CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 210617114827105669

Job options:

ID        	=	 210617114827105669
JOBID     	=	 
USERID    	=	 HSA
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:


ATOM      1  N   HIS A   3      22.804  29.493  13.350  1.00115.31           N  
ANISOU    1  N   HIS A   3    18486  12114  13212   1578  -2751  -1165       N  
ATOM      2  CA  HIS A   3      22.625  29.884  11.922  1.00114.42           C  
ANISOU    2  CA  HIS A   3    18748  11776  12951   1711  -2955  -1186       C  
ATOM      3  C   HIS A   3      22.410  28.626  11.068  1.00113.83           C  
ANISOU    3  C   HIS A   3    18663  11696  12890   1736  -2929  -1193       C  
ATOM      4  O   HIS A   3      21.737  27.667  11.497  1.00121.89           O  
ANISOU    4  O   HIS A   3    19380  12856  14078   1740  -2894  -1302       O  
ATOM      5  CB  HIS A   3      23.855  30.667  11.443  1.00114.63           C  
ANISOU    5  CB  HIS A   3    19121  11670  12763   1618  -2872   -980       C  
ATOM      6  N   LYS A   4      22.950  28.651   9.851  1.00105.77           N  
ANISOU    6  N   LYS A   4    17988  10511  11690   1747  -2948  -1087       N  
ATOM      7  CA  LYS A   4      23.158  27.452   9.050  1.00 97.77           C  
ANISOU    7  CA  LYS A   4    16996   9499  10654   1722  -2852  -1029       C  
ATOM      8  C   LYS A   4      24.543  26.853   9.357  1.00 88.40           C  
ANISOU    8  C   LYS A   4    15749   8415   9424   1517  -2524   -805       C  
ATOM      9  O   LYS A   4      24.781  25.677   9.085  1.00 86.68           O  
ANISOU    9  O   LYS A   4    15432   8261   9243   1468  -2393   -757       O  
ATOM     10  CB  LYS A   4      23.034  27.791   7.557  1.00100.51           C  
ANISOU   10  CB  LYS A   4    17760   9612  10817   1835  -3040  -1040       C  
ATOM     11  CG  LYS A   4      21.745  28.518   7.167  1.00102.35           C  
ANISOU   11  CG  LYS A   4    18108   9707  11074   2059  -3403  -1265       C  
ATOM     12  CD  LYS A   4      21.873  29.217   5.819  1.00103.29           C  
ANISOU   12  CD  LYS A   4    18729   9560  10956   2144  -3591  -1232       C  
ATOM     13  N   SER A   5      25.442  27.652   9.936  1.00 79.83           N  
ANISOU   13  N   SER A   5    14714   7346   8271   1402  -2404   -682       N  
ATOM     14  CA  SER A   5      26.837  27.243  10.155  1.00 73.62           C  
ANISOU   14  CA  SER A   5    13900   6639   7434   1216  -2113   -486       C  
ATOM     15  C   SER A   5      27.311  27.561  11.579  1.00 67.75           C  
ANISOU   15  C   SER A   5    12909   6048   6784   1104  -1973   -431       C  
ATOM     16  O   SER A   5      27.612  28.699  11.887  1.00 73.38           O  
ANISOU   16  O   SER A   5    13741   6713   7428   1080  -2002   -403       O  
ATOM     17  CB  SER A   5      27.741  27.942   9.140  1.00 71.62           C  
ANISOU   17  CB  SER A   5    14045   6218   6950   1161  -2081   -370       C  
ATOM     18  OG  SER A   5      29.107  27.686   9.385  1.00 70.06           O  
ANISOU   18  OG  SER A   5    13809   6100   6711    980  -1804   -208       O  
ATOM     19  N   GLU A   6      27.388  26.551  12.433  1.00 62.49           N  
ANISOU   19  N   GLU A   6    11920   5558   6266   1033  -1826   -414       N  
ATOM     20  CA  GLU A   6      27.788  26.744  13.818  1.00 60.97           C  
ANISOU   20  CA  GLU A   6    11491   5512   6163    927  -1700   -366       C  
ATOM     21  C   GLU A   6      29.117  27.517  13.915  1.00 58.13           C  
ANISOU   21  C   GLU A   6    11280   5125   5683    805  -1558   -212       C  
ATOM     22  O   GLU A   6      29.204  28.480  14.652  1.00 58.45           O  
ANISOU   22  O   GLU A   6    11304   5182   5723    781  -1579   -212       O  
ATOM     23  CB  GLU A   6      27.874  25.414  14.563  1.00 60.81           C  
ANISOU   23  CB  GLU A   6    11166   5656   6282    849  -1547   -340       C  
ATOM     24  CG  GLU A   6      27.906  25.532  16.081  1.00 63.95           C  
ANISOU   24  CG  GLU A   6    11302   6207   6790    764  -1466   -337       C  
ATOM     25  CD  GLU A   6      28.200  24.209  16.817  1.00 67.50           C  
ANISOU   25  CD  GLU A   6    11503   6797   7346    663  -1303   -279       C  
ATOM     26  OE1 GLU A   6      28.271  23.134  16.137  1.00 67.71           O  
ANISOU   26  OE1 GLU A   6    11540   6806   7379    672  -1264   -257       O  
ATOM     27  OE2 GLU A   6      28.365  24.253  18.075  1.00 71.77           O1-
ANISOU   27  OE2 GLU A   6    11856   7457   7956    576  -1222   -255       O1-
ATOM     28  N   ILE A   7      30.124  27.157  13.138  1.00 55.15           N  
ANISOU   28  N   ILE A   7    11053   4700   5201    729  -1419    -96       N  
ATOM     29  CA  ILE A   7      31.399  27.831  13.273  1.00 53.17           C  
ANISOU   29  CA  ILE A   7    10910   4439   4852    596  -1265     29       C  
ATOM     30  C   ILE A   7      31.250  29.313  12.876  1.00 55.99           C  
ANISOU   30  C   ILE A   7    11566   4641   5067    631  -1405      8       C  
ATOM     31  O   ILE A   7      31.836  30.193  13.524  1.00 54.09           O  
ANISOU   31  O   ILE A   7    11335   4418   4800    549  -1347     61       O  
ATOM     32  CB  ILE A   7      32.545  27.111  12.509  1.00 50.92           C  
ANISOU   32  CB  ILE A   7    10707   4148   4492    496  -1071    132       C  
ATOM     33  CG1 ILE A   7      33.919  27.557  13.020  1.00 50.49           C  
ANISOU   33  CG1 ILE A   7    10632   4150   4403    337   -871    241       C  
ATOM     34  CG2 ILE A   7      32.446  27.338  11.040  1.00 51.96           C  
ANISOU   34  CG2 ILE A   7    11183   4105   4455    540  -1145    119       C  
ATOM     35  CD1 ILE A   7      35.077  27.009  12.211  1.00 49.69           C  
ANISOU   35  CD1 ILE A   7    10621   4036   4221    233   -680    312       C  
ATOM     36  N   ALA A   8      30.445  29.592  11.851  1.00 57.82           N  
ANISOU   36  N   ALA A   8    12044   4714   5210    757  -1603    -73       N  
ATOM     37  CA  ALA A   8      30.183  30.976  11.459  1.00 60.39           C  
ANISOU   37  CA  ALA A   8    12679   4867   5398    810  -1778   -105       C  
ATOM     38  C   ALA A   8      29.567  31.793  12.597  1.00 61.57           C  
ANISOU   38  C   ALA A   8    12668   5072   5652    865  -1898   -187       C  
ATOM     39  O   ALA A   8      29.995  32.935  12.869  1.00 60.74           O  
ANISOU   39  O   ALA A   8    12709   4905   5464    814  -1909   -146       O  
ATOM     40  CB  ALA A   8      29.277  31.029  10.233  1.00 58.89           C  
ANISOU   40  CB  ALA A   8    12762   4498   5116    964  -2011   -201       C  
ATOM     41  N   HIS A   9      28.533  31.229  13.214  1.00 64.46           N  
ANISOU   41  N   HIS A   9    12749   5547   6195    964  -1992   -315       N  
ATOM     42  CA  HIS A   9      27.818  31.910  14.292  1.00 69.51           C  
ANISOU   42  CA  HIS A   9    13208   6254   6948   1022  -2107   -426       C  
ATOM     43  C   HIS A   9      28.806  32.240  15.391  1.00 66.04           C  
ANISOU   43  C   HIS A   9    12626   5934   6530    865  -1909   -308       C  
ATOM     44  O   HIS A   9      28.872  33.369  15.852  1.00 68.68           O  
ANISOU   44  O   HIS A   9    13034   6230   6832    863  -1973   -318       O  
ATOM     45  CB  HIS A   9      26.673  31.033  14.828  1.00 77.02           C  
ANISOU   45  CB  HIS A   9    13835   7337   8092   1108  -2174   -581       C  
ATOM     46  CG  HIS A   9      25.806  31.714  15.849  1.00 86.64           C  
ANISOU   46  CG  HIS A   9    14866   8624   9429   1174  -2302   -734       C  
ATOM     47  CD2 HIS A   9      26.070  32.130  17.112  1.00 95.55           C  
ANISOU   47  CD2 HIS A   9    15799   9878  10626   1088  -2208   -716       C  
ATOM     48  ND1 HIS A   9      24.493  32.063  15.603  1.00 97.05           N  
ANISOU   48  ND1 HIS A   9    16185   9879  10810   1353  -2564   -952       N  
ATOM     49  CE1 HIS A   9      23.985  32.659  16.668  1.00 97.27           C  
ANISOU   49  CE1 HIS A   9    16017   9998  10943   1370  -2617  -1067       C  
ATOM     50  NE2 HIS A   9      24.922  32.715  17.599  1.00 98.51           N  
ANISOU   50  NE2 HIS A   9    16060  10269  11100   1208  -2402   -921       N  
ATOM     51  N   ARG A  10      29.619  31.276  15.778  1.00 62.07           N  
ANISOU   51  N   ARG A  10    11938   5566   6079    739  -1677   -198       N  
ATOM     52  CA  ARG A  10      30.561  31.506  16.851  1.00 63.19           C  
ANISOU   52  CA  ARG A  10    11930   5827   6254    598  -1499    -96       C  
ATOM     53  C   ARG A  10      31.500  32.644  16.551  1.00 63.22           C  
ANISOU   53  C   ARG A  10    12196   5721   6105    518  -1457     -2       C  
ATOM     54  O   ARG A  10      31.755  33.491  17.413  1.00 66.85           O  
ANISOU   54  O   ARG A  10    12607   6216   6578    470  -1446     11       O  
ATOM     55  CB  ARG A  10      31.391  30.256  17.158  1.00 62.38           C  
ANISOU   55  CB  ARG A  10    11627   5858   6216    484  -1275      7       C  
ATOM     56  CG  ARG A  10      30.607  29.030  17.585  1.00 61.51           C  
ANISOU   56  CG  ARG A  10    11252   5866   6254    526  -1281    -64       C  
ATOM     57  CD  ARG A  10      29.588  29.272  18.690  1.00 62.56           C  
ANISOU   57  CD  ARG A  10    11166   6094   6510    571  -1378   -188       C  
ATOM     58  NE  ARG A  10      28.759  28.080  18.824  1.00 61.95           N  
ANISOU   58  NE  ARG A  10    10889   6099   6549    605  -1389   -272       N  
ATOM     59  CZ  ARG A  10      27.451  28.068  19.046  1.00 62.67           C  
ANISOU   59  CZ  ARG A  10    10864   6216   6731    698  -1533   -447       C  
ATOM     60  NH1 ARG A  10      26.765  29.183  19.227  1.00 63.74           N1+
ANISOU   60  NH1 ARG A  10    11042   6309   6867    783  -1694   -569       N1+
ATOM     61  NH2 ARG A  10      26.819  26.908  19.094  1.00 66.08           N  
ANISOU   61  NH2 ARG A  10    11130   6720   7259    703  -1516   -512       N  
ATOM     62  N   PHE A  11      32.025  32.661  15.343  1.00 64.12           N  
ANISOU   62  N   PHE A  11    12592   5701   6069    490  -1425     60       N  
ATOM     63  CA  PHE A  11      32.953  33.697  14.947  1.00 66.99           C  
ANISOU   63  CA  PHE A  11    13237   5950   6267    386  -1365    147       C  
ATOM     64  C   PHE A  11      32.268  35.061  14.965  1.00 69.23           C  
ANISOU   64  C   PHE A  11    13727   6094   6483    477  -1591     72       C  
ATOM     65  O   PHE A  11      32.828  36.023  15.466  1.00 66.57           O  
ANISOU   65  O   PHE A  11    13453   5741   6100    395  -1552    119       O  
ATOM     66  CB  PHE A  11      33.516  33.407  13.563  1.00 68.44           C  
ANISOU   66  CB  PHE A  11    13706   6010   6290    336  -1293    206       C  
ATOM     67  CG  PHE A  11      34.717  34.240  13.222  1.00 70.41           C  
ANISOU   67  CG  PHE A  11    14199   6177   6375    170  -1148    305       C  
ATOM     68  CD1 PHE A  11      35.991  33.763  13.471  1.00 69.70           C  
ANISOU   68  CD1 PHE A  11    13971   6205   6306      4   -880    393       C  
ATOM     69  CD2 PHE A  11      34.577  35.500  12.674  1.00 71.15           C  
ANISOU   69  CD2 PHE A  11    14661   6076   6297    177  -1282    300       C  
ATOM     70  CE1 PHE A  11      37.105  34.519  13.164  1.00 71.00           C  
ANISOU   70  CE1 PHE A  11    14342   6306   6329   -165   -730    464       C  
ATOM     71  CE2 PHE A  11      35.692  36.256  12.359  1.00 72.53           C  
ANISOU   71  CE2 PHE A  11    15071   6174   6313      0  -1132    388       C  
ATOM     72  CZ  PHE A  11      36.959  35.770  12.601  1.00 71.17           C  
ANISOU   72  CZ  PHE A  11    14740   6134   6169   -178   -846    465       C  
ATOM     73  N   LYS A  12      31.047  35.132  14.436  1.00 73.75           N  
ANISOU   73  N   LYS A  12    14398   6564   7059    653  -1838    -54       N  
ATOM     74  CA  LYS A  12      30.287  36.387  14.481  1.00 77.44           C  
ANISOU   74  CA  LYS A  12    15046   6896   7483    770  -2091   -154       C  
ATOM     75  C   LYS A  12      30.064  36.860  15.909  1.00 72.56           C  
ANISOU   75  C   LYS A  12    14147   6416   7009    770  -2098   -206       C  
ATOM     76  O   LYS A  12      30.440  37.959  16.222  1.00 75.16           O  
ANISOU   76  O   LYS A  12    14610   6680   7268    725  -2122   -175       O  
ATOM     77  CB  LYS A  12      28.950  36.290  13.735  1.00 80.98           C  
ANISOU   77  CB  LYS A  12    15601   7225   7942    981  -2375   -313       C  
ATOM     78  CG  LYS A  12      29.108  36.464  12.234  1.00 88.45           C  
ANISOU   78  CG  LYS A  12    16983   7946   8677   1000  -2457   -271       C  
ATOM     79  CD  LYS A  12      27.761  36.361  11.525  1.00 95.27           C  
ANISOU   79  CD  LYS A  12    17946   8691   9563   1225  -2762   -441       C  
ATOM     80  CE  LYS A  12      27.906  36.355  10.015  1.00 97.22           C  
ANISOU   80  CE  LYS A  12    18623   8721   9597   1242  -2836   -396       C  
ATOM     81  NZ  LYS A  12      27.310  35.126   9.419  1.00103.36           N1+
ANISOU   81  NZ  LYS A  12    19284   9540  10447   1332  -2864   -463       N1+
ATOM     82  N   ASP A  13      29.458  36.037  16.756  1.00 69.88           N  
ANISOU   82  N   ASP A  13    13434   6260   6858    810  -2074   -286       N  
ATOM     83  CA  ASP A  13      29.095  36.479  18.089  1.00 68.94           C  
ANISOU   83  CA  ASP A  13    13056   6269   6870    817  -2097   -361       C  
ATOM     84  C   ASP A  13      30.313  36.811  18.927  1.00 65.30           C  
ANISOU   84  C   ASP A  13    12523   5898   6392    641  -1882   -217       C  
ATOM     85  O   ASP A  13      30.265  37.760  19.675  1.00 67.11           O  
ANISOU   85  O   ASP A  13    12730   6133   6636    640  -1937   -249       O  
ATOM     86  CB  ASP A  13      28.250  35.438  18.828  1.00 74.18           C  
ANISOU   86  CB  ASP A  13    13345   7117   7725    861  -2081   -473       C  
ATOM     87  CG  ASP A  13      26.781  35.428  18.386  1.00 80.98           C  
ANISOU   87  CG  ASP A  13    14201   7915   8651   1057  -2341   -688       C  
ATOM     88  OD1 ASP A  13      26.423  36.110  17.408  1.00 86.40           O  
ANISOU   88  OD1 ASP A  13    15190   8406   9233   1175  -2547   -741       O  
ATOM     89  OD2 ASP A  13      25.971  34.713  19.014  1.00 89.57           O1-
ANISOU   89  OD2 ASP A  13    14986   9149   9897   1089  -2342   -813       O1-
ATOM     90  N   LEU A  14      31.397  36.050  18.818  1.00 61.38           N  
ANISOU   90  N   LEU A  14    11982   5469   5870    500  -1647    -72       N  
ATOM     91  CA  LEU A  14      32.538  36.215  19.741  1.00 58.31           C  
ANISOU   91  CA  LEU A  14    11462   5193   5499    339  -1442     44       C  
ATOM     92  C   LEU A  14      33.608  37.217  19.315  1.00 59.16           C  
ANISOU   92  C   LEU A  14    11849   5180   5448    227  -1371    147       C  
ATOM     93  O   LEU A  14      34.308  37.784  20.162  1.00 58.67           O  
ANISOU   93  O   LEU A  14    11708   5182   5401    126  -1275    200       O  
ATOM     94  CB  LEU A  14      33.219  34.865  19.984  1.00 55.79           C  
ANISOU   94  CB  LEU A  14    10919   5023   5257    244  -1228    129       C  
ATOM     95  CG  LEU A  14      32.370  33.836  20.740  1.00 53.89           C  
ANISOU   95  CG  LEU A  14    10362   4933   5180    300  -1245     49       C  
ATOM     96  CD1 LEU A  14      32.964  32.426  20.611  1.00 50.58           C  
ANISOU   96  CD1 LEU A  14     9808   4603   4807    231  -1075    130       C  
ATOM     97  CD2 LEU A  14      32.211  34.292  22.186  1.00 49.58           C  
ANISOU   97  CD2 LEU A  14     9597   4511   4728    269  -1241     14       C  
ATOM     98  N   GLY A  15      33.752  37.407  18.008  1.00 59.66           N  
ANISOU   98  N   GLY A  15    12242   5071   5357    233  -1410    174       N  
ATOM     99  CA  GLY A  15      34.857  38.152  17.464  1.00 60.82           C  
ANISOU   99  CA  GLY A  15    12665   5105   5337     89  -1297    277       C  
ATOM    100  C   GLY A  15      36.145  37.351  17.360  1.00 61.12           C  
ANISOU  100  C   GLY A  15    12603   5246   5375    -77  -1017    385       C  
ATOM    101  O   GLY A  15      36.415  36.457  18.141  1.00 57.67           O  
ANISOU  101  O   GLY A  15    11841   4988   5083   -106   -895    401       O  
ATOM    102  N   GLU A  16      36.970  37.714  16.386  1.00 64.96           N  
ANISOU  102  N   GLU A  16    13386   5608   5689   -196   -916    449       N  
ATOM    103  CA  GLU A  16      38.205  37.000  16.119  1.00 66.07           C  
ANISOU  103  CA  GLU A  16    13454   5831   5819   -354   -652    523       C  
ATOM    104  C   GLU A  16      39.110  36.838  17.346  1.00 63.89           C  
ANISOU  104  C   GLU A  16    12856   5742   5679   -460   -477    563       C  
ATOM    105  O   GLU A  16      39.743  35.816  17.492  1.00 65.13           O  
ANISOU  105  O   GLU A  16    12796   6027   5924   -512   -318    586       O  
ATOM    106  CB  GLU A  16      38.956  37.680  14.975  1.00 69.83           C  
ANISOU  106  CB  GLU A  16    14322   6137   6072   -492   -565    569       C  
ATOM    107  CG  GLU A  16      40.188  36.930  14.497  1.00 73.79           C  
ANISOU  107  CG  GLU A  16    14771   6713   6551   -655   -291    614       C  
ATOM    108  CD  GLU A  16      40.734  37.435  13.161  1.00 79.89           C  
ANISOU  108  CD  GLU A  16    15962   7309   7085   -789   -208    638       C  
ATOM    109  OE1 GLU A  16      41.846  36.986  12.776  1.00 85.07           O  
ANISOU  109  OE1 GLU A  16    16585   8025   7712   -951     39    657       O  
ATOM    110  OE2 GLU A  16      40.065  38.266  12.491  1.00 84.25           O1-
ANISOU  110  OE2 GLU A  16    16880   7658   7474   -736   -389    630       O1-
ATOM    111  N   GLU A  17      39.167  37.820  18.224  1.00 63.34           N  
ANISOU  111  N   GLU A  17    12757   5683   5627   -485   -520    563       N  
ATOM    112  CA  GLU A  17      40.150  37.810  19.304  1.00 64.93           C  
ANISOU  112  CA  GLU A  17    12703   6039   5931   -601   -355    602       C  
ATOM    113  C   GLU A  17      39.863  36.635  20.278  1.00 63.86           C  
ANISOU  113  C   GLU A  17    12180   6094   5992   -528   -343    588       C  
ATOM    114  O   GLU A  17      40.708  35.755  20.516  1.00 60.42           O  
ANISOU  114  O   GLU A  17    11546   5777   5636   -599   -179    620       O  
ATOM    115  CB  GLU A  17      40.085  39.154  20.033  1.00 70.11           C  
ANISOU  115  CB  GLU A  17    13427   6652   6560   -622   -437    597       C  
ATOM    116  CG  GLU A  17      41.343  39.576  20.763  1.00 77.10           C  
ANISOU  116  CG  GLU A  17    14198   7625   7473   -787   -256    642       C  
ATOM    117  CD  GLU A  17      41.120  40.816  21.632  1.00 82.42           C  
ANISOU  117  CD  GLU A  17    14898   8271   8145   -782   -362    629       C  
ATOM    118  OE1 GLU A  17      40.602  41.832  21.104  1.00 89.72           O  
ANISOU  118  OE1 GLU A  17    16128   9022   8941   -749   -506    610       O  
ATOM    119  OE2 GLU A  17      41.463  40.776  22.837  1.00 79.07           O1-
ANISOU  119  OE2 GLU A  17    14203   7994   7847   -809   -311    634       O1-
ATOM    120  N   HIS A  18      38.647  36.648  20.825  1.00 60.76           N  
ANISOU  120  N   HIS A  18    11693   5719   5673   -386   -525    527       N  
ATOM    121  CA  HIS A  18      38.190  35.655  21.765  1.00 55.66           C  
ANISOU  121  CA  HIS A  18    10724   5232   5191   -325   -533    504       C  
ATOM    122  C   HIS A  18      38.056  34.318  21.061  1.00 55.15           C  
ANISOU  122  C   HIS A  18    10608   5188   5157   -285   -492    505       C  
ATOM    123  O   HIS A  18      38.376  33.257  21.654  1.00 52.72           O  
ANISOU  123  O   HIS A  18    10053   5015   4964   -307   -399    528       O  
ATOM    124  CB  HIS A  18      36.843  36.078  22.368  1.00 53.80           C  
ANISOU  124  CB  HIS A  18    10432   4998   5010   -194   -734    411       C  
ATOM    125  CG  HIS A  18      36.930  37.241  23.303  1.00 54.43           C  
ANISOU  125  CG  HIS A  18    10495   5091   5095   -224   -774    400       C  
ATOM    126  CD2 HIS A  18      35.964  37.980  23.906  1.00 53.92           C  
ANISOU  126  CD2 HIS A  18    10405   5019   5063   -134   -940    310       C  
ATOM    127  ND1 HIS A  18      38.135  37.740  23.765  1.00 54.62           N  
ANISOU  127  ND1 HIS A  18    10505   5151   5099   -362   -632    475       N  
ATOM    128  CE1 HIS A  18      37.909  38.754  24.583  1.00 53.00           C  
ANISOU  128  CE1 HIS A  18    10286   4949   4904   -356   -711    444       C  
ATOM    129  NE2 HIS A  18      36.601  38.910  24.699  1.00 52.78           N  
ANISOU  129  NE2 HIS A  18    10246   4898   4909   -217   -896    343       N  
ATOM    130  N   PHE A  19      37.584  34.350  19.807  1.00 54.47           N  
ANISOU  130  N   PHE A  19    10768   4964   4965   -226   -569    479       N  
ATOM    131  CA  PHE A  19      37.500  33.104  18.999  1.00 53.62           C  
ANISOU  131  CA  PHE A  19    10640   4862   4872   -191   -527    479       C  
ATOM    132  C   PHE A  19      38.865  32.425  18.986  1.00 53.25           C  
ANISOU  132  C   PHE A  19    10487   4897   4847   -320   -304    548       C  
ATOM    133  O   PHE A  19      38.940  31.261  19.292  1.00 49.04           O  
ANISOU  133  O   PHE A  19     9740   4467   4424   -303   -251    554       O  
ATOM    134  CB  PHE A  19      37.023  33.357  17.564  1.00 53.71           C  
ANISOU  134  CB  PHE A  19    10976   4696   4737   -132   -624    451       C  
ATOM    135  CG  PHE A  19      36.781  32.103  16.776  1.00 52.79           C  
ANISOU  135  CG  PHE A  19    10832   4584   4641    -79   -605    438       C  
ATOM    136  CD1 PHE A  19      37.810  31.489  16.092  1.00 52.19           C  
ANISOU  136  CD1 PHE A  19    10796   4514   4518   -178   -425    491       C  
ATOM    137  CD2 PHE A  19      35.520  31.537  16.717  1.00 53.08           C  
ANISOU  137  CD2 PHE A  19    10797   4622   4750     67   -767    359       C  
ATOM    138  CE1 PHE A  19      37.601  30.340  15.372  1.00 50.51           C  
ANISOU  138  CE1 PHE A  19    10560   4305   4326   -128   -410    475       C  
ATOM    139  CE2 PHE A  19      35.306  30.353  16.020  1.00 52.10           C  
ANISOU  139  CE2 PHE A  19    10641   4504   4650    112   -748    346       C  
ATOM    140  CZ  PHE A  19      36.346  29.777  15.323  1.00 51.04           C  
ANISOU  140  CZ  PHE A  19    10565   4368   4462     18   -574    409       C  
ATOM    141  N   LYS A  20      39.944  33.166  18.681  1.00 54.78           N  
ANISOU  141  N   LYS A  20    10824   5046   4945   -452   -178    589       N  
ATOM    142  CA  LYS A  20      41.285  32.556  18.659  1.00 55.02           C  
ANISOU  142  CA  LYS A  20    10733   5162   5010   -575     36    624       C  
ATOM    143  C   LYS A  20      41.729  32.091  20.057  1.00 52.53           C  
ANISOU  143  C   LYS A  20    10086   5014   4861   -593     87    640       C  
ATOM    144  O   LYS A  20      42.265  31.005  20.210  1.00 52.09           O  
ANISOU  144  O   LYS A  20     9843   5050   4899   -603    176    646       O  
ATOM    145  CB  LYS A  20      42.335  33.475  18.039  1.00 57.71           C  
ANISOU  145  CB  LYS A  20    11290   5425   5213   -730    174    642       C  
ATOM    146  CG  LYS A  20      41.984  33.945  16.632  1.00 62.19           C  
ANISOU  146  CG  LYS A  20    12232   5811   5589   -734    131    634       C  
ATOM    147  CD  LYS A  20      43.078  33.713  15.597  1.00 63.51           C  
ANISOU  147  CD  LYS A  20    12531   5948   5654   -881    338    635       C  
ATOM    148  CE  LYS A  20      44.188  34.744  15.676  1.00 66.05           C  
ANISOU  148  CE  LYS A  20    12956   6250   5891  -1071    494    646       C  
ATOM    149  NZ  LYS A  20      45.159  34.614  14.556  1.00 67.95           N1+
ANISOU  149  NZ  LYS A  20    13362   6447   6007  -1232    702    626       N1+
ATOM    150  N   GLY A  21      41.506  32.901  21.074  1.00 51.35           N  
ANISOU  150  N   GLY A  21     9872   4895   4742   -592     20    643       N  
ATOM    151  CA  GLY A  21      41.800  32.471  22.442  1.00 51.14           C  
ANISOU  151  CA  GLY A  21     9555   5017   4859   -602     44    658       C  
ATOM    152  C   GLY A  21      41.144  31.126  22.789  1.00 50.31           C  
ANISOU  152  C   GLY A  21     9261   4989   4866   -509     -9    649       C  
ATOM    153  O   GLY A  21      41.818  30.150  23.110  1.00 49.98           O  
ANISOU  153  O   GLY A  21     9047   5032   4911   -534     74    668       O  
ATOM    154  N   LEU A  22      39.827  31.069  22.656  1.00 49.55           N  
ANISOU  154  N   LEU A  22     9210   4853   4764   -403   -154    608       N  
ATOM    155  CA  LEU A  22      39.073  29.887  23.027  1.00 47.56           C  
ANISOU  155  CA  LEU A  22     8791   4669   4610   -330   -208    588       C  
ATOM    156  C   LEU A  22      39.547  28.612  22.287  1.00 49.59           C  
ANISOU  156  C   LEU A  22     9019   4931   4892   -328   -125    607       C  
ATOM    157  O   LEU A  22      39.662  27.557  22.880  1.00 52.18           O  
ANISOU  157  O   LEU A  22     9165   5342   5317   -324   -102    622       O  
ATOM    158  CB  LEU A  22      37.600  30.149  22.774  1.00 46.74           C  
ANISOU  158  CB  LEU A  22     8765   4509   4487   -221   -372    513       C  
ATOM    159  CG  LEU A  22      37.046  31.143  23.777  1.00 47.34           C  
ANISOU  159  CG  LEU A  22     8792   4614   4580   -211   -459    474       C  
ATOM    160  CD1 LEU A  22      35.663  31.591  23.340  1.00 48.15           C  
ANISOU  160  CD1 LEU A  22     8998   4640   4657    -95   -633    372       C  
ATOM    161  CD2 LEU A  22      37.037  30.519  25.168  1.00 46.12           C  
ANISOU  161  CD2 LEU A  22     8380   4603   4539   -247   -426    486       C  
ATOM    162  N   VAL A  23      39.826  28.720  20.995  1.00 50.32           N  
ANISOU  162  N   VAL A  23     9304   4926   4888   -334    -84    602       N  
ATOM    163  CA  VAL A  23      40.385  27.630  20.235  1.00 49.12           C  
ANISOU  163  CA  VAL A  23     9136   4777   4751   -341      7    610       C  
ATOM    164  C   VAL A  23      41.802  27.277  20.690  1.00 49.90           C  
ANISOU  164  C   VAL A  23     9084   4961   4915   -434    156    638       C  
ATOM    165  O   VAL A  23      42.152  26.094  20.764  1.00 49.53           O  
ANISOU  165  O   VAL A  23     8895   4968   4954   -416    195    640       O  
ATOM    166  CB  VAL A  23      40.386  27.974  18.739  1.00 49.08           C  
ANISOU  166  CB  VAL A  23     9399   4644   4606   -343     24    592       C  
ATOM    167  CG1 VAL A  23      41.102  26.898  17.957  1.00 47.68           C  
ANISOU  167  CG1 VAL A  23     9197   4478   4442   -364    141    589       C  
ATOM    168  CG2 VAL A  23      38.954  28.111  18.272  1.00 48.12           C  
ANISOU  168  CG2 VAL A  23     9405   4436   4440   -225   -150    547       C  
ATOM    169  N   LEU A  24      42.635  28.279  20.963  1.00 50.64           N  
ANISOU  169  N   LEU A  24     9209   5061   4971   -529    232    650       N  
ATOM    170  CA  LEU A  24      43.984  27.999  21.484  1.00 50.70           C  
ANISOU  170  CA  LEU A  24     9049   5156   5057   -611    361    654       C  
ATOM    171  C   LEU A  24      43.842  27.171  22.757  1.00 51.08           C  
ANISOU  171  C   LEU A  24     8858   5307   5245   -563    297    675       C  
ATOM    172  O   LEU A  24      44.610  26.219  23.011  1.00 51.80           O  
ANISOU  172  O   LEU A  24     8793   5459   5429   -566    349    669       O  
ATOM    173  CB  LEU A  24      44.719  29.296  21.807  1.00 50.52           C  
ANISOU  173  CB  LEU A  24     9078   5132   4984   -719    430    658       C  
ATOM    174  CG  LEU A  24      46.111  29.225  22.443  1.00 50.52           C  
ANISOU  174  CG  LEU A  24     8897   5226   5072   -808    551    642       C  
ATOM    175  CD1 LEU A  24      46.921  28.092  21.812  1.00 50.00           C  
ANISOU  175  CD1 LEU A  24     8741   5193   5066   -814    654    599       C  
ATOM    176  CD2 LEU A  24      46.837  30.582  22.311  1.00 48.58           C  
ANISOU  176  CD2 LEU A  24     8770   4948   4740   -937    647    630       C  
ATOM    177  N   ILE A  25      42.841  27.530  23.556  1.00 48.96           N  
ANISOU  177  N   ILE A  25     8570   5050   4984   -519    180    689       N  
ATOM    178  CA  ILE A  25      42.616  26.833  24.793  1.00 49.91           C  
ANISOU  178  CA  ILE A  25     8500   5257   5208   -494    122    710       C  
ATOM    179  C   ILE A  25      42.220  25.390  24.509  1.00 50.68           C  
ANISOU  179  C   ILE A  25     8538   5356   5361   -429     92    707       C  
ATOM    180  O   ILE A  25      42.828  24.467  25.049  1.00 49.68           O  
ANISOU  180  O   ILE A  25     8273   5283   5321   -433    110    724       O  
ATOM    181  CB  ILE A  25      41.575  27.536  25.677  1.00 48.24           C  
ANISOU  181  CB  ILE A  25     8281   5062   4985   -474     17    707       C  
ATOM    182  CG1 ILE A  25      42.166  28.815  26.279  1.00 47.48           C  
ANISOU  182  CG1 ILE A  25     8196   4983   4862   -544     46    717       C  
ATOM    183  CG2 ILE A  25      41.170  26.610  26.806  1.00 48.24           C  
ANISOU  183  CG2 ILE A  25     8115   5140   5073   -458    -37    723       C  
ATOM    184  CD1 ILE A  25      41.110  29.783  26.736  1.00 47.40           C  
ANISOU  184  CD1 ILE A  25     8240   4958   4812   -518    -57    692       C  
ATOM    185  N   ALA A  26      41.214  25.211  23.652  1.00 52.36           N  
ANISOU  185  N   ALA A  26     8865   5504   5524   -367     36    682       N  
ATOM    186  CA  ALA A  26      40.713  23.883  23.299  1.00 50.98           C  
ANISOU  186  CA  ALA A  26     8651   5323   5397   -306      2    673       C  
ATOM    187  C   ALA A  26      41.880  22.991  22.942  1.00 51.45           C  
ANISOU  187  C   ALA A  26     8646   5397   5506   -321     92    681       C  
ATOM    188  O   ALA A  26      42.088  21.968  23.591  1.00 51.45           O  
ANISOU  188  O   ALA A  26     8514   5440   5593   -308     72    698       O  
ATOM    189  CB  ALA A  26      39.746  23.947  22.132  1.00 52.01           C  
ANISOU  189  CB  ALA A  26     8939   5367   5455   -240    -53    631       C  
ATOM    190  N   PHE A  27      42.678  23.391  21.962  1.00 50.04           N  
ANISOU  190  N   PHE A  27     8562   5179   5270   -356    190    659       N  
ATOM    191  CA  PHE A  27      43.820  22.570  21.584  1.00 52.14           C  
ANISOU  191  CA  PHE A  27     8749   5467   5593   -371    284    638       C  
ATOM    192  C   PHE A  27      44.775  22.367  22.729  1.00 53.13           C  
ANISOU  192  C   PHE A  27     8691   5674   5821   -404    300    648       C  
ATOM    193  O   PHE A  27      45.320  21.279  22.901  1.00 55.32           O  
ANISOU  193  O   PHE A  27     8850   5978   6191   -373    297    634       O  
ATOM    194  CB  PHE A  27      44.565  23.155  20.405  1.00 55.63           C  
ANISOU  194  CB  PHE A  27     9322   5865   5949   -432    410    597       C  
ATOM    195  CG  PHE A  27      43.894  22.908  19.082  1.00 56.69           C  
ANISOU  195  CG  PHE A  27     9633   5912   5993   -389    401    577       C  
ATOM    196  CD1 PHE A  27      43.734  21.626  18.608  1.00 58.22           C  
ANISOU  196  CD1 PHE A  27     9781   6100   6239   -322    384    558       C  
ATOM    197  CD2 PHE A  27      43.434  23.956  18.320  1.00 58.03           C  
ANISOU  197  CD2 PHE A  27    10027   5997   6023   -413    398    575       C  
ATOM    198  CE1 PHE A  27      43.113  21.394  17.387  1.00 61.98           C  
ANISOU  198  CE1 PHE A  27    10423   6495   6632   -280    370    536       C  
ATOM    199  CE2 PHE A  27      42.819  23.738  17.096  1.00 60.08           C  
ANISOU  199  CE2 PHE A  27    10468   6166   6192   -368    374    554       C  
ATOM    200  CZ  PHE A  27      42.660  22.458  16.624  1.00 61.36           C  
ANISOU  200  CZ  PHE A  27    10573   6332   6409   -302    364    533       C  
ATOM    201  N   SER A  28      44.964  23.385  23.553  1.00 53.33           N  
ANISOU  201  N   SER A  28     8695   5734   5835   -458    300    667       N  
ATOM    202  CA  SER A  28      45.830  23.194  24.712  1.00 52.24           C  
ANISOU  202  CA  SER A  28     8386   5669   5794   -481    295    674       C  
ATOM    203  C   SER A  28      45.279  22.188  25.740  1.00 49.73           C  
ANISOU  203  C   SER A  28     7970   5377   5549   -427    178    716       C  
ATOM    204  O   SER A  28      46.045  21.471  26.344  1.00 51.08           O  
ANISOU  204  O   SER A  28     8019   5580   5808   -415    158    711       O  
ATOM    205  CB  SER A  28      46.160  24.531  25.354  1.00 52.21           C  
ANISOU  205  CB  SER A  28     8386   5694   5758   -555    322    683       C  
ATOM    206  OG  SER A  28      46.772  25.396  24.416  1.00 53.64           O  
ANISOU  206  OG  SER A  28     8671   5843   5867   -625    441    644       O  
ATOM    207  N   GLN A  29      43.972  22.107  25.932  1.00 48.58           N  
ANISOU  207  N   GLN A  29     7881   5212   5365   -399     97    745       N  
ATOM    208  CA  GLN A  29      43.426  21.192  26.947  1.00 48.44           C  
ANISOU  208  CA  GLN A  29     7790   5217   5399   -378      3    781       C  
ATOM    209  C   GLN A  29      43.337  19.740  26.457  1.00 49.35           C  
ANISOU  209  C   GLN A  29     7893   5296   5561   -321    -26    776       C  
ATOM    210  O   GLN A  29      43.554  18.819  27.217  1.00 47.89           O  
ANISOU  210  O   GLN A  29     7640   5120   5437   -311    -84    800       O  
ATOM    211  CB  GLN A  29      42.067  21.666  27.452  1.00 48.01           C  
ANISOU  211  CB  GLN A  29     7778   5169   5293   -388    -60    792       C  
ATOM    212  CG  GLN A  29      42.142  22.999  28.179  1.00 48.39           C  
ANISOU  212  CG  GLN A  29     7822   5257   5308   -440    -54    797       C  
ATOM    213  CD  GLN A  29      40.810  23.514  28.679  1.00 48.16           C  
ANISOU  213  CD  GLN A  29     7819   5241   5238   -445   -116    781       C  
ATOM    214  NE2 GLN A  29      40.823  24.125  29.865  1.00 47.25           N  
ANISOU  214  NE2 GLN A  29     7648   5181   5123   -495   -136    796       N  
ATOM    215  OE1 GLN A  29      39.783  23.401  27.994  1.00 49.47           O  
ANISOU  215  OE1 GLN A  29     8050   5371   5376   -403   -149    743       O  
ATOM    216  N   TYR A  30      43.051  19.548  25.173  1.00 51.16           N  
ANISOU  216  N   TYR A  30     8205   5477   5757   -284     10    743       N  
ATOM    217  CA  TYR A  30      43.027  18.214  24.591  1.00 51.30           C  
ANISOU  217  CA  TYR A  30     8216   5456   5819   -228    -10    730       C  
ATOM    218  C   TYR A  30      44.419  17.651  24.399  1.00 51.47           C  
ANISOU  218  C   TYR A  30     8153   5487   5915   -212     35    698       C  
ATOM    219  O   TYR A  30      44.633  16.486  24.653  1.00 54.09           O  
ANISOU  219  O   TYR A  30     8429   5804   6318   -170    -22    700       O  
ATOM    220  CB  TYR A  30      42.315  18.206  23.244  1.00 52.71           C  
ANISOU  220  CB  TYR A  30     8514   5578   5935   -190     12    696       C  
ATOM    221  CG  TYR A  30      40.823  18.208  23.323  1.00 53.66           C  
ANISOU  221  CG  TYR A  30     8691   5680   6018   -172    -66    699       C  
ATOM    222  CD1 TYR A  30      40.109  17.065  23.083  1.00 56.76           C  
ANISOU  222  CD1 TYR A  30     9085   6041   6439   -130   -119    691       C  
ATOM    223  CD2 TYR A  30      40.123  19.365  23.603  1.00 54.89           C  
ANISOU  223  CD2 TYR A  30     8894   5847   6116   -196    -87    693       C  
ATOM    224  CE1 TYR A  30      38.723  17.062  23.133  1.00 58.16           C  
ANISOU  224  CE1 TYR A  30     9297   6209   6593   -120   -184    669       C  
ATOM    225  CE2 TYR A  30      38.750  19.385  23.638  1.00 54.64           C  
ANISOU  225  CE2 TYR A  30     8894   5803   6062   -173   -160    665       C  
ATOM    226  CZ  TYR A  30      38.053  18.239  23.413  1.00 55.82           C  
ANISOU  226  CZ  TYR A  30     9031   5931   6246   -139   -204    648       C  
ATOM    227  OH  TYR A  30      36.692  18.263  23.484  1.00 55.08           O  
ANISOU  227  OH  TYR A  30     8949   5837   6144   -125   -272    598       O  
ATOM    228  N   LEU A  31      45.348  18.462  23.928  1.00 52.71           N  
ANISOU  228  N   LEU A  31     8305   5664   6058   -249    137    655       N  
ATOM    229  CA  LEU A  31      46.696  17.998  23.612  1.00 56.39           C  
ANISOU  229  CA  LEU A  31     8674   6148   6602   -240    197    588       C  
ATOM    230  C   LEU A  31      47.736  18.732  24.457  1.00 56.60           C  
ANISOU  230  C   LEU A  31     8595   6235   6673   -292    227    569       C  
ATOM    231  O   LEU A  31      48.397  19.653  23.998  1.00 58.64           O  
ANISOU  231  O   LEU A  31     8864   6516   6900   -356    342    522       O  
ATOM    232  CB  LEU A  31      46.992  18.222  22.139  1.00 57.66           C  
ANISOU  232  CB  LEU A  31     8918   6284   6708   -255    320    523       C  
ATOM    233  CG  LEU A  31      46.023  17.599  21.136  1.00 59.35           C  
ANISOU  233  CG  LEU A  31     9250   6433   6868   -202    298    529       C  
ATOM    234  CD1 LEU A  31      46.513  17.968  19.727  1.00 56.91           C  
ANISOU  234  CD1 LEU A  31     9035   6099   6488   -237    434    460       C  
ATOM    235  CD2 LEU A  31      45.911  16.071  21.333  1.00 58.34           C  
ANISOU  235  CD2 LEU A  31     9047   6286   6834   -120    206    529       C  
ATOM    236  N   GLN A  32      47.912  18.266  25.681  1.00 56.83           N  
ANISOU  236  N   GLN A  32     8532   6286   6775   -269    122    602       N  
ATOM    237  CA  GLN A  32      48.604  19.033  26.702  1.00 56.55           C  
ANISOU  237  CA  GLN A  32     8413   6304   6768   -315    116    602       C  
ATOM    238  C   GLN A  32      50.125  18.916  26.635  1.00 57.03           C  
ANISOU  238  C   GLN A  32     8332   6403   6933   -311    165    499       C  
ATOM    239  O   GLN A  32      50.817  19.549  27.413  1.00 53.54           O  
ANISOU  239  O   GLN A  32     7807   6007   6527   -347    164    480       O  
ATOM    240  CB  GLN A  32      48.123  18.570  28.082  1.00 55.31           C  
ANISOU  240  CB  GLN A  32     8238   6147   6632   -296    -27    678       C  
ATOM    241  CG  GLN A  32      46.615  18.525  28.244  1.00 54.13           C  
ANISOU  241  CG  GLN A  32     8200   5970   6399   -307    -74    755       C  
ATOM    242  CD  GLN A  32      46.188  17.832  29.519  1.00 53.35           C  
ANISOU  242  CD  GLN A  32     8094   5863   6314   -305   -200    817       C  
ATOM    243  NE2 GLN A  32      46.421  18.463  30.662  1.00 56.18           N  
ANISOU  243  NE2 GLN A  32     8417   6261   6666   -350   -233    845       N  
ATOM    244  OE1 GLN A  32      45.674  16.743  29.474  1.00 51.59           O  
ANISOU  244  OE1 GLN A  32     7908   5593   6099   -271   -264    839       O  
ATOM    245  N   GLN A  33      50.636  18.080  25.739  1.00 60.78           N  
ANISOU  245  N   GLN A  33     8768   6861   7464   -263    202    418       N  
ATOM    246  CA  GLN A  33      52.069  17.874  25.603  1.00 63.60           C  
ANISOU  246  CA  GLN A  33     8968   7261   7936   -252    249    286       C  
ATOM    247  C   GLN A  33      52.627  18.511  24.343  1.00 67.09           C  
ANISOU  247  C   GLN A  33     9424   7728   8340   -329    444    187       C  
ATOM    248  O   GLN A  33      53.839  18.450  24.099  1.00 73.34           O  
ANISOU  248  O   GLN A  33    10075   8567   9224   -343    519     49       O  
ATOM    249  CB  GLN A  33      52.384  16.385  25.546  1.00 64.69           C  
ANISOU  249  CB  GLN A  33     9033   7365   8182   -139    144    236       C  
ATOM    250  CG  GLN A  33      51.992  15.559  26.760  1.00 63.89           C  
ANISOU  250  CG  GLN A  33     8935   7221   8120    -67    -57    320       C  
ATOM    251  CD  GLN A  33      52.522  14.126  26.636  1.00 66.20           C  
ANISOU  251  CD  GLN A  33     9158   7468   8528     48   -166    248       C  
ATOM    252  NE2 GLN A  33      51.630  13.156  26.361  1.00 62.20           N  
ANISOU  252  NE2 GLN A  33     8755   6888   7988     97   -238    314       N  
ATOM    253  OE1 GLN A  33      53.734  13.902  26.755  1.00 70.07           O  
ANISOU  253  OE1 GLN A  33     9496   7987   9142     95   -188    120       O  
ATOM    254  N   CYS A  34      51.765  19.092  23.513  1.00 69.63           N  
ANISOU  254  N   CYS A  34     9919   8013   8524   -382    524    244       N  
ATOM    255  CA  CYS A  34      52.224  19.696  22.256  1.00 70.71           C  
ANISOU  255  CA  CYS A  34    10120   8155   8593   -470    711    160       C  
ATOM    256  C   CYS A  34      52.753  21.085  22.554  1.00 70.87           C  
ANISOU  256  C   CYS A  34    10141   8215   8569   -591    810    144       C  
ATOM    257  O   CYS A  34      52.344  21.693  23.535  1.00 73.37           O  
ANISOU  257  O   CYS A  34    10470   8538   8868   -599    730    229       O  
ATOM    258  CB  CYS A  34      51.097  19.739  21.222  1.00 70.81           C  
ANISOU  258  CB  CYS A  34    10344   8095   8468   -470    734    224       C  
ATOM    259  SG  CYS A  34      50.907  18.192  20.307  1.00 72.21           S  
ANISOU  259  SG  CYS A  34    10516   8231   8691   -366    704    178       S  
ATOM    260  N   PRO A  35      53.672  21.590  21.724  1.00 72.96           N  
ANISOU  260  N   PRO A  35    10397   8509   8816   -696    992     27       N  
ATOM    261  CA  PRO A  35      54.248  22.918  21.964  1.00 70.84           C  
ANISOU  261  CA  PRO A  35    10137   8275   8505   -830   1101      1       C  
ATOM    262  C   PRO A  35      53.439  24.070  21.374  1.00 69.53           C  
ANISOU  262  C   PRO A  35    10230   8040   8148   -922   1164     88       C  
ATOM    263  O   PRO A  35      52.709  23.900  20.386  1.00 68.65           O  
ANISOU  263  O   PRO A  35    10298   7859   7929   -910   1182    123       O  
ATOM    264  CB  PRO A  35      55.633  22.829  21.303  1.00 71.98           C  
ANISOU  264  CB  PRO A  35    10147   8482   8721   -913   1278   -187       C  
ATOM    265  CG  PRO A  35      55.518  21.754  20.270  1.00 74.09           C  
ANISOU  265  CG  PRO A  35    10436   8723   8993   -852   1305   -241       C  
ATOM    266  CD  PRO A  35      54.269  20.938  20.540  1.00 75.03           C  
ANISOU  266  CD  PRO A  35    10634   8775   9097   -707   1115   -100       C  
ATOM    267  N   PHE A  36      53.605  25.241  21.985  1.00 67.49           N  
ANISOU  267  N   PHE A  36     9994   7796   7853  -1008   1186    115       N  
ATOM    268  CA  PHE A  36      52.801  26.414  21.696  1.00 66.33           C  
ANISOU  268  CA  PHE A  36    10090   7575   7538  -1077   1199    205       C  
ATOM    269  C   PHE A  36      52.801  26.781  20.230  1.00 69.31           C  
ANISOU  269  C   PHE A  36    10686   7883   7766  -1175   1348    169       C  
ATOM    270  O   PHE A  36      51.743  27.019  19.662  1.00 70.18           O  
ANISOU  270  O   PHE A  36    11020   7900   7745  -1147   1291    250       O  
ATOM    271  CB  PHE A  36      53.307  27.584  22.539  1.00 66.84           C  
ANISOU  271  CB  PHE A  36    10115   7676   7606  -1172   1226    205       C  
ATOM    272  CG  PHE A  36      52.553  28.863  22.338  1.00 64.70           C  
ANISOU  272  CG  PHE A  36    10092   7322   7170  -1240   1223    288       C  
ATOM    273  CD1 PHE A  36      51.263  29.001  22.795  1.00 62.41           C  
ANISOU  273  CD1 PHE A  36     9898   6983   6833  -1143   1058    402       C  
ATOM    274  CD2 PHE A  36      53.146  29.928  21.712  1.00 66.51           C  
ANISOU  274  CD2 PHE A  36    10458   7519   7293  -1404   1382    241       C  
ATOM    275  CE1 PHE A  36      50.578  30.182  22.626  1.00 63.47           C  
ANISOU  275  CE1 PHE A  36    10253   7036   6827  -1188   1033    460       C  
ATOM    276  CE2 PHE A  36      52.465  31.124  21.539  1.00 67.03           C  
ANISOU  276  CE2 PHE A  36    10774   7491   7203  -1460   1359    317       C  
ATOM    277  CZ  PHE A  36      51.180  31.249  21.994  1.00 65.29           C  
ANISOU  277  CZ  PHE A  36    10639   7220   6948  -1341   1174    423       C  
ATOM    278  N   ASP A  37      53.974  26.807  19.606  1.00 76.04           N  
ANISOU  278  N   ASP A  37    11478   8777   8636  -1292   1535     37       N  
ATOM    279  CA  ASP A  37      54.062  27.159  18.175  1.00 80.44           C  
ANISOU  279  CA  ASP A  37    12265   9267   9033  -1414   1701     -7       C  
ATOM    280  C   ASP A  37      53.180  26.292  17.281  1.00 78.93           C  
ANISOU  280  C   ASP A  37    12204   9005   8779  -1311   1639     34       C  
ATOM    281  O   ASP A  37      52.535  26.804  16.367  1.00 81.03           O  
ANISOU  281  O   ASP A  37    12755   9166   8866  -1356   1661     83       O  
ATOM    282  CB  ASP A  37      55.510  27.110  17.678  1.00 85.29           C  
ANISOU  282  CB  ASP A  37    12749   9959   9699  -1558   1926   -186       C  
ATOM    283  CG  ASP A  37      56.311  28.352  18.076  1.00 91.94           C  
ANISOU  283  CG  ASP A  37    13583  10831  10517  -1731   2049   -234       C  
ATOM    284  OD1 ASP A  37      55.788  29.186  18.845  1.00 93.99           O  
ANISOU  284  OD1 ASP A  37    13916  11057  10738  -1721   1943   -124       O  
ATOM    285  OD2 ASP A  37      57.467  28.505  17.622  1.00 97.87           O1-
ANISOU  285  OD2 ASP A  37    14251  11643  11291  -1884   2257   -393       O1-
ATOM    286  N   GLU A  38      53.128  24.991  17.550  1.00 76.21           N  
ANISOU  286  N   GLU A  38    11669   8709   8578  -1169   1547     14       N  
ATOM    287  CA  GLU A  38      52.313  24.100  16.736  1.00 76.00           C  
ANISOU  287  CA  GLU A  38    11750   8621   8508  -1069   1485     45       C  
ATOM    288  C   GLU A  38      50.836  24.378  16.973  1.00 72.28           C  
ANISOU  288  C   GLU A  38    11449   8064   7950   -976   1307    191       C  
ATOM    289  O   GLU A  38      50.053  24.353  16.044  1.00 73.58           O  
ANISOU  289  O   GLU A  38    11827   8139   7990   -955   1287    224       O  
ATOM    290  CB  GLU A  38      52.629  22.617  16.998  1.00 80.70           C  
ANISOU  290  CB  GLU A  38    12103   9279   9280   -941   1422    -16       C  
ATOM    291  CG  GLU A  38      54.083  22.192  16.755  1.00 85.85           C  
ANISOU  291  CG  GLU A  38    12551  10022  10048  -1004   1577   -194       C  
ATOM    292  CD  GLU A  38      54.599  22.531  15.359  1.00 94.45           C  
ANISOU  292  CD  GLU A  38    13787  11091  11009  -1153   1801   -298       C  
ATOM    293  OE1 GLU A  38      54.521  21.648  14.465  1.00104.80           O  
ANISOU  293  OE1 GLU A  38    15124  12383  12312  -1109   1832   -351       O  
ATOM    294  OE2 GLU A  38      55.083  23.680  15.150  1.00 93.73           O1-
ANISOU  294  OE2 GLU A  38    13798  10998  10817  -1324   1950   -328       O1-
ATOM    295  N   HIS A  39      50.449  24.659  18.213  1.00 70.08           N  
ANISOU  295  N   HIS A  39    11075   7813   7737   -922   1175    265       N  
ATOM    296  CA  HIS A  39      49.049  24.939  18.511  1.00 66.29           C  
ANISOU  296  CA  HIS A  39    10728   7268   7193   -838   1010    376       C  
ATOM    297  C   HIS A  39      48.592  26.266  17.874  1.00 65.18           C  
ANISOU  297  C   HIS A  39    10870   7029   6866   -921   1038    410       C  
ATOM    298  O   HIS A  39      47.458  26.390  17.401  1.00 63.46           O  
ANISOU  298  O   HIS A  39    10838   6723   6553   -855    934    460       O  
ATOM    299  CB  HIS A  39      48.810  24.927  20.021  1.00 66.82           C  
ANISOU  299  CB  HIS A  39    10621   7397   7370   -778    880    432       C  
ATOM    300  CG  HIS A  39      48.583  23.556  20.597  1.00 69.26           C  
ANISOU  300  CG  HIS A  39    10755   7748   7814   -658    771    443       C  
ATOM    301  CD2 HIS A  39      48.566  23.121  21.882  1.00 70.09           C  
ANISOU  301  CD2 HIS A  39    10689   7909   8032   -603    664    476       C  
ATOM    302  ND1 HIS A  39      48.246  22.464  19.826  1.00 68.95           N  
ANISOU  302  ND1 HIS A  39    10736   7677   7786   -585    753    425       N  
ATOM    303  CE1 HIS A  39      48.064  21.413  20.605  1.00 68.00           C  
ANISOU  303  CE1 HIS A  39    10464   7589   7783   -493    643    446       C  
ATOM    304  NE2 HIS A  39      48.257  21.783  21.858  1.00 67.50           N  
ANISOU  304  NE2 HIS A  39    10292   7578   7779   -506    587    478       N  
ATOM    305  N   VAL A  40      49.477  27.251  17.824  1.00 61.83           N  
ANISOU  305  N   VAL A  40    10491   6613   6389  -1066   1173    373       N  
ATOM    306  CA  VAL A  40      49.134  28.482  17.149  1.00 62.39           C  
ANISOU  306  CA  VAL A  40    10863   6572   6270  -1157   1201    403       C  
ATOM    307  C   VAL A  40      48.803  28.254  15.656  1.00 64.78           C  
ANISOU  307  C   VAL A  40    11418   6772   6426  -1171   1250    385       C  
ATOM    308  O   VAL A  40      47.900  28.916  15.112  1.00 64.39           O  
ANISOU  308  O   VAL A  40    11643   6596   6224  -1153   1161    436       O  
ATOM    309  CB  VAL A  40      50.238  29.544  17.283  1.00 62.34           C  
ANISOU  309  CB  VAL A  40    10874   6587   6224  -1337   1362    357       C  
ATOM    310  CG1 VAL A  40      49.911  30.725  16.388  1.00 62.36           C  
ANISOU  310  CG1 VAL A  40    11242   6447   6004  -1443   1397    386       C  
ATOM    311  CG2 VAL A  40      50.365  30.018  18.718  1.00 60.86           C  
ANISOU  311  CG2 VAL A  40    10504   6474   6147  -1320   1286    389       C  
ATOM    312  N   LYS A  41      49.541  27.348  15.005  1.00 64.94           N  
ANISOU  312  N   LYS A  41    11348   6838   6489  -1200   1381    303       N  
ATOM    313  CA  LYS A  41      49.330  27.068  13.588  1.00 66.83           C  
ANISOU  313  CA  LYS A  41    11817   6989   6588  -1223   1443    276       C  
ATOM    314  C   LYS A  41      47.936  26.518  13.435  1.00 68.09           C  
ANISOU  314  C   LYS A  41    12056   7080   6736  -1048   1239    345       C  
ATOM    315  O   LYS A  41      47.183  26.972  12.572  1.00 69.67           O  
ANISOU  315  O   LYS A  41    12550   7150   6770  -1041   1182    376       O  
ATOM    316  CB  LYS A  41      50.340  26.053  13.014  1.00 66.70           C  
ANISOU  316  CB  LYS A  41    11644   7052   6648  -1266   1609    159       C  
ATOM    317  CG  LYS A  41      51.724  26.582  12.658  1.00 67.22           C  
ANISOU  317  CG  LYS A  41    11695   7167   6680  -1474   1859     46       C  
ATOM    318  N   LEU A  42      47.598  25.553  14.295  1.00 68.65           N  
ANISOU  318  N   LEU A  42    11871   7231   6982   -911   1123    363       N  
ATOM    319  CA  LEU A  42      46.310  24.866  14.235  1.00 68.10           C  
ANISOU  319  CA  LEU A  42    11828   7117   6930   -751    941    411       C  
ATOM    320  C   LEU A  42      45.194  25.869  14.446  1.00 67.55           C  
ANISOU  320  C   LEU A  42    11941   6959   6766   -710    789    475       C  
ATOM    321  O   LEU A  42      44.186  25.837  13.746  1.00 69.79           O  
ANISOU  321  O   LEU A  42    12411   7145   6961   -631    679    488       O  
ATOM    322  CB  LEU A  42      46.222  23.721  15.272  1.00 68.37           C  
ANISOU  322  CB  LEU A  42    11561   7253   7164   -641    854    419       C  
ATOM    323  CG  LEU A  42      47.234  22.560  15.137  1.00 69.47           C  
ANISOU  323  CG  LEU A  42    11499   7472   7425   -642    957    344       C  
ATOM    324  CD1 LEU A  42      47.114  21.497  16.223  1.00 66.26           C  
ANISOU  324  CD1 LEU A  42    10839   7141   7198   -534    844    364       C  
ATOM    325  CD2 LEU A  42      47.104  21.885  13.779  1.00 69.60           C  
ANISOU  325  CD2 LEU A  42    11648   7429   7369   -623   1008    298       C  
ATOM    326  N   VAL A  43      45.391  26.788  15.384  1.00 68.18           N  
ANISOU  326  N   VAL A  43    11971   7070   6864   -759    778    504       N  
ATOM    327  CA  VAL A  43      44.383  27.812  15.654  1.00 66.80           C  
ANISOU  327  CA  VAL A  43    11957   6816   6609   -718    629    549       C  
ATOM    328  C   VAL A  43      44.118  28.646  14.420  1.00 66.46           C  
ANISOU  328  C   VAL A  43    12275   6618   6358   -766    632    546       C  
ATOM    329  O   VAL A  43      42.976  28.846  14.024  1.00 66.73           O  
ANISOU  329  O   VAL A  43    12481   6552   6321   -665    470    557       O  
ATOM    330  CB  VAL A  43      44.796  28.766  16.773  1.00 65.26           C  
ANISOU  330  CB  VAL A  43    11671   6673   6452   -784    639    572       C  
ATOM    331  CG1 VAL A  43      43.789  29.906  16.858  1.00 63.79           C  
ANISOU  331  CG1 VAL A  43    11687   6384   6164   -744    488    602       C  
ATOM    332  CG2 VAL A  43      44.892  28.017  18.080  1.00 61.06           C  
ANISOU  332  CG2 VAL A  43    10817   6275   6108   -725    598    584       C  
ATOM    333  N   ASN A  44      45.185  29.129  13.811  1.00 69.32           N  
ANISOU  333  N   ASN A  44    12759   6958   6620   -927    816    521       N  
ATOM    334  CA  ASN A  44      45.048  29.974  12.626  1.00 71.15           C  
ANISOU  334  CA  ASN A  44    13377   7028   6626  -1005    835    522       C  
ATOM    335  C   ASN A  44      44.327  29.255  11.481  1.00 73.61           C  
ANISOU  335  C   ASN A  44    13857   7252   6859   -914    767    508       C  
ATOM    336  O   ASN A  44      43.481  29.837  10.795  1.00 75.72           O  
ANISOU  336  O   ASN A  44    14428   7366   6974   -867    634    525       O  
ATOM    337  CB  ASN A  44      46.421  30.465  12.189  1.00 70.89           C  
ANISOU  337  CB  ASN A  44    13420   7006   6508  -1222   1082    483       C  
ATOM    338  CG  ASN A  44      47.022  31.464  13.167  1.00 70.61           C  
ANISOU  338  CG  ASN A  44    13304   7019   6507  -1323   1131    497       C  
ATOM    339  ND2 ASN A  44      48.302  31.775  12.990  1.00 71.08           N  
ANISOU  339  ND2 ASN A  44    13347   7123   6539  -1515   1358    443       N  
ATOM    340  OD1 ASN A  44      46.345  31.960  14.064  1.00 69.48           O  
ANISOU  340  OD1 ASN A  44    13110   6873   6415  -1234    970    544       O  
ATOM    341  N   GLU A  45      44.643  27.981  11.298  1.00 73.64           N  
ANISOU  341  N   GLU A  45    13664   7345   6971   -878    840    471       N  
ATOM    342  CA  GLU A  45      43.998  27.184  10.273  1.00 74.61           C  
ANISOU  342  CA  GLU A  45    13911   7398   7039   -787    779    452       C  
ATOM    343  C   GLU A  45      42.497  27.143  10.464  1.00 68.94           C  
ANISOU  343  C   GLU A  45    13237   6616   6341   -605    522    479       C  
ATOM    344  O   GLU A  45      41.715  27.451   9.562  1.00 67.50           O  
ANISOU  344  O   GLU A  45    13340   6290   6015   -552    407    476       O  
ATOM    345  CB  GLU A  45      44.552  25.761  10.299  1.00 79.11           C  
ANISOU  345  CB  GLU A  45    14206   8092   7762   -759    877    406       C  
ATOM    346  CG  GLU A  45      45.564  25.491   9.187  1.00 85.51           C  
ANISOU  346  CG  GLU A  45    15120   8894   8476   -893   1093    339       C  
ATOM    347  CD  GLU A  45      46.322  24.184   9.395  1.00 91.47           C  
ANISOU  347  CD  GLU A  45    15559   9786   9410   -872   1197    274       C  
ATOM    348  OE1 GLU A  45      47.243  24.167  10.244  1.00 93.32           O  
ANISOU  348  OE1 GLU A  45    15547  10138   9774   -931   1293    246       O  
ATOM    349  OE2 GLU A  45      45.995  23.167   8.722  1.00 97.52           O1-
ANISOU  349  OE2 GLU A  45    16324  10538  10191   -788   1171    246       O1-
ATOM    350  N   LEU A  46      42.090  26.779  11.661  1.00 65.35           N  
ANISOU  350  N   LEU A  46    12502   6265   6064   -514    429    495       N  
ATOM    351  CA  LEU A  46      40.671  26.682  11.955  1.00 63.34           C  
ANISOU  351  CA  LEU A  46    12239   5975   5854   -353    202    496       C  
ATOM    352  C   LEU A  46      40.023  28.045  11.842  1.00 63.56           C  
ANISOU  352  C   LEU A  46    12525   5874   5749   -340     67    504       C  
ATOM    353  O   LEU A  46      38.904  28.177  11.347  1.00 64.12           O  
ANISOU  353  O   LEU A  46    12758   5841   5765   -221   -116    477       O  
ATOM    354  CB  LEU A  46      40.469  26.114  13.349  1.00 60.91           C  
ANISOU  354  CB  LEU A  46    11589   5808   5747   -295    157    508       C  
ATOM    355  CG  LEU A  46      39.088  25.531  13.602  1.00 61.12           C  
ANISOU  355  CG  LEU A  46    11535   5833   5854   -142    -32    483       C  
ATOM    356  CD1 LEU A  46      38.716  24.552  12.498  1.00 59.41           C  
ANISOU  356  CD1 LEU A  46    11400   5563   5611    -74    -53    450       C  
ATOM    357  CD2 LEU A  46      39.056  24.867  14.982  1.00 56.67           C  
ANISOU  357  CD2 LEU A  46    10646   5412   5474   -123    -38    498       C  
ATOM    358  N   THR A  47      40.744  29.075  12.267  1.00 63.72           N  
ANISOU  358  N   THR A  47    12595   5895   5719   -459    150    532       N  
ATOM    359  CA  THR A  47      40.225  30.418  12.153  1.00 65.87           C  
ANISOU  359  CA  THR A  47    13135   6034   5858   -454     22    540       C  
ATOM    360  C   THR A  47      40.044  30.855  10.702  1.00 67.54           C  
ANISOU  360  C   THR A  47    13758   6056   5847   -475    -11    532       C  
ATOM    361  O   THR A  47      39.051  31.508  10.381  1.00 67.10           O  
ANISOU  361  O   THR A  47    13929   5863   5704   -374   -220    515       O  
ATOM    362  CB  THR A  47      41.075  31.438  12.925  1.00 65.86           C  
ANISOU  362  CB  THR A  47    13107   6069   5848   -589    123    573       C  
ATOM    363  CG2 THR A  47      40.417  32.817  12.878  1.00 64.94           C  
ANISOU  363  CG2 THR A  47    13266   5804   5604   -563    -43    577       C  
ATOM    364  OG1 THR A  47      41.194  31.007  14.284  1.00 62.03           O  
ANISOU  364  OG1 THR A  47    12254   5752   5562   -560    136    580       O  
ATOM    365  N   GLU A  48      40.970  30.500   9.823  1.00 68.75           N  
ANISOU  365  N   GLU A  48    14018   6199   5907   -603    183    532       N  
ATOM    366  CA  GLU A  48      40.754  30.811   8.410  1.00 73.45           C  
ANISOU  366  CA  GLU A  48    15022   6609   6276   -626    151    524       C  
ATOM    367  C   GLU A  48      39.518  30.105   7.885  1.00 69.50           C  
ANISOU  367  C   GLU A  48    14562   6048   5796   -431    -56    489       C  
ATOM    368  O   GLU A  48      38.725  30.674   7.139  1.00 69.85           O  
ANISOU  368  O   GLU A  48    14933   5916   5691   -358   -236    476       O  
ATOM    369  CB  GLU A  48      41.977  30.487   7.543  1.00 79.74           C  
ANISOU  369  CB  GLU A  48    15913   7417   6967   -812    419    514       C  
ATOM    370  CG  GLU A  48      43.030  31.597   7.539  1.00 86.24           C  
ANISOU  370  CG  GLU A  48    16905   8204   7657  -1034    596    533       C  
ATOM    371  CD  GLU A  48      42.542  32.931   6.963  1.00 93.57           C  
ANISOU  371  CD  GLU A  48    18295   8910   8349  -1065    460    564       C  
ATOM    372  OE1 GLU A  48      41.776  32.941   5.955  1.00101.19           O  
ANISOU  372  OE1 GLU A  48    19577   9710   9161   -985    314    559       O  
ATOM    373  OE2 GLU A  48      42.952  33.982   7.512  1.00 95.29           O1-
ANISOU  373  OE2 GLU A  48    18572   9107   8527  -1170    494    591       O1-
ATOM    374  N   PHE A  49      39.341  28.857   8.268  1.00 67.28           N  
ANISOU  374  N   PHE A  49    13958   5905   5700   -344    -42    467       N  
ATOM    375  CA  PHE A  49      38.185  28.142   7.781  1.00 64.67           C  
ANISOU  375  CA  PHE A  49    13647   5525   5400   -170   -228    423       C  
ATOM    376  C   PHE A  49      36.932  28.845   8.282  1.00 62.65           C  
ANISOU  376  C   PHE A  49    13427   5204   5174    -22   -493    394       C  
ATOM    377  O   PHE A  49      36.002  29.086   7.524  1.00 64.25           O  
ANISOU  377  O   PHE A  49    13871   5260   5280     92   -689    351       O  
ATOM    378  CB  PHE A  49      38.199  26.708   8.230  1.00 61.35           C  
ANISOU  378  CB  PHE A  49    12868   5263   5180   -112   -170    406       C  
ATOM    379  CG  PHE A  49      36.979  25.966   7.816  1.00 60.92           C  
ANISOU  379  CG  PHE A  49    12809   5166   5171     60   -358    354       C  
ATOM    380  CD1 PHE A  49      36.010  25.645   8.726  1.00 60.87           C  
ANISOU  380  CD1 PHE A  49    12561   5233   5332    185   -508    321       C  
ATOM    381  CD2 PHE A  49      36.779  25.639   6.505  1.00 61.86           C  
ANISOU  381  CD2 PHE A  49    13178   5170   5158     88   -385    327       C  
ATOM    382  CE1 PHE A  49      34.868  24.976   8.341  1.00 61.15           C  
ANISOU  382  CE1 PHE A  49    12583   5233   5417    334   -676    254       C  
ATOM    383  CE2 PHE A  49      35.642  24.975   6.110  1.00 61.49           C  
ANISOU  383  CE2 PHE A  49    13125   5081   5157    249   -566    268       C  
ATOM    384  CZ  PHE A  49      34.686  24.634   7.028  1.00 60.71           C  
ANISOU  384  CZ  PHE A  49    12766   5062   5239    372   -711    228       C  
ATOM    385  N   ALA A  50      36.930  29.205   9.553  1.00 59.67           N  
ANISOU  385  N   ALA A  50    12811   4932   4928    -24   -502    406       N  
ATOM    386  CA  ALA A  50      35.797  29.938  10.114  1.00 59.36           C  
ANISOU  386  CA  ALA A  50    12781   4846   4928    106   -740    359       C  
ATOM    387  C   ALA A  50      35.423  31.190   9.284  1.00 60.56           C  
ANISOU  387  C   ALA A  50    13364   4777   4869    128   -898    346       C  
ATOM    388  O   ALA A  50      34.239  31.457   9.057  1.00 60.69           O  
ANISOU  388  O   ALA A  50    13485   4694   4879    290  -1149    271       O  
ATOM    389  CB  ALA A  50      36.086  30.316  11.551  1.00 55.71           C  
ANISOU  389  CB  ALA A  50    12048   4520   4600     60   -690    382       C  
ATOM    390  N   LYS A  51      36.419  31.922   8.798  1.00 61.28           N  
ANISOU  390  N   LYS A  51    13712   4786   4786    -36   -757    409       N  
ATOM    391  CA  LYS A  51      36.149  33.126   8.006  1.00 65.35           C  
ANISOU  391  CA  LYS A  51    14681   5073   5078    -37   -901    408       C  
ATOM    392  C   LYS A  51      35.474  32.790   6.675  1.00 66.53           C  
ANISOU  392  C   LYS A  51    15128   5059   5091     62  -1045    367       C  
ATOM    393  O   LYS A  51      34.491  33.419   6.291  1.00 68.14           O  
ANISOU  393  O   LYS A  51    15576   5097   5217    202  -1314    313       O  
ATOM    394  CB  LYS A  51      37.427  33.932   7.765  1.00 66.88           C  
ANISOU  394  CB  LYS A  51    15095   5215   5103   -268   -688    483       C  
ATOM    395  CG  LYS A  51      37.809  34.826   8.931  1.00 67.94           C  
ANISOU  395  CG  LYS A  51    15093   5415   5305   -336   -655    511       C  
ATOM    396  CD  LYS A  51      38.957  35.778   8.574  1.00 72.39           C  
ANISOU  396  CD  LYS A  51    15937   5892   5676   -567   -472    571       C  
ATOM    397  CE  LYS A  51      39.948  36.000   9.722  1.00 74.28           C  
ANISOU  397  CE  LYS A  51    15882   6303   6040   -705   -273    603       C  
ATOM    398  NZ  LYS A  51      41.262  35.317   9.475  1.00 75.84           N1+
ANISOU  398  NZ  LYS A  51    15952   6620   6245   -892     42    619       N1+
ATOM    399  N   THR A  52      36.001  31.794   5.987  1.00 66.83           N  
ANISOU  399  N   THR A  52    15141   5143   5107     -2   -875    383       N  
ATOM    400  CA  THR A  52      35.368  31.292   4.797  1.00 68.97           C  
ANISOU  400  CA  THR A  52    15641   5287   5275     97   -999    341       C  
ATOM    401  C   THR A  52      33.872  31.083   5.011  1.00 69.47           C  
ANISOU  401  C   THR A  52    15603   5327   5465    344  -1305    245       C  
ATOM    402  O   THR A  52      33.061  31.507   4.196  1.00 71.09           O  
ANISOU  402  O   THR A  52    16127   5343   5543    463  -1541    193       O  
ATOM    403  CB  THR A  52      36.010  29.967   4.362  1.00 68.04           C  
ANISOU  403  CB  THR A  52    15356   5289   5207     30   -780    351       C  
ATOM    404  CG2 THR A  52      35.297  29.397   3.151  1.00 69.51           C  
ANISOU  404  CG2 THR A  52    15766   5349   5296    143   -917    302       C  
ATOM    405  OG1 THR A  52      37.388  30.193   4.040  1.00 67.57           O  
ANISOU  405  OG1 THR A  52    15409   5244   5021   -202   -497    409       O  
ATOM    406  N   CYS A  53      33.510  30.425   6.101  1.00 68.91           N  
ANISOU  406  N   CYS A  53    15095   5446   5643    417  -1302    211       N  
ATOM    407  CA  CYS A  53      32.112  30.050   6.340  1.00 69.70           C  
ANISOU  407  CA  CYS A  53    15039   5556   5888    631  -1554     98       C  
ATOM    408  C   CYS A  53      31.223  31.261   6.645  1.00 71.17           C  
ANISOU  408  C   CYS A  53    15365   5624   6053    752  -1824     25       C  
ATOM    409  O   CYS A  53      30.021  31.279   6.307  1.00 69.67           O  
ANISOU  409  O   CYS A  53    15237   5345   5891    941  -2092    -94       O  
ATOM    410  CB  CYS A  53      32.027  29.058   7.498  1.00 69.37           C  
ANISOU  410  CB  CYS A  53    14505   5749   6103    641  -1454     83       C  
ATOM    411  SG  CYS A  53      32.815  27.466   7.184  1.00 73.21           S  
ANISOU  411  SG  CYS A  53    14793   6368   6656    555  -1205    135       S  
ATOM    412  N   VAL A  54      31.819  32.268   7.287  1.00 70.44           N  
ANISOU  412  N   VAL A  54    15314   5531   5919    648  -1759     83       N  
ATOM    413  CA  VAL A  54      31.127  33.516   7.557  1.00 71.23           C  
ANISOU  413  CA  VAL A  54    15577   5506   5981    747  -2004     21       C  
ATOM    414  C   VAL A  54      30.803  34.254   6.248  1.00 74.17           C  
ANISOU  414  C   VAL A  54    16474   5599   6109    807  -2207      3       C  
ATOM    415  O   VAL A  54      29.664  34.712   6.027  1.00 76.46           O  
ANISOU  415  O   VAL A  54    16892   5759   6401   1002  -2522   -117       O  
ATOM    416  CB  VAL A  54      31.974  34.427   8.482  1.00 70.61           C  
ANISOU  416  CB  VAL A  54    15451   5483   5896    601  -1866    100       C  
ATOM    417  CG1 VAL A  54      31.357  35.824   8.561  1.00 70.48           C  
ANISOU  417  CG1 VAL A  54    15689   5292   5796    694  -2126     43       C  
ATOM    418  CG2 VAL A  54      32.084  33.804   9.862  1.00 66.58           C  
ANISOU  418  CG2 VAL A  54    14442   5227   5629    577  -1730     98       C  
ATOM    419  N   ALA A  55      31.818  34.388   5.402  1.00 74.82           N  
ANISOU  419  N   ALA A  55    16864   5588   5977    634  -2029    111       N  
ATOM    420  CA  ALA A  55      31.628  34.884   4.053  1.00 78.63           C  
ANISOU  420  CA  ALA A  55    17870   5805   6200    658  -2182    111       C  
ATOM    421  C   ALA A  55      30.605  34.026   3.285  1.00 80.41           C  
ANISOU  421  C   ALA A  55    18109   5982   6463    851  -2378      9       C  
ATOM    422  O   ALA A  55      29.774  34.572   2.567  1.00 84.93           O  
ANISOU  422  O   ALA A  55    19015   6339   6918   1001  -2676    -66       O  
ATOM    423  CB  ALA A  55      32.967  34.912   3.313  1.00 78.52           C  
ANISOU  423  CB  ALA A  55    18118   5746   5969    405  -1891    235       C  
ATOM    424  N   ASP A  56      30.670  32.697   3.439  1.00 77.77           N  
ANISOU  424  N   ASP A  56    17420   5837   6292    851  -2223      1       N  
ATOM    425  CA  ASP A  56      29.865  31.767   2.632  1.00 77.67           C  
ANISOU  425  CA  ASP A  56    17419   5786   6304   1001  -2361    -84       C  
ATOM    426  C   ASP A  56      29.344  30.535   3.408  1.00 75.43           C  
ANISOU  426  C   ASP A  56    16614   5734   6310   1087  -2320   -154       C  
ATOM    427  O   ASP A  56      29.925  29.444   3.341  1.00 69.69           O  
ANISOU  427  O   ASP A  56    15694   5142   5643    998  -2094   -103       O  
ATOM    428  CB  ASP A  56      30.686  31.305   1.416  1.00 79.14           C  
ANISOU  428  CB  ASP A  56    17895   5892   6282    864  -2182     -1       C  
ATOM    429  CG  ASP A  56      29.886  30.410   0.472  1.00 81.90           C  
ANISOU  429  CG  ASP A  56    18310   6178   6629   1016  -2334    -85       C  
ATOM    430  OD1 ASP A  56      30.509  29.570  -0.253  1.00 81.70           O  
ANISOU  430  OD1 ASP A  56    18330   6180   6530    916  -2140    -35       O  
ATOM    431  OD2 ASP A  56      28.628  30.528   0.492  1.00 82.99           O1-
ANISOU  431  OD2 ASP A  56    18431   6249   6854   1237  -2647   -214       O1-
ATOM    432  N   GLU A  57      28.227  30.708   4.115  1.00 76.72           N  
ANISOU  432  N   GLU A  57    16566   5937   6648   1258  -2544   -284       N  
ATOM    433  CA  GLU A  57      27.692  29.651   4.992  1.00 75.66           C  
ANISOU  433  CA  GLU A  57    15941   6023   6784   1317  -2501   -358       C  
ATOM    434  C   GLU A  57      27.461  28.315   4.291  1.00 72.87           C  
ANISOU  434  C   GLU A  57    15507   5706   6474   1358  -2463   -386       C  
ATOM    435  O   GLU A  57      27.341  27.290   4.960  1.00 70.49           O  
ANISOU  435  O   GLU A  57    14823   5591   6368   1347  -2351   -405       O  
ATOM    436  CB  GLU A  57      26.421  30.116   5.727  1.00 78.47           C  
ANISOU  436  CB  GLU A  57    16118   6396   7302   1495  -2765   -527       C  
ATOM    437  CG  GLU A  57      26.707  31.169   6.808  1.00 83.26           C  
ANISOU  437  CG  GLU A  57    16647   7049   7940   1435  -2741   -500       C  
ATOM    438  CD  GLU A  57      25.531  31.461   7.770  1.00 86.95           C  
ANISOU  438  CD  GLU A  57    16832   7594   8609   1584  -2942   -679       C  
ATOM    439  OE1 GLU A  57      25.819  31.853   8.922  1.00 86.14           O  
ANISOU  439  OE1 GLU A  57    16512   7619   8599   1507  -2840   -652       O  
ATOM    440  OE2 GLU A  57      24.330  31.324   7.398  1.00 92.91           O1-
ANISOU  440  OE2 GLU A  57    17578   8288   9435   1775  -3200   -858       O1-
ATOM    441  N   SER A  58      27.414  28.325   2.964  1.00 72.89           N  
ANISOU  441  N   SER A  58    15881   5525   6288   1398  -2557   -385       N  
ATOM    442  CA  SER A  58      27.204  27.106   2.178  1.00 72.89           C  
ANISOU  442  CA  SER A  58    15848   5539   6308   1441  -2533   -414       C  
ATOM    443  C   SER A  58      28.454  26.326   1.819  1.00 70.01           C  
ANISOU  443  C   SER A  58    15478   5250   5874   1257  -2215   -279       C  
ATOM    444  O   SER A  58      28.356  25.245   1.266  1.00 67.89           O  
ANISOU  444  O   SER A  58    15144   5012   5639   1283  -2172   -299       O  
ATOM    445  CB  SER A  58      26.508  27.432   0.862  1.00 77.28           C  
ANISOU  445  CB  SER A  58    16819   5855   6689   1584  -2803   -493       C  
ATOM    446  OG  SER A  58      25.124  27.476   1.070  1.00 84.00           O  
ANISOU  446  OG  SER A  58    17543   6685   7688   1800  -3103   -675       O  
ATOM    447  N   HIS A  59      29.626  26.864   2.119  1.00 69.37           N  
ANISOU  447  N   HIS A  59    15459   5198   5702   1073  -1994   -155       N  
ATOM    448  CA  HIS A  59      30.852  26.197   1.737  1.00 68.55           C  
ANISOU  448  CA  HIS A  59    15353   5162   5531    898  -1695    -52       C  
ATOM    449  C   HIS A  59      30.974  24.784   2.377  1.00 65.17           C  
ANISOU  449  C   HIS A  59    14476   4950   5336    891  -1542    -57       C  
ATOM    450  O   HIS A  59      30.432  24.510   3.450  1.00 60.79           O  
ANISOU  450  O   HIS A  59    13582   4527   4990    953  -1590    -99       O  
ATOM    451  CB  HIS A  59      32.035  27.106   2.051  1.00 70.17           C  
ANISOU  451  CB  HIS A  59    15673   5368   5619    703  -1497     55       C  
ATOM    452  CG  HIS A  59      33.315  26.658   1.432  1.00 72.70           C  
ANISOU  452  CG  HIS A  59    16080   5718   5824    515  -1206    134       C  
ATOM    453  CD2 HIS A  59      33.990  27.140   0.359  1.00 73.76           C  
ANISOU  453  CD2 HIS A  59    16620   5707   5698    387  -1114    176       C  
ATOM    454  ND1 HIS A  59      34.054  25.588   1.916  1.00 71.47           N  
ANISOU  454  ND1 HIS A  59    15572   5760   5825    435   -970    161       N  
ATOM    455  CE1 HIS A  59      35.126  25.427   1.153  1.00 72.95           C  
ANISOU  455  CE1 HIS A  59    15921   5930   5867    275   -746    203       C  
ATOM    456  NE2 HIS A  59      35.105  26.351   0.201  1.00 75.93           N  
ANISOU  456  NE2 HIS A  59    16757   6105   5987    233   -816    214       N  
ATOM    457  N   ALA A  60      31.597  23.870   1.635  1.00 65.61           N  
ANISOU  457  N   ALA A  60    14561   5025   5343    824  -1379    -25       N  
ATOM    458  CA  ALA A  60      31.875  22.492   2.084  1.00 63.11           C  
ANISOU  458  CA  ALA A  60    13875   4888   5216    805  -1225    -21       C  
ATOM    459  C   ALA A  60      32.417  22.472   3.521  1.00 62.24           C  
ANISOU  459  C   ALA A  60    13412   4958   5277    721  -1082     30       C  
ATOM    460  O   ALA A  60      33.430  23.096   3.807  1.00 62.73           O  
ANISOU  460  O   ALA A  60    13517   5045   5273    580   -919    104       O  
ATOM    461  CB  ALA A  60      32.897  21.853   1.151  1.00 60.98           C  
ANISOU  461  CB  ALA A  60    13726   4611   4832    691  -1012     23       C  
ATOM    462  N   GLY A  61      31.733  21.774   4.418  1.00 61.49           N  
ANISOU  462  N   GLY A  61    12983   4983   5395    800  -1145    -15       N  
ATOM    463  CA  GLY A  61      32.217  21.595   5.778  1.00 60.19           C  
ANISOU  463  CA  GLY A  61    12490   4989   5393    722  -1015     33       C  
ATOM    464  C   GLY A  61      31.604  22.527   6.788  1.00 60.96           C  
ANISOU  464  C   GLY A  61    12502   5108   5553    758  -1138      7       C  
ATOM    465  O   GLY A  61      31.590  22.220   7.983  1.00 60.33           O  
ANISOU  465  O   GLY A  61    12120   5169   5634    732  -1088     16       O  
ATOM    466  N   CYS A  62      31.086  23.662   6.328  1.00 62.07           N  
ANISOU  466  N   CYS A  62    12914   5105   5565    820  -1307    -32       N  
ATOM    467  CA  CYS A  62      30.625  24.706   7.248  1.00 63.13           C  
ANISOU  467  CA  CYS A  62    12995   5249   5743    848  -1419    -61       C  
ATOM    468  C   CYS A  62      29.417  24.309   8.107  1.00 61.95           C  
ANISOU  468  C   CYS A  62    12554   5194   5792    962  -1563   -174       C  
ATOM    469  O   CYS A  62      29.074  25.013   9.055  1.00 62.67           O  
ANISOU  469  O   CYS A  62    12528   5332   5951    972  -1625   -207       O  
ATOM    470  CB  CYS A  62      30.283  25.983   6.469  1.00 66.89           C  
ANISOU  470  CB  CYS A  62    13860   5525   6031    907  -1600    -91       C  
ATOM    471  SG  CYS A  62      31.687  26.764   5.649  1.00 67.50           S  
ANISOU  471  SG  CYS A  62    14309   5486   5852    732  -1421     36       S  
ATOM    472  N   GLU A  63      28.767  23.211   7.747  1.00 62.43           N  
ANISOU  472  N   GLU A  63    12506   5277   5938   1039  -1613   -243       N  
ATOM    473  CA  GLU A  63      27.547  22.737   8.404  1.00 64.88           C  
ANISOU  473  CA  GLU A  63    12554   5669   6428   1135  -1744   -374       C  
ATOM    474  C   GLU A  63      27.885  21.807   9.547  1.00 66.96           C  
ANISOU  474  C   GLU A  63    12472   6118   6853   1035  -1568   -326       C  
ATOM    475  O   GLU A  63      27.026  21.487  10.371  1.00 72.17           O  
ANISOU  475  O   GLU A  63    12888   6871   7661   1065  -1627   -420       O  
ATOM    476  CB  GLU A  63      26.662  21.961   7.423  1.00 66.59           C  
ANISOU  476  CB  GLU A  63    12830   5814   6658   1260  -1884   -482       C  
ATOM    477  CG  GLU A  63      27.149  20.545   7.059  1.00 68.44           C  
ANISOU  477  CG  GLU A  63    12968   6105   6929   1205  -1728   -423       C  
ATOM    478  CD  GLU A  63      28.375  20.515   6.145  1.00 69.20           C  
ANISOU  478  CD  GLU A  63    13305   6130   6858   1122  -1577   -297       C  
ATOM    479  OE1 GLU A  63      28.577  19.530   5.409  1.00 74.20           O  
ANISOU  479  OE1 GLU A  63    13962   6752   7480   1124  -1517   -287       O  
ATOM    480  OE2 GLU A  63      29.148  21.480   6.148  1.00 70.57           O1-
ANISOU  480  OE2 GLU A  63    13644   6260   6910   1045  -1510   -218       O1-
ATOM    481  N   LYS A  64      29.129  21.346   9.571  1.00 64.38           N  
ANISOU  481  N   LYS A  64    12130   5838   6493    913  -1356   -191       N  
ATOM    482  CA  LYS A  64      29.562  20.393  10.558  1.00 62.29           C  
ANISOU  482  CA  LYS A  64    11577   5725   6364    823  -1202   -136       C  
ATOM    483  C   LYS A  64      29.654  21.030  11.942  1.00 58.92           C  
ANISOU  483  C   LYS A  64    10978   5400   6009    758  -1168   -115       C  
ATOM    484  O   LYS A  64      29.949  22.194  12.086  1.00 63.11           O  
ANISOU  484  O   LYS A  64    11626   5892   6461    739  -1185    -91       O  
ATOM    485  CB  LYS A  64      30.917  19.794  10.130  1.00 64.03           C  
ANISOU  485  CB  LYS A  64    11842   5956   6529    728  -1006    -18       C  
ATOM    486  CG  LYS A  64      30.836  18.948   8.862  1.00 65.10           C  
ANISOU  486  CG  LYS A  64    12106   6014   6614    783  -1019    -43       C  
ATOM    487  CD  LYS A  64      32.202  18.606   8.296  1.00 66.25           C  
ANISOU  487  CD  LYS A  64    12335   6156   6681    690   -830     48       C  
ATOM    488  CE  LYS A  64      32.096  17.496   7.270  1.00 68.48           C  
ANISOU  488  CE  LYS A  64    12669   6395   6953    740   -828     17       C  
ATOM    489  NZ  LYS A  64      33.295  17.382   6.388  1.00 71.62           N1+
ANISOU  489  NZ  LYS A  64    13221   6757   7234    664   -667     70       N1+
ATOM    490  N   SER A  65      29.396  20.255  12.965  1.00 56.71           N  
ANISOU  490  N   SER A  65    10432   5245   5871    717  -1120   -126       N  
ATOM    491  CA  SER A  65      29.535  20.728  14.320  1.00 56.80           C  
ANISOU  491  CA  SER A  65    10274   5359   5946    642  -1072   -102       C  
ATOM    492  C   SER A  65      30.980  21.072  14.612  1.00 56.96           C  
ANISOU  492  C   SER A  65    10328   5404   5909    535   -912     38       C  
ATOM    493  O   SER A  65      31.899  20.575  13.955  1.00 59.33           O  
ANISOU  493  O   SER A  65    10705   5678   6160    500   -805    111       O  
ATOM    494  CB  SER A  65      29.080  19.639  15.299  1.00 56.72           C  
ANISOU  494  CB  SER A  65    10001   5470   6081    595  -1031   -127       C  
ATOM    495  OG  SER A  65      29.999  18.551  15.348  1.00 57.65           O  
ANISOU  495  OG  SER A  65    10058   5623   6222    524   -891    -22       O  
ATOM    496  N   LEU A  66      31.190  21.883  15.634  1.00 56.94           N  
ANISOU  496  N   LEU A  66    10250   5462   5924    480   -890     61       N  
ATOM    497  CA  LEU A  66      32.550  22.200  16.051  1.00 59.31           C  
ANISOU  497  CA  LEU A  66    10548   5799   6189    373   -739    179       C  
ATOM    498  C   LEU A  66      33.311  20.957  16.468  1.00 58.20           C  
ANISOU  498  C   LEU A  66    10244   5740   6128    306   -608    250       C  
ATOM    499  O   LEU A  66      34.510  20.834  16.219  1.00 57.29           O  
ANISOU  499  O   LEU A  66    10163   5626   5979    246   -485    325       O  
ATOM    500  CB  LEU A  66      32.524  23.184  17.212  1.00 59.21           C  
ANISOU  500  CB  LEU A  66    10451   5846   6198    330   -751    182       C  
ATOM    501  CG  LEU A  66      32.131  24.537  16.678  1.00 62.41           C  
ANISOU  501  CG  LEU A  66    11065   6146   6501    388   -868    132       C  
ATOM    502  CD1 LEU A  66      31.369  25.349  17.742  1.00 65.47           C  
ANISOU  502  CD1 LEU A  66    11343   6588   6946    405   -962     60       C  
ATOM    503  CD2 LEU A  66      33.425  25.183  16.187  1.00 63.74           C  
ANISOU  503  CD2 LEU A  66    11409   6258   6550    309   -753    230       C  
ATOM    504  N   HIS A  67      32.624  20.065  17.167  1.00 56.74           N  
ANISOU  504  N   HIS A  67     9880   5625   6052    309   -637    216       N  
ATOM    505  CA  HIS A  67      33.254  18.828  17.559  1.00 57.44           C  
ANISOU  505  CA  HIS A  67     9839   5771   6213    256   -542    278       C  
ATOM    506  C   HIS A  67      33.765  18.100  16.342  1.00 56.78           C  
ANISOU  506  C   HIS A  67     9858   5622   6093    290   -500    294       C  
ATOM    507  O   HIS A  67      34.885  17.614  16.365  1.00 58.20           O  
ANISOU  507  O   HIS A  67    10003   5823   6285    243   -392    360       O  
ATOM    508  CB  HIS A  67      32.302  17.932  18.328  1.00 58.34           C  
ANISOU  508  CB  HIS A  67     9792   5946   6429    248   -588    231       C  
ATOM    509  CG  HIS A  67      32.072  18.391  19.719  1.00 57.92           C  
ANISOU  509  CG  HIS A  67     9609   5979   6418    179   -585    231       C  
ATOM    510  CD2 HIS A  67      30.935  18.746  20.363  1.00 60.09           C  
ANISOU  510  CD2 HIS A  67     9803   6298   6730    178   -658    136       C  
ATOM    511  ND1 HIS A  67      33.105  18.577  20.613  1.00 59.00           N  
ANISOU  511  ND1 HIS A  67     9685   6171   6561     99   -499    324       N  
ATOM    512  CE1 HIS A  67      32.606  19.013  21.760  1.00 60.31           C  
ANISOU  512  CE1 HIS A  67     9750   6407   6757     49   -519    299       C  
ATOM    513  NE2 HIS A  67      31.293  19.122  21.635  1.00 61.37           N  
ANISOU  513  NE2 HIS A  67     9867   6540   6911     91   -607    182       N  
ATOM    514  N   THR A  68      32.971  18.031  15.272  1.00 54.94           N  
ANISOU  514  N   THR A  68     9750   5308   5817    375   -588    223       N  
ATOM    515  CA  THR A  68      33.444  17.313  14.114  1.00 53.65           C  
ANISOU  515  CA  THR A  68     9689   5084   5613    404   -544    233       C  
ATOM    516  C   THR A  68      34.666  18.006  13.563  1.00 53.59           C  
ANISOU  516  C   THR A  68     9818   5042   5501    353   -435    289       C  
ATOM    517  O   THR A  68      35.653  17.332  13.195  1.00 51.69           O  
ANISOU  517  O   THR A  68     9562   4812   5266    319   -322    324       O  
ATOM    518  CB  THR A  68      32.370  17.142  13.029  1.00 54.39           C  
ANISOU  518  CB  THR A  68     9909   5089   5669    507   -668    143       C  
ATOM    519  CG2 THR A  68      33.004  16.684  11.710  1.00 51.50           C  
ANISOU  519  CG2 THR A  68     9700   4646   5221    528   -611    158       C  
ATOM    520  OG1 THR A  68      31.460  16.138  13.468  1.00 54.49           O  
ANISOU  520  OG1 THR A  68     9764   5144   5794    531   -727     89       O  
ATOM    521  N   LEU A  69      34.599  19.338  13.495  1.00 51.37           N  
ANISOU  521  N   LEU A  69     9671   4719   5128    345   -468    285       N  
ATOM    522  CA  LEU A  69      35.641  20.084  12.810  1.00 53.41           C  
ANISOU  522  CA  LEU A  69    10106   4925   5263    284   -366    324       C  
ATOM    523  C   LEU A  69      36.916  20.056  13.621  1.00 54.97           C  
ANISOU  523  C   LEU A  69    10157   5215   5512    180   -215    389       C  
ATOM    524  O   LEU A  69      37.960  19.678  13.121  1.00 58.75           O  
ANISOU  524  O   LEU A  69    10650   5700   5971    128    -86    405       O  
ATOM    525  CB  LEU A  69      35.223  21.522  12.538  1.00 53.77           C  
ANISOU  525  CB  LEU A  69    10358   4885   5189    298   -453    305       C  
ATOM    526  CG  LEU A  69      34.171  21.735  11.436  1.00 54.01           C  
ANISOU  526  CG  LEU A  69    10607   4785   5128    407   -611    232       C  
ATOM    527  CD1 LEU A  69      33.553  23.124  11.463  1.00 52.46           C  
ANISOU  527  CD1 LEU A  69    10578   4506   4847    446   -749    198       C  
ATOM    528  CD2 LEU A  69      34.799  21.466  10.088  1.00 53.66           C  
ANISOU  528  CD2 LEU A  69    10774   4655   4959    385   -531    245       C  
ATOM    529  N   PHE A  70      36.819  20.471  14.869  1.00 55.15           N  
ANISOU  529  N   PHE A  70    10038   5312   5604    151   -236    412       N  
ATOM    530  CA  PHE A  70      37.942  20.472  15.788  1.00 54.97           C  
ANISOU  530  CA  PHE A  70     9865   5379   5643     63   -122    466       C  
ATOM    531  C   PHE A  70      38.536  19.072  15.879  1.00 54.77           C  
ANISOU  531  C   PHE A  70     9689   5404   5716     63    -58    477       C  
ATOM    532  O   PHE A  70      39.737  18.894  15.732  1.00 57.26           O  
ANISOU  532  O   PHE A  70     9970   5746   6041      9     62    489       O  
ATOM    533  CB  PHE A  70      37.447  20.943  17.163  1.00 55.27           C  
ANISOU  533  CB  PHE A  70     9769   5486   5746     50   -187    479       C  
ATOM    534  CG  PHE A  70      38.497  20.944  18.234  1.00 54.87           C  
ANISOU  534  CG  PHE A  70     9561   5525   5762    -30    -97    532       C  
ATOM    535  CD1 PHE A  70      39.438  21.961  18.299  1.00 54.68           C  
ANISOU  535  CD1 PHE A  70     9589   5504   5682   -105    -12    555       C  
ATOM    536  CD2 PHE A  70      38.515  19.945  19.199  1.00 54.75           C  
ANISOU  536  CD2 PHE A  70     9358   5583   5861    -33   -107    554       C  
ATOM    537  CE1 PHE A  70      40.397  21.984  19.299  1.00 55.73           C  
ANISOU  537  CE1 PHE A  70     9570   5720   5885   -171     59    590       C  
ATOM    538  CE2 PHE A  70      39.473  19.942  20.207  1.00 56.04           C  
ANISOU  538  CE2 PHE A  70     9390   5819   6085    -96    -48    598       C  
ATOM    539  CZ  PHE A  70      40.417  20.970  20.260  1.00 57.56           C  
ANISOU  539  CZ  PHE A  70     9615   6021   6232   -159     32    611       C  
ATOM    540  N   GLY A  71      37.683  18.085  16.121  1.00 53.55           N  
ANISOU  540  N   GLY A  71     9446   5261   5639    122   -142    461       N  
ATOM    541  CA  GLY A  71      38.080  16.692  16.093  1.00 53.82           C  
ANISOU  541  CA  GLY A  71     9372   5317   5759    137   -111    466       C  
ATOM    542  C   GLY A  71      38.769  16.197  14.832  1.00 55.37           C  
ANISOU  542  C   GLY A  71     9658   5467   5915    152    -32    440       C  
ATOM    543  O   GLY A  71      39.732  15.438  14.899  1.00 57.70           O  
ANISOU  543  O   GLY A  71     9854   5794   6273    136     41    443       O  
ATOM    544  N   ASP A  72      38.298  16.614  13.666  1.00 57.43           N  
ANISOU  544  N   ASP A  72    10110   5645   6065    185    -53    404       N  
ATOM    545  CA  ASP A  72      38.982  16.247  12.430  1.00 56.67           C  
ANISOU  545  CA  ASP A  72    10120   5503   5907    183     38    374       C  
ATOM    546  C   ASP A  72      40.385  16.866  12.428  1.00 57.85           C  
ANISOU  546  C   ASP A  72    10269   5689   6022     83    194    381       C  
ATOM    547  O   ASP A  72      41.296  16.371  11.772  1.00 59.17           O  
ANISOU  547  O   ASP A  72    10434   5863   6187     55    307    345       O  
ATOM    548  CB  ASP A  72      38.207  16.737  11.223  1.00 56.90           C  
ANISOU  548  CB  ASP A  72    10392   5427   5801    228    -22    337       C  
ATOM    549  CG  ASP A  72      36.942  15.949  10.964  1.00 57.22           C  
ANISOU  549  CG  ASP A  72    10429   5430   5884    331   -162    301       C  
ATOM    550  OD1 ASP A  72      36.731  14.841  11.556  1.00 53.67           O  
ANISOU  550  OD1 ASP A  72     9801   5031   5562    357   -190    303       O  
ATOM    551  OD2 ASP A  72      36.155  16.459  10.117  1.00 57.18           O1-
ANISOU  551  OD2 ASP A  72    10618   5334   5776    384   -251    263       O1-
ATOM    552  N   GLU A  73      40.574  17.937  13.181  1.00 57.05           N  
ANISOU  552  N   GLU A  73    10159   5617   5901     24    205    414       N  
ATOM    553  CA  GLU A  73      41.866  18.579  13.213  1.00 60.03           C  
ANISOU  553  CA  GLU A  73    10530   6030   6249    -81    354    411       C  
ATOM    554  C   GLU A  73      42.824  17.788  14.067  1.00 61.70           C  
ANISOU  554  C   GLU A  73    10496   6339   6610    -97    409    407       C  
ATOM    555  O   GLU A  73      43.945  17.521  13.634  1.00 62.66           O  
ANISOU  555  O   GLU A  73    10575   6488   6746   -145    538    356       O  
ATOM    556  CB  GLU A  73      41.749  20.010  13.699  1.00 61.32           C  
ANISOU  556  CB  GLU A  73    10778   6183   6339   -139    340    444       C  
ATOM    557  CG  GLU A  73      42.491  20.990  12.821  1.00 67.17           C  
ANISOU  557  CG  GLU A  73    11718   6871   6932   -243    468    424       C  
ATOM    558  CD  GLU A  73      42.031  20.975  11.364  1.00 70.17           C  
ANISOU  558  CD  GLU A  73    12357   7136   7166   -220    459    395       C  
ATOM    559  OE1 GLU A  73      40.807  21.017  11.106  1.00 74.20           O  
ANISOU  559  OE1 GLU A  73    12981   7575   7639   -124    303    400       O  
ATOM    560  OE2 GLU A  73      42.905  20.921  10.477  1.00 71.96           O1-
ANISOU  560  OE2 GLU A  73    12675   7348   7318   -302    609    354       O1-
ATOM    561  N   LEU A  74      42.396  17.387  15.268  1.00 61.56           N  
ANISOU  561  N   LEU A  74    10321   6368   6699    -57    309    448       N  
ATOM    562  CA  LEU A  74      43.268  16.592  16.137  1.00 61.27           C  
ANISOU  562  CA  LEU A  74    10073   6406   6800    -60    328    447       C  
ATOM    563  C   LEU A  74      43.783  15.396  15.378  1.00 62.53           C  
ANISOU  563  C   LEU A  74    10192   6555   7012    -17    368    390       C  
ATOM    564  O   LEU A  74      44.979  15.130  15.359  1.00 66.02           O  
ANISOU  564  O   LEU A  74    10530   7041   7515    -44    458    337       O  
ATOM    565  CB  LEU A  74      42.549  16.100  17.383  1.00 62.08           C  
ANISOU  565  CB  LEU A  74    10061   6537   6990    -21    200    501       C  
ATOM    566  CG  LEU A  74      42.004  17.134  18.373  1.00 62.59           C  
ANISOU  566  CG  LEU A  74    10125   6628   7029    -58    149    549       C  
ATOM    567  CD1 LEU A  74      41.672  16.418  19.671  1.00 62.14           C  
ANISOU  567  CD1 LEU A  74     9930   6613   7069    -45     58    590       C  
ATOM    568  CD2 LEU A  74      42.961  18.285  18.631  1.00 62.16           C  
ANISOU  568  CD2 LEU A  74    10067   6609   6941   -139    241    549       C  
ATOM    569  N   CYS A  75      42.884  14.682  14.726  1.00 62.67           N  
ANISOU  569  N   CYS A  75    10285   6515   7010     53    299    386       N  
ATOM    570  CA  CYS A  75      43.274  13.493  13.970  1.00 65.82           C  
ANISOU  570  CA  CYS A  75    10653   6897   7458    103    325    329       C  
ATOM    571  C   CYS A  75      44.279  13.738  12.841  1.00 64.81           C  
ANISOU  571  C   CYS A  75    10591   6768   7267     52    483    249       C  
ATOM    572  O   CYS A  75      45.026  12.839  12.470  1.00 63.18           O  
ANISOU  572  O   CYS A  75    10295   6578   7132     77    532    179       O  
ATOM    573  CB  CYS A  75      42.032  12.769  13.454  1.00 67.99           C  
ANISOU  573  CB  CYS A  75    11012   7107   7716    182    219    338       C  
ATOM    574  SG  CYS A  75      41.105  12.082  14.855  1.00 72.85           S  
ANISOU  574  SG  CYS A  75    11503   7740   8438    219     66    403       S  
ATOM    575  N   LYS A  76      44.335  14.961  12.324  1.00 66.47           N  
ANISOU  575  N   LYS A  76    10958   6956   7342    -26    564    249       N  
ATOM    576  CA  LYS A  76      45.301  15.285  11.280  1.00 65.22           C  
ANISOU  576  CA  LYS A  76    10883   6796   7102   -109    736    169       C  
ATOM    577  C   LYS A  76      46.683  15.596  11.857  1.00 65.55           C  
ANISOU  577  C   LYS A  76    10758   6927   7220   -193    859    116       C  
ATOM    578  O   LYS A  76      47.589  15.877  11.089  1.00 72.54           O  
ANISOU  578  O   LYS A  76    11682   7828   8050   -283   1024     29       O  
ATOM    579  CB  LYS A  76      44.781  16.422  10.370  1.00 63.92           C  
ANISOU  579  CB  LYS A  76    11001   6548   6739   -168    768    188       C  
ATOM    580  CG  LYS A  76      43.684  15.989   9.392  1.00 63.67           C  
ANISOU  580  CG  LYS A  76    11149   6420   6623    -85    675    192       C  
ATOM    581  CD  LYS A  76      43.000  17.156   8.665  1.00 61.32           C  
ANISOU  581  CD  LYS A  76    11148   6020   6131   -119    648    219       C  
ATOM    582  N   VAL A  77      46.856  15.530  13.179  1.00 64.32           N  
ANISOU  582  N   VAL A  77    10421   6830   7187   -171    784    155       N  
ATOM    583  CA  VAL A  77      48.155  15.820  13.817  1.00 66.67           C  
ANISOU  583  CA  VAL A  77    10546   7214   7573   -238    877     95       C  
ATOM    584  C   VAL A  77      49.117  14.648  13.626  1.00 71.10           C  
ANISOU  584  C   VAL A  77    10927   7819   8269   -191    915    -20       C  
ATOM    585  O   VAL A  77      48.859  13.523  14.087  1.00 70.86           O  
ANISOU  585  O   VAL A  77    10790   7781   8352    -80    785     -5       O  
ATOM    586  CB  VAL A  77      48.018  16.144  15.337  1.00 65.72           C  
ANISOU  586  CB  VAL A  77    10303   7135   7534   -223    767    173       C  
ATOM    587  CG1 VAL A  77      49.377  16.256  16.023  1.00 63.71           C  
ANISOU  587  CG1 VAL A  77     9848   6966   7393   -269    836     97       C  
ATOM    588  CG2 VAL A  77      47.247  17.438  15.538  1.00 61.80           C  
ANISOU  588  CG2 VAL A  77     9964   6605   6911   -279    747    259       C  
ATOM    589  N   ALA A  78      50.247  14.929  12.975  1.00 77.40           N  
ANISOU  589  N   ALA A  78    11689   8662   9056   -282   1095   -146       N  
ATOM    590  CA  ALA A  78      51.174  13.879  12.543  1.00 80.31           C  
ANISOU  590  CA  ALA A  78    11899   9072   9543   -242   1152   -292       C  
ATOM    591  C   ALA A  78      51.748  13.088  13.732  1.00 82.02           C  
ANISOU  591  C   ALA A  78    11861   9340   9963   -146   1027   -321       C  
ATOM    592  O   ALA A  78      51.845  11.859  13.664  1.00 85.42           O  
ANISOU  592  O   ALA A  78    12196   9757  10501    -35    942   -372       O  
ATOM    593  CB  ALA A  78      52.290  14.465  11.675  1.00 78.86           C  
ANISOU  593  CB  ALA A  78    11718   8940   9305   -384   1389   -441       C  
ATOM    594  N   SER A  79      52.080  13.784  14.823  1.00 81.83           N  
ANISOU  594  N   SER A  79    11748   9361   9983   -183    998   -286       N  
ATOM    595  CA  SER A  79      52.728  13.158  15.998  1.00 83.44           C  
ANISOU  595  CA  SER A  79    11728   9606  10369   -100    873   -320       C  
ATOM    596  C   SER A  79      51.768  12.462  16.982  1.00 80.40           C  
ANISOU  596  C   SER A  79    11359   9165  10025     11    649   -178       C  
ATOM    597  O   SER A  79      52.188  11.975  18.031  1.00 82.13           O  
ANISOU  597  O   SER A  79    11437   9398  10369     77    523   -184       O  
ATOM    598  CB  SER A  79      53.542  14.218  16.760  1.00 87.38           C  
ANISOU  598  CB  SER A  79    12126  10178  10895   -193    939   -352       C  
ATOM    599  OG  SER A  79      52.728  15.309  17.183  1.00 89.79           O  
ANISOU  599  OG  SER A  79    12581  10460  11076   -260    926   -206       O  
ATOM    600  N   LEU A  80      50.489  12.400  16.634  1.00 76.76           N  
ANISOU  600  N   LEU A  80    11074   8636   9455     27    599    -62       N  
ATOM    601  CA  LEU A  80      49.445  12.036  17.591  1.00 74.55           C  
ANISOU  601  CA  LEU A  80    10832   8311   9181     86    421     75       C  
ATOM    602  C   LEU A  80      49.725  10.770  18.383  1.00 72.46           C  
ANISOU  602  C   LEU A  80    10445   8027   9060    191    264     65       C  
ATOM    603  O   LEU A  80      49.714  10.796  19.607  1.00 72.76           O  
ANISOU  603  O   LEU A  80    10432   8071   9144    200    154    128       O  
ATOM    604  CB  LEU A  80      48.092  11.927  16.872  1.00 75.13           C  
ANISOU  604  CB  LEU A  80    11090   8316   9140    100    396    153       C  
ATOM    605  CG  LEU A  80      46.858  11.682  17.735  1.00 74.34           C  
ANISOU  605  CG  LEU A  80    11043   8177   9028    132    244    278       C  
ATOM    606  CD1 LEU A  80      46.693  12.768  18.794  1.00 73.62           C  
ANISOU  606  CD1 LEU A  80    10945   8125   8905     67    228    351       C  
ATOM    607  CD2 LEU A  80      45.620  11.555  16.860  1.00 72.76           C  
ANISOU  607  CD2 LEU A  80    11001   7914   8730    152    229    313       C  
ATOM    608  N   ARG A  81      49.978   9.659  17.698  1.00 74.37           N  
ANISOU  608  N   ARG A  81    10654   8237   9366    269    245    -16       N  
ATOM    609  CA  ARG A  81      50.210   8.387  18.388  1.00 72.24           C  
ANISOU  609  CA  ARG A  81    10297   7924   9225    378     74    -28       C  
ATOM    610  C   ARG A  81      51.567   8.355  19.089  1.00 71.65           C  
ANISOU  610  C   ARG A  81    10037   7900   9287    407     44   -135       C  
ATOM    611  O   ARG A  81      51.656   7.901  20.228  1.00 69.41           O  
ANISOU  611  O   ARG A  81     9712   7586   9074    460   -121    -89       O  
ATOM    612  CB  ARG A  81      50.058   7.192  17.449  1.00 74.52           C  
ANISOU  612  CB  ARG A  81    10610   8156   9546    462     48    -88       C  
ATOM    613  CG  ARG A  81      50.315   5.867  18.157  1.00 75.86           C  
ANISOU  613  CG  ARG A  81    10714   8264   9846    577   -145   -101       C  
ATOM    614  CD  ARG A  81      49.884   4.665  17.347  1.00 76.56           C  
ANISOU  614  CD  ARG A  81    10860   8277   9951    658   -196   -128       C  
ATOM    615  NE  ARG A  81      48.627   4.105  17.837  1.00 75.51           N  
ANISOU  615  NE  ARG A  81    10862   8060   9767    665   -326     18       N  
ATOM    616  CZ  ARG A  81      47.455   4.148  17.199  1.00 77.35           C  
ANISOU  616  CZ  ARG A  81    11229   8264   9896    632   -288     87       C  
ATOM    617  NH1 ARG A  81      46.393   3.603  17.773  1.00 78.13           N1+
ANISOU  617  NH1 ARG A  81    11425   8295   9967    628   -407    197       N1+
ATOM    618  NH2 ARG A  81      47.319   4.727  16.002  1.00 78.22           N  
ANISOU  618  NH2 ARG A  81    11387   8407   9927    597   -137     39       N  
ATOM    619  N   GLU A  82      52.612   8.848  18.422  1.00 73.33           N  
ANISOU  619  N   GLU A  82    10143   8186   9531    366    200   -286       N  
ATOM    620  CA  GLU A  82      53.951   8.945  19.042  1.00 75.22           C  
ANISOU  620  CA  GLU A  82    10182   8489   9911    386    185   -419       C  
ATOM    621  C   GLU A  82      53.884   9.561  20.438  1.00 74.60           C  
ANISOU  621  C   GLU A  82    10090   8420   9834    361     85   -315       C  
ATOM    622  O   GLU A  82      54.534   9.078  21.361  1.00 73.47           O  
ANISOU  622  O   GLU A  82     9833   8269   9814    440    -63   -359       O  
ATOM    623  CB  GLU A  82      54.925   9.767  18.174  1.00 75.04           C  
ANISOU  623  CB  GLU A  82    10067   8561   9885    288    417   -583       C  
ATOM    624  N   THR A  83      53.087  10.619  20.581  1.00 72.12           N  
ANISOU  624  N   THR A  83     9902   8119   9382    257    156   -184       N  
ATOM    625  CA  THR A  83      53.048  11.394  21.815  1.00 71.28           C  
ANISOU  625  CA  THR A  83     9784   8036   9262    213     96    -97       C  
ATOM    626  C   THR A  83      51.965  10.976  22.832  1.00 71.06           C  
ANISOU  626  C   THR A  83     9867   7939   9192    245    -80     73       C  
ATOM    627  O   THR A  83      52.196  11.068  24.050  1.00 72.08           O  
ANISOU  627  O   THR A  83     9954   8071   9361    254   -195    114       O  
ATOM    628  CB  THR A  83      52.890  12.893  21.496  1.00 70.40           C  
ANISOU  628  CB  THR A  83     9738   7980   9031     76    270    -67       C  
ATOM    629  CG2 THR A  83      52.773  13.732  22.798  1.00 67.49           C  
ANISOU  629  CG2 THR A  83     9362   7637   8644     30    205     27       C  
ATOM    630  OG1 THR A  83      54.002  13.329  20.700  1.00 71.49           O  
ANISOU  630  OG1 THR A  83     9773   8186   9205     18    444   -232       O  
ATOM    631  N   TYR A  84      50.799  10.536  22.345  1.00 68.06           N  
ANISOU  631  N   TYR A  84     9631   7500   8729    252    -97    161       N  
ATOM    632  CA  TYR A  84      49.644  10.293  23.217  1.00 65.06           C  
ANISOU  632  CA  TYR A  84     9364   7067   8288    245   -222    311       C  
ATOM    633  C   TYR A  84      49.073   8.856  23.184  1.00 68.17           C  
ANISOU  633  C   TYR A  84     9822   7368   8710    324   -355    343       C  
ATOM    634  O   TYR A  84      47.999   8.600  23.724  1.00 67.44           O  
ANISOU  634  O   TYR A  84     9838   7231   8555    298   -432    455       O  
ATOM    635  CB  TYR A  84      48.538  11.315  22.906  1.00 62.38           C  
ANISOU  635  CB  TYR A  84     9147   6746   7809    155   -127    396       C  
ATOM    636  CG  TYR A  84      48.956  12.787  22.944  1.00 58.85           C  
ANISOU  636  CG  TYR A  84     8675   6371   7313     68     -3    380       C  
ATOM    637  CD1 TYR A  84      48.912  13.526  24.124  1.00 56.07           C  
ANISOU  637  CD1 TYR A  84     8305   6053   6947     19    -46    444       C  
ATOM    638  CD2 TYR A  84      49.368  13.434  21.785  1.00 59.53           C  
ANISOU  638  CD2 TYR A  84     8774   6487   7358     25    159    301       C  
ATOM    639  CE1 TYR A  84      49.280  14.864  24.151  1.00 56.37           C  
ANISOU  639  CE1 TYR A  84     8327   6150   6940    -62     62    429       C  
ATOM    640  CE2 TYR A  84      49.746  14.769  21.798  1.00 60.36           C  
ANISOU  640  CE2 TYR A  84     8880   6646   7409    -68    272    288       C  
ATOM    641  CZ  TYR A  84      49.698  15.485  22.982  1.00 58.71           C  
ANISOU  641  CZ  TYR A  84     8644   6468   7197   -108    220    353       C  
ATOM    642  OH  TYR A  84      50.055  16.814  22.941  1.00 56.89           O  
ANISOU  642  OH  TYR A  84     8424   6282   6909   -202    333    338       O  
ATOM    643  N   GLY A  85      49.790   7.924  22.558  1.00 72.16           N  
ANISOU  643  N   GLY A  85    10261   7847   9311    413   -380    235       N  
ATOM    644  CA  GLY A  85      49.414   6.515  22.551  1.00 71.24           C  
ANISOU  644  CA  GLY A  85    10201   7632   9234    496   -521    253       C  
ATOM    645  C   GLY A  85      47.997   6.213  22.082  1.00 72.13           C  
ANISOU  645  C   GLY A  85    10464   7696   9247    464   -510    346       C  
ATOM    646  O   GLY A  85      47.605   6.589  20.983  1.00 68.55           O  
ANISOU  646  O   GLY A  85    10046   7266   8734    441   -384    321       O  
ATOM    647  N   ASP A  86      47.225   5.549  22.946  1.00 75.90           N  
ANISOU  647  N   ASP A  86    11035   8102   9702    455   -645    448       N  
ATOM    648  CA  ASP A  86      45.845   5.134  22.656  1.00 77.33           C  
ANISOU  648  CA  ASP A  86    11346   8234   9804    419   -652    524       C  
ATOM    649  C   ASP A  86      44.924   6.291  22.254  1.00 73.57           C  
ANISOU  649  C   ASP A  86    10914   7820   9219    334   -523    561       C  
ATOM    650  O   ASP A  86      43.842   6.055  21.741  1.00 73.33           O  
ANISOU  650  O   ASP A  86    10967   7760   9133    318   -511    586       O  
ATOM    651  CB  ASP A  86      45.216   4.446  23.877  1.00 83.25           C  
ANISOU  651  CB  ASP A  86    12190   8911  10532    382   -797    625       C  
ATOM    652  CG  ASP A  86      45.813   3.088  24.163  1.00 94.50           C  
ANISOU  652  CG  ASP A  86    13633  10232  12042    471   -958    602       C  
ATOM    653  OD1 ASP A  86      46.878   2.762  23.598  1.00105.22           O  
ANISOU  653  OD1 ASP A  86    14893  11589  13498    573   -970    494       O  
ATOM    654  OD2 ASP A  86      45.217   2.341  24.975  1.00103.56           O1-
ANISOU  654  OD2 ASP A  86    14898  11294  13156    434  -1077    684       O1-
ATOM    655  N   MET A  87      45.305   7.530  22.535  1.00 68.67           N  
ANISOU  655  N   MET A  87    10244   7278   8570    283   -443    560       N  
ATOM    656  CA  MET A  87      44.478   8.651  22.121  1.00 68.90           C  
ANISOU  656  CA  MET A  87    10328   7353   8499    216   -340    586       C  
ATOM    657  C   MET A  87      44.246   8.641  20.602  1.00 67.15           C  
ANISOU  657  C   MET A  87    10154   7117   8241    248   -250    524       C  
ATOM    658  O   MET A  87      43.180   9.016  20.132  1.00 65.10           O  
ANISOU  658  O   MET A  87     9983   6850   7903    223   -225    546       O  
ATOM    659  CB  MET A  87      45.113   9.976  22.546  1.00 69.06           C  
ANISOU  659  CB  MET A  87    10290   7450   8499    162   -265    581       C  
ATOM    660  CG  MET A  87      44.188  11.164  22.362  1.00 67.02           C  
ANISOU  660  CG  MET A  87    10106   7225   8135     95   -195    617       C  
ATOM    661  SD  MET A  87      44.979  12.652  22.947  1.00 66.42           S  
ANISOU  661  SD  MET A  87     9971   7227   8040     28   -120    615       S  
ATOM    662  CE  MET A  87      43.538  13.672  23.234  1.00 66.94           C  
ANISOU  662  CE  MET A  87    10134   7306   7996    -35   -121    677       C  
ATOM    663  N   ALA A  88      45.269   8.228  19.858  1.00 67.74           N  
ANISOU  663  N   ALA A  88    10169   7191   8377    304   -207    434       N  
ATOM    664  CA  ALA A  88      45.186   8.000  18.416  1.00 67.59           C  
ANISOU  664  CA  ALA A  88    10199   7151   8329    338   -127    366       C  
ATOM    665  C   ALA A  88      44.005   7.119  18.034  1.00 64.61           C  
ANISOU  665  C   ALA A  88     9917   6704   7929    372   -201    400       C  
ATOM    666  O   ALA A  88      43.388   7.343  16.995  1.00 64.79           O  
ANISOU  666  O   ALA A  88    10028   6711   7878    373   -145    380       O  
ATOM    667  CB  ALA A  88      46.478   7.357  17.906  1.00 65.97           C  
ANISOU  667  CB  ALA A  88     9891   6953   8221    399    -97    250       C  
ATOM    668  N   ASP A  89      43.705   6.126  18.858  1.00 62.33           N  
ANISOU  668  N   ASP A  89     9621   6367   7695    393   -329    446       N  
ATOM    669  CA  ASP A  89      42.572   5.240  18.600  1.00 62.75           C  
ANISOU  669  CA  ASP A  89     9759   6352   7731    409   -399    474       C  
ATOM    670  C   ASP A  89      41.244   5.977  18.585  1.00 61.60           C  
ANISOU  670  C   ASP A  89     9691   6222   7493    346   -378    518       C  
ATOM    671  O   ASP A  89      40.305   5.539  17.928  1.00 60.19           O  
ANISOU  671  O   ASP A  89     9579   6002   7287    363   -396    505       O  
ATOM    672  CB  ASP A  89      42.494   4.099  19.630  1.00 65.27           C  
ANISOU  672  CB  ASP A  89    10081   6607   8112    417   -539    524       C  
ATOM    673  CG  ASP A  89      43.623   3.078  19.483  1.00 66.39           C  
ANISOU  673  CG  ASP A  89    10166   6703   8358    511   -604    462       C  
ATOM    674  OD1 ASP A  89      43.998   2.428  20.478  1.00 67.14           O  
ANISOU  674  OD1 ASP A  89    10253   6749   8506    524   -725    494       O  
ATOM    675  OD2 ASP A  89      44.116   2.898  18.361  1.00 72.63           O1-
ANISOU  675  OD2 ASP A  89    10926   7497   9175    573   -541    372       O1-
ATOM    676  N   CYS A  90      41.145   7.111  19.273  1.00 63.02           N  
ANISOU  676  N   CYS A  90     9856   6461   7628    281   -345    556       N  
ATOM    677  CA  CYS A  90      39.899   7.882  19.221  1.00 60.71           C  
ANISOU  677  CA  CYS A  90     9626   6185   7256    234   -334    573       C  
ATOM    678  C   CYS A  90      39.529   8.270  17.809  1.00 59.61           C  
ANISOU  678  C   CYS A  90     9565   6028   7056    274   -277    516       C  
ATOM    679  O   CYS A  90      38.355   8.340  17.491  1.00 60.60           O  
ANISOU  679  O   CYS A  90     9750   6133   7140    275   -310    503       O  
ATOM    680  CB  CYS A  90      39.953   9.110  20.098  1.00 60.78           C  
ANISOU  680  CB  CYS A  90     9606   6259   7227    167   -306    609       C  
ATOM    681  SG  CYS A  90      40.366   8.719  21.815  1.00 65.12           S  
ANISOU  681  SG  CYS A  90    10089   6825   7830    114   -380    679       S  
ATOM    682  N   CYS A  91      40.521   8.472  16.957  1.00 57.68           N  
ANISOU  682  N   CYS A  91     9323   5788   6805    306   -197    470       N  
ATOM    683  CA  CYS A  91      40.267   8.801  15.569  1.00 60.39           C  
ANISOU  683  CA  CYS A  91     9770   6103   7072    336   -140    417       C  
ATOM    684  C   CYS A  91      39.509   7.744  14.756  1.00 61.73           C  
ANISOU  684  C   CYS A  91     9996   6207   7251    397   -196    384       C  
ATOM    685  O   CYS A  91      38.825   8.063  13.778  1.00 61.77           O  
ANISOU  685  O   CYS A  91    10111   6179   7181    421   -190    351       O  
ATOM    686  CB  CYS A  91      41.590   9.104  14.898  1.00 64.31           C  
ANISOU  686  CB  CYS A  91    10252   6621   7561    334    -26    364       C  
ATOM    687  SG  CYS A  91      42.336  10.601  15.591  1.00 69.47           S  
ANISOU  687  SG  CYS A  91    10872   7346   8178    249     56    388       S  
ATOM    688  N   GLU A  92      39.630   6.485  15.149  1.00 62.93           N  
ANISOU  688  N   GLU A  92    10086   6331   7492    426   -260    392       N  
ATOM    689  CA  GLU A  92      38.954   5.409  14.450  1.00 63.25           C  
ANISOU  689  CA  GLU A  92    10174   6307   7550    479   -315    360       C  
ATOM    690  C   GLU A  92      37.466   5.446  14.697  1.00 59.77           C  
ANISOU  690  C   GLU A  92     9777   5851   7082    454   -386    375       C  
ATOM    691  O   GLU A  92      36.733   4.694  14.064  1.00 56.72           O  
ANISOU  691  O   GLU A  92     9436   5413   6703    493   -432    340       O  
ATOM    692  CB  GLU A  92      39.494   4.062  14.908  1.00 70.05           C  
ANISOU  692  CB  GLU A  92    10970   7133   8514    511   -379    366       C  
ATOM    693  CG  GLU A  92      40.941   3.810  14.523  1.00 76.36           C  
ANISOU  693  CG  GLU A  92    11706   7942   9364    558   -325    312       C  
ATOM    694  CD  GLU A  92      41.395   2.425  14.912  1.00 82.94           C  
ANISOU  694  CD  GLU A  92    12489   8722  10303    612   -420    304       C  
ATOM    695  OE1 GLU A  92      42.025   2.300  15.987  1.00 92.17           O  
ANISOU  695  OE1 GLU A  92    13590   9900  11532    600   -472    336       O  
ATOM    696  OE2 GLU A  92      41.109   1.458  14.153  1.00 91.53           O1-
ANISOU  696  OE2 GLU A  92    13616   9748  11413    670   -455    263       O1-
ATOM    697  N   LYS A  93      37.023   6.306  15.619  1.00 58.14           N  
ANISOU  697  N   LYS A  93     9547   5692   6852    390   -393    413       N  
ATOM    698  CA  LYS A  93      35.619   6.371  16.027  1.00 56.22           C  
ANISOU  698  CA  LYS A  93     9313   5449   6597    353   -454    405       C  
ATOM    699  C   LYS A  93      34.856   7.519  15.375  1.00 54.12           C  
ANISOU  699  C   LYS A  93     9116   5193   6255    372   -451    356       C  
ATOM    700  O   LYS A  93      35.447   8.474  14.891  1.00 52.27           O  
ANISOU  700  O   LYS A  93     8932   4970   5959    387   -395    355       O  
ATOM    701  CB  LYS A  93      35.504   6.555  17.535  1.00 56.97           C  
ANISOU  701  CB  LYS A  93     9338   5591   6715    264   -472    461       C  
ATOM    702  CG  LYS A  93      36.209   5.513  18.360  1.00 58.79           C  
ANISOU  702  CG  LYS A  93     9528   5800   7011    240   -503    516       C  
ATOM    703  CD  LYS A  93      36.079   5.805  19.861  1.00 59.21           C  
ANISOU  703  CD  LYS A  93     9540   5895   7063    141   -520    575       C  
ATOM    704  CE  LYS A  93      36.568   4.639  20.718  1.00 59.63           C  
ANISOU  704  CE  LYS A  93     9593   5898   7165    113   -582    630       C  
ATOM    705  NZ  LYS A  93      35.514   4.218  21.689  1.00 61.89           N1+
ANISOU  705  NZ  LYS A  93     9903   6178   7435      1   -618    651       N1+
ATOM    706  N   GLN A  94      33.528   7.417  15.446  1.00 52.87           N  
ANISOU  706  N   GLN A  94     8959   5028   6102    364   -516    307       N  
ATOM    707  CA  GLN A  94      32.594   8.450  15.022  1.00 50.32           C  
ANISOU  707  CA  GLN A  94     8687   4708   5722    390   -553    241       C  
ATOM    708  C   GLN A  94      32.197   9.386  16.163  1.00 52.16           C  
ANISOU  708  C   GLN A  94     8855   5009   5953    322   -558    249       C  
ATOM    709  O   GLN A  94      32.341   9.064  17.340  1.00 50.97           O  
ANISOU  709  O   GLN A  94     8618   4902   5845    241   -541    297       O  
ATOM    710  CB  GLN A  94      31.326   7.811  14.519  1.00 48.46           C  
ANISOU  710  CB  GLN A  94     8462   4437   5514    425   -631    153       C  
ATOM    711  CG  GLN A  94      31.524   7.000  13.284  1.00 49.25           C  
ANISOU  711  CG  GLN A  94     8640   4466   5608    502   -640    129       C  
ATOM    712  CD  GLN A  94      30.310   6.166  12.956  1.00 50.95           C  
ANISOU  712  CD  GLN A  94     8842   4649   5869    523   -718     44       C  
ATOM    713  NE2 GLN A  94      30.545   4.967  12.365  1.00 48.47           N  
ANISOU  713  NE2 GLN A  94     8548   4280   5587    556   -721     45       N  
ATOM    714  OE1 GLN A  94      29.161   6.581  13.239  1.00 52.10           O  
ANISOU  714  OE1 GLN A  94     8948   4818   6028    510   -776    -36       O  
ATOM    715  N   GLU A  95      31.691  10.556  15.799  1.00 55.53           N  
ANISOU  715  N   GLU A  95     9338   5437   6322    356   -589    197       N  
ATOM    716  CA  GLU A  95      31.128  11.476  16.788  1.00 59.43           C  
ANISOU  716  CA  GLU A  95     9769   5994   6819    305   -609    175       C  
ATOM    717  C   GLU A  95      29.750  10.932  17.152  1.00 61.76           C  
ANISOU  717  C   GLU A  95     9983   6308   7175    281   -672     79       C  
ATOM    718  O   GLU A  95      29.097  10.294  16.336  1.00 63.03           O  
ANISOU  718  O   GLU A  95    10172   6422   7354    336   -724      9       O  
ATOM    719  CB  GLU A  95      31.075  12.920  16.250  1.00 58.41           C  
ANISOU  719  CB  GLU A  95     9740   5845   6609    358   -637    143       C  
ATOM    720  CG  GLU A  95      32.462  13.561  16.099  1.00 59.22           C  
ANISOU  720  CG  GLU A  95     9909   5942   6648    342   -550    233       C  
ATOM    721  CD  GLU A  95      33.192  13.840  17.443  1.00 61.86           C  
ANISOU  721  CD  GLU A  95    10136   6355   7014    251   -486    311       C  
ATOM    722  OE1 GLU A  95      32.682  13.452  18.531  1.00 62.64           O  
ANISOU  722  OE1 GLU A  95    10120   6508   7173    192   -502    310       O  
ATOM    723  OE2 GLU A  95      34.309  14.443  17.425  1.00 63.15           O1-
ANISOU  723  OE2 GLU A  95    10332   6524   7137    229   -414    370       O1-
ATOM    724  N   PRO A  96      29.325  11.112  18.390  1.00 60.54           N  
ANISOU  724  N   PRO A  96     9724   6226   7053    188   -660     70       N  
ATOM    725  CA  PRO A  96      29.955  11.745  19.530  1.00 59.64           C  
ANISOU  725  CA  PRO A  96     9561   6174   6925    110   -607    145       C  
ATOM    726  C   PRO A  96      30.981  10.899  20.263  1.00 56.85           C  
ANISOU  726  C   PRO A  96     9182   5826   6591     40   -546    265       C  
ATOM    727  O   PRO A  96      31.646  11.407  21.164  1.00 57.42           O  
ANISOU  727  O   PRO A  96     9224   5943   6651    -15   -507    333       O  
ATOM    728  CB  PRO A  96      28.767  11.995  20.470  1.00 61.94           C  
ANISOU  728  CB  PRO A  96     9749   6534   7250     35   -629     49       C  
ATOM    729  CG  PRO A  96      27.841  10.864  20.184  1.00 63.03           C  
ANISOU  729  CG  PRO A  96     9856   6653   7442     20   -657    -31       C  
ATOM    730  CD  PRO A  96      28.020  10.517  18.729  1.00 61.86           C  
ANISOU  730  CD  PRO A  96     9807   6419   7280    142   -699    -40       C  
ATOM    731  N   GLU A  97      31.092   9.618  19.943  1.00 56.22           N  
ANISOU  731  N   GLU A  97     9117   5698   6546     44   -550    285       N  
ATOM    732  CA  GLU A  97      31.995   8.744  20.713  1.00 57.14           C  
ANISOU  732  CA  GLU A  97     9218   5805   6686    -16   -521    387       C  
ATOM    733  C   GLU A  97      33.449   9.215  20.621  1.00 53.65           C  
ANISOU  733  C   GLU A  97     8795   5363   6227     25   -481    466       C  
ATOM    734  O   GLU A  97      34.210   9.091  21.562  1.00 52.33           O  
ANISOU  734  O   GLU A  97     8596   5215   6071    -27   -467    539       O  
ATOM    735  CB  GLU A  97      31.868   7.274  20.287  1.00 59.88           C  
ANISOU  735  CB  GLU A  97     9594   6085   7075     -5   -548    386       C  
ATOM    736  CG  GLU A  97      30.619   6.563  20.815  1.00 65.18           C  
ANISOU  736  CG  GLU A  97    10234   6760   7770    -99   -570    326       C  
ATOM    737  CD  GLU A  97      29.384   6.595  19.882  1.00 72.05           C  
ANISOU  737  CD  GLU A  97    11097   7623   8656    -50   -606    195       C  
ATOM    738  OE1 GLU A  97      29.482   7.010  18.697  1.00 75.83           O  
ANISOU  738  OE1 GLU A  97    11623   8071   9119     69   -630    158       O  
ATOM    739  OE2 GLU A  97      28.286   6.184  20.342  1.00 74.50           O1-
ANISOU  739  OE2 GLU A  97    11360   7955   8993   -139   -612    117       O1-
ATOM    740  N   ARG A  98      33.821   9.778  19.482  1.00 53.82           N  
ANISOU  740  N   ARG A  98     8873   5361   6215    111   -464    442       N  
ATOM    741  CA  ARG A  98      35.182  10.268  19.278  1.00 52.79           C  
ANISOU  741  CA  ARG A  98     8756   5235   6066    135   -407    493       C  
ATOM    742  C   ARG A  98      35.558  11.326  20.300  1.00 51.60           C  
ANISOU  742  C   ARG A  98     8561   5149   5896     74   -379    532       C  
ATOM    743  O   ARG A  98      36.619  11.245  20.886  1.00 51.28           O  
ANISOU  743  O   ARG A  98     8478   5127   5879     51   -351    589       O  
ATOM    744  CB  ARG A  98      35.334  10.835  17.872  1.00 51.50           C  
ANISOU  744  CB  ARG A  98     8690   5034   5845    211   -381    448       C  
ATOM    745  CG  ARG A  98      36.752  11.224  17.527  1.00 50.63           C  
ANISOU  745  CG  ARG A  98     8594   4929   5715    218   -299    479       C  
ATOM    746  CD  ARG A  98      36.889  11.570  16.062  1.00 50.75           C  
ANISOU  746  CD  ARG A  98     8731   4893   5658    274   -264    433       C  
ATOM    747  NE  ARG A  98      36.217  12.814  15.761  1.00 50.17           N  
ANISOU  747  NE  ARG A  98     8753   4810   5500    278   -286    406       N  
ATOM    748  CZ  ARG A  98      36.460  13.582  14.709  1.00 50.32           C  
ANISOU  748  CZ  ARG A  98     8913   4783   5422    300   -251    382       C  
ATOM    749  NH1 ARG A  98      35.809  14.748  14.578  1.00 52.14           N1+
ANISOU  749  NH1 ARG A  98     9243   4992   5577    307   -299    359       N1+
ATOM    750  NH2 ARG A  98      37.372  13.237  13.825  1.00 50.08           N  
ANISOU  750  NH2 ARG A  98     8936   4726   5365    307   -169    374       N  
ATOM    751  N   ASN A  99      34.688  12.310  20.525  1.00 52.96           N  
ANISOU  751  N   ASN A  99     8738   5353   6031     56   -398    492       N  
ATOM    752  CA  ASN A  99      34.939  13.306  21.583  1.00 53.45           C  
ANISOU  752  CA  ASN A  99     8753   5478   6077     -6   -379    524       C  
ATOM    753  C   ASN A  99      34.908  12.705  22.975  1.00 52.60           C  
ANISOU  753  C   ASN A  99     8568   5409   6007    -95   -389    570       C  
ATOM    754  O   ASN A  99      35.774  13.021  23.785  1.00 52.82           O  
ANISOU  754  O   ASN A  99     8563   5470   6038   -134   -365    631       O  
ATOM    755  CB  ASN A  99      33.957  14.479  21.519  1.00 55.46           C  
ANISOU  755  CB  ASN A  99     9029   5753   6289      2   -411    454       C  
ATOM    756  CG  ASN A  99      34.392  15.662  22.386  1.00 54.75           C  
ANISOU  756  CG  ASN A  99     8910   5718   6172    -46   -385    486       C  
ATOM    757  ND2 ASN A  99      33.492  16.132  23.245  1.00 53.45           N  
ANISOU  757  ND2 ASN A  99     8690   5607   6014    -93   -417    441       N  
ATOM    758  OD1 ASN A  99      35.517  16.153  22.274  1.00 56.38           O  
ANISOU  758  OD1 ASN A  99     9141   5924   6358    -46   -333    539       O  
ATOM    759  N   GLU A 100      33.947  11.834  23.261  1.00 52.55           N  
ANISOU  759  N   GLU A 100     8546   5396   6026   -134   -423    540       N  
ATOM    760  CA  GLU A 100      33.944  11.154  24.560  1.00 56.14           C  
ANISOU  760  CA  GLU A 100     8965   5869   6496   -236   -430    590       C  
ATOM    761  C   GLU A 100      35.283  10.496  24.833  1.00 54.48           C  
ANISOU  761  C   GLU A 100     8765   5623   6310   -223   -434    679       C  
ATOM    762  O   GLU A 100      35.786  10.529  25.952  1.00 55.87           O  
ANISOU  762  O   GLU A 100     8925   5822   6483   -285   -440    738       O  
ATOM    763  CB  GLU A 100      32.838  10.123  24.678  1.00 60.66           C  
ANISOU  763  CB  GLU A 100     9540   6421   7087   -292   -454    543       C  
ATOM    764  CG  GLU A 100      31.416  10.679  24.608  1.00 66.68           C  
ANISOU  764  CG  GLU A 100    10262   7230   7844   -319   -458    425       C  
ATOM    765  CD  GLU A 100      30.355   9.590  24.369  1.00 77.15           C  
ANISOU  765  CD  GLU A 100    11587   8528   9200   -359   -476    353       C  
ATOM    766  OE1 GLU A 100      30.670   8.354  24.501  1.00 83.35           O  
ANISOU  766  OE1 GLU A 100    12416   9255  10000   -394   -484    413       O  
ATOM    767  OE2 GLU A 100      29.190   9.970  24.070  1.00 80.56           O1-
ANISOU  767  OE2 GLU A 100    11973   8992   9645   -355   -490    226       O1-
ATOM    768  N   CYS A 101      35.879   9.965  23.779  1.00 56.28           N  
ANISOU  768  N   CYS A 101     9022   5798   6565   -133   -435    676       N  
ATOM    769  CA  CYS A 101      37.152   9.273  23.846  1.00 57.22           C  
ANISOU  769  CA  CYS A 101     9136   5879   6725    -97   -448    727       C  
ATOM    770  C   CYS A 101      38.306  10.231  24.119  1.00 57.14           C  
ANISOU  770  C   CYS A 101     9083   5913   6714    -85   -409    751       C  
ATOM    771  O   CYS A 101      39.109   9.977  25.043  1.00 56.09           O  
ANISOU  771  O   CYS A 101     8921   5782   6608   -108   -441    800       O  
ATOM    772  CB  CYS A 101      37.396   8.578  22.517  1.00 60.51           C  
ANISOU  772  CB  CYS A 101     9584   6238   7170     -3   -446    689       C  
ATOM    773  SG  CYS A 101      38.855   7.518  22.493  1.00 67.37           S  
ANISOU  773  SG  CYS A 101    10432   7054   8111     59   -480    714       S  
ATOM    774  N   PHE A 102      38.373  11.317  23.323  1.00 51.74           N  
ANISOU  774  N   PHE A 102     8407   5257   5994    -53   -349    714       N  
ATOM    775  CA  PHE A 102      39.355  12.373  23.522  1.00 51.66           C  
ANISOU  775  CA  PHE A 102     8364   5292   5973    -61   -296    726       C  
ATOM    776  C   PHE A 102      39.304  13.003  24.919  1.00 51.22           C  
ANISOU  776  C   PHE A 102     8266   5291   5905   -138   -313    769       C  
ATOM    777  O   PHE A 102      40.312  13.149  25.600  1.00 50.28           O  
ANISOU  777  O   PHE A 102     8097   5194   5813   -152   -313    800       O  
ATOM    778  CB  PHE A 102      39.166  13.505  22.523  1.00 52.02           C  
ANISOU  778  CB  PHE A 102     8465   5343   5956    -38   -237    682       C  
ATOM    779  CG  PHE A 102      39.712  13.227  21.162  1.00 52.28           C  
ANISOU  779  CG  PHE A 102     8546   5334   5984     24   -189    642       C  
ATOM    780  CD1 PHE A 102      40.973  12.706  20.986  1.00 53.02           C  
ANISOU  780  CD1 PHE A 102     8588   5425   6132     46   -152    636       C  
ATOM    781  CD2 PHE A 102      38.966  13.530  20.047  1.00 53.42           C  
ANISOU  781  CD2 PHE A 102     8789   5440   6068     61   -183    598       C  
ATOM    782  CE1 PHE A 102      41.469  12.446  19.724  1.00 52.96           C  
ANISOU  782  CE1 PHE A 102     8620   5386   6116     92    -92    583       C  
ATOM    783  CE2 PHE A 102      39.460  13.296  18.774  1.00 54.42           C  
ANISOU  783  CE2 PHE A 102     8979   5524   6173    107   -131    560       C  
ATOM    784  CZ  PHE A 102      40.716  12.739  18.620  1.00 54.30           C  
ANISOU  784  CZ  PHE A 102     8904   5516   6211    116    -76    551       C  
ATOM    785  N   LEU A 103      38.127  13.403  25.332  1.00 49.79           N  
ANISOU  785  N   LEU A 103     8099   5136   5685   -186   -329    755       N  
ATOM    786  CA  LEU A 103      37.958  13.867  26.690  1.00 50.30           C  
ANISOU  786  CA  LEU A 103     8127   5253   5733   -269   -343    788       C  
ATOM    787  C   LEU A 103      38.549  12.868  27.693  1.00 50.44           C  
ANISOU  787  C   LEU A 103     8134   5249   5782   -306   -393    850       C  
ATOM    788  O   LEU A 103      39.195  13.254  28.659  1.00 51.16           O  
ANISOU  788  O   LEU A 103     8196   5371   5872   -343   -404    891       O  
ATOM    789  CB  LEU A 103      36.453  14.091  26.977  1.00 50.87           C  
ANISOU  789  CB  LEU A 103     8203   5352   5772   -322   -356    738       C  
ATOM    790  CG  LEU A 103      35.855  15.338  26.324  1.00 48.84           C  
ANISOU  790  CG  LEU A 103     7960   5119   5480   -286   -339    670       C  
ATOM    791  CD1 LEU A 103      34.353  15.400  26.542  1.00 49.57           C  
ANISOU  791  CD1 LEU A 103     8035   5238   5564   -323   -366    588       C  
ATOM    792  CD2 LEU A 103      36.553  16.508  26.945  1.00 47.96           C  
ANISOU  792  CD2 LEU A 103     7824   5054   5346   -312   -312    700       C  
ATOM    793  N   SER A 104      38.353  11.577  27.470  1.00 50.76           N  
ANISOU  793  N   SER A 104     8211   5228   5849   -292   -436    857       N  
ATOM    794  CA  SER A 104      38.790  10.607  28.475  1.00 50.63           C  
ANISOU  794  CA  SER A 104     8220   5170   5848   -331   -507    918       C  
ATOM    795  C   SER A 104      40.307  10.499  28.579  1.00 51.24           C  
ANISOU  795  C   SER A 104     8262   5229   5980   -264   -540    940       C  
ATOM    796  O   SER A 104      40.764   9.914  29.524  1.00 52.41           O  
ANISOU  796  O   SER A 104     8436   5342   6136   -288   -617    987       O  
ATOM    797  CB  SER A 104      38.202   9.229  28.229  1.00 49.33           C  
ANISOU  797  CB  SER A 104     8121   4929   5694   -338   -554    919       C  
ATOM    798  OG  SER A 104      39.068   8.473  27.400  1.00 53.20           O  
ANISOU  798  OG  SER A 104     8611   5357   6245   -233   -586    911       O  
ATOM    799  N   HIS A 105      41.079  11.044  27.634  1.00 52.12           N  
ANISOU  799  N   HIS A 105     8319   5360   6125   -187   -484    897       N  
ATOM    800  CA  HIS A 105      42.559  11.074  27.751  1.00 54.80           C  
ANISOU  800  CA  HIS A 105     8592   5701   6527   -132   -500    888       C  
ATOM    801  C   HIS A 105      43.156  12.391  28.277  1.00 54.37           C  
ANISOU  801  C   HIS A 105     8476   5722   6460   -166   -452    888       C  
ATOM    802  O   HIS A 105      44.378  12.519  28.328  1.00 54.71           O  
ANISOU  802  O   HIS A 105     8447   5777   6562   -126   -454    860       O  
ATOM    803  CB  HIS A 105      43.237  10.774  26.400  1.00 57.37           C  
ANISOU  803  CB  HIS A 105     8885   6006   6906    -41   -454    819       C  
ATOM    804  CG  HIS A 105      43.095   9.352  25.942  1.00 58.56           C  
ANISOU  804  CG  HIS A 105     9077   6077   7098     15   -521    810       C  
ATOM    805  CD2 HIS A 105      43.949   8.303  26.005  1.00 59.74           C  
ANISOU  805  CD2 HIS A 105     9206   6168   7326     86   -605    790       C  
ATOM    806  ND1 HIS A 105      41.960   8.884  25.315  1.00 59.52           N  
ANISOU  806  ND1 HIS A 105     9268   6163   7182      8   -513    809       N  
ATOM    807  CE1 HIS A 105      42.121   7.609  25.010  1.00 61.50           C  
ANISOU  807  CE1 HIS A 105     9545   6339   7483     64   -581    799       C  
ATOM    808  NE2 HIS A 105      43.318   7.230  25.424  1.00 60.68           N  
ANISOU  808  NE2 HIS A 105     9391   6216   7449    115   -643    788       N  
ATOM    809  N   LYS A 106      42.314  13.362  28.638  1.00 53.15           N  
ANISOU  809  N   LYS A 106     8341   5618   6237   -235   -411    905       N  
ATOM    810  CA  LYS A 106      42.761  14.582  29.328  1.00 51.78           C  
ANISOU  810  CA  LYS A 106     8120   5508   6044   -278   -380    913       C  
ATOM    811  C   LYS A 106      43.432  14.223  30.648  1.00 52.03           C  
ANISOU  811  C   LYS A 106     8131   5537   6101   -301   -467    957       C  
ATOM    812  O   LYS A 106      42.868  13.521  31.475  1.00 52.21           O  
ANISOU  812  O   LYS A 106     8214   5528   6095   -346   -539   1004       O  
ATOM    813  CB  LYS A 106      41.588  15.523  29.596  1.00 51.76           C  
ANISOU  813  CB  LYS A 106     8149   5551   5966   -345   -346    916       C  
ATOM    814  CG  LYS A 106      41.240  16.426  28.413  1.00 52.75           C  
ANISOU  814  CG  LYS A 106     8297   5686   6059   -316   -269    866       C  
ATOM    815  CD  LYS A 106      40.023  17.289  28.711  1.00 53.97           C  
ANISOU  815  CD  LYS A 106     8478   5876   6152   -363   -265    849       C  
ATOM    816  CE  LYS A 106      39.937  18.480  27.773  1.00 54.68           C  
ANISOU  816  CE  LYS A 106     8607   5968   6202   -336   -212    806       C  
ATOM    817  NZ  LYS A 106      38.657  19.258  27.857  1.00 55.82           N1+
ANISOU  817  NZ  LYS A 106     8782   6131   6297   -352   -232    763       N1+
ATOM    818  N   ASP A 107      44.644  14.707  30.836  1.00 52.12           N  
ANISOU  818  N   ASP A 107     8066   5576   6162   -274   -462    935       N  
ATOM    819  CA  ASP A 107      45.417  14.383  32.003  1.00 53.49           C  
ANISOU  819  CA  ASP A 107     8218   5737   6368   -275   -563    962       C  
ATOM    820  C   ASP A 107      45.208  15.432  33.117  1.00 55.34           C  
ANISOU  820  C   ASP A 107     8450   6031   6545   -357   -557    999       C  
ATOM    821  O   ASP A 107      45.598  16.620  32.975  1.00 52.40           O  
ANISOU  821  O   ASP A 107     8016   5721   6173   -372   -481    969       O  
ATOM    822  CB  ASP A 107      46.871  14.319  31.589  1.00 55.51           C  
ANISOU  822  CB  ASP A 107     8369   5995   6726   -195   -566    890       C  
ATOM    823  CG  ASP A 107      47.712  13.567  32.571  1.00 59.70           C  
ANISOU  823  CG  ASP A 107     8885   6481   7316   -152   -715    896       C  
ATOM    824  OD1 ASP A 107      47.344  13.490  33.759  1.00 58.95           O  
ANISOU  824  OD1 ASP A 107     8863   6370   7166   -206   -799    966       O  
ATOM    825  OD2 ASP A 107      48.764  13.051  32.141  1.00 66.12           O1-
ANISOU  825  OD2 ASP A 107     9618   7273   8231    -63   -751    818       O1-
ATOM    826  N   ASP A 108      44.580  15.008  34.219  1.00 55.31           N  
ANISOU  826  N   ASP A 108     8525   6006   6483   -422   -632   1060       N  
ATOM    827  CA  ASP A 108      44.377  15.899  35.348  1.00 55.51           C  
ANISOU  827  CA  ASP A 108     8555   6087   6450   -504   -631   1091       C  
ATOM    828  C   ASP A 108      45.667  16.109  36.156  1.00 60.10           C  
ANISOU  828  C   ASP A 108     9084   6672   7078   -475   -707   1091       C  
ATOM    829  O   ASP A 108      45.689  16.915  37.087  1.00 61.17           O  
ANISOU  829  O   ASP A 108     9213   6855   7173   -534   -710   1111       O  
ATOM    830  CB  ASP A 108      43.226  15.428  36.228  1.00 54.52           C  
ANISOU  830  CB  ASP A 108     8536   5945   6233   -604   -663   1143       C  
ATOM    831  CG  ASP A 108      41.858  15.763  35.637  1.00 55.98           C  
ANISOU  831  CG  ASP A 108     8733   6167   6371   -652   -569   1113       C  
ATOM    832  OD1 ASP A 108      41.492  16.964  35.551  1.00 55.16           O  
ANISOU  832  OD1 ASP A 108     8580   6133   6244   -676   -497   1080       O  
ATOM    833  OD2 ASP A 108      41.122  14.819  35.266  1.00 59.91           O1-
ANISOU  833  OD2 ASP A 108     9291   6617   6857   -664   -577   1114       O1-
ATOM    834  N   SER A 109      46.743  15.410  35.799  1.00 62.13           N  
ANISOU  834  N   SER A 109     9295   6882   7429   -380   -773   1054       N  
ATOM    835  CA  SER A 109      48.033  15.612  36.460  1.00 66.53           C  
ANISOU  835  CA  SER A 109     9778   7446   8054   -335   -854   1024       C  
ATOM    836  C   SER A 109      49.178  15.385  35.477  1.00 66.42           C  
ANISOU  836  C   SER A 109     9642   7429   8165   -231   -838    924       C  
ATOM    837  O   SER A 109      49.824  14.346  35.500  1.00 74.37           O  
ANISOU  837  O   SER A 109    10644   8368   9245   -146   -956    893       O  
ATOM    838  CB  SER A 109      48.171  14.675  37.652  1.00 68.67           C  
ANISOU  838  CB  SER A 109    10154   7636   8301   -334  -1030   1079       C  
ATOM    839  OG  SER A 109      48.275  13.348  37.198  1.00 77.51           O  
ANISOU  839  OG  SER A 109    11325   8661   9463   -261  -1116   1072       O  
ATOM    840  N   PRO A 110      49.423  16.367  34.601  1.00 64.42           N  
ANISOU  840  N   PRO A 110     9297   7246   7932   -243   -691    864       N  
ATOM    841  CA  PRO A 110      50.365  16.251  33.491  1.00 63.89           C  
ANISOU  841  CA  PRO A 110     9120   7191   7965   -176   -627    756       C  
ATOM    842  C   PRO A 110      51.843  16.155  33.859  1.00 69.05           C  
ANISOU  842  C   PRO A 110     9637   7855   8742   -110   -700    657       C  
ATOM    843  O   PRO A 110      52.642  15.726  33.035  1.00 66.45           O  
ANISOU  843  O   PRO A 110     9212   7525   8511    -43   -675    549       O  
ATOM    844  CB  PRO A 110      50.145  17.529  32.731  1.00 62.99           C  
ANISOU  844  CB  PRO A 110     8985   7145   7804   -243   -452    735       C  
ATOM    845  CG  PRO A 110      48.774  17.956  33.102  1.00 61.94           C  
ANISOU  845  CG  PRO A 110     8968   7014   7551   -315   -438    831       C  
ATOM    846  CD  PRO A 110      48.679  17.628  34.540  1.00 60.90           C  
ANISOU  846  CD  PRO A 110     8872   6866   7401   -332   -571    894       C  
ATOM    847  N   ASP A 111      52.217  16.540  35.075  1.00 76.80           N  
ANISOU  847  N   ASP A 111    10605   8850   9725   -127   -792    678       N  
ATOM    848  CA  ASP A 111      53.627  16.465  35.477  1.00 83.26           C  
ANISOU  848  CA  ASP A 111    11284   9679  10671    -55   -882    567       C  
ATOM    849  C   ASP A 111      54.451  17.314  34.485  1.00 83.38           C  
ANISOU  849  C   ASP A 111    11141   9779  10759    -75   -707    437       C  
ATOM    850  O   ASP A 111      55.455  16.871  33.896  1.00 82.75           O  
ANISOU  850  O   ASP A 111    10930   9707  10806     -4   -706    297       O  
ATOM    851  CB  ASP A 111      54.105  14.996  35.552  1.00 90.43           C  
ANISOU  851  CB  ASP A 111    12198  10493  11666     70  -1061    524       C  
ATOM    852  CG  ASP A 111      53.097  14.072  36.292  1.00 97.58           C  
ANISOU  852  CG  ASP A 111    13307  11298  12470     62  -1201    664       C  
ATOM    853  OD1 ASP A 111      52.724  14.394  37.450  1.00103.17           O  
ANISOU  853  OD1 ASP A 111    14109  11998  13093      0  -1271    754       O  
ATOM    854  OD2 ASP A 111      52.687  13.021  35.726  1.00103.49           O1-
ANISOU  854  OD2 ASP A 111    14128  11976  13220    107  -1236    679       O1-
ATOM    855  N   LEU A 112      53.964  18.538  34.293  1.00 77.12           N  
ANISOU  855  N   LEU A 112    10377   9046   9880   -182   -558    480       N  
ATOM    856  CA  LEU A 112      54.650  19.549  33.528  1.00 73.47           C  
ANISOU  856  CA  LEU A 112     9809   8657   9450   -239   -386    379       C  
ATOM    857  C   LEU A 112      55.421  20.404  34.532  1.00 75.25           C  
ANISOU  857  C   LEU A 112     9942   8935   9716   -271   -421    342       C  
ATOM    858  O   LEU A 112      54.995  20.559  35.676  1.00 71.24           O  
ANISOU  858  O   LEU A 112     9501   8414   9154   -282   -530    435       O  
ATOM    859  CB  LEU A 112      53.635  20.387  32.751  1.00 70.59           C  
ANISOU  859  CB  LEU A 112     9562   8305   8955   -331   -228    450       C  
ATOM    860  CG  LEU A 112      52.927  19.672  31.593  1.00 68.36           C  
ANISOU  860  CG  LEU A 112     9364   7976   8633   -304   -175    467       C  
ATOM    861  CD1 LEU A 112      51.704  20.455  31.165  1.00 64.17           C  
ANISOU  861  CD1 LEU A 112     8977   7441   7965   -377    -85    557       C  
ATOM    862  CD2 LEU A 112      53.870  19.479  30.416  1.00 69.16           C  
ANISOU  862  CD2 LEU A 112     9367   8097   8814   -290    -61    327       C  
ATOM    863  N   PRO A 113      56.573  20.944  34.119  1.00 79.02           N  
ANISOU  863  N   PRO A 113    10262   9473  10289   -293   -325    195       N  
ATOM    864  CA  PRO A 113      57.406  21.687  35.054  1.00 80.75           C  
ANISOU  864  CA  PRO A 113    10373   9742  10567   -316   -367    138       C  
ATOM    865  C   PRO A 113      56.685  22.859  35.701  1.00 80.89           C  
ANISOU  865  C   PRO A 113    10492   9782  10462   -414   -328    256       C  
ATOM    866  O   PRO A 113      55.929  23.555  35.026  1.00 79.51           O  
ANISOU  866  O   PRO A 113    10416   9613  10180   -496   -188    316       O  
ATOM    867  CB  PRO A 113      58.569  22.196  34.191  1.00 82.43           C  
ANISOU  867  CB  PRO A 113    10416  10024  10881   -361   -206    -46       C  
ATOM    868  CG  PRO A 113      58.222  21.904  32.779  1.00 81.47           C  
ANISOU  868  CG  PRO A 113    10347   9889  10719   -385    -56    -64       C  
ATOM    869  CD  PRO A 113      57.172  20.845  32.777  1.00 81.52           C  
ANISOU  869  CD  PRO A 113    10494   9816  10664   -304   -171     63       C  
ATOM    870  N   LYS A 114      56.897  23.053  37.002  1.00 82.22           N  
ANISOU  870  N   LYS A 114    10643   9956  10642   -400   -465    284       N  
ATOM    871  CA  LYS A 114      56.345  24.212  37.690  1.00 81.66           C  
ANISOU  871  CA  LYS A 114    10645   9915  10469   -491   -432    373       C  
ATOM    872  C   LYS A 114      56.992  25.428  37.062  1.00 82.87           C  
ANISOU  872  C   LYS A 114    10711  10132  10643   -586   -252    280       C  
ATOM    873  O   LYS A 114      58.209  25.438  36.849  1.00 88.60           O  
ANISOU  873  O   LYS A 114    11273  10896  11496   -576   -223    129       O  
ATOM    874  CB  LYS A 114      56.634  24.166  39.197  1.00 79.16           C  
ANISOU  874  CB  LYS A 114    10315   9593  10169   -457   -613    399       C  
ATOM    875  N   LEU A 115      56.181  26.431  36.730  1.00 81.09           N  
ANISOU  875  N   LEU A 115    10600   9913  10296   -681   -133    356       N  
ATOM    876  CA  LEU A 115      56.683  27.657  36.114  1.00 77.49           C  
ANISOU  876  CA  LEU A 115    10112   9499   9831   -790     40    285       C  
ATOM    877  C   LEU A 115      57.266  28.537  37.208  1.00 77.52           C  
ANISOU  877  C   LEU A 115    10039   9548   9867   -831     -5    260       C  
ATOM    878  O   LEU A 115      56.641  28.742  38.253  1.00 72.31           O  
ANISOU  878  O   LEU A 115     9446   8882   9147   -820   -113    358       O  
ATOM    879  CB  LEU A 115      55.568  28.390  35.358  1.00 74.57           C  
ANISOU  879  CB  LEU A 115     9921   9099   9315   -862    153    376       C  
ATOM    880  N   LYS A 116      58.481  29.023  36.975  1.00 81.10           N  
ANISOU  880  N   LYS A 116    10345  10051  10418   -882     82    115       N  
ATOM    881  CA  LYS A 116      59.163  29.921  37.911  1.00 85.05           C  
ANISOU  881  CA  LYS A 116    10755  10599  10962   -929     55     66       C  
ATOM    882  C   LYS A 116      59.323  31.289  37.232  1.00 85.24           C  
ANISOU  882  C   LYS A 116    10818  10643  10925  -1081    255     32       C  
ATOM    883  O   LYS A 116      60.278  31.512  36.488  1.00 91.08           O  
ANISOU  883  O   LYS A 116    11453  11416  11736  -1152    395   -111       O  
ATOM    884  CB  LYS A 116      60.524  29.337  38.326  1.00 84.57           C  
ANISOU  884  CB  LYS A 116    10473  10577  11081   -861    -30    -98       C  
ATOM    885  N   PRO A 117      58.380  32.209  37.471  1.00 84.90           N  
ANISOU  885  N   PRO A 117    10934  10575  10748  -1138    270    154       N  
ATOM    886  CA  PRO A 117      58.358  33.414  36.645  1.00 85.92           C  
ANISOU  886  CA  PRO A 117    11160  10693  10794  -1277    449    139       C  
ATOM    887  C   PRO A 117      59.579  34.289  36.859  1.00 87.62           C  
ANISOU  887  C   PRO A 117    11242  10962  11087  -1380    535      8       C  
ATOM    888  O   PRO A 117      59.919  34.595  37.999  1.00 87.12           O  
ANISOU  888  O   PRO A 117    11091  10935  11077  -1361    432     -2       O  
ATOM    889  CB  PRO A 117      57.086  34.134  37.106  1.00 83.86           C  
ANISOU  889  CB  PRO A 117    11077  10392  10393  -1283    393    285       C  
ATOM    890  CG  PRO A 117      56.878  33.675  38.503  1.00 83.97           C  
ANISOU  890  CG  PRO A 117    11029  10432  10444  -1193    209    337       C  
ATOM    891  CD  PRO A 117      57.361  32.249  38.535  1.00 84.87           C  
ANISOU  891  CD  PRO A 117    11028  10553  10664  -1088    125    291       C  
ATOM    892  N   ASP A 118      60.234  34.676  35.765  1.00 90.87           N  
ANISOU  892  N   ASP A 118    11646  11378  11503  -1497    727    -99       N  
ATOM    893  CA  ASP A 118      61.360  35.611  35.820  1.00 92.10           C  
ANISOU  893  CA  ASP A 118    11691  11582  11719  -1632    847   -236       C  
ATOM    894  C   ASP A 118      60.948  36.975  35.255  1.00 88.68           C  
ANISOU  894  C   ASP A 118    11468  11095  11131  -1789    989   -180       C  
ATOM    895  O   ASP A 118      60.673  37.090  34.058  1.00 91.64           O  
ANISOU  895  O   ASP A 118    11995  11417  11408  -1865   1127   -170       O  
ATOM    896  CB  ASP A 118      62.563  35.063  35.044  1.00 96.97           C  
ANISOU  896  CB  ASP A 118    12127  12253  12464  -1675    977   -435       C  
ATOM    897  CG  ASP A 118      63.856  35.792  35.382  1.00101.06           C  
ANISOU  897  CG  ASP A 118    12459  12845  13096  -1788   1063   -613       C  
ATOM    898  OD1 ASP A 118      64.617  35.271  36.234  1.00 99.78           O  
ANISOU  898  OD1 ASP A 118    12070  12743  13097  -1694    934   -719       O  
ATOM    899  OD2 ASP A 118      64.093  36.891  34.816  1.00108.16           O1-
ANISOU  899  OD2 ASP A 118    13449  13732  13916  -1973   1249   -648       O1-
ATOM    900  N   PRO A 119      60.917  38.014  36.107  1.00 83.55           N  
ANISOU  900  N   PRO A 119    10843  10449  10455  -1838    947   -146       N  
ATOM    901  CA  PRO A 119      60.460  39.366  35.747  1.00 82.32           C  
ANISOU  901  CA  PRO A 119    10903  10225  10150  -1971   1040    -83       C  
ATOM    902  C   PRO A 119      61.089  39.972  34.512  1.00 83.21           C  
ANISOU  902  C   PRO A 119    11100  10308  10207  -2158   1273   -178       C  
ATOM    903  O   PRO A 119      60.389  40.604  33.733  1.00 82.13           O  
ANISOU  903  O   PRO A 119    11219  10077   9910  -2229   1339    -97       O  
ATOM    904  CB  PRO A 119      60.851  40.194  36.962  1.00 83.50           C  
ANISOU  904  CB  PRO A 119    10963  10415  10348  -1997    968   -101       C  
ATOM    905  CG  PRO A 119      60.770  39.233  38.085  1.00 83.60           C  
ANISOU  905  CG  PRO A 119    10818  10483  10464  -1827    770    -77       C  
ATOM    906  CD  PRO A 119      61.250  37.923  37.535  1.00 83.86           C  
ANISOU  906  CD  PRO A 119    10719  10546  10598  -1755    783   -158       C  
ATOM    907  N   ASN A 120      62.400  39.802  34.364  1.00 87.30           N  
ANISOU  907  N   ASN A 120    11410  10903  10855  -2240   1390   -359       N  
ATOM    908  CA  ASN A 120      63.110  40.254  33.174  1.00 92.06           C  
ANISOU  908  CA  ASN A 120    12072  11492  11414  -2440   1637   -478       C  
ATOM    909  C   ASN A 120      62.590  39.602  31.924  1.00 91.94           C  
ANISOU  909  C   ASN A 120    12209  11421  11305  -2431   1715   -440       C  
ATOM    910  O   ASN A 120      62.097  40.289  31.029  1.00 93.74           O  
ANISOU  910  O   ASN A 120    12709  11549  11356  -2546   1822   -374       O  
ATOM    911  CB  ASN A 120      64.607  39.946  33.258  1.00 96.30           C  
ANISOU  911  CB  ASN A 120    12307  12145  12140  -2508   1741   -712       C  
ATOM    912  CG  ASN A 120      65.408  41.095  33.822  1.00 99.59           C  
ANISOU  912  CG  ASN A 120    12651  12595  12594  -2659   1813   -807       C  
ATOM    913  ND2 ASN A 120      66.686  41.151  33.445  1.00101.48           N  
ANISOU  913  ND2 ASN A 120    12700  12913  12946  -2803   1992  -1034       N  
ATOM    914  OD1 ASN A 120      64.891  41.925  34.590  1.00 97.62           O  
ANISOU  914  OD1 ASN A 120    12509  12305  12278  -2650   1711   -690       O  
ATOM    915  N   THR A 121      62.714  38.278  31.864  1.00 89.10           N  
ANISOU  915  N   THR A 121    11683  11114  11059  -2291   1652   -485       N  
ATOM    916  CA  THR A 121      62.369  37.554  30.650  1.00 89.46           C  
ANISOU  916  CA  THR A 121    11837  11117  11036  -2283   1736   -477       C  
ATOM    917  C   THR A 121      60.893  37.768  30.346  1.00 85.52           C  
ANISOU  917  C   THR A 121    11636  10503  10355  -2220   1646   -271       C  
ATOM    918  O   THR A 121      60.513  37.874  29.183  1.00 85.72           O  
ANISOU  918  O   THR A 121    11875  10451  10244  -2293   1757   -244       O  
ATOM    919  CB  THR A 121      62.675  36.034  30.720  1.00 90.12           C  
ANISOU  919  CB  THR A 121    11693  11269  11278  -2120   1651   -553       C  
ATOM    920  CG2 THR A 121      64.061  35.757  31.284  1.00 92.38           C  
ANISOU  920  CG2 THR A 121    11653  11671  11777  -2128   1668   -765       C  
ATOM    921  OG1 THR A 121      61.702  35.385  31.533  1.00 95.90           O  
ANISOU  921  OG1 THR A 121    12442  11979  12018  -1920   1415   -399       O  
ATOM    922  N   LEU A 122      60.061  37.825  31.381  1.00 81.47           N  
ANISOU  922  N   LEU A 122    11139   9978   9839  -2087   1445   -140       N  
ATOM    923  CA  LEU A 122      58.633  38.012  31.158  1.00 81.46           C  
ANISOU  923  CA  LEU A 122    11389   9876   9685  -2017   1348     28       C  
ATOM    924  C   LEU A 122      58.372  39.422  30.619  1.00 82.19           C  
ANISOU  924  C   LEU A 122    11747   9871   9609  -2171   1442     67       C  
ATOM    925  O   LEU A 122      57.608  39.602  29.655  1.00 82.06           O  
ANISOU  925  O   LEU A 122    11985   9752   9444  -2188   1469    135       O  
ATOM    926  CB  LEU A 122      57.810  37.707  32.423  1.00 78.12           C  
ANISOU  926  CB  LEU A 122    10905   9475   9302  -1851   1124    137       C  
ATOM    927  CG  LEU A 122      57.707  36.221  32.830  1.00 80.08           C  
ANISOU  927  CG  LEU A 122    10984   9777   9667  -1686   1001    141       C  
ATOM    928  CD1 LEU A 122      57.235  36.073  34.280  1.00 78.88           C  
ANISOU  928  CD1 LEU A 122    10751   9660   9561  -1573    806    218       C  
ATOM    929  CD2 LEU A 122      56.825  35.375  31.906  1.00 77.78           C  
ANISOU  929  CD2 LEU A 122    10819   9428   9307  -1609    989    205       C  
ATOM    930  N   CYS A 123      59.007  40.421  31.221  1.00 80.78           N  
ANISOU  930  N   CYS A 123    11527   9714   9450  -2281   1482     21       N  
ATOM    931  CA  CYS A 123      58.806  41.794  30.759  1.00 81.47           C  
ANISOU  931  CA  CYS A 123    11883   9696   9377  -2433   1562     56       C  
ATOM    932  C   CYS A 123      59.386  42.022  29.354  1.00 81.07           C  
ANISOU  932  C   CYS A 123    11987   9589   9226  -2622   1790    -23       C  
ATOM    933  O   CYS A 123      58.881  42.860  28.611  1.00 81.41           O  
ANISOU  933  O   CYS A 123    12343   9502   9087  -2716   1833     39       O  
ATOM    934  CB  CYS A 123      59.350  42.814  31.769  1.00 82.64           C  
ANISOU  934  CB  CYS A 123    11951   9879   9571  -2510   1549     24       C  
ATOM    935  SG  CYS A 123      58.196  43.203  33.117  1.00 80.77           S  
ANISOU  935  SG  CYS A 123    11735   9630   9325  -2344   1294    163       S  
ATOM    936  N   ASP A 124      60.429  41.279  28.989  1.00 81.50           N  
ANISOU  936  N   ASP A 124    11835   9736   9393  -2677   1931   -168       N  
ATOM    937  CA  ASP A 124      60.971  41.341  27.631  1.00 84.44           C  
ANISOU  937  CA  ASP A 124    12341  10069   9672  -2860   2163   -259       C  
ATOM    938  C   ASP A 124      59.940  40.778  26.653  1.00 83.68           C  
ANISOU  938  C   ASP A 124    12474   9877   9445  -2773   2120   -155       C  
ATOM    939  O   ASP A 124      59.555  41.446  25.681  1.00 84.66           O  
ANISOU  939  O   ASP A 124    12924   9871   9372  -2891   2201   -106       O  
ATOM    940  CB  ASP A 124      62.301  40.573  27.507  1.00 86.64           C  
ANISOU  940  CB  ASP A 124    12306  10485  10126  -2920   2314   -465       C  
ATOM    941  CG  ASP A 124      63.478  41.264  28.236  1.00 90.28           C  
ANISOU  941  CG  ASP A 124    12560  11035  10706  -3055   2402   -610       C  
ATOM    942  OD1 ASP A 124      63.474  42.510  28.419  1.00 92.62           O  
ANISOU  942  OD1 ASP A 124    13020  11268  10902  -3194   2441   -573       O  
ATOM    943  OD2 ASP A 124      64.433  40.548  28.621  1.00 91.95           O1-
ANISOU  943  OD2 ASP A 124    12439  11378  11118  -3020   2424   -774       O1-
ATOM    944  N   GLU A 125      59.464  39.569  26.948  1.00 82.89           N  
ANISOU  944  N   GLU A 125    12216   9830   9448  -2564   1978   -118       N  
ATOM    945  CA  GLU A 125      58.487  38.863  26.101  1.00 82.07           C  
ANISOU  945  CA  GLU A 125    12283   9651   9250  -2458   1922    -31       C  
ATOM    946  C   GLU A 125      57.223  39.695  25.884  1.00 79.50           C  
ANISOU  946  C   GLU A 125    12290   9178   8738  -2430   1808    121       C  
ATOM    947  O   GLU A 125      56.650  39.717  24.786  1.00 79.44           O  
ANISOU  947  O   GLU A 125    12546   9061   8577  -2453   1839    165       O  
ATOM    948  CB  GLU A 125      58.136  37.493  26.710  1.00 81.54           C  
ANISOU  948  CB  GLU A 125    11982   9666   9336  -2235   1760     -8       C  
ATOM    949  CG  GLU A 125      59.279  36.468  26.702  1.00 82.73           C  
ANISOU  949  CG  GLU A 125    11831   9938   9665  -2229   1847   -167       C  
ATOM    950  CD  GLU A 125      58.982  35.196  27.503  1.00 83.36           C  
ANISOU  950  CD  GLU A 125    11693  10084   9897  -2009   1656   -138       C  
ATOM    951  OE1 GLU A 125      59.585  34.140  27.196  1.00 84.74           O  
ANISOU  951  OE1 GLU A 125    11690  10320  10186  -1963   1694   -245       O  
ATOM    952  OE2 GLU A 125      58.142  35.222  28.434  1.00 82.30           O1-
ANISOU  952  OE2 GLU A 125    11571   9936   9764  -1884   1468    -14       O1-
ATOM    953  N   PHE A 126      56.827  40.406  26.931  1.00 76.81           N  
ANISOU  953  N   PHE A 126    11938   8834   8412  -2380   1671    188       N  
ATOM    954  CA  PHE A 126      55.640  41.242  26.904  1.00 76.61           C  
ANISOU  954  CA  PHE A 126    12190   8679   8238  -2333   1535    310       C  
ATOM    955  C   PHE A 126      55.792  42.451  25.977  1.00 81.60           C  
ANISOU  955  C   PHE A 126    13157   9170   8676  -2527   1656    308       C  
ATOM    956  O   PHE A 126      54.945  42.680  25.110  1.00 84.77           O  
ANISOU  956  O   PHE A 126    13858   9434   8918  -2508   1608    375       O  
ATOM    957  CB  PHE A 126      55.317  41.705  28.322  1.00 73.07           C  
ANISOU  957  CB  PHE A 126    11616   8279   7869  -2246   1376    356       C  
ATOM    958  CG  PHE A 126      54.152  42.647  28.402  1.00 71.26           C  
ANISOU  958  CG  PHE A 126    11641   7926   7507  -2195   1230    453       C  
ATOM    959  CD1 PHE A 126      54.350  44.011  28.515  1.00 70.61           C  
ANISOU  959  CD1 PHE A 126    11727   7766   7334  -2321   1255    455       C  
ATOM    960  CD2 PHE A 126      52.861  42.169  28.381  1.00 70.17           C  
ANISOU  960  CD2 PHE A 126    11567   7750   7343  -2019   1061    529       C  
ATOM    961  CE1 PHE A 126      53.278  44.882  28.603  1.00 69.73           C  
ANISOU  961  CE1 PHE A 126    11847   7536   7111  -2258   1100    529       C  
ATOM    962  CE2 PHE A 126      51.784  43.033  28.451  1.00 71.26           C  
ANISOU  962  CE2 PHE A 126    11922   7779   7376  -1960    915    590       C  
ATOM    963  CZ  PHE A 126      51.997  44.401  28.551  1.00 69.69           C  
ANISOU  963  CZ  PHE A 126    11895   7496   7087  -2075    928    589       C  
ATOM    964  N   LYS A 127      56.853  43.236  26.169  1.00 84.98           N  
ANISOU  964  N   LYS A 127    13549   9624   9115  -2715   1804    228       N  
ATOM    965  CA  LYS A 127      57.117  44.379  25.275  1.00 88.39           C  
ANISOU  965  CA  LYS A 127    14316   9916   9352  -2935   1942    219       C  
ATOM    966  C   LYS A 127      57.256  43.874  23.838  1.00 87.74           C  
ANISOU  966  C   LYS A 127    14410   9774   9154  -3026   2095    184       C  
ATOM    967  O   LYS A 127      56.729  44.477  22.903  1.00 85.10           O  
ANISOU  967  O   LYS A 127    14454   9271   8609  -3097   2099    242       O  
ATOM    968  CB  LYS A 127      58.379  45.161  25.680  1.00 87.13           C  
ANISOU  968  CB  LYS A 127    14050   9814   9240  -3148   2112    112       C  
ATOM    969  N   ALA A 128      57.945  42.748  23.682  1.00 86.48           N  
ANISOU  969  N   ALA A 128    13980   9747   9130  -3013   2204     85       N  
ATOM    970  CA  ALA A 128      58.238  42.226  22.366  1.00 89.63           C  
ANISOU  970  CA  ALA A 128    14503  10114   9437  -3115   2376     25       C  
ATOM    971  C   ALA A 128      56.944  41.942  21.602  1.00 91.06           C  
ANISOU  971  C   ALA A 128    14967  10159   9472  -2978   2232    148       C  
ATOM    972  O   ALA A 128      56.768  42.432  20.481  1.00 89.67           O  
ANISOU  972  O   ALA A 128    15147   9838   9085  -3106   2314    167       O  
ATOM    973  CB  ALA A 128      59.094  40.973  22.475  1.00 89.71           C  
ANISOU  973  CB  ALA A 128    14136  10298   9649  -3076   2473   -109       C  
ATOM    974  N   ASP A 129      56.038  41.165  22.208  1.00 87.83           N  
ANISOU  974  N   ASP A 129    14411   9793   9169  -2726   2016    224       N  
ATOM    975  CA  ASP A 129      54.805  40.783  21.533  1.00 83.86           C  
ANISOU  975  CA  ASP A 129    14126   9180   8557  -2581   1872    319       C  
ATOM    976  C   ASP A 129      53.700  40.475  22.526  1.00 82.39           C  
ANISOU  976  C   ASP A 129    13816   9020   8467  -2338   1613    410       C  
ATOM    977  O   ASP A 129      53.580  39.351  23.020  1.00 85.34           O  
ANISOU  977  O   ASP A 129    13919   9508   8997  -2191   1548    403       O  
ATOM    978  CB  ASP A 129      55.059  39.590  20.601  1.00 83.81           C  
ANISOU  978  CB  ASP A 129    14061   9214   8568  -2570   1982    259       C  
ATOM    979  CG  ASP A 129      53.864  39.276  19.706  1.00 84.24           C  
ANISOU  979  CG  ASP A 129    14385   9138   8486  -2452   1857    344       C  
ATOM    980  OD1 ASP A 129      52.815  39.939  19.856  1.00 79.77           O  
ANISOU  980  OD1 ASP A 129    14028   8456   7826  -2362   1671    440       O  
ATOM    981  OD2 ASP A 129      53.971  38.359  18.848  1.00 87.00           O1-
ANISOU  981  OD2 ASP A 129    14731   9500   8825  -2444   1938    303       O1-
ATOM    982  N   GLU A 130      52.860  41.476  22.767  1.00 83.37           N  
ANISOU  982  N   GLU A 130    14158   9030   8489  -2301   1464    488       N  
ATOM    983  CA  GLU A 130      51.764  41.395  23.739  1.00 81.62           C  
ANISOU  983  CA  GLU A 130    13839   8829   8344  -2095   1226    557       C  
ATOM    984  C   GLU A 130      50.691  40.336  23.445  1.00 81.97           C  
ANISOU  984  C   GLU A 130    13863   8870   8413  -1901   1089    595       C  
ATOM    985  O   GLU A 130      50.256  39.630  24.360  1.00 81.75           O  
ANISOU  985  O   GLU A 130    13589   8945   8525  -1754    976    611       O  
ATOM    986  CB  GLU A 130      51.083  42.758  23.881  1.00 83.65           C  
ANISOU  986  CB  GLU A 130    14365   8946   8471  -2102   1099    609       C  
ATOM    987  CG  GLU A 130      51.959  43.824  24.537  1.00 90.81           C  
ANISOU  987  CG  GLU A 130    15247   9870   9386  -2258   1185    582       C  
ATOM    988  CD  GLU A 130      51.176  45.032  25.050  1.00 94.02           C  
ANISOU  988  CD  GLU A 130    15834  10170   9718  -2212   1009    631       C  
ATOM    989  OE1 GLU A 130      50.035  44.849  25.538  1.00 97.76           O  
ANISOU  989  OE1 GLU A 130    16269  10643  10233  -2019    804    668       O  
ATOM    990  OE2 GLU A 130      51.708  46.163  24.973  1.00 91.53           O1-
ANISOU  990  OE2 GLU A 130    15697   9772   9308  -2374   1079    621       O1-
ATOM    991  N   LYS A 131      50.235  40.233  22.201  1.00 79.92           N  
ANISOU  991  N   LYS A 131    13869   8487   8010  -1904   1094    608       N  
ATOM    992  CA  LYS A 131      49.208  39.237  21.875  1.00 78.15           C  
ANISOU  992  CA  LYS A 131    13628   8256   7810  -1723    964    634       C  
ATOM    993  C   LYS A 131      49.769  37.812  22.055  1.00 76.34           C  
ANISOU  993  C   LYS A 131    13086   8178   7741  -1683   1050    595       C  
ATOM    994  O   LYS A 131      49.076  36.933  22.576  1.00 75.94           O  
ANISOU  994  O   LYS A 131    12863   8193   7799  -1522    925    617       O  
ATOM    995  CB  LYS A 131      48.626  39.453  20.459  1.00 81.06           C  
ANISOU  995  CB  LYS A 131    14367   8448   7983  -1733    942    650       C  
ATOM    996  CG  LYS A 131      47.446  38.550  20.067  1.00 81.68           C  
ANISOU  996  CG  LYS A 131    14458   8502   8076  -1541    785    670       C  
ATOM    997  CD  LYS A 131      46.128  38.922  20.742  1.00 81.40           C  
ANISOU  997  CD  LYS A 131    14432   8430   8066  -1369    538    698       C  
ATOM    998  N   LYS A 132      51.016  37.584  21.644  1.00 74.99           N  
ANISOU  998  N   LYS A 132    12843   8062   7589  -1830   1259    526       N  
ATOM    999  CA  LYS A 132      51.659  36.272  21.804  1.00 73.31           C  
ANISOU  999  CA  LYS A 132    12332   7985   7536  -1790   1334    469       C  
ATOM   1000  C   LYS A 132      51.869  35.959  23.294  1.00 71.06           C  
ANISOU 1000  C   LYS A 132    11725   7836   7438  -1709   1251    470       C  
ATOM   1001  O   LYS A 132      51.731  34.822  23.735  1.00 65.61           O  
ANISOU 1001  O   LYS A 132    10822   7229   6878  -1586   1184    469       O  
ATOM   1002  CB  LYS A 132      52.991  36.239  21.057  1.00 75.71           C  
ANISOU 1002  CB  LYS A 132    12623   8320   7823  -1977   1581    364       C  
ATOM   1003  CG  LYS A 132      53.812  34.969  21.243  1.00 77.99           C  
ANISOU 1003  CG  LYS A 132    12589   8752   8292  -1941   1658    275       C  
ATOM   1004  CD  LYS A 132      55.173  35.107  20.545  1.00 84.38           C  
ANISOU 1004  CD  LYS A 132    13372   9600   9088  -2146   1916    139       C  
ATOM   1005  CE  LYS A 132      55.804  33.772  20.144  1.00 86.81           C  
ANISOU 1005  CE  LYS A 132    13458  10004   9521  -2107   2002     32       C  
ATOM   1006  NZ  LYS A 132      56.289  32.909  21.258  1.00 86.62           N1+
ANISOU 1006  NZ  LYS A 132    13062  10120   9732  -1985   1922    -18       N1+
ATOM   1007  N   PHE A 133      52.211  36.982  24.062  1.00 69.97           N  
ANISOU 1007  N   PHE A 133    11572   7709   7303  -1784   1252    473       N  
ATOM   1008  CA  PHE A 133      52.413  36.836  25.505  1.00 67.43           C  
ANISOU 1008  CA  PHE A 133    10979   7503   7137  -1718   1168    476       C  
ATOM   1009  C   PHE A 133      51.151  36.309  26.177  1.00 63.82           C  
ANISOU 1009  C   PHE A 133    10474   7054   6719  -1534    963    554       C  
ATOM   1010  O   PHE A 133      51.177  35.369  26.973  1.00 64.63           O  
ANISOU 1010  O   PHE A 133    10348   7254   6956  -1439    898    555       O  
ATOM   1011  CB  PHE A 133      52.773  38.209  26.081  1.00 66.76           C  
ANISOU 1011  CB  PHE A 133    10955   7400   7012  -1830   1188    476       C  
ATOM   1012  CG  PHE A 133      53.164  38.184  27.525  1.00 64.99           C  
ANISOU 1012  CG  PHE A 133    10466   7291   6935  -1791   1124    466       C  
ATOM   1013  CD1 PHE A 133      54.436  37.775  27.906  1.00 65.51           C  
ANISOU 1013  CD1 PHE A 133    10287   7468   7135  -1852   1229    374       C  
ATOM   1014  CD2 PHE A 133      52.270  38.598  28.501  1.00 62.04           C  
ANISOU 1014  CD2 PHE A 133    10091   6915   6565  -1695    955    536       C  
ATOM   1015  CE1 PHE A 133      54.813  37.783  29.242  1.00 64.32           C  
ANISOU 1015  CE1 PHE A 133     9913   7414   7113  -1813   1153    363       C  
ATOM   1016  CE2 PHE A 133      52.640  38.603  29.829  1.00 61.88           C  
ANISOU 1016  CE2 PHE A 133     9851   6996   6665  -1669    897    528       C  
ATOM   1017  CZ  PHE A 133      53.910  38.191  30.202  1.00 62.39           C  
ANISOU 1017  CZ  PHE A 133     9690   7161   6856  -1725    990    448       C  
ATOM   1018  N   TRP A 134      50.052  36.962  25.841  1.00 61.25           N  
ANISOU 1018  N   TRP A 134    10380   6620   6271  -1492    861    608       N  
ATOM   1019  CA  TRP A 134      48.720  36.616  26.278  1.00 61.07           C  
ANISOU 1019  CA  TRP A 134    10352   6589   6262  -1334    678    659       C  
ATOM   1020  C   TRP A 134      48.399  35.204  25.894  1.00 63.62           C  
ANISOU 1020  C   TRP A 134    10584   6945   6645  -1236    660    659       C  
ATOM   1021  O   TRP A 134      47.946  34.408  26.718  1.00 63.60           O  
ANISOU 1021  O   TRP A 134    10406   7018   6743  -1135    564    678       O  
ATOM   1022  CB  TRP A 134      47.802  37.585  25.586  1.00 61.16           C  
ANISOU 1022  CB  TRP A 134    10664   6456   6120  -1323    598    682       C  
ATOM   1023  CG  TRP A 134      46.343  37.542  25.874  1.00 58.37           C  
ANISOU 1023  CG  TRP A 134    10349   6071   5760  -1173    406    705       C  
ATOM   1024  CD1 TRP A 134      45.652  38.203  26.884  1.00 58.64           C  
ANISOU 1024  CD1 TRP A 134    10341   6121   5817  -1116    275    711       C  
ATOM   1025  CD2 TRP A 134      45.329  36.940  25.042  1.00 58.99           C  
ANISOU 1025  CD2 TRP A 134    10540   6082   5793  -1065    320    706       C  
ATOM   1026  CE2 TRP A 134      44.041  37.246  25.673  1.00 59.01           C  
ANISOU 1026  CE2 TRP A 134    10537   6074   5810   -944    136    700       C  
ATOM   1027  CE3 TRP A 134      45.349  36.170  23.887  1.00 58.34           C  
ANISOU 1027  CE3 TRP A 134    10547   5952   5666  -1055    375    699       C  
ATOM   1028  NE1 TRP A 134      44.304  37.988  26.781  1.00 57.84           N  
ANISOU 1028  NE1 TRP A 134    10291   5982   5703   -982    122    703       N  
ATOM   1029  CZ2 TRP A 134      42.846  36.776  25.152  1.00 56.45           C  
ANISOU 1029  CZ2 TRP A 134    10284   5699   5467   -819     13    681       C  
ATOM   1030  CZ3 TRP A 134      44.142  35.708  23.382  1.00 56.27           C  
ANISOU 1030  CZ3 TRP A 134    10368   5632   5378   -926    244    695       C  
ATOM   1031  CH2 TRP A 134      42.925  35.992  24.010  1.00 55.75           C  
ANISOU 1031  CH2 TRP A 134    10283   5562   5338   -810     67    682       C  
ATOM   1032  N   GLY A 135      48.677  34.856  24.643  1.00 65.65           N  
ANISOU 1032  N   GLY A 135    10963   7145   6835  -1276    759    634       N  
ATOM   1033  CA  GLY A 135      48.427  33.501  24.153  1.00 65.17           C  
ANISOU 1033  CA  GLY A 135    10828   7106   6825  -1188    750    627       C  
ATOM   1034  C   GLY A 135      49.166  32.406  24.904  1.00 64.95           C  
ANISOU 1034  C   GLY A 135    10509   7206   6964  -1158    775    601       C  
ATOM   1035  O   GLY A 135      48.609  31.349  25.172  1.00 65.13           O  
ANISOU 1035  O   GLY A 135    10428   7260   7057  -1046    686    621       O  
ATOM   1036  N   LYS A 136      50.412  32.670  25.275  1.00 66.52           N  
ANISOU 1036  N   LYS A 136    10579   7470   7225  -1257    886    548       N  
ATOM   1037  CA  LYS A 136      51.223  31.697  25.992  1.00 67.42           C  
ANISOU 1037  CA  LYS A 136    10422   7693   7501  -1222    892    505       C  
ATOM   1038  C   LYS A 136      50.706  31.511  27.424  1.00 63.22           C  
ANISOU 1038  C   LYS A 136     9755   7217   7049  -1132    735    562       C  
ATOM   1039  O   LYS A 136      50.702  30.398  27.955  1.00 62.96           O  
ANISOU 1039  O   LYS A 136     9569   7235   7117  -1045    663    567       O  
ATOM   1040  CB  LYS A 136      52.705  32.099  25.976  1.00 73.45           C  
ANISOU 1040  CB  LYS A 136    11079   8513   8317  -1353   1048    407       C  
ATOM   1041  CG  LYS A 136      53.629  31.055  26.581  1.00 78.11           C  
ANISOU 1041  CG  LYS A 136    11391   9205   9083  -1305   1043    335       C  
ATOM   1042  CD  LYS A 136      54.920  30.802  25.797  1.00 83.09           C  
ANISOU 1042  CD  LYS A 136    11930   9875   9765  -1400   1222    194       C  
ATOM   1043  CE  LYS A 136      55.577  29.492  26.272  1.00 84.79           C  
ANISOU 1043  CE  LYS A 136    11885  10172  10161  -1297   1165    120       C  
ATOM   1044  NZ  LYS A 136      56.912  29.163  25.683  1.00 88.55           N1+
ANISOU 1044  NZ  LYS A 136    12209  10707  10727  -1371   1322    -53       N1+
ATOM   1045  N   TYR A 137      50.211  32.574  28.033  1.00 58.82           N  
ANISOU 1045  N   TYR A 137     9272   6641   6435  -1154    677    605       N  
ATOM   1046  CA  TYR A 137      49.575  32.417  29.342  1.00 56.14           C  
ANISOU 1046  CA  TYR A 137     8830   6352   6150  -1077    534    655       C  
ATOM   1047  C   TYR A 137      48.338  31.507  29.232  1.00 53.15           C  
ANISOU 1047  C   TYR A 137     8483   5951   5762   -964    427    699       C  
ATOM   1048  O   TYR A 137      48.241  30.518  29.940  1.00 55.35           O  
ANISOU 1048  O   TYR A 137     8627   6281   6123   -902    358    715       O  
ATOM   1049  CB  TYR A 137      49.207  33.784  29.955  1.00 55.71           C  
ANISOU 1049  CB  TYR A 137     8856   6279   6032  -1120    493    679       C  
ATOM   1050  CG  TYR A 137      48.488  33.669  31.265  1.00 53.91           C  
ANISOU 1050  CG  TYR A 137     8534   6104   5845  -1054    360    719       C  
ATOM   1051  CD1 TYR A 137      49.189  33.578  32.454  1.00 57.10           C  
ANISOU 1051  CD1 TYR A 137     8768   6590   6337  -1069    338    715       C  
ATOM   1052  CD2 TYR A 137      47.105  33.601  31.316  1.00 53.32           C  
ANISOU 1052  CD2 TYR A 137     8539   5999   5722   -978    256    750       C  
ATOM   1053  CE1 TYR A 137      48.528  33.428  33.664  1.00 56.75           C  
ANISOU 1053  CE1 TYR A 137     8656   6593   6314  -1022    223    751       C  
ATOM   1054  CE2 TYR A 137      46.432  33.464  32.508  1.00 52.50           C  
ANISOU 1054  CE2 TYR A 137     8348   5951   5649   -936    153    772       C  
ATOM   1055  CZ  TYR A 137      47.152  33.373  33.678  1.00 55.78           C  
ANISOU 1055  CZ  TYR A 137     8615   6445   6136   -964    142    778       C  
ATOM   1056  OH  TYR A 137      46.494  33.243  34.872  1.00 60.83           O  
ANISOU 1056  OH  TYR A 137     9187   7136   6788   -939     50    800       O  
ATOM   1057  N   LEU A 138      47.390  31.839  28.359  1.00 51.29           N  
ANISOU 1057  N   LEU A 138     8432   5631   5424   -940    405    712       N  
ATOM   1058  CA  LEU A 138      46.298  30.919  28.039  1.00 51.38           C  
ANISOU 1058  CA  LEU A 138     8471   5620   5432   -840    322    731       C  
ATOM   1059  C   LEU A 138      46.800  29.475  27.872  1.00 52.08           C  
ANISOU 1059  C   LEU A 138     8433   5746   5610   -802    349    721       C  
ATOM   1060  O   LEU A 138      46.193  28.536  28.344  1.00 51.95           O  
ANISOU 1060  O   LEU A 138     8343   5754   5643   -733    265    744       O  
ATOM   1061  CB  LEU A 138      45.609  31.354  26.742  1.00 50.86           C  
ANISOU 1061  CB  LEU A 138     8630   5446   5249   -827    324    721       C  
ATOM   1062  CG  LEU A 138      44.747  32.603  26.859  1.00 50.30           C  
ANISOU 1062  CG  LEU A 138     8706   5314   5091   -820    241    724       C  
ATOM   1063  CD1 LEU A 138      43.997  32.849  25.563  1.00 48.78           C  
ANISOU 1063  CD1 LEU A 138     8746   5001   4786   -782    208    710       C  
ATOM   1064  CD2 LEU A 138      43.756  32.455  28.020  1.00 48.75           C  
ANISOU 1064  CD2 LEU A 138     8396   5177   4948   -751    114    732       C  
ATOM   1065  N   TYR A 139      47.910  29.315  27.177  1.00 52.95           N  
ANISOU 1065  N   TYR A 139     8524   5857   5739   -855    467    676       N  
ATOM   1066  CA  TYR A 139      48.436  28.019  26.872  1.00 53.66           C  
ANISOU 1066  CA  TYR A 139     8504   5972   5912   -814    492    646       C  
ATOM   1067  C   TYR A 139      48.945  27.342  28.117  1.00 55.06           C  
ANISOU 1067  C   TYR A 139     8483   6226   6212   -781    425    650       C  
ATOM   1068  O   TYR A 139      48.632  26.169  28.355  1.00 59.57           O  
ANISOU 1068  O   TYR A 139     8990   6803   6840   -704    348    668       O  
ATOM   1069  CB  TYR A 139      49.540  28.178  25.800  1.00 55.46           C  
ANISOU 1069  CB  TYR A 139     8759   6188   6125   -894    653    570       C  
ATOM   1070  CG  TYR A 139      50.464  27.001  25.592  1.00 55.15           C  
ANISOU 1070  CG  TYR A 139     8562   6195   6200   -867    698    502       C  
ATOM   1071  CD1 TYR A 139      50.065  25.894  24.858  1.00 54.09           C  
ANISOU 1071  CD1 TYR A 139     8449   6029   6073   -792    678    498       C  
ATOM   1072  CD2 TYR A 139      51.751  27.011  26.114  1.00 56.06           C  
ANISOU 1072  CD2 TYR A 139     8500   6381   6420   -911    753    427       C  
ATOM   1073  CE1 TYR A 139      50.930  24.829  24.656  1.00 55.02           C  
ANISOU 1073  CE1 TYR A 139     8422   6184   6301   -759    711    423       C  
ATOM   1074  CE2 TYR A 139      52.618  25.942  25.927  1.00 55.93           C  
ANISOU 1074  CE2 TYR A 139     8327   6404   6520   -872    778    341       C  
ATOM   1075  CZ  TYR A 139      52.204  24.859  25.200  1.00 55.44           C  
ANISOU 1075  CZ  TYR A 139     8294   6307   6462   -795    756    341       C  
ATOM   1076  OH  TYR A 139      53.051  23.807  25.038  1.00 57.13           O  
ANISOU 1076  OH  TYR A 139     8354   6556   6799   -747    766    247       O  
ATOM   1077  N   GLU A 140      49.755  28.028  28.919  1.00 56.81           N  
ANISOU 1077  N   GLU A 140     8615   6498   6473   -839    445    631       N  
ATOM   1078  CA  GLU A 140      50.429  27.302  30.002  1.00 57.70           C  
ANISOU 1078  CA  GLU A 140     8546   6673   6706   -802    375    619       C  
ATOM   1079  C   GLU A 140      49.450  26.916  31.102  1.00 57.50           C  
ANISOU 1079  C   GLU A 140     8516   6654   6676   -747    232    699       C  
ATOM   1080  O   GLU A 140      49.622  25.855  31.747  1.00 58.26           O  
ANISOU 1080  O   GLU A 140     8522   6767   6846   -690    145    709       O  
ATOM   1081  CB  GLU A 140      51.667  28.020  30.532  1.00 60.19           C  
ANISOU 1081  CB  GLU A 140     8748   7042   7080   -873    431    557       C  
ATOM   1082  CG  GLU A 140      52.841  28.088  29.527  1.00 65.34           C  
ANISOU 1082  CG  GLU A 140     9354   7704   7768   -937    584    446       C  
ATOM   1083  CD  GLU A 140      53.752  26.832  29.405  1.00 67.03           C  
ANISOU 1083  CD  GLU A 140     9400   7951   8117   -874    576    357       C  
ATOM   1084  OE1 GLU A 140      53.448  25.719  29.882  1.00 65.58           O  
ANISOU 1084  OE1 GLU A 140     9164   7762   7992   -769    447    390       O  
ATOM   1085  OE2 GLU A 140      54.841  26.972  28.810  1.00 75.02           O1-
ANISOU 1085  OE2 GLU A 140    10331   8994   9180   -936    703    237       O1-
ATOM   1086  N   ILE A 141      48.393  27.707  31.281  1.00 53.48           N  
ANISOU 1086  N   ILE A 141     8114   6128   6078   -763    204    745       N  
ATOM   1087  CA  ILE A 141      47.366  27.336  32.249  1.00 51.77           C  
ANISOU 1087  CA  ILE A 141     7895   5926   5849   -728     90    801       C  
ATOM   1088  C   ILE A 141      46.458  26.246  31.688  1.00 51.36           C  
ANISOU 1088  C   ILE A 141     7893   5835   5787   -666     51    819       C  
ATOM   1089  O   ILE A 141      46.071  25.313  32.399  1.00 51.68           O  
ANISOU 1089  O   ILE A 141     7894   5887   5856   -637    -29    851       O  
ATOM   1090  CB  ILE A 141      46.478  28.531  32.636  1.00 51.35           C  
ANISOU 1090  CB  ILE A 141     7920   5873   5716   -760     68    818       C  
ATOM   1091  CG1 ILE A 141      47.299  29.638  33.306  1.00 53.05           C  
ANISOU 1091  CG1 ILE A 141     8092   6126   5939   -825     96    805       C  
ATOM   1092  CG2 ILE A 141      45.360  28.099  33.561  1.00 49.01           C  
ANISOU 1092  CG2 ILE A 141     7615   5601   5407   -738    -29    852       C  
ATOM   1093  CD1 ILE A 141      48.048  29.204  34.542  1.00 51.60           C  
ANISOU 1093  CD1 ILE A 141     7773   6001   5832   -828     42    814       C  
ATOM   1094  N   ALA A 142      46.085  26.368  30.421  1.00 50.71           N  
ANISOU 1094  N   ALA A 142     7912   5700   5654   -652    106    798       N  
ATOM   1095  CA  ALA A 142      45.144  25.423  29.845  1.00 51.53           C  
ANISOU 1095  CA  ALA A 142     8068   5766   5746   -592     66    806       C  
ATOM   1096  C   ALA A 142      45.735  24.003  29.773  1.00 52.55           C  
ANISOU 1096  C   ALA A 142     8116   5894   5956   -549     51    804       C  
ATOM   1097  O   ALA A 142      45.044  23.019  30.057  1.00 48.71           O  
ANISOU 1097  O   ALA A 142     7627   5397   5484   -513    -20    831       O  
ATOM   1098  CB  ALA A 142      44.677  25.888  28.480  1.00 50.12           C  
ANISOU 1098  CB  ALA A 142     8030   5523   5490   -581    115    780       C  
ATOM   1099  N   ARG A 143      47.018  23.880  29.458  1.00 53.76           N  
ANISOU 1099  N   ARG A 143     8201   6059   6168   -558    114    762       N  
ATOM   1100  CA  ARG A 143      47.574  22.532  29.404  1.00 55.21           C  
ANISOU 1100  CA  ARG A 143     8304   6235   6437   -501     80    744       C  
ATOM   1101  C   ARG A 143      47.766  21.891  30.779  1.00 56.17           C  
ANISOU 1101  C   ARG A 143     8342   6379   6619   -483    -36    780       C  
ATOM   1102  O   ARG A 143      47.895  20.655  30.879  1.00 59.57           O  
ANISOU 1102  O   ARG A 143     8744   6783   7106   -426   -106    783       O  
ATOM   1103  CB  ARG A 143      48.825  22.465  28.538  1.00 56.25           C  
ANISOU 1103  CB  ARG A 143     8376   6372   6623   -506    180    660       C  
ATOM   1104  CG  ARG A 143      50.062  23.169  29.030  1.00 57.85           C  
ANISOU 1104  CG  ARG A 143     8470   6629   6881   -558    228    605       C  
ATOM   1105  CD  ARG A 143      50.977  23.368  27.820  1.00 59.01           C  
ANISOU 1105  CD  ARG A 143     8603   6778   7040   -597    376    506       C  
ATOM   1106  NE  ARG A 143      52.400  23.237  28.140  1.00 60.73           N  
ANISOU 1106  NE  ARG A 143     8648   7050   7377   -606    405    405       N  
ATOM   1107  CZ  ARG A 143      53.173  22.202  27.838  1.00 60.67           C  
ANISOU 1107  CZ  ARG A 143     8525   7051   7477   -546    396    316       C  
ATOM   1108  NH1 ARG A 143      54.448  22.210  28.193  1.00 62.78           N1+
ANISOU 1108  NH1 ARG A 143     8622   7372   7860   -553    412    203       N1+
ATOM   1109  NH2 ARG A 143      52.700  21.165  27.184  1.00 60.95           N  
ANISOU 1109  NH2 ARG A 143     8604   7041   7512   -476    366    325       N  
ATOM   1110  N   ARG A 144      47.728  22.700  31.835  1.00 53.18           N  
ANISOU 1110  N   ARG A 144     7947   6041   6220   -530    -65    809       N  
ATOM   1111  CA  ARG A 144      47.784  22.175  33.201  1.00 53.25           C  
ANISOU 1111  CA  ARG A 144     7914   6063   6257   -525   -181    851       C  
ATOM   1112  C   ARG A 144      46.435  21.981  33.864  1.00 52.20           C  
ANISOU 1112  C   ARG A 144     7860   5923   6050   -550   -241    915       C  
ATOM   1113  O   ARG A 144      46.335  21.295  34.873  1.00 53.80           O  
ANISOU 1113  O   ARG A 144     8066   6120   6257   -555   -334    956       O  
ATOM   1114  CB  ARG A 144      48.608  23.109  34.073  1.00 54.05           C  
ANISOU 1114  CB  ARG A 144     7943   6215   6380   -567   -182    836       C  
ATOM   1115  CG  ARG A 144      50.074  23.094  33.679  1.00 54.31           C  
ANISOU 1115  CG  ARG A 144     7863   6263   6510   -547   -140    751       C  
ATOM   1116  CD  ARG A 144      50.850  24.092  34.481  1.00 53.02           C  
ANISOU 1116  CD  ARG A 144     7625   6151   6369   -595   -134    726       C  
ATOM   1117  NE  ARG A 144      52.260  23.993  34.177  1.00 54.63           N  
ANISOU 1117  NE  ARG A 144     7698   6377   6683   -578    -98    621       N  
ATOM   1118  CZ  ARG A 144      52.818  24.450  33.053  1.00 55.53           C  
ANISOU 1118  CZ  ARG A 144     7786   6504   6810   -615     45    540       C  
ATOM   1119  NH1 ARG A 144      52.068  24.996  32.093  1.00 55.88           N1+
ANISOU 1119  NH1 ARG A 144     7953   6524   6757   -660    149    568       N1+
ATOM   1120  NH2 ARG A 144      54.125  24.345  32.879  1.00 54.99           N  
ANISOU 1120  NH2 ARG A 144     7575   6467   6852   -610     81    421       N  
ATOM   1121  N   HIS A 145      45.416  22.616  33.319  1.00 50.51           N  
ANISOU 1121  N   HIS A 145     7715   5710   5768   -570   -191    914       N  
ATOM   1122  CA  HIS A 145      44.075  22.547  33.850  1.00 48.82           C  
ANISOU 1122  CA  HIS A 145     7555   5502   5492   -600   -231    941       C  
ATOM   1123  C   HIS A 145      43.174  22.297  32.663  1.00 49.42           C  
ANISOU 1123  C   HIS A 145     7697   5540   5542   -565   -199    915       C  
ATOM   1124  O   HIS A 145      42.615  23.236  32.055  1.00 48.18           O  
ANISOU 1124  O   HIS A 145     7588   5381   5339   -566   -161    884       O  
ATOM   1125  CB  HIS A 145      43.751  23.866  34.528  1.00 49.47           C  
ANISOU 1125  CB  HIS A 145     7637   5634   5526   -655   -217    936       C  
ATOM   1126  CG  HIS A 145      44.682  24.195  35.644  1.00 49.75           C  
ANISOU 1126  CG  HIS A 145     7609   5706   5585   -687   -248    956       C  
ATOM   1127  CD2 HIS A 145      45.769  25.000  35.698  1.00 51.18           C  
ANISOU 1127  CD2 HIS A 145     7737   5909   5799   -696   -215    936       C  
ATOM   1128  ND1 HIS A 145      44.563  23.629  36.889  1.00 49.65           N  
ANISOU 1128  ND1 HIS A 145     7594   5708   5563   -720   -325    996       N  
ATOM   1129  CE1 HIS A 145      45.528  24.070  37.672  1.00 50.79           C  
ANISOU 1129  CE1 HIS A 145     7685   5879   5734   -735   -351   1001       C  
ATOM   1130  NE2 HIS A 145      46.267  24.919  36.979  1.00 53.12           N  
ANISOU 1130  NE2 HIS A 145     7937   6185   6062   -721   -283    961       N  
ATOM   1131  N   PRO A 146      43.060  21.031  32.272  1.00 49.71           N  
ANISOU 1131  N   PRO A 146     7745   5534   5607   -527   -227    924       N  
ATOM   1132  CA  PRO A 146      42.375  20.719  31.003  1.00 49.73           C  
ANISOU 1132  CA  PRO A 146     7807   5494   5595   -483   -198    892       C  
ATOM   1133  C   PRO A 146      40.865  20.949  31.051  1.00 50.50           C  
ANISOU 1133  C   PRO A 146     7951   5599   5639   -502   -218    871       C  
ATOM   1134  O   PRO A 146      40.202  20.857  30.007  1.00 50.81           O  
ANISOU 1134  O   PRO A 146     8043   5602   5661   -459   -207    833       O  
ATOM   1135  CB  PRO A 146      42.700  19.243  30.767  1.00 50.74           C  
ANISOU 1135  CB  PRO A 146     7926   5577   5776   -440   -235    906       C  
ATOM   1136  CG  PRO A 146      43.211  18.749  32.088  1.00 52.45           C  
ANISOU 1136  CG  PRO A 146     8104   5806   6019   -470   -307    951       C  
ATOM   1137  CD  PRO A 146      43.825  19.902  32.798  1.00 49.90           C  
ANISOU 1137  CD  PRO A 146     7733   5536   5689   -508   -289    952       C  
ATOM   1138  N   TYR A 147      40.331  21.240  32.242  1.00 49.73           N  
ANISOU 1138  N   TYR A 147     7830   5549   5517   -565   -248    880       N  
ATOM   1139  CA  TYR A 147      38.922  21.567  32.404  1.00 48.70           C  
ANISOU 1139  CA  TYR A 147     7715   5442   5346   -591   -261    830       C  
ATOM   1140  C   TYR A 147      38.716  23.002  32.827  1.00 46.35           C  
ANISOU 1140  C   TYR A 147     7406   5190   5015   -615   -253    797       C  
ATOM   1141  O   TYR A 147      37.626  23.391  33.259  1.00 44.00           O  
ANISOU 1141  O   TYR A 147     7095   4929   4693   -644   -270    740       O  
ATOM   1142  CB  TYR A 147      38.280  20.622  33.390  1.00 50.70           C  
ANISOU 1142  CB  TYR A 147     7957   5715   5593   -661   -292    844       C  
ATOM   1143  CG  TYR A 147      38.265  19.218  32.859  1.00 56.27           C  
ANISOU 1143  CG  TYR A 147     8692   6361   6326   -635   -310    865       C  
ATOM   1144  CD1 TYR A 147      39.332  18.349  33.091  1.00 56.87           C  
ANISOU 1144  CD1 TYR A 147     8775   6399   6436   -621   -339    931       C  
ATOM   1145  CD2 TYR A 147      37.183  18.743  32.099  1.00 58.26           C  
ANISOU 1145  CD2 TYR A 147     8968   6591   6578   -615   -309    808       C  
ATOM   1146  CE1 TYR A 147      39.314  17.053  32.591  1.00 58.21           C  
ANISOU 1146  CE1 TYR A 147     8978   6505   6633   -590   -367    945       C  
ATOM   1147  CE2 TYR A 147      37.163  17.444  31.618  1.00 57.77           C  
ANISOU 1147  CE2 TYR A 147     8937   6471   6542   -594   -328    827       C  
ATOM   1148  CZ  TYR A 147      38.236  16.611  31.852  1.00 58.06           C  
ANISOU 1148  CZ  TYR A 147     8987   6467   6608   -581   -355    898       C  
ATOM   1149  OH  TYR A 147      38.223  15.320  31.363  1.00 61.60           O  
ANISOU 1149  OH  TYR A 147     9472   6849   7083   -552   -384    912       O  
ATOM   1150  N   PHE A 148      39.736  23.824  32.664  1.00 45.31           N  
ANISOU 1150  N   PHE A 148     7276   5055   4885   -602   -225    818       N  
ATOM   1151  CA  PHE A 148      39.582  25.185  33.130  1.00 46.64           C  
ANISOU 1151  CA  PHE A 148     7441   5259   5020   -628   -224    791       C  
ATOM   1152  C   PHE A 148      38.464  25.885  32.321  1.00 47.84           C  
ANISOU 1152  C   PHE A 148     7655   5385   5139   -582   -246    712       C  
ATOM   1153  O   PHE A 148      38.353  25.704  31.096  1.00 46.93           O  
ANISOU 1153  O   PHE A 148     7609   5206   5016   -522   -242    694       O  
ATOM   1154  CB  PHE A 148      40.907  25.924  33.060  1.00 47.38           C  
ANISOU 1154  CB  PHE A 148     7531   5349   5122   -635   -184    823       C  
ATOM   1155  CG  PHE A 148      40.946  27.162  33.893  1.00 49.49           C  
ANISOU 1155  CG  PHE A 148     7780   5659   5363   -678   -190    812       C  
ATOM   1156  CD1 PHE A 148      40.212  28.281  33.527  1.00 50.71           C  
ANISOU 1156  CD1 PHE A 148     7994   5799   5474   -660   -204    756       C  
ATOM   1157  CD2 PHE A 148      41.701  27.211  35.060  1.00 49.06           C  
ANISOU 1157  CD2 PHE A 148     7658   5654   5328   -729   -196    851       C  
ATOM   1158  CE1 PHE A 148      40.237  29.420  34.310  1.00 50.56           C  
ANISOU 1158  CE1 PHE A 148     7961   5817   5434   -696   -217    741       C  
ATOM   1159  CE2 PHE A 148      41.739  28.346  35.831  1.00 48.86           C  
ANISOU 1159  CE2 PHE A 148     7616   5669   5279   -768   -202    838       C  
ATOM   1160  CZ  PHE A 148      41.012  29.452  35.457  1.00 49.58           C  
ANISOU 1160  CZ  PHE A 148     7761   5748   5330   -754   -209    783       C  
ATOM   1161  N   TYR A 149      37.622  26.636  33.043  1.00 48.98           N  
ANISOU 1161  N   TYR A 149     7772   5574   5263   -607   -278    655       N  
ATOM   1162  CA  TYR A 149      36.481  27.402  32.506  1.00 48.60           C  
ANISOU 1162  CA  TYR A 149     7765   5506   5193   -555   -329    554       C  
ATOM   1163  C   TYR A 149      37.010  28.399  31.490  1.00 50.41           C  
ANISOU 1163  C   TYR A 149     8108   5659   5385   -503   -330    559       C  
ATOM   1164  O   TYR A 149      37.596  29.413  31.864  1.00 54.35           O  
ANISOU 1164  O   TYR A 149     8623   6165   5862   -529   -319    577       O  
ATOM   1165  CB  TYR A 149      35.802  28.143  33.666  1.00 49.48           C  
ANISOU 1165  CB  TYR A 149     7808   5692   5298   -601   -355    490       C  
ATOM   1166  CG  TYR A 149      34.392  28.701  33.486  1.00 49.38           C  
ANISOU 1166  CG  TYR A 149     7788   5688   5288   -555   -422    348       C  
ATOM   1167  CD1 TYR A 149      33.878  29.621  34.420  1.00 49.31           C  
ANISOU 1167  CD1 TYR A 149     7720   5742   5275   -584   -449    270       C  
ATOM   1168  CD2 TYR A 149      33.582  28.325  32.436  1.00 48.24           C  
ANISOU 1168  CD2 TYR A 149     7683   5491   5155   -479   -467    276       C  
ATOM   1169  CE1 TYR A 149      32.605  30.130  34.314  1.00 48.97           C  
ANISOU 1169  CE1 TYR A 149     7646   5713   5248   -536   -519    114       C  
ATOM   1170  CE2 TYR A 149      32.306  28.840  32.321  1.00 49.43           C  
ANISOU 1170  CE2 TYR A 149     7808   5650   5321   -427   -545    124       C  
ATOM   1171  CZ  TYR A 149      31.819  29.728  33.270  1.00 49.92           C  
ANISOU 1171  CZ  TYR A 149     7799   5780   5388   -455   -571     37       C  
ATOM   1172  OH  TYR A 149      30.551  30.252  33.150  1.00 50.89           O  
ANISOU 1172  OH  TYR A 149     7881   5915   5541   -392   -658   -142       O  
ATOM   1173  N   ALA A 150      36.808  28.112  30.206  1.00 49.49           N  
ANISOU 1173  N   ALA A 150     8085   5466   5253   -437   -342    542       N  
ATOM   1174  CA  ALA A 150      37.517  28.805  29.155  1.00 48.44           C  
ANISOU 1174  CA  ALA A 150     8087   5249   5068   -412   -320    566       C  
ATOM   1175  C   ALA A 150      37.322  30.321  29.193  1.00 49.51           C  
ANISOU 1175  C   ALA A 150     8309   5351   5152   -402   -369    525       C  
ATOM   1176  O   ALA A 150      38.296  31.074  29.202  1.00 51.57           O  
ANISOU 1176  O   ALA A 150     8621   5593   5380   -448   -318    572       O  
ATOM   1177  CB  ALA A 150      37.097  28.254  27.810  1.00 48.90           C  
ANISOU 1177  CB  ALA A 150     8248   5227   5106   -341   -341    540       C  
ATOM   1178  N   PRO A 151      36.078  30.783  29.227  1.00 49.18           N  
ANISOU 1178  N   PRO A 151     8280   5299   5106   -343   -471    426       N  
ATOM   1179  CA  PRO A 151      35.881  32.207  29.297  1.00 51.57           C  
ANISOU 1179  CA  PRO A 151     8670   5560   5364   -323   -537    380       C  
ATOM   1180  C   PRO A 151      36.551  32.887  30.502  1.00 50.91           C  
ANISOU 1180  C   PRO A 151     8505   5549   5291   -403   -494    418       C  
ATOM   1181  O   PRO A 151      37.059  33.994  30.338  1.00 51.58           O  
ANISOU 1181  O   PRO A 151     8697   5579   5324   -417   -499    433       O  
ATOM   1182  CB  PRO A 151      34.362  32.353  29.417  1.00 51.79           C  
ANISOU 1182  CB  PRO A 151     8658   5598   5420   -244   -660    240       C  
ATOM   1183  CG  PRO A 151      33.827  31.112  28.864  1.00 52.11           C  
ANISOU 1183  CG  PRO A 151     8663   5641   5496   -210   -658    220       C  
ATOM   1184  CD  PRO A 151      34.805  30.077  29.329  1.00 51.49           C  
ANISOU 1184  CD  PRO A 151     8493   5625   5444   -298   -534    337       C  
ATOM   1185  N   GLU A 152      36.565  32.254  31.673  1.00 48.92           N  
ANISOU 1185  N   GLU A 152     8086   5408   5094   -460   -455    434       N  
ATOM   1186  CA  GLU A 152      37.191  32.886  32.805  1.00 50.42           C  
ANISOU 1186  CA  GLU A 152     8208   5661   5288   -532   -424    468       C  
ATOM   1187  C   GLU A 152      38.644  32.958  32.503  1.00 51.13           C  
ANISOU 1187  C   GLU A 152     8343   5721   5363   -581   -338    566       C  
ATOM   1188  O   GLU A 152      39.279  33.969  32.806  1.00 53.77           O  
ANISOU 1188  O   GLU A 152     8709   6048   5673   -619   -324    583       O  
ATOM   1189  CB  GLU A 152      37.026  32.162  34.119  1.00 53.81           C  
ANISOU 1189  CB  GLU A 152     8480   6203   5763   -595   -398    475       C  
ATOM   1190  CG  GLU A 152      35.825  32.597  34.924  1.00 58.97           C  
ANISOU 1190  CG  GLU A 152     9061   6919   6426   -593   -458    362       C  
ATOM   1191  CD  GLU A 152      35.865  34.045  35.405  1.00 60.78           C  
ANISOU 1191  CD  GLU A 152     9311   7149   6632   -592   -500    319       C  
ATOM   1192  OE1 GLU A 152      36.575  34.372  36.392  1.00 58.75           O  
ANISOU 1192  OE1 GLU A 152     9002   6948   6372   -663   -461    371       O  
ATOM   1193  OE2 GLU A 152      35.117  34.852  34.810  1.00 65.18           O1-
ANISOU 1193  OE2 GLU A 152     9942   7648   7175   -513   -587    224       O1-
ATOM   1194  N   LEU A 153      39.179  31.935  31.846  1.00 48.17           N  
ANISOU 1194  N   LEU A 153     7972   5328   5004   -580   -281    617       N  
ATOM   1195  CA  LEU A 153      40.583  31.978  31.503  1.00 46.88           C  
ANISOU 1195  CA  LEU A 153     7831   5143   4836   -629   -191    683       C  
ATOM   1196  C   LEU A 153      40.927  33.191  30.608  1.00 49.49           C  
ANISOU 1196  C   LEU A 153     8332   5381   5091   -637   -177    672       C  
ATOM   1197  O   LEU A 153      41.982  33.802  30.774  1.00 50.03           O  
ANISOU 1197  O   LEU A 153     8407   5452   5150   -706   -110    701       O  
ATOM   1198  CB  LEU A 153      40.985  30.696  30.833  1.00 45.29           C  
ANISOU 1198  CB  LEU A 153     7610   4931   4667   -614   -141    715       C  
ATOM   1199  CG  LEU A 153      42.465  30.497  30.579  1.00 44.37           C  
ANISOU 1199  CG  LEU A 153     7470   4816   4573   -664    -42    757       C  
ATOM   1200  CD1 LEU A 153      43.260  30.787  31.824  1.00 42.35           C  
ANISOU 1200  CD1 LEU A 153     7095   4634   4361   -723    -28    781       C  
ATOM   1201  CD2 LEU A 153      42.675  29.088  30.048  1.00 43.04           C  
ANISOU 1201  CD2 LEU A 153     7260   4644   4449   -632    -16    771       C  
ATOM   1202  N   LEU A 154      40.038  33.565  29.691  1.00 50.08           N  
ANISOU 1202  N   LEU A 154     8553   5368   5108   -571   -246    624       N  
ATOM   1203  CA  LEU A 154      40.277  34.763  28.888  1.00 52.30           C  
ANISOU 1203  CA  LEU A 154     9036   5540   5296   -584   -253    616       C  
ATOM   1204  C   LEU A 154      40.413  35.976  29.804  1.00 53.64           C  
ANISOU 1204  C   LEU A 154     9195   5729   5456   -624   -282    605       C  
ATOM   1205  O   LEU A 154      41.307  36.803  29.643  1.00 53.01           O  
ANISOU 1205  O   LEU A 154     9204   5607   5329   -698   -221    634       O  
ATOM   1206  CB  LEU A 154      39.137  34.984  27.894  1.00 52.89           C  
ANISOU 1206  CB  LEU A 154     9277   5508   5310   -486   -366    555       C  
ATOM   1207  CG  LEU A 154      38.952  33.960  26.766  1.00 52.15           C  
ANISOU 1207  CG  LEU A 154     9244   5367   5203   -441   -350    558       C  
ATOM   1208  CD1 LEU A 154      37.808  34.431  25.876  1.00 54.30           C  
ANISOU 1208  CD1 LEU A 154     9699   5523   5410   -338   -492    484       C  
ATOM   1209  CD2 LEU A 154      40.204  33.750  25.935  1.00 51.51           C  
ANISOU 1209  CD2 LEU A 154     9247   5246   5076   -520   -211    619       C  
ATOM   1210  N   TYR A 155      39.513  36.067  30.779  1.00 55.02           N  
ANISOU 1210  N   TYR A 155     9258   5972   5677   -582   -368    555       N  
ATOM   1211  CA  TYR A 155      39.519  37.162  31.744  1.00 54.29           C  
ANISOU 1211  CA  TYR A 155     9137   5908   5583   -611   -406    532       C  
ATOM   1212  C   TYR A 155      40.846  37.247  32.520  1.00 54.78           C  
ANISOU 1212  C   TYR A 155     9101   6038   5673   -715   -299    602       C  
ATOM   1213  O   TYR A 155      41.421  38.307  32.672  1.00 58.04           O  
ANISOU 1213  O   TYR A 155     9581   6420   6052   -767   -284    610       O  
ATOM   1214  CB  TYR A 155      38.356  36.988  32.703  1.00 54.11           C  
ANISOU 1214  CB  TYR A 155     8977   5970   5614   -562   -491    455       C  
ATOM   1215  CG  TYR A 155      38.467  37.790  33.971  1.00 55.26           C  
ANISOU 1215  CG  TYR A 155     9033   6186   5776   -606   -504    437       C  
ATOM   1216  CD1 TYR A 155      38.063  39.120  34.032  1.00 54.91           C  
ANISOU 1216  CD1 TYR A 155     9083   6085   5694   -575   -594    372       C  
ATOM   1217  CD2 TYR A 155      38.940  37.203  35.124  1.00 56.02           C  
ANISOU 1217  CD2 TYR A 155     8963   6399   5923   -675   -441    481       C  
ATOM   1218  CE1 TYR A 155      38.145  39.828  35.220  1.00 56.17           C  
ANISOU 1218  CE1 TYR A 155     9155   6315   5873   -614   -607    350       C  
ATOM   1219  CE2 TYR A 155      39.023  37.902  36.305  1.00 56.09           C  
ANISOU 1219  CE2 TYR A 155     8895   6474   5942   -717   -454    462       C  
ATOM   1220  CZ  TYR A 155      38.629  39.200  36.354  1.00 56.90           C  
ANISOU 1220  CZ  TYR A 155     9075   6531   6012   -688   -531    396       C  
ATOM   1221  OH  TYR A 155      38.763  39.849  37.561  1.00 62.13           O  
ANISOU 1221  OH  TYR A 155     9654   7266   6688   -734   -538    378       O  
ATOM   1222  N   TYR A 156      41.348  36.121  32.990  1.00 53.23           N  
ANISOU 1222  N   TYR A 156     8754   5928   5542   -744   -234    646       N  
ATOM   1223  CA  TYR A 156      42.604  36.116  33.708  1.00 51.46           C  
ANISOU 1223  CA  TYR A 156     8430   5766   5358   -826   -153    695       C  
ATOM   1224  C   TYR A 156      43.732  36.517  32.807  1.00 50.66           C  
ANISOU 1224  C   TYR A 156     8426   5599   5223   -886    -58    718       C  
ATOM   1225  O   TYR A 156      44.650  37.188  33.245  1.00 51.24           O  
ANISOU 1225  O   TYR A 156     8474   5692   5304   -960     -7    728       O  
ATOM   1226  CB  TYR A 156      42.862  34.749  34.353  1.00 53.15           C  
ANISOU 1226  CB  TYR A 156     8482   6065   5646   -828   -131    729       C  
ATOM   1227  CG  TYR A 156      42.020  34.547  35.588  1.00 54.07           C  
ANISOU 1227  CG  TYR A 156     8498   6263   5785   -820   -199    710       C  
ATOM   1228  CD1 TYR A 156      42.130  35.415  36.671  1.00 58.18           C  
ANISOU 1228  CD1 TYR A 156     8972   6832   6302   -860   -222    699       C  
ATOM   1229  CD2 TYR A 156      41.119  33.524  35.667  1.00 55.67           C  
ANISOU 1229  CD2 TYR A 156     8657   6490   6004   -784   -232    696       C  
ATOM   1230  CE1 TYR A 156      41.353  35.266  37.802  1.00 60.70           C  
ANISOU 1230  CE1 TYR A 156     9208   7227   6630   -868   -271    670       C  
ATOM   1231  CE2 TYR A 156      40.341  33.352  36.783  1.00 59.23           C  
ANISOU 1231  CE2 TYR A 156     9025   7015   6463   -801   -274    666       C  
ATOM   1232  CZ  TYR A 156      40.455  34.224  37.854  1.00 62.47           C  
ANISOU 1232  CZ  TYR A 156     9394   7478   6865   -844   -291    652       C  
ATOM   1233  OH  TYR A 156      39.678  34.031  38.980  1.00 63.85           O  
ANISOU 1233  OH  TYR A 156     9491   7731   7036   -876   -320    615       O  
ATOM   1234  N   ALA A 157      43.669  36.122  31.542  1.00 50.94           N  
ANISOU 1234  N   ALA A 157     8576   5559   5218   -863    -26    718       N  
ATOM   1235  CA  ALA A 157      44.744  36.435  30.614  1.00 49.98           C  
ANISOU 1235  CA  ALA A 157     8557   5379   5055   -941     88    728       C  
ATOM   1236  C   ALA A 157      44.797  37.934  30.457  1.00 52.34           C  
ANISOU 1236  C   ALA A 157     9022   5597   5267   -992     76    715       C  
ATOM   1237  O   ALA A 157      45.859  38.529  30.593  1.00 53.33           O  
ANISOU 1237  O   ALA A 157     9145   5729   5389  -1095    166    719       O  
ATOM   1238  CB  ALA A 157      44.544  35.745  29.297  1.00 49.12           C  
ANISOU 1238  CB  ALA A 157     8557   5200   4905   -908    118    726       C  
ATOM   1239  N   ASN A 158      43.645  38.563  30.239  1.00 54.72           N  
ANISOU 1239  N   ASN A 158     9462   5824   5506   -921    -47    688       N  
ATOM   1240  CA  ASN A 158      43.576  40.018  30.287  1.00 55.30           C  
ANISOU 1240  CA  ASN A 158     9693   5816   5503   -953    -94    671       C  
ATOM   1241  C   ASN A 158      44.221  40.562  31.561  1.00 54.98           C  
ANISOU 1241  C   ASN A 158     9506   5865   5520  -1019    -68    678       C  
ATOM   1242  O   ASN A 158      45.186  41.319  31.482  1.00 63.20           O  
ANISOU 1242  O   ASN A 158    10609   6876   6527  -1125     15    689       O  
ATOM   1243  CB  ASN A 158      42.141  40.511  30.199  1.00 56.50           C  
ANISOU 1243  CB  ASN A 158     9951   5900   5616   -836   -267    618       C  
ATOM   1244  CG  ASN A 158      41.540  40.394  28.808  1.00 59.92           C  
ANISOU 1244  CG  ASN A 158    10604   6200   5962   -775   -319    602       C  
ATOM   1245  ND2 ASN A 158      40.259  40.751  28.720  1.00 63.86           N  
ANISOU 1245  ND2 ASN A 158    11179   6642   6444   -655   -488    533       N  
ATOM   1246  OD1 ASN A 158      42.199  40.019  27.821  1.00 61.27           O  
ANISOU 1246  OD1 ASN A 158    10880   6319   6081   -832   -216    637       O  
ATOM   1247  N   LYS A 159      43.720  40.179  32.726  1.00 53.06           N  
ANISOU 1247  N   LYS A 159     9074   5730   5356   -967   -132    666       N  
ATOM   1248  CA  LYS A 159      44.324  40.621  33.983  1.00 54.71           C  
ANISOU 1248  CA  LYS A 159     9144   6027   5618  -1025   -115    672       C  
ATOM   1249  C   LYS A 159      45.839  40.460  33.998  1.00 55.94           C  
ANISOU 1249  C   LYS A 159     9227   6218   5809  -1132     22    702       C  
ATOM   1250  O   LYS A 159      46.558  41.432  34.234  1.00 60.52           O  
ANISOU 1250  O   LYS A 159     9842   6782   6371  -1216     62    697       O  
ATOM   1251  CB  LYS A 159      43.721  39.937  35.219  1.00 53.37           C  
ANISOU 1251  CB  LYS A 159     8778   5978   5523   -975   -175    663       C  
ATOM   1252  CG  LYS A 159      42.864  40.872  36.089  1.00 55.54           C  
ANISOU 1252  CG  LYS A 159     9048   6268   5785   -943   -281    610       C  
ATOM   1253  CD  LYS A 159      43.099  40.770  37.624  1.00 58.02           C  
ANISOU 1253  CD  LYS A 159     9179   6707   6157   -979   -284    615       C  
ATOM   1254  N   TYR A 160      46.319  39.256  33.757  1.00 53.92           N  
ANISOU 1254  N   TYR A 160     8866   6012   5611  -1129     88    720       N  
ATOM   1255  CA  TYR A 160      47.755  38.993  33.686  1.00 56.44           C  
ANISOU 1255  CA  TYR A 160     9094   6369   5981  -1217    212    720       C  
ATOM   1256  C   TYR A 160      48.445  40.063  32.884  1.00 59.53           C  
ANISOU 1256  C   TYR A 160     9647   6675   6296  -1325    306    701       C  
ATOM   1257  O   TYR A 160      49.404  40.662  33.337  1.00 63.78           O  
ANISOU 1257  O   TYR A 160    10127   7243   6862  -1417    370    682       O  
ATOM   1258  CB  TYR A 160      47.983  37.671  32.973  1.00 56.59           C  
ANISOU 1258  CB  TYR A 160     9062   6401   6040  -1186    265    724       C  
ATOM   1259  CG  TYR A 160      49.353  37.048  33.081  1.00 57.11           C  
ANISOU 1259  CG  TYR A 160     8970   6533   6197  -1241    365    701       C  
ATOM   1260  CD1 TYR A 160      49.850  36.624  34.302  1.00 56.73           C  
ANISOU 1260  CD1 TYR A 160     8727   6579   6247  -1227    324    700       C  
ATOM   1261  CD2 TYR A 160      50.118  36.802  31.940  1.00 57.28           C  
ANISOU 1261  CD2 TYR A 160     9037   6519   6206  -1299    491    666       C  
ATOM   1262  CE1 TYR A 160      51.083  35.979  34.389  1.00 57.84           C  
ANISOU 1262  CE1 TYR A 160     8715   6776   6486  -1255    389    658       C  
ATOM   1263  CE2 TYR A 160      51.354  36.187  32.020  1.00 57.41           C  
ANISOU 1263  CE2 TYR A 160     8887   6603   6323  -1339    577    615       C  
ATOM   1264  CZ  TYR A 160      51.831  35.756  33.240  1.00 58.05           C  
ANISOU 1264  CZ  TYR A 160     8766   6775   6516  -1307    516    608       C  
ATOM   1265  OH  TYR A 160      53.066  35.117  33.319  1.00 58.08           O  
ANISOU 1265  OH  TYR A 160     8595   6840   6632  -1328    576    538       O  
ATOM   1266  N   ASN A 161      47.942  40.305  31.679  1.00 62.54           N  
ANISOU 1266  N   ASN A 161    10245   6942   6575  -1320    311    703       N  
ATOM   1267  CA  ASN A 161      48.530  41.301  30.794  1.00 63.65           C  
ANISOU 1267  CA  ASN A 161    10594   6978   6613  -1438    404    690       C  
ATOM   1268  C   ASN A 161      48.515  42.679  31.417  1.00 61.89           C  
ANISOU 1268  C   ASN A 161    10449   6717   6348  -1487    356    685       C  
ATOM   1269  O   ASN A 161      49.502  43.392  31.335  1.00 65.54           O  
ANISOU 1269  O   ASN A 161    10952   7161   6788  -1622    463    667       O  
ATOM   1270  CB  ASN A 161      47.849  41.309  29.412  1.00 66.01           C  
ANISOU 1270  CB  ASN A 161    11149   7141   6789  -1411    387    698       C  
ATOM   1271  CG  ASN A 161      48.578  40.442  28.392  1.00 70.71           C  
ANISOU 1271  CG  ASN A 161    11747   7738   7381  -1468    533    685       C  
ATOM   1272  ND2 ASN A 161      48.585  40.898  27.142  1.00 76.44           N  
ANISOU 1272  ND2 ASN A 161    12743   8333   7969  -1535    588    683       N  
ATOM   1273  OD1 ASN A 161      49.133  39.380  28.717  1.00 70.62           O  
ANISOU 1273  OD1 ASN A 161    11509   7838   7486  -1453    590    672       O  
ATOM   1274  N   GLY A 162      47.416  43.049  32.064  1.00 59.91           N  
ANISOU 1274  N   GLY A 162    10210   6460   6094  -1384    199    689       N  
ATOM   1275  CA  GLY A 162      47.320  44.371  32.710  1.00 59.85           C  
ANISOU 1275  CA  GLY A 162    10274   6416   6052  -1415    134    677       C  
ATOM   1276  C   GLY A 162      48.396  44.623  33.765  1.00 59.01           C  
ANISOU 1276  C   GLY A 162     9978   6413   6028  -1505    207    669       C  
ATOM   1277  O   GLY A 162      48.884  45.744  33.922  1.00 61.60           O  
ANISOU 1277  O   GLY A 162    10396   6695   6316  -1598    232    657       O  
ATOM   1278  N   VAL A 163      48.758  43.567  34.486  1.00 57.80           N  
ANISOU 1278  N   VAL A 163     9576   6394   5991  -1474    230    673       N  
ATOM   1279  CA  VAL A 163      49.823  43.627  35.447  1.00 57.40           C  
ANISOU 1279  CA  VAL A 163     9337   6443   6030  -1544    285    656       C  
ATOM   1280  C   VAL A 163      51.123  43.976  34.733  1.00 61.69           C  
ANISOU 1280  C   VAL A 163     9921   6956   6561  -1692    449    624       C  
ATOM   1281  O   VAL A 163      51.784  44.958  35.099  1.00 64.89           O  
ANISOU 1281  O   VAL A 163    10340   7353   6960  -1793    490    598       O  
ATOM   1282  CB  VAL A 163      49.991  42.316  36.207  1.00 55.43           C  
ANISOU 1282  CB  VAL A 163     8847   6319   5895  -1477    266    664       C  
ATOM   1283  CG1 VAL A 163      51.268  42.400  37.020  1.00 55.15           C  
ANISOU 1283  CG1 VAL A 163     8636   6369   5951  -1552    322    632       C  
ATOM   1284  CG2 VAL A 163      48.788  42.058  37.109  1.00 51.03           C  
ANISOU 1284  CG2 VAL A 163     8239   5805   5345  -1366    124    685       C  
ATOM   1285  N   PHE A 164      51.460  43.232  33.680  1.00 62.70           N  
ANISOU 1285  N   PHE A 164    10079   7063   6679  -1716    548    614       N  
ATOM   1286  CA  PHE A 164      52.688  43.518  32.919  1.00 65.51           C  
ANISOU 1286  CA  PHE A 164    10474   7397   7021  -1875    727    562       C  
ATOM   1287  C   PHE A 164      52.709  44.909  32.299  1.00 67.02           C  
ANISOU 1287  C   PHE A 164    10939   7455   7072  -1998    772    561       C  
ATOM   1288  O   PHE A 164      53.734  45.570  32.345  1.00 68.52           O  
ANISOU 1288  O   PHE A 164    11119   7650   7267  -2149    890    512       O  
ATOM   1289  CB  PHE A 164      53.006  42.419  31.899  1.00 63.92           C  
ANISOU 1289  CB  PHE A 164    10251   7203   6833  -1876    828    540       C  
ATOM   1290  CG  PHE A 164      53.578  41.210  32.539  1.00 63.90           C  
ANISOU 1290  CG  PHE A 164     9959   7333   6986  -1812    827    508       C  
ATOM   1291  CD1 PHE A 164      52.750  40.215  33.013  1.00 64.54           C  
ANISOU 1291  CD1 PHE A 164     9948   7457   7117  -1658    697    556       C  
ATOM   1292  CD2 PHE A 164      54.935  41.115  32.779  1.00 65.14           C  
ANISOU 1292  CD2 PHE A 164     9933   7570   7245  -1906    940    421       C  
ATOM   1293  CE1 PHE A 164      53.269  39.119  33.680  1.00 65.26           C  
ANISOU 1293  CE1 PHE A 164     9800   7654   7343  -1597    673    533       C  
ATOM   1294  CE2 PHE A 164      55.469  40.028  33.439  1.00 66.85           C  
ANISOU 1294  CE2 PHE A 164     9892   7898   7612  -1830    906    383       C  
ATOM   1295  CZ  PHE A 164      54.635  39.022  33.894  1.00 66.49           C  
ANISOU 1295  CZ  PHE A 164     9784   7879   7602  -1674    766    446       C  
ATOM   1296  N   GLN A 165      51.584  45.364  31.767  1.00 69.75           N  
ANISOU 1296  N   GLN A 165    11529   7676   7295  -1935    667    608       N  
ATOM   1297  CA  GLN A 165      51.516  46.700  31.191  1.00 77.11           C  
ANISOU 1297  CA  GLN A 165    12761   8456   8081  -2038    676    613       C  
ATOM   1298  C   GLN A 165      51.878  47.770  32.221  1.00 79.75           C  
ANISOU 1298  C   GLN A 165    13048   8809   8442  -2098    647    598       C  
ATOM   1299  O   GLN A 165      52.599  48.718  31.933  1.00 80.90           O  
ANISOU 1299  O   GLN A 165    13334   8885   8520  -2261    746    575       O  
ATOM   1300  CB  GLN A 165      50.119  46.983  30.660  1.00 82.24           C  
ANISOU 1300  CB  GLN A 165    13657   8973   8619  -1914    510    653       C  
ATOM   1301  CG  GLN A 165      50.031  48.249  29.813  1.00 87.40           C  
ANISOU 1301  CG  GLN A 165    14682   9431   9095  -2015    505    662       C  
ATOM   1302  CD  GLN A 165      48.605  48.649  29.510  1.00 92.58           C  
ANISOU 1302  CD  GLN A 165    15560   9956   9662  -1863    291    682       C  
ATOM   1303  NE2 GLN A 165      48.448  49.637  28.638  1.00 98.50           N  
ANISOU 1303  NE2 GLN A 165    16675  10509  10242  -1932    260    692       N  
ATOM   1304  OE1 GLN A 165      47.649  48.076  30.050  1.00 99.02           O  
ANISOU 1304  OE1 GLN A 165    16226  10840  10558  -1689    152    678       O  
ATOM   1305  N   GLU A 166      51.365  47.593  33.426  1.00 80.56           N  
ANISOU 1305  N   GLU A 166    12960   9009   8641  -1973    515    607       N  
ATOM   1306  CA  GLU A 166      51.590  48.509  34.516  1.00 81.25           C  
ANISOU 1306  CA  GLU A 166    12981   9127   8763  -2003    467    592       C  
ATOM   1307  C   GLU A 166      53.005  48.352  35.055  1.00 79.81           C  
ANISOU 1307  C   GLU A 166    12575   9059   8689  -2122    605    543       C  
ATOM   1308  O   GLU A 166      53.776  49.293  35.081  1.00 83.23           O  
ANISOU 1308  O   GLU A 166    13070   9457   9097  -2267    687    510       O  
ATOM   1309  CB  GLU A 166      50.568  48.189  35.606  1.00 84.30           C  
ANISOU 1309  CB  GLU A 166    13222   9592   9215  -1834    294    609       C  
ATOM   1310  CG  GLU A 166      50.518  49.153  36.777  1.00 89.42           C  
ANISOU 1310  CG  GLU A 166    13820  10268   9888  -1836    211    593       C  
ATOM   1311  CD  GLU A 166      49.767  48.553  37.962  1.00 90.16           C  
ANISOU 1311  CD  GLU A 166    13708  10482  10065  -1698     88    596       C  
ATOM   1312  OE1 GLU A 166      48.524  48.374  37.859  1.00 85.85           O  
ANISOU 1312  OE1 GLU A 166    13224   9908   9487  -1576    -29    599       O  
ATOM   1313  OE2 GLU A 166      50.428  48.246  38.986  1.00 85.19           O1-
ANISOU 1313  OE2 GLU A 166    12862   9975   9532  -1717    110    586       O1-
ATOM   1314  N   CYS A 167      53.346  47.149  35.475  1.00 78.01           N  
ANISOU 1314  N   CYS A 167    12090   8963   8585  -2060    623    530       N  
ATOM   1315  CA  CYS A 167      54.547  46.940  36.249  1.00 76.97           C  
ANISOU 1315  CA  CYS A 167    11710   8952   8582  -2124    696    471       C  
ATOM   1316  C   CYS A 167      55.863  46.969  35.475  1.00 79.51           C  
ANISOU 1316  C   CYS A 167    12011   9276   8921  -2295    898    391       C  
ATOM   1317  O   CYS A 167      56.891  47.244  36.077  1.00 82.70           O  
ANISOU 1317  O   CYS A 167    12253   9754   9415  -2381    959    320       O  
ATOM   1318  CB  CYS A 167      54.457  45.620  37.007  1.00 78.92           C  
ANISOU 1318  CB  CYS A 167    11707   9325   8953  -1989    621    479       C  
ATOM   1319  SG  CYS A 167      53.374  45.653  38.453  1.00 81.97           S  
ANISOU 1319  SG  CYS A 167    12020   9767   9360  -1844    418    533       S  
ATOM   1320  N   CYS A 168      55.882  46.675  34.175  1.00 80.37           N  
ANISOU 1320  N   CYS A 168    12269   9314   8952  -2351   1006    387       N  
ATOM   1321  CA  CYS A 168      57.175  46.671  33.452  1.00 83.68           C  
ANISOU 1321  CA  CYS A 168    12651   9751   9391  -2532   1221    287       C  
ATOM   1322  C   CYS A 168      57.768  48.088  33.279  1.00 87.09           C  
ANISOU 1322  C   CYS A 168    13248  10103   9738  -2735   1327    249       C  
ATOM   1323  O   CYS A 168      58.946  48.236  32.945  1.00 89.61           O  
ANISOU 1323  O   CYS A 168    13497  10459  10094  -2909   1512    143       O  
ATOM   1324  CB  CYS A 168      57.100  45.947  32.097  1.00 84.74           C  
ANISOU 1324  CB  CYS A 168    12901   9837   9459  -2554   1326    282       C  
ATOM   1325  SG  CYS A 168      56.666  44.176  32.171  1.00 84.10           S  
ANISOU 1325  SG  CYS A 168    12609   9853   9493  -2349   1239    303       S  
ATOM   1326  N   GLN A 169      56.951  49.116  33.510  1.00 86.62           N  
ANISOU 1326  N   GLN A 169    13406   9935   9569  -2714   1209    323       N  
ATOM   1327  CA  GLN A 169      57.403  50.506  33.509  1.00 88.28           C  
ANISOU 1327  CA  GLN A 169    13787  10058   9697  -2890   1273    299       C  
ATOM   1328  C   GLN A 169      58.240  50.842  34.755  1.00 87.85           C  
ANISOU 1328  C   GLN A 169    13472  10124   9785  -2926   1274    232       C  
ATOM   1329  O   GLN A 169      59.224  51.568  34.672  1.00 88.46           O  
ANISOU 1329  O   GLN A 169    13557  10193   9860  -3120   1417    152       O  
ATOM   1330  CB  GLN A 169      56.187  51.440  33.441  1.00 88.49           C  
ANISOU 1330  CB  GLN A 169    14118   9928   9576  -2820   1108    392       C  
ATOM   1331  N   ALA A 170      57.848  50.273  35.891  1.00 84.97           N  
ANISOU 1331  N   ALA A 170    12880   9867   9537  -2746   1117    258       N  
ATOM   1332  CA  ALA A 170      58.382  50.606  37.206  1.00 83.59           C  
ANISOU 1332  CA  ALA A 170    12486   9792   9481  -2740   1061    215       C  
ATOM   1333  C   ALA A 170      59.897  50.408  37.373  1.00 83.37           C  
ANISOU 1333  C   ALA A 170    12216   9873   9589  -2872   1215     80       C  
ATOM   1334  O   ALA A 170      60.539  49.778  36.547  1.00 82.92           O  
ANISOU 1334  O   ALA A 170    12104   9843   9560  -2945   1362     10       O  
ATOM   1335  CB  ALA A 170      57.630  49.796  38.257  1.00 80.90           C  
ANISOU 1335  CB  ALA A 170    11971   9545   9225  -2523    873    271       C  
ATOM   1336  N   GLU A 171      60.447  50.938  38.470  1.00 84.86           N  
ANISOU 1336  N   GLU A 171    12248  10129   9867  -2894   1172     30       N  
ATOM   1337  CA  GLU A 171      61.898  50.898  38.727  1.00 84.78           C  
ANISOU 1337  CA  GLU A 171    11995  10221   9997  -3019   1300   -122       C  
ATOM   1338  C   GLU A 171      62.352  49.492  39.098  1.00 82.92           C  
ANISOU 1338  C   GLU A 171    11457  10122   9928  -2889   1260   -182       C  
ATOM   1339  O   GLU A 171      63.314  48.969  38.539  1.00 83.22           O  
ANISOU 1339  O   GLU A 171    11352  10216  10051  -2972   1404   -308       O  
ATOM   1340  CB  GLU A 171      62.269  51.875  39.846  1.00 84.64           C  
ANISOU 1340  CB  GLU A 171    11905  10229  10027  -3061   1237   -154       C  
ATOM   1341  N   ASP A 172      61.657  48.896  40.061  1.00 79.76           N  
ANISOU 1341  N   ASP A 172    10966   9769   9570  -2690   1061   -102       N  
ATOM   1342  CA  ASP A 172      61.855  47.498  40.408  1.00 77.79           C  
ANISOU 1342  CA  ASP A 172    10489   9619   9449  -2543    986   -128       C  
ATOM   1343  C   ASP A 172      60.666  46.679  39.881  1.00 74.89           C  
ANISOU 1343  C   ASP A 172    10256   9203   8996  -2411    917     -5       C  
ATOM   1344  O   ASP A 172      59.674  46.462  40.589  1.00 71.56           O  
ANISOU 1344  O   ASP A 172     9870   8780   8540  -2271    754    100       O  
ATOM   1345  CB  ASP A 172      62.032  47.342  41.925  1.00 78.44           C  
ANISOU 1345  CB  ASP A 172    10378   9788   9639  -2432    813   -137       C  
ATOM   1346  CG  ASP A 172      62.445  45.924  42.336  1.00 82.31           C  
ANISOU 1346  CG  ASP A 172    10637  10369  10270  -2293    724   -185       C  
ATOM   1347  OD1 ASP A 172      62.201  44.959  41.569  1.00 83.22           O  
ANISOU 1347  OD1 ASP A 172    10765  10474  10380  -2236    753   -167       O  
ATOM   1348  OD2 ASP A 172      63.005  45.771  43.442  1.00 83.50           O1-
ANISOU 1348  OD2 ASP A 172    10605  10591  10531  -2234    611   -241       O1-
ATOM   1349  N   LYS A 173      60.793  46.254  38.623  1.00 73.57           N  
ANISOU 1349  N   LYS A 173    10162   8999   8792  -2469   1054    -30       N  
ATOM   1350  CA  LYS A 173      59.871  45.341  37.965  1.00 70.40           C  
ANISOU 1350  CA  LYS A 173     9858   8560   8330  -2355   1014     57       C  
ATOM   1351  C   LYS A 173      59.336  44.262  38.923  1.00 70.55           C  
ANISOU 1351  C   LYS A 173     9734   8647   8426  -2157    827    116       C  
ATOM   1352  O   LYS A 173      58.120  44.106  39.118  1.00 66.41           O  
ANISOU 1352  O   LYS A 173     9328   8084   7821  -2049    710    231       O  
ATOM   1353  CB  LYS A 173      60.595  44.647  36.798  1.00 71.83           C  
ANISOU 1353  CB  LYS A 173     9993   8753   8544  -2428   1181    -37       C  
ATOM   1354  CG  LYS A 173      60.922  45.521  35.592  1.00 73.48           C  
ANISOU 1354  CG  LYS A 173    10409   8875   8636  -2634   1385    -78       C  
ATOM   1355  N   GLY A 174      60.259  43.520  39.528  1.00 73.03           N  
ANISOU 1355  N   GLY A 174     9797   9058   8894  -2114    796     25       N  
ATOM   1356  CA  GLY A 174      59.907  42.363  40.351  1.00 73.74           C  
ANISOU 1356  CA  GLY A 174     9766   9200   9053  -1940    626     70       C  
ATOM   1357  C   GLY A 174      59.059  42.699  41.560  1.00 73.32           C  
ANISOU 1357  C   GLY A 174     9758   9149   8951  -1860    461    171       C  
ATOM   1358  O   GLY A 174      58.069  42.029  41.839  1.00 72.94           O  
ANISOU 1358  O   GLY A 174     9765   9092   8858  -1747    351    267       O  
ATOM   1359  N   ALA A 175      59.436  43.754  42.274  1.00 74.33           N  
ANISOU 1359  N   ALA A 175     9866   9292   9086  -1930    451    140       N  
ATOM   1360  CA  ALA A 175      58.719  44.146  43.484  1.00 73.48           C  
ANISOU 1360  CA  ALA A 175     9790   9195   8935  -1866    303    217       C  
ATOM   1361  C   ALA A 175      57.247  44.454  43.189  1.00 71.68           C  
ANISOU 1361  C   ALA A 175     9775   8898   8564  -1829    270    332       C  
ATOM   1362  O   ALA A 175      56.363  44.158  44.004  1.00 65.60           O  
ANISOU 1362  O   ALA A 175     9021   8147   7759  -1736    142    402       O  
ATOM   1363  CB  ALA A 175      59.405  45.351  44.112  1.00 73.37           C  
ANISOU 1363  CB  ALA A 175     9734   9197   8945  -1965    321    154       C  
ATOM   1364  N   CYS A 176      57.009  45.022  42.000  1.00 74.15           N  
ANISOU 1364  N   CYS A 176    10252   9129   8793  -1907    385    338       N  
ATOM   1365  CA  CYS A 176      55.678  45.420  41.542  1.00 75.13           C  
ANISOU 1365  CA  CYS A 176    10590   9170   8785  -1873    351    422       C  
ATOM   1366  C   CYS A 176      54.806  44.216  41.195  1.00 71.62           C  
ANISOU 1366  C   CYS A 176    10161   8726   8324  -1756    299    480       C  
ATOM   1367  O   CYS A 176      53.679  44.108  41.680  1.00 69.42           O  
ANISOU 1367  O   CYS A 176     9934   8447   7995  -1669    191    539       O  
ATOM   1368  CB  CYS A 176      55.787  46.344  40.314  1.00 80.58           C  
ANISOU 1368  CB  CYS A 176    11477   9755   9385  -1994    479    405       C  
ATOM   1369  SG  CYS A 176      54.238  47.079  39.692  1.00 90.29           S  
ANISOU 1369  SG  CYS A 176    13001  10856  10451  -1951    411    484       S  
ATOM   1370  N   LEU A 177      55.333  43.313  40.372  1.00 69.39           N  
ANISOU 1370  N   LEU A 177     9827   8450   8089  -1758    379    452       N  
ATOM   1371  CA  LEU A 177      54.501  42.275  39.751  1.00 68.06           C  
ANISOU 1371  CA  LEU A 177     9711   8258   7889  -1665    353    504       C  
ATOM   1372  C   LEU A 177      54.470  40.939  40.475  1.00 67.77           C  
ANISOU 1372  C   LEU A 177     9522   8294   7935  -1557    257    522       C  
ATOM   1373  O   LEU A 177      53.443  40.239  40.438  1.00 66.10           O  
ANISOU 1373  O   LEU A 177     9362   8070   7682  -1471    189    583       O  
ATOM   1374  CB  LEU A 177      54.878  42.070  38.281  1.00 66.21           C  
ANISOU 1374  CB  LEU A 177     9558   7968   7631  -1727    494    472       C  
ATOM   1375  CG  LEU A 177      56.264  41.549  37.939  1.00 69.25           C  
ANISOU 1375  CG  LEU A 177     9783   8405   8125  -1788    606    373       C  
ATOM   1376  CD1 LEU A 177      56.288  40.024  37.945  1.00 69.04           C  
ANISOU 1376  CD1 LEU A 177     9625   8425   8181  -1675    554    373       C  
ATOM   1377  CD2 LEU A 177      56.700  42.133  36.591  1.00 70.64           C  
ANISOU 1377  CD2 LEU A 177    10098   8511   8232  -1926    783    326       C  
ATOM   1378  N   LEU A 178      55.571  40.568  41.126  1.00 68.70           N  
ANISOU 1378  N   LEU A 178     9460   8479   8165  -1562    243    461       N  
ATOM   1379  CA  LEU A 178      55.629  39.238  41.744  1.00 67.66           C  
ANISOU 1379  CA  LEU A 178     9209   8393   8105  -1458    138    475       C  
ATOM   1380  C   LEU A 178      54.490  39.011  42.736  1.00 65.34           C  
ANISOU 1380  C   LEU A 178     8968   8110   7748  -1386      3    563       C  
ATOM   1381  O   LEU A 178      53.853  37.979  42.688  1.00 62.66           O  
ANISOU 1381  O   LEU A 178     8649   7764   7395  -1313    -50    611       O  
ATOM   1382  CB  LEU A 178      56.990  38.950  42.380  1.00 69.52           C  
ANISOU 1382  CB  LEU A 178     9250   8690   8475  -1459    110    382       C  
ATOM   1383  CG  LEU A 178      58.092  38.591  41.380  1.00 70.30           C  
ANISOU 1383  CG  LEU A 178     9248   8796   8666  -1500    231    271       C  
ATOM   1384  CD1 LEU A 178      59.435  38.486  42.088  1.00 70.42           C  
ANISOU 1384  CD1 LEU A 178     9055   8876   8827  -1501    192    150       C  
ATOM   1385  CD2 LEU A 178      57.773  37.283  40.675  1.00 68.15           C  
ANISOU 1385  CD2 LEU A 178     8984   8504   8407  -1416    223    292       C  
ATOM   1386  N   PRO A 179      54.192  40.001  43.605  1.00 68.74           N  
ANISOU 1386  N   PRO A 179     9429   8556   8135  -1417    -41    577       N  
ATOM   1387  CA  PRO A 179      53.017  39.849  44.496  1.00 66.23           C  
ANISOU 1387  CA  PRO A 179     9166   8253   7744  -1367   -147    644       C  
ATOM   1388  C   PRO A 179      51.723  39.768  43.711  1.00 63.14           C  
ANISOU 1388  C   PRO A 179     8908   7814   7267  -1340   -126    687       C  
ATOM   1389  O   PRO A 179      50.846  38.979  44.043  1.00 64.52           O  
ANISOU 1389  O   PRO A 179     9102   8002   7411  -1286   -188    728       O  
ATOM   1390  CB  PRO A 179      53.032  41.117  45.354  1.00 63.67           C  
ANISOU 1390  CB  PRO A 179     8851   7950   7392  -1418   -173    628       C  
ATOM   1391  CG  PRO A 179      54.410  41.653  45.220  1.00 67.34           C  
ANISOU 1391  CG  PRO A 179     9225   8423   7937  -1483   -112    557       C  
ATOM   1392  CD  PRO A 179      54.869  41.288  43.832  1.00 67.89           C  
ANISOU 1392  CD  PRO A 179     9305   8453   8037  -1506      5    525       C  
ATOM   1393  N   LYS A 180      51.616  40.567  42.666  1.00 61.96           N  
ANISOU 1393  N   LYS A 180     8859   7606   7078  -1380    -41    669       N  
ATOM   1394  CA  LYS A 180      50.388  40.596  41.886  1.00 60.80           C  
ANISOU 1394  CA  LYS A 180     8848   7402   6850  -1344    -41    695       C  
ATOM   1395  C   LYS A 180      50.084  39.287  41.142  1.00 58.09           C  
ANISOU 1395  C   LYS A 180     8506   7045   6521  -1285    -29    720       C  
ATOM   1396  O   LYS A 180      48.937  38.890  41.085  1.00 57.62           O  
ANISOU 1396  O   LYS A 180     8502   6977   6416  -1232    -76    744       O  
ATOM   1397  CB  LYS A 180      50.391  41.774  40.914  1.00 60.97           C  
ANISOU 1397  CB  LYS A 180     9012   7341   6813  -1400     29    673       C  
ATOM   1398  CG  LYS A 180      50.164  43.121  41.571  1.00 59.88           C  
ANISOU 1398  CG  LYS A 180     8925   7194   6633  -1436    -12    655       C  
ATOM   1399  CD  LYS A 180      50.158  44.223  40.509  1.00 62.67           C  
ANISOU 1399  CD  LYS A 180     9459   7439   6913  -1493     45    638       C  
ATOM   1400  CE  LYS A 180      50.656  45.563  41.038  1.00 63.27           C  
ANISOU 1400  CE  LYS A 180     9562   7500   6976  -1572     47    609       C  
ATOM   1401  NZ  LYS A 180      49.609  46.188  41.900  1.00 61.73           N1+
ANISOU 1401  NZ  LYS A 180     9394   7316   6743  -1514    -72    605       N1+
ATOM   1402  N   ILE A 181      51.085  38.612  40.592  1.00 58.56           N  
ANISOU 1402  N   ILE A 181     8497   7105   6647  -1295     33    700       N  
ATOM   1403  CA  ILE A 181      50.813  37.336  39.921  1.00 60.58           C  
ANISOU 1403  CA  ILE A 181     8750   7346   6919  -1235     37    720       C  
ATOM   1404  C   ILE A 181      50.672  36.179  40.916  1.00 62.67           C  
ANISOU 1404  C   ILE A 181     8924   7661   7225  -1175    -63    752       C  
ATOM   1405  O   ILE A 181      50.027  35.195  40.599  1.00 66.51           O  
ANISOU 1405  O   ILE A 181     9437   8133   7700  -1122    -88    782       O  
ATOM   1406  CB  ILE A 181      51.819  36.980  38.781  1.00 63.47           C  
ANISOU 1406  CB  ILE A 181     9092   7688   7336  -1263    147    674       C  
ATOM   1407  CG1 ILE A 181      53.221  36.659  39.333  1.00 66.22           C  
ANISOU 1407  CG1 ILE A 181     9268   8094   7799  -1281    153    615       C  
ATOM   1408  CG2 ILE A 181      51.867  38.078  37.712  1.00 60.90           C  
ANISOU 1408  CG2 ILE A 181     8906   7296   6939  -1341    254    650       C  
ATOM   1409  CD1 ILE A 181      54.316  36.575  38.269  1.00 67.21           C  
ANISOU 1409  CD1 ILE A 181     9346   8209   7980  -1336    284    532       C  
ATOM   1410  N   GLU A 182      51.263  36.287  42.109  1.00 65.02           N  
ANISOU 1410  N   GLU A 182     9131   8010   7563  -1187   -126    745       N  
ATOM   1411  CA  GLU A 182      51.087  35.279  43.157  1.00 65.72           C  
ANISOU 1411  CA  GLU A 182     9176   8131   7665  -1142   -236    782       C  
ATOM   1412  C   GLU A 182      49.646  35.328  43.662  1.00 66.33           C  
ANISOU 1412  C   GLU A 182     9339   8215   7647  -1140   -280    826       C  
ATOM   1413  O   GLU A 182      49.016  34.287  43.859  1.00 65.50           O  
ANISOU 1413  O   GLU A 182     9258   8107   7521  -1109   -326    862       O  
ATOM   1414  CB  GLU A 182      52.066  35.502  44.321  1.00 68.43           C  
ANISOU 1414  CB  GLU A 182     9422   8517   8061  -1157   -304    757       C  
ATOM   1415  CG  GLU A 182      52.330  34.299  45.223  1.00 69.56           C  
ANISOU 1415  CG  GLU A 182     9527   8668   8234  -1106   -427    783       C  
ATOM   1416  N   THR A 183      49.118  36.537  43.828  1.00 64.29           N  
ANISOU 1416  N   THR A 183     9128   7965   7336  -1176   -262    810       N  
ATOM   1417  CA  THR A 183      47.721  36.714  44.200  1.00 63.85           C  
ANISOU 1417  CA  THR A 183     9137   7923   7202  -1174   -293    818       C  
ATOM   1418  C   THR A 183      46.789  36.163  43.150  1.00 62.11           C  
ANISOU 1418  C   THR A 183     8982   7660   6955  -1133   -266    820       C  
ATOM   1419  O   THR A 183      45.925  35.350  43.450  1.00 62.53           O  
ANISOU 1419  O   THR A 183     9047   7730   6981  -1119   -299    835       O  
ATOM   1420  CB  THR A 183      47.396  38.193  44.448  1.00 64.64           C  
ANISOU 1420  CB  THR A 183     9270   8028   7260  -1207   -288    780       C  
ATOM   1421  CG2 THR A 183      45.879  38.444  44.438  1.00 61.58           C  
ANISOU 1421  CG2 THR A 183     8946   7644   6808  -1188   -310    753       C  
ATOM   1422  OG1 THR A 183      47.921  38.553  45.737  1.00 66.37           O  
ANISOU 1422  OG1 THR A 183     9429   8301   7487  -1243   -335    779       O  
ATOM   1423  N   MET A 184      46.968  36.594  41.917  1.00 60.72           N  
ANISOU 1423  N   MET A 184     8860   7427   6784  -1123   -204    803       N  
ATOM   1424  CA  MET A 184      46.124  36.108  40.849  1.00 61.95           C  
ANISOU 1424  CA  MET A 184     9089   7536   6914  -1078   -186    801       C  
ATOM   1425  C   MET A 184      46.245  34.582  40.734  1.00 62.20           C  
ANISOU 1425  C   MET A 184     9078   7571   6983  -1046   -195    835       C  
ATOM   1426  O   MET A 184      45.235  33.876  40.638  1.00 59.80           O  
ANISOU 1426  O   MET A 184     8802   7266   6654  -1018   -220    841       O  
ATOM   1427  CB  MET A 184      46.477  36.792  39.525  1.00 62.62           C  
ANISOU 1427  CB  MET A 184     9262   7546   6985  -1083   -117    781       C  
ATOM   1428  CG  MET A 184      45.808  36.128  38.333  1.00 68.22           C  
ANISOU 1428  CG  MET A 184    10049   8199   7673  -1031   -101    782       C  
ATOM   1429  SD  MET A 184      45.809  37.059  36.790  1.00 66.32           S  
ANISOU 1429  SD  MET A 184     9979   7850   7371  -1038    -44    757       S  
ATOM   1430  CE  MET A 184      47.395  37.870  36.906  1.00 68.54           C  
ANISOU 1430  CE  MET A 184    10227   8136   7678  -1135     43    750       C  
ATOM   1431  N   ARG A 185      47.476  34.071  40.761  1.00 62.66           N  
ANISOU 1431  N   ARG A 185     9066   7635   7108  -1049   -180    847       N  
ATOM   1432  CA  ARG A 185      47.709  32.635  40.601  1.00 60.67           C  
ANISOU 1432  CA  ARG A 185     8780   7373   6899  -1008   -203    871       C  
ATOM   1433  C   ARG A 185      46.910  31.824  41.594  1.00 60.27           C  
ANISOU 1433  C   ARG A 185     8737   7348   6815  -1006   -281    908       C  
ATOM   1434  O   ARG A 185      46.483  30.722  41.270  1.00 65.56           O  
ANISOU 1434  O   ARG A 185     9430   7994   7486   -976   -297    929       O  
ATOM   1435  CB  ARG A 185      49.191  32.283  40.697  1.00 60.19           C  
ANISOU 1435  CB  ARG A 185     8623   7320   6927  -1004   -201    853       C  
ATOM   1436  CG  ARG A 185      49.445  30.785  40.716  1.00 61.81           C  
ANISOU 1436  CG  ARG A 185     8795   7509   7181   -949   -257    872       C  
ATOM   1437  CD  ARG A 185      50.908  30.401  40.488  1.00 64.37           C  
ANISOU 1437  CD  ARG A 185     9012   7833   7612   -924   -252    820       C  
ATOM   1438  NE  ARG A 185      51.118  28.947  40.585  1.00 67.99           N  
ANISOU 1438  NE  ARG A 185     9449   8265   8120   -858   -335    833       N  
ATOM   1439  N   GLU A 186      46.700  32.342  42.796  1.00 58.88           N  
ANISOU 1439  N   GLU A 186     8551   7218   6603  -1048   -326    912       N  
ATOM   1440  CA  GLU A 186      45.872  31.628  43.772  1.00 58.22           C  
ANISOU 1440  CA  GLU A 186     8496   7160   6466  -1074   -383    940       C  
ATOM   1441  C   GLU A 186      44.401  31.653  43.369  1.00 55.01           C  
ANISOU 1441  C   GLU A 186     8141   6757   6005  -1079   -354    913       C  
ATOM   1442  O   GLU A 186      43.684  30.653  43.509  1.00 51.61           O  
ANISOU 1442  O   GLU A 186     7740   6322   5547  -1090   -370    928       O  
ATOM   1443  CB  GLU A 186      46.037  32.200  45.179  1.00 62.24           C  
ANISOU 1443  CB  GLU A 186     8989   7720   6941  -1128   -431    943       C  
ATOM   1444  CG  GLU A 186      47.403  31.927  45.801  1.00 70.69           C  
ANISOU 1444  CG  GLU A 186    10009   8786   8065  -1117   -494    964       C  
ATOM   1445  CD  GLU A 186      47.508  30.556  46.462  1.00 82.44           C  
ANISOU 1445  CD  GLU A 186    11537  10247   9538  -1111   -582   1013       C  
ATOM   1446  OE1 GLU A 186      48.110  30.456  47.565  1.00 91.13           O  
ANISOU 1446  OE1 GLU A 186    12641  11355  10630  -1127   -669   1031       O  
ATOM   1447  OE2 GLU A 186      46.979  29.574  45.892  1.00 88.33           O1-
ANISOU 1447  OE2 GLU A 186    12327  10957  10277  -1091   -575   1034       O1-
ATOM   1448  N   LYS A 187      43.940  32.782  42.849  1.00 53.78           N  
ANISOU 1448  N   LYS A 187     7999   6600   5834  -1071   -319    863       N  
ATOM   1449  CA  LYS A 187      42.559  32.847  42.404  1.00 55.28           C  
ANISOU 1449  CA  LYS A 187     8227   6790   5987  -1058   -309    812       C  
ATOM   1450  C   LYS A 187      42.345  31.855  41.238  1.00 52.26           C  
ANISOU 1450  C   LYS A 187     7876   6353   5627  -1007   -290    825       C  
ATOM   1451  O   LYS A 187      41.314  31.163  41.177  1.00 53.34           O  
ANISOU 1451  O   LYS A 187     8027   6496   5745  -1008   -297    803       O  
ATOM   1452  CB  LYS A 187      42.157  34.268  42.045  1.00 59.23           C  
ANISOU 1452  CB  LYS A 187     8753   7282   6469  -1042   -304    749       C  
ATOM   1453  CG  LYS A 187      42.213  35.214  43.238  1.00 64.19           C  
ANISOU 1453  CG  LYS A 187     9347   7968   7074  -1091   -327    726       C  
ATOM   1454  CD  LYS A 187      41.631  36.591  42.906  1.00 71.75           C  
ANISOU 1454  CD  LYS A 187    10342   8909   8012  -1067   -341    650       C  
ATOM   1455  CE  LYS A 187      42.483  37.779  43.390  1.00 78.73           C  
ANISOU 1455  CE  LYS A 187    11221   9797   8897  -1096   -345    654       C  
ATOM   1456  NZ  LYS A 187      43.259  38.473  42.299  1.00 84.14           N1+
ANISOU 1456  NZ  LYS A 187    11976  10400   9595  -1076   -314    669       N1+
ATOM   1457  N   VAL A 188      43.343  31.731  40.374  1.00 46.65           N  
ANISOU 1457  N   VAL A 188     7171   5594   4960   -972   -261    853       N  
ATOM   1458  CA  VAL A 188      43.245  30.843  39.235  1.00 45.48           C  
ANISOU 1458  CA  VAL A 188     7054   5393   4832   -922   -239    862       C  
ATOM   1459  C   VAL A 188      43.195  29.392  39.690  1.00 46.48           C  
ANISOU 1459  C   VAL A 188     7161   5524   4974   -927   -272    903       C  
ATOM   1460  O   VAL A 188      42.267  28.648  39.334  1.00 44.82           O  
ANISOU 1460  O   VAL A 188     6981   5300   4748   -914   -277    893       O  
ATOM   1461  CB  VAL A 188      44.389  31.080  38.240  1.00 44.52           C  
ANISOU 1461  CB  VAL A 188     6940   5226   4750   -900   -186    867       C  
ATOM   1462  CG1 VAL A 188      44.402  29.985  37.190  1.00 43.09           C  
ANISOU 1462  CG1 VAL A 188     6781   4998   4594   -852   -165    877       C  
ATOM   1463  CG2 VAL A 188      44.251  32.471  37.608  1.00 44.78           C  
ANISOU 1463  CG2 VAL A 188     7042   5229   4744   -905   -153    829       C  
ATOM   1464  N   LEU A 189      44.161  28.980  40.502  1.00 47.09           N  
ANISOU 1464  N   LEU A 189     7198   5615   5080   -945   -307    944       N  
ATOM   1465  CA  LEU A 189      44.082  27.632  41.048  1.00 48.97           C  
ANISOU 1465  CA  LEU A 189     7451   5841   5316   -953   -360    987       C  
ATOM   1466  C   LEU A 189      42.708  27.310  41.696  1.00 47.27           C  
ANISOU 1466  C   LEU A 189     7279   5653   5028  -1014   -370    978       C  
ATOM   1467  O   LEU A 189      42.137  26.277  41.420  1.00 49.20           O  
ANISOU 1467  O   LEU A 189     7561   5869   5264  -1014   -375    988       O  
ATOM   1468  CB  LEU A 189      45.233  27.366  42.007  1.00 50.86           C  
ANISOU 1468  CB  LEU A 189     7658   6083   5583   -961   -426   1022       C  
ATOM   1469  CG  LEU A 189      46.643  27.309  41.371  1.00 52.40           C  
ANISOU 1469  CG  LEU A 189     7787   6252   5871   -901   -421   1008       C  
ATOM   1470  CD1 LEU A 189      47.601  26.912  42.479  1.00 52.79           C  
ANISOU 1470  CD1 LEU A 189     7807   6302   5950   -900   -520   1028       C  
ATOM   1471  CD2 LEU A 189      46.809  26.391  40.146  1.00 50.40           C  
ANISOU 1471  CD2 LEU A 189     7535   5946   5667   -838   -396    999       C  
ATOM   1472  N   THR A 190      42.144  28.207  42.483  1.00 47.81           N  
ANISOU 1472  N   THR A 190     7339   5779   5048  -1070   -362    945       N  
ATOM   1473  CA  THR A 190      40.804  27.968  43.051  1.00 50.51           C  
ANISOU 1473  CA  THR A 190     7704   6160   5326  -1140   -351    905       C  
ATOM   1474  C   THR A 190      39.748  27.753  41.968  1.00 51.19           C  
ANISOU 1474  C   THR A 190     7796   6229   5424  -1103   -317    846       C  
ATOM   1475  O   THR A 190      39.029  26.752  41.956  1.00 53.71           O  
ANISOU 1475  O   THR A 190     8141   6540   5724  -1136   -311    840       O  
ATOM   1476  CB  THR A 190      40.340  29.150  43.912  1.00 51.05           C  
ANISOU 1476  CB  THR A 190     7743   6300   5352  -1194   -340    849       C  
ATOM   1477  CG2 THR A 190      38.936  28.925  44.485  1.00 49.77           C  
ANISOU 1477  CG2 THR A 190     7586   6192   5132  -1277   -313    777       C  
ATOM   1478  OG1 THR A 190      41.273  29.345  44.975  1.00 54.15           O  
ANISOU 1478  OG1 THR A 190     8136   6709   5729  -1231   -378    900       O  
ATOM   1479  N   SER A 191      39.698  28.692  41.037  1.00 50.88           N  
ANISOU 1479  N   SER A 191     7744   6176   5412  -1035   -300    800       N  
ATOM   1480  CA  SER A 191      38.833  28.612  39.855  1.00 49.70           C  
ANISOU 1480  CA  SER A 191     7613   5993   5277   -976   -288    740       C  
ATOM   1481  C   SER A 191      38.876  27.231  39.177  1.00 51.21           C  
ANISOU 1481  C   SER A 191     7833   6134   5492   -951   -285    782       C  
ATOM   1482  O   SER A 191      37.853  26.633  38.858  1.00 53.02           O  
ANISOU 1482  O   SER A 191     8068   6361   5715   -955   -281    734       O  
ATOM   1483  CB  SER A 191      39.306  29.688  38.865  1.00 48.17           C  
ANISOU 1483  CB  SER A 191     7446   5757   5102   -904   -283    726       C  
ATOM   1484  OG  SER A 191      38.425  29.828  37.794  1.00 49.73           O  
ANISOU 1484  OG  SER A 191     7682   5915   5299   -842   -291    659       O  
ATOM   1485  N   SER A 192      40.092  26.751  38.937  1.00 50.66           N  
ANISOU 1485  N   SER A 192     7771   6023   5455   -922   -290    858       N  
ATOM   1486  CA  SER A 192      40.334  25.503  38.252  1.00 48.50           C  
ANISOU 1486  CA  SER A 192     7522   5693   5213   -885   -295    895       C  
ATOM   1487  C   SER A 192      39.537  24.455  38.941  1.00 50.12           C  
ANISOU 1487  C   SER A 192     7748   5908   5386   -951   -313    901       C  
ATOM   1488  O   SER A 192      38.807  23.697  38.321  1.00 51.95           O  
ANISOU 1488  O   SER A 192     8004   6114   5623   -938   -306    878       O  
ATOM   1489  CB  SER A 192      41.814  25.175  38.368  1.00 49.19           C  
ANISOU 1489  CB  SER A 192     7591   5755   5344   -861   -313    957       C  
ATOM   1490  OG  SER A 192      42.186  24.131  37.530  1.00 50.05           O  
ANISOU 1490  OG  SER A 192     7714   5807   5496   -807   -317    976       O  
ATOM   1491  N   ALA A 193      39.661  24.452  40.261  1.00 51.95           N  
ANISOU 1491  N   ALA A 193     7984   6177   5577  -1032   -335    929       N  
ATOM   1492  CA  ALA A 193      39.131  23.400  41.090  1.00 52.10           C  
ANISOU 1492  CA  ALA A 193     8056   6194   5546  -1121   -352    952       C  
ATOM   1493  C   ALA A 193      37.634  23.529  41.114  1.00 52.65           C  
ANISOU 1493  C   ALA A 193     8111   6313   5580  -1184   -303    859       C  
ATOM   1494  O   ALA A 193      36.921  22.555  41.102  1.00 56.70           O  
ANISOU 1494  O   ALA A 193     8661   6809   6072  -1236   -291    847       O  
ATOM   1495  CB  ALA A 193      39.712  23.507  42.494  1.00 51.40           C  
ANISOU 1495  CB  ALA A 193     7996   6127   5409  -1195   -391   1003       C  
ATOM   1496  N   ARG A 194      37.161  24.756  41.108  1.00 54.10           N  
ANISOU 1496  N   ARG A 194     8237   6555   5765  -1174   -278    780       N  
ATOM   1497  CA  ARG A 194      35.741  25.023  41.207  1.00 54.40           C  
ANISOU 1497  CA  ARG A 194     8235   6651   5782  -1225   -241    658       C  
ATOM   1498  C   ARG A 194      35.007  24.448  40.015  1.00 51.32           C  
ANISOU 1498  C   ARG A 194     7842   6223   5433  -1166   -236    603       C  
ATOM   1499  O   ARG A 194      33.921  23.893  40.160  1.00 53.27           O  
ANISOU 1499  O   ARG A 194     8075   6499   5667  -1235   -206    525       O  
ATOM   1500  CB  ARG A 194      35.549  26.528  41.333  1.00 57.56           C  
ANISOU 1500  CB  ARG A 194     8577   7105   6189  -1195   -242    580       C  
ATOM   1501  CG  ARG A 194      34.172  27.007  41.765  1.00 59.83           C  
ANISOU 1501  CG  ARG A 194     8800   7473   6460  -1254   -214    429       C  
ATOM   1502  CD  ARG A 194      34.288  28.351  42.500  1.00 57.65           C  
ANISOU 1502  CD  ARG A 194     8482   7255   6167  -1263   -222    384       C  
ATOM   1503  NE  ARG A 194      34.538  28.154  43.927  1.00 59.12           N  
ANISOU 1503  NE  ARG A 194     8684   7494   6286  -1393   -195    426       N  
ATOM   1504  CZ  ARG A 194      35.037  29.060  44.755  1.00 61.08           C  
ANISOU 1504  CZ  ARG A 194     8920   7781   6508  -1416   -206    439       C  
ATOM   1505  NH1 ARG A 194      35.382  30.275  44.303  1.00 70.96           N1+
ANISOU 1505  NH1 ARG A 194    10142   9021   7798  -1320   -241    416       N1+
ATOM   1506  NH2 ARG A 194      35.207  28.756  46.033  1.00 58.12           N  
ANISOU 1506  NH2 ARG A 194     8578   7445   6059  -1539   -186    476       N  
ATOM   1507  N   GLN A 195      35.629  24.548  38.845  1.00 49.19           N  
ANISOU 1507  N   GLN A 195     7590   5889   5211  -1047   -259    640       N  
ATOM   1508  CA  GLN A 195      35.064  24.051  37.577  1.00 47.93           C  
ANISOU 1508  CA  GLN A 195     7442   5681   5088   -973   -264    596       C  
ATOM   1509  C   GLN A 195      35.273  22.542  37.424  1.00 51.07           C  
ANISOU 1509  C   GLN A 195     7887   6027   5492   -996   -264    666       C  
ATOM   1510  O   GLN A 195      34.534  21.859  36.673  1.00 51.27           O  
ANISOU 1510  O   GLN A 195     7918   6024   5537   -974   -261    618       O  
ATOM   1511  CB  GLN A 195      35.761  24.764  36.425  1.00 45.35           C  
ANISOU 1511  CB  GLN A 195     7141   5298   4791   -853   -282    616       C  
ATOM   1512  CG  GLN A 195      35.239  24.530  35.026  1.00 45.53           C  
ANISOU 1512  CG  GLN A 195     7196   5263   4839   -763   -296    565       C  
ATOM   1513  CD  GLN A 195      33.800  24.983  34.823  1.00 47.86           C  
ANISOU 1513  CD  GLN A 195     7457   5588   5139   -747   -322    420       C  
ATOM   1514  NE2 GLN A 195      33.166  24.470  33.773  1.00 46.53           N  
ANISOU 1514  NE2 GLN A 195     7311   5374   4994   -683   -344    367       N  
ATOM   1515  OE1 GLN A 195      33.260  25.775  35.599  1.00 49.49           O  
ANISOU 1515  OE1 GLN A 195     7611   5859   5333   -787   -327    345       O  
ATOM   1516  N   ARG A 196      36.316  22.021  38.070  1.00 50.53           N  
ANISOU 1516  N   ARG A 196     7856   5934   5410  -1027   -280    774       N  
ATOM   1517  CA  ARG A 196      36.614  20.615  37.917  1.00 50.06           C  
ANISOU 1517  CA  ARG A 196     7854   5808   5357  -1034   -302    841       C  
ATOM   1518  C   ARG A 196      35.547  19.864  38.669  1.00 50.67           C  
ANISOU 1518  C   ARG A 196     7961   5908   5382  -1163   -279    806       C  
ATOM   1519  O   ARG A 196      35.122  18.793  38.217  1.00 50.21           O  
ANISOU 1519  O   ARG A 196     7942   5803   5332  -1173   -280    804       O  
ATOM   1520  CB  ARG A 196      38.001  20.252  38.422  1.00 49.93           C  
ANISOU 1520  CB  ARG A 196     7873   5752   5348  -1019   -350    947       C  
ATOM   1521  CG  ARG A 196      38.375  18.801  38.157  1.00 51.00           C  
ANISOU 1521  CG  ARG A 196     8075   5803   5501  -1001   -395   1007       C  
ATOM   1522  CD  ARG A 196      38.745  18.623  36.691  1.00 51.99           C  
ANISOU 1522  CD  ARG A 196     8175   5882   5696   -877   -389    993       C  
ATOM   1523  NE  ARG A 196      38.981  17.238  36.299  1.00 52.14           N  
ANISOU 1523  NE  ARG A 196     8249   5821   5741   -848   -432   1031       N  
ATOM   1524  CZ  ARG A 196      38.028  16.343  36.064  1.00 52.87           C  
ANISOU 1524  CZ  ARG A 196     8388   5885   5817   -888   -426   1011       C  
ATOM   1525  NH1 ARG A 196      36.737  16.642  36.224  1.00 53.41           N1+
ANISOU 1525  NH1 ARG A 196     8442   6005   5847   -966   -375    941       N1+
ATOM   1526  NH2 ARG A 196      38.367  15.129  35.665  1.00 52.38           N  
ANISOU 1526  NH2 ARG A 196     8380   5741   5783   -851   -473   1048       N  
ATOM   1527  N   LEU A 197      35.078  20.455  39.775  1.00 50.12           N  
ANISOU 1527  N   LEU A 197     7873   5913   5258  -1268   -250    766       N  
ATOM   1528  CA  LEU A 197      33.943  19.903  40.529  1.00 51.14           C  
ANISOU 1528  CA  LEU A 197     8022   6082   5328  -1421   -201    702       C  
ATOM   1529  C   LEU A 197      32.654  20.015  39.733  1.00 51.91           C  
ANISOU 1529  C   LEU A 197     8042   6217   5467  -1406   -160    557       C  
ATOM   1530  O   LEU A 197      31.830  19.115  39.755  1.00 54.37           O  
ANISOU 1530  O   LEU A 197     8373   6523   5762  -1494   -125    510       O  
ATOM   1531  CB  LEU A 197      33.783  20.589  41.880  1.00 51.74           C  
ANISOU 1531  CB  LEU A 197     8091   6236   5333  -1540   -170    678       C  
ATOM   1532  CG  LEU A 197      32.522  20.235  42.648  1.00 52.89           C  
ANISOU 1532  CG  LEU A 197     8238   6445   5413  -1716    -92    576       C  
ATOM   1533  CD1 LEU A 197      32.372  18.726  42.801  1.00 52.02           C  
ANISOU 1533  CD1 LEU A 197     8251   6262   5254  -1818    -86    636       C  
ATOM   1534  CD2 LEU A 197      32.570  20.950  43.993  1.00 52.76           C  
ANISOU 1534  CD2 LEU A 197     8226   6501   5319  -1828    -63    565       C  
ATOM   1535  N   ARG A 198      32.494  21.091  38.979  1.00 52.41           N  
ANISOU 1535  N   ARG A 198     8025   6304   5583  -1290   -175    483       N  
ATOM   1536  CA  ARG A 198      31.372  21.158  38.049  1.00 52.12           C  
ANISOU 1536  CA  ARG A 198     7925   6280   5597  -1239   -170    345       C  
ATOM   1537  C   ARG A 198      31.384  20.058  36.989  1.00 51.56           C  
ANISOU 1537  C   ARG A 198     7901   6127   5561  -1180   -189    379       C  
ATOM   1538  O   ARG A 198      30.388  19.347  36.832  1.00 51.76           O  
ANISOU 1538  O   ARG A 198     7908   6163   5598  -1237   -163    292       O  
ATOM   1539  CB  ARG A 198      31.314  22.502  37.383  1.00 52.09           C  
ANISOU 1539  CB  ARG A 198     7869   6290   5634  -1111   -209    273       C  
ATOM   1540  CG  ARG A 198      30.888  23.573  38.346  1.00 52.75           C  
ANISOU 1540  CG  ARG A 198     7883   6464   5694  -1170   -192    183       C  
ATOM   1541  CD  ARG A 198      30.506  24.847  37.629  1.00 55.37           C  
ANISOU 1541  CD  ARG A 198     8169   6799   6068  -1044   -248     74       C  
ATOM   1542  NE  ARG A 198      30.551  25.933  38.596  1.00 55.53           N  
ANISOU 1542  NE  ARG A 198     8145   6889   6064  -1085   -242     35       N  
ATOM   1543  CZ  ARG A 198      31.490  26.854  38.680  1.00 53.13           C  
ANISOU 1543  CZ  ARG A 198     7876   6565   5747  -1032   -270    115       C  
ATOM   1544  NH1 ARG A 198      32.500  26.912  37.818  1.00 52.89           N1+
ANISOU 1544  NH1 ARG A 198     7921   6448   5725   -938   -299    230       N1+
ATOM   1545  NH2 ARG A 198      31.394  27.734  39.661  1.00 55.91           N  
ANISOU 1545  NH2 ARG A 198     8181   6987   6076  -1085   -261     65       N  
ATOM   1546  N   CYS A 199      32.494  19.885  36.287  1.00 50.37           N  
ANISOU 1546  N   CYS A 199     7807   5900   5432  -1074   -229    495       N  
ATOM   1547  CA  CYS A 199      32.559  18.807  35.288  1.00 52.71           C  
ANISOU 1547  CA  CYS A 199     8148   6117   5761  -1016   -247    526       C  
ATOM   1548  C   CYS A 199      32.443  17.400  35.889  1.00 54.46           C  
ANISOU 1548  C   CYS A 199     8433   6306   5951  -1131   -233    578       C  
ATOM   1549  O   CYS A 199      31.798  16.539  35.314  1.00 55.23           O  
ANISOU 1549  O   CYS A 199     8544   6372   6070  -1138   -229    537       O  
ATOM   1550  CB  CYS A 199      33.830  18.880  34.475  1.00 51.95           C  
ANISOU 1550  CB  CYS A 199     8092   5953   5692   -893   -280    625       C  
ATOM   1551  SG  CYS A 199      34.013  20.438  33.571  1.00 52.44           S  
ANISOU 1551  SG  CYS A 199     8130   6022   5772   -769   -294    574       S  
ATOM   1552  N   ALA A 200      33.047  17.181  37.047  1.00 54.57           N  
ANISOU 1552  N   ALA A 200     8501   6322   5910  -1224   -234    666       N  
ATOM   1553  CA  ALA A 200      32.943  15.884  37.719  1.00 55.46           C  
ANISOU 1553  CA  ALA A 200     8714   6388   5973  -1348   -233    722       C  
ATOM   1554  C   ALA A 200      31.489  15.585  38.073  1.00 57.73           C  
ANISOU 1554  C   ALA A 200     8976   6730   6228  -1493   -161    599       C  
ATOM   1555  O   ALA A 200      31.023  14.470  37.889  1.00 58.45           O  
ANISOU 1555  O   ALA A 200     9125   6771   6311  -1557   -150    594       O  
ATOM   1556  CB  ALA A 200      33.822  15.849  38.960  1.00 54.09           C  
ANISOU 1556  CB  ALA A 200     8620   6201   5732  -1419   -263    829       C  
ATOM   1557  N   SER A 201      30.767  16.590  38.555  1.00 60.79           N  
ANISOU 1557  N   SER A 201     9272   7222   6606  -1547   -109    485       N  
ATOM   1558  CA  SER A 201      29.358  16.428  38.900  1.00 62.46           C  
ANISOU 1558  CA  SER A 201     9426   7505   6800  -1688    -29    329       C  
ATOM   1559  C   SER A 201      28.571  15.920  37.719  1.00 65.75           C  
ANISOU 1559  C   SER A 201     9792   7898   7291  -1623    -33    232       C  
ATOM   1560  O   SER A 201      27.893  14.912  37.815  1.00 69.17           O  
ANISOU 1560  O   SER A 201    10260   8316   7706  -1742     11    191       O  
ATOM   1561  CB  SER A 201      28.755  17.757  39.365  1.00 60.71           C  
ANISOU 1561  CB  SER A 201     9080   7402   6586  -1705      9    192       C  
ATOM   1562  OG  SER A 201      29.461  18.224  40.477  1.00 59.33           O  
ANISOU 1562  OG  SER A 201     8954   7250   6340  -1769     13    278       O  
ATOM   1563  N   ILE A 202      28.655  16.616  36.590  1.00 65.51           N  
ANISOU 1563  N   ILE A 202     9969   7229   7691   -133    432    254       N  
ATOM   1564  CA  ILE A 202      27.810  16.236  35.455  1.00 68.98           C  
ANISOU 1564  CA  ILE A 202    10540   7558   8112   -166    420    119       C  
ATOM   1565  C   ILE A 202      28.243  14.868  34.937  1.00 64.39           C  
ANISOU 1565  C   ILE A 202    10084   6810   7571   -147    573    173       C  
ATOM   1566  O   ILE A 202      27.416  14.057  34.601  1.00 63.58           O  
ANISOU 1566  O   ILE A 202    10063   6627   7469   -220    599     89       O  
ATOM   1567  CB  ILE A 202      27.754  17.295  34.306  1.00 73.01           C  
ANISOU 1567  CB  ILE A 202    11120   8060   8562   -137    336     23       C  
ATOM   1568  CG1 ILE A 202      29.000  17.263  33.432  1.00 76.25           C  
ANISOU 1568  CG1 ILE A 202    11630   8371   8972    -52    425     95       C  
ATOM   1569  CG2 ILE A 202      27.586  18.707  34.859  1.00 68.49           C  
ANISOU 1569  CG2 ILE A 202    10437   7628   7958   -132    222     -2       C  
ATOM   1570  CD1 ILE A 202      28.958  18.266  32.303  1.00 84.26           C  
ANISOU 1570  CD1 ILE A 202    12721   9372   9922    -25    350      8       C  
ATOM   1571  N   GLN A 203      29.537  14.606  34.913  1.00 64.29           N  
ANISOU 1571  N   GLN A 203    10085   6748   7594    -54    685    317       N  
ATOM   1572  CA  GLN A 203      30.017  13.365  34.352  1.00 68.29           C  
ANISOU 1572  CA  GLN A 203    10726   7076   8145    -16    857    375       C  
ATOM   1573  C   GLN A 203      29.648  12.137  35.202  1.00 68.46           C  
ANISOU 1573  C   GLN A 203    10735   7053   8225    -54    953    435       C  
ATOM   1574  O   GLN A 203      29.288  11.092  34.662  1.00 68.74           O  
ANISOU 1574  O   GLN A 203    10916   6928   8276    -91   1062    386       O  
ATOM   1575  CB  GLN A 203      31.520  13.414  34.130  1.00 72.86           C  
ANISOU 1575  CB  GLN A 203    11306   7623   8755    111    964    535       C  
ATOM   1576  CG  GLN A 203      31.968  12.452  33.035  1.00 81.19           C  
ANISOU 1576  CG  GLN A 203    12551   8462   9834    161   1137    543       C  
ATOM   1577  CD  GLN A 203      33.464  12.217  33.054  1.00 86.21           C  
ANISOU 1577  CD  GLN A 203    13163   9066  10528    302   1282    744       C  
ATOM   1578  NE2 GLN A 203      34.175  12.844  32.104  1.00 92.43           N  
ANISOU 1578  NE2 GLN A 203    14010   9825  11286    362   1290    736       N  
ATOM   1579  OE1 GLN A 203      33.983  11.493  33.916  1.00 82.01           O  
ANISOU 1579  OE1 GLN A 203    12551   8543  10065    361   1387    915       O  
ATOM   1580  N   LYS A 204      29.685  12.285  36.518  1.00 65.75           N  
ANISOU 1580  N   LYS A 204    10227   6851   7903    -59    914    531       N  
ATOM   1581  CA  LYS A 204      29.477  11.159  37.430  1.00 66.97           C  
ANISOU 1581  CA  LYS A 204    10356   6976   8115    -81   1012    620       C  
ATOM   1582  C   LYS A 204      28.092  11.152  38.083  1.00 64.51           C  
ANISOU 1582  C   LYS A 204     9989   6741   7782   -211    912    499       C  
ATOM   1583  O   LYS A 204      27.723  10.162  38.663  1.00 66.83           O  
ANISOU 1583  O   LYS A 204    10292   6984   8115   -250    995    538       O  
ATOM   1584  CB  LYS A 204      30.531  11.167  38.563  1.00 66.55           C  
ANISOU 1584  CB  LYS A 204    10149   7040   8097      2   1053    843       C  
ATOM   1585  CG  LYS A 204      31.991  11.213  38.112  1.00 67.05           C  
ANISOU 1585  CG  LYS A 204    10219   7071   8187    138   1151   1001       C  
ATOM   1586  CD  LYS A 204      32.477   9.938  37.418  1.00 66.46           C  
ANISOU 1586  CD  LYS A 204    10300   6771   8181    222   1366   1079       C  
ATOM   1587  N   PHE A 205      27.348  12.249  38.044  1.00 61.95           N  
ANISOU 1587  N   PHE A 205     9599   6539   7399   -270    746    365       N  
ATOM   1588  CA  PHE A 205      26.051  12.290  38.732  1.00 62.46           C  
ANISOU 1588  CA  PHE A 205     9588   6694   7450   -382    658    265       C  
ATOM   1589  C   PHE A 205      24.953  12.942  37.911  1.00 62.40           C  
ANISOU 1589  C   PHE A 205     9612   6711   7387   -452    532     74       C  
ATOM   1590  O   PHE A 205      23.872  13.211  38.435  1.00 64.58           O  
ANISOU 1590  O   PHE A 205     9801   7087   7648   -532    443     -9       O  
ATOM   1591  CB  PHE A 205      26.175  13.035  40.065  1.00 62.15           C  
ANISOU 1591  CB  PHE A 205     9371   6841   7401   -382    585    337       C  
ATOM   1592  CG  PHE A 205      27.204  12.454  41.001  1.00 63.26           C  
ANISOU 1592  CG  PHE A 205     9448   7006   7581   -324    686    543       C  
ATOM   1593  CD1 PHE A 205      26.828  11.685  42.078  1.00 62.65           C  
ANISOU 1593  CD1 PHE A 205     9312   6962   7532   -372    733    610       C  
ATOM   1594  CD2 PHE A 205      28.547  12.708  40.816  1.00 63.14           C  
ANISOU 1594  CD2 PHE A 205     9422   6997   7571   -221    732    679       C  
ATOM   1595  CE1 PHE A 205      27.782  11.157  42.936  1.00 63.92           C  
ANISOU 1595  CE1 PHE A 205     9404   7161   7723   -311    823    820       C  
ATOM   1596  CE2 PHE A 205      29.498  12.191  41.673  1.00 63.01           C  
ANISOU 1596  CE2 PHE A 205     9324   7030   7586   -163    818    889       C  
ATOM   1597  CZ  PHE A 205      29.118  11.405  42.729  1.00 62.20           C  
ANISOU 1597  CZ  PHE A 205     9164   6961   7509   -204    863    964       C  
ATOM   1598  N   GLY A 206      25.230  13.214  36.640  1.00 62.00           N  
ANISOU 1598  N   GLY A 206     9676   6578   7304   -417    525     16       N  
ATOM   1599  CA  GLY A 206      24.272  13.855  35.766  1.00 66.03           C  
ANISOU 1599  CA  GLY A 206    10215   7122   7753   -471    403   -143       C  
ATOM   1600  C   GLY A 206      24.054  15.345  36.001  1.00 70.44           C  
ANISOU 1600  C   GLY A 206    10656   7832   8277   -436    261   -178       C  
ATOM   1601  O   GLY A 206      24.336  15.881  37.082  1.00 70.31           O  
ANISOU 1601  O   GLY A 206    10517   7919   8277   -411    242   -109       O  
ATOM   1602  N   GLU A 207      23.535  15.998  34.959  1.00 76.47           N  
ANISOU 1602  N   GLU A 207    11467   8605   8985   -440    170   -284       N  
ATOM   1603  CA  GLU A 207      23.120  17.400  34.989  1.00 78.53           C  
ANISOU 1603  CA  GLU A 207    11640   8987   9210   -405     43   -333       C  
ATOM   1604  C   GLU A 207      22.344  17.739  36.244  1.00 77.40           C  
ANISOU 1604  C   GLU A 207    11342   8976   9090   -443     -6   -342       C  
ATOM   1605  O   GLU A 207      22.601  18.739  36.885  1.00 78.01           O  
ANISOU 1605  O   GLU A 207    11339   9134   9165   -397    -39   -314       O  
ATOM   1606  CB  GLU A 207      22.205  17.702  33.801  1.00 82.82           C  
ANISOU 1606  CB  GLU A 207    12236   9540   9693   -435    -51   -450       C  
ATOM   1607  CG  GLU A 207      22.865  17.644  32.435  1.00 89.17           C  
ANISOU 1607  CG  GLU A 207    13198  10231  10450   -399    -23   -461       C  
ATOM   1608  CD  GLU A 207      21.985  18.229  31.336  1.00 97.55           C  
ANISOU 1608  CD  GLU A 207    14287  11343  11434   -419   -142   -560       C  
ATOM   1609  OE1 GLU A 207      20.932  18.832  31.673  1.00 96.99           O  
ANISOU 1609  OE1 GLU A 207    14094  11402  11355   -436   -247   -605       O  
ATOM   1610  OE2 GLU A 207      22.348  18.083  30.136  1.00 96.08           O1-
ANISOU 1610  OE2 GLU A 207    14241  11071  11193   -415   -126   -585       O1-
ATOM   1611  N   ARG A 208      21.361  16.910  36.564  1.00 80.29           N  
ANISOU 1611  N   ARG A 208    11676   9359   9472   -539     -5   -389       N  
ATOM   1612  CA  ARG A 208      20.495  17.137  37.713  1.00 81.06           C  
ANISOU 1612  CA  ARG A 208    11629   9579   9589   -585    -44   -406       C  
ATOM   1613  C   ARG A 208      21.277  17.628  38.942  1.00 80.67           C  
ANISOU 1613  C   ARG A 208    11501   9589   9563   -541     -8   -310       C  
ATOM   1614  O   ARG A 208      20.824  18.529  39.661  1.00 76.31           O  
ANISOU 1614  O   ARG A 208    10847   9145   9002   -536    -59   -335       O  
ATOM   1615  CB  ARG A 208      19.747  15.843  38.032  1.00 86.54           C  
ANISOU 1615  CB  ARG A 208    12322  10250  10309   -699      3   -429       C  
ATOM   1616  CG  ARG A 208      18.640  15.967  39.062  1.00 90.73           C  
ANISOU 1616  CG  ARG A 208    12707  10909  10857   -763    -39   -465       C  
ATOM   1617  CD  ARG A 208      17.764  14.714  39.053  1.00 97.16           C  
ANISOU 1617  CD  ARG A 208    13539  11695  11684   -895     -4   -513       C  
ATOM   1618  NE  ARG A 208      16.720  14.771  40.074  1.00 97.34           N  
ANISOU 1618  NE  ARG A 208    13417  11842  11727   -960    -33   -540       N  
ATOM   1619  CZ  ARG A 208      16.873  14.432  41.354  1.00 99.35           C  
ANISOU 1619  CZ  ARG A 208    13609  12122  12017   -979     33   -472       C  
ATOM   1620  NH1 ARG A 208      18.043  13.984  41.808  1.00 98.12           N1+
ANISOU 1620  NH1 ARG A 208    13511  11886  11883   -936    127   -358       N1+
ATOM   1621  NH2 ARG A 208      15.842  14.539  42.193  1.00100.54           N  
ANISOU 1621  NH2 ARG A 208    13633  12389  12181  -1042      6   -509       N  
ATOM   1622  N   ALA A 209      22.458  17.049  39.165  1.00 79.36           N  
ANISOU 1622  N   ALA A 209    11383   9354   9418   -511     85   -198       N  
ATOM   1623  CA  ALA A 209      23.280  17.394  40.319  1.00 78.05           C  
ANISOU 1623  CA  ALA A 209    11137   9262   9258   -488    116    -90       C  
ATOM   1624  C   ALA A 209      23.843  18.805  40.221  1.00 79.97           C  
ANISOU 1624  C   ALA A 209    11363   9562   9461   -429     63    -94       C  
ATOM   1625  O   ALA A 209      23.938  19.518  41.228  1.00 75.65           O  
ANISOU 1625  O   ALA A 209    10729   9120   8894   -447     47    -73       O  
ATOM   1626  CB  ALA A 209      24.415  16.399  40.453  1.00 80.07           C  
ANISOU 1626  CB  ALA A 209    11437   9439   9545   -458    229     50       C  
ATOM   1627  N   LEU A 210      24.234  19.198  39.010  1.00 76.18           N  
ANISOU 1627  N   LEU A 210    10977   9007   8961   -368     46   -122       N  
ATOM   1628  CA  LEU A 210      24.727  20.544  38.773  1.00 77.36           C  
ANISOU 1628  CA  LEU A 210    11131   9190   9072   -314      2   -134       C  
ATOM   1629  C   LEU A 210      23.601  21.585  38.889  1.00 76.71           C  
ANISOU 1629  C   LEU A 210    10998   9181   8969   -320    -80   -243       C  
ATOM   1630  O   LEU A 210      23.801  22.660  39.477  1.00 75.20           O  
ANISOU 1630  O   LEU A 210    10767   9054   8753   -312    -92   -245       O  
ATOM   1631  CB  LEU A 210      25.413  20.631  37.403  1.00 80.32           C  
ANISOU 1631  CB  LEU A 210    11628   9460   9431   -247     13   -131       C  
ATOM   1632  CG  LEU A 210      26.108  21.950  37.036  1.00 80.71           C  
ANISOU 1632  CG  LEU A 210    11703   9522   9441   -190    -14   -130       C  
ATOM   1633  CD1 LEU A 210      27.241  22.261  37.997  1.00 82.31           C  
ANISOU 1633  CD1 LEU A 210    11844   9792   9637   -201     32    -22       C  
ATOM   1634  CD2 LEU A 210      26.636  21.862  35.620  1.00 80.49           C  
ANISOU 1634  CD2 LEU A 210    11802   9383   9397   -130      2   -133       C  
ATOM   1635  N   LYS A 211      22.423  21.270  38.349  1.00 74.18           N  
ANISOU 1635  N   LYS A 211    10678   8852   8654   -339   -128   -328       N  
ATOM   1636  CA  LYS A 211      21.257  22.154  38.509  1.00 74.87           C  
ANISOU 1636  CA  LYS A 211    10693   9020   8733   -333   -197   -413       C  
ATOM   1637  C   LYS A 211      21.042  22.452  39.984  1.00 69.59           C  
ANISOU 1637  C   LYS A 211     9920   8444   8076   -375   -171   -399       C  
ATOM   1638  O   LYS A 211      20.987  23.597  40.397  1.00 69.11           O  
ANISOU 1638  O   LYS A 211     9833   8429   7997   -346   -177   -422       O  
ATOM   1639  CB  LYS A 211      19.996  21.521  37.930  1.00 76.62           C  
ANISOU 1639  CB  LYS A 211    10895   9255   8961   -373   -249   -485       C  
ATOM   1640  CG  LYS A 211      20.055  21.389  36.422  1.00 80.98           C  
ANISOU 1640  CG  LYS A 211    11554   9736   9479   -345   -288   -515       C  
ATOM   1641  CD  LYS A 211      18.685  21.321  35.755  1.00 83.97           C  
ANISOU 1641  CD  LYS A 211    11891  10176   9837   -377   -375   -594       C  
ATOM   1642  CE  LYS A 211      18.842  21.263  34.230  1.00 86.99           C  
ANISOU 1642  CE  LYS A 211    12391  10497  10163   -357   -416   -620       C  
ATOM   1643  NZ  LYS A 211      17.640  20.760  33.500  1.00 88.63           N1+
ANISOU 1643  NZ  LYS A 211    12574  10766  10334   -435   -494   -688       N1+
ATOM   1644  N   ALA A 212      20.970  21.407  40.783  1.00 68.81           N  
ANISOU 1644  N   ALA A 212     9775   8365   8003   -448   -128   -360       N  
ATOM   1645  CA  ALA A 212      20.691  21.580  42.186  1.00 72.13           C  
ANISOU 1645  CA  ALA A 212    10100   8881   8427   -502   -102   -348       C  
ATOM   1646  C   ALA A 212      21.709  22.546  42.825  1.00 75.80           C  
ANISOU 1646  C   ALA A 212    10569   9382   8851   -490    -76   -301       C  
ATOM   1647  O   ALA A 212      21.321  23.463  43.564  1.00 74.26           O  
ANISOU 1647  O   ALA A 212    10328   9255   8634   -505    -73   -344       O  
ATOM   1648  CB  ALA A 212      20.685  20.233  42.892  1.00 70.23           C  
ANISOU 1648  CB  ALA A 212     9826   8643   8214   -577    -51   -288       C  
ATOM   1649  N   TRP A 213      22.994  22.360  42.514  1.00 75.66           N  
ANISOU 1649  N   TRP A 213    10608   9320   8819   -469    -48   -215       N  
ATOM   1650  CA  TRP A 213      24.040  23.252  43.008  1.00 78.06           C  
ANISOU 1650  CA  TRP A 213    10915   9669   9074   -476    -28   -166       C  
ATOM   1651  C   TRP A 213      23.696  24.673  42.675  1.00 74.05           C  
ANISOU 1651  C   TRP A 213    10442   9155   8537   -438    -56   -258       C  
ATOM   1652  O   TRP A 213      23.672  25.538  43.549  1.00 77.01           O  
ANISOU 1652  O   TRP A 213    10792   9596   8874   -481    -36   -283       O  
ATOM   1653  CB  TRP A 213      25.393  22.894  42.403  1.00 89.25           C  
ANISOU 1653  CB  TRP A 213    12389  11035  10488   -439      0    -63       C  
ATOM   1654  CG  TRP A 213      26.572  23.598  43.046  1.00 99.62           C  
ANISOU 1654  CG  TRP A 213    13680  12425  11745   -476     22     12       C  
ATOM   1655  CD1 TRP A 213      27.036  24.884  42.782  1.00102.53           C  
ANISOU 1655  CD1 TRP A 213    14096  12797  12065   -468     10    -26       C  
ATOM   1656  CD2 TRP A 213      27.490  23.060  44.072  1.00110.16           C  
ANISOU 1656  CD2 TRP A 213    14939  13859  13057   -537     60    149       C  
ATOM   1657  CE2 TRP A 213      28.461  24.126  44.355  1.00115.05           C  
ANISOU 1657  CE2 TRP A 213    15557  14552  13605   -580     59    178       C  
ATOM   1658  CE3 TRP A 213      27.593  21.851  44.763  1.00116.18           C  
ANISOU 1658  CE3 TRP A 213    15637  14661  13847   -564     96    256       C  
ATOM   1659  NE1 TRP A 213      28.131  25.177  43.559  1.00113.54           N  
ANISOU 1659  NE1 TRP A 213    15449  14288  13404   -538     36     63       N  
ATOM   1660  CZ2 TRP A 213      29.490  23.966  45.301  1.00120.75           C  
ANISOU 1660  CZ2 TRP A 213    16198  15406  14275   -655     80    311       C  
ATOM   1661  CZ3 TRP A 213      28.628  21.695  45.708  1.00121.76           C  
ANISOU 1661  CZ3 TRP A 213    16263  15491  14509   -618    122    401       C  
ATOM   1662  CH2 TRP A 213      29.556  22.730  45.972  1.00126.14           C  
ANISOU 1662  CH2 TRP A 213    16802  16139  14986   -667    107    429       C  
ATOM   1663  N   SER A 214      23.411  24.914  41.408  1.00 68.04           N  
ANISOU 1663  N   SER A 214     9749   8314   7790   -358    -94   -306       N  
ATOM   1664  CA  SER A 214      23.110  26.249  40.916  1.00 69.14           C  
ANISOU 1664  CA  SER A 214     9933   8429   7907   -296   -114   -377       C  
ATOM   1665  C   SER A 214      21.884  26.900  41.559  1.00 67.28           C  
ANISOU 1665  C   SER A 214     9635   8247   7680   -298   -115   -456       C  
ATOM   1666  O   SER A 214      21.963  28.032  42.052  1.00 68.81           O  
ANISOU 1666  O   SER A 214     9848   8453   7844   -298    -78   -487       O  
ATOM   1667  CB  SER A 214      22.929  26.195  39.403  1.00 69.95           C  
ANISOU 1667  CB  SER A 214    10111   8448   8020   -212   -161   -401       C  
ATOM   1668  OG  SER A 214      24.169  25.859  38.825  1.00 70.58           O  
ANISOU 1668  OG  SER A 214    10262   8469   8086   -201   -139   -332       O  
ATOM   1669  N   VAL A 215      20.761  26.190  41.554  1.00 63.00           N  
ANISOU 1669  N   VAL A 215     9025   7735   7179   -303   -146   -488       N  
ATOM   1670  CA  VAL A 215      19.586  26.634  42.291  1.00 62.79           C  
ANISOU 1670  CA  VAL A 215     8916   7773   7169   -308   -134   -547       C  
ATOM   1671  C   VAL A 215      19.970  27.157  43.704  1.00 64.43           C  
ANISOU 1671  C   VAL A 215     9103   8034   7342   -383    -62   -543       C  
ATOM   1672  O   VAL A 215      19.526  28.209  44.132  1.00 65.78           O  
ANISOU 1672  O   VAL A 215     9276   8216   7502   -361    -21   -597       O  
ATOM   1673  CB  VAL A 215      18.560  25.488  42.429  1.00 62.30           C  
ANISOU 1673  CB  VAL A 215     8763   7759   7149   -352   -163   -560       C  
ATOM   1674  CG1 VAL A 215      17.454  25.880  43.411  1.00 63.14           C  
ANISOU 1674  CG1 VAL A 215     8770   7947   7275   -370   -134   -609       C  
ATOM   1675  CG2 VAL A 215      17.963  25.128  41.081  1.00 56.64           C  
ANISOU 1675  CG2 VAL A 215     8060   7012   6448   -301   -237   -584       C  
ATOM   1676  N   ALA A 216      20.802  26.415  44.424  1.00 65.38           N  
ANISOU 1676  N   ALA A 216     9210   8191   7441   -472    -39   -475       N  
ATOM   1677  CA  ALA A 216      21.252  26.845  45.734  1.00 65.34           C  
ANISOU 1677  CA  ALA A 216     9187   8257   7382   -565     19   -462       C  
ATOM   1678  C   ALA A 216      22.001  28.145  45.607  1.00 68.08           C  
ANISOU 1678  C   ALA A 216     9621   8572   7674   -555     49   -483       C  
ATOM   1679  O   ALA A 216      21.671  29.143  46.249  1.00 71.45           O  
ANISOU 1679  O   ALA A 216    10067   9013   8068   -580    104   -547       O  
ATOM   1680  CB  ALA A 216      22.149  25.805  46.344  1.00 66.44           C  
ANISOU 1680  CB  ALA A 216     9294   8450   7503   -648     27   -357       C  
ATOM   1681  N   ARG A 217      23.018  28.125  44.761  1.00 70.41           N  
ANISOU 1681  N   ARG A 217     9979   8815   7957   -523     25   -431       N  
ATOM   1682  CA  ARG A 217      23.941  29.228  44.670  1.00 71.11           C  
ANISOU 1682  CA  ARG A 217    10151   8881   7986   -540     57   -435       C  
ATOM   1683  C   ARG A 217      23.214  30.527  44.320  1.00 69.06           C  
ANISOU 1683  C   ARG A 217     9958   8552   7729   -467     88   -533       C  
ATOM   1684  O   ARG A 217      23.436  31.553  44.967  1.00 67.30           O  
ANISOU 1684  O   ARG A 217     9787   8333   7451   -525    155   -577       O  
ATOM   1685  CB  ARG A 217      25.031  28.918  43.653  1.00 77.40           C  
ANISOU 1685  CB  ARG A 217    10998   9627   8783   -499     27   -361       C  
ATOM   1686  CG  ARG A 217      26.394  29.482  44.030  1.00 84.65           C  
ANISOU 1686  CG  ARG A 217    11950  10588   9627   -584     59   -308       C  
ATOM   1687  CD  ARG A 217      27.441  29.124  42.993  1.00 87.25           C  
ANISOU 1687  CD  ARG A 217    12317  10868   9966   -531     39   -227       C  
ATOM   1688  NE  ARG A 217      27.129  29.733  41.693  1.00 93.99           N  
ANISOU 1688  NE  ARG A 217    13267  11600  10846   -417     22   -287       N  
ATOM   1689  CZ  ARG A 217      27.599  30.906  41.255  1.00 98.92           C  
ANISOU 1689  CZ  ARG A 217    13983  12171  11429   -405     48   -320       C  
ATOM   1690  NH1 ARG A 217      28.424  31.643  42.003  1.00 97.07           N1+
ANISOU 1690  NH1 ARG A 217    13764  11994  11123   -517     93   -310       N1+
ATOM   1691  NH2 ARG A 217      27.243  31.353  40.047  1.00 97.55           N  
ANISOU 1691  NH2 ARG A 217    13893  11891  11281   -290     29   -361       N  
ATOM   1692  N   LEU A 218      22.330  30.471  43.329  1.00 67.45           N  
ANISOU 1692  N   LEU A 218     9754   8288   7585   -345     45   -564       N  
ATOM   1693  CA  LEU A 218      21.681  31.677  42.806  1.00 68.56           C  
ANISOU 1693  CA  LEU A 218     9956   8358   7737   -242     73   -629       C  
ATOM   1694  C   LEU A 218      20.564  32.228  43.700  1.00 67.63           C  
ANISOU 1694  C   LEU A 218     9792   8268   7634   -239    137   -695       C  
ATOM   1695  O   LEU A 218      20.392  33.443  43.815  1.00 64.99           O  
ANISOU 1695  O   LEU A 218     9530   7877   7285   -200    215   -744       O  
ATOM   1696  CB  LEU A 218      21.135  31.429  41.396  1.00 65.13           C  
ANISOU 1696  CB  LEU A 218     9525   7872   7349   -114     -4   -621       C  
ATOM   1697  CG  LEU A 218      22.143  31.072  40.300  1.00 65.65           C  
ANISOU 1697  CG  LEU A 218     9663   7883   7400    -92    -51   -569       C  
ATOM   1698  CD1 LEU A 218      21.531  31.367  38.928  1.00 65.63           C  
ANISOU 1698  CD1 LEU A 218     9698   7823   7418     39   -106   -581       C  
ATOM   1699  CD2 LEU A 218      23.442  31.851  40.431  1.00 66.32           C  
ANISOU 1699  CD2 LEU A 218     9842   7929   7426   -139      3   -549       C  
ATOM   1700  N   SER A 219      19.789  31.340  44.300  1.00 68.37           N  
ANISOU 1700  N   SER A 219     9774   8442   7763   -275    117   -695       N  
ATOM   1701  CA  SER A 219      18.777  31.749  45.268  1.00 71.59           C  
ANISOU 1701  CA  SER A 219    10128   8889   8185   -284    189   -752       C  
ATOM   1702  C   SER A 219      19.376  32.437  46.492  1.00 73.84           C  
ANISOU 1702  C   SER A 219    10473   9189   8394   -405    291   -784       C  
ATOM   1703  O   SER A 219      18.776  33.366  47.025  1.00 77.25           O  
ANISOU 1703  O   SER A 219    10935   9595   8822   -386    389   -849       O  
ATOM   1704  CB  SER A 219      17.984  30.545  45.719  1.00 71.46           C  
ANISOU 1704  CB  SER A 219     9980   8962   8210   -325    148   -739       C  
ATOM   1705  OG  SER A 219      17.612  29.795  44.592  1.00 75.21           O  
ANISOU 1705  OG  SER A 219    10414   9428   8733   -255     51   -711       O  
ATOM   1706  N   GLN A 220      20.555  31.989  46.928  1.00 74.37           N  
ANISOU 1706  N   GLN A 220    10557   9303   8397   -531    274   -735       N  
ATOM   1707  CA  GLN A 220      21.325  32.721  47.935  1.00 75.44           C  
ANISOU 1707  CA  GLN A 220    10763   9466   8436   -668    357   -759       C  
ATOM   1708  C   GLN A 220      21.688  34.110  47.415  1.00 76.55           C  
ANISOU 1708  C   GLN A 220    11043   9495   8546   -625    423   -811       C  
ATOM   1709  O   GLN A 220      21.473  35.102  48.108  1.00 83.57           O  
ANISOU 1709  O   GLN A 220    12008  10354   9392   -672    535   -886       O  
ATOM   1710  CB  GLN A 220      22.619  31.991  48.310  1.00 76.61           C  
ANISOU 1710  CB  GLN A 220    10887   9702   8518   -799    311   -670       C  
ATOM   1711  CG  GLN A 220      22.491  30.934  49.397  1.00 79.55           C  
ANISOU 1711  CG  GLN A 220    11152  10200   8874   -903    297   -622       C  
ATOM   1712  CD  GLN A 220      23.845  30.369  49.821  1.00 80.16           C  
ANISOU 1712  CD  GLN A 220    11204  10376   8877  -1024    263   -513       C  
ATOM   1713  NE2 GLN A 220      23.888  29.713  50.974  1.00 77.83           N  
ANISOU 1713  NE2 GLN A 220    10832  10205   8536  -1141    269   -466       N  
ATOM   1714  OE1 GLN A 220      24.836  30.523  49.117  1.00 83.29           O  
ANISOU 1714  OE1 GLN A 220    11643  10746   9258  -1009    234   -463       O  
ATOM   1715  N   LYS A 221      22.244  34.174  46.204  1.00 75.14           N  
ANISOU 1715  N   LYS A 221    10913   9249   8389   -541    365   -771       N  
ATOM   1716  CA  LYS A 221      22.689  35.447  45.610  1.00 75.81           C  
ANISOU 1716  CA  LYS A 221    11139   9220   8445   -499    426   -807       C  
ATOM   1717  C   LYS A 221      21.521  36.369  45.284  1.00 73.42           C  
ANISOU 1717  C   LYS A 221    10879   8818   8199   -352    498   -871       C  
ATOM   1718  O   LYS A 221      21.622  37.577  45.458  1.00 71.37           O  
ANISOU 1718  O   LYS A 221    10745   8470   7904   -357    613   -929       O  
ATOM   1719  CB  LYS A 221      23.466  35.226  44.301  1.00 79.47           C  
ANISOU 1719  CB  LYS A 221    11637   9635   8924   -428    345   -744       C  
ATOM   1720  CG  LYS A 221      24.940  34.888  44.442  1.00 81.99           C  
ANISOU 1720  CG  LYS A 221    11967  10012   9174   -557    318   -678       C  
ATOM   1721  CD  LYS A 221      25.601  34.792  43.066  1.00 83.21           C  
ANISOU 1721  CD  LYS A 221    12168  10097   9351   -466    260   -625       C  
ATOM   1722  N   PHE A 222      20.429  35.786  44.797  1.00 72.02           N  
ANISOU 1722  N   PHE A 222    10599   8659   8108   -224    436   -854       N  
ATOM   1723  CA  PHE A 222      19.266  36.538  44.324  1.00 72.89           C  
ANISOU 1723  CA  PHE A 222    10713   8698   8282    -54    485   -882       C  
ATOM   1724  C   PHE A 222      17.984  36.171  45.065  1.00 71.95           C  
ANISOU 1724  C   PHE A 222    10469   8652   8217    -31    510   -906       C  
ATOM   1725  O   PHE A 222      16.987  35.800  44.451  1.00 71.21           O  
ANISOU 1725  O   PHE A 222    10272   8589   8196     92    448   -879       O  
ATOM   1726  CB  PHE A 222      19.037  36.267  42.836  1.00 70.91           C  
ANISOU 1726  CB  PHE A 222    10440   8420   8084     95    375   -826       C  
ATOM   1727  CG  PHE A 222      20.252  36.411  41.993  1.00 69.07           C  
ANISOU 1727  CG  PHE A 222    10312   8126   7807     79    335   -792       C  
ATOM   1728  CD1 PHE A 222      21.086  37.494  42.130  1.00 68.27           C  
ANISOU 1728  CD1 PHE A 222    10357   7936   7648     35    432   -821       C  
ATOM   1729  CD2 PHE A 222      20.534  35.472  41.008  1.00 70.74           C  
ANISOU 1729  CD2 PHE A 222    10482   8363   8032    107    210   -735       C  
ATOM   1730  CE1 PHE A 222      22.201  37.631  41.324  1.00 67.67           C  
ANISOU 1730  CE1 PHE A 222    10370   7809   7534     20    398   -786       C  
ATOM   1731  CE2 PHE A 222      21.647  35.607  40.197  1.00 65.56           C  
ANISOU 1731  CE2 PHE A 222     9922   7648   7339    101    184   -702       C  
ATOM   1732  CZ  PHE A 222      22.489  36.678  40.365  1.00 64.23           C  
ANISOU 1732  CZ  PHE A 222     9885   7404   7118     58    275   -723       C  
ATOM   1733  N   PRO A 223      17.985  36.301  46.385  1.00 75.35           N  
ANISOU 1733  N   PRO A 223    10906   9120   8605   -157    605   -956       N  
ATOM   1734  CA  PRO A 223      16.803  35.886  47.146  1.00 76.41           C  
ANISOU 1734  CA  PRO A 223    10917   9329   8786   -146    635   -977       C  
ATOM   1735  C   PRO A 223      15.542  36.585  46.680  1.00 76.25           C  
ANISOU 1735  C   PRO A 223    10862   9259   8849     47    693   -985       C  
ATOM   1736  O   PRO A 223      14.445  36.041  46.810  1.00 78.11           O  
ANISOU 1736  O   PRO A 223    10954   9575   9150    102    667   -972       O  
ATOM   1737  CB  PRO A 223      17.150  36.281  48.588  1.00 75.43           C  
ANISOU 1737  CB  PRO A 223    10859   9223   8580   -312    761  -1042       C  
ATOM   1738  CG  PRO A 223      18.242  37.281  48.466  1.00 76.20           C  
ANISOU 1738  CG  PRO A 223    11130   9225   8598   -371    827  -1070       C  
ATOM   1739  CD  PRO A 223      19.009  36.913  47.243  1.00 75.09           C  
ANISOU 1739  CD  PRO A 223    10996   9065   8468   -320    697  -1000       C  
ATOM   1740  N   LYS A 224      15.709  37.780  46.136  1.00 79.85           N  
ANISOU 1740  N   LYS A 224    11446   9587   9304    150    775   -996       N  
ATOM   1741  CA  LYS A 224      14.592  38.584  45.658  1.00 86.11           C  
ANISOU 1741  CA  LYS A 224    12218  10323  10177    356    848   -982       C  
ATOM   1742  C   LYS A 224      13.909  37.971  44.425  1.00 84.63           C  
ANISOU 1742  C   LYS A 224    11893  10203  10059    501    693   -900       C  
ATOM   1743  O   LYS A 224      12.754  38.263  44.155  1.00 84.51           O  
ANISOU 1743  O   LYS A 224    11783  10212  10117    659    718   -867       O  
ATOM   1744  CB  LYS A 224      15.079  40.019  45.382  1.00 92.37           C  
ANISOU 1744  CB  LYS A 224    13208  10946  10943    422    987  -1008       C  
ATOM   1745  CG  LYS A 224      14.202  40.841  44.446  1.00 98.63           C  
ANISOU 1745  CG  LYS A 224    13995  11662  11817    671   1031   -952       C  
ATOM   1746  CD  LYS A 224      14.814  42.194  44.114  1.00103.73           C  
ANISOU 1746  CD  LYS A 224    14857  12122  12432    726   1170   -971       C  
ATOM   1747  CE  LYS A 224      14.277  42.723  42.781  1.00107.62           C  
ANISOU 1747  CE  LYS A 224    15337  12562  12991    970   1139   -876       C  
ATOM   1748  NZ  LYS A 224      12.947  42.148  42.402  1.00107.74           N1+
ANISOU 1748  NZ  LYS A 224    15130  12712  13094   1122   1047   -799       N1+
ATOM   1749  N   ALA A 225      14.606  37.113  43.690  1.00 83.84           N  
ANISOU 1749  N   ALA A 225    11780  10144   9932    443    538   -864       N  
ATOM   1750  CA  ALA A 225      14.055  36.572  42.443  1.00 84.52           C  
ANISOU 1750  CA  ALA A 225    11765  10289  10061    556    393   -796       C  
ATOM   1751  C   ALA A 225      12.965  35.513  42.680  1.00 85.51           C  
ANISOU 1751  C   ALA A 225    11693  10562  10237    538    315   -782       C  
ATOM   1752  O   ALA A 225      13.067  34.704  43.598  1.00 85.51           O  
ANISOU 1752  O   ALA A 225    11643  10625  10223    395    314   -813       O  
ATOM   1753  CB  ALA A 225      15.180  36.003  41.584  1.00 78.54           C  
ANISOU 1753  CB  ALA A 225    11078   9510   9254    491    276   -770       C  
ATOM   1754  N   GLU A 226      11.922  35.523  41.852  1.00 86.69           N  
ANISOU 1754  N   GLU A 226    11725  10775  10436    679    250   -728       N  
ATOM   1755  CA  GLU A 226      10.911  34.466  41.883  1.00 88.20           C  
ANISOU 1755  CA  GLU A 226    11725  11120  10666    647    156   -710       C  
ATOM   1756  C   GLU A 226      11.522  33.168  41.369  1.00 85.10           C  
ANISOU 1756  C   GLU A 226    11331  10769  10233    513     12   -708       C  
ATOM   1757  O   GLU A 226      12.450  33.193  40.570  1.00 80.80           O  
ANISOU 1757  O   GLU A 226    10903  10153   9646    509    -40   -694       O  
ATOM   1758  CB  GLU A 226       9.686  34.834  41.033  1.00 93.14           C  
ANISOU 1758  CB  GLU A 226    12218  11827  11344    823    111   -640       C  
ATOM   1759  CG  GLU A 226       8.783  35.905  41.635  1.00 96.42           C  
ANISOU 1759  CG  GLU A 226    12584  12229  11822    971    265   -626       C  
ATOM   1760  CD  GLU A 226       8.309  35.568  43.048  1.00104.04           C  
ANISOU 1760  CD  GLU A 226    13473  13242  12815    875    364   -683       C  
ATOM   1761  OE1 GLU A 226       8.168  34.362  43.374  1.00106.60           O  
ANISOU 1761  OE1 GLU A 226    13700  13672  13131    729    277   -704       O  
ATOM   1762  OE2 GLU A 226       8.086  36.511  43.843  1.00106.57           O1-
ANISOU 1762  OE2 GLU A 226    13842  13487  13162    942    541   -708       O1-
ATOM   1763  N   PHE A 227      10.997  32.038  41.837  1.00 83.17           N  
ANISOU 1763  N   PHE A 227    10963  10632  10005    403    -38   -721       N  
ATOM   1764  CA  PHE A 227      11.526  30.725  41.470  1.00 80.54           C  
ANISOU 1764  CA  PHE A 227    10637  10324   9640    269   -146   -721       C  
ATOM   1765  C   PHE A 227      11.502  30.451  39.967  1.00 79.40           C  
ANISOU 1765  C   PHE A 227    10503  10192   9472    317   -274   -684       C  
ATOM   1766  O   PHE A 227      12.310  29.681  39.455  1.00 75.47           O  
ANISOU 1766  O   PHE A 227    10085   9655   8936    234   -335   -685       O  
ATOM   1767  CB  PHE A 227      10.766  29.623  42.208  1.00 80.43           C  
ANISOU 1767  CB  PHE A 227    10484  10421   9653    154   -162   -739       C  
ATOM   1768  CG  PHE A 227      11.287  28.240  41.932  1.00 77.63           C  
ANISOU 1768  CG  PHE A 227    10153  10072   9272     14   -243   -739       C  
ATOM   1769  CD1 PHE A 227      12.624  27.938  42.132  1.00 74.16           C  
ANISOU 1769  CD1 PHE A 227     9846   9540   8794    -59   -221   -736       C  
ATOM   1770  CD2 PHE A 227      10.443  27.245  41.465  1.00 76.74           C  
ANISOU 1770  CD2 PHE A 227     9931  10057   9171    -46   -332   -738       C  
ATOM   1771  CE1 PHE A 227      13.113  26.673  41.857  1.00 73.70           C  
ANISOU 1771  CE1 PHE A 227     9814   9469   8717   -167   -274   -725       C  
ATOM   1772  CE2 PHE A 227      10.925  25.976  41.199  1.00 75.61           C  
ANISOU 1772  CE2 PHE A 227     9833   9893   9003   -174   -382   -742       C  
ATOM   1773  CZ  PHE A 227      12.260  25.690  41.400  1.00 74.14           C  
ANISOU 1773  CZ  PHE A 227     9783   9598   8788   -224   -346   -732       C  
ATOM   1774  N   VAL A 228      10.574  31.084  39.263  1.00 85.34           N  
ANISOU 1774  N   VAL A 228    11175  11003  10246    453   -309   -646       N  
ATOM   1775  CA  VAL A 228      10.527  31.002  37.799  1.00 86.45           C  
ANISOU 1775  CA  VAL A 228    11331  11167  10348    505   -430   -604       C  
ATOM   1776  C   VAL A 228      11.862  31.483  37.211  1.00 85.33           C  
ANISOU 1776  C   VAL A 228    11385  10878  10159    532   -415   -601       C  
ATOM   1777  O   VAL A 228      12.516  30.747  36.475  1.00 87.44           O  
ANISOU 1777  O   VAL A 228    11726  11118  10379    457   -490   -605       O  
ATOM   1778  CB  VAL A 228       9.372  31.848  37.205  1.00 91.49           C  
ANISOU 1778  CB  VAL A 228    11850  11898  11014    675   -455   -539       C  
ATOM   1779  CG1 VAL A 228       9.026  31.352  35.806  1.00 90.32           C  
ANISOU 1779  CG1 VAL A 228    11661  11845  10812    671   -612   -498       C  
ATOM   1780  CG2 VAL A 228       8.135  31.830  38.105  1.00 92.99           C  
ANISOU 1780  CG2 VAL A 228    11853  12210  11270    692   -406   -535       C  
ATOM   1781  N   GLU A 229      12.276  32.700  37.570  1.00 86.52           N  
ANISOU 1781  N   GLU A 229    11625  10927  10320    629   -305   -598       N  
ATOM   1782  CA  GLU A 229      13.554  33.274  37.103  1.00 85.91           C  
ANISOU 1782  CA  GLU A 229    11733  10711  10199    647   -275   -596       C  
ATOM   1783  C   GLU A 229      14.776  32.410  37.421  1.00 81.11           C  
ANISOU 1783  C   GLU A 229    11213  10051   9555    491   -279   -628       C  
ATOM   1784  O   GLU A 229      15.580  32.107  36.527  1.00 82.02           O  
ANISOU 1784  O   GLU A 229    11422  10114   9627    473   -334   -612       O  
ATOM   1785  CB  GLU A 229      13.788  34.671  37.693  1.00 90.06           C  
ANISOU 1785  CB  GLU A 229    12346  11132  10740    738   -129   -604       C  
ATOM   1786  CG  GLU A 229      13.293  35.824  36.836  1.00 98.24           C  
ANISOU 1786  CG  GLU A 229    13405  12133  11788    932   -112   -546       C  
ATOM   1787  CD  GLU A 229      14.077  35.985  35.545  1.00104.80           C  
ANISOU 1787  CD  GLU A 229    14358  12898  12564    969   -183   -510       C  
ATOM   1788  OE1 GLU A 229      14.985  35.167  35.291  1.00106.43           O  
ANISOU 1788  OE1 GLU A 229    14627  13086  12726    846   -243   -533       O  
ATOM   1789  OE2 GLU A 229      13.781  36.932  34.781  1.00113.80           O1-
ANISOU 1789  OE2 GLU A 229    15533  14003  13704   1129   -169   -451       O1-
ATOM   1790  N   VAL A 230      14.928  32.039  38.690  1.00 73.42           N  
ANISOU 1790  N   VAL A 230    10208   9092   8596    385   -213   -663       N  
ATOM   1791  CA  VAL A 230      16.082  31.255  39.115  1.00 68.51           C  
ANISOU 1791  CA  VAL A 230     9652   8436   7944    249   -206   -671       C  
ATOM   1792  C   VAL A 230      16.157  30.037  38.231  1.00 70.45           C  
ANISOU 1792  C   VAL A 230     9885   8707   8177    198   -311   -652       C  
ATOM   1793  O   VAL A 230      17.232  29.647  37.797  1.00 72.25           O  
ANISOU 1793  O   VAL A 230    10209   8869   8372    156   -322   -634       O  
ATOM   1794  CB  VAL A 230      16.003  30.834  40.603  1.00 68.25           C  
ANISOU 1794  CB  VAL A 230     9554   8452   7925    136   -138   -697       C  
ATOM   1795  CG1 VAL A 230      16.870  29.623  40.908  1.00 64.05           C  
ANISOU 1795  CG1 VAL A 230     9038   7926   7373      3   -162   -678       C  
ATOM   1796  CG2 VAL A 230      16.377  31.993  41.522  1.00 69.38           C  
ANISOU 1796  CG2 VAL A 230     9766   8545   8052    141    -16   -725       C  
ATOM   1797  N   THR A 231      15.006  29.463  37.913  1.00 71.32           N  
ANISOU 1797  N   THR A 231     9880   8911   8309    199   -381   -657       N  
ATOM   1798  CA  THR A 231      14.994  28.284  37.072  1.00 71.64           C  
ANISOU 1798  CA  THR A 231     9922   8971   8327    128   -471   -654       C  
ATOM   1799  C   THR A 231      15.518  28.577  35.678  1.00 73.03           C  
ANISOU 1799  C   THR A 231    10209   9086   8454    193   -526   -632       C  
ATOM   1800  O   THR A 231      16.316  27.781  35.143  1.00 73.85           O  
ANISOU 1800  O   THR A 231    10403   9131   8527    127   -544   -629       O  
ATOM   1801  CB  THR A 231      13.601  27.658  36.957  1.00 73.02           C  
ANISOU 1801  CB  THR A 231     9948   9276   8521     96   -540   -667       C  
ATOM   1802  CG2 THR A 231      13.703  26.291  36.247  1.00 70.09           C  
ANISOU 1802  CG2 THR A 231     9606   8907   8117    -23   -608   -680       C  
ATOM   1803  OG1 THR A 231      13.054  27.491  38.275  1.00 77.52           O  
ANISOU 1803  OG1 THR A 231    10413   9904   9139     46   -478   -686       O  
ATOM   1804  N   LYS A 232      15.085  29.692  35.074  1.00 70.54           N  
ANISOU 1804  N   LYS A 232     9893   8778   8131    326   -544   -610       N  
ATOM   1805  CA  LYS A 232      15.612  30.025  33.758  1.00 67.85           C  
ANISOU 1805  CA  LYS A 232     9665   8378   7736    389   -593   -584       C  
ATOM   1806  C   LYS A 232      17.111  30.254  33.879  1.00 66.19           C  
ANISOU 1806  C   LYS A 232     9605   8036   7508    370   -520   -580       C  
ATOM   1807  O   LYS A 232      17.890  29.756  33.060  1.00 60.60           O  
ANISOU 1807  O   LYS A 232     8995   7269   6759    338   -546   -572       O  
ATOM   1808  CB  LYS A 232      14.964  31.237  33.114  1.00 70.91           C  
ANISOU 1808  CB  LYS A 232    10035   8790   8118    548   -613   -543       C  
ATOM   1809  CG  LYS A 232      15.872  31.770  32.011  1.00 73.26           C  
ANISOU 1809  CG  LYS A 232    10488   8987   8359    610   -624   -515       C  
ATOM   1810  CD  LYS A 232      15.276  32.848  31.144  1.00 77.71           C  
ANISOU 1810  CD  LYS A 232    11048   9573   8904    770   -656   -457       C  
ATOM   1811  CE  LYS A 232      16.373  33.449  30.278  1.00 79.54           C  
ANISOU 1811  CE  LYS A 232    11458   9679   9085    821   -636   -435       C  
ATOM   1812  NZ  LYS A 232      17.068  32.418  29.465  1.00 78.75           N1+
ANISOU 1812  NZ  LYS A 232    11440   9558   8925    715   -698   -453       N1+
ATOM   1813  N   LEU A 233      17.513  31.006  34.904  1.00 66.57           N  
ANISOU 1813  N   LEU A 233     9668   8043   7582    382   -423   -587       N  
ATOM   1814  CA  LEU A 233      18.933  31.260  35.128  1.00 65.86           C  
ANISOU 1814  CA  LEU A 233     9700   7855   7470    345   -354   -579       C  
ATOM   1815  C   LEU A 233      19.713  29.957  35.263  1.00 64.34           C  
ANISOU 1815  C   LEU A 233     9520   7655   7270    227   -363   -570       C  
ATOM   1816  O   LEU A 233      20.789  29.815  34.696  1.00 62.09           O  
ANISOU 1816  O   LEU A 233     9336   7299   6955    217   -353   -544       O  
ATOM   1817  CB  LEU A 233      19.158  32.136  36.357  1.00 65.90           C  
ANISOU 1817  CB  LEU A 233     9707   7841   7490    334   -249   -597       C  
ATOM   1818  CG  LEU A 233      18.796  33.630  36.265  1.00 68.29           C  
ANISOU 1818  CG  LEU A 233    10056   8094   7796    456   -188   -602       C  
ATOM   1819  CD1 LEU A 233      19.445  34.345  37.443  1.00 68.41           C  
ANISOU 1819  CD1 LEU A 233    10126   8065   7802    392    -68   -632       C  
ATOM   1820  CD2 LEU A 233      19.232  34.298  34.958  1.00 66.35           C  
ANISOU 1820  CD2 LEU A 233     9927   7768   7516    555   -212   -569       C  
ATOM   1821  N   VAL A 234      19.149  28.991  35.979  1.00 65.24           N  
ANISOU 1821  N   VAL A 234     9534   7840   7415    145   -373   -584       N  
ATOM   1822  CA  VAL A 234      19.856  27.743  36.225  1.00 63.55           C  
ANISOU 1822  CA  VAL A 234     9333   7609   7202     43   -360   -563       C  
ATOM   1823  C   VAL A 234      19.991  26.917  34.956  1.00 64.42           C  
ANISOU 1823  C   VAL A 234     9511   7679   7288     37   -413   -558       C  
ATOM   1824  O   VAL A 234      21.080  26.414  34.650  1.00 68.84           O  
ANISOU 1824  O   VAL A 234    10157   8166   7835     12   -379   -524       O  
ATOM   1825  CB  VAL A 234      19.192  26.935  37.347  1.00 65.50           C  
ANISOU 1825  CB  VAL A 234     9465   7934   7488    -44   -345   -577       C  
ATOM   1826  CG1 VAL A 234      19.827  25.561  37.454  1.00 67.44           C  
ANISOU 1826  CG1 VAL A 234     9732   8152   7740   -134   -326   -544       C  
ATOM   1827  CG2 VAL A 234      19.321  27.686  38.679  1.00 66.11           C  
ANISOU 1827  CG2 VAL A 234     9502   8043   7574    -61   -274   -581       C  
ATOM   1828  N   THR A 235      18.899  26.798  34.204  1.00 64.89           N  
ANISOU 1828  N   THR A 235     9530   7790   7335     56   -492   -589       N  
ATOM   1829  CA  THR A 235      18.929  26.132  32.907  1.00 62.89           C  
ANISOU 1829  CA  THR A 235     9354   7505   7035     38   -547   -596       C  
ATOM   1830  C   THR A 235      20.038  26.699  32.041  1.00 59.79           C  
ANISOU 1830  C   THR A 235     9101   7013   6603    104   -526   -567       C  
ATOM   1831  O   THR A 235      20.846  25.960  31.513  1.00 60.27           O  
ANISOU 1831  O   THR A 235     9258   6997   6644     66   -498   -554       O  
ATOM   1832  CB  THR A 235      17.588  26.279  32.153  1.00 66.36           C  
ANISOU 1832  CB  THR A 235     9723   8044   7446     59   -649   -623       C  
ATOM   1833  CG2 THR A 235      17.721  25.890  30.674  1.00 65.08           C  
ANISOU 1833  CG2 THR A 235     9667   7852   7210     45   -709   -631       C  
ATOM   1834  OG1 THR A 235      16.600  25.457  32.774  1.00 67.80           O  
ANISOU 1834  OG1 THR A 235     9784   8318   7658    -32   -671   -653       O  
ATOM   1835  N   ASP A 236      20.063  28.017  31.896  1.00 60.38           N  
ANISOU 1835  N   ASP A 236     9191   7082   6668    206   -528   -554       N  
ATOM   1836  CA  ASP A 236      21.056  28.670  31.055  1.00 58.49           C  
ANISOU 1836  CA  ASP A 236     9084   6752   6388    269   -506   -526       C  
ATOM   1837  C   ASP A 236      22.468  28.424  31.596  1.00 57.06           C  
ANISOU 1837  C   ASP A 236     8962   6496   6222    225   -416   -494       C  
ATOM   1838  O   ASP A 236      23.368  28.035  30.848  1.00 57.03           O  
ANISOU 1838  O   ASP A 236     9059   6418   6191    220   -394   -470       O  
ATOM   1839  CB  ASP A 236      20.779  30.157  30.968  1.00 58.66           C  
ANISOU 1839  CB  ASP A 236     9111   6772   6404    383   -504   -516       C  
ATOM   1840  CG  ASP A 236      19.579  30.494  30.084  1.00 64.35           C  
ANISOU 1840  CG  ASP A 236     9789   7564   7096    458   -597   -515       C  
ATOM   1841  OD1 ASP A 236      19.330  31.719  29.918  1.00 69.45           O  
ANISOU 1841  OD1 ASP A 236    10448   8200   7741    573   -586   -491       O  
ATOM   1842  OD2 ASP A 236      18.884  29.577  29.565  1.00 62.37           O1-
ANISOU 1842  OD2 ASP A 236     9494   7383   6821    402   -676   -533       O1-
ATOM   1843  N   LEU A 237      22.655  28.603  32.902  1.00 57.16           N  
ANISOU 1843  N   LEU A 237     8906   6539   6273    188   -362   -487       N  
ATOM   1844  CA  LEU A 237      23.985  28.453  33.498  1.00 54.88           C  
ANISOU 1844  CA  LEU A 237     8648   6214   5990    141   -286   -439       C  
ATOM   1845  C   LEU A 237      24.466  27.001  33.455  1.00 54.66           C  
ANISOU 1845  C   LEU A 237     8624   6166   5979     77   -264   -405       C  
ATOM   1846  O   LEU A 237      25.646  26.740  33.293  1.00 52.45           O  
ANISOU 1846  O   LEU A 237     8400   5835   5694     71   -209   -348       O  
ATOM   1847  CB  LEU A 237      23.985  28.968  34.918  1.00 54.13           C  
ANISOU 1847  CB  LEU A 237     8476   6176   5915     98   -240   -441       C  
ATOM   1848  CG  LEU A 237      25.335  28.854  35.628  1.00 54.83           C  
ANISOU 1848  CG  LEU A 237     8573   6265   5995     32   -172   -380       C  
ATOM   1849  CD1 LEU A 237      26.334  29.780  34.945  1.00 51.26           C  
ANISOU 1849  CD1 LEU A 237     8225   5746   5503     73   -144   -358       C  
ATOM   1850  CD2 LEU A 237      25.168  29.127  37.121  1.00 53.37           C  
ANISOU 1850  CD2 LEU A 237     8302   6161   5816    -41   -137   -388       C  
ATOM   1851  N   THR A 238      23.547  26.057  33.582  1.00 55.38           N  
ANISOU 1851  N   THR A 238     8657   6294   6092     31   -296   -435       N  
ATOM   1852  CA  THR A 238      23.904  24.655  33.459  1.00 56.39           C  
ANISOU 1852  CA  THR A 238     8810   6379   6236    -27   -259   -407       C  
ATOM   1853  C   THR A 238      24.359  24.298  32.051  1.00 59.14           C  
ANISOU 1853  C   THR A 238     9290   6633   6546      1   -255   -409       C  
ATOM   1854  O   THR A 238      25.301  23.497  31.873  1.00 61.40           O  
ANISOU 1854  O   THR A 238     9640   6844   6844    -11   -179   -356       O  
ATOM   1855  CB  THR A 238      22.727  23.744  33.865  1.00 57.03           C  
ANISOU 1855  CB  THR A 238     8812   6514   6341    -98   -289   -451       C  
ATOM   1856  CG2 THR A 238      23.080  22.273  33.677  1.00 53.87           C  
ANISOU 1856  CG2 THR A 238     8466   6044   5958   -160   -230   -427       C  
ATOM   1857  OG1 THR A 238      22.418  23.971  35.250  1.00 59.14           O  
ANISOU 1857  OG1 THR A 238     8963   6864   6644   -129   -274   -443       O  
ATOM   1858  N   LYS A 239      23.706  24.884  31.050  1.00 60.45           N  
ANISOU 1858  N   LYS A 239     9498   6805   6665     41   -330   -459       N  
ATOM   1859  CA  LYS A 239      24.043  24.573  29.659  1.00 61.56           C  
ANISOU 1859  CA  LYS A 239     9773   6865   6752     55   -333   -469       C  
ATOM   1860  C   LYS A 239      25.434  25.104  29.399  1.00 60.74           C  
ANISOU 1860  C   LYS A 239     9752   6686   6642    114   -263   -409       C  
ATOM   1861  O   LYS A 239      26.250  24.420  28.781  1.00 60.76           O  
ANISOU 1861  O   LYS A 239     9851   6599   6634    110   -197   -382       O  
ATOM   1862  CB  LYS A 239      23.030  25.163  28.666  1.00 60.73           C  
ANISOU 1862  CB  LYS A 239     9682   6809   6583     85   -439   -522       C  
ATOM   1863  CG  LYS A 239      23.380  24.869  27.216  1.00 62.79           C  
ANISOU 1863  CG  LYS A 239    10091   6995   6770     86   -443   -535       C  
ATOM   1864  CD  LYS A 239      22.377  25.407  26.182  1.00 62.28           C  
ANISOU 1864  CD  LYS A 239    10035   7001   6626    108   -559   -572       C  
ATOM   1865  N   VAL A 240      25.704  26.304  29.906  1.00 56.81           N  
ANISOU 1865  N   VAL A 240     9216   6220   6151    163   -266   -389       N  
ATOM   1866  CA  VAL A 240      27.023  26.906  29.776  1.00 55.14           C  
ANISOU 1866  CA  VAL A 240     9067   5954   5931    201   -201   -332       C  
ATOM   1867  C   VAL A 240      28.074  25.919  30.278  1.00 53.52           C  
ANISOU 1867  C   VAL A 240     8850   5721   5765    162   -110   -259       C  
ATOM   1868  O   VAL A 240      29.052  25.609  29.577  1.00 53.22           O  
ANISOU 1868  O   VAL A 240     8899   5607   5717    186    -47   -212       O  
ATOM   1869  CB  VAL A 240      27.103  28.249  30.549  1.00 53.50           C  
ANISOU 1869  CB  VAL A 240     8810   5793   5726    223   -202   -329       C  
ATOM   1870  CG1 VAL A 240      28.534  28.726  30.694  1.00 52.07           C  
ANISOU 1870  CG1 VAL A 240     8668   5579   5537    222   -127   -265       C  
ATOM   1871  CG2 VAL A 240      26.273  29.310  29.863  1.00 53.13           C  
ANISOU 1871  CG2 VAL A 240     8799   5745   5642    295   -265   -376       C  
ATOM   1872  N   HIS A 241      27.864  25.402  31.478  1.00 52.10           N  
ANISOU 1872  N   HIS A 241     8561   5604   5630    108    -95   -238       N  
ATOM   1873  CA  HIS A 241      28.842  24.484  32.045  1.00 53.54           C  
ANISOU 1873  CA  HIS A 241     8715   5774   5852     83     -7   -145       C  
ATOM   1874  C   HIS A 241      28.921  23.155  31.284  1.00 54.98           C  
ANISOU 1874  C   HIS A 241     8981   5860   6049     82     48   -136       C  
ATOM   1875  O   HIS A 241      30.016  22.699  30.949  1.00 54.81           O  
ANISOU 1875  O   HIS A 241     9010   5772   6041    114    139    -57       O  
ATOM   1876  CB  HIS A 241      28.606  24.302  33.527  1.00 54.31           C  
ANISOU 1876  CB  HIS A 241     8680   5971   5985     24     -5   -117       C  
ATOM   1877  CG  HIS A 241      28.916  25.538  34.319  1.00 58.81           C  
ANISOU 1877  CG  HIS A 241     9192   6621   6533      9    -20   -109       C  
ATOM   1878  CD2 HIS A 241      28.167  26.238  35.200  1.00 60.36           C  
ANISOU 1878  CD2 HIS A 241     9317   6895   6723    -26    -59   -161       C  
ATOM   1879  ND1 HIS A 241      30.128  26.197  34.236  1.00 58.35           N  
ANISOU 1879  ND1 HIS A 241     9156   6563   6450     20     21    -47       N  
ATOM   1880  CE1 HIS A 241      30.101  27.254  35.024  1.00 59.40           C  
ANISOU 1880  CE1 HIS A 241     9246   6768   6556    -20      5    -69       C  
ATOM   1881  NE2 HIS A 241      28.928  27.298  35.625  1.00 61.42           N  
ANISOU 1881  NE2 HIS A 241     9448   7065   6823    -44    -38   -138       N  
ATOM   1882  N   LYS A 242      27.783  22.551  30.970  1.00 53.66           N  
ANISOU 1882  N   LYS A 242     8832   5682   5875     42      4   -216       N  
ATOM   1883  CA  LYS A 242      27.804  21.312  30.200  1.00 53.75           C  
ANISOU 1883  CA  LYS A 242     8948   5588   5886     19     67   -227       C  
ATOM   1884  C   LYS A 242      28.616  21.503  28.934  1.00 53.45           C  
ANISOU 1884  C   LYS A 242     9051   5452   5806     75    111   -217       C  
ATOM   1885  O   LYS A 242      29.417  20.661  28.571  1.00 55.12           O  
ANISOU 1885  O   LYS A 242     9343   5563   6037     91    225   -164       O  
ATOM   1886  CB  LYS A 242      26.383  20.876  29.855  1.00 55.96           C  
ANISOU 1886  CB  LYS A 242     9238   5889   6137    -53     -9   -334       C  
ATOM   1887  CG  LYS A 242      26.286  19.534  29.156  1.00 60.74           C  
ANISOU 1887  CG  LYS A 242     9963   6383   6731   -111     64   -364       C  
ATOM   1888  CD  LYS A 242      24.912  19.282  28.525  1.00 61.54           C  
ANISOU 1888  CD  LYS A 242    10089   6522   6772   -201    -30   -481       C  
ATOM   1889  N   GLU A 243      28.451  22.640  28.283  1.00 54.74           N  
ANISOU 1889  N   GLU A 243     9245   5641   5914    112     33   -260       N  
ATOM   1890  CA  GLU A 243      29.212  22.928  27.069  1.00 53.91           C  
ANISOU 1890  CA  GLU A 243     9276   5449   5760    164     71   -251       C  
ATOM   1891  C   GLU A 243      30.721  23.030  27.304  1.00 50.34           C  
ANISOU 1891  C   GLU A 243     8822   4960   5346    217    180   -139       C  
ATOM   1892  O   GLU A 243      31.508  22.375  26.624  1.00 46.97           O  
ANISOU 1892  O   GLU A 243     8495   4431   4921    243    284   -100       O  
ATOM   1893  CB  GLU A 243      28.700  24.197  26.389  1.00 57.83           C  
ANISOU 1893  CB  GLU A 243     9799   5985   6189    199    -35   -306       C  
ATOM   1894  CG  GLU A 243      27.300  24.118  25.788  1.00 63.54           C  
ANISOU 1894  CG  GLU A 243    10536   6751   6854    159   -144   -401       C  
ATOM   1895  CD  GLU A 243      27.168  23.141  24.633  1.00 70.82           C  
ANISOU 1895  CD  GLU A 243    11599   7593   7716    107   -118   -449       C  
ATOM   1896  OE1 GLU A 243      28.169  22.856  23.924  1.00 76.87           O  
ANISOU 1896  OE1 GLU A 243    12491   8251   8465    133    -21   -418       O  
ATOM   1897  OE2 GLU A 243      26.031  22.663  24.416  1.00 82.03           O1-
ANISOU 1897  OE2 GLU A 243    13008   9062   9098     32   -191   -520       O1-
ATOM   1898  N   CYS A 244      31.128  23.814  28.293  1.00 51.25           N  
ANISOU 1898  N   CYS A 244     8822   5163   5488    226    164    -85       N  
ATOM   1899  CA  CYS A 244      32.565  23.892  28.637  1.00 51.06           C  
ANISOU 1899  CA  CYS A 244     8765   5140   5496    259    258     35       C  
ATOM   1900  C   CYS A 244      33.127  22.525  29.019  1.00 49.47           C  
ANISOU 1900  C   CYS A 244     8541   4899   5358    262    372    128       C  
ATOM   1901  O   CYS A 244      34.204  22.138  28.575  1.00 47.88           O  
ANISOU 1901  O   CYS A 244     8385   4632   5175    313    481    215       O  
ATOM   1902  CB  CYS A 244      32.822  24.892  29.760  1.00 54.65           C  
ANISOU 1902  CB  CYS A 244     9094   5715   5955    233    218     70       C  
ATOM   1903  SG  CYS A 244      33.416  26.498  29.178  1.00 60.49           S  
ANISOU 1903  SG  CYS A 244     9893   6456   6636    261    196     56       S  
ATOM   1904  N   CYS A 245      32.377  21.775  29.817  1.00 48.28           N  
ANISOU 1904  N   CYS A 245     8323   4779   5243    214    358    114       N  
ATOM   1905  CA  CYS A 245      32.845  20.478  30.276  1.00 48.91           C  
ANISOU 1905  CA  CYS A 245     8380   4816   5387    223    474    213       C  
ATOM   1906  C   CYS A 245      33.006  19.456  29.167  1.00 50.38           C  
ANISOU 1906  C   CYS A 245     8727   4839   5577    252    584    199       C  
ATOM   1907  O   CYS A 245      33.954  18.672  29.196  1.00 50.23           O  
ANISOU 1907  O   CYS A 245     8721   4754   5609    307    725    316       O  
ATOM   1908  CB  CYS A 245      31.958  19.976  31.396  1.00 50.26           C  
ANISOU 1908  CB  CYS A 245     8450   5057   5589    158    434    197       C  
ATOM   1909  SG  CYS A 245      32.158  20.984  32.916  1.00 50.65           S  
ANISOU 1909  SG  CYS A 245     8309   5296   5638    123    358    256       S  
ATOM   1910  N   HIS A 246      32.151  19.520  28.147  1.00 52.82           N  
ANISOU 1910  N   HIS A 246     9160   5086   5824    217    528     64       N  
ATOM   1911  CA  HIS A 246      32.297  18.663  26.937  1.00 55.08           C  
ANISOU 1911  CA  HIS A 246     9631   5211   6086    223    633     27       C  
ATOM   1912  C   HIS A 246      33.250  19.176  25.874  1.00 51.68           C  
ANISOU 1912  C   HIS A 246     9305   4714   5618    292    688     51       C  
ATOM   1913  O   HIS A 246      33.369  18.588  24.818  1.00 52.35           O  
ANISOU 1913  O   HIS A 246     9555   4667   5669    292    775     11       O  
ATOM   1914  CB  HIS A 246      30.933  18.376  26.316  1.00 58.01           C  
ANISOU 1914  CB  HIS A 246    10090   5561   6390    127    549   -127       C  
ATOM   1915  CG  HIS A 246      30.166  17.399  27.120  1.00 65.84           C  
ANISOU 1915  CG  HIS A 246    11032   6559   7425     53    563   -144       C  
ATOM   1916  CD2 HIS A 246      29.801  17.422  28.426  1.00 68.01           C  
ANISOU 1916  CD2 HIS A 246    11145   6940   7754     33    516   -105       C  
ATOM   1917  ND1 HIS A 246      29.826  16.150  26.641  1.00 74.10           N  
ANISOU 1917  ND1 HIS A 246    12213   7476   8465    -12    662   -194       N  
ATOM   1918  CE1 HIS A 246      29.217  15.472  27.598  1.00 75.27           C  
ANISOU 1918  CE1 HIS A 246    12282   7655   8663    -71    666   -190       C  
ATOM   1919  NE2 HIS A 246      29.187  16.224  28.689  1.00 73.95           N  
ANISOU 1919  NE2 HIS A 246    11931   7633   8533    -41    575   -134       N  
ATOM   1920  N   GLY A 247      33.930  20.270  26.155  1.00 49.97           N  
ANISOU 1920  N   GLY A 247     9000   4585   5402    339    646    113       N  
ATOM   1921  CA  GLY A 247      34.950  20.761  25.250  1.00 51.99           C  
ANISOU 1921  CA  GLY A 247     9339   4784   5630    405    711    153       C  
ATOM   1922  C   GLY A 247      34.462  21.676  24.137  1.00 52.61           C  
ANISOU 1922  C   GLY A 247     9531   4849   5611    393    615     42       C  
ATOM   1923  O   GLY A 247      35.246  22.021  23.248  1.00 51.98           O  
ANISOU 1923  O   GLY A 247     9545   4706   5498    442    675     64       O  
ATOM   1924  N   ASP A 248      33.192  22.094  24.189  1.00 54.46           N  
ANISOU 1924  N   ASP A 248     9746   5148   5799    336    470    -66       N  
ATOM   1925  CA  ASP A 248      32.660  23.046  23.220  1.00 55.41           C  
ANISOU 1925  CA  ASP A 248     9949   5279   5826    336    366   -151       C  
ATOM   1926  C   ASP A 248      32.826  24.455  23.809  1.00 53.36           C  
ANISOU 1926  C   ASP A 248     9584   5121   5571    368    287   -121       C  
ATOM   1927  O   ASP A 248      31.855  25.124  24.189  1.00 52.05           O  
ANISOU 1927  O   ASP A 248     9351   5039   5387    349    168   -177       O  
ATOM   1928  CB  ASP A 248      31.206  22.733  22.860  1.00 58.70           C  
ANISOU 1928  CB  ASP A 248    10400   5721   6184    263    259   -267       C  
ATOM   1929  CG  ASP A 248      30.728  23.454  21.581  1.00 64.11           C  
ANISOU 1929  CG  ASP A 248    11198   6404   6755    266    172   -338       C  
ATOM   1930  OD1 ASP A 248      31.343  24.502  21.201  1.00 61.13           O  
ANISOU 1930  OD1 ASP A 248    10846   6026   6353    333    167   -303       O  
ATOM   1931  OD2 ASP A 248      29.744  22.948  20.952  1.00 72.74           O1-
ANISOU 1931  OD2 ASP A 248    12357   7503   7778    194    112   -425       O1-
ATOM   1932  N   LEU A 249      34.073  24.925  23.798  1.00 51.05           N  
ANISOU 1932  N   LEU A 249     9289   4813   5296    416    365    -35       N  
ATOM   1933  CA  LEU A 249      34.434  26.196  24.416  1.00 51.04           C  
ANISOU 1933  CA  LEU A 249     9200   4894   5297    425    321     -2       C  
ATOM   1934  C   LEU A 249      33.804  27.439  23.766  1.00 49.82           C  
ANISOU 1934  C   LEU A 249     9112   4748   5070    444    222    -75       C  
ATOM   1935  O   LEU A 249      33.464  28.404  24.461  1.00 49.36           O  
ANISOU 1935  O   LEU A 249     8978   4762   5015    435    159    -88       O  
ATOM   1936  CB  LEU A 249      35.962  26.358  24.419  1.00 50.21           C  
ANISOU 1936  CB  LEU A 249     9084   4776   5217    457    433    109       C  
ATOM   1937  CG  LEU A 249      36.720  25.219  25.081  1.00 49.58           C  
ANISOU 1937  CG  LEU A 249     8921   4701   5215    462    542    217       C  
ATOM   1938  CD1 LEU A 249      38.196  25.579  25.098  1.00 49.28           C  
ANISOU 1938  CD1 LEU A 249     8844   4686   5195    493    636    339       C  
ATOM   1939  CD2 LEU A 249      36.202  24.952  26.487  1.00 46.09           C  
ANISOU 1939  CD2 LEU A 249     8326   4364   4821    411    491    233       C  
ATOM   1940  N   LEU A 250      33.659  27.420  22.449  1.00 47.69           N  
ANISOU 1940  N   LEU A 250     8987   4402   4732    470    219   -117       N  
ATOM   1941  CA  LEU A 250      33.028  28.529  21.765  1.00 47.95           C  
ANISOU 1941  CA  LEU A 250     9084   4445   4692    500    127   -168       C  
ATOM   1942  C   LEU A 250      31.586  28.609  22.203  1.00 48.67           C  
ANISOU 1942  C   LEU A 250     9097   4615   4778    479      6   -233       C  
ATOM   1943  O   LEU A 250      31.120  29.663  22.580  1.00 51.24           O  
ANISOU 1943  O   LEU A 250     9374   4993   5102    505    -55   -242       O  
ATOM   1944  CB  LEU A 250      33.111  28.377  20.253  1.00 47.38           C  
ANISOU 1944  CB  LEU A 250     9182   4290   4532    522    143   -194       C  
ATOM   1945  CG  LEU A 250      34.526  28.187  19.722  1.00 46.88           C  
ANISOU 1945  CG  LEU A 250     9202   4139   4473    547    280   -130       C  
ATOM   1946  CD1 LEU A 250      34.535  27.584  18.314  1.00 48.42           C  
ANISOU 1946  CD1 LEU A 250     9572   4240   4584    547    320   -169       C  
ATOM   1947  CD2 LEU A 250      35.240  29.517  19.753  1.00 44.71           C  
ANISOU 1947  CD2 LEU A 250     8926   3873   4190    584    292    -85       C  
ATOM   1948  N   GLU A 251      30.867  27.501  22.220  1.00 51.24           N  
ANISOU 1948  N   GLU A 251     9409   4952   5109    429    -17   -275       N  
ATOM   1949  CA  GLU A 251      29.452  27.590  22.599  1.00 53.19           C  
ANISOU 1949  CA  GLU A 251     9570   5291   5350    405   -135   -332       C  
ATOM   1950  C   GLU A 251      29.316  27.967  24.057  1.00 53.91           C  
ANISOU 1950  C   GLU A 251     9509   5456   5521    398   -143   -312       C  
ATOM   1951  O   GLU A 251      28.394  28.672  24.425  1.00 56.80           O  
ANISOU 1951  O   GLU A 251     9804   5893   5885    415   -223   -340       O  
ATOM   1952  CB  GLU A 251      28.669  26.315  22.305  1.00 54.62           C  
ANISOU 1952  CB  GLU A 251     9769   5474   5510    329   -158   -389       C  
ATOM   1953  CG  GLU A 251      27.186  26.588  22.368  1.00 57.20           C  
ANISOU 1953  CG  GLU A 251    10016   5912   5807    310   -294   -444       C  
ATOM   1954  CD  GLU A 251      26.281  25.441  21.965  1.00 61.53           C  
ANISOU 1954  CD  GLU A 251    10583   6484   6311    211   -336   -510       C  
ATOM   1955  OE1 GLU A 251      25.060  25.628  22.171  1.00 69.76           O  
ANISOU 1955  OE1 GLU A 251    11526   7640   7339    189   -447   -544       O  
ATOM   1956  OE2 GLU A 251      26.739  24.378  21.488  1.00 71.21           O1-
ANISOU 1956  OE2 GLU A 251    11918   7620   7519    151   -253   -529       O1-
ATOM   1957  N   CYS A 252      30.242  27.493  24.888  1.00 55.82           N  
ANISOU 1957  N   CYS A 252     9698   5685   5827    374    -53   -255       N  
ATOM   1958  CA  CYS A 252      30.273  27.845  26.308  1.00 53.24           C  
ANISOU 1958  CA  CYS A 252     9233   5435   5560    350    -52   -229       C  
ATOM   1959  C   CYS A 252      30.435  29.371  26.409  1.00 50.89           C  
ANISOU 1959  C   CYS A 252     8942   5153   5239    389    -70   -227       C  
ATOM   1960  O   CYS A 252      29.641  30.029  27.071  1.00 52.11           O  
ANISOU 1960  O   CYS A 252     9028   5368   5404    390   -121   -261       O  
ATOM   1961  CB  CYS A 252      31.416  27.089  26.988  1.00 54.03           C  
ANISOU 1961  CB  CYS A 252     9286   5526   5715    322     51   -145       C  
ATOM   1962  SG  CYS A 252      31.743  27.534  28.701  1.00 58.10           S  
ANISOU 1962  SG  CYS A 252     9643   6153   6280    273     61    -94       S  
ATOM   1963  N   ALA A 253      31.410  29.924  25.699  1.00 47.52           N  
ANISOU 1963  N   ALA A 253     8611   4666   4781    423    -19   -192       N  
ATOM   1964  CA  ALA A 253      31.664  31.369  25.742  1.00 50.94           C  
ANISOU 1964  CA  ALA A 253     9074   5093   5189    450    -15   -190       C  
ATOM   1965  C   ALA A 253      30.465  32.194  25.288  1.00 52.82           C  
ANISOU 1965  C   ALA A 253     9344   5335   5391    510    -97   -244       C  
ATOM   1966  O   ALA A 253      30.069  33.166  25.941  1.00 54.97           O  
ANISOU 1966  O   ALA A 253     9580   5633   5674    522   -105   -260       O  
ATOM   1967  CB  ALA A 253      32.886  31.743  24.929  1.00 47.44           C  
ANISOU 1967  CB  ALA A 253     8735   4579   4712    471     57   -142       C  
ATOM   1968  N   ASP A 254      29.877  31.796  24.176  1.00 57.20           N  
ANISOU 1968  N   ASP A 254     9968   5868   5899    547   -152   -268       N  
ATOM   1969  CA  ASP A 254      28.760  32.521  23.613  1.00 59.76           C  
ANISOU 1969  CA  ASP A 254    10312   6215   6181    614   -237   -295       C  
ATOM   1970  C   ASP A 254      27.581  32.406  24.575  1.00 57.26           C  
ANISOU 1970  C   ASP A 254     9856   5989   5909    601   -296   -328       C  
ATOM   1971  O   ASP A 254      26.955  33.401  24.932  1.00 52.49           O  
ANISOU 1971  O   ASP A 254     9218   5409   5316    656   -314   -332       O  
ATOM   1972  CB  ASP A 254      28.424  31.947  22.238  1.00 64.85           C  
ANISOU 1972  CB  ASP A 254    11049   6843   6749    628   -290   -309       C  
ATOM   1973  CG  ASP A 254      27.357  32.736  21.509  1.00 75.77           C  
ANISOU 1973  CG  ASP A 254    12450   8267   8073    705   -384   -312       C  
ATOM   1974  OD1 ASP A 254      26.885  33.763  22.058  1.00 72.83           O  
ANISOU 1974  OD1 ASP A 254    12024   7917   7729    767   -393   -299       O  
ATOM   1975  OD2 ASP A 254      27.008  32.312  20.366  1.00 83.08           O1-
ANISOU 1975  OD2 ASP A 254    13448   9202   8917    703   -441   -322       O1-
ATOM   1976  N   ASP A 255      27.303  31.187  25.017  1.00 56.70           N  
ANISOU 1976  N   ASP A 255     9712   5962   5870    529   -311   -349       N  
ATOM   1977  CA  ASP A 255      26.148  30.951  25.871  1.00 58.93           C  
ANISOU 1977  CA  ASP A 255     9861   6336   6193    507   -367   -381       C  
ATOM   1978  C   ASP A 255      26.250  31.731  27.180  1.00 58.98           C  
ANISOU 1978  C   ASP A 255     9790   6366   6255    505   -320   -376       C  
ATOM   1979  O   ASP A 255      25.240  32.203  27.726  1.00 57.50           O  
ANISOU 1979  O   ASP A 255     9520   6238   6090    533   -355   -398       O  
ATOM   1980  CB  ASP A 255      26.006  29.462  26.140  1.00 57.21           C  
ANISOU 1980  CB  ASP A 255     9596   6141   5999    417   -368   -401       C  
ATOM   1981  N   ARG A 256      27.486  31.924  27.645  1.00 61.12           N  
ANISOU 1981  N   ARG A 256    10089   6593   6539    470   -235   -343       N  
ATOM   1982  CA  ARG A 256      27.732  32.669  28.879  1.00 59.23           C  
ANISOU 1982  CA  ARG A 256     9795   6380   6331    438   -183   -343       C  
ATOM   1983  C   ARG A 256      27.544  34.156  28.683  1.00 57.11           C  
ANISOU 1983  C   ARG A 256     9593   6067   6040    508   -163   -353       C  
ATOM   1984  O   ARG A 256      26.988  34.824  29.538  1.00 58.79           O  
ANISOU 1984  O   ARG A 256     9758   6305   6275    511   -143   -379       O  
ATOM   1985  CB  ARG A 256      29.147  32.422  29.367  1.00 58.80           C  
ANISOU 1985  CB  ARG A 256     9744   6315   6284    364   -105   -294       C  
ATOM   1986  CG  ARG A 256      29.387  32.873  30.795  1.00 57.50           C  
ANISOU 1986  CG  ARG A 256     9501   6208   6137    287    -61   -294       C  
ATOM   1987  CD  ARG A 256      30.852  33.176  30.975  1.00 59.73           C  
ANISOU 1987  CD  ARG A 256     9814   6483   6398    227     11   -240       C  
ATOM   1988  NE  ARG A 256      31.270  33.330  32.362  1.00 58.63           N  
ANISOU 1988  NE  ARG A 256     9588   6427   6261    119     49   -226       N  
ATOM   1989  CZ  ARG A 256      32.425  33.880  32.731  1.00 60.75           C  
ANISOU 1989  CZ  ARG A 256     9869   6719   6495     41    108   -186       C  
ATOM   1990  NH1 ARG A 256      33.279  34.379  31.830  1.00 62.69           N1+
ANISOU 1990  NH1 ARG A 256    10209   6899   6711     65    142   -159       N1+
ATOM   1991  NH2 ARG A 256      32.724  33.949  34.020  1.00 64.39           N  
ANISOU 1991  NH2 ARG A 256    10244   7278   6943    -74    131   -174       N  
ATOM   1992  N   ALA A 257      28.016  34.684  27.560  1.00 57.06           N  
ANISOU 1992  N   ALA A 257     9707   5986   5987    567   -154   -331       N  
ATOM   1993  CA  ALA A 257      27.825  36.114  27.278  1.00 56.36           C  
ANISOU 1993  CA  ALA A 257     9701   5838   5877    647   -124   -332       C  
ATOM   1994  C   ALA A 257      26.352  36.416  27.120  1.00 57.50           C  
ANISOU 1994  C   ALA A 257     9794   6022   6031    743   -189   -346       C  
ATOM   1995  O   ALA A 257      25.884  37.437  27.620  1.00 60.45           O  
ANISOU 1995  O   ALA A 257    10170   6376   6424    793   -144   -355       O  
ATOM   1996  CB  ALA A 257      28.610  36.577  26.081  1.00 51.44           C  
ANISOU 1996  CB  ALA A 257     9218   5128   5199    692   -100   -299       C  
ATOM   1997  N   ASP A 258      25.612  35.511  26.484  1.00 59.06           N  
ANISOU 1997  N   ASP A 258     9943   6281   6215    759   -285   -347       N  
ATOM   1998  CA  ASP A 258      24.178  35.714  26.343  1.00 63.28           C  
ANISOU 1998  CA  ASP A 258    10400   6888   6757    841   -358   -347       C  
ATOM   1999  C   ASP A 258      23.551  35.797  27.707  1.00 63.85           C  
ANISOU 1999  C   ASP A 258    10350   7013   6895    815   -329   -378       C  
ATOM   2000  O   ASP A 258      22.703  36.661  27.944  1.00 66.77           O  
ANISOU 2000  O   ASP A 258    10687   7395   7287    907   -316   -369       O  
ATOM   2001  CB  ASP A 258      23.492  34.593  25.578  1.00 65.73           C  
ANISOU 2001  CB  ASP A 258    10661   7279   7033    818   -470   -353       C  
ATOM   2002  CG  ASP A 258      23.844  34.570  24.101  1.00 69.07           C  
ANISOU 2002  CG  ASP A 258    11207   7663   7372    852   -509   -325       C  
ATOM   2003  OD1 ASP A 258      24.529  35.505  23.624  1.00 77.24           O  
ANISOU 2003  OD1 ASP A 258    12358   8609   8381    913   -455   -294       O  
ATOM   2004  OD2 ASP A 258      23.427  33.588  23.417  1.00 74.53           O1-
ANISOU 2004  OD2 ASP A 258    11887   8414   8019    803   -590   -340       O1-
ATOM   2005  N   LEU A 259      23.986  34.919  28.611  1.00 63.10           N  
ANISOU 2005  N   LEU A 259    10194   6949   6831    697   -309   -405       N  
ATOM   2006  CA  LEU A 259      23.399  34.868  29.951  1.00 62.22           C  
ANISOU 2006  CA  LEU A 259     9967   6899   6775    655   -282   -436       C  
ATOM   2007  C   LEU A 259      23.659  36.144  30.730  1.00 62.30           C  
ANISOU 2007  C   LEU A 259    10022   6850   6797    674   -177   -448       C  
ATOM   2008  O   LEU A 259      22.801  36.596  31.466  1.00 65.72           O  
ANISOU 2008  O   LEU A 259    10391   7314   7267    706   -149   -469       O  
ATOM   2009  CB  LEU A 259      23.889  33.661  30.743  1.00 61.04           C  
ANISOU 2009  CB  LEU A 259     9751   6793   6648    526   -277   -449       C  
ATOM   2010  CG  LEU A 259      23.419  33.620  32.215  1.00 61.95           C  
ANISOU 2010  CG  LEU A 259     9757   6973   6810    466   -240   -478       C  
ATOM   2011  CD1 LEU A 259      21.909  33.420  32.267  1.00 61.08           C  
ANISOU 2011  CD1 LEU A 259     9534   6943   6729    516   -303   -498       C  
ATOM   2012  CD2 LEU A 259      24.142  32.557  33.041  1.00 57.39           C  
ANISOU 2012  CD2 LEU A 259     9128   6431   6246    341   -220   -470       C  
ATOM   2013  N   ALA A 260      24.831  36.735  30.562  1.00 61.82           N  
ANISOU 2013  N   ALA A 260    10079   6704   6704    647   -109   -436       N  
ATOM   2014  CA  ALA A 260      25.116  38.001  31.218  1.00 60.57           C  
ANISOU 2014  CA  ALA A 260     9993   6478   6545    645      3   -456       C  
ATOM   2015  C   ALA A 260      24.230  39.131  30.665  1.00 62.75           C  
ANISOU 2015  C   ALA A 260    10323   6693   6826    801     27   -443       C  
ATOM   2016  O   ALA A 260      23.645  39.894  31.451  1.00 62.08           O  
ANISOU 2016  O   ALA A 260    10229   6588   6771    832    106   -469       O  
ATOM   2017  CB  ALA A 260      26.583  38.337  31.082  1.00 60.72           C  
ANISOU 2017  CB  ALA A 260    10121   6430   6520    565     65   -444       C  
ATOM   2018  N   LYS A 261      24.105  39.224  29.331  1.00 61.80           N  
ANISOU 2018  N   LYS A 261    10259   6546   6677    905    -33   -395       N  
ATOM   2019  CA  LYS A 261      23.204  40.214  28.722  1.00 61.82           C  
ANISOU 2019  CA  LYS A 261    10295   6510   6684   1073    -22   -355       C  
ATOM   2020  C   LYS A 261      21.813  40.043  29.334  1.00 62.50           C  
ANISOU 2020  C   LYS A 261    10231   6692   6826   1131    -51   -360       C  
ATOM   2021  O   LYS A 261      21.249  41.004  29.878  1.00 65.94           O  
ANISOU 2021  O   LYS A 261    10675   7082   7298   1213     44   -360       O  
ATOM   2022  CB  LYS A 261      23.158  40.149  27.176  1.00 60.00           C  
ANISOU 2022  CB  LYS A 261    10122   6275   6401   1166   -109   -293       C  
ATOM   2023  N   TYR A 262      21.287  38.823  29.344  1.00 60.63           N  
ANISOU 2023  N   TYR A 262     9860   6581   6598   1080   -164   -368       N  
ATOM   2024  CA  TYR A 262      19.953  38.625  29.900  1.00 63.48           C  
ANISOU 2024  CA  TYR A 262    10064   7046   7010   1126   -194   -369       C  
ATOM   2025  C   TYR A 262      19.874  39.070  31.375  1.00 65.49           C  
ANISOU 2025  C   TYR A 262    10294   7274   7316   1080    -72   -421       C  
ATOM   2026  O   TYR A 262      18.908  39.725  31.789  1.00 64.70           O  
ANISOU 2026  O   TYR A 262    10139   7183   7260   1183    -16   -409       O  
ATOM   2027  CB  TYR A 262      19.500  37.176  29.766  1.00 64.35           C  
ANISOU 2027  CB  TYR A 262    10046   7289   7116   1041   -322   -382       C  
ATOM   2028  CG  TYR A 262      18.178  36.889  30.432  1.00 66.95           C  
ANISOU 2028  CG  TYR A 262    10202   7737   7498   1063   -351   -387       C  
ATOM   2029  CD1 TYR A 262      16.978  37.012  29.738  1.00 67.96           C  
ANISOU 2029  CD1 TYR A 262    10230   7965   7625   1179   -433   -329       C  
ATOM   2030  CD2 TYR A 262      18.129  36.499  31.766  1.00 69.72           C  
ANISOU 2030  CD2 TYR A 262    10481   8114   7895    965   -295   -442       C  
ATOM   2031  CE1 TYR A 262      15.771  36.743  30.356  1.00 71.74           C  
ANISOU 2031  CE1 TYR A 262    10536   8567   8156   1196   -455   -327       C  
ATOM   2032  CE2 TYR A 262      16.928  36.245  32.400  1.00 70.86           C  
ANISOU 2032  CE2 TYR A 262    10468   8367   8090    982   -311   -447       C  
ATOM   2033  CZ  TYR A 262      15.754  36.361  31.695  1.00 73.87           C  
ANISOU 2033  CZ  TYR A 262    10745   8846   8477   1097   -389   -391       C  
ATOM   2034  OH  TYR A 262      14.570  36.098  32.343  1.00 80.08           O  
ANISOU 2034  OH  TYR A 262    11359   9751   9315   1110   -400   -391       O  
ATOM   2035  N   ILE A 263      20.880  38.720  32.167  1.00 62.90           N  
ANISOU 2035  N   ILE A 263    10004   6920   6976    927    -25   -473       N  
ATOM   2036  CA  ILE A 263      20.864  39.133  33.558  1.00 65.17           C  
ANISOU 2036  CA  ILE A 263    10281   7192   7290    860     89   -526       C  
ATOM   2037  C   ILE A 263      20.808  40.660  33.677  1.00 68.73           C  
ANISOU 2037  C   ILE A 263    10854   7515   7744    953    231   -529       C  
ATOM   2038  O   ILE A 263      19.952  41.198  34.374  1.00 73.44           O  
ANISOU 2038  O   ILE A 263    11413   8107   8384   1013    314   -546       O  
ATOM   2039  CB  ILE A 263      22.027  38.514  34.358  1.00 62.44           C  
ANISOU 2039  CB  ILE A 263     9949   6861   6915    671    107   -564       C  
ATOM   2040  CG1 ILE A 263      21.705  37.041  34.652  1.00 61.55           C  
ANISOU 2040  CG1 ILE A 263     9691   6873   6822    594      6   -565       C  
ATOM   2041  CG2 ILE A 263      22.236  39.265  35.656  1.00 61.52           C  
ANISOU 2041  CG2 ILE A 263     9874   6708   6794    590    242   -620       C  
ATOM   2042  CD1 ILE A 263      22.840  36.253  35.238  1.00 59.24           C  
ANISOU 2042  CD1 ILE A 263     9396   6607   6504    435      7   -569       C  
ATOM   2043  N   CYS A 264      21.664  41.371  32.959  1.00 69.44           N  
ANISOU 2043  N   CYS A 264    11098   7494   7793    975    272   -510       N  
ATOM   2044  CA  CYS A 264      21.637  42.837  33.034  1.00 71.62           C  
ANISOU 2044  CA  CYS A 264    11514   7626   8071   1061    426   -513       C  
ATOM   2045  C   CYS A 264      20.333  43.468  32.549  1.00 75.54           C  
ANISOU 2045  C   CYS A 264    11972   8110   8618   1280    443   -450       C  
ATOM   2046  O   CYS A 264      19.891  44.474  33.096  1.00 80.90           O  
ANISOU 2046  O   CYS A 264    12711   8698   9331   1354    592   -462       O  
ATOM   2047  CB  CYS A 264      22.810  43.437  32.277  1.00 69.25           C  
ANISOU 2047  CB  CYS A 264    11387   7210   7714   1037    464   -498       C  
ATOM   2048  SG  CYS A 264      24.374  42.891  32.994  1.00 69.48           S  
ANISOU 2048  SG  CYS A 264    11450   7263   7686    782    473   -557       S  
ATOM   2049  N   ASP A 265      19.707  42.871  31.545  1.00 77.88           N  
ANISOU 2049  N   ASP A 265    12168   8504   8918   1380    297   -379       N  
ATOM   2050  CA  ASP A 265      18.468  43.420  30.998  1.00 78.78           C  
ANISOU 2050  CA  ASP A 265    12218   8642   9073   1593    293   -293       C  
ATOM   2051  C   ASP A 265      17.285  43.247  31.927  1.00 75.70           C  
ANISOU 2051  C   ASP A 265    11666   8343   8752   1632    319   -303       C  
ATOM   2052  O   ASP A 265      16.286  43.932  31.766  1.00 78.20           O  
ANISOU 2052  O   ASP A 265    11935   8659   9116   1816    370   -232       O  
ATOM   2053  CB  ASP A 265      18.141  42.785  29.637  1.00 81.71           C  
ANISOU 2053  CB  ASP A 265    12518   9121   9406   1662    114   -212       C  
ATOM   2054  CG  ASP A 265      19.066  43.268  28.532  1.00 85.38           C  
ANISOU 2054  CG  ASP A 265    13154   9481   9807   1690    113   -174       C  
ATOM   2055  OD1 ASP A 265      20.063  43.973  28.831  1.00 94.36           O  
ANISOU 2055  OD1 ASP A 265    14456  10468  10928   1633    239   -216       O  
ATOM   2056  OD2 ASP A 265      18.806  42.951  27.358  1.00 86.84           O1-
ANISOU 2056  OD2 ASP A 265    13311   9737   9948   1758    -13   -103       O1-
ATOM   2057  N   ASN A 266      17.393  42.327  32.882  1.00 76.46           N  
ANISOU 2057  N   ASN A 266    11674   8521   8856   1468    289   -381       N  
ATOM   2058  CA  ASN A 266      16.291  42.007  33.786  1.00 78.39           C  
ANISOU 2058  CA  ASN A 266    11755   8867   9163   1482    304   -396       C  
ATOM   2059  C   ASN A 266      16.696  42.192  35.241  1.00 81.02           C  
ANISOU 2059  C   ASN A 266    12139   9142   9504   1345    444   -495       C  
ATOM   2060  O   ASN A 266      16.064  41.613  36.139  1.00 88.04           O  
ANISOU 2060  O   ASN A 266    12897  10128  10428   1289    441   -529       O  
ATOM   2061  CB  ASN A 266      15.829  40.553  33.592  1.00 77.75           C  
ANISOU 2061  CB  ASN A 266    11494   8970   9079   1402    123   -392       C  
ATOM   2062  CG  ASN A 266      15.394  40.244  32.175  1.00 79.70           C  
ANISOU 2062  CG  ASN A 266    11684   9301   9297   1500    -28   -304       C  
ATOM   2063  ND2 ASN A 266      16.203  39.446  31.485  1.00 78.40           N  
ANISOU 2063  ND2 ASN A 266    11569   9149   9070   1392   -137   -319       N  
ATOM   2064  OD1 ASN A 266      14.338  40.691  31.710  1.00 77.25           O  
ANISOU 2064  OD1 ASN A 266    11282   9053   9016   1667    -46   -220       O  
ATOM   2065  N   GLN A 267      17.737  42.985  35.493  1.00 77.28           N  
ANISOU 2065  N   GLN A 267    11855   8520   8989   1277    566   -541       N  
ATOM   2066  CA  GLN A 267      18.229  43.132  36.855  1.00 77.85           C  
ANISOU 2066  CA  GLN A 267    11983   8553   9042   1112    688   -638       C  
ATOM   2067  C   GLN A 267      17.135  43.577  37.838  1.00 81.66           C  
ANISOU 2067  C   GLN A 267    12408   9035   9585   1179    819   -664       C  
ATOM   2068  O   GLN A 267      17.181  43.214  39.013  1.00 81.05           O  
ANISOU 2068  O   GLN A 267    12294   9003   9497   1034    863   -737       O  
ATOM   2069  CB  GLN A 267      19.485  44.017  36.937  1.00 75.97           C  
ANISOU 2069  CB  GLN A 267    11963   8162   8740   1016    806   -684       C  
ATOM   2070  CG  GLN A 267      19.381  45.434  36.399  1.00 76.97           C  
ANISOU 2070  CG  GLN A 267    12255   8112   8878   1171    952   -654       C  
ATOM   2071  CD  GLN A 267      20.740  46.110  36.314  1.00 75.31           C  
ANISOU 2071  CD  GLN A 267    12251   7771   8592   1044   1036   -698       C  
ATOM   2072  NE2 GLN A 267      21.218  46.305  35.093  1.00 68.37           N  
ANISOU 2072  NE2 GLN A 267    11444   6841   7692   1120    977   -633       N  
ATOM   2073  OE1 GLN A 267      21.365  46.429  37.341  1.00 79.84           O  
ANISOU 2073  OE1 GLN A 267    12916   8302   9118    865   1149   -788       O  
ATOM   2074  N   ASP A 268      16.122  44.289  37.351  1.00 84.61           N  
ANISOU 2074  N   ASP A 268    12756   9371  10021   1401    875   -593       N  
ATOM   2075  CA  ASP A 268      15.007  44.682  38.208  1.00 90.67           C  
ANISOU 2075  CA  ASP A 268    13451  10143  10857   1492   1007   -601       C  
ATOM   2076  C   ASP A 268      14.244  43.489  38.800  1.00 89.59           C  
ANISOU 2076  C   ASP A 268    13090  10197  10752   1426    897   -613       C  
ATOM   2077  O   ASP A 268      13.777  43.567  39.924  1.00 91.24           O  
ANISOU 2077  O   ASP A 268    13266  10415  10987   1384   1011   -669       O  
ATOM   2078  CB  ASP A 268      14.054  45.649  37.479  1.00 97.28           C  
ANISOU 2078  CB  ASP A 268    14283  10916  11762   1770   1087   -493       C  
ATOM   2079  CG  ASP A 268      14.641  47.077  37.338  1.00101.72           C  
ANISOU 2079  CG  ASP A 268    15100  11242  12309   1837   1290   -502       C  
ATOM   2080  OD1 ASP A 268      15.495  47.478  38.167  1.00 99.20           O  
ANISOU 2080  OD1 ASP A 268    14949  10804  11936   1665   1422   -614       O  
ATOM   2081  OD2 ASP A 268      14.241  47.802  36.391  1.00103.44           O1-
ANISOU 2081  OD2 ASP A 268    15350  11394  12560   2056   1319   -392       O1-
ATOM   2082  N   THR A 269      14.144  42.379  38.076  1.00 89.81           N  
ANISOU 2082  N   THR A 269    12979  10373  10772   1401    687   -567       N  
ATOM   2083  CA  THR A 269      13.531  41.162  38.639  1.00 85.51           C  
ANISOU 2083  CA  THR A 269    12239  10001  10249   1307    584   -586       C  
ATOM   2084  C   THR A 269      14.527  40.068  39.062  1.00 81.03           C  
ANISOU 2084  C   THR A 269    11683   9484   9621   1073    492   -651       C  
ATOM   2085  O   THR A 269      14.133  38.908  39.213  1.00 78.49           O  
ANISOU 2085  O   THR A 269    11212   9301   9311    998    376   -651       O  
ATOM   2086  CB  THR A 269      12.575  40.542  37.629  1.00 86.09           C  
ANISOU 2086  CB  THR A 269    12132  10225  10354   1422    419   -492       C  
ATOM   2087  CG2 THR A 269      11.529  41.557  37.184  1.00 89.36           C  
ANISOU 2087  CG2 THR A 269    12500  10623  10831   1671    497   -398       C  
ATOM   2088  OG1 THR A 269      13.333  40.119  36.499  1.00 88.55           O  
ANISOU 2088  OG1 THR A 269    12502  10537  10607   1388    278   -464       O  
ATOM   2089  N   ILE A 270      15.797  40.435  39.262  1.00 80.39           N  
ANISOU 2089  N   ILE A 270    11773   9295   9478    960    549   -699       N  
ATOM   2090  CA  ILE A 270      16.830  39.503  39.732  1.00 74.87           C  
ANISOU 2090  CA  ILE A 270    11083   8642   8720    750    483   -742       C  
ATOM   2091  C   ILE A 270      17.579  40.029  40.940  1.00 73.31           C  
ANISOU 2091  C   ILE A 270    11001   8381   8472    600    624   -820       C  
ATOM   2092  O   ILE A 270      17.681  39.322  41.942  1.00 75.02           O  
ANISOU 2092  O   ILE A 270    11151   8683   8670    453    617   -857       O  
ATOM   2093  CB  ILE A 270      17.892  39.204  38.670  1.00 74.07           C  
ANISOU 2093  CB  ILE A 270    11061   8512   8572    721    380   -707       C  
ATOM   2094  CG1 ILE A 270      17.264  38.569  37.432  1.00 76.55           C  
ANISOU 2094  CG1 ILE A 270    11276   8900   8911    832    228   -638       C  
ATOM   2095  CG2 ILE A 270      18.940  38.255  39.237  1.00 70.05           C  
ANISOU 2095  CG2 ILE A 270    10547   8056   8013    521    330   -733       C  
ATOM   2096  CD1 ILE A 270      18.216  38.448  36.260  1.00 75.12           C  
ANISOU 2096  CD1 ILE A 270    11192   8669   8681    832    149   -603       C  
ATOM   2097  N   SER A 271      18.142  41.234  40.846  1.00 73.41           N  
ANISOU 2097  N   SER A 271    11191   8249   8453    619    750   -843       N  
ATOM   2098  CA  SER A 271      18.889  41.807  41.986  1.00 75.72           C  
ANISOU 2098  CA  SER A 271    11609   8483   8676    448    891   -927       C  
ATOM   2099  C   SER A 271      19.228  43.292  41.905  1.00 74.40           C  
ANISOU 2099  C   SER A 271    11651   8135   8482    486   1067   -963       C  
ATOM   2100  O   SER A 271      19.481  43.834  40.831  1.00 77.64           O  
ANISOU 2100  O   SER A 271    12147   8453   8901    599   1059   -916       O  
ATOM   2101  CB  SER A 271      20.195  41.041  42.211  1.00 74.74           C  
ANISOU 2101  CB  SER A 271    11492   8433   8475    243    800   -932       C  
ATOM   2102  OG  SER A 271      20.976  41.665  43.216  1.00 77.07           O  
ANISOU 2102  OG  SER A 271    11909   8689   8685     63    925  -1004       O  
ATOM   2103  N   SER A 272      19.285  43.923  43.070  1.00 73.26           N  
ANISOU 2103  N   SER A 272    11600   7938   8296    371   1234  -1050       N  
ATOM   2104  CA  SER A 272      19.644  45.332  43.176  1.00 74.91           C  
ANISOU 2104  CA  SER A 272    12033   7961   8467    366   1433  -1105       C  
ATOM   2105  C   SER A 272      21.141  45.559  43.250  1.00 74.63           C  
ANISOU 2105  C   SER A 272    12136   7899   8320    153   1435  -1144       C  
ATOM   2106  O   SER A 272      21.577  46.700  43.202  1.00 75.76           O  
ANISOU 2106  O   SER A 272    12479   7884   8422    127   1590  -1190       O  
ATOM   2107  CB  SER A 272      19.004  45.967  44.421  1.00 75.72           C  
ANISOU 2107  CB  SER A 272    12199   8006   8565    324   1637  -1193       C  
ATOM   2108  OG  SER A 272      19.690  45.590  45.604  1.00 72.17           O  
ANISOU 2108  OG  SER A 272    11763   7645   8014     54   1647  -1274       O  
ATOM   2109  N   LYS A 273      21.929  44.494  43.362  1.00 77.03           N  
ANISOU 2109  N   LYS A 273    12336   8356   8577      1   1275  -1121       N  
ATOM   2110  CA  LYS A 273      23.383  44.628  43.544  1.00 78.87           C  
ANISOU 2110  CA  LYS A 273    12666   8602   8698   -218   1271  -1145       C  
ATOM   2111  C   LYS A 273      24.210  44.498  42.245  1.00 76.67           C  
ANISOU 2111  C   LYS A 273    12409   8301   8421   -163   1162  -1070       C  
ATOM   2112  O   LYS A 273      25.434  44.379  42.301  1.00 76.42           O  
ANISOU 2112  O   LYS A 273    12411   8316   8309   -334   1127  -1066       O  
ATOM   2113  CB  LYS A 273      23.862  43.596  44.575  1.00 80.95           C  
ANISOU 2113  CB  LYS A 273    12804   9055   8898   -428   1184  -1152       C  
ATOM   2114  N   LEU A 274      23.557  44.536  41.085  1.00 76.35           N  
ANISOU 2114  N   LEU A 274    12346   8198   8466     70   1111  -1005       N  
ATOM   2115  CA  LEU A 274      24.239  44.277  39.807  1.00 75.53           C  
ANISOU 2115  CA  LEU A 274    12250   8084   8363    130    997   -931       C  
ATOM   2116  C   LEU A 274      24.654  45.539  39.009  1.00 80.12           C  
ANISOU 2116  C   LEU A 274    13033   8484   8926    198   1108   -931       C  
ATOM   2117  O   LEU A 274      25.384  45.435  38.024  1.00 82.28           O  
ANISOU 2117  O   LEU A 274    13339   8742   9183    218   1035   -878       O  
ATOM   2118  CB  LEU A 274      23.343  43.417  38.916  1.00 73.66           C  
ANISOU 2118  CB  LEU A 274    11863   7913   8211    321    850   -852       C  
ATOM   2119  CG  LEU A 274      22.927  42.003  39.327  1.00 71.75           C  
ANISOU 2119  CG  LEU A 274    11421   7841   7999    282    715   -832       C  
ATOM   2120  CD1 LEU A 274      21.541  41.673  38.790  1.00 71.79           C  
ANISOU 2120  CD1 LEU A 274    11308   7878   8091    477    651   -791       C  
ATOM   2121  CD2 LEU A 274      23.928  40.978  38.823  1.00 69.78           C  
ANISOU 2121  CD2 LEU A 274    11118   7675   7720    198    579   -781       C  
ATOM   2122  N   LYS A 275      24.174  46.716  39.396  1.00 82.57           N  
ANISOU 2122  N   LYS A 275    13484   8647   9240    242   1295   -986       N  
ATOM   2123  CA  LYS A 275      24.433  47.933  38.635  1.00 82.70           C  
ANISOU 2123  CA  LYS A 275    13701   8473   9250    329   1419   -978       C  
ATOM   2124  C   LYS A 275      25.897  48.069  38.178  1.00 81.80           C  
ANISOU 2124  C   LYS A 275    13686   8344   9052    174   1393   -976       C  
ATOM   2125  O   LYS A 275      26.164  48.246  36.982  1.00 87.17           O  
ANISOU 2125  O   LYS A 275    14414   8960   9745    290   1348   -909       O  
ATOM   2126  CB  LYS A 275      23.999  49.160  39.459  1.00 82.41           C  
ANISOU 2126  CB  LYS A 275    13832   8274   9204    317   1663  -1064       C  
ATOM   2127  N   GLU A 276      26.841  47.979  39.114  1.00 79.65           N  
ANISOU 2127  N   GLU A 276    13435   8141   8687    -91   1419  -1043       N  
ATOM   2128  CA  GLU A 276      28.265  48.181  38.787  1.00 78.70           C  
ANISOU 2128  CA  GLU A 276    13400   8021   8481   -259   1409  -1039       C  
ATOM   2129  C   GLU A 276      28.787  47.076  37.856  1.00 77.00           C  
ANISOU 2129  C   GLU A 276    13042   7928   8288   -209   1210   -939       C  
ATOM   2130  O   GLU A 276      29.562  47.344  36.930  1.00 82.32           O  
ANISOU 2130  O   GLU A 276    13793   8545   8940   -198   1198   -898       O  
ATOM   2131  CB  GLU A 276      29.130  48.295  40.053  1.00 74.82           C  
ANISOU 2131  CB  GLU A 276    12938   7614   7874   -568   1471  -1121       C  
ATOM   2132  N   CYS A 277      28.335  45.850  38.088  1.00 72.61           N  
ANISOU 2132  N   CYS A 277    12287   7525   7775   -176   1070   -901       N  
ATOM   2133  CA  CYS A 277      28.650  44.726  37.213  1.00 71.50           C  
ANISOU 2133  CA  CYS A 277    12018   7483   7666   -109    898   -811       C  
ATOM   2134  C   CYS A 277      28.216  44.958  35.782  1.00 70.76           C  
ANISOU 2134  C   CYS A 277    11976   7285   7625    114    864   -752       C  
ATOM   2135  O   CYS A 277      28.953  44.644  34.837  1.00 63.21           O  
ANISOU 2135  O   CYS A 277    11029   6334   6654    129    793   -695       O  
ATOM   2136  CB  CYS A 277      27.937  43.456  37.673  1.00 68.39           C  
ANISOU 2136  CB  CYS A 277    11426   7237   7323    -81    779   -789       C  
ATOM   2137  SG  CYS A 277      28.706  42.595  39.023  1.00 73.50           S  
ANISOU 2137  SG  CYS A 277    11950   8068   7907   -329    741   -798       S  
ATOM   2138  N   CYS A 278      26.998  45.469  35.633  1.00 71.42           N  
ANISOU 2138  N   CYS A 278    12082   7287   7767    289    913   -759       N  
ATOM   2139  CA  CYS A 278      26.360  45.497  34.330  1.00 72.51           C  
ANISOU 2139  CA  CYS A 278    12221   7373   7955    514    850   -685       C  
ATOM   2140  C   CYS A 278      26.767  46.697  33.510  1.00 74.81           C  
ANISOU 2140  C   CYS A 278    12709   7493   8221    583    956   -668       C  
ATOM   2141  O   CYS A 278      26.230  46.911  32.433  1.00 71.44           O  
ANISOU 2141  O   CYS A 278    12305   7014   7826    775    921   -599       O  
ATOM   2142  CB  CYS A 278      24.854  45.416  34.493  1.00 72.86           C  
ANISOU 2142  CB  CYS A 278    12169   7441   8075    680    840   -673       C  
ATOM   2143  SG  CYS A 278      24.341  43.726  34.862  1.00 73.62           S  
ANISOU 2143  SG  CYS A 278    12020   7746   8205    642    661   -659       S  
ATOM   2144  N   ASP A 279      27.731  47.466  34.016  1.00 80.24           N  
ANISOU 2144  N   ASP A 279    13539   8103   8844    415   1082   -726       N  
ATOM   2145  CA  ASP A 279      28.308  48.564  33.258  1.00 86.97           C  
ANISOU 2145  CA  ASP A 279    14591   8790   9663    444   1190   -714       C  
ATOM   2146  C   ASP A 279      29.688  48.205  32.749  1.00 85.64           C  
ANISOU 2146  C   ASP A 279    14438   8669   9433    307   1126   -690       C  
ATOM   2147  O   ASP A 279      30.319  48.996  32.035  1.00 93.93           O  
ANISOU 2147  O   ASP A 279    15644   9597  10448    311   1201   -674       O  
ATOM   2148  CB  ASP A 279      28.368  49.835  34.107  1.00 91.21           C  
ANISOU 2148  CB  ASP A 279    15309   9179  10169    351   1408   -801       C  
ATOM   2149  CG  ASP A 279      26.994  50.467  34.312  1.00 95.26           C  
ANISOU 2149  CG  ASP A 279    15854   9588  10754    547   1516   -803       C  
ATOM   2150  OD1 ASP A 279      26.057  50.149  33.537  1.00 92.10           O  
ANISOU 2150  OD1 ASP A 279    15359   9212  10424    778   1426   -716       O  
ATOM   2151  OD2 ASP A 279      26.859  51.284  35.252  1.00 97.16           O1-
ANISOU 2151  OD2 ASP A 279    16213   9726  10976    464   1698   -888       O1-
ATOM   2152  N   LYS A 280      30.146  47.005  33.074  1.00 75.35           N  
ANISOU 2152  N   LYS A 280    12970   7539   8120    197    996   -677       N  
ATOM   2153  CA  LYS A 280      31.501  46.635  32.733  1.00 72.94           C  
ANISOU 2153  CA  LYS A 280    12661   7293   7761     61    952   -647       C  
ATOM   2154  C   LYS A 280      31.584  45.993  31.344  1.00 68.43           C  
ANISOU 2154  C   LYS A 280    12057   6731   7215    208    835   -560       C  
ATOM   2155  O   LYS A 280      30.579  45.512  30.804  1.00 62.98           O  
ANISOU 2155  O   LYS A 280    11298   6055   6578    382    749   -526       O  
ATOM   2156  CB  LYS A 280      32.059  45.712  33.816  1.00 76.23           C  
ANISOU 2156  CB  LYS A 280    12925   7890   8151   -131    891   -660       C  
ATOM   2157  CG  LYS A 280      31.946  46.305  35.218  1.00 82.03           C  
ANISOU 2157  CG  LYS A 280    13694   8632   8844   -294   1002   -750       C  
ATOM   2158  CD  LYS A 280      32.792  45.563  36.253  1.00 86.39           C  
ANISOU 2158  CD  LYS A 280    14115   9372   9338   -522    952   -750       C  
ATOM   2159  CE  LYS A 280      33.377  46.483  37.312  1.00 88.25           C  
ANISOU 2159  CE  LYS A 280    14454   9602   9475   -762   1083   -833       C  
ATOM   2160  NZ  LYS A 280      32.293  47.315  37.899  1.00 92.77           N1+
ANISOU 2160  NZ  LYS A 280    15135  10049  10063   -714   1210   -926       N1+
ATOM   2161  N   PRO A 281      32.794  45.973  30.769  1.00 68.50           N  
ANISOU 2161  N   PRO A 281    12111   6739   7177    126    834   -526       N  
ATOM   2162  CA  PRO A 281      33.103  45.262  29.512  1.00 66.73           C  
ANISOU 2162  CA  PRO A 281    11860   6533   6961    227    735   -449       C  
ATOM   2163  C   PRO A 281      32.832  43.773  29.615  1.00 66.69           C  
ANISOU 2163  C   PRO A 281    11670   6674   6995    246    598   -417       C  
ATOM   2164  O   PRO A 281      32.772  43.230  30.727  1.00 65.51           O  
ANISOU 2164  O   PRO A 281    11402   6633   6857    142    579   -443       O  
ATOM   2165  CB  PRO A 281      34.605  45.483  29.326  1.00 67.23           C  
ANISOU 2165  CB  PRO A 281    11979   6600   6965     76    786   -429       C  
ATOM   2166  CG  PRO A 281      34.973  46.619  30.206  1.00 68.33           C  
ANISOU 2166  CG  PRO A 281    12225   6681   7056    -80    923   -497       C  
ATOM   2167  CD  PRO A 281      33.975  46.661  31.323  1.00 69.34           C  
ANISOU 2167  CD  PRO A 281    12301   6833   7211    -87    940   -561       C  
ATOM   2168  N   LEU A 282      32.736  43.115  28.461  1.00 67.44           N  
ANISOU 2168  N   LEU A 282    11752   6769   7102    364    513   -363       N  
ATOM   2169  CA  LEU A 282      32.114  41.794  28.357  1.00 67.22           C  
ANISOU 2169  CA  LEU A 282    11584   6842   7115    421    392   -342       C  
ATOM   2170  C   LEU A 282      32.684  40.730  29.290  1.00 64.38           C  
ANISOU 2170  C   LEU A 282    11080   6614   6769    285    361   -335       C  
ATOM   2171  O   LEU A 282      31.961  40.178  30.112  1.00 67.54           O  
ANISOU 2171  O   LEU A 282    11369   7091   7204    271    321   -359       O  
ATOM   2172  CB  LEU A 282      32.172  41.331  26.901  1.00 71.96           C  
ANISOU 2172  CB  LEU A 282    12230   7411   7702    531    328   -291       C  
ATOM   2173  CG  LEU A 282      31.509  40.013  26.494  1.00 73.97           C  
ANISOU 2173  CG  LEU A 282    12380   7743   7981    591    211   -275       C  
ATOM   2174  CD1 LEU A 282      30.859  40.189  25.121  1.00 77.53           C  
ANISOU 2174  CD1 LEU A 282    12914   8140   8405    737    157   -249       C  
ATOM   2175  CD2 LEU A 282      32.521  38.867  26.498  1.00 67.14           C  
ANISOU 2175  CD2 LEU A 282    11452   6940   7119    502    198   -242       C  
ATOM   2176  N   LEU A 283      33.971  40.444  29.190  1.00 64.31           N  
ANISOU 2176  N   LEU A 283    11065   6638   6733    189    385   -291       N  
ATOM   2177  CA  LEU A 283      34.559  39.423  30.066  1.00 62.75           C  
ANISOU 2177  CA  LEU A 283    10719   6574   6548     75    360   -258       C  
ATOM   2178  C   LEU A 283      34.470  39.802  31.536  1.00 67.13           C  
ANISOU 2178  C   LEU A 283    11216   7202   7090    -59    397   -302       C  
ATOM   2179  O   LEU A 283      34.168  38.955  32.378  1.00 76.91           O  
ANISOU 2179  O   LEU A 283    12324   8545   8354   -101    352   -295       O  
ATOM   2180  CB  LEU A 283      36.005  39.138  29.698  1.00 62.47           C  
ANISOU 2180  CB  LEU A 283    10678   6571   6487      5    391   -184       C  
ATOM   2181  CG  LEU A 283      36.118  38.328  28.406  1.00 64.70           C  
ANISOU 2181  CG  LEU A 283    10986   6809   6789    123    353   -135       C  
ATOM   2182  CD1 LEU A 283      37.553  38.220  27.916  1.00 65.20           C  
ANISOU 2182  CD1 LEU A 283    11062   6883   6829     73    408    -60       C  
ATOM   2183  CD2 LEU A 283      35.475  36.962  28.594  1.00 63.46           C  
ANISOU 2183  CD2 LEU A 283    10716   6714   6683    167    280   -123       C  
ATOM   2184  N   GLU A 284      34.712  41.076  31.834  1.00 71.55           N  
ANISOU 2184  N   GLU A 284    11884   7699   7602   -132    486   -349       N  
ATOM   2185  CA  GLU A 284      34.740  41.586  33.205  1.00 70.02           C  
ANISOU 2185  CA  GLU A 284    11669   7564   7372   -289    542   -403       C  
ATOM   2186  C   GLU A 284      33.336  41.585  33.787  1.00 67.94           C  
ANISOU 2186  C   GLU A 284    11378   7286   7151   -215    529   -465       C  
ATOM   2187  O   GLU A 284      33.149  41.366  34.984  1.00 64.72           O  
ANISOU 2187  O   GLU A 284    10887   6971   6732   -323    533   -494       O  
ATOM   2188  CB  GLU A 284      35.312  43.005  33.223  1.00 75.50           C  
ANISOU 2188  CB  GLU A 284    12523   8164   8000   -385    660   -450       C  
ATOM   2189  CG  GLU A 284      36.037  43.407  34.497  1.00 82.89           C  
ANISOU 2189  CG  GLU A 284    13435   9198   8860   -626    721   -482       C  
ATOM   2190  CD  GLU A 284      36.294  44.915  34.594  1.00 95.82           C  
ANISOU 2190  CD  GLU A 284    15265  10711  10432   -725    859   -559       C  
ATOM   2191  OE1 GLU A 284      36.578  45.567  33.549  1.00101.14           O  
ANISOU 2191  OE1 GLU A 284    16072  11253  11102   -652    907   -548       O  
ATOM   2192  OE2 GLU A 284      36.225  45.452  35.731  1.00103.57           O1-
ANISOU 2192  OE2 GLU A 284    16274  11722  11358   -886    930   -633       O1-
ATOM   2193  N   LYS A 285      32.347  41.840  32.933  1.00 66.63           N  
ANISOU 2193  N   LYS A 285    11276   7013   7028    -33    512   -478       N  
ATOM   2194  CA  LYS A 285      30.950  41.819  33.351  1.00 64.63           C  
ANISOU 2194  CA  LYS A 285    10979   6753   6823     61    497   -521       C  
ATOM   2195  C   LYS A 285      30.539  40.483  33.947  1.00 64.30           C  
ANISOU 2195  C   LYS A 285    10763   6849   6820     40    403   -504       C  
ATOM   2196  O   LYS A 285      29.859  40.462  34.966  1.00 66.41           O  
ANISOU 2196  O   LYS A 285    10970   7163   7101      1    420   -549       O  
ATOM   2197  CB  LYS A 285      30.035  42.169  32.188  1.00 62.09           C  
ANISOU 2197  CB  LYS A 285    10725   6328   6536    267    474   -507       C  
ATOM   2198  CG  LYS A 285      28.569  41.917  32.479  1.00 64.03           C  
ANISOU 2198  CG  LYS A 285    10885   6603   6840    379    433   -527       C  
ATOM   2199  CD  LYS A 285      27.638  42.758  31.620  1.00 67.64           C  
ANISOU 2199  CD  LYS A 285    11426   6954   7320    569    455   -512       C  
ATOM   2200  CE  LYS A 285      27.904  42.577  30.130  1.00 71.76           C  
ANISOU 2200  CE  LYS A 285    12002   7441   7824    670    385   -448       C  
ATOM   2201  NZ  LYS A 285      26.956  43.361  29.282  1.00 74.86           N1+
ANISOU 2201  NZ  LYS A 285    12459   7753   8230    863    394   -413       N1+
ATOM   2202  N   SER A 286      30.945  39.377  33.319  1.00 67.99           N  
ANISOU 2202  N   SER A 286    11159   7369   7304     65    317   -440       N  
ATOM   2203  CA  SER A 286      30.522  38.024  33.748  1.00 70.34           C  
ANISOU 2203  CA  SER A 286    11307   7777   7644     58    235   -418       C  
ATOM   2204  C   SER A 286      31.173  37.602  35.051  1.00 68.93           C  
ANISOU 2204  C   SER A 286    11030   7717   7442   -108    254   -404       C  
ATOM   2205  O   SER A 286      30.498  37.129  35.963  1.00 75.17           O  
ANISOU 2205  O   SER A 286    11725   8580   8254   -140    235   -426       O  
ATOM   2206  CB  SER A 286      30.825  36.972  32.674  1.00 74.09           C  
ANISOU 2206  CB  SER A 286    11761   8253   8139    127    165   -356       C  
ATOM   2207  OG  SER A 286      30.022  37.180  31.523  1.00 78.92           O  
ANISOU 2207  OG  SER A 286    12440   8785   8762    272    125   -369       O  
ATOM   2208  N   HIS A 287      32.487  37.765  35.124  1.00 66.49           N  
ANISOU 2208  N   HIS A 287    10737   7440   7085   -215    290   -359       N  
ATOM   2209  CA  HIS A 287      33.224  37.595  36.363  1.00 67.91           C  
ANISOU 2209  CA  HIS A 287    10831   7752   7220   -390    312   -334       C  
ATOM   2210  C   HIS A 287      32.537  38.331  37.502  1.00 68.86           C  
ANISOU 2210  C   HIS A 287    10968   7886   7311   -473    363   -422       C  
ATOM   2211  O   HIS A 287      32.264  37.739  38.546  1.00 72.45           O  
ANISOU 2211  O   HIS A 287    11314   8448   7764   -547    343   -420       O  
ATOM   2212  CB  HIS A 287      34.645  38.135  36.197  1.00 70.84           C  
ANISOU 2212  CB  HIS A 287    11246   8143   7527   -501    361   -289       C  
ATOM   2213  CG  HIS A 287      35.536  37.880  37.368  1.00 71.83           C  
ANISOU 2213  CG  HIS A 287    11260   8438   7593   -690    368   -238       C  
ATOM   2214  CD2 HIS A 287      35.934  38.687  38.381  1.00 67.89           C  
ANISOU 2214  CD2 HIS A 287    10780   8009   7007   -877    423   -279       C  
ATOM   2215  ND1 HIS A 287      36.144  36.658  37.581  1.00 71.82           N  
ANISOU 2215  ND1 HIS A 287    11110   8564   7613   -704    318   -123       N  
ATOM   2216  CE1 HIS A 287      36.865  36.721  38.687  1.00 74.14           C  
ANISOU 2216  CE1 HIS A 287    11317   9016   7835   -885    330    -83       C  
ATOM   2217  NE2 HIS A 287      36.761  37.942  39.187  1.00 71.53           N  
ANISOU 2217  NE2 HIS A 287    11089   8659   7432  -1005    389   -182       N  
ATOM   2218  N   CYS A 288      32.248  39.615  37.285  1.00 68.88           N  
ANISOU 2218  N   CYS A 288    11115   7767   7291   -454    442   -498       N  
ATOM   2219  CA  CYS A 288      31.642  40.474  38.301  1.00 66.72           C  
ANISOU 2219  CA  CYS A 288    10893   7472   6984   -529    525   -590       C  
ATOM   2220  C   CYS A 288      30.315  39.910  38.764  1.00 67.91           C  
ANISOU 2220  C   CYS A 288    10956   7648   7198   -442    489   -619       C  
ATOM   2221  O   CYS A 288      30.033  39.904  39.965  1.00 65.09           O  
ANISOU 2221  O   CYS A 288    10554   7364   6814   -551    522   -661       O  
ATOM   2222  CB  CYS A 288      31.417  41.877  37.760  1.00 69.22           C  
ANISOU 2222  CB  CYS A 288    11396   7617   7288   -471    629   -655       C  
ATOM   2223  SG  CYS A 288      30.703  43.056  38.944  1.00 75.76           S  
ANISOU 2223  SG  CYS A 288    12329   8378   8077   -556    776   -776       S  
ATOM   2224  N   ILE A 289      29.494  39.437  37.825  1.00 66.58           N  
ANISOU 2224  N   ILE A 289    10762   7428   7106   -257    422   -598       N  
ATOM   2225  CA  ILE A 289      28.215  38.827  38.200  1.00 67.51           C  
ANISOU 2225  CA  ILE A 289    10780   7586   7286   -179    379   -618       C  
ATOM   2226  C   ILE A 289      28.469  37.571  39.040  1.00 68.61           C  
ANISOU 2226  C   ILE A 289    10770   7875   7425   -285    317   -576       C  
ATOM   2227  O   ILE A 289      27.855  37.383  40.098  1.00 65.97           O  
ANISOU 2227  O   ILE A 289    10367   7606   7092   -342    333   -611       O  
ATOM   2228  CB  ILE A 289      27.368  38.416  36.978  1.00 68.08           C  
ANISOU 2228  CB  ILE A 289    10835   7608   7425     12    300   -592       C  
ATOM   2229  CG1 ILE A 289      26.843  39.648  36.225  1.00 65.43           C  
ANISOU 2229  CG1 ILE A 289    10628   7136   7097    146    360   -619       C  
ATOM   2230  CG2 ILE A 289      26.216  37.507  37.422  1.00 66.80           C  
ANISOU 2230  CG2 ILE A 289    10536   7526   7319     52    238   -600       C  
ATOM   2231  CD1 ILE A 289      26.388  39.357  34.811  1.00 59.50           C  
ANISOU 2231  CD1 ILE A 289     9882   6345   6379    310    275   -573       C  
ATOM   2232  N   ALA A 290      29.379  36.720  38.560  1.00 67.38           N  
ANISOU 2232  N   ALA A 290    10567   7765   7267   -303    257   -494       N  
ATOM   2233  CA  ALA A 290      29.698  35.469  39.253  1.00 67.37           C  
ANISOU 2233  CA  ALA A 290    10429   7895   7273   -382    208   -430       C  
ATOM   2234  C   ALA A 290      30.188  35.661  40.674  1.00 67.37           C  
ANISOU 2234  C   ALA A 290    10383   8011   7204   -563    251   -433       C  
ATOM   2235  O   ALA A 290      30.052  34.755  41.463  1.00 73.63           O  
ANISOU 2235  O   ALA A 290    11061   8910   8005   -617    220   -395       O  
ATOM   2236  CB  ALA A 290      30.707  34.632  38.476  1.00 64.66           C  
ANISOU 2236  CB  ALA A 290    10060   7568   6941   -362    166   -331       C  
ATOM   2237  N   GLU A 291      30.756  36.813  41.007  1.00 68.72           N  
ANISOU 2237  N   GLU A 291    10648   8165   7300   -669    326   -476       N  
ATOM   2238  CA  GLU A 291      31.247  37.041  42.363  1.00 72.14           C  
ANISOU 2238  CA  GLU A 291    11045   8721   7643   -871    367   -485       C  
ATOM   2239  C   GLU A 291      30.499  38.181  43.034  1.00 70.67           C  
ANISOU 2239  C   GLU A 291    10963   8468   7420   -920    465   -611       C  
ATOM   2240  O   GLU A 291      31.034  38.861  43.913  1.00 71.28           O  
ANISOU 2240  O   GLU A 291    11088   8599   7396  -1105    532   -650       O  
ATOM   2241  CB  GLU A 291      32.764  37.284  42.350  1.00 76.72           C  
ANISOU 2241  CB  GLU A 291    11631   9377   8142  -1010    376   -418       C  
ATOM   2242  CG  GLU A 291      33.555  35.994  42.582  1.00 82.99           C  
ANISOU 2242  CG  GLU A 291    12263  10329   8942  -1044    301   -275       C  
ATOM   2243  CD  GLU A 291      34.997  36.054  42.078  1.00 92.38           C  
ANISOU 2243  CD  GLU A 291    13439  11571  10091  -1101    298   -178       C  
ATOM   2244  OE1 GLU A 291      35.599  37.172  42.125  1.00 99.10           O  
ANISOU 2244  OE1 GLU A 291    14384  12410  10860  -1221    356   -225       O  
ATOM   2245  OE2 GLU A 291      35.513  34.982  41.634  1.00 78.85           O1-
ANISOU 2245  OE2 GLU A 291    11625   9905   8428  -1026    250    -55       O1-
ATOM   2246  N   VAL A 292      29.246  38.376  42.642  1.00 67.94           N  
ANISOU 2246  N   VAL A 292    10652   8012   7151   -760    479   -670       N  
ATOM   2247  CA  VAL A 292      28.523  39.562  43.067  1.00 70.82           C  
ANISOU 2247  CA  VAL A 292    11135   8276   7497   -763    597   -780       C  
ATOM   2248  C   VAL A 292      28.109  39.431  44.511  1.00 74.33           C  
ANISOU 2248  C   VAL A 292    11527   8819   7898   -897    640   -828       C  
ATOM   2249  O   VAL A 292      27.971  38.315  45.015  1.00 75.63           O  
ANISOU 2249  O   VAL A 292    11547   9110   8078   -923    561   -774       O  
ATOM   2250  CB  VAL A 292      27.270  39.793  42.230  1.00 67.89           C  
ANISOU 2250  CB  VAL A 292    10792   7776   7226   -536    601   -806       C  
ATOM   2251  CG1 VAL A 292      26.268  38.678  42.461  1.00 63.86           C  
ANISOU 2251  CG1 VAL A 292    10128   7346   6789   -458    520   -783       C  
ATOM   2252  CG2 VAL A 292      26.663  41.128  42.588  1.00 72.60           C  
ANISOU 2252  CG2 VAL A 292    11528   8248   7807   -521    751   -903       C  
ATOM   2253  N   GLU A 293      27.910  40.570  45.166  1.00 75.97           N  
ANISOU 2253  N   GLU A 293    11863   8957   8045   -983    775   -929       N  
ATOM   2254  CA  GLU A 293      27.386  40.585  46.526  1.00 81.02           C  
ANISOU 2254  CA  GLU A 293    12480   9668   8636  -1105    840   -993       C  
ATOM   2255  C   GLU A 293      25.934  40.095  46.567  1.00 79.26           C  
ANISOU 2255  C   GLU A 293    12170   9423   8521   -935    827  -1006       C  
ATOM   2256  O   GLU A 293      25.120  40.455  45.726  1.00 81.01           O  
ANISOU 2256  O   GLU A 293    12427   9520   8833   -736    846  -1018       O  
ATOM   2257  CB  GLU A 293      27.490  41.998  47.129  1.00 85.44           C  
ANISOU 2257  CB  GLU A 293    13230  10130   9104  -1236   1014  -1111       C  
ATOM   2258  CG  GLU A 293      27.258  42.061  48.636  1.00 88.78           C  
ANISOU 2258  CG  GLU A 293    13651  10646   9435  -1427   1091  -1182       C  
ATOM   2259  CD  GLU A 293      27.396  43.467  49.213  1.00 90.88           C  
ANISOU 2259  CD  GLU A 293    14132  10800   9598  -1576   1283  -1311       C  
ATOM   2260  OE1 GLU A 293      27.418  44.439  48.426  1.00 89.52           O  
ANISOU 2260  OE1 GLU A 293    14114  10447   9453  -1486   1374  -1349       O  
ATOM   2261  OE2 GLU A 293      27.465  43.593  50.459  1.00 87.86           O1-
ANISOU 2261  OE2 GLU A 293    13773  10506   9103  -1786   1350  -1376       O1-
ATOM   2262  N   LYS A 294      25.623  39.294  47.574  1.00 80.79           N  
ANISOU 2262  N   LYS A 294    12246   9751   8698  -1021    796   -997       N  
ATOM   2263  CA  LYS A 294      24.292  38.748  47.745  1.00 80.59           C  
ANISOU 2263  CA  LYS A 294    12123   9733   8766   -893    783  -1007       C  
ATOM   2264  C   LYS A 294      23.323  39.883  48.030  1.00 83.43           C  
ANISOU 2264  C   LYS A 294    12594   9963   9145   -826    942  -1111       C  
ATOM   2265  O   LYS A 294      23.661  40.816  48.754  1.00 87.80           O  
ANISOU 2265  O   LYS A 294    13280  10475   9604   -967   1074  -1191       O  
ATOM   2266  CB  LYS A 294      24.280  37.730  48.884  1.00 80.13           C  
ANISOU 2266  CB  LYS A 294    11934   9844   8669  -1028    736   -977       C  
ATOM   2267  CG  LYS A 294      25.382  36.684  48.737  1.00 82.74           C  
ANISOU 2267  CG  LYS A 294    12165  10302   8969  -1105    608   -860       C  
ATOM   2268  CD  LYS A 294      25.300  35.539  49.740  1.00 82.08           C  
ANISOU 2268  CD  LYS A 294    11940  10382   8865  -1203    554   -803       C  
ATOM   2269  CE  LYS A 294      26.514  34.615  49.635  1.00 79.86           C  
ANISOU 2269  CE  LYS A 294    11572  10222   8551  -1274    452   -670       C  
ATOM   2270  N   ASP A 295      22.132  39.811  47.435  1.00 84.21           N  
ANISOU 2270  N   ASP A 295    12640   9998   9360   -614    935  -1105       N  
ATOM   2271  CA  ASP A 295      21.082  40.810  47.634  1.00 82.59           C  
ANISOU 2271  CA  ASP A 295    12514   9672   9197   -505   1091  -1178       C  
ATOM   2272  C   ASP A 295      20.458  40.601  49.011  1.00 82.50           C  
ANISOU 2272  C   ASP A 295    12452   9737   9156   -610   1170  -1236       C  
ATOM   2273  O   ASP A 295      20.636  39.552  49.632  1.00 79.05           O  
ANISOU 2273  O   ASP A 295    11893   9451   8690   -725   1077  -1203       O  
ATOM   2274  CB  ASP A 295      20.008  40.682  46.542  1.00 85.98           C  
ANISOU 2274  CB  ASP A 295    12863  10050   9757   -244   1038  -1126       C  
ATOM   2275  CG  ASP A 295      19.256  41.981  46.276  1.00 90.88           C  
ANISOU 2275  CG  ASP A 295    13600  10505  10424    -83   1201  -1166       C  
ATOM   2276  OD1 ASP A 295      19.779  43.066  46.582  1.00 97.04           O  
ANISOU 2276  OD1 ASP A 295    14565  11168  11139   -159   1351  -1231       O  
ATOM   2277  OD2 ASP A 295      18.140  41.919  45.723  1.00 96.68           O1-
ANISOU 2277  OD2 ASP A 295    14243  11231  11261    120   1183  -1124       O1-
ATOM   2278  N   ALA A 296      19.736  41.607  49.488  1.00 80.31           N  
ANISOU 2278  N   ALA A 296    12278   9349   8886   -567   1353  -1318       N  
ATOM   2279  CA  ALA A 296      19.061  41.521  50.766  1.00 79.75           C  
ANISOU 2279  CA  ALA A 296    12178   9334   8791   -654   1454  -1382       C  
ATOM   2280  C   ALA A 296      17.875  40.570  50.630  1.00 83.04           C  
ANISOU 2280  C   ALA A 296    12391   9836   9325   -503   1367  -1326       C  
ATOM   2281  O   ALA A 296      17.331  40.399  49.544  1.00 82.82           O  
ANISOU 2281  O   ALA A 296    12286   9780   9403   -302   1288  -1262       O  
ATOM   2282  CB  ALA A 296      18.598  42.902  51.217  1.00 78.90           C  
ANISOU 2282  CB  ALA A 296    12252   9059   8666   -630   1699  -1484       C  
ATOM   2283  N   ILE A 297      17.477  39.970  51.748  1.00 88.42           N  
ANISOU 2283  N   ILE A 297    12988  10629   9977   -615   1385  -1351       N  
ATOM   2284  CA  ILE A 297      16.373  39.024  51.788  1.00 89.55           C  
ANISOU 2284  CA  ILE A 297    12938  10868  10218   -513   1313  -1307       C  
ATOM   2285  C   ILE A 297      15.077  39.800  51.923  1.00 94.26           C  
ANISOU 2285  C   ILE A 297    13541  11375  10899   -348   1476  -1349       C  
ATOM   2286  O   ILE A 297      14.990  40.674  52.779  1.00101.24           O  
ANISOU 2286  O   ILE A 297    14557  12183  11728   -416   1667  -1437       O  
ATOM   2287  CB  ILE A 297      16.463  38.100  53.021  1.00 90.96           C  
ANISOU 2287  CB  ILE A 297    13033  11200  10328   -706   1285  -1315       C  
ATOM   2288  CG1 ILE A 297      17.836  37.423  53.102  1.00 89.72           C  
ANISOU 2288  CG1 ILE A 297    12877  11140  10073   -885   1155  -1263       C  
ATOM   2289  CG2 ILE A 297      15.351  37.062  52.995  1.00 87.16           C  
ANISOU 2289  CG2 ILE A 297    12353  10815   9950   -610   1207  -1266       C  
ATOM   2290  CD1 ILE A 297      17.922  36.334  54.151  1.00 89.41           C  
ANISOU 2290  CD1 ILE A 297    12728  11266   9978  -1045   1099  -1232       C  
ATOM   2291  N   PRO A 298      14.059  39.472  51.111  1.00 97.47           N  
ANISOU 2291  N   PRO A 298    13802  11798  11432   -138   1408  -1284       N  
ATOM   2292  CA  PRO A 298      12.763  40.154  51.220  1.00102.01           C  
ANISOU 2292  CA  PRO A 298    14348  12313  12100     41   1560  -1298       C  
ATOM   2293  C   PRO A 298      12.258  40.211  52.678  1.00106.18           C  
ANISOU 2293  C   PRO A 298    14881  12872  12590    -72   1718  -1378       C  
ATOM   2294  O   PRO A 298      12.496  39.282  53.453  1.00103.99           O  
ANISOU 2294  O   PRO A 298    14532  12724  12254   -247   1646  -1387       O  
ATOM   2295  CB  PRO A 298      11.836  39.309  50.331  1.00101.23           C  
ANISOU 2295  CB  PRO A 298    14029  12317  12117    205   1402  -1202       C  
ATOM   2296  CG  PRO A 298      12.730  38.488  49.460  1.00100.27           C  
ANISOU 2296  CG  PRO A 298    13882  12248  11968    149   1192  -1146       C  
ATOM   2297  CD  PRO A 298      14.002  38.297  50.223  1.00 97.98           C  
ANISOU 2297  CD  PRO A 298    13704  11970  11555    -86   1190  -1193       C  
ATOM   2298  N   GLU A 299      11.561  41.291  53.030  1.00110.48           N  
ANISOU 2298  N   GLU A 299    15514  13295  13169     34   1942  -1428       N  
ATOM   2299  CA  GLU A 299      11.383  41.673  54.436  1.00112.01           C  
ANISOU 2299  CA  GLU A 299    15801  13467  13290   -106   2142  -1531       C  
ATOM   2300  C   GLU A 299      10.522  40.703  55.255  1.00110.88           C  
ANISOU 2300  C   GLU A 299    15473  13481  13177   -150   2116  -1524       C  
ATOM   2301  O   GLU A 299      10.900  40.333  56.368  1.00112.85           O  
ANISOU 2301  O   GLU A 299    15758  13803  13318   -370   2144  -1585       O  
ATOM   2302  CB  GLU A 299      10.816  43.098  54.535  1.00113.32           C  
ANISOU 2302  CB  GLU A 299    16123  13437  13496     41   2415  -1583       C  
ATOM   2303  CG  GLU A 299      11.321  43.876  55.731  1.00112.93           C  
ANISOU 2303  CG  GLU A 299    16306  13291  13312   -165   2637  -1720       C  
ATOM   2304  CD  GLU A 299      10.903  45.335  55.723  1.00117.92           C  
ANISOU 2304  CD  GLU A 299    17134  13691  13980    -22   2925  -1775       C  
ATOM   2305  OE1 GLU A 299      11.255  46.018  54.740  1.00123.47           O  
ANISOU 2305  OE1 GLU A 299    17933  14263  14717    103   2929  -1738       O  
ATOM   2306  OE2 GLU A 299      10.248  45.802  56.697  1.00111.11           O1-
ANISOU 2306  OE2 GLU A 299    16340  12767  13109    -36   3160  -1853       O1-
ATOM   2307  N   ASN A 300       9.376  40.291  54.720  1.00108.05           N  
ANISOU 2307  N   ASN A 300    14913  13186  12954     47   2062  -1446       N  
ATOM   2308  CA  ASN A 300       8.466  39.436  55.487  1.00109.47           C  
ANISOU 2308  CA  ASN A 300    14916  13508  13169     11   2058  -1441       C  
ATOM   2309  C   ASN A 300       8.115  38.157  54.753  1.00108.32           C  
ANISOU 2309  C   ASN A 300    14541  13520  13097     52   1817  -1343       C  
ATOM   2310  O   ASN A 300       7.073  38.082  54.111  1.00114.43           O  
ANISOU 2310  O   ASN A 300    15154  14334  13989    242   1790  -1275       O  
ATOM   2311  CB  ASN A 300       7.191  40.206  55.877  1.00110.63           C  
ANISOU 2311  CB  ASN A 300    15034  13594  13409    184   2286  -1457       C  
ATOM   2312  N   LEU A 301       8.981  37.146  54.867  1.00105.39           N  
ANISOU 2312  N   LEU A 301    14154  13240  12648   -132   1649  -1331       N  
ATOM   2313  CA  LEU A 301       8.749  35.852  54.221  1.00101.77           C  
ANISOU 2313  CA  LEU A 301    13508  12914  12245   -125   1434  -1249       C  
ATOM   2314  C   LEU A 301       8.109  34.818  55.133  1.00 99.88           C  
ANISOU 2314  C   LEU A 301    13124  12813  12010   -233   1422  -1251       C  
ATOM   2315  O   LEU A 301       8.510  34.671  56.292  1.00 95.07           O  
ANISOU 2315  O   LEU A 301    12584  12230  11308   -409   1494  -1302       O  
ATOM   2316  CB  LEU A 301      10.047  35.290  53.641  1.00 99.53           C  
ANISOU 2316  CB  LEU A 301    13288  12636  11895   -229   1263  -1216       C  
ATOM   2317  CG  LEU A 301      10.364  35.820  52.242  1.00100.20           C  
ANISOU 2317  CG  LEU A 301    13420  12632  12019    -76   1189  -1173       C  
ATOM   2318  CD1 LEU A 301      11.772  35.427  51.825  1.00 93.26           C  
ANISOU 2318  CD1 LEU A 301    12633  11741  11061   -193   1062  -1151       C  
ATOM   2319  CD2 LEU A 301       9.331  35.303  51.246  1.00 98.33           C  
ANISOU 2319  CD2 LEU A 301    12997  12467  11895     85   1076  -1099       C  
ATOM   2320  N   PRO A 302       7.115  34.082  54.600  1.00100.65           N  
ANISOU 2320  N   PRO A 302    13022  13011  12210   -141   1327  -1190       N  
ATOM   2321  CA  PRO A 302       6.517  32.962  55.331  1.00102.39           C  
ANISOU 2321  CA  PRO A 302    13097  13366  12440   -251   1295  -1183       C  
ATOM   2322  C   PRO A 302       7.553  31.908  55.686  1.00100.48           C  
ANISOU 2322  C   PRO A 302    12896  13173  12108   -454   1177  -1170       C  
ATOM   2323  O   PRO A 302       8.456  31.665  54.900  1.00101.51           O  
ANISOU 2323  O   PRO A 302    13084  13272  12214   -465   1050  -1134       O  
ATOM   2324  CB  PRO A 302       5.486  32.383  54.344  1.00102.85           C  
ANISOU 2324  CB  PRO A 302    12949  13516  12612   -123   1175  -1112       C  
ATOM   2325  CG  PRO A 302       5.777  33.009  53.019  1.00101.99           C  
ANISOU 2325  CG  PRO A 302    12885  13331  12534     31   1102  -1072       C  
ATOM   2326  CD  PRO A 302       6.454  34.317  53.302  1.00101.62           C  
ANISOU 2326  CD  PRO A 302    13042  13132  12435     67   1252  -1124       C  
ATOM   2327  N   PRO A 303       7.418  31.270  56.854  1.00104.02           N  
ANISOU 2327  N   PRO A 303    13312  13701  12509   -605   1224  -1189       N  
ATOM   2328  CA  PRO A 303       8.409  30.282  57.256  1.00106.62           C  
ANISOU 2328  CA  PRO A 303    13676  14081  12752   -785   1126  -1157       C  
ATOM   2329  C   PRO A 303       8.275  28.992  56.451  1.00110.85           C  
ANISOU 2329  C   PRO A 303    14089  14679  13351   -783    953  -1082       C  
ATOM   2330  O   PRO A 303       7.186  28.662  55.959  1.00110.86           O  
ANISOU 2330  O   PRO A 303    13946  14727  13448   -696    923  -1068       O  
ATOM   2331  CB  PRO A 303       8.073  30.038  58.724  1.00108.87           C  
ANISOU 2331  CB  PRO A 303    13950  14439  12979   -925   1243  -1193       C  
ATOM   2332  CG  PRO A 303       6.599  30.248  58.794  1.00110.08           C  
ANISOU 2332  CG  PRO A 303    13971  14620  13235   -808   1336  -1216       C  
ATOM   2333  CD  PRO A 303       6.250  31.274  57.750  1.00108.62           C  
ANISOU 2333  CD  PRO A 303    13795  14346  13131   -602   1357  -1221       C  
ATOM   2334  N   LEU A 304       9.384  28.269  56.332  1.00113.54           N  
ANISOU 2334  N   LEU A 304    14487  15021  13632   -884    850  -1033       N  
ATOM   2335  CA  LEU A 304       9.451  27.089  55.477  1.00114.44           C  
ANISOU 2335  CA  LEU A 304    14528  15160  13795   -884    702   -967       C  
ATOM   2336  C   LEU A 304       8.420  26.054  55.903  1.00113.03           C  
ANISOU 2336  C   LEU A 304    14204  15074  13668   -940    700   -955       C  
ATOM   2337  O   LEU A 304       7.737  25.471  55.058  1.00114.47           O  
ANISOU 2337  O   LEU A 304    14285  15281  13928   -889    619   -936       O  
ATOM   2338  CB  LEU A 304      10.865  26.493  55.499  1.00117.38           C  
ANISOU 2338  CB  LEU A 304    14992  15516  14091   -986    630   -906       C  
ATOM   2339  N   THR A 305       8.288  25.860  57.215  1.00113.19           N  
ANISOU 2339  N   THR A 305    14219  15151  13637  -1055    794   -968       N  
ATOM   2340  CA  THR A 305       7.369  24.858  57.763  1.00114.32           C  
ANISOU 2340  CA  THR A 305    14235  15382  13818  -1129    807   -956       C  
ATOM   2341  C   THR A 305       5.979  24.949  57.120  1.00114.25           C  
ANISOU 2341  C   THR A 305    14077  15413  13921  -1019    802   -980       C  
ATOM   2342  O   THR A 305       5.349  23.925  56.868  1.00114.26           O  
ANISOU 2342  O   THR A 305    13967  15472  13973  -1063    742   -954       O  
ATOM   2343  CB  THR A 305       7.241  24.966  59.303  1.00113.96           C  
ANISOU 2343  CB  THR A 305    14206  15393  13699  -1245    940   -982       C  
ATOM   2344  CG2 THR A 305       8.574  24.661  59.998  1.00109.66           C  
ANISOU 2344  CG2 THR A 305    13778  14853  13033  -1380    925   -934       C  
ATOM   2345  OG1 THR A 305       6.815  26.284  59.661  1.00118.02           O  
ANISOU 2345  OG1 THR A 305    14756  15880  14208  -1172   1071  -1059       O  
ATOM   2346  N   ALA A 306       5.525  26.168  56.833  1.00115.31           N  
ANISOU 2346  N   ALA A 306    14209  15515  14089   -879    868  -1021       N  
ATOM   2347  CA  ALA A 306       4.202  26.399  56.238  1.00118.54           C  
ANISOU 2347  CA  ALA A 306    14459  15980  14601   -754    870  -1025       C  
ATOM   2348  C   ALA A 306       3.953  25.540  54.992  1.00119.86           C  
ANISOU 2348  C   ALA A 306    14535  16185  14822   -739    705   -980       C  
ATOM   2349  O   ALA A 306       2.943  24.830  54.906  1.00120.50           O  
ANISOU 2349  O   ALA A 306    14459  16367  14958   -771    676   -968       O  
ATOM   2350  CB  ALA A 306       4.020  27.877  55.910  1.00114.85           C  
ANISOU 2350  CB  ALA A 306    14033  15447  14159   -580    957  -1052       C  
ATOM   2351  N   ASP A 307       4.887  25.589  54.045  1.00118.00           N  
ANISOU 2351  N   ASP A 307    14403  15870  14561   -706    603   -958       N  
ATOM   2352  CA  ASP A 307       4.710  24.944  52.747  1.00117.03           C  
ANISOU 2352  CA  ASP A 307    14223  15769  14476   -684    455   -925       C  
ATOM   2353  C   ASP A 307       5.316  23.526  52.664  1.00111.23           C  
ANISOU 2353  C   ASP A 307    13529  15021  13710   -837    372   -898       C  
ATOM   2354  O   ASP A 307       4.916  22.741  51.807  1.00112.24           O  
ANISOU 2354  O   ASP A 307    13594  15184  13867   -866    273   -884       O  
ATOM   2355  CB  ASP A 307       5.282  25.847  51.635  1.00116.61           C  
ANISOU 2355  CB  ASP A 307    14257  15632  14417   -544    399   -915       C  
ATOM   2356  CG  ASP A 307       4.399  27.076  51.337  1.00117.50           C  
ANISOU 2356  CG  ASP A 307    14292  15767  14584   -365    459   -918       C  
ATOM   2357  OD1 ASP A 307       4.846  27.952  50.574  1.00110.28           O  
ANISOU 2357  OD1 ASP A 307    13461  14776  13665   -242    442   -908       O  
ATOM   2358  OD2 ASP A 307       3.263  27.182  51.847  1.00117.44           O1-
ANISOU 2358  OD2 ASP A 307    14140  15852  14629   -338    532   -923       O1-
ATOM   2359  N   PHE A 308       6.247  23.184  53.550  1.00103.16           N  
ANISOU 2359  N   PHE A 308    12614  13955  12627   -936    419   -885       N  
ATOM   2360  CA  PHE A 308       6.964  21.903  53.443  1.00100.54           C  
ANISOU 2360  CA  PHE A 308    12339  13590  12270  -1053    358   -839       C  
ATOM   2361  C   PHE A 308       6.846  20.934  54.626  1.00104.42           C  
ANISOU 2361  C   PHE A 308    12804  14127  12742  -1198    421   -817       C  
ATOM   2362  O   PHE A 308       7.534  19.906  54.624  1.00 98.06           O  
ANISOU 2362  O   PHE A 308    12061  13281  11916  -1283    391   -764       O  
ATOM   2363  CB  PHE A 308       8.440  22.185  53.198  1.00100.10           C  
ANISOU 2363  CB  PHE A 308    12440  13438  12156  -1033    332   -806       C  
ATOM   2364  CG  PHE A 308       8.681  23.074  52.031  1.00 97.91           C  
ANISOU 2364  CG  PHE A 308    12208  13104  11891   -900    274   -821       C  
ATOM   2365  CD1 PHE A 308       8.580  22.585  50.740  1.00 96.39           C  
ANISOU 2365  CD1 PHE A 308    12007  12888  11728   -869    169   -810       C  
ATOM   2366  CD2 PHE A 308       8.984  24.411  52.223  1.00 99.75           C  
ANISOU 2366  CD2 PHE A 308    12500  13302  12096   -813    332   -849       C  
ATOM   2367  CE1 PHE A 308       8.782  23.413  49.652  1.00 97.31           C  
ANISOU 2367  CE1 PHE A 308    12166  12958  11848   -745    114   -817       C  
ATOM   2368  CE2 PHE A 308       9.191  25.246  51.144  1.00 99.97           C  
ANISOU 2368  CE2 PHE A 308    12576  13272  12137   -686    286   -856       C  
ATOM   2369  CZ  PHE A 308       9.088  24.747  49.854  1.00 98.99           C  
ANISOU 2369  CZ  PHE A 308    12434  13134  12042   -647    173   -836       C  
ATOM   2370  N   ALA A 309       5.999  21.241  55.621  1.00109.51           N  
ANISOU 2370  N   ALA A 309    13364  14850  13395  -1222    517   -850       N  
ATOM   2371  CA  ALA A 309       5.808  20.358  56.800  1.00108.64           C  
ANISOU 2371  CA  ALA A 309    13227  14791  13262  -1362    585   -828       C  
ATOM   2372  C   ALA A 309       4.394  20.397  57.415  1.00108.28           C  
ANISOU 2372  C   ALA A 309    13030  14847  13263  -1383    663   -871       C  
ATOM   2373  O   ALA A 309       3.775  19.356  57.637  1.00108.11           O  
ANISOU 2373  O   ALA A 309    12932  14877  13270  -1486    664   -858       O  
ATOM   2374  CB  ALA A 309       6.836  20.690  57.873  1.00106.44           C  
ANISOU 2374  CB  ALA A 309    13060  14494  12889  -1413    653   -803       C  
ATOM   2375  N   GLU A 310       3.902  21.596  57.710  1.00108.20           N  
ANISOU 2375  N   GLU A 310    12985  14863  13262  -1287    741   -919       N  
ATOM   2376  CA  GLU A 310       2.551  21.777  58.260  1.00109.25           C  
ANISOU 2376  CA  GLU A 310    12966  15094  13448  -1279    832   -954       C  
ATOM   2377  C   GLU A 310       1.447  21.578  57.203  1.00109.73           C  
ANISOU 2377  C   GLU A 310    12863  15228  13601  -1218    753   -954       C  
ATOM   2378  O   GLU A 310       0.343  21.172  57.535  1.00110.16           O  
ANISOU 2378  O   GLU A 310    12767  15386  13703  -1264    792   -961       O  
ATOM   2379  CB  GLU A 310       2.411  23.159  58.918  1.00105.78           C  
ANISOU 2379  CB  GLU A 310    12558  14642  12990  -1185    966  -1002       C  
ATOM   2380  N   ASP A 311       1.751  21.847  55.938  1.00114.54           N  
ANISOU 2380  N   ASP A 311    13496  15796  14228  -1125    641   -943       N  
ATOM   2381  CA  ASP A 311       0.758  21.733  54.867  1.00120.85           C  
ANISOU 2381  CA  ASP A 311    14140  16682  15095  -1071    553   -936       C  
ATOM   2382  C   ASP A 311       0.332  20.280  54.676  1.00124.42           C  
ANISOU 2382  C   ASP A 311    14523  17194  15558  -1237    484   -925       C  
ATOM   2383  O   ASP A 311       1.166  19.374  54.734  1.00119.83           O  
ANISOU 2383  O   ASP A 311    14064  16532  14934  -1349    454   -911       O  
ATOM   2384  CB  ASP A 311       1.310  22.285  53.542  1.00122.80           C  
ANISOU 2384  CB  ASP A 311    14454  16866  15339   -951    443   -921       C  
ATOM   2385  CG  ASP A 311       0.209  22.660  52.558  1.00123.23           C  
ANISOU 2385  CG  ASP A 311    14334  17033  15455   -847    376   -905       C  
ATOM   2386  OD1 ASP A 311      -0.468  23.688  52.791  1.00121.82           O  
ANISOU 2386  OD1 ASP A 311    14064  16903  15320   -708    459   -900       O  
ATOM   2387  OD2 ASP A 311       0.030  21.935  51.554  1.00121.47           O1-
ANISOU 2387  OD2 ASP A 311    14069  16853  15231   -905    246   -892       O1-
ATOM   2388  N   LYS A 312      -0.959  20.083  54.404  1.00129.12           N  
ANISOU 2388  N   LYS A 312    14922  17929  16210  -1250    465   -927       N  
ATOM   2389  CA  LYS A 312      -1.575  18.753  54.374  1.00130.19           C  
ANISOU 2389  CA  LYS A 312    14974  18139  16355  -1431    427   -929       C  
ATOM   2390  C   LYS A 312      -1.605  18.081  52.995  1.00129.38           C  
ANISOU 2390  C   LYS A 312    14865  18047  16244  -1489    276   -926       C  
ATOM   2391  O   LYS A 312      -2.118  16.969  52.876  1.00127.67           O  
ANISOU 2391  O   LYS A 312    14595  17885  16030  -1656    247   -937       O  
ATOM   2392  CB  LYS A 312      -3.007  18.845  54.906  1.00135.09           C  
ANISOU 2392  CB  LYS A 312    15369  18926  17033  -1444    495   -933       C  
ATOM   2393  N   ASP A 313      -1.050  18.739  51.973  1.00128.37           N  
ANISOU 2393  N   ASP A 313    14807  17866  16102  -1365    191   -917       N  
ATOM   2394  CA  ASP A 313      -1.049  18.227  50.592  1.00127.17           C  
ANISOU 2394  CA  ASP A 313    14664  17726  15929  -1413     49   -918       C  
ATOM   2395  C   ASP A 313       0.375  18.018  50.057  1.00122.71           C  
ANISOU 2395  C   ASP A 313    14330  16981  15313  -1405      7   -915       C  
ATOM   2396  O   ASP A 313       0.596  17.994  48.838  1.00125.91           O  
ANISOU 2396  O   ASP A 313    14778  17370  15694  -1386   -101   -916       O  
ATOM   2397  CB  ASP A 313      -1.792  19.209  49.670  1.00129.49           C  
ANISOU 2397  CB  ASP A 313    14808  18144  16247  -1263    -28   -895       C  
ATOM   2398  CG  ASP A 313      -3.298  19.225  49.904  1.00134.41           C  
ANISOU 2398  CG  ASP A 313    15170  18979  16922  -1285    -15   -881       C  
ATOM   2399  OD1 ASP A 313      -3.824  18.328  50.594  1.00134.54           O  
ANISOU 2399  OD1 ASP A 313    15121  19051  16948  -1448     33   -901       O  
ATOM   2400  OD2 ASP A 313      -3.966  20.143  49.380  1.00136.45           O1-
ANISOU 2400  OD2 ASP A 313    15280  19353  17211  -1133    -49   -839       O1-
ATOM   2401  N   VAL A 314       1.332  17.836  50.964  1.00111.77           N  
ANISOU 2401  N   VAL A 314    13088  15474  13908  -1426     93   -906       N  
ATOM   2402  CA  VAL A 314       2.748  17.802  50.596  1.00107.23           C  
ANISOU 2402  CA  VAL A 314    12714  14738  13289  -1393     71   -887       C  
ATOM   2403  C   VAL A 314       3.128  16.616  49.689  1.00107.34           C  
ANISOU 2403  C   VAL A 314    12827  14679  13279  -1511      3   -889       C  
ATOM   2404  O   VAL A 314       3.746  16.810  48.645  1.00105.66           O  
ANISOU 2404  O   VAL A 314    12707  14397  13041  -1452    -71   -887       O  
ATOM   2405  CB  VAL A 314       3.620  17.864  51.864  1.00102.76           C  
ANISOU 2405  CB  VAL A 314    12250  14093  12699  -1400    178   -861       C  
ATOM   2406  CG1 VAL A 314       5.084  17.644  51.543  1.00 99.67           C  
ANISOU 2406  CG1 VAL A 314    12047  13557  12265  -1386    158   -824       C  
ATOM   2407  CG2 VAL A 314       3.428  19.205  52.553  1.00102.17           C  
ANISOU 2407  CG2 VAL A 314    12127  14061  12632  -1275    249   -873       C  
ATOM   2408  N   CYS A 315       2.741  15.402  50.067  1.00113.79           N  
ANISOU 2408  N   CYS A 315    13631  15504  14102  -1680     38   -896       N  
ATOM   2409  CA  CYS A 315       2.988  14.219  49.227  1.00117.08           C  
ANISOU 2409  CA  CYS A 315    14151  15838  14494  -1809     -1   -909       C  
ATOM   2410  C   CYS A 315       2.316  14.376  47.868  1.00119.41           C  
ANISOU 2410  C   CYS A 315    14378  16219  14775  -1818   -123   -950       C  
ATOM   2411  O   CYS A 315       2.913  14.071  46.839  1.00114.31           O  
ANISOU 2411  O   CYS A 315    13859  15483  14092  -1830   -178   -959       O  
ATOM   2412  CB  CYS A 315       2.486  12.924  49.894  1.00121.16           C  
ANISOU 2412  CB  CYS A 315    14656  16358  15024  -2001     72   -915       C  
ATOM   2413  SG  CYS A 315       3.407  12.365  51.358  1.00127.96           S  
ANISOU 2413  SG  CYS A 315    15631  17102  15885  -2025    212   -845       S  
ATOM   2414  N   LYS A 316       1.066  14.839  47.878  1.00125.36           N  
ANISOU 2414  N   LYS A 316    14924  17157  15552  -1813   -160   -967       N  
ATOM   2415  CA  LYS A 316       0.311  15.067  46.647  1.00127.63           C  
ANISOU 2415  CA  LYS A 316    15106  17570  15816  -1819   -286   -988       C  
ATOM   2416  C   LYS A 316       1.108  15.920  45.661  1.00127.99           C  
ANISOU 2416  C   LYS A 316    15252  17547  15832  -1660   -360   -971       C  
ATOM   2417  O   LYS A 316       1.301  15.534  44.503  1.00130.19           O  
ANISOU 2417  O   LYS A 316    15608  17800  16059  -1718   -445   -992       O  
ATOM   2418  N   ASN A 317       1.576  17.072  46.137  1.00122.99           N  
ANISOU 2418  N   ASN A 317    14627  16878  15225  -1471   -319   -937       N  
ATOM   2419  CA  ASN A 317       2.341  18.003  45.302  1.00120.14           C  
ANISOU 2419  CA  ASN A 317    14360  16448  14840  -1309   -374   -917       C  
ATOM   2420  C   ASN A 317       3.705  17.424  44.917  1.00114.18           C  
ANISOU 2420  C   ASN A 317    13838  15502  14045  -1343   -366   -918       C  
ATOM   2421  O   ASN A 317       4.157  17.568  43.777  1.00107.20           O  
ANISOU 2421  O   ASN A 317    13041  14570  13120  -1305   -443   -920       O  
ATOM   2422  CB  ASN A 317       2.524  19.348  46.022  1.00123.72           C  
ANISOU 2422  CB  ASN A 317    14785  16894  15330  -1120   -305   -888       C  
ATOM   2423  CG  ASN A 317       1.196  20.008  46.406  1.00127.31           C  
ANISOU 2423  CG  ASN A 317    15012  17525  15834  -1054   -288   -876       C  
ATOM   2424  ND2 ASN A 317       1.178  20.671  47.560  1.00127.99           N  
ANISOU 2424  ND2 ASN A 317    15075  17599  15958   -976   -170   -870       N  
ATOM   2425  OD1 ASN A 317       0.206  19.926  45.679  1.00126.40           O  
ANISOU 2425  OD1 ASN A 317    14744  17562  15719  -1077   -375   -867       O  
ATOM   2426  N   TYR A 318       4.346  16.763  45.880  1.00108.01           N  
ANISOU 2426  N   TYR A 318    13149  14617  13275  -1411   -268   -908       N  
ATOM   2427  CA  TYR A 318       5.642  16.124  45.660  1.00105.89           C  
ANISOU 2427  CA  TYR A 318    13084  14171  12979  -1437   -238   -889       C  
ATOM   2428  C   TYR A 318       5.541  14.996  44.636  1.00111.07           C  
ANISOU 2428  C   TYR A 318    13817  14783  13601  -1579   -282   -923       C  
ATOM   2429  O   TYR A 318       6.366  14.903  43.726  1.00107.52           O  
ANISOU 2429  O   TYR A 318    13512  14224  13117  -1550   -311   -920       O  
ATOM   2430  CB  TYR A 318       6.214  15.607  46.989  1.00101.73           C  
ANISOU 2430  CB  TYR A 318    12609  13573  12470  -1482   -122   -850       C  
ATOM   2431  CG  TYR A 318       7.368  14.636  46.863  1.00 97.82           C  
ANISOU 2431  CG  TYR A 318    12296  12913  11958  -1533    -73   -811       C  
ATOM   2432  CD1 TYR A 318       8.624  15.056  46.439  1.00 98.61           C  
ANISOU 2432  CD1 TYR A 318    12527  12904  12037  -1426    -79   -770       C  
ATOM   2433  CD2 TYR A 318       7.205  13.298  47.191  1.00 99.22           C  
ANISOU 2433  CD2 TYR A 318    12514  13041  12144  -1685     -9   -806       C  
ATOM   2434  CE1 TYR A 318       9.688  14.165  46.339  1.00100.16           C  
ANISOU 2434  CE1 TYR A 318    12878  12954  12226  -1456    -21   -718       C  
ATOM   2435  CE2 TYR A 318       8.255  12.399  47.092  1.00101.37           C  
ANISOU 2435  CE2 TYR A 318    12954  13151  12410  -1713     57   -755       C  
ATOM   2436  CZ  TYR A 318       9.495  12.834  46.667  1.00102.97           C  
ANISOU 2436  CZ  TYR A 318    13272  13256  12596  -1592     51   -707       C  
ATOM   2437  OH  TYR A 318      10.528  11.924  46.570  1.00105.11           O  
ANISOU 2437  OH  TYR A 318    13698  13371  12869  -1606    129   -641       O  
ATOM   2438  N   GLN A 319       4.527  14.145  44.791  1.00113.34           N  
ANISOU 2438  N   GLN A 319    14016  15154  13894  -1742   -279   -960       N  
ATOM   2439  CA  GLN A 319       4.302  13.034  43.868  1.00112.01           C  
ANISOU 2439  CA  GLN A 319    13925  14950  13682  -1913   -308  -1008       C  
ATOM   2440  C   GLN A 319       4.099  13.516  42.427  1.00113.20           C  
ANISOU 2440  C   GLN A 319    14071  15162  13776  -1884   -437  -1038       C  
ATOM   2441  O   GLN A 319       4.515  12.843  41.480  1.00107.72           O  
ANISOU 2441  O   GLN A 319    13528  14372  13030  -1970   -452  -1070       O  
ATOM   2442  CB  GLN A 319       3.090  12.204  44.314  1.00113.49           C  
ANISOU 2442  CB  GLN A 319    13988  15253  13881  -2104   -289  -1047       C  
ATOM   2443  N   GLU A 320       3.465  14.679  42.273  1.00116.24           N  
ANISOU 2443  N   GLU A 320    14292  15705  14170  -1759   -518  -1022       N  
ATOM   2444  CA  GLU A 320       3.069  15.196  40.961  1.00117.26           C  
ANISOU 2444  CA  GLU A 320    14375  15936  14241  -1728   -650  -1034       C  
ATOM   2445  C   GLU A 320       4.112  16.065  40.259  1.00120.38           C  
ANISOU 2445  C   GLU A 320    14899  16226  14614  -1551   -681  -1004       C  
ATOM   2446  O   GLU A 320       3.948  16.386  39.083  1.00127.34           O  
ANISOU 2446  O   GLU A 320    15782  17166  15435  -1534   -786  -1010       O  
ATOM   2447  CB  GLU A 320       1.739  15.929  41.090  1.00118.94           C  
ANISOU 2447  CB  GLU A 320    14327  16389  14477  -1684   -719  -1015       C  
ATOM   2448  CG  GLU A 320       0.604  14.944  41.330  1.00125.72           C  
ANISOU 2448  CG  GLU A 320    15055  17383  15328  -1904   -724  -1054       C  
ATOM   2449  CD  GLU A 320      -0.656  15.586  41.864  1.00129.30           C  
ANISOU 2449  CD  GLU A 320    15234  18064  15831  -1853   -746  -1020       C  
ATOM   2450  OE1 GLU A 320      -1.195  15.073  42.867  1.00127.50           O  
ANISOU 2450  OE1 GLU A 320    14920  17876  15648  -1949   -668  -1032       O  
ATOM   2451  OE2 GLU A 320      -1.105  16.597  41.285  1.00137.40           O1-
ANISOU 2451  OE2 GLU A 320    16128  19225  16851  -1710   -833   -974       O1-
ATOM   2452  N   ALA A 321       5.188  16.428  40.956  1.00117.07           N  
ANISOU 2452  N   ALA A 321    14587  15660  14234  -1433   -592   -968       N  
ATOM   2453  CA  ALA A 321       6.286  17.183  40.333  1.00110.21           C  
ANISOU 2453  CA  ALA A 321    13854  14678  13343  -1283   -608   -940       C  
ATOM   2454  C   ALA A 321       7.574  17.076  41.165  1.00 99.24           C  
ANISOU 2454  C   ALA A 321    12603  13118  11984  -1233   -496   -905       C  
ATOM   2455  O   ALA A 321       8.131  18.077  41.584  1.00 91.27           O  
ANISOU 2455  O   ALA A 321    11600  12083  10994  -1088   -470   -869       O  
ATOM   2456  CB  ALA A 321       5.880  18.643  40.138  1.00111.60           C  
ANISOU 2456  CB  ALA A 321    13910  14962  13530  -1103   -667   -908       C  
ATOM   2457  N   LYS A 322       8.046  15.850  41.369  1.00 95.20           N  
ANISOU 2457  N   LYS A 322    12205  12495  11471  -1358   -425   -910       N  
ATOM   2458  CA  LYS A 322       9.091  15.567  42.351  1.00 93.03           C  
ANISOU 2458  CA  LYS A 322    12021  12097  11229  -1331   -314   -855       C  
ATOM   2459  C   LYS A 322      10.235  16.556  42.281  1.00 93.62           C  
ANISOU 2459  C   LYS A 322    12173  12100  11298  -1169   -309   -808       C  
ATOM   2460  O   LYS A 322      10.603  17.154  43.290  1.00 93.35           O  
ANISOU 2460  O   LYS A 322    12104  12077  11287  -1101   -259   -769       O  
ATOM   2461  CB  LYS A 322       9.630  14.136  42.187  1.00 88.70           C  
ANISOU 2461  CB  LYS A 322    11622  11406  10674  -1456   -239   -851       C  
ATOM   2462  N   ASP A 323      10.778  16.752  41.085  1.00 97.30           N  
ANISOU 2462  N   ASP A 323    12745  12499  11726  -1120   -358   -815       N  
ATOM   2463  CA  ASP A 323      11.998  17.550  40.923  1.00 96.80           C  
ANISOU 2463  CA  ASP A 323    12777  12350  11654   -985   -344   -767       C  
ATOM   2464  C   ASP A 323      11.746  19.051  41.061  1.00 91.28           C  
ANISOU 2464  C   ASP A 323    11990  11735  10957   -851   -387   -767       C  
ATOM   2465  O   ASP A 323      12.546  19.760  41.664  1.00 90.47           O  
ANISOU 2465  O   ASP A 323    11917  11595  10862   -769   -340   -728       O  
ATOM   2466  CB  ASP A 323      12.674  17.210  39.602  1.00101.31           C  
ANISOU 2466  CB  ASP A 323    13500  12813  12181   -982   -367   -774       C  
ATOM   2467  CG  ASP A 323      13.157  15.762  39.560  1.00107.40           C  
ANISOU 2467  CG  ASP A 323    14393  13459  12957  -1093   -282   -763       C  
ATOM   2468  OD1 ASP A 323      14.386  15.545  39.574  1.00106.73           O  
ANISOU 2468  OD1 ASP A 323    14425  13249  12880  -1041   -210   -701       O  
ATOM   2469  OD2 ASP A 323      12.311  14.835  39.543  1.00114.26           O1-
ANISOU 2469  OD2 ASP A 323    15238  14353  13824  -1233   -277   -810       O1-
ATOM   2470  N   ALA A 324      10.622  19.525  40.529  1.00 90.41           N  
ANISOU 2470  N   ALA A 324    11770  11742  10840   -833   -468   -804       N  
ATOM   2471  CA  ALA A 324      10.205  20.925  40.719  1.00 87.80           C  
ANISOU 2471  CA  ALA A 324    11346  11490  10524   -697   -488   -797       C  
ATOM   2472  C   ALA A 324       9.975  21.260  42.203  1.00 85.74           C  
ANISOU 2472  C   ALA A 324    10999  11272  10308   -690   -403   -788       C  
ATOM   2473  O   ALA A 324      10.416  22.290  42.704  1.00 81.86           O  
ANISOU 2473  O   ALA A 324    10526  10757   9822   -590   -357   -772       O  
ATOM   2474  CB  ALA A 324       8.953  21.222  39.910  1.00 84.80           C  
ANISOU 2474  CB  ALA A 324    10840  11247  10131   -681   -586   -817       C  
ATOM   2475  N   PHE A 325       9.262  20.381  42.894  1.00 86.31           N  
ANISOU 2475  N   PHE A 325    10985  11406  10404   -808   -377   -804       N  
ATOM   2476  CA  PHE A 325       8.981  20.563  44.315  1.00 86.54           C  
ANISOU 2476  CA  PHE A 325    10934  11482  10467   -823   -292   -799       C  
ATOM   2477  C   PHE A 325      10.266  20.590  45.147  1.00 80.51           C  
ANISOU 2477  C   PHE A 325    10283  10618   9689   -821   -211   -760       C  
ATOM   2478  O   PHE A 325      10.409  21.420  46.024  1.00 76.33           O  
ANISOU 2478  O   PHE A 325     9736  10107   9161   -771   -152   -755       O  
ATOM   2479  CB  PHE A 325       8.052  19.450  44.801  1.00 90.12           C  
ANISOU 2479  CB  PHE A 325    11290  12010  10942   -968   -279   -820       C  
ATOM   2480  CG  PHE A 325       7.410  19.736  46.116  1.00 90.31           C  
ANISOU 2480  CG  PHE A 325    11197  12117  11000   -978   -203   -823       C  
ATOM   2481  CD1 PHE A 325       6.326  20.595  46.193  1.00 94.39           C  
ANISOU 2481  CD1 PHE A 325    11564  12753  11545   -901   -212   -840       C  
ATOM   2482  CD2 PHE A 325       7.886  19.151  47.277  1.00 90.85           C  
ANISOU 2482  CD2 PHE A 325    11303  12146  11069  -1057   -115   -800       C  
ATOM   2483  CE1 PHE A 325       5.736  20.876  47.413  1.00 99.30           C  
ANISOU 2483  CE1 PHE A 325    12087  13444  12198   -906   -125   -846       C  
ATOM   2484  CE2 PHE A 325       7.303  19.421  48.501  1.00 92.68           C  
ANISOU 2484  CE2 PHE A 325    11438  12456  11321  -1074    -39   -807       C  
ATOM   2485  CZ  PHE A 325       6.224  20.289  48.573  1.00 97.42           C  
ANISOU 2485  CZ  PHE A 325    11900  13165  11952  -1000    -39   -836       C  
ATOM   2486  N   LEU A 326      11.197  19.687  44.854  1.00 79.05           N  
ANISOU 2486  N   LEU A 326    10216  10334   9486   -877   -204   -728       N  
ATOM   2487  CA  LEU A 326      12.481  19.664  45.542  1.00 79.38           C  
ANISOU 2487  CA  LEU A 326    10350  10301   9510   -872   -138   -668       C  
ATOM   2488  C   LEU A 326      13.324  20.878  45.172  1.00 80.58           C  
ANISOU 2488  C   LEU A 326    10572  10411   9634   -755   -150   -657       C  
ATOM   2489  O   LEU A 326      14.039  21.423  46.015  1.00 83.60           O  
ANISOU 2489  O   LEU A 326    10978  10790   9994   -743    -96   -627       O  
ATOM   2490  CB  LEU A 326      13.258  18.383  45.228  1.00 80.25           C  
ANISOU 2490  CB  LEU A 326    10563  10312   9618   -940   -115   -620       C  
ATOM   2491  CG  LEU A 326      12.807  17.068  45.872  1.00 83.88           C  
ANISOU 2491  CG  LEU A 326    10994  10776  10102  -1068    -62   -606       C  
ATOM   2492  CD1 LEU A 326      13.538  15.903  45.214  1.00 85.36           C  
ANISOU 2492  CD1 LEU A 326    11310  10835  10290  -1109    -32   -565       C  
ATOM   2493  CD2 LEU A 326      13.020  17.065  47.390  1.00 79.12           C  
ANISOU 2493  CD2 LEU A 326    10343  10222   9498  -1101     13   -554       C  
ATOM   2494  N   GLY A 327      13.255  21.305  43.915  1.00 76.97           N  
ANISOU 2494  N   GLY A 327    10152   9925   9168   -682   -219   -681       N  
ATOM   2495  CA  GLY A 327      13.887  22.557  43.539  1.00 75.99           C  
ANISOU 2495  CA  GLY A 327    10089   9764   9020   -568   -226   -676       C  
ATOM   2496  C   GLY A 327      13.313  23.682  44.394  1.00 74.08           C  
ANISOU 2496  C   GLY A 327     9771   9587   8787   -518   -182   -704       C  
ATOM   2497  O   GLY A 327      14.045  24.396  45.080  1.00 74.94           O  
ANISOU 2497  O   GLY A 327     9930   9673   8872   -502   -122   -691       O  
ATOM   2498  N   SER A 328      11.993  23.819  44.349  1.00 71.28           N  
ANISOU 2498  N   SER A 328     9297   9321   8466   -500   -204   -740       N  
ATOM   2499  CA  SER A 328      11.273  24.791  45.150  1.00 71.82           C  
ANISOU 2499  CA  SER A 328     9284   9449   8554   -444   -143   -765       C  
ATOM   2500  C   SER A 328      11.754  24.854  46.589  1.00 70.75           C  
ANISOU 2500  C   SER A 328     9168   9314   8402   -514    -44   -762       C  
ATOM   2501  O   SER A 328      12.107  25.920  47.086  1.00 71.64           O  
ANISOU 2501  O   SER A 328     9328   9400   8491   -467     23   -776       O  
ATOM   2502  CB  SER A 328       9.789  24.472  45.138  1.00 74.14           C  
ANISOU 2502  CB  SER A 328     9417   9859   8892   -456   -170   -787       C  
ATOM   2503  OG  SER A 328       9.139  25.254  46.117  1.00 77.00           O  
ANISOU 2503  OG  SER A 328     9702  10275   9281   -414    -82   -806       O  
ATOM   2504  N   PHE A 329      11.767  23.709  47.258  1.00 71.40           N  
ANISOU 2504  N   PHE A 329     9220   9424   8485   -636    -30   -744       N  
ATOM   2505  CA  PHE A 329      12.308  23.617  48.615  1.00 71.48           C  
ANISOU 2505  CA  PHE A 329     9249   9448   8463   -718     53   -725       C  
ATOM   2506  C   PHE A 329      13.682  24.273  48.643  1.00 69.16           C  
ANISOU 2506  C   PHE A 329     9079   9088   8112   -698     72   -695       C  
ATOM   2507  O   PHE A 329      13.916  25.223  49.382  1.00 68.75           O  
ANISOU 2507  O   PHE A 329     9055   9044   8023   -695    139   -717       O  
ATOM   2508  CB  PHE A 329      12.410  22.147  49.046  1.00 75.18           C  
ANISOU 2508  CB  PHE A 329     9698   9930   8936   -840     54   -681       C  
ATOM   2509  CG  PHE A 329      13.085  21.922  50.386  1.00 76.78           C  
ANISOU 2509  CG  PHE A 329     9921  10159   9094   -928    127   -636       C  
ATOM   2510  CD1 PHE A 329      12.330  21.775  51.535  1.00 79.03           C  
ANISOU 2510  CD1 PHE A 329    10123  10524   9379   -998    191   -654       C  
ATOM   2511  CD2 PHE A 329      14.472  21.811  50.486  1.00 75.68           C  
ANISOU 2511  CD2 PHE A 329     9873   9976   8906   -945    131   -564       C  
ATOM   2512  CE1 PHE A 329      12.938  21.551  52.760  1.00 80.23           C  
ANISOU 2512  CE1 PHE A 329    10294  10714   9475  -1089    252   -606       C  
ATOM   2513  CE2 PHE A 329      15.087  21.588  51.708  1.00 77.12           C  
ANISOU 2513  CE2 PHE A 329    10059  10209   9035  -1033    187   -506       C  
ATOM   2514  CZ  PHE A 329      14.319  21.465  52.852  1.00 78.08           C  
ANISOU 2514  CZ  PHE A 329    10108  10412   9148  -1108    245   -528       C  
ATOM   2515  N   LEU A 330      14.581  23.746  47.826  1.00 66.63           N  
ANISOU 2515  N   LEU A 330     8833   8701   7782   -692     20   -648       N  
ATOM   2516  CA  LEU A 330      15.964  24.184  47.811  1.00 65.96           C  
ANISOU 2516  CA  LEU A 330     8852   8566   7646   -686     32   -603       C  
ATOM   2517  C   LEU A 330      16.015  25.680  47.621  1.00 67.47           C  
ANISOU 2517  C   LEU A 330     9090   8731   7814   -605     55   -653       C  
ATOM   2518  O   LEU A 330      16.719  26.387  48.352  1.00 64.22           O  
ANISOU 2518  O   LEU A 330     8730   8325   7346   -643    112   -651       O  
ATOM   2519  CB  LEU A 330      16.738  23.458  46.708  1.00 64.15           C  
ANISOU 2519  CB  LEU A 330     8690   8259   7424   -663    -23   -551       C  
ATOM   2520  CG  LEU A 330      18.247  23.638  46.595  1.00 63.26           C  
ANISOU 2520  CG  LEU A 330     8668   8101   7266   -660    -13   -482       C  
ATOM   2521  CD1 LEU A 330      18.954  23.594  47.933  1.00 62.66           C  
ANISOU 2521  CD1 LEU A 330     8576   8094   7139   -752     43   -424       C  
ATOM   2522  CD2 LEU A 330      18.781  22.554  45.673  1.00 62.85           C  
ANISOU 2522  CD2 LEU A 330     8665   7977   7238   -649    -43   -426       C  
ATOM   2523  N   TYR A 331      15.237  26.154  46.652  1.00 69.29           N  
ANISOU 2523  N   TYR A 331     9305   8938   8085   -500     15   -694       N  
ATOM   2524  CA  TYR A 331      15.124  27.583  46.373  1.00 70.83           C  
ANISOU 2524  CA  TYR A 331     9546   9094   8271   -399     48   -735       C  
ATOM   2525  C   TYR A 331      14.720  28.380  47.607  1.00 70.87           C  
ANISOU 2525  C   TYR A 331     9533   9133   8260   -424    156   -780       C  
ATOM   2526  O   TYR A 331      15.402  29.327  47.987  1.00 68.44           O  
ANISOU 2526  O   TYR A 331     9319   8784   7902   -433    223   -797       O  
ATOM   2527  CB  TYR A 331      14.126  27.808  45.244  1.00 71.64           C  
ANISOU 2527  CB  TYR A 331     9599   9198   8424   -281    -13   -752       C  
ATOM   2528  CG  TYR A 331      13.535  29.191  45.190  1.00 72.60           C  
ANISOU 2528  CG  TYR A 331     9723   9301   8560   -160     45   -786       C  
ATOM   2529  CD1 TYR A 331      14.253  30.259  44.679  1.00 71.54           C  
ANISOU 2529  CD1 TYR A 331     9711   9075   8398    -83     71   -786       C  
ATOM   2530  CD2 TYR A 331      12.242  29.423  45.622  1.00 74.64           C  
ANISOU 2530  CD2 TYR A 331     9864   9630   8867   -116     85   -810       C  
ATOM   2531  CE1 TYR A 331      13.696  31.524  44.603  1.00 76.01           C  
ANISOU 2531  CE1 TYR A 331    10292   9605   8982     39    143   -809       C  
ATOM   2532  CE2 TYR A 331      11.676  30.685  45.553  1.00 78.19           C  
ANISOU 2532  CE2 TYR A 331    10316  10052   9339     16    157   -827       C  
ATOM   2533  CZ  TYR A 331      12.402  31.732  45.041  1.00 77.12           C  
ANISOU 2533  CZ  TYR A 331    10315   9811   9177     96    190   -825       C  
ATOM   2534  OH  TYR A 331      11.830  32.982  44.992  1.00 80.44           O  
ANISOU 2534  OH  TYR A 331    10752  10188   9626    236    282   -835       O  
ATOM   2535  N   GLU A 332      13.619  27.972  48.228  1.00 71.81           N  
ANISOU 2535  N   GLU A 332     9538   9328   8417   -449    180   -801       N  
ATOM   2536  CA  GLU A 332      13.070  28.676  49.390  1.00 74.63           C  
ANISOU 2536  CA  GLU A 332     9873   9719   8765   -468    296   -850       C  
ATOM   2537  C   GLU A 332      13.974  28.623  50.617  1.00 75.42           C  
ANISOU 2537  C   GLU A 332    10035   9839   8782   -611    361   -846       C  
ATOM   2538  O   GLU A 332      14.172  29.631  51.306  1.00 79.95           O  
ANISOU 2538  O   GLU A 332    10680  10391   9306   -631    461   -891       O  
ATOM   2539  CB  GLU A 332      11.705  28.101  49.754  1.00 74.96           C  
ANISOU 2539  CB  GLU A 332     9765   9849   8868   -471    303   -864       C  
ATOM   2540  CG  GLU A 332      10.607  28.396  48.745  1.00 74.73           C  
ANISOU 2540  CG  GLU A 332     9646   9837   8911   -332    257   -868       C  
ATOM   2541  CD  GLU A 332      10.150  29.838  48.778  1.00 75.25           C  
ANISOU 2541  CD  GLU A 332     9735   9861   8995   -198    356   -899       C  
ATOM   2542  OE1 GLU A 332      10.721  30.646  49.542  1.00 75.86           O  
ANISOU 2542  OE1 GLU A 332     9920   9880   9024   -224    466   -934       O  
ATOM   2543  OE2 GLU A 332       9.199  30.159  48.040  1.00 80.32           O1-
ANISOU 2543  OE2 GLU A 332    10287  10534   9697    -69    329   -884       O1-
ATOM   2544  N   TYR A 333      14.521  27.447  50.885  1.00 76.78           N  
ANISOU 2544  N   TYR A 333    10183  10054   8935   -713    309   -786       N  
ATOM   2545  CA  TYR A 333      15.461  27.280  51.982  1.00 78.12           C  
ANISOU 2545  CA  TYR A 333    10396  10268   9018   -850    350   -754       C  
ATOM   2546  C   TYR A 333      16.726  28.076  51.707  1.00 75.82           C  
ANISOU 2546  C   TYR A 333    10224   9927   8659   -856    351   -741       C  
ATOM   2547  O   TYR A 333      17.285  28.684  52.611  1.00 76.86           O  
ANISOU 2547  O   TYR A 333    10412  10088   8702   -953    418   -757       O  
ATOM   2548  CB  TYR A 333      15.816  25.800  52.171  1.00 79.19           C  
ANISOU 2548  CB  TYR A 333    10479  10451   9158   -929    294   -667       C  
ATOM   2549  CG  TYR A 333      16.152  25.446  53.600  1.00 84.34           C  
ANISOU 2549  CG  TYR A 333    11113  11195   9736  -1071    349   -631       C  
ATOM   2550  CD1 TYR A 333      15.347  24.578  54.332  1.00 86.96           C  
ANISOU 2550  CD1 TYR A 333    11357  11592  10092  -1131    372   -622       C  
ATOM   2551  CD2 TYR A 333      17.258  25.999  54.232  1.00 86.15           C  
ANISOU 2551  CD2 TYR A 333    11413  11457   9861  -1155    377   -605       C  
ATOM   2552  CE1 TYR A 333      15.651  24.259  55.641  1.00 89.63           C  
ANISOU 2552  CE1 TYR A 333    11681  12020  10353  -1261    421   -582       C  
ATOM   2553  CE2 TYR A 333      17.561  25.693  55.541  1.00 86.26           C  
ANISOU 2553  CE2 TYR A 333    11408  11577   9791  -1295    420   -565       C  
ATOM   2554  CZ  TYR A 333      16.762  24.822  56.243  1.00 90.05           C  
ANISOU 2554  CZ  TYR A 333    11803  12115  10296  -1342    442   -550       C  
ATOM   2555  OH  TYR A 333      17.068  24.518  57.554  1.00 97.04           O  
ANISOU 2555  OH  TYR A 333    12672  13112  11088  -1482    483   -502       O  
ATOM   2556  N   SER A 334      17.170  28.067  50.454  1.00 75.17           N  
ANISOU 2556  N   SER A 334    10182   9772   8609   -767    279   -713       N  
ATOM   2557  CA  SER A 334      18.447  28.673  50.105  1.00 74.86           C  
ANISOU 2557  CA  SER A 334    10247   9689   8509   -779    273   -688       C  
ATOM   2558  C   SER A 334      18.368  30.165  50.234  1.00 75.36           C  
ANISOU 2558  C   SER A 334    10399   9698   8537   -752    357   -769       C  
ATOM   2559  O   SER A 334      19.308  30.786  50.733  1.00 77.50           O  
ANISOU 2559  O   SER A 334    10751   9976   8718   -845    402   -772       O  
ATOM   2560  CB  SER A 334      18.895  28.307  48.687  1.00 72.51           C  
ANISOU 2560  CB  SER A 334     9977   9320   8255   -684    186   -643       C  
ATOM   2561  OG  SER A 334      19.301  26.955  48.634  1.00 71.28           O  
ANISOU 2561  OG  SER A 334     9773   9194   8114   -727    133   -558       O  
ATOM   2562  N   ARG A 335      17.262  30.761  49.800  1.00 75.72           N  
ANISOU 2562  N   ARG A 335    10431   9692   8647   -630    388   -830       N  
ATOM   2563  CA  ARG A 335      17.206  32.220  49.795  1.00 79.10           C  
ANISOU 2563  CA  ARG A 335    10963  10039   9052   -580    487   -899       C  
ATOM   2564  C   ARG A 335      17.069  32.815  51.185  1.00 78.44           C  
ANISOU 2564  C   ARG A 335    10917   9986   8900   -693    618   -962       C  
ATOM   2565  O   ARG A 335      17.315  33.997  51.379  1.00 82.13           O  
ANISOU 2565  O   ARG A 335    11506  10381   9320   -701    721  -1022       O  
ATOM   2566  CB  ARG A 335      16.120  32.743  48.873  1.00 81.77           C  
ANISOU 2566  CB  ARG A 335    11276  10313   9480   -395    490   -922       C  
ATOM   2567  CG  ARG A 335      14.688  32.407  49.231  1.00 84.94           C  
ANISOU 2567  CG  ARG A 335    11545  10776   9953   -343    512   -942       C  
ATOM   2568  CD  ARG A 335      13.823  33.425  48.509  1.00 86.15           C  
ANISOU 2568  CD  ARG A 335    11703  10859  10169   -160    561   -962       C  
ATOM   2569  NE  ARG A 335      12.410  33.106  48.478  1.00 85.28           N  
ANISOU 2569  NE  ARG A 335    11440  10819  10143    -73    555   -956       N  
ATOM   2570  CZ  ARG A 335      11.487  33.920  47.989  1.00 88.29           C  
ANISOU 2570  CZ  ARG A 335    11787  11171  10587     96    605   -954       C  
ATOM   2571  NH1 ARG A 335      11.832  35.108  47.503  1.00 88.75           N1+
ANISOU 2571  NH1 ARG A 335    11973  11112  10636    200    673   -961       N1+
ATOM   2572  NH2 ARG A 335      10.215  33.547  47.989  1.00 93.18           N  
ANISOU 2572  NH2 ARG A 335    12241  11882  11279    163    591   -936       N  
ATOM   2573  N   ARG A 336      16.688  31.989  52.146  1.00 77.82           N  
ANISOU 2573  N   ARG A 336    10747  10010   8811   -788    621   -952       N  
ATOM   2574  CA  ARG A 336      16.556  32.426  53.529  1.00 80.25           C  
ANISOU 2574  CA  ARG A 336    11089  10363   9041   -915    743  -1011       C  
ATOM   2575  C   ARG A 336      17.868  32.335  54.297  1.00 82.73           C  
ANISOU 2575  C   ARG A 336    11464  10748   9221  -1107    736   -980       C  
ATOM   2576  O   ARG A 336      18.032  32.981  55.339  1.00 85.13           O  
ANISOU 2576  O   ARG A 336    11842  11078   9425  -1238    843  -1040       O  
ATOM   2577  CB  ARG A 336      15.471  31.606  54.228  1.00 78.91           C  
ANISOU 2577  CB  ARG A 336    10788  10277   8917   -929    755  -1011       C  
ATOM   2578  CG  ARG A 336      14.100  32.197  53.999  1.00 80.15           C  
ANISOU 2578  CG  ARG A 336    10904  10383   9168   -781    834  -1070       C  
ATOM   2579  CD  ARG A 336      12.967  31.198  54.043  1.00 81.82           C  
ANISOU 2579  CD  ARG A 336    10948  10672   9465   -742    790  -1045       C  
ATOM   2580  NE  ARG A 336      11.819  31.787  53.356  1.00 86.61           N  
ANISOU 2580  NE  ARG A 336    11500  11234  10174   -561    825  -1069       N  
ATOM   2581  CZ  ARG A 336      10.835  31.108  52.783  1.00 91.38           C  
ANISOU 2581  CZ  ARG A 336    11956  11892  10872   -476    752  -1037       C  
ATOM   2582  NH1 ARG A 336      10.824  29.778  52.811  1.00100.92           N1+
ANISOU 2582  NH1 ARG A 336    13072  13181  12090   -561    649   -991       N1+
ATOM   2583  NH2 ARG A 336       9.853  31.763  52.170  1.00 92.46           N  
ANISOU 2583  NH2 ARG A 336    12036  12004  11090   -308    785  -1044       N  
ATOM   2584  N   HIS A 337      18.810  31.557  53.781  1.00 81.37           N  
ANISOU 2584  N   HIS A 337    11263  10613   9042  -1128    618   -884       N  
ATOM   2585  CA  HIS A 337      20.034  31.293  54.513  1.00 81.73           C  
ANISOU 2585  CA  HIS A 337    11325  10761   8967  -1303    596   -821       C  
ATOM   2586  C   HIS A 337      21.260  31.476  53.640  1.00 80.17           C  
ANISOU 2586  C   HIS A 337    11183  10532   8748  -1291    530   -763       C  
ATOM   2587  O   HIS A 337      21.793  30.513  53.095  1.00 84.60           O  
ANISOU 2587  O   HIS A 337    11678  11120   9345  -1257    432   -658       O  
ATOM   2588  CB  HIS A 337      19.956  29.895  55.132  1.00 85.01           C  
ANISOU 2588  CB  HIS A 337    11616  11297   9389  -1364    537   -729       C  
ATOM   2589  CG  HIS A 337      18.884  29.773  56.179  1.00 88.16           C  
ANISOU 2589  CG  HIS A 337    11968  11745   9783  -1414    615   -785       C  
ATOM   2590  CD2 HIS A 337      17.580  29.414  56.087  1.00 86.96           C  
ANISOU 2590  CD2 HIS A 337    11741  11568   9733  -1319    634   -823       C  
ATOM   2591  ND1 HIS A 337      19.095  30.104  57.502  1.00 87.93           N  
ANISOU 2591  ND1 HIS A 337    11973  11810   9627  -1586    693   -813       N  
ATOM   2592  CE1 HIS A 337      17.977  29.931  58.184  1.00 88.24           C  
ANISOU 2592  CE1 HIS A 337    11964  11868   9693  -1588    762   -866       C  
ATOM   2593  NE2 HIS A 337      17.041  29.513  57.350  1.00 88.73           N  
ANISOU 2593  NE2 HIS A 337    11953  11862   9898  -1425    727   -870       N  
ATOM   2594  N   PRO A 338      21.694  32.732  53.472  1.00 80.43           N  
ANISOU 2594  N   PRO A 338    11342  10493   8723  -1314    596   -832       N  
ATOM   2595  CA  PRO A 338      22.972  33.002  52.808  1.00 82.02           C  
ANISOU 2595  CA  PRO A 338    11601  10681   8880  -1339    547   -779       C  
ATOM   2596  C   PRO A 338      24.137  32.577  53.676  1.00 84.31           C  
ANISOU 2596  C   PRO A 338    11853  11134   9046  -1532    513   -691       C  
ATOM   2597  O   PRO A 338      25.233  32.350  53.180  1.00 87.18           O  
ANISOU 2597  O   PRO A 338    12205  11531   9388  -1549    447   -600       O  
ATOM   2598  CB  PRO A 338      22.994  34.528  52.646  1.00 81.29           C  
ANISOU 2598  CB  PRO A 338    11668  10474   8747  -1344    657   -892       C  
ATOM   2599  CG  PRO A 338      21.630  35.006  53.001  1.00 82.05           C  
ANISOU 2599  CG  PRO A 338    11783  10498   8894  -1269    761   -993       C  
ATOM   2600  CD  PRO A 338      21.005  33.969  53.871  1.00 80.70           C  
ANISOU 2600  CD  PRO A 338    11483  10445   8736  -1315    736   -963       C  
ATOM   2601  N   GLU A 339      23.900  32.498  54.976  1.00 86.22           N  
ANISOU 2601  N   GLU A 339    12072  11484   9202  -1679    563   -713       N  
ATOM   2602  CA  GLU A 339      24.952  32.124  55.894  1.00 90.89           C  
ANISOU 2602  CA  GLU A 339    12618  12259   9659  -1874    528   -620       C  
ATOM   2603  C   GLU A 339      25.354  30.660  55.703  1.00 86.20           C  
ANISOU 2603  C   GLU A 339    11878  11753   9120  -1821    417   -451       C  
ATOM   2604  O   GLU A 339      26.443  30.279  56.087  1.00 94.14           O  
ANISOU 2604  O   GLU A 339    12828  12902  10040  -1931    367   -329       O  
ATOM   2605  CB  GLU A 339      24.552  32.424  57.364  1.00 91.55           C  
ANISOU 2605  CB  GLU A 339    12723  12441   9621  -2054    614   -688       C  
ATOM   2606  CG  GLU A 339      23.527  31.479  58.010  1.00 89.29           C  
ANISOU 2606  CG  GLU A 339    12336  12201   9388  -2021    616   -671       C  
ATOM   2607  CD  GLU A 339      22.064  31.790  57.691  1.00 90.82           C  
ANISOU 2607  CD  GLU A 339    12557  12247   9705  -1867    692   -791       C  
ATOM   2608  OE1 GLU A 339      21.789  32.714  56.901  1.00 95.07           O  
ANISOU 2608  OE1 GLU A 339    13188  12637  10298  -1760    742   -879       O  
ATOM   2609  OE2 GLU A 339      21.169  31.108  58.242  1.00 85.39           O1-
ANISOU 2609  OE2 GLU A 339    11789  11597   9059  -1851    707   -789       O1-
ATOM   2610  N   TYR A 340      24.479  29.840  55.140  1.00 81.76           N  
ANISOU 2610  N   TYR A 340    11256  11112   8698  -1660    387   -438       N  
ATOM   2611  CA  TYR A 340      24.752  28.402  55.020  1.00 82.23           C  
ANISOU 2611  CA  TYR A 340    11198  11232   8813  -1613    310   -288       C  
ATOM   2612  C   TYR A 340      25.658  28.106  53.841  1.00 79.39           C  
ANISOU 2612  C   TYR A 340    10838  10819   8509  -1513    246   -197       C  
ATOM   2613  O   TYR A 340      25.720  28.874  52.881  1.00 79.43           O  
ANISOU 2613  O   TYR A 340    10926  10706   8547  -1433    250   -267       O  
ATOM   2614  CB  TYR A 340      23.456  27.617  54.834  1.00 81.15           C  
ANISOU 2614  CB  TYR A 340    11009  11026   8799  -1499    311   -319       C  
ATOM   2615  CG  TYR A 340      22.601  27.410  56.067  1.00 82.92           C  
ANISOU 2615  CG  TYR A 340    11191  11329   8985  -1591    365   -358       C  
ATOM   2616  CD1 TYR A 340      21.491  26.591  56.000  1.00 86.34           C  
ANISOU 2616  CD1 TYR A 340    11560  11724   9520  -1513    364   -371       C  
ATOM   2617  CD2 TYR A 340      22.896  27.997  57.287  1.00 86.68           C  
ANISOU 2617  CD2 TYR A 340    11694  11922   9318  -1767    419   -383       C  
ATOM   2618  CE1 TYR A 340      20.687  26.373  57.098  1.00 88.07           C  
ANISOU 2618  CE1 TYR A 340    11738  12014   9711  -1592    419   -404       C  
ATOM   2619  CE2 TYR A 340      22.093  27.780  58.398  1.00 91.00           C  
ANISOU 2619  CE2 TYR A 340    12208  12538   9828  -1849    475   -420       C  
ATOM   2620  CZ  TYR A 340      20.983  26.956  58.292  1.00 91.86           C  
ANISOU 2620  CZ  TYR A 340    12247  12602  10052  -1754    476   -427       C  
ATOM   2621  OH  TYR A 340      20.151  26.704  59.369  1.00 90.40           O  
ANISOU 2621  OH  TYR A 340    12026  12484   9838  -1832    538   -461       O  
ATOM   2622  N   ALA A 341      26.342  26.969  53.916  1.00 80.09           N  
ANISOU 2622  N   ALA A 341    10836  10988   8608  -1510    197    -35       N  
ATOM   2623  CA  ALA A 341      27.203  26.518  52.828  1.00 79.62           C  
ANISOU 2623  CA  ALA A 341    10770  10875   8609  -1406    152     66       C  
ATOM   2624  C   ALA A 341      26.339  25.821  51.795  1.00 76.70           C  
ANISOU 2624  C   ALA A 341    10410  10350   8382  -1240    138     33       C  
ATOM   2625  O   ALA A 341      25.322  25.196  52.133  1.00 75.05           O  
ANISOU 2625  O   ALA A 341    10164  10127   8224  -1223    149      2       O  
ATOM   2626  CB  ALA A 341      28.290  25.578  53.333  1.00 79.73           C  
ANISOU 2626  CB  ALA A 341    10680  11033   8580  -1457    125    268       C  
ATOM   2627  N   VAL A 342      26.739  25.924  50.536  1.00 71.64           N  
ANISOU 2627  N   VAL A 342     9822   9601   7799  -1130    116     36       N  
ATOM   2628  CA  VAL A 342      25.946  25.341  49.454  1.00 73.95           C  
ANISOU 2628  CA  VAL A 342    10138   9750   8208   -989     98     -6       C  
ATOM   2629  C   VAL A 342      25.830  23.814  49.602  1.00 77.34           C  
ANISOU 2629  C   VAL A 342    10499  10188   8697   -965     97    101       C  
ATOM   2630  O   VAL A 342      24.777  23.243  49.318  1.00 78.54           O  
ANISOU 2630  O   VAL A 342    10648  10271   8923   -917     96     43       O  
ATOM   2631  CB  VAL A 342      26.489  25.779  48.077  1.00 72.16           C  
ANISOU 2631  CB  VAL A 342     9993   9413   8013   -889     78    -18       C  
ATOM   2632  CG1 VAL A 342      26.016  24.861  46.971  1.00 69.40           C  
ANISOU 2632  CG1 VAL A 342     9660   8944   7763   -768     56    -16       C  
ATOM   2633  CG2 VAL A 342      26.089  27.228  47.802  1.00 67.61           C  
ANISOU 2633  CG2 VAL A 342     9500   8782   7407   -881     90   -156       C  
ATOM   2634  N   SER A 343      26.877  23.169  50.116  1.00 83.30           N  
ANISOU 2634  N   SER A 343    11195  11036   9418  -1006    105    262       N  
ATOM   2635  CA  SER A 343      26.854  21.719  50.357  1.00 88.33           C  
ANISOU 2635  CA  SER A 343    11775  11675  10110   -981    127    384       C  
ATOM   2636  C   SER A 343      25.852  21.329  51.435  1.00 89.96           C  
ANISOU 2636  C   SER A 343    11930  11943  10308  -1056    144    350       C  
ATOM   2637  O   SER A 343      25.113  20.346  51.274  1.00 99.07           O  
ANISOU 2637  O   SER A 343    13078  13026  11539  -1017    162    349       O  
ATOM   2638  CB  SER A 343      28.244  21.209  50.752  1.00 92.58           C  
ANISOU 2638  CB  SER A 343    12248  12320  10609   -998    139    587       C  
ATOM   2639  OG  SER A 343      29.164  21.459  49.698  1.00101.66           O  
ANISOU 2639  OG  SER A 343    13440  13406  11778   -919    134    627       O  
ATOM   2640  N   VAL A 344      25.852  22.067  52.546  1.00 86.31           N  
ANISOU 2640  N   VAL A 344    11435  11613   9745  -1176    146    324       N  
ATOM   2641  CA  VAL A 344      24.873  21.835  53.610  1.00 83.72           C  
ANISOU 2641  CA  VAL A 344    11064  11347   9398  -1256    171    279       C  
ATOM   2642  C   VAL A 344      23.473  21.942  53.012  1.00 82.33           C  
ANISOU 2642  C   VAL A 344    10924  11048   9308  -1191    174    120       C  
ATOM   2643  O   VAL A 344      22.667  21.017  53.137  1.00 89.36           O  
ANISOU 2643  O   VAL A 344    11782  11909  10261  -1180    190    121       O  
ATOM   2644  CB  VAL A 344      25.024  22.845  54.773  1.00 84.99           C  
ANISOU 2644  CB  VAL A 344    11216  11652   9425  -1402    183    237       C  
ATOM   2645  CG1 VAL A 344      23.776  22.890  55.650  1.00 87.47           C  
ANISOU 2645  CG1 VAL A 344    11514  11992   9731  -1466    222    135       C  
ATOM   2646  CG2 VAL A 344      26.240  22.512  55.621  1.00 82.82           C  
ANISOU 2646  CG2 VAL A 344    10870  11548   9049  -1498    172    416       C  
ATOM   2647  N   LEU A 345      23.207  23.050  52.322  1.00 79.64           N  
ANISOU 2647  N   LEU A 345    10647  10640   8972  -1146    161     -7       N  
ATOM   2648  CA  LEU A 345      21.900  23.282  51.699  1.00 78.01           C  
ANISOU 2648  CA  LEU A 345    10459  10339   8841  -1075    158   -144       C  
ATOM   2649  C   LEU A 345      21.490  22.083  50.838  1.00 75.37           C  
ANISOU 2649  C   LEU A 345    10116   9914   8606   -999    136   -114       C  
ATOM   2650  O   LEU A 345      20.357  21.601  50.934  1.00 77.71           O  
ANISOU 2650  O   LEU A 345    10374  10198   8953  -1003    142   -170       O  
ATOM   2651  CB  LEU A 345      21.903  24.593  50.880  1.00 77.51           C  
ANISOU 2651  CB  LEU A 345    10474  10204   8772  -1010    147   -246       C  
ATOM   2652  CG  LEU A 345      21.926  25.933  51.647  1.00 77.44           C  
ANISOU 2652  CG  LEU A 345    10501  10246   8677  -1083    194   -325       C  
ATOM   2653  CD1 LEU A 345      22.159  27.122  50.723  1.00 77.46           C  
ANISOU 2653  CD1 LEU A 345    10598  10157   8677  -1010    192   -397       C  
ATOM   2654  CD2 LEU A 345      20.626  26.139  52.408  1.00 76.31           C  
ANISOU 2654  CD2 LEU A 345    10321  10128   8544  -1110    243   -420       C  
ATOM   2655  N   LEU A 346      22.422  21.577  50.034  1.00 72.40           N  
ANISOU 2655  N   LEU A 346     9778   9478   8252   -943    120    -26       N  
ATOM   2656  CA  LEU A 346      22.162  20.377  49.221  1.00 74.96           C  
ANISOU 2656  CA  LEU A 346    10120   9704   8659   -887    119      5       C  
ATOM   2657  C   LEU A 346      21.885  19.109  50.039  1.00 75.49           C  
ANISOU 2657  C   LEU A 346    10133   9802   8749   -945    163     85       C  
ATOM   2658  O   LEU A 346      21.009  18.350  49.659  1.00 76.96           O  
ANISOU 2658  O   LEU A 346    10324   9922   8996   -940    169     40       O  
ATOM   2659  CB  LEU A 346      23.298  20.131  48.225  1.00 74.21           C  
ANISOU 2659  CB  LEU A 346    10089   9529   8579   -812    116     87       C  
ATOM   2660  CG  LEU A 346      23.415  21.193  47.121  1.00 75.47           C  
ANISOU 2660  CG  LEU A 346    10319   9623   8732   -741     74     -1       C  
ATOM   2661  CD1 LEU A 346      24.657  20.979  46.264  1.00 73.76           C  
ANISOU 2661  CD1 LEU A 346    10161   9342   8522   -676     83     91       C  
ATOM   2662  CD2 LEU A 346      22.161  21.217  46.258  1.00 77.54           C  
ANISOU 2662  CD2 LEU A 346    10606   9810   9045   -698     39   -128       C  
ATOM   2663  N   ARG A 347      22.596  18.881  51.150  1.00 77.67           N  
ANISOU 2663  N   ARG A 347    10359  10184   8970  -1007    193    206       N  
ATOM   2664  CA  ARG A 347      22.290  17.727  52.037  1.00 84.80           C  
ANISOU 2664  CA  ARG A 347    11210  11122   9887  -1063    241    291       C  
ATOM   2665  C   ARG A 347      20.909  17.848  52.656  1.00 86.93           C  
ANISOU 2665  C   ARG A 347    11438  11429  10162  -1130    246    173       C  
ATOM   2666  O   ARG A 347      20.185  16.869  52.760  1.00 86.74           O  
ANISOU 2666  O   ARG A 347    11400  11367  10191  -1151    278    175       O  
ATOM   2667  CB  ARG A 347      23.293  17.576  53.186  1.00 85.68           C  
ANISOU 2667  CB  ARG A 347    11263  11372   9921  -1122    263    454       C  
ATOM   2668  CG  ARG A 347      24.659  17.064  52.762  1.00 87.64           C  
ANISOU 2668  CG  ARG A 347    11520  11602  10178  -1053    278    625       C  
ATOM   2669  CD  ARG A 347      25.618  16.956  53.938  1.00 85.89           C  
ANISOU 2669  CD  ARG A 347    11214  11552   9867  -1117    288    802       C  
ATOM   2670  NE  ARG A 347      26.969  17.352  53.547  1.00 87.31           N  
ANISOU 2670  NE  ARG A 347    11384  11777  10012  -1076    269    910       N  
ATOM   2671  CZ  ARG A 347      27.742  18.214  54.206  1.00 87.02           C  
ANISOU 2671  CZ  ARG A 347    11295  11907   9861  -1160    231    955       C  
ATOM   2672  NH1 ARG A 347      27.345  18.768  55.347  1.00 88.15           N1+
ANISOU 2672  NH1 ARG A 347    11399  12188   9904  -1294    215    904       N1+
ATOM   2673  NH2 ARG A 347      28.946  18.504  53.727  1.00 86.16           N  
ANISOU 2673  NH2 ARG A 347    11173  11832   9731  -1120    215   1054       N  
ATOM   2674  N   LEU A 348      20.551  19.057  53.075  1.00 89.31           N  
ANISOU 2674  N   LEU A 348    11724  11802  10409  -1165    228     71       N  
ATOM   2675  CA  LEU A 348      19.222  19.294  53.625  1.00 88.35           C  
ANISOU 2675  CA  LEU A 348    11557  11715  10296  -1213    245    -44       C  
ATOM   2676  C   LEU A 348      18.177  18.894  52.601  1.00 87.55           C  
ANISOU 2676  C   LEU A 348    11462  11515  10289  -1156    224   -135       C  
ATOM   2677  O   LEU A 348      17.198  18.236  52.934  1.00 88.71           O  
ANISOU 2677  O   LEU A 348    11560  11672  10473  -1201    247   -164       O  
ATOM   2678  CB  LEU A 348      19.044  20.761  54.033  1.00 87.52           C  
ANISOU 2678  CB  LEU A 348    11459  11670  10127  -1235    248   -147       C  
ATOM   2679  CG  LEU A 348      20.022  21.247  55.105  1.00 85.14           C  
ANISOU 2679  CG  LEU A 348    11157  11486   9708  -1328    268    -76       C  
ATOM   2680  CD1 LEU A 348      19.574  22.595  55.650  1.00 84.11           C  
ANISOU 2680  CD1 LEU A 348    11048  11397   9513  -1375    302   -203       C  
ATOM   2681  CD2 LEU A 348      20.122  20.224  56.229  1.00 86.62           C  
ANISOU 2681  CD2 LEU A 348    11283  11767   9861  -1418    300     40       C  
ATOM   2682  N   ALA A 349      18.401  19.286  51.350  1.00 85.80           N  
ANISOU 2682  N   ALA A 349    11297  11206  10095  -1068    178   -175       N  
ATOM   2683  CA  ALA A 349      17.534  18.875  50.257  1.00 85.02           C  
ANISOU 2683  CA  ALA A 349    11210  11026  10069  -1026    146   -249       C  
ATOM   2684  C   ALA A 349      17.512  17.352  50.120  1.00 82.39           C  
ANISOU 2684  C   ALA A 349    10892  10632   9781  -1063    177   -181       C  
ATOM   2685  O   ALA A 349      16.443  16.751  49.985  1.00 80.81           O  
ANISOU 2685  O   ALA A 349    10660  10421   9622  -1105    180   -240       O  
ATOM   2686  CB  ALA A 349      18.003  19.514  48.956  1.00 82.21           C  
ANISOU 2686  CB  ALA A 349    10927  10591   9718   -930     94   -281       C  
ATOM   2687  N   LYS A 350      18.694  16.736  50.152  1.00 80.97           N  
ANISOU 2687  N   LYS A 350    10761  10411   9592  -1047    211    -53       N  
ATOM   2688  CA  LYS A 350      18.811  15.282  50.017  1.00 84.48           C  
ANISOU 2688  CA  LYS A 350    11243  10772  10084  -1067    268     28       C  
ATOM   2689  C   LYS A 350      18.107  14.562  51.162  1.00 86.82           C  
ANISOU 2689  C   LYS A 350    11475  11128  10384  -1161    320     52       C  
ATOM   2690  O   LYS A 350      17.424  13.562  50.940  1.00 89.07           O  
ANISOU 2690  O   LYS A 350    11779  11346  10719  -1207    356     32       O  
ATOM   2691  CB  LYS A 350      20.278  14.841  49.938  1.00 85.09           C  
ANISOU 2691  CB  LYS A 350    11371  10806  10154  -1012    310    186       C  
ATOM   2692  CG  LYS A 350      20.485  13.349  49.700  1.00 82.65           C  
ANISOU 2692  CG  LYS A 350    11124  10377   9901  -1009    396    280       C  
ATOM   2693  N   GLU A 351      18.268  15.080  52.379  1.00 91.75           N  
ANISOU 2693  N   GLU A 351    12031  11878  10950  -1203    328     91       N  
ATOM   2694  CA  GLU A 351      17.584  14.527  53.550  1.00 95.07           C  
ANISOU 2694  CA  GLU A 351    12388  12371  11363  -1297    378    111       C  
ATOM   2695  C   GLU A 351      16.082  14.736  53.415  1.00 94.36           C  
ANISOU 2695  C   GLU A 351    12250  12296  11308  -1340    359    -42       C  
ATOM   2696  O   GLU A 351      15.315  13.780  53.466  1.00 98.51           O  
ANISOU 2696  O   GLU A 351    12764  12787  11877  -1400    396    -55       O  
ATOM   2697  CB  GLU A 351      18.084  15.155  54.856  1.00 98.31           C  
ANISOU 2697  CB  GLU A 351    12743  12926  11683  -1344    387    175       C  
ATOM   2698  CG  GLU A 351      17.612  14.438  56.133  1.00104.44           C  
ANISOU 2698  CG  GLU A 351    13465  13780  12439  -1441    448    234       C  
ATOM   2699  CD  GLU A 351      18.352  13.128  56.434  1.00107.67           C  
ANISOU 2699  CD  GLU A 351    13896  14151  12862  -1438    510    419       C  
ATOM   2700  OE1 GLU A 351      19.597  13.155  56.583  1.00110.57           O  
ANISOU 2700  OE1 GLU A 351    14270  14554  13187  -1398    508    561       O  
ATOM   2701  OE2 GLU A 351      17.691  12.069  56.546  1.00100.65           O1-
ANISOU 2701  OE2 GLU A 351    13015  13199  12027  -1477    568    431       O1-
ATOM   2702  N   TYR A 352      15.669  15.982  53.221  1.00 92.28           N  
ANISOU 2702  N   TYR A 352    11955  12082  11024  -1308    309   -152       N  
ATOM   2703  CA  TYR A 352      14.259  16.288  53.013  1.00 91.41           C  
ANISOU 2703  CA  TYR A 352    11780  12000  10951  -1325    290   -283       C  
ATOM   2704  C   TYR A 352      13.645  15.334  51.982  1.00 89.97           C  
ANISOU 2704  C   TYR A 352    11619  11733  10834  -1339    272   -319       C  
ATOM   2705  O   TYR A 352      12.557  14.792  52.207  1.00 90.99           O  
ANISOU 2705  O   TYR A 352    11686  11892  10995  -1415    290   -367       O  
ATOM   2706  CB  TYR A 352      14.074  17.743  52.567  1.00 87.88           C  
ANISOU 2706  CB  TYR A 352    11322  11580  10489  -1247    242   -377       C  
ATOM   2707  CG  TYR A 352      12.622  18.134  52.406  1.00 85.56           C  
ANISOU 2707  CG  TYR A 352    10940  11335  10235  -1244    228   -489       C  
ATOM   2708  CD1 TYR A 352      11.814  18.345  53.519  1.00 86.33           C  
ANISOU 2708  CD1 TYR A 352    10952  11526  10324  -1301    285   -521       C  
ATOM   2709  CD2 TYR A 352      12.055  18.276  51.149  1.00 83.91           C  
ANISOU 2709  CD2 TYR A 352    10724  11089  10069  -1186    162   -553       C  
ATOM   2710  CE1 TYR A 352      10.486  18.700  53.382  1.00 86.32           C  
ANISOU 2710  CE1 TYR A 352    10852  11580  10366  -1288    281   -609       C  
ATOM   2711  CE2 TYR A 352      10.721  18.620  51.000  1.00 83.70           C  
ANISOU 2711  CE2 TYR A 352    10592  11132  10078  -1180    146   -635       C  
ATOM   2712  CZ  TYR A 352       9.942  18.829  52.117  1.00 85.49           C  
ANISOU 2712  CZ  TYR A 352    10726  11450  10306  -1225    208   -659       C  
ATOM   2713  OH  TYR A 352       8.614  19.176  51.983  1.00 87.19           O  
ANISOU 2713  OH  TYR A 352    10819  11744  10563  -1207    201   -727       O  
ATOM   2714  N   GLU A 353      14.352  15.112  50.875  1.00 86.89           N  
ANISOU 2714  N   GLU A 353    11320  11239  10457  -1281    243   -297       N  
ATOM   2715  CA  GLU A 353      13.884  14.181  49.848  1.00 90.94           C  
ANISOU 2715  CA  GLU A 353    11880  11659  11013  -1312    234   -335       C  
ATOM   2716  C   GLU A 353      13.659  12.770  50.404  1.00 89.71           C  
ANISOU 2716  C   GLU A 353    11741  11462  10884  -1414    319   -279       C  
ATOM   2717  O   GLU A 353      12.592  12.184  50.207  1.00 92.85           O  
ANISOU 2717  O   GLU A 353    12108  11861  11308  -1503    322   -350       O  
ATOM   2718  CB  GLU A 353      14.856  14.106  48.673  1.00 92.25           C  
ANISOU 2718  CB  GLU A 353    12163  11708  11179  -1236    214   -306       C  
ATOM   2719  CG  GLU A 353      14.323  13.259  47.523  1.00 93.55           C  
ANISOU 2719  CG  GLU A 353    12394  11780  11371  -1284    205   -368       C  
ATOM   2720  CD  GLU A 353      15.294  13.133  46.366  1.00 94.58           C  
ANISOU 2720  CD  GLU A 353    12654  11785  11496  -1213    202   -342       C  
ATOM   2721  OE1 GLU A 353      16.503  13.384  46.555  1.00 88.93           O  
ANISOU 2721  OE1 GLU A 353    11981  11039  10770  -1132    230   -245       O  
ATOM   2722  OE2 GLU A 353      14.841  12.764  45.261  1.00 99.18           O1-
ANISOU 2722  OE2 GLU A 353    13296  12307  12080  -1248    175   -417       O1-
ATOM   2723  N   ALA A 354      14.662  12.231  51.091  1.00 86.59           N  
ANISOU 2723  N   ALA A 354    11391  11032  10478  -1403    389   -145       N  
ATOM   2724  CA  ALA A 354      14.561  10.909  51.720  1.00 84.05           C  
ANISOU 2724  CA  ALA A 354    11093  10660  10181  -1484    487    -66       C  
ATOM   2725  C   ALA A 354      13.380  10.805  52.706  1.00 85.27           C  
ANISOU 2725  C   ALA A 354    11143  10920  10335  -1590    506   -117       C  
ATOM   2726  O   ALA A 354      12.734   9.759  52.799  1.00 82.40           O  
ANISOU 2726  O   ALA A 354    10795  10508  10004  -1685    566   -125       O  
ATOM   2727  CB  ALA A 354      15.863  10.573  52.431  1.00 82.18           C  
ANISOU 2727  CB  ALA A 354    10891  10410   9924  -1433    551    111       C  
ATOM   2728  N   THR A 355      13.110  11.890  53.435  1.00 85.34           N  
ANISOU 2728  N   THR A 355    11055  11065  10306  -1577    468   -153       N  
ATOM   2729  CA  THR A 355      11.975  11.954  54.358  1.00 85.21           C  
ANISOU 2729  CA  THR A 355    10932  11156  10287  -1665    491   -210       C  
ATOM   2730  C   THR A 355      10.669  11.796  53.598  1.00 90.09           C  
ANISOU 2730  C   THR A 355    11500  11778  10951  -1719    455   -338       C  
ATOM   2731  O   THR A 355       9.827  10.987  53.975  1.00 97.69           O  
ANISOU 2731  O   THR A 355    12426  12754  11939  -1827    504   -356       O  
ATOM   2732  CB  THR A 355      11.924  13.288  55.132  1.00 83.04           C  
ANISOU 2732  CB  THR A 355    10580  11011   9960  -1631    467   -243       C  
ATOM   2733  CG2 THR A 355      10.833  13.263  56.198  1.00 77.60           C  
ANISOU 2733  CG2 THR A 355     9791  10427   9268  -1721    516   -286       C  
ATOM   2734  OG1 THR A 355      13.188  13.546  55.758  1.00 77.70           O  
ANISOU 2734  OG1 THR A 355     9947  10353   9223  -1597    483   -130       O  
ATOM   2735  N   LEU A 356      10.511  12.542  52.512  1.00 94.05           N  
ANISOU 2735  N   LEU A 356    11999  12276  11461  -1650    370   -419       N  
ATOM   2736  CA  LEU A 356       9.308  12.413  51.685  1.00100.21           C  
ANISOU 2736  CA  LEU A 356    12719  13084  12272  -1703    320   -528       C  
ATOM   2737  C   LEU A 356       9.127  11.001  51.093  1.00100.64           C  
ANISOU 2737  C   LEU A 356    12856  13032  12351  -1814    356   -529       C  
ATOM   2738  O   LEU A 356       8.042  10.409  51.185  1.00 93.95           O  
ANISOU 2738  O   LEU A 356    11944  12230  11523  -1936    372   -584       O  
ATOM   2739  CB  LEU A 356       9.316  13.453  50.564  1.00 98.84           C  
ANISOU 2739  CB  LEU A 356    12540  12923  12092  -1598    220   -591       C  
ATOM   2740  CG  LEU A 356       9.240  14.908  51.035  1.00 99.19           C  
ANISOU 2740  CG  LEU A 356    12505  13064  12119  -1497    196   -614       C  
ATOM   2741  CD1 LEU A 356       9.051  15.820  49.832  1.00 98.67           C  
ANISOU 2741  CD1 LEU A 356    12429  13007  12055  -1398    103   -674       C  
ATOM   2742  CD2 LEU A 356       8.130  15.120  52.060  1.00 98.58           C  
ANISOU 2742  CD2 LEU A 356    12289  13111  12055  -1550    239   -650       C  
ATOM   2743  N   GLU A 357      10.195  10.467  50.507  1.00101.79           N  
ANISOU 2743  N   GLU A 357    13147  13035  12494  -1776    382   -467       N  
ATOM   2744  CA  GLU A 357      10.144   9.151  49.871  1.00105.38           C  
ANISOU 2744  CA  GLU A 357    13717  13356  12968  -1875    440   -470       C  
ATOM   2745  C   GLU A 357       9.669   8.091  50.858  1.00105.57           C  
ANISOU 2745  C   GLU A 357    13731  13370  13013  -1999    546   -432       C  
ATOM   2746  O   GLU A 357       8.861   7.228  50.500  1.00110.57           O  
ANISOU 2746  O   GLU A 357    14384  13967  13659  -2138    576   -496       O  
ATOM   2747  CB  GLU A 357      11.512   8.763  49.292  1.00109.14           C  
ANISOU 2747  CB  GLU A 357    14355  13670  13443  -1790    486   -384       C  
ATOM   2748  CG  GLU A 357      11.460   7.634  48.260  1.00116.07           C  
ANISOU 2748  CG  GLU A 357    15378  14389  14333  -1876    539   -421       C  
ATOM   2749  CD  GLU A 357      10.723   8.006  46.974  1.00115.59           C  
ANISOU 2749  CD  GLU A 357    15309  14364  14247  -1921    433   -560       C  
ATOM   2750  OE1 GLU A 357      10.935   9.129  46.451  1.00105.69           O  
ANISOU 2750  OE1 GLU A 357    14011  13175  12970  -1812    329   -586       O  
ATOM   2751  OE2 GLU A 357       9.928   7.164  46.490  1.00113.87           O1-
ANISOU 2751  OE2 GLU A 357    15130  14111  14023  -2075    455   -638       O1-
ATOM   2752  N   GLU A 358      10.148   8.172  52.102  1.00115.10           N  
ANISOU 2752  N   GLU A 358    15045  14233  14455  -2888   1308   1313       N  
ATOM   2753  CA  GLU A 358       9.748   7.220  53.154  1.00112.93           C  
ANISOU 2753  CA  GLU A 358    14776  13679  14452  -2841   1379   1633       C  
ATOM   2754  C   GLU A 358       8.373   7.558  53.748  1.00110.55           C  
ANISOU 2754  C   GLU A 358    14503  13388  14112  -2892   1553   1905       C  
ATOM   2755  O   GLU A 358       7.504   6.700  53.783  1.00114.36           O  
ANISOU 2755  O   GLU A 358    14859  13646  14947  -2952   1604   2028       O  
ATOM   2756  CB  GLU A 358      10.805   7.119  54.261  1.00109.14           C  
ANISOU 2756  CB  GLU A 358    14439  13197  13832  -2716   1344   1849       C  
ATOM   2757  N   CYS A 359       8.158   8.803  54.177  1.00109.27           N  
ANISOU 2757  N   CYS A 359    14468  13474  13575  -2874   1638   1964       N  
ATOM   2758  CA  CYS A 359       6.899   9.172  54.857  1.00109.44           C  
ANISOU 2758  CA  CYS A 359    14487  13540  13556  -2911   1815   2174       C  
ATOM   2759  C   CYS A 359       5.646   9.050  53.978  1.00112.75           C  
ANISOU 2759  C   CYS A 359    14751  13855  14235  -3030   1849   2080       C  
ATOM   2760  O   CYS A 359       4.552   8.795  54.494  1.00110.41           O  
ANISOU 2760  O   CYS A 359    14396  13488  14065  -3076   1992   2273       O  
ATOM   2761  CB  CYS A 359       6.961  10.595  55.425  1.00106.16           C  
ANISOU 2761  CB  CYS A 359    14176  13397  12763  -2857   1876   2146       C  
ATOM   2762  SG  CYS A 359       8.072  10.841  56.831  1.00105.71           S  
ANISOU 2762  SG  CYS A 359    14274  13544  12346  -2722   1896   2290       S  
ATOM   2763  N   CYS A 360       5.804   9.224  52.664  1.00116.07           N  
ANISOU 2763  N   CYS A 360    15082  14309  14708  -3094   1719   1791       N  
ATOM   2764  CA  CYS A 360       4.660   9.211  51.743  1.00116.98           C  
ANISOU 2764  CA  CYS A 360    15033  14392  15021  -3216   1724   1684       C  
ATOM   2765  C   CYS A 360       4.100   7.815  51.450  1.00115.75           C  
ANISOU 2765  C   CYS A 360    14709  13965  15305  -3272   1732   1659       C  
ATOM   2766  O   CYS A 360       3.013   7.702  50.892  1.00116.82           O  
ANISOU 2766  O   CYS A 360    14703  14052  15633  -3368   1761   1604       O  
ATOM   2767  CB  CYS A 360       5.013   9.930  50.438  1.00118.43           C  
ANISOU 2767  CB  CYS A 360    15140  14805  15051  -3294   1568   1425       C  
ATOM   2768  SG  CYS A 360       5.205  11.715  50.642  1.00121.03           S  
ANISOU 2768  SG  CYS A 360    15576  15369  15042  -3271   1541   1505       S  
ATOM   2769  N   ALA A 361       4.834   6.768  51.832  1.00118.50           N  
ANISOU 2769  N   ALA A 361    15047  14115  15864  -3213   1688   1702       N  
ATOM   2770  CA  ALA A 361       4.343   5.379  51.744  1.00120.12           C  
ANISOU 2770  CA  ALA A 361    15056  13975  16610  -3254   1679   1723       C  
ATOM   2771  C   ALA A 361       3.620   4.906  53.011  1.00121.21           C  
ANISOU 2771  C   ALA A 361    15220  13929  16905  -3254   1829   2194       C  
ATOM   2772  O   ALA A 361       3.050   3.823  53.016  1.00123.29           O  
ANISOU 2772  O   ALA A 361    15301  13881  17663  -3307   1829   2292       O  
ATOM   2773  CB  ALA A 361       5.487   4.424  51.423  1.00119.26           C  
ANISOU 2773  CB  ALA A 361    14843  13690  16780  -3201   1517   1512       C  
ATOM   2774  N   LYS A 362       3.647   5.704  54.078  1.00125.66           N  
ANISOU 2774  N   LYS A 362    15970  14714  17061  -3206   1952   2474       N  
ATOM   2775  CA  LYS A 362       3.009   5.322  55.352  1.00131.45           C  
ANISOU 2775  CA  LYS A 362    16702  15414  17828  -3230   2110   2939       C  
ATOM   2776  C   LYS A 362       1.500   5.602  55.361  1.00133.22           C  
ANISOU 2776  C   LYS A 362    16835  15671  18111  -3328   2279   2998       C  
ATOM   2777  O   LYS A 362       0.964   6.237  54.450  1.00132.26           O  
ANISOU 2777  O   LYS A 362    16677  15606  17970  -3363   2266   2699       O  
ATOM   2778  CB  LYS A 362       3.683   6.032  56.534  1.00128.53           C  
ANISOU 2778  CB  LYS A 362    16521  15360  16956  -3147   2177   3155       C  
ATOM   2779  N   ASP A 363       0.826   5.113  56.397  1.00137.26           N  
ANISOU 2779  N   ASP A 363    17286  16171  18695  -3385   2429   3413       N  
ATOM   2780  CA  ASP A 363      -0.628   5.247  56.517  1.00142.73           C  
ANISOU 2780  CA  ASP A 363    17861  16890  19481  -3487   2607   3495       C  
ATOM   2781  C   ASP A 363      -1.056   6.701  56.744  1.00145.20           C  
ANISOU 2781  C   ASP A 363    18262  17563  19345  -3458   2736   3320       C  
ATOM   2782  O   ASP A 363      -2.072   7.145  56.204  1.00148.64           O  
ANISOU 2782  O   ASP A 363    18605  17981  19891  -3512   2792   3145       O  
ATOM   2783  CB  ASP A 363      -1.161   4.356  57.648  1.00143.09           C  
ANISOU 2783  CB  ASP A 363    17792  16899  19678  -3578   2741   4030       C  
ATOM   2784  N   ASP A 364      -0.275   7.430  57.541  1.00148.68           N  
ANISOU 2784  N   ASP A 364    18848  18311  19332  -3371   2765   3350       N  
ATOM   2785  CA  ASP A 364      -0.538   8.840  57.861  1.00150.94           C  
ANISOU 2785  CA  ASP A 364    19176  18918  19255  -3325   2864   3137       C  
ATOM   2786  C   ASP A 364       0.735   9.658  57.610  1.00151.26           C  
ANISOU 2786  C   ASP A 364    19379  19070  19025  -3205   2709   2899       C  
ATOM   2787  O   ASP A 364       1.501   9.921  58.537  1.00153.55           O  
ANISOU 2787  O   ASP A 364    19761  19604  18976  -3133   2738   2983       O  
ATOM   2788  CB  ASP A 364      -0.999   8.974  59.321  1.00156.28           C  
ANISOU 2788  CB  ASP A 364    19797  19953  19631  -3354   3097   3385       C  
ATOM   2789  CG  ASP A 364      -1.457  10.390  59.685  1.00155.63           C  
ANISOU 2789  CG  ASP A 364    19671  20182  19280  -3309   3215   3078       C  
ATOM   2790  OD1 ASP A 364      -1.226  11.339  58.910  1.00147.71           O  
ANISOU 2790  OD1 ASP A 364    18708  19098  18316  -3242   3088   2739       O  
ATOM   2791  OD2 ASP A 364      -2.059  10.545  60.768  1.00161.21           O1-
ANISOU 2791  OD2 ASP A 364    20262  21230  19759  -3354   3432   3180       O1-
ATOM   2792  N   PRO A 365       0.974  10.042  56.343  1.00146.62           N  
ANISOU 2792  N   PRO A 365    18802  18337  18572  -3199   2539   2617       N  
ATOM   2793  CA  PRO A 365       2.158  10.813  55.964  1.00140.73           C  
ANISOU 2793  CA  PRO A 365    18177  17687  17606  -3113   2380   2411       C  
ATOM   2794  C   PRO A 365       2.430  12.085  56.785  1.00137.25           C  
ANISOU 2794  C   PRO A 365    17790  17524  16835  -3026   2440   2313       C  
ATOM   2795  O   PRO A 365       3.587  12.347  57.106  1.00134.53           O  
ANISOU 2795  O   PRO A 365    17566  17295  16255  -2938   2363   2276       O  
ATOM   2796  CB  PRO A 365       1.873  11.176  54.507  1.00139.56           C  
ANISOU 2796  CB  PRO A 365    17947  17431  17648  -3179   2232   2180       C  
ATOM   2797  CG  PRO A 365       1.070  10.033  53.995  1.00141.67           C  
ANISOU 2797  CG  PRO A 365    18085  17474  18268  -3276   2253   2240       C  
ATOM   2798  CD  PRO A 365       0.240   9.557  55.157  1.00146.27           C  
ANISOU 2798  CD  PRO A 365    18628  18045  18900  -3294   2467   2512       C  
ATOM   2799  N   HIS A 366       1.391  12.857  57.116  1.00132.68           N  
ANISOU 2799  N   HIS A 366    17093  17041  16278  -3047   2567   2231       N  
ATOM   2800  CA  HIS A 366       1.572  14.148  57.802  1.00127.82           C  
ANISOU 2800  CA  HIS A 366    16453  16659  15453  -2962   2605   2029       C  
ATOM   2801  C   HIS A 366       2.218  13.983  59.175  1.00130.15           C  
ANISOU 2801  C   HIS A 366    16818  17264  15371  -2891   2723   2124       C  
ATOM   2802  O   HIS A 366       3.174  14.681  59.492  1.00128.89           O  
ANISOU 2802  O   HIS A 366    16726  17250  14997  -2794   2648   1970       O  
ATOM   2803  CB  HIS A 366       0.250  14.916  57.928  1.00122.68           C  
ANISOU 2803  CB  HIS A 366    15601  16032  14981  -2998   2722   1877       C  
ATOM   2804  N   ALA A 367       1.715  13.039  59.971  1.00132.44           N  
ANISOU 2804  N   ALA A 367    17070  17672  15580  -2954   2893   2407       N  
ATOM   2805  CA  ALA A 367       2.319  12.699  61.267  1.00131.89           C  
ANISOU 2805  CA  ALA A 367    17040  17956  15117  -2925   2987   2605       C  
ATOM   2806  C   ALA A 367       3.833  12.464  61.142  1.00130.96           C  
ANISOU 2806  C   ALA A 367    17106  17783  14869  -2836   2795   2654       C  
ATOM   2807  O   ALA A 367       4.610  12.820  62.030  1.00130.53           O  
ANISOU 2807  O   ALA A 367    17094  18048  14451  -2762   2804   2628       O  
ATOM   2808  N   CYS A 368       4.235  11.875  60.019  1.00126.53           N  
ANISOU 2808  N   CYS A 368    16626  16844  14607  -2847   2621   2682       N  
ATOM   2809  CA  CYS A 368       5.627  11.554  59.741  1.00120.06           C  
ANISOU 2809  CA  CYS A 368    15949  15930  13739  -2773   2432   2693       C  
ATOM   2810  C   CYS A 368       6.433  12.790  59.320  1.00117.53           C  
ANISOU 2810  C   CYS A 368    15696  15674  13284  -2681   2309   2343       C  
ATOM   2811  O   CYS A 368       7.417  13.128  59.977  1.00119.04           O  
ANISOU 2811  O   CYS A 368    15968  16066  13194  -2589   2268   2305       O  
ATOM   2812  CB  CYS A 368       5.679  10.472  58.655  1.00117.47           C  
ANISOU 2812  CB  CYS A 368    15611  15211  13812  -2830   2303   2764       C  
ATOM   2813  SG  CYS A 368       7.290   9.718  58.349  1.00114.31           S  
ANISOU 2813  SG  CYS A 368    15315  14655  13464  -2755   2083   2784       S  
ATOM   2814  N   TYR A 369       6.015  13.466  58.243  1.00113.68           N  
ANISOU 2814  N   TYR A 369    15153  15030  13011  -2716   2236   2120       N  
ATOM   2815  CA  TYR A 369       6.780  14.609  57.698  1.00108.42           C  
ANISOU 2815  CA  TYR A 369    14513  14384  12297  -2661   2083   1861       C  
ATOM   2816  C   TYR A 369       6.645  15.931  58.471  1.00107.36           C  
ANISOU 2816  C   TYR A 369    14301  14455  12034  -2588   2144   1649       C  
ATOM   2817  O   TYR A 369       7.425  16.854  58.253  1.00101.98           O  
ANISOU 2817  O   TYR A 369    13629  13789  11328  -2530   2011   1466       O  
ATOM   2818  CB  TYR A 369       6.514  14.818  56.187  1.00106.23           C  
ANISOU 2818  CB  TYR A 369    14169  13907  12288  -2754   1938   1770       C  
ATOM   2819  CG  TYR A 369       5.110  15.241  55.756  1.00108.33           C  
ANISOU 2819  CG  TYR A 369    14274  14087  12800  -2842   1992   1742       C  
ATOM   2820  CD1 TYR A 369       4.623  16.522  56.014  1.00110.55           C  
ANISOU 2820  CD1 TYR A 369    14435  14417  13152  -2817   2003   1593       C  
ATOM   2821  CD2 TYR A 369       4.296  14.380  55.028  1.00110.85           C  
ANISOU 2821  CD2 TYR A 369    14526  14250  13340  -2949   2007   1832       C  
ATOM   2822  CE1 TYR A 369       3.352  16.911  55.592  1.00111.39           C  
ANISOU 2822  CE1 TYR A 369    14370  14415  13540  -2894   2028   1568       C  
ATOM   2823  CE2 TYR A 369       3.029  14.760  54.604  1.00110.77           C  
ANISOU 2823  CE2 TYR A 369    14361  14163  13564  -3030   2041   1809       C  
ATOM   2824  CZ  TYR A 369       2.556  16.023  54.883  1.00111.56           C  
ANISOU 2824  CZ  TYR A 369    14352  14307  13728  -3003   2048   1693       C  
ATOM   2825  OH  TYR A 369       1.287  16.385  54.458  1.00111.01           O  
ANISOU 2825  OH  TYR A 369    14105  14133  13941  -3080   2063   1674       O  
ATOM   2826  N   SER A 370       5.682  16.013  59.387  1.00113.85           N  
ANISOU 2826  N   SER A 370    15014  15447  12799  -2597   2341   1649       N  
ATOM   2827  CA  SER A 370       5.482  17.213  60.223  1.00117.03           C  
ANISOU 2827  CA  SER A 370    15275  16084  13109  -2525   2418   1354       C  
ATOM   2828  C   SER A 370       6.742  17.687  60.953  1.00117.37           C  
ANISOU 2828  C   SER A 370    15387  16359  12850  -2406   2358   1209       C  
ATOM   2829  O   SER A 370       6.975  18.887  61.078  1.00118.16           O  
ANISOU 2829  O   SER A 370    15375  16495  13026  -2334   2295    884       O  
ATOM   2830  CB  SER A 370       4.388  16.964  61.270  1.00120.19           C  
ANISOU 2830  CB  SER A 370    15531  16757  13379  -2564   2675   1380       C  
ATOM   2831  OG  SER A 370       3.110  16.876  60.671  1.00121.27           O  
ANISOU 2831  OG  SER A 370    15546  16687  13843  -2658   2735   1407       O  
ATOM   2832  N   THR A 371       7.544  16.742  61.434  1.00117.42           N  
ANISOU 2832  N   THR A 371    15551  16498  12567  -2387   2361   1450       N  
ATOM   2833  CA  THR A 371       8.657  17.047  62.330  1.00117.34           C  
ANISOU 2833  CA  THR A 371    15592  16782  12209  -2280   2328   1347       C  
ATOM   2834  C   THR A 371      10.003  17.155  61.616  1.00112.64           C  
ANISOU 2834  C   THR A 371    15150  15990  11660  -2219   2102   1316       C  
ATOM   2835  O   THR A 371      11.048  17.032  62.255  1.00109.99           O  
ANISOU 2835  O   THR A 371    14899  15847  11045  -2140   2052   1331       O  
ATOM   2836  CB  THR A 371       8.775  15.951  63.403  1.00118.21           C  
ANISOU 2836  CB  THR A 371    15749  17208  11958  -2306   2445   1689       C  
ATOM   2837  CG2 THR A 371       7.441  15.766  64.111  1.00122.80           C  
ANISOU 2837  CG2 THR A 371    16156  18047  12455  -2398   2685   1765       C  
ATOM   2838  OG1 THR A 371       9.177  14.717  62.786  1.00114.98           O  
ANISOU 2838  OG1 THR A 371    15488  16503  11695  -2351   2340   2052       O  
ATOM   2839  N   VAL A 372       9.986  17.398  60.309  1.00110.23           N  
ANISOU 2839  N   VAL A 372    14855  15349  11679  -2267   1963   1278       N  
ATOM   2840  CA  VAL A 372      11.204  17.240  59.504  1.00110.19           C  
ANISOU 2840  CA  VAL A 372    14976  15192  11698  -2250   1767   1298       C  
ATOM   2841  C   VAL A 372      12.295  18.280  59.782  1.00108.06           C  
ANISOU 2841  C   VAL A 372    14706  15028  11324  -2147   1651   1056       C  
ATOM   2842  O   VAL A 372      13.474  17.951  59.721  1.00108.65           O  
ANISOU 2842  O   VAL A 372    14902  15117  11264  -2099   1542   1090       O  
ATOM   2843  CB  VAL A 372      10.895  17.210  57.989  1.00109.16           C  
ANISOU 2843  CB  VAL A 372    14813  14787  11876  -2362   1652   1329       C  
ATOM   2844  CG1 VAL A 372      10.729  18.623  57.443  1.00109.91           C  
ANISOU 2844  CG1 VAL A 372    14765  14814  12181  -2382   1545   1140       C  
ATOM   2845  CG2 VAL A 372      11.985  16.458  57.241  1.00106.70           C  
ANISOU 2845  CG2 VAL A 372    14613  14393  11537  -2375   1511   1394       C  
ATOM   2846  N   PHE A 373      11.920  19.518  60.100  1.00110.27           N  
ANISOU 2846  N   PHE A 373    14822  15362  11714  -2111   1663    788       N  
ATOM   2847  CA  PHE A 373      12.918  20.583  60.308  1.00108.99           C  
ANISOU 2847  CA  PHE A 373    14612  15246  11554  -2017   1532    527       C  
ATOM   2848  C   PHE A 373      13.676  20.459  61.628  1.00108.93           C  
ANISOU 2848  C   PHE A 373    14654  15584  11151  -1897   1594    416       C  
ATOM   2849  O   PHE A 373      14.701  21.118  61.821  1.00107.34           O  
ANISOU 2849  O   PHE A 373    14444  15432  10909  -1812   1475    219       O  
ATOM   2850  CB  PHE A 373      12.273  21.964  60.184  1.00108.89           C  
ANISOU 2850  CB  PHE A 373    14346  15114  11913  -2016   1489    252       C  
ATOM   2851  CG  PHE A 373      11.777  22.262  58.803  1.00107.61           C  
ANISOU 2851  CG  PHE A 373    14111  14631  12144  -2144   1355    404       C  
ATOM   2852  CD1 PHE A 373      10.448  22.042  58.454  1.00106.47           C  
ANISOU 2852  CD1 PHE A 373    13880  14382  12193  -2234   1442    503       C  
ATOM   2853  CD2 PHE A 373      12.650  22.729  57.836  1.00105.98           C  
ANISOU 2853  CD2 PHE A 373    13908  14274  12086  -2193   1136    477       C  
ATOM   2854  CE1 PHE A 373       9.999  22.298  57.168  1.00103.29           C  
ANISOU 2854  CE1 PHE A 373    13392  13737  12116  -2366   1299    670       C  
ATOM   2855  CE2 PHE A 373      12.206  22.986  56.550  1.00103.38           C  
ANISOU 2855  CE2 PHE A 373    13481  13745  12054  -2343   1001    670       C  
ATOM   2856  CZ  PHE A 373      10.881  22.770  56.216  1.00102.21           C  
ANISOU 2856  CZ  PHE A 373    13247  13503  12086  -2427   1075    768       C  
ATOM   2857  N   ASP A 374      13.174  19.609  62.520  1.00110.33           N  
ANISOU 2857  N   ASP A 374    14862  16023  11037  -1904   1769    572       N  
ATOM   2858  CA  ASP A 374      13.941  19.185  63.681  1.00116.72           C  
ANISOU 2858  CA  ASP A 374    15734  17209  11407  -1827   1805    614       C  
ATOM   2859  C   ASP A 374      15.041  18.201  63.229  1.00117.96           C  
ANISOU 2859  C   ASP A 374    16107  17211  11503  -1820   1663    908       C  
ATOM   2860  O   ASP A 374      16.184  18.278  63.701  1.00123.45           O  
ANISOU 2860  O   ASP A 374    16862  18058  11984  -1730   1566    847       O  
ATOM   2861  CB  ASP A 374      13.027  18.551  64.740  1.00119.82           C  
ANISOU 2861  CB  ASP A 374    16050  17976  11500  -1877   2024    777       C  
ATOM   2862  N   LYS A 375      14.693  17.283  62.320  1.00114.55           N  
ANISOU 2862  N   LYS A 375    15757  16479  11287  -1911   1644   1181       N  
ATOM   2863  CA  LYS A 375      15.647  16.310  61.766  1.00111.44           C  
ANISOU 2863  CA  LYS A 375    15508  15894  10942  -1909   1505   1385       C  
ATOM   2864  C   LYS A 375      16.719  16.975  60.892  1.00109.37           C  
ANISOU 2864  C   LYS A 375    15280  15477  10799  -1874   1324   1162       C  
ATOM   2865  O   LYS A 375      17.808  16.430  60.729  1.00109.73           O  
ANISOU 2865  O   LYS A 375    15417  15473  10805  -1832   1203   1216       O  
ATOM   2866  CB  LYS A 375      14.911  15.229  60.960  1.00107.08           C  
ANISOU 2866  CB  LYS A 375    14967  15064  10657  -2020   1532   1631       C  
ATOM   2867  N   LEU A 376      16.416  18.145  60.329  1.00108.24           N  
ANISOU 2867  N   LEU A 376    15034  15257  10835  -1900   1295    933       N  
ATOM   2868  CA  LEU A 376      17.394  18.881  59.524  1.00106.04           C  
ANISOU 2868  CA  LEU A 376    14747  14871  10674  -1896   1120    775       C  
ATOM   2869  C   LEU A 376      18.318  19.737  60.396  1.00107.00           C  
ANISOU 2869  C   LEU A 376    14845  15173  10636  -1768   1063    542       C  
ATOM   2870  O   LEU A 376      19.513  19.828  60.122  1.00108.73           O  
ANISOU 2870  O   LEU A 376    15119  15373  10822  -1730    926    487       O  
ATOM   2871  CB  LEU A 376      16.696  19.742  58.464  1.00104.94           C  
ANISOU 2871  CB  LEU A 376    14467  14552  10853  -2008   1069    722       C  
ATOM   2872  CG  LEU A 376      15.932  18.972  57.381  1.00103.66           C  
ANISOU 2872  CG  LEU A 376    14302  14239  10844  -2149   1086    910       C  
ATOM   2873  CD1 LEU A 376      15.187  19.919  56.455  1.00106.78           C  
ANISOU 2873  CD1 LEU A 376    14528  14513  11530  -2267   1017    900       C  
ATOM   2874  CD2 LEU A 376      16.862  18.078  56.584  1.00104.36           C  
ANISOU 2874  CD2 LEU A 376    14475  14296  10882  -2188    988    972       C  
ATOM   2875  N   LYS A 377      17.780  20.340  61.453  1.00108.98           N  
ANISOU 2875  N   LYS A 377    14990  15630  10788  -1704   1169    368       N  
ATOM   2876  CA  LYS A 377      18.614  21.044  62.443  1.00111.51           C  
ANISOU 2876  CA  LYS A 377    15257  16195  10917  -1575   1129     94       C  
ATOM   2877  C   LYS A 377      19.931  20.291  62.752  1.00110.61           C  
ANISOU 2877  C   LYS A 377    15309  16191  10526  -1504   1037    216       C  
ATOM   2878  O   LYS A 377      21.009  20.886  62.785  1.00106.07           O  
ANISOU 2878  O   LYS A 377    14725  15629   9948  -1431    906     24       O  
ATOM   2879  CB  LYS A 377      17.826  21.259  63.740  1.00112.73           C  
ANISOU 2879  CB  LYS A 377    15279  16711  10844  -1528   1304    -72       C  
ATOM   2880  N   HIS A 378      19.827  18.981  62.967  1.00111.69           N  
ANISOU 2880  N   HIS A 378    15570  16376  10490  -1530   1090    546       N  
ATOM   2881  CA  HIS A 378      20.986  18.122  63.236  1.00113.00           C  
ANISOU 2881  CA  HIS A 378    15866  16592  10479  -1469    982    713       C  
ATOM   2882  C   HIS A 378      22.075  18.198  62.158  1.00112.90           C  
ANISOU 2882  C   HIS A 378    15909  16317  10670  -1468    809    630       C  
ATOM   2883  O   HIS A 378      23.273  18.211  62.475  1.00114.11           O  
ANISOU 2883  O   HIS A 378    16107  16550  10700  -1378    690    557       O  
ATOM   2884  CB  HIS A 378      20.530  16.668  63.396  1.00112.52           C  
ANISOU 2884  CB  HIS A 378    15874  16492  10386  -1526   1037   1126       C  
ATOM   2885  N   LEU A 379      21.664  18.253  60.890  1.00110.96           N  
ANISOU 2885  N   LEU A 379    15639  15809  10712  -1578    794    638       N  
ATOM   2886  CA  LEU A 379      22.622  18.291  59.778  1.00104.91           C  
ANISOU 2886  CA  LEU A 379    14883  14884  10096  -1617    649    563       C  
ATOM   2887  C   LEU A 379      23.401  19.602  59.698  1.00104.59           C  
ANISOU 2887  C   LEU A 379    14766  14884  10091  -1581    543    315       C  
ATOM   2888  O   LEU A 379      24.388  19.693  58.971  1.00108.57           O  
ANISOU 2888  O   LEU A 379    15264  15333  10654  -1607    421    253       O  
ATOM   2889  CB  LEU A 379      21.937  18.006  58.434  1.00103.47           C  
ANISOU 2889  CB  LEU A 379    14649  14516  10150  -1773    660    640       C  
ATOM   2890  CG  LEU A 379      21.702  16.520  58.090  1.00103.18           C  
ANISOU 2890  CG  LEU A 379    14657  14360  10188  -1814    687    812       C  
ATOM   2891  CD1 LEU A 379      21.450  16.370  56.602  1.00100.33           C  
ANISOU 2891  CD1 LEU A 379    14202  13898  10019  -1966    652    764       C  
ATOM   2892  CD2 LEU A 379      22.841  15.592  58.495  1.00103.70           C  
ANISOU 2892  CD2 LEU A 379    14790  14413  10197  -1716    594    844       C  
ATOM   2893  N   VAL A 380      22.953  20.625  60.412  1.00104.99           N  
ANISOU 2893  N   VAL A 380    14719  15029  10142  -1532    587    150       N  
ATOM   2894  CA  VAL A 380      23.693  21.876  60.476  1.00105.44           C  
ANISOU 2894  CA  VAL A 380    14662  15089  10311  -1484    471   -107       C  
ATOM   2895  C   VAL A 380      24.731  21.820  61.605  1.00108.38           C  
ANISOU 2895  C   VAL A 380    15087  15688  10404  -1327    429   -259       C  
ATOM   2896  O   VAL A 380      25.844  22.322  61.459  1.00108.59           O  
ANISOU 2896  O   VAL A 380    15087  15694  10478  -1286    295   -404       O  
ATOM   2897  CB  VAL A 380      22.738  23.061  60.672  1.00106.71           C  
ANISOU 2897  CB  VAL A 380    14625  15200  10721  -1498    509   -287       C  
ATOM   2898  CG1 VAL A 380      23.507  24.370  60.597  1.00112.42           C  
ANISOU 2898  CG1 VAL A 380    15179  15838  11699  -1465    352   -537       C  
ATOM   2899  CG2 VAL A 380      21.635  23.039  59.624  1.00101.24           C  
ANISOU 2899  CG2 VAL A 380    13876  14303  10289  -1654    540    -92       C  
ATOM   2900  N   ASP A 381      24.373  21.177  62.713  1.00110.20           N  
ANISOU 2900  N   ASP A 381    15375  16166  10331  -1256    537   -193       N  
ATOM   2901  CA  ASP A 381      25.251  21.079  63.883  1.00112.38           C  
ANISOU 2901  CA  ASP A 381    15674  16745  10279  -1123    494   -295       C  
ATOM   2902  C   ASP A 381      26.425  20.116  63.691  1.00113.05           C  
ANISOU 2902  C   ASP A 381    15906  16778  10270  -1087    369   -109       C  
ATOM   2903  O   ASP A 381      27.518  20.362  64.198  1.00114.89           O  
ANISOU 2903  O   ASP A 381    16137  17145  10369   -986    257   -258       O  
ATOM   2904  CB  ASP A 381      24.441  20.660  65.115  1.00115.50           C  
ANISOU 2904  CB  ASP A 381    16043  17509  10332  -1097    644   -214       C  
ATOM   2905  CG  ASP A 381      23.400  21.695  65.507  1.00117.81           C  
ANISOU 2905  CG  ASP A 381    16135  17927  10702  -1105    768   -521       C  
ATOM   2906  OD1 ASP A 381      23.753  22.889  65.625  1.00118.48           O  
ANISOU 2906  OD1 ASP A 381    16058  18009  10950  -1042    699   -924       O  
ATOM   2907  OD2 ASP A 381      22.225  21.316  65.698  1.00118.17           O1-
ANISOU 2907  OD2 ASP A 381    16153  18055  10691  -1174    927   -378       O1-
ATOM   2908  N   GLU A 382      26.205  19.016  62.978  1.00117.45           N  
ANISOU 2908  N   GLU A 382    16559  17132  10935  -1165    379    180       N  
ATOM   2909  CA  GLU A 382      27.266  18.023  62.779  1.00124.83           C  
ANISOU 2909  CA  GLU A 382    17582  17975  11872  -1128    251    318       C  
ATOM   2910  C   GLU A 382      28.553  18.671  62.204  1.00129.25           C  
ANISOU 2910  C   GLU A 382    18115  18459  12534  -1094    105     63       C  
ATOM   2911  O   GLU A 382      29.625  18.542  62.807  1.00135.10           O  
ANISOU 2911  O   GLU A 382    18882  19313  13137   -986     -8     10       O  
ATOM   2912  CB  GLU A 382      26.754  16.826  61.943  1.00123.88           C  
ANISOU 2912  CB  GLU A 382    17499  17600  11969  -1225    279    568       C  
ATOM   2913  CG  GLU A 382      27.792  15.756  61.636  1.00125.42           C  
ANISOU 2913  CG  GLU A 382    17723  17641  12290  -1188    135    647       C  
ATOM   2914  N   PRO A 383      28.449  19.400  61.069  1.00127.58           N  
ANISOU 2914  N   PRO A 383    17830  18087  12557  -1199     97    -66       N  
ATOM   2915  CA  PRO A 383      29.599  20.154  60.539  1.00126.23           C  
ANISOU 2915  CA  PRO A 383    17594  17883  12484  -1198    -33   -275       C  
ATOM   2916  C   PRO A 383      30.301  21.090  61.548  1.00126.15           C  
ANISOU 2916  C   PRO A 383    17536  18036  12361  -1065   -103   -513       C  
ATOM   2917  O   PRO A 383      31.532  21.162  61.557  1.00125.03           O  
ANISOU 2917  O   PRO A 383    17391  17914  12199  -1004   -227   -632       O  
ATOM   2918  CB  PRO A 383      28.975  20.980  59.402  1.00126.72           C  
ANISOU 2918  CB  PRO A 383    17538  17819  12793  -1361    -13   -284       C  
ATOM   2919  CG  PRO A 383      27.831  20.157  58.932  1.00125.85           C  
ANISOU 2919  CG  PRO A 383    17466  17630  12719  -1457    100    -78       C  
ATOM   2920  CD  PRO A 383      27.289  19.481  60.158  1.00128.11           C  
ANISOU 2920  CD  PRO A 383    17852  18013  12814  -1346    192     27       C  
ATOM   2921  N   GLN A 384      29.527  21.798  62.373  1.00122.14           N  
ANISOU 2921  N   GLN A 384    16958  17657  11794  -1022    -25   -626       N  
ATOM   2922  CA  GLN A 384      30.079  22.803  63.295  1.00119.60           C  
ANISOU 2922  CA  GLN A 384    16524  17509  11411   -902    -88   -950       C  
ATOM   2923  C   GLN A 384      31.063  22.250  64.338  1.00115.80           C  
ANISOU 2923  C   GLN A 384    16116  17292  10589   -760   -162   -980       C  
ATOM   2924  O   GLN A 384      31.897  22.997  64.841  1.00114.24           O  
ANISOU 2924  O   GLN A 384    15827  17207  10370   -666   -261  -1268       O  
ATOM   2925  CB  GLN A 384      28.955  23.568  64.004  1.00119.72           C  
ANISOU 2925  CB  GLN A 384    16397  17654  11439   -885     25  -1136       C  
ATOM   2926  N   ASN A 385      30.983  20.954  64.644  1.00112.22           N  
ANISOU 2926  N   ASN A 385    15801  16920   9917   -750   -137   -668       N  
ATOM   2927  CA  ASN A 385      31.953  20.307  65.544  1.00110.52           C  
ANISOU 2927  CA  ASN A 385    15642  16929   9421   -634   -248   -596       C  
ATOM   2928  C   ASN A 385      33.355  20.184  64.926  1.00106.22           C  
ANISOU 2928  C   ASN A 385    15124  16196   9037   -597   -418   -674       C  
ATOM   2929  O   ASN A 385      34.341  20.680  65.485  1.00104.96           O  
ANISOU 2929  O   ASN A 385    14916  16189   8777   -493   -533   -895       O  
ATOM   2930  CB  ASN A 385      31.446  18.922  65.962  1.00110.16           C  
ANISOU 2930  CB  ASN A 385    15693  16955   9209   -656   -208   -161       C  
ATOM   2931  N   LEU A 386      33.429  19.546  63.761  1.00102.74           N  
ANISOU 2931  N   LEU A 386    14732  15457   8847   -688   -427   -536       N  
ATOM   2932  CA  LEU A 386      34.706  19.366  63.049  1.00103.19           C  
ANISOU 2932  CA  LEU A 386    14776  15363   9068   -677   -565   -642       C  
ATOM   2933  C   LEU A 386      35.482  20.678  62.923  1.00101.11           C  
ANISOU 2933  C   LEU A 386    14408  15131   8877   -658   -636   -968       C  
ATOM   2934  O   LEU A 386      36.654  20.765  63.307  1.00 97.91           O  
ANISOU 2934  O   LEU A 386    13984  14798   8420   -557   -769  -1112       O  
ATOM   2935  CB  LEU A 386      34.474  18.786  61.643  1.00104.73           C  
ANISOU 2935  CB  LEU A 386    14962  15309   9523   -819   -526   -563       C  
ATOM   2936  N   ILE A 387      34.813  21.697  62.384  1.00 97.69           N  
ANISOU 2936  N   ILE A 387    13882  14621   8614   -759   -565  -1064       N  
ATOM   2937  CA  ILE A 387      35.438  22.990  62.174  1.00 97.19           C  
ANISOU 2937  CA  ILE A 387    13670  14521   8736   -767   -648  -1324       C  
ATOM   2938  C   ILE A 387      36.156  23.431  63.432  1.00 98.98           C  
ANISOU 2938  C   ILE A 387    13859  14956   8794   -594   -736  -1576       C  
ATOM   2939  O   ILE A 387      37.362  23.673  63.395  1.00102.22           O  
ANISOU 2939  O   ILE A 387    14224  15361   9253   -543   -865  -1731       O  
ATOM   2940  CB  ILE A 387      34.416  24.070  61.775  1.00 94.77           C  
ANISOU 2940  CB  ILE A 387    13227  14101   8680   -875   -582  -1360       C  
ATOM   2941  N   LYS A 388      35.421  23.510  64.544  1.00102.67           N  
ANISOU 2941  N   LYS A 388    14322  15653   9036   -512   -663  -1631       N  
ATOM   2942  CA  LYS A 388      35.987  24.005  65.809  1.00107.64           C  
ANISOU 2942  CA  LYS A 388    14865  16586   9449   -358   -738  -1928       C  
ATOM   2943  C   LYS A 388      37.254  23.234  66.182  1.00107.69           C  
ANISOU 2943  C   LYS A 388    14962  16704   9251   -259   -880  -1861       C  
ATOM   2944  O   LYS A 388      38.291  23.841  66.459  1.00103.63           O  
ANISOU 2944  O   LYS A 388    14355  16243   8777   -175  -1010  -2139       O  
ATOM   2945  CB  LYS A 388      34.961  23.926  66.951  1.00109.36           C  
ANISOU 2945  CB  LYS A 388    15052  17159   9342   -313   -616  -1954       C  
ATOM   2946  N   GLN A 389      37.162  21.903  66.164  1.00108.80           N  
ANISOU 2946  N   GLN A 389    15257  16845   9237   -269   -871  -1494       N  
ATOM   2947  CA  GLN A 389      38.299  21.036  66.495  1.00113.95           C  
ANISOU 2947  CA  GLN A 389    15972  17551   9773   -177  -1031  -1378       C  
ATOM   2948  C   GLN A 389      39.481  21.235  65.546  1.00109.23           C  
ANISOU 2948  C   GLN A 389    15341  16693   9470   -188  -1144  -1541       C  
ATOM   2949  O   GLN A 389      40.629  21.400  65.980  1.00104.78           O  
ANISOU 2949  O   GLN A 389    14732  16222   8858    -83  -1294  -1712       O  
ATOM   2950  CB  GLN A 389      37.883  19.555  66.488  1.00118.52           C  
ANISOU 2950  CB  GLN A 389    16671  18066  10296   -207  -1018   -929       C  
ATOM   2951  CG  GLN A 389      37.451  19.013  67.851  1.00123.57           C  
ANISOU 2951  CG  GLN A 389    17323  19098  10531   -151  -1024   -672       C  
ATOM   2952  CD  GLN A 389      37.100  17.532  67.808  1.00127.09           C  
ANISOU 2952  CD  GLN A 389    17846  19408  11034   -194  -1049   -169       C  
ATOM   2953  NE2 GLN A 389      36.821  16.958  68.975  1.00126.10           N  
ANISOU 2953  NE2 GLN A 389    17707  19641  10567   -172  -1086    164       N  
ATOM   2954  OE1 GLN A 389      37.077  16.911  66.736  1.00126.30           O  
ANISOU 2954  OE1 GLN A 389    17785  18907  11298   -256  -1044    -83       O  
ATOM   2955  N   ASN A 390      39.193  21.215  64.251  1.00104.49           N  
ANISOU 2955  N   ASN A 390    14739  15813   9149   -329  -1071  -1489       N  
ATOM   2956  CA  ASN A 390      40.233  21.418  63.255  1.00100.42           C  
ANISOU 2956  CA  ASN A 390    14152  15129   8876   -382  -1151  -1635       C  
ATOM   2957  C   ASN A 390      40.820  22.832  63.245  1.00 98.27           C  
ANISOU 2957  C   ASN A 390    13730  14872   8734   -381  -1211  -1939       C  
ATOM   2958  O   ASN A 390      42.003  23.012  62.960  1.00 97.72           O  
ANISOU 2958  O   ASN A 390    13589  14769   8770   -362  -1324  -2093       O  
ATOM   2959  CB  ASN A 390      39.727  21.005  61.878  1.00100.18           C  
ANISOU 2959  CB  ASN A 390    14115  14906   9043   -560  -1054  -1498       C  
ATOM   2960  CG  ASN A 390      39.783  19.499  61.692  1.00100.67           C  
ANISOU 2960  CG  ASN A 390    14250  14879   9119   -542  -1071  -1317       C  
ATOM   2961  ND2 ASN A 390      38.655  18.883  61.366  1.00100.85           N  
ANISOU 2961  ND2 ASN A 390    14326  14823   9169   -624   -954  -1106       N  
ATOM   2962  OD1 ASN A 390      40.832  18.899  61.878  1.00 99.65           O  
ANISOU 2962  OD1 ASN A 390    14105  14731   9025   -449  -1204  -1377       O  
ATOM   2963  N   CYS A 391      40.013  23.827  63.586  1.00 96.99           N  
ANISOU 2963  N   CYS A 391    13491  14746   8614   -396  -1146  -2044       N  
ATOM   2964  CA  CYS A 391      40.524  25.192  63.694  1.00 95.53           C  
ANISOU 2964  CA  CYS A 391    13115  14529   8651   -382  -1229  -2353       C  
ATOM   2965  C   CYS A 391      41.394  25.374  64.926  1.00 93.45           C  
ANISOU 2965  C   CYS A 391    12815  14496   8195   -191  -1351  -2630       C  
ATOM   2966  O   CYS A 391      42.403  26.080  64.874  1.00 89.58           O  
ANISOU 2966  O   CYS A 391    12191  13956   7888   -161  -1474  -2871       O  
ATOM   2967  CB  CYS A 391      39.387  26.202  63.661  1.00 96.00           C  
ANISOU 2967  CB  CYS A 391    13045  14506   8925   -451  -1148  -2423       C  
ATOM   2968  SG  CYS A 391      38.770  26.460  61.971  1.00 96.17           S  
ANISOU 2968  SG  CYS A 391    13004  14239   9298   -713  -1086  -2131       S  
ATOM   2969  N   ASP A 392      41.036  24.706  66.016  1.00 96.18           N  
ANISOU 2969  N   ASP A 392    13259  15126   8159    -78  -1328  -2570       N  
ATOM   2970  CA  ASP A 392      41.903  24.674  67.204  1.00100.19           C  
ANISOU 2970  CA  ASP A 392    13733  15945   8391     91  -1462  -2770       C  
ATOM   2971  C   ASP A 392      43.231  24.026  66.839  1.00 98.06           C  
ANISOU 2971  C   ASP A 392    13520  15568   8170    129  -1609  -2698       C  
ATOM   2972  O   ASP A 392      44.297  24.573  67.113  1.00 93.19           O  
ANISOU 2972  O   ASP A 392    12794  14996   7617    211  -1746  -2977       O  
ATOM   2973  CB  ASP A 392      41.254  23.899  68.357  1.00104.04           C  
ANISOU 2973  CB  ASP A 392    14303  16823   8406    160  -1417  -2588       C  
ATOM   2974  CG  ASP A 392      40.005  24.578  68.901  1.00108.55           C  
ANISOU 2974  CG  ASP A 392    14768  17597   8877    138  -1268  -2752       C  
ATOM   2975  OD1 ASP A 392      39.589  25.627  68.362  1.00109.43           O  
ANISOU 2975  OD1 ASP A 392    14743  17480   9353     78  -1213  -2997       O  
ATOM   2976  OD2 ASP A 392      39.426  24.049  69.872  1.00115.03           O1-
ANISOU 2976  OD2 ASP A 392    15613  18820   9272    169  -1213  -2620       O1-
ATOM   2977  N   GLN A 393      43.154  22.862  66.197  1.00 98.58           N  
ANISOU 2977  N   GLN A 393    13726  15478   8252     70  -1583  -2359       N  
ATOM   2978  CA  GLN A 393      44.351  22.145  65.759  1.00 99.37           C  
ANISOU 2978  CA  GLN A 393    13844  15448   8463    100  -1716  -2323       C  
ATOM   2979  C   GLN A 393      45.198  23.002  64.804  1.00 97.15           C  
ANISOU 2979  C   GLN A 393    13428  14984   8501     24  -1750  -2578       C  
ATOM   2980  O   GLN A 393      46.434  22.934  64.838  1.00 95.14           O  
ANISOU 2980  O   GLN A 393    13115  14726   8308     94  -1891  -2729       O  
ATOM   2981  CB  GLN A 393      43.973  20.815  65.111  1.00101.67           C  
ANISOU 2981  CB  GLN A 393    14243  15561   8824     34  -1669  -1991       C  
ATOM   2982  CG  GLN A 393      45.104  19.793  65.041  1.00104.68           C  
ANISOU 2982  CG  GLN A 393    14618  15847   9307    112  -1837  -1944       C  
ATOM   2983  CD  GLN A 393      44.649  18.467  64.438  1.00110.28           C  
ANISOU 2983  CD  GLN A 393    15377  16343  10181     53  -1803  -1670       C  
ATOM   2984  NE2 GLN A 393      45.613  17.637  64.021  1.00110.28           N  
ANISOU 2984  NE2 GLN A 393    15306  16172  10423     92  -1935  -1720       N  
ATOM   2985  OE1 GLN A 393      43.443  18.192  64.338  1.00112.74           O  
ANISOU 2985  OE1 GLN A 393    15762  16630  10446    -25  -1666  -1451       O  
ATOM   2986  N   PHE A 394      44.539  23.831  63.990  1.00 93.25           N  
ANISOU 2986  N   PHE A 394    12860  14354   8217   -129  -1635  -2599       N  
ATOM   2987  CA  PHE A 394      45.254  24.768  63.121  1.00 93.11           C  
ANISOU 2987  CA  PHE A 394    12669  14200   8508   -238  -1676  -2764       C  
ATOM   2988  C   PHE A 394      45.904  25.887  63.925  1.00 93.76           C  
ANISOU 2988  C   PHE A 394    12601  14348   8677   -128  -1797  -3099       C  
ATOM   2989  O   PHE A 394      47.095  26.173  63.746  1.00 92.90           O  
ANISOU 2989  O   PHE A 394    12385  14207   8705   -111  -1913  -3268       O  
ATOM   2990  CB  PHE A 394      44.338  25.376  62.048  1.00 92.85           C  
ANISOU 2990  CB  PHE A 394    12559  14018   8701   -453  -1554  -2615       C  
ATOM   2991  CG  PHE A 394      44.933  26.584  61.367  1.00 92.36           C  
ANISOU 2991  CG  PHE A 394    12265  13845   8983   -580  -1621  -2722       C  
ATOM   2992  CD1 PHE A 394      45.986  26.444  60.477  1.00 92.03           C  
ANISOU 2992  CD1 PHE A 394    12130  13805   9033   -687  -1669  -2721       C  
ATOM   2993  CD2 PHE A 394      44.469  27.867  61.652  1.00 92.43           C  
ANISOU 2993  CD2 PHE A 394    12107  13748   9264   -597  -1650  -2836       C  
ATOM   2994  CE1 PHE A 394      46.557  27.556  59.873  1.00 92.40           C  
ANISOU 2994  CE1 PHE A 394    11936  13775   9398   -828  -1739  -2757       C  
ATOM   2995  CE2 PHE A 394      45.034  28.979  61.047  1.00 92.15           C  
ANISOU 2995  CE2 PHE A 394    11819  13565   9628   -725  -1744  -2879       C  
ATOM   2996  CZ  PHE A 394      46.076  28.825  60.151  1.00 90.86           C  
ANISOU 2996  CZ  PHE A 394    11579  13429   9516   -851  -1787  -2802       C  
ATOM   2997  N   GLU A 395      45.113  26.524  64.794  1.00 94.71           N  
ANISOU 2997  N   GLU A 395    12679  14569   8736    -58  -1766  -3234       N  
ATOM   2998  CA  GLU A 395      45.610  27.597  65.663  1.00 95.98           C  
ANISOU 2998  CA  GLU A 395    12649  14821   8997     60  -1881  -3642       C  
ATOM   2999  C   GLU A 395      46.855  27.121  66.416  1.00 97.59           C  
ANISOU 2999  C   GLU A 395    12883  15226   8970    224  -2034  -3794       C  
ATOM   3000  O   GLU A 395      47.834  27.850  66.520  1.00 98.57           O  
ANISOU 3000  O   GLU A 395    12840  15311   9299    269  -2163  -4084       O  
ATOM   3001  CB  GLU A 395      44.519  28.069  66.636  1.00 94.96           C  
ANISOU 3001  CB  GLU A 395    12460  14878   8741    132  -1810  -3821       C  
ATOM   3002  N   LYS A 396      46.816  25.881  66.898  1.00 99.81           N  
ANISOU 3002  N   LYS A 396    13356  15695   8871    302  -2036  -3563       N  
ATOM   3003  CA  LYS A 396      47.901  25.288  67.697  1.00103.74           C  
ANISOU 3003  CA  LYS A 396    13881  16403   9133    460  -2208  -3625       C  
ATOM   3004  C   LYS A 396      49.194  25.064  66.915  1.00103.06           C  
ANISOU 3004  C   LYS A 396    13760  16105   9294    441  -2316  -3657       C  
ATOM   3005  O   LYS A 396      50.275  25.387  67.400  1.00107.32           O  
ANISOU 3005  O   LYS A 396    14195  16732   9849    550  -2475  -3915       O  
ATOM   3006  CB  LYS A 396      47.437  23.943  68.287  1.00105.13           C  
ANISOU 3006  CB  LYS A 396    14240  16775   8931    512  -2202  -3251       C  
ATOM   3007  CG  LYS A 396      48.366  23.342  69.334  1.00107.06           C  
ANISOU 3007  CG  LYS A 396    14484  17305   8891    672  -2407  -3237       C  
ATOM   3008  CD  LYS A 396      47.665  22.277  70.167  1.00108.26           C  
ANISOU 3008  CD  LYS A 396    14750  17735   8647    701  -2409  -2828       C  
ATOM   3009  CE  LYS A 396      48.511  21.855  71.357  1.00112.41           C  
ANISOU 3009  CE  LYS A 396    15225  18643   8843    843  -2637  -2785       C  
ATOM   3010  NZ  LYS A 396      47.681  21.316  72.476  1.00115.63           N1+
ANISOU 3010  NZ  LYS A 396    15655  19530   8750    848  -2627  -2464       N1+
ATOM   3011  N   LEU A 397      49.072  24.508  65.710  1.00101.91           N  
ANISOU 3011  N   LEU A 397    13675  15717   9328    299  -2227  -3429       N  
ATOM   3012  CA  LEU A 397      50.224  24.029  64.939  1.00 96.60           C  
ANISOU 3012  CA  LEU A 397    12956  14907   8839    270  -2306  -3457       C  
ATOM   3013  C   LEU A 397      50.681  24.984  63.846  1.00 96.41           C  
ANISOU 3013  C   LEU A 397    12753  14730   9149    104  -2268  -3600       C  
ATOM   3014  O   LEU A 397      51.836  24.922  63.426  1.00 94.70           O  
ANISOU 3014  O   LEU A 397    12432  14477   9073     95  -2354  -3736       O  
ATOM   3015  CB  LEU A 397      49.882  22.688  64.296  1.00 92.74           C  
ANISOU 3015  CB  LEU A 397    12586  14314   8339    212  -2241  -3171       C  
ATOM   3016  CG  LEU A 397      49.649  21.554  65.286  1.00 94.09           C  
ANISOU 3016  CG  LEU A 397    12892  14587   8269    359  -2327  -2942       C  
ATOM   3017  CD1 LEU A 397      48.841  20.450  64.631  1.00 90.78           C  
ANISOU 3017  CD1 LEU A 397    12565  14011   7915    270  -2221  -2647       C  
ATOM   3018  CD2 LEU A 397      50.979  21.032  65.806  1.00 94.53           C  
ANISOU 3018  CD2 LEU A 397    12893  14676   8347    512  -2552  -3038       C  
ATOM   3019  N   GLY A 398      49.782  25.852  63.375  1.00 97.22           N  
ANISOU 3019  N   GLY A 398    12795  14750   9395    -41  -2152  -3540       N  
ATOM   3020  CA  GLY A 398      50.045  26.672  62.187  1.00 96.00           C  
ANISOU 3020  CA  GLY A 398    12449  14463   9565   -257  -2117  -3526       C  
ATOM   3021  C   GLY A 398      49.981  25.821  60.927  1.00 95.20           C  
ANISOU 3021  C   GLY A 398    12372  14361   9440   -435  -2010  -3311       C  
ATOM   3022  O   GLY A 398      49.937  24.591  61.006  1.00 94.38           O  
ANISOU 3022  O   GLY A 398    12411  14295   9153   -360  -1991  -3245       O  
ATOM   3023  N   GLU A 399      50.000  26.469  59.762  1.00 94.53           N  
ANISOU 3023  N   GLU A 399    12106  14252   9560   -681  -1954  -3204       N  
ATOM   3024  CA  GLU A 399      49.788  25.780  58.478  1.00 90.98           C  
ANISOU 3024  CA  GLU A 399    11625  13898   9047   -892  -1832  -3026       C  
ATOM   3025  C   GLU A 399      50.628  24.507  58.316  1.00 90.29           C  
ANISOU 3025  C   GLU A 399    11570  13899   8838   -814  -1851  -3183       C  
ATOM   3026  O   GLU A 399      50.073  23.411  58.197  1.00 88.76           O  
ANISOU 3026  O   GLU A 399    11499  13704   8521   -784  -1783  -3112       O  
ATOM   3027  CB  GLU A 399      50.042  26.732  57.294  1.00 91.82           C  
ANISOU 3027  CB  GLU A 399    11458  14073   9355  -1186  -1812  -2894       C  
ATOM   3028  CG  GLU A 399      49.783  26.107  55.927  1.00 91.75           C  
ANISOU 3028  CG  GLU A 399    11364  14284   9214  -1439  -1680  -2731       C  
ATOM   3029  CD  GLU A 399      49.533  27.132  54.831  1.00 92.74           C  
ANISOU 3029  CD  GLU A 399    11231  14523   9484  -1770  -1655  -2435       C  
ATOM   3030  OE1 GLU A 399      48.632  27.974  54.998  1.00 93.13           O  
ANISOU 3030  OE1 GLU A 399    11275  14400   9712  -1816  -1673  -2212       O  
ATOM   3031  OE2 GLU A 399      50.206  27.077  53.782  1.00 92.16           O1-
ANISOU 3031  OE2 GLU A 399    10931  14735   9350  -1999  -1621  -2410       O1-
ATOM   3032  N   TYR A 400      51.954  24.648  58.318  1.00 81.15           N  
ANISOU 3032  N   TYR A 400    10636  11319   8877   -197  -1597  -2132       N  
ATOM   3033  CA  TYR A 400      52.836  23.526  57.978  1.00 78.55           C  
ANISOU 3033  CA  TYR A 400    10291  11009   8546   -208  -1632  -1977       C  
ATOM   3034  C   TYR A 400      52.603  22.342  58.893  1.00 79.37           C  
ANISOU 3034  C   TYR A 400    10545  11341   8273    -91  -1676  -1888       C  
ATOM   3035  O   TYR A 400      52.272  21.256  58.427  1.00 78.72           O  
ANISOU 3035  O   TYR A 400    10540  11291   8079   -107  -1560  -1644       O  
ATOM   3036  CB  TYR A 400      54.298  23.928  58.033  1.00 79.33           C  
ANISOU 3036  CB  TYR A 400    10217  11011   8915   -224  -1812  -2137       C  
ATOM   3037  CG  TYR A 400      55.219  22.782  57.737  1.00 79.12           C  
ANISOU 3037  CG  TYR A 400    10169  11007   8886   -222  -1843  -1978       C  
ATOM   3038  CD1 TYR A 400      55.151  22.111  56.529  1.00 81.28           C  
ANISOU 3038  CD1 TYR A 400    10457  11190   9236   -295  -1662  -1724       C  
ATOM   3039  CD2 TYR A 400      56.153  22.362  58.662  1.00 81.74           C  
ANISOU 3039  CD2 TYR A 400    10474  11451   9133   -134  -2059  -2087       C  
ATOM   3040  CE1 TYR A 400      55.994  21.051  56.251  1.00 83.09           C  
ANISOU 3040  CE1 TYR A 400    10674  11433   9465   -283  -1682  -1581       C  
ATOM   3041  CE2 TYR A 400      57.002  21.311  58.401  1.00 83.45           C  
ANISOU 3041  CE2 TYR A 400    10665  11685   9358   -127  -2083  -1935       C  
ATOM   3042  CZ  TYR A 400      56.924  20.657  57.198  1.00 85.00           C  
ANISOU 3042  CZ  TYR A 400    10875  11782   9638   -203  -1887  -1683       C  
ATOM   3043  OH  TYR A 400      57.776  19.602  56.946  1.00 86.42           O  
ANISOU 3043  OH  TYR A 400    11035  11972   9827   -185  -1904  -1537       O  
ATOM   3044  N   GLY A 401      52.756  22.559  60.194  1.00 80.29           N  
ANISOU 3044  N   GLY A 401    10704  11609   8193     39  -1843  -2084       N  
ATOM   3045  CA  GLY A 401      52.491  21.515  61.179  1.00 81.18           C  
ANISOU 3045  CA  GLY A 401    10967  11955   7925    182  -1874  -1994       C  
ATOM   3046  C   GLY A 401      51.107  20.897  61.045  1.00 83.98           C  
ANISOU 3046  C   GLY A 401    11458  12379   8073    191  -1652  -1758       C  
ATOM   3047  O   GLY A 401      50.944  19.693  61.251  1.00 86.84           O  
ANISOU 3047  O   GLY A 401    11908  12853   8235    244  -1602  -1553       O  
ATOM   3048  N   PHE A 402      50.110  21.720  60.704  1.00 83.52           N  
ANISOU 3048  N   PHE A 402    11405  12242   8085    139  -1520  -1781       N  
ATOM   3049  CA  PHE A 402      48.723  21.258  60.531  1.00 80.71           C  
ANISOU 3049  CA  PHE A 402    11150  11927   7587    138  -1311  -1564       C  
ATOM   3050  C   PHE A 402      48.615  20.316  59.331  1.00 81.54           C  
ANISOU 3050  C   PHE A 402    11243  11926   7813     16  -1192  -1299       C  
ATOM   3051  O   PHE A 402      47.946  19.280  59.407  1.00 86.90           O  
ANISOU 3051  O   PHE A 402    12008  12679   8333     43  -1093  -1081       O  
ATOM   3052  CB  PHE A 402      47.753  22.461  60.398  1.00 78.24           C  
ANISOU 3052  CB  PHE A 402    10826  11541   7361    109  -1212  -1666       C  
ATOM   3053  CG  PHE A 402      46.294  22.086  60.243  1.00 75.46           C  
ANISOU 3053  CG  PHE A 402    10554  11221   6899    108  -1005  -1450       C  
ATOM   3054  CD1 PHE A 402      45.709  21.118  61.040  1.00 76.48           C  
ANISOU 3054  CD1 PHE A 402    10794  11523   6742    225   -940  -1288       C  
ATOM   3055  CD2 PHE A 402      45.493  22.731  59.304  1.00 73.58           C  
ANISOU 3055  CD2 PHE A 402    10266  10830   6860     -5   -872  -1400       C  
ATOM   3056  CE1 PHE A 402      44.365  20.782  60.891  1.00 76.09           C  
ANISOU 3056  CE1 PHE A 402    10789  11481   6641    219   -748  -1079       C  
ATOM   3057  CE2 PHE A 402      44.151  22.400  59.156  1.00 70.44           C  
ANISOU 3057  CE2 PHE A 402     9920  10451   6392     -9   -699  -1205       C  
ATOM   3058  CZ  PHE A 402      43.583  21.426  59.952  1.00 71.63           C  
ANISOU 3058  CZ  PHE A 402    10166  10762   6288     98   -637  -1045       C  
ATOM   3059  N   GLN A 403      49.265  20.658  58.226  1.00 79.71           N  
ANISOU 3059  N   GLN A 403    10906  11514   7867   -107  -1199  -1315       N  
ATOM   3060  CA  GLN A 403      49.281  19.755  57.064  1.00 77.46           C  
ANISOU 3060  CA  GLN A 403    10625  11129   7678   -198  -1105  -1087       C  
ATOM   3061  C   GLN A 403      49.870  18.398  57.439  1.00 78.83           C  
ANISOU 3061  C   GLN A 403    10850  11404   7697   -138  -1163   -961       C  
ATOM   3062  O   GLN A 403      49.403  17.369  56.977  1.00 79.42           O  
ANISOU 3062  O   GLN A 403    10989  11468   7720   -162  -1073   -749       O  
ATOM   3063  CB  GLN A 403      50.115  20.322  55.939  1.00 73.81           C  
ANISOU 3063  CB  GLN A 403    10045  10477   7521   -298  -1109  -1130       C  
ATOM   3064  CG  GLN A 403      49.605  21.622  55.367  1.00 74.66           C  
ANISOU 3064  CG  GLN A 403    10088  10453   7824   -365  -1033  -1218       C  
ATOM   3065  CD  GLN A 403      50.572  22.189  54.359  1.00 75.72           C  
ANISOU 3065  CD  GLN A 403    10095  10407   8270   -439  -1030  -1248       C  
ATOM   3066  NE2 GLN A 403      50.060  22.989  53.419  1.00 74.33           N  
ANISOU 3066  NE2 GLN A 403     9879  10089   8273   -506   -909  -1217       N  
ATOM   3067  OE1 GLN A 403      51.762  21.874  54.389  1.00 74.95           O  
ANISOU 3067  OE1 GLN A 403     9928  10292   8255   -428  -1123  -1275       O  
ATOM   3068  N   ASN A 404      50.895  18.409  58.283  1.00 80.98           N  
ANISOU 3068  N   ASN A 404    11091  11768   7911    -56  -1326  -1098       N  
ATOM   3069  CA  ASN A 404      51.573  17.178  58.685  1.00 83.98           C  
ANISOU 3069  CA  ASN A 404    11508  12246   8156     13  -1394   -985       C  
ATOM   3070  C   ASN A 404      50.706  16.284  59.587  1.00 83.82           C  
ANISOU 3070  C   ASN A 404    11619  12401   7829    124  -1334   -837       C  
ATOM   3071  O   ASN A 404      50.910  15.069  59.654  1.00 82.02           O  
ANISOU 3071  O   ASN A 404    11435  12221   7509    159  -1321   -658       O  
ATOM   3072  CB  ASN A 404      52.917  17.500  59.370  1.00 86.60           C  
ANISOU 3072  CB  ASN A 404    11756  12629   8521     79  -1606  -1182       C  
ATOM   3073  CG  ASN A 404      53.906  18.183  58.435  1.00 87.43           C  
ANISOU 3073  CG  ASN A 404    11704  12541   8975    -28  -1650  -1277       C  
ATOM   3074  ND2 ASN A 404      54.855  18.920  58.998  1.00 87.75           N  
ANISOU 3074  ND2 ASN A 404    11636  12583   9123      6  -1836  -1504       N  
ATOM   3075  OD1 ASN A 404      53.808  18.053  57.219  1.00 92.47           O  
ANISOU 3075  OD1 ASN A 404    12317  13027   9789   -131  -1517  -1145       O  
ATOM   3076  N   ALA A 405      49.753  16.892  60.288  1.00 83.51           N  
ANISOU 3076  N   ALA A 405    11634  12451   7644    188  -1285   -901       N  
ATOM   3077  CA  ALA A 405      48.785  16.132  61.064  1.00 80.58           C  
ANISOU 3077  CA  ALA A 405    11376  12228   7013    296  -1180   -728       C  
ATOM   3078  C   ALA A 405      47.799  15.487  60.082  1.00 75.89           C  
ANISOU 3078  C   ALA A 405    10794  11510   6529    182  -1002   -486       C  
ATOM   3079  O   ALA A 405      47.435  14.319  60.229  1.00 79.18           O  
ANISOU 3079  O   ALA A 405    11263  11969   6851    216   -929   -263       O  
ATOM   3080  CB  ALA A 405      48.062  17.030  62.067  1.00 76.33           C  
ANISOU 3080  CB  ALA A 405    10893  11814   6297    413  -1163   -868       C  
ATOM   3081  N   LEU A 406      47.369  16.255  59.085  1.00 71.27           N  
ANISOU 3081  N   LEU A 406    10157  10768   6157     53   -941   -531       N  
ATOM   3082  CA  LEU A 406      46.423  15.746  58.104  1.00 70.56           C  
ANISOU 3082  CA  LEU A 406    10076  10554   6180    -51   -805   -333       C  
ATOM   3083  C   LEU A 406      47.029  14.585  57.302  1.00 68.89           C  
ANISOU 3083  C   LEU A 406     9867  10254   6054   -109   -825   -187       C  
ATOM   3084  O   LEU A 406      46.348  13.594  57.057  1.00 70.80           O  
ANISOU 3084  O   LEU A 406    10149  10466   6286   -127   -746     15       O  
ATOM   3085  CB  LEU A 406      45.942  16.861  57.181  1.00 66.96           C  
ANISOU 3085  CB  LEU A 406     9565   9953   5923   -159   -754   -422       C  
ATOM   3086  CG  LEU A 406      45.058  17.923  57.817  1.00 66.70           C  
ANISOU 3086  CG  LEU A 406     9533   9977   5831   -114   -697   -527       C  
ATOM   3087  CD1 LEU A 406      44.964  19.158  56.927  1.00 65.44           C  
ANISOU 3087  CD1 LEU A 406     9300   9667   5897   -213   -679   -654       C  
ATOM   3088  CD2 LEU A 406      43.687  17.328  58.028  1.00 65.60           C  
ANISOU 3088  CD2 LEU A 406     9442   9876   5608    -92   -555   -321       C  
ATOM   3089  N   ILE A 407      48.308  14.694  56.949  1.00 69.95           N  
ANISOU 3089  N   ILE A 407     9953  10342   6284   -128   -930   -289       N  
ATOM   3090  CA  ILE A 407      49.046  13.603  56.313  1.00 69.42           C  
ANISOU 3090  CA  ILE A 407     9893  10206   6279   -154   -953   -167       C  
ATOM   3091  C   ILE A 407      48.918  12.329  57.128  1.00 71.48           C  
ANISOU 3091  C   ILE A 407    10218  10582   6358    -64   -946      0       C  
ATOM   3092  O   ILE A 407      48.580  11.271  56.611  1.00 73.90           O  
ANISOU 3092  O   ILE A 407    10562  10816   6700    -97   -888    182       O  
ATOM   3093  CB  ILE A 407      50.546  13.931  56.189  1.00 72.74           C  
ANISOU 3093  CB  ILE A 407    10236  10601   6801   -148  -1072   -304       C  
ATOM   3094  CG1 ILE A 407      50.784  14.944  55.066  1.00 72.67           C  
ANISOU 3094  CG1 ILE A 407    10153  10427   7032   -247  -1044   -402       C  
ATOM   3095  CG2 ILE A 407      51.363  12.671  55.913  1.00 75.13           C  
ANISOU 3095  CG2 ILE A 407    10555  10882   7110   -130  -1099   -171       C  
ATOM   3096  CD1 ILE A 407      52.210  14.992  54.567  1.00 72.83           C  
ANISOU 3096  CD1 ILE A 407    10086  10367   7220   -258  -1112   -456       C  
ATOM   3097  N   VAL A 408      49.204  12.448  58.413  1.00 75.38           N  
ANISOU 3097  N   VAL A 408    10726  11254   6659     62  -1012    -66       N  
ATOM   3098  CA  VAL A 408      49.082  11.342  59.347  1.00 77.85           C  
ANISOU 3098  CA  VAL A 408    11102  11703   6773    181   -995    100       C  
ATOM   3099  C   VAL A 408      47.668  10.779  59.348  1.00 77.66           C  
ANISOU 3099  C   VAL A 408    11124  11661   6721    170   -835    308       C  
ATOM   3100  O   VAL A 408      47.467   9.577  59.146  1.00 75.50           O  
ANISOU 3100  O   VAL A 408    10873  11339   6473    162   -780    516       O  
ATOM   3101  CB  VAL A 408      49.505  11.780  60.781  1.00 79.65           C  
ANISOU 3101  CB  VAL A 408    11354  12147   6763    347  -1095    -32       C  
ATOM   3102  CG1 VAL A 408      48.728  11.027  61.865  1.00 79.21           C  
ANISOU 3102  CG1 VAL A 408    11384  12253   6458    494   -999    155       C  
ATOM   3103  CG2 VAL A 408      51.013  11.634  60.939  1.00 79.60           C  
ANISOU 3103  CG2 VAL A 408    11300  12171   6772    386  -1269   -138       C  
ATOM   3104  N   ARG A 409      46.691  11.650  59.566  1.00 79.15           N  
ANISOU 3104  N   ARG A 409    11315  11873   6884    168   -760    253       N  
ATOM   3105  CA  ARG A 409      45.303  11.214  59.651  1.00 79.55           C  
ANISOU 3105  CA  ARG A 409    11386  11908   6931    165   -604    453       C  
ATOM   3106  C   ARG A 409      44.871  10.507  58.367  1.00 78.72           C  
ANISOU 3106  C   ARG A 409    11258  11597   7056     18   -562    592       C  
ATOM   3107  O   ARG A 409      44.315   9.417  58.414  1.00 83.85           O  
ANISOU 3107  O   ARG A 409    11918  12213   7730     23   -489    810       O  
ATOM   3108  CB  ARG A 409      44.395  12.406  59.914  1.00 82.01           C  
ANISOU 3108  CB  ARG A 409    11690  12252   7219    174   -535    348       C  
ATOM   3109  CG  ARG A 409      42.979  12.019  60.311  1.00 84.61           C  
ANISOU 3109  CG  ARG A 409    12029  12603   7517    212   -362    561       C  
ATOM   3110  CD  ARG A 409      42.012  13.180  60.164  1.00 86.43           C  
ANISOU 3110  CD  ARG A 409    12231  12801   7808    176   -284    472       C  
ATOM   3111  NE  ARG A 409      42.485  14.388  60.836  1.00 87.81           N  
ANISOU 3111  NE  ARG A 409    12428  13091   7844    263   -352    218       N  
ATOM   3112  CZ  ARG A 409      41.850  15.553  60.805  1.00 92.74           C  
ANISOU 3112  CZ  ARG A 409    13033  13696   8509    249   -304     92       C  
ATOM   3113  NH1 ARG A 409      40.705  15.693  60.133  1.00 94.40           N1+
ANISOU 3113  NH1 ARG A 409    13195  13787   8886    153   -185    205       N1+
ATOM   3114  NH2 ARG A 409      42.362  16.588  61.451  1.00 97.29           N  
ANISOU 3114  NH2 ARG A 409    13632  14365   8969    334   -385   -155       N  
ATOM   3115  N   TYR A 410      45.133  11.128  57.224  1.00 73.58           N  
ANISOU 3115  N   TYR A 410    10575  10805   6577   -103   -610    466       N  
ATOM   3116  CA  TYR A 410      44.651  10.596  55.954  1.00 73.54           C  
ANISOU 3116  CA  TYR A 410    10566  10610   6767   -224   -585    567       C  
ATOM   3117  C   TYR A 410      45.464   9.377  55.455  1.00 72.85           C  
ANISOU 3117  C   TYR A 410    10504  10445   6729   -236   -640    657       C  
ATOM   3118  O   TYR A 410      44.893   8.479  54.841  1.00 70.30           O  
ANISOU 3118  O   TYR A 410    10197   9998   6516   -290   -614    800       O  
ATOM   3119  CB  TYR A 410      44.509  11.719  54.889  1.00 70.91           C  
ANISOU 3119  CB  TYR A 410    10203  10161   6580   -324   -596    423       C  
ATOM   3120  CG  TYR A 410      43.154  12.439  54.967  1.00 71.64           C  
ANISOU 3120  CG  TYR A 410    10270  10247   6704   -351   -507    438       C  
ATOM   3121  CD1 TYR A 410      42.918  13.441  55.910  1.00 74.70           C  
ANISOU 3121  CD1 TYR A 410    10641  10760   6980   -281   -472    331       C  
ATOM   3122  CD2 TYR A 410      42.103  12.089  54.118  1.00 70.92           C  
ANISOU 3122  CD2 TYR A 410    10169  10019   6758   -435   -466    557       C  
ATOM   3123  CE1 TYR A 410      41.681  14.077  55.994  1.00 75.79           C  
ANISOU 3123  CE1 TYR A 410    10753  10891   7154   -296   -376    357       C  
ATOM   3124  CE2 TYR A 410      40.863  12.719  54.191  1.00 70.94           C  
ANISOU 3124  CE2 TYR A 410    10132  10011   6810   -458   -385    585       C  
ATOM   3125  CZ  TYR A 410      40.657  13.712  55.127  1.00 74.76           C  
ANISOU 3125  CZ  TYR A 410    10599  10623   7184   -387   -329    492       C  
ATOM   3126  OH  TYR A 410      39.430  14.339  55.201  1.00 77.91           O  
ANISOU 3126  OH  TYR A 410    10955  11008   7639   -401   -235    527       O  
ATOM   3127  N   THR A 411      46.765   9.323  55.741  1.00 71.34           N  
ANISOU 3127  N   THR A 411    10314  10320   6472   -180   -723    574       N  
ATOM   3128  CA  THR A 411      47.561   8.153  55.382  1.00 70.79           C  
ANISOU 3128  CA  THR A 411    10268  10188   6441   -172   -764    667       C  
ATOM   3129  C   THR A 411      47.127   6.918  56.169  1.00 75.51           C  
ANISOU 3129  C   THR A 411    10891  10838   6959   -103   -714    880       C  
ATOM   3130  O   THR A 411      47.139   5.799  55.637  1.00 74.40           O  
ANISOU 3130  O   THR A 411    10773  10580   6917   -132   -708   1011       O  
ATOM   3131  CB  THR A 411      49.054   8.389  55.604  1.00 72.06           C  
ANISOU 3131  CB  THR A 411    10404  10414   6564   -120   -862    543       C  
ATOM   3132  CG2 THR A 411      49.898   7.266  54.988  1.00 72.19           C  
ANISOU 3132  CG2 THR A 411    10441  10333   6656   -121   -892    632       C  
ATOM   3133  OG1 THR A 411      49.418   9.612  54.970  1.00 72.03           O  
ANISOU 3133  OG1 THR A 411    10354  10354   6659   -178   -891    360       O  
ATOM   3134  N   ARG A 412      46.731   7.117  57.423  1.00 77.79           N  
ANISOU 3134  N   ARG A 412    11180  11298   7077     -1   -670    918       N  
ATOM   3135  CA  ARG A 412      46.104   6.045  58.210  1.00 81.09           C  
ANISOU 3135  CA  ARG A 412    11613  11766   7430     77   -580   1156       C  
ATOM   3136  C   ARG A 412      44.727   5.659  57.671  1.00 79.25           C  
ANISOU 3136  C   ARG A 412    11357  11385   7367    -13   -479   1307       C  
ATOM   3137  O   ARG A 412      44.378   4.482  57.639  1.00 81.76           O  
ANISOU 3137  O   ARG A 412    11669  11618   7777    -15   -433   1508       O  
ATOM   3138  CB  ARG A 412      45.936   6.477  59.657  1.00 85.82           C  
ANISOU 3138  CB  ARG A 412    12230  12593   7784    233   -538   1160       C  
ATOM   3139  CG  ARG A 412      47.223   6.459  60.451  1.00 88.26           C  
ANISOU 3139  CG  ARG A 412    12564  13066   7907    360   -649   1073       C  
ATOM   3140  CD  ARG A 412      47.007   6.907  61.888  1.00 89.02           C  
ANISOU 3140  CD  ARG A 412    12701  13398   7725    541   -621   1060       C  
ATOM   3141  NE  ARG A 412      48.246   6.752  62.656  1.00 94.02           N  
ANISOU 3141  NE  ARG A 412    13359  14186   8177    676   -755    987       N  
ATOM   3142  CZ  ARG A 412      48.653   7.547  63.649  1.00 98.33           C  
ANISOU 3142  CZ  ARG A 412    13938  14927   8494    817   -845    817       C  
ATOM   3143  NH1 ARG A 412      47.941   8.605  64.027  1.00 99.32           N1+
ANISOU 3143  NH1 ARG A 412    14086  15121   8532    849   -805    691       N1+
ATOM   3144  NH2 ARG A 412      49.800   7.286  64.267  1.00101.23           N  
ANISOU 3144  NH2 ARG A 412    14319  15421   8724    935   -990    760       N  
ATOM   3145  N   LYS A 413      43.945   6.661  57.285  1.00 77.45           N  
ANISOU 3145  N   LYS A 413    11107  11123   7199    -82   -451   1211       N  
ATOM   3146  CA  LYS A 413      42.599   6.451  56.738  1.00 78.65           C  
ANISOU 3146  CA  LYS A 413    11219  11131   7532   -173   -376   1332       C  
ATOM   3147  C   LYS A 413      42.648   5.670  55.428  1.00 74.35           C  
ANISOU 3147  C   LYS A 413    10681  10367   7202   -289   -448   1358       C  
ATOM   3148  O   LYS A 413      41.914   4.705  55.247  1.00 73.12           O  
ANISOU 3148  O   LYS A 413    10498  10088   7196   -324   -416   1531       O  
ATOM   3149  CB  LYS A 413      41.913   7.791  56.452  1.00 81.69           C  
ANISOU 3149  CB  LYS A 413    11578  11519   7943   -225   -354   1195       C  
ATOM   3150  CG  LYS A 413      41.240   8.492  57.622  1.00 84.69           C  
ANISOU 3150  CG  LYS A 413    11943  12063   8172   -123   -243   1214       C  
ATOM   3151  CD  LYS A 413      40.715   9.856  57.164  1.00 84.05           C  
ANISOU 3151  CD  LYS A 413    11836  11956   8144   -187   -237   1051       C  
ATOM   3152  CE  LYS A 413      39.774  10.503  58.172  1.00 85.30           C  
ANISOU 3152  CE  LYS A 413    11976  12240   8196    -94   -104   1091       C  
ATOM   3153  NZ  LYS A 413      39.447  11.893  57.760  1.00 83.81           N1+
ANISOU 3153  NZ  LYS A 413    11764  12027   8052   -146   -109    908       N1+
ATOM   3154  N   VAL A 414      43.520   6.101  54.522  1.00 69.56           N  
ANISOU 3154  N   VAL A 414    10110   9704   6615   -337   -546   1183       N  
ATOM   3155  CA  VAL A 414      43.579   5.546  53.180  1.00 66.53           C  
ANISOU 3155  CA  VAL A 414     9757   9120   6400   -425   -617   1171       C  
ATOM   3156  C   VAL A 414      45.029   5.325  52.715  1.00 66.15           C  
ANISOU 3156  C   VAL A 414     9760   9060   6315   -398   -692   1076       C  
ATOM   3157  O   VAL A 414      45.527   6.020  51.821  1.00 67.34           O  
ANISOU 3157  O   VAL A 414     9933   9160   6493   -433   -734    931       O  
ATOM   3158  CB  VAL A 414      42.800   6.435  52.191  1.00 66.33           C  
ANISOU 3158  CB  VAL A 414     9724   8997   6484   -516   -633   1073       C  
ATOM   3159  CG1 VAL A 414      41.307   6.243  52.419  1.00 67.73           C  
ANISOU 3159  CG1 VAL A 414     9840   9123   6773   -556   -573   1211       C  
ATOM   3160  CG2 VAL A 414      43.180   7.908  52.328  1.00 62.41           C  
ANISOU 3160  CG2 VAL A 414     9213   8610   5889   -503   -622    899       C  
ATOM   3161  N   PRO A 415      45.705   4.327  53.304  1.00 66.49           N  
ANISOU 3161  N   PRO A 415     9815   9143   6307   -329   -696   1177       N  
ATOM   3162  CA  PRO A 415      47.105   4.030  53.013  1.00 66.42           C  
ANISOU 3162  CA  PRO A 415     9839   9131   6267   -289   -757   1113       C  
ATOM   3163  C   PRO A 415      47.396   3.484  51.630  1.00 66.30           C  
ANISOU 3163  C   PRO A 415     9883   8922   6387   -338   -805   1083       C  
ATOM   3164  O   PRO A 415      48.543   3.531  51.187  1.00 67.62           O  
ANISOU 3164  O   PRO A 415    10073   9077   6542   -307   -837   1005       O  
ATOM   3165  CB  PRO A 415      47.441   2.958  54.035  1.00 67.01           C  
ANISOU 3165  CB  PRO A 415     9907   9283   6271   -199   -736   1273       C  
ATOM   3166  CG  PRO A 415      46.143   2.270  54.251  1.00 68.83           C  
ANISOU 3166  CG  PRO A 415    10119   9442   6594   -227   -669   1450       C  
ATOM   3167  CD  PRO A 415      45.169   3.396  54.310  1.00 68.56           C  
ANISOU 3167  CD  PRO A 415    10051   9451   6547   -273   -629   1382       C  
ATOM   3168  N  AGLN A 416      46.385   2.943  50.959  0.50 66.08           N  
ANISOU 3168  N  AGLN A 416     9879   8738   6491   -403   -812   1146       N  
ATOM   3169  N  BGLN A 416      46.382   2.945  50.964  0.50 65.72           N  
ANISOU 3169  N  BGLN A 416     9833   8693   6445   -402   -812   1146       N  
ATOM   3170  CA AGLN A 416      46.565   2.425  49.610  0.50 65.11           C  
ANISOU 3170  CA AGLN A 416     9835   8429   6476   -431   -874   1099       C  
ATOM   3171  CA BGLN A 416      46.544   2.418  49.623  0.50 64.56           C  
ANISOU 3171  CA BGLN A 416     9764   8358   6407   -431   -874   1101       C  
ATOM   3172  C  AGLN A 416      46.796   3.535  48.594  0.50 63.74           C  
ANISOU 3172  C  AGLN A 416     9697   8233   6290   -452   -890    937       C  
ATOM   3173  C  BGLN A 416      46.779   3.528  48.596  0.50 63.43           C  
ANISOU 3173  C  BGLN A 416     9657   8192   6251   -453   -891    938       C  
ATOM   3174  O  AGLN A 416      47.325   3.282  47.514  0.50 65.43           O  
ANISOU 3174  O  AGLN A 416     9991   8334   6535   -433   -925    878       O  
ATOM   3175  O  BGLN A 416      47.313   3.274  47.520  0.50 65.11           O  
ANISOU 3175  O  BGLN A 416     9951   8294   6496   -434   -925    879       O  
ATOM   3176  CB AGLN A 416      45.320   1.670  49.174  0.50 67.80           C  
ANISOU 3176  CB AGLN A 416    10182   8605   6976   -495   -908   1183       C  
ATOM   3177  CB BGLN A 416      45.284   1.651  49.233  0.50 66.72           C  
ANISOU 3177  CB BGLN A 416    10041   8471   6839   -495   -905   1191       C  
ATOM   3178  CG AGLN A 416      44.776   0.658  50.155  0.50 67.69           C  
ANISOU 3178  CG AGLN A 416    10106   8585   7027   -486   -867   1376       C  
ATOM   3179  CG BGLN A 416      44.587   0.882  50.359  0.50 66.18           C  
ANISOU 3179  CG BGLN A 416     9896   8429   6823   -490   -850   1383       C  
ATOM   3180  CD AGLN A 416      45.171  -0.736  49.741  0.50 66.50           C  
ANISOU 3180  CD AGLN A 416    10005   8274   6988   -467   -917   1442       C  
ATOM   3181  CD BGLN A 416      43.524   1.730  51.045  0.50 63.82           C  
ANISOU 3181  CD BGLN A 416     9514   8230   6505   -519   -781   1421       C  
ATOM   3182  NE2AGLN A 416      44.194  -1.629  49.671  0.50 67.08           N  
ANISOU 3182  NE2AGLN A 416    10044   8189   7256   -516   -940   1558       N  
ATOM   3183  OE1AGLN A 416      46.340  -0.999  49.449  0.50 63.58           O  
ANISOU 3183  OE1AGLN A 416     9697   7908   6553   -409   -936   1388       O  
ATOM   3184  NE2BGLN A 416      42.260   1.344  50.914  0.50 63.99           N  
ANISOU 3184  NE2BGLN A 416     9482   8129   6702   -583   -780   1521       N  
ATOM   3185  OE1BGLN A 416      43.839   2.727  51.662  0.50 60.98           O  
ANISOU 3185  OE1BGLN A 416     9135   8045   5991   -482   -733   1354       O  
ATOM   3186  N   VAL A 417      46.370   4.754  48.918  1.00 62.53           N  
ANISOU 3186  N   VAL A 417     9488   8179   6092   -480   -856    872       N  
ATOM   3187  CA  VAL A 417      46.405   5.868  47.950  1.00 59.96           C  
ANISOU 3187  CA  VAL A 417     9184   7820   5780   -502   -856    742       C  
ATOM   3188  C   VAL A 417      47.829   6.246  47.604  1.00 60.66           C  
ANISOU 3188  C   VAL A 417     9285   7932   5831   -446   -843    658       C  
ATOM   3189  O   VAL A 417      48.718   6.150  48.448  1.00 66.59           O  
ANISOU 3189  O   VAL A 417     9988   8785   6527   -401   -835    665       O  
ATOM   3190  CB  VAL A 417      45.674   7.124  48.494  1.00 59.28           C  
ANISOU 3190  CB  VAL A 417     9022   7835   5669   -539   -812    694       C  
ATOM   3191  CG1 VAL A 417      45.993   8.351  47.669  1.00 55.02           C  
ANISOU 3191  CG1 VAL A 417     8485   7277   5144   -546   -796    567       C  
ATOM   3192  CG2 VAL A 417      44.165   6.898  48.530  1.00 59.00           C  
ANISOU 3192  CG2 VAL A 417     8965   7743   5709   -599   -816    777       C  
ATOM   3193  N   SER A 418      48.052   6.681  46.374  1.00 60.06           N  
ANISOU 3193  N   SER A 418     9267   7763   5791   -437   -838    588       N  
ATOM   3194  CA  SER A 418      49.388   7.033  45.950  1.00 62.66           C  
ANISOU 3194  CA  SER A 418     9596   8094   6120   -376   -801    534       C  
ATOM   3195  C   SER A 418      49.954   8.176  46.815  1.00 62.16           C  
ANISOU 3195  C   SER A 418     9409   8161   6046   -381   -769    463       C  
ATOM   3196  O   SER A 418      49.227   9.044  47.289  1.00 62.64           O  
ANISOU 3196  O   SER A 418     9415   8286   6101   -428   -761    421       O  
ATOM   3197  CB  SER A 418      49.395   7.413  44.469  1.00 67.28           C  
ANISOU 3197  CB  SER A 418    10267   8561   6733   -347   -777    490       C  
ATOM   3198  OG  SER A 418      49.137   8.797  44.287  1.00 74.90           O  
ANISOU 3198  OG  SER A 418    11176   9560   7724   -374   -729    425       O  
ATOM   3199  N   THR A 419      51.263   8.164  47.014  1.00 61.48           N  
ANISOU 3199  N   THR A 419     9277   8105   5976   -329   -760    444       N  
ATOM   3200  CA  THR A 419      51.900   9.129  47.890  1.00 60.68           C  
ANISOU 3200  CA  THR A 419     9051   8116   5889   -328   -765    362       C  
ATOM   3201  C   THR A 419      51.790  10.561  47.368  1.00 61.86           C  
ANISOU 3201  C   THR A 419     9146   8235   6124   -359   -715    268       C  
ATOM   3202  O   THR A 419      51.447  11.463  48.143  1.00 59.32           O  
ANISOU 3202  O   THR A 419     8747   7995   5796   -392   -731    189       O  
ATOM   3203  CB  THR A 419      53.367   8.776  48.139  1.00 58.69           C  
ANISOU 3203  CB  THR A 419     8743   7883   5673   -265   -782    365       C  
ATOM   3204  CG2 THR A 419      53.975   9.742  49.109  1.00 59.69           C  
ANISOU 3204  CG2 THR A 419     8734   8119   5828   -265   -826    259       C  
ATOM   3205  OG1 THR A 419      53.442   7.462  48.696  1.00 57.31           O  
ANISOU 3205  OG1 THR A 419     8614   7741   5420   -231   -825    462       O  
ATOM   3206  N   PRO A 420      52.072  10.780  46.067  1.00 60.53           N  
ANISOU 3206  N   PRO A 420     9023   7947   6030   -335   -648    280       N  
ATOM   3207  CA  PRO A 420      51.939  12.163  45.576  1.00 59.78           C  
ANISOU 3207  CA  PRO A 420     8868   7816   6029   -357   -584    213       C  
ATOM   3208  C   PRO A 420      50.531  12.692  45.774  1.00 58.73           C  
ANISOU 3208  C   PRO A 420     8750   7711   5853   -421   -597    188       C  
ATOM   3209  O   PRO A 420      50.369  13.874  46.113  1.00 64.78           O  
ANISOU 3209  O   PRO A 420     9425   8507   6682   -454   -576    109       O  
ATOM   3210  CB  PRO A 420      52.307  12.073  44.085  1.00 58.60           C  
ANISOU 3210  CB  PRO A 420     8801   7539   5924   -292   -498    268       C  
ATOM   3211  CG  PRO A 420      53.064  10.780  43.932  1.00 59.40           C  
ANISOU 3211  CG  PRO A 420     8971   7614   5984   -228   -514    335       C  
ATOM   3212  CD  PRO A 420      52.531   9.857  45.010  1.00 60.14           C  
ANISOU 3212  CD  PRO A 420     9080   7790   5978   -270   -616    353       C  
ATOM   3213  N   THR A 421      49.528  11.827  45.623  1.00 56.04           N  
ANISOU 3213  N   THR A 421     8509   7354   5428   -439   -635    255       N  
ATOM   3214  CA  THR A 421      48.134  12.238  45.845  1.00 55.57           C  
ANISOU 3214  CA  THR A 421     8451   7316   5349   -500   -646    251       C  
ATOM   3215  C   THR A 421      47.918  12.634  47.297  1.00 57.63           C  
ANISOU 3215  C   THR A 421     8619   7709   5567   -526   -665    206       C  
ATOM   3216  O   THR A 421      47.430  13.721  47.558  1.00 59.75           O  
ANISOU 3216  O   THR A 421     8827   8008   5867   -555   -636    139       O  
ATOM   3217  CB  THR A 421      47.127  11.140  45.460  1.00 57.37           C  
ANISOU 3217  CB  THR A 421     8779   7484   5536   -517   -698    337       C  
ATOM   3218  CG2 THR A 421      45.706  11.574  45.860  1.00 55.77           C  
ANISOU 3218  CG2 THR A 421     8541   7309   5341   -580   -705    347       C  
ATOM   3219  OG1 THR A 421      47.182  10.901  44.031  1.00 59.66           O  
ANISOU 3219  OG1 THR A 421     9175   7651   5843   -476   -698    351       O  
ATOM   3220  N   LEU A 422      48.327  11.769  48.237  1.00 57.10           N  
ANISOU 3220  N   LEU A 422     8548   7723   5424   -499   -708    242       N  
ATOM   3221  CA  LEU A 422      48.237  12.069  49.657  1.00 56.69           C  
ANISOU 3221  CA  LEU A 422     8431   7817   5293   -487   -730    200       C  
ATOM   3222  C   LEU A 422      48.935  13.371  50.032  1.00 59.87           C  
ANISOU 3222  C   LEU A 422     8735   8264   5747   -479   -734     51       C  
ATOM   3223  O   LEU A 422      48.391  14.173  50.808  1.00 58.94           O  
ANISOU 3223  O   LEU A 422     8575   8225   5594   -485   -732    -25       O  
ATOM   3224  CB  LEU A 422      48.815  10.945  50.504  1.00 58.20           C  
ANISOU 3224  CB  LEU A 422     8637   8088   5391   -433   -777    269       C  
ATOM   3225  CG  LEU A 422      48.021   9.642  50.663  1.00 59.27           C  
ANISOU 3225  CG  LEU A 422     8838   8207   5475   -434   -775    424       C  
ATOM   3226  CD1 LEU A 422      48.878   8.593  51.354  1.00 56.13           C  
ANISOU 3226  CD1 LEU A 422     8447   7872   5007   -367   -813    493       C  
ATOM   3227  CD2 LEU A 422      46.719   9.865  51.430  1.00 55.66           C  
ANISOU 3227  CD2 LEU A 422     8364   7820   4964   -451   -738    468       C  
ATOM   3228  N   VAL A 423      50.134  13.583  49.503  1.00 61.53           N  
ANISOU 3228  N   VAL A 423     8905   8416   6059   -461   -737      8       N  
ATOM   3229  CA  VAL A 423      50.881  14.805  49.816  1.00 63.99           C  
ANISOU 3229  CA  VAL A 423     9097   8738   6476   -460   -752   -135       C  
ATOM   3230  C   VAL A 423      50.127  16.045  49.312  1.00 67.02           C  
ANISOU 3230  C   VAL A 423     9452   9058   6955   -508   -685   -193       C  
ATOM   3231  O   VAL A 423      49.950  16.998  50.067  1.00 63.75           O  
ANISOU 3231  O   VAL A 423     8967   8698   6558   -516   -708   -314       O  
ATOM   3232  CB  VAL A 423      52.315  14.767  49.241  1.00 64.69           C  
ANISOU 3232  CB  VAL A 423     9125   8749   6704   -432   -750   -139       C  
ATOM   3233  CG1 VAL A 423      52.956  16.146  49.277  1.00 64.22           C  
ANISOU 3233  CG1 VAL A 423     8924   8646   6833   -447   -747   -273       C  
ATOM   3234  CG2 VAL A 423      53.169  13.751  50.001  1.00 63.60           C  
ANISOU 3234  CG2 VAL A 423     8983   8693   6487   -378   -834   -110       C  
ATOM   3235  N   GLU A 424      49.665  16.020  48.055  1.00 66.93           N  
ANISOU 3235  N   GLU A 424     9500   8934   6995   -527   -610   -111       N  
ATOM   3236  CA  GLU A 424      48.998  17.186  47.448  1.00 64.95           C  
ANISOU 3236  CA  GLU A 424     9221   8614   6843   -560   -539   -145       C  
ATOM   3237  C   GLU A 424      47.706  17.523  48.186  1.00 66.05           C  
ANISOU 3237  C   GLU A 424     9367   8827   6901   -593   -548   -173       C  
ATOM   3238  O   GLU A 424      47.506  18.661  48.640  1.00 68.02           O  
ANISOU 3238  O   GLU A 424     9538   9091   7214   -608   -532   -280       O  
ATOM   3239  CB  GLU A 424      48.685  16.922  45.974  1.00 65.46           C  
ANISOU 3239  CB  GLU A 424     9376   8564   6932   -548   -474    -39       C  
ATOM   3240  CG  GLU A 424      48.233  18.142  45.179  1.00 67.19           C  
ANISOU 3240  CG  GLU A 424     9562   8700   7267   -560   -390    -53       C  
ATOM   3241  CD  GLU A 424      47.696  17.789  43.792  1.00 70.39           C  
ANISOU 3241  CD  GLU A 424    10086   9018   7639   -528   -350     53       C  
ATOM   3242  OE1 GLU A 424      48.441  17.198  42.974  1.00 69.81           O  
ANISOU 3242  OE1 GLU A 424    10079   8889   7557   -464   -324    115       O  
ATOM   3243  OE2 GLU A 424      46.521  18.121  43.509  1.00 73.79           O1-
ANISOU 3243  OE2 GLU A 424    10548   9438   8050   -554   -348     72       O1-
ATOM   3244  N   VAL A 425      46.840  16.522  48.299  1.00 62.46           N  
ANISOU 3244  N   VAL A 425     8998   8407   6326   -599   -567    -71       N  
ATOM   3245  CA  VAL A 425      45.570  16.660  48.996  1.00 63.96           C  
ANISOU 3245  CA  VAL A 425     9191   8665   6447   -620   -557    -58       C  
ATOM   3246  C   VAL A 425      45.713  17.117  50.452  1.00 68.03           C  
ANISOU 3246  C   VAL A 425     9651   9315   6884   -587   -581   -161       C  
ATOM   3247  O   VAL A 425      44.977  17.982  50.900  1.00 69.00           O  
ANISOU 3247  O   VAL A 425     9738   9469   7010   -593   -545   -222       O  
ATOM   3248  CB  VAL A 425      44.798  15.335  49.033  1.00 62.73           C  
ANISOU 3248  CB  VAL A 425     9113   8517   6206   -626   -579     84       C  
ATOM   3249  CG1 VAL A 425      43.511  15.510  49.825  1.00 60.79           C  
ANISOU 3249  CG1 VAL A 425     8845   8338   5913   -639   -545    119       C  
ATOM   3250  CG2 VAL A 425      44.504  14.866  47.625  1.00 64.57           C  
ANISOU 3250  CG2 VAL A 425     9416   8616   6501   -648   -584    162       C  
ATOM   3251  N   SER A 426      46.637  16.521  51.204  1.00 72.63           N  
ANISOU 3251  N   SER A 426    10232   9981   7385   -539   -646   -183       N  
ATOM   3252  CA  SER A 426      46.800  16.897  52.618  1.00 71.29           C  
ANISOU 3252  CA  SER A 426    10029   9954   7105   -480   -691   -292       C  
ATOM   3253  C   SER A 426      47.287  18.324  52.706  1.00 71.88           C  
ANISOU 3253  C   SER A 426    10013   9999   7300   -487   -709   -481       C  
ATOM   3254  O   SER A 426      46.870  19.068  53.570  1.00 75.03           O  
ANISOU 3254  O   SER A 426    10392  10473   7644   -455   -716   -591       O  
ATOM   3255  CB  SER A 426      47.769  15.977  53.352  1.00 71.60           C  
ANISOU 3255  CB  SER A 426    10083  10088   7033   -414   -775   -278       C  
ATOM   3256  OG  SER A 426      47.210  14.691  53.548  1.00 73.71           O  
ANISOU 3256  OG  SER A 426    10426  10396   7184   -395   -752   -103       O  
ATOM   3257  N   ARG A 427      48.159  18.700  51.790  1.00 72.90           N  
ANISOU 3257  N   ARG A 427    10085  10007   7607   -522   -709   -511       N  
ATOM   3258  CA  ARG A 427      48.649  20.053  51.702  1.00 76.70           C  
ANISOU 3258  CA  ARG A 427    10457  10416   8269   -540   -713   -668       C  
ATOM   3259  C   ARG A 427      47.487  21.031  51.519  1.00 77.35           C  
ANISOU 3259  C   ARG A 427    10534  10459   8397   -572   -630   -695       C  
ATOM   3260  O   ARG A 427      47.356  22.017  52.257  1.00 78.79           O  
ANISOU 3260  O   ARG A 427    10661  10670   8606   -556   -654   -851       O  
ATOM   3261  CB  ARG A 427      49.587  20.136  50.496  1.00 78.39           C  
ANISOU 3261  CB  ARG A 427    10619  10484   8681   -567   -674   -620       C  
ATOM   3262  CG  ARG A 427      50.476  21.343  50.488  1.00 88.52           C  
ANISOU 3262  CG  ARG A 427    11755  11678  10199   -578   -692   -766       C  
ATOM   3263  CD  ARG A 427      51.586  21.150  51.484  1.00 97.41           C  
ANISOU 3263  CD  ARG A 427    12813  12878  11319   -539   -835   -886       C  
ATOM   3264  NE  ARG A 427      52.781  20.663  50.855  1.00100.25           N  
ANISOU 3264  NE  ARG A 427    13118  13162  11809   -532   -835   -814       N  
ATOM   3265  CZ  ARG A 427      53.646  21.436  50.223  1.00102.48           C  
ANISOU 3265  CZ  ARG A 427    13264  13299  12374   -553   -796   -844       C  
ATOM   3266  NH1 ARG A 427      54.708  20.871  49.720  1.00111.73           N1+
ANISOU 3266  NH1 ARG A 427    14391  14415  13645   -531   -784   -758       N1+
ATOM   3267  NH2 ARG A 427      53.470  22.747  50.082  1.00 96.31           N  
ANISOU 3267  NH2 ARG A 427    12382  12418  11794   -588   -758   -943       N  
ATOM   3268  N   SER A 428      46.628  20.750  50.549  1.00 73.08           N  
ANISOU 3268  N   SER A 428    10050   9851   7865   -609   -544   -550       N  
ATOM   3269  CA  SER A 428      45.499  21.624  50.280  1.00 70.62           C  
ANISOU 3269  CA  SER A 428     9727   9496   7609   -637   -466   -553       C  
ATOM   3270  C   SER A 428      44.486  21.640  51.405  1.00 69.17           C  
ANISOU 3270  C   SER A 428     9572   9435   7275   -608   -462   -578       C  
ATOM   3271  O   SER A 428      43.897  22.678  51.690  1.00 69.83           O  
ANISOU 3271  O   SER A 428     9613   9509   7410   -607   -419   -665       O  
ATOM   3272  CB  SER A 428      44.834  21.219  48.979  1.00 71.95           C  
ANISOU 3272  CB  SER A 428     9955   9572   7809   -671   -403   -392       C  
ATOM   3273  OG  SER A 428      45.696  21.555  47.901  1.00 74.37           O  
ANISOU 3273  OG  SER A 428    10232   9760   8265   -674   -370   -379       O  
ATOM   3274  N   LEU A 429      44.260  20.487  52.026  1.00 66.93           N  
ANISOU 3274  N   LEU A 429     9358   9258   6813   -574   -491   -487       N  
ATOM   3275  CA  LEU A 429      43.371  20.411  53.179  1.00 66.87           C  
ANISOU 3275  CA  LEU A 429     9379   9379   6647   -519   -465   -484       C  
ATOM   3276  C   LEU A 429      43.870  21.314  54.299  1.00 68.05           C  
ANISOU 3276  C   LEU A 429     9494   9615   6746   -450   -516   -693       C  
ATOM   3277  O   LEU A 429      43.088  21.985  54.955  1.00 67.55           O  
ANISOU 3277  O   LEU A 429     9431   9604   6630   -408   -467   -756       O  
ATOM   3278  CB  LEU A 429      43.256  18.979  53.694  1.00 66.35           C  
ANISOU 3278  CB  LEU A 429     9384   9410   6416   -479   -483   -337       C  
ATOM   3279  CG  LEU A 429      42.351  18.087  52.862  1.00 66.32           C  
ANISOU 3279  CG  LEU A 429     9415   9328   6455   -537   -434   -136       C  
ATOM   3280  CD1 LEU A 429      42.449  16.640  53.309  1.00 65.44           C  
ANISOU 3280  CD1 LEU A 429     9358   9280   6227   -502   -458      5       C  
ATOM   3281  CD2 LEU A 429      40.927  18.608  52.963  1.00 68.74           C  
ANISOU 3281  CD2 LEU A 429     9700   9628   6790   -549   -342    -86       C  
ATOM   3282  N   GLY A 430      45.180  21.334  54.492  1.00 67.87           N  
ANISOU 3282  N   GLY A 430     9438   9599   6750   -432   -622   -808       N  
ATOM   3283  CA  GLY A 430      45.791  22.173  55.495  1.00 68.72           C  
ANISOU 3283  CA  GLY A 430     9505   9771   6835   -366   -715  -1035       C  
ATOM   3284  C   GLY A 430      45.591  23.658  55.236  1.00 69.37           C  
ANISOU 3284  C   GLY A 430     9507   9742   7110   -401   -684  -1190       C  
ATOM   3285  O   GLY A 430      45.282  24.401  56.168  1.00 71.65           O  
ANISOU 3285  O   GLY A 430     9798  10096   7328   -334   -706  -1350       O  
ATOM   3286  N   LYS A 431      45.778  24.083  53.981  1.00 66.37           N  
ANISOU 3286  N   LYS A 431     9058   9193   6966   -493   -628  -1140       N  
ATOM   3287  CA  LYS A 431      45.577  25.480  53.569  1.00 67.07           C  
ANISOU 3287  CA  LYS A 431     9058   9149   7276   -532   -576  -1250       C  
ATOM   3288  C   LYS A 431      44.193  25.979  53.973  1.00 67.35           C  
ANISOU 3288  C   LYS A 431     9134   9228   7229   -506   -485  -1249       C  
ATOM   3289  O   LYS A 431      43.979  27.191  54.098  1.00 70.27           O  
ANISOU 3289  O   LYS A 431     9441   9527   7733   -505   -461  -1390       O  
ATOM   3290  CB  LYS A 431      45.700  25.655  52.036  1.00 66.94           C  
ANISOU 3290  CB  LYS A 431     8994   8964   7478   -612   -485  -1116       C  
ATOM   3291  CG  LYS A 431      47.014  26.233  51.514  1.00 69.22           C  
ANISOU 3291  CG  LYS A 431     9162   9116   8023   -641   -519  -1193       C  
ATOM   3292  CD  LYS A 431      46.855  26.913  50.149  1.00 66.65           C  
ANISOU 3292  CD  LYS A 431     8779   8618   7926   -689   -387  -1088       C  
ATOM   3293  N   VAL A 432      43.249  25.062  54.137  1.00 62.34           N  
ANISOU 3293  N   VAL A 432     8590   8692   6405   -485   -427  -1083       N  
ATOM   3294  CA  VAL A 432      41.882  25.459  54.420  1.00 67.23           C  
ANISOU 3294  CA  VAL A 432     9233   9340   6972   -462   -320  -1042       C  
ATOM   3295  C   VAL A 432      41.812  26.162  55.763  1.00 72.00           C  
ANISOU 3295  C   VAL A 432     9850  10047   7459   -357   -349  -1244       C  
ATOM   3296  O   VAL A 432      40.999  27.068  55.961  1.00 74.45           O  
ANISOU 3296  O   VAL A 432    10142  10331   7813   -335   -269  -1305       O  
ATOM   3297  CB  VAL A 432      40.920  24.264  54.407  1.00 68.78           C  
ANISOU 3297  CB  VAL A 432     9502   9612   7018   -457   -256   -813       C  
ATOM   3298  CG1 VAL A 432      39.554  24.693  54.894  1.00 69.36           C  
ANISOU 3298  CG1 VAL A 432     9583   9727   7045   -415   -141   -774       C  
ATOM   3299  CG2 VAL A 432      40.837  23.673  53.002  1.00 63.15           C  
ANISOU 3299  CG2 VAL A 432     8785   8781   6427   -552   -240   -639       C  
ATOM   3300  N   GLY A 433      42.696  25.764  56.670  1.00 74.74           N  
ANISOU 3300  N   GLY A 433    10232  10507   7657   -281   -471  -1356       N  
ATOM   3301  CA  GLY A 433      42.842  26.445  57.940  1.00 77.51           C  
ANISOU 3301  CA  GLY A 433    10609  10958   7884   -161   -540  -1588       C  
ATOM   3302  C   GLY A 433      43.182  27.915  57.799  1.00 81.45           C  
ANISOU 3302  C   GLY A 433    11012  11315   8619   -190   -580  -1824       C  
ATOM   3303  O   GLY A 433      42.615  28.772  58.500  1.00 86.57           O  
ANISOU 3303  O   GLY A 433    11680  11990   9224   -111   -554  -1975       O  
ATOM   3304  N   THR A 434      44.108  28.209  56.895  1.00 80.71           N  
ANISOU 3304  N   THR A 434    10812  11065   8789   -293   -634  -1851       N  
ATOM   3305  CA  THR A 434      44.512  29.583  56.647  1.00 83.32           C  
ANISOU 3305  CA  THR A 434    11023  11227   9408   -334   -663  -2048       C  
ATOM   3306  C   THR A 434      43.406  30.381  55.992  1.00 82.53           C  
ANISOU 3306  C   THR A 434    10894  11017   9448   -378   -497  -1973       C  
ATOM   3307  O   THR A 434      43.182  31.548  56.338  1.00 87.46           O  
ANISOU 3307  O   THR A 434    11472  11569  10192   -352   -491  -2157       O  
ATOM   3308  CB  THR A 434      45.725  29.643  55.718  1.00 83.44           C  
ANISOU 3308  CB  THR A 434    10916  11087   9700   -430   -719  -2035       C  
ATOM   3309  CG2 THR A 434      46.405  30.988  55.822  1.00 84.21           C  
ANISOU 3309  CG2 THR A 434    10874  11024  10099   -449   -797  -2282       C  
ATOM   3310  OG1 THR A 434      46.644  28.599  56.066  1.00 87.91           O  
ANISOU 3310  OG1 THR A 434    11514  11758  10131   -403   -843  -2015       O  
ATOM   3311  N   ARG A 435      42.709  29.752  55.055  1.00 79.63           N  
ANISOU 3311  N   ARG A 435    10553  10633   9069   -440   -373  -1711       N  
ATOM   3312  CA  ARG A 435      41.710  30.461  54.261  1.00 81.75           C  
ANISOU 3312  CA  ARG A 435    10783  10788   9491   -487   -227  -1614       C  
ATOM   3313  C   ARG A 435      40.416  30.684  55.049  1.00 84.92           C  
ANISOU 3313  C   ARG A 435    11247  11286   9732   -409   -139  -1620       C  
ATOM   3314  O   ARG A 435      39.660  31.599  54.721  1.00 91.11           O  
ANISOU 3314  O   ARG A 435    11982  11974  10660   -423    -37  -1622       O  
ATOM   3315  CB  ARG A 435      41.438  29.748  52.928  1.00 75.67           C  
ANISOU 3315  CB  ARG A 435    10021   9959   8773   -568   -152  -1350       C  
ATOM   3316  N   CYS A 436      40.169  29.889  56.095  1.00 84.91           N  
ANISOU 3316  N   CYS A 436    11348  11470   9443   -315   -164  -1613       N  
ATOM   3317  CA  CYS A 436      38.875  29.954  56.801  1.00 86.62           C  
ANISOU 3317  CA  CYS A 436    11625  11786   9499   -227    -45  -1563       C  
ATOM   3318  C   CYS A 436      38.889  30.309  58.298  1.00 89.46           C  
ANISOU 3318  C   CYS A 436    12062  12286   9644    -66    -85  -1776       C  
ATOM   3319  O   CYS A 436      38.092  31.143  58.728  1.00 96.40           O  
ANISOU 3319  O   CYS A 436    12946  13158  10524      3      7  -1855       O  
ATOM   3320  CB  CYS A 436      38.115  28.638  56.619  1.00 86.22           C  
ANISOU 3320  CB  CYS A 436    11633  11828   9298   -236     29  -1281       C  
ATOM   3321  SG  CYS A 436      37.789  28.182  54.898  1.00 84.38           S  
ANISOU 3321  SG  CYS A 436    11340  11445   9273   -392     73  -1032       S  
ATOM   3322  N   CYS A 437      39.751  29.687  59.099  1.00 88.77           N  
ANISOU 3322  N   CYS A 437    12040  12329   9359     10   -218  -1867       N  
ATOM   3323  CA  CYS A 437      39.627  29.808  60.566  1.00 92.36           C  
ANISOU 3323  CA  CYS A 437    12603  12958   9532    200   -248  -2031       C  
ATOM   3324  C   CYS A 437      39.808  31.264  61.066  1.00 92.75           C  
ANISOU 3324  C   CYS A 437    12627  12931   9681    262   -310  -2357       C  
ATOM   3325  O   CYS A 437      39.109  31.721  61.972  1.00 90.45           O  
ANISOU 3325  O   CYS A 437    12417  12730   9221    412   -242  -2455       O  
ATOM   3326  CB  CYS A 437      40.588  28.850  61.289  1.00 92.62           C  
ANISOU 3326  CB  CYS A 437    12712  13147   9331    279   -400  -2064       C  
ATOM   3327  SG  CYS A 437      40.389  27.084  60.898  1.00 88.07           S  
ANISOU 3327  SG  CYS A 437    12177  12664   8624    233   -331  -1698       S  
ATOM   3328  N   THR A 438      40.748  31.971  60.450  1.00 93.74           N  
ANISOU 3328  N   THR A 438    12637  12881  10098    153   -430  -2515       N  
ATOM   3329  CA  THR A 438      40.914  33.418  60.617  1.00 94.19           C  
ANISOU 3329  CA  THR A 438    12626  12795  10366    166   -480  -2800       C  
ATOM   3330  C   THR A 438      39.634  34.247  60.418  1.00 92.44           C  
ANISOU 3330  C   THR A 438    12392  12498  10232    177   -284  -2753       C  
ATOM   3331  O   THR A 438      39.523  35.336  60.953  1.00 92.25           O  
ANISOU 3331  O   THR A 438    12364  12413  10273    253   -306  -3000       O  
ATOM   3332  CB  THR A 438      41.977  33.952  59.626  1.00 95.36           C  
ANISOU 3332  CB  THR A 438    12609  12719  10904      7   -576  -2866       C  
ATOM   3333  CG2 THR A 438      41.699  33.458  58.195  1.00 94.57           C  
ANISOU 3333  CG2 THR A 438    12441  12522  10969   -147   -437  -2547       C  
ATOM   3334  OG1 THR A 438      41.967  35.381  59.628  1.00 98.48           O  
ANISOU 3334  OG1 THR A 438    12915  12936  11566      0   -586  -3095       O  
ATOM   3335  N   LYS A 439      38.680  33.753  59.640  1.00 92.07           N  
ANISOU 3335  N   LYS A 439    12333  12444  10205    105   -105  -2447       N  
ATOM   3336  CA  LYS A 439      37.467  34.516  59.357  1.00 93.62           C  
ANISOU 3336  CA  LYS A 439    12497  12560  10514    108     77  -2378       C  
ATOM   3337  C   LYS A 439      36.572  34.618  60.584  1.00 96.17           C  
ANISOU 3337  C   LYS A 439    12940  13042  10560    299    170  -2439       C  
ATOM   3338  O   LYS A 439      36.780  33.907  61.561  1.00 99.16           O  
ANISOU 3338  O   LYS A 439    13438  13612  10629    428    115  -2472       O  
ATOM   3339  CB  LYS A 439      36.709  33.893  58.188  1.00 92.41           C  
ANISOU 3339  CB  LYS A 439    12294  12360  10457    -15    213  -2037       C  
ATOM   3340  CG  LYS A 439      37.426  34.086  56.855  1.00 91.53           C  
ANISOU 3340  CG  LYS A 439    12068  12066  10644   -177    165  -1980       C  
ATOM   3341  CD  LYS A 439      36.543  33.760  55.653  1.00 88.88           C  
ANISOU 3341  CD  LYS A 439    11688  11663  10421   -275    294  -1684       C  
ATOM   3342  CE  LYS A 439      37.033  34.472  54.399  1.00 86.64           C  
ANISOU 3342  CE  LYS A 439    11289  11173  10458   -388    294  -1666       C  
ATOM   3343  NZ  LYS A 439      38.521  34.415  54.280  1.00 89.81           N1+
ANISOU 3343  NZ  LYS A 439    11654  11522  10946   -429    151  -1795       N1+
ATOM   3344  N   PRO A 440      35.593  35.533  60.557  1.00 99.38           N  
ANISOU 3344  N   PRO A 440    13317  13369  11073    333    319  -2454       N  
ATOM   3345  CA  PRO A 440      34.602  35.638  61.637  1.00102.16           C  
ANISOU 3345  CA  PRO A 440    13779  13865  11174    527    454  -2470       C  
ATOM   3346  C   PRO A 440      33.983  34.296  62.025  1.00 98.43           C  
ANISOU 3346  C   PRO A 440    13391  13592  10414    596    558  -2189       C  
ATOM   3347  O   PRO A 440      33.449  33.603  61.168  1.00 94.42           O  
ANISOU 3347  O   PRO A 440    12817  13051  10006    474    646  -1893       O  
ATOM   3348  CB  PRO A 440      33.539  36.561  61.031  1.00102.46           C  
ANISOU 3348  CB  PRO A 440    13723  13750  11456    484    632  -2393       C  
ATOM   3349  CG  PRO A 440      34.314  37.461  60.127  1.00101.23           C  
ANISOU 3349  CG  PRO A 440    13439  13366  11657    335    528  -2532       C  
ATOM   3350  CD  PRO A 440      35.499  36.671  59.622  1.00 99.69           C  
ANISOU 3350  CD  PRO A 440    13220  13173  11485    218    359  -2498       C  
ATOM   3351  N   GLU A 441      34.052  33.954  63.308  1.00101.15           N  
ANISOU 3351  N   GLU A 441    13880  14136  10415    800    545  -2284       N  
ATOM   3352  CA  GLU A 441      33.615  32.642  63.826  1.00107.37           C  
ANISOU 3352  CA  GLU A 441    14753  15122  10919    892    641  -2023       C  
ATOM   3353  C   GLU A 441      32.415  32.013  63.105  1.00109.93           C  
ANISOU 3353  C   GLU A 441    14994  15411  11364    799    846  -1642       C  
ATOM   3354  O   GLU A 441      32.423  30.812  62.810  1.00108.70           O  
ANISOU 3354  O   GLU A 441    14829  15309  11164    734    849  -1398       O  
ATOM   3355  CB  GLU A 441      33.302  32.732  65.324  1.00105.27           C  
ANISOU 3355  CB  GLU A 441    14652  15059  10285   1178    709  -2139       C  
ATOM   3356  N   SER A 442      31.390  32.820  62.832  1.00111.46           N  
ANISOU 3356  N   SER A 442    15121  15506  11725    797   1007  -1599       N  
ATOM   3357  CA  SER A 442      30.163  32.324  62.194  1.00109.29           C  
ANISOU 3357  CA  SER A 442    14750  15187  11589    721   1192  -1253       C  
ATOM   3358  C   SER A 442      30.391  31.867  60.738  1.00103.48           C  
ANISOU 3358  C   SER A 442    13893  14302  11121    475   1099  -1094       C  
ATOM   3359  O   SER A 442      29.819  30.872  60.301  1.00 99.69           O  
ANISOU 3359  O   SER A 442    13367  13833  10676    407   1158   -808       O  
ATOM   3360  CB  SER A 442      29.052  33.387  62.261  1.00110.15           C  
ANISOU 3360  CB  SER A 442    14808  15220  11825    787   1376  -1262       C  
ATOM   3361  OG  SER A 442      29.271  34.423  61.312  1.00108.70           O  
ANISOU 3361  OG  SER A 442    14522  14833  11944    644   1306  -1394       O  
ATOM   3362  N   GLU A 443      31.225  32.596  59.999  1.00100.16           N  
ANISOU 3362  N   GLU A 443    13423  13740  10894    355    957  -1279       N  
ATOM   3363  CA  GLU A 443      31.528  32.271  58.595  1.00 93.68           C  
ANISOU 3363  CA  GLU A 443    12507  12780  10307    152    874  -1149       C  
ATOM   3364  C   GLU A 443      32.428  31.032  58.391  1.00 86.71           C  
ANISOU 3364  C   GLU A 443    11666  11962   9318     87    736  -1072       C  
ATOM   3365  O   GLU A 443      32.564  30.548  57.269  1.00 83.20           O  
ANISOU 3365  O   GLU A 443    11164  11425   9023    -58    683   -929       O  
ATOM   3366  CB  GLU A 443      32.201  33.473  57.915  1.00 95.39           C  
ANISOU 3366  CB  GLU A 443    12654  12822  10767     68    791  -1356       C  
ATOM   3367  CG  GLU A 443      31.405  34.779  57.928  1.00 97.24           C  
ANISOU 3367  CG  GLU A 443    12830  12952  11165    110    916  -1437       C  
ATOM   3368  CD  GLU A 443      32.178  35.957  57.328  1.00 98.60           C  
ANISOU 3368  CD  GLU A 443    12927  12939  11598     35    834  -1644       C  
ATOM   3369  OE1 GLU A 443      33.432  35.936  57.320  1.00 98.25           O  
ANISOU 3369  OE1 GLU A 443    12892  12872  11566     -3    675  -1807       O  
ATOM   3370  OE2 GLU A 443      31.533  36.924  56.866  1.00 98.72           O1-
ANISOU 3370  OE2 GLU A 443    12860  12822  11828     16    934  -1635       O1-
ATOM   3371  N   ARG A 444      33.019  30.522  59.468  1.00 87.00           N  
ANISOU 3371  N   ARG A 444    11809  12159   9088    207    679  -1166       N  
ATOM   3372  CA  ARG A 444      34.006  29.434  59.407  1.00 88.76           C  
ANISOU 3372  CA  ARG A 444    12075  12447   9202    166    540  -1127       C  
ATOM   3373  C   ARG A 444      33.559  28.165  58.654  1.00 88.14           C  
ANISOU 3373  C   ARG A 444    11963  12355   9170     62    571   -816       C  
ATOM   3374  O   ARG A 444      34.279  27.695  57.762  1.00 81.54           O  
ANISOU 3374  O   ARG A 444    11102  11443   8436    -64    456   -782       O  
ATOM   3375  CB  ARG A 444      34.475  29.043  60.827  1.00 90.76           C  
ANISOU 3375  CB  ARG A 444    12455  12901   9126    350    500  -1240       C  
ATOM   3376  CG  ARG A 444      35.426  30.037  61.490  1.00 93.38           C  
ANISOU 3376  CG  ARG A 444    12831  13243   9405    434    359  -1601       C  
ATOM   3377  CD  ARG A 444      36.082  29.458  62.737  1.00 93.70           C  
ANISOU 3377  CD  ARG A 444    13004  13489   9109    608    266  -1704       C  
ATOM   3378  N   MET A 445      32.398  27.616  59.014  1.00 90.63           N  
ANISOU 3378  N   MET A 445    12276  12734   9424    121    726   -595       N  
ATOM   3379  CA  MET A 445      31.919  26.360  58.429  1.00 92.89           C  
ANISOU 3379  CA  MET A 445    12525  13000   9770     34    746   -308       C  
ATOM   3380  C   MET A 445      31.609  26.486  56.920  1.00 86.84           C  
ANISOU 3380  C   MET A 445    11659  12050   9287   -144    703   -216       C  
ATOM   3381  O   MET A 445      32.123  25.706  56.120  1.00 86.94           O  
ANISOU 3381  O   MET A 445    11670  12009   9355   -248    592   -144       O  
ATOM   3382  CB  MET A 445      30.712  25.805  59.209  1.00 99.39           C  
ANISOU 3382  CB  MET A 445    13342  13916  10507    145    934    -82       C  
ATOM   3383  CG  MET A 445      30.030  24.609  58.547  1.00105.34           C  
ANISOU 3383  CG  MET A 445    14020  14605  11401     42    957    218       C  
ATOM   3384  SD  MET A 445      28.239  24.534  58.774  1.00117.75           S  
ANISOU 3384  SD  MET A 445    15479  16152  13107     89   1188    493       S  
ATOM   3385  CE  MET A 445      27.638  25.545  57.408  1.00110.97           C  
ANISOU 3385  CE  MET A 445    14501  15096  12566    -63   1149    458       C  
ATOM   3386  N   PRO A 446      30.774  27.456  56.525  1.00 80.75           N  
ANISOU 3386  N   PRO A 446    10812  11185   8684   -163    790   -218       N  
ATOM   3387  CA  PRO A 446      30.550  27.692  55.102  1.00 80.47           C  
ANISOU 3387  CA  PRO A 446    10696  10987   8893   -306    737   -150       C  
ATOM   3388  C   PRO A 446      31.837  27.805  54.291  1.00 78.85           C  
ANISOU 3388  C   PRO A 446    10514  10709   8735   -391    583   -281       C  
ATOM   3389  O   PRO A 446      31.922  27.288  53.168  1.00 84.68           O  
ANISOU 3389  O   PRO A 446    11234  11361   9580   -493    507   -172       O  
ATOM   3390  CB  PRO A 446      29.815  29.028  55.094  1.00 81.91           C  
ANISOU 3390  CB  PRO A 446    10814  11102   9206   -273    847   -220       C  
ATOM   3391  CG  PRO A 446      29.059  29.020  56.368  1.00 80.70           C  
ANISOU 3391  CG  PRO A 446    10683  11071   8909   -128   1000   -185       C  
ATOM   3392  CD  PRO A 446      29.884  28.272  57.359  1.00 81.77           C  
ANISOU 3392  CD  PRO A 446    10929  11359   8780    -39    953   -249       C  
ATOM   3393  N   CYS A 447      32.823  28.492  54.844  1.00 76.31           N  
ANISOU 3393  N   CYS A 447    10232  10417   8345   -341    538   -515       N  
ATOM   3394  CA  CYS A 447      34.096  28.628  54.165  1.00 76.73           C  
ANISOU 3394  CA  CYS A 447    10289  10398   8468   -412    409   -632       C  
ATOM   3395  C   CYS A 447      34.750  27.274  53.970  1.00 72.61           C  
ANISOU 3395  C   CYS A 447     9821   9926   7840   -448    311   -532       C  
ATOM   3396  O   CYS A 447      35.114  26.918  52.851  1.00 79.74           O  
ANISOU 3396  O   CYS A 447    10712  10738   8846   -538    247   -458       O  
ATOM   3397  CB  CYS A 447      35.036  29.530  54.945  1.00 78.83           C  
ANISOU 3397  CB  CYS A 447    10569  10684   8698   -346    359   -907       C  
ATOM   3398  SG  CYS A 447      36.650  29.721  54.159  1.00 85.18           S  
ANISOU 3398  SG  CYS A 447    11344  11382   9639   -431    214  -1035       S  
ATOM   3399  N   THR A 448      34.890  26.522  55.050  1.00 70.63           N  
ANISOU 3399  N   THR A 448     9636   9822   7377   -365    306   -525       N  
ATOM   3400  CA  THR A 448      35.636  25.268  55.013  1.00 72.30           C  
ANISOU 3400  CA  THR A 448     9901  10087   7482   -384    212   -450       C  
ATOM   3401  C   THR A 448      34.882  24.192  54.254  1.00 73.03           C  
ANISOU 3401  C   THR A 448     9980  10131   7638   -457    227   -201       C  
ATOM   3402  O   THR A 448      35.489  23.377  53.567  1.00 73.23           O  
ANISOU 3402  O   THR A 448    10030  10115   7681   -520    136   -142       O  
ATOM   3403  CB  THR A 448      35.902  24.700  56.417  1.00 71.71           C  
ANISOU 3403  CB  THR A 448     9902  10191   7153   -256    212   -482       C  
ATOM   3404  CG2 THR A 448      36.688  25.646  57.284  1.00 72.99           C  
ANISOU 3404  CG2 THR A 448    10093  10415   7225   -164    158   -753       C  
ATOM   3405  OG1 THR A 448      34.655  24.448  57.035  1.00 74.49           O  
ANISOU 3405  OG1 THR A 448    10254  10611   7436   -183    356   -328       O  
ATOM   3406  N   GLU A 449      33.560  24.201  54.361  1.00 76.30           N  
ANISOU 3406  N   GLU A 449    10350  10538   8102   -446    338    -59       N  
ATOM   3407  CA  GLU A 449      32.754  23.226  53.647  1.00 77.99           C  
ANISOU 3407  CA  GLU A 449    10529  10685   8419   -519    334    167       C  
ATOM   3408  C   GLU A 449      32.875  23.386  52.137  1.00 76.43           C  
ANISOU 3408  C   GLU A 449    10308  10338   8394   -629    243    176       C  
ATOM   3409  O   GLU A 449      32.916  22.397  51.408  1.00 78.58           O  
ANISOU 3409  O   GLU A 449    10598  10554   8704   -689    158    287       O  
ATOM   3410  CB  GLU A 449      31.281  23.273  54.083  1.00 79.55           C  
ANISOU 3410  CB  GLU A 449    10656  10893   8677   -482    475    323       C  
ATOM   3411  CG  GLU A 449      30.981  22.549  55.396  1.00 83.09           C  
ANISOU 3411  CG  GLU A 449    11131  11480   8959   -370    577    427       C  
ATOM   3412  CD  GLU A 449      31.037  21.031  55.288  1.00 84.51           C  
ANISOU 3412  CD  GLU A 449    11319  11655   9135   -407    526    611       C  
ATOM   3413  OE1 GLU A 449      30.076  20.362  55.739  1.00 85.78           O  
ANISOU 3413  OE1 GLU A 449    11424  11828   9339   -374    632    821       O  
ATOM   3414  OE2 GLU A 449      32.034  20.497  54.756  1.00 82.70           O1-
ANISOU 3414  OE2 GLU A 449    11145  11399   8878   -464    389    555       O1-
ATOM   3415  N   ASP A 450      32.939  24.620  51.661  1.00 78.04           N  
ANISOU 3415  N   ASP A 450    10479  10474   8699   -641    261     62       N  
ATOM   3416  CA  ASP A 450      33.083  24.832  50.230  1.00 78.44           C  
ANISOU 3416  CA  ASP A 450    10518  10394   8891   -717    191     82       C  
ATOM   3417  C   ASP A 450      34.437  24.354  49.745  1.00 73.14           C  
ANISOU 3417  C   ASP A 450     9914   9709   8165   -738     88     18       C  
ATOM   3418  O   ASP A 450      34.505  23.622  48.750  1.00 71.22           O  
ANISOU 3418  O   ASP A 450     9705   9401   7955   -783      9    110       O  
ATOM   3419  CB  ASP A 450      32.905  26.296  49.832  1.00 85.17           C  
ANISOU 3419  CB  ASP A 450    11313  11171   9876   -714    253     -9       C  
ATOM   3420  CG  ASP A 450      32.732  26.465  48.315  1.00 90.25           C  
ANISOU 3420  CG  ASP A 450    11944  11688  10658   -768    202     69       C  
ATOM   3421  OD1 ASP A 450      31.794  25.822  47.753  1.00 92.44           O  
ANISOU 3421  OD1 ASP A 450    12209  11931  10985   -799    163    222       O  
ATOM   3422  OD2 ASP A 450      33.540  27.215  47.695  1.00 91.02           O1-
ANISOU 3422  OD2 ASP A 450    12043  11719  10820   -770    197    -19       O1-
ATOM   3423  N   TYR A 451      35.510  24.777  50.420  1.00 67.98           N  
ANISOU 3423  N   TYR A 451     9279   9111   7440   -699     82   -144       N  
ATOM   3424  CA  TYR A 451      36.861  24.413  49.970  1.00 66.23           C  
ANISOU 3424  CA  TYR A 451     9100   8868   7198   -715     -5   -203       C  
ATOM   3425  C   TYR A 451      37.077  22.929  50.066  1.00 63.81           C  
ANISOU 3425  C   TYR A 451     8858   8611   6774   -721    -73    -96       C  
ATOM   3426  O   TYR A 451      37.585  22.326  49.147  1.00 61.78           O  
ANISOU 3426  O   TYR A 451     8641   8291   6539   -753   -138    -46       O  
ATOM   3427  CB  TYR A 451      37.953  25.157  50.725  1.00 68.47           C  
ANISOU 3427  CB  TYR A 451     9366   9189   7461   -675    -18   -403       C  
ATOM   3428  CG  TYR A 451      38.195  26.528  50.143  1.00 72.08           C  
ANISOU 3428  CG  TYR A 451     9753   9531   8104   -692     22   -505       C  
ATOM   3429  CD1 TYR A 451      37.651  27.674  50.750  1.00 74.56           C  
ANISOU 3429  CD1 TYR A 451    10012   9840   8476   -660     93   -613       C  
ATOM   3430  CD2 TYR A 451      38.914  26.687  48.957  1.00 72.61           C  
ANISOU 3430  CD2 TYR A 451     9808   9485   8297   -728      5   -478       C  
ATOM   3431  CE1 TYR A 451      37.841  28.946  50.211  1.00 74.23           C  
ANISOU 3431  CE1 TYR A 451     9894   9674   8636   -676    138   -696       C  
ATOM   3432  CE2 TYR A 451      39.106  27.957  48.405  1.00 76.20           C  
ANISOU 3432  CE2 TYR A 451    10186   9822   8945   -735     64   -541       C  
ATOM   3433  CZ  TYR A 451      38.570  29.092  49.039  1.00 75.96           C  
ANISOU 3433  CZ  TYR A 451    10090   9777   8993   -716    127   -652       C  
ATOM   3434  OH  TYR A 451      38.759  30.365  48.505  1.00 73.71           O  
ANISOU 3434  OH  TYR A 451     9719   9358   8930   -723    191   -709       O  
ATOM   3435  N   LEU A 452      36.634  22.322  51.151  1.00 63.83           N  
ANISOU 3435  N   LEU A 452     8874   8723   6656   -679    -47    -48       N  
ATOM   3436  CA  LEU A 452      36.815  20.898  51.279  1.00 63.14           C  
ANISOU 3436  CA  LEU A 452     8838   8673   6480   -681   -101     68       C  
ATOM   3437  C   LEU A 452      36.177  20.207  50.090  1.00 62.61           C  
ANISOU 3437  C   LEU A 452     8776   8489   6523   -751   -147    213       C  
ATOM   3438  O   LEU A 452      36.707  19.240  49.536  1.00 61.50           O  
ANISOU 3438  O   LEU A 452     8690   8310   6368   -773   -229    262       O  
ATOM   3439  CB  LEU A 452      36.208  20.381  52.576  1.00 64.01           C  
ANISOU 3439  CB  LEU A 452     8948   8906   6465   -613    -33    145       C  
ATOM   3440  CG  LEU A 452      37.189  20.126  53.706  1.00 62.90           C  
ANISOU 3440  CG  LEU A 452     8858   8904   6138   -527    -57     54       C  
ATOM   3441  CD1 LEU A 452      38.324  21.121  53.666  1.00 60.12           C  
ANISOU 3441  CD1 LEU A 452     8502   8546   5794   -519   -115   -166       C  
ATOM   3442  CD2 LEU A 452      36.416  20.154  55.011  1.00 62.49           C  
ANISOU 3442  CD2 LEU A 452     8806   8981   5956   -424     52    101       C  
ATOM   3443  N   SER A 453      35.018  20.705  49.707  1.00 62.75           N  
ANISOU 3443  N   SER A 453     8738   8449   6656   -777   -103    275       N  
ATOM   3444  CA  SER A 453      34.320  20.140  48.585  1.00 61.51           C  
ANISOU 3444  CA  SER A 453     8581   8179   6612   -834   -172    394       C  
ATOM   3445  C   SER A 453      35.229  20.169  47.350  1.00 60.63           C  
ANISOU 3445  C   SER A 453     8537   7987   6513   -849   -258    336       C  
ATOM   3446  O   SER A 453      35.281  19.220  46.577  1.00 59.58           O  
ANISOU 3446  O   SER A 453     8461   7790   6388   -869   -355    400       O  
ATOM   3447  CB  SER A 453      33.068  20.955  48.328  1.00 64.83           C  
ANISOU 3447  CB  SER A 453     8919   8551   7164   -849   -117    441       C  
ATOM   3448  OG  SER A 453      32.412  20.485  47.181  1.00 72.69           O  
ANISOU 3448  OG  SER A 453     9912   9434   8272   -897   -214    535       O  
ATOM   3449  N   LEU A 454      35.949  21.269  47.174  1.00 58.23           N  
ANISOU 3449  N   LEU A 454     8226   7679   6220   -828   -215    216       N  
ATOM   3450  CA  LEU A 454      36.824  21.421  46.027  1.00 55.28           C  
ANISOU 3450  CA  LEU A 454     7906   7230   5869   -822   -257    182       C  
ATOM   3451  C   LEU A 454      38.016  20.476  46.080  1.00 53.37           C  
ANISOU 3451  C   LEU A 454     7734   7011   5532   -806   -315    163       C  
ATOM   3452  O   LEU A 454      38.433  19.943  45.079  1.00 49.60           O  
ANISOU 3452  O   LEU A 454     7329   6468   5048   -797   -372    197       O  
ATOM   3453  CB  LEU A 454      37.332  22.862  45.959  1.00 57.73           C  
ANISOU 3453  CB  LEU A 454     8163   7518   6255   -802   -176     72       C  
ATOM   3454  CG  LEU A 454      36.223  23.899  45.863  1.00 60.66           C  
ANISOU 3454  CG  LEU A 454     8461   7855   6731   -808   -108     88       C  
ATOM   3455  CD1 LEU A 454      36.828  25.276  45.705  1.00 61.18           C  
ANISOU 3455  CD1 LEU A 454     8472   7873   6902   -789    -29    -17       C  
ATOM   3456  CD2 LEU A 454      35.297  23.582  44.701  1.00 62.07           C  
ANISOU 3456  CD2 LEU A 454     8666   7957   6962   -821   -164    212       C  
ATOM   3457  N   ILE A 455      38.597  20.314  47.256  1.00 54.24           N  
ANISOU 3457  N   ILE A 455     7828   7219   5562   -789   -298    102       N  
ATOM   3458  CA  ILE A 455      39.802  19.531  47.410  1.00 53.18           C  
ANISOU 3458  CA  ILE A 455     7744   7114   5349   -769   -348     78       C  
ATOM   3459  C   ILE A 455      39.497  18.035  47.416  1.00 52.68           C  
ANISOU 3459  C   ILE A 455     7740   7052   5223   -779   -414    197       C  
ATOM   3460  O   ILE A 455      40.193  17.245  46.766  1.00 51.95           O  
ANISOU 3460  O   ILE A 455     7717   6913   5110   -770   -473    221       O  
ATOM   3461  CB  ILE A 455      40.478  19.897  48.723  1.00 57.17           C  
ANISOU 3461  CB  ILE A 455     8207   7730   5784   -734   -329    -34       C  
ATOM   3462  CG1 ILE A 455      40.978  21.348  48.675  1.00 59.69           C  
ANISOU 3462  CG1 ILE A 455     8458   8017   6203   -728   -284   -175       C  
ATOM   3463  CG2 ILE A 455      41.622  18.939  49.023  1.00 57.14           C  
ANISOU 3463  CG2 ILE A 455     8247   7771   5692   -708   -392    -38       C  
ATOM   3464  CD1 ILE A 455      41.358  21.834  50.069  1.00 62.11           C  
ANISOU 3464  CD1 ILE A 455     8723   8433   6443   -686   -287   -313       C  
ATOM   3465  N   LEU A 456      38.460  17.639  48.146  1.00 49.83           N  
ANISOU 3465  N   LEU A 456     7348   6735   4849   -791   -396    278       N  
ATOM   3466  CA  LEU A 456      38.066  16.251  48.137  1.00 48.62           C  
ANISOU 3466  CA  LEU A 456     7228   6556   4688   -807   -452    405       C  
ATOM   3467  C   LEU A 456      37.721  15.840  46.722  1.00 50.37           C  
ANISOU 3467  C   LEU A 456     7500   6640   4997   -840   -540    449       C  
ATOM   3468  O   LEU A 456      37.969  14.670  46.348  1.00 50.77           O  
ANISOU 3468  O   LEU A 456     7614   6637   5040   -843   -620    501       O  
ATOM   3469  CB  LEU A 456      36.907  15.978  49.075  1.00 49.24           C  
ANISOU 3469  CB  LEU A 456     7243   6683   4783   -810   -394    513       C  
ATOM   3470  CG  LEU A 456      37.216  15.972  50.593  1.00 49.87           C  
ANISOU 3470  CG  LEU A 456     7306   6916   4726   -743   -316    503       C  
ATOM   3471  CD1 LEU A 456      36.063  15.394  51.400  1.00 48.50           C  
ANISOU 3471  CD1 LEU A 456     7079   6775   4575   -729   -242    665       C  
ATOM   3472  CD2 LEU A 456      38.507  15.238  50.894  1.00 48.75           C  
ANISOU 3472  CD2 LEU A 456     7225   6827   4472   -706   -369    471       C  
ATOM   3473  N   ASN A 457      37.222  16.785  45.908  1.00 48.86           N  
ANISOU 3473  N   ASN A 457     7293   6392   4881   -851   -532    419       N  
ATOM   3474  CA  ASN A 457      36.929  16.446  44.525  1.00 47.68           C  
ANISOU 3474  CA  ASN A 457     7210   6124   4782   -855   -630    447       C  
ATOM   3475  C   ASN A 457      38.186  16.167  43.806  1.00 47.64           C  
ANISOU 3475  C   ASN A 457     7305   6092   4704   -808   -659    395       C  
ATOM   3476  O   ASN A 457      38.245  15.244  42.998  1.00 53.64           O  
ANISOU 3476  O   ASN A 457     8155   6775   5451   -793   -758    422       O  
ATOM   3477  CB  ASN A 457      36.213  17.528  43.750  1.00 48.26           C  
ANISOU 3477  CB  ASN A 457     7255   6150   4933   -855   -616    437       C  
ATOM   3478  CG  ASN A 457      35.809  17.050  42.360  1.00 49.12           C  
ANISOU 3478  CG  ASN A 457     7447   6148   5069   -839   -746    467       C  
ATOM   3479  ND2 ASN A 457      36.330  17.689  41.297  1.00 47.30           N  
ANISOU 3479  ND2 ASN A 457     7287   5884   4802   -777   -738    426       N  
ATOM   3480  OD1 ASN A 457      35.072  16.080  42.253  1.00 50.15           O  
ANISOU 3480  OD1 ASN A 457     7580   6221   5254   -872   -855    528       O  
ATOM   3481  N   ARG A 458      39.198  16.966  44.057  1.00 46.24           N  
ANISOU 3481  N   ARG A 458     7110   5966   4492   -778   -575    317       N  
ATOM   3482  CA  ARG A 458      40.493  16.688  43.441  1.00 47.66           C  
ANISOU 3482  CA  ARG A 458     7367   6120   4622   -725   -580    284       C  
ATOM   3483  C   ARG A 458      40.983  15.287  43.821  1.00 48.82           C  
ANISOU 3483  C   ARG A 458     7568   6279   4703   -721   -644    318       C  
ATOM   3484  O   ARG A 458      41.558  14.600  42.995  1.00 50.58           O  
ANISOU 3484  O   ARG A 458     7887   6438   4891   -678   -690    329       O  
ATOM   3485  CB  ARG A 458      41.527  17.712  43.853  1.00 46.95           C  
ANISOU 3485  CB  ARG A 458     7212   6076   4552   -704   -486    199       C  
ATOM   3486  CG  ARG A 458      42.947  17.347  43.507  1.00 47.56           C  
ANISOU 3486  CG  ARG A 458     7334   6136   4602   -652   -477    180       C  
ATOM   3487  CD  ARG A 458      43.288  17.795  42.136  1.00 50.41           C  
ANISOU 3487  CD  ARG A 458     7751   6408   4995   -591   -435    201       C  
ATOM   3488  NE  ARG A 458      44.673  17.517  41.800  1.00 52.29           N  
ANISOU 3488  NE  ARG A 458     8017   6623   5227   -530   -397    198       N  
ATOM   3489  CZ  ARG A 458      45.132  17.374  40.548  1.00 56.03           C  
ANISOU 3489  CZ  ARG A 458     8587   7022   5680   -442   -364    246       C  
ATOM   3490  NH1 ARG A 458      44.319  17.431  39.473  1.00 51.38           N1+
ANISOU 3490  NH1 ARG A 458     8093   6378   5051   -398   -388    291       N1+
ATOM   3491  NH2 ARG A 458      46.427  17.136  40.362  1.00 58.40           N  
ANISOU 3491  NH2 ARG A 458     8892   7305   5993   -383   -310    254       N  
ATOM   3492  N   LEU A 459      40.752  14.858  45.056  1.00 49.03           N  
ANISOU 3492  N   LEU A 459     7537   6384   4706   -752   -638    343       N  
ATOM   3493  CA  LEU A 459      41.208  13.521  45.474  1.00 50.18           C  
ANISOU 3493  CA  LEU A 459     7726   6541   4801   -742   -688    395       C  
ATOM   3494  C   LEU A 459      40.509  12.425  44.663  1.00 52.87           C  
ANISOU 3494  C   LEU A 459     8137   6763   5187   -759   -790    468       C  
ATOM   3495  O   LEU A 459      41.142  11.454  44.242  1.00 50.67           O  
ANISOU 3495  O   LEU A 459     7940   6431   4880   -728   -846    479       O  
ATOM   3496  CB  LEU A 459      40.960  13.292  46.968  1.00 50.21           C  
ANISOU 3496  CB  LEU A 459     7658   6658   4763   -752   -648    433       C  
ATOM   3497  CG  LEU A 459      41.100  11.863  47.512  1.00 53.28           C  
ANISOU 3497  CG  LEU A 459     8073   7053   5119   -743   -687    530       C  
ATOM   3498  CD1 LEU A 459      42.513  11.348  47.253  1.00 55.95           C  
ANISOU 3498  CD1 LEU A 459     8473   7386   5398   -696   -716    491       C  
ATOM   3499  CD2 LEU A 459      40.747  11.741  48.988  1.00 52.37           C  
ANISOU 3499  CD2 LEU A 459     7891   7062   4945   -726   -624    591       C  
ATOM   3500  N   CYS A 460      39.204  12.597  44.440  1.00 52.49           N  
ANISOU 3500  N   CYS A 460     8051   6667   5225   -803   -822    510       N  
ATOM   3501  CA  CYS A 460      38.441  11.627  43.692  1.00 52.78           C  
ANISOU 3501  CA  CYS A 460     8135   6578   5341   -825   -948    562       C  
ATOM   3502  C   CYS A 460      38.868  11.545  42.243  1.00 53.84           C  
ANISOU 3502  C   CYS A 460     8401   6621   5437   -767  -1030    498       C  
ATOM   3503  O   CYS A 460      38.917  10.489  41.658  1.00 53.96           O  
ANISOU 3503  O   CYS A 460     8502   6540   5461   -749  -1140    502       O  
ATOM   3504  CB  CYS A 460      36.981  11.985  43.724  1.00 54.26           C  
ANISOU 3504  CB  CYS A 460     8233   6731   5652   -881   -970    615       C  
ATOM   3505  SG  CYS A 460      36.355  11.948  45.396  1.00 60.69           S  
ANISOU 3505  SG  CYS A 460     8906   7646   6508   -920   -855    718       S  
ATOM   3506  N   VAL A 461      39.158  12.681  41.650  1.00 54.40           N  
ANISOU 3506  N   VAL A 461     8488   6714   5466   -726   -972    442       N  
ATOM   3507  CA  VAL A 461      39.525  12.678  40.261  1.00 53.23           C  
ANISOU 3507  CA  VAL A 461     8473   6492   5260   -643  -1026    401       C  
ATOM   3508  C   VAL A 461      40.876  12.032  40.045  1.00 54.99           C  
ANISOU 3508  C   VAL A 461     8791   6710   5392   -572  -1002    378       C  
ATOM   3509  O   VAL A 461      41.061  11.323  39.063  1.00 56.74           O  
ANISOU 3509  O   VAL A 461     9148   6848   5563   -502  -1088    359       O  
ATOM   3510  CB  VAL A 461      39.624  14.087  39.736  1.00 51.70           C  
ANISOU 3510  CB  VAL A 461     8264   6327   5052   -601   -933    374       C  
ATOM   3511  CG1 VAL A 461      40.711  14.135  38.660  1.00 52.42           C  
ANISOU 3511  CG1 VAL A 461     8485   6386   5046   -482   -898    348       C  
ATOM   3512  CG2 VAL A 461      38.260  14.538  39.275  1.00 48.67           C  
ANISOU 3512  CG2 VAL A 461     7851   5902   4740   -628  -1006    394       C  
ATOM   3513  N   LEU A 462      41.824  12.320  40.932  1.00 54.98           N  
ANISOU 3513  N   LEU A 462     8722   6797   5372   -579   -890    372       N  
ATOM   3514  CA  LEU A 462      43.147  11.719  40.858  1.00 55.89           C  
ANISOU 3514  CA  LEU A 462     8898   6912   5425   -516   -860    362       C  
ATOM   3515  C   LEU A 462      43.043  10.210  41.132  1.00 58.39           C  
ANISOU 3515  C   LEU A 462     9263   7180   5742   -532   -960    399       C  
ATOM   3516  O   LEU A 462      43.760   9.407  40.528  1.00 58.39           O  
ANISOU 3516  O   LEU A 462     9373   7119   5694   -462   -989    391       O  
ATOM   3517  CB  LEU A 462      44.094  12.383  41.861  1.00 56.24           C  
ANISOU 3517  CB  LEU A 462     8832   7061   5475   -529   -748    341       C  
ATOM   3518  CG  LEU A 462      44.459  13.876  41.645  1.00 56.56           C  
ANISOU 3518  CG  LEU A 462     8806   7127   5556   -511   -638    298       C  
ATOM   3519  CD1 LEU A 462      45.039  14.457  42.913  1.00 55.40           C  
ANISOU 3519  CD1 LEU A 462     8528   7080   5443   -549   -580    254       C  
ATOM   3520  CD2 LEU A 462      45.432  14.101  40.502  1.00 53.61           C  
ANISOU 3520  CD2 LEU A 462     8507   6693   5167   -407   -572    302       C  
ATOM   3521  N   HIS A 463      42.134   9.823  42.023  1.00 57.24           N  
ANISOU 3521  N   HIS A 463     9034   7051   5662   -617  -1000    449       N  
ATOM   3522  CA  HIS A 463      42.047   8.442  42.432  1.00 57.32           C  
ANISOU 3522  CA  HIS A 463     9061   7011   5708   -637  -1071    506       C  
ATOM   3523  C   HIS A 463      41.300   7.607  41.410  1.00 60.61           C  
ANISOU 3523  C   HIS A 463     9571   7272   6184   -631  -1222    496       C  
ATOM   3524  O   HIS A 463      41.605   6.428  41.206  1.00 58.63           O  
ANISOU 3524  O   HIS A 463     9394   6935   5949   -606  -1295    505       O  
ATOM   3525  CB  HIS A 463      41.374   8.336  43.800  1.00 58.29           C  
ANISOU 3525  CB  HIS A 463     9052   7207   5888   -710  -1034    588       C  
ATOM   3526  CG  HIS A 463      41.263   6.936  44.300  1.00 58.79           C  
ANISOU 3526  CG  HIS A 463     9112   7215   6010   -727  -1083    677       C  
ATOM   3527  CD2 HIS A 463      42.164   6.130  44.906  1.00 62.98           C  
ANISOU 3527  CD2 HIS A 463     9655   7778   6496   -692  -1056    719       C  
ATOM   3528  ND1 HIS A 463      40.118   6.191  44.162  1.00 59.57           N  
ANISOU 3528  ND1 HIS A 463     9184   7195   6254   -781  -1175    743       N  
ATOM   3529  CE1 HIS A 463      40.311   4.983  44.660  1.00 62.89           C  
ANISOU 3529  CE1 HIS A 463     9599   7568   6727   -782  -1193    826       C  
ATOM   3530  NE2 HIS A 463      41.546   4.920  45.121  1.00 65.83           N  
ANISOU 3530  NE2 HIS A 463    10001   8038   6974   -725  -1119    816       N  
ATOM   3531  N   GLU A 464      40.321   8.218  40.759  1.00 63.65           N  
ANISOU 3531  N   GLU A 464     9956   7618   6612   -649  -1281    471       N  
ATOM   3532  CA  GLU A 464      39.534   7.531  39.736  1.00 68.10           C  
ANISOU 3532  CA  GLU A 464    10606   8032   7238   -638  -1460    438       C  
ATOM   3533  C   GLU A 464      40.367   6.913  38.585  1.00 70.60           C  
ANISOU 3533  C   GLU A 464    11113   8267   7444   -518  -1528    359       C  
ATOM   3534  O   GLU A 464      39.937   5.925  37.994  1.00 71.88           O  
ANISOU 3534  O   GLU A 464    11356   8294   7662   -504  -1693    323       O  
ATOM   3535  CB  GLU A 464      38.449   8.468  39.194  1.00 71.06           C  
ANISOU 3535  CB  GLU A 464    10945   8397   7656   -658  -1509    420       C  
ATOM   3536  CG  GLU A 464      37.442   7.833  38.244  1.00 78.80           C  
ANISOU 3536  CG  GLU A 464    11986   9226   8728   -656  -1728    380       C  
ATOM   3537  CD  GLU A 464      37.605   8.299  36.804  1.00 89.73           C  
ANISOU 3537  CD  GLU A 464    13535  10583   9974   -531  -1802    285       C  
ATOM   3538  OE1 GLU A 464      37.929   9.505  36.609  1.00101.06           O  
ANISOU 3538  OE1 GLU A 464    14970  12118  11311   -485  -1671    287       O  
ATOM   3539  OE2 GLU A 464      37.395   7.481  35.870  1.00 92.42           O1-
ANISOU 3539  OE2 GLU A 464    14008  10801  10306   -469  -1989    210       O1-
ATOM   3540  N   LYS A 465      41.551   7.452  38.286  1.00 69.54           N  
ANISOU 3540  N   LYS A 465    11046   8206   7172   -426  -1402    333       N  
ATOM   3541  CA  LYS A 465      42.335   6.947  37.154  1.00 74.03           C  
ANISOU 3541  CA  LYS A 465    11801   8704   7622   -287  -1437    271       C  
ATOM   3542  C   LYS A 465      43.019   5.619  37.516  1.00 77.76           C  
ANISOU 3542  C   LYS A 465    12313   9118   8113   -276  -1462    284       C  
ATOM   3543  O   LYS A 465      42.844   4.601  36.821  1.00 84.19           O  
ANISOU 3543  O   LYS A 465    13254   9801   8933   -225  -1604    230       O  
ATOM   3544  CB  LYS A 465      43.342   7.999  36.644  1.00 70.62           C  
ANISOU 3544  CB  LYS A 465    11413   8353   7066   -181  -1272    266       C  
ATOM   3545  N   THR A 466      43.784   5.631  38.605  1.00 76.47           N  
ANISOU 3545  N   THR A 466    12044   9048   7964   -318  -1334    348       N  
ATOM   3546  CA  THR A 466      44.446   4.433  39.155  1.00 74.16           C  
ANISOU 3546  CA  THR A 466    11758   8719   7699   -314  -1338    386       C  
ATOM   3547  C   THR A 466      43.694   4.066  40.413  1.00 71.43           C  
ANISOU 3547  C   THR A 466    11260   8398   7483   -441  -1356    472       C  
ATOM   3548  O   THR A 466      44.109   4.530  41.504  1.00 73.61           O  
ANISOU 3548  O   THR A 466    11419   8808   7741   -477  -1239    529       O  
ATOM   3549  CB  THR A 466      45.908   4.731  39.600  1.00 71.20           C  
ANISOU 3549  CB  THR A 466    11354   8449   7250   -258  -1179    413       C  
ATOM   3550  CG2 THR A 466      45.973   5.797  40.697  1.00 62.94           C  
ANISOU 3550  CG2 THR A 466    10140   7555   6218   -334  -1071    449       C  
ATOM   3551  OG1 THR A 466      46.496   3.537  40.124  1.00 69.52           O  
ANISOU 3551  OG1 THR A 466    11147   8200   7069   -249  -1191    458       O  
ATOM   3552  N   PRO A 467      42.578   3.295  40.289  1.00 66.13           N  
ANISOU 3552  N   PRO A 467    10582   7598   6945   -500  -1499    484       N  
ATOM   3553  CA  PRO A 467      41.752   3.032  41.487  1.00 64.93           C  
ANISOU 3553  CA  PRO A 467    10268   7468   6936   -613  -1486    598       C  
ATOM   3554  C   PRO A 467      42.347   1.912  42.314  1.00 66.88           C  
ANISOU 3554  C   PRO A 467    10486   7700   7225   -610  -1451    689       C  
ATOM   3555  O   PRO A 467      42.480   0.783  41.822  1.00 68.10           O  
ANISOU 3555  O   PRO A 467    10722   7704   7447   -581  -1548    671       O  
ATOM   3556  CB  PRO A 467      40.354   2.674  40.929  1.00 62.06           C  
ANISOU 3556  CB  PRO A 467     9890   6950   6740   -673  -1654    583       C  
ATOM   3557  CG  PRO A 467      40.480   2.696  39.443  1.00 62.87           C  
ANISOU 3557  CG  PRO A 467    10168   6958   6761   -583  -1779    442       C  
ATOM   3558  CD  PRO A 467      41.945   2.755  39.076  1.00 65.60           C  
ANISOU 3558  CD  PRO A 467    10640   7365   6919   -464  -1680    395       C  
ATOM   3559  N   VAL A 468      42.739   2.251  43.547  1.00 65.55           N  
ANISOU 3559  N   VAL A 468    10211   7689   7008   -627  -1316    776       N  
ATOM   3560  CA  VAL A 468      43.442   1.325  44.440  1.00 64.77           C  
ANISOU 3560  CA  VAL A 468    10082   7616   6914   -604  -1263    876       C  
ATOM   3561  C   VAL A 468      42.880   1.224  45.870  1.00 65.12           C  
ANISOU 3561  C   VAL A 468     9979   7753   7010   -653  -1181   1028       C  
ATOM   3562  O   VAL A 468      43.272   0.325  46.614  1.00 71.76           O  
ANISOU 3562  O   VAL A 468    10792   8599   7875   -628  -1145   1138       O  
ATOM   3563  CB  VAL A 468      44.933   1.705  44.550  1.00 62.79           C  
ANISOU 3563  CB  VAL A 468     9872   7486   6501   -521  -1175    831       C  
ATOM   3564  CG1 VAL A 468      45.618   1.529  43.207  1.00 58.24           C  
ANISOU 3564  CG1 VAL A 468     9446   6805   5876   -442  -1223    722       C  
ATOM   3565  CG2 VAL A 468      45.090   3.119  45.121  1.00 58.25           C  
ANISOU 3565  CG2 VAL A 468     9217   7091   5823   -532  -1079    799       C  
ATOM   3566  N   SER A 469      41.980   2.127  46.241  1.00 63.60           N  
ANISOU 3566  N   SER A 469     9700   7635   6831   -705  -1142   1043       N  
ATOM   3567  CA  SER A 469      41.390   2.155  47.560  1.00 65.80           C  
ANISOU 3567  CA  SER A 469     9852   8014   7135   -727  -1044   1188       C  
ATOM   3568  C   SER A 469      39.862   2.114  47.529  1.00 67.89           C  
ANISOU 3568  C   SER A 469    10024   8179   7593   -806  -1072   1266       C  
ATOM   3569  O   SER A 469      39.224   3.109  47.211  1.00 69.05           O  
ANISOU 3569  O   SER A 469    10145   8353   7738   -841  -1075   1202       O  
ATOM   3570  CB  SER A 469      41.807   3.414  48.295  1.00 64.57           C  
ANISOU 3570  CB  SER A 469     9661   8072   6800   -695   -938   1141       C  
ATOM   3571  OG  SER A 469      40.908   3.651  49.364  1.00 66.00           O  
ANISOU 3571  OG  SER A 469     9734   8339   7004   -709   -848   1260       O  
ATOM   3572  N   GLU A 470      39.291   0.977  47.917  1.00 69.25           N  
ANISOU 3572  N   GLU A 470    10128   8233   7950   -832  -1081   1418       N  
ATOM   3573  CA  GLU A 470      37.841   0.789  47.969  1.00 70.96           C  
ANISOU 3573  CA  GLU A 470    10223   8330   8407   -910  -1103   1524       C  
ATOM   3574  C   GLU A 470      37.090   1.853  48.777  1.00 70.73           C  
ANISOU 3574  C   GLU A 470    10087   8451   8334   -918   -971   1590       C  
ATOM   3575  O   GLU A 470      35.909   2.119  48.513  1.00 74.09           O  
ANISOU 3575  O   GLU A 470    10424   8791   8936   -984  -1003   1621       O  
ATOM   3576  CB  GLU A 470      37.501  -0.598  48.549  1.00 73.79           C  
ANISOU 3576  CB  GLU A 470    10497   8558   8982   -921  -1084   1721       C  
ATOM   3577  CG  GLU A 470      38.023  -1.787  47.736  1.00 76.26           C  
ANISOU 3577  CG  GLU A 470    10899   8672   9404   -920  -1227   1665       C  
ATOM   3578  N   LYS A 471      37.757   2.449  49.759  1.00 67.60           N  
ANISOU 3578  N   LYS A 471     9700   8274   7712   -845   -833   1604       N  
ATOM   3579  CA  LYS A 471      37.116   3.417  50.645  1.00 67.63           C  
ANISOU 3579  CA  LYS A 471     9617   8429   7648   -828   -696   1660       C  
ATOM   3580  C   LYS A 471      36.996   4.786  49.983  1.00 65.11           C  
ANISOU 3580  C   LYS A 471     9329   8159   7251   -855   -730   1482       C  
ATOM   3581  O   LYS A 471      35.968   5.464  50.101  1.00 64.30           O  
ANISOU 3581  O   LYS A 471     9142   8063   7225   -887   -683   1515       O  
ATOM   3582  CB  LYS A 471      37.909   3.542  51.947  1.00 70.00           C  
ANISOU 3582  CB  LYS A 471     9931   8946   7718   -720   -561   1717       C  
ATOM   3583  CG  LYS A 471      37.862   2.288  52.789  1.00 74.50           C  
ANISOU 3583  CG  LYS A 471    10454   9494   8360   -673   -487   1939       C  
ATOM   3584  CD  LYS A 471      38.652   2.453  54.073  1.00 78.82           C  
ANISOU 3584  CD  LYS A 471    11028  10274   8644   -542   -369   1988       C  
ATOM   3585  CE  LYS A 471      40.158   2.437  53.839  1.00 79.79           C  
ANISOU 3585  CE  LYS A 471    11261  10466   8592   -500   -454   1837       C  
ATOM   3586  NZ  LYS A 471      40.886   2.139  55.115  1.00 77.06           N1+
ANISOU 3586  NZ  LYS A 471    10928  10307   8044   -366   -368   1933       N1+
ATOM   3587  N   VAL A 472      38.053   5.194  49.292  1.00 60.59           N  
ANISOU 3587  N   VAL A 472     8868   7614   6538   -835   -797   1310       N  
ATOM   3588  CA  VAL A 472      38.007   6.413  48.504  1.00 59.15           C  
ANISOU 3588  CA  VAL A 472     8719   7449   6308   -855   -831   1153       C  
ATOM   3589  C   VAL A 472      36.944   6.242  47.437  1.00 60.03           C  
ANISOU 3589  C   VAL A 472     8813   7380   6616   -927   -949   1149       C  
ATOM   3590  O   VAL A 472      36.021   7.054  47.323  1.00 61.15           O  
ANISOU 3590  O   VAL A 472     8888   7524   6823   -962   -933   1146       O  
ATOM   3591  CB  VAL A 472      39.364   6.715  47.846  1.00 57.44           C  
ANISOU 3591  CB  VAL A 472     8618   7261   5945   -812   -874   1000       C  
ATOM   3592  CG1 VAL A 472      39.213   7.693  46.708  1.00 56.05           C  
ANISOU 3592  CG1 VAL A 472     8485   7040   5772   -830   -925    869       C  
ATOM   3593  CG2 VAL A 472      40.327   7.239  48.889  1.00 57.47           C  
ANISOU 3593  CG2 VAL A 472     8613   7452   5770   -747   -775    970       C  
ATOM   3594  N   THR A 473      37.043   5.149  46.691  1.00 60.21           N  
ANISOU 3594  N   THR A 473     8893   7241   6744   -943  -1078   1148       N  
ATOM   3595  CA  THR A 473      36.031   4.835  45.685  1.00 62.38           C  
ANISOU 3595  CA  THR A 473     9154   7329   7220  -1004  -1232   1131       C  
ATOM   3596  C   THR A 473      34.598   4.892  46.235  1.00 64.27           C  
ANISOU 3596  C   THR A 473     9224   7525   7670  -1069  -1195   1273       C  
ATOM   3597  O   THR A 473      33.710   5.452  45.592  1.00 62.21           O  
ANISOU 3597  O   THR A 473     8923   7201   7514  -1111  -1272   1234       O  
ATOM   3598  CB  THR A 473      36.270   3.453  45.052  1.00 61.33           C  
ANISOU 3598  CB  THR A 473     9091   7013   7200  -1006  -1378   1124       C  
ATOM   3599  CG2 THR A 473      35.329   3.247  43.861  1.00 58.88           C  
ANISOU 3599  CG2 THR A 473     8791   6510   7069  -1052  -1581   1051       C  
ATOM   3600  OG1 THR A 473      37.623   3.374  44.602  1.00 59.95           O  
ANISOU 3600  OG1 THR A 473     9067   6881   6830   -931  -1385   1012       O  
ATOM   3601  N   LYS A 474      34.380   4.310  47.410  1.00 66.60           N  
ANISOU 3601  N   LYS A 474     9417   7855   8032  -1066  -1072   1450       N  
ATOM   3602  CA  LYS A 474      33.051   4.343  48.041  1.00 72.60           C  
ANISOU 3602  CA  LYS A 474    10002   8580   9004  -1110   -994   1620       C  
ATOM   3603  C   LYS A 474      32.682   5.793  48.362  1.00 71.36           C  
ANISOU 3603  C   LYS A 474     9809   8578   8728  -1094   -881   1582       C  
ATOM   3604  O   LYS A 474      31.601   6.256  48.008  1.00 74.72           O  
ANISOU 3604  O   LYS A 474    10141   8934   9317  -1145   -914   1601       O  
ATOM   3605  CB  LYS A 474      33.032   3.465  49.312  1.00 77.25           C  
ANISOU 3605  CB  LYS A 474    10505   9201   9647  -1075   -843   1840       C  
ATOM   3606  CG  LYS A 474      31.706   3.380  50.068  1.00 79.18           C  
ANISOU 3606  CG  LYS A 474    10557   9406  10124  -1100   -720   2062       C  
ATOM   3607  CD  LYS A 474      30.968   2.064  49.864  1.00 84.76           C  
ANISOU 3607  CD  LYS A 474    11142   9862  11199  -1169   -803   2215       C  
ATOM   3608  CE  LYS A 474      30.030   1.756  51.030  1.00 88.19           C  
ANISOU 3608  CE  LYS A 474    11386  10299  11824  -1149   -596   2507       C  
ATOM   3609  NZ  LYS A 474      28.930   0.803  50.676  1.00 89.45           N1+
ANISOU 3609  NZ  LYS A 474    11366  10178  12444  -1245   -688   2653       N1+
ATOM   3610  N   CYS A 475      33.589   6.524  48.995  1.00 66.83           N  
ANISOU 3610  N   CYS A 475     9305   8203   7885  -1020   -761   1516       N  
ATOM   3611  CA  CYS A 475      33.280   7.888  49.376  1.00 68.46           C  
ANISOU 3611  CA  CYS A 475     9477   8546   7987   -997   -651   1469       C  
ATOM   3612  C   CYS A 475      33.126   8.805  48.182  1.00 66.64           C  
ANISOU 3612  C   CYS A 475     9290   8265   7766  -1035   -760   1310       C  
ATOM   3613  O   CYS A 475      32.377   9.780  48.251  1.00 71.26           O  
ANISOU 3613  O   CYS A 475     9805   8885   8386  -1045   -701   1307       O  
ATOM   3614  CB  CYS A 475      34.337   8.447  50.326  1.00 70.04           C  
ANISOU 3614  CB  CYS A 475     9742   8958   7913   -906   -528   1409       C  
ATOM   3615  SG  CYS A 475      34.158   7.856  52.018  1.00 77.45           S  
ANISOU 3615  SG  CYS A 475    10611  10024   8793   -819   -341   1619       S  
ATOM   3616  N   CYS A 476      33.846   8.533  47.101  1.00 64.27           N  
ANISOU 3616  N   CYS A 476     9109   7887   7423  -1040   -904   1185       N  
ATOM   3617  CA  CYS A 476      33.807   9.428  45.929  1.00 62.73           C  
ANISOU 3617  CA  CYS A 476     8976   7658   7203  -1047   -994   1044       C  
ATOM   3618  C   CYS A 476      32.576   9.190  45.085  1.00 62.90           C  
ANISOU 3618  C   CYS A 476     8937   7515   7448  -1107  -1138   1075       C  
ATOM   3619  O   CYS A 476      31.975  10.124  44.578  1.00 66.77           O  
ANISOU 3619  O   CYS A 476     9400   8003   7968  -1117  -1156   1032       O  
ATOM   3620  CB  CYS A 476      35.070   9.281  45.081  1.00 60.26           C  
ANISOU 3620  CB  CYS A 476     8822   7335   6741  -1000  -1070    910       C  
ATOM   3621  SG  CYS A 476      36.548   9.984  45.878  1.00 59.03           S  
ANISOU 3621  SG  CYS A 476     8715   7370   6345   -930   -921    835       S  
ATOM   3622  N   THR A 477      32.156   7.944  44.987  1.00 64.88           N  
ANISOU 3622  N   THR A 477     9152   7620   7878  -1147  -1243   1155       N  
ATOM   3623  CA  THR A 477      31.062   7.602  44.101  1.00 67.92           C  
ANISOU 3623  CA  THR A 477     9482   7826   8500  -1205  -1429   1159       C  
ATOM   3624  C   THR A 477      29.679   7.533  44.762  1.00 70.56           C  
ANISOU 3624  C   THR A 477     9604   8100   9104  -1270  -1377   1331       C  
ATOM   3625  O   THR A 477      28.672   7.480  44.060  1.00 70.43           O  
ANISOU 3625  O   THR A 477     9512   7944   9305  -1321  -1531   1333       O  
ATOM   3626  CB  THR A 477      31.347   6.261  43.409  1.00 66.24           C  
ANISOU 3626  CB  THR A 477     9349   7441   8376  -1213  -1619   1118       C  
ATOM   3627  CG2 THR A 477      32.665   6.329  42.654  1.00 65.06           C  
ANISOU 3627  CG2 THR A 477     9410   7340   7970  -1133  -1662    957       C  
ATOM   3628  OG1 THR A 477      31.449   5.251  44.399  1.00 66.53           O  
ANISOU 3628  OG1 THR A 477     9310   7454   8513  -1232  -1533   1263       O  
ATOM   3629  N   GLU A 478      29.614   7.519  46.086  1.00 75.00           N  
ANISOU 3629  N   GLU A 478    10070   8767   9658  -1257  -1166   1480       N  
ATOM   3630  CA  GLU A 478      28.340   7.221  46.749  1.00 82.98           C  
ANISOU 3630  CA  GLU A 478    10874   9701  10953  -1304  -1094   1683       C  
ATOM   3631  C   GLU A 478      27.411   8.393  46.687  1.00 82.52           C  
ANISOU 3631  C   GLU A 478    10718   9683  10953  -1316  -1042   1691       C  
ATOM   3632  O   GLU A 478      26.235   8.231  46.394  1.00 92.54           O  
ANISOU 3632  O   GLU A 478    11836  10811  12516  -1377  -1122   1778       O  
ATOM   3633  CB  GLU A 478      28.513   6.781  48.202  1.00 85.92           C  
ANISOU 3633  CB  GLU A 478    11181  10175  11289  -1258   -865   1867       C  
ATOM   3634  CG  GLU A 478      28.618   5.271  48.345  1.00 93.22           C  
ANISOU 3634  CG  GLU A 478    12074  10955  12393  -1283   -922   1982       C  
ATOM   3635  CD  GLU A 478      28.280   4.784  49.738  1.00 99.95           C  
ANISOU 3635  CD  GLU A 478    12796  11859  13320  -1240   -689   2239       C  
ATOM   3636  OE1 GLU A 478      28.427   5.568  50.700  1.00106.56           O  
ANISOU 3636  OE1 GLU A 478    13641  12903  13944  -1157   -479   2283       O  
ATOM   3637  OE2 GLU A 478      27.866   3.613  49.868  1.00103.47           O1-
ANISOU 3637  OE2 GLU A 478    13136  12135  14043  -1280   -717   2398       O1-
ATOM   3638  N   SER A 479      27.939   9.568  46.972  1.00 79.10           N  
ANISOU 3638  N   SER A 479    10360   9432  10262  -1256   -911   1602       N  
ATOM   3639  CA  SER A 479      27.166  10.788  46.870  1.00 77.93           C  
ANISOU 3639  CA  SER A 479    10136   9327  10148  -1256   -854   1591       C  
ATOM   3640  C   SER A 479      28.101  11.967  46.736  1.00 70.52           C  
ANISOU 3640  C   SER A 479     9334   8542   8917  -1196   -792   1420       C  
ATOM   3641  O   SER A 479      29.177  11.971  47.302  1.00 69.79           O  
ANISOU 3641  O   SER A 479     9340   8570   8606  -1144   -704   1366       O  
ATOM   3642  CB  SER A 479      26.295  10.960  48.111  1.00 80.38           C  
ANISOU 3642  CB  SER A 479    10278   9693  10569  -1237   -632   1787       C  
ATOM   3643  OG  SER A 479      25.668  12.230  48.137  1.00 87.73           O  
ANISOU 3643  OG  SER A 479    11149  10686  11499  -1220   -545   1768       O  
ATOM   3644  N   LEU A 480      27.680  12.964  45.983  1.00 66.68           N  
ANISOU 3644  N   LEU A 480     8843   8042   8452  -1203   -843   1342       N  
ATOM   3645  CA  LEU A 480      28.470  14.162  45.822  1.00 67.81           C  
ANISOU 3645  CA  LEU A 480     9087   8304   8372  -1149   -773   1197       C  
ATOM   3646  C   LEU A 480      28.415  15.052  47.059  1.00 66.87           C  
ANISOU 3646  C   LEU A 480     8908   8334   8164  -1102   -542   1225       C  
ATOM   3647  O   LEU A 480      29.415  15.636  47.438  1.00 67.70           O  
ANISOU 3647  O   LEU A 480     9102   8557   8064  -1050   -459   1115       O  
ATOM   3648  CB  LEU A 480      27.985  14.944  44.604  1.00 67.23           C  
ANISOU 3648  CB  LEU A 480     9022   8160   8361  -1159   -893   1125       C  
ATOM   3649  CG  LEU A 480      28.852  16.140  44.227  1.00 63.33           C  
ANISOU 3649  CG  LEU A 480     8633   7757   7673  -1102   -832    984       C  
ATOM   3650  CD1 LEU A 480      30.303  15.716  44.078  1.00 59.80           C  
ANISOU 3650  CD1 LEU A 480     8339   7352   7030  -1066   -852    885       C  
ATOM   3651  CD2 LEU A 480      28.308  16.729  42.933  1.00 63.74           C  
ANISOU 3651  CD2 LEU A 480     8698   7727   7793  -1097   -963    945       C  
ATOM   3652  N   VAL A 481      27.241  15.133  47.674  1.00 70.88           N  
ANISOU 3652  N   VAL A 481     9265   8827   8841  -1112   -444   1371       N  
ATOM   3653  CA  VAL A 481      26.994  16.018  48.824  1.00 72.66           C  
ANISOU 3653  CA  VAL A 481     9433   9185   8990  -1047   -219   1402       C  
ATOM   3654  C   VAL A 481      27.595  15.487  50.132  1.00 75.50           C  
ANISOU 3654  C   VAL A 481     9828   9672   9187   -978    -77   1454       C  
ATOM   3655  O   VAL A 481      28.124  16.257  50.928  1.00 77.37           O  
ANISOU 3655  O   VAL A 481    10117  10053   9226   -899     54   1370       O  
ATOM   3656  CB  VAL A 481      25.477  16.204  49.064  1.00 73.32           C  
ANISOU 3656  CB  VAL A 481     9333   9205   9321  -1065   -141   1570       C  
ATOM   3657  CG1 VAL A 481      24.738  16.381  47.752  1.00 74.97           C  
ANISOU 3657  CG1 VAL A 481     9486   9265   9736  -1137   -326   1556       C  
ATOM   3658  CG2 VAL A 481      24.886  15.006  49.789  1.00 78.63           C  
ANISOU 3658  CG2 VAL A 481     9896   9829  10150  -1073    -81   1783       C  
ATOM   3659  N   ASN A 482      27.502  14.173  50.344  1.00 77.49           N  
ANISOU 3659  N   ASN A 482    10051   9862   9529  -1000   -111   1591       N  
ATOM   3660  CA  ASN A 482      27.982  13.540  51.566  1.00 78.72           C  
ANISOU 3660  CA  ASN A 482    10233  10132   9545   -923     24   1679       C  
ATOM   3661  C   ASN A 482      29.463  13.126  51.501  1.00 78.49           C  
ANISOU 3661  C   ASN A 482    10361  10166   9295   -902    -59   1546       C  
ATOM   3662  O   ASN A 482      29.925  12.386  52.369  1.00 80.60           O  
ANISOU 3662  O   ASN A 482    10656  10509   9460   -842     11   1627       O  
ATOM   3663  CB  ASN A 482      27.136  12.294  51.902  1.00 81.91           C  
ANISOU 3663  CB  ASN A 482    10508  10428  10187   -949     54   1927       C  
ATOM   3664  CG  ASN A 482      25.655  12.604  52.129  1.00 83.34           C  
ANISOU 3664  CG  ASN A 482    10503  10545  10618   -959    165   2099       C  
ATOM   3665  ND2 ASN A 482      24.800  11.749  51.584  1.00 85.66           N  
ANISOU 3665  ND2 ASN A 482    10661  10645  11240  -1049     62   2239       N  
ATOM   3666  OD1 ASN A 482      25.282  13.570  52.802  1.00 80.38           O  
ANISOU 3666  OD1 ASN A 482    10100  10283  10159   -882    340   2106       O  
ATOM   3667  N   ARG A 483      30.208  13.580  50.490  1.00 74.72           N  
ANISOU 3667  N   ARG A 483     9982   9659   8751   -939   -198   1360       N  
ATOM   3668  CA  ARG A 483      31.634  13.232  50.386  1.00 71.49           C  
ANISOU 3668  CA  ARG A 483     9707   9301   8155   -915   -267   1241       C  
ATOM   3669  C   ARG A 483      32.431  13.640  51.593  1.00 69.60           C  
ANISOU 3669  C   ARG A 483     9516   9247   7681   -816   -141   1187       C  
ATOM   3670  O   ARG A 483      33.265  12.880  52.058  1.00 68.63           O  
ANISOU 3670  O   ARG A 483     9453   9180   7443   -777   -151   1201       O  
ATOM   3671  CB  ARG A 483      32.294  13.904  49.187  1.00 70.46           C  
ANISOU 3671  CB  ARG A 483     9663   9125   7984   -945   -387   1061       C  
ATOM   3672  CG  ARG A 483      32.331  13.076  47.929  1.00 70.30           C  
ANISOU 3672  CG  ARG A 483     9691   8948   8071  -1003   -568   1056       C  
ATOM   3673  CD  ARG A 483      32.754  13.925  46.747  1.00 68.49           C  
ANISOU 3673  CD  ARG A 483     9538   8684   7800  -1005   -648    909       C  
ATOM   3674  NE  ARG A 483      32.789  13.122  45.538  1.00 66.24           N  
ANISOU 3674  NE  ARG A 483     9324   8260   7583  -1031   -826    893       N  
ATOM   3675  CZ  ARG A 483      33.271  13.531  44.379  1.00 63.40           C  
ANISOU 3675  CZ  ARG A 483     9064   7859   7167  -1009   -911    786       C  
ATOM   3676  NH1 ARG A 483      33.749  14.765  44.249  1.00 61.46           N1+
ANISOU 3676  NH1 ARG A 483     8838   7686   6830   -972   -826    698       N1+
ATOM   3677  NH2 ARG A 483      33.259  12.694  43.341  1.00 63.89           N  
ANISOU 3677  NH2 ARG A 483     9206   7798   7271  -1011  -1079    769       N  
ATOM   3678  N   ARG A 484      32.228  14.863  52.070  1.00 70.86           N  
ANISOU 3678  N   ARG A 484     9656   9500   7767   -770    -38   1108       N  
ATOM   3679  CA  ARG A 484      33.032  15.349  53.195  1.00 72.90           C  
ANISOU 3679  CA  ARG A 484     9971   9934   7792   -664     49   1012       C  
ATOM   3680  C   ARG A 484      32.773  14.527  54.468  1.00 73.58           C  
ANISOU 3680  C   ARG A 484    10043  10123   7793   -571    168   1182       C  
ATOM   3681  O   ARG A 484      33.730  14.073  55.110  1.00 76.03           O  
ANISOU 3681  O   ARG A 484    10427  10536   7923   -501    157   1154       O  
ATOM   3682  CB  ARG A 484      32.834  16.848  53.439  1.00 73.60           C  
ANISOU 3682  CB  ARG A 484    10045  10085   7837   -626    125    875       C  
ATOM   3683  CG  ARG A 484      34.023  17.512  54.118  1.00 79.65           C  
ANISOU 3683  CG  ARG A 484    10889  10983   8391   -546    123    681       C  
ATOM   3684  CD  ARG A 484      34.012  17.425  55.646  1.00 78.86           C  
ANISOU 3684  CD  ARG A 484    10815  11057   8093   -405    238    711       C  
ATOM   3685  NE  ARG A 484      32.823  18.061  56.206  1.00 78.43           N  
ANISOU 3685  NE  ARG A 484    10698  11033   8067   -348    392    777       N  
ATOM   3686  CZ  ARG A 484      31.908  17.460  56.970  1.00 82.49           C  
ANISOU 3686  CZ  ARG A 484    11170  11594   8580   -277    533    988       C  
ATOM   3687  NH1 ARG A 484      32.034  16.186  57.337  1.00 82.45           N1+
ANISOU 3687  NH1 ARG A 484    11175  11610   8542   -252    542   1159       N1+
ATOM   3688  NH2 ARG A 484      30.855  18.149  57.394  1.00 82.53           N  
ANISOU 3688  NH2 ARG A 484    11115  11618   8627   -221    683   1041       N  
ATOM   3689  N   PRO A 485      31.490  14.310  54.825  1.00 71.76           N  
ANISOU 3689  N   PRO A 485     9708   9859   7698   -561    287   1374       N  
ATOM   3690  CA  PRO A 485      31.181  13.417  55.959  1.00 72.64           C  
ANISOU 3690  CA  PRO A 485     9794  10049   7757   -464    424   1584       C  
ATOM   3691  C   PRO A 485      31.690  11.979  55.791  1.00 70.58           C  
ANISOU 3691  C   PRO A 485     9553   9722   7542   -497    341   1697       C  
ATOM   3692  O   PRO A 485      32.274  11.434  56.718  1.00 70.41           O  
ANISOU 3692  O   PRO A 485     9586   9823   7343   -391    402   1757       O  
ATOM   3693  CB  PRO A 485      29.657  13.454  56.024  1.00 74.44           C  
ANISOU 3693  CB  PRO A 485     9876  10194   8212   -480    549   1780       C  
ATOM   3694  CG  PRO A 485      29.274  14.753  55.380  1.00 73.15           C  
ANISOU 3694  CG  PRO A 485     9690   9994   8108   -530    522   1626       C  
ATOM   3695  CD  PRO A 485      30.279  14.969  54.300  1.00 70.75           C  
ANISOU 3695  CD  PRO A 485     9475   9633   7774   -619    322   1416       C  
ATOM   3696  N   CYS A 486      31.484  11.390  54.615  1.00 69.79           N  
ANISOU 3696  N   CYS A 486     9417   9432   7669   -630    197   1715       N  
ATOM   3697  CA  CYS A 486      32.024  10.079  54.309  1.00 69.44           C  
ANISOU 3697  CA  CYS A 486     9401   9300   7683   -667     97   1786       C  
ATOM   3698  C   CYS A 486      33.498   9.991  54.639  1.00 68.70           C  
ANISOU 3698  C   CYS A 486     9440   9334   7330   -601     51   1654       C  
ATOM   3699  O   CYS A 486      33.934   9.045  55.278  1.00 77.87           O  
ANISOU 3699  O   CYS A 486    10622  10538   8425   -540     84   1769       O  
ATOM   3700  CB  CYS A 486      31.833   9.742  52.847  1.00 70.89           C  
ANISOU 3700  CB  CYS A 486     9573   9277   8085   -803    -93   1729       C  
ATOM   3701  SG  CYS A 486      32.147   8.007  52.427  1.00 79.45           S  
ANISOU 3701  SG  CYS A 486    10665  10199   9322   -854   -214   1842       S  
ATOM   3702  N   PHE A 487      34.274  10.973  54.221  1.00 68.14           N  
ANISOU 3702  N   PHE A 487     9445   9317   7130   -608    -23   1425       N  
ATOM   3703  CA  PHE A 487      35.719  10.949  54.472  1.00 69.58           C  
ANISOU 3703  CA  PHE A 487     9731   9604   7103   -553    -82   1290       C  
ATOM   3704  C   PHE A 487      36.052  11.184  55.937  1.00 71.67           C  
ANISOU 3704  C   PHE A 487    10025  10078   7129   -405     32   1301       C  
ATOM   3705  O   PHE A 487      36.938  10.539  56.487  1.00 73.49           O  
ANISOU 3705  O   PHE A 487    10311  10392   7219   -335     10   1318       O  
ATOM   3706  CB  PHE A 487      36.452  11.963  53.587  1.00 67.55           C  
ANISOU 3706  CB  PHE A 487     9524   9325   6817   -601   -183   1056       C  
ATOM   3707  CG  PHE A 487      36.779  11.427  52.225  1.00 68.68           C  
ANISOU 3707  CG  PHE A 487     9703   9304   7090   -694   -321   1025       C  
ATOM   3708  CD1 PHE A 487      37.780  10.472  52.070  1.00 68.45           C  
ANISOU 3708  CD1 PHE A 487     9737   9255   7014   -682   -396   1029       C  
ATOM   3709  CD2 PHE A 487      36.075  11.837  51.110  1.00 68.95           C  
ANISOU 3709  CD2 PHE A 487     9710   9205   7281   -776   -377    996       C  
ATOM   3710  CE1 PHE A 487      38.080   9.944  50.836  1.00 65.39           C  
ANISOU 3710  CE1 PHE A 487     9399   8719   6727   -744   -514    997       C  
ATOM   3711  CE2 PHE A 487      36.378  11.319  49.863  1.00 69.93           C  
ANISOU 3711  CE2 PHE A 487     9890   9189   7491   -832   -509    960       C  
ATOM   3712  CZ  PHE A 487      37.380  10.369  49.731  1.00 68.77           C  
ANISOU 3712  CZ  PHE A 487     9817   9024   7288   -813   -573    958       C  
ATOM   3713  N   SER A 488      35.341  12.111  56.562  1.00 72.82           N  
ANISOU 3713  N   SER A 488    10138  10310   7221   -346    148   1287       N  
ATOM   3714  CA  SER A 488      35.551  12.410  57.969  1.00 76.32           C  
ANISOU 3714  CA  SER A 488    10625  10959   7413   -179    257   1283       C  
ATOM   3715  C   SER A 488      35.385  11.151  58.819  1.00 81.15           C  
ANISOU 3715  C   SER A 488    11233  11627   7975    -84    353   1533       C  
ATOM   3716  O   SER A 488      36.159  10.915  59.739  1.00 82.19           O  
ANISOU 3716  O   SER A 488    11440  11918   7871     49    361   1520       O  
ATOM   3717  CB  SER A 488      34.552  13.465  58.435  1.00 76.35           C  
ANISOU 3717  CB  SER A 488    10587  11016   7404   -124    392   1269       C  
ATOM   3718  OG  SER A 488      34.809  14.709  57.835  1.00 75.96           O  
ANISOU 3718  OG  SER A 488    10547  10937   7377   -184    317   1033       O  
ATOM   3719  N   ALA A 489      34.373  10.348  58.484  1.00 85.69           N  
ANISOU 3719  N   ALA A 489    11712  12059   8789   -151    418   1762       N  
ATOM   3720  CA  ALA A 489      33.989   9.176  59.277  1.00 85.32           C  
ANISOU 3720  CA  ALA A 489    11626  12031   8760    -65    547   2046       C  
ATOM   3721  C   ALA A 489      34.921   7.977  59.101  1.00 83.58           C  
ANISOU 3721  C   ALA A 489    11449  11769   8540    -82    445   2099       C  
ATOM   3722  O   ALA A 489      34.847   7.026  59.870  1.00 87.55           O  
ANISOU 3722  O   ALA A 489    11937  12312   9015     14    550   2322       O  
ATOM   3723  CB  ALA A 489      32.555   8.774  58.958  1.00 84.92           C  
ANISOU 3723  CB  ALA A 489    11427  11814   9025   -141    647   2274       C  
ATOM   3724  N   LEU A 490      35.789   8.001  58.096  1.00 83.96           N  
ANISOU 3724  N   LEU A 490    11547  11729   8624   -192    256   1910       N  
ATOM   3725  CA  LEU A 490      36.739   6.899  57.910  1.00 85.80           C  
ANISOU 3725  CA  LEU A 490    11826  11920   8853   -199    162   1946       C  
ATOM   3726  C   LEU A 490      37.692   6.801  59.090  1.00 86.57           C  
ANISOU 3726  C   LEU A 490    12006  12238   8648    -30    197   1941       C  
ATOM   3727  O   LEU A 490      38.062   7.817  59.687  1.00 89.87           O  
ANISOU 3727  O   LEU A 490    12478  12827   8840     61    203   1779       O  
ATOM   3728  CB  LEU A 490      37.555   7.078  56.622  1.00 84.28           C  
ANISOU 3728  CB  LEU A 490    11684  11612   8728   -323    -29   1732       C  
ATOM   3729  CG  LEU A 490      36.843   7.017  55.269  1.00 84.07           C  
ANISOU 3729  CG  LEU A 490    11608  11359   8974   -479   -117   1712       C  
ATOM   3730  CD1 LEU A 490      37.921   6.951  54.203  1.00 84.29           C  
ANISOU 3730  CD1 LEU A 490    11719  11311   8998   -541   -280   1534       C  
ATOM   3731  CD2 LEU A 490      35.895   5.836  55.131  1.00 85.44           C  
ANISOU 3731  CD2 LEU A 490    11690  11365   9407   -530    -87   1947       C  
ATOM   3732  N   THR A 491      38.077   5.578  59.433  1.00 86.98           N  
ANISOU 3732  N   THR A 491    12065  12280   8703     21    212   2115       N  
ATOM   3733  CA  THR A 491      39.072   5.344  60.489  1.00 90.70           C  
ANISOU 3733  CA  THR A 491    12617  12955   8889    189    219   2121       C  
ATOM   3734  C   THR A 491      40.139   4.408  59.941  1.00 91.44           C  
ANISOU 3734  C   THR A 491    12744  12963   9038    141     86   2107       C  
ATOM   3735  O   THR A 491      39.910   3.753  58.919  1.00 87.97           O  
ANISOU 3735  O   THR A 491    12263  12305   8857      3     29   2150       O  
ATOM   3736  CB  THR A 491      38.429   4.702  61.723  1.00 91.06           C  
ANISOU 3736  CB  THR A 491    12640  13109   8848    356    421   2413       C  
ATOM   3737  CG2 THR A 491      37.423   5.652  62.363  1.00 88.80           C  
ANISOU 3737  CG2 THR A 491    12335  12930   8477    438    575   2430       C  
ATOM   3738  OG1 THR A 491      37.773   3.497  61.315  1.00 92.26           O  
ANISOU 3738  OG1 THR A 491    12697  13057   9300    275    480   2668       O  
ATOM   3739  N   PRO A 492      41.303   4.327  60.617  1.00 93.24           N  
ANISOU 3739  N   PRO A 492    13044  13356   9025    264     29   2043       N  
ATOM   3740  CA  PRO A 492      42.357   3.440  60.098  1.00 93.56           C  
ANISOU 3740  CA  PRO A 492    13109  13312   9126    226    -89   2035       C  
ATOM   3741  C   PRO A 492      41.880   1.996  60.026  1.00 98.37           C  
ANISOU 3741  C   PRO A 492    13669  13773   9934    209    -12   2317       C  
ATOM   3742  O   PRO A 492      41.053   1.588  60.837  1.00 99.34           O  
ANISOU 3742  O   PRO A 492    13749  13938  10056    297    149   2553       O  
ATOM   3743  CB  PRO A 492      43.491   3.577  61.122  1.00 90.91           C  
ANISOU 3743  CB  PRO A 492    12841  13209   8492    395   -138   1969       C  
ATOM   3744  CG  PRO A 492      43.152   4.777  61.952  1.00 92.69           C  
ANISOU 3744  CG  PRO A 492    13094  13626   8499    497    -94   1852       C  
ATOM   3745  CD  PRO A 492      41.661   4.919  61.918  1.00 91.97           C  
ANISOU 3745  CD  PRO A 492    12946  13461   8537    458     68   1995       C  
ATOM   3746  N   ASP A 493      42.387   1.231  59.063  1.00104.16           N  
ANISOU 3746  N   ASP A 493    14406  14324  10848    107   -116   2297       N  
ATOM   3747  CA  ASP A 493      41.955  -0.155  58.902  1.00109.76           C  
ANISOU 3747  CA  ASP A 493    15062  14854  11787     79    -65   2540       C  
ATOM   3748  C   ASP A 493      43.017  -1.170  59.316  1.00106.84           C  
ANISOU 3748  C   ASP A 493    14730  14522  11343    175    -87   2639       C  
ATOM   3749  O   ASP A 493      44.102  -1.203  58.749  1.00106.10           O  
ANISOU 3749  O   ASP A 493    14691  14408  11216    149   -218   2480       O  
ATOM   3750  CB  ASP A 493      41.488  -0.397  57.465  1.00116.82           C  
ANISOU 3750  CB  ASP A 493    15928  15474  12984   -105   -163   2465       C  
ATOM   3751  CG  ASP A 493      39.969  -0.326  57.330  1.00125.46           C  
ANISOU 3751  CG  ASP A 493    16922  16447  14300   -181    -79   2587       C  
ATOM   3752  OD1 ASP A 493      39.266  -0.999  58.120  1.00137.92           O  
ANISOU 3752  OD1 ASP A 493    18421  18016  15965   -118     68   2854       O  
ATOM   3753  OD2 ASP A 493      39.470   0.404  56.448  1.00126.80           O1-
ANISOU 3753  OD2 ASP A 493    17082  16528  14567   -295   -152   2431       O1-
ATOM   3754  N   GLU A 494      42.682  -1.999  60.303  1.00105.65           N  
ANISOU 3754  N   GLU A 494    14543  14422  11178    296     55   2920       N  
ATOM   3755  CA  GLU A 494      43.606  -3.014  60.838  1.00108.59           C  
ANISOU 3755  CA  GLU A 494    14943  14843  11475    412     57   3059       C  
ATOM   3756  C   GLU A 494      43.858  -4.132  59.824  1.00107.51           C  
ANISOU 3756  C   GLU A 494    14786  14433  11631    296    -22   3093       C  
ATOM   3757  O   GLU A 494      44.791  -4.928  59.980  1.00101.45           O  
ANISOU 3757  O   GLU A 494    14047  13668  10830    364    -55   3154       O  
ATOM   3758  CB  GLU A 494      43.081  -3.603  62.163  1.00112.11           C  
ANISOU 3758  CB  GLU A 494    15353  15410  11833    590    256   3384       C  
ATOM   3759  N   THR A 495      42.999  -4.199  58.809  1.00108.79           N  
ANISOU 3759  N   THR A 495    14899  14358  12078    132    -55   3054       N  
ATOM   3760  CA  THR A 495      43.212  -5.069  57.648  1.00111.78           C  
ANISOU 3760  CA  THR A 495    15282  14464  12723     14   -170   3007       C  
ATOM   3761  C   THR A 495      44.542  -4.774  56.926  1.00109.01           C  
ANISOU 3761  C   THR A 495    15034  14140  12244      1   -322   2755       C  
ATOM   3762  O   THR A 495      45.276  -5.693  56.547  1.00113.04           O  
ANISOU 3762  O   THR A 495    15575  14536  12840     10   -376   2776       O  
ATOM   3763  CB  THR A 495      42.046  -4.951  56.634  1.00109.88           C  
ANISOU 3763  CB  THR A 495    14985  13990  12772   -151   -219   2951       C  
ATOM   3764  CG2 THR A 495      41.760  -3.502  56.288  1.00110.17           C  
ANISOU 3764  CG2 THR A 495    15050  14134  12676   -205   -261   2730       C  
ATOM   3765  OG1 THR A 495      42.388  -5.631  55.420  1.00112.75           O  
ANISOU 3765  OG1 THR A 495    15391  14113  13336   -246   -366   2837       O  
ATOM   3766  N   TYR A 496      44.856  -3.491  56.779  1.00100.35           N  
ANISOU 3766  N   TYR A 496    13982  13191  10957    -10   -376   2532       N  
ATOM   3767  CA  TYR A 496      46.004  -3.046  55.995  1.00 92.52           C  
ANISOU 3767  CA  TYR A 496    13064  12205   9882    -34   -503   2294       C  
ATOM   3768  C   TYR A 496      47.339  -3.655  56.436  1.00 91.67           C  
ANISOU 3768  C   TYR A 496    12988  12183   9659     77   -529   2331       C  
ATOM   3769  O   TYR A 496      47.807  -3.434  57.559  1.00 92.32           O  
ANISOU 3769  O   TYR A 496    13065  12487   9527    202   -493   2385       O  
ATOM   3770  CB  TYR A 496      46.073  -1.520  56.026  1.00 87.31           C  
ANISOU 3770  CB  TYR A 496    12419  11707   9048    -46   -529   2087       C  
ATOM   3771  CG  TYR A 496      47.325  -0.952  55.443  1.00 85.38           C  
ANISOU 3771  CG  TYR A 496    12225  11499   8715    -47   -633   1872       C  
ATOM   3772  CD1 TYR A 496      47.614  -1.088  54.083  1.00 84.59           C  
ANISOU 3772  CD1 TYR A 496    12171  11212   8756   -132   -709   1752       C  
ATOM   3773  CD2 TYR A 496      48.227  -0.260  56.241  1.00 85.65           C  
ANISOU 3773  CD2 TYR A 496    12259  11750   8532     48   -656   1786       C  
ATOM   3774  CE1 TYR A 496      48.776  -0.562  53.540  1.00 81.50           C  
ANISOU 3774  CE1 TYR A 496    11816  10849   8303   -120   -775   1582       C  
ATOM   3775  CE2 TYR A 496      49.389   0.270  55.709  1.00 86.11           C  
ANISOU 3775  CE2 TYR A 496    12337  11825   8558     43   -746   1603       C  
ATOM   3776  CZ  TYR A 496      49.658   0.115  54.361  1.00 80.96           C  
ANISOU 3776  CZ  TYR A 496    11720  10983   8059    -40   -790   1515       C  
ATOM   3777  OH  TYR A 496      50.810   0.646  53.866  1.00 73.73           O  
ANISOU 3777  OH  TYR A 496    10810  10082   7124    -30   -849   1362       O  
ATOM   3778  N   VAL A 497      47.939  -4.429  55.537  1.00 88.71           N  
ANISOU 3778  N   VAL A 497    12651  11629   9426     40   -597   2297       N  
ATOM   3779  CA  VAL A 497      49.268  -4.969  55.756  1.00 87.82           C  
ANISOU 3779  CA  VAL A 497    12564  11570   9233    135   -631   2311       C  
ATOM   3780  C   VAL A 497      50.255  -3.856  55.434  1.00 86.87           C  
ANISOU 3780  C   VAL A 497    12472  11569   8965    139   -711   2075       C  
ATOM   3781  O   VAL A 497      50.283  -3.368  54.301  1.00 86.91           O  
ANISOU 3781  O   VAL A 497    12514  11459   9047     51   -763   1906       O  
ATOM   3782  CB  VAL A 497      49.565  -6.156  54.830  1.00 87.13           C  
ANISOU 3782  CB  VAL A 497    12513  11232   9361    101   -668   2345       C  
ATOM   3783  CG1 VAL A 497      50.919  -6.757  55.178  1.00 85.60           C  
ANISOU 3783  CG1 VAL A 497    12332  11103   9091    213   -684   2391       C  
ATOM   3784  CG2 VAL A 497      48.460  -7.199  54.915  1.00 88.32           C  
ANISOU 3784  CG2 VAL A 497    12619  11200   9739     63   -607   2548       C  
ATOM   3785  N   PRO A 498      51.061  -3.444  56.422  1.00 87.18           N  
ANISOU 3785  N   PRO A 498    12491  11835   8800    249   -726   2066       N  
ATOM   3786  CA  PRO A 498      51.984  -2.321  56.226  1.00 85.96           C  
ANISOU 3786  CA  PRO A 498    12333  11789   8540    250   -809   1844       C  
ATOM   3787  C   PRO A 498      53.016  -2.576  55.138  1.00 83.42           C  
ANISOU 3787  C   PRO A 498    12035  11327   8333    224   -864   1748       C  
ATOM   3788  O   PRO A 498      53.488  -3.695  54.993  1.00 80.28           O  
ANISOU 3788  O   PRO A 498    11654  10835   8015    266   -857   1861       O  
ATOM   3789  CB  PRO A 498      52.666  -2.176  57.584  1.00 87.68           C  
ANISOU 3789  CB  PRO A 498    12519  12251   8544    394   -835   1886       C  
ATOM   3790  CG  PRO A 498      52.474  -3.486  58.263  1.00 90.20           C  
ANISOU 3790  CG  PRO A 498    12840  12564   8868    483   -765   2147       C  
ATOM   3791  CD  PRO A 498      51.153  -4.000  57.780  1.00 89.85           C  
ANISOU 3791  CD  PRO A 498    12802  12335   9000    388   -673   2264       C  
ATOM   3792  N   LYS A 499      53.339  -1.530  54.383  1.00 80.77           N  
ANISOU 3792  N   LYS A 499    11700  10976   8012    165   -903   1550       N  
ATOM   3793  CA  LYS A 499      54.328  -1.603  53.317  1.00 78.78           C  
ANISOU 3793  CA  LYS A 499    11469  10603   7859    157   -930   1459       C  
ATOM   3794  C   LYS A 499      55.685  -2.079  53.852  1.00 80.73           C  
ANISOU 3794  C   LYS A 499    11672  10930   8072    263   -967   1505       C  
ATOM   3795  O   LYS A 499      56.093  -1.724  54.978  1.00 77.18           O  
ANISOU 3795  O   LYS A 499    11160  10675   7489    335  -1014   1509       O  
ATOM   3796  CB  LYS A 499      54.468  -0.220  52.682  1.00 78.28           C  
ANISOU 3796  CB  LYS A 499    11388  10552   7801     98   -947   1263       C  
ATOM   3797  CG  LYS A 499      55.143  -0.173  51.320  1.00 79.74           C  
ANISOU 3797  CG  LYS A 499    11614  10581   8103     83   -935   1180       C  
ATOM   3798  CD  LYS A 499      54.888   1.164  50.613  1.00 77.85           C  
ANISOU 3798  CD  LYS A 499    11366  10327   7884     16   -924   1024       C  
ATOM   3799  CE  LYS A 499      55.714   1.305  49.333  1.00 79.41           C  
ANISOU 3799  CE  LYS A 499    11598  10395   8178     36   -889    959       C  
ATOM   3800  NZ  LYS A 499      55.502   2.565  48.564  1.00 78.64           N1+
ANISOU 3800  NZ  LYS A 499    11494  10271   8113    -13   -858    835       N1+
ATOM   3801  N   ALA A 500      56.388  -2.881  53.054  1.00 80.68           N  
ANISOU 3801  N   ALA A 500    11699  10775   8180    286   -955   1536       N  
ATOM   3802  CA  ALA A 500      57.738  -3.341  53.435  1.00 83.22           C  
ANISOU 3802  CA  ALA A 500    11968  11152   8500    387   -987   1583       C  
ATOM   3803  C   ALA A 500      58.737  -2.173  53.461  1.00 81.13           C  
ANISOU 3803  C   ALA A 500    11613  10990   8221    399  -1044   1428       C  
ATOM   3804  O   ALA A 500      58.617  -1.215  52.689  1.00 80.83           O  
ANISOU 3804  O   ALA A 500    11576  10901   8233    330  -1029   1289       O  
ATOM   3805  CB  ALA A 500      58.221  -4.427  52.479  1.00 81.28           C  
ANISOU 3805  CB  ALA A 500    11784  10704   8393    412   -946   1643       C  
ATOM   3806  N   PHE A 501      59.720  -2.243  54.343  1.00 80.59           N  
ANISOU 3806  N   PHE A 501    11460  11060   8102    490  -1115   1455       N  
ATOM   3807  CA  PHE A 501      60.707  -1.175  54.409  1.00 80.90           C  
ANISOU 3807  CA  PHE A 501    11387  11176   8173    500  -1190   1307       C  
ATOM   3808  C   PHE A 501      61.456  -1.022  53.099  1.00 79.57           C  
ANISOU 3808  C   PHE A 501    11207  10837   8188    476  -1129   1251       C  
ATOM   3809  O   PHE A 501      61.816  -2.009  52.479  1.00 77.05           O  
ANISOU 3809  O   PHE A 501    10939  10388   7948    515  -1067   1348       O  
ATOM   3810  CB  PHE A 501      61.734  -1.421  55.496  1.00 79.58           C  
ANISOU 3810  CB  PHE A 501    11125  11164   7949    613  -1299   1349       C  
ATOM   3811  CG  PHE A 501      62.721  -0.305  55.636  1.00 79.41           C  
ANISOU 3811  CG  PHE A 501    10966  11211   7996    617  -1404   1186       C  
ATOM   3812  CD1 PHE A 501      63.993  -0.410  55.092  1.00 79.57           C  
ANISOU 3812  CD1 PHE A 501    10890  11146   8198    648  -1410   1183       C  
ATOM   3813  CD2 PHE A 501      62.374   0.863  56.309  1.00 81.20           C  
ANISOU 3813  CD2 PHE A 501    11149  11574   8129    592  -1494   1034       C  
ATOM   3814  CE1 PHE A 501      64.911   0.621  55.228  1.00 80.27           C  
ANISOU 3814  CE1 PHE A 501    10822  11275   8400    646  -1511   1041       C  
ATOM   3815  CE2 PHE A 501      63.285   1.900  56.450  1.00 82.77           C  
ANISOU 3815  CE2 PHE A 501    11205  11813   8431    590  -1608    870       C  
ATOM   3816  CZ  PHE A 501      64.558   1.779  55.908  1.00 81.56           C  
ANISOU 3816  CZ  PHE A 501    10938  11565   8487    612  -1619    878       C  
ATOM   3817  N   ASP A 502      61.714   0.227  52.720  1.00 80.95           N  
ANISOU 3817  N   ASP A 502    11311  11014   8432    425  -1141   1101       N  
ATOM   3818  CA  ASP A 502      62.457   0.541  51.512  1.00 79.91           C  
ANISOU 3818  CA  ASP A 502    11153  10734   8475    420  -1062   1059       C  
ATOM   3819  C   ASP A 502      63.369   1.757  51.732  1.00 79.58           C  
ANISOU 3819  C   ASP A 502    10939  10750   8548    414  -1126    935       C  
ATOM   3820  O   ASP A 502      62.920   2.899  51.705  1.00 73.83           O  
ANISOU 3820  O   ASP A 502    10178  10047   7826    344  -1140    811       O  
ATOM   3821  CB  ASP A 502      61.487   0.792  50.366  1.00 79.84           C  
ANISOU 3821  CB  ASP A 502    11270  10592   8475    349   -959   1022       C  
ATOM   3822  CG  ASP A 502      62.192   1.160  49.057  1.00 81.68           C  
ANISOU 3822  CG  ASP A 502    11497  10679   8860    369   -852    992       C  
ATOM   3823  OD1 ASP A 502      63.440   1.177  49.017  1.00 79.45           O  
ANISOU 3823  OD1 ASP A 502    11102  10383   8701    433   -843   1013       O  
ATOM   3824  OD2 ASP A 502      61.479   1.426  48.060  1.00 82.40           O1-
ANISOU 3824  OD2 ASP A 502    11696  10667   8945    333   -774    957       O1-
ATOM   3825  N   GLU A 503      64.659   1.471  51.901  1.00 83.58           N  
ANISOU 3825  N   GLU A 503    11327  11257   9171    489  -1163    974       N  
ATOM   3826  CA  GLU A 503      65.695   2.479  52.141  1.00 86.54           C  
ANISOU 3826  CA  GLU A 503    11504  11663   9713    491  -1243    871       C  
ATOM   3827  C   GLU A 503      65.632   3.685  51.201  1.00 84.75           C  
ANISOU 3827  C   GLU A 503    11230  11327   9642    419  -1153    771       C  
ATOM   3828  O   GLU A 503      65.855   4.809  51.629  1.00 90.43           O  
ANISOU 3828  O   GLU A 503    11813  12096  10449    378  -1243    640       O  
ATOM   3829  CB  GLU A 503      67.093   1.835  52.036  1.00 91.00           C  
ANISOU 3829  CB  GLU A 503    11956  12179  10441    583  -1243    966       C  
ATOM   3830  CG  GLU A 503      68.255   2.773  52.367  1.00 94.70           C  
ANISOU 3830  CG  GLU A 503    12184  12667  11129    589  -1349    872       C  
ATOM   3831  N   LYS A 504      65.332   3.454  49.927  1.00 80.49           N  
ANISOU 3831  N   LYS A 504    10806  10637   9137    415   -980    831       N  
ATOM   3832  CA  LYS A 504      65.362   4.514  48.928  1.00 77.42           C  
ANISOU 3832  CA  LYS A 504    10380  10138   8899    376   -866    773       C  
ATOM   3833  C   LYS A 504      64.367   5.636  49.258  1.00 79.17           C  
ANISOU 3833  C   LYS A 504    10605  10425   9053    277   -919    638       C  
ATOM   3834  O   LYS A 504      64.577   6.796  48.876  1.00 80.09           O  
ANISOU 3834  O   LYS A 504    10614  10487   9331    238   -881    561       O  
ATOM   3835  CB  LYS A 504      65.102   3.936  47.529  1.00 75.22           C  
ANISOU 3835  CB  LYS A 504    10269   9707   8605    420   -681    864       C  
ATOM   3836  CG  LYS A 504      65.997   2.735  47.163  1.00 76.46           C  
ANISOU 3836  CG  LYS A 504    10452   9789   8810    531   -614    995       C  
ATOM   3837  CD  LYS A 504      65.887   2.293  45.701  1.00 71.72           C  
ANISOU 3837  CD  LYS A 504    10018   9029   8204    603   -429   1061       C  
ATOM   3838  N   LEU A 505      63.310   5.302  49.997  1.00 77.93           N  
ANISOU 3838  N   LEU A 505    10556  10377   8676    244   -998    620       N  
ATOM   3839  CA  LEU A 505      62.274   6.272  50.348  1.00 77.94           C  
ANISOU 3839  CA  LEU A 505    10574  10444   8595    162  -1038    504       C  
ATOM   3840  C   LEU A 505      62.724   7.251  51.426  1.00 80.65           C  
ANISOU 3840  C   LEU A 505    10752  10901   8992    147  -1190    363       C  
ATOM   3841  O   LEU A 505      62.184   8.348  51.532  1.00 82.73           O  
ANISOU 3841  O   LEU A 505    10983  11179   9271     84  -1207    241       O  
ATOM   3842  CB  LEU A 505      60.997   5.556  50.815  1.00 78.41           C  
ANISOU 3842  CB  LEU A 505    10792  10578   8421    144  -1057    552       C  
ATOM   3843  CG  LEU A 505      60.331   4.585  49.819  1.00 77.60           C  
ANISOU 3843  CG  LEU A 505    10863  10354   8269    146   -944    664       C  
ATOM   3844  CD1 LEU A 505      58.974   4.126  50.344  1.00 70.28           C  
ANISOU 3844  CD1 LEU A 505    10047   9487   7169    108   -970    699       C  
ATOM   3845  CD2 LEU A 505      60.200   5.201  48.427  1.00 70.38           C  
ANISOU 3845  CD2 LEU A 505     9990   9294   7456    123   -821    636       C  
ATOM   3846  N   PHE A 506      63.716   6.862  52.219  1.00 81.01           N  
ANISOU 3846  N   PHE A 506    10691  11022   9068    212  -1311    369       N  
ATOM   3847  CA  PHE A 506      64.157   7.662  53.359  1.00 82.80           C  
ANISOU 3847  CA  PHE A 506    10772  11370   9319    219  -1501    217       C  
ATOM   3848  C   PHE A 506      65.545   8.272  53.184  1.00 83.08           C  
ANISOU 3848  C   PHE A 506    10582  11321   9661    228  -1555    160       C  
ATOM   3849  O   PHE A 506      66.009   9.011  54.053  1.00 83.86           O  
ANISOU 3849  O   PHE A 506    10539  11494   9831    231  -1736      8       O  
ATOM   3850  CB  PHE A 506      64.083   6.804  54.629  1.00 83.38           C  
ANISOU 3850  CB  PHE A 506    10898  11626   9154    301  -1640    254       C  
ATOM   3851  CG  PHE A 506      62.757   6.122  54.793  1.00 80.22           C  
ANISOU 3851  CG  PHE A 506    10695  11287   8498    297  -1566    346       C  
ATOM   3852  CD1 PHE A 506      61.690   6.797  55.362  1.00 80.51           C  
ANISOU 3852  CD1 PHE A 506    10791  11419   8379    264  -1594    250       C  
ATOM   3853  CD2 PHE A 506      62.558   4.839  54.320  1.00 77.15           C  
ANISOU 3853  CD2 PHE A 506    10422  10838   8052    325  -1459    528       C  
ATOM   3854  CE1 PHE A 506      60.455   6.194  55.487  1.00 77.84           C  
ANISOU 3854  CE1 PHE A 506    10609  11120   7846    258  -1512    352       C  
ATOM   3855  CE2 PHE A 506      61.323   4.234  54.427  1.00 77.14           C  
ANISOU 3855  CE2 PHE A 506    10576  10863   7871    310  -1392    616       C  
ATOM   3856  CZ  PHE A 506      60.269   4.914  55.013  1.00 76.49           C  
ANISOU 3856  CZ  PHE A 506    10536  10879   7648    275  -1415    536       C  
ATOM   3857  N   THR A 507      66.191   7.969  52.062  1.00 85.03           N  
ANISOU 3857  N   THR A 507    10797  11410  10099    242  -1398    278       N  
ATOM   3858  CA  THR A 507      67.462   8.582  51.700  1.00 87.88           C  
ANISOU 3858  CA  THR A 507    10931  11657  10804    249  -1396    259       C  
ATOM   3859  C   THR A 507      67.206   9.995  51.211  1.00 85.98           C  
ANISOU 3859  C   THR A 507    10602  11318  10747    166  -1339    148       C  
ATOM   3860  O   THR A 507      66.318  10.211  50.405  1.00 82.38           O  
ANISOU 3860  O   THR A 507    10282  10803  10217    127  -1183    180       O  
ATOM   3861  CB  THR A 507      68.181   7.818  50.560  1.00 86.94           C  
ANISOU 3861  CB  THR A 507    10819  11392  10823    311  -1201    446       C  
ATOM   3862  CG2 THR A 507      69.637   8.292  50.437  1.00 88.05           C  
ANISOU 3862  CG2 THR A 507    10688  11432  11334    338  -1219    453       C  
ATOM   3863  OG1 THR A 507      68.147   6.403  50.804  1.00 86.61           O  
ANISOU 3863  OG1 THR A 507    10911  11414  10581    383  -1208    568       O  
ATOM   3864  N   PHE A 508      67.981  10.950  51.708  1.00 94.12           N  
ANISOU 3864  N   PHE A 508    11401  12326  12033    141  -1478     15       N  
ATOM   3865  CA  PHE A 508      67.918  12.319  51.211  1.00101.80           C  
ANISOU 3865  CA  PHE A 508    12251  13172  13258     66  -1415    -78       C  
ATOM   3866  C   PHE A 508      69.266  12.708  50.638  1.00103.37           C  
ANISOU 3866  C   PHE A 508    12193  13198  13883     82  -1352    -17       C  
ATOM   3867  O   PHE A 508      70.298  12.376  51.211  1.00103.43           O  
ANISOU 3867  O   PHE A 508    12043  13226  14029    125  -1496    -22       O  
ATOM   3868  CB  PHE A 508      67.522  13.278  52.329  1.00107.10           C  
ANISOU 3868  CB  PHE A 508    12860  13940  13894     14  -1639   -316       C  
ATOM   3869  CG  PHE A 508      66.150  13.027  52.880  1.00109.40           C  
ANISOU 3869  CG  PHE A 508    13386  14391  13789      5  -1671   -365       C  
ATOM   3870  CD1 PHE A 508      65.968  12.618  54.193  1.00113.45           C  
ANISOU 3870  CD1 PHE A 508    13957  15100  14047     57  -1882   -456       C  
ATOM   3871  CD2 PHE A 508      65.036  13.190  52.077  1.00111.90           C  
ANISOU 3871  CD2 PHE A 508    13864  14661  13991    -41  -1483   -307       C  
ATOM   3872  CE1 PHE A 508      64.702  12.386  54.701  1.00115.06           C  
ANISOU 3872  CE1 PHE A 508    14365  15445  13906     61  -1883   -475       C  
ATOM   3873  CE2 PHE A 508      63.766  12.960  52.576  1.00114.41           C  
ANISOU 3873  CE2 PHE A 508    14376  15113  13983    -51  -1504   -337       C  
ATOM   3874  CZ  PHE A 508      63.598  12.557  53.890  1.00114.96           C  
ANISOU 3874  CZ  PHE A 508    14492  15371  13817      0  -1692   -413       C  
ATOM   3875  N   HIS A 509      69.246  13.402  49.504  1.00107.06           N  
ANISOU 3875  N   HIS A 509    12618  13498  14564     58  -1131     56       N  
ATOM   3876  CA  HIS A 509      70.469  13.805  48.815  1.00116.46           C  
ANISOU 3876  CA  HIS A 509    13562  14501  16185     84  -1011    157       C  
ATOM   3877  C   HIS A 509      70.719  15.306  48.956  1.00118.33           C  
ANISOU 3877  C   HIS A 509    13554  14619  16786      1  -1070     17       C  
ATOM   3878  O   HIS A 509      69.793  16.088  49.160  1.00118.56           O  
ANISOU 3878  O   HIS A 509    13651  14676  16721    -69  -1110   -118       O  
ATOM   3879  CB  HIS A 509      70.402  13.418  47.327  1.00120.65           C  
ANISOU 3879  CB  HIS A 509    14218  14913  16711    153   -679    384       C  
ATOM   3880  CG  HIS A 509      71.040  12.100  47.003  1.00125.24           C  
ANISOU 3880  CG  HIS A 509    14868  15502  17216    262   -597    555       C  
ATOM   3881  CD2 HIS A 509      70.643  10.829  47.250  1.00124.20           C  
ANISOU 3881  CD2 HIS A 509    14954  15492  16743    310   -639    598       C  
ATOM   3882  ND1 HIS A 509      72.236  11.999  46.321  1.00128.23           N  
ANISOU 3882  ND1 HIS A 509    15074  15736  17913    342   -436    716       N  
ATOM   3883  CE1 HIS A 509      72.549  10.726  46.167  1.00127.58           C  
ANISOU 3883  CE1 HIS A 509    15110  15691  17674    438   -389    840       C  
ATOM   3884  NE2 HIS A 509      71.600   9.995  46.723  1.00129.76           N  
ANISOU 3884  NE2 HIS A 509    15621  16124  17557    416   -515    769       N  
ATOM   3885  N   ALA A 510      71.978  15.705  48.810  1.00118.91           N  
ANISOU 3885  N   ALA A 510    13332  14542  17306     12  -1066     60       N  
ATOM   3886  CA  ALA A 510      72.365  17.117  48.915  1.00118.18           C  
ANISOU 3886  CA  ALA A 510    12962  14295  17646    -67  -1124    -62       C  
ATOM   3887  C   ALA A 510      71.544  18.041  48.013  1.00116.28           C  
ANISOU 3887  C   ALA A 510    12788  13945  17447   -108   -894    -24       C  
ATOM   3888  O   ALA A 510      71.445  19.237  48.278  1.00109.85           O  
ANISOU 3888  O   ALA A 510    11816  13041  16883   -189   -973   -173       O  
ATOM   3889  CB  ALA A 510      73.844  17.285  48.615  1.00121.54           C  
ANISOU 3889  CB  ALA A 510    13055  14538  18587    -36  -1079     50       C  
ATOM   3890  N   ASP A 511      70.975  17.482  46.945  1.00116.16           N  
ANISOU 3890  N   ASP A 511    13007  13934  17194    -44   -620    170       N  
ATOM   3891  CA  ASP A 511      70.043  18.196  46.073  1.00115.32           C  
ANISOU 3891  CA  ASP A 511    13022  13761  17034    -63   -410    217       C  
ATOM   3892  C   ASP A 511      68.932  18.894  46.855  1.00114.85           C  
ANISOU 3892  C   ASP A 511    13046  13799  16794   -163   -590    -14       C  
ATOM   3893  O   ASP A 511      68.398  19.906  46.404  1.00111.66           O  
ANISOU 3893  O   ASP A 511    12620  13300  16507   -207   -481    -31       O  
ATOM   3894  CB  ASP A 511      69.419  17.220  45.065  1.00113.63           C  
ANISOU 3894  CB  ASP A 511    13115  13600  16459     32   -182    406       C  
ATOM   3895  CG  ASP A 511      68.248  17.826  44.302  1.00111.14           C  
ANISOU 3895  CG  ASP A 511    12973  13264  15990     17    -21    427       C  
ATOM   3896  N   ILE A 512      68.583  18.332  48.012  1.00114.23           N  
ANISOU 3896  N   ILE A 512    13069  13909  16424   -185   -850   -175       N  
ATOM   3897  CA  ILE A 512      67.556  18.893  48.893  1.00111.75           C  
ANISOU 3897  CA  ILE A 512    12844  13709  15905   -257  -1030   -397       C  
ATOM   3898  C   ILE A 512      67.772  20.368  49.271  1.00113.75           C  
ANISOU 3898  C   ILE A 512    12856  13836  16528   -337  -1133   -582       C  
ATOM   3899  O   ILE A 512      66.819  21.149  49.249  1.00114.68           O  
ANISOU 3899  O   ILE A 512    13047  13948  16578   -388  -1106   -673       O  
ATOM   3900  CB  ILE A 512      67.399  18.038  50.180  1.00111.50           C  
ANISOU 3900  CB  ILE A 512    12923  13901  15543   -236  -1295   -524       C  
ATOM   3901  CG1 ILE A 512      66.120  18.416  50.927  1.00111.03           C  
ANISOU 3901  CG1 ILE A 512    13026  13980  15179   -279  -1410   -699       C  
ATOM   3902  CG2 ILE A 512      68.612  18.169  51.097  1.00114.12           C  
ANISOU 3902  CG2 ILE A 512    13003  14223  16133   -229  -1546   -651       C  
ATOM   3903  CD1 ILE A 512      65.727  17.408  51.984  1.00109.95           C  
ANISOU 3903  CD1 ILE A 512    13062  14073  14640   -230  -1587   -750       C  
ATOM   3904  N   CYS A 513      69.005  20.757  49.596  1.00113.82           N  
ANISOU 3904  N   CYS A 513    12570  13728  16950   -347  -1254   -638       N  
ATOM   3905  CA  CYS A 513      69.280  22.134  50.023  1.00114.88           C  
ANISOU 3905  CA  CYS A 513    12452  13718  17479   -425  -1388   -837       C  
ATOM   3906  C   CYS A 513      69.050  23.164  48.909  1.00116.00           C  
ANISOU 3906  C   CYS A 513    12508  13646  17921   -461  -1111   -720       C  
ATOM   3907  O   CYS A 513      68.871  24.345  49.193  1.00115.39           O  
ANISOU 3907  O   CYS A 513    12292  13460  18092   -532  -1188   -887       O  
ATOM   3908  CB  CYS A 513      70.704  22.272  50.564  1.00116.12           C  
ANISOU 3908  CB  CYS A 513    12288  13775  18058   -428  -1590   -913       C  
ATOM   3909  SG  CYS A 513      71.258  20.920  51.634  1.00115.61           S  
ANISOU 3909  SG  CYS A 513    12291  13938  17696   -353  -1866   -966       S  
ATOM   3910  N   THR A 514      69.064  22.715  47.655  1.00118.95           N  
ANISOU 3910  N   THR A 514    12968  13959  18268   -397   -792   -435       N  
ATOM   3911  CA  THR A 514      68.759  23.568  46.491  1.00122.72           C  
ANISOU 3911  CA  THR A 514    13413  14260  18955   -396   -493   -280       C  
ATOM   3912  C   THR A 514      67.255  23.847  46.314  1.00118.13           C  
ANISOU 3912  C   THR A 514    13094  13775  18014   -421   -431   -327       C  
ATOM   3913  O   THR A 514      66.876  24.883  45.755  1.00117.76           O  
ANISOU 3913  O   THR A 514    12984  13591  18167   -449   -282   -298       O  
ATOM   3914  CB  THR A 514      69.313  22.941  45.181  1.00126.63           C  
ANISOU 3914  CB  THR A 514    13935  14673  19505   -283   -167     48       C  
ATOM   3915  CG2 THR A 514      68.742  23.621  43.929  1.00126.65           C  
ANISOU 3915  CG2 THR A 514    14003  14555  19562   -244    156    231       C  
ATOM   3916  OG1 THR A 514      70.742  23.052  45.162  1.00126.92           O  
ANISOU 3916  OG1 THR A 514    13654  14549  20019   -265   -161    125       O  
ATOM   3917  N   LEU A 515      66.404  22.935  46.779  1.00114.57           N  
ANISOU 3917  N   LEU A 515    12922  13548  17060   -408   -536   -385       N  
ATOM   3918  CA  LEU A 515      64.959  23.057  46.556  1.00108.71           C  
ANISOU 3918  CA  LEU A 515    12431  12900  15975   -424   -468   -401       C  
ATOM   3919  C   LEU A 515      64.342  24.239  47.324  1.00104.66           C  
ANISOU 3919  C   LEU A 515    11844  12370  15553   -513   -615   -642       C  
ATOM   3920  O   LEU A 515      64.704  24.497  48.479  1.00103.27           O  
ANISOU 3920  O   LEU A 515    11548  12232  15457   -553   -877   -869       O  
ATOM   3921  CB  LEU A 515      64.253  21.752  46.937  1.00103.99           C  
ANISOU 3921  CB  LEU A 515    12117  12529  14866   -390   -552   -398       C  
ATOM   3922  N   PRO A 516      63.430  24.981  46.675  1.00103.74           N  
ANISOU 3922  N   PRO A 516    11799  12192  15426   -531   -451   -597       N  
ATOM   3923  CA  PRO A 516      62.619  26.008  47.361  1.00105.87           C  
ANISOU 3923  CA  PRO A 516    12052  12464  15710   -604   -569   -816       C  
ATOM   3924  C   PRO A 516      61.723  25.459  48.478  1.00106.20           C  
ANISOU 3924  C   PRO A 516    12297  12740  15312   -614   -780   -994       C  
ATOM   3925  O   PRO A 516      61.319  24.293  48.427  1.00105.44           O  
ANISOU 3925  O   PRO A 516    12413  12803  14846   -570   -766   -894       O  
ATOM   3926  CB  PRO A 516      61.757  26.585  46.234  1.00103.58           C  
ANISOU 3926  CB  PRO A 516    11851  12089  15417   -594   -308   -659       C  
ATOM   3927  CG  PRO A 516      62.557  26.363  44.995  1.00104.74           C  
ANISOU 3927  CG  PRO A 516    11930  12102  15766   -521    -60   -389       C  
ATOM   3928  CD  PRO A 516      63.337  25.095  45.208  1.00103.08           C  
ANISOU 3928  CD  PRO A 516    11759  11990  15418   -471   -135   -334       C  
ATOM   3929  N   ASP A 517      61.397  26.311  49.453  1.00105.69           N  
ANISOU 3929  N   ASP A 517    12170  12688  15301   -661   -960  -1248       N  
ATOM   3930  CA  ASP A 517      60.633  25.915  50.653  1.00106.29           C  
ANISOU 3930  CA  ASP A 517    12416  12984  14985   -649  -1163  -1430       C  
ATOM   3931  C   ASP A 517      59.464  24.950  50.406  1.00105.52           C  
ANISOU 3931  C   ASP A 517    12607  13061  14426   -617  -1058  -1289       C  
ATOM   3932  O   ASP A 517      59.234  24.025  51.197  1.00101.87           O  
ANISOU 3932  O   ASP A 517    12283  12790  13634   -578  -1186  -1324       O  
ATOM   3933  CB  ASP A 517      60.076  27.151  51.361  1.00108.96           C  
ANISOU 3933  CB  ASP A 517    12696  13284  15420   -689  -1272  -1680       C  
ATOM   3934  CG  ASP A 517      61.153  28.022  51.948  1.00113.99           C  
ANISOU 3934  CG  ASP A 517    13062  13775  16474   -719  -1463  -1894       C  
ATOM   3935  OD1 ASP A 517      62.281  27.996  51.413  1.00123.51           O  
ANISOU 3935  OD1 ASP A 517    14072  14832  18025   -729  -1421  -1790       O  
ATOM   3936  OD2 ASP A 517      60.868  28.735  52.934  1.00111.72           O1-
ANISOU 3936  OD2 ASP A 517    12754  13513  16182   -724  -1655  -2167       O1-
ATOM   3937  N   THR A 518      58.711  25.181  49.333  1.00 99.75           N  
ANISOU 3937  N   THR A 518    11958  12259  13683   -629   -835  -1128       N  
ATOM   3938  CA  THR A 518      57.554  24.353  49.050  1.00 96.10           C  
ANISOU 3938  CA  THR A 518    11747  11934  12833   -607   -753  -1006       C  
ATOM   3939  C   THR A 518      57.998  22.936  48.654  1.00 92.08           C  
ANISOU 3939  C   THR A 518    11343  11494  12150   -555   -720   -832       C  
ATOM   3940  O   THR A 518      57.499  21.960  49.213  1.00 90.35           O  
ANISOU 3940  O   THR A 518    11281  11439  11609   -532   -800   -826       O  
ATOM   3941  CB  THR A 518      56.610  25.012  48.010  1.00 96.36           C  
ANISOU 3941  CB  THR A 518    11837  11873  12902   -624   -550   -895       C  
ATOM   3942  CG2 THR A 518      56.078  26.353  48.555  1.00 91.56           C  
ANISOU 3942  CG2 THR A 518    11139  11210  12441   -672   -595  -1082       C  
ATOM   3943  OG1 THR A 518      57.305  25.249  46.785  1.00100.59           O  
ANISOU 3943  OG1 THR A 518    12280  12240  13698   -601   -366   -722       O  
ATOM   3944  N   GLU A 519      58.948  22.818  47.732  1.00 88.95           N  
ANISOU 3944  N   GLU A 519    10853  10967  11976   -527   -597   -686       N  
ATOM   3945  CA  GLU A 519      59.450  21.499  47.332  1.00 87.79           C  
ANISOU 3945  CA  GLU A 519    10801  10870  11686   -466   -560   -528       C  
ATOM   3946  C   GLU A 519      60.255  20.847  48.450  1.00 86.99           C  
ANISOU 3946  C   GLU A 519    10637  10872  11542   -452   -767   -628       C  
ATOM   3947  O   GLU A 519      60.378  19.625  48.501  1.00 89.90           O  
ANISOU 3947  O   GLU A 519    11124  11335  11699   -405   -787   -535       O  
ATOM   3948  CB  GLU A 519      60.293  21.594  46.060  1.00 93.71           C  
ANISOU 3948  CB  GLU A 519    11466  11452  12688   -416   -355   -341       C  
ATOM   3949  CG  GLU A 519      59.508  22.020  44.822  1.00 99.44           C  
ANISOU 3949  CG  GLU A 519    12295  12097  13391   -393   -137   -202       C  
ATOM   3950  CD  GLU A 519      60.363  22.769  43.797  1.00105.99           C  
ANISOU 3950  CD  GLU A 519    12960  12730  14582   -348     67    -64       C  
ATOM   3951  OE1 GLU A 519      61.347  22.186  43.272  1.00101.24           O  
ANISOU 3951  OE1 GLU A 519    12318  12075  14073   -274    159     74       O  
ATOM   3952  OE2 GLU A 519      60.037  23.945  43.510  1.00109.16           O1-
ANISOU 3952  OE2 GLU A 519    13269  13026  15182   -378    152    -81       O1-
ATOM   3953  N   LYS A 520      60.826  21.656  49.337  1.00 86.77           N  
ANISOU 3953  N   LYS A 520    10423  10820  11725   -484   -931   -820       N  
ATOM   3954  CA  LYS A 520      61.510  21.126  50.525  1.00 86.91           C  
ANISOU 3954  CA  LYS A 520    10388  10957  11676   -458  -1167   -945       C  
ATOM   3955  C   LYS A 520      60.506  20.381  51.402  1.00 83.42           C  
ANISOU 3955  C   LYS A 520    10165  10735  10798   -432  -1268   -993       C  
ATOM   3956  O   LYS A 520      60.714  19.223  51.766  1.00 84.36           O  
ANISOU 3956  O   LYS A 520    10373  10974  10705   -380  -1328   -922       O  
ATOM   3957  CB  LYS A 520      62.163  22.249  51.350  1.00 89.52           C  
ANISOU 3957  CB  LYS A 520    10491  11219  12305   -492  -1357  -1184       C  
ATOM   3958  CG  LYS A 520      63.682  22.307  51.322  1.00 90.13           C  
ANISOU 3958  CG  LYS A 520    10318  11174  12752   -485  -1430  -1183       C  
ATOM   3959  CD  LYS A 520      64.179  23.432  52.224  1.00 92.53           C  
ANISOU 3959  CD  LYS A 520    10406  11409  13343   -523  -1661  -1457       C  
ATOM   3960  CE  LYS A 520      65.564  23.940  51.836  1.00 93.81           C  
ANISOU 3960  CE  LYS A 520    10255  11352  14037   -547  -1666  -1435       C  
ATOM   3961  NZ  LYS A 520      65.664  25.423  51.992  1.00 92.55           N1+
ANISOU 3961  NZ  LYS A 520     9884  11009  14273   -616  -1733  -1625       N1+
ATOM   3962  N   GLN A 521      59.421  21.071  51.737  1.00 79.03           N  
ANISOU 3962  N   GLN A 521     9682  10220  10128   -462  -1272  -1101       N  
ATOM   3963  CA  GLN A 521      58.337  20.487  52.521  1.00 77.01           C  
ANISOU 3963  CA  GLN A 521     9622  10156   9482   -433  -1329  -1124       C  
ATOM   3964  C   GLN A 521      57.719  19.277  51.803  1.00 73.38           C  
ANISOU 3964  C   GLN A 521     9349   9740   8793   -417  -1184   -895       C  
ATOM   3965  O   GLN A 521      57.429  18.264  52.430  1.00 70.66           O  
ANISOU 3965  O   GLN A 521     9126   9544   8179   -371  -1246   -849       O  
ATOM   3966  CB  GLN A 521      57.268  21.539  52.812  1.00 76.06           C  
ANISOU 3966  CB  GLN A 521     9531  10039   9329   -466  -1315  -1256       C  
ATOM   3967  CG  GLN A 521      57.722  22.627  53.768  1.00 78.07           C  
ANISOU 3967  CG  GLN A 521     9639  10279   9746   -466  -1499  -1525       C  
ATOM   3968  CD  GLN A 521      56.858  23.873  53.724  1.00 80.62           C  
ANISOU 3968  CD  GLN A 521     9947  10529  10156   -509  -1443  -1643       C  
ATOM   3969  NE2 GLN A 521      57.232  24.879  54.529  1.00 83.37           N  
ANISOU 3969  NE2 GLN A 521    10168  10841  10666   -506  -1611  -1900       N  
ATOM   3970  OE1 GLN A 521      55.878  23.948  52.973  1.00 77.63           O  
ANISOU 3970  OE1 GLN A 521     9665  10119   9714   -540  -1263  -1513       O  
ATOM   3971  N   ILE A 522      57.548  19.372  50.492  1.00 71.36           N  
ANISOU 3971  N   ILE A 522     9112   9349   8652   -443   -997   -751       N  
ATOM   3972  CA  ILE A 522      57.048  18.241  49.742  1.00 73.34           C  
ANISOU 3972  CA  ILE A 522     9535   9618   8712   -421   -886   -558       C  
ATOM   3973  C   ILE A 522      57.902  17.015  50.050  1.00 74.79           C  
ANISOU 3973  C   ILE A 522     9735   9865   8817   -364   -956   -486       C  
ATOM   3974  O   ILE A 522      57.363  15.965  50.392  1.00 72.33           O  
ANISOU 3974  O   ILE A 522     9566   9661   8254   -338   -982   -414       O  
ATOM   3975  CB  ILE A 522      56.996  18.491  48.212  1.00 75.66           C  
ANISOU 3975  CB  ILE A 522     9846   9753   9147   -425   -688   -419       C  
ATOM   3976  CG1 ILE A 522      55.826  19.426  47.872  1.00 78.60           C  
ANISOU 3976  CG1 ILE A 522    10259  10092   9515   -470   -612   -449       C  
ATOM   3977  CG2 ILE A 522      56.854  17.169  47.463  1.00 71.33           C  
ANISOU 3977  CG2 ILE A 522     9463   9212   8427   -377   -613   -244       C  
ATOM   3978  CD1 ILE A 522      55.794  19.996  46.456  1.00 80.69           C  
ANISOU 3978  CD1 ILE A 522    10515  10201   9941   -460   -426   -334       C  
ATOM   3979  N   LYS A 523      59.224  17.139  49.934  1.00 79.14           N  
ANISOU 3979  N   LYS A 523    10129  10339   9601   -344   -981   -492       N  
ATOM   3980  CA  LYS A 523      60.101  15.977  50.121  1.00 82.73           C  
ANISOU 3980  CA  LYS A 523    10588  10839  10008   -284  -1033   -406       C  
ATOM   3981  C   LYS A 523      59.978  15.406  51.528  1.00 81.93           C  
ANISOU 3981  C   LYS A 523    10528  10924   9677   -251  -1222   -488       C  
ATOM   3982  O   LYS A 523      59.925  14.180  51.701  1.00 79.81           O  
ANISOU 3982  O   LYS A 523    10373  10735   9217   -203  -1230   -376       O  
ATOM   3983  CB  LYS A 523      61.561  16.308  49.814  1.00 88.67           C  
ANISOU 3983  CB  LYS A 523    11131  11469  11089   -266  -1030   -400       C  
ATOM   3984  CG  LYS A 523      61.873  16.506  48.335  1.00 96.71           C  
ANISOU 3984  CG  LYS A 523    12130  12311  12303   -253   -804   -247       C  
ATOM   3985  CD  LYS A 523      61.908  15.189  47.559  1.00100.83           C  
ANISOU 3985  CD  LYS A 523    12815  12831  12664   -183   -689    -60       C  
ATOM   3986  CE  LYS A 523      61.998  15.416  46.048  1.00102.33           C  
ANISOU 3986  CE  LYS A 523    13038  12867  12976   -142   -453     86       C  
ATOM   3987  NZ  LYS A 523      61.490  14.270  45.238  1.00101.11           N1+
ANISOU 3987  NZ  LYS A 523    13116  12720  12582    -79   -354    223       N1+
ATOM   3988  N   LYS A 524      59.919  16.294  52.521  1.00 79.82           N  
ANISOU 3988  N   LYS A 524    10178  10723   9428   -263  -1368   -683       N  
ATOM   3989  CA  LYS A 524      59.746  15.878  53.914  1.00 79.25           C  
ANISOU 3989  CA  LYS A 524    10160  10845   9105   -204  -1546   -772       C  
ATOM   3990  C   LYS A 524      58.372  15.245  54.094  1.00 75.47           C  
ANISOU 3990  C   LYS A 524     9887  10475   8312   -195  -1471   -681       C  
ATOM   3991  O   LYS A 524      58.223  14.209  54.746  1.00 75.39           O  
ANISOU 3991  O   LYS A 524     9974  10598   8072   -130  -1518   -601       O  
ATOM   3992  CB  LYS A 524      59.871  17.063  54.887  1.00 81.52           C  
ANISOU 3992  CB  LYS A 524    10337  11174   9462   -204  -1719  -1025       C  
ATOM   3993  CG  LYS A 524      61.210  17.794  54.865  1.00 84.11           C  
ANISOU 3993  CG  LYS A 524    10428  11382  10147   -220  -1833  -1147       C  
ATOM   3994  N   GLN A 525      57.365  15.881  53.519  1.00 71.95           N  
ANISOU 3994  N   GLN A 525     9494   9966   7878   -256  -1350   -681       N  
ATOM   3995  CA  GLN A 525      56.011  15.385  53.636  1.00 71.55           C  
ANISOU 3995  CA  GLN A 525     9609   9995   7582   -257  -1276   -593       C  
ATOM   3996  C   GLN A 525      55.831  14.066  52.862  1.00 70.61           C  
ANISOU 3996  C   GLN A 525     9604   9836   7387   -252  -1174   -379       C  
ATOM   3997  O   GLN A 525      55.066  13.185  53.272  1.00 71.10           O  
ANISOU 3997  O   GLN A 525     9784   9988   7243   -226  -1163   -281       O  
ATOM   3998  CB  GLN A 525      55.030  16.469  53.204  1.00 71.85           C  
ANISOU 3998  CB  GLN A 525     9653   9964   7682   -322  -1186   -655       C  
ATOM   3999  CG  GLN A 525      54.999  17.619  54.198  1.00 74.37           C  
ANISOU 3999  CG  GLN A 525     9894  10345   8017   -309  -1299   -875       C  
ATOM   4000  CD  GLN A 525      54.119  18.779  53.772  1.00 78.71           C  
ANISOU 4000  CD  GLN A 525    10431  10812   8665   -371  -1207   -943       C  
ATOM   4001  NE2 GLN A 525      53.369  19.322  54.721  1.00 80.93           N  
ANISOU 4001  NE2 GLN A 525    10747  11196   8805   -341  -1256  -1067       N  
ATOM   4002  OE1 GLN A 525      54.112  19.190  52.609  1.00 80.45           O  
ANISOU 4002  OE1 GLN A 525    10614  10878   9076   -431  -1088   -879       O  
ATOM   4003  N   THR A 526      56.566  13.906  51.772  1.00 70.22           N  
ANISOU 4003  N   THR A 526     9516   9648   7516   -266  -1099   -305       N  
ATOM   4004  CA  THR A 526      56.607  12.622  51.087  1.00 70.98           C  
ANISOU 4004  CA  THR A 526     9718   9701   7550   -241  -1028   -130       C  
ATOM   4005  C   THR A 526      57.163  11.551  52.052  1.00 70.89           C  
ANISOU 4005  C   THR A 526     9716   9809   7408   -171  -1133    -84       C  
ATOM   4006  O   THR A 526      56.612  10.441  52.149  1.00 71.49           O  
ANISOU 4006  O   THR A 526     9912   9923   7328   -148  -1110     42       O  
ATOM   4007  CB  THR A 526      57.436  12.689  49.767  1.00 71.16           C  
ANISOU 4007  CB  THR A 526     9700   9559   7780   -237   -919    -65       C  
ATOM   4008  CG2 THR A 526      57.521  11.316  49.111  1.00 69.00           C  
ANISOU 4008  CG2 THR A 526     9549   9241   7426   -192   -859     94       C  
ATOM   4009  OG1 THR A 526      56.832  13.610  48.837  1.00 70.24           O  
ANISOU 4009  OG1 THR A 526     9593   9339   7756   -284   -808    -79       O  
ATOM   4010  N   ALA A 527      58.242  11.882  52.761  1.00 69.82           N  
ANISOU 4010  N   ALA A 527     9450   9726   7353   -133  -1254   -181       N  
ATOM   4011  CA  ALA A 527      58.889  10.914  53.656  1.00 71.67           C  
ANISOU 4011  CA  ALA A 527     9683  10077   7473    -51  -1365   -135       C  
ATOM   4012  C   ALA A 527      57.954  10.513  54.785  1.00 72.46           C  
ANISOU 4012  C   ALA A 527     9887  10349   7296     -6  -1418   -123       C  
ATOM   4013  O   ALA A 527      57.927   9.352  55.198  1.00 69.95           O  
ANISOU 4013  O   ALA A 527     9642  10102   6833     55  -1426     10       O  
ATOM   4014  CB  ALA A 527      60.186  11.469  54.214  1.00 72.83           C  
ANISOU 4014  CB  ALA A 527     9653  10244   7774    -17  -1512   -263       C  
ATOM   4015  N   LEU A 528      57.170  11.479  55.257  1.00 73.45           N  
ANISOU 4015  N   LEU A 528    10017  10532   7358    -30  -1437   -248       N  
ATOM   4016  CA  LEU A 528      56.215  11.242  56.320  1.00 73.43           C  
ANISOU 4016  CA  LEU A 528    10112  10693   7096     27  -1459   -233       C  
ATOM   4017  C   LEU A 528      55.128  10.272  55.886  1.00 72.47           C  
ANISOU 4017  C   LEU A 528    10119  10538   6876      4  -1320    -35       C  
ATOM   4018  O   LEU A 528      54.738   9.378  56.639  1.00 70.44           O  
ANISOU 4018  O   LEU A 528     9936  10392   6436     75  -1319     84       O  
ATOM   4019  CB  LEU A 528      55.596  12.570  56.762  1.00 74.25           C  
ANISOU 4019  CB  LEU A 528    10193  10838   7183      8  -1486   -415       C  
ATOM   4020  CG  LEU A 528      54.592  12.452  57.903  1.00 75.63           C  
ANISOU 4020  CG  LEU A 528    10468  11188   7081     89  -1489   -405       C  
ATOM   4021  CD1 LEU A 528      55.183  11.649  59.052  1.00 77.32           C  
ANISOU 4021  CD1 LEU A 528    10707  11576   7094    228  -1606   -368       C  
ATOM   4022  CD2 LEU A 528      54.153  13.834  58.353  1.00 76.61           C  
ANISOU 4022  CD2 LEU A 528    10562  11345   7201     86  -1528   -614       C  
ATOM   4023  N   VAL A 529      54.624  10.465  54.674  1.00 71.44           N  
ANISOU 4023  N   VAL A 529    10012  10252   6879    -90  -1206      2       N  
ATOM   4024  CA  VAL A 529      53.594   9.582  54.154  1.00 71.14           C  
ANISOU 4024  CA  VAL A 529    10084  10155   6790   -121  -1101    167       C  
ATOM   4025  C   VAL A 529      54.115   8.159  54.137  1.00 74.59           C  
ANISOU 4025  C   VAL A 529    10564  10581   7198    -70  -1107    321       C  
ATOM   4026  O   VAL A 529      53.460   7.244  54.632  1.00 77.32           O  
ANISOU 4026  O   VAL A 529    10977  10976   7426    -38  -1080    457       O  
ATOM   4027  CB  VAL A 529      53.177   9.970  52.723  1.00 66.79           C  
ANISOU 4027  CB  VAL A 529     9555   9430   6393   -211  -1008    170       C  
ATOM   4028  CG1 VAL A 529      52.252   8.915  52.127  1.00 60.47           C  
ANISOU 4028  CG1 VAL A 529     8863   8549   5563   -237   -939    327       C  
ATOM   4029  CG2 VAL A 529      52.528  11.349  52.725  1.00 66.57           C  
ANISOU 4029  CG2 VAL A 529     9487   9404   6401   -261   -987     40       C  
ATOM   4030  N   GLU A 530      55.296   7.989  53.553  1.00 79.49           N  
ANISOU 4030  N   GLU A 530    11134  11122   7945    -60  -1128    310       N  
ATOM   4031  CA  GLU A 530      55.918   6.676  53.421  1.00 82.58           C  
ANISOU 4031  CA  GLU A 530    11559  11481   8336     -8  -1127    448       C  
ATOM   4032  C   GLU A 530      56.202   6.022  54.781  1.00 84.05           C  
ANISOU 4032  C   GLU A 530    11736  11835   8362     90  -1211    506       C  
ATOM   4033  O   GLU A 530      56.194   4.797  54.920  1.00 90.69           O  
ANISOU 4033  O   GLU A 530    12633  12671   9154    136  -1189    663       O  
ATOM   4034  CB  GLU A 530      57.207   6.792  52.600  1.00 84.16           C  
ANISOU 4034  CB  GLU A 530    11688  11574   8714      0  -1125    416       C  
ATOM   4035  CG  GLU A 530      56.983   7.030  51.111  1.00 87.82           C  
ANISOU 4035  CG  GLU A 530    12200  11862   9307    -56  -1013    422       C  
ATOM   4036  CD  GLU A 530      56.196   5.912  50.420  1.00 90.40           C  
ANISOU 4036  CD  GLU A 530    12669  12091   9586    -64   -947    550       C  
ATOM   4037  OE1 GLU A 530      56.133   4.783  50.959  1.00 95.08           O  
ANISOU 4037  OE1 GLU A 530    13306  12719  10100    -24   -972    659       O  
ATOM   4038  OE2 GLU A 530      55.641   6.164  49.327  1.00 85.35           O1-
ANISOU 4038  OE2 GLU A 530    12098  11334   8998   -105   -877    540       O1-
ATOM   4039  N   LEU A 531      56.451   6.847  55.781  1.00 80.13           N  
ANISOU 4039  N   LEU A 531    11175  11485   7784    134  -1310    378       N  
ATOM   4040  CA  LEU A 531      56.669   6.364  57.131  1.00 82.09           C  
ANISOU 4040  CA  LEU A 531    11430  11920   7842    253  -1399    418       C  
ATOM   4041  C   LEU A 531      55.426   5.683  57.696  1.00 81.14           C  
ANISOU 4041  C   LEU A 531    11414  11870   7546    287  -1314    573       C  
ATOM   4042  O   LEU A 531      55.488   4.577  58.241  1.00 84.08           O  
ANISOU 4042  O   LEU A 531    11826  12302   7820    370  -1304    739       O  
ATOM   4043  CB  LEU A 531      57.046   7.547  58.008  1.00 82.85           C  
ANISOU 4043  CB  LEU A 531    11451  12149   7880    296  -1535    209       C  
ATOM   4044  CG  LEU A 531      57.757   7.331  59.321  1.00 83.78           C  
ANISOU 4044  CG  LEU A 531    11544  12459   7828    441  -1691    177       C  
ATOM   4045  CD1 LEU A 531      58.913   6.360  59.188  1.00 82.23           C  
ANISOU 4045  CD1 LEU A 531    11300  12235   7709    489  -1742    282       C  
ATOM   4046  CD2 LEU A 531      58.235   8.720  59.745  1.00 85.32           C  
ANISOU 4046  CD2 LEU A 531    11643  12704   8069    443  -1842    -88       C  
ATOM   4047  N   LEU A 532      54.297   6.363  57.565  1.00 75.06           N  
ANISOU 4047  N   LEU A 532    10677  11086   6757    225  -1243    530       N  
ATOM   4048  CA  LEU A 532      53.043   5.851  58.065  1.00 72.04           C  
ANISOU 4048  CA  LEU A 532    10368  10754   6248    250  -1145    680       C  
ATOM   4049  C   LEU A 532      52.548   4.670  57.242  1.00 72.71           C  
ANISOU 4049  C   LEU A 532    10502  10677   6448    191  -1047    873       C  
ATOM   4050  O   LEU A 532      51.849   3.812  57.767  1.00 74.71           O  
ANISOU 4050  O   LEU A 532    10796  10962   6630    237   -978   1054       O  
ATOM   4051  CB  LEU A 532      51.998   6.958  58.082  1.00 73.48           C  
ANISOU 4051  CB  LEU A 532    10558  10951   6412    198  -1096    577       C  
ATOM   4052  CG  LEU A 532      52.026   7.922  59.281  1.00 77.24           C  
ANISOU 4052  CG  LEU A 532    11022  11620   6704    297  -1168    427       C  
ATOM   4053  CD1 LEU A 532      51.519   7.226  60.535  1.00 76.98           C  
ANISOU 4053  CD1 LEU A 532    11055  11764   6429    445  -1127    582       C  
ATOM   4054  CD2 LEU A 532      53.406   8.541  59.526  1.00 76.17           C  
ANISOU 4054  CD2 LEU A 532    10812  11536   6593    335  -1336    231       C  
ATOM   4055  N   LYS A 533      52.907   4.602  55.958  1.00 90.36           N  
ANISOU 4055  N   LYS A 533    12900  14719   6716   1013  -1978   1150       N  
ATOM   4056  CA  LYS A 533      52.562   3.424  55.141  1.00 89.74           C  
ANISOU 4056  CA  LYS A 533    13151  14389   6557    761  -2038   1353       C  
ATOM   4057  C   LYS A 533      53.302   2.155  55.614  1.00 93.40           C  
ANISOU 4057  C   LYS A 533    14001  14586   6902    774  -2122   1498       C  
ATOM   4058  O   LYS A 533      52.793   1.043  55.502  1.00 95.82           O  
ANISOU 4058  O   LYS A 533    14578  14725   7105    500  -2137   1700       O  
ATOM   4059  CB  LYS A 533      52.868   3.681  53.666  1.00 86.86           C  
ANISOU 4059  CB  LYS A 533    12811  13792   6399    838  -2028   1267       C  
ATOM   4060  CG  LYS A 533      51.845   4.558  52.955  1.00 84.02           C  
ANISOU 4060  CG  LYS A 533    12147  13692   6084    783  -1931   1256       C  
ATOM   4061  CD  LYS A 533      52.027   4.513  51.451  1.00 81.35           C  
ANISOU 4061  CD  LYS A 533    11859  13204   5846    843  -1929   1246       C  
ATOM   4062  CE  LYS A 533      51.247   5.625  50.769  1.00 80.78           C  
ANISOU 4062  CE  LYS A 533    11439  13426   5830    948  -1794   1266       C  
ATOM   4063  NZ  LYS A 533      51.517   5.767  49.314  1.00 76.62           N1+
ANISOU 4063  NZ  LYS A 533    10891  12843   5376   1108  -1761   1286       N1+
ATOM   4064  N   HIS A 534      54.496   2.346  56.169  1.00 93.79           N  
ANISOU 4064  N   HIS A 534    14054  14605   6975   1102  -2156   1384       N  
ATOM   4065  CA  HIS A 534      55.340   1.252  56.631  1.00 95.37           C  
ANISOU 4065  CA  HIS A 534    14595  14597   7045   1237  -2224   1531       C  
ATOM   4066  C   HIS A 534      55.173   1.026  58.147  1.00 99.29           C  
ANISOU 4066  C   HIS A 534    15022  15452   7253   1300  -2207   1694       C  
ATOM   4067  O   HIS A 534      55.140  -0.120  58.613  1.00100.65           O  
ANISOU 4067  O   HIS A 534    15504  15488   7250   1254  -2202   2011       O  
ATOM   4068  CB  HIS A 534      56.802   1.548  56.256  1.00 93.92           C  
ANISOU 4068  CB  HIS A 534    14426  14253   7006   1599  -2277   1303       C  
ATOM   4069  CG  HIS A 534      57.810   0.720  56.998  1.00 95.27           C  
ANISOU 4069  CG  HIS A 534    14825  14381   6991   1877  -2343   1403       C  
ATOM   4070  CD2 HIS A 534      58.549   0.996  58.098  1.00 93.57           C  
ANISOU 4070  CD2 HIS A 534    14428  14521   6603   2185  -2363   1303       C  
ATOM   4071  ND1 HIS A 534      58.160  -0.557  56.610  1.00 96.50           N  
ANISOU 4071  ND1 HIS A 534    15431  14126   7108   1894  -2387   1617       N  
ATOM   4072  CE1 HIS A 534      59.057  -1.036  57.452  1.00 95.96           C  
ANISOU 4072  CE1 HIS A 534    15470  14149   6841   2232  -2422   1705       C  
ATOM   4073  NE2 HIS A 534      59.312  -0.113  58.360  1.00 94.58           N  
ANISOU 4073  NE2 HIS A 534    14897  14483   6555   2415  -2418   1511       N  
ATOM   4074  N   LYS A 535      55.061   2.106  58.919  1.00 99.16           N  
ANISOU 4074  N   LYS A 535    14590  15896   7189   1422  -2178   1486       N  
ATOM   4075  CA  LYS A 535      54.840   1.993  60.373  1.00102.73           C  
ANISOU 4075  CA  LYS A 535    14892  16825   7315   1510  -2164   1606       C  
ATOM   4076  C   LYS A 535      53.523   2.692  60.741  1.00102.41           C  
ANISOU 4076  C   LYS A 535    14521  17177   7211   1274  -2094   1582       C  
ATOM   4077  O   LYS A 535      53.536   3.751  61.378  1.00100.31           O  
ANISOU 4077  O   LYS A 535    13851  17326   6937   1434  -2076   1282       O  
ATOM   4078  CB  LYS A 535      56.034   2.565  61.165  1.00100.41           C  
ANISOU 4078  CB  LYS A 535    14351  16856   6945   1934  -2210   1301       C  
ATOM   4079  N   PRO A 536      52.376   2.089  60.337  1.00101.47           N  
ANISOU 4079  N   PRO A 536    14556  16944   7054    888  -2049   1862       N  
ATOM   4080  CA  PRO A 536      51.050   2.714  60.455  1.00100.52           C  
ANISOU 4080  CA  PRO A 536    14127  17192   6875    645  -1985   1840       C  
ATOM   4081  C   PRO A 536      50.507   2.879  61.871  1.00103.20           C  
ANISOU 4081  C   PRO A 536    14191  18138   6883    681  -1950   1925       C  
ATOM   4082  O   PRO A 536      49.612   3.699  62.078  1.00102.31           O  
ANISOU 4082  O   PRO A 536    13729  18415   6729    602  -1908   1790       O  
ATOM   4083  CB  PRO A 536      50.147   1.766  59.660  1.00101.23           C  
ANISOU 4083  CB  PRO A 536    14482  17003   6978    214  -1953   2107       C  
ATOM   4084  CG  PRO A 536      50.818   0.445  59.755  1.00103.02           C  
ANISOU 4084  CG  PRO A 536    15161  16814   7169    211  -1966   2378       C  
ATOM   4085  CD  PRO A 536      52.287   0.740  59.743  1.00101.35           C  
ANISOU 4085  CD  PRO A 536    15005  16447   7057    654  -2046   2178       C  
ATOM   4086  N   LYS A 537      51.022   2.112  62.828  1.00106.67           N  
ANISOU 4086  N   LYS A 537    14770  18700   7061    835  -1958   2162       N  
ATOM   4087  CA  LYS A 537      50.575   2.236  64.219  1.00110.65           C  
ANISOU 4087  CA  LYS A 537    14981  19874   7186    925  -1921   2266       C  
ATOM   4088  C   LYS A 537      51.462   3.184  65.030  1.00111.20           C  
ANISOU 4088  C   LYS A 537    14680  20394   7176   1372  -1982   1846       C  
ATOM   4089  O   LYS A 537      51.250   3.346  66.228  1.00115.15           O  
ANISOU 4089  O   LYS A 537    14885  21540   7326   1526  -1971   1855       O  
ATOM   4090  CB  LYS A 537      50.491   0.856  64.888  1.00115.48           C  
ANISOU 4090  CB  LYS A 537    15909  20461   7508    854  -1851   2833       C  
ATOM   4091  CG  LYS A 537      49.129   0.184  64.728  1.00117.33           C  
ANISOU 4091  CG  LYS A 537    16251  20636   7692    342  -1733   3204       C  
ATOM   4092  N   ALA A 538      52.448   3.803  64.380  1.00107.96           N  
ANISOU 4092  N   ALA A 538    14254  19681   7083   1567  -2036   1455       N  
ATOM   4093  CA  ALA A 538      53.394   4.706  65.052  1.00108.28           C  
ANISOU 4093  CA  ALA A 538    13926  20097   7120   1946  -2079    963       C  
ATOM   4094  C   ALA A 538      52.679   5.839  65.785  1.00109.40           C  
ANISOU 4094  C   ALA A 538    13547  20817   7204   1970  -2038    609       C  
ATOM   4095  O   ALA A 538      51.751   6.425  65.238  1.00109.09           O  
ANISOU 4095  O   ALA A 538    13415  20668   7369   1748  -1975    554       O  
ATOM   4096  CB  ALA A 538      54.374   5.284  64.043  1.00102.97           C  
ANISOU 4096  CB  ALA A 538    13302  18933   6890   2044  -2096    601       C  
ATOM   4097  N   THR A 539      53.127   6.159  67.003  1.00111.88           N  
ANISOU 4097  N   THR A 539    13500  21783   7225   2273  -2073    341       N  
ATOM   4098  CA  THR A 539      52.404   7.101  67.874  1.00115.26           C  
ANISOU 4098  CA  THR A 539    13416  22858   7519   2321  -2041      2       C  
ATOM   4099  C   THR A 539      52.767   8.567  67.644  1.00115.39           C  
ANISOU 4099  C   THR A 539    13059  22799   7983   2424  -1995   -721       C  
ATOM   4100  O   THR A 539      53.908   8.896  67.297  1.00112.40           O  
ANISOU 4100  O   THR A 539    12675  22139   7891   2570  -2006  -1069       O  
ATOM   4101  CB  THR A 539      52.618   6.796  69.379  1.00118.63           C  
ANISOU 4101  CB  THR A 539    13549  24158   7367   2620  -2091     10       C  
ATOM   4102  CG2 THR A 539      52.253   5.354  69.715  1.00118.11           C  
ANISOU 4102  CG2 THR A 539    13844  24161   6870   2547  -2077    791       C  
ATOM   4103  OG1 THR A 539      53.983   7.045  69.736  1.00119.52           O  
ANISOU 4103  OG1 THR A 539    13485  24454   7473   2972  -2160   -426       O  
ATOM   4104  N   GLU A 540      51.779   9.440  67.869  1.00118.00           N  
ANISOU 4104  N   GLU A 540    13068  23387   8381   2351  -1924   -943       N  
ATOM   4105  CA  GLU A 540      51.935  10.887  67.682  1.00118.90           C  
ANISOU 4105  CA  GLU A 540    12828  23373   8976   2438  -1824  -1605       C  
ATOM   4106  C   GLU A 540      53.237  11.384  68.315  1.00122.91           C  
ANISOU 4106  C   GLU A 540    13024  24114   9562   2712  -1853  -2233       C  
ATOM   4107  O   GLU A 540      54.016  12.105  67.684  1.00125.64           O  
ANISOU 4107  O   GLU A 540    13332  23973  10431   2733  -1770  -2635       O  
ATOM   4108  CB  GLU A 540      50.733  11.635  68.275  1.00115.80           C  
ANISOU 4108  CB  GLU A 540    12057  23461   8480   2427  -1762  -1785       C  
ATOM   4109  N   GLU A 541      53.484  10.956  69.547  1.00125.26           N  
ANISOU 4109  N   GLU A 541    13083  25192   9316   2924  -1960  -2297       N  
ATOM   4110  CA  GLU A 541      54.690  11.348  70.268  1.00129.90           C  
ANISOU 4110  CA  GLU A 541    13300  26195   9861   3208  -2008  -2930       C  
ATOM   4111  C   GLU A 541      55.965  10.902  69.544  1.00127.63           C  
ANISOU 4111  C   GLU A 541    13313  25399   9782   3251  -2043  -2883       C  
ATOM   4112  O   GLU A 541      56.937  11.660  69.487  1.00133.84           O  
ANISOU 4112  O   GLU A 541    13831  26108  10914   3342  -2003  -3528       O  
ATOM   4113  CB  GLU A 541      54.681  10.784  71.701  1.00131.68           C  
ANISOU 4113  CB  GLU A 541    13233  27464   9337   3483  -2126  -2876       C  
ATOM   4114  N   GLN A 542      55.964   9.680  69.005  1.00121.92           N  
ANISOU 4114  N   GLN A 542    13124  24338   8863   3179  -2104  -2155       N  
ATOM   4115  CA  GLN A 542      57.136   9.147  68.293  1.00117.59           C  
ANISOU 4115  CA  GLN A 542    12891  23324   8464   3248  -2148  -2061       C  
ATOM   4116  C   GLN A 542      57.494   9.975  67.063  1.00114.70           C  
ANISOU 4116  C   GLN A 542    12598  22179   8805   3072  -2033  -2355       C  
ATOM   4117  O   GLN A 542      58.659  10.276  66.835  1.00118.33           O  
ANISOU 4117  O   GLN A 542    12956  22506   9497   3184  -2026  -2748       O  
ATOM   4118  CB  GLN A 542      56.904   7.706  67.843  1.00115.05           C  
ANISOU 4118  CB  GLN A 542    13159  22674   7878   3170  -2204  -1231       C  
ATOM   4119  CG  GLN A 542      56.986   6.673  68.945  1.00117.07           C  
ANISOU 4119  CG  GLN A 542    13441  23577   7464   3427  -2285   -838       C  
ATOM   4120  CD  GLN A 542      56.658   5.277  68.453  1.00115.85           C  
ANISOU 4120  CD  GLN A 542    13899  22957   7160   3297  -2283    -18       C  
ATOM   4121  NE2 GLN A 542      57.510   4.326  68.793  1.00117.21           N  
ANISOU 4121  NE2 GLN A 542    14275  23253   7006   3602  -2338    272       N  
ATOM   4122  OE1 GLN A 542      55.643   5.052  67.788  1.00113.13           O  
ANISOU 4122  OE1 GLN A 542    13825  22165   6993   2937  -2222    333       O  
ATOM   4123  N   LEU A 543      56.486  10.338  66.278  1.00109.57           N  
ANISOU 4123  N   LEU A 543    12100  21063   8469   2813  -1928  -2144       N  
ATOM   4124  CA  LEU A 543      56.695  11.147  65.083  1.00105.86           C  
ANISOU 4124  CA  LEU A 543    11696  19879   8646   2681  -1779  -2321       C  
ATOM   4125  C   LEU A 543      57.267  12.535  65.421  1.00107.12           C  
ANISOU 4125  C   LEU A 543    11354  20100   9246   2767  -1639  -3124       C  
ATOM   4126  O   LEU A 543      58.023  13.101  64.637  1.00104.47           O  
ANISOU 4126  O   LEU A 543    11023  19249   9421   2734  -1513  -3363       O  
ATOM   4127  CB  LEU A 543      55.379  11.304  64.298  1.00104.25           C  
ANISOU 4127  CB  LEU A 543    11680  19328   8604   2453  -1687  -1933       C  
ATOM   4128  CG  LEU A 543      54.556  10.065  63.893  1.00102.38           C  
ANISOU 4128  CG  LEU A 543    11880  19006   8014   2272  -1783  -1215       C  
ATOM   4129  CD1 LEU A 543      53.194  10.469  63.357  1.00100.22           C  
ANISOU 4129  CD1 LEU A 543    11603  18621   7855   2079  -1684  -1008       C  
ATOM   4130  CD2 LEU A 543      55.261   9.197  62.871  1.00 97.88           C  
ANISOU 4130  CD2 LEU A 543    11760  17904   7524   2228  -1839   -888       C  
ATOM   4131  N   LYS A 544      56.899  13.091  66.576  1.00111.17           N  
ANISOU 4131  N   LYS A 544    11419  21237   9582   2865  -1639  -3558       N  
ATOM   4132  CA  LYS A 544      57.446  14.382  66.999  1.00114.36           C  
ANISOU 4132  CA  LYS A 544    11311  21721  10419   2929  -1497  -4418       C  
ATOM   4133  C   LYS A 544      58.965  14.319  66.924  1.00115.87           C  
ANISOU 4133  C   LYS A 544    11415  21875  10736   3018  -1522  -4792       C  
ATOM   4134  O   LYS A 544      59.606  15.143  66.261  1.00114.76           O  
ANISOU 4134  O   LYS A 544    11183  21193  11227   2924  -1334  -5166       O  
ATOM   4135  CB  LYS A 544      56.984  14.750  68.420  1.00116.88           C  
ANISOU 4135  CB  LYS A 544    11129  22906  10375   3075  -1553  -4876       C  
ATOM   4136  N   THR A 545      59.529  13.314  67.583  1.00119.39           N  
ANISOU 4136  N   THR A 545    11892  22901  10571   3212  -1735  -4644       N  
ATOM   4137  CA  THR A 545      60.973  13.125  67.598  1.00126.10           C  
ANISOU 4137  CA  THR A 545    12637  23865  11412   3352  -1791  -4973       C  
ATOM   4138  C   THR A 545      61.544  12.749  66.220  1.00121.51           C  
ANISOU 4138  C   THR A 545    12522  22474  11172   3236  -1746  -4576       C  
ATOM   4139  O   THR A 545      62.630  13.204  65.861  1.00123.44           O  
ANISOU 4139  O   THR A 545    12604  22522  11775   3230  -1665  -5014       O  
ATOM   4140  CB  THR A 545      61.398  12.070  68.645  1.00132.70           C  
ANISOU 4140  CB  THR A 545    13408  25574  11439   3673  -2023  -4818       C  
ATOM   4141  CG2 THR A 545      61.249  12.628  70.074  1.00136.62           C  
ANISOU 4141  CG2 THR A 545    13264  27041  11604   3856  -2061  -5455       C  
ATOM   4142  OG1 THR A 545      60.594  10.891  68.497  1.00132.07           O  
ANISOU 4142  OG1 THR A 545    13838  25409  10931   3672  -2124  -3915       O  
ATOM   4143  N   VAL A 546      60.820  11.939  65.451  1.00117.28           N  
ANISOU 4143  N   VAL A 546    12527  21509  10527   3133  -1790  -3794       N  
ATOM   4144  CA  VAL A 546      61.282  11.562  64.115  1.00112.28           C  
ANISOU 4144  CA  VAL A 546    12318  20164  10180   3040  -1756  -3429       C  
ATOM   4145  C   VAL A 546      61.320  12.788  63.215  1.00113.85           C  
ANISOU 4145  C   VAL A 546    12391  19739  11127   2856  -1497  -3721       C  
ATOM   4146  O   VAL A 546      62.319  13.041  62.548  1.00114.56           O  
ANISOU 4146  O   VAL A 546    12473  19491  11564   2846  -1410  -3908       O  
ATOM   4147  CB  VAL A 546      60.399  10.490  63.453  1.00106.96           C  
ANISOU 4147  CB  VAL A 546    12203  19175   9262   2935  -1842  -2611       C  
ATOM   4148  CG1 VAL A 546      60.893  10.219  62.037  1.00103.28           C  
ANISOU 4148  CG1 VAL A 546    12105  18025   9111   2856  -1801  -2336       C  
ATOM   4149  CG2 VAL A 546      60.396   9.209  64.272  1.00104.52           C  
ANISOU 4149  CG2 VAL A 546    12078  19355   8278   3112  -2043  -2233       C  
ATOM   4150  N   MET A 547      60.230  13.545  63.200  1.00118.34           N  
ANISOU 4150  N   MET A 547    12857  20167  11938   2733  -1353  -3731       N  
ATOM   4151  CA  MET A 547      60.197  14.819  62.482  1.00122.60           C  
ANISOU 4151  CA  MET A 547    13241  20130  13213   2614  -1053  -4003       C  
ATOM   4152  C   MET A 547      61.305  15.735  63.002  1.00128.05           C  
ANISOU 4152  C   MET A 547    13448  20921  14286   2634   -917  -4838       C  
ATOM   4153  O   MET A 547      62.089  16.276  62.215  1.00131.47           O  
ANISOU 4153  O   MET A 547    13856  20842  15254   2555   -718  -4999       O  
ATOM   4154  CB  MET A 547      58.844  15.527  62.653  1.00124.08           C  
ANISOU 4154  CB  MET A 547    13318  20290  13535   2558   -923  -3963       C  
ATOM   4155  CG  MET A 547      57.699  14.970  61.825  1.00119.51           C  
ANISOU 4155  CG  MET A 547    13150  19475  12784   2482   -958  -3212       C  
ATOM   4156  SD  MET A 547      56.192  15.843  62.285  1.00123.70           S  
ANISOU 4156  SD  MET A 547    13440  20174  13388   2478   -825  -3284       S  
ATOM   4157  CE  MET A 547      54.962  14.963  61.329  1.00114.87           C  
ANISOU 4157  CE  MET A 547    12771  18933  11941   2372   -914  -2422       C  
ATOM   4158  N   GLU A 548      61.363  15.906  64.324  1.00130.17           N  
ANISOU 4158  N   GLU A 548    13301  21886  14272   2733  -1014  -5383       N  
ATOM   4159  CA  GLU A 548      62.395  16.746  64.937  1.00134.40           C  
ANISOU 4159  CA  GLU A 548    13299  22644  15123   2736   -902  -6295       C  
ATOM   4160  C   GLU A 548      63.780  16.355  64.414  1.00136.36           C  
ANISOU 4160  C   GLU A 548    13609  22775  15428   2750   -934  -6359       C  
ATOM   4161  O   GLU A 548      64.612  17.218  64.113  1.00139.59           O  
ANISOU 4161  O   GLU A 548    13739  22863  16434   2620   -702  -6901       O  
ATOM   4162  CB  GLU A 548      62.358  16.643  66.467  1.00133.95           C  
ANISOU 4162  CB  GLU A 548    12797  23576  14523   2911  -1089  -6808       C  
ATOM   4163  N   ASN A 549      64.013  15.048  64.290  1.00133.22           N  
ANISOU 4163  N   ASN A 549    13577  22612  14428   2905  -1199  -5797       N  
ATOM   4164  CA  ASN A 549      65.313  14.545  63.867  1.00132.14           C  
ANISOU 4164  CA  ASN A 549    13506  22470  14232   2984  -1268  -5831       C  
ATOM   4165  C   ASN A 549      65.572  14.662  62.361  1.00130.35           C  
ANISOU 4165  C   ASN A 549    13626  21390  14512   2829  -1094  -5446       C  
ATOM   4166  O   ASN A 549      66.729  14.734  61.963  1.00131.30           O  
ANISOU 4166  O   ASN A 549    13642  21425  14822   2828  -1042  -5694       O  
ATOM   4167  CB  ASN A 549      65.519  13.109  64.366  1.00129.49           C  
ANISOU 4167  CB  ASN A 549    13418  22712  13069   3268  -1594  -5399       C  
ATOM   4168  CG  ASN A 549      65.662  13.044  65.886  1.00132.45           C  
ANISOU 4168  CG  ASN A 549    13330  24084  12911   3499  -1744  -5876       C  
ATOM   4169  ND2 ASN A 549      65.096  12.006  66.491  1.00131.43           N  
ANISOU 4169  ND2 ASN A 549    13433  24405  12101   3709  -1951  -5345       N  
ATOM   4170  OD1 ASN A 549      66.251  13.932  66.507  1.00131.84           O  
ANISOU 4170  OD1 ASN A 549    12672  24379  13041   3484  -1655  -6722       O  
ATOM   4171  N   PHE A 550      64.520  14.683  61.535  1.00126.57           N  
ANISOU 4171  N   PHE A 550    13516  20361  14213   2718  -1004  -4856       N  
ATOM   4172  CA  PHE A 550      64.689  14.965  60.098  1.00125.01           C  
ANISOU 4172  CA  PHE A 550    13570  19414  14514   2599   -798  -4517       C  
ATOM   4173  C   PHE A 550      65.187  16.405  59.938  1.00128.33           C  
ANISOU 4173  C   PHE A 550    13578  19458  15721   2440   -427  -5109       C  
ATOM   4174  O   PHE A 550      66.133  16.656  59.194  1.00127.62           O  
ANISOU 4174  O   PHE A 550    13457  19037  15997   2377   -269  -5189       O  
ATOM   4175  CB  PHE A 550      63.382  14.805  59.276  1.00124.51           C  
ANISOU 4175  CB  PHE A 550    13902  18941  14466   2541   -756  -3819       C  
ATOM   4176  CG  PHE A 550      63.069  13.386  58.798  1.00122.70           C  
ANISOU 4176  CG  PHE A 550    14177  18761  13681   2613  -1027  -3142       C  
ATOM   4177  CD1 PHE A 550      64.068  12.437  58.555  1.00120.40           C  
ANISOU 4177  CD1 PHE A 550    14082  18563  13102   2732  -1207  -3035       C  
ATOM   4178  CD2 PHE A 550      61.737  13.023  58.528  1.00122.46           C  
ANISOU 4178  CD2 PHE A 550    14420  18657  13453   2553  -1077  -2625       C  
ATOM   4179  CE1 PHE A 550      63.743  11.157  58.108  1.00117.51           C  
ANISOU 4179  CE1 PHE A 550    14189  18161  12301   2788  -1422  -2453       C  
ATOM   4180  CE2 PHE A 550      61.411  11.744  58.074  1.00117.82           C  
ANISOU 4180  CE2 PHE A 550    14274  18065  12426   2565  -1291  -2068       C  
ATOM   4181  CZ  PHE A 550      62.416  10.810  57.866  1.00115.52           C  
ANISOU 4181  CZ  PHE A 550    14194  17803  11896   2680  -1457  -1988       C  
ATOM   4182  N   VAL A 551      64.547  17.342  60.643  1.00131.40           N  
ANISOU 4182  N   VAL A 551    13649  19890  16389   2370   -270  -5529       N  
ATOM   4183  CA  VAL A 551      64.911  18.765  60.564  1.00134.62           C  
ANISOU 4183  CA  VAL A 551    13666  19856  17629   2200    133  -6126       C  
ATOM   4184  C   VAL A 551      66.281  19.029  61.177  1.00140.58           C  
ANISOU 4184  C   VAL A 551    13956  20955  18506   2137    149  -6950       C  
ATOM   4185  O   VAL A 551      67.067  19.812  60.636  1.00143.67           O  
ANISOU 4185  O   VAL A 551    14154  20874  19561   1962    468  -7262       O  
ATOM   4186  CB  VAL A 551      63.877  19.665  61.275  1.00134.96           C  
ANISOU 4186  CB  VAL A 551    13464  19899  17915   2174    283  -6449       C  
ATOM   4187  CG1 VAL A 551      64.391  21.099  61.385  1.00138.01           C  
ANISOU 4187  CG1 VAL A 551    13400  19848  19188   1994    707  -7212       C  
ATOM   4188  CG2 VAL A 551      62.539  19.618  60.552  1.00129.61           C  
ANISOU 4188  CG2 VAL A 551    13180  18842  17224   2229    340  -5682       C  
ATOM   4189  N   ALA A 552      66.554  18.384  62.311  1.00142.54           N  
ANISOU 4189  N   ALA A 552    13995  22062  18101   2288   -175  -7294       N  
ATOM   4190  CA  ALA A 552      67.872  18.449  62.940  1.00145.85           C  
ANISOU 4190  CA  ALA A 552    13947  23011  18460   2290   -226  -8062       C  
ATOM   4191  C   ALA A 552      68.938  17.929  61.978  1.00143.05           C  
ANISOU 4191  C   ALA A 552    13800  22431  18123   2292   -235  -7776       C  
ATOM   4192  O   ALA A 552      70.031  18.482  61.887  1.00148.84           O  
ANISOU 4192  O   ALA A 552    14163  23133  19256   2148    -56  -8363       O  
ATOM   4193  CB  ALA A 552      67.887  17.645  64.231  1.00146.17           C  
ANISOU 4193  CB  ALA A 552    13800  24098  17638   2557   -603  -8272       C  
ATOM   4194  N   PHE A 553      68.594  16.865  61.260  1.00136.45           N  
ANISOU 4194  N   PHE A 553    13537  21449  16860   2445   -438  -6901       N  
ATOM   4195  CA  PHE A 553      69.476  16.244  60.268  1.00131.72           C  
ANISOU 4195  CA  PHE A 553    13201  20640  16206   2495   -479  -6536       C  
ATOM   4196  C   PHE A 553      69.641  17.133  59.039  1.00131.63           C  
ANISOU 4196  C   PHE A 553    13233  19784  16998   2260    -81  -6405       C  
ATOM   4197  O   PHE A 553      70.765  17.414  58.631  1.00132.32           O  
ANISOU 4197  O   PHE A 553    13108  19783  17386   2168     68  -6702       O  
ATOM   4198  CB  PHE A 553      68.913  14.864  59.893  1.00126.18           C  
ANISOU 4198  CB  PHE A 553    13100  19995  14848   2716   -794  -5680       C  
ATOM   4199  CG  PHE A 553      69.452  14.287  58.617  1.00122.06           C  
ANISOU 4199  CG  PHE A 553    12950  19076  14351   2757   -800  -5171       C  
ATOM   4200  CD1 PHE A 553      70.814  14.156  58.406  1.00124.13           C  
ANISOU 4200  CD1 PHE A 553    13029  19518  14615   2815   -808  -5473       C  
ATOM   4201  CD2 PHE A 553      68.583  13.820  57.645  1.00118.36           C  
ANISOU 4201  CD2 PHE A 553    12988  18140  13843   2755   -817  -4414       C  
ATOM   4202  CE1 PHE A 553      71.297  13.603  57.233  1.00121.91           C  
ANISOU 4202  CE1 PHE A 553    13078  18921  14321   2880   -824  -5012       C  
ATOM   4203  CE2 PHE A 553      69.063  13.269  56.473  1.00116.43           C  
ANISOU 4203  CE2 PHE A 553    13056  17597  13584   2815   -836  -3988       C  
ATOM   4204  CZ  PHE A 553      70.420  13.161  56.266  1.00117.15           C  
ANISOU 4204  CZ  PHE A 553    12976  17844  13691   2885   -839  -4276       C  
ATOM   4205  N   VAL A 554      68.526  17.587  58.464  1.00132.20           N  
ANISOU 4205  N   VAL A 554    13550  19280  17398   2183    109  -5947       N  
ATOM   4206  CA  VAL A 554      68.567  18.423  57.257  1.00132.83           C  
ANISOU 4206  CA  VAL A 554    13698  18564  18207   2028    520  -5687       C  
ATOM   4207  C   VAL A 554      69.295  19.739  57.529  1.00138.97           C  
ANISOU 4207  C   VAL A 554    13943  19081  19777   1776    926  -6469       C  
ATOM   4208  O   VAL A 554      70.184  20.129  56.771  1.00139.98           O  
ANISOU 4208  O   VAL A 554    13973  18853  20362   1646   1190  -6509       O  
ATOM   4209  CB  VAL A 554      67.155  18.723  56.702  1.00131.08           C  
ANISOU 4209  CB  VAL A 554    13783  17875  18146   2054    657  -5076       C  
ATOM   4210  CG1 VAL A 554      67.229  19.708  55.543  1.00131.51           C  
ANISOU 4210  CG1 VAL A 554    13845  17152  18973   1952   1138  -4818       C  
ATOM   4211  CG2 VAL A 554      66.473  17.442  56.258  1.00127.26           C  
ANISOU 4211  CG2 VAL A 554    13808  17583  16962   2237    304  -4324       C  
ATOM   4212  N   ASP A 555      68.921  20.412  58.617  1.00143.08           N  
ANISOU 4212  N   ASP A 555    14104  19793  20468   1697    986  -7112       N  
ATOM   4213  CA  ASP A 555      69.600  21.643  59.028  1.00148.61           C  
ANISOU 4213  CA  ASP A 555    14248  20283  21935   1426   1365  -8003       C  
ATOM   4214  C   ASP A 555      71.084  21.381  59.310  1.00150.91           C  
ANISOU 4214  C   ASP A 555    14174  21069  22097   1347   1270  -8609       C  
ATOM   4215  O   ASP A 555      71.917  22.261  59.096  1.00156.67           O  
ANISOU 4215  O   ASP A 555    14537  21455  23537   1069   1645  -9136       O  
ATOM   4216  CB  ASP A 555      68.917  22.267  60.256  1.00149.20           C  
ANISOU 4216  CB  ASP A 555    13978  20622  22089   1397   1374  -8663       C  
ATOM   4217  N   LYS A 556      71.407  20.168  59.766  1.00148.03           N  
ANISOU 4217  N   LYS A 556    13908  21502  20837   1599    792  -8509       N  
ATOM   4218  CA  LYS A 556      72.791  19.784  60.111  1.00148.13           C  
ANISOU 4218  CA  LYS A 556    13567  22148  20567   1619    642  -9056       C  
ATOM   4219  C   LYS A 556      73.754  19.624  58.936  1.00145.31           C  
ANISOU 4219  C   LYS A 556    13337  21444  20429   1551    783  -8744       C  
ATOM   4220  O   LYS A 556      74.969  19.715  59.127  1.00146.94           O  
ANISOU 4220  O   LYS A 556    13124  22031  20677   1462    811  -9348       O  
ATOM   4221  CB  LYS A 556      72.805  18.471  60.903  1.00144.51           C  
ANISOU 4221  CB  LYS A 556    13231  22626  19052   1997    109  -8912       C  
ATOM   4222  N   CYS A 557      73.230  19.364  57.740  1.00140.40           N  
ANISOU 4222  N   CYS A 557    13252  20195  19897   1609    860  -7833       N  
ATOM   4223  CA  CYS A 557      74.088  19.088  56.579  1.00139.47           C  
ANISOU 4223  CA  CYS A 557    13283  19832  19876   1605    955  -7455       C  
ATOM   4224  C   CYS A 557      74.127  20.208  55.545  1.00142.94           C  
ANISOU 4224  C   CYS A 557    13679  19382  21251   1327   1515  -7277       C  
ATOM   4225  O   CYS A 557      75.153  20.413  54.892  1.00145.79           O  
ANISOU 4225  O   CYS A 557    13869  19613  21911   1197   1726  -7356       O  
ATOM   4226  CB  CYS A 557      73.669  17.785  55.906  1.00132.02           C  
ANISOU 4226  CB  CYS A 557    12955  18970  18235   1929    597  -6558       C  
ATOM   4227  SG  CYS A 557      74.137  16.292  56.809  1.00128.26           S  
ANISOU 4227  SG  CYS A 557    12560  19482  16691   2301      6  -6654       S  
ATOM   4228  N   CYS A 558      73.027  20.939  55.391  1.00145.09           N  
ANISOU 4228  N   CYS A 558    14090  19058  21981   1259   1779  -7013       N  
ATOM   4229  CA  CYS A 558      73.005  22.047  54.440  1.00149.39           C  
ANISOU 4229  CA  CYS A 558    14601  18724  23435   1051   2363  -6776       C  
ATOM   4230  C   CYS A 558      73.943  23.190  54.862  1.00156.97           C  
ANISOU 4230  C   CYS A 558    14956  19470  25216    661   2798  -7690       C  
ATOM   4231  O   CYS A 558      74.298  24.025  54.036  1.00162.18           O  
ANISOU 4231  O   CYS A 558    15532  19440  26648    455   3316  -7537       O  
ATOM   4232  CB  CYS A 558      71.570  22.544  54.194  1.00148.89           C  
ANISOU 4232  CB  CYS A 558    14829  18112  23628   1140   2546  -6250       C  
ATOM   4233  SG  CYS A 558      70.445  21.326  53.448  1.00140.91           S  
ANISOU 4233  SG  CYS A 558    14491  17261  21786   1525   2138  -5156       S  
ATOM   4234  N   ALA A 559      74.366  23.211  56.128  1.00159.68           N  
ANISOU 4234  N   ALA A 559    14854  20433  25385    561   2603  -8640       N  
ATOM   4235  CA  ALA A 559      75.367  24.182  56.603  1.00164.89           C  
ANISOU 4235  CA  ALA A 559    14863  21039  26750    161   2966  -9659       C  
ATOM   4236  C   ALA A 559      76.812  23.652  56.585  1.00164.58           C  
ANISOU 4236  C   ALA A 559    14509  21636  26387    104   2804 -10060       C  
ATOM   4237  O   ALA A 559      77.751  24.440  56.701  1.00171.72           O  
ANISOU 4237  O   ALA A 559    14880  22438  27927   -272   3161 -10810       O  
ATOM   4238  CB  ALA A 559      75.009  24.663  58.004  1.00168.30           C  
ANISOU 4238  CB  ALA A 559    14879  21829  27238     69   2897 -10599       C  
ATOM   4239  N   ALA A 560      76.991  22.339  56.433  1.00157.02           N  
ANISOU 4239  N   ALA A 560    13867  21317  24478    469   2293  -9582       N  
ATOM   4240  CA  ALA A 560      78.314  21.704  56.573  1.00157.24           C  
ANISOU 4240  CA  ALA A 560    13596  22109  24039    520   2058  -9984       C  
ATOM   4241  C   ALA A 560      79.264  21.967  55.399  1.00156.71           C  
ANISOU 4241  C   ALA A 560    13471  21646  24428    328   2403  -9747       C  
ATOM   4242  O   ALA A 560      78.824  22.196  54.272  1.00154.64           O  
ANISOU 4242  O   ALA A 560    13593  20625  24540    320   2681  -8941       O  
ATOM   4243  CB  ALA A 560      78.157  20.207  56.783  1.00152.49           C  
ANISOU 4243  CB  ALA A 560    13391  22240  22308   1016   1434  -9504       C  
ATOM   4244  N   ASP A 561      80.567  21.898  55.681  1.00158.07           N  
ANISOU 4244  N   ASP A 561    13132  22426  24500    205   2371 -10444       N  
ATOM   4245  CA  ASP A 561      81.625  22.244  54.714  1.00158.92           C  
ANISOU 4245  CA  ASP A 561    13036  22273  25073    -41   2733 -10400       C  
ATOM   4246  C   ASP A 561      81.502  21.512  53.372  1.00151.30           C  
ANISOU 4246  C   ASP A 561    12665  21027  23797    253   2652  -9267       C  
ATOM   4247  O   ASP A 561      81.495  22.152  52.319  1.00151.40           O  
ANISOU 4247  O   ASP A 561    12772  20284  24469     61   3123  -8783       O  
ATOM   4248  CB  ASP A 561      83.009  21.987  55.322  1.00161.70           C  
ANISOU 4248  CB  ASP A 561    12768  23584  25086   -105   2563 -11302       C  
ATOM   4249  N   ASP A 562      81.426  20.182  53.415  1.00143.95           N  
ANISOU 4249  N   ASP A 562    12108  20714  21874    730   2081  -8862       N  
ATOM   4250  CA  ASP A 562      81.141  19.373  52.229  1.00136.80           C  
ANISOU 4250  CA  ASP A 562    11798  19588  20591   1051   1936  -7833       C  
ATOM   4251  C   ASP A 562      79.799  18.679  52.429  1.00128.38           C  
ANISOU 4251  C   ASP A 562    11312  18442  19024   1373   1584  -7248       C  
ATOM   4252  O   ASP A 562      79.749  17.542  52.892  1.00124.52           O  
ANISOU 4252  O   ASP A 562    11053  18554  17707   1732   1078  -7166       O  
ATOM   4253  CB  ASP A 562      82.249  18.340  51.982  1.00134.98           C  
ANISOU 4253  CB  ASP A 562    11534  20092  19662   1336   1594  -7845       C  
ATOM   4254  N   LYS A 563      78.719  19.384  52.084  1.00126.28           N  
ANISOU 4254  N   LYS A 563    11265  17431  19283   1245   1882  -6840       N  
ATOM   4255  CA  LYS A 563      77.338  18.884  52.253  1.00121.91           C  
ANISOU 4255  CA  LYS A 563    11210  16761  18348   1486   1615  -6309       C  
ATOM   4256  C   LYS A 563      77.161  17.465  51.693  1.00117.21           C  
ANISOU 4256  C   LYS A 563    11144  16473  16916   1895   1155  -5628       C  
ATOM   4257  O   LYS A 563      76.507  16.620  52.311  1.00115.78           O  
ANISOU 4257  O   LYS A 563    11248  16619  16126   2128    749  -5507       O  
ATOM   4258  CB  LYS A 563      76.330  19.841  51.598  1.00119.62           C  
ANISOU 4258  CB  LYS A 563    11089  15613  18748   1343   2058  -5821       C  
ATOM   4259  N   GLU A 564      77.763  17.206  50.531  1.00115.70           N  
ANISOU 4259  N   GLU A 564    11068  16178  16716   1975   1240  -5205       N  
ATOM   4260  CA  GLU A 564      77.766  15.877  49.930  1.00110.69           C  
ANISOU 4260  CA  GLU A 564    10885  15829  15343   2352    833  -4663       C  
ATOM   4261  C   GLU A 564      78.309  14.870  50.941  1.00111.38           C  
ANISOU 4261  C   GLU A 564    10938  16663  14717   2589    360  -5086       C  
ATOM   4262  O   GLU A 564      77.640  13.897  51.279  1.00105.33           O  
ANISOU 4262  O   GLU A 564    10571  16078  13372   2851    -17  -4801       O  
ATOM   4263  CB  GLU A 564      78.612  15.867  48.651  1.00111.93           C  
ANISOU 4263  CB  GLU A 564    11012  15895  15620   2388   1022  -4346       C  
ATOM   4264  N   ALA A 565      79.517  15.134  51.440  1.00118.72           N  
ANISOU 4264  N   ALA A 565    11365  18038  15704   2498    410  -5768       N  
ATOM   4265  CA  ALA A 565      80.141  14.302  52.482  1.00120.29           C  
ANISOU 4265  CA  ALA A 565    11427  19052  15227   2764      4  -6231       C  
ATOM   4266  C   ALA A 565      79.246  14.130  53.731  1.00119.02           C  
ANISOU 4266  C   ALA A 565    11328  19109  14783   2834   -220  -6407       C  
ATOM   4267  O   ALA A 565      79.242  13.066  54.352  1.00116.70           O  
ANISOU 4267  O   ALA A 565    11235  19338  13770   3196   -621  -6339       O  
ATOM   4268  CB  ALA A 565      81.504  14.871  52.873  1.00124.14           C  
ANISOU 4268  CB  ALA A 565    11236  20015  15915   2588    164  -7045       C  
ATOM   4269  N   CYS A 566      78.479  15.158  54.082  1.00119.06           N  
ANISOU 4269  N   CYS A 566    11173  18713  15352   2517     56  -6595       N  
ATOM   4270  CA  CYS A 566      77.610  15.077  55.254  1.00121.49           C  
ANISOU 4270  CA  CYS A 566    11493  19261  15407   2573   -131  -6780       C  
ATOM   4271  C   CYS A 566      76.527  14.017  55.094  1.00116.69           C  
ANISOU 4271  C   CYS A 566    11535  18541  14261   2856   -445  -6009       C  
ATOM   4272  O   CYS A 566      76.462  13.062  55.875  1.00116.86           O  
ANISOU 4272  O   CYS A 566    11694  19102  13604   3158   -808  -5987       O  
ATOM   4273  CB  CYS A 566      76.949  16.423  55.548  1.00125.44           C  
ANISOU 4273  CB  CYS A 566    11716  19281  16665   2190    254  -7111       C  
ATOM   4274  SG  CYS A 566      76.138  16.477  57.167  1.00129.30           S  
ANISOU 4274  SG  CYS A 566    12019  20265  16845   2247     43  -7587       S  
ATOM   4275  N   PHE A 567      75.689  14.189  54.077  1.00113.39           N  
ANISOU 4275  N   PHE A 567    11492  17442  14147   2762   -282  -5377       N  
ATOM   4276  CA  PHE A 567      74.561  13.289  53.843  1.00110.69           C  
ANISOU 4276  CA  PHE A 567    11727  16946  13384   2950   -530  -4689       C  
ATOM   4277  C   PHE A 567      75.007  11.827  53.726  1.00106.18           C  
ANISOU 4277  C   PHE A 567    11509  16744  12092   3316   -921  -4398       C  
ATOM   4278  O   PHE A 567      74.335  10.923  54.236  1.00103.86           O  
ANISOU 4278  O   PHE A 567    11549  16616  11298   3504  -1205  -4123       O  
ATOM   4279  CB  PHE A 567      73.784  13.706  52.586  1.00111.08           C  
ANISOU 4279  CB  PHE A 567    12052  16307  13847   2824   -278  -4090       C  
ATOM   4280  CG  PHE A 567      72.978  14.958  52.765  1.00114.51           C  
ANISOU 4280  CG  PHE A 567    12287  16321  14902   2557     72  -4202       C  
ATOM   4281  CD1 PHE A 567      71.866  14.966  53.588  1.00113.86           C  
ANISOU 4281  CD1 PHE A 567    12287  16298  14676   2546    -38  -4200       C  
ATOM   4282  CD2 PHE A 567      73.338  16.133  52.125  1.00119.55           C  
ANISOU 4282  CD2 PHE A 567    12648  16497  16280   2329    535  -4299       C  
ATOM   4283  CE1 PHE A 567      71.123  16.122  53.771  1.00115.83           C  
ANISOU 4283  CE1 PHE A 567    12349  16169  15491   2341    285  -4326       C  
ATOM   4284  CE2 PHE A 567      72.597  17.292  52.307  1.00121.14           C  
ANISOU 4284  CE2 PHE A 567    12684  16252  17091   2121    889  -4397       C  
ATOM   4285  CZ  PHE A 567      71.486  17.286  53.126  1.00117.88           C  
ANISOU 4285  CZ  PHE A 567    12360  15917  16511   2141    752  -4424       C  
ATOM   4286  N   ALA A 568      76.149  11.609  53.080  1.00102.79           N  
ANISOU 4286  N   ALA A 568    10992  16434  11629   3419   -912  -4466       N  
ATOM   4287  CA  ALA A 568      76.711  10.269  52.937  1.00100.99           C  
ANISOU 4287  CA  ALA A 568    11070  16543  10760   3806  -1254  -4245       C  
ATOM   4288  C   ALA A 568      76.705   9.510  54.259  1.00102.95           C  
ANISOU 4288  C   ALA A 568    11331  17369  10416   4075  -1562  -4431       C  
ATOM   4289  O   ALA A 568      76.197   8.389  54.323  1.00101.04           O  
ANISOU 4289  O   ALA A 568    11568  17118   9706   4327  -1819  -3978       O  
ATOM   4290  CB  ALA A 568      78.126  10.337  52.387  1.00101.45           C  
ANISOU 4290  CB  ALA A 568    10848  16837  10862   3882  -1185  -4512       C  
ATOM   4291  N   VAL A 569      77.256  10.128  55.308  1.00105.38           N  
ANISOU 4291  N   VAL A 569    11095  18190  10755   4022  -1513  -5101       N  
ATOM   4292  CA  VAL A 569      77.415   9.459  56.602  1.00106.63           C  
ANISOU 4292  CA  VAL A 569    11163  19062  10290   4345  -1788  -5314       C  
ATOM   4293  C   VAL A 569      76.226   9.685  57.523  1.00104.12           C  
ANISOU 4293  C   VAL A 569    10869  18750   9943   4236  -1806  -5286       C  
ATOM   4294  O   VAL A 569      75.758   8.764  58.191  1.00100.22           O  
ANISOU 4294  O   VAL A 569    10654  18526   8899   4518  -2047  -4979       O  
ATOM   4295  CB  VAL A 569      78.699   9.922  57.313  1.00112.74           C  
ANISOU 4295  CB  VAL A 569    11263  20583  10989   4406  -1764  -6119       C  
ATOM   4296  CG1 VAL A 569      78.954   9.087  58.564  1.00113.09           C  
ANISOU 4296  CG1 VAL A 569    11223  21482  10265   4864  -2068  -6253       C  
ATOM   4297  CG2 VAL A 569      79.881   9.818  56.354  1.00114.62           C  
ANISOU 4297  CG2 VAL A 569    11419  20827  11306   4467  -1709  -6176       C  
ATOM   4298  N   GLU A 570      75.731  10.913  57.539  1.00106.07           N  
ANISOU 4298  N   GLU A 570    10826  18679  10798   3837  -1526  -5582       N  
ATOM   4299  CA  GLU A 570      74.674  11.303  58.464  1.00107.48           C  
ANISOU 4299  CA  GLU A 570    10919  18929  10989   3724  -1516  -5681       C  
ATOM   4300  C   GLU A 570      73.315  10.726  58.090  1.00105.56           C  
ANISOU 4300  C   GLU A 570    11268  18207  10633   3716  -1597  -4923       C  
ATOM   4301  O   GLU A 570      72.484  10.460  58.963  1.00106.25           O  
ANISOU 4301  O   GLU A 570    11421  18536  10413   3781  -1720  -4825       O  
ATOM   4302  CB  GLU A 570      74.588  12.828  58.523  1.00109.60           C  
ANISOU 4302  CB  GLU A 570    10703  18930  12009   3312  -1157  -6254       C  
ATOM   4303  CG  GLU A 570      75.827  13.495  59.097  1.00114.04           C  
ANISOU 4303  CG  GLU A 570    10582  20026  12722   3242  -1054  -7153       C  
ATOM   4304  CD  GLU A 570      76.109  13.053  60.515  1.00117.43           C  
ANISOU 4304  CD  GLU A 570    10685  21440  12493   3538  -1325  -7604       C  
ATOM   4305  OE1 GLU A 570      75.128  12.870  61.271  1.00116.10           O  
ANISOU 4305  OE1 GLU A 570    10629  21430  12053   3620  -1444  -7449       O  
ATOM   4306  OE2 GLU A 570      77.303  12.880  60.861  1.00119.66           O1-
ANISOU 4306  OE2 GLU A 570    10580  22387  12497   3712  -1414  -8092       O1-
ATOM   4307  N   GLY A 571      73.089  10.536  56.790  1.00106.15           N  
ANISOU 4307  N   GLY A 571    11734  17660  10936   3634  -1521  -4408       N  
ATOM   4308  CA  GLY A 571      71.834   9.949  56.289  1.00102.08           C  
ANISOU 4308  CA  GLY A 571    11756  16716  10313   3606  -1595  -3722       C  
ATOM   4309  C   GLY A 571      71.530   8.594  56.916  1.00100.26           C  
ANISOU 4309  C   GLY A 571    11894  16797   9404   3895  -1912  -3372       C  
ATOM   4310  O   GLY A 571      70.585   8.466  57.702  1.00100.55           O  
ANISOU 4310  O   GLY A 571    11988  16969   9248   3866  -1975  -3254       O  
ATOM   4311  N   PRO A 572      72.356   7.584  56.605  1.00 97.35           N  
ANISOU 4311  N   PRO A 572    11760  16551   8676   4192  -2090  -3205       N  
ATOM   4312  CA  PRO A 572      72.273   6.273  57.246  1.00 97.69           C  
ANISOU 4312  CA  PRO A 572    12141  16875   8100   4527  -2348  -2882       C  
ATOM   4313  C   PRO A 572      72.093   6.353  58.772  1.00101.57           C  
ANISOU 4313  C   PRO A 572    12336  18008   8249   4654  -2420  -3134       C  
ATOM   4314  O   PRO A 572      71.405   5.510  59.347  1.00104.63           O  
ANISOU 4314  O   PRO A 572    13026  18483   8245   4793  -2547  -2729       O  
ATOM   4315  CB  PRO A 572      73.617   5.643  56.914  1.00 98.50           C  
ANISOU 4315  CB  PRO A 572    12268  17197   7959   4868  -2461  -2968       C  
ATOM   4316  CG  PRO A 572      74.050   6.310  55.663  1.00 96.12           C  
ANISOU 4316  CG  PRO A 572    11876  16500   8147   4656  -2288  -3070       C  
ATOM   4317  CD  PRO A 572      73.518   7.698  55.709  1.00 95.23           C  
ANISOU 4317  CD  PRO A 572    11393  16210   8581   4254  -2028  -3359       C  
ATOM   4318  N   LYS A 573      72.706   7.347  59.418  1.00102.44           N  
ANISOU 4318  N   LYS A 573    11836  18582   8504   4605  -2325  -3808       N  
ATOM   4319  CA  LYS A 573      72.407   7.635  60.821  1.00105.93           C  
ANISOU 4319  CA  LYS A 573    11907  19666   8674   4679  -2366  -4133       C  
ATOM   4320  C   LYS A 573      70.890   7.738  61.029  1.00105.30           C  
ANISOU 4320  C   LYS A 573    12045  19290   8676   4446  -2323  -3777       C  
ATOM   4321  O   LYS A 573      70.317   6.983  61.806  1.00105.45           O  
ANISOU 4321  O   LYS A 573    12244  19605   8217   4632  -2459  -3443       O  
ATOM   4322  CB  LYS A 573      73.097   8.924  61.282  1.00107.77           C  
ANISOU 4322  CB  LYS A 573    11421  20287   9242   4519  -2209  -5007       C  
ATOM   4323  N   LEU A 574      70.243   8.641  60.294  1.00105.53           N  
ANISOU 4323  N   LEU A 574    12063  18737   9297   4061  -2119  -3801       N  
ATOM   4324  CA  LEU A 574      68.788   8.846  60.401  1.00106.62           C  
ANISOU 4324  CA  LEU A 574    12363  18610   9538   3835  -2061  -3498       C  
ATOM   4325  C   LEU A 574      67.990   7.544  60.247  1.00106.15           C  
ANISOU 4325  C   LEU A 574    12892  18372   9071   3925  -2226  -2755       C  
ATOM   4326  O   LEU A 574      67.165   7.211  61.113  1.00109.61           O  
ANISOU 4326  O   LEU A 574    13369  19096   9183   3955  -2296  -2565       O  
ATOM   4327  CB  LEU A 574      68.303   9.873  59.363  1.00104.65           C  
ANISOU 4327  CB  LEU A 574    12095  17696   9970   3488  -1805  -3508       C  
ATOM   4328  N   VAL A 575      68.259   6.816  59.160  1.00101.42           N  
ANISOU 4328  N   VAL A 575    12720  17317   8499   3961  -2272  -2370       N  
ATOM   4329  CA  VAL A 575      67.586   5.542  58.861  1.00100.05           C  
ANISOU 4329  CA  VAL A 575    13120  16868   8026   4006  -2400  -1722       C  
ATOM   4330  C   VAL A 575      67.667   4.579  60.049  1.00104.77           C  
ANISOU 4330  C   VAL A 575    13808  17963   8035   4321  -2555  -1538       C  
ATOM   4331  O   VAL A 575      66.648   4.142  60.578  1.00106.51           O  
ANISOU 4331  O   VAL A 575    14203  18219   8048   4244  -2574  -1189       O  
ATOM   4332  CB  VAL A 575      68.177   4.869  57.590  1.00 98.67           C  
ANISOU 4332  CB  VAL A 575    13321  16236   7934   4079  -2444  -1483       C  
ATOM   4333  CG1 VAL A 575      67.600   3.470  57.380  1.00 96.62           C  
ANISOU 4333  CG1 VAL A 575    13638  15695   7379   4139  -2569   -908       C  
ATOM   4334  CG2 VAL A 575      67.925   5.725  56.349  1.00 91.86           C  
ANISOU 4334  CG2 VAL A 575    12406  14901   7597   3793  -2273  -1525       C  
ATOM   4335  N   VAL A 576      68.885   4.282  60.481  1.00108.86           N  
ANISOU 4335  N   VAL A 576    14174  18915   8273   4692  -2645  -1762       N  
ATOM   4336  CA  VAL A 576      69.120   3.437  61.654  1.00114.17           C  
ANISOU 4336  CA  VAL A 576    14865  20170   8343   5094  -2768  -1589       C  
ATOM   4337  C   VAL A 576      68.429   3.941  62.931  1.00115.45           C  
ANISOU 4337  C   VAL A 576    14652  20920   8294   5064  -2744  -1749       C  
ATOM   4338  O   VAL A 576      67.866   3.159  63.702  1.00114.56           O  
ANISOU 4338  O   VAL A 576    14727  21040   7760   5225  -2791  -1313       O  
ATOM   4339  CB  VAL A 576      70.626   3.329  61.918  1.00118.41           C  
ANISOU 4339  CB  VAL A 576    15138  21226   8626   5519  -2852  -1949       C  
ATOM   4340  CG1 VAL A 576      70.885   2.600  63.228  1.00123.23           C  
ANISOU 4340  CG1 VAL A 576    15669  22587   8566   6006  -2958  -1795       C  
ATOM   4341  CG2 VAL A 576      71.315   2.632  60.745  1.00117.95           C  
ANISOU 4341  CG2 VAL A 576    15488  20655   8671   5633  -2898  -1727       C  
ATOM   4342  N   SER A 577      68.470   5.253  63.138  1.00117.11           N  
ANISOU 4342  N   SER A 577    14324  21353   8817   4857  -2649  -2374       N  
ATOM   4343  CA  SER A 577      67.848   5.882  64.295  1.00117.91           C  
ANISOU 4343  CA  SER A 577    14000  22033   8768   4818  -2621  -2654       C  
ATOM   4344  C   SER A 577      66.325   5.739  64.259  1.00114.48           C  
ANISOU 4344  C   SER A 577    13853  21254   8391   4529  -2570  -2174       C  
ATOM   4345  O   SER A 577      65.699   5.217  65.177  1.00111.71           O  
ANISOU 4345  O   SER A 577    13533  21308   7602   4654  -2619  -1870       O  
ATOM   4346  CB  SER A 577      68.223   7.360  64.325  1.00119.36           C  
ANISOU 4346  CB  SER A 577    13586  22349   9416   4606  -2491  -3474       C  
ATOM   4347  OG  SER A 577      67.653   7.992  65.459  1.00126.99           O  
ANISOU 4347  OG  SER A 577    14106  23904  10241   4589  -2469  -3830       O  
ATOM   4348  N   THR A 578      65.738   6.198  63.169  1.00112.67           N  
ANISOU 4348  N   THR A 578    13812  20313   8683   4155  -2460  -2090       N  
ATOM   4349  CA  THR A 578      64.300   6.120  62.995  1.00112.75           C  
ANISOU 4349  CA  THR A 578    14060  20010   8770   3862  -2407  -1680       C  
ATOM   4350  C   THR A 578      63.758   4.698  63.087  1.00111.82           C  
ANISOU 4350  C   THR A 578    14460  19772   8252   3930  -2496   -965       C  
ATOM   4351  O   THR A 578      62.730   4.469  63.719  1.00118.09           O  
ANISOU 4351  O   THR A 578    15283  20760   8825   3832  -2483   -685       O  
ATOM   4352  CB  THR A 578      63.900   6.759  61.664  1.00111.93           C  
ANISOU 4352  CB  THR A 578    14083  19198   9249   3527  -2275  -1672       C  
ATOM   4353  CG2 THR A 578      62.484   6.352  61.236  1.00112.06           C  
ANISOU 4353  CG2 THR A 578    14443  18865   9270   3256  -2252  -1148       C  
ATOM   4354  OG1 THR A 578      63.984   8.180  61.820  1.00114.29           O  
ANISOU 4354  OG1 THR A 578    13883  19594   9949   3411  -2126  -2266       O  
ATOM   4355  N   GLN A 579      64.440   3.744  62.473  1.00107.27           N  
ANISOU 4355  N   GLN A 579    14285  18870   7603   4092  -2565   -679       N  
ATOM   4356  CA  GLN A 579      63.980   2.365  62.537  1.00108.32           C  
ANISOU 4356  CA  GLN A 579    14936  18787   7435   4150  -2608    -20       C  
ATOM   4357  C   GLN A 579      63.842   1.879  63.973  1.00112.52           C  
ANISOU 4357  C   GLN A 579    15349  19982   7421   4434  -2634    189       C  
ATOM   4358  O   GLN A 579      62.820   1.294  64.331  1.00109.99           O  
ANISOU 4358  O   GLN A 579    15247  19607   6936   4288  -2587    662       O  
ATOM   4359  CB  GLN A 579      64.912   1.450  61.752  1.00109.36           C  
ANISOU 4359  CB  GLN A 579    15473  18511   7567   4366  -2674    167       C  
ATOM   4360  CG  GLN A 579      64.665   1.478  60.252  1.00106.37           C  
ANISOU 4360  CG  GLN A 579    15380  17403   7632   4053  -2644    216       C  
ATOM   4361  CD  GLN A 579      65.468   0.428  59.526  1.00106.69           C  
ANISOU 4361  CD  GLN A 579    15854  17053   7630   4278  -2716    427       C  
ATOM   4362  NE2 GLN A 579      64.788  -0.412  58.758  1.00107.78           N  
ANISOU 4362  NE2 GLN A 579    16461  16608   7881   4059  -2702    803       N  
ATOM   4363  OE1 GLN A 579      66.687   0.371  59.658  1.00107.09           O  
ANISOU 4363  OE1 GLN A 579    15795  17351   7545   4647  -2781    216       O  
ATOM   4364  N   THR A 580      64.876   2.124  64.779  1.00117.78           N  
ANISOU 4364  N   THR A 580    15638  21322   7792   4844  -2697   -165       N  
ATOM   4365  CA  THR A 580      64.875   1.773  66.204  1.00125.80           C  
ANISOU 4365  CA  THR A 580    16431  23150   8217   5207  -2723    -22       C  
ATOM   4366  C   THR A 580      63.742   2.472  66.943  1.00129.26           C  
ANISOU 4366  C   THR A 580    16530  23973   8609   4963  -2663   -127       C  
ATOM   4367  O   THR A 580      63.028   1.849  67.741  1.00127.88           O  
ANISOU 4367  O   THR A 580    16449  24093   8048   5037  -2630    354       O  
ATOM   4368  CB  THR A 580      66.192   2.192  66.885  1.00130.18           C  
ANISOU 4368  CB  THR A 580    16481  24500   8484   5663  -2808   -577       C  
ATOM   4369  CG2 THR A 580      66.301   1.629  68.322  1.00134.81           C  
ANISOU 4369  CG2 THR A 580    16865  26012   8344   6162  -2842   -336       C  
ATOM   4370  OG1 THR A 580      67.294   1.738  66.095  1.00131.58           O  
ANISOU 4370  OG1 THR A 580    16899  24341   8753   5866  -2864   -591       O  
ATOM   4371  N   ALA A 581      63.582   3.765  66.651  1.00129.21           N  
ANISOU 4371  N   ALA A 581    16137  23939   9019   4680  -2628   -739       N  
ATOM   4372  CA  ALA A 581      62.564   4.599  67.290  1.00129.24           C  
ANISOU 4372  CA  ALA A 581    15767  24301   9038   4467  -2568   -959       C  
ATOM   4373  C   ALA A 581      61.159   4.047  67.071  1.00127.63           C  
ANISOU 4373  C   ALA A 581    15944  23712   8839   4143  -2504   -331       C  
ATOM   4374  O   ALA A 581      60.369   3.983  68.006  1.00129.30           O  
ANISOU 4374  O   ALA A 581    15985  24434   8711   4157  -2481   -159       O  
ATOM   4375  CB  ALA A 581      62.650   6.026  66.766  1.00125.26           C  
ANISOU 4375  CB  ALA A 581    14893  23594   9107   4208  -2495  -1662       C  
ATOM   4376  N   LEU A 582      60.871   3.630  65.838  1.00125.87           N  
ANISOU 4376  N   LEU A 582    16203  22649   8975   3858  -2472    -13       N  
ATOM   4377  CA  LEU A 582      59.544   3.119  65.465  1.00124.39           C  
ANISOU 4377  CA  LEU A 582    16355  22063   8844   3488  -2405    507       C  
ATOM   4378  C   LEU A 582      59.341   1.638  65.827  1.00126.74           C  
ANISOU 4378  C   LEU A 582    17102  22284   8771   3585  -2393   1220       C  
ATOM   4379  O   LEU A 582      58.262   1.091  65.613  1.00124.48           O  
ANISOU 4379  O   LEU A 582    17089  21697   8511   3257  -2319   1658       O  
ATOM   4380  CB  LEU A 582      59.304   3.335  63.960  1.00118.20           C  
ANISOU 4380  CB  LEU A 582    15835  20488   8586   3148  -2371    486       C  
ATOM   4381  N   ALA A 583      60.378   0.993  66.363  1.00131.59           N  
ANISOU 4381  N   ALA A 583    17782  23162   9054   4039  -2444   1336       N  
ATOM   4382  CA  ALA A 583      60.294  -0.404  66.797  1.00136.03           C  
ANISOU 4382  CA  ALA A 583    18771  23642   9273   4219  -2388   2050       C  
ATOM   4383  C   ALA A 583      59.691  -1.279  65.700  1.00135.06           C  
ANISOU 4383  C   ALA A 583    19247  22579   9489   3828  -2318   2481       C  
ATOM   4384  O   ALA A 583      59.807  -2.499  65.737  1.00139.54           O  
ANISOU 4384  O   ALA A 583    20271  22809   9937   3950  -2250   3024       O  
ATOM   4385  CB  ALA A 583      59.487  -0.520  68.091  1.00137.42           C  
ANISOU 4385  CB  ALA A 583    18713  24506   8994   4281  -2312   2357       C  
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.