CNRS Nantes University UFIP UFIP
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***  5JWP  ***

elNémo ID: 21051011104331631

Job options:

ID        	=	 21051011104331631
JOBID     	=	 5JWP
USERID    	=	 100428706
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 5JWP

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



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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.