE A 111      28.994  38.768  45.208  1.00 35.84           C  
ATOM    778  N   GLN A 112      25.315  36.267  51.085  1.00 40.62           N  
ATOM    779  CA  GLN A 112      24.286  35.852  52.029  1.00 41.31           C  
ATOM    780  C   GLN A 112      22.915  36.430  51.721  1.00 41.10           C  
ATOM    781  O   GLN A 112      21.906  35.827  52.060  1.00 41.31           O  
ATOM    782  CB  GLN A 112      24.701  36.236  53.451  1.00 41.65           C  
ATOM    783  CG  GLN A 112      26.058  35.694  53.882  1.00 43.80           C  
ATOM    784  CD  GLN A 112      26.104  34.177  53.938  1.00 46.42           C  
ATOM    785  OE1 GLN A 112      25.394  33.501  53.191  1.00 48.56           O  
ATOM    786  NE2 GLN A 112      26.951  33.637  54.816  1.00 46.94           N  
ATOM    787  N   ASN A 113      22.876  37.588  51.074  1.00 41.02           N  
ATOM    788  CA  ASN A 113      21.606  38.229  50.749  1.00 40.98           C  
ATOM    789  C   ASN A 113      20.954  37.760  49.440  1.00 40.71           C  
ATOM    790  O   ASN A 113      19.889  38.251  49.071  1.00 40.77           O  
ATOM    791  CB  ASN A 113      21.778  39.753  50.737  1.00 41.09           C  
ATOM    792  CG  ASN A 113      22.129  40.314  52.123  1.00 41.51           C  
ATOM    793  OD1 ASN A 113      21.717  39.772  53.158  1.00 40.60           O  
ATOM    794  ND2 ASN A 113      22.892  41.401  52.141  1.00 41.19           N  
ATOM    795  N   PHE A 114      21.571  36.826  48.725  1.00 40.34           N  
ATOM    796  CA  PHE A 114      20.934  36.321  47.515  1.00 39.86           C  
ATOM    797  C   PHE A 114      19.908  35.266  47.902  1.00 39.46           C  
ATOM    798  O   PHE A 114      20.235  34.299  48.584  1.00 38.82           O  
ATOM    799  CB  PHE A 114      21.940  35.714  46.552  1.00 39.96           C  
ATOM    800  CG  PHE A 114      21.298  35.059  45.362  1.00 40.54           C  
ATOM    801  CD1 PHE A 114      20.670  35.828  44.395  1.00 40.29           C  
ATOM    802  CD2 PHE A 114      21.295  33.679  45.224  1.00 40.62           C  
ATOM    803  CE1 PHE A 114      20.061  35.237  43.307  1.00 40.20           C  
ATOM    804  CE2 PHE A 114      20.684  33.082  44.126  1.00 40.36           C  
ATOM    805  CZ  PHE A 114      20.066  33.866  43.172  1.00 40.52           C  
ATOM    806  N   LYS A 115      18.669  35.457  47.461  1.00 39.11           N  
ATOM    807  CA  LYS A 115      17.596  34.529  47.787  1.00 39.02           C  
ATOM    808  C   LYS A 115      17.042  33.938  46.497  1.00 38.71           C  
ATOM    809  O   LYS A 115      16.285  34.590  45.787  1.00 39.00           O  
ATOM    810  CB  LYS A 115      16.498  35.251  48.578  1.00 39.14           C  
ATOM    811  N   PRO A 116      17.389  32.691  46.213  1.00 38.17           N  
ATOM    812  CA  PRO A 116      17.027  32.060  44.938  1.00 37.95           C  
ATOM    813  C   PRO A 116      15.532  31.889  44.783  1.00 37.38           C  
ATOM    814  O   PRO A 116      14.865  31.506  45.733  1.00 37.36           O  
ATOM    815  CB  PRO A 116      17.684  30.679  45.004  1.00 38.15           C  
ATOM    816  CG  PRO A 116      18.416  30.604  46.297  1.00 38.40           C  
ATOM    817  CD  PRO A 116      18.079  31.775  47.125  1.00 38.19           C  
ATOM    818  N   ARG A 117      15.027  32.161  43.590  1.00 36.84           N  
ATOM    819  CA  ARG A 117      13.611  32.028  43.293  1.00 36.61           C  
ATOM    820  C   ARG A 117      13.259  30.581  42.984  1.00 36.38           C  
ATOM    821  O   ARG A 117      12.084  30.230  42.913  1.00 36.44           O  
ATOM    822  CB  ARG A 117      13.235  32.913  42.122  1.00 36.62           C  
ATOM    823  N   SER A 118      14.271  29.745  42.777  1.00 35.79           N  
ATOM    824  CA  SER A 118      14.025  28.339  42.538  1.00 35.51           C  
ATOM    825  C   SER A 118      14.844  27.491  43.512  1.00 35.35           C  
ATOM    826  O   SER A 118      15.888  27.923  43.991  1.00 35.16           O  
ATOM    827  CB  SER A 118      14.330  27.976  41.086  1.00 35.26           C  
ATOM    828  OG  SER A 118      15.689  28.164  40.795  1.00 35.14           O  
ATOM    829  N   ASN A 119      14.329  26.306  43.824  1.00 35.11           N  
ATOM    830  CA  ASN A 119      14.997  25.373  44.715  1.00 35.21           C  
ATOM    831  C   ASN A 119      15.233  24.049  44.022  1.00 34.26           C  
ATOM    832  O   ASN A 119      14.401  23.595  43.244  1.00 34.11           O  
ATOM    833  CB  ASN A 119      14.145  25.110  45.957  1.00 35.95           C  
ATOM    834  CG  ASN A 119      13.636  26.382  46.592  1.00 38.47           C  
ATOM    835  OD1 ASN A 119      14.417  27.245  47.025  1.00 41.76           O  
ATOM    836  ND2 ASN A 119      12.314  26.511  46.657  1.00 42.21           N  
ATOM    837  N   ARG A 120      16.368  23.434  44.326  1.00 33.75           N  
ATOM    838  CA  ARG A 120      16.750  22.149  43.761  1.00 33.33           C  
ATOM    839  C   ARG A 120      16.327  21.045  44.699  1.00 33.26           C  
ATOM    840  O   ARG A 120      16.523  21.138  45.910  1.00 33.07           O  
ATOM    841  CB  ARG A 120      18.270  22.075  43.592  1.00 33.37           C  
ATOM    842  CG  ARG A 120      18.759  20.889  42.771  1.00 32.70           C  
ATOM    843  CD  ARG A 120      20.277  20.732  42.743  1.00 31.64           C  
ATOM    844  NE  ARG A 120      20.892  21.165  43.992  1.00 31.16           N  
ATOM    845  CZ  ARG A 120      21.233  20.357  44.993  1.00 31.33           C  
ATOM    846  NH1 ARG A 120      21.027  19.047  44.920  1.00 30.77           N  
ATOM    847  NH2 ARG A 120      21.789  20.867  46.077  1.00 31.01           N  
ATOM    848  N   GLU A 121      15.735  20.001  44.137  1.00 32.98           N  
ATOM    849  CA  GLU A 121      15.379  18.827  44.904  1.00 32.85           C  
ATOM    850  C   GLU A 121      15.846  17.630  44.095  1.00 32.17           C  
ATOM    851  O   GLU A 121      15.744  17.612  42.864  1.00 32.36           O  
ATOM    852  CB  GLU A 121      13.874  18.767  45.179  1.00 33.21           C  
ATOM    853  CG  GLU A 121      13.420  17.468  45.826  1.00 35.39           C  
ATOM    854  CD  GLU A 121      12.189  17.629  46.699  1.00 38.11           C  
ATOM    855  OE1 GLU A 121      12.326  18.152  47.830  1.00 41.26           O  
ATOM    856  OE2 GLU A 121      11.091  17.221  46.270  1.00 39.55           O  
ATOM    857  N   GLU A 122      16.400  16.648  44.786  1.00 31.28           N  
ATOM    858  CA  GLU A 122      16.886  15.448  44.150  1.00 30.61           C  
ATOM    859  C   GLU A 122      15.814  14.392  44.298  1.00 30.31           C  
ATOM    860  O   GLU A 122      15.328  14.165  45.395  1.00 30.07           O  
ATOM    861  CB  GLU A 122      18.163  14.980  44.833  1.00 30.52           C  
ATOM    862  CG  GLU A 122      19.293  15.983  44.771  1.00 29.67           C  
ATOM    863  CD  GLU A 122      19.747  16.253  43.348  1.00 29.79           C  
ATOM    864  OE1 GLU A 122      20.120  15.280  42.667  1.00 28.28           O  
ATOM    865  OE2 GLU A 122      19.734  17.439  42.914  1.00 27.93           O  
ATOM    866  N   MET A 123      15.432  13.751  43.202  1.00 29.74           N  
ATOM    867  CA  MET A 123      14.407  12.728  43.277  1.00 29.77           C  
ATOM    868  C   MET A 123      14.594  11.683  42.202  1.00 29.31           C  
ATOM    869  O   MET A 123      15.408  11.842  41.294  1.00 29.42           O  
ATOM    870  CB  MET A 123      13.016  13.354  43.165  1.00 29.81           C  
ATOM    871  CG  MET A 123      12.749  14.057  41.865  1.00 30.27           C  
ATOM    872  SD  MET A 123      11.181  14.960  41.871  1.00 31.65           S  
ATOM    873  CE  MET A 123      11.582  16.371  42.804  1.00 31.47           C  
ATOM    874  N   LYS A 124      13.835  10.604  42.332  1.00 28.82           N  
ATOM    875  CA  LYS A 124      13.841   9.535  41.352  1.00 28.33           C  
ATOM    876  C   LYS A 124      12.959   9.976  40.191  1.00 27.51           C  
ATOM    877  O   LYS A 124      12.077  10.817  40.361  1.00 26.52           O  
ATOM    878  CB  LYS A 124      13.330   8.242  41.984  1.00 28.45           C  
ATOM    879  CG  LYS A 124      14.153   7.783  43.204  1.00 29.42           C  
ATOM    880  CD  LYS A 124      15.597   7.442  42.804  1.00 30.46           C  
ATOM    881  CE  LYS A 124      16.479   7.067  43.992  1.00 30.52           C  
ATOM    882  NZ  LYS A 124      17.928   7.324  43.699  1.00 30.05           N  
ATOM    883  N   PHE A 125      13.188   9.407  39.014  1.00 26.98           N  
ATOM    884  CA  PHE A 125      12.477   9.871  37.826  1.00 26.83           C  
ATOM    885  C   PHE A 125      10.974   9.762  37.972  1.00 26.77           C  
ATOM    886  O   PHE A 125      10.245  10.673  37.585  1.00 26.38           O  
ATOM    887  CB  PHE A 125      12.927   9.138  36.568  1.00 26.71           C  
ATOM    888  CG  PHE A 125      12.613   9.891  35.316  1.00 26.32           C  
ATOM    889  CD1 PHE A 125      13.476  10.876  34.849  1.00 26.29           C  
ATOM    890  CD2 PHE A 125      11.438   9.657  34.635  1.00 26.06           C  
ATOM    891  CE1 PHE A 125      13.183  11.594  33.715  1.00 25.70           C  
ATOM    892  CE2 PHE A 125      11.140  10.368  33.483  1.00 26.70           C  
ATOM    893  CZ  PHE A 125      12.018  11.341  33.025  1.00 26.87           C  
ATOM    894  N   HIS A 126      10.527   8.649  38.550  1.00 26.77           N  
ATOM    895  CA  HIS A 126       9.113   8.396  38.753  1.00 26.82           C  
ATOM    896  C   HIS A 126       8.517   9.390  39.734  1.00 26.68           C  
ATOM    897  O   HIS A 126       7.326   9.670  39.687  1.00 26.03           O  
ATOM    898  CB  HIS A 126       8.882   6.951  39.238  1.00 27.07           C  
ATOM    899  CG  HIS A 126       9.028   6.767  40.717  1.00 27.39           C  
ATOM    900  ND1 HIS A 126       7.959   6.836  41.582  1.00 28.48           N  
ATOM    901  CD2 HIS A 126      10.115   6.505  41.484  1.00 28.33           C  
ATOM    902  CE1 HIS A 126       8.382   6.636  42.819  1.00 28.68           C  
ATOM    903  NE2 HIS A 126       9.687   6.439  42.788  1.00 27.97           N  
ATOM    904  N   GLU A 127       9.342   9.918  40.630  1.00 27.00           N  
ATOM    905  CA  GLU A 127       8.876  10.930  41.572  1.00 27.34           C  
ATOM    906  C   GLU A 127       8.683  12.259  40.838  1.00 27.36           C  
ATOM    907  O   GLU A 127       7.761  13.026  41.126  1.00 26.86           O  
ATOM    908  CB  GLU A 127       9.862  11.084  42.728  1.00 27.31           C  
ATOM    909  CG  GLU A 127      10.018   9.821  43.552  1.00 28.69           C  
ATOM    910  CD  GLU A 127      10.959   9.992  44.722  1.00 29.65           C  
ATOM    911  OE1 GLU A 127      12.139  10.318  44.485  1.00 29.56           O  
ATOM    912  OE2 GLU A 127      10.509   9.787  45.876  1.00 30.92           O  
ATOM    913  N   PHE A 128       9.554  12.519  39.876  1.00 27.91           N  
ATOM    914  CA  PHE A 128       9.453  13.736  39.068  1.00 28.21           C  
ATOM    915  C   PHE A 128       8.149  13.658  38.282  1.00 29.04           C  
ATOM    916  O   PHE A 128       7.354  14.600  38.255  1.00 29.03           O  
ATOM    917  CB  PHE A 128      10.643  13.838  38.115  1.00 27.74           C  
ATOM    918  CG  PHE A 128      10.427  14.792  36.959  1.00 27.06           C  
ATOM    919  CD1 PHE A 128      10.189  16.138  37.185  1.00 25.41           C  
ATOM    920  CD2 PHE A 128      10.480  14.343  35.657  1.00 25.60           C  
ATOM    921  CE1 PHE A 128       9.985  17.000  36.144  1.00 25.41           C  
ATOM    922  CE2 PHE A 128      10.281  15.215  34.604  1.00 26.59           C  
ATOM    923  CZ  PHE A 128      10.032  16.540  34.846  1.00 25.61           C  
ATOM    924  N   VAL A 129       7.925  12.500  37.677  1.00 29.90           N  
ATOM    925  CA  VAL A 129       6.756  12.285  36.847  1.00 30.82           C  
ATOM    926  C   VAL A 129       5.476  12.447  37.669  1.00 31.61           C  
ATOM    927  O   VAL A 129       4.515  13.091  37.234  1.00 31.39           O  
ATOM    928  CB  VAL A 129       6.793  10.883  36.213  1.00 30.92           C  
ATOM    929  CG1 VAL A 129       5.479  10.582  35.503  1.00 31.15           C  
ATOM    930  CG2 VAL A 129       7.975  10.751  35.253  1.00 30.61           C  
ATOM    931  N   GLU A 130       5.475  11.858  38.861  1.00 32.42           N  
ATOM    932  CA  GLU A 130       4.332  11.946  39.761  1.00 33.13           C  
ATOM    933  C   GLU A 130       4.070  13.403  40.126  1.00 33.42           C  
ATOM    934  O   GLU A 130       2.930  13.867  40.081  1.00 33.01           O  
ATOM    935  CB  GLU A 130       4.587  11.108  41.017  1.00 33.20           C  
ATOM    936  CG  GLU A 130       4.537   9.609  40.755  1.00 34.22           C  
ATOM    937  CD  GLU A 130       5.294   8.792  41.789  1.00 35.55           C  
ATOM    938  OE1 GLU A 130       5.630   9.339  42.861  1.00 37.02           O  
ATOM    939  OE2 GLU A 130       5.558   7.598  41.525  1.00 35.99           O  
ATOM    940  N   LYS A 131       5.128  14.120  40.486  1.00 34.00           N  
ATOM    941  CA  LYS A 131       4.994  15.538  40.800  1.00 34.79           C  
ATOM    942  C   LYS A 131       4.354  16.286  39.637  1.00 35.25           C  
ATOM    943  O   LYS A 131       3.449  17.089  39.835  1.00 34.81           O  
ATOM    944  CB  LYS A 131       6.345  16.171  41.100  1.00 34.89           C  
ATOM    945  CG  LYS A 131       6.597  16.477  42.554  1.00 35.57           C  
ATOM    946  CD  LYS A 131       7.191  17.868  42.694  1.00 36.25           C  
ATOM    947  CE  LYS A 131       7.862  18.072  44.034  1.00 37.30           C  
ATOM    948  NZ  LYS A 131       8.108  19.526  44.332  1.00 37.49           N  
ATOM    949  N   LEU A 132       4.829  16.038  38.422  1.00 36.00           N  
ATOM    950  CA  LEU A 132       4.243  16.701  37.268  1.00 37.05           C  
ATOM    951  C   LEU A 132       2.755  16.406  37.170  1.00 37.67           C  
ATOM    952  O   LEU A 132       1.963  17.300  36.870  1.00 37.77           O  
ATOM    953  CB  LEU A 132       4.919  16.260  35.979  1.00 37.39           C  
ATOM    954  CG  LEU A 132       6.310  16.803  35.710  1.00 38.29           C  
ATOM    955  CD1 LEU A 132       6.783  16.289  34.363  1.00 39.35           C  
ATOM    956  CD2 LEU A 132       6.306  18.314  35.721  1.00 39.70           C  
ATOM    957  N   GLN A 133       2.386  15.151  37.417  1.00 38.34           N  
ATOM    958  CA  GLN A 133       0.989  14.730  37.373  1.00 39.11           C  
ATOM    959  C   GLN A 133       0.132  15.434  38.427  1.00 39.73           C  
ATOM    960  O   GLN A 133      -0.966  15.897  38.126  1.00 39.61           O  
ATOM    961  CB  GLN A 133       0.886  13.213  37.538  1.00 39.05           C  
ATOM    962  N   ASP A 134       0.629  15.507  39.658  1.00 40.61           N  
ATOM    963  CA  ASP A 134      -0.108  16.149  40.747  1.00 41.70           C  
ATOM    964  C   ASP A 134      -0.398  17.626  40.451  1.00 41.68           C  
ATOM    965  O   ASP A 134      -1.470  18.137  40.770  1.00 41.28           O  
ATOM    966  CB  ASP A 134       0.678  16.030  42.056  1.00 42.32           C  
ATOM    967  CG  ASP A 134      -0.165  16.351  43.286  1.00 44.92           C  
ATOM    968  OD1 ASP A 134      -1.235  16.991  43.152  1.00 48.33           O  
ATOM    969  OD2 ASP A 134       0.164  15.991  44.442  1.00 48.64           O  
ATOM    970  N   ILE A 135       0.563  18.312  39.842  1.00 41.92           N  
ATOM    971  CA  ILE A 135       0.383  19.717  39.512  1.00 42.18           C  
ATOM    972  C   ILE A 135      -0.715  19.862  38.471  1.00 42.41           C  
ATOM    973  O   ILE A 135      -1.635  20.664  38.634  1.00 42.49           O  
ATOM    974  CB  ILE A 135       1.696  20.324  38.997  1.00 42.17           C  
ATOM    975  CG1 ILE A 135       2.720  20.399  40.131  1.00 42.25           C  
ATOM    976  CG2 ILE A 135       1.451  21.708  38.437  1.00 42.11           C  
ATOM    977  CD1 ILE A 135       4.151  20.438  39.653  1.00 42.91           C  
ATOM    978  N   GLN A 136      -0.614  19.075  37.407  1.00 42.71           N  
ATOM    979  CA  GLN A 136      -1.593  19.114  36.333  1.00 43.09           C  
ATOM    980  C   GLN A 136      -2.991  18.935  36.900  1.00 43.56           C  
ATOM    981  O   GLN A 136      -3.863  19.785  36.707  1.00 43.93           O  
ATOM    982  CB  GLN A 136      -1.298  18.031  35.317  1.00 43.10           C  
ATOM    983  N   GLN A 137      -3.181  17.844  37.635  1.00 43.82           N  
ATOM    984  CA  GLN A 137      -4.486  17.493  38.182  1.00 44.02           C  
ATOM    985  C   GLN A 137      -5.023  18.540  39.144  1.00 44.08           C  
ATOM    986  O   GLN A 137      -6.202  18.891  39.080  1.00 44.46           O  
ATOM    987  CB  GLN A 137      -4.425  16.124  38.868  1.00 44.00           C  
ATOM    988  N   ARG A 138      -4.169  19.043  40.031  1.00 43.93           N  
ATOM    989  CA  ARG A 138      -4.606  20.022  41.024  1.00 43.76           C  
ATOM    990  C   ARG A 138      -4.578  21.445  40.463  1.00 43.34           C  
ATOM    991  O   ARG A 138      -4.681  22.415  41.214  1.00 43.54           O  
ATOM    992  CB  ARG A 138      -3.751  19.919  42.299  1.00 43.84           C  
ATOM    993  CG  ARG A 138      -2.420  20.679  42.279  1.00 44.85           C  
ATOM    994  CD  ARG A 138      -1.493  20.279  43.420  1.00 45.82           C  
ATOM    995  NE  ARG A 138      -0.372  21.197  43.620  1.00 46.44           N  
ATOM    996  CZ  ARG A 138       0.914  20.863  43.499  1.00 47.95           C  
ATOM    997  NH1 ARG A 138       1.262  19.627  43.162  1.00 49.02           N  
ATOM    998  NH2 ARG A 138       1.864  21.767  43.709  1.00 47.70           N  
ATOM    999  N   GLY A 139      -4.450  21.569  39.143  1.00 42.62           N  
ATOM   1000  CA  GLY A 139      -4.371  22.871  38.504  1.00 41.93           C  
ATOM   1001  C   GLY A 139      -3.389  23.820  39.174  1.00 41.28           C  
ATOM   1002  O   GLY A 139      -3.607  25.030  39.196  1.00 41.58           O  
ATOM   1003  N   GLY A 140      -2.291  23.292  39.703  1.00 40.31           N  
ATOM   1004  CA  GLY A 140      -1.329  24.119  40.410  1.00 39.43           C  
ATOM   1005  C   GLY A 140      -0.563  25.070  39.512  1.00 38.71           C  
ATOM   1006  O   GLY A 140      -0.495  24.871  38.294  1.00 38.40           O  
ATOM   1007  N   GLU A 141       0.003  26.117  40.110  1.00 37.82           N  
ATOM   1008  CA  GLU A 141       0.829  27.066  39.363  1.00 37.20           C  
ATOM   1009  C   GLU A 141       2.320  26.726  39.491  1.00 35.94           C  
ATOM   1010  O   GLU A 141       3.160  27.356  38.845  1.00 35.76           O  
ATOM   1011  CB  GLU A 141       0.590  28.510  39.828  1.00 37.63           C  
ATOM   1012  CG  GLU A 141      -0.729  29.146  39.379  1.00 39.51           C  
ATOM   1013  CD  GLU A 141      -0.936  29.164  37.866  1.00 41.63           C  
ATOM   1014  OE1 GLU A 141       0.056  29.147  37.102  1.00 42.42           O  
ATOM   1015  OE2 GLU A 141      -2.115  29.202  37.434  1.00 43.77           O  
ATOM   1016  N   GLU A 142       2.652  25.742  40.326  1.00 34.29           N  
ATOM   1017  CA  GLU A 142       4.045  25.351  40.510  1.00 33.08           C  
ATOM   1018  C   GLU A 142       4.655  24.938  39.170  1.00 31.87           C  
ATOM   1019  O   GLU A 142       3.958  24.443  38.296  1.00 31.87           O  
ATOM   1020  CB  GLU A 142       4.170  24.201  41.519  1.00 32.96           C  
ATOM   1021  CG  GLU A 142       5.610  23.914  41.942  1.00 32.71           C  
ATOM   1022  CD  GLU A 142       5.761  22.730  42.896  1.00 33.55           C  
ATOM   1023  OE1 GLU A 142       4.778  22.001  43.146  1.00 32.41           O  
ATOM   1024  OE2 GLU A 142       6.888  22.520  43.398  1.00 34.13           O  
ATOM   1025  N   ARG A 143       5.954  25.156  39.017  1.00 30.56           N  
ATOM   1026  CA  ARG A 143       6.662  24.766  37.803  1.00 29.79           C  
ATOM   1027  C   ARG A 143       7.878  23.939  38.142  1.00 28.70           C  
ATOM   1028  O   ARG A 143       8.565  24.210  39.127  1.00 28.88           O  
ATOM   1029  CB  ARG A 143       7.142  25.991  37.040  1.00 29.90           C  
ATOM   1030  CG  ARG A 143       6.043  26.832  36.441  1.00 30.80           C  
ATOM   1031  CD  ARG A 143       6.591  27.992  35.636  1.00 30.70           C  
ATOM   1032  NE  ARG A 143       5.538  28.715  34.935  1.00 30.86           N  
ATOM   1033  CZ  ARG A 143       5.168  28.487  33.682  1.00 29.53           C  
ATOM   1034  NH1 ARG A 143       5.763  27.547  32.941  1.00 27.51           N  
ATOM   1035  NH2 ARG A 143       4.196  29.216  33.168  1.00 30.04           N  
ATOM   1036  N   LEU A 144       8.156  22.943  37.315  1.00 27.27           N  
ATOM   1037  CA  LEU A 144       9.319  22.102  37.518  1.00 26.47           C  
ATOM   1038  C   LEU A 144      10.220  22.148  36.297  1.00 25.40           C  
ATOM   1039  O   LEU A 144       9.755  22.330  35.172  1.00 25.39           O  
ATOM   1040  CB  LEU A 144       8.893  20.652  37.753  1.00 26.70           C  
ATOM   1041  CG  LEU A 144       7.922  20.416  38.915  1.00 27.15           C  
ATOM   1042  CD1 LEU A 144       7.575  18.921  39.059  1.00 27.40           C  
ATOM   1043  CD2 LEU A 144       8.488  20.956  40.221  1.00 27.42           C  
ATOM   1044  N   TYR A 145      11.511  21.974  36.527  1.00 23.90           N  
ATOM   1045  CA  TYR A 145      12.458  21.871  35.441  1.00 23.15           C  
ATOM   1046  C   TYR A 145      13.516  20.857  35.868  1.00 23.04           C  
ATOM   1047  O   TYR A 145      14.328  21.130  36.740  1.00 22.58           O  
ATOM   1048  CB  TYR A 145      13.080  23.235  35.107  1.00 23.01           C  
ATOM   1049  CG  TYR A 145      13.522  23.419  33.666  1.00 21.34           C  
ATOM   1050  CD1 TYR A 145      13.824  22.333  32.863  1.00 20.11           C  
ATOM   1051  CD2 TYR A 145      13.662  24.691  33.119  1.00 21.14           C  
ATOM   1052  CE1 TYR A 145      14.219  22.494  31.563  1.00 20.22           C  
ATOM   1053  CE2 TYR A 145      14.075  24.866  31.807  1.00 19.81           C  
ATOM   1054  CZ  TYR A 145      14.349  23.764  31.027  1.00 19.19           C  
ATOM   1055  OH  TYR A 145      14.736  23.903  29.699  1.00 18.36           O  
ATOM   1056  N   LEU A 146      13.461  19.666  35.287  1.00 22.75           N  
ATOM   1057  CA  LEU A 146      14.490  18.661  35.516  1.00 23.17           C  
ATOM   1058  C   LEU A 146      15.720  19.005  34.679  1.00 22.99           C  
ATOM   1059  O   LEU A 146      15.604  19.264  33.490  1.00 22.81           O  
ATOM   1060  CB  LEU A 146      13.980  17.282  35.115  1.00 23.33           C  
ATOM   1061  CG  LEU A 146      14.992  16.141  35.274  1.00 24.98           C  
ATOM   1062  CD1 LEU A 146      14.276  14.846  35.622  1.00 24.56           C  
ATOM   1063  CD2 LEU A 146      15.849  15.946  34.016  1.00 26.13           C  
ATOM   1064  N   GLN A 147      16.891  18.983  35.299  1.00 23.05           N  
ATOM   1065  CA  GLN A 147      18.135  19.314  34.619  1.00 23.65           C  
ATOM   1066  C   GLN A 147      19.158  18.394  35.231  1.00 23.86           C  
ATOM   1067  O   GLN A 147      19.573  18.597  36.364  1.00 24.61           O  
ATOM   1068  CB  GLN A 147      18.516  20.793  34.821  1.00 23.53           C  
ATOM   1069  CG  GLN A 147      17.386  21.770  34.461  1.00 24.34           C  
ATOM   1070  CD  GLN A 147      17.800  23.238  34.482  1.00 26.20           C  
ATOM   1071  OE1 GLN A 147      17.034  24.114  34.035  1.00 29.67           O  
ATOM   1072  NE2 GLN A 147      18.979  23.514  34.988  1.00 21.33           N  
ATOM   1073  N   GLN A 148      19.542  17.369  34.485  1.00 24.35           N  
ATOM   1074  CA  GLN A 148      20.393  16.314  35.006  1.00 24.70           C  
ATOM   1075  C   GLN A 148      21.319  15.753  33.964  1.00 25.16           C  
ATOM   1076  O   GLN A 148      20.898  15.378  32.866  1.00 24.21           O  
ATOM   1077  CB  GLN A 148      19.525  15.172  35.526  1.00 24.97           C  
ATOM   1078  CG  GLN A 148      20.317  13.940  35.953  1.00 25.54           C  
ATOM   1079  CD  GLN A 148      21.275  14.256  37.085  1.00 26.98           C  
ATOM   1080  OE1 GLN A 148      20.892  14.941  38.042  1.00 26.73           O  
ATOM   1081  NE2 GLN A 148      22.522  13.786  36.976  1.00 26.37           N  
ATOM   1082  N   THR A 149      22.592  15.704  34.321  1.00 25.94           N  
ATOM   1083  CA  THR A 149      23.603  15.134  33.466  1.00 27.43           C  
ATOM   1084  C   THR A 149      23.369  13.632  33.324  1.00 27.29           C  
ATOM   1085  O   THR A 149      23.081  12.965  34.303  1.00 27.40           O  
ATOM   1086  CB  THR A 149      24.990  15.430  34.075  1.00 27.91           C  
ATOM   1087  OG1 THR A 149      25.282  16.829  33.901  1.00 30.41           O  
ATOM   1088  CG2 THR A 149      26.078  14.776  33.276  1.00 30.12           C  
ATOM   1089  N   LEU A 150      23.461  13.117  32.100  1.00 27.79           N  
ATOM   1090  CA  LEU A 150      23.321  11.690  31.832  1.00 28.02           C  
ATOM   1091  C   LEU A 150      24.549  10.935  32.364  1.00 28.42           C  
ATOM   1092  O   LEU A 150      25.682  11.261  32.002  1.00 28.86           O  
ATOM   1093  CB  LEU A 150      23.194  11.435  30.326  1.00 28.08           C  
ATOM   1094  CG  LEU A 150      21.929  11.937  29.622  1.00 28.70           C  
ATOM   1095  CD1 LEU A 150      22.016  11.725  28.117  1.00 28.62           C  
ATOM   1096  CD2 LEU A 150      20.697  11.260  30.175  1.00 29.47           C  
ATOM   1097  N   ASN A 151      24.332   9.928  33.203  1.00 28.58           N  
ATOM   1098  CA  ASN A 151      25.434   9.156  33.781  1.00 28.79           C  
ATOM   1099  C   ASN A 151      25.194   7.636  33.782  1.00 29.24           C  
ATOM   1100  O   ASN A 151      24.197   7.163  33.238  1.00 29.60           O  
ATOM   1101  CB  ASN A 151      25.657   9.631  35.208  1.00 28.77           C  
ATOM   1102  CG  ASN A 151      24.459   9.367  36.084  1.00 28.05           C  
ATOM   1103  OD1 ASN A 151      23.936   8.246  36.126  1.00 29.02           O  
ATOM   1104  ND2 ASN A 151      24.000  10.396  36.772  1.00 26.99           N  
ATOM   1105  N   ASP A 152      26.083   6.885  34.437  1.00 29.71           N  
ATOM   1106  CA  ASP A 152      26.039   5.410  34.448  1.00 30.06           C  
ATOM   1107  C   ASP A 152      24.850   4.733  35.075  1.00 29.51           C  
ATOM   1108  O   ASP A 152      24.771   3.503  35.026  1.00 28.98           O  
ATOM   1109  CB  ASP A 152      27.199   4.829  35.250  1.00 30.99           C  
ATOM   1110  CG  ASP A 152      28.447   5.561  35.048  1.00 33.80           C  
ATOM   1111  OD1 ASP A 152      28.636   6.071  33.918  1.00 40.13           O  
ATOM   1112  OD2 ASP A 152      29.274   5.719  35.960  1.00 35.65           O  
ATOM   1113  N   THR A 153      23.959   5.468  35.722  1.00 28.96           N  
ATOM   1114  CA  THR A 153      22.831   4.792  36.359  1.00 28.42           C  
ATOM   1115  C   THR A 153      21.685   4.594  35.387  1.00 27.75           C  
ATOM   1116  O   THR A 153      20.730   3.909  35.712  1.00 27.68           O  
ATOM   1117  CB  THR A 153      22.330   5.552  37.584  1.00 28.53           C  
ATOM   1118  OG1 THR A 153      21.833   6.836  37.193  1.00 28.91           O  
ATOM   1119  CG2 THR A 153      23.473   5.855  38.540  1.00 29.18           C  
ATOM   1120  N   VAL A 154      21.766   5.171  34.194  1.00 26.76           N  
ATOM   1121  CA  VAL A 154      20.671   4.996  33.246  1.00 26.61           C  
ATOM   1122  C   VAL A 154      20.583   3.531  32.895  1.00 26.77           C  
ATOM   1123  O   VAL A 154      21.592   2.832  32.923  1.00 27.36           O  
ATOM   1124  CB  VAL A 154      20.838   5.826  31.964  1.00 26.05           C  
ATOM   1125  CG1 VAL A 154      20.914   7.279  32.312  1.00 26.14           C  
ATOM   1126  CG2 VAL A 154      22.071   5.383  31.182  1.00 25.62           C  
ATOM   1127  N   GLY A 155      19.379   3.072  32.568  1.00 26.71           N  
ATOM   1128  CA  GLY A 155      19.147   1.674  32.252  1.00 26.42           C  
ATOM   1129  C   GLY A 155      19.531   1.266  30.840  1.00 26.67           C  
ATOM   1130  O   GLY A 155      19.894   2.093  29.983  1.00 26.52           O  
ATOM   1131  N   ARG A 156      19.390  -0.028  30.599  1.00 26.49           N  
ATOM   1132  CA  ARG A 156      19.811  -0.684  29.364  1.00 26.54           C  
ATOM   1133  C   ARG A 156      19.305  -0.053  28.068  1.00 25.95           C  
ATOM   1134  O   ARG A 156      20.089   0.194  27.160  1.00 26.26           O  
ATOM   1135  CB  ARG A 156      19.429  -2.165  29.418  1.00 26.28           C  
ATOM   1136  N   LYS A 157      18.004   0.175  27.964  1.00 25.43           N  
ATOM   1137  CA  LYS A 157      17.460   0.777  26.756  1.00 25.11           C  
ATOM   1138  C   LYS A 157      18.026   2.198  26.517  1.00 25.50           C  
ATOM   1139  O   LYS A 157      18.249   2.595  25.372  1.00 25.14           O  
ATOM   1140  CB  LYS A 157      15.927   0.796  26.809  1.00 24.88           C  
ATOM   1141  CG  LYS A 157      15.255  -0.572  26.516  1.00 24.25           C  
ATOM   1142  N   ILE A 158      18.257   2.956  27.585  1.00 25.35           N  
ATOM   1143  CA  ILE A 158      18.766   4.326  27.432  1.00 25.61           C  
ATOM   1144  C   ILE A 158      20.205   4.250  26.971  1.00 25.76           C  
ATOM   1145  O   ILE A 158      20.661   5.058  26.166  1.00 25.39           O  
ATOM   1146  CB  ILE A 158      18.662   5.107  28.740  1.00 25.41           C  
ATOM   1147  CG1 ILE A 158      17.202   5.245  29.162  1.00 25.92           C  
ATOM   1148  CG2 ILE A 158      19.297   6.475  28.601  1.00 25.61           C  
ATOM   1149  CD1 ILE A 158      16.331   5.924  28.174  1.00 27.88           C  
ATOM   1150  N   VAL A 159      20.909   3.251  27.481  1.00 26.10           N  
ATOM   1151  CA  VAL A 159      22.276   3.010  27.079  1.00 26.57           C  
ATOM   1152  C   VAL A 159      22.279   2.703  25.585  1.00 26.40           C  
ATOM   1153  O   VAL A 159      23.074   3.248  24.840  1.00 26.32           O  
ATOM   1154  CB  VAL A 159      22.895   1.850  27.883  1.00 26.94           C  
ATOM   1155  CG1 VAL A 159      24.136   1.310  27.193  1.00 27.73           C  
ATOM   1156  CG2 VAL A 159      23.223   2.308  29.298  1.00 26.73           C  
ATOM   1157  N   MET A 160      21.363   1.852  25.145  1.00 26.48           N  
ATOM   1158  CA  MET A 160      21.270   1.518  23.721  1.00 26.52           C  
ATOM   1159  C   MET A 160      20.985   2.771  22.880  1.00 25.02           C  
ATOM   1160  O   MET A 160      21.600   2.986  21.845  1.00 24.31           O  
ATOM   1161  CB  MET A 160      20.183   0.476  23.485  1.00 27.05           C  
ATOM   1162  CG  MET A 160      20.540  -0.900  24.001  1.00 30.45           C  
ATOM   1163  SD  MET A 160      21.843  -1.730  23.058  1.00 34.87           S  
ATOM   1164  CE  MET A 160      20.957  -2.028  21.496  1.00 36.94           C  
ATOM   1165  N   ASP A 161      20.047   3.589  23.342  1.00 23.96           N  
ATOM   1166  CA  ASP A 161      19.699   4.831  22.665  1.00 23.14           C  
ATOM   1167  C   ASP A 161      20.890   5.781  22.550  1.00 21.93           C  
ATOM   1168  O   ASP A 161      21.167   6.323  21.480  1.00 21.41           O  
ATOM   1169  CB  ASP A 161      18.549   5.528  23.402  1.00 23.13           C  
ATOM   1170  CG  ASP A 161      17.250   4.762  23.293  1.00 24.08           C  
ATOM   1171  OD1 ASP A 161      17.182   3.812  22.478  1.00 21.27           O  
ATOM   1172  OD2 ASP A 161      16.248   5.035  23.980  1.00 25.87           O  
ATOM   1173  N   PHE A 162      21.575   5.973  23.671  1.00 20.59           N  
ATOM   1174  CA  PHE A 162      22.712   6.859  23.765  1.00 19.97           C  
ATOM   1175  C   PHE A 162      23.802   6.409  22.809  1.00 19.19           C  
ATOM   1176  O   PHE A 162      24.410   7.213  22.160  1.00 18.98           O  
ATOM   1177  CB  PHE A 162      23.223   6.859  25.220  1.00 20.44           C  
ATOM   1178  CG  PHE A 162      24.386   7.755  25.470  1.00 20.78           C  
ATOM   1179  CD1 PHE A 162      24.206   9.107  25.673  1.00 25.50           C  
ATOM   1180  CD2 PHE A 162      25.662   7.245  25.542  1.00 23.71           C  
ATOM   1181  CE1 PHE A 162      25.290   9.930  25.935  1.00 25.85           C  
ATOM   1182  CE2 PHE A 162      26.755   8.072  25.795  1.00 24.89           C  
ATOM   1183  CZ  PHE A 162      26.572   9.394  26.001  1.00 23.50           C  
ATOM   1184  N   LEU A 163      24.062   5.115  22.744  1.00 19.25           N  
ATOM   1185  CA  LEU A 163      25.084   4.597  21.838  1.00 19.42           C  
ATOM   1186  C   LEU A 163      24.715   4.804  20.361  1.00 18.63           C  
ATOM   1187  O   LEU A 163      25.585   4.831  19.493  1.00 18.21           O  
ATOM   1188  CB  LEU A 163      25.297   3.115  22.104  1.00 19.49           C  
ATOM   1189  CG  LEU A 163      25.988   2.812  23.422  1.00 20.88           C  
ATOM   1190  CD1 LEU A 163      25.980   1.319  23.651  1.00 22.44           C  
ATOM   1191  CD2 LEU A 163      27.407   3.368  23.396  1.00 21.73           C  
ATOM   1192  N   GLY A 164      23.419   4.917  20.104  1.00 18.01           N  
ATOM   1193  CA  GLY A 164      22.889   5.158  18.779  1.00 18.55           C  
ATOM   1194  C   GLY A 164      22.873   6.622  18.355  1.00 18.40           C  
ATOM   1195  O   GLY A 164      22.406   6.921  17.256  1.00 19.24           O  
ATOM   1196  N   PHE A 165      23.365   7.521  19.209  1.00 17.50           N  
ATOM   1197  CA  PHE A 165      23.493   8.913  18.831  1.00 17.67           C  
ATOM   1198  C   PHE A 165      24.497   8.955  17.663  1.00 17.49           C  
ATOM   1199  O   PHE A 165      25.293   8.028  17.497  1.00 16.10           O  
ATOM   1200  CB  PHE A 165      23.984   9.753  20.018  1.00 17.47           C  
ATOM   1201  CG  PHE A 165      22.932  10.004  21.098  1.00 18.51           C  
ATOM   1202  CD1 PHE A 165      21.645   9.479  21.009  1.00 19.26           C  
ATOM   1203  CD2 PHE A 165      23.242  10.784  22.203  1.00 18.52           C  
ATOM   1204  CE1 PHE A 165      20.697   9.730  21.996  1.00 18.44           C  
ATOM   1205  CE2 PHE A 165      22.303  11.030  23.199  1.00 18.52           C  
ATOM   1206  CZ  PHE A 165      21.032  10.500  23.100  1.00 18.90           C  
ATOM   1207  N   ASN A 166      24.466  10.009  16.854  1.00 17.77           N  
ATOM   1208  CA  ASN A 166      25.393  10.110  15.712  1.00 18.29           C  
ATOM   1209  C   ASN A 166      26.787  10.622  16.129  1.00 18.73           C  
ATOM   1210  O   ASN A 166      27.156  11.795  15.897  1.00 19.54           O  
ATOM   1211  CB  ASN A 166      24.793  10.972  14.598  1.00 17.92           C  
ATOM   1212  CG  ASN A 166      25.571  10.861  13.293  1.00 17.28           C  
ATOM   1213  OD1 ASN A 166      26.679  10.289  13.262  1.00 16.53           O  
ATOM   1214  ND2 ASN A 166      24.994  11.395  12.204  1.00 12.92           N  
ATOM   1215  N   TRP A 167      27.527   9.739  16.789  1.00 19.26           N  
ATOM   1216  CA  TRP A 167      28.867  10.035  17.264  1.00 19.76           C  
ATOM   1217  C   TRP A 167      29.785  10.266  16.084  1.00 19.88           C  
ATOM   1218  O   TRP A 167      30.731  11.031  16.169  1.00 19.35           O  
ATOM   1219  CB  TRP A 167      29.384   8.864  18.130  1.00 19.92           C  
ATOM   1220  CG  TRP A 167      28.556   8.728  19.351  1.00 20.39           C  
ATOM   1221  CD1 TRP A 167      27.686   7.727  19.656  1.00 20.85           C  
ATOM   1222  CD2 TRP A 167      28.445   9.686  20.400  1.00 20.99           C  
ATOM   1223  NE1 TRP A 167      27.059   7.995  20.851  1.00 21.18           N  
ATOM   1224  CE2 TRP A 167      27.509   9.194  21.325  1.00 20.70           C  
ATOM   1225  CE3 TRP A 167      29.065  10.916  20.664  1.00 21.55           C  
ATOM   1226  CZ2 TRP A 167      27.183   9.871  22.488  1.00 22.63           C  
ATOM   1227  CZ3 TRP A 167      28.731  11.589  21.804  1.00 21.78           C  
ATOM   1228  CH2 TRP A 167      27.789  11.071  22.706  1.00 22.79           C  
ATOM   1229  N   ASN A 168      29.529   9.577  14.979  1.00 20.07           N  
ATOM   1230  CA  ASN A 168      30.374   9.759  13.818  1.00 20.50           C  
ATOM   1231  C   ASN A 168      30.396  11.237  13.421  1.00 20.67           C  
ATOM   1232  O   ASN A 168      31.465  11.806  13.207  1.00 19.54           O  
ATOM   1233  CB  ASN A 168      29.917   8.930  12.628  1.00 20.87           C  
ATOM   1234  CG  ASN A 168      30.818   9.129  11.423  1.00 22.96           C  
ATOM   1235  OD1 ASN A 168      32.027   8.923  11.522  1.00 25.54           O  
ATOM   1236  ND2 ASN A 168      30.247   9.578  10.295  1.00 23.09           N  
ATOM   1237  N   TRP A 169      29.211  11.844  13.338  1.00 20.57           N  
ATOM   1238  CA  TRP A 169      29.106  13.226  12.917  1.00 20.23           C  
ATOM   1239  C   TRP A 169      29.653  14.188  13.972  1.00 20.59           C  
ATOM   1240  O   TRP A 169      30.367  15.118  13.634  1.00 20.09           O  
ATOM   1241  CB  TRP A 169      27.662  13.618  12.570  1.00 20.35           C  
ATOM   1242  CG  TRP A 169      27.542  15.101  12.238  1.00 19.49           C  
ATOM   1243  CD1 TRP A 169      27.769  15.693  11.026  1.00 19.03           C  
ATOM   1244  CD2 TRP A 169      27.203  16.157  13.137  1.00 20.25           C  
ATOM   1245  NE1 TRP A 169      27.578  17.052  11.117  1.00 20.36           N  
ATOM   1246  CE2 TRP A 169      27.244  17.366  12.406  1.00 19.45           C  
ATOM   1247  CE3 TRP A 169      26.874  16.207  14.492  1.00 20.60           C  
ATOM   1248  CZ2 TRP A 169      26.964  18.600  12.975  1.00 21.03           C  
ATOM   1249  CZ3 TRP A 169      26.614  17.433  15.064  1.00 23.09           C  
ATOM   1250  CH2 TRP A 169      26.649  18.621  14.297  1.00 23.61           C  
ATOM   1251  N   ILE A 170      29.326  13.979  15.239  1.00 20.47           N  
ATOM   1252  CA  ILE A 170      29.759  14.926  16.241  1.00 20.67           C  
ATOM   1253  C   ILE A 170      31.262  14.772  16.567  1.00 21.18           C  
ATOM   1254  O   ILE A 170      31.943  15.758  16.836  1.00 21.20           O  
ATOM   1255  CB  ILE A 170      28.842  14.892  17.483  1.00 20.61           C  
ATOM   1256  CG1 ILE A 170      28.900  16.231  18.221  1.00 20.05           C  
ATOM   1257  CG2 ILE A 170      29.191  13.755  18.402  1.00 19.89           C  
ATOM   1258  CD1 ILE A 170      27.865  16.353  19.329  1.00 21.00           C  
ATOM   1259  N   ASN A 171      31.780  13.556  16.527  1.00 20.74           N  
ATOM   1260  CA  ASN A 171      33.214  13.355  16.715  1.00 21.80           C  
ATOM   1261  C   ASN A 171      34.024  14.093  15.634  1.00 22.34           C  
ATOM   1262  O   ASN A 171      35.093  14.652  15.916  1.00 21.98           O  
ATOM   1263  CB  ASN A 171      33.581  11.857  16.718  1.00 21.55           C  
ATOM   1264  CG  ASN A 171      33.111  11.124  17.981  1.00 21.20           C  
ATOM   1265  OD1 ASN A 171      32.637  11.724  18.963  1.00 21.35           O  
ATOM   1266  ND2 ASN A 171      33.263   9.830  17.962  1.00 19.36           N  
ATOM   1267  N   LYS A 172      33.529  14.097  14.400  1.00 22.97           N  
ATOM   1268  CA  LYS A 172      34.218  14.847  13.353  1.00 24.09           C  
ATOM   1269  C   LYS A 172      34.167  16.342  13.656  1.00 23.61           C  
ATOM   1270  O   LYS A 172      35.166  17.041  13.511  1.00 23.54           O  
ATOM   1271  CB  LYS A 172      33.669  14.529  11.961  1.00 24.58           C  
ATOM   1272  CG  LYS A 172      34.087  13.163  11.491  1.00 27.56           C  
ATOM   1273  CD  LYS A 172      33.653  12.852  10.034  1.00 31.03           C  
ATOM   1274  CE  LYS A 172      34.323  11.576   9.565  1.00 33.01           C  
ATOM   1275  NZ  LYS A 172      34.357  11.406   8.070  1.00 36.89           N  
ATOM   1276  N   GLN A 173      33.019  16.834  14.109  1.00 23.74           N  
ATOM   1277  CA  GLN A 173      32.914  18.245  14.482  1.00 23.87           C  
ATOM   1278  C   GLN A 173      33.960  18.578  15.547  1.00 23.86           C  
ATOM   1279  O   GLN A 173      34.739  19.500  15.374  1.00 24.25           O  
ATOM   1280  CB  GLN A 173      31.517  18.590  14.993  1.00 23.63           C  
ATOM   1281  CG  GLN A 173      30.451  18.619  13.916  1.00 24.53           C  
ATOM   1282  CD  GLN A 173      30.753  19.634  12.851  1.00 25.08           C  
ATOM   1283  OE1 GLN A 173      31.194  20.740  13.157  1.00 26.69           O  
ATOM   1284  NE2 GLN A 173      30.512  19.273  11.601  1.00 23.36           N  
ATOM   1285  N   GLN A 174      33.963  17.822  16.635  1.00 23.63           N  
ATOM   1286  CA  GLN A 174      34.925  17.995  17.717  1.00 23.91           C  
ATOM   1287  C   GLN A 174      36.365  18.053  17.161  1.00 24.01           C  
ATOM   1288  O   GLN A 174      37.133  18.962  17.480  1.00 23.39           O  
ATOM   1289  CB  GLN A 174      34.783  16.840  18.717  1.00 23.67           C  
ATOM   1290  CG  GLN A 174      35.688  16.913  19.934  1.00 24.07           C  
ATOM   1291  CD  GLN A 174      35.595  15.668  20.799  1.00 25.12           C  
ATOM   1292  OE1 GLN A 174      35.229  14.602  20.312  1.00 25.70           O  
ATOM   1293  NE2 GLN A 174      35.901  15.803  22.084  1.00 23.63           N  
ATOM   1294  N   GLY A 175      36.706  17.080  16.334  1.00 23.75           N  
ATOM   1295  CA  GLY A 175      38.005  17.028  15.696  1.00 24.73           C  
ATOM   1296  C   GLY A 175      38.268  18.209  14.768  1.00 25.21           C  
ATOM   1297  O   GLY A 175      39.310  18.842  14.854  1.00 25.60           O  
ATOM   1298  N   LYS A 176      37.327  18.518  13.888  1.00 25.81           N  
ATOM   1299  CA  LYS A 176      37.491  19.634  12.961  1.00 26.88           C  
ATOM   1300  C   LYS A 176      37.719  20.997  13.638  1.00 26.95           C  
ATOM   1301  O   LYS A 176      38.490  21.803  13.136  1.00 26.74           O  
ATOM   1302  CB  LYS A 176      36.256  19.778  12.077  1.00 27.35           C  
ATOM   1303  CG  LYS A 176      36.093  18.716  11.009  1.00 29.87           C  
ATOM   1304  CD  LYS A 176      34.894  19.085  10.137  1.00 33.21           C  
ATOM   1305  CE  LYS A 176      33.948  17.932   9.961  1.00 35.30           C  
ATOM   1306  NZ  LYS A 176      32.558  18.388   9.643  1.00 37.22           N  
ATOM   1307  N   ARG A 177      37.031  21.257  14.749  1.00 26.93           N  
ATOM   1308  CA  ARG A 177      37.153  22.539  15.435  1.00 27.36           C  
ATOM   1309  C   ARG A 177      38.241  22.611  16.509  1.00 26.63           C  
ATOM   1310  O   ARG A 177      38.402  23.650  17.135  1.00 25.85           O  
ATOM   1311  CB  ARG A 177      35.832  22.902  16.114  1.00 27.86           C  
ATOM   1312  CG  ARG A 177      34.625  22.712  15.267  1.00 29.88           C  
ATOM   1313  CD  ARG A 177      34.653  23.460  13.973  1.00 32.39           C  
ATOM   1314  NE  ARG A 177      33.683  22.854  13.084  1.00 34.54           N  
ATOM   1315  CZ  ARG A 177      33.841  22.701  11.790  1.00 37.31           C  
ATOM   1316  NH1 ARG A 177      34.952  23.110  11.189  1.00 38.34           N  
ATOM   1317  NH2 ARG A 177      32.877  22.126  11.088  1.00 38.88           N  
ATOM   1318  N   GLY A 178      38.950  21.510  16.743  1.00 26.35           N  
ATOM   1319  CA  GLY A 178      39.998  21.470  17.753  1.00 25.46           C  
ATOM   1320  C   GLY A 178      39.473  21.514  19.176  1.00 25.27           C  
ATOM   1321  O   GLY A 178      40.213  21.818  20.123  1.00 25.46           O  
ATOM   1322  N   TRP A 179      38.199  21.202  19.359  1.00 24.30           N  
ATOM   1323  CA  TRP A 179      37.639  21.260  20.692  1.00 24.02           C  
ATOM   1324  C   TRP A 179      38.290  20.266  21.638  1.00 23.85           C  
ATOM   1325  O   TRP A 179      38.958  19.333  21.226  1.00 22.62           O  
ATOM   1326  CB  TRP A 179      36.136  21.011  20.674  1.00 23.73           C  
ATOM   1327  CG  TRP A 179      35.346  22.061  19.962  1.00 23.92           C  
ATOM   1328  CD1 TRP A 179      35.787  23.291  19.531  1.00 22.69           C  
ATOM   1329  CD2 TRP A 179      33.968  21.981  19.594  1.00 23.74           C  
ATOM   1330  NE1 TRP A 179      34.765  23.968  18.912  1.00 24.45           N  
ATOM   1331  CE2 TRP A 179      33.636  23.183  18.929  1.00 24.47           C  
ATOM   1332  CE3 TRP A 179      32.984  21.002  19.730  1.00 23.10           C  
ATOM   1333  CZ2 TRP A 179      32.379  23.422  18.414  1.00 23.69           C  
ATOM   1334  CZ3 TRP A 179      31.733  21.241  19.211  1.00 21.89           C  
ATOM   1335  CH2 TRP A 179      31.435  22.445  18.573  1.00 23.90           C  
ATOM   1336  N   GLY A 180      38.080  20.499  22.925  1.00 24.08           N  
ATOM   1337  CA  GLY A 180      38.488  19.558  23.941  1.00 24.08           C  
ATOM   1338  C   GLY A 180      37.437  18.476  24.103  1.00 24.64           C  
ATOM   1339  O   GLY A 180      36.618  18.234  23.202  1.00 24.66           O  
ATOM   1340  N   GLN A 181      37.437  17.830  25.261  1.00 24.77           N  
ATOM   1341  CA  GLN A 181      36.575  16.682  25.471  1.00 25.23           C  
ATOM   1342  C   GLN A 181      35.117  17.039  25.725  1.00 24.50           C  
ATOM   1343  O   GLN A 181      34.779  18.151  26.149  1.00 24.42           O  
ATOM   1344  CB  GLN A 181      37.094  15.847  26.646  1.00 25.76           C  
ATOM   1345  CG  GLN A 181      36.720  16.409  28.025  1.00 28.85           C  
ATOM   1346  CD  GLN A 181      37.046  15.434  29.156  1.00 33.38           C  
ATOM   1347  OE1 GLN A 181      38.186  15.003  29.293  1.00 36.10           O  
ATOM   1348  NE2 GLN A 181      36.044  15.085  29.958  1.00 36.04           N  
ATOM   1349  N   LEU A 182      34.262  16.078  25.423  1.00 23.71           N  
ATOM   1350  CA  LEU A 182      32.857  16.110  25.792  1.00 23.70           C  
ATOM   1351  C   LEU A 182      32.876  16.040  27.317  1.00 22.68           C  
ATOM   1352  O   LEU A 182      33.406  15.079  27.849  1.00 21.72           O  
ATOM   1353  CB  LEU A 182      32.179  14.836  25.273  1.00 23.82           C  
ATOM   1354  CG  LEU A 182      30.661  14.693  25.199  1.00 26.38           C  
ATOM   1355  CD1 LEU A 182      30.243  13.231  25.368  1.00 26.04           C  
ATOM   1356  CD2 LEU A 182      29.977  15.501  26.192  1.00 29.73           C  
ATOM   1357  N   THR A 183      32.323  17.031  28.021  1.00 21.93           N  
ATOM   1358  CA  THR A 183      32.300  16.971  29.484  1.00 21.44           C  
ATOM   1359  C   THR A 183      31.004  16.388  29.984  1.00 21.27           C  
ATOM   1360  O   THR A 183      30.972  15.766  31.032  1.00 21.29           O  
ATOM   1361  CB  THR A 183      32.490  18.362  30.150  1.00 21.73           C  
ATOM   1362  OG1 THR A 183      31.463  19.257  29.715  1.00 20.35           O  
ATOM   1363  CG2 THR A 183      33.796  19.015  29.725  1.00 20.91           C  
ATOM   1364  N   SER A 184      29.918  16.590  29.251  1.00 21.42           N  
ATOM   1365  CA  SER A 184      28.649  16.053  29.689  1.00 21.45           C  
ATOM   1366  C   SER A 184      27.537  16.272  28.714  1.00 21.46           C  
ATOM   1367  O   SER A 184      27.672  17.031  27.753  1.00 21.17           O  
ATOM   1368  CB  SER A 184      28.243  16.687  31.006  1.00 21.74           C  
ATOM   1369  OG  SER A 184      27.919  18.049  30.845  1.00 23.24           O  
ATOM   1370  N   ASN A 185      26.445  15.575  28.982  1.00 21.21           N  
ATOM   1371  CA  ASN A 185      25.216  15.712  28.245  1.00 22.29           C  
ATOM   1372  C   ASN A 185      24.154  16.005  29.273  1.00 22.08           C  
ATOM   1373  O   ASN A 185      23.886  15.184  30.135  1.00 22.25           O  
ATOM   1374  CB  ASN A 185      24.856  14.416  27.497  1.00 22.67           C  
ATOM   1375  CG  ASN A 185      25.885  14.037  26.454  1.00 23.57           C  
ATOM   1376  OD1 ASN A 185      26.646  13.097  26.655  1.00 27.51           O  
ATOM   1377  ND2 ASN A 185      25.905  14.754  25.329  1.00 24.27           N  
ATOM   1378  N   LEU A 186      23.574  17.189  29.202  1.00 22.01           N  
ATOM   1379  CA  LEU A 186      22.529  17.563  30.135  1.00 22.03           C  
ATOM   1380  C   LEU A 186      21.170  17.219  29.558  1.00 22.00           C  
ATOM   1381  O   LEU A 186      20.844  17.592  28.435  1.00 22.34           O  
ATOM   1382  CB  LEU A 186      22.578  19.065  30.423  1.00 21.68           C  
ATOM   1383  CG  LEU A 186      21.707  19.538  31.588  1.00 22.25           C  
ATOM   1384  CD1 LEU A 186      22.252  18.985  32.891  1.00 22.43           C  
ATOM   1385  CD2 LEU A 186      21.643  21.098  31.648  1.00 23.35           C  
ATOM   1386  N   LEU A 187      20.377  16.518  30.344  1.00 22.19           N  
ATOM   1387  CA  LEU A 187      19.009  16.198  29.979  1.00 21.95           C  
ATOM   1388  C   LEU A 187      18.149  17.286  30.603  1.00 21.91           C  
ATOM   1389  O   LEU A 187      18.232  17.521  31.823  1.00 21.61           O  
ATOM   1390  CB  LEU A 187      18.616  14.830  30.527  1.00 21.55           C  
ATOM   1391  CG  LEU A 187      17.129  14.488  30.477  1.00 22.78           C  
ATOM   1392  CD1 LEU A 187      16.616  14.429  29.054  1.00 23.66           C  
ATOM   1393  CD2 LEU A 187      16.866  13.143  31.174  1.00 22.84           C  
ATOM   1394  N   LEU A 188      17.348  17.956  29.770  1.00 21.56           N  
ATOM   1395  CA  LEU A 188      16.461  19.000  30.227  1.00 22.26           C  
ATOM   1396  C   LEU A 188      14.993  18.662  29.920  1.00 22.55           C  
ATOM   1397  O   LEU A 188      14.588  18.517  28.760  1.00 23.16           O  
ATOM   1398  CB  LEU A 188      16.827  20.327  29.562  1.00 22.84           C  
ATOM   1399  CG  LEU A 188      18.244  20.840  29.821  1.00 22.60           C  
ATOM   1400  CD1 LEU A 188      18.967  21.111  28.523  1.00 23.92           C  
ATOM   1401  CD2 LEU A 188      18.177  22.088  30.655  1.00 24.56           C  
ATOM   1402  N   ILE A 189      14.181  18.577  30.958  1.00 22.15           N  
ATOM   1403  CA  ILE A 189      12.769  18.315  30.756  1.00 22.34           C  
ATOM   1404  C   ILE A 189      11.996  19.395  31.460  1.00 22.37           C  
ATOM   1405  O   ILE A 189      12.072  19.528  32.692  1.00 22.77           O  
ATOM   1406  CB  ILE A 189      12.377  16.953  31.281  1.00 21.60           C  
ATOM   1407  CG1 ILE A 189      13.254  15.888  30.638  1.00 21.85           C  
ATOM   1408  CG2 ILE A 189      10.928  16.708  30.958  1.00 22.51           C  
ATOM   1409  CD1 ILE A 189      12.918  14.425  31.075  1.00 23.06           C  
ATOM   1410  N   GLY A 190      11.276  20.186  30.673  1.00 22.37           N  
ATOM   1411  CA  GLY A 190      10.587  21.336  31.206  1.00 22.29           C  
ATOM   1412  C   GLY A 190       9.124  21.342  30.902  1.00 22.48           C  
ATOM   1413  O   GLY A 190       8.652  20.633  30.007  1.00 22.39           O  
ATOM   1414  N   MET A 191       8.402  22.134  31.687  1.00 22.74           N  
ATOM   1415  CA  MET A 191       6.991  22.339  31.467  1.00 23.16           C  
ATOM   1416  C   MET A 191       6.838  23.482  30.478  1.00 22.94           C  
ATOM   1417  O   MET A 191       7.738  24.329  30.338  1.00 23.03           O  
ATOM   1418  CB  MET A 191       6.283  22.673  32.784  1.00 23.69           C  
ATOM   1419  CG  MET A 191       6.224  21.513  33.741  1.00 25.02           C  
ATOM   1420  SD  MET A 191       5.664  21.927  35.415  1.00 28.11           S  
ATOM   1421  CE  MET A 191       4.016  22.460  35.097  1.00 28.35           C  
ATOM   1422  N   GLU A 192       5.712  23.492  29.773  1.00 22.60           N  
ATOM   1423  CA  GLU A 192       5.410  24.544  28.810  1.00 22.83           C  
ATOM   1424  C   GLU A 192       5.495  25.895  29.490  1.00 22.51           C  
ATOM   1425  O   GLU A 192       5.062  26.046  30.614  1.00 22.41           O  
ATOM   1426  CB  GLU A 192       4.005  24.342  28.249  1.00 22.86           C  
ATOM   1427  CG  GLU A 192       2.925  24.367  29.315  1.00 24.36           C  
ATOM   1428  CD  GLU A 192       1.572  23.891  28.814  1.00 25.71           C  
ATOM   1429  OE1 GLU A 192       1.503  23.294  27.718  1.00 25.51           O  
ATOM   1430  OE2 GLU A 192       0.582  24.128  29.525  1.00 26.30           O  
ATOM   1431  N   GLY A 193       6.069  26.888  28.828  1.00 22.95           N  
ATOM   1432  CA  GLY A 193       6.185  28.199  29.444  1.00 22.50           C  
ATOM   1433  C   GLY A 193       7.465  28.414  30.254  1.00 22.36           C  
ATOM   1434  O   GLY A 193       7.756  29.544  30.602  1.00 23.08           O  
ATOM   1435  N   ASN A 194       8.219  27.361  30.566  1.00 21.60           N  
ATOM   1436  CA  ASN A 194       9.456  27.506  31.341  1.00 21.44           C  
ATOM   1437  C   ASN A 194      10.489  28.320  30.581  1.00 21.19           C  
ATOM   1438  O   ASN A 194      10.635  28.134  29.372  1.00 22.08           O  
ATOM   1439  CB  ASN A 194      10.099  26.147  31.629  1.00 21.05           C  
ATOM   1440  CG  ASN A 194       9.494  25.435  32.801  1.00 20.86           C  
ATOM   1441  OD1 ASN A 194       8.509  25.883  33.385  1.00 22.48           O  
ATOM   1442  ND2 ASN A 194      10.092  24.312  33.167  1.00 17.74           N  
ATOM   1443  N   VAL A 195      11.213  29.183  31.290  1.00 20.69           N  
ATOM   1444  CA  VAL A 195      12.268  29.993  30.701  1.00 20.84           C  
ATOM   1445  C   VAL A 195      13.572  29.854  31.450  1.00 20.06           C  
ATOM   1446  O   VAL A 195      13.601  29.874  32.681  1.00 20.75           O  
ATOM   1447  CB  VAL A 195      11.903  31.502  30.686  1.00 21.41           C  
ATOM   1448  CG1 VAL A 195      13.081  32.357  30.219  1.00 22.24           C  
ATOM   1449  CG2 VAL A 195      10.666  31.767  29.843  1.00 22.30           C  
ATOM   1450  N   THR A 196      14.651  29.673  30.702  1.00 19.51           N  
ATOM   1451  CA  THR A 196      15.993  29.737  31.257  1.00 19.52           C  
ATOM   1452  C   THR A 196      16.487  31.117  30.820  1.00 19.98           C  
ATOM   1453  O   THR A 196      16.653  31.352  29.620  1.00 19.56           O  
ATOM   1454  CB  THR A 196      16.896  28.677  30.675  1.00 19.26           C  
ATOM   1455  OG1 THR A 196      16.526  27.366  31.162  1.00 21.13           O  
ATOM   1456  CG2 THR A 196      18.309  28.886  31.185  1.00 19.85           C  
ATOM   1457  N   PRO A 197      16.627  32.043  31.767  1.00 20.27           N  
ATOM   1458  CA  PRO A 197      17.046  33.412  31.463  1.00 20.52           C  
ATOM   1459  C   PRO A 197      18.431  33.497  30.836  1.00 20.89           C  
ATOM   1460  O   PRO A 197      19.277  32.609  31.025  1.00 20.66           O  
ATOM   1461  CB  PRO A 197      17.018  34.099  32.825  1.00 21.22           C  
ATOM   1462  CG  PRO A 197      16.144  33.263  33.657  1.00 21.01           C  
ATOM   1463  CD  PRO A 197      16.309  31.872  33.189  1.00 20.28           C  
ATOM   1464  N   ALA A 198      18.633  34.577  30.089  1.00 20.28           N  
ATOM   1465  CA  ALA A 198      19.841  34.817  29.341  1.00 20.22           C  
ATOM   1466  C   ALA A 198      21.130  34.634  30.146  1.00 20.58           C  
ATOM   1467  O   ALA A 198      21.284  35.186  31.235  1.00 19.91           O  
ATOM   1468  CB  ALA A 198      19.791  36.222  28.759  1.00 20.52           C  
ATOM   1469  N   HIS A 199      22.062  33.891  29.563  1.00 20.87           N  
ATOM   1470  CA  HIS A 199      23.371  33.646  30.158  1.00 21.41           C  
ATOM   1471  C   HIS A 199      24.281  33.168  29.063  1.00 21.82           C  
ATOM   1472  O   HIS A 199      23.826  32.892  27.943  1.00 21.80           O  
ATOM   1473  CB  HIS A 199      23.305  32.534  31.198  1.00 21.44           C  
ATOM   1474  CG  HIS A 199      22.915  31.220  30.617  1.00 22.21           C  
ATOM   1475  ND1 HIS A 199      21.619  30.940  30.253  1.00 21.93           N  
ATOM   1476  CD2 HIS A 199      23.644  30.120  30.296  1.00 22.04           C  
ATOM   1477  CE1 HIS A 199      21.561  29.721  29.749  1.00 23.76           C  
ATOM   1478  NE2 HIS A 199      22.777  29.214  29.737  1.00 22.57           N  
ATOM   1479  N   TYR A 200      25.568  33.060  29.384  1.00 22.40           N  
ATOM   1480  CA  TYR A 200      26.536  32.456  28.469  1.00 22.34           C  
ATOM   1481  C   TYR A 200      27.225  31.316  29.197  1.00 22.03           C  
ATOM   1482  O   TYR A 200      27.328  31.330  30.425  1.00 21.90           O  
ATOM   1483  CB  TYR A 200      27.544  33.458  27.924  1.00 22.22           C  
ATOM   1484  CG  TYR A 200      28.517  34.051  28.924  1.00 22.16           C  
ATOM   1485  CD1 TYR A 200      29.746  33.454  29.171  1.00 21.36           C  
ATOM   1486  CD2 TYR A 200      28.236  35.246  29.565  1.00 22.58           C  
ATOM   1487  CE1 TYR A 200      30.638  33.997  30.052  1.00 21.48           C  
ATOM   1488  CE2 TYR A 200      29.128  35.806  30.462  1.00 21.46           C  
ATOM   1489  CZ  TYR A 200      30.334  35.189  30.695  1.00 22.03           C  
ATOM   1490  OH  TYR A 200      31.230  35.733  31.593  1.00 20.69           O  
ATOM   1491  N   ASP A 201      27.681  30.310  28.444  1.00 22.42           N  
ATOM   1492  CA  ASP A 201      28.381  29.152  29.048  1.00 22.10           C  
ATOM   1493  C   ASP A 201      29.801  29.142  28.531  1.00 21.96           C  
ATOM   1494  O   ASP A 201      30.018  29.601  27.433  1.00 22.26           O  
ATOM   1495  CB  ASP A 201      27.722  27.840  28.661  1.00 21.97           C  
ATOM   1496  CG  ASP A 201      26.311  27.714  29.181  1.00 21.99           C  
ATOM   1497  OD1 ASP A 201      26.126  27.649  30.421  1.00 22.61           O  
ATOM   1498  OD2 ASP A 201      25.330  27.624  28.412  1.00 19.35           O  
ATOM   1499  N   GLU A 202      30.769  28.620  29.283  1.00 21.66           N  
ATOM   1500  CA  GLU A 202      32.146  28.612  28.773  1.00 23.16           C  
ATOM   1501  C   GLU A 202      32.515  27.334  28.035  1.00 23.38           C  
ATOM   1502  O   GLU A 202      33.684  26.951  28.049  1.00 25.48           O  
ATOM   1503  CB  GLU A 202      33.178  28.774  29.897  1.00 23.46           C  
ATOM   1504  CG  GLU A 202      33.110  30.064  30.681  1.00 26.52           C  
ATOM   1505  CD  GLU A 202      34.233  30.132  31.704  1.00 28.11           C  
ATOM   1506  OE1 GLU A 202      34.207  29.387  32.698  1.00 29.06           O  
ATOM   1507  OE2 GLU A 202      35.148  30.920  31.490  1.00 31.04           O  
ATOM   1508  N   GLN A 203      31.538  26.632  27.476  1.00 22.70           N  
ATOM   1509  CA  GLN A 203      31.808  25.451  26.685  1.00 22.01           C  
ATOM   1510  C   GLN A 203      31.049  25.576  25.373  1.00 21.93           C  
ATOM   1511  O   GLN A 203      30.113  26.378  25.253  1.00 22.49           O  
ATOM   1512  CB  GLN A 203      31.409  24.169  27.427  1.00 22.02           C  
ATOM   1513  CG  GLN A 203      32.287  23.822  28.657  1.00 22.33           C  
ATOM   1514  CD  GLN A 203      32.103  22.379  29.165  1.00 23.14           C  
ATOM   1515  OE1 GLN A 203      31.948  21.448  28.370  1.00 21.46           O  
ATOM   1516  NE2 GLN A 203      32.138  22.203  30.489  1.00 21.21           N  
ATOM   1517  N   GLN A 204      31.486  24.807  24.380  1.00 21.81           N  
ATOM   1518  CA  GLN A 204      30.806  24.720  23.092  1.00 21.45           C  
ATOM   1519  C   GLN A 204      29.610  23.799  23.295  1.00 21.12           C  
ATOM   1520  O   GLN A 204      29.673  22.862  24.088  1.00 20.29           O  
ATOM   1521  CB  GLN A 204      31.740  24.140  22.040  1.00 21.75           C  
ATOM   1522  CG  GLN A 204      33.033  24.928  21.852  1.00 21.56           C  
ATOM   1523  CD  GLN A 204      32.856  26.198  21.000  1.00 21.57           C  
ATOM   1524  OE1 GLN A 204      31.741  26.609  20.692  1.00 20.30           O  
ATOM   1525  NE2 GLN A 204      33.966  26.776  20.594  1.00 18.60           N  
ATOM   1526  N   ASN A 205      28.522  24.060  22.580  1.00 21.25           N  
ATOM   1527  CA  ASN A 205      27.291  23.316  22.795  1.00 21.04           C  
ATOM   1528  C   ASN A 205      26.529  22.977  21.526  1.00 21.25           C  
ATOM   1529  O   ASN A 205      26.160  23.880  20.747  1.00 20.22           O  
ATOM   1530  CB  ASN A 205      26.387  24.194  23.654  1.00 21.95           C  
ATOM   1531  CG  ASN A 205      25.116  23.507  24.098  1.00 21.98           C  
ATOM   1532  OD1 ASN A 205      24.759  22.418  23.643  1.00 21.21           O  
ATOM   1533  ND2 ASN A 205      24.400  24.178  24.979  1.00 17.72           N  
ATOM   1534  N   PHE A 206      26.314  21.677  21.319  1.00 19.90           N  
ATOM   1535  CA  PHE A 206      25.339  21.230  20.354  1.00 19.77           C  
ATOM   1536  C   PHE A 206      24.085  20.869  21.150  1.00 19.25           C  
ATOM   1537  O   PHE A 206      24.094  19.939  21.959  1.00 19.15           O  
ATOM   1538  CB  PHE A 206      25.849  20.049  19.545  1.00 20.09           C  
ATOM   1539  CG  PHE A 206      26.786  20.442  18.454  1.00 19.77           C  
ATOM   1540  CD1 PHE A 206      26.371  21.294  17.453  1.00 22.21           C  
ATOM   1541  CD2 PHE A 206      28.079  19.973  18.435  1.00 20.21           C  
ATOM   1542  CE1 PHE A 206      27.213  21.643  16.434  1.00 22.06           C  
ATOM   1543  CE2 PHE A 206      28.941  20.336  17.418  1.00 20.66           C  
ATOM   1544  CZ  PHE A 206      28.504  21.190  16.427  1.00 22.18           C  
ATOM   1545  N   PHE A 207      23.009  21.596  20.869  1.00 18.42           N  
ATOM   1546  CA  PHE A 207      21.760  21.590  21.620  1.00 18.78           C  
ATOM   1547  C   PHE A 207      20.732  20.841  20.804  1.00 19.36           C  
ATOM   1548  O   PHE A 207      20.241  21.359  19.818  1.00 19.26           O  
ATOM   1549  CB  PHE A 207      21.366  23.063  21.836  1.00 18.70           C  
ATOM   1550  CG  PHE A 207      20.120  23.301  22.635  1.00 17.94           C  
ATOM   1551  CD1 PHE A 207      18.899  23.404  22.007  1.00 17.78           C  
ATOM   1552  CD2 PHE A 207      20.188  23.548  23.989  1.00 18.50           C  
ATOM   1553  CE1 PHE A 207      17.772  23.684  22.713  1.00 19.52           C  
ATOM   1554  CE2 PHE A 207      19.052  23.823  24.705  1.00 20.66           C  
ATOM   1555  CZ  PHE A 207      17.836  23.909  24.053  1.00 19.44           C  
ATOM   1556  N   ALA A 208      20.435  19.618  21.234  1.00 19.90           N  
ATOM   1557  CA  ALA A 208      19.628  18.670  20.469  1.00 20.17           C  
ATOM   1558  C   ALA A 208      18.210  18.541  20.991  1.00 20.52           C  
ATOM   1559  O   ALA A 208      17.971  17.946  22.047  1.00 20.61           O  
ATOM   1560  CB  ALA A 208      20.294  17.308  20.494  1.00 19.33           C  
ATOM   1561  N   GLN A 209      17.270  19.076  20.219  1.00 20.94           N  
ATOM   1562  CA  GLN A 209      15.880  19.062  20.627  1.00 20.82           C  
ATOM   1563  C   GLN A 209      15.227  17.712  20.323  1.00 20.75           C  
ATOM   1564  O   GLN A 209      15.401  17.129  19.224  1.00 19.59           O  
ATOM   1565  CB  GLN A 209      15.141  20.216  19.961  1.00 20.91           C  
ATOM   1566  CG  GLN A 209      13.735  20.431  20.463  1.00 20.52           C  
ATOM   1567  CD  GLN A 209      13.673  20.840  21.928  1.00 20.69           C  
ATOM   1568  OE1 GLN A 209      14.702  21.155  22.562  1.00 19.72           O  
ATOM   1569  NE2 GLN A 209      12.460  20.852  22.473  1.00 19.21           N  
ATOM   1570  N   ILE A 210      14.442  17.248  21.296  1.00 20.72           N  
ATOM   1571  CA  ILE A 210      13.853  15.922  21.252  1.00 21.43           C  
ATOM   1572  C   ILE A 210      12.334  15.911  21.292  1.00 21.72           C  
ATOM   1573  O   ILE A 210      11.728  15.195  20.534  1.00 22.12           O  
ATOM   1574  CB  ILE A 210      14.396  15.095  22.424  1.00 21.84           C  
ATOM   1575  CG1 ILE A 210      15.859  14.733  22.156  1.00 22.48           C  
ATOM   1576  CG2 ILE A 210      13.581  13.832  22.622  1.00 21.83           C  
ATOM   1577  CD1 ILE A 210      16.631  14.354  23.382  1.00 24.34           C  
ATOM   1578  N   LYS A 211      11.728  16.677  22.188  1.00 22.08           N  
ATOM   1579  CA  LYS A 211      10.279  16.715  22.319  1.00 21.72           C  
ATOM   1580  C   LYS A 211       9.858  18.130  22.564  1.00 21.67           C  
ATOM   1581  O   LYS A 211      10.468  18.841  23.372  1.00 20.87           O  
ATOM   1582  CB  LYS A 211       9.797  15.856  23.487  1.00 22.44           C  
ATOM   1583  CG  LYS A 211       8.267  15.562  23.479  1.00 23.29           C  
ATOM   1584  CD  LYS A 211       7.791  15.022  24.824  1.00 25.02           C  
ATOM   1585  CE  LYS A 211       6.494  14.215  24.757  1.00 26.00           C  
ATOM   1586  NZ  LYS A 211       5.561  14.522  23.634  1.00 26.43           N  
ATOM   1587  N   GLY A 212       8.798  18.541  21.875  1.00 21.35           N  
ATOM   1588  CA  GLY A 212       8.306  19.891  21.994  1.00 21.71           C  
ATOM   1589  C   GLY A 212       9.195  20.906  21.297  1.00 21.63           C  
ATOM   1590  O   GLY A 212      10.150  20.572  20.591  1.00 21.32           O  
ATOM   1591  N   TYR A 213       8.871  22.166  21.522  1.00 22.35           N  
ATOM   1592  CA  TYR A 213       9.533  23.279  20.862  1.00 22.42           C  
ATOM   1593  C   TYR A 213      10.028  24.293  21.868  1.00 22.33           C  
ATOM   1594  O   TYR A 213       9.340  24.589  22.853  1.00 21.55           O  
ATOM   1595  CB  TYR A 213       8.556  23.951  19.916  1.00 23.46           C  
ATOM   1596  CG  TYR A 213       8.114  23.034  18.815  1.00 24.81           C  
ATOM   1597  CD1 TYR A 213       7.100  22.112  19.020  1.00 28.16           C  
ATOM   1598  CD2 TYR A 213       8.751  23.051  17.589  1.00 26.74           C  
ATOM   1599  CE1 TYR A 213       6.716  21.237  18.011  1.00 28.91           C  
ATOM   1600  CE2 TYR A 213       8.378  22.193  16.585  1.00 28.63           C  
ATOM   1601  CZ  TYR A 213       7.366  21.295  16.795  1.00 29.44           C  
ATOM   1602  OH  TYR A 213       7.013  20.456  15.756  1.00 33.67           O  
ATOM   1603  N   LYS A 214      11.239  24.788  21.609  1.00 21.60           N  
ATOM   1604  CA  LYS A 214      11.875  25.793  22.414  1.00 21.89           C  
ATOM   1605  C   LYS A 214      12.312  26.947  21.528  1.00 21.62           C  
ATOM   1606  O   LYS A 214      12.878  26.747  20.442  1.00 22.07           O  
ATOM   1607  CB  LYS A 214      13.103  25.239  23.140  1.00 22.10           C  
ATOM   1608  CG  LYS A 214      12.796  24.385  24.338  1.00 22.63           C  
ATOM   1609  CD  LYS A 214      14.103  23.893  24.964  1.00 24.24           C  
ATOM   1610  CE  LYS A 214      13.923  23.478  26.402  1.00 23.54           C  
ATOM   1611  NZ  LYS A 214      15.169  22.872  26.951  1.00 22.10           N  
ATOM   1612  N   ARG A 215      12.007  28.156  21.974  1.00 20.97           N  
ATOM   1613  CA  ARG A 215      12.447  29.347  21.277  1.00 20.73           C  
ATOM   1614  C   ARG A 215      13.778  29.724  21.900  1.00 20.03           C  
ATOM   1615  O   ARG A 215      13.885  29.828  23.113  1.00 19.70           O  
ATOM   1616  CB  ARG A 215      11.461  30.470  21.493  1.00 21.30           C  
ATOM   1617  CG  ARG A 215      11.754  31.760  20.726  1.00 22.21           C  
ATOM   1618  CD  ARG A 215      11.177  32.925  21.473  1.00 24.71           C  
ATOM   1619  NE  ARG A 215      11.122  34.156  20.715  1.00 25.47           N  
ATOM   1620  CZ  ARG A 215      10.479  35.235  21.130  1.00 26.28           C  
ATOM   1621  NH1 ARG A 215       9.844  35.245  22.299  1.00 26.07           N  
ATOM   1622  NH2 ARG A 215      10.483  36.314  20.384  1.00 28.83           N  
ATOM   1623  N   CYS A 216      14.794  29.877  21.074  1.00 19.45           N  
ATOM   1624  CA  CYS A 216      16.116  30.219  21.554  1.00 19.58           C  
ATOM   1625  C   CYS A 216      16.503  31.587  20.993  1.00 19.92           C  
ATOM   1626  O   CYS A 216      16.503  31.774  19.789  1.00 20.16           O  
ATOM   1627  CB  CYS A 216      17.110  29.186  21.073  1.00 20.01           C  
ATOM   1628  SG  CYS A 216      16.693  27.450  21.462  1.00 21.39           S  
ATOM   1629  N   ILE A 217      16.812  32.530  21.878  1.00 19.28           N  
ATOM   1630  CA  ILE A 217      17.286  33.845  21.504  1.00 19.58           C  
ATOM   1631  C   ILE A 217      18.742  33.961  21.937  1.00 19.21           C  
ATOM   1632  O   ILE A 217      19.055  33.849  23.126  1.00 19.05           O  
ATOM   1633  CB  ILE A 217      16.424  34.943  22.168  1.00 19.88           C  
ATOM   1634  CG1 ILE A 217      14.926  34.687  21.878  1.00 20.56           C  
ATOM   1635  CG2 ILE A 217      16.803  36.312  21.627  1.00 20.25           C  
ATOM   1636  CD1 ILE A 217      13.984  35.692  22.488  1.00 20.99           C  
ATOM   1637  N   LEU A 218      19.620  34.176  20.965  1.00 19.01           N  
ATOM   1638  CA  LEU A 218      21.048  34.271  21.222  1.00 19.61           C  
ATOM   1639  C   LEU A 218      21.568  35.682  20.970  1.00 20.43           C  
ATOM   1640  O   LEU A 218      21.018  36.414  20.136  1.00 19.76           O  
ATOM   1641  CB  LEU A 218      21.816  33.329  20.308  1.00 19.66           C  
ATOM   1642  CG  LEU A 218      21.906  31.881  20.778  1.00 19.74           C  
ATOM   1643  CD1 LEU A 218      20.549  31.237  20.905  1.00 20.56           C  
ATOM   1644  CD2 LEU A 218      22.733  31.099  19.798  1.00 21.32           C  
ATOM   1645  N   PHE A 219      22.626  36.046  21.700  1.00 20.11           N  
ATOM   1646  CA  PHE A 219      23.282  37.324  21.524  1.00 20.96           C  
ATOM   1647  C   PHE A 219      24.805  37.078  21.453  1.00 21.19           C  
ATOM   1648  O   PHE A 219      25.351  36.313  22.257  1.00 21.20           O  
ATOM   1649  CB  PHE A 219      22.942  38.304  22.678  1.00 20.97           C  
ATOM   1650  CG  PHE A 219      21.463  38.456  22.954  1.00 20.44           C  
ATOM   1651  CD1 PHE A 219      20.821  37.637  23.846  1.00 21.46           C  
ATOM   1652  CD2 PHE A 219      20.724  39.447  22.334  1.00 22.49           C  
ATOM   1653  CE1 PHE A 219      19.472  37.790  24.108  1.00 22.33           C  
ATOM   1654  CE2 PHE A 219      19.387  39.605  22.605  1.00 21.32           C  
ATOM   1655  CZ  PHE A 219      18.760  38.773  23.480  1.00 21.50           C  
ATOM   1656  N   PRO A 220      25.485  37.705  20.498  1.00 21.20           N  
ATOM   1657  CA  PRO A 220      26.936  37.541  20.368  1.00 21.72           C  
ATOM   1658  C   PRO A 220      27.683  38.108  21.569  1.00 21.31           C  
ATOM   1659  O   PRO A 220      27.165  38.972  22.280  1.00 20.90           O  
ATOM   1660  CB  PRO A 220      27.302  38.341  19.120  1.00 21.41           C  
ATOM   1661  CG  PRO A 220      26.020  38.781  18.510  1.00 23.12           C  
ATOM   1662  CD  PRO A 220      24.938  38.637  19.508  1.00 22.22           C  
ATOM   1663  N   PRO A 221      28.884  37.594  21.806  1.00 21.46           N  
ATOM   1664  CA  PRO A 221      29.721  38.053  22.918  1.00 21.33           C  
ATOM   1665  C   PRO A 221      29.961  39.556  22.940  1.00 21.04           C  
ATOM   1666  O   PRO A 221      30.220  40.096  24.009  1.00 20.68           O  
ATOM   1667  CB  PRO A 221      31.032  37.325  22.681  1.00 21.42           C  
ATOM   1668  CG  PRO A 221      30.656  36.134  21.939  1.00 22.42           C  
ATOM   1669  CD  PRO A 221      29.522  36.510  21.041  1.00 21.53           C  
ATOM   1670  N   ASP A 222      29.877  40.225  21.792  1.00 21.47           N  
ATOM   1671  CA  ASP A 222      30.128  41.669  21.749  1.00 21.80           C  
ATOM   1672  C   ASP A 222      28.946  42.464  22.271  1.00 21.74           C  
ATOM   1673  O   ASP A 222      28.970  43.685  22.261  1.00 22.16           O  
ATOM   1674  CB  ASP A 222      30.568  42.148  20.355  1.00 21.85           C  
ATOM   1675  CG  ASP A 222      29.433  42.151  19.325  1.00 24.83           C  
ATOM   1676  OD1 ASP A 222      28.311  41.668  19.585  1.00 25.32           O  
ATOM   1677  OD2 ASP A 222      29.595  42.607  18.186  1.00 29.30           O  
ATOM   1678  N   GLN A 223      27.916  41.775  22.748  1.00 21.94           N  
ATOM   1679  CA  GLN A 223      26.794  42.453  23.388  1.00 22.17           C  
ATOM   1680  C   GLN A 223      26.897  42.388  24.928  1.00 21.93           C  
ATOM   1681  O   GLN A 223      25.926  42.681  25.660  1.00 21.70           O  
ATOM   1682  CB  GLN A 223      25.456  41.911  22.832  1.00 22.84           C  
ATOM   1683  CG  GLN A 223      25.149  42.508  21.412  1.00 25.34           C  
ATOM   1684  CD  GLN A 223      23.728  42.283  20.965  1.00 27.81           C  
ATOM   1685  OE1 GLN A 223      22.801  42.473  21.750  1.00 30.00           O  
ATOM   1686  NE2 GLN A 223      23.543  41.850  19.709  1.00 29.69           N  
ATOM   1687  N   PHE A 224      28.079  42.027  25.417  1.00 21.04           N  
ATOM   1688  CA  PHE A 224      28.363  42.035  26.860  1.00 21.41           C  
ATOM   1689  C   PHE A 224      27.886  43.350  27.527  1.00 21.57           C  
ATOM   1690  O   PHE A 224      27.240  43.315  28.561  1.00 21.34           O  
ATOM   1691  CB  PHE A 224      29.883  41.874  27.076  1.00 20.95           C  
ATOM   1692  CG  PHE A 224      30.304  41.773  28.529  1.00 21.82           C  
ATOM   1693  CD1 PHE A 224      30.452  42.912  29.319  1.00 19.33           C  
ATOM   1694  CD2 PHE A 224      30.595  40.552  29.089  1.00 20.01           C  
ATOM   1695  CE1 PHE A 224      30.870  42.807  30.630  1.00 20.89           C  
ATOM   1696  CE2 PHE A 224      31.025  40.449  30.397  1.00 20.59           C  
ATOM   1697  CZ  PHE A 224      31.151  41.579  31.171  1.00 20.99           C  
ATOM   1698  N   GLU A 225      28.195  44.495  26.916  1.00 22.10           N  
ATOM   1699  CA  GLU A 225      27.823  45.800  27.466  1.00 23.01           C  
ATOM   1700  C   GLU A 225      26.337  46.042  27.574  1.00 22.26           C  
ATOM   1701  O   GLU A 225      25.928  46.946  28.311  1.00 21.91           O  
ATOM   1702  CB  GLU A 225      28.401  46.935  26.624  1.00 24.27           C  
ATOM   1703  CG  GLU A 225      29.886  47.133  26.857  1.00 29.26           C  
ATOM   1704  CD  GLU A 225      30.312  48.579  27.062  1.00 35.91           C  
ATOM   1705  OE1 GLU A 225      29.745  49.317  27.942  1.00 39.92           O  
ATOM   1706  OE2 GLU A 225      31.281  48.958  26.368  1.00 40.78           O  
ATOM   1707  N   CYS A 226      25.539  45.258  26.836  1.00 21.15           N  
ATOM   1708  CA  CYS A 226      24.081  45.396  26.851  1.00 21.01           C  
ATOM   1709  C   CYS A 226      23.359  44.417  27.768  1.00 20.67           C  
ATOM   1710  O   CYS A 226      22.159  44.601  28.043  1.00 18.85           O  
ATOM   1711  CB  CYS A 226      23.520  45.190  25.447  1.00 20.88           C  
ATOM   1712  SG  CYS A 226      24.194  46.296  24.190  1.00 22.39           S  
ATOM   1713  N   LEU A 227      24.085  43.399  28.256  1.00 20.56           N  
ATOM   1714  CA  LEU A 227      23.461  42.304  28.985  1.00 20.48           C  
ATOM   1715  C   LEU A 227      23.795  42.185  30.466  1.00 20.42           C  
ATOM   1716  O   LEU A 227      23.180  41.398  31.187  1.00 20.78           O  
ATOM   1717  CB  LEU A 227      23.737  41.003  28.232  1.00 21.20           C  
ATOM   1718  CG  LEU A 227      22.865  40.993  26.963  1.00 22.96           C  
ATOM   1719  CD1 LEU A 227      23.373  40.023  25.929  1.00 24.99           C  
ATOM   1720  CD2 LEU A 227      21.420  40.655  27.323  1.00 24.79           C  
ATOM   1721  N   TYR A 228      24.793  42.939  30.901  1.00 20.08           N  
ATOM   1722  CA  TYR A 228      25.060  43.127  32.303  1.00 19.66           C  
ATOM   1723  C   TYR A 228      25.061  41.858  33.165  1.00 19.95           C  
ATOM   1724  O   TYR A 228      24.229  41.697  34.058  1.00 19.69           O  
ATOM   1725  CB  TYR A 228      24.050  44.137  32.857  1.00 19.77           C  
ATOM   1726  CG  TYR A 228      24.028  45.481  32.119  1.00 19.37           C  
ATOM   1727  CD1 TYR A 228      24.836  46.513  32.515  1.00 18.65           C  
ATOM   1728  CD2 TYR A 228      23.180  45.697  31.036  1.00 19.82           C  
ATOM   1729  CE1 TYR A 228      24.819  47.759  31.862  1.00 20.56           C  
ATOM   1730  CE2 TYR A 228      23.143  46.920  30.380  1.00 20.78           C  
ATOM   1731  CZ  TYR A 228      23.962  47.956  30.801  1.00 20.88           C  
ATOM   1732  OH  TYR A 228      23.944  49.174  30.152  1.00 19.73           O  
ATOM   1733  N   PRO A 229      26.028  40.981  32.941  1.00 19.99           N  
ATOM   1734  CA  PRO A 229      26.140  39.781  33.768  1.00 20.44           C  
ATOM   1735  C   PRO A 229      26.481  40.141  35.196  1.00 19.99           C  
ATOM   1736  O   PRO A 229      27.130  41.166  35.451  1.00 20.03           O  
ATOM   1737  CB  PRO A 229      27.334  39.043  33.157  1.00 20.11           C  
ATOM   1738  CG  PRO A 229      28.125  40.130  32.541  1.00 21.04           C  
ATOM   1739  CD  PRO A 229      27.099  41.050  31.935  1.00 19.79           C  
ATOM   1740  N   TYR A 230      26.044  39.294  36.115  1.00 19.50           N  
ATOM   1741  CA  TYR A 230      26.348  39.458  37.511  1.00 19.17           C  
ATOM   1742  C   TYR A 230      27.860  39.464  37.704  1.00 19.14           C  
ATOM   1743  O   TYR A 230      28.598  39.060  36.832  1.00 18.83           O  
ATOM   1744  CB  TYR A 230      25.746  38.313  38.320  1.00 18.51           C  
ATOM   1745  CG  TYR A 230      24.253  38.411  38.531  1.00 18.95           C  
ATOM   1746  CD1 TYR A 230      23.368  37.949  37.560  1.00 18.39           C  
ATOM   1747  CD2 TYR A 230      23.719  38.969  39.707  1.00 18.65           C  
ATOM   1748  CE1 TYR A 230      22.001  38.006  37.751  1.00 17.34           C  
ATOM   1749  CE2 TYR A 230      22.337  39.043  39.903  1.00 17.05           C  
ATOM   1750  CZ  TYR A 230      21.492  38.550  38.909  1.00 17.79           C  
ATOM   1751  OH  TYR A 230      20.127  38.601  39.051  1.00 19.77           O  
ATOM   1752  N   PRO A 231      28.316  39.963  38.843  1.00 19.95           N  
ATOM   1753  CA  PRO A 231      29.722  39.829  39.213  1.00 20.42           C  
ATOM   1754  C   PRO A 231      30.157  38.339  39.187  1.00 20.93           C  
ATOM   1755  O   PRO A 231      29.345  37.463  39.506  1.00 20.71           O  
ATOM   1756  CB  PRO A 231      29.755  40.369  40.642  1.00 20.70           C  
ATOM   1757  CG  PRO A 231      28.588  41.341  40.716  1.00 20.76           C  
ATOM   1758  CD  PRO A 231      27.528  40.701  39.845  1.00 19.53           C  
ATOM   1759  N   VAL A 232      31.413  38.067  38.831  1.00 20.93           N  
ATOM   1760  CA  VAL A 232      31.906  36.685  38.742  1.00 21.31           C  
ATOM   1761  C   VAL A 232      31.722  35.843  40.014  1.00 20.95           C  
ATOM   1762  O   VAL A 232      31.431  34.650  39.934  1.00 20.50           O  
ATOM   1763  CB  VAL A 232      33.398  36.655  38.304  1.00 21.35           C  
ATOM   1764  CG1 VAL A 232      34.029  35.280  38.552  1.00 22.23           C  
ATOM   1765  CG2 VAL A 232      33.533  37.031  36.850  1.00 21.71           C  
ATOM   1766  N   HIS A 233      31.872  36.455  41.181  1.00 21.10           N  
ATOM   1767  CA  HIS A 233      31.742  35.721  42.438  1.00 21.01           C  
ATOM   1768  C   HIS A 233      30.302  35.571  42.944  1.00 20.95           C  
ATOM   1769  O   HIS A 233      30.045  34.864  43.914  1.00 19.92           O  
ATOM   1770  CB  HIS A 233      32.606  36.363  43.501  1.00 21.12           C  
ATOM   1771  CG  HIS A 233      34.063  36.342  43.174  1.00 21.52           C  
ATOM   1772  ND1 HIS A 233      34.720  37.424  42.625  1.00 22.78           N  
ATOM   1773  CD2 HIS A 233      34.993  35.368  43.318  1.00 22.27           C  
ATOM   1774  CE1 HIS A 233      35.994  37.114  42.446  1.00 24.00           C  
ATOM   1775  NE2 HIS A 233      36.186  35.870  42.857  1.00 23.34           N  
ATOM   1776  N   HIS A 234      29.364  36.236  42.288  1.00 20.94           N  
ATOM   1777  CA  HIS A 234      27.959  36.081  42.630  1.00 21.27           C  
ATOM   1778  C   HIS A 234      27.493  34.722  42.103  1.00 21.28           C  
ATOM   1779  O   HIS A 234      28.022  34.233  41.107  1.00 21.02           O  
ATOM   1780  CB  HIS A 234      27.169  37.203  41.989  1.00 21.52           C  
ATOM   1781  CG  HIS A 234      25.730  37.253  42.374  1.00 21.54           C  
ATOM   1782  ND1 HIS A 234      24.769  36.498  41.740  1.00 21.95           N  
ATOM   1783  CD2 HIS A 234      25.073  38.028  43.269  1.00 22.67           C  
ATOM   1784  CE1 HIS A 234      23.585  36.779  42.254  1.00 22.38           C  
ATOM   1785  NE2 HIS A 234      23.743  37.700  43.187  1.00 21.91           N  
ATOM   1786  N   PRO A 235      26.551  34.087  42.792  1.00 21.11           N  
ATOM   1787  CA  PRO A 235      25.999  32.809  42.338  1.00 21.46           C  
ATOM   1788  C   PRO A 235      25.461  32.835  40.916  1.00 21.10           C  
ATOM   1789  O   PRO A 235      25.517  31.802  40.244  1.00 20.37           O  
ATOM   1790  CB  PRO A 235      24.860  32.551  43.325  1.00 21.90           C  
ATOM   1791  CG  PRO A 235      25.316  33.240  44.574  1.00 22.00           C  
ATOM   1792  CD  PRO A 235      26.007  34.485  44.100  1.00 21.41           C  
ATOM   1793  N   CYS A 236      24.997  33.989  40.452  1.00 20.41           N  
ATOM   1794  CA  CYS A 236      24.456  34.077  39.110  1.00 20.17           C  
ATOM   1795  C   CYS A 236      25.503  34.554  38.107  1.00 20.00           C  
ATOM   1796  O   CYS A 236      25.180  35.111  37.061  1.00 20.30           O  
ATOM   1797  CB  CYS A 236      23.195  34.924  39.090  1.00 19.66           C  
ATOM   1798  SG  CYS A 236      21.914  34.209  40.133  1.00 20.71           S  
ATOM   1799  N   ASP A 237      26.768  34.311  38.433  1.00 19.87           N  
ATOM   1800  CA  ASP A 237      27.857  34.498  37.485  1.00 19.60           C  
ATOM   1801  C   ASP A 237      27.459  33.915  36.105  1.00 19.48           C  
ATOM   1802  O   ASP A 237      26.883  32.834  36.020  1.00 18.94           O  
ATOM   1803  CB  ASP A 237      29.075  33.789  38.031  1.00 19.20           C  
ATOM   1804  CG  ASP A 237      30.268  33.842  37.107  1.00 20.58           C  
ATOM   1805  OD1 ASP A 237      30.477  34.871  36.373  1.00 18.56           O  
ATOM   1806  OD2 ASP A 237      31.070  32.868  37.077  1.00 19.51           O  
ATOM   1807  N   ARG A 238      27.749  34.675  35.056  1.00 19.85           N  
ATOM   1808  CA  ARG A 238      27.459  34.332  33.664  1.00 20.90           C  
ATOM   1809  C   ARG A 238      26.002  34.572  33.247  1.00 20.67           C  
ATOM   1810  O   ARG A 238      25.709  34.491  32.059  1.00 21.20           O  
ATOM   1811  CB  ARG A 238      27.854  32.876  33.319  1.00 21.44           C  
ATOM   1812  CG  ARG A 238      29.330  32.585  33.482  1.00 21.04           C  
ATOM   1813  CD  ARG A 238      29.710  31.150  33.145  1.00 22.38           C  
ATOM   1814  NE  ARG A 238      29.080  30.243  34.085  1.00 23.86           N  
ATOM   1815  CZ  ARG A 238      27.937  29.584  33.874  1.00 25.81           C  
ATOM   1816  NH1 ARG A 238      27.262  29.686  32.712  1.00 24.18           N  
ATOM   1817  NH2 ARG A 238      27.471  28.810  34.849  1.00 27.18           N  
ATOM   1818  N   GLN A 239      25.105  34.845  34.190  1.00 19.94           N  
ATOM   1819  CA  GLN A 239      23.722  35.141  33.833  1.00 20.58           C  
ATOM   1820  C   GLN A 239      23.535  36.661  33.740  1.00 20.50           C  
ATOM   1821  O   GLN A 239      24.219  37.402  34.446  1.00 20.63           O  
ATOM   1822  CB  GLN A 239      22.735  34.591  34.863  1.00 20.32           C  
ATOM   1823  CG  GLN A 239      23.159  33.314  35.594  1.00 20.84           C  
ATOM   1824  CD  GLN A 239      23.367  32.137  34.673  1.00 21.23           C  
ATOM   1825  OE1 GLN A 239      22.434  31.675  34.014  1.00 21.22           O  
ATOM   1826  NE2 GLN A 239      24.591  31.655  34.616  1.00 20.93           N  
ATOM   1827  N   SER A 240      22.600  37.112  32.900  1.00 20.07           N  
ATOM   1828  CA  SER A 240      22.282  38.533  32.768  1.00 20.18           C  
ATOM   1829  C   SER A 240      21.498  39.027  33.969  1.00 20.71           C  
ATOM   1830  O   SER A 240      20.619  38.316  34.467  1.00 20.85           O  
ATOM   1831  CB  SER A 240      21.405  38.776  31.539  1.00 20.29           C  
ATOM   1832  OG  SER A 240      21.007  40.137  31.454  1.00 21.43           O  
ATOM   1833  N   GLN A 241      21.793  40.246  34.426  1.00 20.46           N  
ATOM   1834  CA  GLN A 241      21.013  40.839  35.496  1.00 20.42           C  
ATOM   1835  C   GLN A 241      19.711  41.433  34.965  1.00 20.26           C  
ATOM   1836  O   GLN A 241      18.839  41.767  35.726  1.00 19.62           O  
ATOM   1837  CB  GLN A 241      21.770  41.949  36.201  1.00 20.32           C  
ATOM   1838  CG  GLN A 241      23.019  41.544  36.912  1.00 20.58           C  
ATOM   1839  CD  GLN A 241      23.771  42.767  37.423  1.00 21.94           C  
ATOM   1840  OE1 GLN A 241      23.524  43.210  38.514  1.00 23.52           O  
ATOM   1841  NE2 GLN A 241      24.670  43.304  36.624  1.00 20.84           N  
ATOM   1842  N   VAL A 242      19.557  41.563  33.659  1.00 20.57           N  
ATOM   1843  CA  VAL A 242      18.361  42.229  33.182  1.00 20.73           C  
ATOM   1844  C   VAL A 242      17.173  41.309  33.246  1.00 20.69           C  
ATOM   1845  O   VAL A 242      17.244  40.190  32.757  1.00 21.13           O  
ATOM   1846  CB  VAL A 242      18.498  42.667  31.712  1.00 21.03           C  
ATOM   1847  CG1 VAL A 242      17.204  43.377  31.250  1.00 20.85           C  
ATOM   1848  CG2 VAL A 242      19.723  43.527  31.498  1.00 20.71           C  
ATOM   1849  N   ASP A 243      16.071  41.786  33.813  1.00 20.62           N  
ATOM   1850  CA  ASP A 243      14.807  41.042  33.788  1.00 20.64           C  
ATOM   1851  C   ASP A 243      14.148  41.348  32.448  1.00 20.94           C  
ATOM   1852  O   ASP A 243      13.591  42.438  32.230  1.00 19.75           O  
ATOM   1853  CB  ASP A 243      13.916  41.471  34.963  1.00 20.88           C  
ATOM   1854  CG  ASP A 243      12.526  40.894  34.898  1.00 21.39           C  
ATOM   1855  OD1 ASP A 243      12.209  40.153  33.941  1.00 23.25           O  
ATOM   1856  OD2 ASP A 243      11.672  41.130  35.784  1.00 23.49           O  
ATOM   1857  N   PHE A 244      14.238  40.385  31.541  1.00 21.19           N  
ATOM   1858  CA  PHE A 244      13.717  40.549  30.197  1.00 21.56           C  
ATOM   1859  C   PHE A 244      12.225  40.916  30.204  1.00 22.49           C  
ATOM   1860  O   PHE A 244      11.734  41.521  29.260  1.00 21.85           O  
ATOM   1861  CB  PHE A 244      13.940  39.275  29.378  1.00 21.85           C  
ATOM   1862  CG  PHE A 244      15.316  39.152  28.743  1.00 20.87           C  
ATOM   1863  CD1 PHE A 244      16.457  39.540  29.399  1.00 20.74           C  
ATOM   1864  CD2 PHE A 244      15.446  38.617  27.483  1.00 21.00           C  
ATOM   1865  CE1 PHE A 244      17.691  39.407  28.810  1.00 19.77           C  
ATOM   1866  CE2 PHE A 244      16.687  38.470  26.890  1.00 20.94           C  
ATOM   1867  CZ  PHE A 244      17.805  38.881  27.551  1.00 20.34           C  
ATOM   1868  N   ASP A 245      11.500  40.554  31.259  1.00 23.56           N  
ATOM   1869  CA  ASP A 245      10.072  40.831  31.311  1.00 24.26           C  
ATOM   1870  C   ASP A 245       9.794  42.256  31.814  1.00 24.66           C  
ATOM   1871  O   ASP A 245       8.711  42.762  31.607  1.00 24.21           O  
ATOM   1872  CB  ASP A 245       9.353  39.841  32.222  1.00 24.74           C  
ATOM   1873  CG  ASP A 245       9.408  38.427  31.721  1.00 26.56           C  
ATOM   1874  OD1 ASP A 245       9.368  38.210  30.493  1.00 28.81           O  
ATOM   1875  OD2 ASP A 245       9.489  37.455  32.498  1.00 28.39           O  
ATOM   1876  N   ASN A 246      10.758  42.876  32.492  1.00 24.80           N  
ATOM   1877  CA  ASN A 246      10.605  44.244  32.989  1.00 25.56           C  
ATOM   1878  C   ASN A 246      11.960  44.902  33.106  1.00 25.31           C  
ATOM   1879  O   ASN A 246      12.500  45.064  34.205  1.00 25.43           O  
ATOM   1880  CB  ASN A 246       9.912  44.285  34.345  1.00 26.09           C  
ATOM   1881  CG  ASN A 246       9.555  45.716  34.765  1.00 29.59           C  
ATOM   1882  OD1 ASN A 246       9.366  46.598  33.912  1.00 32.67           O  
ATOM   1883  ND2 ASN A 246       9.468  45.954  36.075  1.00 33.42           N  
ATOM   1884  N   PRO A 247      12.525  45.257  31.961  1.00 25.08           N  
ATOM   1885  CA  PRO A 247      13.885  45.782  31.911  1.00 24.89           C  
ATOM   1886  C   PRO A 247      13.992  47.144  32.579  1.00 24.95           C  
ATOM   1887  O   PRO A 247      13.217  48.049  32.297  1.00 24.55           O  
ATOM   1888  CB  PRO A 247      14.182  45.899  30.413  1.00 25.05           C  
ATOM   1889  CG  PRO A 247      13.016  45.325  29.702  1.00 25.39           C  
ATOM   1890  CD  PRO A 247      11.890  45.184  30.640  1.00 25.02           C  
ATOM   1891  N   ASP A 248      14.976  47.267  33.460  1.00 24.53           N  
ATOM   1892  CA  ASP A 248      15.216  48.489  34.167  1.00 24.65           C  
ATOM   1893  C   ASP A 248      16.271  49.284  33.389  1.00 24.54           C  
ATOM   1894  O   ASP A 248      17.472  49.077  33.552  1.00 23.15           O  
ATOM   1895  CB  ASP A 248      15.706  48.144  35.564  1.00 24.64           C  
ATOM   1896  CG  ASP A 248      15.787  49.343  36.454  1.00 26.02           C  
ATOM   1897  OD1 ASP A 248      16.035  50.466  35.944  1.00 26.95           O  
ATOM   1898  OD2 ASP A 248      15.609  49.249  37.684  1.00 27.69           O  
ATOM   1899  N   TYR A 249      15.812  50.181  32.525  1.00 24.81           N  
ATOM   1900  CA  TYR A 249      16.720  50.936  31.673  1.00 25.45           C  
ATOM   1901  C   TYR A 249      17.573  51.954  32.426  1.00 25.90           C  
ATOM   1902  O   TYR A 249      18.585  52.421  31.897  1.00 25.80           O  
ATOM   1903  CB  TYR A 249      15.948  51.615  30.544  1.00 25.57           C  
ATOM   1904  CG  TYR A 249      15.244  50.651  29.630  1.00 24.58           C  
ATOM   1905  CD1 TYR A 249      15.930  49.624  29.003  1.00 25.44           C  
ATOM   1906  CD2 TYR A 249      13.890  50.764  29.404  1.00 24.48           C  
ATOM   1907  CE1 TYR A 249      15.276  48.731  28.173  1.00 25.01           C  
ATOM   1908  CE2 TYR A 249      13.234  49.892  28.583  1.00 24.43           C  
ATOM   1909  CZ  TYR A 249      13.927  48.883  27.969  1.00 24.47           C  
ATOM   1910  OH  TYR A 249      13.252  48.043  27.142  1.00 25.97           O  
ATOM   1911  N   GLU A 250      17.195  52.278  33.660  1.00 26.10           N  
ATOM   1912  CA  GLU A 250      17.999  53.190  34.458  1.00 26.93           C  
ATOM   1913  C   GLU A 250      19.259  52.492  34.929  1.00 25.85           C  
ATOM   1914  O   GLU A 250      20.329  53.086  34.964  1.00 25.90           O  
ATOM   1915  CB  GLU A 250      17.219  53.740  35.661  1.00 27.56           C  
ATOM   1916  CG  GLU A 250      16.021  54.576  35.246  1.00 32.34           C  
ATOM   1917  CD  GLU A 250      15.420  55.366  36.385  1.00 36.85           C  
ATOM   1918  OE1 GLU A 250      15.945  55.309  37.516  1.00 42.35           O  
ATOM   1919  OE2 GLU A 250      14.422  56.057  36.142  1.00 40.82           O  
ATOM   1920  N   ARG A 251      19.136  51.233  35.315  1.00 24.58           N  
ATOM   1921  CA  ARG A 251      20.297  50.502  35.756  1.00 23.76           C  
ATOM   1922  C   ARG A 251      21.030  49.909  34.568  1.00 22.91           C  
ATOM   1923  O   ARG A 251      22.242  49.773  34.602  1.00 22.42           O  
ATOM   1924  CB  ARG A 251      19.896  49.374  36.696  1.00 24.55           C  
ATOM   1925  CG  ARG A 251      19.421  49.802  38.077  1.00 25.88           C  
ATOM   1926  CD  ARG A 251      18.894  48.629  38.921  1.00 29.50           C  
ATOM   1927  NE  ARG A 251      19.993  47.764  39.349  1.00 31.63           N  
ATOM   1928  CZ  ARG A 251      19.894  46.467  39.623  1.00 33.13           C  
ATOM   1929  NH1 ARG A 251      18.736  45.826  39.521  1.00 33.12           N  
ATOM   1930  NH2 ARG A 251      20.978  45.805  39.998  1.00 33.93           N  
ATOM   1931  N   PHE A 252      20.300  49.560  33.515  1.00 21.47           N  
ATOM   1932  CA  PHE A 252      20.898  48.863  32.379  1.00 21.32           C  
ATOM   1933  C   PHE A 252      20.576  49.552  31.056  1.00 20.68           C  
ATOM   1934  O   PHE A 252      19.934  48.984  30.187  1.00 20.79           O  
ATOM   1935  CB  PHE A 252      20.355  47.434  32.344  1.00 21.09           C  
ATOM   1936  CG  PHE A 252      20.373  46.738  33.690  1.00 20.96           C  
ATOM   1937  CD1 PHE A 252      21.555  46.560  34.376  1.00 19.28           C  
ATOM   1938  CD2 PHE A 252      19.207  46.238  34.247  1.00 21.43           C  
ATOM   1939  CE1 PHE A 252      21.571  45.891  35.609  1.00 20.54           C  
ATOM   1940  CE2 PHE A 252      19.217  45.588  35.488  1.00 22.13           C  
ATOM   1941  CZ  PHE A 252      20.403  45.414  36.156  1.00 20.96           C  
ATOM   1942  N   PRO A 253      21.057  50.767  30.884  1.00 20.56           N  
ATOM   1943  CA  PRO A 253      20.658  51.566  29.714  1.00 20.38           C  
ATOM   1944  C   PRO A 253      20.984  50.916  28.361  1.00 20.20           C  
ATOM   1945  O   PRO A 253      20.191  51.053  27.428  1.00 19.48           O  
ATOM   1946  CB  PRO A 253      21.383  52.903  29.928  1.00 19.77           C  
ATOM   1947  CG  PRO A 253      22.562  52.555  30.895  1.00 20.60           C  
ATOM   1948  CD  PRO A 253      21.986  51.484  31.782  1.00 20.69           C  
ATOM   1949  N   ASN A 254      22.091  50.187  28.240  1.00 20.32           N  
ATOM   1950  CA  ASN A 254      22.409  49.613  26.938  1.00 20.12           C  
ATOM   1951  C   ASN A 254      21.572  48.393  26.554  1.00 19.96           C  
ATOM   1952  O   ASN A 254      21.675  47.892  25.441  1.00 19.16           O  
ATOM   1953  CB  ASN A 254      23.893  49.336  26.784  1.00 20.06           C  
ATOM   1954  CG  ASN A 254      24.706  50.601  26.697  1.00 21.51           C  
ATOM   1955  OD1 ASN A 254      25.502  50.896  27.598  1.00 23.96           O  
ATOM   1956  ND2 ASN A 254      24.514  51.373  25.614  1.00 20.38           N  
ATOM   1957  N   PHE A 255      20.724  47.922  27.455  1.00 19.81           N  
ATOM   1958  CA  PHE A 255      19.807  46.858  27.063  1.00 19.54           C  
ATOM   1959  C   PHE A 255      18.855  47.384  25.977  1.00 19.69           C  
ATOM   1960  O   PHE A 255      18.194  46.606  25.274  1.00 19.77           O  
ATOM   1961  CB  PHE A 255      19.023  46.330  28.252  1.00 19.22           C  
ATOM   1962  CG  PHE A 255      18.269  45.105  27.940  1.00 20.47           C  
ATOM   1963  CD1 PHE A 255      18.928  43.922  27.736  1.00 20.23           C  
ATOM   1964  CD2 PHE A 255      16.909  45.148  27.758  1.00 20.13           C  
ATOM   1965  CE1 PHE A 255      18.243  42.786  27.416  1.00 21.65           C  
ATOM   1966  CE2 PHE A 255      16.227  44.023  27.432  1.00 20.73           C  
ATOM   1967  CZ  PHE A 255      16.886  42.842  27.257  1.00 22.63           C  
ATOM   1968  N   GLN A 256      18.790  48.707  25.841  1.00 19.89           N  
ATOM   1969  CA  GLN A 256      17.969  49.345  24.794  1.00 20.24           C  
ATOM   1970  C   GLN A 256      18.595  49.160  23.403  1.00 19.74           C  
ATOM   1971  O   GLN A 256      17.969  49.443  22.384  1.00 19.92           O  
ATOM   1972  CB  GLN A 256      17.778  50.849  25.095  1.00 20.01           C  
ATOM   1973  CG  GLN A 256      16.736  51.095  26.197  1.00 21.20           C  
ATOM   1974  CD  GLN A 256      16.741  52.513  26.764  1.00 22.14           C  
ATOM   1975  OE1 GLN A 256      15.711  53.195  26.741  1.00 23.01           O  
ATOM   1976  NE2 GLN A 256      17.874  52.943  27.298  1.00 21.42           N  
ATOM   1977  N   ASN A 257      19.845  48.716  23.385  1.00 19.66           N  
ATOM   1978  CA  ASN A 257      20.580  48.485  22.155  1.00 20.07           C  
ATOM   1979  C   ASN A 257      20.757  47.005  21.811  1.00 20.73           C  
ATOM   1980  O   ASN A 257      21.416  46.694  20.823  1.00 20.96           O  
ATOM   1981  CB  ASN A 257      21.969  49.100  22.232  1.00 19.17           C  
ATOM   1982  CG  ASN A 257      21.941  50.550  22.635  1.00 20.82           C  
ATOM   1983  OD1 ASN A 257      22.413  50.902  23.722  1.00 21.51           O  
ATOM   1984  ND2 ASN A 257      21.396  51.407  21.763  1.00 16.92           N  
ATOM   1985  N   VAL A 258      20.190  46.098  22.596  1.00 21.59           N  
ATOM   1986  CA  VAL A 258      20.410  44.660  22.347  1.00 23.34           C  
ATOM   1987  C   VAL A 258      19.671  44.172  21.112  1.00 23.85           C  
ATOM   1988  O   VAL A 258      18.549  44.611  20.818  1.00 24.10           O  
ATOM   1989  CB  VAL A 258      20.015  43.806  23.573  1.00 23.68           C  
ATOM   1990  CG1 VAL A 258      18.507  43.720  23.685  1.00 24.12           C  
ATOM   1991  CG2 VAL A 258      20.570  42.436  23.445  1.00 28.30           C  
ATOM   1992  N   VAL A 259      20.314  43.286  20.360  1.00 24.47           N  
ATOM   1993  CA  VAL A 259      19.705  42.721  19.154  1.00 24.91           C  
ATOM   1994  C   VAL A 259      20.004  41.215  19.140  1.00 24.93           C  
ATOM   1995  O   VAL A 259      21.152  40.829  19.119  1.00 25.32           O  
ATOM   1996  CB  VAL A 259      20.281  43.362  17.895  1.00 24.88           C  
ATOM   1997  CG1 VAL A 259      19.667  42.738  16.670  1.00 26.38           C  
ATOM   1998  CG2 VAL A 259      20.051  44.869  17.909  1.00 24.83           C  
ATOM   1999  N   GLY A 260      18.974  40.381  19.186  1.00 25.06           N  
ATOM   2000  CA  GLY A 260      19.166  38.944  19.232  1.00 25.64           C  
ATOM   2001  C   GLY A 260      19.076  38.221  17.887  1.00 25.42           C  
ATOM   2002  O   GLY A 260      18.679  38.796  16.869  1.00 25.77           O  
ATOM   2003  N   TYR A 261      19.497  36.965  17.907  1.00 25.04           N  
ATOM   2004  CA  TYR A 261      19.380  36.049  16.792  1.00 25.30           C  
ATOM   2005  C   TYR A 261      18.428  34.973  17.328  1.00 24.63           C  
ATOM   2006  O   TYR A 261      18.676  34.417  18.392  1.00 24.77           O  
ATOM   2007  CB  TYR A 261      20.729  35.414  16.482  1.00 25.84           C  
ATOM   2008  CG  TYR A 261      21.750  36.315  15.825  1.00 28.57           C  
ATOM   2009  CD1 TYR A 261      21.821  36.423  14.447  1.00 34.41           C  
ATOM   2010  CD2 TYR A 261      22.631  37.049  16.574  1.00 29.87           C  
ATOM   2011  CE1 TYR A 261      22.752  37.255  13.838  1.00 35.64           C  
ATOM   2012  CE2 TYR A 261      23.576  37.852  15.986  1.00 32.26           C  
ATOM   2013  CZ  TYR A 261      23.644  37.949  14.623  1.00 34.92           C  
ATOM   2014  OH  TYR A 261      24.582  38.772  14.047  1.00 38.39           O  
ATOM   2015  N   GLU A 262      17.325  34.698  16.658  1.00 23.64           N  
ATOM   2016  CA  GLU A 262      16.376  33.758  17.244  1.00 24.03           C  
ATOM   2017  C   GLU A 262      15.933  32.660  16.306  1.00 23.15           C  
ATOM   2018  O   GLU A 262      16.063  32.766  15.078  1.00 22.51           O  
ATOM   2019  CB  GLU A 262      15.172  34.482  17.861  1.00 24.11           C  
ATOM   2020  CG  GLU A 262      13.899  34.502  17.057  1.00 26.35           C  
ATOM   2021  CD  GLU A 262      12.744  35.177  17.785  1.00 27.98           C  
ATOM   2022  OE1 GLU A 262      12.743  36.415  17.872  1.00 27.19           O  
ATOM   2023  OE2 GLU A 262      11.818  34.476  18.254  1.00 29.21           O  
ATOM   2024  N   THR A 263      15.455  31.587  16.917  1.00 22.58           N  
ATOM   2025  CA  THR A 263      14.939  30.458  16.170  1.00 22.52           C  
ATOM   2026  C   THR A 263      14.047  29.617  17.076  1.00 22.48           C  
ATOM   2027  O   THR A 263      14.107  29.712  18.313  1.00 22.14           O  
ATOM   2028  CB  THR A 263      16.117  29.607  15.659  1.00 22.55           C  
ATOM   2029  OG1 THR A 263      15.665  28.666  14.675  1.00 22.25           O  
ATOM   2030  CG2 THR A 263      16.693  28.743  16.770  1.00 22.79           C  
ATOM   2031  N   VAL A 264      13.208  28.797  16.472  1.00 21.62           N  
ATOM   2032  CA  VAL A 264      12.453  27.860  17.263  1.00 22.45           C  
ATOM   2033  C   VAL A 264      12.871  26.474  16.837  1.00 22.76           C  
ATOM   2034  O   VAL A 264      12.779  26.134  15.673  1.00 22.77           O  
ATOM   2035  CB  VAL A 264      10.964  28.027  17.087  1.00 23.08           C  
ATOM   2036  CG1 VAL A 264      10.234  26.805  17.643  1.00 23.67           C  
ATOM   2037  CG2 VAL A 264      10.499  29.344  17.767  1.00 22.75           C  
ATOM   2038  N   VAL A 265      13.389  25.695  17.777  1.00 22.93           N  
ATOM   2039  CA  VAL A 265      13.779  24.329  17.458  1.00 23.08           C  
ATOM   2040  C   VAL A 265      12.738  23.317  17.886  1.00 22.86           C  
ATOM   2041  O   VAL A 265      12.105  23.473  18.932  1.00 23.06           O  
ATOM   2042  CB  VAL A 265      15.143  23.937  18.075  1.00 22.94           C  
ATOM   2043  CG1 VAL A 265      16.243  24.745  17.404  1.00 23.66           C  
ATOM   2044  CG2 VAL A 265      15.169  24.122  19.592  1.00 22.99           C  
ATOM   2045  N   GLY A 266      12.574  22.290  17.056  1.00 21.77           N  
ATOM   2046  CA  GLY A 266      11.683  21.178  17.355  1.00 21.98           C  
ATOM   2047  C   GLY A 266      12.376  19.826  17.263  1.00 20.97           C  
ATOM   2048  O   GLY A 266      13.562  19.757  16.999  1.00 20.63           O  
ATOM   2049  N   PRO A 267      11.643  18.737  17.461  1.00 21.23           N  
ATOM   2050  CA  PRO A 267      12.253  17.403  17.427  1.00 20.68           C  
ATOM   2051  C   PRO A 267      13.126  17.183  16.203  1.00 20.04           C  
ATOM   2052  O   PRO A 267      12.666  17.371  15.081  1.00 19.35           O  
ATOM   2053  CB  PRO A 267      11.039  16.463  17.379  1.00 21.29           C  
ATOM   2054  CG  PRO A 267       9.970  17.202  18.037  1.00 22.85           C  
ATOM   2055  CD  PRO A 267      10.188  18.676  17.710  1.00 21.61           C  
ATOM   2056  N   GLY A 268      14.376  16.787  16.411  1.00 20.31           N  
ATOM   2057  CA  GLY A 268      15.278  16.518  15.305  1.00 19.95           C  
ATOM   2058  C   GLY A 268      16.256  17.627  14.993  1.00 20.50           C  
ATOM   2059  O   GLY A 268      17.277  17.400  14.311  1.00 21.62           O  
ATOM   2060  N   ASP A 269      15.965  18.831  15.477  1.00 19.81           N  
ATOM   2061  CA  ASP A 269      16.818  19.977  15.217  1.00 19.75           C  
ATOM   2062  C   ASP A 269      17.970  20.003  16.215  1.00 19.67           C  
ATOM   2063  O   ASP A 269      17.811  19.625  17.377  1.00 18.76           O  
ATOM   2064  CB  ASP A 269      16.032  21.288  15.386  1.00 19.99           C  
ATOM   2065  CG  ASP A 269      14.916  21.464  14.374  1.00 20.91           C  
ATOM   2066  OD1 ASP A 269      14.935  20.842  13.287  1.00 22.13           O  
ATOM   2067  OD2 ASP A 269      13.987  22.259  14.576  1.00 23.27           O  
ATOM   2068  N   VAL A 270      19.116  20.481  15.746  1.00 19.56           N  
ATOM   2069  CA  VAL A 270      20.276  20.700  16.595  1.00 19.57           C  
ATOM   2070  C   VAL A 270      20.747  22.137  16.444  1.00 19.33           C  
ATOM   2071  O   VAL A 270      21.033  22.594  15.352  1.00 19.78           O  
ATOM   2072  CB  VAL A 270      21.404  19.776  16.215  1.00 19.55           C  
ATOM   2073  CG1 VAL A 270      22.646  20.154  16.966  1.00 20.05           C  
ATOM   2074  CG2 VAL A 270      21.001  18.342  16.535  1.00 19.44           C  
ATOM   2075  N   LEU A 271      20.786  22.870  17.539  1.00 19.33           N  
ATOM   2076  CA  LEU A 271      21.263  24.229  17.501  1.00 19.02           C  
ATOM   2077  C   LEU A 271      22.677  24.272  18.036  1.00 19.15           C  
ATOM   2078  O   LEU A 271      22.961  23.787  19.130  1.00 18.74           O  
ATOM   2079  CB  LEU A 271      20.376  25.120  18.331  1.00 19.93           C  
ATOM   2080  CG  LEU A 271      20.892  26.549  18.573  1.00 20.11           C  
ATOM   2081  CD1 LEU A 271      21.011  27.358  17.296  1.00 19.41           C  
ATOM   2082  CD2 LEU A 271      19.979  27.245  19.555  1.00 20.25           C  
ATOM   2083  N   TYR A 272      23.582  24.818  17.244  1.00 19.15           N  
ATOM   2084  CA  TYR A 272      24.924  25.051  17.718  1.00 19.70           C  
ATOM   2085  C   TYR A 272      24.914  26.360  18.483  1.00 19.63           C  
ATOM   2086  O   TYR A 272      24.646  27.395  17.897  1.00 20.44           O  
ATOM   2087  CB  TYR A 272      25.908  25.172  16.547  1.00 19.86           C  
ATOM   2088  CG  TYR A 272      27.293  25.654  16.962  1.00 21.59           C  
ATOM   2089  CD1 TYR A 272      27.952  25.093  18.048  1.00 22.02           C  
ATOM   2090  CD2 TYR A 272      27.936  26.668  16.278  1.00 20.87           C  
ATOM   2091  CE1 TYR A 272      29.214  25.522  18.421  1.00 19.87           C  
ATOM   2092  CE2 TYR A 272      29.200  27.098  16.649  1.00 20.88           C  
ATOM   2093  CZ  TYR A 272      29.834  26.517  17.721  1.00 21.07           C  
ATOM   2094  OH  TYR A 272      31.091  26.937  18.104  1.00 18.93           O  
ATOM   2095  N   ILE A 273      25.210  26.308  19.776  1.00 19.80           N  
ATOM   2096  CA  ILE A 273      25.342  27.500  20.598  1.00 20.12           C  
ATOM   2097  C   ILE A 273      26.837  27.683  20.883  1.00 20.39           C  
ATOM   2098  O   ILE A 273      27.393  27.000  21.760  1.00 19.88           O  
ATOM   2099  CB  ILE A 273      24.576  27.366  21.901  1.00 19.72           C  
ATOM   2100  CG1 ILE A 273      23.111  27.045  21.624  1.00 20.57           C  
ATOM   2101  CG2 ILE A 273      24.661  28.695  22.696  1.00 20.99           C  
ATOM   2102  CD1 ILE A 273      22.296  26.797  22.876  1.00 20.93           C  
ATOM   2103  N   PRO A 274      27.487  28.611  20.182  1.00 20.23           N  
ATOM   2104  CA  PRO A 274      28.938  28.743  20.326  1.00 21.16           C  
ATOM   2105  C   PRO A 274      29.289  29.264  21.704  1.00 21.39           C  
ATOM   2106  O   PRO A 274      28.520  30.027  22.317  1.00 20.89           O  
ATOM   2107  CB  PRO A 274      29.353  29.757  19.230  1.00 21.62           C  
ATOM   2108  CG  PRO A 274      28.089  30.056  18.410  1.00 21.22           C  
ATOM   2109  CD  PRO A 274      26.919  29.621  19.282  1.00 20.51           C  
ATOM   2110  N   MET A 275      30.450  28.831  22.180  1.00 21.53           N  
ATOM   2111  CA  MET A 275      30.953  29.207  23.479  1.00 22.30           C  
ATOM   2112  C   MET A 275      30.920  30.734  23.636  1.00 21.94           C  
ATOM   2113  O   MET A 275      31.160  31.442  22.675  1.00 20.78           O  
ATOM   2114  CB  MET A 275      32.367  28.695  23.589  1.00 23.06           C  
ATOM   2115  CG  MET A 275      32.937  28.734  24.966  1.00 27.00           C  
ATOM   2116  SD  MET A 275      34.545  27.926  24.991  1.00 33.74           S  
ATOM   2117  CE  MET A 275      35.263  28.479  23.499  1.00 32.50           C  
ATOM   2118  N   TYR A 276      30.583  31.211  24.832  1.00 21.96           N  
ATOM   2119  CA  TYR A 276      30.485  32.656  25.138  1.00 23.15           C  
ATOM   2120  C   TYR A 276      29.256  33.365  24.546  1.00 22.39           C  
ATOM   2121  O   TYR A 276      28.989  34.496  24.899  1.00 22.58           O  
ATOM   2122  CB  TYR A 276      31.776  33.409  24.760  1.00 23.80           C  
ATOM   2123  CG  TYR A 276      32.904  33.136  25.729  1.00 28.82           C  
ATOM   2124  CD1 TYR A 276      32.940  33.756  26.951  1.00 32.73           C  
ATOM   2125  CD2 TYR A 276      33.935  32.246  25.415  1.00 35.83           C  
ATOM   2126  CE1 TYR A 276      33.956  33.507  27.864  1.00 35.96           C  
ATOM   2127  CE2 TYR A 276      34.975  31.992  26.336  1.00 38.59           C  
ATOM   2128  CZ  TYR A 276      34.958  32.628  27.562  1.00 38.60           C  
ATOM   2129  OH  TYR A 276      35.951  32.421  28.513  1.00 45.18           O  
ATOM   2130  N   TRP A 277      28.488  32.709  23.684  1.00 21.71           N  
ATOM   2131  CA  TRP A 277      27.281  33.350  23.149  1.00 21.24           C  
ATOM   2132  C   TRP A 277      26.184  33.278  24.152  1.00 20.90           C  
ATOM   2133  O   TRP A 277      25.914  32.217  24.708  1.00 21.96           O  
ATOM   2134  CB  TRP A 277      26.790  32.711  21.856  1.00 21.01           C  
ATOM   2135  CG  TRP A 277      27.547  33.166  20.670  1.00 19.98           C  
ATOM   2136  CD1 TRP A 277      28.875  33.013  20.462  1.00 17.90           C  
ATOM   2137  CD2 TRP A 277      27.030  33.832  19.519  1.00 19.76           C  
ATOM   2138  NE1 TRP A 277      29.218  33.533  19.247  1.00 18.64           N  
ATOM   2139  CE2 TRP A 277      28.106  34.071  18.662  1.00 18.29           C  
ATOM   2140  CE3 TRP A 277      25.764  34.305  19.151  1.00 20.56           C  
ATOM   2141  CZ2 TRP A 277      27.963  34.716  17.442  1.00 19.63           C  
ATOM   2142  CZ3 TRP A 277      25.624  34.950  17.943  1.00 21.16           C  
ATOM   2143  CH2 TRP A 277      26.720  35.137  17.095  1.00 19.92           C  
ATOM   2144  N   TRP A 278      25.574  34.426  24.405  1.00 20.32           N  
ATOM   2145  CA  TRP A 278      24.452  34.533  25.316  1.00 20.13           C  
ATOM   2146  C   TRP A 278      23.268  33.787  24.741  1.00 19.99           C  
ATOM   2147  O   TRP A 278      23.083  33.758  23.538  1.00 20.42           O  
ATOM   2148  CB  TRP A 278      24.025  35.999  25.441  1.00 20.65           C  
ATOM   2149  CG  TRP A 278      25.031  36.864  26.107  1.00 20.56           C  
ATOM   2150  CD1 TRP A 278      26.078  37.526  25.519  1.00 19.63           C  
ATOM   2151  CD2 TRP A 278      25.096  37.160  27.501  1.00 19.59           C  
ATOM   2152  NE1 TRP A 278      26.772  38.233  26.469  1.00 20.70           N  
ATOM   2153  CE2 TRP A 278      26.191  38.012  27.699  1.00 20.10           C  
ATOM   2154  CE3 TRP A 278      24.318  36.811  28.601  1.00 20.98           C  
ATOM   2155  CZ2 TRP A 278      26.527  38.516  28.951  1.00 20.24           C  
ATOM   2156  CZ3 TRP A 278      24.668  37.299  29.849  1.00 23.26           C  
ATOM   2157  CH2 TRP A 278      25.759  38.146  30.011  1.00 20.41           C  
ATOM   2158  N   HIS A 279      22.463  33.194  25.591  1.00 19.84           N  
ATOM   2159  CA  HIS A 279      21.269  32.530  25.122  1.00 20.78           C  
ATOM   2160  C   HIS A 279      20.202  32.495  26.192  1.00 20.37           C  
ATOM   2161  O   HIS A 279      20.479  32.275  27.370  1.00 20.66           O  
ATOM   2162  CB  HIS A 279      21.540  31.098  24.604  1.00 20.86           C  
ATOM   2163  CG  HIS A 279      22.349  30.238  25.528  1.00 21.83           C  
ATOM   2164  ND1 HIS A 279      23.720  30.324  25.608  1.00 23.19           N  
ATOM   2165  CD2 HIS A 279      21.988  29.240  26.371  1.00 23.96           C  
ATOM   2166  CE1 HIS A 279      24.175  29.411  26.449  1.00 22.20           C  
ATOM   2167  NE2 HIS A 279      23.144  28.747  26.940  1.00 23.84           N  
ATOM   2168  N   HIS A 280      18.994  32.718  25.711  1.00 20.90           N  
ATOM   2169  CA  HIS A 280      17.742  32.758  26.441  1.00 21.22           C  
ATOM   2170  C   HIS A 280      16.910  31.676  25.793  1.00 21.42           C  
ATOM   2171  O   HIS A 280      16.749  31.685  24.580  1.00 21.70           O  
ATOM   2172  CB  HIS A 280      17.099  34.124  26.224  1.00 21.04           C  
ATOM   2173  CG  HIS A 280      15.632  34.168  26.489  1.00 21.54           C  
ATOM   2174  ND1 HIS A 280      15.096  34.836  27.571  1.00 22.76           N  
ATOM   2175  CD2 HIS A 280      14.581  33.660  25.802  1.00 22.74           C  
ATOM   2176  CE1 HIS A 280      13.779  34.721  27.546  1.00 23.23           C  
ATOM   2177  NE2 HIS A 280      13.441  34.014  26.482  1.00 23.05           N  
ATOM   2178  N   ILE A 281      16.367  30.755  26.584  1.00 22.31           N  
ATOM   2179  CA  ILE A 281      15.649  29.599  26.040  1.00 22.39           C  
ATOM   2180  C   ILE A 281      14.304  29.443  26.722  1.00 22.72           C  
ATOM   2181  O   ILE A 281      14.216  29.419  27.945  1.00 22.70           O  
ATOM   2182  CB  ILE A 281      16.527  28.336  26.189  1.00 22.98           C  
ATOM   2183  CG1 ILE A 281      17.771  28.504  25.305  1.00 24.90           C  
ATOM   2184  CG2 ILE A 281      15.770  27.059  25.771  1.00 21.60           C  
ATOM   2185  CD1 ILE A 281      18.795  27.556  25.554  1.00 27.31           C  
ATOM   2186  N   GLU A 282      13.252  29.350  25.920  1.00 22.93           N  
ATOM   2187  CA  GLU A 282      11.903  29.205  26.458  1.00 23.35           C  
ATOM   2188  C   GLU A 282      11.101  28.105  25.769  1.00 22.59           C  
ATOM   2189  O   GLU A 282      11.092  27.982  24.549  1.00 21.77           O  
ATOM   2190  CB  GLU A 282      11.144  30.538  26.393  1.00 23.47           C  
ATOM   2191  CG  GLU A 282      10.830  31.055  25.009  1.00 25.70           C  
ATOM   2192  CD  GLU A 282      10.281  32.483  25.023  1.00 25.79           C  
ATOM   2193  OE1 GLU A 282      10.898  33.356  25.665  1.00 27.49           O  
ATOM   2194  OE2 GLU A 282       9.241  32.740  24.391  1.00 26.03           O  
ATOM   2195  N   SER A 283      10.456  27.293  26.588  1.00 22.44           N  
ATOM   2196  CA  SER A 283       9.570  26.246  26.103  1.00 23.00           C  
ATOM   2197  C   SER A 283       8.256  26.916  25.753  1.00 23.56           C  
ATOM   2198  O   SER A 283       7.685  27.615  26.584  1.00 24.14           O  
ATOM   2199  CB  SER A 283       9.346  25.204  27.188  1.00 22.59           C  
ATOM   2200  OG  SER A 283      10.496  24.400  27.345  1.00 22.67           O  
ATOM   2201  N   LEU A 284       7.763  26.694  24.541  1.00 24.07           N  
ATOM   2202  CA  LEU A 284       6.581  27.412  24.070  1.00 24.80           C  
ATOM   2203  C   LEU A 284       5.386  27.324  25.004  1.00 24.51           C  
ATOM   2204  O   LEU A 284       5.098  26.271  25.602  1.00 23.93           O  
ATOM   2205  CB  LEU A 284       6.161  26.947  22.682  1.00 25.09           C  
ATOM   2206  CG  LEU A 284       7.185  27.083  21.555  1.00 26.46           C  
ATOM   2207  CD1 LEU A 284       6.475  27.236  20.215  1.00 28.29           C  
ATOM   2208  CD2 LEU A 284       8.123  28.188  21.775  1.00 26.10           C  
ATOM   2209  N   LEU A 285       4.718  28.463  25.136  1.00 24.41           N  
ATOM   2210  CA  LEU A 285       3.506  28.554  25.930  1.00 24.83           C  
ATOM   2211  C   LEU A 285       2.526  27.583  25.323  1.00 24.68           C  
ATOM   2212  O   LEU A 285       2.393  27.516  24.110  1.00 24.08           O  
ATOM   2213  CB  LEU A 285       2.927  29.961  25.872  1.00 24.79           C  
ATOM   2214  CG  LEU A 285       3.825  31.078  26.397  1.00 25.19           C  
ATOM   2215  CD1 LEU A 285       3.298  32.434  25.954  1.00 26.02           C  
ATOM   2216  CD2 LEU A 285       3.925  30.999  27.898  1.00 26.27           C  
ATOM   2217  N   ASN A 286       1.867  26.815  26.173  1.00 25.20           N  
ATOM   2218  CA  ASN A 286       0.867  25.848  25.730  1.00 25.85           C  
ATOM   2219  C   ASN A 286       1.371  24.791  24.742  1.00 25.23           C  
ATOM   2220  O   ASN A 286       0.594  24.267  23.965  1.00 24.38           O  
ATOM   2221  CB  ASN A 286      -0.319  26.599  25.124  1.00 26.54           C  
ATOM   2222  CG  ASN A 286      -0.957  27.546  26.109  1.00 29.40           C  
ATOM   2223  OD1 ASN A 286      -1.478  27.118  27.140  1.00 33.49           O  
ATOM   2224  ND2 ASN A 286      -0.893  28.843  25.821  1.00 33.58           N  
ATOM   2225  N   GLY A 287       2.669  24.487  24.774  1.00 24.55           N  
ATOM   2226  CA  GLY A 287       3.243  23.518  23.863  1.00 24.10           C  
ATOM   2227  C   GLY A 287       3.524  22.167  24.487  1.00 23.80           C  
ATOM   2228  O   GLY A 287       4.110  21.301  23.838  1.00 24.10           O  
ATOM   2229  N   GLY A 288       3.100  21.971  25.734  1.00 23.32           N  
ATOM   2230  CA  GLY A 288       3.360  20.730  26.439  1.00 23.24           C  
ATOM   2231  C   GLY A 288       4.808  20.673  26.903  1.00 23.49           C  
ATOM   2232  O   GLY A 288       5.548  21.646  26.741  1.00 22.86           O  
ATOM   2233  N   ILE A 289       5.220  19.539  27.462  1.00 23.36           N  
ATOM   2234  CA  ILE A 289       6.571  19.406  27.983  1.00 23.99           C  
ATOM   2235  C   ILE A 289       7.601  19.374  26.874  1.00 23.28           C  
ATOM   2236  O   ILE A 289       7.324  18.958  25.755  1.00 23.68           O  
ATOM   2237  CB  ILE A 289       6.750  18.123  28.817  1.00 24.68           C  
ATOM   2238  CG1 ILE A 289       6.819  16.912  27.901  1.00 26.90           C  
ATOM   2239  CG2 ILE A 289       5.648  17.983  29.885  1.00 25.75           C  
ATOM   2240  CD1 ILE A 289       7.294  15.640  28.613  1.00 29.37           C  
ATOM   2241  N   THR A 290       8.811  19.790  27.210  1.00 22.42           N  
ATOM   2242  CA  THR A 290       9.904  19.768  26.264  1.00 21.38           C  
ATOM   2243  C   THR A 290      11.030  18.880  26.774  1.00 20.56           C  
ATOM   2244  O   THR A 290      11.243  18.743  27.986  1.00 19.81           O  
ATOM   2245  CB  THR A 290      10.461  21.175  26.053  1.00 21.70           C  
ATOM   2246  OG1 THR A 290      10.823  21.761  27.308  1.00 20.15           O  
ATOM   2247  CG2 THR A 290       9.405  22.108  25.460  1.00 21.76           C  
ATOM   2248  N   ILE A 291      11.757  18.296  25.841  1.00 19.36           N  
ATOM   2249  CA  ILE A 291      12.903  17.503  26.190  1.00 19.73           C  
ATOM   2250  C   ILE A 291      14.044  17.865  25.286  1.00 19.29           C  
ATOM   2251  O   ILE A 291      13.862  17.976  24.083  1.00 19.81           O  
ATOM   2252  CB  ILE A 291      12.598  15.992  26.085  1.00 20.08           C  
ATOM   2253  CG1 ILE A 291      11.467  15.609  27.044  1.00 20.06           C  
ATOM   2254  CG2 ILE A 291      13.873  15.214  26.378  1.00 20.21           C  
ATOM   2255  CD1 ILE A 291      11.028  14.131  26.931  1.00 21.77           C  
ATOM   2256  N   THR A 292      15.215  18.070  25.882  1.00 18.95           N  
ATOM   2257  CA  THR A 292      16.406  18.407  25.156  1.00 19.17           C  
ATOM   2258  C   THR A 292      17.589  17.691  25.753  1.00 19.18           C  
ATOM   2259  O   THR A 292      17.671  17.497  26.965  1.00 19.21           O  
ATOM   2260  CB  THR A 292      16.703  19.937  25.259  1.00 19.83           C  
ATOM   2261  OG1 THR A 292      15.559  20.724  24.879  1.00 20.23           O  
ATOM   2262  CG2 THR A 292      17.787  20.350  24.270  1.00 20.15           C  
ATOM   2263  N   VAL A 293      18.530  17.314  24.903  1.00 19.25           N  
ATOM   2264  CA  VAL A 293      19.809  16.824  25.387  1.00 19.51           C  
ATOM   2265  C   VAL A 293      20.912  17.667  24.749  1.00 19.58           C  
ATOM   2266  O   VAL A 293      20.962  17.792  23.535  1.00 18.47           O  
ATOM   2267  CB  VAL A 293      20.024  15.345  25.063  1.00 19.73           C  
ATOM   2268  CG1 VAL A 293      21.490  14.951  25.250  1.00 20.24           C  
ATOM   2269  CG2 VAL A 293      19.146  14.478  25.968  1.00 20.65           C  
ATOM   2270  N   ASN A 294      21.766  18.277  25.569  1.00 19.85           N  
ATOM   2271  CA  ASN A 294      22.882  19.057  25.039  1.00 20.26           C  
ATOM   2272  C   ASN A 294      24.179  18.232  25.052  1.00 20.35           C  
ATOM   2273  O   ASN A 294      24.233  17.131  25.634  1.00 21.82           O  
ATOM   2274  CB  ASN A 294      23.008  20.443  25.727  1.00 20.82           C  
ATOM   2275  CG  ASN A 294      23.676  20.388  27.102  1.00 21.84           C  
ATOM   2276  OD1 ASN A 294      24.209  19.354  27.495  1.00 21.66           O  
ATOM   2277  ND2 ASN A 294      23.630  21.519  27.849  1.00 21.23           N  
ATOM   2278  N   PHE A 295      25.186  18.729  24.346  1.00 20.69           N  
ATOM   2279  CA  PHE A 295      26.490  18.095  24.233  1.00 20.46           C  
ATOM   2280  C   PHE A 295      27.452  19.240  24.494  1.00 21.42           C  
ATOM   2281  O   PHE A 295      27.573  20.167  23.653  1.00 20.85           O  
ATOM   2282  CB  PHE A 295      26.728  17.569  22.814  1.00 20.62           C  
ATOM   2283  CG  PHE A 295      25.898  16.366  22.440  1.00 21.15           C  
ATOM   2284  CD1 PHE A 295      24.526  16.468  22.247  1.00 21.98           C  
ATOM   2285  CD2 PHE A 295      26.498  15.130  22.256  1.00 19.31           C  
ATOM   2286  CE1 PHE A 295      23.791  15.343  21.902  1.00 19.77           C  
ATOM   2287  CE2 PHE A 295      25.762  14.037  21.885  1.00 17.96           C  
ATOM   2288  CZ  PHE A 295      24.424  14.138  21.720  1.00 17.87           C  
ATOM   2289  N   TRP A 296      28.123  19.196  25.645  1.00 21.19           N  
ATOM   2290  CA  TRP A 296      29.023  20.275  26.050  1.00 21.46           C  
ATOM   2291  C   TRP A 296      30.481  19.834  25.873  1.00 21.42           C  
ATOM   2292  O   TRP A 296      30.898  18.795  26.387  1.00 21.96           O  
ATOM   2293  CB  TRP A 296      28.760  20.669  27.498  1.00 21.13           C  
ATOM   2294  CG  TRP A 296      27.853  21.859  27.710  1.00 21.95           C  
ATOM   2295  CD1 TRP A 296      27.797  22.987  26.955  1.00 23.23           C  
ATOM   2296  CD2 TRP A 296      26.935  22.067  28.797  1.00 22.27           C  
ATOM   2297  NE1 TRP A 296      26.882  23.869  27.478  1.00 22.26           N  
ATOM   2298  CE2 TRP A 296      26.336  23.329  28.607  1.00 22.53           C  
ATOM   2299  CE3 TRP A 296      26.531  21.298  29.894  1.00 24.83           C  
ATOM   2300  CZ2 TRP A 296      25.362  23.840  29.463  1.00 22.34           C  
ATOM   2301  CZ3 TRP A 296      25.557  21.810  30.754  1.00 24.59           C  
ATOM   2302  CH2 TRP A 296      24.993  23.075  30.531  1.00 23.75           C  
ATOM   2303  N   TYR A 297      31.235  20.632  25.126  1.00 21.64           N  
ATOM   2304  CA  TYR A 297      32.633  20.361  24.845  1.00 21.81           C  
ATOM   2305  C   TYR A 297      33.482  21.523  25.320  1.00 22.41           C  
ATOM   2306  O   TYR A 297      33.110  22.682  25.146  1.00 21.78           O  
ATOM   2307  CB  TYR A 297      32.862  20.198  23.344  1.00 21.49           C  
ATOM   2308  CG  TYR A 297      32.287  18.943  22.761  1.00 21.77           C  
ATOM   2309  CD1 TYR A 297      30.934  18.870  22.415  1.00 21.68           C  
ATOM   2310  CD2 TYR A 297      33.083  17.841  22.526  1.00 19.80           C  
ATOM   2311  CE1 TYR A 297      30.405  17.734  21.890  1.00 22.16           C  
ATOM   2312  CE2 TYR A 297      32.555  16.690  21.993  1.00 20.99           C  
ATOM   2313  CZ  TYR A 297      31.215  16.637  21.686  1.00 21.46           C  
ATOM   2314  OH  TYR A 297      30.673  15.494  21.159  1.00 22.11           O  
ATOM   2315  N   LYS A 298      34.632  21.220  25.899  1.00 23.17           N  
ATOM   2316  CA  LYS A 298      35.566  22.273  26.288  1.00 24.45           C  
ATOM   2317  C   LYS A 298      36.074  22.912  25.021  1.00 24.21           C  
ATOM   2318  O   LYS A 298      36.264  22.228  24.025  1.00 23.35           O  
ATOM   2319  CB  LYS A 298      36.748  21.699  27.085  1.00 24.85           C  
ATOM   2320  CG  LYS A 298      36.436  21.416  28.552  1.00 28.00           C  
ATOM   2321  CD  LYS A 298      37.657  20.865  29.298  1.00 31.59           C  
ATOM   2322  CE  LYS A 298      37.309  20.447  30.730  1.00 33.77           C  
ATOM   2323  NZ  LYS A 298      38.406  19.627  31.367  1.00 36.02           N  
ATOM   2324  N   GLY A 299      36.317  24.216  25.056  1.00 25.28           N  
ATOM   2325  CA  GLY A 299      36.818  24.909  23.886  1.00 26.38           C  
ATOM   2326  C   GLY A 299      38.254  24.542  23.547  1.00 27.78           C  
ATOM   2327  O   GLY A 299      38.935  23.895  24.315  1.00 27.16           O  
ATOM   2328  N   ALA A 300      38.690  24.949  22.366  1.00 30.42           N  
ATOM   2329  CA  ALA A 300      40.062  24.762  21.918  1.00 32.93           C  
ATOM   2330  C   ALA A 300      41.021  25.544  22.819  1.00 35.12           C  
ATOM   2331  O   ALA A 300      40.597  26.337  23.646  1.00 34.87           O  
ATOM   2332  CB  ALA A 300      40.199  25.249  20.472  1.00 32.98           C  
ATOM   2333  N   PRO A 301      42.318  25.355  22.615  1.00 38.54           N  
ATOM   2334  CA  PRO A 301      43.347  26.012  23.440  1.00 40.37           C  
ATOM   2335  C   PRO A 301      43.548  27.484  23.102  1.00 41.99           C  
ATOM   2336  O   PRO A 301      43.379  27.853  21.950  1.00 42.88           O  
ATOM   2337  CB  PRO A 301      44.615  25.246  23.061  1.00 40.42           C  
ATOM   2338  CG  PRO A 301      44.397  24.879  21.638  1.00 39.87           C  
ATOM   2339  CD  PRO A 301      42.919  24.544  21.535  1.00 38.98           C  
ATOM   2340  N   THR A 302      43.915  28.293  24.090  1.00 44.60           N  
ATOM   2341  CA  THR A 302      44.209  29.725  23.912  1.00 46.30           C  
ATOM   2342  C   THR A 302      45.593  29.790  23.315  1.00 47.41           C  
ATOM   2343  O   THR A 302      46.534  29.388  23.992  1.00 47.96           O  
ATOM   2344  CB  THR A 302      44.242  30.391  25.294  1.00 46.57           C  
ATOM   2345  OG1 THR A 302      42.941  30.320  25.895  1.00 48.00           O  
ATOM   2346  CG2 THR A 302      44.526  31.869  25.199  1.00 47.24           C  
ATOM   2347  N   PRO A 303      45.782  30.336  22.112  1.00 48.55           N  
ATOM   2348  CA  PRO A 303      47.090  30.170  21.473  1.00 48.80           C  
ATOM   2349  C   PRO A 303      48.210  30.717  22.341  1.00 48.76           C  
ATOM   2350  O   PRO A 303      47.874  31.450  23.269  1.00 49.07           O  
ATOM   2351  CB  PRO A 303      46.967  30.980  20.185  1.00 49.07           C  
ATOM   2352  CG  PRO A 303      45.504  31.101  19.952  1.00 48.93           C  
ATOM   2353  CD  PRO A 303      44.916  31.243  21.330  1.00 48.62           C  
ATOM   2354  N   GLU A 307      46.795  36.776  18.436  1.00 52.62           N  
ATOM   2355  CA  GLU A 307      46.885  37.814  17.415  1.00 52.76           C  
ATOM   2356  C   GLU A 307      45.865  38.906  17.636  1.00 52.00           C  
ATOM   2357  O   GLU A 307      44.757  38.658  18.096  1.00 52.48           O  
ATOM   2358  CB  GLU A 307      46.686  37.246  15.996  1.00 53.32           C  
ATOM   2359  CG  GLU A 307      46.893  38.307  14.908  1.00 54.63           C  
ATOM   2360  CD  GLU A 307      46.862  37.764  13.487  1.00 56.43           C  
ATOM   2361  OE1 GLU A 307      46.527  36.574  13.290  1.00 57.49           O  
ATOM   2362  OE2 GLU A 307      47.173  38.543  12.558  1.00 57.89           O  
ATOM   2363  N   TYR A 308      46.255  40.125  17.303  1.00 51.19           N  
ATOM   2364  CA  TYR A 308      45.367  41.267  17.405  1.00 50.55           C  
ATOM   2365  C   TYR A 308      44.747  41.494  16.039  1.00 49.51           C  
ATOM   2366  O   TYR A 308      45.300  41.053  15.028  1.00 49.70           O  
ATOM   2367  CB  TYR A 308      46.151  42.485  17.867  1.00 50.82           C  
ATOM   2368  CG  TYR A 308      46.702  42.286  19.259  1.00 52.47           C  
ATOM   2369  CD1 TYR A 308      45.949  42.632  20.373  1.00 53.15           C  
ATOM   2370  CD2 TYR A 308      47.948  41.696  19.462  1.00 53.79           C  
ATOM   2371  CE1 TYR A 308      46.426  42.426  21.643  1.00 54.22           C  
ATOM   2372  CE2 TYR A 308      48.437  41.487  20.736  1.00 54.76           C  
ATOM   2373  CZ  TYR A 308      47.670  41.857  21.824  1.00 55.10           C  
ATOM   2374  OH  TYR A 308      48.146  41.659  23.101  1.00 56.68           O  
ATOM   2375  N   PRO A 309      43.584  42.135  15.987  1.00 47.88           N  
ATOM   2376  CA  PRO A 309      42.843  42.621  17.169  1.00 46.21           C  
ATOM   2377  C   PRO A 309      42.139  41.503  17.952  1.00 43.75           C  
ATOM   2378  O   PRO A 309      41.768  40.503  17.369  1.00 44.10           O  
ATOM   2379  CB  PRO A 309      41.804  43.566  16.562  1.00 46.39           C  
ATOM   2380  CG  PRO A 309      41.610  43.069  15.128  1.00 47.65           C  
ATOM   2381  CD  PRO A 309      42.899  42.431  14.716  1.00 48.06           C  
ATOM   2382  N   LEU A 310      41.973  41.672  19.256  1.00 40.94           N  
ATOM   2383  CA  LEU A 310      41.349  40.650  20.093  1.00 38.75           C  
ATOM   2384  C   LEU A 310      39.863  40.491  19.817  1.00 36.87           C  
ATOM   2385  O   LEU A 310      39.148  41.474  19.610  1.00 37.02           O  
ATOM   2386  CB  LEU A 310      41.499  41.017  21.566  1.00 38.63           C  
ATOM   2387  CG  LEU A 310      42.571  40.351  22.435  1.00 37.97           C  
ATOM   2388  CD1 LEU A 310      43.840  40.049  21.711  1.00 37.27           C  
ATOM   2389  CD2 LEU A 310      42.836  41.234  23.637  1.00 37.27           C  
ATOM   2390  N   LYS A 311      39.392  39.254  19.847  1.00 34.04           N  
ATOM   2391  CA  LYS A 311      37.972  38.998  19.702  1.00 32.20           C  
ATOM   2392  C   LYS A 311      37.208  39.376  20.968  1.00 30.33           C  
ATOM   2393  O   LYS A 311      37.760  39.421  22.072  1.00 29.17           O  
ATOM   2394  CB  LYS A 311      37.733  37.564  19.371  1.00 32.59           C  
ATOM   2395  N   ALA A 312      35.924  39.641  20.788  1.00 28.23           N  
ATOM   2396  CA  ALA A 312      35.074  40.011  21.895  1.00 27.38           C  
ATOM   2397  C   ALA A 312      35.148  38.973  23.005  1.00 26.28           C  
ATOM   2398  O   ALA A 312      35.271  39.334  24.172  1.00 24.54           O  
ATOM   2399  CB  ALA A 312      33.641  40.205  21.421  1.00 27.09           C  
ATOM   2400  N   HIS A 313      35.101  37.689  22.649  1.00 25.72           N  
ATOM   2401  CA  HIS A 313      35.086  36.669  23.674  1.00 25.82           C  
ATOM   2402  C   HIS A 313      36.399  36.609  24.428  1.00 24.79           C  
ATOM   2403  O   HIS A 313      36.428  36.183  25.557  1.00 24.19           O  
ATOM   2404  CB  HIS A 313      34.688  35.293  23.129  1.00 26.92           C  
ATOM   2405  CG  HIS A 313      35.741  34.641  22.303  1.00 29.84           C  
ATOM   2406  ND1 HIS A 313      35.896  34.903  20.954  1.00 35.52           N  
ATOM   2407  CD2 HIS A 313      36.702  33.746  22.627  1.00 33.54           C  
ATOM   2408  CE1 HIS A 313      36.921  34.208  20.489  1.00 35.03           C  
ATOM   2409  NE2 HIS A 313      37.424  33.491  21.481  1.00 35.78           N  
ATOM   2410  N   GLN A 314      37.479  37.042  23.803  1.00 24.43           N  
ATOM   2411  CA  GLN A 314      38.762  37.092  24.465  1.00 24.34           C  
ATOM   2412  C   GLN A 314      38.762  38.226  25.510  1.00 24.39           C  
ATOM   2413  O   GLN A 314      39.327  38.081  26.590  1.00 24.82           O  
ATOM   2414  CB  GLN A 314      39.882  37.290  23.439  1.00 24.47           C  
ATOM   2415  CG  GLN A 314      40.032  36.106  22.472  1.00 25.49           C  
ATOM   2416  CD  GLN A 314      41.036  36.362  21.366  1.00 25.52           C  
ATOM   2417  OE1 GLN A 314      40.878  37.287  20.563  1.00 27.59           O  
ATOM   2418  NE2 GLN A 314      42.078  35.553  21.330  1.00 28.22           N  
ATOM   2419  N   LYS A 315      38.113  39.337  25.196  1.00 23.51           N  
ATOM   2420  CA  LYS A 315      38.000  40.423  26.154  1.00 23.79           C  
ATOM   2421  C   LYS A 315      37.125  39.979  27.325  1.00 23.05           C  
ATOM   2422  O   LYS A 315      37.373  40.347  28.465  1.00 21.38           O  
ATOM   2423  CB  LYS A 315      37.421  41.667  25.504  1.00 24.09           C  
ATOM   2424  CG  LYS A 315      38.382  42.286  24.533  1.00 26.96           C  
ATOM   2425  CD  LYS A 315      37.849  43.552  23.947  1.00 31.28           C  
ATOM   2426  CE  LYS A 315      38.856  44.156  22.977  1.00 34.34           C  
ATOM   2427  NZ  LYS A 315      38.207  45.098  22.005  1.00 36.25           N  
ATOM   2428  N   VAL A 316      36.109  39.177  27.041  1.00 22.30           N  
ATOM   2429  CA  VAL A 316      35.276  38.673  28.113  1.00 22.39           C  
ATOM   2430  C   VAL A 316      36.124  37.800  29.063  1.00 22.29           C  
ATOM   2431  O   VAL A 316      36.040  37.932  30.274  1.00 21.27           O  
ATOM   2432  CB  VAL A 316      34.065  37.887  27.595  1.00 22.03           C  
ATOM   2433  CG1 VAL A 316      33.309  37.282  28.750  1.00 21.64           C  
ATOM   2434  CG2 VAL A 316      33.123  38.796  26.802  1.00 22.46           C  
ATOM   2435  N   ALA A 317      36.964  36.941  28.499  1.00 22.09           N  
ATOM   2436  CA  ALA A 317      37.848  36.086  29.295  1.00 21.98           C  
ATOM   2437  C   ALA A 317      38.783  36.916  30.164  1.00 21.61           C  
ATOM   2438  O   ALA A 317      39.042  36.573  31.300  1.00 21.05           O  
ATOM   2439  CB  ALA A 317      38.668  35.147  28.380  1.00 22.01           C  
ATOM   2440  N   ILE A 318      39.273  38.016  29.606  1.00 21.45           N  
ATOM   2441  CA  ILE A 318      40.162  38.917  30.318  1.00 21.24           C  
ATOM   2442  C   ILE A 318      39.431  39.511  31.524  1.00 21.38           C  
ATOM   2443  O   ILE A 318      39.937  39.462  32.646  1.00 20.76           O  
ATOM   2444  CB  ILE A 318      40.709  40.023  29.377  1.00 20.58           C  
ATOM   2445  CG1 ILE A 318      41.715  39.434  28.400  1.00 21.19           C  
ATOM   2446  CG2 ILE A 318      41.354  41.167  30.185  1.00 20.20           C  
ATOM   2447  CD1 ILE A 318      42.223  40.419  27.353  1.00 21.35           C  
ATOM   2448  N   MET A 319      38.234  40.030  31.287  1.00 20.83           N  
ATOM   2449  CA  MET A 319      37.446  40.622  32.355  1.00 21.31           C  
ATOM   2450  C   MET A 319      37.154  39.617  33.454  1.00 21.52           C  
ATOM   2451  O   MET A 319      37.326  39.911  34.651  1.00 21.13           O  
ATOM   2452  CB  MET A 319      36.177  41.260  31.818  1.00 21.01           C  
ATOM   2453  CG  MET A 319      36.423  42.519  30.971  1.00 21.17           C  
ATOM   2454  SD  MET A 319      34.860  43.346  30.459  1.00 22.71           S  
ATOM   2455  CE  MET A 319      34.204  42.152  29.206  1.00 22.13           C  
ATOM   2456  N   ARG A 320      36.767  38.408  33.068  1.00 21.34           N  
ATOM   2457  CA  ARG A 320      36.532  37.399  34.075  1.00 21.12           C  
ATOM   2458  C   ARG A 320      37.801  37.186  34.898  1.00 21.25           C  
ATOM   2459  O   ARG A 320      37.747  37.064  36.122  1.00 21.48           O  
ATOM   2460  CB  ARG A 320      36.102  36.095  33.427  1.00 21.01           C  
ATOM   2461  CG  ARG A 320      34.723  36.145  32.741  1.00 20.63           C  
ATOM   2462  CD  ARG A 320      34.324  34.795  32.142  1.00 18.73           C  
ATOM   2463  NE  ARG A 320      34.225  33.824  33.225  1.00 19.25           N  
ATOM   2464  CZ  ARG A 320      33.247  33.809  34.115  1.00 19.86           C  
ATOM   2465  NH1 ARG A 320      32.259  34.689  34.062  1.00 21.08           N  
ATOM   2466  NH2 ARG A 320      33.263  32.923  35.081  1.00 23.29           N  
ATOM   2467  N   ASN A 321      38.947  37.123  34.231  1.00 20.94           N  
ATOM   2468  CA  ASN A 321      40.184  36.855  34.939  1.00 20.88           C  
ATOM   2469  C   ASN A 321      40.535  37.981  35.916  1.00 20.93           C  
ATOM   2470  O   ASN A 321      40.962  37.716  37.047  1.00 21.77           O  
ATOM   2471  CB  ASN A 321      41.324  36.552  33.958  1.00 21.04           C  
ATOM   2472  CG  ASN A 321      41.288  35.099  33.447  1.00 22.80           C  
ATOM   2473  OD1 ASN A 321      40.924  34.193  34.185  1.00 23.97           O  
ATOM   2474  ND2 ASN A 321      41.666  34.887  32.193  1.00 21.35           N  
ATOM   2475  N   ILE A 322      40.355  39.233  35.505  1.00 20.14           N  
ATOM   2476  CA  ILE A 322      40.633  40.336  36.408  1.00 20.06           C  
ATOM   2477  C   ILE A 322      39.742  40.196  37.650  1.00 19.42           C  
ATOM   2478  O   ILE A 322      40.207  40.345  38.767  1.00 18.73           O  
ATOM   2479  CB  ILE A 322      40.372  41.690  35.715  1.00 20.21           C  
ATOM   2480  CG1 ILE A 322      41.320  41.894  34.535  1.00 21.54           C  
ATOM   2481  CG2 ILE A 322      40.504  42.823  36.699  1.00 20.53           C  
ATOM   2482  CD1 ILE A 322      42.806  41.798  34.868  1.00 24.56           C  
ATOM   2483  N   GLU A 323      38.458  39.904  37.454  1.00 18.94           N  
ATOM   2484  CA  GLU A 323      37.553  39.757  38.576  1.00 18.98           C  
ATOM   2485  C   GLU A 323      38.027  38.651  39.492  1.00 19.33           C  
ATOM   2486  O   GLU A 323      38.084  38.832  40.707  1.00 19.05           O  
ATOM   2487  CB  GLU A 323      36.113  39.538  38.106  1.00 19.25           C  
ATOM   2488  CG  GLU A 323      35.518  40.803  37.484  1.00 19.34           C  
ATOM   2489  CD  GLU A 323      34.143  40.616  36.855  1.00 18.71           C  
ATOM   2490  OE1 GLU A 323      33.183  40.332  37.573  1.00 19.19           O  
ATOM   2491  OE2 GLU A 323      34.024  40.805  35.636  1.00 19.56           O  
ATOM   2492  N   LYS A 324      38.425  37.528  38.908  1.00 19.55           N  
ATOM   2493  CA  LYS A 324      38.874  36.379  39.693  1.00 20.24           C  
ATOM   2494  C   LYS A 324      40.115  36.707  40.513  1.00 20.68           C  
ATOM   2495  O   LYS A 324      40.157  36.405  41.699  1.00 20.83           O  
ATOM   2496  CB  LYS A 324      39.175  35.175  38.789  1.00 20.07           C  
ATOM   2497  CG  LYS A 324      37.924  34.507  38.212  1.00 20.57           C  
ATOM   2498  CD  LYS A 324      38.331  33.318  37.350  1.00 20.28           C  
ATOM   2499  CE  LYS A 324      37.137  32.689  36.621  1.00 19.29           C  
ATOM   2500  NZ  LYS A 324      37.596  31.460  35.876  1.00 17.17           N  
ATOM   2501  N   MET A 325      41.112  37.320  39.885  1.00 21.21           N  
ATOM   2502  CA  MET A 325      42.366  37.657  40.568  1.00 22.87           C  
ATOM   2503  C   MET A 325      42.162  38.665  41.699  1.00 22.44           C  
ATOM   2504  O   MET A 325      42.763  38.560  42.771  1.00 22.08           O  
ATOM   2505  CB  MET A 325      43.380  38.232  39.572  1.00 23.32           C  
ATOM   2506  CG  MET A 325      43.993  37.195  38.671  1.00 27.47           C  
ATOM   2507  SD  MET A 325      44.795  37.924  37.197  1.00 35.56           S  
ATOM   2508  CE  MET A 325      45.664  39.189  38.009  1.00 34.71           C  
ATOM   2509  N   LEU A 326      41.309  39.641  41.452  1.00 22.71           N  
ATOM   2510  CA  LEU A 326      41.043  40.670  42.449  1.00 23.24           C  
ATOM   2511  C   LEU A 326      40.385  40.073  43.679  1.00 23.15           C  
ATOM   2512  O   LEU A 326      40.735  40.417  44.795  1.00 22.40           O  
ATOM   2513  CB  LEU A 326      40.151  41.735  41.865  1.00 23.01           C  
ATOM   2514  CG  LEU A 326      40.677  43.139  41.625  1.00 25.86           C  
ATOM   2515  CD1 LEU A 326      42.187  43.277  41.529  1.00 26.53           C  
ATOM   2516  CD2 LEU A 326      39.986  43.672  40.377  1.00 25.54           C  
ATOM   2517  N   GLY A 327      39.441  39.164  43.460  1.00 23.29           N  
ATOM   2518  CA  GLY A 327      38.760  38.489  44.547  1.00 23.97           C  
ATOM   2519  C   GLY A 327      39.728  37.723  45.418  1.00 24.63           C  
ATOM   2520  O   GLY A 327      39.659  37.783  46.649  1.00 24.75           O  
ATOM   2521  N   GLU A 328      40.644  37.002  44.778  1.00 25.03           N  
ATOM   2522  CA  GLU A 328      41.671  36.265  45.506  1.00 26.08           C  
ATOM   2523  C   GLU A 328      42.661  37.180  46.223  1.00 25.43           C  
ATOM   2524  O   GLU A 328      43.029  36.926  47.367  1.00 25.16           O  
ATOM   2525  CB  GLU A 328      42.442  35.368  44.546  1.00 26.76           C  
ATOM   2526  CG  GLU A 328      41.576  34.278  43.947  1.00 30.36           C  
ATOM   2527  CD  GLU A 328      41.719  32.957  44.676  1.00 35.76           C  
ATOM   2528  OE1 GLU A 328      42.091  32.986  45.878  1.00 38.79           O  
ATOM   2529  OE2 GLU A 328      41.483  31.896  44.034  1.00 38.82           O  
ATOM   2530  N   ALA A 329      43.094  38.240  45.552  1.00 24.91           N  
ATOM   2531  CA  ALA A 329      44.102  39.119  46.134  1.00 24.95           C  
ATOM   2532  C   ALA A 329      43.535  39.929  47.285  1.00 24.94           C  
ATOM   2533  O   ALA A 329      44.197  40.147  48.276  1.00 24.57           O  
ATOM   2534  CB  ALA A 329      44.682  40.022  45.088  1.00 24.88           C  
ATOM   2535  N   LEU A 330      42.290  40.354  47.161  1.00 25.47           N  
ATOM   2536  CA  LEU A 330      41.672  41.133  48.219  1.00 26.16           C  
ATOM   2537  C   LEU A 330      41.212  40.265  49.379  1.00 26.80           C  
ATOM   2538  O   LEU A 330      40.994  40.761  50.471  1.00 27.00           O  
ATOM   2539  CB  LEU A 330      40.504  41.930  47.669  1.00 26.08           C  
ATOM   2540  CG  LEU A 330      40.954  42.981  46.653  1.00 26.04           C  
ATOM   2541  CD1 LEU A 330      39.760  43.489  45.888  1.00 26.16           C  
ATOM   2542  CD2 LEU A 330      41.688  44.134  47.353  1.00 26.65           C  
ATOM   2543  N   GLY A 331      41.037  38.977  49.126  1.00 27.87           N  
ATOM   2544  CA  GLY A 331      40.645  38.039  50.158  1.00 28.89           C  
ATOM   2545  C   GLY A 331      39.176  38.086  50.526  1.00 29.43           C  
ATOM   2546  O   GLY A 331      38.763  37.435  51.478  1.00 30.62           O  
ATOM   2547  N   ASN A 332      38.400  38.887  49.808  1.00 29.59           N  
ATOM   2548  CA  ASN A 332      36.963  38.995  50.023  1.00 29.64           C  
ATOM   2549  C   ASN A 332      36.367  39.500  48.718  1.00 29.00           C  
ATOM   2550  O   ASN A 332      36.649  40.605  48.303  1.00 28.70           O  
ATOM   2551  CB  ASN A 332      36.656  39.973  51.156  1.00 30.15           C  
ATOM   2552  CG  ASN A 332      35.162  40.094  51.441  1.00 31.82           C  
ATOM   2553  OD1 ASN A 332      34.335  39.531  50.734  1.00 34.71           O  
ATOM   2554  ND2 ASN A 332      34.818  40.818  52.504  1.00 35.11           N  
ATOM   2555  N   PRO A 333      35.528  38.706  48.081  1.00 28.53           N  
ATOM   2556  CA  PRO A 333      35.001  39.075  46.771  1.00 28.25           C  
ATOM   2557  C   PRO A 333      34.176  40.343  46.807  1.00 27.91           C  
ATOM   2558  O   PRO A 333      34.033  40.984  45.776  1.00 26.99           O  
ATOM   2559  CB  PRO A 333      34.120  37.893  46.368  1.00 28.16           C  
ATOM   2560  CG  PRO A 333      34.137  36.938  47.468  1.00 28.91           C  
ATOM   2561  CD  PRO A 333      35.022  37.415  48.561  1.00 28.96           C  
ATOM   2562  N   GLN A 334      33.638  40.701  47.965  1.00 27.80           N  
ATOM   2563  CA  GLN A 334      32.814  41.896  48.039  1.00 27.97           C  
ATOM   2564  C   GLN A 334      33.665  43.155  47.975  1.00 26.77           C  
ATOM   2565  O   GLN A 334      33.144  44.245  47.764  1.00 26.51           O  
ATOM   2566  CB  GLN A 334      31.906  41.867  49.278  1.00 28.98           C  
ATOM   2567  CG  GLN A 334      30.675  40.969  49.038  1.00 32.17           C  
ATOM   2568  CD  GLN A 334      29.661  40.962  50.175  1.00 35.54           C  
ATOM   2569  OE1 GLN A 334      29.682  41.840  51.048  1.00 37.92           O  
ATOM   2570  NE2 GLN A 334      28.760  39.961  50.163  1.00 36.72           N  
ATOM   2571  N   GLU A 335      34.974  43.007  48.132  1.00 25.19           N  
ATOM   2572  CA  GLU A 335      35.860  44.151  48.018  1.00 24.41           C  
ATOM   2573  C   GLU A 335      36.170  44.466  46.537  1.00 22.68           C  
ATOM   2574  O   GLU A 335      36.700  45.521  46.228  1.00 21.42           O  
ATOM   2575  CB  GLU A 335      37.150  43.928  48.835  1.00 24.98           C  
ATOM   2576  CG  GLU A 335      36.974  44.148  50.343  1.00 27.94           C  
ATOM   2577  CD  GLU A 335      38.264  44.055  51.139  1.00 31.85           C  
ATOM   2578  OE1 GLU A 335      39.248  44.736  50.777  1.00 34.79           O  
ATOM   2579  OE2 GLU A 335      38.298  43.312  52.158  1.00 36.87           O  
ATOM   2580  N   VAL A 336      35.809  43.566  45.625  1.00 21.32           N  
ATOM   2581  CA  VAL A 336      36.113  43.751  44.201  1.00 20.37           C  
ATOM   2582  C   VAL A 336      35.541  45.034  43.603  1.00 20.01           C  
ATOM   2583  O   VAL A 336      36.247  45.798  42.954  1.00 19.07           O  
ATOM   2584  CB  VAL A 336      35.647  42.554  43.371  1.00 20.60           C  
ATOM   2585  CG1 VAL A 336      35.785  42.841  41.883  1.00 21.06           C  
ATOM   2586  CG2 VAL A 336      36.463  41.316  43.743  1.00 20.68           C  
ATOM   2587  N   GLY A 337      34.260  45.275  43.842  1.00 19.61           N  
ATOM   2588  CA  GLY A 337      33.593  46.437  43.317  1.00 19.45           C  
ATOM   2589  C   GLY A 337      34.205  47.760  43.731  1.00 19.51           C  
ATOM   2590  O   GLY A 337      34.522  48.576  42.871  1.00 18.93           O  
ATOM   2591  N   PRO A 338      34.333  48.010  45.032  1.00 20.41           N  
ATOM   2592  CA  PRO A 338      34.959  49.253  45.503  1.00 20.40           C  
ATOM   2593  C   PRO A 338      36.368  49.500  44.923  1.00 20.13           C  
ATOM   2594  O   PRO A 338      36.674  50.630  44.548  1.00 19.20           O  
ATOM   2595  CB  PRO A 338      34.960  49.092  47.035  1.00 20.63           C  
ATOM   2596  CG  PRO A 338      33.749  48.261  47.298  1.00 21.17           C  
ATOM   2597  CD  PRO A 338      33.782  47.221  46.151  1.00 20.95           C  
ATOM   2598  N   LEU A 339      37.199  48.470  44.831  1.00 20.34           N  
ATOM   2599  CA  LEU A 339      38.518  48.655  44.234  1.00 20.55           C  
ATOM   2600  C   LEU A 339      38.382  49.060  42.768  1.00 20.06           C  
ATOM   2601  O   LEU A 339      39.020  50.019  42.330  1.00 19.61           O  
ATOM   2602  CB  LEU A 339      39.383  47.408  44.358  1.00 20.81           C  
ATOM   2603  CG  LEU A 339      40.855  47.618  43.943  1.00 22.54           C  
ATOM   2604  CD1 LEU A 339      41.809  46.817  44.786  1.00 25.30           C  
ATOM   2605  CD2 LEU A 339      41.035  47.209  42.496  1.00 23.17           C  
ATOM   2606  N   LEU A 340      37.526  48.361  42.023  1.00 19.51           N  
ATOM   2607  CA  LEU A 340      37.327  48.687  40.600  1.00 19.36           C  
ATOM   2608  C   LEU A 340      36.827  50.120  40.427  1.00 19.30           C  
ATOM   2609  O   LEU A 340      37.318  50.861  39.566  1.00 17.55           O  
ATOM   2610  CB  LEU A 340      36.361  47.721  39.952  1.00 19.31           C  
ATOM   2611  CG  LEU A 340      36.929  46.333  39.637  1.00 21.99           C  
ATOM   2612  CD1 LEU A 340      35.842  45.506  39.069  1.00 22.03           C  
ATOM   2613  CD2 LEU A 340      38.140  46.390  38.673  1.00 21.20           C  
ATOM   2614  N   ASN A 341      35.879  50.521  41.270  1.00 19.17           N  
ATOM   2615  CA  ASN A 341      35.369  51.887  41.232  1.00 20.20           C  
ATOM   2616  C   ASN A 341      36.465  52.914  41.530  1.00 19.98           C  
ATOM   2617  O   ASN A 341      36.598  53.920  40.848  1.00 19.61           O  
ATOM   2618  CB  ASN A 341      34.181  52.043  42.196  1.00 20.66           C  
ATOM   2619  CG  ASN A 341      32.898  51.459  41.619  1.00 24.17           C  
ATOM   2620  OD1 ASN A 341      32.484  51.843  40.531  1.00 30.93           O  
ATOM   2621  ND2 ASN A 341      32.294  50.499  42.317  1.00 26.37           N  
ATOM   2622  N   THR A 342      37.245  52.633  42.558  1.00 20.07           N  
ATOM   2623  CA  THR A 342      38.351  53.489  42.939  1.00 20.49           C  
ATOM   2624  C   THR A 342      39.322  53.613  41.763  1.00 20.27           C  
ATOM   2625  O   THR A 342      39.835  54.688  41.502  1.00 19.66           O  
ATOM   2626  CB  THR A 342      39.001  52.909  44.189  1.00 20.82           C  
ATOM   2627  OG1 THR A 342      38.123  53.124  45.320  1.00 22.13           O  
ATOM   2628  CG2 THR A 342      40.308  53.625  44.545  1.00 21.01           C  
ATOM   2629  N   MET A 343      39.517  52.525  41.024  1.00 20.30           N  
ATOM   2630  CA  MET A 343      40.402  52.543  39.873  1.00 20.66           C  
ATOM   2631  C   MET A 343      39.932  53.445  38.758  1.00 20.29           C  
ATOM   2632  O   MET A 343      40.750  54.119  38.129  1.00 19.31           O  
ATOM   2633  CB  MET A 343      40.560  51.157  39.270  1.00 20.76           C  
ATOM   2634  CG  MET A 343      41.810  50.453  39.625  1.00 23.39           C  
ATOM   2635  SD  MET A 343      42.247  49.059  38.524  1.00 25.69           S  
ATOM   2636  CE  MET A 343      41.161  48.058  38.968  1.00 26.74           C  
ATOM   2637  N   ILE A 344      38.631  53.438  38.466  1.00 20.76           N  
ATOM   2638  CA  ILE A 344      38.167  54.187  37.312  1.00 21.23           C  
ATOM   2639  C   ILE A 344      37.648  55.577  37.565  1.00 20.71           C  
ATOM   2640  O   ILE A 344      37.763  56.403  36.666  1.00 20.65           O  
ATOM   2641  CB  ILE A 344      37.109  53.400  36.458  1.00 22.07           C  
ATOM   2642  CG1 ILE A 344      35.710  53.613  36.992  1.00 23.91           C  
ATOM   2643  CG2 ILE A 344      37.482  51.943  36.352  1.00 24.35           C  
ATOM   2644  CD1 ILE A 344      34.650  53.199  36.033  1.00 28.26           C  
ATOM   2645  N   LYS A 345      37.069  55.886  38.726  1.00 20.84           N  
ATOM   2646  CA  LYS A 345      36.482  57.231  38.817  1.00 21.15           C  
ATOM   2647  C   LYS A 345      37.464  58.376  38.784  1.00 19.86           C  
ATOM   2648  O   LYS A 345      38.459  58.429  39.517  1.00 19.23           O  
ATOM   2649  CB  LYS A 345      35.438  57.451  39.922  1.00 22.66           C  
ATOM   2650  CG  LYS A 345      35.562  56.714  41.190  1.00 27.82           C  
ATOM   2651  CD  LYS A 345      34.214  56.021  41.489  1.00 30.51           C  
ATOM   2652  CE  LYS A 345      33.398  56.782  42.502  1.00 32.51           C  
ATOM   2653  NZ  LYS A 345      34.069  56.806  43.829  1.00 37.63           N  
ATOM   2654  N   GLY A 346      37.143  59.307  37.899  1.00 18.18           N  
ATOM   2655  CA  GLY A 346      37.978  60.453  37.644  1.00 17.22           C  
ATOM   2656  C   GLY A 346      39.303  60.105  36.978  1.00 16.31           C  
ATOM   2657  O   GLY A 346      40.172  60.949  36.889  1.00 16.63           O  
ATOM   2658  N   ARG A 347      39.453  58.872  36.531  1.00 16.85           N  
ATOM   2659  CA  ARG A 347      40.697  58.413  35.904  1.00 17.52           C  
ATOM   2660  C   ARG A 347      40.469  57.811  34.502  1.00 17.57           C  
ATOM   2661  O   ARG A 347      41.178  58.143  33.559  1.00 17.10           O  
ATOM   2662  CB  ARG A 347      41.379  57.384  36.812  1.00 17.20           C  
ATOM   2663  CG  ARG A 347      41.822  57.949  38.181  1.00 16.77           C  
ATOM   2664  CD  ARG A 347      43.287  57.491  38.583  1.00 18.88           C  
ATOM   2665  NE  ARG A 347      43.254  56.087  38.618  1.00 17.77           N  
ATOM   2666  CZ  ARG A 347      44.115  55.220  38.149  1.00 16.11           C  
ATOM   2667  NH1 ARG A 347      45.323  55.512  37.658  1.00 16.59           N  
ATOM   2668  NH2 ARG A 347      43.734  53.978  38.276  1.00 13.22           N  
ATOM   2669  N   TYR A 348      39.472  56.954  34.375  1.00 18.74           N  
ATOM   2670  CA  TYR A 348      39.138  56.317  33.091  1.00 20.48           C  
ATOM   2671  C   TYR A 348      37.674  56.499  32.671  1.00 21.75           C  
ATOM   2672  O   TYR A 348      37.296  56.047  31.596  1.00 22.39           O  
ATOM   2673  CB  TYR A 348      39.411  54.800  33.124  1.00 19.97           C  
ATOM   2674  CG  TYR A 348      40.874  54.384  33.199  1.00 19.65           C  
ATOM   2675  CD1 TYR A 348      41.661  54.310  32.054  1.00 18.48           C  
ATOM   2676  CD2 TYR A 348      41.458  54.051  34.414  1.00 17.73           C  
ATOM   2677  CE1 TYR A 348      42.986  53.921  32.122  1.00 19.00           C  
ATOM   2678  CE2 TYR A 348      42.775  53.667  34.494  1.00 18.72           C  
ATOM   2679  CZ  TYR A 348      43.543  53.600  33.339  1.00 18.96           C  
ATOM   2680  OH  TYR A 348      44.856  53.203  33.419  1.00 17.77           O  
ATOM   2681  N   ASN A 349      36.837  57.123  33.488  1.00 23.99           N  
ATOM   2682  CA  ASN A 349      35.429  57.244  33.089  1.00 26.57           C  
ATOM   2683  C   ASN A 349      34.947  58.611  32.689  1.00 27.62           C  
ATOM   2684  O   ASN A 349      35.646  59.606  32.655  1.00 28.49           O  
ATOM   2685  CB  ASN A 349      34.496  56.720  34.150  1.00 26.11           C  
ATOM   2686  CG  ASN A 349      34.511  57.552  35.386  1.00 28.01           C  
ATOM   2687  OD1 ASN A 349      35.282  58.518  35.517  1.00 29.49           O  
ATOM   2688  ND2 ASN A 349      33.658  57.173  36.342  1.00 31.84           N  
ATOM   2689  OXT ASN A 349      33.761  58.686  32.399  1.00 31.04           O  
TER    2690      ASN A 349                                                      
ATOM   2691  N   LEU S 795      45.837  35.555  30.600  1.00 35.49           N  
ATOM   2692  CA  LEU S 795      44.757  36.539  30.946  1.00 35.77           C  
ATOM   2693  C   LEU S 795      43.580  36.250  30.030  1.00 35.54           C  
ATOM   2694  O   LEU S 795      42.418  36.338  30.412  1.00 34.79           O  
ATOM   2695  CB  LEU S 795      45.257  37.967  30.787  1.00 36.01           C  
ATOM   2696  CG  LEU S 795      44.695  38.978  31.791  1.00 37.16           C  
ATOM   2697  CD1 LEU S 795      44.761  38.459  33.204  1.00 37.65           C  
ATOM   2698  CD2 LEU S 795      45.450  40.289  31.718  1.00 38.07           C  
ATOM   2699  N   THR S 796      43.936  35.940  28.796  1.00 35.47           N  
ATOM   2700  CA  THR S 796      43.060  35.351  27.800  1.00 36.25           C  
ATOM   2701  C   THR S 796      42.644  33.888  28.079  1.00 35.84           C  
ATOM   2702  O   THR S 796      41.819  33.331  27.365  1.00 36.38           O  
ATOM   2703  CB  THR S 796      43.817  35.429  26.457  1.00 36.63           C  
ATOM   2704  OG1 THR S 796      43.251  34.528  25.524  1.00 38.48           O  
ATOM   2705  CG2 THR S 796      45.257  34.907  26.593  1.00 37.07           C  
ATOM   2706  N   SER S 797      43.197  33.251  29.101  1.00 35.44           N  
ATOM   2707  CA  SER S 797      42.835  31.860  29.377  1.00 35.29           C  
ATOM   2708  C   SER S 797      41.426  31.760  29.984  1.00 35.18           C  
ATOM   2709  O   SER S 797      40.925  32.701  30.611  1.00 33.96           O  
ATOM   2710  CB  SER S 797      43.856  31.189  30.291  1.00 35.17           C  
ATOM   2711  OG  SER S 797      43.716  31.654  31.624  1.00 36.65           O  
ATOM   2712  N   TYR S 798      40.789  30.611  29.790  1.00 35.36           N  
ATOM   2713  CA  TYR S 798      39.427  30.430  30.256  1.00 35.94           C  
ATOM   2714  C   TYR S 798      39.148  29.075  30.890  1.00 35.14           C  
ATOM   2715  O   TYR S 798      39.845  28.095  30.657  1.00 35.54           O  
ATOM   2716  CB  TYR S 798      38.440  30.707  29.120  1.00 36.37           C  
ATOM   2717  CG  TYR S 798      38.554  29.794  27.920  1.00 39.89           C  
ATOM   2718  CD1 TYR S 798      39.587  29.934  26.996  1.00 42.41           C  
ATOM   2719  CD2 TYR S 798      37.606  28.808  27.697  1.00 43.13           C  
ATOM   2720  CE1 TYR S 798      39.681  29.095  25.893  1.00 43.97           C  
ATOM   2721  CE2 TYR S 798      37.687  27.963  26.597  1.00 44.94           C  
ATOM   2722  CZ  TYR S 798      38.723  28.109  25.698  1.00 44.95           C  
ATOM   2723  OH  TYR S 798      38.781  27.270  24.613  1.00 44.37           O  
ATOM   2724  N   ASP S 799      38.108  29.046  31.709  1.00 34.54           N  
ATOM   2725  CA  ASP S 799      37.685  27.840  32.392  1.00 33.87           C  
ATOM   2726  C   ASP S 799      36.600  27.187  31.545  1.00 32.58           C  
ATOM   2727  O   ASP S 799      36.465  27.501  30.366  1.00 32.32           O  
ATOM   2728  CB  ASP S 799      37.140  28.208  33.770  1.00 34.50           C  
ATOM   2729  CG  ASP S 799      37.299  27.104  34.773  1.00 36.07           C  
ATOM   2730  OD1 ASP S 799      36.790  25.986  34.551  1.00 37.15           O  
ATOM   2731  OD2 ASP S 799      37.918  27.279  35.833  1.00 41.54           O  
ATOM   2732  N   CYS S 800      35.812  26.301  32.141  1.00 30.83           N  
ATOM   2733  CA  CYS S 800      34.798  25.586  31.392  1.00 29.83           C  
ATOM   2734  C   CYS S 800      33.490  25.511  32.161  1.00 29.15           C  
ATOM   2735  O   CYS S 800      32.794  24.502  32.092  1.00 28.68           O  
ATOM   2736  CB  CYS S 800      35.273  24.167  31.092  1.00 29.46           C  
ATOM   2737  SG  CYS S 800      35.576  23.194  32.601  1.00 30.36           S  
ATOM   2738  N   GLU S 801      33.152  26.578  32.874  1.00 28.36           N  
ATOM   2739  CA  GLU S 801      31.936  26.605  33.670  1.00 28.63           C  
ATOM   2740  C   GLU S 801      30.667  26.793  32.829  1.00 28.34           C  
ATOM   2741  O   GLU S 801      30.626  27.562  31.867  1.00 27.30           O  
ATOM   2742  CB  GLU S 801      32.038  27.688  34.751  1.00 28.61           C  
ATOM   2743  CG  GLU S 801      33.252  27.501  35.655  1.00 30.83           C  
ATOM   2744  CD  GLU S 801      33.188  28.346  36.907  1.00 32.58           C  
ATOM   2745  OE1 GLU S 801      32.414  27.985  37.805  1.00 33.57           O  
ATOM   2746  OE2 GLU S 801      33.910  29.362  36.989  1.00 33.97           O  
ATOM   2747  N   VAL S 802      29.627  26.062  33.212  1.00 28.85           N  
ATOM   2748  CA  VAL S 802      28.350  26.079  32.515  1.00 29.03           C  
ATOM   2749  C   VAL S 802      27.233  26.056  33.546  1.00 29.80           C  
ATOM   2750  O   VAL S 802      27.505  25.948  34.726  1.00 29.92           O  
ATOM   2751  CB  VAL S 802      28.221  24.834  31.606  1.00 28.44           C  
ATOM   2752  CG1 VAL S 802      29.288  24.856  30.523  1.00 26.99           C  
ATOM   2753  CG2 VAL S 802      28.333  23.551  32.428  1.00 29.08           C  
ATOM   2754  N   ASN S 803      25.978  26.135  33.111  1.00 31.09           N  
ATOM   2755  CA  ASN S 803      24.853  26.053  34.042  1.00 32.53           C  
ATOM   2756  C   ASN S 803      24.550  24.641  34.497  1.00 33.81           C  
ATOM   2757  O   ASN S 803      23.456  24.143  34.270  1.00 34.27           O  
ATOM   2758  CB  ASN S 803      23.575  26.659  33.463  1.00 32.29           C  
ATOM   2759  CG  ASN S 803      23.640  28.146  33.367  1.00 31.77           C  
ATOM   2760  OD1 ASN S 803      24.688  28.741  33.616  1.00 33.47           O  
ATOM   2761  ND2 ASN S 803      22.525  28.772  33.005  1.00 29.83           N  
ATOM   2762  N   ALA S 804      25.521  24.015  35.147  1.00 35.23           N  
ATOM   2763  CA  ALA S 804      25.365  22.689  35.740  1.00 36.86           C  
ATOM   2764  C   ALA S 804      26.577  22.452  36.638  1.00 37.98           C  
ATOM   2765  O   ALA S 804      27.660  22.949  36.360  1.00 37.44           O  
ATOM   2766  CB  ALA S 804      25.285  21.610  34.676  1.00 36.63           C  
ATOM   2767  N   PRO S 805      26.394  21.694  37.711  1.00 40.20           N  
ATOM   2768  CA  PRO S 805      27.495  21.381  38.635  1.00 41.46           C  
ATOM   2769  C   PRO S 805      28.572  20.511  37.983  1.00 42.51           C  
ATOM   2770  O   PRO S 805      28.342  19.931  36.938  1.00 43.07           O  
ATOM   2771  CB  PRO S 805      26.799  20.615  39.774  1.00 41.54           C  
ATOM   2772  CG  PRO S 805      25.506  20.116  39.185  1.00 41.29           C  
ATOM   2773  CD  PRO S 805      25.117  21.076  38.115  1.00 40.40           C  
ATOM   2774  N   ILE S 806      29.728  20.406  38.622  1.00 44.25           N  
ATOM   2775  CA  ILE S 806      30.854  19.627  38.099  1.00 44.96           C  
ATOM   2776  C   ILE S 806      30.770  18.169  38.532  1.00 45.18           C  
ATOM   2777  O   ILE S 806      29.902  17.801  39.323  1.00 45.78           O  
ATOM   2778  CB  ILE S 806      32.197  20.246  38.569  1.00 45.19           C  
ATOM   2779  CG1 ILE S 806      32.412  20.018  40.070  1.00 46.10           C  
ATOM   2780  CG2 ILE S 806      32.230  21.743  38.246  1.00 46.08           C  
ATOM   2781  CD1 ILE S 806      33.740  20.574  40.597  1.00 46.98           C  
ATOM   2782  N   LEU S 812      29.934   8.629  39.561  1.00 43.80           N  
ATOM   2783  CA  LEU S 812      29.027   8.736  38.425  1.00 43.90           C  
ATOM   2784  C   LEU S 812      29.761   9.243  37.182  1.00 43.45           C  
ATOM   2785  O   LEU S 812      30.160  10.410  37.114  1.00 43.36           O  
ATOM   2786  CB  LEU S 812      27.862   9.678  38.757  1.00 44.22           C  
ATOM   2787  CG  LEU S 812      26.979   9.292  39.951  1.00 45.50           C  
ATOM   2788  CD1 LEU S 812      25.871  10.341  40.144  1.00 46.20           C  
ATOM   2789  CD2 LEU S 812      26.385   7.894  39.793  1.00 45.08           C  
ATOM   2790  N   LEU S 813      29.928   8.375  36.190  1.00 42.70           N  
ATOM   2791  CA  LEU S 813      30.620   8.776  34.969  1.00 42.21           C  
ATOM   2792  C   LEU S 813      29.711   9.604  34.057  1.00 41.46           C  
ATOM   2793  O   LEU S 813      28.492   9.438  34.062  1.00 41.23           O  
ATOM   2794  CB  LEU S 813      31.167   7.554  34.225  1.00 42.30           C  
ATOM   2795  CG  LEU S 813      32.093   6.644  35.046  1.00 42.35           C  
ATOM   2796  CD1 LEU S 813      32.494   5.419  34.233  1.00 42.48           C  
ATOM   2797  CD2 LEU S 813      33.322   7.398  35.527  1.00 41.80           C  
ATOM   2798  N   GLN S 814      30.326  10.492  33.283  1.00 40.74           N  
ATOM   2799  CA  GLN S 814      29.603  11.385  32.378  1.00 40.26           C  
ATOM   2800  C   GLN S 814      30.475  11.775  31.190  1.00 39.82           C  
ATOM   2801  O   GLN S 814      31.674  11.514  31.176  1.00 39.19           O  
ATOM   2802  CB  GLN S 814      29.173  12.649  33.122  1.00 40.24           C  
ATOM   2803  CG  GLN S 814      30.336  13.501  33.615  1.00 40.51           C  
ATOM   2804  CD  GLN S 814      29.879  14.725  34.406  1.00 41.88           C  
ATOM   2805  OE1 GLN S 814      29.200  14.590  35.419  1.00 41.86           O  
ATOM   2806  NE2 GLN S 814      30.253  15.919  33.940  1.00 40.63           N  
ATOM   2807  N   GLY S 815      29.864  12.416  30.200  1.00 39.81           N  
ATOM   2808  CA  GLY S 815      30.568  12.851  29.012  1.00 39.53           C  
ATOM   2809  C   GLY S 815      31.402  11.755  28.365  1.00 39.85           C  
ATOM   2810  O   GLY S 815      30.962  10.609  28.210  1.00 38.55           O  
ATOM   2811  N   GLU S 816      32.624  12.123  27.995  1.00 40.44           N  
ATOM   2812  CA  GLU S 816      33.553  11.208  27.352  1.00 41.24           C  
ATOM   2813  C   GLU S 816      33.744   9.926  28.154  1.00 41.73           C  
ATOM   2814  O   GLU S 816      33.895   8.852  27.577  1.00 41.11           O  
ATOM   2815  CB  GLU S 816      34.909  11.884  27.148  1.00 41.24           C  
ATOM   2816  CG  GLU S 816      35.752  11.238  26.063  1.00 42.19           C  
ATOM   2817  CD  GLU S 816      37.161  11.790  26.019  1.00 43.70           C  
ATOM   2818  OE1 GLU S 816      37.985  11.311  26.814  1.00 45.25           O  
ATOM   2819  OE2 GLU S 816      37.447  12.696  25.201  1.00 44.50           O  
ATOM   2820  N   GLU S 817      33.724  10.039  29.479  1.00 42.66           N  
ATOM   2821  CA  GLU S 817      33.925   8.877  30.340  1.00 43.73           C  
ATOM   2822  C   GLU S 817      32.744   7.917  30.268  1.00 44.19           C  
ATOM   2823  O   GLU S 817      32.930   6.699  30.252  1.00 43.99           O  
ATOM   2824  CB  GLU S 817      34.167   9.308  31.788  1.00 43.81           C  
ATOM   2825  CG  GLU S 817      35.463  10.077  31.989  1.00 44.98           C  
ATOM   2826  CD  GLU S 817      35.337  11.569  31.688  1.00 46.95           C  
ATOM   2827  OE1 GLU S 817      34.221  12.052  31.394  1.00 48.87           O  
ATOM   2828  OE2 GLU S 817      36.362  12.277  31.748  1.00 49.02           O  
ATOM   2829  N   LEU S 818      31.536   8.470  30.231  1.00 44.93           N  
ATOM   2830  CA  LEU S 818      30.335   7.663  30.149  1.00 45.78           C  
ATOM   2831  C   LEU S 818      30.359   6.882  28.846  1.00 46.89           C  
ATOM   2832  O   LEU S 818      30.163   5.663  28.833  1.00 46.50           O  
ATOM   2833  CB  LEU S 818      29.077   8.537  30.219  1.00 45.65           C  
ATOM   2834  CG  LEU S 818      27.741   7.788  30.147  1.00 45.58           C  
ATOM   2835  CD1 LEU S 818      27.612   6.809  31.318  1.00 45.36           C  
ATOM   2836  CD2 LEU S 818      26.551   8.719  30.133  1.00 43.95           C  
ATOM   2837  N   LEU S 819      30.654   7.588  27.760  1.00 48.01           N  
ATOM   2838  CA  LEU S 819      30.607   7.014  26.420  1.00 49.24           C  
ATOM   2839  C   LEU S 819      31.559   5.829  26.247  1.00 50.32           C  
ATOM   2840  O   LEU S 819      31.169   4.777  25.731  1.00 50.11           O  
ATOM   2841  CB  LEU S 819      30.903   8.105  25.380  1.00 49.22           C  
ATOM   2842  CG  LEU S 819      30.848   7.724  23.901  1.00 49.32           C  
ATOM   2843  CD1 LEU S 819      29.495   7.178  23.497  1.00 48.73           C  
ATOM   2844  CD2 LEU S 819      31.205   8.940  23.058  1.00 49.85           C  
ATOM   2845  N   ARG S 820      32.801   6.005  26.684  1.00 51.33           N  
ATOM   2846  CA  ARG S 820      33.807   4.966  26.550  1.00 52.53           C  
ATOM   2847  C   ARG S 820      33.471   3.748  27.414  1.00 52.95           C  
ATOM   2848  O   ARG S 820      33.534   2.606  26.942  1.00 53.06           O  
ATOM   2849  CB  ARG S 820      35.185   5.529  26.898  1.00 52.91           C  
ATOM   2850  CG  ARG S 820      35.620   6.583  25.904  1.00 54.20           C  
ATOM   2851  CD  ARG S 820      37.044   7.046  26.040  1.00 55.94           C  
ATOM   2852  NE  ARG S 820      37.320   8.113  25.081  1.00 58.09           N  
ATOM   2853  CZ  ARG S 820      38.453   8.808  25.022  1.00 59.82           C  
ATOM   2854  NH1 ARG S 820      39.448   8.555  25.867  1.00 60.28           N  
ATOM   2855  NH2 ARG S 820      38.590   9.765  24.108  1.00 60.61           N  
ATOM   2856  N   ALA S 821      33.106   3.994  28.670  1.00 53.36           N  
ATOM   2857  CA  ALA S 821      32.698   2.920  29.561  1.00 53.67           C  
ATOM   2858  C   ALA S 821      31.598   2.094  28.892  1.00 54.08           C  
ATOM   2859  O   ALA S 821      31.648   0.862  28.897  1.00 54.01           O  
ATOM   2860  CB  ALA S 821      32.215   3.479  30.883  1.00 53.55           C  
ATOM   2861  N   LEU S 822      30.616   2.777  28.308  1.00 54.44           N  
ATOM   2862  CA  LEU S 822      29.516   2.110  27.622  1.00 54.93           C  
ATOM   2863  C   LEU S 822      30.007   1.342  26.398  1.00 55.41           C  
ATOM   2864  O   LEU S 822      29.557   0.230  26.143  1.00 55.60           O  
ATOM   2865  CB  LEU S 822      28.445   3.117  27.212  1.00 54.90           C  
ATOM   2866  CG  LEU S 822      27.667   3.756  28.361  1.00 54.80           C  
ATOM   2867  CD1 LEU S 822      26.531   4.601  27.801  1.00 54.39           C  
ATOM   2868  CD2 LEU S 822      27.139   2.702  29.335  1.00 54.48           C  
ATOM   2869  N   ASP S 823      30.911   1.949  25.634  1.00 55.82           N  
ATOM   2870  CA  ASP S 823      31.525   1.282  24.492  1.00 56.04           C  
ATOM   2871  C   ASP S 823      32.893   0.735  24.901  1.00 56.10           C  
ATOM   2872  O   ASP S 823      33.186  -0.451  24.731  1.00 56.09           O  
ATOM   2873  CB  ASP S 823      31.688   2.252  23.320  1.00 56.21           C  
ATOM   2874  CG  ASP S 823      31.858   1.535  21.997  1.00 56.45           C  
ATOM   2875  OD1 ASP S 823      32.245   0.351  22.028  1.00 58.65           O  
ATOM   2876  OD2 ASP S 823      31.628   2.056  20.885  1.00 56.19           O  
TER    2877      ASP S 823                                                      
HETATM 2878 FE   FE2 A1350      23.294  27.501  28.594  1.00 20.46          FE  
HETATM 2879  C1  OGA A1351      22.091  25.173  27.594  1.00 24.79           C  
HETATM 2880  C2  OGA A1351      21.066  25.829  28.202  1.00 24.27           C  
HETATM 2881  C4  OGA A1351      18.756  25.714  29.004  1.00 23.09           C  
HETATM 2882  C5  OGA A1351      17.415  25.241  28.495  1.00 23.17           C  
HETATM 2883  O1  OGA A1351      21.909  24.061  27.090  1.00 25.24           O  
HETATM 2884  O2  OGA A1351      23.219  25.658  27.531  1.00 24.40           O  
HETATM 2885  O2' OGA A1351      21.192  26.959  28.711  1.00 21.19           O  
HETATM 2886  O3  OGA A1351      16.416  25.662  29.055  1.00 23.03           O  
HETATM 2887  N1  OGA A1351      19.886  25.203  28.228  1.00 21.70           N  
HETATM 2888  O4  OGA A1351      17.332  24.475  27.537  1.00 23.98           O  
HETATM 2889  S   SO4 A1352       0.316  25.182  43.602  1.00 77.77           S  
HETATM 2890  O1  SO4 A1352       1.239  25.980  44.403  1.00 77.64           O  
HETATM 2891  O2  SO4 A1352       1.075  24.260  42.760  1.00 77.88           O  
HETATM 2892  O3  SO4 A1352      -0.525  24.416  44.514  1.00 78.38           O  
HETATM 2893  O4  SO4 A1352      -0.507  26.042  42.757  1.00 76.90           O  
HETATM 2894  S   SO4 A1353       1.990  28.487  29.834  1.00 69.20           S  
HETATM 2895  O1  SO4 A1353       3.243  29.065  30.309  1.00 68.34           O  
HETATM 2896  O2  SO4 A1353       2.236  27.438  28.847  1.00 67.90           O  
HETATM 2897  O3  SO4 A1353       1.298  27.948  31.009  1.00 70.32           O  
HETATM 2898  O4  SO4 A1353       1.162  29.517  29.203  1.00 69.63           O  
HETATM 2899  O   HOH A2001       9.466  21.720  12.039  1.00 63.79           O  
HETATM 2900  O   HOH A2002       1.367  21.270   7.724  1.00 60.01           O  
HETATM 2901  O   HOH A2003       3.426  13.325   8.811  1.00 43.04           O  
HETATM 2902  O   HOH A2004      -0.760  13.029   7.574  1.00 47.08           O  
HETATM 2903  O   HOH A2005       2.515  19.304   5.195  1.00 46.76           O  
HETATM 2904  O   HOH A2006       4.861  33.534  13.331  1.00 75.60           O  
HETATM 2905  O   HOH A2007       1.403  29.250  13.007  1.00 46.80           O  
HETATM 2906  O   HOH A2008      13.563  35.806  31.131  1.00 39.09           O  
HETATM 2907  O   HOH A2009       1.614  32.100  13.758  1.00 66.18           O  
HETATM 2908  O   HOH A2010      12.671  34.540  13.968  1.00 43.83           O  
HETATM 2909  O   HOH A2011      11.399   2.867  17.750  1.00 68.06           O  
HETATM 2910  O   HOH A2012      -1.220  30.205  22.820  1.00 80.54           O  
HETATM 2911  O   HOH A2013       6.576  36.529  29.511  1.00 43.88           O  
HETATM 2912  O   HOH A2014       3.525  32.513  31.866  1.00 65.87           O  
HETATM 2913  O   HOH A2015       5.033  37.447  27.566  1.00 54.03           O  
HETATM 2914  O   HOH A2016      10.981  35.615  30.196  1.00 36.24           O  
HETATM 2915  O   HOH A2017      12.816  42.461  26.787  1.00 37.83           O  
HETATM 2916  O   HOH A2018      13.508  37.138  13.905  1.00 50.79           O  
HETATM 2917  O   HOH A2019      11.439   7.927  15.708  1.00 63.10           O  
HETATM 2918  O   HOH A2020      16.409   3.305  16.425  1.00 59.87           O  
HETATM 2919  O   HOH A2021      14.424   4.598  17.530  1.00 54.39           O  
HETATM 2920  O   HOH A2022      15.821  30.360  12.573  1.00 43.61           O  
HETATM 2921  O   HOH A2023      13.496  22.189   7.246  1.00 57.93           O  
HETATM 2922  O   HOH A2024      17.591  29.863   7.160  1.00 49.97           O  
HETATM 2923  O   HOH A2025      14.617  26.200  13.898  1.00 48.56           O  
HETATM 2924  O   HOH A2026      20.840  23.785   3.695  1.00 38.79           O  
HETATM 2925  O   HOH A2027      27.946  19.151   9.101  1.00 43.14           O  
HETATM 2926  O   HOH A2028      23.279  21.788   0.672  1.00 62.23           O  
HETATM 2927  O   HOH A2029      27.443  22.009  43.177  1.00 68.81           O  
HETATM 2928  O   HOH A2030      27.326  30.900   5.769  1.00 84.31           O  
HETATM 2929  O   HOH A2031      16.938  35.662  41.749  1.00 51.88           O  
HETATM 2930  O   HOH A2032      36.792  29.262  21.033  1.00 42.38           O  
HETATM 2931  O   HOH A2033      26.719  37.403  13.167  1.00 60.20           O  
HETATM 2932  O   HOH A2034      29.797  37.021  10.379  1.00 60.24           O  
HETATM 2933  O   HOH A2035      28.365  37.713  15.023  1.00 68.08           O  
HETATM 2934  O   HOH A2036      27.471  34.815   9.298  1.00 63.90           O  
HETATM 2935  O   HOH A2037      24.262  32.919  12.792  1.00 45.02           O  
HETATM 2936  O   HOH A2038      19.704  17.909  13.178  1.00 28.78           O  
HETATM 2937  O   HOH A2039      22.022  12.870   8.792  1.00 48.37           O  
HETATM 2938  O   HOH A2040      18.151  14.971  12.982  1.00 36.76           O  
HETATM 2939  O   HOH A2041      29.160   5.439  16.977  1.00 44.05           O  
HETATM 2940  O   HOH A2042      18.863  14.590  16.204  1.00 30.84           O  
HETATM 2941  O   HOH A2043      12.149   5.293  13.385  1.00 72.13           O  
HETATM 2942  O   HOH A2044      15.651   2.782  13.845  1.00 41.52           O  
HETATM 2943  O   HOH A2045      14.014   7.467  18.234  1.00 52.22           O  
HETATM 2944  O   HOH A2046      40.791  21.415  26.920  1.00 58.98           O  
HETATM 2945  O   HOH A2047       5.548  12.548  27.846  1.00 38.03           O  
HETATM 2946  O   HOH A2048      12.742   5.782  36.187  1.00 51.07           O  
HETATM 2947  O   HOH A2049      19.063   6.567  36.600  1.00 49.16           O  
HETATM 2948  O   HOH A2050       7.710  14.276  19.473  1.00 48.41           O  
HETATM 2949  O   HOH A2051      19.545   2.633  38.104  1.00 67.28           O  
HETATM 2950  O   HOH A2052      15.732   7.234  38.833  1.00 54.12           O  
HETATM 2951  O   HOH A2053      21.932  13.291  44.351  1.00 62.49           O  
HETATM 2952  O   HOH A2054      33.998  44.086  25.334  1.00 53.56           O  
HETATM 2953  O   HOH A2055      12.673  21.178  43.612  1.00 63.01           O  
HETATM 2954  O   HOH A2056       8.172  26.738  44.107  1.00 61.46           O  
HETATM 2955  O   HOH A2057       9.613  30.854  42.520  1.00 54.56           O  
HETATM 2956  O   HOH A2058      15.688  37.473  35.304  1.00 47.58           O  
HETATM 2957  O   HOH A2059       7.422  43.868  25.982  1.00 75.57           O  
HETATM 2958  O   HOH A2060       7.978  38.223  34.865  1.00 59.51           O  
HETATM 2959  O   HOH A2061      17.035  27.760  38.288  1.00 52.22           O  
HETATM 2960  O   HOH A2062      16.338  30.836  40.223  1.00 38.80           O  
HETATM 2961  O   HOH A2063      22.131  25.023  41.390  1.00 55.16           O  
HETATM 2962  O   HOH A2064      31.794  27.570  41.962  1.00 48.59           O  
HETATM 2963  O   HOH A2065      29.869  29.910  39.122  1.00 47.28           O  
HETATM 2964  O   HOH A2066      28.353  24.399  41.766  1.00 60.35           O  
HETATM 2965  O   HOH A2067      24.838  24.783  42.190  1.00 52.90           O  
HETATM 2966  O   HOH A2068      28.058  28.695  48.927  1.00 65.95           O  
HETATM 2967  O   HOH A2069      11.541  32.183  15.082  1.00 63.99           O  
HETATM 2968  O   HOH A2070      31.599  33.767  45.823  1.00 44.28           O  
HETATM 2969  O   HOH A2071      24.728  38.721  49.282  1.00 48.25           O  
HETATM 2970  O   HOH A2072      17.845  37.716  46.244  1.00 57.93           O  
HETATM 2971  O   HOH A2073      16.271  36.399  44.087  1.00 58.46           O  
HETATM 2972  O   HOH A2074      16.480  33.117  41.520  1.00 59.15           O  
HETATM 2973  O   HOH A2075      21.842  17.819  48.106  1.00 67.11           O  
HETATM 2974  O   HOH A2076       8.791  17.468  46.626  1.00 63.28           O  
HETATM 2975  O   HOH A2077      21.626  14.804  40.702  1.00 53.91           O  
HETATM 2976  O   HOH A2078      17.141  16.914  47.607  1.00 52.87           O  
HETATM 2977  O   HOH A2079      39.117  50.091  47.735  1.00 57.17           O  
HETATM 2978  O   HOH A2080      10.617  19.257  44.587  1.00 69.00           O  
HETATM 2979  O   HOH A2081       1.682  24.435  36.842  1.00 55.40           O  
HETATM 2980  O   HOH A2082       4.627  30.781  36.487  1.00 53.38           O  
HETATM 2981  O   HOH A2083      18.429  25.785  36.464  1.00 54.65           O  
HETATM 2982  O   HOH A2084      17.463  26.906  33.818  1.00 38.64           O  
HETATM 2983  O   HOH A2085      23.466  17.336  36.578  1.00 41.94           O  
HETATM 2984  O   HOH A2086      26.890  12.949  30.365  1.00 49.34           O  
HETATM 2985  O   HOH A2087      21.694  10.405  34.333  1.00 45.95           O  
HETATM 2986  O   HOH A2088      20.030   9.589  36.847  1.00 52.33           O  
HETATM 2987  O   HOH A2089      18.447  -1.706  32.981  1.00 66.29           O  
HETATM 2988  O   HOH A2090      16.300  -0.205  30.017  1.00 50.70           O  
HETATM 2989  O   HOH A2091      17.950   1.645  20.589  1.00 51.55           O  
HETATM 2990  O   HOH A2092      26.301   5.439  16.918  1.00 36.67           O  
HETATM 2991  O   HOH A2093      33.944  10.218  13.383  1.00 51.60           O  
HETATM 2992  O   HOH A2094      30.893  16.371  11.174  1.00 40.00           O  
HETATM 2993  O   HOH A2095      32.606  13.689  20.709  1.00 45.01           O  
HETATM 2994  O   HOH A2096      36.957  10.422   7.614  1.00 76.91           O  
HETATM 2995  O   HOH A2097      31.860  10.158   7.765  1.00 58.55           O  
HETATM 2996  O   HOH A2098      35.951  16.836  31.735  1.00 59.28           O  
HETATM 2997  O   HOH A2099      39.867  18.412  27.150  1.00 50.38           O  
HETATM 2998  O   HOH A2100      13.436  20.952  28.355  1.00 27.89           O  
HETATM 2999  O   HOH A2101       3.992  21.265  30.540  1.00 43.76           O  
HETATM 3000  O   HOH A2102      30.735  37.910  33.103  1.00 30.45           O  
HETATM 3001  O   HOH A2103      25.986  26.303  26.047  1.00 26.08           O  
HETATM 3002  O   HOH A2104      35.845  25.360  27.653  1.00 33.53           O  
HETATM 3003  O   HOH A2105      36.837  32.025  33.001  1.00 37.86           O  
HETATM 3004  O   HOH A2106      31.874  20.474  33.040  1.00 55.47           O  
HETATM 3005  O   HOH A2107      36.793  26.619  20.918  1.00 34.57           O  
HETATM 3006  O   HOH A2108      17.114  16.909  17.862  1.00 35.83           O  
HETATM 3007  O   HOH A2109       9.968  13.510  19.464  1.00 37.10           O  
HETATM 3008  O   HOH A2110       5.274  16.717  22.023  1.00 44.26           O  
HETATM 3009  O   HOH A2111       7.041  16.862  20.149  1.00 37.71           O  
HETATM 3010  O   HOH A2112       6.517  22.763  22.963  1.00 38.94           O  
HETATM 3011  O   HOH A2113      32.253  43.121  24.229  1.00 53.95           O  
HETATM 3012  O   HOH A2114      29.471  38.812  26.249  1.00 22.19           O  
HETATM 3013  O   HOH A2115      30.645  39.042  18.925  1.00 33.21           O  
HETATM 3014  O   HOH A2116      28.797  40.227  16.136  1.00 64.15           O  
HETATM 3015  O   HOH A2117      25.466  42.302  17.883  1.00 64.00           O  
HETATM 3016  O   HOH A2118      27.698  44.486  31.068  1.00 26.13           O  
HETATM 3017  O   HOH A2119      27.635  48.525  29.776  1.00 35.59           O  
HETATM 3018  O   HOH A2120      30.274  44.879  25.031  1.00 38.32           O  
HETATM 3019  O   HOH A2121      25.933  50.527  30.463  1.00 35.79           O  
HETATM 3020  O   HOH A2122      26.614  31.094  38.158  1.00 32.11           O  
HETATM 3021  O   HOH A2123      29.486  36.934  35.226  1.00 27.40           O  
HETATM 3022  O   HOH A2124      30.510  30.229  36.300  1.00 31.99           O  
HETATM 3023  O   HOH A2125      19.859  31.575  33.786  1.00 31.77           O  
HETATM 3024  O   HOH A2126      19.538  36.155  33.217  1.00 30.91           O  
HETATM 3025  O   HOH A2127      18.490  38.301  36.415  1.00 43.54           O  
HETATM 3026  O   HOH A2128      21.227  42.704  39.938  1.00 38.88           O  
HETATM 3027  O   HOH A2129      25.386  44.358  40.124  1.00 54.33           O  
HETATM 3028  O   HOH A2130      17.603  37.763  31.961  1.00 35.39           O  
HETATM 3029  O   HOH A2131       9.290  41.007  35.589  1.00 51.53           O  
HETATM 3030  O   HOH A2132      15.089  37.816  32.481  1.00 32.05           O  
HETATM 3031  O   HOH A2133       9.348  43.374  27.752  1.00 61.17           O  
HETATM 3032  O   HOH A2134      10.824  48.278  31.295  1.00 52.52           O  
HETATM 3033  O   HOH A2135      15.962  46.870  38.981  1.00 51.42           O  
HETATM 3034  O   HOH A2136      15.691  44.668  34.824  1.00 31.47           O  
HETATM 3035  O   HOH A2137      14.202  48.658  24.558  1.00 43.59           O  
HETATM 3036  O   HOH A2138      13.481  51.613  32.894  1.00 45.77           O  
HETATM 3037  O   HOH A2139      16.193  44.497  37.574  1.00 58.87           O  
HETATM 3038  O   HOH A2140      15.573  46.265  24.419  1.00 39.51           O  
HETATM 3039  O   HOH A2141      15.284  50.258  22.000  1.00 32.96           O  
HETATM 3040  O   HOH A2142      14.817  55.477  27.388  1.00 52.87           O  
HETATM 3041  O   HOH A2143      18.684  55.873  28.304  1.00 58.28           O  
HETATM 3042  O   HOH A2144      23.651  46.151  19.718  1.00 33.04           O  
HETATM 3043  O   HOH A2145      16.751  46.565  21.800  1.00 33.97           O  
HETATM 3044  O   HOH A2146      12.595  29.171  13.536  1.00 39.79           O  
HETATM 3045  O   HOH A2147      10.812  19.188  14.084  1.00 50.88           O  
HETATM 3046  O   HOH A2148      14.521  18.471  12.156  1.00 37.16           O  
HETATM 3047  O   HOH A2149      11.495  21.508  13.792  1.00 44.23           O  
HETATM 3048  O   HOH A2150      33.566  26.082  16.801  1.00 38.34           O  
HETATM 3049  O   HOH A2151      27.798  27.494  24.390  1.00 25.11           O  
HETATM 3050  O   HOH A2152      30.253  36.176  26.688  1.00 27.79           O  
HETATM 3051  O   HOH A2153      27.363  30.094  25.612  1.00 23.74           O  
HETATM 3052  O   HOH A2154      32.762  34.069  19.065  1.00 47.61           O  
HETATM 3053  O   HOH A2155      16.282  36.168  29.566  1.00 33.13           O  
HETATM 3054  O   HOH A2156      13.289  26.522  28.472  1.00 47.17           O  
HETATM 3055  O   HOH A2157       7.556  30.888  24.716  1.00 44.35           O  
HETATM 3056  O   HOH A2158       7.790  30.392  27.265  1.00 37.71           O  
HETATM 3057  O   HOH A2159       3.910  21.360  21.198  1.00 60.23           O  
HETATM 3058  O   HOH A2160       6.411  23.837  25.422  1.00 40.51           O  
HETATM 3059  O   HOH A2161       5.352  18.754  24.064  1.00 42.17           O  
HETATM 3060  O   HOH A2162       3.001  17.561  27.759  1.00 55.61           O  
HETATM 3061  O   HOH A2163      40.897  21.985  24.633  1.00 54.83           O  
HETATM 3062  O   HOH A2164      42.626  37.977  17.732  1.00 71.69           O  
HETATM 3063  O   HOH A2165      42.463  44.114  19.559  1.00 54.59           O  
HETATM 3064  O   HOH A2166      33.754  36.855  19.984  1.00 36.17           O  
HETATM 3065  O   HOH A2167      33.194  39.271  33.406  1.00 28.26           O  
HETATM 3066  O   HOH A2168      38.789  34.566  42.752  1.00 40.46           O  
HETATM 3067  O   HOH A2169      37.482  29.751  37.743  1.00 57.74           O  
HETATM 3068  O   HOH A2170      32.020  40.390  44.008  1.00 38.46           O  
HETATM 3069  O   HOH A2171      31.865  44.151  45.174  1.00 45.64           O  
HETATM 3070  O   HOH A2172      38.498  47.344  48.085  1.00 60.19           O  
HETATM 3071  O   HOH A2173      41.427  43.475  51.164  1.00 50.64           O  
HETATM 3072  O   HOH A2174      35.239  52.784  45.826  1.00 54.63           O  
HETATM 3073  O   HOH A2175      32.343  51.933  45.286  1.00 58.03           O  
HETATM 3074  O   HOH A2176      39.267  57.239  41.745  1.00 26.45           O  
HETATM 3075  O   HOH A2177      32.755  59.287  44.804  1.00 60.46           O  
HETATM 3076  O   HOH A2178      37.840  55.111  29.241  1.00 44.20           O  
HETATM 3077  O   HOH A2179      46.839  53.182  31.757  1.00 31.38           O  
HETATM 3078  O   HOH S2001      35.955  31.618  40.285  1.00 80.01           O  
HETATM 3079  O   HOH S2002      38.513  33.804  31.613  1.00 33.04           O  
HETATM 3080  O   HOH S2003      38.106  25.337  29.179  1.00 54.79           O  
HETATM 3081  O   HOH S2004      36.648  25.786  38.779  1.00 76.96           O  
HETATM 3082  O   HOH S2005      30.766  25.787  37.613  1.00 54.75           O  
HETATM 3083  O   HOH S2006      33.667  28.867  40.196  1.00 59.66           O  
HETATM 3084  O   HOH S2007      33.934  31.237  38.711  1.00 40.66           O  
HETATM 3085  O   HOH S2008      34.990  30.561  34.967  1.00 30.13           O  
HETATM 3086  O   HOH S2009      28.622  27.043  37.556  1.00 57.58           O  
HETATM 3087  O   HOH S2010      19.894  26.655  33.706  1.00 54.88           O  
HETATM 3088  O   HOH S2011      30.052  24.213  35.628  1.00 41.23           O  
HETATM 3089  O   HOH S2012      28.737  12.960  37.083  1.00 59.80           O  
HETATM 3090  O   HOH S2013      35.568  13.822  23.888  1.00 38.00           O  
HETATM 3091  O   HOH S2014      32.110   2.136  17.673  1.00 69.92           O  
HETATM 3092  O   HOH S2015      30.722  -1.323  21.296  1.00 48.92           O  
CONECT 1478 2878                                                                
CONECT 1498 2878                                                                
CONECT 2167 2878                                                                
CONECT 2878 1478 1498 2167 2884                                                 
CONECT 2878 2885                                                                
CONECT 2879 2880 2883 2884                                                      
CONECT 2880 2879 2885 2887                                                      
CONECT 2881 2882 2887                                                           
CONECT 2882 2881 2886 2888                                                      
CONECT 2883 2879                                                                
CONECT 2884 2878 2879                                                           
CONECT 2885 2878 2880                                                           
CONECT 2886 2882                                                                
CONECT 2887 2880 2881                                                           
CONECT 2888 2882                                                                
CONECT 2889 2890 2891 2892 2893                                                 
CONECT 2890 2889                                                                
CONECT 2891 2889                                                                
CONECT 2892 2889                                                                
CONECT 2893 2889                                                                
CONECT 2894 2895 2896 2897 2898                                                 
CONECT 2895 2894                                                                
CONECT 2896 2894                                                                
CONECT 2897 2894                                                                
CONECT 2898 2894                                                                
MASTER      440    0    4   15   20    0    7    6 3090    2   25   31          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.