CNRS Nantes University UFIP UFIP
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***  3udi_protein  ***

elNémo ID: 22050909451747517

Job options:

ID        	=	 22050909451747517
JOBID     	=	 3udi_protein
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 3udi_protein

ATOM      1  N   LYS A  27      25.147  42.284 -15.571  1.00 76.32           N
ANISOU    1  N   LYS A  27    10711   6964  11324    607   -636   -931       N
ATOM      2  CA  LYS A  27      25.897  41.113 -16.050  1.00 76.47           C
ANISOU    2  CA  LYS A  27    10790   6930  11333    607   -630   -961       C
ATOM      3  C   LYS A  27      26.361  40.205 -14.865  1.00 77.39           C
ANISOU    3  C   LYS A  27    10776   7086  11542    566   -592   -933       C
ATOM      4  O   LYS A  27      27.463  40.417 -14.326  1.00 75.61           O
ANISOU    4  O   LYS A  27    10525   6885  11318    561   -489   -931       O
ATOM      5  CB  LYS A  27      27.056  41.522 -17.005  1.00 79.52           C
ANISOU    5  CB  LYS A  27    11330   7266  11617    646   -525  -1000       C
ATOM      6  CG  LYS A  27      27.862  42.777 -16.583  1.00 84.79           C
ANISOU    6  CG  LYS A  27    11972   7977  12269    654   -389   -991       C
ATOM      7  CD  LYS A  27      29.028  43.099 -17.544  1.00 84.03           C
ANISOU    7  CD  LYS A  27    12014   7805  12108    695   -259  -1025       C
ATOM      8  CE  LYS A  27      30.108  43.950 -16.912  1.00 82.76           C
ANISOU    8  CE  LYS A  27    11779   7670  11995    691   -121  -1018       C
ATOM      9  NZ  LYS A  27      29.700  45.386 -16.778  1.00 83.97           N
ANISOU    9  NZ  LYS A  27    11934   7866  12106    708    -99  -1007       N
ATOM     10  N   PRO A  28      25.537  39.214 -14.393  1.00 72.65           N
ANISOU   10  N   PRO A  28    10088   6482  11033    538   -675   -910       N
ATOM     11  CA  PRO A  28      25.978  38.446 -13.224  1.00 70.26           C
ANISOU   11  CA  PRO A  28     9679   6212  10802    508   -630   -878       C
ATOM     12  C   PRO A  28      26.875  37.267 -13.524  1.00 68.24           C
ANISOU   12  C   PRO A  28     9455   5915  10556    502   -617   -902       C
ATOM     13  O   PRO A  28      26.930  36.799 -14.673  1.00 67.55           O
ANISOU   13  O   PRO A  28     9472   5765  10430    517   -656   -943       O
ATOM     14  CB  PRO A  28      24.655  37.977 -12.601  1.00 72.37           C
ANISOU   14  CB  PRO A  28     9843   6480  11174    487   -700   -836       C
ATOM     15  CG  PRO A  28      23.760  37.760 -13.747  1.00 78.23           C
ANISOU   15  CG  PRO A  28    10638   7158  11929    499   -821   -866       C
ATOM     16  CD  PRO A  28      24.194  38.753 -14.835  1.00 74.77           C
ANISOU   16  CD  PRO A  28    10341   6705  11361    536   -812   -909       C
ATOM     17  N   LEU A  29      27.554  36.767 -12.471  1.00 61.02           N
ANISOU   17  N   LEU A  29     8463   5030   9691    482   -565   -877       N
ATOM     18  CA  LEU A  29      28.354  35.545 -12.534  1.00 59.06           C
ANISOU   18  CA  LEU A  29     8215   4745   9479    471   -554   -890       C
ATOM     19  C   LEU A  29      27.353  34.418 -12.863  1.00 62.48           C
ANISOU   19  C   LEU A  29     8633   5140   9966    457   -648   -888       C
ATOM     20  O   LEU A  29      26.317  34.279 -12.211  1.00 60.89           O
ANISOU   20  O   LEU A  29     8349   4956   9831    443   -691   -850       O
ATOM     21  CB  LEU A  29      29.043  35.292 -11.175  1.00 57.77           C
ANISOU   21  CB  LEU A  29     7965   4619   9366    457   -510   -856       C
ATOM     22  CG  LEU A  29      30.253  34.324 -11.092  1.00 60.33           C
ANISOU   22  CG  LEU A  29     8281   4907   9734    450   -479   -869       C
ATOM     23  CD1 LEU A  29      29.847  32.922 -10.902  1.00 58.76           C
ANISOU   23  CD1 LEU A  29     8043   4688   9594    430   -525   -852       C
ATOM     24  CD2 LEU A  29      31.250  34.489 -12.229  1.00 61.78           C
ANISOU   24  CD2 LEU A  29     8547   5032   9894    465   -419   -917       C
ATOM     25  N   GLN A  30      27.607  33.719 -13.956  1.00 61.17           N
ANISOU   25  N   GLN A  30     8556   4908   9776    465   -679   -931       N
ATOM     26  CA  GLN A  30      26.752  32.633 -14.407  1.00 62.53           C
ANISOU   26  CA  GLN A  30     8727   5028  10003    454   -784   -941       C
ATOM     27  C   GLN A  30      27.448  31.269 -14.243  1.00 65.92           C
ANISOU   27  C   GLN A  30     9135   5428  10482    436   -761   -943       C
ATOM     28  O   GLN A  30      28.616  31.094 -14.614  1.00 64.61           O
ANISOU   28  O   GLN A  30     9034   5238  10276    445   -687   -967       O
ATOM     29  CB  GLN A  30      26.307  32.871 -15.845  1.00 65.00           C
ANISOU   29  CB  GLN A  30     9186   5272  10240    485   -867   -992       C
ATOM     30  CG  GLN A  30      25.254  33.957 -15.976  1.00 82.24           C
ANISOU   30  CG  GLN A  30    11364   7470  12413    498   -937   -985       C
ATOM     31  CD  GLN A  30      24.669  33.984 -17.360  1.00113.86           C
ANISOU   31  CD  GLN A  30    15518  11388  16356    532  -1062  -1037       C
ATOM     32  OE1 GLN A  30      25.389  33.977 -18.366  1.00112.53           O
ANISOU   32  OE1 GLN A  30    15522  11164  16071    565  -1035  -1081       O
ATOM     33  NE2 GLN A  30      23.345  33.993 -17.447  1.00107.72           N
ANISOU   33  NE2 GLN A  30    14686  10581  15662    528  -1204  -1034       N
ATOM     34  N   VAL A  31      26.717  30.319 -13.655  1.00 63.67           N
ANISOU   34  N   VAL A  31     8751   5140  10302    411   -815   -915       N
ATOM     35  CA  VAL A  31      27.172  28.945 -13.399  1.00 63.48           C
ANISOU   35  CA  VAL A  31     8689   5088  10341    392   -803   -910       C
ATOM     36  C   VAL A  31      26.394  27.967 -14.288  1.00 67.04           C
ANISOU   36  C   VAL A  31     9171   5460  10839    387   -916   -943       C
ATOM     37  O   VAL A  31      25.156  27.921 -14.242  1.00 66.49           O
ANISOU   37  O   VAL A  31     9041   5372  10852    380  -1006   -932       O
ATOM     38  CB  VAL A  31      27.056  28.576 -11.893  1.00 66.70           C
ANISOU   38  CB  VAL A  31     8966   5543  10832    373   -759   -846       C
ATOM     39  CG1 VAL A  31      27.655  27.197 -11.619  1.00 66.10           C
ANISOU   39  CG1 VAL A  31     8861   5439  10814    358   -741   -840       C
ATOM     40  CG2 VAL A  31      27.701  29.650 -11.004  1.00 65.72           C
ANISOU   40  CG2 VAL A  31     8830   5485  10654    385   -679   -819       C
ATOM     41  N   TYR A  32      27.132  27.205 -15.109  1.00 64.64           N
ANISOU   41  N   TYR A  32     8964   5100  10497    393   -910   -985       N
ATOM     42  CA  TYR A  32      26.591  26.183 -16.029  1.00 65.23           C
ANISOU   42  CA  TYR A  32     9098   5086  10600    392  -1020  -1027       C
ATOM     43  C   TYR A  32      27.085  24.776 -15.668  1.00 68.03           C
ANISOU   43  C   TYR A  32     9396   5419  11031    368   -988  -1017       C
ATOM     44  O   TYR A  32      28.141  24.631 -15.073  1.00 66.98           O
ANISOU   44  O   TYR A  32     9235   5321  10892    361   -876   -995       O
ATOM     45  CB  TYR A  32      27.025  26.493 -17.477  1.00 67.54           C
ANISOU   45  CB  TYR A  32     9602   5307  10753    431  -1037  -1091       C
ATOM     46  CG  TYR A  32      26.424  27.765 -18.049  1.00 70.41           C
ANISOU   46  CG  TYR A  32    10051   5670  11033    463  -1094  -1109       C
ATOM     47  CD1 TYR A  32      25.278  27.726 -18.836  1.00 73.05           C
ANISOU   47  CD1 TYR A  32    10447   5934  11373    479  -1267  -1145       C
ATOM     48  CD2 TYR A  32      27.002  29.014 -17.801  1.00 71.29           C
ANISOU   48  CD2 TYR A  32    10176   5842  11070    478   -984  -1091       C
ATOM     49  CE1 TYR A  32      24.712  28.893 -19.356  1.00 72.81           C
ANISOU   49  CE1 TYR A  32    10497   5898  11270    512  -1331  -1160       C
ATOM     50  CE2 TYR A  32      26.442  30.190 -18.315  1.00 72.57           C
ANISOU   50  CE2 TYR A  32    10415   6004  11155    508  -1032  -1105       C
ATOM     51  CZ  TYR A  32      25.293  30.124 -19.086  1.00 81.44           C
ANISOU   51  CZ  TYR A  32    11603   7060  12278    526  -1205  -1137       C
ATOM     52  OH  TYR A  32      24.743  31.276 -19.607  1.00 83.68           O
ANISOU   52  OH  TYR A  32    11969   7338  12490    559  -1262  -1150       O
ATOM     53  N   THR A  33      26.372  23.731 -16.078  1.00 65.48           N
ANISOU   53  N   THR A  33     9062   5029  10788    356  -1093  -1038       N
ATOM     54  CA  THR A  33      26.856  22.351 -15.854  1.00 64.09           C
ANISOU   54  CA  THR A  33     8847   4825  10681    334  -1062  -1033       C
ATOM     55  C   THR A  33      27.674  21.931 -17.084  1.00 68.26           C
ANISOU   55  C   THR A  33     9553   5277  11107    355  -1050  -1093       C
ATOM     56  O   THR A  33      27.806  22.713 -18.042  1.00 66.28           O
ANISOU   56  O   THR A  33     9460   4993  10732    390  -1062  -1134       O
ATOM     57  CB  THR A  33      25.693  21.386 -15.645  1.00 65.98           C
ANISOU   57  CB  THR A  33     8979   5017  11074    312  -1169  -1025       C
ATOM     58  OG1 THR A  33      24.830  21.500 -16.772  1.00 72.30           O
ANISOU   58  OG1 THR A  33     9871   5735  11865    328  -1326  -1084       O
ATOM     59  CG2 THR A  33      24.949  21.626 -14.356  1.00 57.34           C
ANISOU   59  CG2 THR A  33     7713   3976  10098    295  -1139   -955       C
ATOM     60  N   ALA A  34      28.187  20.678 -17.071  1.00 67.80           N
ANISOU   60  N   ALA A  34     9482   5179  11100    339  -1021  -1097       N
ATOM     61  CA  ALA A  34      28.949  20.107 -18.175  1.00 69.13           C
ANISOU   61  CA  ALA A  34     9819   5259  11187    358   -992  -1149       C
ATOM     62  C   ALA A  34      28.105  19.998 -19.464  1.00 78.26           C
ANISOU   62  C   ALA A  34    11143   6315  12278    386  -1144  -1217       C
ATOM     63  O   ALA A  34      28.679  20.019 -20.555  1.00 79.07           O
ANISOU   63  O   ALA A  34    11453   6337  12254    423  -1113  -1264       O
ATOM     64  CB  ALA A  34      29.557  18.777 -17.770  1.00 69.42           C
ANISOU   64  CB  ALA A  34     9785   5279  11314    331   -934  -1132       C
ATOM     65  N   ASP A  35      26.750  20.026 -19.352  1.00 77.34           N
ANISOU   65  N   ASP A  35    10949   6190  12245    377  -1307  -1221       N
ATOM     66  CA  ASP A  35      25.819  20.014 -20.494  1.00 79.18           C
ANISOU   66  CA  ASP A  35    11327   6319  12440    406  -1498  -1288       C
ATOM     67  C   ASP A  35      25.379  21.422 -20.920  1.00 85.72           C
ANISOU   67  C   ASP A  35    12247   7157  13166    442  -1553  -1301       C
ATOM     68  O   ASP A  35      24.325  21.589 -21.550  1.00 88.13           O
ANISOU   68  O   ASP A  35    12617   7388  13479    463  -1743  -1344       O
ATOM     69  CB  ASP A  35      24.606  19.127 -20.213  1.00 82.14           C
ANISOU   69  CB  ASP A  35    11555   6649  13006    375  -1661  -1291       C
ATOM     70  CG  ASP A  35      24.087  19.207 -18.800  1.00 94.45           C
ANISOU   70  CG  ASP A  35    12854   8297  14736    335  -1610  -1215       C
ATOM     71  OD1 ASP A  35      24.667  18.512 -17.908  1.00 95.09           O
ANISOU   71  OD1 ASP A  35    12818   8430  14883    306  -1482  -1165       O
ATOM     72  OD2 ASP A  35      23.088  19.929 -18.579  1.00 98.32           O
ANISOU   72  OD2 ASP A  35    13266   8794  15298    337  -1696  -1202       O
ATOM     73  N   ASN A  36      26.205  22.437 -20.578  1.00 80.29           N
ANISOU   73  N   ASN A  36    11563   6553  12391    451  -1392  -1267       N
ATOM     74  CA  ASN A  36      26.020  23.859 -20.868  1.00 78.83           C
ANISOU   74  CA  ASN A  36    11458   6393  12102    485  -1397  -1270       C
ATOM     75  C   ASN A  36      24.698  24.431 -20.349  1.00 79.43           C
ANISOU   75  C   ASN A  36    11389   6503  12289    470  -1531  -1248       C
ATOM     76  O   ASN A  36      24.239  25.458 -20.847  1.00 78.54           O
ANISOU   76  O   ASN A  36    11365   6376  12100    503  -1600  -1267       O
ATOM     77  CB  ASN A  36      26.271  24.174 -22.351  1.00 81.49           C
ANISOU   77  CB  ASN A  36    12095   6620  12249    548  -1431  -1336       C
ATOM     78  CG  ASN A  36      27.646  23.785 -22.837  1.00104.87           C
ANISOU   78  CG  ASN A  36    15201   9536  15111    568  -1253  -1348       C
ATOM     79  OD1 ASN A  36      27.923  22.607 -23.091  1.00107.68           O
ANISOU   79  OD1 ASN A  36    15584   9831  15499    557  -1254  -1367       O
ATOM     80  ND2 ASN A  36      28.527  24.764 -23.007  1.00 89.53           N
ANISOU   80  ND2 ASN A  36    13352   7607  13060    599  -1089  -1337       N
ATOM     81  N   GLN A  37      24.114  23.788 -19.316  1.00 74.36           N
ANISOU   81  N   GLN A  37    10522   5899  11834    424  -1547  -1204       N
ATOM     82  CA  GLN A  37      22.867  24.234 -18.696  1.00 73.85           C
ANISOU   82  CA  GLN A  37    10294   5852  11914    407  -1637  -1171       C
ATOM     83  C   GLN A  37      23.073  25.173 -17.487  1.00 74.30           C
ANISOU   83  C   GLN A  37    10219   6030  11982    392  -1487  -1100       C
ATOM     84  O   GLN A  37      23.877  24.895 -16.591  1.00 72.60           O
ANISOU   84  O   GLN A  37     9930   5883  11770    372  -1340  -1056       O
ATOM     85  CB  GLN A  37      21.901  23.072 -18.420  1.00 75.84           C
ANISOU   85  CB  GLN A  37    10398   6038  12381    376  -1750  -1168       C
ATOM     86  CG  GLN A  37      21.332  22.430 -19.701  1.00 99.68           C
ANISOU   86  CG  GLN A  37    13547   8918  15411    397  -1965  -1250       C
ATOM     87  CD  GLN A  37      20.718  23.394 -20.705  1.00123.76           C
ANISOU   87  CD  GLN A  37    16752  11904  18369    443  -2128  -1302       C
ATOM     88  OE1 GLN A  37      21.210  23.550 -21.833  1.00120.25           O
ANISOU   88  OE1 GLN A  37    16557  11404  17730    489  -2168  -1361       O
ATOM     89  NE2 GLN A  37      19.611  24.036 -20.336  1.00116.59           N
ANISOU   89  NE2 GLN A  37    15708  10990  17601    437  -2221  -1280       N
ATOM     90  N   LEU A  38      22.319  26.282 -17.473  1.00 68.32           N
ANISOU   90  N   LEU A  38     9438   5288  11231    405  -1538  -1089       N
ATOM     91  CA  LEU A  38      22.468  27.330 -16.476  1.00 66.56           C
ANISOU   91  CA  LEU A  38     9127   5169  10996    399  -1410  -1030       C
ATOM     92  C   LEU A  38      21.772  26.927 -15.202  1.00 71.83           C
ANISOU   92  C   LEU A  38     9587   5858  11848    366  -1368   -963       C
ATOM     93  O   LEU A  38      20.589  26.612 -15.241  1.00 73.70           O
ANISOU   93  O   LEU A  38     9729   6025  12248    356  -1478   -961       O
ATOM     94  CB  LEU A  38      21.939  28.676 -17.029  1.00 66.43           C
ANISOU   94  CB  LEU A  38     9181   5152  10909    429  -1475  -1047       C
ATOM     95  CG  LEU A  38      22.030  29.930 -16.134  1.00 67.68           C
ANISOU   95  CG  LEU A  38     9268   5408  11039    428  -1354   -994       C
ATOM     96  CD1 LEU A  38      23.458  30.394 -15.964  1.00 66.25           C
ANISOU   96  CD1 LEU A  38     9168   5298  10705    438  -1199   -991       C
ATOM     97  CD2 LEU A  38      21.212  31.043 -16.701  1.00 67.56           C
ANISOU   97  CD2 LEU A  38     9294   5371  11004    453  -1451  -1009       C
ATOM     98  N   ILE A  39      22.513  26.873 -14.083  1.00 66.54           N
ANISOU   98  N   ILE A  39     8853   5267  11162    352  -1211   -910       N
ATOM     99  CA  ILE A  39      21.954  26.449 -12.785  1.00 64.76           C
ANISOU   99  CA  ILE A  39     8466   5054  11087    331  -1140   -838       C
ATOM    100  C   ILE A  39      21.902  27.565 -11.776  1.00 65.89           C
ANISOU  100  C   ILE A  39     8565   5272  11200    338  -1032   -782       C
ATOM    101  O   ILE A  39      21.036  27.553 -10.897  1.00 65.94           O
ANISOU  101  O   ILE A  39     8455   5261  11337    332   -988   -724       O
ATOM    102  CB  ILE A  39      22.604  25.149 -12.207  1.00 66.87           C
ANISOU  102  CB  ILE A  39     8696   5320  11394    313  -1072   -818       C
ATOM    103  CG1 ILE A  39      24.125  25.310 -12.004  1.00 65.90           C
ANISOU  103  CG1 ILE A  39     8655   5266  11117    321   -969   -821       C
ATOM    104  CG2 ILE A  39      22.278  23.956 -13.079  1.00 67.39           C
ANISOU  104  CG2 ILE A  39     8772   5294  11540    302  -1188   -866       C
ATOM    105  CD1 ILE A  39      24.766  24.303 -11.088  1.00 69.04           C
ANISOU  105  CD1 ILE A  39     9000   5678  11556    309   -885   -780       C
ATOM    106  N   ALA A  40      22.839  28.533 -11.887  1.00 60.74           N
ANISOU  106  N   ALA A  40     8008   4689  10382    355   -977   -796       N
ATOM    107  CA  ALA A  40      22.915  29.664 -10.956  1.00 58.50           C
ANISOU  107  CA  ALA A  40     7701   4475  10050    365   -880   -750       C
ATOM    108  C   ALA A  40      23.382  30.965 -11.586  1.00 60.91           C
ANISOU  108  C   ALA A  40     8106   4822  10216    385   -881   -785       C
ATOM    109  O   ALA A  40      24.240  30.943 -12.472  1.00 61.49           O
ANISOU  109  O   ALA A  40     8285   4889  10190    395   -896   -837       O
ATOM    110  CB  ALA A  40      23.819  29.297  -9.789  1.00 58.31           C
ANISOU  110  CB  ALA A  40     7662   4498   9996    363   -768   -709       C
ATOM    111  N   GLU A  41      22.825  32.097 -11.115  1.00 55.89           N
ANISOU  111  N   GLU A  41     7438   4220   9578    394   -850   -754       N
ATOM    112  CA  GLU A  41      23.200  33.481 -11.478  1.00 53.64           C
ANISOU  112  CA  GLU A  41     7228   3981   9170    414   -829   -774       C
ATOM    113  C   GLU A  41      23.446  34.189 -10.184  1.00 54.61           C
ANISOU  113  C   GLU A  41     7312   4168   9270    417   -718   -722       C
ATOM    114  O   GLU A  41      22.630  34.081  -9.254  1.00 50.61           O
ANISOU  114  O   GLU A  41     6722   3653   8856    411   -681   -666       O
ATOM    115  CB  GLU A  41      22.142  34.225 -12.303  1.00 55.07           C
ANISOU  115  CB  GLU A  41     7424   4127   9373    426   -925   -794       C
ATOM    116  CG  GLU A  41      22.115  33.793 -13.758  1.00 68.53           C
ANISOU  116  CG  GLU A  41     9234   5763  11043    439  -1050   -861       C
ATOM    117  CD  GLU A  41      21.466  34.740 -14.752  1.00107.76           C
ANISOU  117  CD  GLU A  41    14281  10699  15966    467  -1150   -894       C
ATOM    118  OE1 GLU A  41      20.215  34.750 -14.844  1.00125.01           O
ANISOU  118  OE1 GLU A  41    16390  12829  18278    463  -1257   -885       O
ATOM    119  OE2 GLU A  41      22.217  35.411 -15.499  1.00 99.11           O
ANISOU  119  OE2 GLU A  41    13325   9615  14717    495  -1124   -931       O
ATOM    120  N   TYR A  42      24.624  34.830 -10.094  1.00 53.41           N
ANISOU  120  N   TYR A  42     7224   4064   9004    428   -659   -740       N
ATOM    121  CA  TYR A  42      25.060  35.531  -8.901  1.00 53.97           C
ANISOU  121  CA  TYR A  42     7283   4190   9036    436   -574   -704       C
ATOM    122  C   TYR A  42      25.331  36.988  -9.181  1.00 61.21           C
ANISOU  122  C   TYR A  42     8247   5144   9865    453   -550   -724       C
ATOM    123  O   TYR A  42      26.371  37.325  -9.762  1.00 61.59           O
ANISOU  123  O   TYR A  42     8357   5199   9846    462   -534   -766       O
ATOM    124  CB  TYR A  42      26.265  34.839  -8.272  1.00 54.39           C
ANISOU  124  CB  TYR A  42     7345   4250   9071    435   -539   -703       C
ATOM    125  CG  TYR A  42      25.903  33.536  -7.599  1.00 57.71           C
ANISOU  125  CG  TYR A  42     7713   4639   9574    424   -540   -665       C
ATOM    126  CD1 TYR A  42      25.364  33.520  -6.315  1.00 60.42           C
ANISOU  126  CD1 TYR A  42     8027   4984   9946    433   -485   -602       C
ATOM    127  CD2 TYR A  42      26.140  32.311  -8.228  1.00 58.55           C
ANISOU  127  CD2 TYR A  42     7814   4704   9726    409   -581   -690       C
ATOM    128  CE1 TYR A  42      25.031  32.326  -5.687  1.00 61.73           C
ANISOU  128  CE1 TYR A  42     8155   5109  10189    429   -467   -562       C
ATOM    129  CE2 TYR A  42      25.820  31.108  -7.603  1.00 59.48           C
ANISOU  129  CE2 TYR A  42     7882   4790   9927    399   -575   -654       C
ATOM    130  CZ  TYR A  42      25.242  31.125  -6.341  1.00 66.33           C
ANISOU  130  CZ  TYR A  42     8716   5658  10827    410   -515   -588       C
ATOM    131  OH  TYR A  42      24.921  29.961  -5.698  1.00 65.71           O
ANISOU  131  OH  TYR A  42     8598   5538  10832    407   -490   -547       O
ATOM    132  N   GLY A  43      24.369  37.830  -8.795  1.00 58.30           N
ANISOU  132  N   GLY A  43     7848   4791   9513    458   -536   -691       N
ATOM    133  CA  GLY A  43      24.443  39.270  -8.995  1.00 58.50           C
ANISOU  133  CA  GLY A  43     7910   4852   9464    474   -510   -703       C
ATOM    134  C   GLY A  43      25.348  39.934  -7.989  1.00 63.42           C
ANISOU  134  C   GLY A  43     8550   5520  10026    484   -437   -691       C
ATOM    135  O   GLY A  43      25.201  39.707  -6.782  1.00 64.50           O
ANISOU  135  O   GLY A  43     8663   5661  10181    486   -399   -645       O
ATOM    136  N   GLY A  44      26.288  40.729  -8.493  1.00 58.49           N
ANISOU  136  N   GLY A  44     7977   4913   9335    495   -418   -733       N
ATOM    137  CA  GLY A  44      27.225  41.477  -7.667  1.00 57.53           C
ANISOU  137  CA  GLY A  44     7867   4819   9171    506   -370   -735       C
ATOM    138  C   GLY A  44      26.846  42.941  -7.575  1.00 58.92           C
ANISOU  138  C   GLY A  44     8057   5030   9302    519   -336   -729       C
ATOM    139  O   GLY A  44      25.691  43.261  -7.267  1.00 59.54           O
ANISOU  139  O   GLY A  44     8113   5117   9394    519   -329   -690       O
ATOM    140  N   LYS A  45      27.807  43.836  -7.886  1.00 51.90           N
ANISOU  140  N   LYS A  45     7196   4148   8374    531   -305   -767       N
ATOM    141  CA  LYS A  45      27.649  45.298  -7.882  1.00 49.50           C
ANISOU  141  CA  LYS A  45     6908   3873   8026    545   -266   -769       C
ATOM    142  C   LYS A  45      26.663  45.717  -8.962  1.00 54.47           C
ANISOU  142  C   LYS A  45     7558   4501   8638    550   -279   -771       C
ATOM    143  O   LYS A  45      26.814  45.338 -10.126  1.00 56.43           O
ANISOU  143  O   LYS A  45     7846   4715   8878    554   -302   -803       O
ATOM    144  CB  LYS A  45      29.002  46.006  -8.062  1.00 48.71           C
ANISOU  144  CB  LYS A  45     6826   3761   7920    557   -228   -815       C
ATOM    145  CG  LYS A  45      29.831  45.959  -6.797  1.00 57.36           C
ANISOU  145  CG  LYS A  45     7902   4854   9039    559   -242   -813       C
ATOM    146  CD  LYS A  45      31.216  46.565  -6.995  1.00 71.84           C
ANISOU  146  CD  LYS A  45     9727   6653  10916    569   -217   -862       C
ATOM    147  CE  LYS A  45      32.017  46.619  -5.700  1.00 89.07           C
ANISOU  147  CE  LYS A  45    11893   8819  13132    575   -265   -867       C
ATOM    148  NZ  LYS A  45      32.400  45.272  -5.166  1.00 96.18           N
ANISOU  148  NZ  LYS A  45    12782   9692  14071    569   -326   -856       N
ATOM    149  N   LEU A  46      25.613  46.440  -8.563  1.00 48.64           N
ANISOU  149  N   LEU A  46     6798   3786   7896    552   -269   -736       N
ATOM    150  CA  LEU A  46      24.570  46.851  -9.484  1.00 47.54           C
ANISOU  150  CA  LEU A  46     6668   3636   7760    558   -303   -734       C
ATOM    151  C   LEU A  46      24.600  48.368  -9.680  1.00 54.30           C
ANISOU  151  C   LEU A  46     7553   4518   8560    577   -255   -742       C
ATOM    152  O   LEU A  46      24.886  49.100  -8.737  1.00 53.27           O
ANISOU  152  O   LEU A  46     7407   4420   8412    578   -198   -727       O
ATOM    153  CB  LEU A  46      23.200  46.367  -8.959  1.00 46.62           C
ANISOU  153  CB  LEU A  46     6483   3503   7728    545   -333   -681       C
ATOM    154  CG  LEU A  46      21.981  46.577  -9.848  1.00 50.38           C
ANISOU  154  CG  LEU A  46     6943   3945   8253    550   -401   -677       C
ATOM    155  CD1 LEU A  46      22.156  45.904 -11.196  1.00 49.96           C
ANISOU  155  CD1 LEU A  46     6952   3848   8184    557   -494   -726       C
ATOM    156  CD2 LEU A  46      20.678  46.173  -9.129  1.00 52.40           C
ANISOU  156  CD2 LEU A  46     7102   4168   8639    536   -405   -618       C
ATOM    157  N   SER A  47      24.330  48.815 -10.927  1.00 53.31           N
ANISOU  157  N   SER A  47     7483   4371   8400    595   -283   -768       N
ATOM    158  CA  SER A  47      24.226  50.195 -11.373  1.00 54.30           C
ANISOU  158  CA  SER A  47     7649   4511   8472    618   -246   -777       C
ATOM    159  C   SER A  47      23.288  50.241 -12.574  1.00 61.01           C
ANISOU  159  C   SER A  47     8551   5319   9312    637   -330   -786       C
ATOM    160  O   SER A  47      23.511  49.540 -13.556  1.00 61.50           O
ANISOU  160  O   SER A  47     8688   5332   9348    650   -383   -819       O
ATOM    161  CB  SER A  47      25.596  50.784 -11.729  1.00 58.88           C
ANISOU  161  CB  SER A  47     8287   5088   8997    636   -165   -818       C
ATOM    162  OG  SER A  47      25.541  52.197 -11.928  1.00 71.80           O
ANISOU  162  OG  SER A  47     9950   6741  10589    657   -111   -821       O
ATOM    163  N   ILE A  48      22.200  51.020 -12.467  1.00 58.00           N
ANISOU  163  N   ILE A  48     8134   4945   8959    641   -352   -756       N
ATOM    164  CA  ILE A  48      21.242  51.184 -13.552  1.00 57.52           C
ANISOU  164  CA  ILE A  48     8121   4833   8901    664   -458   -765       C
ATOM    165  C   ILE A  48      21.205  52.672 -13.819  1.00 61.66           C
ANISOU  165  C   ILE A  48     8688   5379   9362    691   -404   -765       C
ATOM    166  O   ILE A  48      20.460  53.400 -13.169  1.00 62.01           O
ANISOU  166  O   ILE A  48     8654   5448   9460    682   -382   -726       O
ATOM    167  CB  ILE A  48      19.831  50.569 -13.278  1.00 60.31           C
ANISOU  167  CB  ILE A  48     8372   5148   9395    645   -560   -728       C
ATOM    168  CG1 ILE A  48      19.905  49.077 -12.938  1.00 59.49           C
ANISOU  168  CG1 ILE A  48     8219   5021   9362    618   -598   -726       C
ATOM    169  CG2 ILE A  48      18.867  50.831 -14.449  1.00 62.08           C
ANISOU  169  CG2 ILE A  48     8649   5304   9635    674   -701   -746       C
ATOM    170  CD1 ILE A  48      19.206  48.706 -11.697  1.00 62.03           C
ANISOU  170  CD1 ILE A  48     8410   5353   9805    588   -549   -668       C
ATOM    171  N   PRO A  49      22.066  53.174 -14.715  1.00 59.03           N
ANISOU  171  N   PRO A  49     8480   5031   8919    726   -360   -805       N
ATOM    172  CA  PRO A  49      22.066  54.614 -14.973  1.00 57.63           C
ANISOU  172  CA  PRO A  49     8345   4869   8682    754   -297   -804       C
ATOM    173  C   PRO A  49      20.731  55.080 -15.544  1.00 59.57           C
ANISOU  173  C   PRO A  49     8601   5082   8951    774   -407   -787       C
ATOM    174  O   PRO A  49      20.110  54.380 -16.340  1.00 58.15           O
ANISOU  174  O   PRO A  49     8472   4837   8785    789   -545   -802       O
ATOM    175  CB  PRO A  49      23.243  54.810 -15.931  1.00 59.62           C
ANISOU  175  CB  PRO A  49     8741   5084   8828    793   -222   -849       C
ATOM    176  CG  PRO A  49      24.083  53.591 -15.789  1.00 64.65           C
ANISOU  176  CG  PRO A  49     9372   5706   9485    773   -209   -869       C
ATOM    177  CD  PRO A  49      23.091  52.488 -15.527  1.00 61.31           C
ANISOU  177  CD  PRO A  49     8880   5275   9138    745   -343   -850       C
ATOM    178  N   VAL A  50      20.261  56.224 -15.036  1.00 56.48           N
ANISOU  178  N   VAL A  50     8150   4728   8582    772   -356   -756       N
ATOM    179  CA  VAL A  50      19.022  56.900 -15.412  1.00 57.09           C
ANISOU  179  CA  VAL A  50     8212   4776   8704    789   -442   -734       C
ATOM    180  C   VAL A  50      19.354  58.320 -15.896  1.00 67.49           C
ANISOU  180  C   VAL A  50     9617   6107   9919    829   -363   -743       C
ATOM    181  O   VAL A  50      20.340  58.913 -15.445  1.00 64.72           O
ANISOU  181  O   VAL A  50     9270   5804   9514    825   -219   -750       O
ATOM    182  CB  VAL A  50      17.963  56.901 -14.274  1.00 58.96           C
ANISOU  182  CB  VAL A  50     8276   5030   9095    750   -442   -676       C
ATOM    183  CG1 VAL A  50      17.545  55.477 -13.924  1.00 59.56           C
ANISOU  183  CG1 VAL A  50     8272   5072   9285    718   -519   -665       C
ATOM    184  CG2 VAL A  50      18.446  57.646 -13.029  1.00 57.04           C
ANISOU  184  CG2 VAL A  50     7969   4863   8842    727   -279   -649       C
ATOM    185  N   GLU A  51      18.544  58.853 -16.823  1.00 71.64           N
ANISOU  185  N   GLU A  51    10215   6578  10427    869   -465   -745       N
ATOM    186  CA  GLU A  51      18.716  60.221 -17.316  1.00 74.69           C
ANISOU  186  CA  GLU A  51    10689   6969  10722    911   -396   -748       C
ATOM    187  C   GLU A  51      18.160  61.140 -16.221  1.00 79.93           C
ANISOU  187  C   GLU A  51    11201   7695  11476    878   -318   -700       C
ATOM    188  O   GLU A  51      17.153  60.789 -15.606  1.00 80.08           O
ANISOU  188  O   GLU A  51    11087   7707  11632    845   -381   -663       O
ATOM    189  CB  GLU A  51      17.958  60.431 -18.647  1.00 78.20           C
ANISOU  189  CB  GLU A  51    11273   7323  11115    971   -553   -764       C
ATOM    190  CG  GLU A  51      18.479  59.594 -19.814  1.00 97.00           C
ANISOU  190  CG  GLU A  51    13852   9625  13378   1017   -627   -814       C
ATOM    191  CD  GLU A  51      19.307  60.342 -20.845  1.00133.32           C
ANISOU  191  CD  GLU A  51    18670  14187  17799   1086   -524   -843       C
ATOM    192  OE1 GLU A  51      18.718  61.093 -21.660  1.00137.66           O
ANISOU  192  OE1 GLU A  51    19334  14688  18283   1141   -579   -842       O
ATOM    193  OE2 GLU A  51      20.545  60.143 -20.864  1.00130.52           O
ANISOU  193  OE2 GLU A  51    18378  13835  17378   1088   -386   -865       O
ATOM    194  N   TYR A  52      18.816  62.281 -15.943  1.00 76.32           N
ANISOU  194  N   TYR A  52    10759   7285  10954    887   -172   -700       N
ATOM    195  CA  TYR A  52      18.367  63.176 -14.873  1.00 75.84           C
ANISOU  195  CA  TYR A  52    10573   7278  10965    858    -87   -657       C
ATOM    196  C   TYR A  52      16.890  63.532 -14.963  1.00 81.91           C
ANISOU  196  C   TYR A  52    11272   8010  11838    861   -184   -616       C
ATOM    197  O   TYR A  52      16.201  63.528 -13.937  1.00 82.17           O
ANISOU  197  O   TYR A  52    11169   8060  11990    825   -152   -571       O
ATOM    198  CB  TYR A  52      19.261  64.419 -14.729  1.00 76.65           C
ANISOU  198  CB  TYR A  52    10716   7424  10986    874     67   -670       C
ATOM    199  CG  TYR A  52      19.136  65.103 -13.381  1.00 77.94           C
ANISOU  199  CG  TYR A  52    10761   7646  11207    838    170   -636       C
ATOM    200  CD1 TYR A  52      19.748  64.572 -12.249  1.00 79.75           C
ANISOU  200  CD1 TYR A  52    10927   7912  11461    800    226   -636       C
ATOM    201  CD2 TYR A  52      18.403  66.278 -13.237  1.00 78.26           C
ANISOU  201  CD2 TYR A  52    10768   7696  11272    846    206   -604       C
ATOM    202  CE1 TYR A  52      19.637  65.195 -11.006  1.00 80.68           C
ANISOU  202  CE1 TYR A  52    10974   8070  11612    776    314   -608       C
ATOM    203  CE2 TYR A  52      18.282  66.909 -12.000  1.00 78.63           C
ANISOU  203  CE2 TYR A  52    10728   7786  11361    818    307   -573       C
ATOM    204  CZ  TYR A  52      18.905  66.366 -10.887  1.00 88.26           C
ANISOU  204  CZ  TYR A  52    11908   9037  12590    785    360   -577       C
ATOM    205  OH  TYR A  52      18.791  66.968  -9.659  1.00 91.82           O
ANISOU  205  OH  TYR A  52    12308   9517  13063    766    454   -549       O
ATOM    206  N   LYS A  53      16.389  63.756 -16.196  1.00 79.80           N
ANISOU  206  N   LYS A  53    11106   7677  11536    909   -309   -632       N
ATOM    207  CA  LYS A  53      14.981  64.073 -16.472  1.00 80.64           C
ANISOU  207  CA  LYS A  53    11153   7725  11761    920   -440   -600       C
ATOM    208  C   LYS A  53      14.027  62.950 -15.994  1.00 84.05           C
ANISOU  208  C   LYS A  53    11445   8110  12381    881   -555   -574       C
ATOM    209  O   LYS A  53      12.947  63.258 -15.484  1.00 85.63           O
ANISOU  209  O   LYS A  53    11510   8278  12748    864   -580   -528       O
ATOM    210  CB  LYS A  53      14.759  64.442 -17.963  1.00 84.49           C
ANISOU  210  CB  LYS A  53    11815   8136  12151    990   -575   -631       C
ATOM    211  CG  LYS A  53      15.396  63.476 -18.986  1.00 96.30           C
ANISOU  211  CG  LYS A  53    13489   9580  13522   1027   -661   -686       C
ATOM    212  CD  LYS A  53      15.391  64.011 -20.421  1.00100.65           C
ANISOU  212  CD  LYS A  53    14264  10047  13931   1110   -761   -716       C
ATOM    213  CE  LYS A  53      15.922  62.977 -21.392  1.00102.70           C
ANISOU  213  CE  LYS A  53    14722  10245  14054   1151   -817   -768       C
ATOM    214  NZ  LYS A  53      15.937  63.457 -22.801  1.00105.26           N
ANISOU  214  NZ  LYS A  53    15304  10465  14226   1244   -927   -797       N
ATOM    215  N   GLN A  54      14.465  61.671 -16.089  1.00 77.16           N
ANISOU  215  N   GLN A  54    10595   7227  11495    866   -602   -602       N
ATOM    216  CA  GLN A  54      13.707  60.479 -15.665  1.00 76.55           C
ANISOU  216  CA  GLN A  54    10391   7101  11594    831   -698   -582       C
ATOM    217  C   GLN A  54      13.497  60.402 -14.134  1.00 75.40           C
ANISOU  217  C   GLN A  54    10079   7000  11572    778   -549   -526       C
ATOM    218  O   GLN A  54      12.770  59.508 -13.672  1.00 75.96           O
ANISOU  218  O   GLN A  54    10028   7018  11814    749   -596   -497       O
ATOM    219  CB  GLN A  54      14.441  59.175 -16.074  1.00 78.13           C
ANISOU  219  CB  GLN A  54    10673   7291  11724    828   -757   -627       C
ATOM    220  CG  GLN A  54      14.692  58.930 -17.558  1.00 97.92           C
ANISOU  220  CG  GLN A  54    13374   9732  14098    884   -901   -685       C
ATOM    221  CD  GLN A  54      15.547  57.704 -17.783  1.00120.45           C
ANISOU  221  CD  GLN A  54    16302  12584  16880    877   -911   -724       C
ATOM    222  OE1 GLN A  54      15.909  56.976 -16.853  1.00114.91           O
ANISOU  222  OE1 GLN A  54    15493  11926  16240    829   -833   -708       O
ATOM    223  NE2 GLN A  54      15.880  57.436 -19.034  1.00118.97           N
ANISOU  223  NE2 GLN A  54    16312  12335  16557    930  -1004   -775       N
ATOM    224  N   ILE A  55      14.198  61.263 -13.346  1.00 65.21           N
ANISOU  224  N   ILE A  55     8795   5793  10188    769   -367   -513       N
ATOM    225  CA  ILE A  55      14.140  61.220 -11.879  1.00 60.33           C
ANISOU  225  CA  ILE A  55     8072   5211   9640    730   -217   -464       C
ATOM    226  C   ILE A  55      12.949  61.997 -11.333  1.00 61.50           C
ANISOU  226  C   ILE A  55     8105   5322   9939    724   -168   -402       C
ATOM    227  O   ILE A  55      12.784  63.172 -11.700  1.00 60.84           O
ANISOU  227  O   ILE A  55     8050   5250   9817    746   -150   -401       O
ATOM    228  CB  ILE A  55      15.493  61.594 -11.211  1.00 60.29           C
ANISOU  228  CB  ILE A  55     8136   5296   9476    725    -71   -486       C
ATOM    229  CG1 ILE A  55      16.644  60.786 -11.826  1.00 59.11           C
ANISOU  229  CG1 ILE A  55     8085   5162   9211    732   -118   -545       C
ATOM    230  CG2 ILE A  55      15.457  61.398  -9.690  1.00 60.01           C
ANISOU  230  CG2 ILE A  55     8030   5281   9491    694     58   -442       C
ATOM    231  CD1 ILE A  55      18.002  61.328 -11.566  1.00 64.39           C
ANISOU  231  CD1 ILE A  55     8828   5893   9744    738     -7   -580       C
ATOM    232  N   PRO A  56      12.109  61.369 -10.457  1.00 56.61           N
ANISOU  232  N   PRO A  56     7359   4648   9502    697   -129   -348       N
ATOM    233  CA  PRO A  56      10.998  62.113  -9.854  1.00 56.45           C
ANISOU  233  CA  PRO A  56     7227   4577   9644    692    -46   -281       C
ATOM    234  C   PRO A  56      11.546  63.278  -9.022  1.00 58.39           C
ANISOU  234  C   PRO A  56     7524   4899   9764    694    138   -266       C
ATOM    235  O   PRO A  56      12.576  63.119  -8.346  1.00 56.26           O
ANISOU  235  O   PRO A  56     7328   4697   9351    687    230   -284       O
ATOM    236  CB  PRO A  56      10.325  61.070  -8.947  1.00 58.54           C
ANISOU  236  CB  PRO A  56     7375   4767  10098    665      8   -228       C
ATOM    237  CG  PRO A  56      10.755  59.774  -9.435  1.00 62.70           C
ANISOU  237  CG  PRO A  56     7930   5288  10605    658   -118   -271       C
ATOM    238  CD  PRO A  56      12.158  59.995  -9.916  1.00 58.17           C
ANISOU  238  CD  PRO A  56     7512   4819   9771    672   -133   -338       C
ATOM    239  N   PRO A  57      10.913  64.465  -9.080  1.00 55.84           N
ANISOU  239  N   PRO A  57     7166   4560   9491    706    181   -237       N
ATOM    240  CA  PRO A  57      11.415  65.608  -8.295  1.00 54.75           C
ANISOU  240  CA  PRO A  57     7079   4488   9234    709    352   -225       C
ATOM    241  C   PRO A  57      11.527  65.332  -6.794  1.00 56.68           C
ANISOU  241  C   PRO A  57     7320   4732   9483    692    524   -182       C
ATOM    242  O   PRO A  57      12.499  65.779  -6.190  1.00 56.28           O
ANISOU  242  O   PRO A  57     7364   4752   9269    695    615   -204       O
ATOM    243  CB  PRO A  57      10.421  66.734  -8.620  1.00 56.76           C
ANISOU  243  CB  PRO A  57     7269   4698   9600    723    357   -188       C
ATOM    244  CG  PRO A  57       9.868  66.364  -9.927  1.00 62.15           C
ANISOU  244  CG  PRO A  57     7925   5322  10367    739    148   -212       C
ATOM    245  CD  PRO A  57       9.740  64.862  -9.879  1.00 59.01           C
ANISOU  245  CD  PRO A  57     7484   4877  10060    721     64   -217       C
ATOM    246  N   ASN A  58      10.597  64.552  -6.215  1.00 52.74           N
ANISOU  246  N   ASN A  58     6725   4143   9172    679    561   -124       N
ATOM    247  CA  ASN A  58      10.608  64.180  -4.798  1.00 53.10           C
ANISOU  247  CA  ASN A  58     6790   4162   9223    672    733    -75       C
ATOM    248  C   ASN A  58      11.846  63.407  -4.385  1.00 57.07           C
ANISOU  248  C   ASN A  58     7404   4732   9549    669    725   -119       C
ATOM    249  O   ASN A  58      12.232  63.468  -3.217  1.00 58.85           O
ANISOU  249  O   ASN A  58     7710   4963   9686    676    859    -99       O
ATOM    250  CB  ASN A  58       9.362  63.397  -4.434  1.00 56.72           C
ANISOU  250  CB  ASN A  58     7118   4491   9941    663    775     -4       C
ATOM    251  CG  ASN A  58       8.130  64.253  -4.535  1.00 80.64           C
ANISOU  251  CG  ASN A  58    10030   7434  13173    668    825     52       C
ATOM    252  OD1 ASN A  58       8.007  65.301  -3.869  1.00 64.32           O
ANISOU  252  OD1 ASN A  58     7998   5375  11067    678    976     85       O
ATOM    253  ND2 ASN A  58       7.222  63.863  -5.395  1.00 76.67           N
ANISOU  253  ND2 ASN A  58     9390   6845  12896    661    688     61       N
ATOM    254  N   PHE A  59      12.477  62.696  -5.335  1.00 50.81           N
ANISOU  254  N   PHE A  59     6627   3978   8700    664    566   -181       N
ATOM    255  CA  PHE A  59      13.704  61.968  -5.064  1.00 49.71           C
ANISOU  255  CA  PHE A  59     6581   3898   8409    660    544   -227       C
ATOM    256  C   PHE A  59      14.840  62.944  -4.935  1.00 53.55           C
ANISOU  256  C   PHE A  59     7171   4468   8708    672    580   -275       C
ATOM    257  O   PHE A  59      15.634  62.833  -4.000  1.00 54.25           O
ANISOU  257  O   PHE A  59     7339   4582   8692    675    642   -285       O
ATOM    258  CB  PHE A  59      13.998  60.918  -6.144  1.00 51.06           C
ANISOU  258  CB  PHE A  59     6738   4072   8592    653    378   -275       C
ATOM    259  CG  PHE A  59      14.651  59.660  -5.619  1.00 50.72           C
ANISOU  259  CG  PHE A  59     6729   4034   8510    642    371   -287       C
ATOM    260  CD1 PHE A  59      15.212  59.622  -4.343  1.00 52.72           C
ANISOU  260  CD1 PHE A  59     7053   4304   8676    646    487   -270       C
ATOM    261  CD2 PHE A  59      14.709  58.512  -6.397  1.00 51.11           C
ANISOU  261  CD2 PHE A  59     6752   4063   8604    632    241   -315       C
ATOM    262  CE1 PHE A  59      15.815  58.456  -3.862  1.00 52.39           C
ANISOU  262  CE1 PHE A  59     7048   4260   8597    640    471   -280       C
ATOM    263  CE2 PHE A  59      15.296  57.347  -5.907  1.00 51.72           C
ANISOU  263  CE2 PHE A  59     6856   4143   8651    623    238   -324       C
ATOM    264  CZ  PHE A  59      15.831  57.326  -4.640  1.00 49.51           C
ANISOU  264  CZ  PHE A  59     6640   3881   8291    627    354   -304       C
ATOM    265  N   ILE A  60      14.890  63.930  -5.851  1.00 49.73           N
ANISOU  265  N   ILE A  60     6688   4016   8192    682    538   -303       N
ATOM    266  CA  ILE A  60      15.880  65.002  -5.839  1.00 47.41           C
ANISOU  266  CA  ILE A  60     6473   3788   7752    694    580   -347       C
ATOM    267  C   ILE A  60      15.698  65.807  -4.553  1.00 50.25           C
ANISOU  267  C   ILE A  60     6861   4142   8089    698    727   -308       C
ATOM    268  O   ILE A  60      16.666  65.998  -3.827  1.00 48.92           O
ANISOU  268  O   ILE A  60     6775   4007   7806    703    766   -339       O
ATOM    269  CB  ILE A  60      15.807  65.826  -7.146  1.00 50.11           C
ANISOU  269  CB  ILE A  60     6814   4145   8080    710    515   -375       C
ATOM    270  CG1 ILE A  60      16.320  64.972  -8.316  1.00 50.68           C
ANISOU  270  CG1 ILE A  60     6917   4218   8121    716    380   -426       C
ATOM    271  CG2 ILE A  60      16.603  67.168  -7.042  1.00 50.99           C
ANISOU  271  CG2 ILE A  60     6987   4310   8077    725    593   -407       C
ATOM    272  CD1 ILE A  60      15.637  65.213  -9.604  1.00 62.41           C
ANISOU  272  CD1 ILE A  60     8394   5669   9652    736    275   -429       C
ATOM    273  N   HIS A  61      14.446  66.147  -4.211  1.00 48.82           N
ANISOU  273  N   HIS A  61     6616   3904   8031    699    804   -240       N
ATOM    274  CA  HIS A  61      14.098  66.873  -2.994  1.00 49.85           C
ANISOU  274  CA  HIS A  61     6784   4006   8152    708    965   -192       C
ATOM    275  C   HIS A  61      14.565  66.177  -1.747  1.00 55.48           C
ANISOU  275  C   HIS A  61     7587   4698   8794    713   1031   -181       C
ATOM    276  O   HIS A  61      14.991  66.863  -0.820  1.00 56.98           O
ANISOU  276  O   HIS A  61     7879   4894   8877    729   1122   -182       O
ATOM    277  CB  HIS A  61      12.591  67.113  -2.911  1.00 51.95           C
ANISOU  277  CB  HIS A  61     6946   4187   8605    707   1042   -113       C
ATOM    278  CG  HIS A  61      12.111  68.151  -3.867  1.00 56.03           C
ANISOU  278  CG  HIS A  61     7398   4716   9173    711    999   -118       C
ATOM    279  ND1 HIS A  61      10.768  68.333  -4.106  1.00 59.25           N
ANISOU  279  ND1 HIS A  61     7687   5042   9785    709   1016    -57       N
ATOM    280  CD2 HIS A  61      12.816  69.026  -4.622  1.00 57.83           C
ANISOU  280  CD2 HIS A  61     7669   5017   9284    719    941   -174       C
ATOM    281  CE1 HIS A  61      10.694  69.315  -4.984  1.00 59.15           C
ANISOU  281  CE1 HIS A  61     7658   5060   9757    718    956    -80       C
ATOM    282  NE2 HIS A  61      11.904  69.758  -5.328  1.00 58.69           N
ANISOU  282  NE2 HIS A  61     7701   5097   9503    726    919   -149       N
ATOM    283  N   ALA A  62      14.481  64.826  -1.721  1.00 50.46           N
ANISOU  283  N   ALA A  62     6926   4032   8215    704    981   -171       N
ATOM    284  CA  ALA A  62      14.897  63.990  -0.604  1.00 49.53           C
ANISOU  284  CA  ALA A  62     6902   3885   8033    713   1030   -158       C
ATOM    285  C   ALA A  62      16.395  64.151  -0.363  1.00 52.79           C
ANISOU  285  C   ALA A  62     7427   4366   8263    721    965   -233       C
ATOM    286  O   ALA A  62      16.814  64.330   0.783  1.00 53.33           O
ANISOU  286  O   ALA A  62     7621   4415   8228    743   1031   -229       O
ATOM    287  CB  ALA A  62      14.546  62.541  -0.889  1.00 50.05           C
ANISOU  287  CB  ALA A  62     6897   3911   8208    699    967   -141       C
ATOM    288  N   PHE A  63      17.188  64.164  -1.451  1.00 46.93           N
ANISOU  288  N   PHE A  63     6649   3691   7490    708    838   -301       N
ATOM    289  CA  PHE A  63      18.629  64.361  -1.375  1.00 44.37           C
ANISOU  289  CA  PHE A  63     6399   3417   7041    713    774   -375       C
ATOM    290  C   PHE A  63      18.978  65.768  -0.950  1.00 50.04           C
ANISOU  290  C   PHE A  63     7176   4154   7684    728    834   -395       C
ATOM    291  O   PHE A  63      19.928  65.941  -0.206  1.00 51.92           O
ANISOU  291  O   PHE A  63     7505   4393   7828    741    818   -434       O
ATOM    292  CB  PHE A  63      19.313  63.965  -2.679  1.00 44.17           C
ANISOU  292  CB  PHE A  63     6322   3434   7026    699    656   -434       C
ATOM    293  CG  PHE A  63      19.521  62.476  -2.837  1.00 44.11           C
ANISOU  293  CG  PHE A  63     6299   3412   7047    687    579   -439       C
ATOM    294  CD1 PHE A  63      20.654  61.856  -2.318  1.00 45.96           C
ANISOU  294  CD1 PHE A  63     6594   3652   7216    690    531   -480       C
ATOM    295  CD2 PHE A  63      18.610  61.702  -3.538  1.00 47.00           C
ANISOU  295  CD2 PHE A  63     6588   3751   7520    675    543   -406       C
ATOM    296  CE1 PHE A  63      20.851  60.474  -2.459  1.00 46.85           C
ANISOU  296  CE1 PHE A  63     6693   3751   7358    679    465   -483       C
ATOM    297  CE2 PHE A  63      18.799  60.306  -3.671  1.00 50.69           C
ANISOU  297  CE2 PHE A  63     7042   4201   8017    664    474   -412       C
ATOM    298  CZ  PHE A  63      19.924  59.705  -3.135  1.00 47.56           C
ANISOU  298  CZ  PHE A  63     6709   3819   7544    666    443   -449       C
ATOM    299  N   LEU A  64      18.194  66.772  -1.358  1.00 47.54           N
ANISOU  299  N   LEU A  64     6810   3841   7413    728    897   -367       N
ATOM    300  CA  LEU A  64      18.374  68.187  -0.992  1.00 46.07           C
ANISOU  300  CA  LEU A  64     6669   3669   7167    741    968   -379       C
ATOM    301  C   LEU A  64      18.114  68.461   0.479  1.00 50.15           C
ANISOU  301  C   LEU A  64     7297   4133   7625    763   1075   -341       C
ATOM    302  O   LEU A  64      18.702  69.385   1.021  1.00 50.91           O
ANISOU  302  O   LEU A  64     7476   4235   7632    778   1094   -375       O
ATOM    303  CB  LEU A  64      17.468  69.091  -1.832  1.00 45.96           C
ANISOU  303  CB  LEU A  64     6570   3663   7229    738   1009   -351       C
ATOM    304  CG  LEU A  64      17.724  69.093  -3.336  1.00 50.34           C
ANISOU  304  CG  LEU A  64     7056   4258   7812    731    910   -391       C
ATOM    305  CD1 LEU A  64      16.851  70.102  -4.014  1.00 49.66           C
ANISOU  305  CD1 LEU A  64     6909   4169   7789    736    944   -361       C
ATOM    306  CD2 LEU A  64      19.203  69.340  -3.674  1.00 51.66           C
ANISOU  306  CD2 LEU A  64     7268   4468   7891    736    859   -472       C
ATOM    307  N   ALA A  65      17.192  67.712   1.108  1.00 47.10           N
ANISOU  307  N   ALA A  65     6921   3683   7294    768   1152   -270       N
ATOM    308  CA  ALA A  65      16.847  67.819   2.532  1.00 47.38           C
ANISOU  308  CA  ALA A  65     7093   3643   7266    798   1278   -222       C
ATOM    309  C   ALA A  65      17.699  66.898   3.399  1.00 53.01           C
ANISOU  309  C   ALA A  65     7937   4331   7871    818   1221   -247       C
ATOM    310  O   ALA A  65      17.634  66.992   4.627  1.00 53.58           O
ANISOU  310  O   ALA A  65     8171   4335   7853    854   1307   -219       O
ATOM    311  CB  ALA A  65      15.373  67.495   2.743  1.00 48.41           C
ANISOU  311  CB  ALA A  65     7166   3692   7534    800   1419   -124       C
ATOM    312  N   ALA A  66      18.484  65.999   2.771  1.00 50.19           N
ANISOU  312  N   ALA A  66     7529   4020   7523    799   1077   -298       N
ATOM    313  CA  ALA A  66      19.332  65.019   3.465  1.00 50.42           C
ANISOU  313  CA  ALA A  66     7663   4026   7469    815   1000   -325       C
ATOM    314  C   ALA A  66      20.437  65.650   4.327  1.00 56.60           C
ANISOU  314  C   ALA A  66     8598   4797   8110    845    942   -385       C
ATOM    315  O   ALA A  66      20.830  65.064   5.340  1.00 56.07           O
ANISOU  315  O   ALA A  66     8678   4674   7952    877    916   -386       O
ATOM    316  CB  ALA A  66      19.913  64.031   2.470  1.00 50.26           C
ANISOU  316  CB  ALA A  66     7534   4054   7508    785    867   -366       C
ATOM    317  N   GLU A  67      20.931  66.834   3.929  1.00 55.42           N
ANISOU  317  N   GLU A  67     8418   4692   7948    838    912   -438       N
ATOM    318  CA  GLU A  67      21.952  67.550   4.692  1.00 57.27           C
ANISOU  318  CA  GLU A  67     8779   4905   8078    864    843   -503       C
ATOM    319  C   GLU A  67      21.491  68.905   5.037  1.00 66.65           C
ANISOU  319  C   GLU A  67    10015   6081   9229    878    945   -490       C
ATOM    320  O   GLU A  67      20.805  69.529   4.235  1.00 66.90           O
ANISOU  320  O   GLU A  67     9926   6156   9339    855   1019   -467       O
ATOM    321  CB  GLU A  67      23.273  67.647   3.935  1.00 58.09           C
ANISOU  321  CB  GLU A  67     8794   5054   8223    843    693   -595       C
ATOM    322  CG  GLU A  67      23.910  66.309   3.634  1.00 65.28           C
ANISOU  322  CG  GLU A  67     9663   5969   9172    831    584   -616       C
ATOM    323  CD  GLU A  67      24.143  65.350   4.785  1.00 79.86           C
ANISOU  323  CD  GLU A  67    11658   7750  10937    863    531   -605       C
ATOM    324  OE1 GLU A  67      24.204  64.138   4.490  1.00 63.66           O
ANISOU  324  OE1 GLU A  67     9560   5704   8926    850    489   -593       O
ATOM    325  OE2 GLU A  67      24.279  65.785   5.956  1.00 74.17           O
ANISOU  325  OE2 GLU A  67    11109   6965  10106    904    526   -611       O
ATOM    326  N   ASP A  68      21.863  69.374   6.230  1.00 68.45           N
ANISOU  326  N   ASP A  68    10432   6242   9333    920    942   -506       N
ATOM    327  CA  ASP A  68      21.490  70.708   6.712  1.00 70.77           C
ANISOU  327  CA  ASP A  68    10804   6512   9573    940   1040   -498       C
ATOM    328  C   ASP A  68      22.105  71.829   5.856  1.00 72.74           C
ANISOU  328  C   ASP A  68    10931   6826   9881    914    984   -567       C
ATOM    329  O   ASP A  68      21.393  72.727   5.398  1.00 70.59           O
ANISOU  329  O   ASP A  68    10584   6584   9654    900   1096   -536       O
ATOM    330  CB  ASP A  68      21.860  70.893   8.207  1.00 75.17           C
ANISOU  330  CB  ASP A  68    11627   6968   9965   1000   1024   -511       C
ATOM    331  CG  ASP A  68      20.681  71.119   9.160  1.00 92.80           C
ANISOU  331  CG  ASP A  68    14015   9120  12126   1038   1232   -419       C
ATOM    332  OD1 ASP A  68      19.544  71.330   8.671  1.00 92.65           O
ANISOU  332  OD1 ASP A  68    13872   9121  12212   1014   1391   -345       O
ATOM    333  OD2 ASP A  68      20.898  71.080  10.394  1.00103.99           O
ANISOU  333  OD2 ASP A  68    15685  10438  13389   1097   1234   -421       O
ATOM    334  N   SER A  69      23.418  71.743   5.602  1.00 69.27           N
ANISOU  334  N   SER A  69    10461   6399   9459    907    819   -656       N
ATOM    335  CA  SER A  69      24.088  72.794   4.842  1.00 67.72           C
ANISOU  335  CA  SER A  69    10155   6243   9333    888    782   -721       C
ATOM    336  C   SER A  69      24.876  72.330   3.640  1.00 66.87           C
ANISOU  336  C   SER A  69     9879   6186   9343    855    698   -767       C
ATOM    337  O   SER A  69      25.677  71.385   3.719  1.00 67.25           O
ANISOU  337  O   SER A  69     9927   6214   9410    855    578   -803       O
ATOM    338  CB  SER A  69      24.913  73.695   5.756  1.00 73.41           C
ANISOU  338  CB  SER A  69    11002   6901   9989    919    702   -791       C
ATOM    339  OG  SER A  69      25.856  72.994   6.554  1.00 85.49           O
ANISOU  339  OG  SER A  69    12641   8366  11477    944    536   -844       O
ATOM    340  N   SER A  70      24.612  73.003   2.512  1.00 58.80           N
ANISOU  340  N   SER A  70     8725   5220   8396    832    772   -761       N
ATOM    341  CA  SER A  70      25.219  72.773   1.200  1.00 55.95           C
ANISOU  341  CA  SER A  70     8221   4900   8139    808    737   -796       C
ATOM    342  C   SER A  70      25.909  74.077   0.764  1.00 56.34           C
ANISOU  342  C   SER A  70     8216   4949   8243    810    754   -853       C
ATOM    343  O   SER A  70      25.329  75.163   0.893  1.00 58.03           O
ANISOU  343  O   SER A  70     8448   5173   8429    816    845   -832       O
ATOM    344  CB  SER A  70      24.151  72.344   0.202  1.00 57.81           C
ANISOU  344  CB  SER A  70     8375   5187   8405    791    813   -729       C
ATOM    345  OG  SER A  70      24.569  72.532  -1.136  1.00 68.89           O
ANISOU  345  OG  SER A  70     9673   6621   9882    779    811   -758       O
ATOM    346  N   PHE A  71      27.161  73.981   0.299  1.00 47.93           N
ANISOU  346  N   PHE A  71     7084   3859   7269    805    676   -924       N
ATOM    347  CA  PHE A  71      27.970  75.144  -0.103  1.00 44.60           C
ANISOU  347  CA  PHE A  71     6600   3414   6933    809    696   -983       C
ATOM    348  C   PHE A  71      28.656  74.934  -1.452  1.00 50.38           C
ANISOU  348  C   PHE A  71     7214   4147   7780    799    720  -1010       C
ATOM    349  O   PHE A  71      29.722  75.498  -1.680  1.00 52.90           O
ANISOU  349  O   PHE A  71     7473   4414   8212    803    709  -1074       O
ATOM    350  CB  PHE A  71      29.059  75.445   0.961  1.00 45.76           C
ANISOU  350  CB  PHE A  71     6797   3479   7110    824    573  -1060       C
ATOM    351  CG  PHE A  71      28.698  75.284   2.423  1.00 47.14           C
ANISOU  351  CG  PHE A  71     7134   3619   7156    845    504  -1049       C
ATOM    352  CD1 PHE A  71      29.109  74.161   3.141  1.00 49.64           C
ANISOU  352  CD1 PHE A  71     7524   3894   7444    855    374  -1062       C
ATOM    353  CD2 PHE A  71      28.006  76.280   3.098  1.00 48.17           C
ANISOU  353  CD2 PHE A  71     7363   3747   7194    861    572  -1027       C
ATOM    354  CE1 PHE A  71      28.787  74.021   4.493  1.00 50.07           C
ANISOU  354  CE1 PHE A  71     7763   3901   7362    886    318  -1049       C
ATOM    355  CE2 PHE A  71      27.706  76.147   4.459  1.00 50.57           C
ANISOU  355  CE2 PHE A  71     7850   4000   7366    891    523  -1016       C
ATOM    356  CZ  PHE A  71      28.121  75.033   5.151  1.00 48.35           C
ANISOU  356  CZ  PHE A  71     7655   3671   7044    907    395  -1028       C
ATOM    357  N   PHE A  72      28.089  74.131  -2.344  1.00 45.84           N
ANISOU  357  N   PHE A  72     6612   3617   7190    790    755   -964       N
ATOM    358  CA  PHE A  72      28.768  73.856  -3.612  1.00 44.10           C
ANISOU  358  CA  PHE A  72     6314   3381   7060    789    784   -988       C
ATOM    359  C   PHE A  72      28.760  75.042  -4.593  1.00 58.13           C
ANISOU  359  C   PHE A  72     8053   5160   8872    803    907   -991       C
ATOM    360  O   PHE A  72      27.686  75.629  -4.766  1.00 69.66           O
ANISOU  360  O   PHE A  72     9540   6671  10259    807    973   -942       O
ATOM    361  CB  PHE A  72      28.155  72.620  -4.267  1.00 44.38           C
ANISOU  361  CB  PHE A  72     6355   3452   7054    781    771   -943       C
ATOM    362  CG  PHE A  72      28.157  71.387  -3.411  1.00 45.10           C
ANISOU  362  CG  PHE A  72     6481   3538   7115    769    666   -935       C
ATOM    363  CD1 PHE A  72      29.355  70.766  -3.055  1.00 47.01           C
ANISOU  363  CD1 PHE A  72     6705   3724   7433    767    573   -990       C
ATOM    364  CD2 PHE A  72      26.965  70.822  -2.985  1.00 47.07           C
ANISOU  364  CD2 PHE A  72     6778   3828   7279    763    663   -870       C
ATOM    365  CE1 PHE A  72      29.356  69.626  -2.272  1.00 47.98           C
ANISOU  365  CE1 PHE A  72     6871   3838   7520    762    475   -980       C
ATOM    366  CE2 PHE A  72      26.964  69.654  -2.224  1.00 49.13           C
ANISOU  366  CE2 PHE A  72     7079   4075   7512    757    581   -859       C
ATOM    367  CZ  PHE A  72      28.159  69.070  -1.867  1.00 47.37           C
ANISOU  367  CZ  PHE A  72     6852   3804   7340    758    485   -914       C
ATOM    368  N   GLN A 133      18.958  78.097  -2.221  1.00 75.35           N
ANISOU  368  N   GLN A 133    10372   7509  10749    801   1383   -487       N
ATOM    369  CA  GLN A 133      19.107  77.126  -1.133  1.00 75.04           C
ANISOU  369  CA  GLN A 133    10404   7438  10671    799   1353   -483       C
ATOM    370  C   GLN A 133      19.176  75.711  -1.703  1.00 80.02           C
ANISOU  370  C   GLN A 133    10994   8076  11334    787   1256   -482       C
ATOM    371  O   GLN A 133      18.230  75.251  -2.360  1.00 80.82           O
ANISOU  371  O   GLN A 133    11027   8175  11506    779   1253   -432       O
ATOM    372  CB  GLN A 133      18.031  77.302  -0.024  1.00 76.34           C
ANISOU  372  CB  GLN A 133    10626   7552  10827    806   1467   -411       C
ATOM    373  CG  GLN A 133      16.553  77.020  -0.392  1.00 77.88           C
ANISOU  373  CG  GLN A 133    10738   7723  11131    799   1532   -322       C
ATOM    374  CD  GLN A 133      15.929  77.954  -1.419  1.00 83.60           C
ANISOU  374  CD  GLN A 133    11365   8470  11930    798   1562   -301       C
ATOM    375  OE1 GLN A 133      16.100  77.775  -2.639  1.00 73.72           O
ANISOU  375  OE1 GLN A 133    10045   7254  10711    794   1473   -325       O
ATOM    376  NE2 GLN A 133      15.121  78.917  -0.950  1.00 68.27           N
ANISOU  376  NE2 GLN A 133     9425   6495  10019    805   1690   -251       N
ATOM    377  N   ASN A 134      20.347  75.060  -1.550  1.00 75.98           N
ANISOU  377  N   ASN A 134    10515   7567  10786    785   1166   -544       N
ATOM    378  CA  ASN A 134      20.615  73.713  -2.082  1.00 74.79           C
ANISOU  378  CA  ASN A 134    10334   7422  10660    774   1072   -554       C
ATOM    379  C   ASN A 134      20.444  73.629  -3.631  1.00 73.22           C
ANISOU  379  C   ASN A 134    10056   7250  10514    771   1041   -555       C
ATOM    380  O   ASN A 134      20.557  72.543  -4.193  1.00 74.34           O
ANISOU  380  O   ASN A 134    10175   7392  10678    764    967   -559       O
ATOM    381  CB  ASN A 134      19.772  72.631  -1.348  1.00 79.94           C
ANISOU  381  CB  ASN A 134    11012   8041  11319    769   1078   -495       C
ATOM    382  CG  ASN A 134      20.121  72.419   0.113  1.00115.67           C
ANISOU  382  CG  ASN A 134    15656  12526  15767    783   1085   -501       C
ATOM    383  OD1 ASN A 134      21.149  71.817   0.453  1.00111.71           O
ANISOU  383  OD1 ASN A 134    15197  12017  15232    785    992   -549       O
ATOM    384  ND2 ASN A 134      19.225  72.827   1.010  1.00109.39           N
ANISOU  384  ND2 ASN A 134    14929  11690  14944    798   1194   -450       N
ATOM    385  N   LEU A 135      20.187  74.772  -4.304  1.00 64.34           N
ANISOU  385  N   LEU A 135     8906   6141   9401    782   1095   -554       N
ATOM    386  CA  LEU A 135      19.984  74.884  -5.740  1.00 62.24           C
ANISOU  386  CA  LEU A 135     8602   5885   9160    793   1072   -554       C
ATOM    387  C   LEU A 135      21.188  74.431  -6.554  1.00 62.15           C
ANISOU  387  C   LEU A 135     8606   5874   9134    800   1019   -617       C
ATOM    388  O   LEU A 135      20.995  73.835  -7.616  1.00 63.17           O
ANISOU  388  O   LEU A 135     8734   5996   9270    809    965   -614       O
ATOM    389  CB  LEU A 135      19.537  76.307  -6.109  1.00 63.14           C
ANISOU  389  CB  LEU A 135     8705   6008   9277    809   1153   -539       C
ATOM    390  CG  LEU A 135      18.996  76.557  -7.550  1.00 68.73           C
ANISOU  390  CG  LEU A 135     9396   6713  10004    831   1130   -523       C
ATOM    391  CD1 LEU A 135      17.986  75.463  -8.003  1.00 70.27           C
ANISOU  391  CD1 LEU A 135     9560   6887  10254    825   1038   -478       C
ATOM    392  CD2 LEU A 135      18.424  77.969  -7.693  1.00 66.40           C
ANISOU  392  CD2 LEU A 135     9090   6422   9716    846   1216   -499       C
ATOM    393  N   SER A 136      22.422  74.656  -6.052  1.00 54.56           N
ANISOU  393  N   SER A 136     7663   4906   8163    799   1028   -675       N
ATOM    394  CA  SER A 136      23.654  74.188  -6.716  1.00 52.21           C
ANISOU  394  CA  SER A 136     7367   4588   7884    805    995   -733       C
ATOM    395  C   SER A 136      23.908  72.714  -6.419  1.00 52.12           C
ANISOU  395  C   SER A 136     7358   4568   7878    789    905   -738       C
ATOM    396  O   SER A 136      24.638  72.073  -7.158  1.00 51.01           O
ANISOU  396  O   SER A 136     7217   4406   7756    793    875   -770       O
ATOM    397  CB  SER A 136      24.854  75.009  -6.286  1.00 56.40           C
ANISOU  397  CB  SER A 136     7892   5093   8445    810   1032   -794       C
ATOM    398  OG  SER A 136      25.005  74.920  -4.877  1.00 69.80           O
ANISOU  398  OG  SER A 136     9607   6784  10129    796    994   -803       O
ATOM    399  N   LYS A 137      23.287  72.156  -5.357  1.00 47.80           N
ANISOU  399  N   LYS A 137     6822   4027   7314    773    875   -703       N
ATOM    400  CA  LYS A 137      23.368  70.725  -5.046  1.00 45.42           C
ANISOU  400  CA  LYS A 137     6525   3716   7016    759    796   -698       C
ATOM    401  C   LYS A 137      22.595  69.990  -6.128  1.00 49.48           C
ANISOU  401  C   LYS A 137     7017   4236   7549    758    762   -666       C
ATOM    402  O   LYS A 137      23.097  69.003  -6.638  1.00 50.41           O
ANISOU  402  O   LYS A 137     7135   4342   7678    754    701   -688       O
ATOM    403  CB  LYS A 137      22.828  70.410  -3.643  1.00 46.15           C
ANISOU  403  CB  LYS A 137     6654   3799   7081    751    797   -660       C
ATOM    404  CG  LYS A 137      23.142  68.997  -3.185  1.00 46.44           C
ANISOU  404  CG  LYS A 137     6709   3819   7117    742    719   -663       C
ATOM    405  CD  LYS A 137      22.697  68.687  -1.765  1.00 46.33           C
ANISOU  405  CD  LYS A 137     6763   3779   7061    745    735   -624       C
ATOM    406  CE  LYS A 137      22.800  67.197  -1.432  1.00 40.67           C
ANISOU  406  CE  LYS A 137     6063   3042   6347    739    667   -615       C
ATOM    407  NZ  LYS A 137      22.535  66.930   0.021  1.00 36.51           N
ANISOU  407  NZ  LYS A 137     5637   2473   5760    755    692   -582       N
ATOM    408  N   GLU A 138      21.443  70.530  -6.571  1.00 47.54           N
ANISOU  408  N   GLU A 138     6752   3997   7314    764    792   -620       N
ATOM    409  CA  GLU A 138      20.649  69.945  -7.649  1.00 49.02           C
ANISOU  409  CA  GLU A 138     6923   4173   7528    770    733   -594       C
ATOM    410  C   GLU A 138      21.464  69.750  -8.959  1.00 58.99           C
ANISOU  410  C   GLU A 138     8228   5423   8763    791    701   -642       C
ATOM    411  O   GLU A 138      21.302  68.742  -9.658  1.00 61.95           O
ANISOU  411  O   GLU A 138     8617   5778   9143    794    623   -643       O
ATOM    412  CB  GLU A 138      19.410  70.789  -7.887  1.00 50.44           C
ANISOU  412  CB  GLU A 138     7075   4351   7741    778    764   -544       C
ATOM    413  CG  GLU A 138      18.343  70.074  -8.695  1.00 66.57           C
ANISOU  413  CG  GLU A 138     9087   6362   9845    780    674   -509       C
ATOM    414  CD  GLU A 138      17.144  70.906  -9.104  1.00106.07           C
ANISOU  414  CD  GLU A 138    14053  11346  14905    793    680   -463       C
ATOM    415  OE1 GLU A 138      16.006  70.417  -8.926  1.00118.75           O
ANISOU  415  OE1 GLU A 138    15592  12912  16615    782    639   -414       O
ATOM    416  OE2 GLU A 138      17.336  72.024  -9.638  1.00110.62           O
ANISOU  416  OE2 GLU A 138    14659  11934  15437    816    726   -476       O
ATOM    417  N   ASP A 139      22.376  70.683  -9.258  1.00 56.24           N
ANISOU  417  N   ASP A 139     7905   5073   8389    809    772   -683       N
ATOM    418  CA  ASP A 139      23.224  70.604 -10.442  1.00 55.41           C
ANISOU  418  CA  ASP A 139     7854   4936   8263    837    784   -724       C
ATOM    419  C   ASP A 139      24.323  69.570 -10.226  1.00 58.35           C
ANISOU  419  C   ASP A 139     8223   5288   8659    823    756   -764       C
ATOM    420  O   ASP A 139      24.531  68.733 -11.106  1.00 60.88           O
ANISOU  420  O   ASP A 139     8587   5578   8966    835    720   -777       O
ATOM    421  CB  ASP A 139      23.808  71.978 -10.804  1.00 57.37           C
ANISOU  421  CB  ASP A 139     8122   5173   8503    863    893   -748       C
ATOM    422  CG  ASP A 139      22.831  73.130 -11.077  1.00 78.76           C
ANISOU  422  CG  ASP A 139    10839   7898  11189    882    931   -710       C
ATOM    423  OD1 ASP A 139      23.211  74.068 -11.831  1.00 82.72           O
ANISOU  423  OD1 ASP A 139    11383   8377  11669    916   1012   -726       O
ATOM    424  OD2 ASP A 139      21.748  73.167 -10.438  1.00 84.62           O
ANISOU  424  OD2 ASP A 139    11537   8667  11946    862    896   -664       O
ATOM    425  N   ILE A 140      25.002  69.585  -9.052  1.00 50.56           N
ANISOU  425  N   ILE A 140     7195   4310   7706    800    761   -784       N
ATOM    426  CA  ILE A 140      26.071  68.614  -8.774  1.00 48.27           C
ANISOU  426  CA  ILE A 140     6893   3993   7455    787    720   -823       C
ATOM    427  C   ILE A 140      25.526  67.189  -8.529  1.00 48.57           C
ANISOU  427  C   ILE A 140     6929   4042   7485    767    627   -796       C
ATOM    428  O   ILE A 140      26.278  66.229  -8.707  1.00 48.48           O
ANISOU  428  O   ILE A 140     6917   4003   7499    761    590   -823       O
ATOM    429  CB  ILE A 140      27.064  69.073  -7.669  1.00 51.17           C
ANISOU  429  CB  ILE A 140     7226   4344   7871    777    728   -863       C
ATOM    430  CG1 ILE A 140      27.259  70.559  -7.661  1.00 53.54           C
ANISOU  430  CG1 ILE A 140     7519   4641   8184    792    813   -878       C
ATOM    431  CG2 ILE A 140      28.417  68.374  -7.800  1.00 50.46           C
ANISOU  431  CG2 ILE A 140     7115   4199   7859    776    706   -915       C
ATOM    432  CD1 ILE A 140      28.666  70.983  -7.313  1.00 73.04           C
ANISOU  432  CD1 ILE A 140     9950   7054  10748    795    831   -941       C
ATOM    433  N   LEU A 141      24.239  67.054  -8.127  1.00 43.59           N
ANISOU  433  N   LEU A 141     6287   3440   6834    756    598   -742       N
ATOM    434  CA  LEU A 141      23.598  65.767  -7.868  1.00 44.96           C
ANISOU  434  CA  LEU A 141     6448   3614   7021    738    524   -710       C
ATOM    435  C   LEU A 141      23.574  64.873  -9.125  1.00 52.27           C
ANISOU  435  C   LEU A 141     7398   4516   7947    746    467   -721       C
ATOM    436  O   LEU A 141      23.801  63.654  -9.035  1.00 49.97           O
ANISOU  436  O   LEU A 141     7102   4212   7673    733    409   -727       O
ATOM    437  CB  LEU A 141      22.181  65.990  -7.329  1.00 45.19           C
ANISOU  437  CB  LEU A 141     6450   3656   7064    730    533   -647       C
ATOM    438  CG  LEU A 141      21.372  64.749  -6.819  1.00 48.76           C
ANISOU  438  CG  LEU A 141     6874   4093   7559    711    481   -603       C
ATOM    439  CD1 LEU A 141      22.104  63.982  -5.703  1.00 48.04           C
ANISOU  439  CD1 LEU A 141     6803   3998   7454    700    471   -614       C
ATOM    440  CD2 LEU A 141      19.988  65.172  -6.340  1.00 46.29           C
ANISOU  440  CD2 LEU A 141     6523   3770   7293    709    524   -538       C
ATOM    441  N   SER A 142      23.332  65.508 -10.299  1.00 52.08           N
ANISOU  441  N   SER A 142     7416   4478   7895    775    485   -726       N
ATOM    442  CA  SER A 142      23.296  64.873 -11.627  1.00 52.50           C
ANISOU  442  CA  SER A 142     7535   4492   7922    798    434   -741       C
ATOM    443  C   SER A 142      24.567  64.109 -11.931  1.00 56.61           C
ANISOU  443  C   SER A 142     8086   4980   8443    800    448   -786       C
ATOM    444  O   SER A 142      24.510  63.078 -12.599  1.00 58.30           O
ANISOU  444  O   SER A 142     8342   5164   8647    805    384   -793       O
ATOM    445  CB  SER A 142      23.036  65.910 -12.717  1.00 57.95           C
ANISOU  445  CB  SER A 142     8297   5161   8562    840    471   -743       C
ATOM    446  OG  SER A 142      24.089  66.854 -12.827  1.00 71.20           O
ANISOU  446  OG  SER A 142     9999   6828  10225    859    588   -776       O
ATOM    447  N   LEU A 143      25.708  64.588 -11.412  1.00 52.50           N
ANISOU  447  N   LEU A 143     7539   4455   7951    796    524   -818       N
ATOM    448  CA  LEU A 143      27.028  63.964 -11.581  1.00 52.07           C
ANISOU  448  CA  LEU A 143     7490   4356   7938    797    550   -861       C
ATOM    449  C   LEU A 143      27.176  62.650 -10.813  1.00 59.61           C
ANISOU  449  C   LEU A 143     8400   5320   8929    764    466   -859       C
ATOM    450  O   LEU A 143      27.867  61.738 -11.281  1.00 59.97           O
ANISOU  450  O   LEU A 143     8464   5324   8999    765    457   -883       O
ATOM    451  CB  LEU A 143      28.147  64.920 -11.124  1.00 51.30           C
ANISOU  451  CB  LEU A 143     7353   4238   7902    800    639   -896       C
ATOM    452  CG  LEU A 143      28.352  66.248 -11.864  1.00 54.51           C
ANISOU  452  CG  LEU A 143     7797   4617   8298    836    753   -907       C
ATOM    453  CD1 LEU A 143      29.588  66.912 -11.367  1.00 53.95           C
ANISOU  453  CD1 LEU A 143     7665   4506   8329    834    826   -948       C
ATOM    454  CD2 LEU A 143      28.490  66.043 -13.358  1.00 57.01           C
ANISOU  454  CD2 LEU A 143     8221   4871   8568    878    808   -913       C
ATOM    455  N   TYR A 144      26.554  62.569  -9.612  1.00 56.94           N
ANISOU  455  N   TYR A 144     8012   5028   8594    738    419   -828       N
ATOM    456  CA  TYR A 144      26.673  61.424  -8.700  1.00 56.00           C
ANISOU  456  CA  TYR A 144     7862   4914   8502    712    350   -821       C
ATOM    457  C   TYR A 144      25.486  60.463  -8.638  1.00 57.01           C
ANISOU  457  C   TYR A 144     7984   5057   8621    698    283   -775       C
ATOM    458  O   TYR A 144      25.664  59.302  -8.264  1.00 56.46           O
ANISOU  458  O   TYR A 144     7901   4978   8574    682    230   -773       O
ATOM    459  CB  TYR A 144      27.070  61.935  -7.297  1.00 56.75           C
ANISOU  459  CB  TYR A 144     7931   5021   8610    703    353   -825       C
ATOM    460  CG  TYR A 144      28.399  62.669  -7.300  1.00 57.88           C
ANISOU  460  CG  TYR A 144     8060   5128   8803    714    394   -880       C
ATOM    461  CD1 TYR A 144      29.599  61.973  -7.389  1.00 61.03           C
ANISOU  461  CD1 TYR A 144     8436   5475   9276    711    371   -921       C
ATOM    462  CD2 TYR A 144      28.454  64.058  -7.270  1.00 57.47           C
ANISOU  462  CD2 TYR A 144     8006   5081   8749    727    460   -890       C
ATOM    463  CE1 TYR A 144      30.818  62.638  -7.461  1.00 63.64           C
ANISOU  463  CE1 TYR A 144     8733   5750   9696    722    413   -972       C
ATOM    464  CE2 TYR A 144      29.675  64.737  -7.307  1.00 58.72           C
ANISOU  464  CE2 TYR A 144     8137   5191   8984    737    501   -942       C
ATOM    465  CZ  TYR A 144      30.857  64.018  -7.396  1.00 68.66           C
ANISOU  465  CZ  TYR A 144     9363   6389  10337    735    477   -983       C
ATOM    466  OH  TYR A 144      32.084  64.639  -7.457  1.00 70.92           O
ANISOU  466  OH  TYR A 144     9600   6604  10741    745    519  -1034       O
ATOM    467  N   VAL A 145      24.294  60.940  -9.028  1.00 50.94           N
ANISOU  467  N   VAL A 145     7216   4301   7836    705    282   -740       N
ATOM    468  CA  VAL A 145      23.018  60.223  -8.969  1.00 49.28           C
ANISOU  468  CA  VAL A 145     6978   4088   7657    693    221   -693       C
ATOM    469  C   VAL A 145      23.019  58.728  -9.385  1.00 53.21           C
ANISOU  469  C   VAL A 145     7476   4558   8182    682    140   -699       C
ATOM    470  O   VAL A 145      22.322  57.924  -8.765  1.00 53.42           O
ANISOU  470  O   VAL A 145     7459   4579   8258    664    106   -663       O
ATOM    471  CB  VAL A 145      21.863  61.088  -9.535  1.00 52.58           C
ANISOU  471  CB  VAL A 145     7392   4505   8081    707    222   -664       C
ATOM    472  CG1 VAL A 145      21.747  61.020 -11.062  1.00 52.23           C
ANISOU  472  CG1 VAL A 145     7410   4427   8007    734    166   -688       C
ATOM    473  CG2 VAL A 145      20.548  60.790  -8.843  1.00 52.66           C
ANISOU  473  CG2 VAL A 145     7336   4507   8166    690    204   -604       C
ATOM    474  N   ASN A 146      23.852  58.351 -10.365  1.00 49.45           N
ANISOU  474  N   ASN A 146     7054   4056   7678    696    126   -744       N
ATOM    475  CA  ASN A 146      23.974  56.969 -10.868  1.00 48.92           C
ANISOU  475  CA  ASN A 146     7004   3957   7628    689     56   -757       C
ATOM    476  C   ASN A 146      25.161  56.205 -10.342  1.00 52.50           C
ANISOU  476  C   ASN A 146     7445   4405   8098    675     70   -782       C
ATOM    477  O   ASN A 146      25.278  55.002 -10.609  1.00 56.31           O
ANISOU  477  O   ASN A 146     7932   4863   8600    666     17   -789       O
ATOM    478  CB  ASN A 146      23.985  56.951 -12.386  1.00 48.83           C
ANISOU  478  CB  ASN A 146     7084   3900   7568    721     27   -786       C
ATOM    479  CG  ASN A 146      22.673  57.401 -12.974  1.00 61.09           C
ANISOU  479  CG  ASN A 146     8652   5440   9118    736    -38   -761       C
ATOM    480  OD1 ASN A 146      21.602  57.026 -12.493  1.00 53.46           O
ANISOU  480  OD1 ASN A 146     7612   4476   8223    716   -102   -723       O
ATOM    481  ND2 ASN A 146      22.728  58.169 -14.058  1.00 48.89           N
ANISOU  481  ND2 ASN A 146     7204   3867   7504    777    -24   -781       N
ATOM    482  N   LYS A 147      26.016  56.862  -9.570  1.00 46.86           N
ANISOU  482  N   LYS A 147     6711   3705   7387    674    129   -797       N
ATOM    483  CA  LYS A 147      27.209  56.252  -9.009  1.00 46.21           C
ANISOU  483  CA  LYS A 147     6611   3606   7343    664    127   -825       C
ATOM    484  C   LYS A 147      27.272  56.131  -7.466  1.00 47.44           C
ANISOU  484  C   LYS A 147     6732   3781   7510    649    105   -805       C
ATOM    485  O   LYS A 147      27.992  55.256  -6.965  1.00 48.63           O
ANISOU  485  O   LYS A 147     6872   3912   7694    640     66   -818       O
ATOM    486  CB  LYS A 147      28.499  56.833  -9.653  1.00 50.59           C
ANISOU  486  CB  LYS A 147     7183   4118   7919    682    196   -875       C
ATOM    487  CG  LYS A 147      28.636  58.359  -9.651  1.00 73.57           C
ANISOU  487  CG  LYS A 147    10094   7039  10821    699    269   -885       C
ATOM    488  CD  LYS A 147      29.667  58.832 -10.683  1.00 92.55           C
ANISOU  488  CD  LYS A 147    12531   9382  13254    725    360   -926       C
ATOM    489  CE  LYS A 147      31.029  59.164 -10.101  1.00104.72           C
ANISOU  489  CE  LYS A 147    14014  10877  14900    723    398   -966       C
ATOM    490  NZ  LYS A 147      32.005  59.505 -11.170  1.00112.42           N
ANISOU  490  NZ  LYS A 147    15015  11767  15931    751    512   -999       N
ATOM    491  N   ILE A 148      26.526  56.965  -6.728  1.00 42.01           N
ANISOU  491  N   ILE A 148     6044   3124   6794    651    130   -773       N
ATOM    492  CA  ILE A 148      26.495  56.945  -5.258  1.00 42.40           C
ANISOU  492  CA  ILE A 148     6103   3178   6830    649    121   -750       C
ATOM    493  C   ILE A 148      26.329  55.522  -4.730  1.00 44.93           C
ANISOU  493  C   ILE A 148     6422   3482   7166    638     70   -726       C
ATOM    494  O   ILE A 148      25.385  54.850  -5.120  1.00 43.41           O
ANISOU  494  O   ILE A 148     6209   3291   6994    629     62   -691       O
ATOM    495  CB  ILE A 148      25.390  57.872  -4.647  1.00 46.36           C
ANISOU  495  CB  ILE A 148     6616   3701   7296    656    175   -703       C
ATOM    496  CG1 ILE A 148      25.500  59.297  -5.137  1.00 47.35           C
ANISOU  496  CG1 ILE A 148     6742   3844   7405    667    227   -725       C
ATOM    497  CG2 ILE A 148      25.453  57.848  -3.114  1.00 48.51           C
ANISOU  497  CG2 ILE A 148     6939   3960   7533    665    177   -682       C
ATOM    498  CD1 ILE A 148      24.522  60.362  -4.429  1.00 60.67           C
ANISOU  498  CD1 ILE A 148     8442   5548   9062    674    291   -681       C
ATOM    499  N   PHE A 149      27.245  55.075  -3.847  1.00 42.69           N
ANISOU  499  N   PHE A 149     6161   3176   6885    642     28   -745       N
ATOM    500  CA  PHE A 149      27.177  53.763  -3.190  1.00 41.68           C
ANISOU  500  CA  PHE A 149     6047   3027   6763    638    -17   -720       C
ATOM    501  C   PHE A 149      26.091  53.906  -2.128  1.00 49.80           C
ANISOU  501  C   PHE A 149     7121   4054   7745    650     29   -658       C
ATOM    502  O   PHE A 149      26.107  54.851  -1.344  1.00 49.58           O
ANISOU  502  O   PHE A 149     7147   4024   7666    668     57   -654       O
ATOM    503  CB  PHE A 149      28.525  53.358  -2.559  1.00 41.86           C
ANISOU  503  CB  PHE A 149     6089   3014   6803    646    -87   -761       C
ATOM    504  CG  PHE A 149      28.433  52.083  -1.751  1.00 41.95           C
ANISOU  504  CG  PHE A 149     6133   3000   6805    649   -131   -731       C
ATOM    505  CD1 PHE A 149      28.023  50.884  -2.345  1.00 44.17           C
ANISOU  505  CD1 PHE A 149     6376   3282   7125    631   -136   -711       C
ATOM    506  CD2 PHE A 149      28.714  52.077  -0.388  1.00 42.44           C
ANISOU  506  CD2 PHE A 149     6281   3029   6813    675   -169   -722       C
ATOM    507  CE1 PHE A 149      27.898  49.703  -1.591  1.00 42.73           C
ANISOU  507  CE1 PHE A 149     6223   3073   6939    635   -165   -680       C
ATOM    508  CE2 PHE A 149      28.616  50.879   0.358  1.00 44.01           C
ANISOU  508  CE2 PHE A 149     6529   3197   6995    685   -201   -689       C
ATOM    509  CZ  PHE A 149      28.196  49.711  -0.249  1.00 40.21           C
ANISOU  509  CZ  PHE A 149     5993   2723   6564    663   -191   -666       C
ATOM    510  N   LEU A 150      25.105  53.022  -2.176  1.00 48.42           N
ANISOU  510  N   LEU A 150     6926   3870   7601    641     47   -608       N
ATOM    511  CA  LEU A 150      23.944  53.089  -1.309  1.00 48.61           C
ANISOU  511  CA  LEU A 150     6981   3873   7616    653    123   -539       C
ATOM    512  C   LEU A 150      23.757  51.830  -0.469  1.00 55.92           C
ANISOU  512  C   LEU A 150     7946   4754   8548    661    126   -499       C
ATOM    513  O   LEU A 150      22.654  51.547  -0.021  1.00 57.52           O
ANISOU  513  O   LEU A 150     8149   4922   8785    667    204   -434       O
ATOM    514  CB  LEU A 150      22.698  53.421  -2.156  1.00 48.04           C
ANISOU  514  CB  LEU A 150     6832   3809   7613    638    166   -507       C
ATOM    515  CG  LEU A 150      22.663  54.832  -2.708  1.00 50.77           C
ANISOU  515  CG  LEU A 150     7166   4188   7934    640    190   -530       C
ATOM    516  CD1 LEU A 150      21.789  54.908  -3.909  1.00 50.29           C
ANISOU  516  CD1 LEU A 150     7032   4133   7945    627    174   -524       C
ATOM    517  CD2 LEU A 150      22.235  55.828  -1.651  1.00 52.62           C
ANISOU  517  CD2 LEU A 150     7458   4413   8123    661    278   -494       C
ATOM    518  N   GLY A 151      24.853  51.121  -0.226  1.00 53.41           N
ANISOU  518  N   GLY A 151     7659   4427   8207    665     48   -535       N
ATOM    519  CA  GLY A 151      24.884  49.905   0.572  1.00 53.62           C
ANISOU  519  CA  GLY A 151     7736   4410   8228    678     37   -504       C
ATOM    520  C   GLY A 151      24.351  48.691  -0.147  1.00 58.00           C
ANISOU  520  C   GLY A 151     8203   4958   8876    652     31   -484       C
ATOM    521  O   GLY A 151      23.557  48.812  -1.094  1.00 57.43           O
ANISOU  521  O   GLY A 151     8045   4901   8874    629     49   -476       O
ATOM    522  N   LYS A 152      24.791  47.497   0.322  1.00 54.77           N
ANISOU  522  N   LYS A 152     7824   4518   8469    658     -7   -478       N
ATOM    523  CA  LYS A 152      24.356  46.184  -0.157  1.00 53.38           C
ANISOU  523  CA  LYS A 152     7578   4323   8380    637    -15   -458       C
ATOM    524  C   LYS A 152      24.448  46.061  -1.697  1.00 54.52           C
ANISOU  524  C   LYS A 152     7620   4503   8593    601    -75   -505       C
ATOM    525  O   LYS A 152      23.445  45.725  -2.352  1.00 55.89           O
ANISOU  525  O   LYS A 152     7721   4663   8849    583    -62   -482       O
ATOM    526  CB  LYS A 152      22.921  45.890   0.367  1.00 56.23           C
ANISOU  526  CB  LYS A 152     7932   4633   8798    646     95   -377       C
ATOM    527  CG  LYS A 152      22.777  45.955   1.899  1.00 69.48           C
ANISOU  527  CG  LYS A 152     9749   6257  10394    693    182   -323       C
ATOM    528  CD  LYS A 152      22.198  44.669   2.520  1.00 82.42           C
ANISOU  528  CD  LYS A 152    11411   7823  12084    708    249   -260       C
ATOM    529  CE  LYS A 152      23.069  43.426   2.415  1.00 96.73           C
ANISOU  529  CE  LYS A 152    13222   9636  13897    702    155   -288       C
ATOM    530  NZ  LYS A 152      22.596  42.486   1.351  1.00103.54           N
ANISOU  530  NZ  LYS A 152    13939  10501  14901    659    128   -292       N
ATOM    531  N   ASN A 153      25.648  46.361  -2.271  1.00 46.76           N
ANISOU  531  N   ASN A 153     6638   3547   7582    595   -139   -570       N
ATOM    532  CA  ASN A 153      25.944  46.319  -3.720  1.00 46.16           C
ANISOU  532  CA  ASN A 153     6506   3488   7543    573   -179   -619       C
ATOM    533  C   ASN A 153      25.175  47.335  -4.588  1.00 49.54           C
ANISOU  533  C   ASN A 153     6909   3939   7974    569   -153   -622       C
ATOM    534  O   ASN A 153      25.178  47.174  -5.817  1.00 49.50           O
ANISOU  534  O   ASN A 153     6883   3932   7992    559   -188   -653       O
ATOM    535  CB  ASN A 153      25.716  44.912  -4.317  1.00 55.06           C
ANISOU  535  CB  ASN A 153     7593   4592   8737    554   -217   -617       C
ATOM    536  CG  ASN A 153      26.739  43.854  -4.003  1.00 86.05           C
ANISOU  536  CG  ASN A 153    11529   8496  12670    553   -259   -636       C
ATOM    537  OD1 ASN A 153      27.955  44.086  -4.063  1.00 85.28           O
ANISOU  537  OD1 ASN A 153    11447   8397  12558    558   -285   -680       O
ATOM    538  ND2 ASN A 153      26.247  42.636  -3.787  1.00 77.24           N
ANISOU  538  ND2 ASN A 153    10393   7352  11602    545   -268   -604       N
ATOM    539  N   ALA A 154      24.499  48.361  -3.984  1.00 43.83           N
ANISOU  539  N   ALA A 154     6201   3228   7226    582    -95   -589       N
ATOM    540  CA  ALA A 154      23.738  49.327  -4.774  1.00 41.49           C
ANISOU  540  CA  ALA A 154     5878   2948   6939    580    -77   -589       C
ATOM    541  C   ALA A 154      24.517  50.591  -5.074  1.00 44.65           C
ANISOU  541  C   ALA A 154     6309   3380   7278    591    -62   -632       C
ATOM    542  O   ALA A 154      24.934  51.285  -4.155  1.00 43.79           O
ANISOU  542  O   ALA A 154     6237   3280   7121    604    -30   -631       O
ATOM    543  CB  ALA A 154      22.406  49.640  -4.113  1.00 42.07           C
ANISOU  543  CB  ALA A 154     5929   3001   7054    585    -12   -523       C
ATOM    544  N   TYR A 155      24.716  50.877  -6.374  1.00 42.07           N
ANISOU  544  N   TYR A 155     5977   3058   6951    589    -85   -671       N
ATOM    545  CA  TYR A 155      25.405  52.066  -6.883  1.00 42.58           C
ANISOU  545  CA  TYR A 155     6068   3139   6972    602    -55   -711       C
ATOM    546  C   TYR A 155      24.450  52.859  -7.746  1.00 46.32           C
ANISOU  546  C   TYR A 155     6541   3620   7440    610    -46   -701       C
ATOM    547  O   TYR A 155      24.143  52.465  -8.874  1.00 45.83           O
ANISOU  547  O   TYR A 155     6490   3535   7387    612    -92   -715       O
ATOM    548  CB  TYR A 155      26.666  51.688  -7.674  1.00 44.80           C
ANISOU  548  CB  TYR A 155     6367   3397   7257    605    -68   -767       C
ATOM    549  CG  TYR A 155      27.729  51.063  -6.806  1.00 48.68           C
ANISOU  549  CG  TYR A 155     6851   3873   7773    600    -87   -781       C
ATOM    550  CD1 TYR A 155      28.715  51.840  -6.219  1.00 51.32           C
ANISOU  550  CD1 TYR A 155     7187   4202   8110    610    -71   -809       C
ATOM    551  CD2 TYR A 155      27.736  49.692  -6.550  1.00 49.90           C
ANISOU  551  CD2 TYR A 155     6992   4009   7958    587   -133   -769       C
ATOM    552  CE1 TYR A 155      29.702  51.273  -5.417  1.00 53.88           C
ANISOU  552  CE1 TYR A 155     7505   4497   8470    610   -116   -826       C
ATOM    553  CE2 TYR A 155      28.693  49.119  -5.712  1.00 51.42           C
ANISOU  553  CE2 TYR A 155     7182   4181   8174    587   -164   -781       C
ATOM    554  CZ  TYR A 155      29.682  49.914  -5.154  1.00 61.55           C
ANISOU  554  CZ  TYR A 155     8471   5452   9462    599   -163   -811       C
ATOM    555  OH  TYR A 155      30.651  49.394  -4.328  1.00 64.70           O
ANISOU  555  OH  TYR A 155     8870   5818   9897    603   -219   -827       O
ATOM    556  N   GLY A 156      23.973  53.965  -7.195  1.00 42.62           N
ANISOU  556  N   GLY A 156     6068   3174   6953    617      5   -677       N
ATOM    557  CA  GLY A 156      23.013  54.829  -7.856  1.00 42.13           C
ANISOU  557  CA  GLY A 156     5999   3115   6894    626     14   -662       C
ATOM    558  C   GLY A 156      21.601  54.540  -7.412  1.00 45.49           C
ANISOU  558  C   GLY A 156     6369   3522   7393    617      8   -602       C
ATOM    559  O   GLY A 156      21.274  53.443  -6.962  1.00 45.13           O
ANISOU  559  O   GLY A 156     6293   3451   7403    604    -14   -577       O
ATOM    560  N   ILE A 157      20.755  55.533  -7.567  1.00 42.19           N
ANISOU  560  N   ILE A 157     5933   3105   6993    625     35   -577       N
ATOM    561  CA  ILE A 157      19.357  55.516  -7.162  1.00 42.01           C
ANISOU  561  CA  ILE A 157     5842   3048   7072    619     51   -516       C
ATOM    562  C   ILE A 157      18.545  54.343  -7.699  1.00 47.60           C
ANISOU  562  C   ILE A 157     6493   3701   7893    607    -39   -503       C
ATOM    563  O   ILE A 157      17.815  53.714  -6.930  1.00 47.93           O
ANISOU  563  O   ILE A 157     6474   3700   8035    596     -6   -452       O
ATOM    564  CB  ILE A 157      18.698  56.918  -7.313  1.00 44.19           C
ANISOU  564  CB  ILE A 157     6106   3331   7352    631     95   -498       C
ATOM    565  CG1 ILE A 157      18.753  57.433  -8.756  1.00 43.86           C
ANISOU  565  CG1 ILE A 157     6100   3293   7273    648     20   -541       C
ATOM    566  CG2 ILE A 157      19.403  57.913  -6.385  1.00 43.95           C
ANISOU  566  CG2 ILE A 157     6123   3343   7233    639    198   -499       C
ATOM    567  CD1 ILE A 157      17.703  58.393  -9.104  1.00 49.53           C
ANISOU  567  CD1 ILE A 157     6783   3990   8045    659     14   -514       C
ATOM    568  N   ALA A 158      18.719  54.000  -8.985  1.00 44.87           N
ANISOU  568  N   ALA A 158     6176   3341   7531    613   -146   -549       N
ATOM    569  CA  ALA A 158      17.973  52.898  -9.590  1.00 44.40           C
ANISOU  569  CA  ALA A 158     6072   3219   7579    605   -258   -547       C
ATOM    570  C   ALA A 158      18.367  51.560  -9.002  1.00 51.17           C
ANISOU  570  C   ALA A 158     6911   4068   8463    586   -254   -542       C
ATOM    571  O   ALA A 158      17.472  50.764  -8.677  1.00 52.48           O
ANISOU  571  O   ALA A 158     6995   4177   8766    572   -276   -505       O
ATOM    572  CB  ALA A 158      18.109  52.898 -11.096  1.00 44.66           C
ANISOU  572  CB  ALA A 158     6179   3229   7560    625   -378   -601       C
ATOM    573  N   ALA A 159      19.682  51.324  -8.789  1.00 46.84           N
ANISOU  573  N   ALA A 159     6429   3564   7804    586   -219   -576       N
ATOM    574  CA  ALA A 159      20.158  50.069  -8.182  1.00 45.61           C
ANISOU  574  CA  ALA A 159     6263   3400   7666    570   -216   -571       C
ATOM    575  C   ALA A 159      19.646  49.934  -6.740  1.00 49.45           C
ANISOU  575  C   ALA A 159     6706   3875   8210    565   -124   -506       C
ATOM    576  O   ALA A 159      19.273  48.838  -6.350  1.00 53.06           O
ANISOU  576  O   ALA A 159     7120   4290   8751    554   -129   -478       O
ATOM    577  CB  ALA A 159      21.676  49.992  -8.228  1.00 45.46           C
ANISOU  577  CB  ALA A 159     6315   3420   7539    575   -200   -619       C
ATOM    578  N   ALA A 160      19.569  51.037  -5.972  1.00 43.48           N
ANISOU  578  N   ALA A 160     5968   3142   7409    577    -32   -481       N
ATOM    579  CA  ALA A 160      19.044  51.012  -4.605  1.00 43.18           C
ANISOU  579  CA  ALA A 160     5925   3077   7406    582     76   -416       C
ATOM    580  C   ALA A 160      17.525  50.783  -4.582  1.00 49.60           C
ANISOU  580  C   ALA A 160     6640   3815   8390    576    103   -356       C
ATOM    581  O   ALA A 160      17.030  50.082  -3.695  1.00 49.49           O
ANISOU  581  O   ALA A 160     6606   3746   8453    578    178   -302       O
ATOM    582  CB  ALA A 160      19.410  52.277  -3.867  1.00 43.02           C
ANISOU  582  CB  ALA A 160     5968   3092   7286    600    160   -411       C
ATOM    583  N   ALA A 161      16.789  51.343  -5.576  1.00 47.19           N
ANISOU  583  N   ALA A 161     6276   3495   8160    573     38   -366       N
ATOM    584  CA  ALA A 161      15.338  51.151  -5.712  1.00 47.65           C
ANISOU  584  CA  ALA A 161     6217   3465   8423    566     33   -317       C
ATOM    585  C   ALA A 161      15.045  49.684  -6.005  1.00 51.10           C
ANISOU  585  C   ALA A 161     6592   3842   8981    551    -47   -319       C
ATOM    586  O   ALA A 161      14.078  49.149  -5.465  1.00 50.57           O
ANISOU  586  O   ALA A 161     6433   3687   9095    545      9   -261       O
ATOM    587  CB  ALA A 161      14.780  52.038  -6.815  1.00 48.40           C
ANISOU  587  CB  ALA A 161     6278   3554   8557    571    -58   -340       C
ATOM    588  N   LYS A 162      15.923  49.019  -6.799  1.00 48.07           N
ANISOU  588  N   LYS A 162     6262   3497   8506    545   -161   -383       N
ATOM    589  CA  LYS A 162      15.824  47.596  -7.160  1.00 48.28           C
ANISOU  589  CA  LYS A 162     6247   3474   8622    530   -247   -396       C
ATOM    590  C   LYS A 162      16.211  46.672  -6.018  1.00 51.60           C
ANISOU  590  C   LYS A 162     6679   3889   9037    526   -147   -360       C
ATOM    591  O   LYS A 162      15.475  45.729  -5.739  1.00 52.00           O
ANISOU  591  O   LYS A 162     6647   3861   9249    517   -135   -323       O
ATOM    592  CB  LYS A 162      16.691  47.255  -8.393  1.00 50.56           C
ANISOU  592  CB  LYS A 162     6614   3799   8800    531   -385   -475       C
ATOM    593  CG  LYS A 162      16.415  45.869  -8.997  1.00 65.43           C
ANISOU  593  CG  LYS A 162     8456   5617  10789    517   -502   -496       C
ATOM    594  CD  LYS A 162      15.175  45.865  -9.883  1.00 86.24           C
ANISOU  594  CD  LYS A 162    11008   8160  13597    518   -633   -498       C
ATOM    595  CE  LYS A 162      14.597  44.481 -10.074  1.00114.62           C
ANISOU  595  CE  LYS A 162    14524  11667  17360    501   -724   -500       C
ATOM    596  NZ  LYS A 162      13.121  44.523 -10.313  1.00128.83           N
ANISOU  596  NZ  LYS A 162    16188  13351  19411    498   -809   -474       N
ATOM    597  N   ILE A 163      17.374  46.915  -5.389  1.00 46.09           N
ANISOU  597  N   ILE A 163     6083   3263   8165    536    -85   -374       N
ATOM    598  CA  ILE A 163      17.919  46.089  -4.296  1.00 45.06           C
ANISOU  598  CA  ILE A 163     5997   3129   7995    541     -9   -347       C
ATOM    599  C   ILE A 163      17.055  46.100  -3.017  1.00 52.59           C
ANISOU  599  C   ILE A 163     6936   4015   9031    557    145   -262       C
ATOM    600  O   ILE A 163      16.805  45.039  -2.455  1.00 52.72           O
ANISOU  600  O   ILE A 163     6934   3973   9126    558    192   -224       O
ATOM    601  CB  ILE A 163      19.442  46.391  -4.054  1.00 44.77           C
ANISOU  601  CB  ILE A 163     6072   3170   7767    551    -18   -394       C
ATOM    602  CG1 ILE A 163      20.287  45.732  -5.189  1.00 43.81           C
ANISOU  602  CG1 ILE A 163     5957   3074   7613    536   -138   -464       C
ATOM    603  CG2 ILE A 163      19.943  46.030  -2.619  1.00 40.87           C
ANISOU  603  CG2 ILE A 163     5656   2667   7206    571     71   -358       C
ATOM    604  CD1 ILE A 163      21.747  46.157  -5.323  1.00 47.84           C
ANISOU  604  CD1 ILE A 163     6547   3644   7985    543   -156   -519       C
ATOM    605  N   TYR A 164      16.649  47.279  -2.546  1.00 50.34           N
ANISOU  605  N   TYR A 164     6671   3731   8723    573    236   -231       N
ATOM    606  CA  TYR A 164      15.894  47.415  -1.310  1.00 51.92           C
ANISOU  606  CA  TYR A 164     6888   3857   8981    596    409   -149       C
ATOM    607  C   TYR A 164      14.391  47.193  -1.432  1.00 57.14           C
ANISOU  607  C   TYR A 164     7408   4407   9894    588    467    -89       C
ATOM    608  O   TYR A 164      13.761  46.767  -0.459  1.00 56.91           O
ANISOU  608  O   TYR A 164     7378   4284   9959    607    622    -14       O
ATOM    609  CB  TYR A 164      16.148  48.802  -0.702  1.00 53.73           C
ANISOU  609  CB  TYR A 164     7214   4126   9074    619    491   -142       C
ATOM    610  CG  TYR A 164      17.554  49.015  -0.198  1.00 56.35           C
ANISOU  610  CG  TYR A 164     7690   4531   9189    636    462   -186       C
ATOM    611  CD1 TYR A 164      17.983  48.446   0.998  1.00 60.19           C
ANISOU  611  CD1 TYR A 164     8294   4983   9593    666    532   -156       C
ATOM    612  CD2 TYR A 164      18.445  49.830  -0.884  1.00 55.43           C
ANISOU  612  CD2 TYR A 164     7598   4503   8961    628    367   -257       C
ATOM    613  CE1 TYR A 164      19.285  48.635   1.464  1.00 60.99           C
ANISOU  613  CE1 TYR A 164     8522   5135   9515    684    475   -202       C
ATOM    614  CE2 TYR A 164      19.756  50.004  -0.439  1.00 54.76           C
ANISOU  614  CE2 TYR A 164     7622   4466   8718    642    329   -301       C
ATOM    615  CZ  TYR A 164      20.162  49.424   0.746  1.00 60.13           C
ANISOU  615  CZ  TYR A 164     8409   5110   9329    669    372   -275       C
ATOM    616  OH  TYR A 164      21.419  49.656   1.234  1.00 62.34           O
ANISOU  616  OH  TYR A 164     8794   5419   9471    687    313   -321       O
ATOM    617  N   TYR A 165      13.804  47.542  -2.587  1.00 54.40           N
ANISOU  617  N   TYR A 165     6950   4057   9664    566    350   -119       N
ATOM    618  CA  TYR A 165      12.350  47.484  -2.750  1.00 55.12           C
ANISOU  618  CA  TYR A 165     6889   4029  10027    559    383    -67       C
ATOM    619  C   TYR A 165      11.814  46.706  -3.955  1.00 59.54           C
ANISOU  619  C   TYR A 165     7317   4537  10768    533    201   -104       C
ATOM    620  O   TYR A 165      10.608  46.464  -4.002  1.00 60.58           O
ANISOU  620  O   TYR A 165     7305   4545  11167    527    220    -60       O
ATOM    621  CB  TYR A 165      11.732  48.916  -2.676  1.00 54.59           C
ANISOU  621  CB  TYR A 165     6803   3954   9987    569    453    -39       C
ATOM    622  CG  TYR A 165      12.144  49.713  -1.450  1.00 54.71           C
ANISOU  622  CG  TYR A 165     6954   3998   9836    599    635      0       C
ATOM    623  CD1 TYR A 165      11.696  49.360  -0.179  1.00 57.42           C
ANISOU  623  CD1 TYR A 165     7333   4245  10238    624    841     83       C
ATOM    624  CD2 TYR A 165      12.992  50.817  -1.560  1.00 53.40           C
ANISOU  624  CD2 TYR A 165     6894   3942   9454    606    605    -46       C
ATOM    625  CE1 TYR A 165      12.070  50.092   0.953  1.00 56.51           C
ANISOU  625  CE1 TYR A 165     7376   4142   9952    660    999    116       C
ATOM    626  CE2 TYR A 165      13.391  51.543  -0.431  1.00 53.10           C
ANISOU  626  CE2 TYR A 165     6991   3921   9263    636    751    -17       C
ATOM    627  CZ  TYR A 165      12.928  51.175   0.824  1.00 60.09           C
ANISOU  627  CZ  TYR A 165     7931   4709  10191    664    941     62       C
ATOM    628  OH  TYR A 165      13.297  51.889   1.946  1.00 57.77           O
ANISOU  628  OH  TYR A 165     7801   4417   9731    702   1077     89       O
ATOM    629  N   ASN A 166      12.681  46.321  -4.919  1.00 55.46           N
ANISOU  629  N   ASN A 166     6852   4098  10124    521     27   -185       N
ATOM    630  CA  ASN A 166      12.276  45.615  -6.149  1.00 56.48           C
ANISOU  630  CA  ASN A 166     6897   4176  10386    503   -170   -233       C
ATOM    631  C   ASN A 166      11.364  46.531  -6.989  1.00 62.49           C
ANISOU  631  C   ASN A 166     7582   4892  11268    506   -271   -243       C
ATOM    632  O   ASN A 166      10.379  46.110  -7.603  1.00 62.05           O
ANISOU  632  O   ASN A 166     7403   4727  11444    497   -391   -245       O
ATOM    633  CB  ASN A 166      11.641  44.250  -5.818  1.00 61.47           C
ANISOU  633  CB  ASN A 166     7420   4697  11238    491   -150   -197       C
ATOM    634  CG  ASN A 166      11.651  43.217  -6.907  1.00 84.67           C
ANISOU  634  CG  ASN A 166    10319   7602  14249    474   -353   -258       C
ATOM    635  OD1 ASN A 166      12.432  43.248  -7.855  1.00 80.09           O
ANISOU  635  OD1 ASN A 166     9832   7093  13506    474   -499   -333       O
ATOM    636  ND2 ASN A 166      10.781  42.249  -6.768  1.00 82.74           N
ANISOU  636  ND2 ASN A 166     9943   7236  14260    462   -353   -226       N
ATOM    637  N   LYS A 167      11.715  47.828  -6.978  1.00 59.65           N
ANISOU  637  N   LYS A 167     7299   4610  10753    520   -227   -250       N
ATOM    638  CA  LYS A 167      10.977  48.883  -7.660  1.00 59.24           C
ANISOU  638  CA  LYS A 167     7201   4531  10778    528   -302   -255       C
ATOM    639  C   LYS A 167      11.870  49.647  -8.618  1.00 62.88           C
ANISOU  639  C   LYS A 167     7794   5093  11004    542   -410   -327       C
ATOM    640  O   LYS A 167      13.100  49.576  -8.529  1.00 61.25           O
ANISOU  640  O   LYS A 167     7709   4983  10579    544   -380   -363       O
ATOM    641  CB  LYS A 167      10.388  49.883  -6.628  1.00 60.90           C
ANISOU  641  CB  LYS A 167     7372   4719  11047    537   -104   -179       C
ATOM    642  CG  LYS A 167       9.181  49.388  -5.871  1.00 66.28           C
ANISOU  642  CG  LYS A 167     7904   5258  12022    531     15    -98       C
ATOM    643  CD  LYS A 167       8.622  50.508  -4.997  1.00 69.30           C
ANISOU  643  CD  LYS A 167     8270   5613  12447    546    212    -27       C
ATOM    644  CE  LYS A 167       7.296  50.153  -4.355  1.00 57.67           C
ANISOU  644  CE  LYS A 167     6631   3968  11314    545    341     59       C
ATOM    645  NZ  LYS A 167       6.693  51.302  -3.630  1.00 65.08           N
ANISOU  645  NZ  LYS A 167     7558   4866  12302    562    535    127       N
ATOM    646  N   SER A 168      11.225  50.420  -9.513  1.00 61.03           N
ANISOU  646  N   SER A 168     7535   4823  10831    554   -528   -345       N
ATOM    647  CA  SER A 168      11.881  51.378 -10.395  1.00 59.35           C
ANISOU  647  CA  SER A 168     7451   4687  10414    576   -601   -401       C
ATOM    648  C   SER A 168      11.803  52.678  -9.588  1.00 63.69           C
ANISOU  648  C   SER A 168     7996   5282  10921    582   -433   -354       C
ATOM    649  O   SER A 168      11.016  52.757  -8.628  1.00 64.62           O
ANISOU  649  O   SER A 168     8008   5344  11200    573   -306   -284       O
ATOM    650  CB  SER A 168      11.142  51.493 -11.727  1.00 61.63           C
ANISOU  650  CB  SER A 168     7729   4894  10794    594   -824   -440       C
ATOM    651  OG  SER A 168       9.875  52.115 -11.604  1.00 72.03           O
ANISOU  651  OG  SER A 168     8914   6125  12330    596   -834   -393       O
ATOM    652  N   ILE A 169      12.615  53.685  -9.938  1.00 59.10           N
ANISOU  652  N   ILE A 169     7534   4791  10132    600   -416   -390       N
ATOM    653  CA  ILE A 169      12.610  54.956  -9.203  1.00 56.70           C
ANISOU  653  CA  ILE A 169     7236   4533   9776    607   -263   -352       C
ATOM    654  C   ILE A 169      11.257  55.666  -9.181  1.00 62.98           C
ANISOU  654  C   ILE A 169     7913   5246  10771    610   -261   -302       C
ATOM    655  O   ILE A 169      10.904  56.265  -8.165  1.00 64.26           O
ANISOU  655  O   ILE A 169     8031   5401  10983    607    -94   -243       O
ATOM    656  CB  ILE A 169      13.819  55.865  -9.506  1.00 57.46           C
ANISOU  656  CB  ILE A 169     7470   4734   9628    624   -232   -401       C
ATOM    657  CG1 ILE A 169      13.854  56.274 -10.998  1.00 56.90           C
ANISOU  657  CG1 ILE A 169     7471   4653   9494    650   -388   -456       C
ATOM    658  CG2 ILE A 169      15.116  55.158  -9.053  1.00 57.49           C
ANISOU  658  CG2 ILE A 169     7553   4801   9488    615   -182   -430       C
ATOM    659  CD1 ILE A 169      14.705  57.481 -11.326  1.00 56.05           C
ANISOU  659  CD1 ILE A 169     7474   4619   9201    674   -330   -487       C
ATOM    660  N   ASN A 170      10.467  55.531 -10.251  1.00 60.20           N
ANISOU  660  N   ASN A 170     7510   4813  10549    619   -447   -323       N
ATOM    661  CA  ASN A 170       9.142  56.166 -10.295  1.00 61.46           C
ANISOU  661  CA  ASN A 170     7540   4875  10936    623   -471   -278       C
ATOM    662  C   ASN A 170       8.067  55.409  -9.490  1.00 65.61           C
ANISOU  662  C   ASN A 170     7887   5278  11762    601   -404   -210       C
ATOM    663  O   ASN A 170       7.000  55.972  -9.205  1.00 66.17           O
ANISOU  663  O   ASN A 170     7831   5259  12051    601   -358   -155       O
ATOM    664  CB  ASN A 170       8.704  56.444 -11.727  1.00 66.08           C
ANISOU  664  CB  ASN A 170     8151   5407  11548    650   -712   -328       C
ATOM    665  CG  ASN A 170       9.690  57.302 -12.483  1.00100.19           C
ANISOU  665  CG  ASN A 170    12654   9827  15585    680   -739   -384       C
ATOM    666  OD1 ASN A 170      10.595  56.802 -13.172  1.00101.82           O
ANISOU  666  OD1 ASN A 170    12998  10077  15614    693   -817   -445       O
ATOM    667  ND2 ASN A 170       9.568  58.615 -12.327  1.00 90.28           N
ANISOU  667  ND2 ASN A 170    11406   8604  14291    693   -654   -360       N
ATOM    668  N   GLU A 171       8.366  54.155  -9.085  1.00 60.07           N
ANISOU  668  N   GLU A 171     7176   4567  11082    584   -380   -209       N
ATOM    669  CA  GLU A 171       7.461  53.348  -8.275  1.00 60.07           C
ANISOU  669  CA  GLU A 171     7020   4444  11358    566   -286   -142       C
ATOM    670  C   GLU A 171       7.644  53.618  -6.771  1.00 61.48           C
ANISOU  670  C   GLU A 171     7223   4649  11487    565      1    -70       C
ATOM    671  O   GLU A 171       6.786  53.211  -5.982  1.00 61.54           O
ANISOU  671  O   GLU A 171     7114   4539  11729    560    136      2       O
ATOM    672  CB  GLU A 171       7.640  51.847  -8.577  1.00 62.04           C
ANISOU  672  CB  GLU A 171     7252   4657  11663    552   -400   -175       C
ATOM    673  CG  GLU A 171       7.098  51.407  -9.928  1.00 72.18           C
ANISOU  673  CG  GLU A 171     8486   5857  13085    556   -684   -232       C
ATOM    674  CD  GLU A 171       7.356  49.957 -10.305  1.00 83.64           C
ANISOU  674  CD  GLU A 171     9939   7277  14564    544   -807   -274       C
ATOM    675  OE1 GLU A 171       8.443  49.431  -9.970  1.00 84.54           O
ANISOU  675  OE1 GLU A 171    10166   7491  14464    538   -729   -292       O
ATOM    676  OE2 GLU A 171       6.485  49.357 -10.979  1.00 67.91           O
ANISOU  676  OE2 GLU A 171     7837   5153  12813    541   -998   -292       O
ATOM    677  N   LEU A 172       8.758  54.283  -6.370  1.00 55.98           N
ANISOU  677  N   LEU A 172     6687   4089  10495    575     94    -90       N
ATOM    678  CA  LEU A 172       9.060  54.561  -4.957  1.00 55.28           C
ANISOU  678  CA  LEU A 172     6666   4025  10315    583    338    -34       C
ATOM    679  C   LEU A 172       8.082  55.517  -4.296  1.00 63.00           C
ANISOU  679  C   LEU A 172     7574   4924  11440    593    505     41       C
ATOM    680  O   LEU A 172       7.532  56.415  -4.956  1.00 64.29           O
ANISOU  680  O   LEU A 172     7678   5074  11676    596    434     35       O
ATOM    681  CB  LEU A 172      10.477  55.113  -4.767  1.00 53.65           C
ANISOU  681  CB  LEU A 172     6637   3966   9781    593    361    -84       C
ATOM    682  CG  LEU A 172      11.664  54.260  -5.197  1.00 56.49           C
ANISOU  682  CG  LEU A 172     7088   4406   9969    586    249   -152       C
ATOM    683  CD1 LEU A 172      12.908  55.016  -5.000  1.00 55.06           C
ANISOU  683  CD1 LEU A 172     7049   4343   9528    597    282   -194       C
ATOM    684  CD2 LEU A 172      11.772  52.956  -4.410  1.00 58.95           C
ANISOU  684  CD2 LEU A 172     7398   4676  10327    580    316   -122       C
ATOM    685  N   SER A 173       7.881  55.335  -2.972  1.00 58.55           N
ANISOU  685  N   SER A 173     7032   4300  10912    604    735    115       N
ATOM    686  CA  SER A 173       7.043  56.220  -2.163  1.00 57.33           C
ANISOU  686  CA  SER A 173     6844   4062  10878    620    943    195       C
ATOM    687  C   SER A 173       7.948  57.355  -1.662  1.00 62.11           C
ANISOU  687  C   SER A 173     7625   4788  11187    638   1028    176       C
ATOM    688  O   SER A 173       9.170  57.261  -1.802  1.00 61.99           O
ANISOU  688  O   SER A 173     7739   4897  10916    638    943    109       O
ATOM    689  CB  SER A 173       6.421  55.452  -1.000  1.00 58.33           C
ANISOU  689  CB  SER A 173     6943   4050  11170    632   1166    283       C
ATOM    690  OG  SER A 173       7.329  55.168   0.051  1.00 61.13           O
ANISOU  690  OG  SER A 173     7490   4458  11280    655   1299    291       O
ATOM    691  N   ILE A 174       7.367  58.425  -1.094  1.00 59.87           N
ANISOU  691  N   ILE A 174     7340   4456  10951    653   1195    232       N
ATOM    692  CA  ILE A 174       8.132  59.560  -0.545  1.00 58.32           C
ANISOU  692  CA  ILE A 174     7307   4355  10497    672   1285    217       C
ATOM    693  C   ILE A 174       9.048  59.082   0.604  1.00 61.18           C
ANISOU  693  C   ILE A 174     7859   4748  10637    695   1394    219       C
ATOM    694  O   ILE A 174      10.228  59.442   0.636  1.00 60.14           O
ANISOU  694  O   ILE A 174     7864   4737  10250    700   1325    155       O
ATOM    695  CB  ILE A 174       7.197  60.751  -0.181  1.00 61.09           C
ANISOU  695  CB  ILE A 174     7610   4628  10975    685   1449    283       C
ATOM    696  CG1 ILE A 174       6.690  61.429  -1.470  1.00 60.24           C
ANISOU  696  CG1 ILE A 174     7365   4540  10982    667   1278    250       C
ATOM    697  CG2 ILE A 174       7.888  61.769   0.741  1.00 61.79           C
ANISOU  697  CG2 ILE A 174     7889   4772  10815    712   1604    288       C
ATOM    698  CD1 ILE A 174       5.454  62.327  -1.328  1.00 65.37           C
ANISOU  698  CD1 ILE A 174     7894   5075  11869    673   1404    322       C
ATOM    699  N   ALA A 175       8.516  58.196   1.474  1.00 57.21           N
ANISOU  699  N   ALA A 175     7360   4125  10250    710   1548    289       N
ATOM    700  CA  ALA A 175       9.220  57.583   2.594  1.00 55.58           C
ANISOU  700  CA  ALA A 175     7341   3917   9862    740   1652    301       C
ATOM    701  C   ALA A 175      10.406  56.725   2.108  1.00 57.24           C
ANISOU  701  C   ALA A 175     7598   4240   9909    724   1450    218       C
ATOM    702  O   ALA A 175      11.469  56.735   2.738  1.00 56.39           O
ANISOU  702  O   ALA A 175     7669   4197   9561    745   1447    185       O
ATOM    703  CB  ALA A 175       8.254  56.725   3.389  1.00 57.54           C
ANISOU  703  CB  ALA A 175     7556   3992  10314    761   1855    398       C
ATOM    704  N   GLN A 176      10.235  56.004   0.986  1.00 52.50           N
ANISOU  704  N   GLN A 176     6846   3655   9448    689   1276    182       N
ATOM    705  CA  GLN A 176      11.290  55.159   0.428  1.00 51.41           C
ANISOU  705  CA  GLN A 176     6743   3611   9180    673   1095    106       C
ATOM    706  C   GLN A 176      12.412  55.992  -0.163  1.00 56.14           C
ANISOU  706  C   GLN A 176     7418   4351   9560    667    962     21       C
ATOM    707  O   GLN A 176      13.591  55.711   0.081  1.00 56.23           O
ANISOU  707  O   GLN A 176     7547   4435   9383    673    907    -27       O
ATOM    708  CB  GLN A 176      10.719  54.160  -0.569  1.00 52.53           C
ANISOU  708  CB  GLN A 176     6717   3708   9533    643    958     94       C
ATOM    709  CG  GLN A 176       9.873  53.109   0.134  1.00 58.06           C
ANISOU  709  CG  GLN A 176     7354   4266  10438    651   1095    172       C
ATOM    710  CD  GLN A 176       9.030  52.292  -0.796  1.00 73.25           C
ANISOU  710  CD  GLN A 176     9082   6112  12636    622    972    170       C
ATOM    711  OE1 GLN A 176       8.504  52.775  -1.796  1.00 69.46           O
ANISOU  711  OE1 GLN A 176     8485   5628  12279    604    839    143       O
ATOM    712  NE2 GLN A 176       8.859  51.028  -0.473  1.00 69.41           N
ANISOU  712  NE2 GLN A 176     8561   5550  12260    621   1007    197       N
ATOM    713  N   MET A 177      12.036  57.057  -0.888  1.00 52.66           N
ANISOU  713  N   MET A 177     6912   3935   9160    658    923      8       N
ATOM    714  CA  MET A 177      12.925  58.048  -1.484  1.00 50.35           C
ANISOU  714  CA  MET A 177     6680   3757   8693    657    831    -62       C
ATOM    715  C   MET A 177      13.773  58.708  -0.388  1.00 55.23           C
ANISOU  715  C   MET A 177     7463   4415   9107    682    934    -67       C
ATOM    716  O   MET A 177      14.995  58.823  -0.540  1.00 54.96           O
ANISOU  716  O   MET A 177     7511   4466   8904    683    847   -135       O
ATOM    717  CB  MET A 177      12.096  59.101  -2.223  1.00 52.32           C
ANISOU  717  CB  MET A 177     6834   3994   9053    652    814    -52       C
ATOM    718  CG  MET A 177      11.699  58.682  -3.618  1.00 55.56           C
ANISOU  718  CG  MET A 177     7129   4394   9588    634    631    -86       C
ATOM    719  SD  MET A 177      10.559  59.877  -4.334  1.00 59.79           S
ANISOU  719  SD  MET A 177     7554   4884  10281    636    612    -61       S
ATOM    720  CE  MET A 177      10.084  59.041  -5.770  1.00 57.36           C
ANISOU  720  CE  MET A 177     7143   4532  10121    624    375   -100       C
ATOM    721  N   ALA A 178      13.130  59.090   0.737  1.00 51.90           N
ANISOU  721  N   ALA A 178     7093   3915   8711    706   1120      4       N
ATOM    722  CA  ALA A 178      13.811  59.686   1.893  1.00 51.29           C
ANISOU  722  CA  ALA A 178     7199   3849   8440    740   1218      4       C
ATOM    723  C   ALA A 178      14.783  58.684   2.558  1.00 56.10           C
ANISOU  723  C   ALA A 178     7935   4466   8915    755   1177    -20       C
ATOM    724  O   ALA A 178      15.855  59.088   2.998  1.00 54.31           O
ANISOU  724  O   ALA A 178     7842   4290   8504    772   1133    -70       O
ATOM    725  CB  ALA A 178      12.793  60.193   2.899  1.00 52.34           C
ANISOU  725  CB  ALA A 178     7374   3871   8640    768   1440     93       C
ATOM    726  N   MET A 179      14.414  57.383   2.597  1.00 55.45           N
ANISOU  726  N   MET A 179     7802   4327   8939    750   1180     12       N
ATOM    727  CA  MET A 179      15.226  56.301   3.165  1.00 56.02           C
ANISOU  727  CA  MET A 179     7979   4397   8910    764   1139     -4       C
ATOM    728  C   MET A 179      16.573  56.171   2.420  1.00 57.18           C
ANISOU  728  C   MET A 179     8126   4657   8943    743    939   -102       C
ATOM    729  O   MET A 179      17.641  56.228   3.065  1.00 56.22           O
ANISOU  729  O   MET A 179     8143   4560   8656    765    897   -140       O
ATOM    730  CB  MET A 179      14.437  54.989   3.176  1.00 60.02           C
ANISOU  730  CB  MET A 179     8401   4816   9589    758   1189     53       C
ATOM    731  CG  MET A 179      15.206  53.780   3.774  1.00 66.17           C
ANISOU  731  CG  MET A 179     9287   5583  10272    776   1156     44       C
ATOM    732  SD  MET A 179      15.863  54.014   5.452  1.00 72.68           S
ANISOU  732  SD  MET A 179    10396   6357  10860    844   1265     66       S
ATOM    733  CE  MET A 179      14.373  53.826   6.430  1.00 71.52           C
ANISOU  733  CE  MET A 179    10285   6037  10852    884   1550    194       C
ATOM    734  N   ILE A 180      16.507  56.069   1.056  1.00 50.36           N
ANISOU  734  N   ILE A 180     7113   3846   8174    704    817   -142       N
ATOM    735  CA  ILE A 180      17.659  55.995   0.147  1.00 47.03           C
ANISOU  735  CA  ILE A 180     6680   3514   7674    685    654   -229       C
ATOM    736  C   ILE A 180      18.499  57.287   0.250  1.00 51.63           C
ANISOU  736  C   ILE A 180     7340   4158   8120    696    642   -278       C
ATOM    737  O   ILE A 180      19.725  57.211   0.252  1.00 51.44           O
ANISOU  737  O   ILE A 180     7372   4175   7997    698    556   -339       O
ATOM    738  CB  ILE A 180      17.178  55.675  -1.290  1.00 48.17           C
ANISOU  738  CB  ILE A 180     6682   3675   7947    653    553   -249       C
ATOM    739  CG1 ILE A 180      16.578  54.250  -1.360  1.00 49.01           C
ANISOU  739  CG1 ILE A 180     6714   3716   8191    641    538   -214       C
ATOM    740  CG2 ILE A 180      18.292  55.845  -2.322  1.00 45.82           C
ANISOU  740  CG2 ILE A 180     6391   3456   7563    642    421   -334       C
ATOM    741  CD1 ILE A 180      15.821  53.862  -2.726  1.00 49.97           C
ANISOU  741  CD1 ILE A 180     6700   3823   8464    615    420   -231       C
ATOM    742  N   ALA A 181      17.832  58.459   0.380  1.00 49.53           N
ANISOU  742  N   ALA A 181     7069   3883   7866    704    731   -250       N
ATOM    743  CA  ALA A 181      18.465  59.778   0.522  1.00 49.44           C
ANISOU  743  CA  ALA A 181     7123   3918   7745    716    737   -290       C
ATOM    744  C   ALA A 181      19.342  59.915   1.762  1.00 55.13           C
ANISOU  744  C   ALA A 181     8005   4623   8321    747    751   -307       C
ATOM    745  O   ALA A 181      20.186  60.810   1.797  1.00 52.70           O
ANISOU  745  O   ALA A 181     7744   4352   7928    754    711   -361       O
ATOM    746  CB  ALA A 181      17.413  60.858   0.554  1.00 50.36           C
ANISOU  746  CB  ALA A 181     7204   4012   7919    720    847   -243       C
ATOM    747  N   GLY A 182      19.130  59.042   2.758  1.00 53.95           N
ANISOU  747  N   GLY A 182     7943   4406   8148    770    804   -262       N
ATOM    748  CA  GLY A 182      19.851  59.077   4.026  1.00 54.62           C
ANISOU  748  CA  GLY A 182     8214   4453   8085    812    807   -273       C
ATOM    749  C   GLY A 182      21.047  58.165   4.122  1.00 59.41           C
ANISOU  749  C   GLY A 182     8865   5073   8636    814    666   -327       C
ATOM    750  O   GLY A 182      21.819  58.233   5.081  1.00 61.07           O
ANISOU  750  O   GLY A 182     9230   5248   8724    851    623   -351       O
ATOM    751  N   LEU A 183      21.198  57.314   3.138  1.00 55.06           N
ANISOU  751  N   LEU A 183     8185   4561   8176    779    587   -347       N
ATOM    752  CA  LEU A 183      22.262  56.338   3.061  1.00 54.86           C
ANISOU  752  CA  LEU A 183     8169   4546   8130    774    460   -395       C
ATOM    753  C   LEU A 183      23.633  56.857   2.613  1.00 64.37           C
ANISOU  753  C   LEU A 183     9357   5797   9304    765    332   -485       C
ATOM    754  O   LEU A 183      24.608  56.277   3.073  1.00 65.49           O
ANISOU  754  O   LEU A 183     9558   5918   9407    778    236   -521       O
ATOM    755  CB  LEU A 183      21.822  55.151   2.168  1.00 53.39           C
ANISOU  755  CB  LEU A 183     7854   4370   8063    741    438   -378       C
ATOM    756  CG  LEU A 183      20.530  54.411   2.570  1.00 56.40           C
ANISOU  756  CG  LEU A 183     8220   4685   8522    747    554   -292       C
ATOM    757  CD1 LEU A 183      20.153  53.375   1.551  1.00 55.55           C
ANISOU  757  CD1 LEU A 183     7974   4588   8545    712    502   -291       C
ATOM    758  CD2 LEU A 183      20.667  53.754   3.905  1.00 55.53           C
ANISOU  758  CD2 LEU A 183     8266   4502   8329    790    604   -254       C
ATOM    759  N   PRO A 184      23.786  57.840   1.677  1.00 64.17           N
ANISOU  759  N   PRO A 184     9244   5825   9314    744    326   -522       N
ATOM    760  CA  PRO A 184      25.142  58.196   1.197  1.00 64.47           C
ANISOU  760  CA  PRO A 184     9252   5887   9356    736    223   -605       C
ATOM    761  C   PRO A 184      26.240  58.469   2.224  1.00 69.75           C
ANISOU  761  C   PRO A 184    10029   6514   9958    765    141   -651       C
ATOM    762  O   PRO A 184      27.330  57.942   2.055  1.00 68.00           O
ANISOU  762  O   PRO A 184     9783   6279   9775    761     35   -703       O
ATOM    763  CB  PRO A 184      24.888  59.399   0.282  1.00 66.35           C
ANISOU  763  CB  PRO A 184     9417   6168   9624    722    273   -620       C
ATOM    764  CG  PRO A 184      23.506  59.233  -0.178  1.00 70.76           C
ANISOU  764  CG  PRO A 184     9921   6738  10228    709    353   -556       C
ATOM    765  CD  PRO A 184      22.759  58.633   0.964  1.00 66.33           C
ANISOU  765  CD  PRO A 184     9438   6126   9639    728    413   -491       C
ATOM    766  N   LYS A 185      25.939  59.285   3.271  1.00 70.77           N
ANISOU  766  N   LYS A 185    10282   6610   9997    798    184   -633       N
ATOM    767  CA  LYS A 185      26.823  59.711   4.370  1.00 71.98           C
ANISOU  767  CA  LYS A 185    10572   6707  10070    836     94   -677       C
ATOM    768  C   LYS A 185      27.582  58.543   5.015  1.00 78.43           C
ANISOU  768  C   LYS A 185    11464   7470  10865    857    -26   -693       C
ATOM    769  O   LYS A 185      28.807  58.620   5.141  1.00 78.94           O
ANISOU  769  O   LYS A 185    11530   7504  10960    864   -168   -764       O
ATOM    770  CB  LYS A 185      26.036  60.511   5.419  1.00 74.54           C
ANISOU  770  CB  LYS A 185    11050   6991  10280    875    189   -633       C
ATOM    771  CG  LYS A 185      26.855  61.629   6.073  1.00 83.99           C
ANISOU  771  CG  LYS A 185    12344   8150  11418    903    106   -697       C
ATOM    772  CD  LYS A 185      25.992  62.685   6.793  1.00 86.16           C
ANISOU  772  CD  LYS A 185    12747   8399  11592    934    228   -657       C
ATOM    773  CE  LYS A 185      25.586  62.294   8.198  1.00 97.37           C
ANISOU  773  CE  LYS A 185    14407   9726  12864    994    261   -610       C
ATOM    774  NZ  LYS A 185      24.328  62.966   8.628  1.00101.71           N
ANISOU  774  NZ  LYS A 185    15034  10254  13358   1012    464   -529       N
ATOM    775  N   ALA A 186      26.863  57.446   5.372  1.00 75.63           N
ANISOU  775  N   ALA A 186    11159   7096  10481    866     30   -628       N
ATOM    776  CA  ALA A 186      27.425  56.217   5.956  1.00 75.65           C
ANISOU  776  CA  ALA A 186    11235   7048  10459    888    -66   -630       C
ATOM    777  C   ALA A 186      26.516  55.032   5.616  1.00 78.44           C
ANISOU  777  C   ALA A 186    11533   7416  10857    870     26   -561       C
ATOM    778  O   ALA A 186      25.581  54.755   6.366  1.00 78.64           O
ANISOU  778  O   ALA A 186    11666   7395  10820    899    138   -489       O
ATOM    779  CB  ALA A 186      27.576  56.358   7.468  1.00 77.51           C
ANISOU  779  CB  ALA A 186    11713   7192  10546    955   -105   -622       C
ATOM    780  N   PRO A 187      26.747  54.337   4.478  1.00 74.43           N
ANISOU  780  N   PRO A 187    10860   6957  10464    824    -10   -581       N
ATOM    781  CA  PRO A 187      25.845  53.235   4.078  1.00 74.60           C
ANISOU  781  CA  PRO A 187    10816   6985  10542    804     66   -521       C
ATOM    782  C   PRO A 187      25.898  51.942   4.910  1.00 82.11           C
ANISOU  782  C   PRO A 187    11866   7877  11457    832     47   -487       C
ATOM    783  O   PRO A 187      25.698  50.850   4.378  1.00 81.14           O
ANISOU  783  O   PRO A 187    11657   7762  11409    808     47   -469       O
ATOM    784  CB  PRO A 187      26.180  53.019   2.592  1.00 74.93           C
ANISOU  784  CB  PRO A 187    10681   7090  10699    753     21   -564       C
ATOM    785  CG  PRO A 187      27.068  54.154   2.202  1.00 78.63           C
ANISOU  785  CG  PRO A 187    11119   7583  11174    747    -34   -632       C
ATOM    786  CD  PRO A 187      27.764  54.580   3.443  1.00 74.93           C
ANISOU  786  CD  PRO A 187    10790   7061  10619    790   -102   -656       C
ATOM    787  N   SER A 188      26.138  52.070   6.224  1.00 83.02           N
ANISOU  787  N   SER A 188    12176   7921  11446    889     31   -475       N
ATOM    788  CA  SER A 188      26.187  50.958   7.186  1.00 84.85           C
ANISOU  788  CA  SER A 188    12551   8077  11611    933     19   -438       C
ATOM    789  C   SER A 188      25.615  51.398   8.541  1.00 90.57           C
ANISOU  789  C   SER A 188    13512   8715  12187   1002    118   -384       C
ATOM    790  O   SER A 188      24.810  50.673   9.126  1.00 91.20           O
ANISOU  790  O   SER A 188    13679   8732  12240   1032    246   -307       O
ATOM    791  CB  SER A 188      27.595  50.383   7.303  1.00 87.68           C
ANISOU  791  CB  SER A 188    12927   8418  11969    941   -175   -505       C
ATOM    792  OG  SER A 188      27.948  49.727   6.095  1.00 91.76           O
ANISOU  792  OG  SER A 188    13244   8996  12625    882   -221   -536       O
ATOM    793  N   LYS A 189      25.970  52.613   8.995  1.00 87.69           N
ANISOU  793  N   LYS A 189    13249   8337  11733   1028     76   -422       N
ATOM    794  CA  LYS A 189      25.432  53.215  10.223  1.00 89.14           C
ANISOU  794  CA  LYS A 189    13677   8432  11761   1097    175   -377       C
ATOM    795  C   LYS A 189      23.913  53.536  10.034  1.00 94.82           C
ANISOU  795  C   LYS A 189    14343   9152  12531   1084    421   -290       C
ATOM    796  O   LYS A 189      23.172  53.561  11.019  1.00 95.78           O
ANISOU  796  O   LYS A 189    14657   9179  12558   1142    572   -219       O
ATOM    797  CB  LYS A 189      26.231  54.488  10.604  1.00 90.89           C
ANISOU  797  CB  LYS A 189    13993   8642  11897   1120     54   -450       C
ATOM    798  CG  LYS A 189      25.962  55.014  12.025  1.00 99.44           C
ANISOU  798  CG  LYS A 189    15391   9611  12782   1207    104   -421       C
ATOM    799  CD  LYS A 189      26.395  56.480  12.231  1.00101.29           C
ANISOU  799  CD  LYS A 189    15688   9842  12955   1220     28   -484       C
ATOM    800  CE  LYS A 189      25.925  57.026  13.561  1.00102.65           C
ANISOU  800  CE  LYS A 189    16186   9894  12923   1308    110   -446       C
ATOM    801  NZ  LYS A 189      25.831  58.514  13.558  1.00105.79           N
ANISOU  801  NZ  LYS A 189    16604  10304  13288   1307    127   -480       N
ATOM    802  N   TYR A 190      23.469  53.765   8.756  1.00 90.56           N
ANISOU  802  N   TYR A 190    13551   8706  12151   1012    457   -295       N
ATOM    803  CA  TYR A 190      22.084  54.094   8.360  1.00 89.94           C
ANISOU  803  CA  TYR A 190    13370   8631  12170    990    651   -223       C
ATOM    804  C   TYR A 190      21.395  52.988   7.533  1.00 88.86           C
ANISOU  804  C   TYR A 190    13049   8512  12201    946    699   -183       C
ATOM    805  O   TYR A 190      20.221  53.130   7.218  1.00 88.89           O
ANISOU  805  O   TYR A 190    12955   8501  12319    928    842   -124       O
ATOM    806  CB  TYR A 190      22.006  55.451   7.590  1.00 91.54           C
ANISOU  806  CB  TYR A 190    13454   8911  12418    953    647   -261       C
ATOM    807  CG  TYR A 190      22.603  56.655   8.298  1.00 95.52           C
ANISOU  807  CG  TYR A 190    14114   9397  12783    990    607   -303       C
ATOM    808  CD1 TYR A 190      22.121  57.074   9.538  1.00 99.17           C
ANISOU  808  CD1 TYR A 190    14802   9761  13117   1054    731   -252       C
ATOM    809  CD2 TYR A 190      23.602  57.421   7.696  1.00 95.82           C
ANISOU  809  CD2 TYR A 190    14074   9504  12830    963    460   -393       C
ATOM    810  CE1 TYR A 190      22.665  58.184  10.192  1.00101.34           C
ANISOU  810  CE1 TYR A 190    15233  10011  13259   1091    681   -296       C
ATOM    811  CE2 TYR A 190      24.138  58.547   8.331  1.00 97.13           C
ANISOU  811  CE2 TYR A 190    14370   9645  12889    996    414   -436       C
ATOM    812  CZ  TYR A 190      23.675  58.918   9.586  1.00105.87           C
ANISOU  812  CZ  TYR A 190    15712  10659  13856   1059    513   -390       C
ATOM    813  OH  TYR A 190      24.205  60.015  10.231  1.00106.38           O
ANISOU  813  OH  TYR A 190    15921  10690  13809   1095    455   -438       O
ATOM    814  N   ASN A 191      22.101  51.905   7.187  1.00 81.99           N
ANISOU  814  N   ASN A 191    12127   7665  11359    929    576   -216       N
ATOM    815  CA  ASN A 191      21.569  50.804   6.371  1.00 80.85           C
ANISOU  815  CA  ASN A 191    11814   7537  11370    887    594   -190       C
ATOM    816  C   ASN A 191      20.276  50.208   6.985  1.00 83.37           C
ANISOU  816  C   ASN A 191    12170   7755  11753    913    792    -87       C
ATOM    817  O   ASN A 191      20.333  49.788   8.141  1.00 84.53           O
ANISOU  817  O   ASN A 191    12510   7815  11795    972    857    -46       O
ATOM    818  CB  ASN A 191      22.645  49.724   6.219  1.00 83.38           C
ANISOU  818  CB  ASN A 191    12129   7875  11677    879    442   -237       C
ATOM    819  CG  ASN A 191      22.514  48.827   5.017  1.00107.78           C
ANISOU  819  CG  ASN A 191    15021  11014  14917    823    394   -250       C
ATOM    820  OD1 ASN A 191      21.417  48.467   4.570  1.00102.90           O
ANISOU  820  OD1 ASN A 191    14295  10377  14425    801    489   -200       O
ATOM    821  ND2 ASN A 191      23.650  48.383   4.511  1.00 99.85           N
ANISOU  821  ND2 ASN A 191    13973  10055  13911    802    243   -318       N
ATOM    822  N   PRO A 192      19.103  50.188   6.285  1.00 77.54           N
ANISOU  822  N   PRO A 192    11261   7009  11192    877    893    -42       N
ATOM    823  CA  PRO A 192      17.879  49.636   6.913  1.00 77.95           C
ANISOU  823  CA  PRO A 192    11332   6941  11345    905   1098     59       C
ATOM    824  C   PRO A 192      17.899  48.119   7.163  1.00 79.83           C
ANISOU  824  C   PRO A 192    11574   7124  11634    913   1107     89       C
ATOM    825  O   PRO A 192      17.087  47.618   7.935  1.00 79.94           O
ANISOU  825  O   PRO A 192    11650   7018  11707    950   1290    174       O
ATOM    826  CB  PRO A 192      16.759  50.075   5.969  1.00 78.95           C
ANISOU  826  CB  PRO A 192    11246   7075  11678    858   1154     81       C
ATOM    827  CG  PRO A 192      17.412  50.179   4.660  1.00 81.83           C
ANISOU  827  CG  PRO A 192    11464   7561  12067    802    953     -6       C
ATOM    828  CD  PRO A 192      18.822  50.645   4.912  1.00 77.13           C
ANISOU  828  CD  PRO A 192    10998   7038  11269    817    825    -80       C
ATOM    829  N   VAL A 193      18.876  47.421   6.586  1.00 75.37           N
ANISOU  829  N   VAL A 193    10959   6634  11042    885    923     21       N
ATOM    830  CA  VAL A 193      19.076  45.992   6.801  1.00 76.13           C
ANISOU  830  CA  VAL A 193    11065   6691  11168    892    904     38       C
ATOM    831  C   VAL A 193      19.845  45.829   8.113  1.00 81.86           C
ANISOU  831  C   VAL A 193    12054   7362  11689    963    906     47       C
ATOM    832  O   VAL A 193      19.319  45.265   9.066  1.00 82.26           O
ANISOU  832  O   VAL A 193    12232   7298  11724   1015   1057    123       O
ATOM    833  CB  VAL A 193      19.809  45.324   5.601  1.00 78.93           C
ANISOU  833  CB  VAL A 193    11258   7145  11585    832    709    -40       C
ATOM    834  CG1 VAL A 193      20.282  43.910   5.936  1.00 79.32           C
ANISOU  834  CG1 VAL A 193    11345   7163  11630    843    666    -34       C
ATOM    835  CG2 VAL A 193      18.927  45.307   4.364  1.00 78.17           C
ANISOU  835  CG2 VAL A 193    10938   7075  11687    775    703    -43       C
ATOM    836  N   VAL A 194      21.076  46.368   8.156  1.00 79.78           N
ANISOU  836  N   VAL A 194    11875   7163  11275    970    738    -30       N
ATOM    837  CA  VAL A 194      22.011  46.247   9.274  1.00 80.64           C
ANISOU  837  CA  VAL A 194    12229   7221  11190   1036    670    -44       C
ATOM    838  C   VAL A 194      21.723  47.121  10.495  1.00 85.06           C
ANISOU  838  C   VAL A 194    13040   7690  11589   1112    788     -2       C
ATOM    839  O   VAL A 194      22.158  46.783  11.601  1.00 85.06           O
ANISOU  839  O   VAL A 194    13285   7600  11433   1185    786     18       O
ATOM    840  CB  VAL A 194      23.508  46.187   8.863  1.00 84.24           C
ANISOU  840  CB  VAL A 194    12659   7753  11594   1016    422   -144       C
ATOM    841  CG1 VAL A 194      24.225  45.072   9.626  1.00 85.08           C
ANISOU  841  CG1 VAL A 194    12908   7798  11622   1061    345   -140       C
ATOM    842  CG2 VAL A 194      23.676  45.983   7.352  1.00 82.60           C
ANISOU  842  CG2 VAL A 194    12186   7654  11546    932    331   -199       C
ATOM    843  N   ASN A 195      20.961  48.212  10.314  1.00 81.79           N
ANISOU  843  N   ASN A 195    12581   7288  11208   1099    895     15       N
ATOM    844  CA  ASN A 195      20.569  49.072  11.426  1.00 82.98           C
ANISOU  844  CA  ASN A 195    12969   7345  11216   1169   1035     60       C
ATOM    845  C   ASN A 195      19.172  49.689  11.184  1.00 87.36           C
ANISOU  845  C   ASN A 195    13414   7869  11910   1150   1258    130       C
ATOM    846  O   ASN A 195      19.081  50.914  11.014  1.00 85.40           O
ANISOU  846  O   ASN A 195    13143   7663  11641   1137   1260    105       O
ATOM    847  CB  ASN A 195      21.623  50.163  11.694  1.00 84.19           C
ANISOU  847  CB  ASN A 195    13245   7538  11204   1188    868    -23       C
ATOM    848  CG  ASN A 195      21.623  50.669  13.120  1.00112.08           C
ANISOU  848  CG  ASN A 195    17119  10946  14520   1286    943      9       C
ATOM    849  OD1 ASN A 195      22.636  50.628  13.809  1.00107.61           O
ANISOU  849  OD1 ASN A 195    16754  10344  13791   1338    782    -38       O
ATOM    850  ND2 ASN A 195      20.458  51.056  13.643  1.00104.32           N
ANISOU  850  ND2 ASN A 195    16229   9874  13534   1321   1195     95       N
ATOM    851  N   PRO A 196      18.064  48.887  11.204  1.00 84.96           N
ANISOU  851  N   PRO A 196    13039   7480  11762   1152   1452    219       N
ATOM    852  CA  PRO A 196      16.724  49.477  10.957  1.00 84.67           C
ANISOU  852  CA  PRO A 196    12876   7396  11900   1133   1657    286       C
ATOM    853  C   PRO A 196      16.313  50.655  11.862  1.00 88.04           C
ANISOU  853  C   PRO A 196    13502   7743  12207   1191   1823    327       C
ATOM    854  O   PRO A 196      15.634  51.573  11.389  1.00 85.34           O
ANISOU  854  O   PRO A 196    13027   7421  11977   1158   1895    339       O
ATOM    855  CB  PRO A 196      15.770  48.280  11.067  1.00 87.01           C
ANISOU  855  CB  PRO A 196    13100   7579  12380   1140   1833    375       C
ATOM    856  CG  PRO A 196      16.544  47.223  11.772  1.00 92.00           C
ANISOU  856  CG  PRO A 196    13925   8170  12862   1191   1781    374       C
ATOM    857  CD  PRO A 196      17.971  47.421  11.387  1.00 86.49           C
ANISOU  857  CD  PRO A 196    13241   7610  12013   1167   1490    261       C
ATOM    858  N   GLU A 197      16.779  50.635  13.138  1.00 86.50           N
ANISOU  858  N   GLU A 197    13636   7456  11775   1279   1864    344       N
ATOM    859  CA  GLU A 197      16.554  51.617  14.210  1.00 88.03           C
ANISOU  859  CA  GLU A 197    14103   7548  11794   1355   2012    379       C
ATOM    860  C   GLU A 197      16.918  53.045  13.768  1.00 89.00           C
ANISOU  860  C   GLU A 197    14170   7778  11869   1320   1897    308       C
ATOM    861  O   GLU A 197      16.046  53.904  13.660  1.00 87.52           O
ANISOU  861  O   GLU A 197    13926   7562  11768   1311   2062    351       O
ATOM    862  CB  GLU A 197      17.400  51.212  15.439  1.00 91.25           C
ANISOU  862  CB  GLU A 197    14877   7869  11925   1451   1954    371       C
ATOM    863  CG  GLU A 197      16.627  51.150  16.748  1.00111.39           C
ANISOU  863  CG  GLU A 197    17736  10214  14374   1556   2251    481       C
ATOM    864  CD  GLU A 197      17.473  51.082  18.009  1.00148.05           C
ANISOU  864  CD  GLU A 197    22798  14760  18694   1665   2175    463       C
ATOM    865  OE1 GLU A 197      18.399  50.238  18.073  1.00146.86           O
ANISOU  865  OE1 GLU A 197    22700  14639  18463   1676   1972    416       O
ATOM    866  OE2 GLU A 197      17.188  51.859  18.950  1.00149.19           O
ANISOU  866  OE2 GLU A 197    23230  14788  18668   1745   2317    497       O
ATOM    867  N   ARG A 198      18.216  53.272  13.499  1.00 84.87           N
ANISOU  867  N   ARG A 198    13654   7366  11225   1300   1618    200       N
ATOM    868  CA  ARG A 198      18.803  54.523  13.026  1.00 83.45           C
ANISOU  868  CA  ARG A 198    13413   7292  11001   1266   1473    117       C
ATOM    869  C   ARG A 198      18.295  54.893  11.625  1.00 83.16           C
ANISOU  869  C   ARG A 198    13036   7371  11191   1173   1464    102       C
ATOM    870  O   ARG A 198      18.114  56.086  11.360  1.00 82.63           O
ANISOU  870  O   ARG A 198    12923   7344  11129   1155   1484     84       O
ATOM    871  CB  ARG A 198      20.342  54.432  13.042  1.00 85.70           C
ANISOU  871  CB  ARG A 198    13766   7644  11151   1269   1180      9       C
ATOM    872  CG  ARG A 198      20.978  54.879  14.355  1.00103.87           C
ANISOU  872  CG  ARG A 198    16421   9848  13198   1360   1127    -13       C
ATOM    873  CD  ARG A 198      21.136  53.753  15.360  1.00123.64           C
ANISOU  873  CD  ARG A 198    19180  12228  15570   1440   1150     30       C
ATOM    874  NE  ARG A 198      20.450  54.049  16.620  1.00141.75           N
ANISOU  874  NE  ARG A 198    21799  14359  17702   1537   1370    109       N
ATOM    875  CZ  ARG A 198      20.486  53.269  17.698  1.00159.31           C
ANISOU  875  CZ  ARG A 198    24326  16439  19764   1631   1432    158       C
ATOM    876  NH1 ARG A 198      21.176  52.134  17.683  1.00143.17           N
ANISOU  876  NH1 ARG A 198    22289  14401  17707   1638   1278    135       N
ATOM    877  NH2 ARG A 198      19.834  53.620  18.800  1.00149.96           N
ANISOU  877  NH2 ARG A 198    23454  15096  18429   1724   1656    233       N
ATOM    878  N   ALA A 199      18.062  53.877  10.738  1.00 76.56           N
ANISOU  878  N   ALA A 199    11975   6580  10535   1118   1429    110       N
ATOM    879  CA  ALA A 199      17.528  54.067   9.386  1.00 74.85           C
ANISOU  879  CA  ALA A 199    11457   6452  10532   1039   1405     98       C
ATOM    880  C   ALA A 199      16.195  54.805   9.427  1.00 81.37           C
ANISOU  880  C   ALA A 199    12224   7211  11484   1040   1625    175       C
ATOM    881  O   ALA A 199      16.012  55.760   8.671  1.00 81.94           O
ANISOU  881  O   ALA A 199    12154   7354  11624    999   1591    147       O
ATOM    882  CB  ALA A 199      17.352  52.734   8.693  1.00 75.40           C
ANISOU  882  CB  ALA A 199    11356   6537  10757   1000   1357    106       C
ATOM    883  N   LEU A 200      15.276  54.403  10.326  1.00 78.90           N
ANISOU  883  N   LEU A 200    12026   6749  11205   1091   1861    275       N
ATOM    884  CA  LEU A 200      13.997  55.091  10.494  1.00 78.83           C
ANISOU  884  CA  LEU A 200    11973   6645  11334   1100   2099    358       C
ATOM    885  C   LEU A 200      14.219  56.520  11.006  1.00 81.97           C
ANISOU  885  C   LEU A 200    12532   7050  11564   1131   2134    339       C
ATOM    886  O   LEU A 200      13.607  57.453  10.479  1.00 81.10           O
ANISOU  886  O   LEU A 200    12283   6962  11568   1100   2189    349       O
ATOM    887  CB  LEU A 200      13.100  54.324  11.475  1.00 80.53           C
ANISOU  887  CB  LEU A 200    12312   6675  11612   1161   2367    471       C
ATOM    888  CG  LEU A 200      11.860  53.579  10.952  1.00 86.01           C
ANISOU  888  CG  LEU A 200    12761   7283  12636   1127   2511    548       C
ATOM    889  CD1 LEU A 200      11.682  53.690   9.441  1.00 85.18           C
ANISOU  889  CD1 LEU A 200    12326   7300  12740   1037   2327    493       C
ATOM    890  CD2 LEU A 200      11.865  52.122  11.413  1.00 88.85           C
ANISOU  890  CD2 LEU A 200    13181   7553  13025   1157   2572    592       C
ATOM    891  N   GLU A 201      15.107  56.686  12.019  1.00 78.48           N
ANISOU  891  N   GLU A 201    12381   6584  10854   1194   2084    308       N
ATOM    892  CA  GLU A 201      15.418  57.985  12.633  1.00 78.62           C
ANISOU  892  CA  GLU A 201    12590   6594  10689   1233   2098    281       C
ATOM    893  C   GLU A 201      15.927  58.984  11.587  1.00 79.79           C
ANISOU  893  C   GLU A 201    12547   6898  10872   1166   1916    193       C
ATOM    894  O   GLU A 201      15.464  60.127  11.537  1.00 78.46           O
ANISOU  894  O   GLU A 201    12358   6729  10725   1161   2009    206       O
ATOM    895  CB  GLU A 201      16.417  57.824  13.789  1.00 81.31           C
ANISOU  895  CB  GLU A 201    13270   6878  10745   1312   2012    247       C
ATOM    896  CG  GLU A 201      15.807  57.141  15.007  1.00101.12           C
ANISOU  896  CG  GLU A 201    16048   9199  13174   1402   2252    347       C
ATOM    897  CD  GLU A 201      16.702  56.967  16.220  1.00129.48           C
ANISOU  897  CD  GLU A 201    20022  12706  16468   1496   2173    321       C
ATOM    898  OE1 GLU A 201      16.945  55.802  16.614  1.00100.76           O
ANISOU  898  OE1 GLU A 201    16489   9011  12785   1532   2156    342       O
ATOM    899  OE2 GLU A 201      17.097  57.992  16.824  1.00135.83           O
ANISOU  899  OE2 GLU A 201    21038  13485  17086   1540   2136    284       O
ATOM    900  N   ARG A 202      16.853  58.524  10.727  1.00 74.57           N
ANISOU  900  N   ARG A 202    11744   6362  10229   1116   1674    109       N
ATOM    901  CA  ARG A 202      17.431  59.305   9.647  1.00 71.07           C
ANISOU  901  CA  ARG A 202    11121   6058   9825   1055   1503     24       C
ATOM    902  C   ARG A 202      16.316  59.661   8.635  1.00 71.12           C
ANISOU  902  C   ARG A 202    10875   6093  10054   1002   1597     65       C
ATOM    903  O   ARG A 202      16.083  60.848   8.396  1.00 68.25           O
ANISOU  903  O   ARG A 202    10475   5759   9698    991   1632     56       O
ATOM    904  CB  ARG A 202      18.585  58.513   9.011  1.00 68.40           C
ANISOU  904  CB  ARG A 202    10701   5811   9476   1023   1266    -58       C
ATOM    905  CG  ARG A 202      19.243  59.189   7.812  1.00 77.32           C
ANISOU  905  CG  ARG A 202    11649   7071  10657    965   1103   -144       C
ATOM    906  CD  ARG A 202      20.385  60.131   8.150  1.00 81.84           C
ANISOU  906  CD  ARG A 202    12338   7674  11085    983    972   -227       C
ATOM    907  NE  ARG A 202      21.042  60.584   6.925  1.00 82.74           N
ANISOU  907  NE  ARG A 202    12263   7898  11275    929    837   -303       N
ATOM    908  CZ  ARG A 202      21.249  61.856   6.603  1.00 92.61           C
ANISOU  908  CZ  ARG A 202    13481   9192  12515    918    825   -342       C
ATOM    909  NH1 ARG A 202      20.904  62.826   7.442  1.00 83.52           N
ANISOU  909  NH1 ARG A 202    12473   7990  11273    955    922   -321       N
ATOM    910  NH2 ARG A 202      21.829  62.169   5.452  1.00 73.72           N
ANISOU  910  NH2 ARG A 202    10927   6886  10198    875    723   -404       N
ATOM    911  N   ARG A 203      15.589  58.639   8.108  1.00 67.18           N
ANISOU  911  N   ARG A 203    10213   5570   9741    973   1636    112       N
ATOM    912  CA  ARG A 203      14.486  58.808   7.147  1.00 66.73           C
ANISOU  912  CA  ARG A 203     9914   5518   9924    926   1695    150       C
ATOM    913  C   ARG A 203      13.498  59.891   7.547  1.00 71.40           C
ANISOU  913  C   ARG A 203    10525   6034  10571    946   1895    214       C
ATOM    914  O   ARG A 203      13.221  60.784   6.754  1.00 69.80           O
ANISOU  914  O   ARG A 203    10182   5890  10449    911   1860    195       O
ATOM    915  CB  ARG A 203      13.740  57.479   6.921  1.00 67.28           C
ANISOU  915  CB  ARG A 203     9860   5517  10185    912   1745    206       C
ATOM    916  CG  ARG A 203      12.563  57.588   5.946  1.00 72.76           C
ANISOU  916  CG  ARG A 203    10304   6189  11154    869   1782    244       C
ATOM    917  CD  ARG A 203      11.617  56.410   6.058  1.00 81.62           C
ANISOU  917  CD  ARG A 203    11331   7190  12491    869   1890    318       C
ATOM    918  NE  ARG A 203      10.735  56.509   7.222  1.00 80.70           N
ANISOU  918  NE  ARG A 203    11325   6911  12426    921   2172    422       N
ATOM    919  CZ  ARG A 203       9.621  55.804   7.369  1.00 86.73           C
ANISOU  919  CZ  ARG A 203    11981   7532  13441    926   2334    507       C
ATOM    920  NH1 ARG A 203       9.237  54.956   6.425  1.00 64.64           N
ANISOU  920  NH1 ARG A 203     8956   4737  10866    879   2220    496       N
ATOM    921  NH2 ARG A 203       8.878  55.946   8.458  1.00 74.83           N
ANISOU  921  NH2 ARG A 203    10595   5863  11974    980   2618    604       N
ATOM    922  N   ASN A 204      12.967  59.796   8.776  1.00 71.40           N
ANISOU  922  N   ASN A 204    10708   5895  10526   1005   2112    294       N
ATOM    923  CA  ASN A 204      11.980  60.715   9.332  1.00 72.23           C
ANISOU  923  CA  ASN A 204    10863   5895  10686   1034   2348    369       C
ATOM    924  C   ASN A 204      12.560  62.079   9.539  1.00 77.07           C
ANISOU  924  C   ASN A 204    11595   6571  11119   1046   2307    317       C
ATOM    925  O   ASN A 204      11.851  63.065   9.310  1.00 78.17           O
ANISOU  925  O   ASN A 204    11651   6696  11354   1035   2409    346       O
ATOM    926  CB  ASN A 204      11.384  60.161  10.606  1.00 74.27           C
ANISOU  926  CB  ASN A 204    11322   5975  10923   1104   2601    466       C
ATOM    927  CG  ASN A 204      10.695  58.827  10.422  1.00 98.89           C
ANISOU  927  CG  ASN A 204    14306   9010  14259   1093   2675    528       C
ATOM    928  OD1 ASN A 204      10.054  58.547   9.398  1.00 89.64           O
ANISOU  928  OD1 ASN A 204    12853   7862  13344   1034   2621    533       O
ATOM    929  ND2 ASN A 204      10.826  57.964  11.416  1.00 95.10           N
ANISOU  929  ND2 ASN A 204    14035   8419  13679   1154   2793    574       N
ATOM    930  N   TRP A 205      13.856  62.163   9.909  1.00 73.89           N
ANISOU  930  N   TRP A 205    11366   6235  10475   1067   2143    235       N
ATOM    931  CA  TRP A 205      14.523  63.464  10.039  1.00 74.67           C
ANISOU  931  CA  TRP A 205    11560   6394  10416   1075   2073    172       C
ATOM    932  C   TRP A 205      14.459  64.188   8.679  1.00 70.89           C
ANISOU  932  C   TRP A 205    10820   6040  10073   1007   1963    126       C
ATOM    933  O   TRP A 205      14.003  65.324   8.627  1.00 70.23           O
ANISOU  933  O   TRP A 205    10716   5955  10013   1005   2052    140       O
ATOM    934  CB  TRP A 205      15.979  63.340  10.559  1.00 75.37           C
ANISOU  934  CB  TRP A 205    11846   6522  10269   1105   1878     83       C
ATOM    935  CG  TRP A 205      16.624  64.677  10.783  1.00 77.79           C
ANISOU  935  CG  TRP A 205    12254   6867  10437   1117   1811     18       C
ATOM    936  CD1 TRP A 205      16.396  65.527  11.821  1.00 82.18           C
ANISOU  936  CD1 TRP A 205    13038   7329  10856   1175   1946     44       C
ATOM    937  CD2 TRP A 205      17.494  65.371   9.879  1.00 77.35           C
ANISOU  937  CD2 TRP A 205    12060   6941  10387   1070   1615    -79       C
ATOM    938  NE1 TRP A 205      17.074  66.708  11.629  1.00 82.22           N
ANISOU  938  NE1 TRP A 205    13048   7405  10788   1163   1831    -34       N
ATOM    939  CE2 TRP A 205      17.771  66.634  10.450  1.00 82.44           C
ANISOU  939  CE2 TRP A 205    12849   7568  10906   1100   1632   -110       C
ATOM    940  CE3 TRP A 205      18.086  65.041   8.645  1.00 78.12           C
ANISOU  940  CE3 TRP A 205    11938   7159  10585   1010   1437   -142       C
ATOM    941  CZ2 TRP A 205      18.607  67.575   9.827  1.00 81.02           C
ANISOU  941  CZ2 TRP A 205    12583   7485  10716   1069   1479   -200       C
ATOM    942  CZ3 TRP A 205      18.925  65.967   8.036  1.00 79.16           C
ANISOU  942  CZ3 TRP A 205    12000   7380  10697    984   1300   -228       C
ATOM    943  CH2 TRP A 205      19.161  67.224   8.616  1.00 80.14           C
ANISOU  943  CH2 TRP A 205    12251   7484  10715   1011   1324   -255       C
ATOM    944  N   ILE A 206      14.817  63.478   7.586  1.00 61.78           N
ANISOU  944  N   ILE A 206     9478   4980   9015    956   1791     80       N
ATOM    945  CA  ILE A 206      14.769  63.940   6.202  1.00 58.66           C
ANISOU  945  CA  ILE A 206     8856   4690   8742    899   1678     38       C
ATOM    946  C   ILE A 206      13.355  64.391   5.827  1.00 63.01           C
ANISOU  946  C   ILE A 206     9258   5185   9498    884   1828    115       C
ATOM    947  O   ILE A 206      13.195  65.506   5.311  1.00 63.25           O
ANISOU  947  O   ILE A 206     9217   5261   9553    868   1824     99       O
ATOM    948  CB  ILE A 206      15.390  62.902   5.213  1.00 59.45           C
ANISOU  948  CB  ILE A 206     8826   4870   8893    859   1484    -17       C
ATOM    949  CG1 ILE A 206      16.897  62.711   5.527  1.00 58.84           C
ANISOU  949  CG1 ILE A 206     8877   4848   8631    872   1327   -102       C
ATOM    950  CG2 ILE A 206      15.175  63.299   3.735  1.00 56.34           C
ANISOU  950  CG2 ILE A 206     8219   4558   8631    810   1386    -48       C
ATOM    951  CD1 ILE A 206      17.565  61.543   4.872  1.00 56.85           C
ANISOU  951  CD1 ILE A 206     8554   4641   8407    848   1176   -143       C
ATOM    952  N   LEU A 207      12.337  63.568   6.134  1.00 58.94           N
ANISOU  952  N   LEU A 207     8699   4557   9140    892   1967    201       N
ATOM    953  CA  LEU A 207      10.934  63.894   5.854  1.00 58.92           C
ANISOU  953  CA  LEU A 207     8538   4468   9380    880   2116    281       C
ATOM    954  C   LEU A 207      10.552  65.166   6.574  1.00 67.06           C
ANISOU  954  C   LEU A 207     9679   5447  10355    912   2293    318       C
ATOM    955  O   LEU A 207       9.988  66.081   5.939  1.00 68.23           O
ANISOU  955  O   LEU A 207     9693   5614  10618    888   2304    325       O
ATOM    956  CB  LEU A 207       9.989  62.738   6.195  1.00 59.61           C
ANISOU  956  CB  LEU A 207     8569   4419   9660    890   2250    366       C
ATOM    957  CG  LEU A 207      10.220  61.419   5.416  1.00 62.05           C
ANISOU  957  CG  LEU A 207     8744   4768  10064    855   2078    333       C
ATOM    958  CD1 LEU A 207       9.779  60.227   6.227  1.00 62.91           C
ANISOU  958  CD1 LEU A 207     8904   4746  10255    884   2222    405       C
ATOM    959  CD2 LEU A 207       9.527  61.440   4.080  1.00 61.89           C
ANISOU  959  CD2 LEU A 207     8464   4771  10281    806   1961    324       C
ATOM    960  N   GLY A 208      10.964  65.266   7.851  1.00 63.88           N
ANISOU  960  N   GLY A 208     9536   4982   9752    967   2408    333       N
ATOM    961  CA  GLY A 208      10.783  66.466   8.677  1.00 63.58           C
ANISOU  961  CA  GLY A 208     9663   4889   9606   1006   2570    358       C
ATOM    962  C   GLY A 208      11.388  67.698   8.024  1.00 64.19           C
ANISOU  962  C   GLY A 208     9691   5096   9604    979   2432    280       C
ATOM    963  O   GLY A 208      10.714  68.730   7.911  1.00 65.17           O
ANISOU  963  O   GLY A 208     9755   5197   9808    974   2543    313       O
ATOM    964  N   ARG A 209      12.650  67.562   7.504  1.00 57.50           N
ANISOU  964  N   ARG A 209     8844   4380   8623    957   2191    177       N
ATOM    965  CA  ARG A 209      13.383  68.610   6.766  1.00 55.68           C
ANISOU  965  CA  ARG A 209     8554   4274   8329    930   2046     93       C
ATOM    966  C   ARG A 209      12.709  68.959   5.425  1.00 57.23           C
ANISOU  966  C   ARG A 209     8494   4524   8726    881   2004    101       C
ATOM    967  O   ARG A 209      12.661  70.123   5.062  1.00 55.43           O
ANISOU  967  O   ARG A 209     8227   4338   8496    873   2012     83       O
ATOM    968  CB  ARG A 209      14.876  68.244   6.562  1.00 55.69           C
ANISOU  968  CB  ARG A 209     8609   4371   8179    922   1820    -11       C
ATOM    969  CG  ARG A 209      15.855  68.823   7.592  1.00 64.30           C
ANISOU  969  CG  ARG A 209     9937   5447   9047    966   1788    -63       C
ATOM    970  CD  ARG A 209      15.666  70.329   7.804  1.00 72.24           C
ANISOU  970  CD  ARG A 209    10980   6455  10012    974   1867    -70       C
ATOM    971  NE  ARG A 209      16.670  70.930   8.690  1.00 82.13           N
ANISOU  971  NE  ARG A 209    12452   7689  11063   1014   1806   -133       N
ATOM    972  CZ  ARG A 209      16.519  71.126  10.001  1.00 96.22           C
ANISOU  972  CZ  ARG A 209    14491   9360  12708   1075   1923   -100       C
ATOM    973  NH1 ARG A 209      17.492  71.689  10.711  1.00 71.19           N
ANISOU  973  NH1 ARG A 209    11519   6170   9360   1112   1825   -170       N
ATOM    974  NH2 ARG A 209      15.405  70.742  10.615  1.00 88.74           N
ANISOU  974  NH2 ARG A 209    13610   8303  11805   1103   2136      4       N
ATOM    975  N   MET A 210      12.152  67.950   4.718  1.00 54.98           N
ANISOU  975  N   MET A 210     8045   4227   8616    854   1957    128       N
ATOM    976  CA  MET A 210      11.419  68.125   3.453  1.00 54.43           C
ANISOU  976  CA  MET A 210     7750   4185   8748    816   1894    137       C
ATOM    977  C   MET A 210      10.152  68.939   3.676  1.00 62.23           C
ANISOU  977  C   MET A 210     8674   5078   9895    824   2081    220       C
ATOM    978  O   MET A 210       9.779  69.733   2.813  1.00 60.64           O
ANISOU  978  O   MET A 210     8343   4910   9786    804   2036    213       O
ATOM    979  CB  MET A 210      11.019  66.772   2.858  1.00 55.97           C
ANISOU  979  CB  MET A 210     7809   4354   9102    793   1809    152       C
ATOM    980  CG  MET A 210      12.136  66.070   2.148  1.00 57.46           C
ANISOU  980  CG  MET A 210     8000   4647   9185    774   1598     66       C
ATOM    981  SD  MET A 210      11.685  64.388   1.720  1.00 60.40           S
ANISOU  981  SD  MET A 210     8254   4970   9724    755   1525     89       S
ATOM    982  CE  MET A 210      11.216  64.622   0.020  1.00 56.57           C
ANISOU  982  CE  MET A 210     7570   4530   9393    720   1355     58       C
ATOM    983  N   LEU A 211       9.476  68.707   4.823  1.00 62.43           N
ANISOU  983  N   LEU A 211     8792   4969   9958    857   2298    302       N
ATOM    984  CA  LEU A 211       8.252  69.420   5.172  1.00 63.82           C
ANISOU  984  CA  LEU A 211     8917   5029  10304    869   2512    391       C
ATOM    985  C   LEU A 211       8.590  70.869   5.462  1.00 69.38           C
ANISOU  985  C   LEU A 211     9728   5777  10856    884   2565    366       C
ATOM    986  O   LEU A 211       7.935  71.777   4.918  1.00 70.04           O
ANISOU  986  O   LEU A 211     9684   5857  11070    868   2598    387       O
ATOM    987  CB  LEU A 211       7.535  68.758   6.365  1.00 65.54           C
ANISOU  987  CB  LEU A 211     9231   5074  10595    908   2759    487       C
ATOM    988  CG  LEU A 211       6.302  69.491   6.929  1.00 70.44           C
ANISOU  988  CG  LEU A 211     9826   5543  11396    930   3033    590       C
ATOM    989  CD1 LEU A 211       5.153  69.517   5.930  1.00 69.75           C
ANISOU  989  CD1 LEU A 211     9438   5409  11655    890   3004    630       C
ATOM    990  CD2 LEU A 211       5.853  68.855   8.218  1.00 74.99           C
ANISOU  990  CD2 LEU A 211    10559   5945  11988    982   3295    679       C
ATOM    991  N   GLN A 212       9.650  71.094   6.279  1.00 64.47           N
ANISOU  991  N   GLN A 212     9339   5195   9962    914   2553    315       N
ATOM    992  CA  GLN A 212      10.147  72.442   6.627  1.00 61.93           C
ANISOU  992  CA  GLN A 212     9142   4915   9474    930   2580    276       C
ATOM    993  C   GLN A 212      10.525  73.235   5.385  1.00 60.40           C
ANISOU  993  C   GLN A 212     8793   4854   9304    890   2411    209       C
ATOM    994  O   GLN A 212      10.229  74.426   5.330  1.00 62.40           O
ANISOU  994  O   GLN A 212     9031   5109   9569    892   2486    218       O
ATOM    995  CB  GLN A 212      11.356  72.357   7.564  1.00 63.12           C
ANISOU  995  CB  GLN A 212     9551   5086   9347    967   2523    214       C
ATOM    996  CG  GLN A 212      11.020  71.900   8.984  1.00 71.79           C
ANISOU  996  CG  GLN A 212    10881   6035  10359   1026   2717    280       C
ATOM    997  CD  GLN A 212      12.267  71.552   9.751  1.00 91.27           C
ANISOU  997  CD  GLN A 212    13588   8523  12567   1062   2593    208       C
ATOM    998  OE1 GLN A 212      12.303  70.600  10.542  1.00 86.79           O
ANISOU  998  OE1 GLN A 212    13171   7874  11931   1100   2636    236       O
ATOM    999  NE2 GLN A 212      13.326  72.312   9.517  1.00 83.40           N
ANISOU  999  NE2 GLN A 212    12626   7626  11435   1052   2427    112       N
ATOM   1000  N   LEU A 213      11.163  72.582   4.388  1.00 52.76           N
ANISOU 1000  N   LEU A 213     7719   3985   8342    859   2197    145       N
ATOM   1001  CA  LEU A 213      11.563  73.205   3.115  1.00 51.03           C
ANISOU 1001  CA  LEU A 213     7371   3879   8138    829   2040     82       C
ATOM   1002  C   LEU A 213      10.420  73.427   2.063  1.00 57.15           C
ANISOU 1002  C   LEU A 213     7935   4634   9145    806   2035    128       C
ATOM   1003  O   LEU A 213      10.662  74.041   1.011  1.00 57.00           O
ANISOU 1003  O   LEU A 213     7833   4694   9130    790   1919     83       O
ATOM   1004  CB  LEU A 213      12.754  72.460   2.480  1.00 49.53           C
ANISOU 1004  CB  LEU A 213     7180   3787   7854    813   1830     -5       C
ATOM   1005  CG  LEU A 213      14.025  72.321   3.331  1.00 52.15           C
ANISOU 1005  CG  LEU A 213     7694   4144   7976    833   1782    -69       C
ATOM   1006  CD1 LEU A 213      14.847  71.159   2.885  1.00 50.73           C
ANISOU 1006  CD1 LEU A 213     7498   4010   7767    819   1621   -121       C
ATOM   1007  CD2 LEU A 213      14.851  73.569   3.316  1.00 51.62           C
ANISOU 1007  CD2 LEU A 213     7678   4138   7796    838   1749   -135       C
ATOM   1008  N   GLY A 214       9.203  72.951   2.366  1.00 54.52           N
ANISOU 1008  N   GLY A 214     7524   4181   9009    808   2161    218       N
ATOM   1009  CA  GLY A 214       8.038  73.074   1.492  1.00 54.32           C
ANISOU 1009  CA  GLY A 214     7293   4105   9242    790   2147    266       C
ATOM   1010  C   GLY A 214       8.108  72.186   0.272  1.00 59.03           C
ANISOU 1010  C   GLY A 214     7758   4744   9926    765   1927    227       C
ATOM   1011  O   GLY A 214       7.453  72.464  -0.740  1.00 58.45           O
ANISOU 1011  O   GLY A 214     7536   4659  10014    753   1834    234       O
ATOM   1012  N   TYR A 215       8.934  71.099   0.362  1.00 55.80           N
ANISOU 1012  N   TYR A 215     7419   4379   9404    761   1831    182       N
ATOM   1013  CA  TYR A 215       9.120  70.095  -0.683  1.00 53.32           C
ANISOU 1013  CA  TYR A 215     7014   4100   9145    741   1629    141       C
ATOM   1014  C   TYR A 215       7.922  69.179  -0.653  1.00 58.28           C
ANISOU 1014  C   TYR A 215     7504   4600  10038    733   1665    212       C
ATOM   1015  O   TYR A 215       7.356  68.882  -1.707  1.00 59.64           O
ANISOU 1015  O   TYR A 215     7531   4750  10378    718   1521    208       O
ATOM   1016  CB  TYR A 215      10.401  69.306  -0.452  1.00 53.85           C
ANISOU 1016  CB  TYR A 215     7203   4244   9012    741   1544     75       C
ATOM   1017  CG  TYR A 215      11.682  70.074  -0.689  1.00 56.29           C
ANISOU 1017  CG  TYR A 215     7613   4670   9104    745   1470     -8       C
ATOM   1018  CD1 TYR A 215      11.719  71.158  -1.559  1.00 58.62           C
ANISOU 1018  CD1 TYR A 215     7865   5017   9392    744   1423    -36       C
ATOM   1019  CD2 TYR A 215      12.869  69.687  -0.085  1.00 57.05           C
ANISOU 1019  CD2 TYR A 215     7843   4814   9020    752   1440    -60       C
ATOM   1020  CE1 TYR A 215      12.899  71.862  -1.789  1.00 60.36           C
ANISOU 1020  CE1 TYR A 215     8167   5329   9439    749   1372   -110       C
ATOM   1021  CE2 TYR A 215      14.060  70.375  -0.316  1.00 57.50           C
ANISOU 1021  CE2 TYR A 215     7970   4958   8919    755   1371   -138       C
ATOM   1022  CZ  TYR A 215      14.075  71.460  -1.175  1.00 66.09           C
ANISOU 1022  CZ  TYR A 215     9007   6093  10012    753   1345   -162       C
ATOM   1023  OH  TYR A 215      15.255  72.136  -1.403  1.00 66.08           O
ANISOU 1023  OH  TYR A 215     9065   6161   9879    758   1295   -236       O
ATOM   1024  N   ILE A 216       7.521  68.744   0.553  1.00 53.31           N
ANISOU 1024  N   ILE A 216     6930   3872   9454    748   1857    279       N
ATOM   1025  CA  ILE A 216       6.351  67.905   0.725  1.00 54.04           C
ANISOU 1025  CA  ILE A 216     6887   3817   9828    744   1935    357       C
ATOM   1026  C   ILE A 216       5.296  68.646   1.541  1.00 65.02           C
ANISOU 1026  C   ILE A 216     8253   5074  11377    763   2188    452       C
ATOM   1027  O   ILE A 216       5.636  69.484   2.385  1.00 64.20           O
ANISOU 1027  O   ILE A 216     8305   4985  11102    786   2340    462       O
ATOM   1028  CB  ILE A 216       6.670  66.505   1.303  1.00 55.35           C
ANISOU 1028  CB  ILE A 216     7114   3950   9966    748   1952    364       C
ATOM   1029  CG1 ILE A 216       7.223  66.573   2.748  1.00 54.42           C
ANISOU 1029  CG1 ILE A 216     7223   3813   9641    784   2148    388       C
ATOM   1030  CG2 ILE A 216       7.541  65.696   0.350  1.00 54.06           C
ANISOU 1030  CG2 ILE A 216     6938   3899   9704    726   1699    277       C
ATOM   1031  CD1 ILE A 216       7.490  65.214   3.441  1.00 52.79           C
ANISOU 1031  CD1 ILE A 216     7102   3559   9396    798   2185    403       C
ATOM   1032  N   SER A 217       4.011  68.321   1.295  1.00 66.63           N
ANISOU 1032  N   SER A 217     8261   5133  11922    754   2233    522       N
ATOM   1033  CA  SER A 217       2.885  68.860   2.055  1.00 67.98           C
ANISOU 1033  CA  SER A 217     8379   5141  12310    771   2496    624       C
ATOM   1034  C   SER A 217       2.763  68.036   3.344  1.00 72.88           C
ANISOU 1034  C   SER A 217     9116   5642  12932    800   2737    692       C
ATOM   1035  O   SER A 217       3.364  66.956   3.452  1.00 69.15           O
ANISOU 1035  O   SER A 217     8709   5206  12359    800   2660    661       O
ATOM   1036  CB  SER A 217       1.596  68.816   1.232  1.00 72.04           C
ANISOU 1036  CB  SER A 217     8620   5532  13221    751   2430    667       C
ATOM   1037  OG  SER A 217       1.194  67.509   0.864  1.00 80.05           O
ANISOU 1037  OG  SER A 217     9497   6467  14451    736   2327    674       O
ATOM   1038  N   GLN A 218       2.022  68.556   4.331  1.00 74.70           N
ANISOU 1038  N   GLN A 218     9391   5726  13267    831   3036    785       N
ATOM   1039  CA  GLN A 218       1.830  67.848   5.598  1.00 77.52           C
ANISOU 1039  CA  GLN A 218     9888   5943  13625    871   3300    860       C
ATOM   1040  C   GLN A 218       1.052  66.543   5.407  1.00 81.09           C
ANISOU 1040  C   GLN A 218    10155   6257  14397    858   3308    908       C
ATOM   1041  O   GLN A 218       1.366  65.564   6.081  1.00 81.69           O
ANISOU 1041  O   GLN A 218    10355   6294  14388    881   3388    924       O
ATOM   1042  CB  GLN A 218       1.240  68.752   6.704  1.00 81.07           C
ANISOU 1042  CB  GLN A 218    10466   6253  14083    915   3643    949       C
ATOM   1043  CG  GLN A 218       1.578  68.240   8.120  1.00108.11           C
ANISOU 1043  CG  GLN A 218    14208   9628  17243    973   3847    975       C
ATOM   1044  CD  GLN A 218       1.490  69.262   9.231  1.00135.75           C
ANISOU 1044  CD  GLN A 218    17915  13003  20660   1029   4171   1049       C
ATOM   1045  OE1 GLN A 218       0.994  70.388   9.058  1.00133.99           O
ANISOU 1045  OE1 GLN A 218    17598  12726  20587   1024   4281   1088       O
ATOM   1046  NE2 GLN A 218       1.971  68.878  10.415  1.00127.25           N
ANISOU 1046  NE2 GLN A 218    17147  11873  19330   1089   4328   1066       N
ATOM   1047  N   ALA A 219       0.106  66.507   4.433  1.00 76.53           N
ANISOU 1047  N   ALA A 219     9286   5612  14181    823   3191    922       N
ATOM   1048  CA  ALA A 219      -0.673  65.310   4.078  1.00 77.12           C
ANISOU 1048  CA  ALA A 219     9144   5551  14606    805   3147    956       C
ATOM   1049  C   ALA A 219       0.281  64.216   3.624  1.00 80.74           C
ANISOU 1049  C   ALA A 219     9658   6146  14873    787   2905    871       C
ATOM   1050  O   ALA A 219       0.151  63.064   4.056  1.00 81.99           O
ANISOU 1050  O   ALA A 219     9816   6214  15124    796   2983    904       O
ATOM   1051  CB  ALA A 219      -1.648  65.632   2.963  1.00 78.42           C
ANISOU 1051  CB  ALA A 219     9010   5651  15136    771   2980    957       C
ATOM   1052  N   GLU A 220       1.282  64.595   2.789  1.00 75.35           N
ANISOU 1052  N   GLU A 220     9036   5676  13917    766   2631    763       N
ATOM   1053  CA  GLU A 220       2.343  63.701   2.310  1.00 73.26           C
ANISOU 1053  CA  GLU A 220     8844   5557  13433    750   2399    674       C
ATOM   1054  C   GLU A 220       3.276  63.371   3.465  1.00 75.52           C
ANISOU 1054  C   GLU A 220     9397   5886  13409    783   2545    675       C
ATOM   1055  O   GLU A 220       3.776  62.260   3.536  1.00 74.76           O
ANISOU 1055  O   GLU A 220     9346   5812  13248    782   2477    651       O
ATOM   1056  CB  GLU A 220       3.143  64.352   1.171  1.00 72.82           C
ANISOU 1056  CB  GLU A 220     8801   5693  13176    727   2117    569       C
ATOM   1057  CG  GLU A 220       2.351  64.592  -0.105  1.00 78.78           C
ANISOU 1057  CG  GLU A 220     9327   6414  14189    701   1913    552       C
ATOM   1058  CD  GLU A 220       3.136  65.277  -1.204  1.00 85.51           C
ANISOU 1058  CD  GLU A 220    10225   7440  14825    690   1664    456       C
ATOM   1059  OE1 GLU A 220       3.767  66.317  -0.918  1.00 53.13           O
ANISOU 1059  OE1 GLU A 220     6263   3440  10484    702   1730    435       O
ATOM   1060  OE2 GLU A 220       3.125  64.774  -2.351  1.00 82.56           O
ANISOU 1060  OE2 GLU A 220     9757   7089  14522    673   1408    401       O
ATOM   1061  N   TYR A 221       3.499  64.329   4.374  1.00 73.73           N
ANISOU 1061  N   TYR A 221     9355   5663  12996    817   2737    701       N
ATOM   1062  CA  TYR A 221       4.368  64.129   5.528  1.00 73.94           C
ANISOU 1062  CA  TYR A 221     9664   5714  12717    859   2861    699       C
ATOM   1063  C   TYR A 221       3.819  63.074   6.481  1.00 78.41           C
ANISOU 1063  C   TYR A 221    10281   6104  13408    893   3089    787       C
ATOM   1064  O   TYR A 221       4.551  62.158   6.828  1.00 78.46           O
ANISOU 1064  O   TYR A 221    10420   6149  13244    907   3041    760       O
ATOM   1065  CB  TYR A 221       4.722  65.461   6.249  1.00 75.53           C
ANISOU 1065  CB  TYR A 221    10065   5947  12685    891   2992    700       C
ATOM   1066  CG  TYR A 221       5.601  65.227   7.457  1.00 77.72           C
ANISOU 1066  CG  TYR A 221    10653   6228  12650    942   3093    693       C
ATOM   1067  CD1 TYR A 221       6.926  64.836   7.311  1.00 78.43           C
ANISOU 1067  CD1 TYR A 221    10863   6469  12467    937   2876    598       C
ATOM   1068  CD2 TYR A 221       5.081  65.291   8.743  1.00 79.93           C
ANISOU 1068  CD2 TYR A 221    11108   6336  12924   1001   3405    786       C
ATOM   1069  CE1 TYR A 221       7.721  64.551   8.416  1.00 79.59           C
ANISOU 1069  CE1 TYR A 221    11292   6603  12344    987   2938    589       C
ATOM   1070  CE2 TYR A 221       5.867  65.007   9.856  1.00 80.86           C
ANISOU 1070  CE2 TYR A 221    11538   6440  12746   1058   3479    780       C
ATOM   1071  CZ  TYR A 221       7.192  64.647   9.688  1.00 86.87           C
ANISOU 1071  CZ  TYR A 221    12408   7358  13240   1050   3230    678       C
ATOM   1072  OH  TYR A 221       7.989  64.372  10.770  1.00 90.23           O
ANISOU 1072  OH  TYR A 221    13143   7760  13381   1109   3270    666       O
ATOM   1073  N   GLN A 222       2.537  63.189   6.882  1.00 76.64           N
ANISOU 1073  N   GLN A 222     9949   5678  13491    909   3343    894       N
ATOM   1074  CA  GLN A 222       1.887  62.236   7.788  1.00 78.52           C
ANISOU 1074  CA  GLN A 222    10226   5716  13890    948   3606    991       C
ATOM   1075  C   GLN A 222       1.809  60.828   7.158  1.00 81.18           C
ANISOU 1075  C   GLN A 222    10389   6041  14414    916   3447    972       C
ATOM   1076  O   GLN A 222       2.054  59.836   7.851  1.00 80.56           O
ANISOU 1076  O   GLN A 222    10435   5900  14275    947   3553   1001       O
ATOM   1077  CB  GLN A 222       0.475  62.686   8.226  1.00 82.34           C
ANISOU 1077  CB  GLN A 222    10599   5967  14719    970   3924   1112       C
ATOM   1078  CG  GLN A 222       0.163  64.163   8.471  1.00106.68           C
ANISOU 1078  CG  GLN A 222    13720   9038  17775    981   4050   1136       C
ATOM   1079  CD  GLN A 222       0.770  64.836   9.682  1.00137.48           C
ANISOU 1079  CD  GLN A 222    17977  12943  21317   1043   4252   1151       C
ATOM   1080  OE1 GLN A 222       0.056  65.458  10.464  1.00138.80           O
ANISOU 1080  OE1 GLN A 222    18218  12944  21575   1085   4564   1242       O
ATOM   1081  NE2 GLN A 222       2.064  65.111   9.613  1.00128.96           N
ANISOU 1081  NE2 GLN A 222    17080  12071  19849   1040   4036   1048       N
ATOM   1082  N   LYS A 223       1.488  60.749   5.841  1.00 76.11           N
ANISOU 1082  N   LYS A 223     9476   5456  13987    858   3186    921       N
ATOM   1083  CA  LYS A 223       1.413  59.512   5.057  1.00 74.66           C
ANISOU 1083  CA  LYS A 223     9114   5271  13983    822   2986    888       C
ATOM   1084  C   LYS A 223       2.771  58.811   5.120  1.00 78.19           C
ANISOU 1084  C   LYS A 223     9752   5885  14073    824   2826    807       C
ATOM   1085  O   LYS A 223       2.830  57.633   5.491  1.00 80.78           O
ANISOU 1085  O   LYS A 223    10105   6149  14438    835   2875    829       O
ATOM   1086  CB  LYS A 223       1.025  59.851   3.591  1.00 75.24           C
ANISOU 1086  CB  LYS A 223     8930   5398  14260    769   2697    829       C
ATOM   1087  CG  LYS A 223       0.667  58.684   2.625  1.00 74.88           C
ANISOU 1087  CG  LYS A 223     8661   5310  14481    732   2474    798       C
ATOM   1088  CD  LYS A 223       1.857  57.777   2.083  1.00 83.28           C
ANISOU 1088  CD  LYS A 223     9815   6544  15281    713   2217    699       C
ATOM   1089  CE  LYS A 223       2.855  58.305   1.010  1.00 91.82           C
ANISOU 1089  CE  LYS A 223    10949   7845  16093    688   1907    582       C
ATOM   1090  NZ  LYS A 223       4.334  58.026   1.240  1.00 66.52           N
ANISOU 1090  NZ  LYS A 223     7979   4819  12479    696   1840    513       N
ATOM   1091  N   ALA A 224       3.852  59.533   4.750  1.00 72.18           N
ANISOU 1091  N   ALA A 224     9113   5324  12987    813   2639    716       N
ATOM   1092  CA  ALA A 224       5.207  59.000   4.684  1.00 71.34           C
ANISOU 1092  CA  ALA A 224     9164   5379  12562    811   2461    631       C
ATOM   1093  C   ALA A 224       5.829  58.633   6.030  1.00 76.23           C
ANISOU 1093  C   ALA A 224    10059   5971  12934    864   2638    660       C
ATOM   1094  O   ALA A 224       6.302  57.516   6.173  1.00 75.63           O
ANISOU 1094  O   ALA A 224    10035   5910  12790    868   2576    641       O
ATOM   1095  CB  ALA A 224       6.105  59.952   3.917  1.00 70.68           C
ANISOU 1095  CB  ALA A 224     9117   5487  12252    788   2241    533       C
ATOM   1096  N   VAL A 225       5.829  59.556   7.009  1.00 74.67           N
ANISOU 1096  N   VAL A 225    10050   5724  12596    910   2848    703       N
ATOM   1097  CA  VAL A 225       6.424  59.362   8.338  1.00 75.45           C
ANISOU 1097  CA  VAL A 225    10458   5782  12429    974   3009    728       C
ATOM   1098  C   VAL A 225       5.874  58.132   9.115  1.00 81.77           C
ANISOU 1098  C   VAL A 225    11302   6406  13362   1013   3217    816       C
ATOM   1099  O   VAL A 225       6.622  57.482   9.857  1.00 82.72           O
ANISOU 1099  O   VAL A 225    11648   6527  13253   1055   3233    808       O
ATOM   1100  CB  VAL A 225       6.434  60.699   9.140  1.00 80.18           C
ANISOU 1100  CB  VAL A 225    11255   6355  12856   1017   3177    752       C
ATOM   1101  CG1 VAL A 225       5.133  60.944   9.896  1.00 81.92           C
ANISOU 1101  CG1 VAL A 225    11473   6353  13298   1057   3528    878       C
ATOM   1102  CG2 VAL A 225       7.639  60.799  10.062  1.00 80.07           C
ANISOU 1102  CG2 VAL A 225    11573   6399  12452   1069   3150    707       C
ATOM   1103  N   ALA A 226       4.586  57.793   8.888  1.00 79.03           N
ANISOU 1103  N   ALA A 226    10729   5899  13401    998   3362    897       N
ATOM   1104  CA  ALA A 226       3.873  56.678   9.517  1.00 80.19           C
ANISOU 1104  CA  ALA A 226    10865   5850  13755   1031   3589    990       C
ATOM   1105  C   ALA A 226       4.164  55.332   8.869  1.00 83.87           C
ANISOU 1105  C   ALA A 226    11199   6366  14302    995   3389    946       C
ATOM   1106  O   ALA A 226       3.809  54.293   9.438  1.00 84.75           O
ANISOU 1106  O   ALA A 226    11344   6338  14519   1026   3552   1010       O
ATOM   1107  CB  ALA A 226       2.377  56.941   9.498  1.00 82.42           C
ANISOU 1107  CB  ALA A 226    10928   5928  14459   1028   3819   1090       C
ATOM   1108  N   GLU A 227       4.802  55.345   7.685  1.00 79.17           N
ANISOU 1108  N   GLU A 227    10466   5958  13658    932   3049    839       N
ATOM   1109  CA  GLU A 227       5.147  54.141   6.930  1.00 78.44           C
ANISOU 1109  CA  GLU A 227    10248   5929  13626    893   2827    784       C
ATOM   1110  C   GLU A 227       6.223  53.299   7.612  1.00 83.22           C
ANISOU 1110  C   GLU A 227    11088   6591  13941    926   2804    758       C
ATOM   1111  O   GLU A 227       7.151  53.849   8.214  1.00 82.90           O
ANISOU 1111  O   GLU A 227    11293   6639  13567    959   2792    724       O
ATOM   1112  CB  GLU A 227       5.634  54.495   5.512  1.00 77.65           C
ANISOU 1112  CB  GLU A 227     9999   6013  13493    830   2485    674       C
ATOM   1113  CG  GLU A 227       4.540  54.853   4.523  1.00 84.03           C
ANISOU 1113  CG  GLU A 227    10521   6758  14647    789   2414    684       C
ATOM   1114  CD  GLU A 227       4.975  54.849   3.068  1.00 89.69           C
ANISOU 1114  CD  GLU A 227    11106   7624  15347    736   2068    578       C
ATOM   1115  OE1 GLU A 227       6.014  54.219   2.750  1.00 67.99           O
ANISOU 1115  OE1 GLU A 227     8443   5004  12387    724   1895    505       O
ATOM   1116  OE2 GLU A 227       4.225  55.404   2.234  1.00 73.87           O
ANISOU 1116  OE2 GLU A 227     8914   5589  13564    709   1974    573       O
ATOM   1117  N   PRO A 228       6.147  51.967   7.460  1.00 80.01           N
ANISOU 1117  N   PRO A 228    10598   6137  13664    916   2768    766       N
ATOM   1118  CA  PRO A 228       7.220  51.098   7.982  1.00 79.75           C
ANISOU 1118  CA  PRO A 228    10770   6167  13364    943   2709    734       C
ATOM   1119  C   PRO A 228       8.398  51.063   6.989  1.00 82.24           C
ANISOU 1119  C   PRO A 228    11056   6702  13488    893   2366    608       C
ATOM   1120  O   PRO A 228       8.333  51.732   5.951  1.00 82.06           O
ANISOU 1120  O   PRO A 228    10879   6772  13529    845   2197    553       O
ATOM   1121  CB  PRO A 228       6.544  49.723   8.070  1.00 82.52           C
ANISOU 1121  CB  PRO A 228    11001   6374  13980    944   2809    794       C
ATOM   1122  CG  PRO A 228       5.102  49.935   7.568  1.00 87.85           C
ANISOU 1122  CG  PRO A 228    11394   6903  15082    916   2911    853       C
ATOM   1123  CD  PRO A 228       5.112  51.175   6.772  1.00 82.30           C
ANISOU 1123  CD  PRO A 228    10600   6311  14359    878   2758    798       C
ATOM   1124  N   ILE A 229       9.461  50.276   7.277  1.00 77.00           N
ANISOU 1124  N   ILE A 229    10542   6109  12606    908   2266    566       N
ATOM   1125  CA  ILE A 229      10.630  50.159   6.391  1.00 74.88           C
ANISOU 1125  CA  ILE A 229    10254   6027  12171    866   1967    453       C
ATOM   1126  C   ILE A 229      10.230  49.596   5.021  1.00 78.31           C
ANISOU 1126  C   ILE A 229    10417   6493  12844    801   1787    412       C
ATOM   1127  O   ILE A 229      10.720  50.091   4.003  1.00 76.65           O
ANISOU 1127  O   ILE A 229    10134   6413  12576    761   1576    330       O
ATOM   1128  CB  ILE A 229      11.710  49.268   7.035  1.00 20.00           C
ATOM   1129  CG1 ILE A 229      12.277  49.939   8.288  1.00 20.00           C
ATOM   1130  CG2 ILE A 229      12.818  48.969   6.037  1.00 20.00           C
ATOM   1131  CD1 ILE A 229      13.146  49.029   9.126  1.00 20.00           C
ATOM   1132  N   ASN A 230       9.277  48.618   5.005  1.00 75.75           N
ANISOU 1132  N   ASN A 230     9949   6030  12800    795   1881    473       N
ATOM   1133  CA  ASN A 230       8.666  47.980   3.819  1.00 74.79           C
ANISOU 1133  CA  ASN A 230     9570   5889  12957    742   1728    447       C
ATOM   1134  C   ASN A 230       9.652  47.438   2.801  1.00 74.60           C
ANISOU 1134  C   ASN A 230     9522   6014  12809    702   1445    343       C
ATOM   1135  O   ASN A 230       9.443  47.587   1.587  1.00 73.13           O
ANISOU 1135  O   ASN A 230     9181   5872  12733    660   1253    287       O
ATOM   1136  CB  ASN A 230       7.663  48.928   3.130  1.00 75.54           C
ANISOU 1136  CB  ASN A 230     9481   5942  13280    716   1710    457       C
ATOM   1137  CG  ASN A 230       6.340  49.056   3.808  1.00 82.29           C
ANISOU 1137  CG  ASN A 230    10247   6596  14424    740   1973    566       C
ATOM   1138  OD1 ASN A 230       6.025  48.348   4.767  1.00 83.02           O
ANISOU 1138  OD1 ASN A 230    10401   6556  14586    777   2194    643       O
ATOM   1139  ND2 ASN A 230       5.525  49.944   3.291  1.00 68.23           N
ANISOU 1139  ND2 ASN A 230     8315   4775  12834    722   1958    576       N
ATOM   1140  N   LEU A 231      10.717  46.796   3.283  1.00 69.23           N
ANISOU 1140  N   LEU A 231     9002   5397  11903    720   1419    318       N
ATOM   1141  CA  LEU A 231      11.674  46.233   2.360  1.00 67.80           C
ANISOU 1141  CA  LEU A 231     8802   5341  11617    686   1177    225       C
ATOM   1142  C   LEU A 231      11.026  45.074   1.615  1.00 73.39           C
ANISOU 1142  C   LEU A 231     9322   5979  12585    652   1095    224       C
ATOM   1143  O   LEU A 231      10.139  44.390   2.146  1.00 74.13           O
ANISOU 1143  O   LEU A 231     9348   5928  12890    666   1249    299       O
ATOM   1144  CB  LEU A 231      12.953  45.785   3.074  1.00 67.20           C
ANISOU 1144  CB  LEU A 231     8929   5331  11275    714   1166    203       C
ATOM   1145  CG  LEU A 231      13.769  46.874   3.750  1.00 71.07           C
ANISOU 1145  CG  LEU A 231     9611   5896  11496    746   1188    182       C
ATOM   1146  CD1 LEU A 231      14.165  46.458   5.151  1.00 71.76           C
ANISOU 1146  CD1 LEU A 231     9916   5927  11422    805   1316    226       C
ATOM   1147  CD2 LEU A 231      14.971  47.274   2.906  1.00 71.37           C
ANISOU 1147  CD2 LEU A 231     9656   6087  11375    716    966     78       C
ATOM   1148  N   ASN A 232      11.402  44.939   0.350  1.00 69.76           N
ANISOU 1148  N   ASN A 232     8776   5605  12124    612    860    140       N
ATOM   1149  CA  ASN A 232      10.992  43.870  -0.546  1.00 70.40           C
ANISOU 1149  CA  ASN A 232     8701   5637  12409    579    723    113       C
ATOM   1150  C   ASN A 232      12.255  43.598  -1.363  1.00 73.76           C
ANISOU 1150  C   ASN A 232     9200   6203  12623    559    517     17       C
ATOM   1151  O   ASN A 232      12.357  43.983  -2.527  1.00 74.30           O
ANISOU 1151  O   ASN A 232     9219   6324  12685    536    338    -50       O
ATOM   1152  CB  ASN A 232       9.790  44.287  -1.405  1.00 69.29           C
ANISOU 1152  CB  ASN A 232     8372   5416  12540    557    649    116       C
ATOM   1153  CG  ASN A 232       9.298  43.233  -2.378  1.00 85.33           C
ANISOU 1153  CG  ASN A 232    10244   7376  14803    526    481     83       C
ATOM   1154  OD1 ASN A 232       9.316  42.015  -2.119  1.00 92.22           O
ANISOU 1154  OD1 ASN A 232    11086   8187  15767    524    515    101       O
ATOM   1155  ND2 ASN A 232       8.844  43.683  -3.532  1.00 68.40           N
ANISOU 1155  ND2 ASN A 232     8004   5230  12753    506    287     30       N
ATOM   1156  N   MET A 233      13.258  43.011  -0.699  1.00 67.47           N
ANISOU 1156  N   MET A 233     8538   5457  11642    575    553     12       N
ATOM   1157  CA  MET A 233      14.543  42.779  -1.319  1.00 65.37           C
ANISOU 1157  CA  MET A 233     8347   5310  11181    561    393    -71       C
ATOM   1158  C   MET A 233      14.498  41.586  -2.243  1.00 71.87           C
ANISOU 1158  C   MET A 233     9074   6111  12122    531    252   -111       C
ATOM   1159  O   MET A 233      14.290  40.470  -1.759  1.00 72.41           O
ANISOU 1159  O   MET A 233     9117   6110  12286    534    312    -75       O
ATOM   1160  CB  MET A 233      15.656  42.648  -0.271  1.00 66.98           C
ANISOU 1160  CB  MET A 233     8722   5563  11164    591    464    -65       C
ATOM   1161  CG  MET A 233      15.812  43.873   0.612  1.00 70.93           C
ANISOU 1161  CG  MET A 233     9344   6085  11523    625    578    -38       C
ATOM   1162  SD  MET A 233      17.298  43.860   1.627  1.00 75.37           S
ANISOU 1162  SD  MET A 233    10119   6708  11811    661    581    -59       S
ATOM   1163  CE  MET A 233      18.558  44.096   0.343  1.00 70.80           C
ANISOU 1163  CE  MET A 233     9515   6259  11126    624    363   -172       C
ATOM   1164  N   PRO A 234      14.671  41.774  -3.578  1.00 69.93           N
ANISOU 1164  N   PRO A 234     8788   5913  11870    507     67   -186       N
ATOM   1165  CA  PRO A 234      14.684  40.607  -4.477  1.00 69.93           C
ANISOU 1165  CA  PRO A 234     8724   5885  11963    483    -77   -230       C
ATOM   1166  C   PRO A 234      15.961  39.777  -4.282  1.00 76.17           C
ANISOU 1166  C   PRO A 234     9614   6740  12586    483    -95   -262       C
ATOM   1167  O   PRO A 234      16.999  40.332  -3.918  1.00 76.04           O
ANISOU 1167  O   PRO A 234     9713   6810  12366    497    -68   -281       O
ATOM   1168  CB  PRO A 234      14.600  41.231  -5.874  1.00 71.08           C
ANISOU 1168  CB  PRO A 234     8853   6057  12098    472   -254   -299       C
ATOM   1169  CG  PRO A 234      15.202  42.555  -5.733  1.00 74.91           C
ANISOU 1169  CG  PRO A 234     9434   6634  12394    487   -212   -311       C
ATOM   1170  CD  PRO A 234      14.943  43.025  -4.320  1.00 70.91           C
ANISOU 1170  CD  PRO A 234     8949   6113  11882    507    -14   -235       C
ATOM   1171  N   ASN A 235      15.882  38.449  -4.446  1.00 74.68           N
ANISOU 1171  N   ASN A 235     9374   6499  12501    469   -135   -265       N
ATOM   1172  CA  ASN A 235      17.095  37.661  -4.300  1.00 74.42           C
ANISOU 1172  CA  ASN A 235     9429   6523  12325    469   -157   -295       C
ATOM   1173  C   ASN A 235      17.833  37.660  -5.623  1.00 76.93           C
ANISOU 1173  C   ASN A 235     9781   6899  12549    452   -322   -383       C
ATOM   1174  O   ASN A 235      17.320  37.172  -6.650  1.00 77.58           O
ANISOU 1174  O   ASN A 235     9801   6933  12743    436   -446   -419       O
ATOM   1175  CB  ASN A 235      16.854  36.269  -3.731  1.00 77.16           C
ANISOU 1175  CB  ASN A 235     9731   6795  12790    467   -100   -253       C
ATOM   1176  CG  ASN A 235      18.038  35.343  -3.864  1.00101.24           C
ANISOU 1176  CG  ASN A 235    12849   9894  15724    461   -158   -294       C
ATOM   1177  OD1 ASN A 235      18.006  34.425  -4.680  1.00 92.92           O
ANISOU 1177  OD1 ASN A 235    11742   8813  14752    439   -261   -332       O
ATOM   1178  ND2 ASN A 235      19.120  35.593  -3.114  1.00 91.96           N
ANISOU 1178  ND2 ASN A 235    11793   8785  14364    482   -108   -293       N
ATOM   1179  N   ARG A 236      19.008  38.286  -5.599  1.00 69.50           N
ANISOU 1179  N   ARG A 236     8948   6049  11411    462   -320   -418       N
ATOM   1180  CA  ARG A 236      19.865  38.430  -6.763  1.00 67.74           C
ANISOU 1180  CA  ARG A 236     8783   5874  11082    455   -432   -496       C
ATOM   1181  C   ARG A 236      20.845  37.243  -6.956  1.00 70.21           C
ANISOU 1181  C   ARG A 236     9130   6193  11355    446   -469   -528       C
ATOM   1182  O   ARG A 236      21.486  37.119  -8.009  1.00 69.04           O
ANISOU 1182  O   ARG A 236     9031   6059  11143    442   -551   -590       O
ATOM   1183  CB  ARG A 236      20.555  39.771  -6.690  1.00 66.87           C
ANISOU 1183  CB  ARG A 236     8750   5837  10822    471   -398   -515       C
ATOM   1184  CG  ARG A 236      19.529  40.926  -6.831  1.00 70.69           C
ANISOU 1184  CG  ARG A 236     9196   6309  11352    478   -388   -494       C
ATOM   1185  CD  ARG A 236      20.152  42.290  -6.920  1.00 64.70           C
ANISOU 1185  CD  ARG A 236     8510   5620  10454    493   -359   -517       C
ATOM   1186  NE  ARG A 236      21.185  42.351  -7.959  1.00 62.05           N
ANISOU 1186  NE  ARG A 236     8246   5317  10012    494   -429   -587       N
ATOM   1187  CZ  ARG A 236      22.482  42.523  -7.719  1.00 64.86           C
ANISOU 1187  CZ  ARG A 236     8667   5719  10258    500   -394   -614       C
ATOM   1188  NH1 ARG A 236      22.926  42.658  -6.465  1.00 34.11           N
ANISOU 1188  NH1 ARG A 236     4784   1847   6327    507   -318   -582       N
ATOM   1189  NH2 ARG A 236      23.345  42.578  -8.725  1.00 44.88           N
ANISOU 1189  NH2 ARG A 236     6196   3197   7658    505   -434   -672       N
ATOM   1190  N   ASP A 237      20.893  36.334  -5.959  1.00 66.18           N
ANISOU 1190  N   ASP A 237     8599   5657  10887    447   -401   -482       N
ATOM   1191  CA  ASP A 237      21.735  35.143  -5.985  1.00 65.16           C
ANISOU 1191  CA  ASP A 237     8492   5526  10739    439   -427   -503       C
ATOM   1192  C   ASP A 237      20.859  33.928  -6.264  1.00 65.64           C
ANISOU 1192  C   ASP A 237     8466   5509  10966    421   -463   -489       C
ATOM   1193  O   ASP A 237      20.559  33.170  -5.341  1.00 65.74           O
ANISOU 1193  O   ASP A 237     8445   5480  11051    426   -386   -434       O
ATOM   1194  CB  ASP A 237      22.537  34.991  -4.666  1.00 67.50           C
ANISOU 1194  CB  ASP A 237     8848   5847  10954    458   -340   -466       C
ATOM   1195  CG  ASP A 237      23.680  35.970  -4.456  1.00 86.07           C
ANISOU 1195  CG  ASP A 237    11282   8264  13157    473   -337   -497       C
ATOM   1196  OD1 ASP A 237      23.994  36.740  -5.402  1.00 87.36           O
ANISOU 1196  OD1 ASP A 237    11459   8460  13273    467   -385   -548       O
ATOM   1197  OD2 ASP A 237      24.302  35.933  -3.361  1.00 95.87           O
ANISOU 1197  OD2 ASP A 237    12582   9513  14332    495   -292   -471       O
ATOM   1198  N   LEU A 238      20.450  33.752  -7.547  1.00 60.57           N
ANISOU 1198  N   LEU A 238     7798   4835  10383    406   -584   -540       N
ATOM   1199  CA  LEU A 238      19.574  32.666  -8.034  1.00 61.50           C
ANISOU 1199  CA  LEU A 238     7829   4863  10675    389   -659   -543       C
ATOM   1200  C   LEU A 238      20.282  31.306  -8.074  1.00 64.58           C
ANISOU 1200  C   LEU A 238     8234   5243  11062    378   -673   -560       C
ATOM   1201  O   LEU A 238      21.169  31.098  -8.910  1.00 63.55           O
ANISOU 1201  O   LEU A 238     8181   5138  10826    375   -738   -619       O
ATOM   1202  CB  LEU A 238      19.042  32.958  -9.445  1.00 62.33           C
ANISOU 1202  CB  LEU A 238     7938   4929  10815    385   -815   -604       C
ATOM   1203  CG  LEU A 238      18.618  34.362  -9.811  1.00 67.29           C
ANISOU 1203  CG  LEU A 238     8589   5580  11398    399   -841   -613       C
ATOM   1204  CD1 LEU A 238      18.409  34.458 -11.315  1.00 68.24           C
ANISOU 1204  CD1 LEU A 238     8771   5660  11499    405  -1014   -687       C
ATOM   1205  CD2 LEU A 238      17.378  34.787  -9.039  1.00 69.87           C
ANISOU 1205  CD2 LEU A 238     8799   5858  11891    400   -776   -547       C
ATOM   1206  N   ASN A 239      19.884  30.376  -7.192  1.00 60.65           N
ANISOU 1206  N   ASN A 239     7665   4694  10684    374   -600   -505       N
ATOM   1207  CA  ASN A 239      20.504  29.052  -7.106  1.00 59.86           C
ANISOU 1207  CA  ASN A 239     7572   4580  10594    364   -602   -512       C
ATOM   1208  C   ASN A 239      19.458  28.099  -6.553  1.00 60.98           C
ANISOU 1208  C   ASN A 239     7598   4625  10946    358   -555   -458       C
ATOM   1209  O   ASN A 239      19.418  27.808  -5.353  1.00 59.44           O
ANISOU 1209  O   ASN A 239     7398   4416  10772    375   -421   -389       O
ATOM   1210  CB  ASN A 239      21.777  29.147  -6.233  1.00 60.18           C
ANISOU 1210  CB  ASN A 239     7700   4692  10474    381   -516   -494       C
ATOM   1211  CG  ASN A 239      22.498  27.865  -5.990  1.00 65.81           C
ANISOU 1211  CG  ASN A 239     8423   5392  11189    375   -509   -494       C
ATOM   1212  OD1 ASN A 239      22.758  27.069  -6.900  1.00 54.96           O
ANISOU 1212  OD1 ASN A 239     7044   3997   9842    356   -592   -544       O
ATOM   1213  ND2 ASN A 239      22.847  27.667  -4.741  1.00 54.46           N
ANISOU 1213  ND2 ASN A 239     7016   3962   9715    397   -411   -439       N
ATOM   1214  N   ASN A 240      18.556  27.704  -7.440  1.00 58.41           N
ANISOU 1214  N   ASN A 240     7189   4220  10783    340   -667   -489       N
ATOM   1215  CA  ASN A 240      17.383  26.896  -7.142  1.00 60.67           C
ANISOU 1215  CA  ASN A 240     7335   4388  11327    331   -645   -447       C
ATOM   1216  C   ASN A 240      17.368  25.498  -7.791  1.00 64.79           C
ANISOU 1216  C   ASN A 240     7814   4845  11958    309   -746   -488       C
ATOM   1217  O   ASN A 240      16.460  24.725  -7.478  1.00 63.51           O
ANISOU 1217  O   ASN A 240     7526   4576  12028    302   -717   -452       O
ATOM   1218  CB  ASN A 240      16.134  27.670  -7.632  1.00 66.13           C
ANISOU 1218  CB  ASN A 240     7935   5011  12182    328   -717   -451       C
ATOM   1219  CG  ASN A 240      15.604  28.694  -6.671  1.00106.32           C
ANISOU 1219  CG  ASN A 240    13008  10112  17276    348   -575   -383       C
ATOM   1220  OD1 ASN A 240      14.713  28.410  -5.859  1.00107.43           O
ANISOU 1220  OD1 ASN A 240    13051  10165  17602    356   -442   -308       O
ATOM   1221  ND2 ASN A 240      16.121  29.915  -6.761  1.00101.30           N
ANISOU 1221  ND2 ASN A 240    12470   9572  16446    359   -589   -406       N
ATOM   1222  N   ILE A 241      18.313  25.196  -8.734  1.00 62.51           N
ANISOU 1222  N   ILE A 241     7626   4605  11520    301   -857   -563       N
ATOM   1223  CA  ILE A 241      18.316  23.938  -9.527  1.00 63.11           C
ANISOU 1223  CA  ILE A 241     7684   4614  11681    282   -972   -613       C
ATOM   1224  C   ILE A 241      19.129  22.810  -8.885  1.00 64.32           C
ANISOU 1224  C   ILE A 241     7850   4786  11803    277   -876   -587       C
ATOM   1225  O   ILE A 241      18.588  21.724  -8.662  1.00 65.07           O
ANISOU 1225  O   ILE A 241     7849   4797  12078    266   -866   -566       O
ATOM   1226  CB  ILE A 241      18.664  24.199 -11.035  1.00 66.15           C
ANISOU 1226  CB  ILE A 241     8183   5005  11947    282  -1151   -710       C
ATOM   1227  CG1 ILE A 241      17.667  25.206 -11.653  1.00 67.04           C
ANISOU 1227  CG1 ILE A 241     8273   5076  12124    291  -1265   -733       C
ATOM   1228  CG2 ILE A 241      18.738  22.889 -11.865  1.00 65.59           C
ANISOU 1228  CG2 ILE A 241     8123   4858  11939    267  -1270   -768       C
ATOM   1229  CD1 ILE A 241      18.224  26.006 -12.694  1.00 75.52           C
ANISOU 1229  CD1 ILE A 241     9502   6188  13004    308  -1369   -802       C
ATOM   1230  N   HIS A 242      20.413  23.085  -8.606  1.00 57.96           N
ANISOU 1230  N   HIS A 242     7157   4080  10785    288   -813   -589       N
ATOM   1231  CA  HIS A 242      21.374  22.201  -7.962  1.00 57.41           C
ANISOU 1231  CA  HIS A 242     7119   4038  10657    290   -730   -565       C
ATOM   1232  C   HIS A 242      22.138  23.092  -7.000  1.00 60.62           C
ANISOU 1232  C   HIS A 242     7597   4531  10904    314   -622   -525       C
ATOM   1233  O   HIS A 242      23.244  23.570  -7.304  1.00 58.89           O
ANISOU 1233  O   HIS A 242     7471   4381  10525    319   -641   -562       O
ATOM   1234  CB  HIS A 242      22.265  21.486  -9.003  1.00 58.44           C
ANISOU 1234  CB  HIS A 242     7320   4172  10712    275   -821   -638       C
ATOM   1235  CG  HIS A 242      21.489  20.569  -9.903  1.00 63.12           C
ANISOU 1235  CG  HIS A 242     7859   4667  11456    255   -940   -682       C
ATOM   1236  ND1 HIS A 242      20.639  19.600  -9.384  1.00 65.96           N
ANISOU 1236  ND1 HIS A 242     8093   4944  12023    245   -914   -641       N
ATOM   1237  CD2 HIS A 242      21.412  20.543 -11.254  1.00 65.37           C
ANISOU 1237  CD2 HIS A 242     8209   4915  11716    250  -1088   -762       C
ATOM   1238  CE1 HIS A 242      20.081  19.012 -10.431  1.00 66.41           C
ANISOU 1238  CE1 HIS A 242     8128   4918  12189    229  -1060   -702       C
ATOM   1239  NE2 HIS A 242      20.515  19.544 -11.579  1.00 66.45           N
ANISOU 1239  NE2 HIS A 242     8256   4944  12047    234  -1176   -777       N
ATOM   1240  N   PRO A 243      21.477  23.436  -5.868  1.00 57.50           N
ANISOU 1240  N   PRO A 243     7164   4119  10565    334   -509   -449       N
ATOM   1241  CA  PRO A 243      22.044  24.445  -4.959  1.00 57.26           C
ANISOU 1241  CA  PRO A 243     7216   4157  10381    363   -424   -414       C
ATOM   1242  C   PRO A 243      23.452  24.268  -4.407  1.00 59.65           C
ANISOU 1242  C   PRO A 243     7616   4519  10531    379   -400   -415       C
ATOM   1243  O   PRO A 243      24.201  25.252  -4.302  1.00 63.21           O
ANISOU 1243  O   PRO A 243     8141   5036  10841    392   -407   -434       O
ATOM   1244  CB  PRO A 243      20.963  24.618  -3.894  1.00 59.55           C
ANISOU 1244  CB  PRO A 243     7459   4387  10779    385   -296   -330       C
ATOM   1245  CG  PRO A 243      19.714  24.188  -4.579  1.00 64.17           C
ANISOU 1245  CG  PRO A 243     7913   4882  11586    361   -345   -339       C
ATOM   1246  CD  PRO A 243      20.134  23.029  -5.411  1.00 59.08           C
ANISOU 1246  CD  PRO A 243     7249   4220  10979    334   -449   -393       C
ATOM   1247  N   TYR A 244      23.822  23.052  -4.091  1.00 50.70           N
ANISOU 1247  N   TYR A 244     6475   3353   9437    378   -380   -399       N
ATOM   1248  CA  TYR A 244      25.137  22.765  -3.560  1.00 48.95           C
ANISOU 1248  CA  TYR A 244     6331   3168   9099    394   -374   -399       C
ATOM   1249  C   TYR A 244      26.240  22.988  -4.629  1.00 51.60           C
ANISOU 1249  C   TYR A 244     6698   3551   9355    374   -466   -479       C
ATOM   1250  O   TYR A 244      27.332  23.495  -4.301  1.00 53.04           O
ANISOU 1250  O   TYR A 244     6945   3777   9432    390   -471   -490       O
ATOM   1251  CB  TYR A 244      25.158  21.350  -2.965  1.00 49.82           C
ANISOU 1251  CB  TYR A 244     6422   3221   9287    401   -326   -358       C
ATOM   1252  CG  TYR A 244      24.572  21.261  -1.567  1.00 49.63           C
ANISOU 1252  CG  TYR A 244     6430   3150   9278    443   -200   -268       C
ATOM   1253  CD1 TYR A 244      25.155  21.947  -0.492  1.00 52.34           C
ANISOU 1253  CD1 TYR A 244     6892   3519   9475    489   -158   -234       C
ATOM   1254  CD2 TYR A 244      23.476  20.453  -1.302  1.00 48.57           C
ANISOU 1254  CD2 TYR A 244     6221   2928   9307    444   -117   -217       C
ATOM   1255  CE1 TYR A 244      24.658  21.821   0.810  1.00 52.65           C
ANISOU 1255  CE1 TYR A 244     7003   3499   9504    539    -32   -149       C
ATOM   1256  CE2 TYR A 244      22.972  20.318  -0.002  1.00 49.33           C
ANISOU 1256  CE2 TYR A 244     6367   2961   9415    491     30   -128       C
ATOM   1257  CZ  TYR A 244      23.566  21.001   1.051  1.00 56.32           C
ANISOU 1257  CZ  TYR A 244     7400   3873  10126    542     76    -93       C
ATOM   1258  OH  TYR A 244      23.055  20.891   2.332  1.00 58.48           O
ANISOU 1258  OH  TYR A 244     7761   4069  10389    600    231     -3       O
ATOM   1259  N   ALA A 245      25.908  22.716  -5.909  1.00 43.00           N
ANISOU 1259  N   ALA A 245     5573   2443   8323    344   -538   -534       N
ATOM   1260  CA  ALA A 245      26.783  22.914  -7.062  1.00 40.91           C
ANISOU 1260  CA  ALA A 245     5356   2198   7989    330   -602   -607       C
ATOM   1261  C   ALA A 245      27.010  24.407  -7.366  1.00 52.01           C
ANISOU 1261  C   ALA A 245     6815   3656   9292    341   -610   -633       C
ATOM   1262  O   ALA A 245      28.136  24.799  -7.642  1.00 54.37           O
ANISOU 1262  O   ALA A 245     7165   3980   9512    346   -608   -666       O
ATOM   1263  CB  ALA A 245      26.190  22.232  -8.267  1.00 41.23           C
ANISOU 1263  CB  ALA A 245     5374   2184   8107    306   -677   -654       C
ATOM   1264  N   GLY A 246      25.946  25.223  -7.332  1.00 49.35           N
ANISOU 1264  N   GLY A 246     6455   3324   8972    345   -614   -618       N
ATOM   1265  CA  GLY A 246      26.045  26.647  -7.580  1.00 47.10           C
ANISOU 1265  CA  GLY A 246     6214   3086   8594    357   -617   -638       C
ATOM   1266  C   GLY A 246      26.762  27.359  -6.461  1.00 50.54           C
ANISOU 1266  C   GLY A 246     6684   3570   8948    380   -554   -605       C
ATOM   1267  O   GLY A 246      27.607  28.220  -6.703  1.00 48.61           O
ANISOU 1267  O   GLY A 246     6488   3362   8619    388   -557   -637       O
ATOM   1268  N   GLU A 247      26.436  26.986  -5.225  1.00 49.72           N
ANISOU 1268  N   GLU A 247     6564   3453   8873    395   -497   -541       N
ATOM   1269  CA  GLU A 247      27.085  27.559  -4.058  1.00 50.49           C
ANISOU 1269  CA  GLU A 247     6720   3579   8884    426   -455   -509       C
ATOM   1270  C   GLU A 247      28.573  27.245  -4.008  1.00 53.46           C
ANISOU 1270  C   GLU A 247     7131   3963   9216    429   -490   -541       C
ATOM   1271  O   GLU A 247      29.350  28.078  -3.578  1.00 51.97           O
ANISOU 1271  O   GLU A 247     6989   3800   8956    448   -499   -551       O
ATOM   1272  CB  GLU A 247      26.386  27.107  -2.772  1.00 52.78           C
ANISOU 1272  CB  GLU A 247     7018   3831   9204    451   -378   -431       C
ATOM   1273  CG  GLU A 247      26.755  27.976  -1.577  1.00 64.14           C
ANISOU 1273  CG  GLU A 247     8550   5287  10532    493   -339   -397       C
ATOM   1274  CD  GLU A 247      26.695  29.480  -1.751  1.00 90.03           C
ANISOU 1274  CD  GLU A 247    11857   8615  13736    498   -345   -419       C
ATOM   1275  OE1 GLU A 247      25.747  30.002  -2.387  1.00 93.77           O
ANISOU 1275  OE1 GLU A 247    12279   9096  14253    481   -334   -425       O
ATOM   1276  OE2 GLU A 247      27.610  30.143  -1.219  1.00 91.50           O
ANISOU 1276  OE2 GLU A 247    12116   8823  13826    523   -369   -431       O
ATOM   1277  N   MET A 248      28.956  26.054  -4.455  1.00 52.43           N
ANISOU 1277  N   MET A 248     6973   3802   9147    411   -512   -557       N
ATOM   1278  CA  MET A 248      30.338  25.588  -4.544  1.00 52.80           C
ANISOU 1278  CA  MET A 248     7034   3838   9191    411   -540   -587       C
ATOM   1279  C   MET A 248      31.176  26.599  -5.352  1.00 56.40           C
ANISOU 1279  C   MET A 248     7508   4315   9607    407   -557   -645       C
ATOM   1280  O   MET A 248      32.255  26.991  -4.911  1.00 54.78           O
ANISOU 1280  O   MET A 248     7320   4109   9387    422   -571   -656       O
ATOM   1281  CB  MET A 248      30.378  24.174  -5.176  1.00 55.05           C
ANISOU 1281  CB  MET A 248     7279   4081   9558    387   -550   -599       C
ATOM   1282  CG  MET A 248      31.771  23.639  -5.371  1.00 58.66           C
ANISOU 1282  CG  MET A 248     7738   4514  10035    383   -568   -630       C
ATOM   1283  SD  MET A 248      31.967  22.170  -6.431  1.00 62.73           S
ANISOU 1283  SD  MET A 248     8223   4975  10635    353   -572   -660       S
ATOM   1284  CE  MET A 248      31.004  22.627  -7.963  1.00 58.31           C
ANISOU 1284  CE  MET A 248     7685   4413  10057    332   -590   -711       C
ATOM   1285  N   VAL A 249      30.648  27.060  -6.493  1.00 54.10           N
ANISOU 1285  N   VAL A 249     7219   4031   9305    391   -558   -680       N
ATOM   1286  CA  VAL A 249      31.319  28.042  -7.346  1.00 54.52           C
ANISOU 1286  CA  VAL A 249     7305   4092   9317    392   -551   -731       C
ATOM   1287  C   VAL A 249      31.442  29.409  -6.611  1.00 59.90           C
ANISOU 1287  C   VAL A 249     8004   4817   9940    413   -541   -720       C
ATOM   1288  O   VAL A 249      32.556  29.958  -6.501  1.00 60.86           O
ANISOU 1288  O   VAL A 249     8133   4931  10059    424   -537   -744       O
ATOM   1289  CB  VAL A 249      30.579  28.164  -8.712  1.00 58.31           C
ANISOU 1289  CB  VAL A 249     7814   4558   9782    381   -564   -768       C
ATOM   1290  CG1 VAL A 249      31.179  29.265  -9.582  1.00 58.23           C
ANISOU 1290  CG1 VAL A 249     7861   4548   9715    392   -538   -814       C
ATOM   1291  CG2 VAL A 249      30.574  26.840  -9.456  1.00 58.00           C
ANISOU 1291  CG2 VAL A 249     7776   4465   9795    364   -584   -788       C
ATOM   1292  N   ARG A 250      30.294  29.947  -6.117  1.00 53.66           N
ANISOU 1292  N   ARG A 250     7214   4059   9117    420   -534   -683       N
ATOM   1293  CA  ARG A 250      30.283  31.229  -5.429  1.00 52.63           C
ANISOU 1293  CA  ARG A 250     7109   3964   8923    441   -520   -670       C
ATOM   1294  C   ARG A 250      31.183  31.230  -4.195  1.00 56.13           C
ANISOU 1294  C   ARG A 250     7576   4400   9351    465   -536   -652       C
ATOM   1295  O   ARG A 250      32.007  32.123  -4.054  1.00 55.24           O
ANISOU 1295  O   ARG A 250     7480   4294   9216    477   -551   -679       O
ATOM   1296  CB  ARG A 250      28.856  31.688  -5.076  1.00 50.10           C
ANISOU 1296  CB  ARG A 250     6784   3664   8589    446   -495   -627       C
ATOM   1297  CG  ARG A 250      28.795  33.161  -4.668  1.00 45.61           C
ANISOU 1297  CG  ARG A 250     6247   3132   7948    464   -474   -624       C
ATOM   1298  CD  ARG A 250      27.758  33.437  -3.591  1.00 63.39           C
ANISOU 1298  CD  ARG A 250     8514   5386  10186    483   -427   -560       C
ATOM   1299  NE  ARG A 250      28.044  32.675  -2.366  1.00 80.77           N
ANISOU 1299  NE  ARG A 250    10754   7557  12379    506   -413   -517       N
ATOM   1300  CZ  ARG A 250      28.833  33.090  -1.373  1.00103.80           C
ANISOU 1300  CZ  ARG A 250    13744  10471  15223    538   -428   -511       C
ATOM   1301  NH1 ARG A 250      29.416  34.282  -1.430  1.00103.62           N
ANISOU 1301  NH1 ARG A 250    13746  10477  15147    546   -453   -546       N
ATOM   1302  NH2 ARG A 250      29.029  32.323  -0.305  1.00 81.69           N
ANISOU 1302  NH2 ARG A 250    11001   7631  12406    567   -425   -470       N
ATOM   1303  N   SER A 251      31.026  30.237  -3.325  1.00 53.83           N
ANISOU 1303  N   SER A 251     7292   4085   9077    476   -540   -609       N
ATOM   1304  CA  SER A 251      31.783  30.145  -2.083  1.00 55.09           C
ANISOU 1304  CA  SER A 251     7501   4221   9208    509   -575   -588       C
ATOM   1305  C   SER A 251      33.291  29.961  -2.290  1.00 57.40           C
ANISOU 1305  C   SER A 251     7772   4482   9554    507   -635   -634       C
ATOM   1306  O   SER A 251      34.080  30.528  -1.534  1.00 56.96           O
ANISOU 1306  O   SER A 251     7752   4410   9481    534   -691   -642       O
ATOM   1307  CB  SER A 251      31.239  29.020  -1.217  1.00 60.35           C
ANISOU 1307  CB  SER A 251     8195   4856   9880    525   -554   -528       C
ATOM   1308  OG  SER A 251      31.382  27.803  -1.921  1.00 77.94           O
ANISOU 1308  OG  SER A 251    10362   7060  12190    498   -559   -540       O
ATOM   1309  N   GLU A 252      33.686  29.192  -3.298  1.00 52.80           N
ANISOU 1309  N   GLU A 252     7134   3880   9049    478   -626   -664       N
ATOM   1310  CA  GLU A 252      35.104  28.959  -3.563  1.00 53.27           C
ANISOU 1310  CA  GLU A 252     7159   3891   9192    475   -660   -704       C
ATOM   1311  C   GLU A 252      35.803  30.163  -4.177  1.00 57.16           C
ANISOU 1311  C   GLU A 252     7633   4378   9704    473   -648   -753       C
ATOM   1312  O   GLU A 252      36.956  30.454  -3.829  1.00 57.08           O
ANISOU 1312  O   GLU A 252     7600   4322   9765    486   -693   -777       O
ATOM   1313  CB  GLU A 252      35.354  27.662  -4.364  1.00 54.24           C
ANISOU 1313  CB  GLU A 252     7238   3976   9394    449   -638   -715       C
ATOM   1314  CG  GLU A 252      35.345  26.419  -3.487  1.00 60.43           C
ANISOU 1314  CG  GLU A 252     8025   4734  10201    459   -672   -674       C
ATOM   1315  CD  GLU A 252      36.572  26.255  -2.605  1.00 83.54           C
ANISOU 1315  CD  GLU A 252    10949   7608  13183    484   -750   -677       C
ATOM   1316  OE1 GLU A 252      37.707  26.239  -3.143  1.00 69.61           O
ANISOU 1316  OE1 GLU A 252     9130   5795  11526    473   -758   -718       O
ATOM   1317  OE2 GLU A 252      36.391  26.123  -1.371  1.00 82.88           O
ANISOU 1317  OE2 GLU A 252    10927   7519  13045    519   -802   -637       O
ATOM   1318  N   LEU A 253      35.105  30.882  -5.061  1.00 52.09           N
ANISOU 1318  N   LEU A 253     7004   3775   9014    461   -590   -768       N
ATOM   1319  CA  LEU A 253      35.701  32.064  -5.663  1.00 51.27           C
ANISOU 1319  CA  LEU A 253     6894   3663   8923    464   -559   -810       C
ATOM   1320  C   LEU A 253      35.860  33.175  -4.640  1.00 56.29           C
ANISOU 1320  C   LEU A 253     7546   4318   9523    488   -604   -805       C
ATOM   1321  O   LEU A 253      36.860  33.897  -4.670  1.00 56.27           O
ANISOU 1321  O   LEU A 253     7516   4277   9588    497   -614   -840       O
ATOM   1322  CB  LEU A 253      34.898  32.537  -6.880  1.00 50.66           C
ANISOU 1322  CB  LEU A 253     6847   3614   8787    452   -496   -826       C
ATOM   1323  CG  LEU A 253      35.039  31.700  -8.143  1.00 54.84           C
ANISOU 1323  CG  LEU A 253     7387   4098   9351    436   -450   -852       C
ATOM   1324  CD1 LEU A 253      33.957  32.035  -9.131  1.00 54.41           C
ANISOU 1324  CD1 LEU A 253     7388   4069   9216    433   -430   -861       C
ATOM   1325  CD2 LEU A 253      36.437  31.847  -8.761  1.00 56.82           C
ANISOU 1325  CD2 LEU A 253     7622   4273   9695    441   -391   -892       C
ATOM   1326  N   VAL A 254      34.885  33.292  -3.730  1.00 53.32           N
ANISOU 1326  N   VAL A 254     7219   3989   9053    502   -626   -761       N
ATOM   1327  CA  VAL A 254      34.880  34.287  -2.663  1.00 54.53           C
ANISOU 1327  CA  VAL A 254     7419   4155   9144    532   -667   -750       C
ATOM   1328  C   VAL A 254      35.944  33.955  -1.595  1.00 59.42           C
ANISOU 1328  C   VAL A 254     8053   4714   9808    559   -769   -754       C
ATOM   1329  O   VAL A 254      36.669  34.854  -1.162  1.00 59.24           O
ANISOU 1329  O   VAL A 254     8037   4666   9807    578   -828   -783       O
ATOM   1330  CB  VAL A 254      33.446  34.559  -2.120  1.00 59.61           C
ANISOU 1330  CB  VAL A 254     8121   4849   9678    542   -629   -698       C
ATOM   1331  CG1 VAL A 254      33.469  35.459  -0.890  1.00 60.74           C
ANISOU 1331  CG1 VAL A 254     8344   4991   9744    580   -667   -681       C
ATOM   1332  CG2 VAL A 254      32.570  35.196  -3.202  1.00 58.82           C
ANISOU 1332  CG2 VAL A 254     7999   4795   9557    520   -560   -707       C
ATOM   1333  N   LYS A 255      36.105  32.664  -1.254  1.00 56.16           N
ANISOU 1333  N   LYS A 255     7642   4270   9428    561   -800   -730       N
ATOM   1334  CA  LYS A 255      37.122  32.208  -0.296  1.00 56.17           C
ANISOU 1334  CA  LYS A 255     7661   4201   9478    590   -914   -734       C
ATOM   1335  C   LYS A 255      38.524  32.624  -0.773  1.00 59.12           C
ANISOU 1335  C   LYS A 255     7946   4511  10005    582   -961   -795       C
ATOM   1336  O   LYS A 255      39.242  33.292  -0.031  1.00 60.95           O
ANISOU 1336  O   LYS A 255     8195   4696  10266    611  -1064   -818       O
ATOM   1337  CB  LYS A 255      37.046  30.675  -0.102  1.00 57.59           C
ANISOU 1337  CB  LYS A 255     7842   4357   9682    588   -920   -700       C
ATOM   1338  CG  LYS A 255      37.792  30.146   1.124  1.00 57.80           C
ANISOU 1338  CG  LYS A 255     7928   4313   9721    631  -1048   -688       C
ATOM   1339  CD  LYS A 255      37.765  28.654   1.209  1.00 60.64           C
ANISOU 1339  CD  LYS A 255     8282   4648  10110    629  -1042   -655       C
ATOM   1340  CE  LYS A 255      39.131  28.012   1.148  1.00 73.87           C
ANISOU 1340  CE  LYS A 255     9886   6242  11939    627  -1135   -687       C
ATOM   1341  NZ  LYS A 255      39.066  26.549   0.810  1.00 65.00           N
ANISOU 1341  NZ  LYS A 255     8726   5104  10865    609  -1097   -661       N
ATOM   1342  N   HIS A 256      38.872  32.299  -2.020  1.00 52.72           N
ANISOU 1342  N   HIS A 256     7049   3688   9296    547   -880   -821       N
ATOM   1343  CA  HIS A 256      40.186  32.594  -2.569  1.00 53.39           C
ANISOU 1343  CA  HIS A 256     7040   3691   9555    539   -884   -871       C
ATOM   1344  C   HIS A 256      40.416  34.011  -3.098  1.00 59.24           C
ANISOU 1344  C   HIS A 256     7755   4431  10323    537   -832   -909       C
ATOM   1345  O   HIS A 256      41.573  34.454  -3.134  1.00 60.10           O
ANISOU 1345  O   HIS A 256     7788   4453  10595    543   -862   -949       O
ATOM   1346  CB  HIS A 256      40.531  31.585  -3.651  1.00 54.92           C
ANISOU 1346  CB  HIS A 256     7173   3847   9847    510   -797   -879       C
ATOM   1347  CG  HIS A 256      40.623  30.193  -3.117  1.00 60.01           C
ANISOU 1347  CG  HIS A 256     7819   4468  10512    512   -855   -850       C
ATOM   1348  ND1 HIS A 256      39.483  29.442  -2.856  1.00 62.57           N
ANISOU 1348  ND1 HIS A 256     8209   4859  10705    509   -841   -804       N
ATOM   1349  CD2 HIS A 256      41.703  29.492  -2.718  1.00 63.35           C
ANISOU 1349  CD2 HIS A 256     8186   4802  11082    520   -933   -858       C
ATOM   1350  CE1 HIS A 256      39.912  28.295  -2.355  1.00 63.20           C
ANISOU 1350  CE1 HIS A 256     8276   4893  10843    516   -899   -785       C
ATOM   1351  NE2 HIS A 256      41.238  28.276  -2.251  1.00 64.16           N
ANISOU 1351  NE2 HIS A 256     8328   4923  11127    523   -961   -817       N
ATOM   1352  N   PHE A 257      39.353  34.693  -3.581  1.00 53.75           N
ANISOU 1352  N   PHE A 257     7111   3820   9493    530   -750   -898       N
ATOM   1353  CA  PHE A 257      39.526  35.971  -4.257  1.00 53.38           C
ANISOU 1353  CA  PHE A 257     7043   3771   9466    528   -680   -931       C
ATOM   1354  C   PHE A 257      38.637  37.124  -3.824  1.00 56.78           C
ANISOU 1354  C   PHE A 257     7539   4280   9757    541   -684   -919       C
ATOM   1355  O   PHE A 257      38.720  38.184  -4.431  1.00 56.14           O
ANISOU 1355  O   PHE A 257     7444   4202   9685    539   -617   -944       O
ATOM   1356  CB  PHE A 257      39.421  35.769  -5.794  1.00 55.15           C
ANISOU 1356  CB  PHE A 257     7256   3987   9711    506   -537   -945       C
ATOM   1357  CG  PHE A 257      40.146  34.568  -6.349  1.00 57.32           C
ANISOU 1357  CG  PHE A 257     7487   4187  10106    493   -504   -952       C
ATOM   1358  CD1 PHE A 257      41.541  34.536  -6.401  1.00 61.35           C
ANISOU 1358  CD1 PHE A 257     7909   4583  10819    497   -499   -983       C
ATOM   1359  CD2 PHE A 257      39.439  33.459  -6.812  1.00 58.90           C
ANISOU 1359  CD2 PHE A 257     7725   4419  10235    477   -478   -929       C
ATOM   1360  CE1 PHE A 257      42.211  33.408  -6.903  1.00 62.81           C
ANISOU 1360  CE1 PHE A 257     8050   4690  11124    486   -456   -986       C
ATOM   1361  CE2 PHE A 257      40.110  32.349  -7.342  1.00 61.18           C
ANISOU 1361  CE2 PHE A 257     7980   4635  10631    466   -441   -936       C
ATOM   1362  CZ  PHE A 257      41.488  32.319  -7.356  1.00 59.86           C
ANISOU 1362  CZ  PHE A 257     7730   4359  10656    470   -427   -962       C
ATOM   1363  N   GLY A 258      37.783  36.909  -2.828  1.00 54.45           N
ANISOU 1363  N   GLY A 258     7317   4036   9336    555   -743   -877       N
ATOM   1364  CA  GLY A 258      36.848  37.915  -2.336  1.00 53.56           C
ANISOU 1364  CA  GLY A 258     7274   3989   9089    569   -734   -857       C
ATOM   1365  C   GLY A 258      35.678  38.228  -3.252  1.00 56.72           C
ANISOU 1365  C   GLY A 258     7687   4460   9406    550   -627   -840       C
ATOM   1366  O   GLY A 258      35.550  37.664  -4.348  1.00 54.58           O
ANISOU 1366  O   GLY A 258     7385   4187   9165    527   -566   -847       O
ATOM   1367  N   GLU A 259      34.828  39.170  -2.807  1.00 54.97           N
ANISOU 1367  N   GLU A 259     7517   4289   9081    562   -612   -819       N
ATOM   1368  CA  GLU A 259      33.626  39.620  -3.521  1.00 55.80           C
ANISOU 1368  CA  GLU A 259     7633   4454   9114    549   -531   -801       C
ATOM   1369  C   GLU A 259      33.823  40.150  -4.938  1.00 62.47           C
ANISOU 1369  C   GLU A 259     8446   5299   9993    533   -463   -839       C
ATOM   1370  O   GLU A 259      32.936  39.997  -5.774  1.00 63.27           O
ANISOU 1370  O   GLU A 259     8557   5426  10056    521   -420   -829       O
ATOM   1371  CB  GLU A 259      32.819  40.580  -2.667  1.00 57.43           C
ANISOU 1371  CB  GLU A 259     7899   4700   9224    569   -525   -771       C
ATOM   1372  CG  GLU A 259      31.432  40.071  -2.302  1.00 75.01           C
ANISOU 1372  CG  GLU A 259    10160   6954  11386    570   -488   -710       C
ATOM   1373  CD  GLU A 259      31.256  38.686  -1.717  1.00109.60           C
ANISOU 1373  CD  GLU A 259    14551  11308  15785    571   -507   -674       C
ATOM   1374  OE1 GLU A 259      31.900  38.379  -0.686  1.00107.66           O
ANISOU 1374  OE1 GLU A 259    14356  11026  15525    597   -565   -665       O
ATOM   1375  OE2 GLU A 259      30.460  37.907  -2.292  1.00106.54           O
ANISOU 1375  OE2 GLU A 259    14125  10929  15427    549   -472   -656       O
ATOM   1376  N   GLN A 260      34.992  40.696  -5.231  1.00 61.77           N
ANISOU 1376  N   GLN A 260     8322   5161   9986    538   -455   -884       N
ATOM   1377  CA  GLN A 260      35.371  41.157  -6.570  1.00 62.69           C
ANISOU 1377  CA  GLN A 260     8425   5250  10145    534   -368   -920       C
ATOM   1378  C   GLN A 260      35.312  40.002  -7.608  1.00 67.58           C
ANISOU 1378  C   GLN A 260     9052   5841  10784    520   -329   -923       C
ATOM   1379  O   GLN A 260      35.234  40.277  -8.811  1.00 68.87           O
ANISOU 1379  O   GLN A 260     9251   5986  10930    522   -251   -942       O
ATOM   1380  CB  GLN A 260      36.781  41.796  -6.532  1.00 64.74           C
ANISOU 1380  CB  GLN A 260     8629   5434  10537    544   -361   -963       C
ATOM   1381  CG  GLN A 260      36.817  43.300  -6.960  1.00 79.10           C
ANISOU 1381  CG  GLN A 260    10452   7258  12346    557   -297   -986       C
ATOM   1382  CD  GLN A 260      35.823  44.228  -6.281  1.00 88.47           C
ANISOU 1382  CD  GLN A 260    11682   8525  13407    564   -327   -961       C
ATOM   1383  OE1 GLN A 260      35.740  44.315  -5.045  1.00 79.58           O
ANISOU 1383  OE1 GLN A 260    10567   7414  12255    573   -413   -948       O
ATOM   1384  NE2 GLN A 260      35.055  44.955  -7.089  1.00 86.70           N
ANISOU 1384  NE2 GLN A 260    11498   8344  13100    565   -253   -954       N
ATOM   1385  N   ALA A 261      35.329  38.720  -7.136  1.00 61.59           N
ANISOU 1385  N   ALA A 261     8277   5072  10051    509   -383   -903       N
ATOM   1386  CA  ALA A 261      35.237  37.550  -8.004  1.00 61.20           C
ANISOU 1386  CA  ALA A 261     8238   4995  10019    495   -358   -905       C
ATOM   1387  C   ALA A 261      33.833  37.381  -8.611  1.00 64.67           C
ANISOU 1387  C   ALA A 261     8729   5483  10359    488   -354   -886       C
ATOM   1388  O   ALA A 261      33.698  36.726  -9.657  1.00 65.08           O
ANISOU 1388  O   ALA A 261     8817   5503  10408    483   -328   -902       O
ATOM   1389  CB  ALA A 261      35.662  36.288  -7.269  1.00 61.88           C
ANISOU 1389  CB  ALA A 261     8287   5056  10167    487   -418   -888       C
ATOM   1390  N   ILE A 262      32.810  37.996  -7.974  1.00 60.08           N
ANISOU 1390  N   ILE A 262     8155   4964   9707    491   -382   -855       N
ATOM   1391  CA  ILE A 262      31.396  37.937  -8.382  1.00 60.32           C
ANISOU 1391  CA  ILE A 262     8211   5029   9680    485   -394   -833       C
ATOM   1392  C   ILE A 262      30.999  39.138  -9.228  1.00 68.84           C
ANISOU 1392  C   ILE A 262     9333   6121  10702    497   -359   -853       C
ATOM   1393  O   ILE A 262      30.039  39.051  -9.999  1.00 68.77           O
ANISOU 1393  O   ILE A 262     9358   6112  10660    496   -378   -853       O
ATOM   1394  CB  ILE A 262      30.454  37.706  -7.169  1.00 62.87           C
ANISOU 1394  CB  ILE A 262     8511   5389   9989    483   -426   -779       C
ATOM   1395  CG1 ILE A 262      30.964  36.566  -6.224  1.00 63.08           C
ANISOU 1395  CG1 ILE A 262     8515   5393  10060    481   -456   -757       C
ATOM   1396  CG2 ILE A 262      29.004  37.459  -7.594  1.00 63.31           C
ANISOU 1396  CG2 ILE A 262     8562   5455  10038    473   -440   -755       C
ATOM   1397  CD1 ILE A 262      31.291  35.118  -6.860  1.00 56.00           C
ANISOU 1397  CD1 ILE A 262     7600   4453   9224    463   -471   -770       C
ATOM   1398  N   ASP A 263      31.775  40.245  -9.125  1.00 67.83           N
ANISOU 1398  N   ASP A 263     9208   5994  10572    511   -315   -873       N
ATOM   1399  CA  ASP A 263      31.538  41.452  -9.910  1.00 68.69           C
ANISOU 1399  CA  ASP A 263     9363   6110  10627    527   -269   -891       C
ATOM   1400  C   ASP A 263      32.158  41.396 -11.326  1.00 77.27           C
ANISOU 1400  C   ASP A 263    10519   7130  11710    542   -207   -932       C
ATOM   1401  O   ASP A 263      31.901  42.287 -12.132  1.00 79.52           O
ANISOU 1401  O   ASP A 263    10873   7411  11931    561   -173   -945       O
ATOM   1402  CB  ASP A 263      31.958  42.712  -9.135  1.00 69.73           C
ANISOU 1402  CB  ASP A 263     9469   6267  10759    537   -245   -892       C
ATOM   1403  CG  ASP A 263      31.390  42.801  -7.731  1.00 73.57           C
ANISOU 1403  CG  ASP A 263     9924   6802  11226    533   -295   -852       C
ATOM   1404  OD1 ASP A 263      30.281  42.273  -7.500  1.00 72.15           O
ANISOU 1404  OD1 ASP A 263     9745   6648  11022    524   -324   -815       O
ATOM   1405  OD2 ASP A 263      32.068  43.368  -6.856  1.00 78.68           O
ANISOU 1405  OD2 ASP A 263    10555   7448  11892    542   -303   -858       O
ATOM   1406  N   SER A 264      32.889  40.320 -11.650  1.00 74.80           N
ANISOU 1406  N   SER A 264    10205   6759  11458    536   -189   -948       N
ATOM   1407  CA  SER A 264      33.564  40.093 -12.934  1.00 75.20           C
ANISOU 1407  CA  SER A 264    10337   6723  11511    555   -107   -983       C
ATOM   1408  C   SER A 264      32.653  39.735 -14.149  1.00 79.47           C
ANISOU 1408  C   SER A 264    11000   7241  11954    569   -133   -993       C
ATOM   1409  O   SER A 264      33.145  39.802 -15.288  1.00 80.10           O
ANISOU 1409  O   SER A 264    11191   7240  12002    598    -51  -1022       O
ATOM   1410  CB  SER A 264      34.742  39.126 -12.775  1.00 77.93           C
ANISOU 1410  CB  SER A 264    10636   7004  11971    545    -72   -994       C
ATOM   1411  OG  SER A 264      34.384  37.906 -12.145  1.00 87.74           O
ANISOU 1411  OG  SER A 264    11831   8271  13235    520   -159   -972       O
ATOM   1412  N   GLY A 265      31.365  39.369 -13.903  1.00 73.99           N
ANISOU 1412  N   GLY A 265    10291   6601  11222    554   -243   -971       N
ATOM   1413  CA  GLY A 265      30.384  39.029 -14.942  1.00 72.76           C
ANISOU 1413  CA  GLY A 265    10235   6416  10995    567   -312   -984       C
ATOM   1414  C   GLY A 265      30.688  37.808 -15.807  1.00 73.61           C
ANISOU 1414  C   GLY A 265    10426   6443  11100    573   -318  -1011       C
ATOM   1415  O   GLY A 265      30.028  37.584 -16.832  1.00 72.52           O
ANISOU 1415  O   GLY A 265    10410   6255  10888    595   -376  -1034       O
ATOM   1416  N   TYR A 266      31.698  37.011 -15.383  1.00 67.74           N
ANISOU 1416  N   TYR A 266     9623   5678  10437    555   -265  -1009       N
ATOM   1417  CA  TYR A 266      32.189  35.799 -16.025  1.00 67.42           C
ANISOU 1417  CA  TYR A 266     9643   5560  10415    556   -247  -1031       C
ATOM   1418  C   TYR A 266      31.145  34.672 -16.123  1.00 67.64           C
ANISOU 1418  C   TYR A 266     9670   5589  10440    538   -376  -1028       C
ATOM   1419  O   TYR A 266      30.177  34.636 -15.369  1.00 67.81           O
ANISOU 1419  O   TYR A 266     9598   5675  10490    515   -467   -999       O
ATOM   1420  CB  TYR A 266      33.409  35.253 -15.255  1.00 69.36           C
ANISOU 1420  CB  TYR A 266     9783   5793  10779    536   -179  -1021       C
ATOM   1421  CG  TYR A 266      34.703  36.054 -15.275  1.00 72.00           C
ANISOU 1421  CG  TYR A 266    10103   6080  11172    553    -46  -1032       C
ATOM   1422  CD1 TYR A 266      34.918  37.061 -16.216  1.00 75.02           C
ANISOU 1422  CD1 TYR A 266    10599   6413  11492    591     51  -1053       C
ATOM   1423  CD2 TYR A 266      35.733  35.765 -14.386  1.00 72.32           C
ANISOU 1423  CD2 TYR A 266    10021   6111  11347    534    -19  -1023       C
ATOM   1424  CE1 TYR A 266      36.108  37.792 -16.234  1.00 76.96           C
ANISOU 1424  CE1 TYR A 266    10817   6600  11824    608    187  -1063       C
ATOM   1425  CE2 TYR A 266      36.927  36.483 -14.400  1.00 73.46           C
ANISOU 1425  CE2 TYR A 266    10131   6194  11587    549     92  -1036       C
ATOM   1426  CZ  TYR A 266      37.111  37.498 -15.323  1.00 82.91           C
ANISOU 1426  CZ  TYR A 266    11425   7341  12737    584    204  -1055       C
ATOM   1427  OH  TYR A 266      38.297  38.196 -15.328  1.00 85.30           O
ANISOU 1427  OH  TYR A 266    11678   7566  13165    599    326  -1067       O
ATOM   1428  N   LYS A 267      31.353  33.762 -17.067  1.00 61.50           N
ANISOU 1428  N   LYS A 267     9001   4727   9637    550   -375  -1058       N
ATOM   1429  CA  LYS A 267      30.530  32.576 -17.244  1.00 60.91           C
ANISOU 1429  CA  LYS A 267     8930   4634   9580    534   -495  -1063       C
ATOM   1430  C   LYS A 267      31.437  31.418 -16.842  1.00 58.18           C
ANISOU 1430  C   LYS A 267     8519   4265   9321    510   -441  -1056       C
ATOM   1431  O   LYS A 267      32.492  31.217 -17.454  1.00 55.41           O
ANISOU 1431  O   LYS A 267     8250   3839   8964    528   -331  -1078       O
ATOM   1432  CB  LYS A 267      30.082  32.423 -18.706  1.00 65.88           C
ANISOU 1432  CB  LYS A 267     9762   5168  10100    574   -550  -1110       C
ATOM   1433  CG  LYS A 267      28.855  33.229 -19.078  1.00 94.95           C
ANISOU 1433  CG  LYS A 267    13495   8863  13720    593   -672  -1118       C
ATOM   1434  CD  LYS A 267      28.697  33.283 -20.591  1.00113.42           C
ANISOU 1434  CD  LYS A 267    16082  11089  15923    649   -714  -1169       C
ATOM   1435  CE  LYS A 267      27.443  33.992 -21.049  1.00128.67           C
ANISOU 1435  CE  LYS A 267    18077  13014  17799    674   -867  -1183       C
ATOM   1436  NZ  LYS A 267      26.286  33.055 -21.172  1.00139.91           N
ANISOU 1436  NZ  LYS A 267    19461  14405  19292    656  -1070  -1197       N
ATOM   1437  N   VAL A 268      31.067  30.722 -15.763  1.00 53.44           N
ANISOU 1437  N   VAL A 268     7773   3722   8811    473   -500  -1021       N
ATOM   1438  CA  VAL A 268      31.811  29.564 -15.252  1.00 53.08           C
ANISOU 1438  CA  VAL A 268     7654   3658   8854    449   -467  -1009       C
ATOM   1439  C   VAL A 268      31.104  28.299 -15.710  1.00 57.53           C
ANISOU 1439  C   VAL A 268     8245   4179   9434    437   -556  -1023       C
ATOM   1440  O   VAL A 268      29.930  28.048 -15.386  1.00 55.49           O
ANISOU 1440  O   VAL A 268     7927   3949   9206    422   -662  -1006       O
ATOM   1441  CB  VAL A 268      31.976  29.583 -13.715  1.00 55.16           C
ANISOU 1441  CB  VAL A 268     7761   3998   9198    425   -468   -960       C
ATOM   1442  CG1 VAL A 268      32.800  28.391 -13.251  1.00 54.32           C
ANISOU 1442  CG1 VAL A 268     7595   3864   9181    407   -443   -950       C
ATOM   1443  CG2 VAL A 268      32.580  30.900 -13.219  1.00 53.81           C
ANISOU 1443  CG2 VAL A 268     7565   3866   9016    438   -406   -953       C
ATOM   1444  N   TYR A 269      31.832  27.528 -16.502  1.00 57.38           N
ANISOU 1444  N   TYR A 269     8316   4077   9407    447   -506  -1053       N
ATOM   1445  CA  TYR A 269      31.415  26.233 -17.055  1.00 57.64           C
ANISOU 1445  CA  TYR A 269     8395   4049   9455    438   -577  -1075       C
ATOM   1446  C   TYR A 269      32.043  25.152 -16.208  1.00 56.96           C
ANISOU 1446  C   TYR A 269     8187   3974   9481    407   -540  -1046       C
ATOM   1447  O   TYR A 269      33.258  24.930 -16.262  1.00 55.12           O
ANISOU 1447  O   TYR A 269     7962   3702   9280    411   -429  -1048       O
ATOM   1448  CB  TYR A 269      31.804  26.127 -18.545  1.00 61.12           C
ANISOU 1448  CB  TYR A 269     9051   4377   9794    478   -538  -1129       C
ATOM   1449  CG  TYR A 269      30.984  27.058 -19.421  1.00 65.54           C
ANISOU 1449  CG  TYR A 269     9757   4915  10232    515   -611  -1159       C
ATOM   1450  CD1 TYR A 269      29.767  26.649 -19.958  1.00 68.69           C
ANISOU 1450  CD1 TYR A 269    10215   5278  10604    521   -783  -1187       C
ATOM   1451  CD2 TYR A 269      31.398  28.370 -19.664  1.00 67.13           C
ANISOU 1451  CD2 TYR A 269    10025   5123  10358    547   -519  -1160       C
ATOM   1452  CE1 TYR A 269      29.000  27.505 -20.745  1.00 71.60           C
ANISOU 1452  CE1 TYR A 269    10720   5617  10869    560   -873  -1216       C
ATOM   1453  CE2 TYR A 269      30.639  29.236 -20.454  1.00 68.89           C
ANISOU 1453  CE2 TYR A 269    10389   5322  10464    586   -589  -1186       C
ATOM   1454  CZ  TYR A 269      29.439  28.798 -20.989  1.00 82.51           C
ANISOU 1454  CZ  TYR A 269    12181   7011  12159    593   -773  -1214       C
ATOM   1455  OH  TYR A 269      28.679  29.640 -21.763  1.00 91.51           O
ANISOU 1455  OH  TYR A 269    13463   8117  13190    636   -866  -1241       O
ATOM   1456  N   THR A 270      31.210  24.551 -15.347  1.00 52.35           N
ANISOU 1456  N   THR A 270     7480   3437   8971    379   -624  -1013       N
ATOM   1457  CA  THR A 270      31.607  23.509 -14.400  1.00 51.88           C
ANISOU 1457  CA  THR A 270     7304   3393   9015    352   -605   -977       C
ATOM   1458  C   THR A 270      31.737  22.127 -15.029  1.00 59.08           C
ANISOU 1458  C   THR A 270     8255   4230   9964    342   -620  -1002       C
ATOM   1459  O   THR A 270      31.358  21.932 -16.187  1.00 59.66           O
ANISOU 1459  O   THR A 270     8453   4236   9980    356   -668  -1049       O
ATOM   1460  CB  THR A 270      30.660  23.482 -13.189  1.00 58.42           C
ANISOU 1460  CB  THR A 270     8004   4291   9904    335   -661   -925       C
ATOM   1461  OG1 THR A 270      29.410  22.874 -13.539  1.00 63.48           O
ANISOU 1461  OG1 THR A 270     8635   4901  10584    324   -759   -933       O
ATOM   1462  CG2 THR A 270      30.430  24.844 -12.602  1.00 54.01           C
ANISOU 1462  CG2 THR A 270     7421   3800   9302    347   -649   -902       C
ATOM   1463  N   THR A 271      32.260  21.167 -14.228  1.00 56.45           N
ANISOU 1463  N   THR A 271     7824   3902   9723    322   -589   -970       N
ATOM   1464  CA  THR A 271      32.479  19.747 -14.542  1.00 56.68           C
ANISOU 1464  CA  THR A 271     7857   3869   9810    307   -591   -981       C
ATOM   1465  C   THR A 271      31.249  18.906 -14.102  1.00 61.97           C
ANISOU 1465  C   THR A 271     8445   4549  10552    285   -689   -961       C
ATOM   1466  O   THR A 271      31.201  17.685 -14.342  1.00 64.11           O
ANISOU 1466  O   THR A 271     8710   4769  10881    271   -708   -971       O
ATOM   1467  CB  THR A 271      33.744  19.236 -13.805  1.00 60.59           C
ANISOU 1467  CB  THR A 271     8278   4362  10383    299   -504   -952       C
ATOM   1468  OG1 THR A 271      33.563  19.447 -12.410  1.00 55.37           O
ANISOU 1468  OG1 THR A 271     7498   3777   9765    293   -525   -897       O
ATOM   1469  CG2 THR A 271      35.035  19.936 -14.268  1.00 58.40           C
ANISOU 1469  CG2 THR A 271     8058   4044  10087    319   -396   -973       C
ATOM   1470  N   ILE A 272      30.274  19.558 -13.443  1.00 54.77           N
ANISOU 1470  N   ILE A 272     7465   3694   9651    284   -738   -930       N
ATOM   1471  CA  ILE A 272      29.082  18.899 -12.934  1.00 53.15           C
ANISOU 1471  CA  ILE A 272     7164   3485   9545    267   -806   -902       C
ATOM   1472  C   ILE A 272      28.207  18.307 -14.031  1.00 60.34           C
ANISOU 1472  C   ILE A 272     8126   4316  10484    262   -916   -954       C
ATOM   1473  O   ILE A 272      27.883  18.955 -15.014  1.00 60.22           O
ANISOU 1473  O   ILE A 272     8216   4273  10394    279   -981  -1001       O
ATOM   1474  CB  ILE A 272      28.275  19.795 -11.951  1.00 54.39           C
ANISOU 1474  CB  ILE A 272     7239   3705   9722    271   -806   -851       C
ATOM   1475  CG1 ILE A 272      29.152  20.355 -10.812  1.00 52.99           C
ANISOU 1475  CG1 ILE A 272     7031   3594   9507    282   -716   -804       C
ATOM   1476  CG2 ILE A 272      27.020  19.079 -11.400  1.00 54.46           C
ANISOU 1476  CG2 ILE A 272     7139   3685   9869    257   -846   -814       C
ATOM   1477  CD1 ILE A 272      29.268  19.513  -9.514  1.00 43.37           C
ANISOU 1477  CD1 ILE A 272     5730   2386   8364    279   -673   -740       C
ATOM   1478  N   ASN A 273      27.824  17.054 -13.826  1.00 60.49           N
ANISOU 1478  N   ASN A 273     8075   4292  10616    242   -945   -944       N
ATOM   1479  CA  ASN A 273      26.880  16.336 -14.663  1.00 61.40           C
ANISOU 1479  CA  ASN A 273     8208   4320  10801    235  -1070   -990       C
ATOM   1480  C   ASN A 273      25.537  16.578 -13.969  1.00 66.81           C
ANISOU 1480  C   ASN A 273     8757   5010  11616    226  -1122   -950       C
ATOM   1481  O   ASN A 273      25.382  16.216 -12.793  1.00 65.71           O
ANISOU 1481  O   ASN A 273     8493   4901  11572    215  -1045   -883       O
ATOM   1482  CB  ASN A 273      27.224  14.850 -14.663  1.00 58.55           C
ANISOU 1482  CB  ASN A 273     7821   3907  10518    216  -1054   -993       C
ATOM   1483  CG  ASN A 273      26.382  14.043 -15.590  1.00 71.87           C
ANISOU 1483  CG  ASN A 273     9542   5490  12273    210  -1193  -1051       C
ATOM   1484  OD1 ASN A 273      25.207  13.730 -15.327  1.00 69.52           O
ANISOU 1484  OD1 ASN A 273     9135   5154  12125    197  -1279  -1042       O
ATOM   1485  ND2 ASN A 273      26.982  13.676 -16.691  1.00 60.03           N
ANISOU 1485  ND2 ASN A 273     8200   3929  10679    222  -1213  -1113       N
ATOM   1486  N   ALA A 274      24.590  17.225 -14.665  1.00 64.90           N
ANISOU 1486  N   ALA A 274     8546   4730  11382    236  -1244   -987       N
ATOM   1487  CA  ALA A 274      23.293  17.530 -14.057  1.00 65.11           C
ANISOU 1487  CA  ALA A 274     8434   4746  11560    229  -1286   -949       C
ATOM   1488  C   ALA A 274      22.466  16.298 -13.708  1.00 70.34           C
ANISOU 1488  C   ALA A 274     8959   5328  12440    206  -1321   -931       C
ATOM   1489  O   ALA A 274      21.848  16.270 -12.637  1.00 70.82           O
ANISOU 1489  O   ALA A 274     8878   5395  12636    199  -1247   -862       O
ATOM   1490  CB  ALA A 274      22.501  18.480 -14.938  1.00 66.27           C
ANISOU 1490  CB  ALA A 274     8642   4856  11681    246  -1423   -996       C
ATOM   1491  N   LYS A 275      22.467  15.282 -14.599  1.00 66.49           N
ANISOU 1491  N   LYS A 275     8522   4755  11986    198  -1423   -991       N
ATOM   1492  CA  LYS A 275      21.727  14.033 -14.388  1.00 66.12           C
ANISOU 1492  CA  LYS A 275     8346   4618  12158    176  -1465   -984       C
ATOM   1493  C   LYS A 275      22.228  13.379 -13.102  1.00 65.88           C
ANISOU 1493  C   LYS A 275     8216   4640  12176    164  -1285   -902       C
ATOM   1494  O   LYS A 275      21.435  13.130 -12.181  1.00 65.22           O
ANISOU 1494  O   LYS A 275     7982   4529  12269    157  -1226   -840       O
ATOM   1495  CB  LYS A 275      21.880  13.108 -15.611  1.00 68.93           C
ANISOU 1495  CB  LYS A 275     8810   4879  12499    174  -1603  -1070       C
ATOM   1496  CG  LYS A 275      21.322  11.706 -15.437  1.00 95.43           C
ANISOU 1496  CG  LYS A 275    12043   8144  16070    149  -1635  -1068       C
ATOM   1497  CD  LYS A 275      20.024  11.520 -16.256  1.00107.96           C
ANISOU 1497  CD  LYS A 275    13559   9595  17865    145  -1844  -1118       C
ATOM   1498  CE  LYS A 275      19.512  10.095 -16.268  1.00107.54           C
ANISOU 1498  CE  LYS A 275    13428   9428  18004    123  -1916  -1146       C
ATOM   1499  NZ  LYS A 275      18.563   9.868 -17.394  1.00107.33           N
ANISOU 1499  NZ  LYS A 275    13442   9256  18085    130  -2182  -1240       N
ATOM   1500  N   ARG A 276      23.566  13.225 -13.001  1.00 58.10           N
ANISOU 1500  N   ARG A 276     7323   3723  11031    168  -1189   -898       N
ATOM   1501  CA  ARG A 276      24.229  12.649 -11.837  1.00 56.07           C
ANISOU 1501  CA  ARG A 276     7005   3514  10787    166  -1038   -827       C
ATOM   1502  C   ARG A 276      24.005  13.482 -10.590  1.00 60.11           C
ANISOU 1502  C   ARG A 276     7454   4091  11296    181   -931   -747       C
ATOM   1503  O   ARG A 276      23.798  12.908  -9.520  1.00 59.18           O
ANISOU 1503  O   ARG A 276     7249   3964  11274    184   -833   -678       O
ATOM   1504  CB  ARG A 276      25.720  12.415 -12.118  1.00 52.56           C
ANISOU 1504  CB  ARG A 276     6670   3111  10189    169   -982   -848       C
ATOM   1505  CG  ARG A 276      25.938  11.105 -12.839  1.00 49.77           C
ANISOU 1505  CG  ARG A 276     6342   2681   9889    152  -1026   -893       C
ATOM   1506  CD  ARG A 276      27.292  10.915 -13.491  1.00 55.76           C
ANISOU 1506  CD  ARG A 276     7231   3446  10509    157   -988   -932       C
ATOM   1507  NE  ARG A 276      27.260   9.649 -14.225  1.00 64.95           N
ANISOU 1507  NE  ARG A 276     8422   4520  11737    142  -1043   -979       N
ATOM   1508  CZ  ARG A 276      28.310   9.015 -14.730  1.00 71.56           C
ANISOU 1508  CZ  ARG A 276     9346   5331  12512    141   -995  -1006       C
ATOM   1509  NH1 ARG A 276      29.523   9.532 -14.620  1.00 54.12           N
ANISOU 1509  NH1 ARG A 276     7197   3172  10192    154   -890   -992       N
ATOM   1510  NH2 ARG A 276      28.154   7.859 -15.353  1.00 71.65           N
ANISOU 1510  NH2 ARG A 276     9382   5255  12588    129  -1049  -1048       N
ATOM   1511  N   GLN A 277      23.997  14.832 -10.734  1.00 56.87           N
ANISOU 1511  N   GLN A 277     7098   3736  10775    196   -947   -757       N
ATOM   1512  CA  GLN A 277      23.762  15.736  -9.614  1.00 56.29           C
ANISOU 1512  CA  GLN A 277     6984   3718  10684    213   -851   -687       C
ATOM   1513  C   GLN A 277      22.361  15.553  -9.032  1.00 62.09           C
ANISOU 1513  C   GLN A 277     7586   4383  11623    211   -832   -637       C
ATOM   1514  O   GLN A 277      22.229  15.488  -7.815  1.00 61.93           O
ANISOU 1514  O   GLN A 277     7519   4368  11642    227   -702   -558       O
ATOM   1515  CB  GLN A 277      24.049  17.194 -10.011  1.00 57.40           C
ANISOU 1515  CB  GLN A 277     7211   3924  10672    228   -877   -714       C
ATOM   1516  CG  GLN A 277      23.935  18.219  -8.880  1.00 61.24           C
ANISOU 1516  CG  GLN A 277     7679   4473  11116    248   -779   -648       C
ATOM   1517  CD  GLN A 277      24.926  18.067  -7.759  1.00 62.18           C
ANISOU 1517  CD  GLN A 277     7826   4645  11153    265   -669   -597       C
ATOM   1518  OE1 GLN A 277      26.102  17.771  -7.966  1.00 57.42           O
ANISOU 1518  OE1 GLN A 277     7285   4070  10463    264   -668   -623       O
ATOM   1519  NE2 GLN A 277      24.498  18.408  -6.560  1.00 45.42           N
ANISOU 1519  NE2 GLN A 277     5675   2532   9052    286   -576   -524       N
ATOM   1520  N   ALA A 278      21.335  15.405  -9.885  1.00 60.59           N
ANISOU 1520  N   ALA A 278     7340   4107  11575    197   -958   -683       N
ATOM   1521  CA  ALA A 278      19.943  15.182  -9.465  1.00 60.62           C
ANISOU 1521  CA  ALA A 278     7191   4014  11827    192   -949   -643       C
ATOM   1522  C   ALA A 278      19.755  13.861  -8.721  1.00 65.17           C
ANISOU 1522  C   ALA A 278     7671   4524  12566    186   -851   -590       C
ATOM   1523  O   ALA A 278      19.024  13.812  -7.729  1.00 65.47           O
ANISOU 1523  O   ALA A 278     7611   4514  12750    198   -726   -512       O
ATOM   1524  CB  ALA A 278      19.034  15.227 -10.670  1.00 62.06           C
ANISOU 1524  CB  ALA A 278     7342   4104  12134    178  -1145   -718       C
ATOM   1525  N   ILE A 279      20.424  12.788  -9.201  1.00 61.69           N
ANISOU 1525  N   ILE A 279     7266   4072  12100    171   -895   -631       N
ATOM   1526  CA  ILE A 279      20.399  11.444  -8.610  1.00 60.74           C
ANISOU 1526  CA  ILE A 279     7069   3892  12116    165   -809   -589       C
ATOM   1527  C   ILE A 279      20.950  11.500  -7.179  1.00 62.58           C
ANISOU 1527  C   ILE A 279     7328   4185  12263    194   -615   -494       C
ATOM   1528  O   ILE A 279      20.313  10.984  -6.259  1.00 62.46           O
ANISOU 1528  O   ILE A 279     7227   4103  12404    207   -490   -420       O
ATOM   1529  CB  ILE A 279      21.175  10.425  -9.522  1.00 63.60           C
ANISOU 1529  CB  ILE A 279     7494   4243  12427    144   -901   -660       C
ATOM   1530  CG1 ILE A 279      20.370  10.053 -10.778  1.00 64.73           C
ANISOU 1530  CG1 ILE A 279     7609   4282  12702    123  -1098   -748       C
ATOM   1531  CG2 ILE A 279      21.603   9.163  -8.761  1.00 64.24           C
ANISOU 1531  CG2 ILE A 279     7531   4302  12574    143   -784   -608       C
ATOM   1532  CD1 ILE A 279      21.248   9.573 -12.028  1.00 69.26           C
ANISOU 1532  CD1 ILE A 279     8327   4859  13129    113  -1213   -840       C
ATOM   1533  N   ALA A 280      22.133  12.141  -7.019  1.00 58.24           N
ANISOU 1533  N   ALA A 280     6907   3750  11473    208   -593   -498       N
ATOM   1534  CA  ALA A 280      22.853  12.314  -5.761  1.00 57.34           C
ANISOU 1534  CA  ALA A 280     6854   3696  11238    242   -454   -425       C
ATOM   1535  C   ALA A 280      21.988  13.060  -4.756  1.00 65.00           C
ANISOU 1535  C   ALA A 280     7795   4646  12258    272   -341   -348       C
ATOM   1536  O   ALA A 280      21.863  12.611  -3.608  1.00 65.22           O
ANISOU 1536  O   ALA A 280     7824   4637  12320    303   -199   -267       O
ATOM   1537  CB  ALA A 280      24.149  13.057  -6.009  1.00 56.45           C
ANISOU 1537  CB  ALA A 280     6864   3688  10897    247   -494   -462       C
ATOM   1538  N   GLU A 281      21.336  14.165  -5.206  1.00 62.80           N
ANISOU 1538  N   GLU A 281     7496   4375  11989    266   -397   -372       N
ATOM   1539  CA  GLU A 281      20.428  14.968  -4.384  1.00 62.29           C
ANISOU 1539  CA  GLU A 281     7399   4280  11988    292   -289   -304       C
ATOM   1540  C   GLU A 281      19.300  14.083  -3.802  1.00 67.24           C
ANISOU 1540  C   GLU A 281     7899   4771  12877    298   -176   -239       C
ATOM   1541  O   GLU A 281      19.108  14.071  -2.576  1.00 66.78           O
ANISOU 1541  O   GLU A 281     7867   4679  12827    338      2   -149       O
ATOM   1542  CB  GLU A 281      19.890  16.159  -5.183  1.00 63.20           C
ANISOU 1542  CB  GLU A 281     7497   4416  12100    279   -393   -353       C
ATOM   1543  CG  GLU A 281      20.880  17.310  -5.282  1.00 72.22           C
ANISOU 1543  CG  GLU A 281     8770   5683  12988    290   -426   -381       C
ATOM   1544  CD  GLU A 281      20.707  18.356  -6.383  1.00 78.58           C
ANISOU 1544  CD  GLU A 281     9594   6523  13740    274   -559   -451       C
ATOM   1545  OE1 GLU A 281      19.699  18.323  -7.127  1.00 65.42           O
ANISOU 1545  OE1 GLU A 281     7841   4781  12235    256   -654   -483       O
ATOM   1546  OE2 GLU A 281      21.604  19.219  -6.501  1.00 61.86           O
ANISOU 1546  OE2 GLU A 281     7581   4500  11423    284   -575   -476       O
ATOM   1547  N   LYS A 282      18.638  13.269  -4.661  1.00 64.13           N
ANISOU 1547  N   LYS A 282     7382   4288  12695    263   -276   -286       N
ATOM   1548  CA  LYS A 282      17.566  12.366  -4.226  1.00 66.19           C
ANISOU 1548  CA  LYS A 282     7498   4401  13250    264   -180   -233       C
ATOM   1549  C   LYS A 282      18.084  11.272  -3.297  1.00 72.80           C
ANISOU 1549  C   LYS A 282     8370   5217  14075    288    -30   -168       C
ATOM   1550  O   LYS A 282      17.440  11.001  -2.278  1.00 74.25           O
ANISOU 1550  O   LYS A 282     8511   5306  14394    320    159    -77       O
ATOM   1551  CB  LYS A 282      16.829  11.761  -5.442  1.00 69.58           C
ANISOU 1551  CB  LYS A 282     7795   4736  13906    220   -362   -313       C
ATOM   1552  CG  LYS A 282      15.641  10.849  -5.112  1.00 91.64           C
ANISOU 1552  CG  LYS A 282    10406   7355  17057    216   -285   -270       C
ATOM   1553  CD  LYS A 282      14.473  11.557  -4.394  1.00104.61           C
ANISOU 1553  CD  LYS A 282    11945   8899  18902    239   -138   -191       C
ATOM   1554  CE  LYS A 282      13.227  10.702  -4.342  1.00117.99           C
ANISOU 1554  CE  LYS A 282    13428  10395  21006    228    -97   -167       C
ATOM   1555  NZ  LYS A 282      12.402  11.006  -3.143  1.00124.91           N
ANISOU 1555  NZ  LYS A 282    14240  11164  22058    268    171    -49       N
ATOM   1556  N   ALA A 283      19.248  10.672  -3.639  1.00 68.88           N
ANISOU 1556  N   ALA A 283     7958   4798  13416    276   -104   -212       N
ATOM   1557  CA  ALA A 283      19.892   9.592  -2.886  1.00 69.09           C
ANISOU 1557  CA  ALA A 283     8027   4813  13411    296      5   -163       C
ATOM   1558  C   ALA A 283      20.220   9.990  -1.453  1.00 72.94           C
ANISOU 1558  C   ALA A 283     8634   5323  13758    357    185    -66       C
ATOM   1559  O   ALA A 283      19.927   9.238  -0.517  1.00 74.93           O
ANISOU 1559  O   ALA A 283     8881   5487  14101    392    349     15       O
ATOM   1560  CB  ALA A 283      21.155   9.114  -3.607  1.00 69.01           C
ANISOU 1560  CB  ALA A 283     8092   4890  13240    272   -122   -234       C
ATOM   1561  N   VAL A 284      20.819  11.172  -1.283  1.00 67.20           N
ANISOU 1561  N   VAL A 284     8025   4700  12808    374    154    -75       N
ATOM   1562  CA  VAL A 284      21.186  11.683   0.033  1.00 65.67           C
ANISOU 1562  CA  VAL A 284     7974   4528  12451    437    291      4       C
ATOM   1563  C   VAL A 284      19.921  11.973   0.843  1.00 70.34           C
ANISOU 1563  C   VAL A 284     8529   5007  13192    473    475     90       C
ATOM   1564  O   VAL A 284      19.843  11.540   1.992  1.00 71.04           O
ANISOU 1564  O   VAL A 284     8698   5025  13267    529    650    179       O
ATOM   1565  CB  VAL A 284      22.186  12.851  -0.050  1.00 67.22           C
ANISOU 1565  CB  VAL A 284     8294   4854  12391    443    195    -37       C
ATOM   1566  CG1 VAL A 284      22.462  13.438   1.330  1.00 67.35           C
ANISOU 1566  CG1 VAL A 284     8470   4874  12246    512    318     40       C
ATOM   1567  CG2 VAL A 284      23.491  12.393  -0.696  1.00 65.95           C
ANISOU 1567  CG2 VAL A 284     8171   4773  12115    417     60   -106       C
ATOM   1568  N   GLN A 285      18.895  12.586   0.214  1.00 65.70           N
ANISOU 1568  N   GLN A 285     7815   4380  12767    443    441     66       N
ATOM   1569  CA  GLN A 285      17.625  12.860   0.866  1.00 66.75           C
ANISOU 1569  CA  GLN A 285     7882   4387  13094    471    619    145       C
ATOM   1570  C   GLN A 285      16.906  11.579   1.308  1.00 75.80           C
ANISOU 1570  C   GLN A 285     8929   5376  14495    484    772    209       C
ATOM   1571  O   GLN A 285      16.525  11.481   2.472  1.00 77.90           O
ANISOU 1571  O   GLN A 285     9263   5547  14786    545   1002    311       O
ATOM   1572  CB  GLN A 285      16.737  13.701  -0.050  1.00 68.36           C
ANISOU 1572  CB  GLN A 285     7949   4576  13448    430    511     94       C
ATOM   1573  CG  GLN A 285      15.492  14.259   0.650  1.00 80.38           C
ANISOU 1573  CG  GLN A 285     9407   5971  15162    461    699    177       C
ATOM   1574  CD  GLN A 285      14.455  14.767  -0.314  1.00 90.19           C
ANISOU 1574  CD  GLN A 285    10467   7157  16643    416    580    127       C
ATOM   1575  OE1 GLN A 285      14.625  15.812  -0.941  1.00 86.91           O
ANISOU 1575  OE1 GLN A 285    10078   6838  16107    396    436     67       O
ATOM   1576  NE2 GLN A 285      13.349  14.039  -0.443  1.00 77.50           N
ANISOU 1576  NE2 GLN A 285     8670   5381  15394    402    634    150       N
ATOM   1577  N   ASP A 286      16.760  10.585   0.416  1.00 73.62           N
ANISOU 1577  N   ASP A 286     8513   5064  14397    434    655    151       N
ATOM   1578  CA  ASP A 286      16.085   9.316   0.742  1.00 74.86           C
ANISOU 1578  CA  ASP A 286     8555   5067  14824    440    786    202       C
ATOM   1579  C   ASP A 286      16.769   8.479   1.804  1.00 77.30           C
ANISOU 1579  C   ASP A 286     9005   5365  15003    494    946    277       C
ATOM   1580  O   ASP A 286      16.073   7.854   2.619  1.00 79.02           O
ANISOU 1580  O   ASP A 286     9193   5434  15396    536   1168    368       O
ATOM   1581  CB  ASP A 286      15.907   8.444  -0.511  1.00 77.13           C
ANISOU 1581  CB  ASP A 286     8681   5327  15297    373    590    109       C
ATOM   1582  CG  ASP A 286      14.955   8.986  -1.556  1.00 95.74           C
ANISOU 1582  CG  ASP A 286    10871   7629  17875    327    435     42       C
ATOM   1583  OD1 ASP A 286      14.194   9.955  -1.238  1.00100.86           O
ANISOU 1583  OD1 ASP A 286    11486   8234  18602    344    512     81       O
ATOM   1584  OD2 ASP A 286      14.957   8.447  -2.690  1.00 96.78           O
ANISOU 1584  OD2 ASP A 286    10916   7753  18102    277    233    -50       O
ATOM   1585  N   GLY A 287      18.105   8.410   1.730  1.00 69.55           N
ANISOU 1585  N   GLY A 287     8164   4522  13741    494    830    236       N
ATOM   1586  CA  GLY A 287      18.940   7.626   2.630  1.00 68.23           C
ANISOU 1586  CA  GLY A 287     8143   4358  13423    544    928    292       C
ATOM   1587  C   GLY A 287      18.929   8.125   4.052  1.00 71.60           C
ANISOU 1587  C   GLY A 287     8756   4743  13705    632   1132    397       C
ATOM   1588  O   GLY A 287      18.998   7.333   4.996  1.00 72.43           O
ANISOU 1588  O   GLY A 287     8954   4763  13802    690   1297    478       O
ATOM   1589  N   LEU A 288      18.835   9.444   4.206  1.00 68.67           N
ANISOU 1589  N   LEU A 288     8455   4425  13210    645   1123    396       N
ATOM   1590  CA  LEU A 288      18.793  10.111   5.502  1.00 69.41           C
ANISOU 1590  CA  LEU A 288     8749   4478  13144    731   1303    487       C
ATOM   1591  C   LEU A 288      17.386   9.995   6.074  1.00 76.80           C
ANISOU 1591  C   LEU A 288     9613   5230  14337    765   1561    580       C
ATOM   1592  O   LEU A 288      17.243   9.696   7.269  1.00 78.41           O
ANISOU 1592  O   LEU A 288     9975   5325  14491    849   1789    683       O
ATOM   1593  CB  LEU A 288      19.285  11.562   5.418  1.00 68.31           C
ANISOU 1593  CB  LEU A 288     8714   4466  12774    731   1187    444       C
ATOM   1594  CG  LEU A 288      20.756  11.788   5.018  1.00 71.52           C
ANISOU 1594  CG  LEU A 288     9211   5035  12929    710    961    363       C
ATOM   1595  CD1 LEU A 288      21.092  13.279   4.970  1.00 71.60           C
ANISOU 1595  CD1 LEU A 288     9305   5148  12753    711    872    326       C
ATOM   1596  CD2 LEU A 288      21.719  11.095   5.976  1.00 73.36           C
ANISOU 1596  CD2 LEU A 288     9634   5258  12981    774    995    408       C
ATOM   1597  N   GLU A 289      16.348  10.134   5.201  1.00 73.09           N
ANISOU 1597  N   GLU A 289     8904   4707  14161    703   1528    544       N
ATOM   1598  CA  GLU A 289      14.936   9.907   5.550  1.00 74.70           C
ANISOU 1598  CA  GLU A 289     8972   4711  14699    722   1757    623       C
ATOM   1599  C   GLU A 289      14.756   8.440   6.006  1.00 78.33           C
ANISOU 1599  C   GLU A 289     9401   5036  15326    749   1916    684       C
ATOM   1600  O   GLU A 289      13.989   8.187   6.937  1.00 78.99           O
ANISOU 1600  O   GLU A 289     9512   4944  15558    812   2204    793       O
ATOM   1601  CB  GLU A 289      14.033  10.176   4.329  1.00 76.51           C
ANISOU 1601  CB  GLU A 289     8930   4915  15226    640   1612    549       C
ATOM   1602  CG  GLU A 289      13.371  11.545   4.328  1.00 88.00           C
ANISOU 1602  CG  GLU A 289    10367   6365  16705    643   1639    558       C
ATOM   1603  CD  GLU A 289      13.167  12.224   2.980  1.00 99.47           C
ANISOU 1603  CD  GLU A 289    11660   7900  18236    565   1370    447       C
ATOM   1604  OE1 GLU A 289      12.899  11.530   1.964  1.00 70.98           O
ANISOU 1604  OE1 GLU A 289     7868   4264  14839    505   1204    375       O
ATOM   1605  OE2 GLU A 289      13.234  13.477   2.965  1.00 83.75           O
ANISOU 1605  OE2 GLU A 289     9739   5989  16092    570   1328    433       O
ATOM   1606  N   ALA A 290      15.479   7.486   5.360  1.00 74.30           N
ANISOU 1606  N   ALA A 290     8842   4599  14790    704   1745    617       N
ATOM   1607  CA  ALA A 290      15.456   6.062   5.716  1.00 75.85           C
ANISOU 1607  CA  ALA A 290     9012   4687  15120    725   1869    665       C
ATOM   1608  C   ALA A 290      15.972   5.839   7.138  1.00 81.86           C
ANISOU 1608  C   ALA A 290    10047   5406  15652    830   2084    772       C
ATOM   1609  O   ALA A 290      15.327   5.134   7.930  1.00 82.35           O
ANISOU 1609  O   ALA A 290    10122   5289  15878    887   2350    872       O
ATOM   1610  CB  ALA A 290      16.288   5.254   4.730  1.00 75.30           C
ANISOU 1610  CB  ALA A 290     8869   4728  15014    658   1623    566       C
ATOM   1611  N   TYR A 291      17.131   6.452   7.458  1.00 79.43           N
ANISOU 1611  N   TYR A 291     9964   5248  14969    858   1964    750       N
ATOM   1612  CA  TYR A 291      17.763   6.343   8.775  1.00 80.84           C
ANISOU 1612  CA  TYR A 291    10439   5397  14879    963   2105    836       C
ATOM   1613  C   TYR A 291      16.858   6.959   9.838  1.00 86.81           C
ANISOU 1613  C   TYR A 291    11324   6003  15657   1048   2395    946       C
ATOM   1614  O   TYR A 291      16.616   6.348  10.888  1.00 86.90           O
ANISOU 1614  O   TYR A 291    11489   5863  15666   1138   2649   1053       O
ATOM   1615  CB  TYR A 291      19.149   7.025   8.786  1.00 80.00           C
ANISOU 1615  CB  TYR A 291    10517   5475  14405    968   1875    773       C
ATOM   1616  CG  TYR A 291      19.713   7.168  10.186  1.00 82.34           C
ANISOU 1616  CG  TYR A 291    11143   5727  14415   1085   1993    856       C
ATOM   1617  CD1 TYR A 291      20.591   6.223  10.707  1.00 83.79           C
ANISOU 1617  CD1 TYR A 291    11473   5902  14463   1133   1973    880       C
ATOM   1618  CD2 TYR A 291      19.335   8.230  11.008  1.00 84.30           C
ANISOU 1618  CD2 TYR A 291    11571   5926  14531   1154   2127    914       C
ATOM   1619  CE1 TYR A 291      21.093   6.337  12.005  1.00 85.01           C
ANISOU 1619  CE1 TYR A 291    11955   5998  14349   1250   2062    955       C
ATOM   1620  CE2 TYR A 291      19.810   8.343  12.312  1.00 86.86           C
ANISOU 1620  CE2 TYR A 291    12230   6189  14583   1271   2231    990       C
ATOM   1621  CZ  TYR A 291      20.694   7.397  12.807  1.00 97.66           C
ANISOU 1621  CZ  TYR A 291    13749   7545  15810   1321   2189   1009       C
ATOM   1622  OH  TYR A 291      21.156   7.535  14.097  1.00103.97           O
ANISOU 1622  OH  TYR A 291    14904   8271  16330   1446   2270   1080       O
ATOM   1623  N   ASP A 292      16.415   8.200   9.566  1.00 83.41           N
ANISOU 1623  N   ASP A 292    10850   5613  15230   1024   2361    921       N
ATOM   1624  CA  ASP A 292      15.537   8.971  10.429  1.00 84.22           C
ANISOU 1624  CA  ASP A 292    11058   5582  15359   1094   2621   1014       C
ATOM   1625  C   ASP A 292      14.259   8.165  10.764  1.00 91.85           C
ANISOU 1625  C   ASP A 292    11889   6309  16701   1120   2930   1110       C
ATOM   1626  O   ASP A 292      14.041   7.877  11.940  1.00 93.95           O
ANISOU 1626  O   ASP A 292    12365   6422  16911   1225   3217   1226       O
ATOM   1627  CB  ASP A 292      15.218  10.314   9.774  1.00 84.05           C
ANISOU 1627  CB  ASP A 292    10938   5654  15344   1040   2493    952       C
ATOM   1628  CG  ASP A 292      14.574  11.291  10.705  1.00 87.71           C
ANISOU 1628  CG  ASP A 292    11559   6013  15756   1116   2731   1040       C
ATOM   1629  OD1 ASP A 292      15.296  11.849  11.570  1.00 84.31           O
ANISOU 1629  OD1 ASP A 292    11430   5624  14980   1193   2748   1069       O
ATOM   1630  OD2 ASP A 292      13.353  11.531  10.553  1.00 95.12           O
ANISOU 1630  OD2 ASP A 292    12319   6817  17004   1101   2892   1078       O
ATOM   1631  N   ARG A 293      13.504   7.686   9.732  1.00 87.99           N
ANISOU 1631  N   ARG A 293    11065   5778  16589   1031   2863   1061       N
ATOM   1632  CA  ARG A 293      12.275   6.894   9.920  1.00 89.13           C
ANISOU 1632  CA  ARG A 293    11030   5684  17153   1044   3131   1140       C
ATOM   1633  C   ARG A 293      12.493   5.703  10.812  1.00 92.90           C
ANISOU 1633  C   ARG A 293    11653   6041  17605   1122   3347   1229       C
ATOM   1634  O   ARG A 293      11.675   5.484  11.702  1.00 94.16           O
ANISOU 1634  O   ARG A 293    11863   5980  17933   1198   3695   1348       O
ATOM   1635  CB  ARG A 293      11.610   6.474   8.593  1.00 89.38           C
ANISOU 1635  CB  ARG A 293    10685   5699  17577    932   2954   1051       C
ATOM   1636  CG  ARG A 293      10.845   7.612   7.927  1.00102.08           C
ANISOU 1636  CG  ARG A 293    12120   7307  19358    881   2872   1009       C
ATOM   1637  CD  ARG A 293       9.987   7.167   6.753  1.00116.27           C
ANISOU 1637  CD  ARG A 293    13559   9036  21583    787   2714    933       C
ATOM   1638  NE  ARG A 293       8.962   8.170   6.443  1.00126.62           N
ANISOU 1638  NE  ARG A 293    14704  10271  23135    761   2720    928       N
ATOM   1639  CZ  ARG A 293       7.718   8.148   6.915  1.00143.18           C
ANISOU 1639  CZ  ARG A 293    16657  12125  25619    790   2993   1017       C
ATOM   1640  NH1 ARG A 293       7.315   7.153   7.694  1.00132.74           N
ANISOU 1640  NH1 ARG A 293    15336  10606  24493    847   3294   1119       N
ATOM   1641  NH2 ARG A 293       6.862   9.112   6.596  1.00129.33           N
ANISOU 1641  NH2 ARG A 293    14751  10311  24076    764   2973   1007       N
ATOM   1642  N   ARG A 294      13.604   4.950  10.615  1.00 88.10           N
ANISOU 1642  N   ARG A 294    11125   5564  16787   1108   3159   1178       N
ATOM   1643  CA  ARG A 294      13.891   3.796  11.474  1.00 88.31           C
ANISOU 1643  CA  ARG A 294    11307   5482  16765   1186   3348   1262       C
ATOM   1644  C   ARG A 294      14.212   4.121  12.945  1.00 92.48           C
ANISOU 1644  C   ARG A 294    12229   5936  16976   1325   3579   1375       C
ATOM   1645  O   ARG A 294      13.942   3.285  13.805  1.00 93.71           O
ANISOU 1645  O   ARG A 294    12506   5916  17182   1411   3851   1479       O
ATOM   1646  CB  ARG A 294      14.838   2.757  10.835  1.00 86.36           C
ANISOU 1646  CB  ARG A 294    10995   5358  16458   1131   3109   1184       C
ATOM   1647  CG  ARG A 294      16.306   3.146  10.664  1.00 86.97           C
ANISOU 1647  CG  ARG A 294    11244   5667  16133   1118   2813   1103       C
ATOM   1648  CD  ARG A 294      17.049   2.038   9.907  1.00 73.89           C
ANISOU 1648  CD  ARG A 294     9468   4096  14511   1054   2614   1029       C
ATOM   1649  NE  ARG A 294      18.437   2.382   9.580  1.00 69.62           N
ANISOU 1649  NE  ARG A 294     9040   3764  13648   1028   2323    943       N
ATOM   1650  CZ  ARG A 294      18.854   2.763   8.373  1.00 79.74           C
ANISOU 1650  CZ  ARG A 294    10164   5203  14931    929   2044    822       C
ATOM   1651  NH1 ARG A 294      17.992   2.869   7.366  1.00 68.80           N
ANISOU 1651  NH1 ARG A 294     8516   3797  13828    848   1991    766       N
ATOM   1652  NH2 ARG A 294      20.139   3.026   8.158  1.00 48.78           N
ANISOU 1652  NH2 ARG A 294     6351   1446  10737    915   1817    755       N
ATOM   1653  N   HIS A 295      14.695   5.336  13.253  1.00 87.83           N
ANISOU 1653  N   HIS A 295    11842   5453  16075   1355   3491   1358       N
ATOM   1654  CA  HIS A 295      14.991   5.705  14.640  1.00 88.53           C
ANISOU 1654  CA  HIS A 295    12331   5459  15847   1493   3689   1458       C
ATOM   1655  C   HIS A 295      13.832   6.374  15.385  1.00 94.70           C
ANISOU 1655  C   HIS A 295    13186   6041  16755   1565   4039   1565       C
ATOM   1656  O   HIS A 295      13.960   6.685  16.573  1.00 94.32           O
ANISOU 1656  O   HIS A 295    13495   5890  16454   1691   4242   1658       O
ATOM   1657  CB  HIS A 295      16.293   6.493  14.742  1.00 87.73           C
ANISOU 1657  CB  HIS A 295    12461   5560  15313   1505   3404   1388       C
ATOM   1658  CG  HIS A 295      17.503   5.654  14.529  1.00 90.29           C
ANISOU 1658  CG  HIS A 295    12832   6005  15471   1490   3170   1332       C
ATOM   1659  ND1 HIS A 295      17.572   4.731  13.497  1.00 91.34           N
ANISOU 1659  ND1 HIS A 295    12668   6205  15831   1387   3018   1260       N
ATOM   1660  CD2 HIS A 295      18.667   5.633  15.215  1.00 92.22           C
ANISOU 1660  CD2 HIS A 295    13382   6302  15355   1566   3057   1336       C
ATOM   1661  CE1 HIS A 295      18.767   4.171  13.597  1.00 90.31           C
ANISOU 1661  CE1 HIS A 295    12669   6167  15478   1402   2841   1229       C
ATOM   1662  NE2 HIS A 295      19.467   4.689  14.607  1.00 91.11           N
ANISOU 1662  NE2 HIS A 295    13122   6263  15232   1507   2847   1271       N
ATOM   1663  N   GLY A 296      12.717   6.580  14.675  1.00 93.23           N
ANISOU 1663  N   GLY A 296    12672   5789  16963   1487   4101   1551       N
ATOM   1664  CA  GLY A 296      11.469   7.096  15.233  1.00 94.94           C
ANISOU 1664  CA  GLY A 296    12879   5786  17406   1540   4452   1653       C
ATOM   1665  C   GLY A 296      11.247   8.592  15.282  1.00 97.92           C
ANISOU 1665  C   GLY A 296    13322   6217  17667   1541   4431   1641       C
ATOM   1666  O   GLY A 296      12.159   9.385  15.000  1.00 95.34           O
ANISOU 1666  O   GLY A 296    13099   6108  17019   1512   4140   1554       O
ATOM   1667  N   TRP A 297       9.989   8.962  15.664  1.00 96.46           N
ANISOU 1667  N   TRP A 297    13066   5813  17773   1576   4764   1733       N
ATOM   1668  CA  TRP A 297       9.487  10.321  15.848  1.00 96.95           C
ANISOU 1668  CA  TRP A 297    13177   5857  17804   1590   4843   1751       C
ATOM   1669  C   TRP A 297      10.183  10.963  17.051  1.00101.89           C
ANISOU 1669  C   TRP A 297    14284   6488  17941   1718   4945   1810       C
ATOM   1670  O   TRP A 297      10.197  10.371  18.132  1.00103.31           O
ANISOU 1670  O   TRP A 297    14746   6496  18009   1839   5228   1920       O
ATOM   1671  CB  TRP A 297       7.952  10.295  16.039  1.00 97.94           C
ANISOU 1671  CB  TRP A 297    13099   5700  18415   1606   5217   1851       C
ATOM   1672  CG  TRP A 297       7.284  11.624  16.334  1.00 99.57           C
ANISOU 1672  CG  TRP A 297    13353   5837  18640   1632   5373   1892       C
ATOM   1673  CD1 TRP A 297       6.566  11.944  17.448  1.00104.70           C
ANISOU 1673  CD1 TRP A 297    14216   6239  19326   1749   5811   2033       C
ATOM   1674  CD2 TRP A 297       7.197  12.766  15.462  1.00 97.92           C
ANISOU 1674  CD2 TRP A 297    12961   5790  18456   1539   5112   1796       C
ATOM   1675  NE1 TRP A 297       6.060  13.221  17.340  1.00104.14           N
ANISOU 1675  NE1 TRP A 297    14103   6170  19294   1733   5835   2029       N
ATOM   1676  CE2 TRP A 297       6.436  13.752  16.134  1.00103.23           C
ANISOU 1676  CE2 TRP A 297    13743   6307  19171   1604   5405   1884       C
ATOM   1677  CE3 TRP A 297       7.674  13.049  14.170  1.00 96.97           C
ANISOU 1677  CE3 TRP A 297    12603   5917  18325   1411   4672   1646       C
ATOM   1678  CZ2 TRP A 297       6.158  15.008  15.566  1.00101.51           C
ANISOU 1678  CZ2 TRP A 297    13398   6187  18984   1543   5259   1826       C
ATOM   1679  CZ3 TRP A 297       7.414  14.301  13.616  1.00 97.52           C
ANISOU 1679  CZ3 TRP A 297    12564   6080  18408   1356   4530   1589       C
ATOM   1680  CH2 TRP A 297       6.668  15.264  14.311  1.00 99.36           C
ANISOU 1680  CH2 TRP A 297    12901   6166  18684   1420   4815   1678       C
ATOM   1681  N   ARG A 298      10.752  12.167  16.856  1.00 96.53           N
ANISOU 1681  N   ARG A 298    13705   5996  16975   1694   4710   1736       N
ATOM   1682  CA  ARG A 298      11.483  12.929  17.868  1.00 96.59           C
ANISOU 1682  CA  ARG A 298    14155   6035  16510   1802   4729   1766       C
ATOM   1683  C   ARG A 298      10.676  14.112  18.399  1.00103.08           C
ANISOU 1683  C   ARG A 298    15084   6735  17348   1855   4976   1833       C
ATOM   1684  O   ARG A 298      11.176  14.878  19.222  1.00103.56           O
ANISOU 1684  O   ARG A 298    15512   6806  17031   1945   4998   1856       O
ATOM   1685  CB  ARG A 298      12.830  13.413  17.293  1.00 94.93           C
ANISOU 1685  CB  ARG A 298    13989   6119  15962   1741   4273   1629       C
ATOM   1686  CG  ARG A 298      13.853  12.296  17.080  1.00104.73           C
ANISOU 1686  CG  ARG A 298    15249   7462  17082   1726   4060   1580       C
ATOM   1687  CD  ARG A 298      15.115  12.824  16.429  1.00106.63           C
ANISOU 1687  CD  ARG A 298    15487   7973  17056   1657   3629   1446       C
ATOM   1688  NE  ARG A 298      14.988  12.949  14.967  1.00104.60           N
ANISOU 1688  NE  ARG A 298    14827   7871  17047   1508   3383   1334       N
ATOM   1689  CZ  ARG A 298      14.868  14.092  14.289  1.00114.69           C
ANISOU 1689  CZ  ARG A 298    15967   9265  18344   1438   3235   1264       C
ATOM   1690  NH1 ARG A 298      14.848  15.253  14.929  1.00106.58           N
ANISOU 1690  NH1 ARG A 298    15151   8225  17118   1496   3310   1293       N
ATOM   1691  NH2 ARG A 298      14.781  14.082  12.966  1.00101.89           N
ANISOU 1691  NH2 ARG A 298    14013   7769  16932   1314   3009   1165       N
ATOM   1692  N   GLY A 299       9.436  14.237  17.942  1.00100.92           N
ANISOU 1692  N   GLY A 299    14493   6332  17519   1801   5156   1865       N
ATOM   1693  CA  GLY A 299       8.580  15.360  18.301  1.00102.77           C
ANISOU 1693  CA  GLY A 299    14763   6446  17837   1834   5388   1925       C
ATOM   1694  C   GLY A 299       8.674  16.460  17.256  1.00106.10           C
ANISOU 1694  C   GLY A 299    14951   7083  18278   1717   5064   1805       C
ATOM   1695  O   GLY A 299       9.486  16.367  16.327  1.00103.93           O
ANISOU 1695  O   GLY A 299    14532   7047  17910   1622   4670   1679       O
ATOM   1696  N   ALA A 300       7.825  17.491  17.382  1.00103.14           N
ANISOU 1696  N   ALA A 300    14537   6613  18039   1725   5241   1847       N
ATOM   1697  CA  ALA A 300       7.773  18.628  16.459  1.00101.22           C
ANISOU 1697  CA  ALA A 300    14085   6544  17831   1626   4979   1749       C
ATOM   1698  C   ALA A 300       9.066  19.451  16.507  1.00103.55           C
ANISOU 1698  C   ALA A 300    14641   7086  17616   1632   4674   1661       C
ATOM   1699  O   ALA A 300       9.726  19.467  17.550  1.00104.90           O
ANISOU 1699  O   ALA A 300    15212   7228  17417   1742   4765   1709       O
ATOM   1700  CB  ALA A 300       6.580  19.504  16.788  1.00103.25           C
ANISOU 1700  CB  ALA A 300    14290   6610  18330   1655   5287   1833       C
ATOM   1701  N   GLU A 301       9.441  20.121  15.388  1.00 95.86           N
ANISOU 1701  N   GLU A 301    13454   6343  16626   1520   4310   1534       N
ATOM   1702  CA  GLU A 301      10.672  20.907  15.364  1.00 93.83           C
ANISOU 1702  CA  GLU A 301    13410   6313  15930   1519   4019   1446       C
ATOM   1703  C   GLU A 301      10.672  22.150  16.267  1.00 98.53           C
ANISOU 1703  C   GLU A 301    14311   6867  16257   1603   4161   1493       C
ATOM   1704  O   GLU A 301      11.746  22.656  16.614  1.00 97.43           O
ANISOU 1704  O   GLU A 301    14437   6861  15719   1638   3976   1444       O
ATOM   1705  CB  GLU A 301      11.221  21.155  13.941  1.00 93.12           C
ANISOU 1705  CB  GLU A 301    13043   6472  15868   1386   3602   1299       C
ATOM   1706  CG  GLU A 301      10.537  22.203  13.073  1.00104.04           C
ANISOU 1706  CG  GLU A 301    14161   7902  17465   1304   3520   1252       C
ATOM   1707  CD  GLU A 301      11.236  22.378  11.739  1.00128.61           C
ANISOU 1707  CD  GLU A 301    17075  11256  20535   1193   3112   1108       C
ATOM   1708  OE1 GLU A 301      11.855  23.443  11.521  1.00120.22           O
ANISOU 1708  OE1 GLU A 301    16098  10348  19232   1177   2935   1044       O
ATOM   1709  OE2 GLU A 301      11.223  21.418  10.940  1.00132.73           O
ANISOU 1709  OE2 GLU A 301    17377  11806  21250   1127   2974   1060       O
ATOM   1710  N   ALA A 302       9.465  22.603  16.677  1.00 95.49           N
ANISOU 1710  N   ALA A 302    13894   6280  16109   1640   4498   1590       N
ATOM   1711  CA  ALA A 302       9.237  23.729  17.580  1.00 95.03           C
ANISOU 1711  CA  ALA A 302    14119   6135  15853   1727   4704   1653       C
ATOM   1712  C   ALA A 302       7.805  23.677  18.127  1.00 99.60           C
ANISOU 1712  C   ALA A 302    14646   6417  16781   1782   5165   1791       C
ATOM   1713  O   ALA A 302       6.957  22.965  17.581  1.00 99.91           O
ANISOU 1713  O   ALA A 302    14356   6346  17258   1728   5265   1816       O
ATOM   1714  CB  ALA A 302       9.471  25.037  16.852  1.00 93.99           C
ANISOU 1714  CB  ALA A 302    13872   6199  15641   1649   4444   1555       C
ATOM   1715  N   HIS A 303       7.549  24.405  19.221  1.00 96.25           N
ANISOU 1715  N   HIS A 303    14554   5848  16170   1893   5450   1880       N
ATOM   1716  CA  HIS A 303       6.227  24.534  19.841  1.00 97.84           C
ANISOU 1716  CA  HIS A 303    14752   5749  16672   1959   5924   2019       C
ATOM   1717  C   HIS A 303       6.085  25.980  20.267  1.00100.87           C
ANISOU 1717  C   HIS A 303    15331   6129  16866   1999   6006   2033       C
ATOM   1718  O   HIS A 303       7.057  26.571  20.756  1.00 99.47           O
ANISOU 1718  O   HIS A 303    15500   6076  16217   2052   5847   1991       O
ATOM   1719  CB  HIS A 303       6.054  23.574  21.037  1.00100.90           C
ANISOU 1719  CB  HIS A 303    15457   5884  16998   2099   6304   2151       C
ATOM   1720  CG  HIS A 303       4.623  23.387  21.470  1.00106.41           C
ANISOU 1720  CG  HIS A 303    16059   6248  18123   2151   6808   2295       C
ATOM   1721  ND1 HIS A 303       4.044  24.202  22.419  1.00109.65           N
ANISOU 1721  ND1 HIS A 303    16771   6450  18443   2265   7188   2405       N
ATOM   1722  CD2 HIS A 303       3.708  22.473  21.073  1.00108.41           C
ANISOU 1722  CD2 HIS A 303    15950   6338  18902   2105   6982   2342       C
ATOM   1723  CE1 HIS A 303       2.801  23.767  22.557  1.00110.93           C
ANISOU 1723  CE1 HIS A 303    16735   6326  19087   2283   7595   2520       C
ATOM   1724  NE2 HIS A 303       2.555  22.731  21.767  1.00110.68           N
ANISOU 1724  NE2 HIS A 303    16297   6309  19447   2188   7481   2485       N
ATOM   1725  N   ASP A 304       4.919  26.587  20.003  1.00 98.09           N
ANISOU 1725  N   ASP A 304    14735   5646  16891   1966   6215   2082       N
ATOM   1726  CA  ASP A 304       4.659  27.990  20.314  1.00 97.49           C
ANISOU 1726  CA  ASP A 304    14793   5556  16694   1993   6310   2098       C
ATOM   1727  C   ASP A 304       5.692  28.901  19.687  1.00 98.35           C
ANISOU 1727  C   ASP A 304    14909   5984  16477   1920   5854   1954       C
ATOM   1728  O   ASP A 304       6.201  29.806  20.348  1.00 98.24           O
ANISOU 1728  O   ASP A 304    15233   6009  16085   1987   5851   1950       O
ATOM   1729  CB  ASP A 304       4.562  28.229  21.833  1.00101.64           C
ANISOU 1729  CB  ASP A 304    15836   5856  16929   2164   6709   2224       C
ATOM   1730  CG  ASP A 304       3.231  28.778  22.291  1.00110.33           C
ANISOU 1730  CG  ASP A 304    16916   6677  18327   2215   7169   2350       C
ATOM   1731  OD1 ASP A 304       2.725  29.724  21.648  1.00104.12           O
ANISOU 1731  OD1 ASP A 304    15865   5951  17744   2134   7093   2313       O
ATOM   1732  OD2 ASP A 304       2.687  28.252  23.287  1.00124.65           O
ANISOU 1732  OD2 ASP A 304    18980   8200  20180   2340   7616   2488       O
ATOM   1733  N   LYS A 305       6.057  28.622  18.428  1.00 92.82           N
ANISOU 1733  N   LYS A 305    13856   5502  15909   1789   5469   1834       N
ATOM   1734  CA  LYS A 305       7.004  29.454  17.671  1.00 90.23           C
ANISOU 1734  CA  LYS A 305    13486   5473  15326   1709   5037   1694       C
ATOM   1735  C   LYS A 305       6.325  29.968  16.373  1.00 93.81           C
ANISOU 1735  C   LYS A 305    13485   6007  16152   1580   4875   1631       C
ATOM   1736  O   LYS A 305       5.277  29.414  16.017  1.00 93.97           O
ANISOU 1736  O   LYS A 305    13211   5868  16626   1547   5034   1681       O
ATOM   1737  CB  LYS A 305       8.384  28.789  17.502  1.00 90.84           C
ANISOU 1737  CB  LYS A 305    13677   5752  15086   1695   4699   1600       C
ATOM   1738  CG  LYS A 305       9.090  28.550  18.846  1.00 98.54           C
ANISOU 1738  CG  LYS A 305    15144   6644  15653   1833   4828   1657       C
ATOM   1739  CD  LYS A 305      10.589  28.858  18.841  1.00102.75           C
ANISOU 1739  CD  LYS A 305    15895   7405  15739   1835   4455   1547       C
ATOM   1740  CE  LYS A 305      11.471  27.673  18.469  1.00107.64           C
ANISOU 1740  CE  LYS A 305    16463   8140  16294   1803   4205   1485       C
ATOM   1741  NZ  LYS A 305      11.286  26.491  19.363  1.00116.30           N
ANISOU 1741  NZ  LYS A 305    17767   9040  17381   1903   4460   1586       N
ATOM   1742  N   PRO A 306       6.745  31.104  15.754  1.00 90.40           N
ANISOU 1742  N   PRO A 306    13001   5776  15571   1520   4609   1537       N
ATOM   1743  CA  PRO A 306       5.975  31.628  14.614  1.00 90.26           C
ANISOU 1743  CA  PRO A 306    12585   5797  15913   1414   4490   1491       C
ATOM   1744  C   PRO A 306       6.238  30.937  13.280  1.00 96.49           C
ANISOU 1744  C   PRO A 306    13045   6740  16875   1301   4139   1383       C
ATOM   1745  O   PRO A 306       7.400  30.809  12.870  1.00 94.99           O
ANISOU 1745  O   PRO A 306    12928   6768  16397   1270   3828   1283       O
ATOM   1746  CB  PRO A 306       6.357  33.102  14.597  1.00 90.35           C
ANISOU 1746  CB  PRO A 306    12723   5944  15662   1411   4376   1443       C
ATOM   1747  CG  PRO A 306       7.703  33.168  15.190  1.00 93.19           C
ANISOU 1747  CG  PRO A 306    13439   6446  15524   1464   4226   1396       C
ATOM   1748  CD  PRO A 306       7.926  31.953  16.028  1.00 90.33           C
ANISOU 1748  CD  PRO A 306    13281   5957  15082   1544   4392   1464       C
ATOM   1749  N   LEU A 307       5.142  30.528  12.588  1.00 95.39           N
ANISOU 1749  N   LEU A 307    12544   6477  17223   1242   4185   1401       N
ATOM   1750  CA  LEU A 307       5.141  29.814  11.297  1.00 94.44           C
ANISOU 1750  CA  LEU A 307    12093   6451  17339   1140   3879   1307       C
ATOM   1751  C   LEU A 307       5.891  30.539  10.152  1.00 97.28           C
ANISOU 1751  C   LEU A 307    12370   7081  17511   1056   3463   1167       C
ATOM   1752  O   LEU A 307       6.396  29.875   9.238  1.00 97.54           O
ANISOU 1752  O   LEU A 307    12266   7241  17554    991   3178   1075       O
ATOM   1753  CB  LEU A 307       3.698  29.424  10.900  1.00 95.98           C
ANISOU 1753  CB  LEU A 307    11934   6419  18114   1106   4027   1360       C
ATOM   1754  CG  LEU A 307       3.466  28.457   9.710  1.00100.18           C
ANISOU 1754  CG  LEU A 307    12126   6971  18968   1016   3765   1282       C
ATOM   1755  CD1 LEU A 307       4.227  27.144   9.861  1.00 99.82           C
ANISOU 1755  CD1 LEU A 307    12176   6976  18776   1026   3702   1263       C
ATOM   1756  CD2 LEU A 307       1.995  28.168   9.534  1.00103.97           C
ANISOU 1756  CD2 LEU A 307    12286   7183  20036   1000   3952   1350       C
ATOM   1757  N   SER A 308       6.017  31.880  10.245  1.00 91.70           N
ANISOU 1757  N   SER A 308    11771   6456  16615   1065   3444   1152       N
ATOM   1758  CA  SER A 308       6.717  32.730   9.283  1.00 89.22           C
ANISOU 1758  CA  SER A 308    11413   6381  16105    999   3098   1032       C
ATOM   1759  C   SER A 308       8.228  32.487   9.304  1.00 92.59           C
ANISOU 1759  C   SER A 308    12059   7013  16110   1004   2878    954       C
ATOM   1760  O   SER A 308       8.911  32.782   8.319  1.00 89.37           O
ANISOU 1760  O   SER A 308    11575   6797  15586    941   2567    845       O
ATOM   1761  CB  SER A 308       6.448  34.200   9.596  1.00 92.01           C
ANISOU 1761  CB  SER A 308    11855   6741  16365   1021   3190   1054       C
ATOM   1762  OG  SER A 308       7.290  34.708  10.622  1.00 97.76           O
ANISOU 1762  OG  SER A 308    12943   7519  16681   1096   3284   1076       O
ATOM   1763  N   GLU A 309       8.740  31.989  10.449  1.00 91.82           N
ANISOU 1763  N   GLU A 309    12241   6857  15787   1086   3049   1014       N
ATOM   1764  CA  GLU A 309      10.157  31.741  10.714  1.00 91.05           C
ANISOU 1764  CA  GLU A 309    12380   6915  15299   1108   2873    956       C
ATOM   1765  C   GLU A 309      10.694  30.396  10.209  1.00 96.20           C
ANISOU 1765  C   GLU A 309    12937   7618  15996   1072   2712    910       C
ATOM   1766  O   GLU A 309      11.875  30.103  10.411  1.00 95.63           O
ANISOU 1766  O   GLU A 309    13045   7659  15632   1090   2568    866       O
ATOM   1767  CB  GLU A 309      10.435  31.923  12.216  1.00 93.41           C
ANISOU 1767  CB  GLU A 309    13056   7115  15320   1224   3113   1040       C
ATOM   1768  CG  GLU A 309      11.219  33.179  12.543  1.00100.81           C
ANISOU 1768  CG  GLU A 309    14217   8176  15909   1249   3007    995       C
ATOM   1769  CD  GLU A 309      11.166  33.574  14.003  1.00119.83           C
ANISOU 1769  CD  GLU A 309    16988  10443  18099   1367   3279   1087       C
ATOM   1770  OE1 GLU A 309      11.777  32.870  14.838  1.00112.01           O
ANISOU 1770  OE1 GLU A 309    16259   9401  16899   1443   3329   1117       O
ATOM   1771  OE2 GLU A 309      10.541  34.613  14.308  1.00115.13           O
ANISOU 1771  OE2 GLU A 309    16429   9783  17531   1388   3435   1127       O
ATOM   1772  N   PHE A 310       9.860  29.595   9.531  1.00 93.94           N
ANISOU 1772  N   PHE A 310    12365   7246  16082   1020   2720    917       N
ATOM   1773  CA  PHE A 310      10.273  28.287   9.013  1.00 93.81           C
ANISOU 1773  CA  PHE A 310    12244   7262  16136    983   2577    875       C
ATOM   1774  C   PHE A 310      10.159  28.232   7.492  1.00 96.49           C
ANISOU 1774  C   PHE A 310    12290   7706  16665    881   2286    771       C
ATOM   1775  O   PHE A 310       9.168  28.715   6.948  1.00 97.45           O
ANISOU 1775  O   PHE A 310    12204   7761  17062    845   2295    773       O
ATOM   1776  CB  PHE A 310       9.430  27.177   9.652  1.00 97.81           C
ANISOU 1776  CB  PHE A 310    12708   7544  16912   1026   2860    979       C
ATOM   1777  CG  PHE A 310       9.505  27.114  11.160  1.00101.07           C
ANISOU 1777  CG  PHE A 310    13444   7829  17129   1140   3165   1088       C
ATOM   1778  CD1 PHE A 310      10.469  26.336  11.794  1.00103.63           C
ANISOU 1778  CD1 PHE A 310    14004   8188  17181   1192   3144   1091       C
ATOM   1779  CD2 PHE A 310       8.612  27.833  11.948  1.00104.63           C
ANISOU 1779  CD2 PHE A 310    13980   8111  17663   1201   3474   1187       C
ATOM   1780  CE1 PHE A 310      10.532  26.267  13.192  1.00105.64           C
ANISOU 1780  CE1 PHE A 310    14591   8310  17236   1308   3414   1191       C
ATOM   1781  CE2 PHE A 310       8.684  27.774  13.344  1.00108.47           C
ANISOU 1781  CE2 PHE A 310    14805   8463  17944   1318   3763   1288       C
ATOM   1782  CZ  PHE A 310       9.640  26.986  13.954  1.00106.34           C
ANISOU 1782  CZ  PHE A 310    14783   8228  17392   1373   3725   1288       C
ATOM   1783  N   ARG A 311      11.163  27.660   6.800  1.00 90.67           N
ANISOU 1783  N   ARG A 311    11545   7121  15785    838   2027    679       N
ATOM   1784  CA  ARG A 311      11.141  27.549   5.329  1.00 89.06           C
ANISOU 1784  CA  ARG A 311    11106   7010  15724    750   1745    576       C
ATOM   1785  C   ARG A 311      10.712  26.164   4.884  1.00 91.48           C
ANISOU 1785  C   ARG A 311    11228   7221  16309    719   1721    574       C
ATOM   1786  O   ARG A 311      10.945  25.200   5.609  1.00 90.58           O
ANISOU 1786  O   ARG A 311    11204   7040  16171    758   1855    626       O
ATOM   1787  CB  ARG A 311      12.528  27.827   4.699  1.00 88.81           C
ANISOU 1787  CB  ARG A 311    11175   7198  15371    720   1471    470       C
ATOM   1788  CG  ARG A 311      13.118  29.222   4.847  1.00104.55           C
ANISOU 1788  CG  ARG A 311    13326   9311  17086    737   1426    444       C
ATOM   1789  CD  ARG A 311      12.326  30.317   4.171  1.00121.37           C
ANISOU 1789  CD  ARG A 311    15320  11454  19342    702   1370    419       C
ATOM   1790  NE  ARG A 311      11.746  31.134   5.224  1.00133.28           N
ANISOU 1790  NE  ARG A 311    16944  12883  20813    758   1601    502       N
ATOM   1791  CZ  ARG A 311      10.775  32.019   5.065  1.00152.07           C
ANISOU 1791  CZ  ARG A 311    19199  15165  23414    753   1708    542       C
ATOM   1792  NH1 ARG A 311      10.223  32.205   3.871  1.00144.28           N
ANISOU 1792  NH1 ARG A 311    17960  14147  22712    694   1579    503       N
ATOM   1793  NH2 ARG A 311      10.322  32.703   6.099  1.00141.57           N
ANISOU 1793  NH2 ARG A 311    18004  13758  22030    810   1939    621       N
ATOM   1794  N   ALA A 312      10.132  26.055   3.671  1.00 88.41           N
ANISOU 1794  N   ALA A 312    10593   6824  16175    651   1533    508       N
ATOM   1795  CA  ALA A 312       9.795  24.760   3.059  1.00 89.40           C
ANISOU 1795  CA  ALA A 312    10536   6870  16562    613   1451    484       C
ATOM   1796  C   ALA A 312      11.015  24.304   2.219  1.00 91.55           C
ANISOU 1796  C   ALA A 312    10864   7322  16598    573   1177    377       C
ATOM   1797  O   ALA A 312      11.736  25.159   1.682  1.00 89.24           O
ANISOU 1797  O   ALA A 312    10655   7189  16066    555   1006    307       O
ATOM   1798  CB  ALA A 312       8.570  24.887   2.169  1.00 91.03           C
ANISOU 1798  CB  ALA A 312    10466   6960  17161    566   1362    461       C
ATOM   1799  N   TYR A 313      11.272  22.978   2.144  1.00 87.53           N
ANISOU 1799  N   TYR A 313    10319   6779  16159    564   1156    370       N
ATOM   1800  CA  TYR A 313      12.405  22.406   1.396  1.00 86.11           C
ANISOU 1800  CA  TYR A 313    10189   6742  15786    529    928    278       C
ATOM   1801  C   TYR A 313      12.387  20.902   1.417  1.00 91.14           C
ANISOU 1801  C   TYR A 313    10756   7296  16575    522    953    289       C
ATOM   1802  O   TYR A 313      11.766  20.329   2.306  1.00 94.39           O
ANISOU 1802  O   TYR A 313    11148   7560  17156    561   1186    382       O
ATOM   1803  CB  TYR A 313      13.752  22.891   1.946  1.00 86.27           C
ANISOU 1803  CB  TYR A 313    10456   6920  15403    561    917    268       C
ATOM   1804  CG  TYR A 313      14.006  22.557   3.401  1.00 88.46           C
ANISOU 1804  CG  TYR A 313    10912   7139  15559    634   1157    365       C
ATOM   1805  CD1 TYR A 313      14.576  21.348   3.769  1.00 90.41           C
ANISOU 1805  CD1 TYR A 313    11220   7369  15765    651   1188    382       C
ATOM   1806  CD2 TYR A 313      13.770  23.489   4.400  1.00 89.66           C
ANISOU 1806  CD2 TYR A 313    11203   7257  15607    690   1340    436       C
ATOM   1807  CE1 TYR A 313      14.841  21.050   5.103  1.00 92.14           C
ANISOU 1807  CE1 TYR A 313    11633   7527  15851    727   1395    470       C
ATOM   1808  CE2 TYR A 313      14.047  23.207   5.736  1.00 90.94           C
ANISOU 1808  CE2 TYR A 313    11574   7355  15624    768   1549    522       C
ATOM   1809  CZ  TYR A 313      14.567  21.982   6.086  1.00 97.56           C
ANISOU 1809  CZ  TYR A 313    12473   8169  16425    788   1573    539       C
ATOM   1810  OH  TYR A 313      14.869  21.723   7.403  1.00100.06           O
ANISOU 1810  OH  TYR A 313    13024   8415  16579    874   1766    624       O
ATOM   1811  N   ALA A 314      13.121  20.249   0.488  1.00 85.38           N
ANISOU 1811  N   ALA A 314    10007   6658  15775    479    732    199       N
ATOM   1812  CA  ALA A 314      13.211  18.775   0.370  1.00 84.96           C
ANISOU 1812  CA  ALA A 314     9888   6542  15850    466    724    195       C
ATOM   1813  C   ALA A 314      11.830  18.117   0.414  1.00 89.99           C
ANISOU 1813  C   ALA A 314    10311   6971  16910    459    833    243       C
ATOM   1814  O   ALA A 314      11.671  17.043   1.002  1.00 92.13           O
ANISOU 1814  O   ALA A 314    10560   7138  17307    480    983    301       O
ATOM   1815  CB  ALA A 314      14.128  18.189   1.447  1.00 85.27           C
ANISOU 1815  CB  ALA A 314    10114   6616  15668    515    867    251       C
ATOM   1816  N   ASN A 315      10.828  18.786  -0.212  1.00 84.80           N
ANISOU 1816  N   ASN A 315     9492   6242  16487    433    756    220       N
ATOM   1817  CA  ASN A 315       9.432  18.360  -0.300  1.00 85.24           C
ANISOU 1817  CA  ASN A 315     9309   6083  16995    422    825    256       C
ATOM   1818  C   ASN A 315       8.796  18.165   1.095  1.00 89.97           C
ANISOU 1818  C   ASN A 315     9918   6523  17743    481   1191    394       C
ATOM   1819  O   ASN A 315       8.122  17.159   1.374  1.00 91.79           O
ANISOU 1819  O   ASN A 315    10013   6579  18286    487   1326    443       O
ATOM   1820  CB  ASN A 315       9.282  17.143  -1.231  1.00 84.10           C
ANISOU 1820  CB  ASN A 315     9012   5876  17064    375    640    185       C
ATOM   1821  CG  ASN A 315       7.863  16.888  -1.698  1.00 98.50           C
ANISOU 1821  CG  ASN A 315    10563   7489  19375    350    597    182       C
ATOM   1822  OD1 ASN A 315       7.107  17.814  -2.045  1.00107.80           O
ANISOU 1822  OD1 ASN A 315    11641   8615  20702    341    535    172       O
ATOM   1823  ND2 ASN A 315       7.474  15.620  -1.728  1.00 71.06           N
ANISOU 1823  ND2 ASN A 315     6950   3876  16173    338    621    188       N
ATOM   1824  N   THR A 316       9.094  19.127   1.991  1.00 84.74           N
ANISOU 1824  N   THR A 316     9442   5921  16833    531   1358    454       N
ATOM   1825  CA  THR A 316       8.583  19.230   3.358  1.00 85.29           C
ANISOU 1825  CA  THR A 316     9592   5852  16963    601   1716    586       C
ATOM   1826  C   THR A 316       8.140  20.670   3.558  1.00 87.96           C
ANISOU 1826  C   THR A 316     9958   6194  17268    617   1780    612       C
ATOM   1827  O   THR A 316       8.847  21.616   3.194  1.00 84.77           O
ANISOU 1827  O   THR A 316     9666   5968  16574    603   1613    549       O
ATOM   1828  CB  THR A 316       9.546  18.717   4.441  1.00 96.55           C
ANISOU 1828  CB  THR A 316    11281   7328  18076    664   1879    644       C
ATOM   1829  OG1 THR A 316      10.545  19.690   4.694  1.00 99.05           O
ANISOU 1829  OG1 THR A 316    11829   7826  17979    685   1808    619       O
ATOM   1830  CG2 THR A 316      10.151  17.335   4.140  1.00 92.42           C
ANISOU 1830  CG2 THR A 316    10738   6831  17546    643   1779    606       C
ATOM   1831  N   TYR A 317       6.929  20.824   4.080  1.00 86.69           N
ANISOU 1831  N   TYR A 317     9677   5824  17438    644   2025    703       N
ATOM   1832  CA  TYR A 317       6.259  22.102   4.236  1.00 85.92           C
ANISOU 1832  CA  TYR A 317     9556   5685  17405    656   2111    736       C
ATOM   1833  C   TYR A 317       5.814  22.320   5.677  1.00 85.78           C
ANISOU 1833  C   TYR A 317     9678   5512  17402    741   2520    877       C
ATOM   1834  O   TYR A 317       5.016  21.531   6.198  1.00 85.82           O
ANISOU 1834  O   TYR A 317     9581   5297  17728    769   2766    962       O
ATOM   1835  CB  TYR A 317       5.071  22.184   3.239  1.00 90.09           C
ANISOU 1835  CB  TYR A 317     9756   6082  18392    598   1969    696       C
ATOM   1836  CG  TYR A 317       5.457  21.796   1.819  1.00 93.65           C
ANISOU 1836  CG  TYR A 317    10091   6649  18841    525   1572    559       C
ATOM   1837  CD1 TYR A 317       5.913  22.753   0.915  1.00 94.68           C
ANISOU 1837  CD1 TYR A 317    10262   6955  18758    489   1294    462       C
ATOM   1838  CD2 TYR A 317       5.449  20.457   1.406  1.00 95.37           C
ANISOU 1838  CD2 TYR A 317    10192   6804  19242    498   1484    526       C
ATOM   1839  CE1 TYR A 317       6.359  22.390  -0.361  1.00 96.58           C
ANISOU 1839  CE1 TYR A 317    10449   7296  18951    434    948    339       C
ATOM   1840  CE2 TYR A 317       5.922  20.082   0.146  1.00 95.70           C
ANISOU 1840  CE2 TYR A 317    10179   6954  19227    440   1129    400       C
ATOM   1841  CZ  TYR A 317       6.359  21.051  -0.741  1.00105.24           C
ANISOU 1841  CZ  TYR A 317    11445   8326  20215    411    866    308       C
ATOM   1842  OH  TYR A 317       6.784  20.667  -1.993  1.00106.93           O
ANISOU 1842  OH  TYR A 317    11628   8624  20378    362    536    188       O
ATOM   1843  N   PRO A 318       6.349  23.394   6.326  1.00 80.59           N
ANISOU 1843  N   PRO A 318     9269   4959  16393    786   2598    901       N
ATOM   1844  CA  PRO A 318       5.953  23.726   7.709  1.00 82.00           C
ANISOU 1844  CA  PRO A 318     9629   4987  16541    876   2987   1033       C
ATOM   1845  C   PRO A 318       4.459  23.957   7.898  1.00 88.27           C
ANISOU 1845  C   PRO A 318    10210   5527  17802    885   3234   1118       C
ATOM   1846  O   PRO A 318       3.800  24.639   7.098  1.00 85.63           O
ANISOU 1846  O   PRO A 318     9658   5183  17694    832   3097   1075       O
ATOM   1847  CB  PRO A 318       6.748  25.008   8.020  1.00 82.13           C
ANISOU 1847  CB  PRO A 318     9898   5180  16127    901   2926   1008       C
ATOM   1848  CG  PRO A 318       7.840  25.016   7.059  1.00 83.97           C
ANISOU 1848  CG  PRO A 318    10141   5658  16107    841   2554    880       C
ATOM   1849  CD  PRO A 318       7.314  24.386   5.816  1.00 79.63           C
ANISOU 1849  CD  PRO A 318     9277   5083  15897    759   2340    808       C
ATOM   1850  N   ALA A 319       3.939  23.362   8.973  1.00 89.92           N
ANISOU 1850  N   ALA A 319    10488   5517  18160    959   3607   1241       N
ATOM   1851  CA  ALA A 319       2.538  23.428   9.350  1.00 93.70           C
ANISOU 1851  CA  ALA A 319    10783   5710  19110    983   3920   1345       C
ATOM   1852  C   ALA A 319       2.405  23.591  10.856  1.00102.45           C
ANISOU 1852  C   ALA A 319    12185   6660  20080   1099   4366   1487       C
ATOM   1853  O   ALA A 319       3.108  22.907  11.607  1.00103.06           O
ANISOU 1853  O   ALA A 319    12521   6753  19885   1161   4478   1524       O
ATOM   1854  CB  ALA A 319       1.826  22.158   8.902  1.00 95.46           C
ANISOU 1854  CB  ALA A 319    10708   5757  19807    947   3928   1349       C
ATOM   1855  N   GLN A 320       1.508  24.498  11.294  1.00100.80           N
ANISOU 1855  N   GLN A 320    11951   6291  20056   1132   4620   1567       N
ATOM   1856  CA  GLN A 320       1.209  24.712  12.707  1.00102.48           C
ANISOU 1856  CA  GLN A 320    12444   6311  20182   1249   5083   1711       C
ATOM   1857  C   GLN A 320      -0.049  23.911  13.027  1.00111.74           C
ANISOU 1857  C   GLN A 320    13394   7143  21920   1275   5438   1823       C
ATOM   1858  O   GLN A 320      -1.108  24.245  12.497  1.00114.59           O
ANISOU 1858  O   GLN A 320    13429   7362  22747   1227   5458   1830       O
ATOM   1859  CB  GLN A 320       0.991  26.203  12.998  1.00103.03           C
ANISOU 1859  CB  GLN A 320    12643   6401  20103   1276   5173   1735       C
ATOM   1860  CG  GLN A 320       0.592  26.488  14.442  1.00107.51           C
ANISOU 1860  CG  GLN A 320    13528   6749  20572   1405   5664   1886       C
ATOM   1861  CD  GLN A 320       1.184  27.749  15.013  1.00125.29           C
ANISOU 1861  CD  GLN A 320    16104   9116  22385   1455   5685   1887       C
ATOM   1862  OE1 GLN A 320       1.834  28.556  14.332  1.00114.62           O
ANISOU 1862  OE1 GLN A 320    14755   8024  20772   1394   5332   1775       O
ATOM   1863  NE2 GLN A 320       0.957  27.950  16.297  1.00127.28           N
ANISOU 1863  NE2 GLN A 320    16651   9161  22548   1572   6113   2017       N
ATOM   1864  N   VAL A 321       0.064  22.870  13.886  1.00109.40           N
ANISOU 1864  N   VAL A 321    13269   6703  21595   1354   5717   1910       N
ATOM   1865  CA  VAL A 321      -1.037  21.992  14.314  1.00112.34           C
ANISOU 1865  CA  VAL A 321    13470   6733  22483   1394   6103   2028       C
ATOM   1866  C   VAL A 321      -2.106  22.837  15.005  1.00122.19           C
ANISOU 1866  C   VAL A 321    14725   7722  23977   1455   6512   2151       C
ATOM   1867  O   VAL A 321      -1.778  23.606  15.914  1.00122.28           O
ANISOU 1867  O   VAL A 321    15104   7752  23605   1540   6705   2208       O
ATOM   1868  CB  VAL A 321      -0.516  20.832  15.208  1.00116.11           C
ANISOU 1868  CB  VAL A 321    14222   7135  22759   1483   6327   2100       C
ATOM   1869  CG1 VAL A 321      -1.660  20.063  15.858  1.00119.07           C
ANISOU 1869  CG1 VAL A 321    14474   7127  23642   1545   6804   2243       C
ATOM   1870  CG2 VAL A 321       0.379  19.885  14.415  1.00113.55           C
ANISOU 1870  CG2 VAL A 321    13824   7036  22283   1412   5929   1981       C
ATOM   1871  N   THR A 322      -3.366  22.743  14.535  1.00122.44           N
ANISOU 1871  N   THR A 322    14348   7516  24655   1410   6622   2183       N
ATOM   1872  CA  THR A 322      -4.484  23.528  15.075  1.00125.39           C
ANISOU 1872  CA  THR A 322    14660   7620  25361   1457   7008   2298       C
ATOM   1873  C   THR A 322      -5.513  22.722  15.881  1.00134.76           C
ANISOU 1873  C   THR A 322    15763   8400  27039   1534   7535   2454       C
ATOM   1874  O   THR A 322      -6.178  23.296  16.749  1.00137.11           O
ANISOU 1874  O   THR A 322    16172   8454  27467   1616   7977   2583       O
ATOM   1875  CB  THR A 322      -5.125  24.437  14.000  1.00132.95           C
ANISOU 1875  CB  THR A 322    15242   8623  26652   1353   6722   2217       C
ATOM   1876  OG1 THR A 322      -5.351  23.690  12.798  1.00135.90           O
ANISOU 1876  OG1 THR A 322    15212   9024  27398   1248   6365   2114       O
ATOM   1877  CG2 THR A 322      -4.301  25.700  13.716  1.00125.27           C
ANISOU 1877  CG2 THR A 322    14465   7969  25162   1325   6414   2123       C
ATOM   1878  N   LYS A 323      -5.664  21.418  15.585  1.00132.35           N
ANISOU 1878  N   LYS A 323    15259   8007  27021   1508   7503   2444       N
ATOM   1879  CA  LYS A 323      -6.609  20.537  16.280  1.00135.70           C
ANISOU 1879  CA  LYS A 323    15577   8041  27943   1576   7991   2586       C
ATOM   1880  C   LYS A 323      -6.088  19.111  16.242  1.00140.58           C
ANISOU 1880  C   LYS A 323    16221   8693  28500   1578   7919   2564       C
ATOM   1881  O   LYS A 323      -5.562  18.685  15.214  1.00138.34           O
ANISOU 1881  O   LYS A 323    15767   8651  28144   1478   7438   2422       O
ATOM   1882  CB  LYS A 323      -8.011  20.610  15.642  1.00140.12           C
ANISOU 1882  CB  LYS A 323    15600   8330  29308   1507   8033   2599       C
ATOM   1883  CG  LYS A 323      -9.123  20.004  16.499  1.00153.30           C
ANISOU 1883  CG  LYS A 323    17320   9838  31087   1546   8286   2673       C
ATOM   1884  CD  LYS A 323     -10.495  20.112  15.846  1.00158.18           C
ANISOU 1884  CD  LYS A 323    17769  10860  31471   1382   7542   2463       C
ATOM   1885  CE  LYS A 323     -10.707  19.231  14.634  1.00160.79           C
ANISOU 1885  CE  LYS A 323    17971  11680  31443   1220   6671   2208       C
ATOM   1886  NZ  LYS A 323     -12.118  18.796  14.489  1.00160.26           N
ANISOU 1886  NZ  LYS A 323    17934  11936  31023   1126   6173   2064       N
ATOM   1887  N   VAL A 324      -6.229  18.382  17.365  1.00140.24           N
ANISOU 1887  N   VAL A 324    16407   8402  28476   1696   8407   2706       N
ATOM   1888  CA  VAL A 324      -5.806  16.982  17.496  1.00140.82           C
ANISOU 1888  CA  VAL A 324    16531   8460  28514   1717   8423   2711       C
ATOM   1889  C   VAL A 324      -7.035  16.101  17.843  1.00149.30           C
ANISOU 1889  C   VAL A 324    17370   9180  30176   1742   8780   2811       C
ATOM   1890  O   VAL A 324      -7.660  16.298  18.894  1.00148.39           O
ANISOU 1890  O   VAL A 324    17578   9143  29660   1787   8846   2835       O
ATOM   1891  CB  VAL A 324      -4.648  16.788  18.524  1.00143.70           C
ANISOU 1891  CB  VAL A 324    17478   8961  28159   1832   8537   2752       C
ATOM   1892  CG1 VAL A 324      -4.109  15.363  18.471  1.00143.19           C
ANISOU 1892  CG1 VAL A 324    17429   8928  28048   1834   8463   2733       C
ATOM   1893  CG2 VAL A 324      -3.514  17.787  18.310  1.00140.46           C
ANISOU 1893  CG2 VAL A 324    17334   8934  27101   1804   8137   2640       C
ATOM   1894  N   ASN A 325      -7.348  15.099  16.992  1.00148.31           N
ANISOU 1894  N   ASN A 325    16797   8930  30623   1666   8664   2771       N
ATOM   1895  CA  ASN A 325      -8.489  14.192  17.205  1.00147.82           C
ANISOU 1895  CA  ASN A 325    16666   8956  30541   1610   8452   2707       C
ATOM   1896  C   ASN A 325      -8.081  12.715  17.469  1.00152.05           C
ANISOU 1896  C   ASN A 325    17337   9590  30844   1619   8361   2680       C
ATOM   1897  O   ASN A 325      -6.889  12.422  17.590  1.00151.81           O
ANISOU 1897  O   ASN A 325    17487   9538  30657   1684   8512   2726       O
ATOM   1898  CB  ASN A 325      -9.516  14.321  16.067  1.00149.57           C
ANISOU 1898  CB  ASN A 325    16422   9243  31165   1469   8025   2579       C
ATOM   1899  CG  ASN A 325      -9.902  15.745  15.748  1.00166.73           C
ANISOU 1899  CG  ASN A 325    19161  12641  31547   1270   6596   2177       C
ATOM   1900  OD1 ASN A 325     -10.648  16.398  16.492  1.00163.30           O
ANISOU 1900  OD1 ASN A 325    18804  12067  31174   1317   6868   2260       O
ATOM   1901  ND2 ASN A 325      -9.383  16.252  14.634  1.00161.78           N
ANISOU 1901  ND2 ASN A 325    18156  11795  31519   1247   6671   2195       N
ATOM   1902  N   SER A 326      -9.069  11.800  17.582  1.00149.55           N
ANISOU 1902  N   SER A 326    16834   9136  30853   1600   8417   2690       N
ATOM   1903  CA  SER A 326      -8.848  10.378  17.874  1.00149.55           C
ANISOU 1903  CA  SER A 326    16913   9151  30760   1617   8418   2687       C
ATOM   1904  C   SER A 326      -7.883   9.635  16.935  1.00151.95           C
ANISOU 1904  C   SER A 326    17076   9607  31050   1552   8090   2588       C
ATOM   1905  O   SER A 326      -7.159   8.744  17.399  1.00152.07           O
ANISOU 1905  O   SER A 326    17306   9624  30852   1613   8218   2628       O
ATOM   1906  CB  SER A 326     -10.172   9.625  17.963  1.00152.92           C
ANISOU 1906  CB  SER A 326    17259   9744  31099   1537   8087   2586       C
ATOM   1907  OG  SER A 326     -10.988  10.114  19.016  1.00161.02           O
ANISOU 1907  OG  SER A 326    18750  11230  31200   1512   7690   2483       O
ATOM   1908  N   SER A 327      -7.891   9.976  15.626  1.00148.96           N
ANISOU 1908  N   SER A 327    16182   9050  31365   1474   8004   2554       N
ATOM   1909  CA  SER A 327      -7.043   9.326  14.616  1.00148.77           C
ANISOU 1909  CA  SER A 327    15829   8909  31787   1430   7924   2523       C
ATOM   1910  C   SER A 327      -6.425  10.307  13.613  1.00145.63           C
ANISOU 1910  C   SER A 327    15404   8874  31053   1329   7356   2360       C
ATOM   1911  O   SER A 327      -5.634   9.884  12.780  1.00142.70           O
ANISOU 1911  O   SER A 327    14984   8766  30469   1247   6896   2221       O
ATOM   1912  CB  SER A 327      -7.816   8.222  13.888  1.00151.04           C
ANISOU 1912  CB  SER A 327    15902   9401  32087   1310   7405   2361       C
ATOM   1913  OG  SER A 327      -8.932   8.722  13.170  1.00157.15           O
ANISOU 1913  OG  SER A 327    16590  10514  32605   1186   6796   2182       O
ATOM   1914  N   SER A 328      -6.800  11.602  13.664  1.00139.59           N
ANISOU 1914  N   SER A 328    14666   8114  30259   1334   7395   2378       N
ATOM   1915  CA  SER A 328      -6.301  12.600  12.713  1.00135.06           C
ANISOU 1915  CA  SER A 328    14058   7857  29400   1243   6888   2233       C
ATOM   1916  C   SER A 328      -6.027  13.969  13.327  1.00134.11           C
ANISOU 1916  C   SER A 328    14259   7846  28851   1300   7017   2280       C
ATOM   1917  O   SER A 328      -6.720  14.358  14.264  1.00136.54           O
ANISOU 1917  O   SER A 328    14648   7892  29340   1387   7494   2422       O
ATOM   1918  CB  SER A 328      -7.269  12.744  11.537  1.00139.31           C
ANISOU 1918  CB  SER A 328    14079   8278  30575   1135   6600   2145       C
ATOM   1919  OG  SER A 328      -8.273  13.722  11.763  1.00149.02           O
ANISOU 1919  OG  SER A 328    15172   9294  32156   1154   6834   2221       O
ATOM   1920  N   PHE A 329      -5.052  14.722  12.769  1.00124.10           N
ANISOU 1920  N   PHE A 329    13160   6949  27044   1250   6596   2158       N
ATOM   1921  CA  PHE A 329      -4.778  16.089  13.214  1.00121.10           C
ANISOU 1921  CA  PHE A 329    13052   6688  26271   1291   6658   2183       C
ATOM   1922  C   PHE A 329      -5.003  17.104  12.097  1.00122.11           C
ANISOU 1922  C   PHE A 329    12929   6962  26506   1189   6252   2064       C
ATOM   1923  O   PHE A 329      -5.097  16.737  10.921  1.00120.39           O
ANISOU 1923  O   PHE A 329    12397   6819  26527   1087   5847   1941       O
ATOM   1924  CB  PHE A 329      -3.418  16.255  13.929  1.00120.08           C
ANISOU 1924  CB  PHE A 329    13441   6818  25367   1361   6649   2185       C
ATOM   1925  CG  PHE A 329      -2.181  16.102  13.081  1.00117.23           C
ANISOU 1925  CG  PHE A 329    13144   6830  24569   1285   6125   2027       C
ATOM   1926  CD1 PHE A 329      -1.593  17.205  12.476  1.00116.71           C
ANISOU 1926  CD1 PHE A 329    13138   7047  24160   1229   5764   1920       C
ATOM   1927  CD2 PHE A 329      -1.572  14.861  12.930  1.00117.64           C
ANISOU 1927  CD2 PHE A 329    13212   6943  24543   1274   6015   1993       C
ATOM   1928  CE1 PHE A 329      -0.444  17.063  11.694  1.00114.84           C
ANISOU 1928  CE1 PHE A 329    12962   7134  23536   1163   5309   1780       C
ATOM   1929  CE2 PHE A 329      -0.423  14.714  12.145  1.00117.39           C
ANISOU 1929  CE2 PHE A 329    13239   7241  24125   1206   5551   1851       C
ATOM   1930  CZ  PHE A 329       0.140  15.817  11.539  1.00113.61           C
ANISOU 1930  CZ  PHE A 329    12814   7028  23323   1152   5209   1747       C
ATOM   1931  N   GLU A 330      -5.154  18.376  12.480  1.00118.52           N
ANISOU 1931  N   GLU A 330    12615   6520  25896   1222   6379   2107       N
ATOM   1932  CA  GLU A 330      -5.364  19.463  11.549  1.00117.26           C
ANISOU 1932  CA  GLU A 330    12264   6492  25799   1140   6038   2009       C
ATOM   1933  C   GLU A 330      -4.280  20.476  11.769  1.00118.88           C
ANISOU 1933  C   GLU A 330    12849   7010  25309   1161   5894   1966       C
ATOM   1934  O   GLU A 330      -4.011  20.848  12.914  1.00119.77           O
ANISOU 1934  O   GLU A 330    13320   7088  25098   1261   6237   2069       O
ATOM   1935  CB  GLU A 330      -6.738  20.100  11.746  1.00121.49           C
ANISOU 1935  CB  GLU A 330    12545   6711  26905   1154   6331   2102       C
ATOM   1936  CG  GLU A 330      -7.875  19.255  11.207  1.00137.72           C
ANISOU 1936  CG  GLU A 330    14128   8466  29732   1107   6350   2109       C
ATOM   1937  CD  GLU A 330      -9.004  20.092  10.647  1.00166.56           C
ANISOU 1937  CD  GLU A 330    17604  12211  33472   1031   6039   2028       C
ATOM   1938  OE1 GLU A 330     -10.025  20.249  11.353  1.00165.19           O
ANISOU 1938  OE1 GLU A 330    17677  12220  32868   1034   5986   2014       O
ATOM   1939  OE2 GLU A 330      -8.852  20.628   9.526  1.00162.24           O
ANISOU 1939  OE2 GLU A 330    16704  11590  33351    967   5800   1964       O
ATOM   1940  N   ALA A 331      -3.633  20.901  10.676  1.00111.40           N
ANISOU 1940  N   ALA A 331    11839   6360  24128   1071   5385   1813       N
ATOM   1941  CA  ALA A 331      -2.565  21.881  10.726  1.00107.40           C
ANISOU 1941  CA  ALA A 331    11651   6162  22995   1077   5196   1754       C
ATOM   1942  C   ALA A 331      -2.768  23.006   9.712  1.00108.43           C
ANISOU 1942  C   ALA A 331    11595   6426  23177    998   4855   1655       C
ATOM   1943  O   ALA A 331      -3.340  22.789   8.642  1.00108.50           O
ANISOU 1943  O   ALA A 331    11252   6395  23578    916   4579   1576       O
ATOM   1944  CB  ALA A 331      -1.231  21.199  10.511  1.00105.88           C
ANISOU 1944  CB  ALA A 331    11661   6235  22332   1063   4926   1667       C
ATOM   1945  N   LEU A 332      -2.297  24.216  10.071  1.00102.18           N
ANISOU 1945  N   LEU A 332    11057   5785  21983   1027   4872   1659       N
ATOM   1946  CA  LEU A 332      -2.324  25.428   9.262  1.00 99.60           C
ANISOU 1946  CA  LEU A 332    10634   5612  21599    967   4579   1572       C
ATOM   1947  C   LEU A 332      -1.036  25.542   8.431  1.00102.88           C
ANISOU 1947  C   LEU A 332    11176   6383  21531    911   4123   1426       C
ATOM   1948  O   LEU A 332       0.068  25.538   8.991  1.00102.74           O
ANISOU 1948  O   LEU A 332    11494   6538  21003    954   4140   1423       O
ATOM   1949  CB  LEU A 332      -2.463  26.654  10.170  1.00 99.32           C
ANISOU 1949  CB  LEU A 332    10823   5541  21371   1034   4867   1659       C
ATOM   1950  CG  LEU A 332      -2.276  27.996   9.472  1.00101.20           C
ANISOU 1950  CG  LEU A 332    11022   5965  21463    981   4582   1574       C
ATOM   1951  CD1 LEU A 332      -3.516  28.391   8.690  1.00102.96           C
ANISOU 1951  CD1 LEU A 332    10844   6001  22276    928   4530   1573       C
ATOM   1952  CD2 LEU A 332      -1.840  29.048  10.455  1.00101.02           C
ANISOU 1952  CD2 LEU A 332    11356   6019  21007   1052   4789   1629       C
ATOM   1953  N   MET A 333      -1.181  25.667   7.100  1.00 97.28           N
ANISOU 1953  N   MET A 333    10207   5768  20987    820   3718   1305       N
ATOM   1954  CA  MET A 333      -0.046  25.761   6.183  1.00 93.52           C
ANISOU 1954  CA  MET A 333     9823   5601  20108    765   3290   1165       C
ATOM   1955  C   MET A 333       0.358  27.202   6.014  1.00 91.79           C
ANISOU 1955  C   MET A 333     9743   5565  19566    760   3171   1125       C
ATOM   1956  O   MET A 333      -0.414  28.090   6.352  1.00 93.34           O
ANISOU 1956  O   MET A 333     9893   5640  19933    783   3359   1191       O
ATOM   1957  CB  MET A 333      -0.376  25.138   4.813  1.00 96.27           C
ANISOU 1957  CB  MET A 333     9859   5946  20774    680   2915   1053       C
ATOM   1958  CG  MET A 333      -0.887  23.675   4.846  1.00101.65           C
ANISOU 1958  CG  MET A 333    10348   6424  21851    675   3002   1081       C
ATOM   1959  SD  MET A 333       0.237  22.444   5.510  1.00105.25           S
ANISOU 1959  SD  MET A 333    11066   6980  21944    714   3106   1100       S
ATOM   1960  CE  MET A 333       1.533  22.524   4.332  1.00 98.80           C
ANISOU 1960  CE  MET A 333    10342   6501  20696    647   2605    932       C
ATOM   1961  N   GLN A 334       1.548  27.439   5.469  1.00 83.29           N
ANISOU 1961  N   GLN A 334     8827   4771  18048    730   2864   1018       N
ATOM   1962  CA  GLN A 334       2.097  28.779   5.225  1.00 80.54           C
ANISOU 1962  CA  GLN A 334     8620   4620  17362    723   2720    967       C
ATOM   1963  C   GLN A 334       1.308  29.595   4.184  1.00 87.32           C
ANISOU 1963  C   GLN A 334     9226   5452  18500    667   2507    912       C
ATOM   1964  O   GLN A 334       1.401  30.828   4.169  1.00 84.25           O
ANISOU 1964  O   GLN A 334     8920   5155  17935    671   2484    903       O
ATOM   1965  CB  GLN A 334       3.579  28.705   4.847  1.00 78.24           C
ANISOU 1965  CB  GLN A 334     8544   4613  16571    705   2455    868       C
ATOM   1966  CG  GLN A 334       4.473  28.258   5.987  1.00 76.28           C
ANISOU 1966  CG  GLN A 334     8603   4410  15969    773   2660    925       C
ATOM   1967  CD  GLN A 334       5.895  28.185   5.545  1.00 83.13           C
ANISOU 1967  CD  GLN A 334     9645   5537  16405    751   2387    825       C
ATOM   1968  OE1 GLN A 334       6.317  27.229   4.867  1.00 82.76           O
ANISOU 1968  OE1 GLN A 334     9522   5551  16374    711   2186    757       O
ATOM   1969  NE2 GLN A 334       6.660  29.205   5.902  1.00 53.14           N
ANISOU 1969  NE2 GLN A 334     6077   1885  12230    778   2376    812       N
ATOM   1970  N   ASP A 335       0.527  28.902   3.327  1.00 89.10           N
ANISOU 1970  N   ASP A 335     9148   5540  19168    619   2346    875       N
ATOM   1971  CA  ASP A 335      -0.321  29.528   2.309  1.00 91.26           C
ANISOU 1971  CA  ASP A 335     9163   5748  19763    571   2120    822       C
ATOM   1972  C   ASP A 335      -1.671  30.006   2.898  1.00100.86           C
ANISOU 1972  C   ASP A 335    10197   6692  21435    598   2421    934       C
ATOM   1973  O   ASP A 335      -2.383  30.781   2.254  1.00101.63           O
ANISOU 1973  O   ASP A 335    10110   6729  21775    570   2280    908       O
ATOM   1974  CB  ASP A 335      -0.523  28.589   1.096  1.00 93.37           C
ANISOU 1974  CB  ASP A 335     9206   5984  20288    511   1771    719       C
ATOM   1975  CG  ASP A 335      -1.285  27.295   1.344  1.00104.43           C
ANISOU 1975  CG  ASP A 335    10410   7149  22120    512   1906    767       C
ATOM   1976  OD1 ASP A 335      -1.531  26.561   0.371  1.00105.27           O
ANISOU 1976  OD1 ASP A 335    10349   7225  22423    466   1618    681       O
ATOM   1977  OD2 ASP A 335      -1.629  27.016   2.512  1.00110.45           O
ANISOU 1977  OD2 ASP A 335    11196   7748  23023    563   2305    892       O
ATOM   1978  N   GLY A 336      -1.994  29.536   4.107  1.00100.04           N
ANISOU 1978  N   GLY A 336    10154   6415  21441    656   2835   1060       N
ATOM   1979  CA  GLY A 336      -3.210  29.902   4.823  1.00102.55           C
ANISOU 1979  CA  GLY A 336    10331   6451  22184    693   3194   1184       C
ATOM   1980  C   GLY A 336      -4.222  28.792   4.921  1.00109.57           C
ANISOU 1980  C   GLY A 336    10936   7042  23656    691   3340   1239       C
ATOM   1981  O   GLY A 336      -5.172  28.903   5.696  1.00112.38           O
ANISOU 1981  O   GLY A 336    11190   7130  24378    733   3711   1360       O
ATOM   1982  N   SER A 337      -4.035  27.727   4.133  1.00105.93           N
ANISOU 1982  N   SER A 337    10342   6610  23298    643   3059   1152       N
ATOM   1983  CA  SER A 337      -4.953  26.594   4.113  1.00108.56           C
ANISOU 1983  CA  SER A 337    10386   6661  24199    635   3153   1190       C
ATOM   1984  C   SER A 337      -4.739  25.638   5.285  1.00115.43           C
ANISOU 1984  C   SER A 337    11417   7432  25011    698   3551   1297       C
ATOM   1985  O   SER A 337      -3.636  25.542   5.826  1.00114.11           O
ANISOU 1985  O   SER A 337    11580   7468  24309    732   3603   1298       O
ATOM   1986  CB  SER A 337      -4.861  25.850   2.783  1.00111.27           C
ANISOU 1986  CB  SER A 337    10534   7064  24680    561   2684   1050       C
ATOM   1987  OG  SER A 337      -3.579  25.284   2.568  1.00115.74           O
ANISOU 1987  OG  SER A 337    11337   7886  24754    552   2508    975       O
ATOM   1988  N   THR A 338      -5.804  24.925   5.662  1.00115.61           N
ANISOU 1988  N   THR A 338    11200   7127  25599    717   3825   1388       N
ATOM   1989  CA  THR A 338      -5.786  23.920   6.723  1.00116.71           C
ANISOU 1989  CA  THR A 338    11453   7116  25777    782   4224   1498       C
ATOM   1990  C   THR A 338      -6.054  22.535   6.120  1.00120.77           C
ANISOU 1990  C   THR A 338    11709   7516  26660    738   4059   1447       C
ATOM   1991  O   THR A 338      -7.035  22.365   5.396  1.00121.36           O
ANISOU 1991  O   THR A 338    11414   7404  27295    687   3896   1410       O
ATOM   1992  CB  THR A 338      -6.755  24.315   7.869  1.00124.95           C
ANISOU 1992  CB  THR A 338    12484   7854  27138    858   4766   1666       C
ATOM   1993  OG1 THR A 338      -6.440  25.646   8.316  1.00118.87           O
ANISOU 1993  OG1 THR A 338    11958   7213  25994    892   4859   1694       O
ATOM   1994  CG2 THR A 338      -6.708  23.332   9.049  1.00124.85           C
ANISOU 1994  CG2 THR A 338    12647   7675  27116    942   5221   1792       C
ATOM   1995  N   VAL A 339      -5.208  21.541   6.432  1.00117.18           N
ANISOU 1995  N   VAL A 339    11447   7162  25916    759   4098   1445       N
ATOM   1996  CA  VAL A 339      -5.394  20.163   5.944  1.00118.17           C
ANISOU 1996  CA  VAL A 339    11353   7182  26365    722   3970   1401       C
ATOM   1997  C   VAL A 339      -5.607  19.146   7.046  1.00123.94           C
ANISOU 1997  C   VAL A 339    12148   7699  27243    792   4421   1530       C
ATOM   1998  O   VAL A 339      -5.237  19.398   8.189  1.00123.07           O
ANISOU 1998  O   VAL A 339    12362   7613  26787    874   4771   1632       O
ATOM   1999  CB  VAL A 339      -4.373  19.663   4.895  1.00119.94           C
ANISOU 1999  CB  VAL A 339    11629   7690  26254    655   3479   1243       C
ATOM   2000  CG1 VAL A 339      -5.011  19.602   3.512  1.00120.75           C
ANISOU 2000  CG1 VAL A 339    11361   7703  26816    573   3074   1128       C
ATOM   2001  CG2 VAL A 339      -3.081  20.480   4.894  1.00116.87           C
ANISOU 2001  CG2 VAL A 339    11562   7653  25189    653   3278   1176       C
ATOM   2002  N   THR A 340      -6.193  17.994   6.707  1.00123.46           N
ANISOU 2002  N   THR A 340    11794   7425  27690    765   4409   1525       N
ATOM   2003  CA  THR A 340      -6.417  16.929   7.683  1.00126.32           C
ANISOU 2003  CA  THR A 340    12196   7568  28231    831   4835   1645       C
ATOM   2004  C   THR A 340      -5.513  15.693   7.426  1.00131.85           C
ANISOU 2004  C   THR A 340    12985   8419  28691    811   4645   1576       C
ATOM   2005  O   THR A 340      -5.835  14.840   6.584  1.00133.30           O
ANISOU 2005  O   THR A 340    12878   8521  29250    748   4400   1498       O
ATOM   2006  CB  THR A 340      -7.932  16.627   7.855  1.00137.78           C
ANISOU 2006  CB  THR A 340    13267   8591  30492    841   5128   1738       C
ATOM   2007  OG1 THR A 340      -8.621  17.822   8.230  1.00136.55           O
ANISOU 2007  OG1 THR A 340    13088   8316  30481    870   5341   1813       O
ATOM   2008  CG2 THR A 340      -8.209  15.546   8.900  1.00138.63           C
ANISOU 2008  CG2 THR A 340    13428   8447  30797    919   5618   1876       C
ATOM   2009  N   VAL A 341      -4.391  15.598   8.177  1.00126.63           N
ANISOU 2009  N   VAL A 341    12730   7964  27419    867   4762   1606       N
ATOM   2010  CA  VAL A 341      -3.460  14.461   8.116  1.00124.87           C
ANISOU 2010  CA  VAL A 341    12638   7881  26925    862   4642   1560       C
ATOM   2011  C   VAL A 341      -4.156  13.278   8.803  1.00130.48           C
ANISOU 2011  C   VAL A 341    13228   8273  28077    912   5033   1674       C
ATOM   2012  O   VAL A 341      -4.427  13.353   9.996  1.00130.17           O
ANISOU 2012  O   VAL A 341    13365   8060  28033   1008   5509   1821       O
ATOM   2013  CB  VAL A 341      -2.074  14.792   8.752  1.00126.10           C
ANISOU 2013  CB  VAL A 341    13260   8327  26324    914   4653   1564       C
ATOM   2014  CG1 VAL A 341      -1.053  13.685   8.490  1.00124.16           C
ANISOU 2014  CG1 VAL A 341    13116   8254  25805    893   4445   1493       C
ATOM   2015  CG2 VAL A 341      -1.547  16.130   8.248  1.00123.75           C
ANISOU 2015  CG2 VAL A 341    13081   8289  25649    881   4370   1481       C
ATOM   2016  N   GLN A 342      -4.502  12.230   8.031  1.00129.50           N
ANISOU 2016  N   GLN A 342    12799   8051  28356    850   4837   1607       N
ATOM   2017  CA  GLN A 342      -5.179  11.019   8.519  1.00132.63           C
ANISOU 2017  CA  GLN A 342    13028   8138  29229    885   5162   1698       C
ATOM   2018  C   GLN A 342      -4.216  10.070   9.224  1.00137.64           C
ANISOU 2018  C   GLN A 342    13971   8870  29455    944   5323   1742       C
ATOM   2019  O   GLN A 342      -3.002  10.247   9.121  1.00134.42           O
ANISOU 2019  O   GLN A 342    13856   8782  28437    939   5098   1676       O
ATOM   2020  CB  GLN A 342      -5.909  10.282   7.380  1.00135.18           C
ANISOU 2020  CB  GLN A 342    12898   8312  30153    794   4856   1598       C
ATOM   2021  CG  GLN A 342      -6.938  11.121   6.614  1.00148.35           C
ANISOU 2021  CG  GLN A 342    14227   9851  32288    735   4653   1547       C
ATOM   2022  CD  GLN A 342      -8.104  11.628   7.433  1.00161.37           C
ANISOU 2022  CD  GLN A 342    15850  11296  34168    786   5018   1665       C
ATOM   2023  OE1 GLN A 342      -8.490  11.066   8.465  1.00155.22           O
ANISOU 2023  OE1 GLN A 342    14999  10141  33836    871   5607   1837       O
ATOM   2024  NE2 GLN A 342      -8.723  12.690   6.951  1.00157.89           N
ANISOU 2024  NE2 GLN A 342    15140  10700  34153    759   4958   1660       N
ATOM   2025  N   TRP A 343      -4.763   9.052   9.927  1.00138.79           N
ANISOU 2025  N   TRP A 343    14044   8731  29958   1000   5710   1853       N
ATOM   2026  CA  TRP A 343      -3.998   8.065  10.691  1.00139.00           C
ANISOU 2026  CA  TRP A 343    14350   8794  29670   1067   5916   1913       C
ATOM   2027  C   TRP A 343      -2.805   7.446   9.970  1.00141.39           C
ANISOU 2027  C   TRP A 343    14750   9411  29561   1007   5486   1779       C
ATOM   2028  O   TRP A 343      -1.694   7.482  10.513  1.00140.50           O
ANISOU 2028  O   TRP A 343    15018   9508  28856   1059   5508   1794       O
ATOM   2029  CB  TRP A 343      -4.893   6.998  11.342  1.00140.93           C
ANISOU 2029  CB  TRP A 343    14427   8658  30461   1123   6358   2038       C
ATOM   2030  CG  TRP A 343      -4.141   6.148  12.323  1.00142.25           C
ANISOU 2030  CG  TRP A 343    14943   8845  30261   1215   6635   2125       C
ATOM   2031  CD1 TRP A 343      -3.804   4.832  12.180  1.00145.22           C
ANISOU 2031  CD1 TRP A 343    15267   9218  30690   1201   6575   2099       C
ATOM   2032  CD2 TRP A 343      -3.509   6.596  13.531  1.00142.15           C
ANISOU 2032  CD2 TRP A 343    15414   8893  29702   1334   6949   2234       C
ATOM   2033  NE1 TRP A 343      -3.051   4.415  13.254  1.00144.50           N
ANISOU 2033  NE1 TRP A 343    15586   9165  30151   1307   6857   2194       N
ATOM   2034  CE2 TRP A 343      -2.837   5.483  14.088  1.00146.04           C
ANISOU 2034  CE2 TRP A 343    16125   9403  29959   1391   7073   2274       C
ATOM   2035  CE3 TRP A 343      -3.450   7.833  14.203  1.00143.33           C
ANISOU 2035  CE3 TRP A 343    15843   9075  29539   1401   7131   2300       C
ATOM   2036  CZ2 TRP A 343      -2.121   5.568  15.286  1.00145.48           C
ANISOU 2036  CZ2 TRP A 343    16547   9372  29355   1517   7358   2377       C
ATOM   2037  CZ3 TRP A 343      -2.730   7.918  15.383  1.00144.78           C
ANISOU 2037  CZ3 TRP A 343    16519   9301  29188   1524   7410   2398       C
ATOM   2038  CH2 TRP A 343      -2.087   6.793  15.921  1.00145.52           C
ANISOU 2038  CH2 TRP A 343    16827   9400  29062   1584   7519   2436       C
ATOM   2039  N   SER A 344      -3.019   6.930   8.736  1.00136.41           N
ANISOU 2039  N   SER A 344    13786   8804  29238    902   5086   1646       N
ATOM   2040  CA  SER A 344      -1.972   6.321   7.901  1.00133.16           C
ANISOU 2040  CA  SER A 344    13430   8669  28498    836   4661   1509       C
ATOM   2041  C   SER A 344      -0.769   7.267   7.627  1.00131.91           C
ANISOU 2041  C   SER A 344    13574   8885  27661    821   4366   1427       C
ATOM   2042  O   SER A 344       0.334   6.792   7.349  1.00129.14           O
ANISOU 2042  O   SER A 344    13397   8767  26904    803   4148   1356       O
ATOM   2043  CB  SER A 344      -2.566   5.786   6.598  1.00137.14           C
ANISOU 2043  CB  SER A 344    13527   9097  29483    732   4287   1381       C
ATOM   2044  OG  SER A 344      -3.654   4.903   6.832  1.00146.59           O
ANISOU 2044  OG  SER A 344    14417   9935  31346    743   4540   1451       O
ATOM   2045  N   GLY A 345      -0.991   8.576   7.755  1.00126.94           N
ANISOU 2045  N   GLY A 345    13003   8295  26932    831   4384   1441       N
ATOM   2046  CA  GLY A 345       0.034   9.594   7.555  1.00123.80           C
ANISOU 2046  CA  GLY A 345    12874   8221  25943    820   4140   1373       C
ATOM   2047  C   GLY A 345       0.911   9.869   8.763  1.00125.80           C
ANISOU 2047  C   GLY A 345    13560   8583  25654    917   4401   1464       C
ATOM   2048  O   GLY A 345       1.952  10.515   8.622  1.00122.37           O
ANISOU 2048  O   GLY A 345    13364   8428  24703    910   4180   1400       O
ATOM   2049  N   MET A 346       0.497   9.391   9.962  1.00124.39           N
ANISOU 2049  N   MET A 346    13494   8172  25595   1014   4872   1615       N
ATOM   2050  CA  MET A 346       1.231   9.587  11.220  1.00123.89           C
ANISOU 2050  CA  MET A 346    13870   8161  25041   1126   5153   1715       C
ATOM   2051  C   MET A 346       1.522   8.296  12.001  1.00125.64           C
ANISOU 2051  C   MET A 346    14241   8272  25223   1197   5408   1798       C
ATOM   2052  O   MET A 346       2.316   8.339  12.939  1.00125.01           O
ANISOU 2052  O   MET A 346    14550   8273  24674   1285   5547   1855       O
ATOM   2053  CB  MET A 346       0.487  10.588  12.124  1.00128.25           C
ANISOU 2053  CB  MET A 346    14535   8534  25660   1206   5531   1838       C
ATOM   2054  CG  MET A 346      -0.819  10.051  12.646  1.00135.83           C
ANISOU 2054  CG  MET A 346    15287   9107  27215   1250   5962   1963       C
ATOM   2055  SD  MET A 346      -1.833  11.310  13.415  1.00142.90           S
ANISOU 2055  SD  MET A 346    16232   9782  28281   1321   6360   2088       S
ATOM   2056  CE  MET A 346      -2.870  11.661  12.128  1.00140.22           C
ANISOU 2056  CE  MET A 346    15363   9353  28562   1200   6100   2000       C
ATOM   2057  N   SER A 347       0.864   7.171  11.645  1.00121.13           N
ANISOU 2057  N   SER A 347    13370   7503  25148   1166   5471   1805       N
ATOM   2058  CA  SER A 347       0.989   5.871  12.335  1.00121.09           C
ANISOU 2058  CA  SER A 347    13460   7357  25192   1231   5738   1888       C
ATOM   2059  C   SER A 347       2.410   5.306  12.495  1.00121.77           C
ANISOU 2059  C   SER A 347    13848   7692  24727   1250   5560   1845       C
ATOM   2060  O   SER A 347       2.630   4.495  13.402  1.00123.01           O
ANISOU 2060  O   SER A 347    14212   7738  24788   1339   5848   1944       O
ATOM   2061  CB  SER A 347       0.042   4.828  11.745  1.00124.70           C
ANISOU 2061  CB  SER A 347    13496   7582  26301   1174   5759   1876       C
ATOM   2062  OG  SER A 347       0.262   4.649  10.357  1.00129.02           O
ANISOU 2062  OG  SER A 347    13778   8303  26940   1047   5259   1710       O
ATOM   2063  N   TRP A 348       3.368   5.756  11.637  1.00113.38           N
ANISOU 2063  N   TRP A 348    12817   6950  23311   1171   5100   1704       N
ATOM   2064  CA  TRP A 348       4.790   5.363  11.634  1.00109.71           C
ANISOU 2064  CA  TRP A 348    12608   6745  22332   1173   4869   1643       C
ATOM   2065  C   TRP A 348       5.522   5.902  12.866  1.00110.93           C
ANISOU 2065  C   TRP A 348    13224   6956  21969   1291   5069   1731       C
ATOM   2066  O   TRP A 348       6.584   5.385  13.229  1.00107.95           O
ANISOU 2066  O   TRP A 348    13097   6707  21211   1329   4997   1725       O
ATOM   2067  CB  TRP A 348       5.488   5.923  10.372  1.00105.64           C
ANISOU 2067  CB  TRP A 348    11991   6524  21625   1060   4359   1475       C
ATOM   2068  CG  TRP A 348       5.615   7.426  10.368  1.00105.19           C
ANISOU 2068  CG  TRP A 348    12054   6597  21315   1061   4268   1452       C
ATOM   2069  CD1 TRP A 348       4.653   8.323  10.010  1.00108.62           C
ANISOU 2069  CD1 TRP A 348    12290   6944  22036   1028   4281   1448       C
ATOM   2070  CD2 TRP A 348       6.738   8.203  10.835  1.00103.17           C
ANISOU 2070  CD2 TRP A 348    12152   6559  20487   1105   4180   1440       C
ATOM   2071  NE1 TRP A 348       5.110   9.610  10.198  1.00106.55           N
ANISOU 2071  NE1 TRP A 348    12237   6841  21404   1047   4210   1434       N
ATOM   2072  CE2 TRP A 348       6.382   9.566  10.711  1.00106.42           C
ANISOU 2072  CE2 TRP A 348    12561   7010  20864   1094   4148   1428       C
ATOM   2073  CE3 TRP A 348       8.012   7.877  11.357  1.00103.05           C
ANISOU 2073  CE3 TRP A 348    12453   6698  20002   1154   4120   1439       C
ATOM   2074  CZ2 TRP A 348       7.256  10.606  11.060  1.00104.15           C
ANISOU 2074  CZ2 TRP A 348    12568   6914  20091   1127   4054   1410       C
ATOM   2075  CZ3 TRP A 348       8.888   8.909  11.690  1.00103.12           C
ANISOU 2075  CZ3 TRP A 348    12747   6890  19542   1187   4010   1418       C
ATOM   2076  CH2 TRP A 348       8.507  10.256  11.536  1.00103.39           C
ANISOU 2076  CH2 TRP A 348    12767   6964  19554   1172   3979   1402       C
ATOM   2077  N   ALA A 349       4.990   7.006  13.443  1.00108.07           N
ANISOU 2077  N   ALA A 349    12972   6505  21586   1345   5284   1802       N
ATOM   2078  CA  ALA A 349       5.568   7.750  14.560  1.00107.43           C
ANISOU 2078  CA  ALA A 349    13329   6465  21025   1457   5451   1876       C
ATOM   2079  C   ALA A 349       5.742   7.017  15.905  1.00111.35           C
ANISOU 2079  C   ALA A 349    14168   6788  21351   1598   5832   2014       C
ATOM   2080  O   ALA A 349       5.228   7.466  16.941  1.00112.40           O
ANISOU 2080  O   ALA A 349    14523   6724  21460   1708   6216   2140       O
ATOM   2081  CB  ALA A 349       4.878   9.098  14.725  1.00108.55           C
ANISOU 2081  CB  ALA A 349    13472   6548  21223   1470   5570   1908       C
ATOM   2082  N   ARG A 350       6.521   5.905  15.880  1.00105.88           N
ANISOU 2082  N   ARG A 350    13542   6172  20514   1600   5716   1989       N
ATOM   2083  CA  ARG A 350       6.927   5.151  17.070  1.00106.59           C
ANISOU 2083  CA  ARG A 350    13992   6142  20366   1734   5997   2102       C
ATOM   2084  C   ARG A 350       7.913   6.120  17.763  1.00108.79           C
ANISOU 2084  C   ARG A 350    14708   6579  20050   1810   5904   2099       C
ATOM   2085  O   ARG A 350       8.809   6.636  17.087  1.00105.26           O
ANISOU 2085  O   ARG A 350    14246   6410  19339   1734   5496   1974       O
ATOM   2086  CB  ARG A 350       7.610   3.814  16.693  1.00105.44           C
ANISOU 2086  CB  ARG A 350    13777   6079  20204   1698   5819   2052       C
ATOM   2087  CG  ARG A 350       6.641   2.739  16.199  1.00116.37           C
ANISOU 2087  CG  ARG A 350    14782   7266  22168   1646   5961   2071       C
ATOM   2088  CD  ARG A 350       7.204   1.331  16.300  1.00130.56           C
ANISOU 2088  CD  ARG A 350    16615   9065  23926   1660   5940   2074       C
ATOM   2089  NE  ARG A 350       8.009   0.964  15.132  1.00142.51           N
ANISOU 2089  NE  ARG A 350    17935  10843  25368   1535   5467   1919       N
ATOM   2090  CZ  ARG A 350       8.689  -0.174  15.012  1.00162.15           C
ANISOU 2090  CZ  ARG A 350    20439  13396  27773   1524   5353   1891       C
ATOM   2091  NH1 ARG A 350       8.674  -1.073  15.990  1.00157.45           N
ANISOU 2091  NH1 ARG A 350    20045  12629  27151   1632   5664   2007       N
ATOM   2092  NH2 ARG A 350       9.395  -0.419  13.915  1.00145.23           N
ANISOU 2092  NH2 ARG A 350    18125  11485  25570   1410   4936   1749       N
ATOM   2093  N   PRO A 351       7.675   6.518  19.033  1.00107.43           N
ANISOU 2093  N   PRO A 351    14905   6224  19691   1955   6272   2230       N
ATOM   2094  CA  PRO A 351       8.508   7.563  19.645  1.00106.74           C
ANISOU 2094  CA  PRO A 351    15213   6272  19070   2023   6161   2218       C
ATOM   2095  C   PRO A 351       9.974   7.213  19.811  1.00109.20           C
ANISOU 2095  C   PRO A 351    15796   6788  18905   2049   5860   2156       C
ATOM   2096  O   PRO A 351      10.306   6.099  20.173  1.00109.36           O
ANISOU 2096  O   PRO A 351    15923   6742  18888   2100   5936   2198       O
ATOM   2097  CB  PRO A 351       7.815   7.821  20.992  1.00111.24           C
ANISOU 2097  CB  PRO A 351    16121   6546  19599   2184   6669   2384       C
ATOM   2098  CG  PRO A 351       6.432   7.281  20.831  1.00117.49           C
ANISOU 2098  CG  PRO A 351    16586   7066  20988   2166   7024   2466       C
ATOM   2099  CD  PRO A 351       6.626   6.080  19.971  1.00111.90           C
ANISOU 2099  CD  PRO A 351    15557   6436  20523   2068   6812   2394       C
ATOM   2100  N   TYR A 352      10.845   8.173  19.540  1.00104.12           N
ANISOU 2100  N   TYR A 352    15255   6387  17919   2012   5518   2057       N
ATOM   2101  CA  TYR A 352      12.283   8.010  19.674  1.00102.94           C
ANISOU 2101  CA  TYR A 352    15351   6434  17328   2032   5201   1989       C
ATOM   2102  C   TYR A 352      12.627   7.951  21.173  1.00108.66           C
ANISOU 2102  C   TYR A 352    16609   6999  17677   2215   5440   2103       C
ATOM   2103  O   TYR A 352      12.265   8.872  21.908  1.00108.65           O
ANISOU 2103  O   TYR A 352    16860   6893  17529   2301   5637   2166       O
ATOM   2104  CB  TYR A 352      12.984   9.198  18.985  1.00102.76           C
ANISOU 2104  CB  TYR A 352    15278   6677  17091   1947   4812   1860       C
ATOM   2105  CG  TYR A 352      14.462   9.318  19.266  1.00104.32           C
ANISOU 2105  CG  TYR A 352    15762   7054  16822   1981   4499   1795       C
ATOM   2106  CD1 TYR A 352      15.396   8.672  18.466  1.00104.62           C
ANISOU 2106  CD1 TYR A 352    15639   7278  16833   1896   4163   1693       C
ATOM   2107  CD2 TYR A 352      14.932  10.081  20.336  1.00105.72           C
ANISOU 2107  CD2 TYR A 352    16376   7198  16597   2103   4537   1834       C
ATOM   2108  CE1 TYR A 352      16.762   8.784  18.719  1.00103.51           C
ANISOU 2108  CE1 TYR A 352    15741   7284  16304   1927   3874   1634       C
ATOM   2109  CE2 TYR A 352      16.293  10.157  20.627  1.00105.66           C
ANISOU 2109  CE2 TYR A 352    16627   7330  16190   2139   4234   1773       C
ATOM   2110  CZ  TYR A 352      17.205   9.513  19.810  1.00107.88           C
ANISOU 2110  CZ  TYR A 352    16715   7793  16480   2048   3903   1673       C
ATOM   2111  OH  TYR A 352      18.546   9.578  20.087  1.00104.09           O
ANISOU 2111  OH  TYR A 352    16466   7434  15649   2083   3605   1614       O
ATOM   2112  N   ARG A 353      13.285   6.868  21.633  1.00107.08           N
ANISOU 2112  N   ARG A 353    16592   6766  17327   2280   5434   2132       N
ATOM   2113  CA  ARG A 353      13.699   6.733  23.040  1.00109.08           C
ANISOU 2113  CA  ARG A 353    17385   6866  17196   2463   5622   2234       C
ATOM   2114  C   ARG A 353      15.195   7.005  23.214  1.00112.84           C
ANISOU 2114  C   ARG A 353    18128   7545  17201   2485   5214   2146       C
ATOM   2115  O   ARG A 353      15.589   7.652  24.183  1.00112.98           O
ANISOU 2115  O   ARG A 353    18578   7508  16840   2608   5236   2181       O
ATOM   2116  CB  ARG A 353      13.269   5.408  23.661  1.00110.38           C
ANISOU 2116  CB  ARG A 353    17637   6794  17508   2553   5963   2354       C
ATOM   2117  CG  ARG A 353      13.013   5.553  25.147  1.00122.80           C
ANISOU 2117  CG  ARG A 353    19737   8099  18822   2755   6351   2501       C
ATOM   2118  CD  ARG A 353      12.542   4.267  25.770  1.00138.40           C
ANISOU 2118  CD  ARG A 353    21807   9824  20957   2851   6722   2627       C
ATOM   2119  NE  ARG A 353      12.928   4.194  27.177  1.00150.23           N
ANISOU 2119  NE  ARG A 353    23914  11129  22036   3059   6938   2738       N
ATOM   2120  CZ  ARG A 353      13.999   3.550  27.628  1.00166.29           C
ANISOU 2120  CZ  ARG A 353    26260  13201  23720   3140   6755   2731       C
ATOM   2121  NH1 ARG A 353      14.798   2.903  26.787  1.00150.12           N
ANISOU 2121  NH1 ARG A 353    23957  11376  21704   3029   6371   2623       N
ATOM   2122  NH2 ARG A 353      14.275   3.538  28.924  1.00156.76           N
ANISOU 2122  NH2 ARG A 353    25634  11798  22131   3339   6954   2834       N
ATOM   2123  N   ASN A 354      16.013   6.501  22.267  1.00108.57           N
ANISOU 2123  N   ASN A 354    17323   7225  16702   2366   4841   2029       N
ATOM   2124  CA  ASN A 354      17.448   6.744  22.089  1.00106.97           C
ANISOU 2124  CA  ASN A 354    17235   7244  16164   2344   4400   1919       C
ATOM   2125  C   ASN A 354      17.861   6.165  20.741  1.00107.90           C
ANISOU 2125  C   ASN A 354    16915   7567  16516   2180   4102   1803       C
ATOM   2126  O   ASN A 354      16.964   5.744  20.002  1.00107.65           O
ANISOU 2126  O   ASN A 354    16526   7498  16879   2092   4236   1807       O
ATOM   2127  CB  ASN A 354      18.319   6.290  23.272  1.00110.55           C
ANISOU 2127  CB  ASN A 354    18172   7606  16226   2502   4386   1975       C
ATOM   2128  CG  ASN A 354      18.361   4.816  23.555  1.00134.97           C
ANISOU 2128  CG  ASN A 354    21296  10576  19412   2552   4534   2044       C
ATOM   2129  OD1 ASN A 354      18.847   4.006  22.755  1.00127.02           O
ANISOU 2129  OD1 ASN A 354    20006   9695  18560   2452   4332   1976       O
ATOM   2130  ND2 ASN A 354      17.978   4.465  24.768  1.00129.72           N
ANISOU 2130  ND2 ASN A 354    21021   9659  18606   2719   4874   2178       N
ATOM   2131  N   ALA A 355      19.174   6.182  20.376  1.00101.50           N
ANISOU 2131  N   ALA A 355    16118   6959  15488   2135   3701   1696       N
ATOM   2132  CA  ALA A 355      19.619   5.658  19.073  1.00 98.47           C
ANISOU 2132  CA  ALA A 355    15343   6763  15309   1984   3425   1584       C
ATOM   2133  C   ALA A 355      19.242   4.173  18.905  1.00102.82           C
ANISOU 2133  C   ALA A 355    15733   7212  16121   1972   3585   1632       C
ATOM   2134  O   ALA A 355      18.769   3.768  17.842  1.00102.04           O
ANISOU 2134  O   ALA A 355    15248   7167  16354   1850   3552   1582       O
ATOM   2135  CB  ALA A 355      21.119   5.876  18.890  1.00 97.42           C
ANISOU 2135  CB  ALA A 355    15302   6819  14894   1964   3021   1482       C
ATOM   2136  N   ASN A 356      19.368   3.401  19.995  1.00100.27           N
ANISOU 2136  N   ASN A 356    15724   6722  15651   2107   3774   1735       N
ATOM   2137  CA  ASN A 356      19.097   1.970  20.059  1.00100.71           C
ANISOU 2137  CA  ASN A 356    15700   6659  15908   2122   3949   1796       C
ATOM   2138  C   ASN A 356      17.683   1.587  20.547  1.00105.75           C
ANISOU 2138  C   ASN A 356    16324   7039  16818   2184   4421   1926       C
ATOM   2139  O   ASN A 356      17.350   0.394  20.599  1.00103.72           O
ANISOU 2139  O   ASN A 356    15985   6659  16763   2199   4601   1984       O
ATOM   2140  CB  ASN A 356      20.169   1.307  20.899  1.00100.01           C
ANISOU 2140  CB  ASN A 356    15954   6545  15501   2232   3851   1824       C
ATOM   2141  CG  ASN A 356      21.475   1.277  20.171  1.00120.69           C
ANISOU 2141  CG  ASN A 356    18459   9397  18001   2143   3408   1695       C
ATOM   2142  OD1 ASN A 356      21.670   0.500  19.229  1.00117.34           O
ANISOU 2142  OD1 ASN A 356    17719   9068  17795   2034   3282   1633       O
ATOM   2143  ND2 ASN A 356      22.302   2.262  20.445  1.00108.46           N
ANISOU 2143  ND2 ASN A 356    17119   7947  16145   2173   3167   1642       N
ATOM   2144  N   SER A 357      16.837   2.587  20.850  1.00104.42           N
ANISOU 2144  N   SER A 357    16211   6779  16684   2215   4626   1972       N
ATOM   2145  CA  SER A 357      15.495   2.309  21.349  1.00107.15           C
ANISOU 2145  CA  SER A 357    16550   6857  17306   2280   5095   2101       C
ATOM   2146  C   SER A 357      14.422   3.245  20.796  1.00110.18           C
ANISOU 2146  C   SER A 357    16658   7221  17983   2201   5203   2088       C
ATOM   2147  O   SER A 357      14.616   4.461  20.718  1.00106.70           O
ANISOU 2147  O   SER A 357    16283   6893  17365   2183   5054   2037       O
ATOM   2148  CB  SER A 357      15.495   2.343  22.876  1.00114.65           C
ANISOU 2148  CB  SER A 357    18033   7593  17938   2478   5387   2235       C
ATOM   2149  OG  SER A 357      14.262   1.933  23.444  1.00128.45           O
ANISOU 2149  OG  SER A 357    19809   9048  19946   2559   5883   2375       O
ATOM   2150  N   VAL A 358      13.277   2.646  20.414  1.00108.85           N
ANISOU 2150  N   VAL A 358    16172   6898  18289   2154   5459   2134       N
ATOM   2151  CA  VAL A 358      12.072   3.339  19.952  1.00108.86           C
ANISOU 2151  CA  VAL A 358    15887   6819  18656   2090   5615   2142       C
ATOM   2152  C   VAL A 358      10.865   2.776  20.694  1.00114.13           C
ANISOU 2152  C   VAL A 358    16576   7150  19638   2183   6136   2295       C
ATOM   2153  O   VAL A 358      10.814   1.584  21.001  1.00114.52           O
ANISOU 2153  O   VAL A 358    16638   7069  19807   2227   6305   2356       O
ATOM   2154  CB  VAL A 358      11.857   3.437  18.414  1.00111.02           C
ANISOU 2154  CB  VAL A 358    15657   7269  19258   1905   5307   2006       C
ATOM   2155  CG1 VAL A 358      13.131   3.876  17.706  1.00108.47           C
ANISOU 2155  CG1 VAL A 358    15335   7259  18619   1824   4822   1862       C
ATOM   2156  CG2 VAL A 358      11.314   2.144  17.810  1.00111.32           C
ANISOU 2156  CG2 VAL A 358    15349   7209  19737   1839   5378   2006       C
ATOM   2157  N   GLY A 359       9.921   3.652  20.984  1.00111.11           N
ANISOU 2157  N   GLY A 359    16202   6624  19392   2215   6394   2358       N
ATOM   2158  CA  GLY A 359       8.704   3.315  21.696  1.00113.86           C
ANISOU 2158  CA  GLY A 359    16567   6631  20065   2305   6921   2509       C
ATOM   2159  C   GLY A 359       7.723   2.546  20.848  1.00120.12           C
ANISOU 2159  C   GLY A 359    16851   7312  21475   2199   7008   2499       C
ATOM   2160  O   GLY A 359       7.918   2.385  19.640  1.00117.07           O
ANISOU 2160  O   GLY A 359    16096   7121  21264   2050   6642   2367       O
ATOM   2161  N   ALA A 360       6.650   2.080  21.497  1.00122.58           N
ANISOU 2161  N   ALA A 360    17158   7291  22127   2283   7503   2640       N
ATOM   2162  CA  ALA A 360       5.574   1.316  20.878  1.00124.87           C
ANISOU 2162  CA  ALA A 360    16983   7400  23062   2206   7663   2655       C
ATOM   2163  C   ALA A 360       4.879   2.143  19.805  1.00129.21           C
ANISOU 2163  C   ALA A 360    17105   8024  23967   2066   7463   2561       C
ATOM   2164  O   ALA A 360       4.923   3.368  19.863  1.00127.68           O
ANISOU 2164  O   ALA A 360    17024   7924  23563   2066   7382   2539       O
ATOM   2165  CB  ALA A 360       4.566   0.896  21.940  1.00129.14           C
ANISOU 2165  CB  ALA A 360    17658   7543  23866   2344   8279   2840       C
ATOM   2166  N   ALA A 361       4.245   1.477  18.824  1.00127.94           N
ANISOU 2166  N   ALA A 361    16462   7815  24336   1948   7369   2504       N
ATOM   2167  CA  ALA A 361       3.499   2.138  17.757  1.00128.11           C
ANISOU 2167  CA  ALA A 361    16059   7874  24742   1818   7168   2414       C
ATOM   2168  C   ALA A 361       2.446   3.071  18.389  1.00136.96           C
ANISOU 2168  C   ALA A 361    17214   8754  26072   1885   7555   2525       C
ATOM   2169  O   ALA A 361       1.807   2.685  19.378  1.00140.11           O
ANISOU 2169  O   ALA A 361    17761   8846  26626   2005   8055   2679       O
ATOM   2170  CB  ALA A 361       2.830   1.104  16.865  1.00129.35           C
ANISOU 2170  CB  ALA A 361    15740   7931  25478   1715   7091   2363       C
ATOM   2171  N   PRO A 362       2.314   4.327  17.910  1.00133.52           N
ANISOU 2171  N   PRO A 362    16684   8446  25602   1822   7353   2456       N
ATOM   2172  CA  PRO A 362       1.337   5.236  18.527  1.00135.92           C
ANISOU 2172  CA  PRO A 362    17027   8518  26097   1887   7728   2564       C
ATOM   2173  C   PRO A 362      -0.088   4.712  18.399  1.00144.10           C
ANISOU 2173  C   PRO A 362    17672   9205  27873   1872   8056   2639       C
ATOM   2174  O   PRO A 362      -0.425   4.106  17.380  1.00143.18           O
ANISOU 2174  O   PRO A 362    17132   9100  28172   1756   7821   2551       O
ATOM   2175  CB  PRO A 362       1.554   6.555  17.782  1.00135.49           C
ANISOU 2175  CB  PRO A 362    16883   8711  25885   1795   7354   2446       C
ATOM   2176  CG  PRO A 362       2.151   6.169  16.476  1.00137.37           C
ANISOU 2176  CG  PRO A 362    16840   9218  26136   1652   6824   2277       C
ATOM   2177  CD  PRO A 362       2.991   4.958  16.760  1.00132.43           C
ANISOU 2177  CD  PRO A 362    16388   8648  25281   1689   6798   2282       C
ATOM   2178  N   SER A 363      -0.887   4.864  19.469  1.00144.73           N
ANISOU 2178  N   SER A 363    17915   8958  28117   1997   8611   2806       N
ATOM   2179  CA  SER A 363      -2.270   4.399  19.521  1.00147.97           C
ANISOU 2179  CA  SER A 363    17982   8987  29254   2003   9001   2901       C
ATOM   2180  C   SER A 363      -3.310   5.493  19.239  1.00154.46           C
ANISOU 2180  C   SER A 363    18550   9675  30463   1963   9090   2914       C
ATOM   2181  O   SER A 363      -4.441   5.169  18.871  1.00153.69           O
ANISOU 2181  O   SER A 363    18168   9655  30570   1856   8812   2820       O
ATOM   2182  CB  SER A 363      -2.552   3.694  20.838  1.00152.71           C
ANISOU 2182  CB  SER A 363    18899   9309  29814   2158   9537   3069       C
ATOM   2183  OG  SER A 363      -2.883   2.353  20.542  1.00157.54           O
ANISOU 2183  OG  SER A 363    19361  10174  30322   2047   9071   2928       O
ATOM   2184  N   ARG A 364      -2.933   6.777  19.397  1.00149.81           N
ANISOU 2184  N   ARG A 364    18197   9262  29462   1976   8975   2890       N
ATOM   2185  CA  ARG A 364      -3.801   7.929  19.131  1.00150.84           C
ANISOU 2185  CA  ARG A 364    18122   9303  29887   1939   9024   2894       C
ATOM   2186  C   ARG A 364      -2.959   9.151  18.708  1.00152.72           C
ANISOU 2186  C   ARG A 364    18526   9909  29593   1886   8597   2777       C
ATOM   2187  O   ARG A 364      -1.757   9.180  18.992  1.00151.33           O
ANISOU 2187  O   ARG A 364    18726   9984  28788   1923   8411   2737       O
ATOM   2188  CB  ARG A 364      -4.741   8.222  20.322  1.00152.39           C
ANISOU 2188  CB  ARG A 364    18605   9463  29833   2005   9217   2957       C
ATOM   2189  CG  ARG A 364      -4.044   8.725  21.592  1.00162.46           C
ANISOU 2189  CG  ARG A 364    20600  11219  29909   2049   8833   2875       C
ATOM   2190  CD  ARG A 364      -4.831   8.461  22.856  1.00172.00           C
ANISOU 2190  CD  ARG A 364    22167  12902  30283   1983   8251   2726       C
ATOM   2191  NE  ARG A 364      -5.004   9.691  23.636  1.00178.55           N
ANISOU 2191  NE  ARG A 364    23271  14001  30568   1960   7972   2659       N
ATOM   2192  CZ  ARG A 364      -5.968   9.891  24.527  1.00186.87           C
ANISOU 2192  CZ  ARG A 364    24514  15429  31060   1877   7469   2529       C
ATOM   2193  NH1 ARG A 364      -6.859   8.940  24.778  1.00181.38           N
ANISOU 2193  NH1 ARG A 364    23712  14311  30891   1963   8025   2680       N
ATOM   2194  NH2 ARG A 364      -6.051  11.047  25.172  1.00173.49           N
ANISOU 2194  NH2 ARG A 364    22929  13006  29981   2103   8608   2848       N
ATOM   2195  N   ALA A 365      -3.578  10.140  18.022  1.00147.94           N
ANISOU 2195  N   ALA A 365    17634   9324  29253   1802   8437   2721       N
ATOM   2196  CA  ALA A 365      -2.883  11.329  17.518  1.00145.27           C
ANISOU 2196  CA  ALA A 365    17401   9317  28477   1744   8033   2606       C
ATOM   2197  C   ALA A 365      -2.332  12.282  18.589  1.00148.46           C
ANISOU 2197  C   ALA A 365    18328   9778  28301   1862   8235   2679       C
ATOM   2198  O   ALA A 365      -1.417  13.060  18.286  1.00145.20           O
ANISOU 2198  O   ALA A 365    18085   9679  27405   1827   7874   2578       O
ATOM   2199  CB  ALA A 365      -3.757  12.079  16.530  1.00146.14           C
ANISOU 2199  CB  ALA A 365    17071   9405  29052   1632   7834   2536       C
ATOM   2200  N   SER A 366      -2.877  12.228  19.831  1.00147.80           N
ANISOU 2200  N   SER A 366    18510   9381  28265   2006   8811   2852       N
ATOM   2201  CA  SER A 366      -2.432  13.079  20.946  1.00147.19           C
ANISOU 2201  CA  SER A 366    18969   9309  27647   2137   9043   2933       C
ATOM   2202  C   SER A 366      -1.046  12.677  21.459  1.00146.71           C
ANISOU 2202  C   SER A 366    19367   9467  26909   2204   8875   2903       C
ATOM   2203  O   SER A 366      -0.320  13.507  22.009  1.00144.75           O
ANISOU 2203  O   SER A 366    19529   9359  26112   2270   8819   2898       O
ATOM   2204  CB  SER A 366      -3.462  13.106  22.074  1.00154.43           C
ANISOU 2204  CB  SER A 366    20039   9802  28837   2275   9718   3127       C
ATOM   2205  OG  SER A 366      -3.778  11.816  22.569  1.00159.37           O
ANISOU 2205  OG  SER A 366    20733  10622  29201   2230   9414   3050       O
ATOM   2206  N   GLN A 367      -0.678  11.406  21.240  1.00140.92           N
ANISOU 2206  N   GLN A 367    18549   8762  26232   2184   8773   2878       N
ATOM   2207  CA  GLN A 367       0.625  10.849  21.606  1.00138.80           C
ANISOU 2207  CA  GLN A 367    18652   8694  25393   2235   8579   2842       C
ATOM   2208  C   GLN A 367       1.724  11.362  20.663  1.00139.94           C
ANISOU 2208  C   GLN A 367    18740   9258  25173   2117   7958   2661       C
ATOM   2209  O   GLN A 367       2.901  11.357  21.037  1.00138.46           O
ANISOU 2209  O   GLN A 367    18913   9264  24430   2165   7765   2624       O
ATOM   2210  CB  GLN A 367       0.584   9.319  21.553  1.00140.24           C
ANISOU 2210  CB  GLN A 367    18703   8764  25818   2238   8666   2869       C
ATOM   2211  CG  GLN A 367      -0.403   8.687  22.527  1.00138.92           C
ANISOU 2211  CG  GLN A 367    18614   8170  25997   2364   9298   3053       C
ATOM   2212  CD  GLN A 367      -0.550   7.199  22.342  1.00145.22           C
ANISOU 2212  CD  GLN A 367    19201   8851  27123   2347   9369   3071       C
ATOM   2213  OE1 GLN A 367      -0.057   6.601  21.379  1.00134.77           O
ANISOU 2213  OE1 GLN A 367    17600   7746  25861   2226   8945   2942       O
ATOM   2214  NE2 GLN A 367      -1.238   6.566  23.272  1.00137.22           N
ANISOU 2214  NE2 GLN A 367    18325   7479  26334   2474   9924   3234       N
ATOM   2215  N   ILE A 368       1.338  11.788  19.439  1.00134.01           N
ANISOU 2215  N   ILE A 368    17539   8630  24747   1969   7648   2550       N
ATOM   2216  CA  ILE A 368       2.252  12.282  18.404  1.00129.52           C
ANISOU 2216  CA  ILE A 368    16867   8435  23910   1849   7078   2378       C
ATOM   2217  C   ILE A 368       2.360  13.815  18.406  1.00131.77           C
ANISOU 2217  C   ILE A 368    17272   8847  23946   1843   6973   2345       C
ATOM   2218  O   ILE A 368       3.471  14.346  18.430  1.00129.53           O
ANISOU 2218  O   ILE A 368    17242   8825  23149   1843   6683   2268       O
ATOM   2219  CB  ILE A 368       1.895  11.715  16.992  1.00130.84           C
ANISOU 2219  CB  ILE A 368    16503   8673  24537   1695   6754   2263       C
ATOM   2220  CG1 ILE A 368       1.617  10.194  17.032  1.00131.73           C
ANISOU 2220  CG1 ILE A 368    16463   8611  24977   1703   6908   2307       C
ATOM   2221  CG2 ILE A 368       2.992  12.040  15.975  1.00127.62           C
ANISOU 2221  CG2 ILE A 368    16048   8643  23797   1588   6186   2091       C
ATOM   2222  CD1 ILE A 368       0.453   9.752  16.210  1.00134.15           C
ANISOU 2222  CD1 ILE A 368    16256   8732  25982   1613   6927   2293       C
ATOM   2223  N   VAL A 369       1.219  14.518  18.353  1.00129.29           N
ANISOU 2223  N   VAL A 369    16760   8346  24019   1834   7198   2400       N
ATOM   2224  CA  VAL A 369       1.192  15.986  18.286  1.00127.82           C
ANISOU 2224  CA  VAL A 369    16641   8265  23660   1820   7111   2370       C
ATOM   2225  C   VAL A 369       0.349  16.678  19.372  1.00133.97           C
ANISOU 2225  C   VAL A 369    17622   8758  24522   1936   7621   2521       C
ATOM   2226  O   VAL A 369      -0.619  16.114  19.889  1.00136.02           O
ANISOU 2226  O   VAL A 369    17790   8690  25202   1992   8053   2645       O
ATOM   2227  CB  VAL A 369       0.853  16.530  16.863  1.00129.59           C
ANISOU 2227  CB  VAL A 369    16409   8647  24181   1663   6714   2237       C
ATOM   2228  CG1 VAL A 369       1.997  16.296  15.883  1.00126.21           C
ANISOU 2228  CG1 VAL A 369    15924   8564  23467   1566   6176   2076       C
ATOM   2229  CG2 VAL A 369      -0.463  15.960  16.330  1.00131.18           C
ANISOU 2229  CG2 VAL A 369    16142   8593  25108   1606   6859   2270       C
ATOM   2230  N   LYS A 370       0.749  17.926  19.690  1.00129.53           N
ANISOU 2230  N   LYS A 370    17334   8320  23559   1969   7564   2506       N
ATOM   2231  CA  LYS A 370       0.133  18.879  20.618  1.00130.32           C
ANISOU 2231  CA  LYS A 370    17671   8216  23628   2070   7965   2623       C
ATOM   2232  C   LYS A 370      -0.368  20.041  19.749  1.00130.74           C
ANISOU 2232  C   LYS A 370    17406   8366  23905   1963   7763   2550       C
ATOM   2233  O   LYS A 370       0.246  20.327  18.715  1.00127.97           O
ANISOU 2233  O   LYS A 370    16869   8313  23442   1847   7273   2402       O
ATOM   2234  CB  LYS A 370       1.196  19.458  21.579  1.00132.24           C
ANISOU 2234  CB  LYS A 370    18493   8581  23172   2182   7952   2632       C
ATOM   2235  CG  LYS A 370       1.723  18.525  22.669  1.00149.57           C
ANISOU 2235  CG  LYS A 370    21125  10643  25063   2326   8206   2725       C
ATOM   2236  CD  LYS A 370       2.973  19.125  23.341  1.00154.44           C
ANISOU 2236  CD  LYS A 370    22241  11470  24969   2398   7978   2674       C
ATOM   2237  CE  LYS A 370       3.223  18.596  24.751  1.00163.03           C
ANISOU 2237  CE  LYS A 370    23885  12349  25710   2586   8334   2800       C
ATOM   2238  NZ  LYS A 370       3.537  17.131  24.820  1.00164.01           N
ANISOU 2238  NZ  LYS A 370    24021  12411  25886   2615   8376   2828       N
ATOM   2239  N   VAL A 371      -1.447  20.731  20.166  1.00126.81           N
ANISOU 2239  N   VAL A 371    16861   7614  23706   2006   8140   2653       N
ATOM   2240  CA  VAL A 371      -1.947  21.895  19.429  1.00124.39           C
ANISOU 2240  CA  VAL A 371    16279   7382  23601   1916   7971   2594       C
ATOM   2241  C   VAL A 371      -0.886  23.017  19.593  1.00124.40           C
ANISOU 2241  C   VAL A 371    16629   7670  22968   1930   7711   2519       C
ATOM   2242  O   VAL A 371      -0.359  23.198  20.696  1.00124.73           O
ANISOU 2242  O   VAL A 371    17154   7672  22565   2055   7921   2587       O
ATOM   2243  CB  VAL A 371      -3.379  22.308  19.879  1.00130.76           C
ANISOU 2243  CB  VAL A 371    16943   7823  24918   1962   8463   2732       C
ATOM   2244  CG1 VAL A 371      -3.830  23.599  19.205  1.00129.67           C
ANISOU 2244  CG1 VAL A 371    16557   7767  24944   1878   8283   2674       C
ATOM   2245  CG2 VAL A 371      -4.386  21.192  19.602  1.00132.64           C
ANISOU 2245  CG2 VAL A 371    16796   7778  25824   1939   8680   2794       C
ATOM   2246  N   LYS A 372      -0.527  23.694  18.474  1.00116.37           N
ANISOU 2246  N   LYS A 372    15375   6935  21904   1805   7240   2375       N
ATOM   2247  CA  LYS A 372       0.478  24.763  18.366  1.00113.08           C
ANISOU 2247  CA  LYS A 372    15194   6813  20959   1791   6924   2279       C
ATOM   2248  C   LYS A 372       1.908  24.248  18.139  1.00112.97           C
ANISOU 2248  C   LYS A 372    15358   7086  20478   1771   6538   2171       C
ATOM   2249  O   LYS A 372       2.885  24.988  18.326  1.00110.43           O
ANISOU 2249  O   LYS A 372    15319   6974  19666   1789   6331   2109       O
ATOM   2250  CB  LYS A 372       0.382  25.828  19.489  1.00116.30           C
ANISOU 2250  CB  LYS A 372    15998   7110  21081   1907   7245   2372       C
ATOM   2251  CG  LYS A 372      -0.617  26.951  19.214  1.00115.56           C
ANISOU 2251  CG  LYS A 372    15684   6907  21316   1873   7380   2402       C
ATOM   2252  CD  LYS A 372      -0.591  27.990  20.343  1.00119.06           C
ANISOU 2252  CD  LYS A 372    16565   7254  21417   1993   7684   2488       C
ATOM   2253  CE  LYS A 372      -1.343  29.267  20.029  1.00113.40           C
ANISOU 2253  CE  LYS A 372    15676   6513  20899   1950   7723   2489       C
ATOM   2254  NZ  LYS A 372      -1.956  29.863  21.259  1.00109.98           N
ANISOU 2254  NZ  LYS A 372    15580   5810  20398   2084   8234   2634       N
ATOM   2255  N   ASP A 373       2.011  22.986  17.677  1.00108.98           N
ANISOU 2255  N   ASP A 373    14663   6585  20160   1729   6432   2143       N
ATOM   2256  CA  ASP A 373       3.263  22.298  17.330  1.00106.38           C
ANISOU 2256  CA  ASP A 373    14431   6503  19488   1698   6072   2042       C
ATOM   2257  C   ASP A 373       3.642  22.653  15.893  1.00107.40           C
ANISOU 2257  C   ASP A 373    14240   6907  19660   1553   5576   1883       C
ATOM   2258  O   ASP A 373       2.783  22.590  15.008  1.00107.31           O
ANISOU 2258  O   ASP A 373    13827   6836  20108   1466   5512   1857       O
ATOM   2259  CB  ASP A 373       3.068  20.763  17.389  1.00108.83           C
ANISOU 2259  CB  ASP A 373    14631   6674  20044   1709   6192   2085       C
ATOM   2260  CG  ASP A 373       3.566  20.027  18.623  1.00116.50           C
ANISOU 2260  CG  ASP A 373    16025   7526  20715   1846   6463   2182       C
ATOM   2261  OD1 ASP A 373       4.486  20.537  19.289  1.00116.78           O
ANISOU 2261  OD1 ASP A 373    16466   7673  20230   1919   6400   2173       O
ATOM   2262  OD2 ASP A 373       3.134  18.877  18.837  1.00120.24           O
ANISOU 2262  OD2 ASP A 373    16415   7812  21461   1874   6682   2252       O
ATOM   2263  N   ILE A 374       4.927  22.979  15.648  1.00101.44           N
ANISOU 2263  N   ILE A 374    13664   6436  18444   1530   5223   1777       N
ATOM   2264  CA  ILE A 374       5.439  23.254  14.299  1.00 98.17           C
ANISOU 2264  CA  ILE A 374    12993   6285  18022   1403   4759   1626       C
ATOM   2265  C   ILE A 374       5.980  21.932  13.719  1.00 99.82           C
ANISOU 2265  C   ILE A 374    13069   6574  18285   1352   4547   1564       C
ATOM   2266  O   ILE A 374       7.078  21.491  14.076  1.00 98.06           O
ANISOU 2266  O   ILE A 374    13087   6471  17699   1386   4433   1537       O
ATOM   2267  CB  ILE A 374       6.449  24.445  14.226  1.00 98.93           C
ANISOU 2267  CB  ILE A 374    13305   6629  17654   1397   4501   1542       C
ATOM   2268  CG1 ILE A 374       5.861  25.764  14.802  1.00 99.59           C
ANISOU 2268  CG1 ILE A 374    13517   6623  17699   1447   4722   1605       C
ATOM   2269  CG2 ILE A 374       6.993  24.646  12.811  1.00 97.99           C
ANISOU 2269  CG2 ILE A 374    12935   6763  17533   1273   4049   1392       C
ATOM   2270  CD1 ILE A 374       4.575  26.377  14.101  1.00106.63           C
ANISOU 2270  CD1 ILE A 374    14049   7405  19062   1382   4794   1619       C
ATOM   2271  N   VAL A 375       5.158  21.284  12.869  1.00 95.72           N
ANISOU 2271  N   VAL A 375    12164   5965  18241   1275   4505   1545       N
ATOM   2272  CA  VAL A 375       5.458  20.018  12.192  1.00 94.32           C
ANISOU 2272  CA  VAL A 375    11808   5835  18195   1217   4313   1485       C
ATOM   2273  C   VAL A 375       5.762  20.237  10.694  1.00 96.88           C
ANISOU 2273  C   VAL A 375    11865   6371  18572   1093   3864   1334       C
ATOM   2274  O   VAL A 375       5.505  21.319  10.156  1.00 97.81           O
ANISOU 2274  O   VAL A 375    11881   6557  18725   1050   3737   1288       O
ATOM   2275  CB  VAL A 375       4.343  18.948  12.394  1.00 99.99           C
ANISOU 2275  CB  VAL A 375    12314   6266  19411   1234   4603   1576       C
ATOM   2276  CG1 VAL A 375       4.131  18.625  13.870  1.00101.62           C
ANISOU 2276  CG1 VAL A 375    12823   6257  19530   1367   5058   1727       C
ATOM   2277  CG2 VAL A 375       3.032  19.346  11.716  1.00100.78           C
ANISOU 2277  CG2 VAL A 375    12042   6210  20041   1174   4643   1581       C
ATOM   2278  N   ARG A 376       6.292  19.201  10.029  1.00 91.33           N
ANISOU 2278  N   ARG A 376    11063   5761  17877   1042   3638   1260       N
ATOM   2279  CA  ARG A 376       6.576  19.221   8.595  1.00 88.81           C
ANISOU 2279  CA  ARG A 376    10515   5617  17613    933   3229   1120       C
ATOM   2280  C   ARG A 376       5.732  18.187   7.894  1.00 93.69           C
ANISOU 2280  C   ARG A 376    10801   6085  18710    878   3196   1105       C
ATOM   2281  O   ARG A 376       5.641  17.029   8.331  1.00 91.83           O
ANISOU 2281  O   ARG A 376    10562   5726  18601    908   3356   1159       O
ATOM   2282  CB  ARG A 376       8.058  19.016   8.293  1.00 83.44           C
ANISOU 2282  CB  ARG A 376    10015   5188  16500    915   2951   1029       C
ATOM   2283  CG  ARG A 376       8.857  20.199   8.729  1.00 78.32           C
ANISOU 2283  CG  ARG A 376     9636   4695  15425    951   2907   1016       C
ATOM   2284  CD  ARG A 376      10.106  20.300   7.948  1.00 75.63           C
ANISOU 2284  CD  ARG A 376     9345   4607  14784    898   2552    894       C
ATOM   2285  NE  ARG A 376      10.802  21.538   8.268  1.00 78.07           N
ANISOU 2285  NE  ARG A 376     9867   5055  14739    923   2490    873       N
ATOM   2286  CZ  ARG A 376      10.829  22.605   7.480  1.00 91.53           C
ANISOU 2286  CZ  ARG A 376    11484   6881  16410    869   2294    797       C
ATOM   2287  NH1 ARG A 376      10.238  22.577   6.288  1.00 82.90           N
ANISOU 2287  NH1 ARG A 376    10112   5792  15594    789   2121    731       N
ATOM   2288  NH2 ARG A 376      11.476  23.698   7.858  1.00 76.81           N
ANISOU 2288  NH2 ARG A 376     9822   5131  14230    897   2258    783       N
ATOM   2289  N   LEU A 377       5.076  18.631   6.816  1.00 92.86           N
ANISOU 2289  N   LEU A 377    10419   5977  18885    802   2985   1033       N
ATOM   2290  CA  LEU A 377       4.181  17.773   6.048  1.00 94.72           C
ANISOU 2290  CA  LEU A 377    10320   6056  19615    746   2907   1006       C
ATOM   2291  C   LEU A 377       4.652  17.496   4.623  1.00 96.86           C
ANISOU 2291  C   LEU A 377    10453   6491  19859    657   2467    856       C
ATOM   2292  O   LEU A 377       5.438  18.259   4.051  1.00 94.14           O
ANISOU 2292  O   LEU A 377    10220   6369  19181    628   2216    770       O
ATOM   2293  CB  LEU A 377       2.727  18.320   6.080  1.00 96.68           C
ANISOU 2293  CB  LEU A 377    10324   6065  20344    746   3078   1067       C
ATOM   2294  CG  LEU A 377       2.099  18.587   7.462  1.00102.54           C
ANISOU 2294  CG  LEU A 377    11187   6598  21175    839   3556   1225       C
ATOM   2295  CD1 LEU A 377       0.724  19.139   7.311  1.00105.90           C
ANISOU 2295  CD1 LEU A 377    11340   6799  22100    825   3677   1268       C
ATOM   2296  CD2 LEU A 377       2.050  17.334   8.324  1.00102.64           C
ANISOU 2296  CD2 LEU A 377    11270   6446  21281    899   3857   1319       C
ATOM   2297  N   ARG A 378       4.185  16.391   4.058  1.00 93.93           N
ANISOU 2297  N   ARG A 378     9851   5998  19840    617   2384    825       N
ATOM   2298  CA  ARG A 378       4.564  16.048   2.711  1.00 93.71           C
ANISOU 2298  CA  ARG A 378     9707   6095  19802    539   1979    685       C
ATOM   2299  C   ARG A 378       3.354  15.684   1.915  1.00104.56           C
ANISOU 2299  C   ARG A 378    10739   7265  21723    491   1863    651       C
ATOM   2300  O   ARG A 378       2.539  14.877   2.373  1.00107.26           O
ANISOU 2300  O   ARG A 378    10919   7374  22462    509   2082    724       O
ATOM   2301  CB  ARG A 378       5.608  14.917   2.703  1.00 90.88           C
ANISOU 2301  CB  ARG A 378     9475   5847  19208    537   1910    652       C
ATOM   2302  CG  ARG A 378       6.010  14.424   1.319  1.00 98.94           C
ANISOU 2302  CG  ARG A 378    10397   6978  20217    462   1514    510       C
ATOM   2303  CD  ARG A 378       7.242  13.560   1.365  1.00102.70           C
ANISOU 2303  CD  ARG A 378    11050   7603  20370    465   1455    480       C
ATOM   2304  NE  ARG A 378       8.450  14.378   1.517  1.00102.06           N
ANISOU 2304  NE  ARG A 378    11235   7760  19785    481   1383    454       N
ATOM   2305  CZ  ARG A 378       9.652  13.892   1.797  1.00100.96           C
ANISOU 2305  CZ  ARG A 378    11293   7759  19308    497   1370    444       C
ATOM   2306  NH1 ARG A 378       9.824  12.593   1.971  1.00 88.95           N
ANISOU 2306  NH1 ARG A 378     9748   6175  17873    502   1430    462       N
ATOM   2307  NH2 ARG A 378      10.689  14.703   1.923  1.00 80.20           N
ANISOU 2307  NH2 ARG A 378     8878   5322  16270    511   1297    418       N
ATOM   2308  N   PRO A 379       3.280  16.224   0.677  1.00103.88           N
ANISOU 2308  N   PRO A 379    10548   7261  21661    432   1500    533       N
ATOM   2309  CA  PRO A 379       2.182  15.859  -0.216  1.00107.75           C
ANISOU 2309  CA  PRO A 379    10718   7557  22665    385   1313    480       C
ATOM   2310  C   PRO A 379       2.411  14.466  -0.826  1.00118.85           C
ANISOU 2310  C   PRO A 379    12038   8936  24182    349   1136    409       C
ATOM   2311  O   PRO A 379       3.087  13.627  -0.225  1.00118.95           O
ANISOU 2311  O   PRO A 379    12185   9001  24009    372   1286    447       O
ATOM   2312  CB  PRO A 379       2.210  16.979  -1.261  1.00108.12           C
ANISOU 2312  CB  PRO A 379    10760   7724  22595    348    984    379       C
ATOM   2313  CG  PRO A 379       3.623  17.403  -1.323  1.00108.83           C
ANISOU 2313  CG  PRO A 379    11152   8108  22090    353    887    332       C
ATOM   2314  CD  PRO A 379       4.205  17.179   0.030  1.00103.48           C
ANISOU 2314  CD  PRO A 379    10676   7469  21173    411   1238    442       C
ATOM   2315  N   ASN A 380       1.798  14.199  -1.992  1.00120.32           N
ANISOU 2315  N   ASN A 380    12001   9023  24691    297    818    309       N
ATOM   2316  CA  ASN A 380       1.939  12.944  -2.736  1.00121.76           C
ANISOU 2316  CA  ASN A 380    12095   9168  25001    260    603    225       C
ATOM   2317  C   ASN A 380       2.516  13.318  -4.126  1.00128.61           C
ANISOU 2317  C   ASN A 380    13050  10209  25609    216    157     73       C
ATOM   2318  O   ASN A 380       3.505  14.071  -4.184  1.00126.46           O
ANISOU 2318  O   ASN A 380    13026  10176  24847    224    109     48       O
ATOM   2319  CB  ASN A 380       0.581  12.218  -2.821  1.00121.35           C
ANISOU 2319  CB  ASN A 380    11698   8794  25614    246    634    245       C
ATOM   2320  CG  ASN A 380      -0.040  11.860  -1.485  1.00125.59           C
ANISOU 2320  CG  ASN A 380    12151   9133  26436    294   1101    401       C
ATOM   2321  OD1 ASN A 380       0.577  12.007  -0.415  1.00112.83           O
ANISOU 2321  OD1 ASN A 380    10759   7614  24499    345   1416    498       O
ATOM   2322  ND2 ASN A 380      -1.278  11.357  -1.523  1.00110.52           N
ANISOU 2322  ND2 ASN A 380     9923   6923  25148    284   1155    426       N
ATOM   2323  N   GLU A 381       1.899  12.835  -5.231  1.00128.24           N
ANISOU 2323  N   GLU A 381    12809  10026  25889    176   -164    -29       N
ATOM   2324  CA  GLU A 381       2.328  13.190  -6.586  1.00127.55           C
ANISOU 2324  CA  GLU A 381    12819  10063  25583    145   -586   -173       C
ATOM   2325  C   GLU A 381       1.829  14.614  -6.853  1.00131.52           C
ANISOU 2325  C   GLU A 381    13309  10577  26087    151   -678   -180       C
ATOM   2326  O   GLU A 381       2.641  15.549  -6.882  1.00129.19           O
ANISOU 2326  O   GLU A 381    13242  10502  25344    164   -690   -190       O
ATOM   2327  CB  GLU A 381       1.757  12.217  -7.635  1.00130.61           C
ANISOU 2327  CB  GLU A 381    13025  10276  26323    110   -905   -279       C
ATOM   2328  CG  GLU A 381       2.336  10.817  -7.588  1.00141.38           C
ANISOU 2328  CG  GLU A 381    14413  11641  27662     99   -858   -289       C
ATOM   2329  CD  GLU A 381       2.159  10.079  -8.897  1.00161.87           C
ANISOU 2329  CD  GLU A 381    16968  14170  30364     65  -1262   -433       C
ATOM   2330  OE1 GLU A 381       1.126   9.389  -9.061  1.00151.78           O
ANISOU 2330  OE1 GLU A 381    15428  12641  29599     48  -1360   -455       O
ATOM   2331  OE2 GLU A 381       3.034  10.233  -9.779  1.00155.49           O
ANISOU 2331  OE2 GLU A 381    16394  13548  29137     58  -1484   -525       O
ATOM   2332  N   ALA A 382       0.480  14.775  -6.967  1.00129.67           N
ANISOU 2332  N   ALA A 382    12795  10094  26379    145   -719   -166       N
ATOM   2333  CA  ALA A 382      -0.200  16.051  -7.226  1.00129.39           C
ANISOU 2333  CA  ALA A 382    12698  10022  26442    151   -810   -168       C
ATOM   2334  C   ALA A 382      -0.702  16.728  -5.938  1.00130.21           C
ANISOU 2334  C   ALA A 382    12734  10053  26685    184   -395    -19       C
ATOM   2335  O   ALA A 382      -0.388  17.900  -5.708  1.00127.12           O
ANISOU 2335  O   ALA A 382    12487   9803  26010    202   -327      8       O
ATOM   2336  CB  ALA A 382      -1.349  15.842  -8.207  1.00132.56           C
ANISOU 2336  CB  ALA A 382    12841  10185  27341    125  -1156   -255       C
ATOM   2337  N   LYS A 383      -1.484  15.981  -5.116  1.00126.97           N
ANISOU 2337  N   LYS A 383    12113   9413  26717    195   -112     76       N
ATOM   2338  CA  LYS A 383      -2.060  16.409  -3.837  1.00126.82           C
ANISOU 2338  CA  LYS A 383    12024   9268  26892    235    329    228       C
ATOM   2339  C   LYS A 383      -2.722  15.197  -3.186  1.00131.56           C
ANISOU 2339  C   LYS A 383    12414   9615  27956    244    584    306       C
ATOM   2340  O   LYS A 383      -2.004  14.326  -2.695  1.00129.79           O
ANISOU 2340  O   LYS A 383    12327   9469  27519    258    744    336       O
ATOM   2341  CB  LYS A 383      -3.054  17.594  -4.002  1.00129.76           C
ANISOU 2341  CB  LYS A 383    12232   9514  27556    236    288    245       C
ATOM   2342  CG  LYS A 383      -2.733  18.802  -3.116  1.00129.22           C
ANISOU 2342  CG  LYS A 383    12352   9573  27174    277    586    342       C
ATOM   2343  CD  LYS A 383      -2.057  19.935  -3.892  1.00129.15           C
ANISOU 2343  CD  LYS A 383    12535   9809  26728    265    303    255       C
ATOM   2344  CE  LYS A 383      -0.896  20.544  -3.144  1.00124.58           C
ANISOU 2344  CE  LYS A 383    12295   9502  25539    295    497    296       C
ATOM   2345  NZ  LYS A 383      -0.074  21.418  -4.017  1.00118.96           N
ANISOU 2345  NZ  LYS A 383    11771   9031  24399    280    197    196       N
ATOM   2346  N   THR A 384      -4.081  15.123  -3.234  1.00130.82           N
ANISOU 2346  N   THR A 384    11983   9209  28513    237    607    333       N
ATOM   2347  CA  THR A 384      -4.966  14.073  -2.691  1.00132.95           C
ANISOU 2347  CA  THR A 384    11985   9173  29358    244    847    408       C
ATOM   2348  C   THR A 384      -4.913  13.966  -1.159  1.00136.21           C
ANISOU 2348  C   THR A 384    12501   9533  29720    306   1417    579       C
ATOM   2349  O   THR A 384      -5.835  14.434  -0.483  1.00137.08           O
ANISOU 2349  O   THR A 384    12460   9426  30199    336   1719    687       O
ATOM   2350  CB  THR A 384      -4.871  12.724  -3.458  1.00142.91           C
ANISOU 2350  CB  THR A 384    13138  10377  30785    205    571    306       C
ATOM   2351  OG1 THR A 384      -3.687  12.014  -3.080  1.00143.81           O
ANISOU 2351  OG1 THR A 384    13520  10706  30416    217    677    312       O
ATOM   2352  CG2 THR A 384      -4.943  12.890  -4.974  1.00140.73           C
ANISOU 2352  CG2 THR A 384    12800  10134  30538    156      3    136       C
ATOM   2353  N   ALA A 385      -3.819  13.364  -0.625  1.00130.67           N
ANISOU 2353  N   ALA A 385    12071   9023  28553    329   1559    602       N
ATOM   2354  CA  ALA A 385      -3.543  13.169   0.805  1.00129.52           C
ANISOU 2354  CA  ALA A 385    12104   8860  28246    397   2061    752       C
ATOM   2355  C   ALA A 385      -2.199  13.827   1.233  1.00127.45           C
ANISOU 2355  C   ALA A 385    12251   8933  27240    427   2103    759       C
ATOM   2356  O   ALA A 385      -1.379  14.190   0.378  1.00124.84           O
ANISOU 2356  O   ALA A 385    12055   8853  26526    389   1747    642       O
ATOM   2357  CB  ALA A 385      -3.540  11.678   1.137  1.00131.17           C
ANISOU 2357  CB  ALA A 385    12241   8939  28661    404   2208    783       C
ATOM   2358  N   TRP A 386      -2.012  14.016   2.562  1.00121.14           N
ANISOU 2358  N   TRP A 386    11652   8117  26260    500   2543    897       N
ATOM   2359  CA  TRP A 386      -0.801  14.574   3.181  1.00116.87           C
ANISOU 2359  CA  TRP A 386    11499   7845  25062    542   2633    921       C
ATOM   2360  C   TRP A 386      -0.229  13.586   4.212  1.00117.29           C
ANISOU 2360  C   TRP A 386    11749   7883  24934    602   2946   1012       C
ATOM   2361  O   TRP A 386      -0.949  12.711   4.715  1.00117.86           O
ANISOU 2361  O   TRP A 386    11673   7700  25409    629   3218   1096       O
ATOM   2362  CB  TRP A 386      -1.055  15.931   3.850  1.00115.13           C
ANISOU 2362  CB  TRP A 386    11392   7627  24725    585   2841    998       C
ATOM   2363  CG  TRP A 386      -1.220  17.083   2.917  1.00115.06           C
ANISOU 2363  CG  TRP A 386    11304   7725  24687    535   2516    904       C
ATOM   2364  CD1 TRP A 386      -2.381  17.502   2.341  1.00119.58           C
ANISOU 2364  CD1 TRP A 386    11572   8112  25753    501   2407    884       C
ATOM   2365  CD2 TRP A 386      -0.229  18.064   2.582  1.00112.52           C
ANISOU 2365  CD2 TRP A 386    11225   7701  23825    525   2303    834       C
ATOM   2366  NE1 TRP A 386      -2.176  18.678   1.657  1.00117.83           N
ANISOU 2366  NE1 TRP A 386    11399   8059  25310    472   2135    806       N
ATOM   2367  CE2 TRP A 386      -0.861  19.045   1.783  1.00116.74           C
ANISOU 2367  CE2 TRP A 386    11595   8220  24542    485   2074    775       C
ATOM   2368  CE3 TRP A 386       1.136  18.220   2.888  1.00111.41           C
ANISOU 2368  CE3 TRP A 386    11422   7829  23080    547   2284    818       C
ATOM   2369  CZ2 TRP A 386      -0.169  20.145   1.256  1.00113.83           C
ANISOU 2369  CZ2 TRP A 386    11392   8098  23760    468   1838    699       C
ATOM   2370  CZ3 TRP A 386       1.817  19.322   2.383  1.00110.77           C
ANISOU 2370  CZ3 TRP A 386    11489   7984  22614    528   2052    742       C
ATOM   2371  CH2 TRP A 386       1.172  20.255   1.558  1.00111.61           C
ANISOU 2371  CH2 TRP A 386    11431   8074  22902    488   1836    683       C
ATOM   2372  N   SER A 387       1.068  13.760   4.535  1.00109.54           N
ANISOU 2372  N   SER A 387    11103   7165  23352    626   2908    996       N
ATOM   2373  CA  SER A 387       1.808  12.896   5.442  1.00107.69           C
ANISOU 2373  CA  SER A 387    11101   6959  22857    685   3136   1065       C
ATOM   2374  C   SER A 387       2.595  13.711   6.448  1.00108.24           C
ANISOU 2374  C   SER A 387    11541   7168  22418    758   3328   1133       C
ATOM   2375  O   SER A 387       3.074  14.804   6.131  1.00105.91           O
ANISOU 2375  O   SER A 387    11359   7062  21822    741   3148   1078       O
ATOM   2376  CB  SER A 387       2.776  12.019   4.649  1.00108.60           C
ANISOU 2376  CB  SER A 387    11248   7259  22754    633   2814    952       C
ATOM   2377  OG  SER A 387       2.186  11.469   3.482  1.00117.42           O
ANISOU 2377  OG  SER A 387    12056   8297  24263    556   2531    854       O
ATOM   2378  N   LEU A 388       2.723  13.180   7.666  1.00104.07           N
ANISOU 2378  N   LEU A 388    11210   6535  21795    844   3691   1252       N
ATOM   2379  CA  LEU A 388       3.547  13.776   8.705  1.00101.84           C
ANISOU 2379  CA  LEU A 388    11318   6367  21010    927   3865   1316       C
ATOM   2380  C   LEU A 388       4.920  13.194   8.433  1.00102.15           C
ANISOU 2380  C   LEU A 388    11535   6648  20631    909   3612   1236       C
ATOM   2381  O   LEU A 388       5.073  11.976   8.360  1.00102.62           O
ANISOU 2381  O   LEU A 388    11542   6657  20791    905   3622   1236       O
ATOM   2382  CB  LEU A 388       3.066  13.384  10.117  1.00103.62           C
ANISOU 2382  CB  LEU A 388    11699   6343  21326   1038   4368   1482       C
ATOM   2383  CG  LEU A 388       4.001  13.756  11.276  1.00106.33           C
ANISOU 2383  CG  LEU A 388    12495   6782  21125   1139   4540   1549       C
ATOM   2384  CD1 LEU A 388       3.852  15.228  11.683  1.00105.27           C
ANISOU 2384  CD1 LEU A 388    12515   6679  20804   1174   4625   1579       C
ATOM   2385  CD2 LEU A 388       3.799  12.820  12.447  1.00109.26           C
ANISOU 2385  CD2 LEU A 388    13031   6930  21554   1243   4954   1686       C
ATOM   2386  N   VAL A 389       5.892  14.057   8.199  1.00 95.09           N
ANISOU 2386  N   VAL A 389    10821   6006  19304    893   3374   1161       N
ATOM   2387  CA  VAL A 389       7.269  13.644   7.915  1.00 91.66           C
ANISOU 2387  CA  VAL A 389    10554   5806  18468    875   3123   1081       C
ATOM   2388  C   VAL A 389       8.189  14.275   8.947  1.00 93.57           C
ANISOU 2388  C   VAL A 389    11175   6155  18223    957   3230   1129       C
ATOM   2389  O   VAL A 389       7.729  15.009   9.836  1.00 95.28           O
ANISOU 2389  O   VAL A 389    11532   6263  18409   1027   3499   1222       O
ATOM   2390  CB  VAL A 389       7.726  13.927   6.450  1.00 92.76           C
ANISOU 2390  CB  VAL A 389    10542   6148  18553    772   2683    925       C
ATOM   2391  CG1 VAL A 389       7.146  12.901   5.489  1.00 92.36           C
ANISOU 2391  CG1 VAL A 389    10185   6003  18903    702   2536    866       C
ATOM   2392  CG2 VAL A 389       7.396  15.364   6.005  1.00 92.19           C
ANISOU 2392  CG2 VAL A 389    10427   6143  18458    745   2570    887       C
ATOM   2393  N   GLN A 390       9.483  14.009   8.822  1.00 86.53           N
ANISOU 2393  N   GLN A 390    10452   5464  16960    949   3016   1063       N
ATOM   2394  CA  GLN A 390      10.453  14.540   9.758  1.00 85.34           C
ANISOU 2394  CA  GLN A 390    10659   5414  16354   1026   3067   1095       C
ATOM   2395  C   GLN A 390      11.790  14.865   9.092  1.00 86.15           C
ANISOU 2395  C   GLN A 390    10843   5782  16107    977   2708    976       C
ATOM   2396  O   GLN A 390      12.340  14.057   8.349  1.00 85.53           O
ANISOU 2396  O   GLN A 390    10658   5793  16045    920   2498    900       O
ATOM   2397  CB  GLN A 390      10.619  13.539  10.912  1.00 88.22           C
ANISOU 2397  CB  GLN A 390    11230   5642  16647   1121   3333   1200       C
ATOM   2398  CG  GLN A 390      11.463  14.050  12.061  1.00 99.35           C
ANISOU 2398  CG  GLN A 390    13041   7092  17614   1224   3429   1253       C
ATOM   2399  CD  GLN A 390      11.430  13.084  13.204  1.00104.78           C
ANISOU 2399  CD  GLN A 390    13939   7607  18266   1328   3719   1367       C
ATOM   2400  OE1 GLN A 390      11.790  11.920  13.076  1.00 98.00           O
ANISOU 2400  OE1 GLN A 390    13043   6751  17443   1318   3668   1356       O
ATOM   2401  NE2 GLN A 390      11.011  13.566  14.351  1.00 96.66           N
ANISOU 2401  NE2 GLN A 390    13156   6420  17148   1435   4033   1479       N
ATOM   2402  N   VAL A 391      12.307  16.052   9.362  1.00 82.52           N
ANISOU 2402  N   VAL A 391    10570   5438  15347   1001   2648    960       N
ATOM   2403  CA  VAL A 391      13.594  16.452   8.820  1.00 80.09           C
ANISOU 2403  CA  VAL A 391    10349   5362  14719    963   2337    854       C
ATOM   2404  C   VAL A 391      14.649  15.783   9.678  1.00 83.58           C
ANISOU 2404  C   VAL A 391    11053   5829  14874   1032   2361    884       C
ATOM   2405  O   VAL A 391      14.658  15.944  10.909  1.00 84.05           O
ANISOU 2405  O   VAL A 391    11372   5793  14771   1131   2576    976       O
ATOM   2406  CB  VAL A 391      13.790  17.991   8.705  1.00 82.57           C
ANISOU 2406  CB  VAL A 391    10739   5793  14840    956   2237    814       C
ATOM   2407  CG1 VAL A 391      15.262  18.382   8.608  1.00 80.69           C
ANISOU 2407  CG1 VAL A 391    10675   5757  14227    952   1993    735       C
ATOM   2408  CG2 VAL A 391      13.049  18.537   7.504  1.00 81.77           C
ANISOU 2408  CG2 VAL A 391    10358   5718  14994    869   2101    748       C
ATOM   2409  N   PRO A 392      15.524  14.986   9.043  1.00 78.65           N
ANISOU 2409  N   PRO A 392    10373   5316  14194    984   2143    809       N
ATOM   2410  CA  PRO A 392      16.583  14.340   9.814  1.00 78.12           C
ANISOU 2410  CA  PRO A 392    10543   5272  13867   1047   2136    832       C
ATOM   2411  C   PRO A 392      17.450  15.333  10.605  1.00 80.66           C
ANISOU 2411  C   PRO A 392    11162   5672  13814   1113   2087    834       C
ATOM   2412  O   PRO A 392      17.788  16.410  10.095  1.00 78.26           O
ANISOU 2412  O   PRO A 392    10836   5499  13400   1072   1915    762       O
ATOM   2413  CB  PRO A 392      17.398  13.614   8.732  1.00 78.56           C
ANISOU 2413  CB  PRO A 392    10448   5463  13939    964   1864    728       C
ATOM   2414  CG  PRO A 392      16.460  13.431   7.595  1.00 82.93           C
ANISOU 2414  CG  PRO A 392    10689   5988  14831    877   1816    684       C
ATOM   2415  CD  PRO A 392      15.607  14.641   7.606  1.00 78.82           C
ANISOU 2415  CD  PRO A 392    10131   5437  14380    877   1892    701       C
ATOM   2416  N   LYS A 393      17.789  14.961  11.861  1.00 79.07           N
ANISOU 2416  N   LYS A 393    11247   5376  13422   1220   2238    916       N
ATOM   2417  CA  LYS A 393      18.737  15.668  12.731  1.00 79.24           C
ANISOU 2417  CA  LYS A 393    11588   5444  13073   1298   2168    918       C
ATOM   2418  C   LYS A 393      20.125  15.172  12.234  1.00 81.88           C
ANISOU 2418  C   LYS A 393    11914   5929  13267   1258   1870    828       C
ATOM   2419  O   LYS A 393      21.133  15.880  12.353  1.00 80.06           O
ANISOU 2419  O   LYS A 393    11826   5804  12790   1271   1677    773       O
ATOM   2420  CB  LYS A 393      18.492  15.287  14.222  1.00 84.21           C
ANISOU 2420  CB  LYS A 393    12536   5884  13575   1435   2445   1043       C
ATOM   2421  CG  LYS A 393      19.182  16.193  15.276  1.00 95.07           C
ANISOU 2421  CG  LYS A 393    14286   7260  14577   1536   2413   1059       C
ATOM   2422  CD  LYS A 393      18.894  15.740  16.737  1.00101.25           C
ANISOU 2422  CD  LYS A 393    15418   7830  15222   1684   2701   1188       C
ATOM   2423  CE  LYS A 393      20.128  15.546  17.603  1.00108.48           C
ANISOU 2423  CE  LYS A 393    16674   8748  15797   1778   2556   1185       C
ATOM   2424  NZ  LYS A 393      20.045  14.340  18.496  1.00111.98           N
ANISOU 2424  NZ  LYS A 393    17324   9006  16216   1883   2779   1290       N
ATOM   2425  N   VAL A 394      20.134  13.950  11.635  1.00 77.69           N
ANISOU 2425  N   VAL A 394    11199   5396  12924   1207   1838    811       N
ATOM   2426  CA  VAL A 394      21.297  13.311  11.039  1.00 76.09           C
ANISOU 2426  CA  VAL A 394    10940   5312  12657   1159   1591    731       C
ATOM   2427  C   VAL A 394      21.663  14.000   9.721  1.00 77.70           C
ANISOU 2427  C   VAL A 394    10937   5684  12900   1053   1349    614       C
ATOM   2428  O   VAL A 394      20.785  14.516   9.027  1.00 77.40           O
ANISOU 2428  O   VAL A 394    10718   5653  13038    997   1379    594       O
ATOM   2429  CB  VAL A 394      21.092  11.773  10.888  1.00 80.57           C
ANISOU 2429  CB  VAL A 394    11393   5804  13418   1146   1669    761       C
ATOM   2430  CG1 VAL A 394      20.178  11.412   9.718  1.00 80.04           C
ANISOU 2430  CG1 VAL A 394    10994   5735  13682   1046   1673    723       C
ATOM   2431  CG2 VAL A 394      22.420  11.060  10.751  1.00 79.65           C
ANISOU 2431  CG2 VAL A 394    11326   5771  13167   1139   1465    710       C
ATOM   2432  N   GLN A 395      22.949  13.993   9.377  1.00 71.83           N
ANISOU 2432  N   GLN A 395    10224   5061  12006   1030   1114    537       N
ATOM   2433  CA  GLN A 395      23.431  14.559   8.126  1.00 69.65           C
ANISOU 2433  CA  GLN A 395     9777   4931  11755    937    897    428       C
ATOM   2434  C   GLN A 395      24.125  13.537   7.263  1.00 72.22           C
ANISOU 2434  C   GLN A 395     9963   5312  12165    875    755    366       C
ATOM   2435  O   GLN A 395      24.376  12.403   7.696  1.00 72.02           O
ANISOU 2435  O   GLN A 395     9984   5225  12155    906    800    405       O
ATOM   2436  CB  GLN A 395      24.337  15.775   8.360  1.00 70.21           C
ANISOU 2436  CB  GLN A 395     9991   5093  11591    958    751    383       C
ATOM   2437  CG  GLN A 395      23.579  17.046   8.708  1.00 77.43           C
ANISOU 2437  CG  GLN A 395    10971   5992  12456    983    849    410       C
ATOM   2438  CD  GLN A 395      22.665  17.568   7.628  1.00 90.27           C
ANISOU 2438  CD  GLN A 395    12369   7655  14273    904    858    373       C
ATOM   2439  OE1 GLN A 395      22.769  17.253   6.440  1.00 79.18           O
ANISOU 2439  OE1 GLN A 395    10768   6320  12997    823    734    302       O
ATOM   2440  NE2 GLN A 395      21.752  18.411   8.034  1.00 90.88           N
ANISOU 2440  NE2 GLN A 395    12484   7678  14368    932   1003    422       N
ATOM   2441  N   GLY A 396      24.403  13.949   6.031  1.00 66.72           N
ANISOU 2441  N   GLY A 396     9107   4723  11520    793    593    273       N
ATOM   2442  CA  GLY A 396      25.094  13.131   5.051  1.00 65.10           C
ANISOU 2442  CA  GLY A 396     8775   4575  11386    730    453    203       C
ATOM   2443  C   GLY A 396      25.730  13.971   3.973  1.00 62.76           C
ANISOU 2443  C   GLY A 396     8407   4397  11040    669    273    104       C
ATOM   2444  O   GLY A 396      25.535  15.182   3.928  1.00 62.42           O
ANISOU 2444  O   GLY A 396     8393   4398  10925    671    256     89       O
ATOM   2445  N   GLN A 397      26.488  13.324   3.096  1.00 54.54           N
ANISOU 2445  N   GLN A 397     7280   3401  10041    619    153     40       N
ATOM   2446  CA  GLN A 397      27.126  13.949   1.947  1.00 51.57           C
ANISOU 2446  CA  GLN A 397     6838   3119   9638    563      4    -54       C
ATOM   2447  C   GLN A 397      27.408  12.907   0.864  1.00 54.17           C
ANISOU 2447  C   GLN A 397     7048   3451  10084    505    -63   -109       C
ATOM   2448  O   GLN A 397      27.496  11.708   1.153  1.00 53.20           O
ANISOU 2448  O   GLN A 397     6913   3274  10026    513    -23    -78       O
ATOM   2449  CB  GLN A 397      28.394  14.738   2.346  1.00 51.35           C
ANISOU 2449  CB  GLN A 397     6929   3149   9434    591    -95    -79       C
ATOM   2450  CG  GLN A 397      29.609  13.913   2.737  1.00 58.01           C
ANISOU 2450  CG  GLN A 397     7827   3977  10236    613   -160    -79       C
ATOM   2451  CD  GLN A 397      30.371  13.403   1.526  1.00 74.09           C
ANISOU 2451  CD  GLN A 397     9750   6049  12350    551   -256   -154       C
ATOM   2452  OE1 GLN A 397      30.849  14.167   0.680  1.00 70.47           O
ANISOU 2452  OE1 GLN A 397     9253   5648  11872    516   -334   -221       O
ATOM   2453  NE2 GLN A 397      30.519  12.097   1.416  1.00 57.74           N
ANISOU 2453  NE2 GLN A 397     7634   3937  10368    540   -238   -142       N
ATOM   2454  N   LEU A 398      27.594  13.384  -0.366  1.00 49.32           N
ANISOU 2454  N   LEU A 398     6364   2893   9483    452   -162   -189       N
ATOM   2455  CA  LEU A 398      27.996  12.587  -1.516  1.00 48.03           C
ANISOU 2455  CA  LEU A 398     6121   2732   9396    401   -236   -253       C
ATOM   2456  C   LEU A 398      28.937  13.427  -2.372  1.00 53.63           C
ANISOU 2456  C   LEU A 398     6853   3510  10014    378   -337   -329       C
ATOM   2457  O   LEU A 398      28.649  14.589  -2.670  1.00 55.34           O
ANISOU 2457  O   LEU A 398     7083   3769  10177    374   -359   -353       O
ATOM   2458  CB  LEU A 398      26.787  12.126  -2.345  1.00 47.51           C
ANISOU 2458  CB  LEU A 398     5941   2617   9493    362   -229   -272       C
ATOM   2459  CG  LEU A 398      27.097  11.172  -3.489  1.00 49.55           C
ANISOU 2459  CG  LEU A 398     6139   2857   9830    316   -303   -336       C
ATOM   2460  CD1 LEU A 398      26.052  10.116  -3.585  1.00 49.57           C
ANISOU 2460  CD1 LEU A 398     6043   2772  10018    301   -263   -316       C
ATOM   2461  CD2 LEU A 398      27.362  11.931  -4.829  1.00 46.68           C
ANISOU 2461  CD2 LEU A 398     5785   2539   9414    282   -411   -426       C
ATOM   2462  N   ILE A 399      30.052  12.832  -2.763  1.00 49.77           N
ANISOU 2462  N   ILE A 399     6366   3024   9519    364   -384   -364       N
ATOM   2463  CA  ILE A 399      31.018  13.451  -3.650  1.00 48.87           C
ANISOU 2463  CA  ILE A 399     6268   2950   9352    343   -452   -433       C
ATOM   2464  C   ILE A 399      31.411  12.392  -4.659  1.00 50.58           C
ANISOU 2464  C   ILE A 399     6441   3130   9646    307   -473   -479       C
ATOM   2465  O   ILE A 399      31.773  11.306  -4.254  1.00 51.48           O
ANISOU 2465  O   ILE A 399     6540   3208   9814    311   -453   -452       O
ATOM   2466  CB  ILE A 399      32.214  14.142  -2.923  1.00 51.96           C
ANISOU 2466  CB  ILE A 399     6724   3368   9651    376   -483   -426       C
ATOM   2467  CG1 ILE A 399      33.144  14.894  -3.912  1.00 52.00           C
ANISOU 2467  CG1 ILE A 399     6729   3398   9631    354   -530   -498       C
ATOM   2468  CG2 ILE A 399      33.023  13.188  -2.000  1.00 51.13           C
ANISOU 2468  CG2 ILE A 399     6641   3222   9563    405   -486   -386       C
ATOM   2469  CD1 ILE A 399      32.542  16.035  -4.650  1.00 57.14           C
ANISOU 2469  CD1 ILE A 399     7389   4088  10233    341   -536   -534       C
ATOM   2470  N   ALA A 400      31.221  12.677  -5.963  1.00 45.98           N
ANISOU 2470  N   ALA A 400     5854   2549   9068    275   -509   -545       N
ATOM   2471  CA  ALA A 400      31.557  11.818  -7.098  1.00 44.75           C
ANISOU 2471  CA  ALA A 400     5690   2350   8963    244   -530   -599       C
ATOM   2472  C   ALA A 400      32.522  12.563  -8.022  1.00 49.24           C
ANISOU 2472  C   ALA A 400     6317   2929   9461    239   -544   -659       C
ATOM   2473  O   ALA A 400      32.301  13.737  -8.390  1.00 47.92           O
ANISOU 2473  O   ALA A 400     6187   2796   9223    244   -562   -683       O
ATOM   2474  CB  ALA A 400      30.309  11.410  -7.853  1.00 45.73           C
ANISOU 2474  CB  ALA A 400     5782   2435   9158    221   -563   -624       C
ATOM   2475  N   ILE A 401      33.662  11.916  -8.319  1.00 45.93           N
ANISOU 2475  N   ILE A 401     5905   2474   9072    233   -522   -676       N
ATOM   2476  CA  ILE A 401      34.712  12.526  -9.142  1.00 45.15           C
ANISOU 2476  CA  ILE A 401     5858   2360   8937    233   -502   -725       C
ATOM   2477  C   ILE A 401      35.197  11.581 -10.225  1.00 49.44           C
ANISOU 2477  C   ILE A 401     6430   2829   9524    214   -473   -769       C
ATOM   2478  O   ILE A 401      35.179  10.372 -10.009  1.00 49.69           O
ANISOU 2478  O   ILE A 401     6422   2829   9629    202   -468   -751       O
ATOM   2479  CB  ILE A 401      35.889  13.054  -8.273  1.00 47.01           C
ANISOU 2479  CB  ILE A 401     6073   2610   9178    255   -490   -700       C
ATOM   2480  CG1 ILE A 401      36.767  11.914  -7.719  1.00 47.01           C
ANISOU 2480  CG1 ILE A 401     6026   2565   9271    256   -478   -671       C
ATOM   2481  CG2 ILE A 401      35.403  13.980  -7.173  1.00 47.13           C
ANISOU 2481  CG2 ILE A 401     6085   2689   9132    279   -521   -659       C
ATOM   2482  CD1 ILE A 401      38.220  12.295  -7.488  1.00 44.32           C
ANISOU 2482  CD1 ILE A 401     5666   2191   8982    270   -472   -677       C
ATOM   2483  N   ASN A 402      35.656  12.116 -11.377  1.00 46.52           N
ANISOU 2483  N   ASN A 402     6144   2424   9108    215   -442   -824       N
ATOM   2484  CA  ASN A 402      36.214  11.249 -12.418  1.00 48.36           C
ANISOU 2484  CA  ASN A 402     6433   2570   9371    205   -393   -864       C
ATOM   2485  C   ASN A 402      37.669  10.896 -12.035  1.00 52.69           C
ANISOU 2485  C   ASN A 402     6931   3077  10011    208   -319   -844       C
ATOM   2486  O   ASN A 402      38.487  11.806 -11.905  1.00 52.16           O
ANISOU 2486  O   ASN A 402     6859   3009   9949    223   -282   -845       O
ATOM   2487  CB  ASN A 402      36.102  11.882 -13.816  1.00 52.02           C
ANISOU 2487  CB  ASN A 402     7036   2989   9740    215   -375   -927       C
ATOM   2488  CG  ASN A 402      36.771  11.057 -14.878  1.00 86.73           C
ANISOU 2488  CG  ASN A 402    11524   7279  14152    214   -303   -967       C
ATOM   2489  OD1 ASN A 402      37.912  11.298 -15.263  1.00 82.08           O
ANISOU 2489  OD1 ASN A 402    10971   6631  13585    226   -195   -976       O
ATOM   2490  ND2 ASN A 402      36.136   9.978 -15.265  1.00 89.45           N
ANISOU 2490  ND2 ASN A 402    11894   7584  14508    199   -352   -987       N
ATOM   2491  N   PRO A 403      38.012   9.606 -11.806  1.00 50.28           N
ANISOU 2491  N   PRO A 403     6577   2730   9798    195   -303   -826       N
ATOM   2492  CA  PRO A 403      39.387   9.271 -11.358  1.00 50.17           C
ANISOU 2492  CA  PRO A 403     6498   2668   9896    199   -249   -803       C
ATOM   2493  C   PRO A 403      40.572   9.565 -12.293  1.00 54.99           C
ANISOU 2493  C   PRO A 403     7155   3186  10554    205   -140   -839       C
ATOM   2494  O   PRO A 403      41.718   9.548 -11.839  1.00 56.32           O
ANISOU 2494  O   PRO A 403     7248   3309  10841    212   -106   -820       O
ATOM   2495  CB  PRO A 403      39.293   7.784 -11.008  1.00 52.87           C
ANISOU 2495  CB  PRO A 403     6789   2982  10315    184   -256   -778       C
ATOM   2496  CG  PRO A 403      38.110   7.266 -11.770  1.00 57.15           C
ANISOU 2496  CG  PRO A 403     7393   3523  10798    168   -283   -809       C
ATOM   2497  CD  PRO A 403      37.149   8.408 -11.843  1.00 52.79           C
ANISOU 2497  CD  PRO A 403     6880   3038  10141    176   -341   -821       C
ATOM   2498  N   ASN A 404      40.321   9.834 -13.583  1.00 52.10           N
ANISOU 2498  N   ASN A 404     6916   2774  10106    208    -85   -890       N
ATOM   2499  CA  ASN A 404      41.389  10.096 -14.546  1.00 52.38           C
ANISOU 2499  CA  ASN A 404     7022   2700  10181    221     53   -921       C
ATOM   2500  C   ASN A 404      41.909  11.522 -14.510  1.00 57.53           C
ANISOU 2500  C   ASN A 404     7672   3358  10828    243     92   -925       C
ATOM   2501  O   ASN A 404      43.090  11.730 -14.788  1.00 58.44           O
ANISOU 2501  O   ASN A 404     7770   3379  11058    253    208   -927       O
ATOM   2502  CB  ASN A 404      40.958   9.729 -15.964  1.00 52.70           C
ANISOU 2502  CB  ASN A 404     7237   2665  10120    227    105   -973       C
ATOM   2503  CG  ASN A 404      42.118   9.481 -16.902  1.00 76.56           C
ANISOU 2503  CG  ASN A 404    10340   5542  13209    242    280   -994       C
ATOM   2504  OD1 ASN A 404      42.841   8.492 -16.790  1.00 76.06           O
ANISOU 2504  OD1 ASN A 404    10213   5410  13275    230    344   -977       O
ATOM   2505  ND2 ASN A 404      42.319  10.369 -17.849  1.00 72.38           N
ANISOU 2505  ND2 ASN A 404     9957   4950  12596    272    374  -1027       N
ATOM   2506  N   ASP A 405      41.050  12.502 -14.174  1.00 53.56           N
ANISOU 2506  N   ASP A 405     7183   2954  10211    249      4   -925       N
ATOM   2507  CA  ASP A 405      41.415  13.933 -14.157  1.00 52.90           C
ANISOU 2507  CA  ASP A 405     7107   2885  10109    269     34   -932       C
ATOM   2508  C   ASP A 405      41.101  14.671 -12.853  1.00 55.78           C
ANISOU 2508  C   ASP A 405     7369   3359  10466    270    -79   -897       C
ATOM   2509  O   ASP A 405      41.660  15.761 -12.608  1.00 54.99           O
ANISOU 2509  O   ASP A 405     7240   3260  10394    285    -60   -898       O
ATOM   2510  CB  ASP A 405      40.748  14.657 -15.336  1.00 54.99           C
ANISOU 2510  CB  ASP A 405     7538   3138  10216    287     67   -976       C
ATOM   2511  CG  ASP A 405      39.265  14.335 -15.524  1.00 74.94           C
ANISOU 2511  CG  ASP A 405    10128   5733  12614    277    -54   -989       C
ATOM   2512  OD1 ASP A 405      38.551  14.162 -14.505  1.00 74.01           O
ANISOU 2512  OD1 ASP A 405     9908   5709  12505    261   -164   -955       O
ATOM   2513  OD2 ASP A 405      38.811  14.294 -16.684  1.00 89.38           O
ANISOU 2513  OD2 ASP A 405    12113   7509  14338    291    -40  -1033       O
ATOM   2514  N   GLY A 406      40.198  14.087 -12.055  1.00 51.13           N
ANISOU 2514  N   GLY A 406     6736   2850   9843    258   -185   -866       N
ATOM   2515  CA  GLY A 406      39.737  14.651 -10.793  1.00 50.48           C
ANISOU 2515  CA  GLY A 406     6589   2861   9731    265   -283   -828       C
ATOM   2516  C   GLY A 406      38.501  15.531 -10.920  1.00 53.31           C
ANISOU 2516  C   GLY A 406     7004   3300   9952    269   -330   -836       C
ATOM   2517  O   GLY A 406      38.145  16.210  -9.965  1.00 51.95           O
ANISOU 2517  O   GLY A 406     6797   3196   9745    279   -389   -807       O
ATOM   2518  N   SER A 407      37.814  15.504 -12.076  1.00 49.80           N
ANISOU 2518  N   SER A 407     6655   2836   9430    264   -312   -875       N
ATOM   2519  CA  SER A 407      36.610  16.288 -12.334  1.00 49.39           C
ANISOU 2519  CA  SER A 407     6658   2843   9266    268   -368   -888       C
ATOM   2520  C   SER A 407      35.511  15.994 -11.347  1.00 54.04           C
ANISOU 2520  C   SER A 407     7177   3500   9853    259   -452   -845       C
ATOM   2521  O   SER A 407      35.193  14.836 -11.127  1.00 55.89           O
ANISOU 2521  O   SER A 407     7376   3718  10144    245   -471   -829       O
ATOM   2522  CB  SER A 407      36.087  15.993 -13.731  1.00 54.40           C
ANISOU 2522  CB  SER A 407     7415   3419   9835    267   -363   -939       C
ATOM   2523  OG  SER A 407      37.018  16.400 -14.717  1.00 63.41           O
ANISOU 2523  OG  SER A 407     8654   4483  10957    285   -260   -976       O
ATOM   2524  N   ILE A 408      34.905  17.027 -10.778  1.00 50.88           N
ANISOU 2524  N   ILE A 408     6765   3169   9397    270   -488   -826       N
ATOM   2525  CA  ILE A 408      33.793  16.847  -9.851  1.00 51.43           C
ANISOU 2525  CA  ILE A 408     6780   3288   9471    268   -539   -780       C
ATOM   2526  C   ILE A 408      32.484  16.746 -10.639  1.00 56.51           C
ANISOU 2526  C   ILE A 408     7453   3922  10098    256   -589   -806       C
ATOM   2527  O   ILE A 408      32.025  17.751 -11.192  1.00 55.55           O
ANISOU 2527  O   ILE A 408     7382   3818   9908    264   -612   -832       O
ATOM   2528  CB  ILE A 408      33.760  17.905  -8.707  1.00 54.14           C
ANISOU 2528  CB  ILE A 408     7099   3696   9775    289   -547   -740       C
ATOM   2529  CG1 ILE A 408      35.007  17.764  -7.802  1.00 55.87           C
ANISOU 2529  CG1 ILE A 408     7287   3905  10035    304   -536   -716       C
ATOM   2530  CG2 ILE A 408      32.474  17.805  -7.865  1.00 53.59           C
ANISOU 2530  CG2 ILE A 408     6994   3659   9708    293   -570   -690       C
ATOM   2531  CD1 ILE A 408      35.432  19.132  -7.135  1.00 64.12           C
ANISOU 2531  CD1 ILE A 408     8343   4990  11031    328   -549   -710       C
ATOM   2532  N   GLU A 409      31.870  15.534 -10.644  1.00 52.88           N
ANISOU 2532  N   GLU A 409     6954   3424   9712    240   -615   -798       N
ATOM   2533  CA  GLU A 409      30.607  15.225 -11.339  1.00 52.07           C
ANISOU 2533  CA  GLU A 409     6859   3288   9638    228   -687   -824       C
ATOM   2534  C   GLU A 409      29.339  15.478 -10.523  1.00 51.09           C
ANISOU 2534  C   GLU A 409     6653   3191   9569    228   -714   -778       C
ATOM   2535  O   GLU A 409      28.283  15.724 -11.101  1.00 51.03           O
ANISOU 2535  O   GLU A 409     6647   3159   9584    224   -785   -803       O
ATOM   2536  CB  GLU A 409      30.596  13.747 -11.795  1.00 54.36           C
ANISOU 2536  CB  GLU A 409     7139   3507  10009    209   -702   -842       C
ATOM   2537  CG  GLU A 409      31.830  13.311 -12.575  1.00 64.44           C
ANISOU 2537  CG  GLU A 409     8492   4737  11253    208   -653   -881       C
ATOM   2538  CD  GLU A 409      31.625  12.608 -13.896  1.00 89.94           C
ANISOU 2538  CD  GLU A 409    11820   7880  14471    202   -696   -946       C
ATOM   2539  OE1 GLU A 409      30.462  12.314 -14.268  1.00 75.99           O
ANISOU 2539  OE1 GLU A 409    10052   6082  12739    195   -795   -969       O
ATOM   2540  OE2 GLU A 409      32.653  12.366 -14.571  1.00 88.99           O
ANISOU 2540  OE2 GLU A 409    11785   7712  14316    209   -631   -976       O
ATOM   2541  N   ALA A 410      29.402  15.275  -9.215  1.00 45.27           N
ANISOU 2541  N   ALA A 410     5851   2483   8868    237   -659   -710       N
ATOM   2542  CA  ALA A 410      28.255  15.425  -8.313  1.00 46.46           C
ANISOU 2542  CA  ALA A 410     5932   2640   9080    245   -645   -654       C
ATOM   2543  C   ALA A 410      28.777  15.760  -6.937  1.00 53.02           C
ANISOU 2543  C   ALA A 410     6766   3515   9865    272   -574   -589       C
ATOM   2544  O   ALA A 410      29.829  15.256  -6.512  1.00 51.90           O
ANISOU 2544  O   ALA A 410     6641   3375   9705    280   -549   -577       O
ATOM   2545  CB  ALA A 410      27.389  14.154  -8.258  1.00 47.58           C
ANISOU 2545  CB  ALA A 410     5995   2712   9371    229   -652   -636       C
ATOM   2546  N   ILE A 411      28.043  16.653  -6.257  1.00 50.57           N
ANISOU 2546  N   ILE A 411     6449   3231   9536    291   -548   -550       N
ATOM   2547  CA  ILE A 411      28.366  17.156  -4.931  1.00 49.39           C
ANISOU 2547  CA  ILE A 411     6333   3112   9319    326   -489   -490       C
ATOM   2548  C   ILE A 411      27.080  17.497  -4.182  1.00 54.12           C
ANISOU 2548  C   ILE A 411     6904   3693   9967    343   -430   -431       C
ATOM   2549  O   ILE A 411      26.263  18.252  -4.692  1.00 53.81           O
ANISOU 2549  O   ILE A 411     6839   3658   9947    333   -452   -449       O
ATOM   2550  CB  ILE A 411      29.396  18.326  -5.029  1.00 50.62           C
ANISOU 2550  CB  ILE A 411     6554   3327   9352    338   -516   -522       C
ATOM   2551  CG1 ILE A 411      29.969  18.704  -3.654  1.00 50.52           C
ANISOU 2551  CG1 ILE A 411     6594   3332   9268    378   -486   -471       C
ATOM   2552  CG2 ILE A 411      28.879  19.530  -5.846  1.00 49.67           C
ANISOU 2552  CG2 ILE A 411     6445   3238   9189    328   -546   -562       C
ATOM   2553  CD1 ILE A 411      31.167  19.516  -3.710  1.00 43.36           C
ANISOU 2553  CD1 ILE A 411     5730   2458   8286    387   -526   -506       C
ATOM   2554  N   VAL A 412      26.866  16.863  -3.024  1.00 52.13           N
ANISOU 2554  N   VAL A 412     6658   3404   9747    372   -348   -359       N
ATOM   2555  CA  VAL A 412      25.728  17.080  -2.113  1.00 52.80           C
ANISOU 2555  CA  VAL A 412     6731   3445   9884    400   -248   -287       C
ATOM   2556  C   VAL A 412      26.353  17.225  -0.700  1.00 58.86           C
ANISOU 2556  C   VAL A 412     7616   4217  10532    456   -182   -225       C
ATOM   2557  O   VAL A 412      26.998  16.271  -0.233  1.00 59.23           O
ANISOU 2557  O   VAL A 412     7694   4238  10573    472   -173   -204       O
ATOM   2558  CB  VAL A 412      24.671  15.945  -2.188  1.00 56.05           C
ANISOU 2558  CB  VAL A 412     7042   3766  10489    386   -196   -258       C
ATOM   2559  CG1 VAL A 412      23.524  16.213  -1.223  1.00 56.63           C
ANISOU 2559  CG1 VAL A 412     7103   3775  10638    419    -61   -176       C
ATOM   2560  CG2 VAL A 412      24.140  15.805  -3.610  1.00 55.60           C
ANISOU 2560  CG2 VAL A 412     6891   3694  10542    336   -300   -330       C
ATOM   2561  N   GLY A 413      26.242  18.433  -0.109  1.00 53.28           N
ANISOU 2561  N   GLY A 413     6983   3539   9723    487   -155   -204       N
ATOM   2562  CA  GLY A 413      26.860  18.799   1.169  1.00 52.58           C
ANISOU 2562  CA  GLY A 413     7036   3450   9493    546   -123   -158       C
ATOM   2563  C   GLY A 413      26.083  18.579   2.457  1.00 57.49           C
ANISOU 2563  C   GLY A 413     7740   3992  10112    605     23    -63       C
ATOM   2564  O   GLY A 413      26.592  18.859   3.538  1.00 56.93           O
ANISOU 2564  O   GLY A 413     7820   3907   9903    664     40    -27       O
ATOM   2565  N   GLY A 414      24.860  18.094   2.350  1.00 54.89           N
ANISOU 2565  N   GLY A 414     7321   3595   9939    593    128    -24       N
ATOM   2566  CA  GLY A 414      23.995  17.825   3.490  1.00 55.97           C
ANISOU 2566  CA  GLY A 414     7524   3631  10110    650    306     73       C
ATOM   2567  C   GLY A 414      22.628  17.368   3.025  1.00 59.24           C
ANISOU 2567  C   GLY A 414     7779   3968  10763    618    399     95       C
ATOM   2568  O   GLY A 414      22.414  17.183   1.818  1.00 58.22           O
ANISOU 2568  O   GLY A 414     7501   3866  10755    555    296     30       O
ATOM   2569  N   TYR A 415      21.680  17.208   3.965  1.00 56.29           N
ANISOU 2569  N   TYR A 415     7441   3482  10466    667    593    187       N
ATOM   2570  CA  TYR A 415      20.318  16.787   3.638  1.00 58.59           C
ANISOU 2570  CA  TYR A 415     7565   3669  11028    642    697    217       C
ATOM   2571  C   TYR A 415      19.661  17.718   2.614  1.00 64.65           C
ANISOU 2571  C   TYR A 415     8195   4474  11897    589    607    161       C
ATOM   2572  O   TYR A 415      19.003  17.246   1.682  1.00 64.58           O
ANISOU 2572  O   TYR A 415     8009   4425  12102    537    547    124       O
ATOM   2573  CB  TYR A 415      19.465  16.706   4.908  1.00 62.01           C
ANISOU 2573  CB  TYR A 415     8082   3964  11515    714    950    332       C
ATOM   2574  CG  TYR A 415      17.993  16.479   4.647  1.00 66.48           C
ANISOU 2574  CG  TYR A 415     8463   4402  12396    693   1076    370       C
ATOM   2575  CD1 TYR A 415      17.507  15.213   4.320  1.00 69.56           C
ANISOU 2575  CD1 TYR A 415     8705   4700  13024    668   1109    378       C
ATOM   2576  CD2 TYR A 415      17.078  17.512   4.783  1.00 67.74           C
ANISOU 2576  CD2 TYR A 415     8591   4516  12632    702   1171    400       C
ATOM   2577  CE1 TYR A 415      16.146  14.993   4.102  1.00 71.55           C
ANISOU 2577  CE1 TYR A 415     8769   4812  13603    650   1218    411       C
ATOM   2578  CE2 TYR A 415      15.717  17.304   4.568  1.00 70.01           C
ANISOU 2578  CE2 TYR A 415     8690   4663  13246    684   1286    437       C
ATOM   2579  CZ  TYR A 415      15.254  16.042   4.227  1.00 75.14           C
ANISOU 2579  CZ  TYR A 415     9184   5216  14149    658   1305    441       C
ATOM   2580  OH  TYR A 415      13.917  15.828   4.001  1.00 73.10           O
ANISOU 2580  OH  TYR A 415     8722   4803  14248    640   1405    473       O
ATOM   2581  N   ASN A 416      19.820  19.041   2.819  1.00 61.07           N
ANISOU 2581  N   ASN A 416     7829   4084  11291    605    593    154       N
ATOM   2582  CA  ASN A 416      19.275  20.066   1.959  1.00 60.22           C
ANISOU 2582  CA  ASN A 416     7621   4014  11244    565    513    106       C
ATOM   2583  C   ASN A 416      19.976  21.385   2.225  1.00 67.89           C
ANISOU 2583  C   ASN A 416     8731   5088  11976    586    468     86       C
ATOM   2584  O   ASN A 416      20.235  21.738   3.373  1.00 69.47           O
ANISOU 2584  O   ASN A 416     9092   5271  12032    647    577    143       O
ATOM   2585  CB  ASN A 416      17.791  20.205   2.180  1.00 58.14           C
ANISOU 2585  CB  ASN A 416     7249   3624  11220    572    663    168       C
ATOM   2586  CG  ASN A 416      17.115  20.993   1.091  1.00 66.16           C
ANISOU 2586  CG  ASN A 416     8122   4658  12357    523    546    111       C
ATOM   2587  OD1 ASN A 416      17.087  22.237   1.115  1.00 57.65           O
ANISOU 2587  OD1 ASN A 416     7095   3636  11174    530    535    103       O
ATOM   2588  ND2 ASN A 416      16.531  20.300   0.120  1.00 52.59           N
ANISOU 2588  ND2 ASN A 416     6231   2885  10867    475    448     68       N
ATOM   2589  N   PHE A 417      20.281  22.109   1.150  1.00 64.71           N
ANISOU 2589  N   PHE A 417     8276   4780  11532    541    307      2       N
ATOM   2590  CA  PHE A 417      20.927  23.408   1.132  1.00 64.96           C
ANISOU 2590  CA  PHE A 417     8402   4909  11369    549    243    -33       C
ATOM   2591  C   PHE A 417      20.174  24.516   1.913  1.00 73.47           C
ANISOU 2591  C   PHE A 417     9535   5953  12428    586    375     26       C
ATOM   2592  O   PHE A 417      20.800  25.449   2.431  1.00 71.61           O
ANISOU 2592  O   PHE A 417     9432   5775  12001    617    370     24       O
ATOM   2593  CB  PHE A 417      21.157  23.826  -0.337  1.00 66.48           C
ANISOU 2593  CB  PHE A 417     8508   5181  11571    492     68   -129       C
ATOM   2594  CG  PHE A 417      21.947  25.095  -0.468  1.00 67.79           C
ANISOU 2594  CG  PHE A 417     8762   5446  11550    497      1   -171       C
ATOM   2595  CD1 PHE A 417      23.320  25.104  -0.230  1.00 70.38           C
ANISOU 2595  CD1 PHE A 417     9194   5838  11711    511    -59   -201       C
ATOM   2596  CD2 PHE A 417      21.315  26.297  -0.751  1.00 69.32           C
ANISOU 2596  CD2 PHE A 417     8931   5657  11751    493      4   -177       C
ATOM   2597  CE1 PHE A 417      24.042  26.288  -0.289  1.00 69.65           C
ANISOU 2597  CE1 PHE A 417     9171   5821  11473    518   -114   -238       C
ATOM   2598  CE2 PHE A 417      22.043  27.484  -0.812  1.00 71.05           C
ANISOU 2598  CE2 PHE A 417     9231   5961  11803    500    -45   -213       C
ATOM   2599  CZ  PHE A 417      23.400  27.469  -0.585  1.00 68.08           C
ANISOU 2599  CZ  PHE A 417     8951   5644  11274    512   -103   -244       C
ATOM   2600  N   TYR A 418      18.851  24.456   1.935  1.00 74.56           N
ANISOU 2600  N   TYR A 418     9563   5991  12775    583    484     74       N
ATOM   2601  CA  TYR A 418      18.065  25.434   2.657  1.00 76.76           C
ANISOU 2601  CA  TYR A 418     9883   6216  13066    619    634    137       C
ATOM   2602  C   TYR A 418      18.120  25.172   4.159  1.00 83.01           C
ANISOU 2602  C   TYR A 418    10849   6928  13764    694    829    230       C
ATOM   2603  O   TYR A 418      18.102  26.117   4.940  1.00 84.50           O
ANISOU 2603  O   TYR A 418    11176   7112  13820    740    921    267       O
ATOM   2604  CB  TYR A 418      16.626  25.484   2.124  1.00 80.70           C
ANISOU 2604  CB  TYR A 418    10188   6616  13856    590    681    156       C
ATOM   2605  CG  TYR A 418      16.547  25.752   0.634  1.00 84.68           C
ANISOU 2605  CG  TYR A 418    10556   7187  14432    526    468     62       C
ATOM   2606  CD1 TYR A 418      17.145  26.879   0.073  1.00 86.14           C
ANISOU 2606  CD1 TYR A 418    10801   7495  14433    513    342     -2       C
ATOM   2607  CD2 TYR A 418      15.868  24.884  -0.215  1.00 87.02           C
ANISOU 2607  CD2 TYR A 418    10675   7408  14979    485    392     35       C
ATOM   2608  CE1 TYR A 418      17.092  27.120  -1.300  1.00 88.03           C
ANISOU 2608  CE1 TYR A 418    10948   7782  14717    466    156    -86       C
ATOM   2609  CE2 TYR A 418      15.796  25.120  -1.588  1.00 88.24           C
ANISOU 2609  CE2 TYR A 418    10740   7608  15178    438    183    -54       C
ATOM   2610  CZ  TYR A 418      16.415  26.237  -2.127  1.00 97.42           C
ANISOU 2610  CZ  TYR A 418    11986   8893  16135    431     72   -112       C
ATOM   2611  OH  TYR A 418      16.340  26.473  -3.482  1.00101.91           O
ANISOU 2611  OH  TYR A 418    12499   9494  16730    394   -122   -197       O
ATOM   2612  N   GLN A 419      18.245  23.908   4.568  1.00 80.21           N
ANISOU 2612  N   GLN A 419    10511   6509  13458    712    887    265       N
ATOM   2613  CA  GLN A 419      18.319  23.528   5.978  1.00 81.12           C
ANISOU 2613  CA  GLN A 419    10818   6534  13472    793   1070    354       C
ATOM   2614  C   GLN A 419      19.653  24.013   6.522  1.00 88.88           C
ANISOU 2614  C   GLN A 419    12010   7614  14147    828    961    321       C
ATOM   2615  O   GLN A 419      19.686  24.663   7.564  1.00 90.14           O
ANISOU 2615  O   GLN A 419    12352   7746  14151    890   1053    364       O
ATOM   2616  CB  GLN A 419      18.128  22.012   6.114  1.00 82.18           C
ANISOU 2616  CB  GLN A 419    10897   6579  13750    796   1137    389       C
ATOM   2617  CG  GLN A 419      18.553  21.399   7.437  1.00 92.23           C
ANISOU 2617  CG  GLN A 419    12392   7768  14882    883   1286    469       C
ATOM   2618  CD  GLN A 419      19.120  20.022   7.203  1.00105.74           C
ANISOU 2618  CD  GLN A 419    14070   9485  16623    868   1213    451       C
ATOM   2619  OE1 GLN A 419      20.019  19.813   6.364  1.00 95.09           O
ANISOU 2619  OE1 GLN A 419    12659   8255  15217    816    997    364       O
ATOM   2620  NE2 GLN A 419      18.627  19.052   7.969  1.00102.95           N
ANISOU 2620  NE2 GLN A 419    13768   8992  16357    920   1407    538       N
ATOM   2621  N   SER A 420      20.728  23.780   5.758  1.00 85.57           N
ANISOU 2621  N   SER A 420    11553   7303  13654    787    754    238       N
ATOM   2622  CA  SER A 420      22.086  24.185   6.091  1.00 84.44           C
ANISOU 2622  CA  SER A 420    11567   7247  13270    810    617    194       C
ATOM   2623  C   SER A 420      22.865  24.473   4.785  1.00 84.81           C
ANISOU 2623  C   SER A 420    11487   7421  13314    738    405     87       C
ATOM   2624  O   SER A 420      22.939  23.594   3.907  1.00 86.26           O
ANISOU 2624  O   SER A 420    11536   7621  13617    688    333     48       O
ATOM   2625  CB  SER A 420      22.768  23.081   6.911  1.00 89.08           C
ANISOU 2625  CB  SER A 420    12292   7784  13770    862    628    228       C
ATOM   2626  OG  SER A 420      22.791  21.834   6.227  1.00 97.54           O
ANISOU 2626  OG  SER A 420    13221   8851  14991    817    589    210       O
ATOM   2627  N   LYS A 421      23.431  25.686   4.652  1.00 76.31           N
ANISOU 2627  N   LYS A 421    10465   6424  12104    736    317     40       N
ATOM   2628  CA  LYS A 421      24.223  26.044   3.468  1.00 74.49           C
ANISOU 2628  CA  LYS A 421    10141   6300  11861    679    142    -56       C
ATOM   2629  C   LYS A 421      25.644  25.457   3.532  1.00 75.48           C
ANISOU 2629  C   LYS A 421    10323   6458  11900    684     18    -97       C
ATOM   2630  O   LYS A 421      26.438  25.643   2.606  1.00 76.14           O
ANISOU 2630  O   LYS A 421    10337   6610  11984    641   -108   -172       O
ATOM   2631  CB  LYS A 421      24.239  27.577   3.222  1.00 78.58           C
ANISOU 2631  CB  LYS A 421    10677   6881  12297    673    108    -89       C
ATOM   2632  CG  LYS A 421      24.594  28.438   4.445  1.00108.41           C
ANISOU 2632  CG  LYS A 421    14646  10643  15900    739    147    -56       C
ATOM   2633  CD  LYS A 421      26.062  28.883   4.487  1.00124.85           C
ANISOU 2633  CD  LYS A 421    16806  12786  17845    747    -11   -121       C
ATOM   2634  CE  LYS A 421      26.440  29.524   5.814  1.00140.53           C
ANISOU 2634  CE  LYS A 421    19004  14732  19658    822      2    -90       C
ATOM   2635  NZ  LYS A 421      27.208  28.585   6.687  1.00147.49           N
ANISOU 2635  NZ  LYS A 421    20017  15556  20466    873    -45    -71       N
ATOM   2636  N   PHE A 422      25.948  24.745   4.634  1.00 68.51           N
ANISOU 2636  N   PHE A 422     9571   5510  10951    741     61    -44       N
ATOM   2637  CA  PHE A 422      27.211  24.093   4.920  1.00 66.24           C
ANISOU 2637  CA  PHE A 422     9350   5225  10595    758    -50    -68       C
ATOM   2638  C   PHE A 422      27.417  22.904   3.998  1.00 67.88           C
ANISOU 2638  C   PHE A 422     9413   5442  10937    705    -93    -98       C
ATOM   2639  O   PHE A 422      26.502  22.097   3.814  1.00 68.44           O
ANISOU 2639  O   PHE A 422     9405   5466  11132    690      3    -61       O
ATOM   2640  CB  PHE A 422      27.247  23.657   6.389  1.00 68.53           C
ANISOU 2640  CB  PHE A 422     9839   5423  10777    843     23      7       C
ATOM   2641  CG  PHE A 422      28.602  23.232   6.861  1.00 70.31           C
ANISOU 2641  CG  PHE A 422    10163   5640  10911    876   -120    -18       C
ATOM   2642  CD1 PHE A 422      29.610  24.169   7.067  1.00 72.95           C
ANISOU 2642  CD1 PHE A 422    10575   6008  11135    893   -264    -70       C
ATOM   2643  CD2 PHE A 422      28.873  21.898   7.123  1.00 72.81           C
ANISOU 2643  CD2 PHE A 422    10491   5905  11269    890   -116      9       C
ATOM   2644  CE1 PHE A 422      30.866  23.776   7.513  1.00 74.20           C
ANISOU 2644  CE1 PHE A 422    10811   6140  11241    924   -414    -96       C
ATOM   2645  CE2 PHE A 422      30.130  21.502   7.570  1.00 75.43           C
ANISOU 2645  CE2 PHE A 422    10910   6219  11532    922   -260    -14       C
ATOM   2646  CZ  PHE A 422      31.118  22.440   7.765  1.00 73.76           C
ANISOU 2646  CZ  PHE A 422    10767   6033  11226    939   -414    -67       C
ATOM   2647  N   ASN A 423      28.596  22.832   3.368  1.00 61.23           N
ANISOU 2647  N   ASN A 423     8530   4650  10086    676   -232   -167       N
ATOM   2648  CA  ASN A 423      28.919  21.759   2.444  1.00 59.51           C
ANISOU 2648  CA  ASN A 423     8191   4439   9983    627   -276   -202       C
ATOM   2649  C   ASN A 423      29.880  20.819   3.105  1.00 62.88           C
ANISOU 2649  C   ASN A 423     8685   4824  10381    659   -326   -188       C
ATOM   2650  O   ASN A 423      31.084  21.072   3.159  1.00 62.81           O
ANISOU 2650  O   ASN A 423     8708   4832  10326    666   -440   -230       O
ATOM   2651  CB  ASN A 423      29.439  22.282   1.094  1.00 56.88           C
ANISOU 2651  CB  ASN A 423     7755   4172   9684    569   -366   -287       C
ATOM   2652  CG  ASN A 423      29.686  21.200   0.093  1.00 72.53           C
ANISOU 2652  CG  ASN A 423     9633   6148  11775    522   -395   -323       C
ATOM   2653  OD1 ASN A 423      30.263  20.171   0.393  1.00 79.81           O
ANISOU 2653  OD1 ASN A 423    10563   7037  12724    531   -412   -311       O
ATOM   2654  ND2 ASN A 423      29.245  21.392  -1.120  1.00 62.78           N
ANISOU 2654  ND2 ASN A 423     8311   4939  10603    476   -405   -367       N
ATOM   2655  N   ARG A 424      29.338  19.707   3.583  1.00 58.92           N
ANISOU 2655  N   ARG A 424     8196   4260   9930    678   -239   -129       N
ATOM   2656  CA  ARG A 424      30.089  18.693   4.302  1.00 58.48           C
ANISOU 2656  CA  ARG A 424     8217   4152   9852    716   -270   -102       C
ATOM   2657  C   ARG A 424      31.090  17.935   3.436  1.00 59.92           C
ANISOU 2657  C   ARG A 424     8292   4357  10119    669   -372   -161       C
ATOM   2658  O   ARG A 424      32.016  17.355   3.987  1.00 59.85           O
ANISOU 2658  O   ARG A 424     8344   4313  10084    700   -440   -155       O
ATOM   2659  CB  ARG A 424      29.146  17.756   5.071  1.00 58.54           C
ANISOU 2659  CB  ARG A 424     8275   4075   9893    756   -121    -15       C
ATOM   2660  CG  ARG A 424      28.444  18.458   6.232  1.00 59.24           C
ANISOU 2660  CG  ARG A 424     8529   4110   9868    828     -9     54       C
ATOM   2661  CD  ARG A 424      27.103  17.824   6.532  1.00 70.25           C
ANISOU 2661  CD  ARG A 424     9903   5422  11364    842    189    133       C
ATOM   2662  NE  ARG A 424      26.306  18.635   7.451  1.00 82.96           N
ANISOU 2662  NE  ARG A 424    11653   6977  12890    903    324    196       N
ATOM   2663  CZ  ARG A 424      25.522  19.643   7.087  1.00 88.54           C
ANISOU 2663  CZ  ARG A 424    12297   7711  13634    878    376    189       C
ATOM   2664  NH1 ARG A 424      25.437  20.002   5.809  1.00 61.01           N
ANISOU 2664  NH1 ARG A 424     8621   4308  10252    796    290    118       N
ATOM   2665  NH2 ARG A 424      24.834  20.314   7.997  1.00 83.73           N
ANISOU 2665  NH2 ARG A 424    11827   7037  12948    939    516    253       N
ATOM   2666  N   ALA A 425      30.945  17.985   2.097  1.00 54.31           N
ANISOU 2666  N   ALA A 425     7438   3694   9502    600   -387   -219       N
ATOM   2667  CA  ALA A 425      31.835  17.317   1.149  1.00 53.36           C
ANISOU 2667  CA  ALA A 425     7227   3585   9463    555   -459   -276       C
ATOM   2668  C   ALA A 425      33.173  18.043   1.070  1.00 59.22           C
ANISOU 2668  C   ALA A 425     7990   4349  10163    559   -569   -328       C
ATOM   2669  O   ALA A 425      34.217  17.394   0.966  1.00 59.81           O
ANISOU 2669  O   ALA A 425     8040   4396  10288    555   -631   -348       O
ATOM   2670  CB  ALA A 425      31.195  17.256  -0.229  1.00 53.39           C
ANISOU 2670  CB  ALA A 425     7113   3616   9557    492   -438   -321       C
ATOM   2671  N   LEU A 426      33.148  19.385   1.152  1.00 56.46           N
ANISOU 2671  N   LEU A 426     7678   4037   9737    569   -591   -346       N
ATOM   2672  CA  LEU A 426      34.342  20.219   1.067  1.00 56.58           C
ANISOU 2672  CA  LEU A 426     7700   4062   9736    573   -690   -398       C
ATOM   2673  C   LEU A 426      34.796  20.790   2.406  1.00 63.19           C
ANISOU 2673  C   LEU A 426     8667   4869  10472    638   -761   -373       C
ATOM   2674  O   LEU A 426      35.929  21.263   2.496  1.00 65.54           O
ANISOU 2674  O   LEU A 426     8965   5150  10787    647   -868   -414       O
ATOM   2675  CB  LEU A 426      34.109  21.378   0.087  1.00 55.76           C
ANISOU 2675  CB  LEU A 426     7544   4015   9627    537   -676   -448       C
ATOM   2676  CG  LEU A 426      33.575  21.024  -1.299  1.00 59.20           C
ANISOU 2676  CG  LEU A 426     7885   4472  10134    481   -624   -480       C
ATOM   2677  CD1 LEU A 426      33.189  22.257  -2.053  1.00 56.22           C
ANISOU 2677  CD1 LEU A 426     7496   4144   9722    462   -610   -517       C
ATOM   2678  CD2 LEU A 426      34.559  20.154  -2.097  1.00 59.49           C
ANISOU 2678  CD2 LEU A 426     7859   4477  10268    452   -648   -520       C
ATOM   2679  N   GLN A 427      33.919  20.809   3.425  1.00 59.10           N
ANISOU 2679  N   GLN A 427     8267   4331   9856    687   -700   -308       N
ATOM   2680  CA  GLN A 427      34.218  21.442   4.713  1.00 59.35           C
ANISOU 2680  CA  GLN A 427     8466   4325   9760    759   -762   -283       C
ATOM   2681  C   GLN A 427      34.015  20.570   5.949  1.00 63.07           C
ANISOU 2681  C   GLN A 427     9089   4718  10156    829   -740   -211       C
ATOM   2682  O   GLN A 427      34.479  20.946   7.026  1.00 61.02           O
ANISOU 2682  O   GLN A 427     8994   4406   9784    898   -825   -198       O
ATOM   2683  CB  GLN A 427      33.381  22.719   4.879  1.00 60.78           C
ANISOU 2683  CB  GLN A 427     8701   4543   9849    769   -699   -274       C
ATOM   2684  CG  GLN A 427      33.334  23.684   3.693  1.00 72.28           C
ANISOU 2684  CG  GLN A 427    10029   6075  11359    708   -694   -334       C
ATOM   2685  CD  GLN A 427      32.174  24.640   3.851  1.00101.73           C
ANISOU 2685  CD  GLN A 427    13801   9834  15017    716   -596   -305       C
ATOM   2686  OE1 GLN A 427      31.152  24.544   3.160  1.00 94.91           O
ANISOU 2686  OE1 GLN A 427    12851   8998  14212    678   -498   -294       O
ATOM   2687  NE2 GLN A 427      32.292  25.559   4.799  1.00103.22           N
ANISOU 2687  NE2 GLN A 427    14128  10005  15086    769   -626   -292       N
ATOM   2688  N   GLY A 428      33.308  19.440   5.792  1.00 62.00           N
ANISOU 2688  N   GLY A 428     8909   4565  10082    815   -627   -166       N
ATOM   2689  CA  GLY A 428      32.970  18.524   6.880  1.00 62.81           C
ANISOU 2689  CA  GLY A 428     9153   4586  10126    881   -565    -89       C
ATOM   2690  C   GLY A 428      34.078  17.608   7.305  1.00 68.68           C
ANISOU 2690  C   GLY A 428     9940   5274  10882    911   -684    -92       C
ATOM   2691  O   GLY A 428      34.139  16.472   6.831  1.00 70.19           O
ANISOU 2691  O   GLY A 428    10028   5457  11183    878   -655    -87       O
ATOM   2692  N   TRP A 429      34.942  18.091   8.217  1.00 66.01           N
ANISOU 2692  N   TRP A 429     9758   4886  10436    978   -828   -100       N
ATOM   2693  CA  TRP A 429      36.071  17.351   8.771  1.00 66.98           C
ANISOU 2693  CA  TRP A 429     9945   4937  10567   1020   -978   -104       C
ATOM   2694  C   TRP A 429      35.545  16.284   9.725  1.00 75.54           C
ANISOU 2694  C   TRP A 429    11189   5939  11574   1090   -885    -17       C
ATOM   2695  O   TRP A 429      34.888  16.612  10.719  1.00 77.37           O
ANISOU 2695  O   TRP A 429    11630   6118  11649   1166   -808     41       O
ATOM   2696  CB  TRP A 429      37.071  18.278   9.476  1.00 65.52           C
ANISOU 2696  CB  TRP A 429     9886   4709  10301   1075  -1182   -144       C
ATOM   2697  CG  TRP A 429      37.781  19.222   8.553  1.00 65.13           C
ANISOU 2697  CG  TRP A 429     9669   4720  10359   1010  -1277   -230       C
ATOM   2698  CD1 TRP A 429      37.405  20.495   8.240  1.00 67.21           C
ANISOU 2698  CD1 TRP A 429     9912   5043  10582    987  -1244   -258       C
ATOM   2699  CD2 TRP A 429      38.991  18.969   7.827  1.00 64.62           C
ANISOU 2699  CD2 TRP A 429     9433   4647  10472    962  -1400   -293       C
ATOM   2700  NE1 TRP A 429      38.314  21.058   7.375  1.00 65.87           N
ANISOU 2700  NE1 TRP A 429     9577   4904  10547    931  -1338   -336       N
ATOM   2701  CE2 TRP A 429      39.307  20.150   7.115  1.00 67.52           C
ANISOU 2701  CE2 TRP A 429     9692   5065  10896    916  -1431   -358       C
ATOM   2702  CE3 TRP A 429      39.843  17.861   7.712  1.00 66.31           C
ANISOU 2702  CE3 TRP A 429     9575   4808  10813    955  -1477   -299       C
ATOM   2703  CZ2 TRP A 429      40.408  20.240   6.262  1.00 66.33           C
ANISOU 2703  CZ2 TRP A 429     9364   4906  10931    865  -1513   -425       C
ATOM   2704  CZ3 TRP A 429      40.958  17.963   6.892  1.00 67.43           C
ANISOU 2704  CZ3 TRP A 429     9537   4941  11143    903  -1569   -367       C
ATOM   2705  CH2 TRP A 429      41.229  19.140   6.177  1.00 67.27           C
ANISOU 2705  CH2 TRP A 429     9414   4964  11183    860  -1578   -428       C
ATOM   2706  N   ARG A 430      35.790  15.007   9.380  1.00 71.74           N
ANISOU 2706  N   ARG A 430    10611   5442  11206   1065   -869     -6       N
ATOM   2707  CA  ARG A 430      35.329  13.862  10.149  1.00 72.13           C
ANISOU 2707  CA  ARG A 430    10781   5411  11213   1123   -767     75       C
ATOM   2708  C   ARG A 430      36.397  12.809  10.205  1.00 77.51           C
ANISOU 2708  C   ARG A 430    11433   6045  11971   1130   -897     63       C
ATOM   2709  O   ARG A 430      37.347  12.849   9.420  1.00 76.68           O
ANISOU 2709  O   ARG A 430    11166   5977  11993   1071  -1027     -7       O
ATOM   2710  CB  ARG A 430      34.030  13.270   9.555  1.00 69.19           C
ANISOU 2710  CB  ARG A 430    10286   5068  10935   1072   -538    116       C
ATOM   2711  CG  ARG A 430      32.822  14.217   9.564  1.00 77.79           C
ANISOU 2711  CG  ARG A 430    11397   6184  11975   1069   -388    139       C
ATOM   2712  CD  ARG A 430      32.400  14.715  10.946  1.00 82.41           C
ANISOU 2712  CD  ARG A 430    12263   6683  12367   1178   -322    209       C
ATOM   2713  NE  ARG A 430      31.627  13.698  11.663  1.00 92.42           N
ANISOU 2713  NE  ARG A 430    13642   7851  13623   1236   -137    304       N
ATOM   2714  CZ  ARG A 430      30.647  13.961  12.521  1.00 95.67           C
ANISOU 2714  CZ  ARG A 430    14236   8180  13933   1310     47    383       C
ATOM   2715  NH1 ARG A 430      30.328  15.212  12.809  1.00 68.73           N
ANISOU 2715  NH1 ARG A 430    10927   4778  10409   1335     60    379       N
ATOM   2716  NH2 ARG A 430      29.978  12.973  13.097  1.00 82.13           N
ANISOU 2716  NH2 ARG A 430    12605   6364  12237   1361    233    470       N
ATOM   2717  N   GLN A 431      36.259  11.870  11.146  1.00 76.03           N
ANISOU 2717  N   GLN A 431    11409   5766  11713   1206   -855    135       N
ATOM   2718  CA  GLN A 431      37.201  10.772  11.228  1.00 76.63           C
ANISOU 2718  CA  GLN A 431    11459   5791  11868   1216   -968    131       C
ATOM   2719  C   GLN A 431      36.790   9.757  10.143  1.00 78.17           C
ANISOU 2719  C   GLN A 431    11419   6037  12245   1126   -830    130       C
ATOM   2720  O   GLN A 431      35.604   9.412  10.054  1.00 76.43           O
ANISOU 2720  O   GLN A 431    11184   5823  12032   1115   -626    181       O
ATOM   2721  CB  GLN A 431      37.203  10.147  12.629  1.00 80.20           C
ANISOU 2721  CB  GLN A 431    12193   6116  12162   1340   -978    209       C
ATOM   2722  CG  GLN A 431      37.575  11.143  13.717  1.00102.00           C
ANISOU 2722  CG  GLN A 431    15220   8812  14724   1438  -1126    206       C
ATOM   2723  CD  GLN A 431      37.714  10.521  15.080  1.00127.75           C
ANISOU 2723  CD  GLN A 431    18800  11931  17807   1572  -1157    279       C
ATOM   2724  OE1 GLN A 431      36.843   9.776  15.556  1.00121.30           O
ANISOU 2724  OE1 GLN A 431    18101  11061  16927   1619   -945    365       O
ATOM   2725  NE2 GLN A 431      38.796  10.862  15.765  1.00125.23           N
ANISOU 2725  NE2 GLN A 431    18643  11535  17404   1644  -1423    245       N
ATOM   2726  N   PRO A 432      37.722   9.332   9.256  1.00 74.15           N
ANISOU 2726  N   PRO A 432    10717   5557  11898   1058   -933     70       N
ATOM   2727  CA  PRO A 432      37.342   8.367   8.213  1.00 73.15           C
ANISOU 2727  CA  PRO A 432    10392   5471  11932    976   -809     64       C
ATOM   2728  C   PRO A 432      37.077   6.950   8.751  1.00 78.16           C
ANISOU 2728  C   PRO A 432    11086   6031  12579   1017   -722    136       C
ATOM   2729  O   PRO A 432      36.392   6.151   8.093  1.00 78.57           O
ANISOU 2729  O   PRO A 432    11010   6102  12739    964   -579    149       O
ATOM   2730  CB  PRO A 432      38.549   8.392   7.284  1.00 74.06           C
ANISOU 2730  CB  PRO A 432    10332   5612  12194    911   -945    -16       C
ATOM   2731  CG  PRO A 432      39.699   8.690   8.188  1.00 79.10           C
ANISOU 2731  CG  PRO A 432    11093   6178  12784    981  -1150    -24       C
ATOM   2732  CD  PRO A 432      39.161   9.671   9.176  1.00 75.10           C
ANISOU 2732  CD  PRO A 432    10797   5657  12081   1056  -1159      6       C
ATOM   2733  N   GLY A 433      37.593   6.675   9.951  1.00 74.80           N
ANISOU 2733  N   GLY A 433    10865   5513  12041   1115   -812    181       N
ATOM   2734  CA  GLY A 433      37.495   5.371  10.598  1.00 75.70           C
ANISOU 2734  CA  GLY A 433    11074   5543  12147   1171   -748    252       C
ATOM   2735  C   GLY A 433      38.256   4.315   9.830  1.00 78.25           C
ANISOU 2735  C   GLY A 433    11208   5870  12652   1109   -797    221       C
ATOM   2736  O   GLY A 433      39.458   4.440   9.612  1.00 75.86           O
ANISOU 2736  O   GLY A 433    10840   5562  12421   1093   -981    166       O
ATOM   2737  N   SER A 434      37.529   3.325   9.342  1.00 77.37           N
ANISOU 2737  N   SER A 434    10993   5766  12639   1068   -626    251       N
ATOM   2738  CA  SER A 434      38.032   2.169   8.594  1.00 77.74           C
ANISOU 2738  CA  SER A 434    10867   5812  12859   1008   -629    230       C
ATOM   2739  C   SER A 434      38.247   2.432   7.114  1.00 78.20           C
ANISOU 2739  C   SER A 434    10688   5957  13066    894   -641    144       C
ATOM   2740  O   SER A 434      38.975   1.671   6.483  1.00 77.49           O
ANISOU 2740  O   SER A 434    10470   5858  13113    849   -680    114       O
ATOM   2741  CB  SER A 434      37.101   0.977   8.792  1.00 85.46           C
ANISOU 2741  CB  SER A 434    11851   6745  13875   1020   -436    301       C
ATOM   2742  OG  SER A 434      37.669   0.096   9.741  1.00103.03           O
ANISOU 2742  OG  SER A 434    14215   8874  16056   1101   -484    357       O
ATOM   2743  N   THR A 435      37.641   3.513   6.562  1.00 72.67           N
ANISOU 2743  N   THR A 435     9942   5331  12338    853   -605    106       N
ATOM   2744  CA  THR A 435      37.769   3.877   5.145  1.00 70.48           C
ANISOU 2744  CA  THR A 435     9475   5129  12176    755   -609     25       C
ATOM   2745  C   THR A 435      39.184   4.285   4.773  1.00 73.03           C
ANISOU 2745  C   THR A 435     9735   5450  12563    735   -768    -38       C
ATOM   2746  O   THR A 435      39.468   4.463   3.592  1.00 72.28           O
ANISOU 2746  O   THR A 435     9498   5395  12570    661   -760   -101       O
ATOM   2747  CB  THR A 435      36.675   4.870   4.667  1.00 73.01           C
ANISOU 2747  CB  THR A 435     9771   5518  12450    722   -526      6       C
ATOM   2748  OG1 THR A 435      36.421   5.842   5.659  1.00 69.81           O
ANISOU 2748  OG1 THR A 435     9523   5108  11893    788   -553     36       O
ATOM   2749  CG2 THR A 435      35.383   4.193   4.345  1.00 70.14           C
ANISOU 2749  CG2 THR A 435     9354   5151  12145    697   -362     39       C
ATOM   2750  N   ILE A 436      40.078   4.410   5.775  1.00 69.19           N
ANISOU 2750  N   ILE A 436     9361   4901  12026    805   -912    -21       N
ATOM   2751  CA  ILE A 436      41.487   4.753   5.579  1.00 67.99           C
ANISOU 2751  CA  ILE A 436     9144   4717  11972    797  -1079    -75       C
ATOM   2752  C   ILE A 436      42.371   3.540   5.306  1.00 72.16           C
ANISOU 2752  C   ILE A 436     9576   5182  12660    779  -1112    -76       C
ATOM   2753  O   ILE A 436      43.369   3.661   4.602  1.00 73.03           O
ANISOU 2753  O   ILE A 436     9557   5272  12920    738  -1180   -130       O
ATOM   2754  CB  ILE A 436      42.042   5.705   6.676  1.00 70.78           C
ANISOU 2754  CB  ILE A 436     9651   5026  12215    876  -1252    -73       C
ATOM   2755  CG1 ILE A 436      42.897   6.753   6.033  1.00 71.40           C
ANISOU 2755  CG1 ILE A 436     9620   5121  12389    835  -1354   -150       C
ATOM   2756  CG2 ILE A 436      42.813   5.008   7.809  1.00 69.68           C
ANISOU 2756  CG2 ILE A 436     9639   4778  12060    960  -1398    -32       C
ATOM   2757  CD1 ILE A 436      42.157   7.838   5.427  1.00 80.99           C
ANISOU 2757  CD1 ILE A 436    10808   6428  13538    794  -1266   -181       C
ATOM   2758  N   LYS A 437      42.000   2.387   5.872  1.00 67.83           N
ANISOU 2758  N   LYS A 437     9091   4594  12089    814  -1051    -13       N
ATOM   2759  CA  LYS A 437      42.719   1.111   5.784  1.00 67.25           C
ANISOU 2759  CA  LYS A 437     8947   4454  12150    808  -1072      1       C
ATOM   2760  C   LYS A 437      43.198   0.733   4.377  1.00 69.36           C
ANISOU 2760  C   LYS A 437     9005   4740  12606    713  -1015    -59       C
ATOM   2761  O   LYS A 437      44.395   0.484   4.250  1.00 68.88           O
ANISOU 2761  O   LYS A 437     8869   4614  12687    709  -1117    -83       O
ATOM   2762  CB  LYS A 437      41.964  -0.027   6.502  1.00 68.98           C
ANISOU 2762  CB  LYS A 437     9267   4639  12303    855   -968     81       C
ATOM   2763  CG  LYS A 437      41.822   0.234   7.992  1.00 75.21           C
ANISOU 2763  CG  LYS A 437    10297   5369  12909    968  -1040    144       C
ATOM   2764  CD  LYS A 437      41.145  -0.871   8.705  1.00 85.94           C
ANISOU 2764  CD  LYS A 437    11768   6676  14209   1023   -921    228       C
ATOM   2765  CE  LYS A 437      40.759  -0.508  10.135  1.00100.25           C
ANISOU 2765  CE  LYS A 437    13859   8424  15806   1143   -946    295       C
ATOM   2766  NZ  LYS A 437      41.894   0.010  10.955  1.00111.03           N
ANISOU 2766  NZ  LYS A 437    15358   9719  17110   1216  -1198    279       N
ATOM   2767  N   PRO A 438      42.367   0.801   3.292  1.00 63.38           N
ANISOU 2767  N   PRO A 438     8161   4057  11862    641   -870    -90       N
ATOM   2768  CA  PRO A 438      42.883   0.484   1.955  1.00 62.08           C
ANISOU 2768  CA  PRO A 438     7839   3893  11856    563   -819   -149       C
ATOM   2769  C   PRO A 438      44.131   1.260   1.541  1.00 68.42           C
ANISOU 2769  C   PRO A 438     8569   4664  12765    547   -916   -205       C
ATOM   2770  O   PRO A 438      44.899   0.736   0.748  1.00 69.99           O
ANISOU 2770  O   PRO A 438     8655   4815  13123    504   -886   -236       O
ATOM   2771  CB  PRO A 438      41.703   0.800   1.053  1.00 61.94           C
ANISOU 2771  CB  PRO A 438     7796   3955  11785    509   -690   -175       C
ATOM   2772  CG  PRO A 438      40.543   0.492   1.889  1.00 65.75           C
ANISOU 2772  CG  PRO A 438     8373   4452  12156    550   -632   -111       C
ATOM   2773  CD  PRO A 438      40.917   1.063   3.219  1.00 62.83           C
ANISOU 2773  CD  PRO A 438     8138   4055  11680    633   -744    -71       C
ATOM   2774  N   PHE A 439      44.357   2.472   2.071  1.00 64.75           N
ANISOU 2774  N   PHE A 439     8165   4208  12229    583  -1023   -217       N
ATOM   2775  CA  PHE A 439      45.570   3.228   1.719  1.00 64.60           C
ANISOU 2775  CA  PHE A 439     8062   4139  12344    571  -1116   -269       C
ATOM   2776  C   PHE A 439      46.772   2.652   2.420  1.00 74.89           C
ANISOU 2776  C   PHE A 439     9341   5329  13786    612  -1259   -253       C
ATOM   2777  O   PHE A 439      47.803   2.461   1.777  1.00 76.28           O
ANISOU 2777  O   PHE A 439     9383   5433  14169    578  -1261   -286       O
ATOM   2778  CB  PHE A 439      45.449   4.720   2.029  1.00 64.37           C
ANISOU 2778  CB  PHE A 439     8096   4149  12211    594  -1191   -293       C
ATOM   2779  CG  PHE A 439      44.189   5.369   1.536  1.00 62.52           C
ANISOU 2779  CG  PHE A 439     7901   4023  11829    565  -1071   -302       C
ATOM   2780  CD1 PHE A 439      43.818   5.279   0.203  1.00 62.70           C
ANISOU 2780  CD1 PHE A 439     7840   4087  11898    496   -932   -341       C
ATOM   2781  CD2 PHE A 439      43.396   6.116   2.392  1.00 63.37           C
ANISOU 2781  CD2 PHE A 439     8141   4181  11758    611  -1103   -275       C
ATOM   2782  CE1 PHE A 439      42.648   5.873  -0.248  1.00 62.18           C
ANISOU 2782  CE1 PHE A 439     7809   4109  11708    472   -845   -352       C
ATOM   2783  CE2 PHE A 439      42.248   6.753   1.924  1.00 64.68           C
ANISOU 2783  CE2 PHE A 439     8327   4436  11813    583   -996   -284       C
ATOM   2784  CZ  PHE A 439      41.894   6.646   0.604  1.00 61.49           C
ANISOU 2784  CZ  PHE A 439     7827   4071  11467    513   -879   -324       C
ATOM   2785  N   LEU A 440      46.625   2.347   3.728  1.00 73.79           N
ANISOU 2785  N   LEU A 440     9339   5161  13539    688  -1370   -198       N
ATOM   2786  CA  LEU A 440      47.654   1.757   4.577  1.00 75.24           C
ANISOU 2786  CA  LEU A 440     9536   5227  13823    744  -1537   -175       C
ATOM   2787  C   LEU A 440      48.007   0.325   4.119  1.00 77.96           C
ANISOU 2787  C   LEU A 440     9777   5524  14320    712  -1458   -156       C
ATOM   2788  O   LEU A 440      49.189  -0.028   4.096  1.00 78.87           O
ANISOU 2788  O   LEU A 440     9794   5535  14640    714  -1556   -170       O
ATOM   2789  CB  LEU A 440      47.194   1.823   6.050  1.00 76.54           C
ANISOU 2789  CB  LEU A 440     9924   5376  13780    842  -1650   -118       C
ATOM   2790  CG  LEU A 440      47.961   1.018   7.102  1.00 83.56           C
ANISOU 2790  CG  LEU A 440    10894   6145  14709    920  -1822    -77       C
ATOM   2791  CD1 LEU A 440      49.355   1.553   7.292  1.00 85.12           C
ANISOU 2791  CD1 LEU A 440    11018   6234  15090    939  -2052   -125       C
ATOM   2792  CD2 LEU A 440      47.236   1.050   8.419  1.00 87.49           C
ANISOU 2792  CD2 LEU A 440    11653   6634  14953   1019  -1870    -15       C
ATOM   2793  N   TYR A 441      46.995  -0.468   3.711  1.00 72.56           N
ANISOU 2793  N   TYR A 441     9104   4906  13558    680  -1280   -129       N
ATOM   2794  CA  TYR A 441      47.190  -1.834   3.216  1.00 71.52           C
ANISOU 2794  CA  TYR A 441     8882   4738  13556    646  -1186   -113       C
ATOM   2795  C   TYR A 441      47.810  -1.838   1.826  1.00 73.81           C
ANISOU 2795  C   TYR A 441     8999   5011  14036    564  -1093   -173       C
ATOM   2796  O   TYR A 441      48.505  -2.773   1.484  1.00 73.43           O
ANISOU 2796  O   TYR A 441     8856   4890  14154    544  -1066   -170       O
ATOM   2797  CB  TYR A 441      45.886  -2.626   3.251  1.00 72.73           C
ANISOU 2797  CB  TYR A 441     9101   4955  13579    641  -1034    -68       C
ATOM   2798  CG  TYR A 441      45.478  -3.118   4.629  1.00 76.11           C
ANISOU 2798  CG  TYR A 441     9694   5353  13871    728  -1087      8       C
ATOM   2799  CD1 TYR A 441      45.223  -4.461   4.862  1.00 77.44           C
ANISOU 2799  CD1 TYR A 441     9873   5487  14063    741  -1011     60       C
ATOM   2800  CD2 TYR A 441      45.268  -2.226   5.680  1.00 78.56           C
ANISOU 2800  CD2 TYR A 441    10169   5664  14017    803  -1196     31       C
ATOM   2801  CE1 TYR A 441      44.814  -4.915   6.120  1.00 78.94           C
ANISOU 2801  CE1 TYR A 441    10237   5637  14119    830  -1036    136       C
ATOM   2802  CE2 TYR A 441      44.873  -2.671   6.945  1.00 80.59           C
ANISOU 2802  CE2 TYR A 441    10615   5877  14129    895  -1226    105       C
ATOM   2803  CZ  TYR A 441      44.645  -4.017   7.160  1.00 87.95           C
ANISOU 2803  CZ  TYR A 441    11558   6770  15089    909  -1140    159       C
ATOM   2804  OH  TYR A 441      44.236  -4.444   8.399  1.00 92.53           O
ANISOU 2804  OH  TYR A 441    12344   7295  15519   1007  -1148    237       O
ATOM   2805  N   ALA A 442      47.614  -0.775   1.044  1.00 71.23           N
ANISOU 2805  N   ALA A 442     8641   4738  13684    524  -1040   -225       N
ATOM   2806  CA  ALA A 442      48.248  -0.620  -0.271  1.00 70.62           C
ANISOU 2806  CA  ALA A 442     8433   4628  13772    459   -941   -282       C
ATOM   2807  C   ALA A 442      49.747  -0.461  -0.093  1.00 73.16           C
ANISOU 2807  C   ALA A 442     8653   4822  14322    475  -1056   -297       C
ATOM   2808  O   ALA A 442      50.532  -1.045  -0.838  1.00 73.95           O
ANISOU 2808  O   ALA A 442     8636   4838  14624    439   -980   -314       O
ATOM   2809  CB  ALA A 442      47.701   0.613  -0.970  1.00 70.71           C
ANISOU 2809  CB  ALA A 442     8465   4718  13683    429   -877   -329       C
ATOM   2810  N   LEU A 443      50.125   0.321   0.914  1.00 68.47           N
ANISOU 2810  N   LEU A 443     8109   4204  13704    532  -1242   -291       N
ATOM   2811  CA  LEU A 443      51.497   0.623   1.278  1.00 69.28           C
ANISOU 2811  CA  LEU A 443     8120   4173  14029    559  -1403   -308       C
ATOM   2812  C   LEU A 443      52.249  -0.607   1.771  1.00 73.32           C
ANISOU 2812  C   LEU A 443     8583   4575  14700    583  -1481   -271       C
ATOM   2813  O   LEU A 443      53.449  -0.707   1.534  1.00 73.65           O
ANISOU 2813  O   LEU A 443     8483   4487  15015    575  -1533   -291       O
ATOM   2814  CB  LEU A 443      51.533   1.801   2.286  1.00 69.83           C
ANISOU 2814  CB  LEU A 443     8288   4249  13994    620  -1602   -314       C
ATOM   2815  CG  LEU A 443      50.990   3.150   1.774  1.00 72.47           C
ANISOU 2815  CG  LEU A 443     8648   4674  14212    595  -1538   -356       C
ATOM   2816  CD1 LEU A 443      50.583   4.025   2.903  1.00 73.18           C
ANISOU 2816  CD1 LEU A 443     8893   4803  14111    660  -1702   -344       C
ATOM   2817  CD2 LEU A 443      51.985   3.859   0.903  1.00 73.49           C
ANISOU 2817  CD2 LEU A 443     8619   4724  14580    554  -1502   -412       C
ATOM   2818  N   ALA A 444      51.526  -1.558   2.412  1.00 70.88           N
ANISOU 2818  N   ALA A 444     8384   4310  14236    613  -1474   -215       N
ATOM   2819  CA  ALA A 444      52.011  -2.861   2.877  1.00 71.64           C
ANISOU 2819  CA  ALA A 444     8460   4321  14438    639  -1522   -171       C
ATOM   2820  C   ALA A 444      52.315  -3.707   1.650  1.00 74.20           C
ANISOU 2820  C   ALA A 444     8633   4614  14944    564  -1330   -187       C
ATOM   2821  O   ALA A 444      53.360  -4.342   1.588  1.00 75.90           O
ANISOU 2821  O   ALA A 444     8733   4706  15399    562  -1370   -183       O
ATOM   2822  CB  ALA A 444      50.939  -3.546   3.721  1.00 72.66           C
ANISOU 2822  CB  ALA A 444     8762   4521  14325    686  -1508   -108       C
ATOM   2823  N   LEU A 445      51.424  -3.671   0.656  1.00 68.40           N
ANISOU 2823  N   LEU A 445     7906   3980  14104    505  -1127   -209       N
ATOM   2824  CA  LEU A 445      51.571  -4.369  -0.609  1.00 68.94           C
ANISOU 2824  CA  LEU A 445     7872   4023  14301    437   -932   -232       C
ATOM   2825  C   LEU A 445      52.779  -3.829  -1.366  1.00 75.71           C
ANISOU 2825  C   LEU A 445     8586   4767  15412    408   -904   -278       C
ATOM   2826  O   LEU A 445      53.515  -4.596  -1.979  1.00 73.86           O
ANISOU 2826  O   LEU A 445     8246   4433  15385    377   -807   -281       O
ATOM   2827  CB  LEU A 445      50.296  -4.172  -1.432  1.00 67.96           C
ANISOU 2827  CB  LEU A 445     7817   4024  13979    392   -768   -255       C
ATOM   2828  CG  LEU A 445      49.180  -5.190  -1.229  1.00 71.28           C
ANISOU 2828  CG  LEU A 445     8314   4515  14252    393   -701   -215       C
ATOM   2829  CD1 LEU A 445      47.833  -4.535  -1.359  1.00 69.36           C
ANISOU 2829  CD1 LEU A 445     8170   4398  13786    384   -650   -226       C
ATOM   2830  CD2 LEU A 445      49.267  -6.274  -2.283  1.00 76.70           C
ANISOU 2830  CD2 LEU A 445     8931   5162  15048    338   -541   -229       C
ATOM   2831  N   GLU A 446      53.009  -2.508  -1.278  1.00 76.62           N
ANISOU 2831  N   GLU A 446     8700   4885  15528    420   -981   -311       N
ATOM   2832  CA  GLU A 446      54.140  -1.835  -1.917  1.00 78.31           C
ANISOU 2832  CA  GLU A 446     8777   4979  15999    399   -952   -353       C
ATOM   2833  C   GLU A 446      55.480  -2.267  -1.323  1.00 86.27           C
ANISOU 2833  C   GLU A 446     9656   5818  17307    430  -1099   -337       C
ATOM   2834  O   GLU A 446      56.488  -2.290  -2.038  1.00 86.52           O
ANISOU 2834  O   GLU A 446     9538   5712  17624    403  -1015   -359       O
ATOM   2835  CB  GLU A 446      53.981  -0.323  -1.823  1.00 79.52           C
ANISOU 2835  CB  GLU A 446     8966   5179  16068    411  -1013   -389       C
ATOM   2836  CG  GLU A 446      54.460   0.365  -3.079  1.00 90.97           C
ANISOU 2836  CG  GLU A 446    10323   6562  17680    368   -845   -438       C
ATOM   2837  CD  GLU A 446      54.254   1.859  -3.079  1.00117.13           C
ANISOU 2837  CD  GLU A 446    13671   9926  20906    376   -883   -474       C
ATOM   2838  OE1 GLU A 446      54.790   2.538  -2.172  1.00115.15           O
ANISOU 2838  OE1 GLU A 446    13390   9627  20734    417  -1084   -478       O
ATOM   2839  OE2 GLU A 446      53.596   2.356  -4.020  1.00117.61           O
ANISOU 2839  OE2 GLU A 446    13794  10064  20828    343   -718   -501       O
ATOM   2840  N   ARG A 447      55.481  -2.628  -0.018  1.00 84.82           N
ANISOU 2840  N   ARG A 447     9536   5630  17062    490  -1316   -296       N
ATOM   2841  CA  ARG A 447      56.659  -3.090   0.721  1.00 85.94           C
ANISOU 2841  CA  ARG A 447     9580   5610  17464    531  -1507   -277       C
ATOM   2842  C   ARG A 447      57.042  -4.542   0.340  1.00 89.97           C
ANISOU 2842  C   ARG A 447    10004   6045  18135    507  -1396   -246       C
ATOM   2843  O   ARG A 447      58.144  -4.984   0.687  1.00 92.77           O
ANISOU 2843  O   ARG A 447    10239   6242  18768    528  -1516   -234       O
ATOM   2844  CB  ARG A 447      56.452  -2.943   2.248  1.00 86.20           C
ANISOU 2844  CB  ARG A 447     9759   5660  17334    616  -1786   -247       C
ATOM   2845  CG  ARG A 447      56.421  -1.503   2.793  1.00 99.04           C
ANISOU 2845  CG  ARG A 447    11451   7307  18874    653  -1951   -280       C
ATOM   2846  CD  ARG A 447      57.785  -0.858   3.007  1.00115.33           C
ANISOU 2846  CD  ARG A 447    13361   9192  21267    672  -2140   -318       C
ATOM   2847  NE  ARG A 447      58.671  -1.682   3.834  1.00132.35           N
ANISOU 2847  NE  ARG A 447    15473  11196  23617    724  -2355   -290       N
ATOM   2848  CZ  ARG A 447      59.713  -2.368   3.370  1.00148.51           C
ANISOU 2848  CZ  ARG A 447    17319  13087  26021    697  -2321   -290       C
ATOM   2849  NH1 ARG A 447      60.027  -2.322   2.080  1.00135.25           N
ANISOU 2849  NH1 ARG A 447    15475  11374  24539    622  -2067   -316       N
ATOM   2850  NH2 ARG A 447      60.453  -3.097   4.193  1.00136.97           N
ANISOU 2850  NH2 ARG A 447    15830  11490  24722    750  -2540   -263       N
ATOM   2851  N   GLY A 448      56.155  -5.236  -0.388  1.00 82.95           N
ANISOU 2851  N   GLY A 448     9171   5259  17087    462  -1177   -237       N
ATOM   2852  CA  GLY A 448      56.348  -6.605  -0.864  1.00 82.46           C
ANISOU 2852  CA  GLY A 448     9047   5144  17140    432  -1041   -211       C
ATOM   2853  C   GLY A 448      55.229  -7.598  -0.580  1.00 85.07           C
ANISOU 2853  C   GLY A 448     9506   5592  17226    437   -990   -169       C
ATOM   2854  O   GLY A 448      55.250  -8.709  -1.114  1.00 85.87           O
ANISOU 2854  O   GLY A 448     9563   5663  17400    405   -853   -154       O
ATOM   2855  N   MET A 449      54.258  -7.225   0.277  1.00 79.77           N
ANISOU 2855  N   MET A 449     8991   5039  16276    480  -1090   -149       N
ATOM   2856  CA  MET A 449      53.145  -8.094   0.662  1.00 78.38           C
ANISOU 2856  CA  MET A 449     8939   4962  15882    493  -1038   -104       C
ATOM   2857  C   MET A 449      52.154  -8.377  -0.461  1.00 78.71           C
ANISOU 2857  C   MET A 449     8998   5101  15808    426   -806   -128       C
ATOM   2858  O   MET A 449      52.233  -7.772  -1.539  1.00 77.37           O
ANISOU 2858  O   MET A 449     8781   4940  15678    376   -690   -181       O
ATOM   2859  CB  MET A 449      52.436  -7.574   1.912  1.00 81.18           C
ANISOU 2859  CB  MET A 449     9463   5389  15993    565  -1193    -71       C
ATOM   2860  CG  MET A 449      53.136  -7.954   3.182  1.00 86.80           C
ANISOU 2860  CG  MET A 449    10219   6001  16761    647  -1420    -28       C
ATOM   2861  SD  MET A 449      52.178  -7.458   4.629  1.00 92.36           S
ANISOU 2861  SD  MET A 449    11178   6782  17132    740  -1553     18       S
ATOM   2862  CE  MET A 449      53.420  -6.628   5.546  1.00 90.46           C
ANISOU 2862  CE  MET A 449    10958   6402  17012    821  -1876     11       C
ATOM   2863  N   THR A 450      51.260  -9.358  -0.221  1.00 73.49           N
ANISOU 2863  N   THR A 450     8407   4497  15019    430   -742    -88       N
ATOM   2864  CA  THR A 450      50.237  -9.808  -1.161  1.00 72.51           C
ANISOU 2864  CA  THR A 450     8304   4451  14794    375   -553   -108       C
ATOM   2865  C   THR A 450      48.882  -9.878  -0.426  1.00 76.52           C
ANISOU 2865  C   THR A 450     8944   5065  15067    407   -562    -69       C
ATOM   2866  O   THR A 450      48.892  -9.872   0.809  1.00 77.19           O
ANISOU 2866  O   THR A 450     9106   5139  15082    477   -691    -18       O
ATOM   2867  CB  THR A 450      50.610 -11.199  -1.764  1.00 82.15           C
ANISOU 2867  CB  THR A 450     9442   5598  16173    337   -433   -100       C
ATOM   2868  OG1 THR A 450      50.149 -12.262  -0.916  1.00 87.69           O
ANISOU 2868  OG1 THR A 450    10190   6306  16821    373   -456    -38       O
ATOM   2869  CG2 THR A 450      52.090 -11.357  -2.094  1.00 78.35           C
ANISOU 2869  CG2 THR A 450     8829   4977  15963    326   -441   -113       C
ATOM   2870  N   PRO A 451      47.724 -10.027  -1.124  1.00 72.37           N
ANISOU 2870  N   PRO A 451     8449   4619  14431    365   -428    -90       N
ATOM   2871  CA  PRO A 451      46.440 -10.180  -0.400  1.00 72.98           C
ANISOU 2871  CA  PRO A 451     8629   4770  14330    397   -417    -46       C
ATOM   2872  C   PRO A 451      46.391 -11.457   0.442  1.00 79.14           C
ANISOU 2872  C   PRO A 451     9432   5502  15135    439   -415     24       C
ATOM   2873  O   PRO A 451      45.595 -11.566   1.376  1.00 79.29           O
ANISOU 2873  O   PRO A 451     9554   5549  15025    491   -423     79       O
ATOM   2874  CB  PRO A 451      45.404 -10.284  -1.527  1.00 73.98           C
ANISOU 2874  CB  PRO A 451     8742   4955  14410    333   -278    -92       C
ATOM   2875  CG  PRO A 451      46.094  -9.776  -2.743  1.00 77.31           C
ANISOU 2875  CG  PRO A 451     9101   5353  14919    280   -238   -164       C
ATOM   2876  CD  PRO A 451      47.523 -10.092  -2.585  1.00 73.08           C
ANISOU 2876  CD  PRO A 451     8490   4717  14560    292   -284   -152       C
ATOM   2877  N   TYR A 452      47.249 -12.421   0.091  1.00 77.22           N
ANISOU 2877  N   TYR A 452     9098   5178  15063    417   -390     25       N
ATOM   2878  CA  TYR A 452      47.338 -13.729   0.731  1.00 77.97           C
ANISOU 2878  CA  TYR A 452     9199   5217  15209    450   -378     88       C
ATOM   2879  C   TYR A 452      48.338 -13.777   1.871  1.00 81.51           C
ANISOU 2879  C   TYR A 452     9682   5587  15702    525   -544    137       C
ATOM   2880  O   TYR A 452      48.203 -14.648   2.723  1.00 82.05           O
ANISOU 2880  O   TYR A 452     9815   5620  15741    579   -558    203       O
ATOM   2881  CB  TYR A 452      47.541 -14.847  -0.313  1.00 79.42           C
ANISOU 2881  CB  TYR A 452     9275   5357  15544    384   -246     63       C
ATOM   2882  CG  TYR A 452      46.501 -14.779  -1.407  1.00 82.71           C
ANISOU 2882  CG  TYR A 452     9685   5839  15902    319   -114      9       C
ATOM   2883  CD1 TYR A 452      45.200 -15.215  -1.185  1.00 85.19           C
ANISOU 2883  CD1 TYR A 452    10046   6201  16122    322    -43     33       C
ATOM   2884  CD2 TYR A 452      46.783 -14.171  -2.625  1.00 84.26           C
ANISOU 2884  CD2 TYR A 452     9841   6041  16135    262    -68    -66       C
ATOM   2885  CE1 TYR A 452      44.214 -15.083  -2.165  1.00 87.24           C
ANISOU 2885  CE1 TYR A 452    10298   6507  16340    266     44    -23       C
ATOM   2886  CE2 TYR A 452      45.801 -14.017  -3.606  1.00 85.21           C
ANISOU 2886  CE2 TYR A 452     9983   6214  16181    212     22   -120       C
ATOM   2887  CZ  TYR A 452      44.517 -14.479  -3.375  1.00 93.11           C
ANISOU 2887  CZ  TYR A 452    11017   7258  17102    213     64   -101       C
ATOM   2888  OH  TYR A 452      43.549 -14.326  -4.343  1.00 91.46           O
ANISOU 2888  OH  TYR A 452    10823   7086  16842    166    124   -159       O
ATOM   2889  N   SER A 453      49.278 -12.803   1.945  1.00 76.93           N
ANISOU 2889  N   SER A 453     9072   4971  15186    537   -678    107       N
ATOM   2890  CA  SER A 453      50.274 -12.696   3.022  1.00 77.34           C
ANISOU 2890  CA  SER A 453     9157   4933  15297    612   -880    142       C
ATOM   2891  C   SER A 453      49.610 -12.801   4.408  1.00 79.57           C
ANISOU 2891  C   SER A 453     9631   5227  15374    707   -962    212       C
ATOM   2892  O   SER A 453      48.556 -12.209   4.643  1.00 77.66           O
ANISOU 2892  O   SER A 453     9500   5071  14935    722   -916    218       O
ATOM   2893  CB  SER A 453      51.062 -11.388   2.912  1.00 80.66           C
ANISOU 2893  CB  SER A 453     9535   5330  15782    612  -1010     91       C
ATOM   2894  OG  SER A 453      51.852 -11.309   1.736  1.00 88.47           O
ANISOU 2894  OG  SER A 453    10357   6272  16985    539   -929     36       O
ATOM   2895  N   MET A 454      50.225 -13.572   5.303  1.00 76.43           N
ANISOU 2895  N   MET A 454     9280   4734  15027    774  -1074    267       N
ATOM   2896  CA  MET A 454      49.714 -13.807   6.646  1.00 76.47           C
ANISOU 2896  CA  MET A 454     9494   4721  14839    878  -1142    341       C
ATOM   2897  C   MET A 454      50.086 -12.691   7.581  1.00 81.65           C
ANISOU 2897  C   MET A 454    10291   5347  15385    957  -1362    339       C
ATOM   2898  O   MET A 454      51.272 -12.396   7.779  1.00 81.15           O
ANISOU 2898  O   MET A 454    10175   5192  15465    979  -1562    316       O
ATOM   2899  CB  MET A 454      50.139 -15.186   7.181  1.00 79.50           C
ANISOU 2899  CB  MET A 454     9895   5009  15303    922  -1157    403       C
ATOM   2900  CG  MET A 454      49.405 -16.330   6.527  1.00 82.21           C
ANISOU 2900  CG  MET A 454    10160   5390  15685    863   -922    420       C
ATOM   2901  SD  MET A 454      47.632 -16.323   6.909  1.00 86.34           S
ANISOU 2901  SD  MET A 454    10834   6007  15964    884   -732    463       S
ATOM   2902  CE  MET A 454      47.099 -17.864   6.147  1.00 82.76           C
ANISOU 2902  CE  MET A 454    10263   5547  15636    824   -512    483       C
ATOM   2903  N   VAL A 455      49.047 -12.022   8.113  1.00 79.88           N
ANISOU 2903  N   VAL A 455    10238   5194  14919    998  -1321    359       N
ATOM   2904  CA  VAL A 455      49.157 -10.895   9.061  1.00 80.58           C
ANISOU 2904  CA  VAL A 455    10503   5263  14849   1081  -1507    360       C
ATOM   2905  C   VAL A 455      48.603 -11.342  10.434  1.00 88.65           C
ANISOU 2905  C   VAL A 455    11800   6232  15653   1204  -1532    447       C
ATOM   2906  O   VAL A 455      47.840 -12.313  10.477  1.00 88.24           O
ANISOU 2906  O   VAL A 455    11780   6191  15557   1207  -1348    502       O
ATOM   2907  CB  VAL A 455      48.510  -9.601   8.523  1.00 81.85           C
ANISOU 2907  CB  VAL A 455    10651   5536  14914   1032  -1441    308       C
ATOM   2908  CG1 VAL A 455      49.296  -9.027   7.341  1.00 79.93           C
ANISOU 2908  CG1 VAL A 455    10180   5311  14879    937  -1462    224       C
ATOM   2909  CG2 VAL A 455      47.048  -9.832   8.154  1.00 80.91           C
ANISOU 2909  CG2 VAL A 455    10554   5517  14673    995  -1188    331       C
ATOM   2910  N   ASN A 456      49.050 -10.732  11.562  1.00 88.29           N
ANISOU 2910  N   ASN A 456    11959   6107  15482   1311  -1761    463       N
ATOM   2911  CA  ASN A 456      48.558 -11.245  12.847  1.00 90.11           C
ANISOU 2911  CA  ASN A 456    12480   6264  15491   1439  -1768    551       C
ATOM   2912  C   ASN A 456      47.664 -10.364  13.666  1.00 92.48           C
ANISOU 2912  C   ASN A 456    13039   6588  15510   1516  -1736    580       C
ATOM   2913  O   ASN A 456      48.032  -9.267  14.099  1.00 91.56           O
ANISOU 2913  O   ASN A 456    13021   6457  15312   1554  -1920    544       O
ATOM   2914  CB  ASN A 456      49.601 -12.053  13.674  1.00 98.17           C
ANISOU 2914  CB  ASN A 456    13601   7132  16569   1533  -1993    587       C
ATOM   2915  CG  ASN A 456      50.195 -11.438  14.918  1.00133.75           C
ANISOU 2915  CG  ASN A 456    18363  11520  20935   1663  -2298    593       C
ATOM   2916  OD1 ASN A 456      50.684 -10.305  14.925  1.00132.35           O
ANISOU 2916  OD1 ASN A 456    18203  11354  20730   1664  -2451    537       O
ATOM   2917  ND2 ASN A 456      50.309 -12.248  15.953  1.00128.64           N
ANISOU 2917  ND2 ASN A 456    17907  10741  20228   1775  -2422    655       N
ATOM   2918  N   ASP A 457      46.448 -10.875  13.838  1.00 88.36           N
ANISOU 2918  N   ASP A 457    12619   6096  14859   1535  -1484    646       N
ATOM   2919  CA  ASP A 457      45.414 -10.250  14.631  1.00 88.27           C
ANISOU 2919  CA  ASP A 457    12864   6087  14586   1614  -1386    694       C
ATOM   2920  C   ASP A 457      45.619 -10.752  16.069  1.00 95.91           C
ANISOU 2920  C   ASP A 457    14167   6904  15370   1776  -1491    776       C
ATOM   2921  O   ASP A 457      45.200 -11.859  16.428  1.00 96.73           O
ANISOU 2921  O   ASP A 457    14351   6953  15449   1821  -1338    852       O
ATOM   2922  CB  ASP A 457      44.023 -10.595  14.081  1.00 88.21           C
ANISOU 2922  CB  ASP A 457    12776   6164  14576   1553  -1052    724       C
ATOM   2923  CG  ASP A 457      42.893  -9.773  14.665  1.00 91.81           C
ANISOU 2923  CG  ASP A 457    13434   6636  14814   1608   -919    761       C
ATOM   2924  OD1 ASP A 457      43.173  -8.827  15.421  1.00 91.42           O
ANISOU 2924  OD1 ASP A 457    13594   6546  14594   1690  -1082    757       O
ATOM   2925  OD2 ASP A 457      41.731 -10.074  14.363  1.00 97.58           O
ANISOU 2925  OD2 ASP A 457    14110   7408  15556   1571   -655    793       O
ATOM   2926  N   SER A 458      46.347  -9.954  16.861  1.00 94.00           N
ANISOU 2926  N   SER A 458    14116   6585  15015   1865  -1773    755       N
ATOM   2927  CA  SER A 458      46.687 -10.238  18.254  1.00 95.62           C
ANISOU 2927  CA  SER A 458    14678   6629  15023   2031  -1941    818       C
ATOM   2928  C   SER A 458      46.593  -8.934  19.078  1.00100.63           C
ANISOU 2928  C   SER A 458    15593   7226  15414   2124  -2088    805       C
ATOM   2929  O   SER A 458      46.587  -7.856  18.477  1.00 97.10           O
ANISOU 2929  O   SER A 458    15002   6875  15016   2046  -2122    733       O
ATOM   2930  CB  SER A 458      48.103 -10.800  18.330  1.00 99.36           C
ANISOU 2930  CB  SER A 458    15068   7006  15677   2046  -2238    789       C
ATOM   2931  OG  SER A 458      48.210 -11.977  17.550  1.00112.30           O
ANISOU 2931  OG  SER A 458    16434   8682  17553   1952  -2102    794       O
ATOM   2932  N   PRO A 459      46.527  -8.989  20.437  1.00100.88           N
ANISOU 2932  N   PRO A 459    16040   7113  15179   2295  -2179    872       N
ATOM   2933  CA  PRO A 459      46.476  -7.742  21.212  1.00101.55           C
ANISOU 2933  CA  PRO A 459    16407   7151  15026   2386  -2332    854       C
ATOM   2934  C   PRO A 459      47.776  -6.958  21.105  1.00107.45           C
ANISOU 2934  C   PRO A 459    17059   7867  15899   2371  -2730    755       C
ATOM   2935  O   PRO A 459      48.866  -7.517  21.271  1.00107.52           O
ANISOU 2935  O   PRO A 459    17035   7775  16041   2401  -2990    738       O
ATOM   2936  CB  PRO A 459      46.212  -8.219  22.650  1.00105.46           C
ANISOU 2936  CB  PRO A 459    17379   7472  15219   2579  -2334    953       C
ATOM   2937  CG  PRO A 459      45.798  -9.639  22.536  1.00110.05           C
ANISOU 2937  CG  PRO A 459    17903   8038  15874   2574  -2091   1032       C
ATOM   2938  CD  PRO A 459      46.517 -10.160  21.337  1.00104.12           C
ANISOU 2938  CD  PRO A 459    16701   7382  15476   2419  -2151    966       C
ATOM   2939  N   ILE A 460      47.646  -5.655  20.834  1.00105.45           N
ANISOU 2939  N   ILE A 460    16757   7690  15618   2325  -2775    690       N
ATOM   2940  CA  ILE A 460      48.794  -4.771  20.689  1.00106.07           C
ANISOU 2940  CA  ILE A 460    16724   7742  15838   2302  -3128    591       C
ATOM   2941  C   ILE A 460      48.912  -3.726  21.813  1.00113.57           C
ANISOU 2941  C   ILE A 460    18042   8582  16528   2437  -3376    576       C
ATOM   2942  O   ILE A 460      48.257  -2.684  21.785  1.00112.01           O
ANISOU 2942  O   ILE A 460    17890   8458  16212   2418  -3299    551       O
ATOM   2943  CB  ILE A 460      48.969  -4.253  19.225  1.00106.63           C
ANISOU 2943  CB  ILE A 460    16340   7970  16203   2118  -3049    506       C
ATOM   2944  CG1 ILE A 460      50.295  -3.499  18.995  1.00107.30           C
ANISOU 2944  CG1 ILE A 460    16260   8001  16507   2089  -3401    407       C
ATOM   2945  CG2 ILE A 460      47.743  -3.527  18.678  1.00104.78           C
ANISOU 2945  CG2 ILE A 460    16049   7892  15871   2044  -2749    507       C
ATOM   2946  CD1 ILE A 460      51.453  -4.418  18.594  1.00112.29           C
ANISOU 2946  CD1 ILE A 460    16652   8561  17454   2049  -3553    386       C
ATOM   2947  N   THR A 461      49.728  -4.060  22.833  1.00114.06           N
ANISOU 2947  N   THR A 461    18381   8457  16498   2579  -3682    592       N
ATOM   2948  CA  THR A 461      50.021  -3.204  23.988  1.00116.33           C
ANISOU 2948  CA  THR A 461    19059   8599  16542   2728  -3986    573       C
ATOM   2949  C   THR A 461      51.007  -2.112  23.560  1.00121.36           C
ANISOU 2949  C   THR A 461    19473   9242  17398   2661  -4303    453       C
ATOM   2950  O   THR A 461      50.922  -0.981  24.048  1.00122.10           O
ANISOU 2950  O   THR A 461    19767   9304  17321   2717  -4437    416       O
ATOM   2951  CB  THR A 461      50.552  -4.029  25.193  1.00127.82           C
ANISOU 2951  CB  THR A 461    20876   9839  17850   2902  -4229    625       C
ATOM   2952  OG1 THR A 461      50.986  -5.343  24.793  1.00124.51           O
ANISOU 2952  OG1 THR A 461    20241   9414  17653   2856  -4179    657       O
ATOM   2953  CG2 THR A 461      49.534  -4.135  26.316  1.00129.07           C
ANISOU 2953  CG2 THR A 461    21553   9908  17580   3066  -4061    724       C
ATOM   2954  N   ILE A 462      51.910  -2.459  22.604  1.00117.71           N
ANISOU 2954  N   ILE A 462    18585   8814  17324   2538  -4392    395       N
ATOM   2955  CA  ILE A 462      52.974  -1.624  22.025  1.00117.58           C
ANISOU 2955  CA  ILE A 462    18275   8789  17612   2456  -4660    285       C
ATOM   2956  C   ILE A 462      52.525  -0.176  21.723  1.00121.23           C
ANISOU 2956  C   ILE A 462    18705   9355  18002   2405  -4604    228       C
ATOM   2957  O   ILE A 462      51.577   0.067  20.968  1.00118.60           O
ANISOU 2957  O   ILE A 462    18231   9198  17634   2306  -4258    243       O
ATOM   2958  CB  ILE A 462      53.813  -2.333  20.896  1.00119.59           C
ANISOU 2958  CB  ILE A 462    18064   9074  18300   2321  -4647    251       C
ATOM   2959  CG1 ILE A 462      54.118  -3.834  21.254  1.00120.63           C
ANISOU 2959  CG1 ILE A 462    18258   9107  18468   2380  -4668    320       C
ATOM   2960  CG2 ILE A 462      55.118  -1.553  20.606  1.00121.16           C
ANISOU 2960  CG2 ILE A 462    18027   9182  18827   2282  -4996    145       C
ATOM   2961  CD1 ILE A 462      54.793  -4.745  20.150  1.00122.17           C
ANISOU 2961  CD1 ILE A 462    18021   9334  19064   2251  -4587    305       C
ATOM   2962  N   GLY A 463      53.187   0.752  22.399  1.00119.75           N
ANISOU 2962  N   GLY A 463    18673   9044  17782   2483  -4964    164       N
ATOM   2963  CA  GLY A 463      52.883   2.171  22.344  1.00118.96           C
ANISOU 2963  CA  GLY A 463    18604   9004  17592   2463  -4981    107       C
ATOM   2964  C   GLY A 463      52.114   2.562  23.589  1.00124.35           C
ANISOU 2964  C   GLY A 463    19803   9612  17832   2621  -5005    156       C
ATOM   2965  O   GLY A 463      51.457   3.611  23.602  1.00123.59           O
ANISOU 2965  O   GLY A 463    19800   9587  17571   2615  -4913    137       O
ATOM   2966  N   LYS A 464      52.181   1.688  24.644  1.00121.95           N
ANISOU 2966  N   LYS A 464    19854   9155  17328   2770  -5117    223       N
ATOM   2967  CA  LYS A 464      51.510   1.812  25.951  1.00123.47           C
ANISOU 2967  CA  LYS A 464    20604   9234  17077   2949  -5129    286       C
ATOM   2968  C   LYS A 464      50.095   2.437  25.859  1.00127.68           C
ANISOU 2968  C   LYS A 464    21254   9908  17351   2928  -4729    334       C
ATOM   2969  O   LYS A 464      49.655   3.225  26.698  1.00127.47           O
ANISOU 2969  O   LYS A 464    21587   9819  17028   3032  -4775    337       O
ATOM   2970  CB  LYS A 464      52.417   2.459  27.008  1.00127.78           C
ANISOU 2970  CB  LYS A 464    21458   9565  17528   3092  -5631    222       C
ATOM   2971  CG  LYS A 464      53.550   1.546  27.492  1.00134.26           C
ANISOU 2971  CG  LYS A 464    22344  10192  18478   3179  -5994    218       C
ATOM   2972  CD  LYS A 464      54.257   2.120  28.717  1.00136.66           C
ANISOU 2972  CD  LYS A 464    23066  10256  18602   3355  -6484    169       C
ATOM   2973  CE  LYS A 464      55.757   2.146  28.571  1.00133.12           C
ANISOU 2973  CE  LYS A 464    22377   9664  18540   3340  -6967     73       C
ATOM   2974  NZ  LYS A 464      56.380   3.056  29.564  1.00133.66           N
ANISOU 2974  NZ  LYS A 464    22781   9523  18479   3481  -7452     -3       N
ATOM   2975  N   TRP A 465      49.407   2.030  24.786  1.00123.91           N
ANISOU 2975  N   TRP A 465    20454   9613  17012   2789  -4339    370       N
ATOM   2976  CA  TRP A 465      48.062   2.342  24.324  1.00122.37           C
ANISOU 2976  CA  TRP A 465    20217   9579  16699   2721  -3910    417       C
ATOM   2977  C   TRP A 465      47.644   1.033  23.647  1.00125.30           C
ANISOU 2977  C   TRP A 465    20351  10037  17219   2639  -3608    481       C
ATOM   2978  O   TRP A 465      48.360   0.540  22.765  1.00124.08           O
ANISOU 2978  O   TRP A 465    19830   9932  17384   2531  -3676    438       O
ATOM   2979  CB  TRP A 465      48.130   3.501  23.320  1.00119.50           C
ANISOU 2979  CB  TRP A 465    19519   9362  16522   2580  -3905    325       C
ATOM   2980  CG  TRP A 465      47.007   3.601  22.329  1.00118.34           C
ANISOU 2980  CG  TRP A 465    19129   9413  16421   2451  -3486    351       C
ATOM   2981  CD1 TRP A 465      45.794   4.190  22.528  1.00120.99           C
ANISOU 2981  CD1 TRP A 465    19638   9808  16525   2471  -3214    398       C
ATOM   2982  CD2 TRP A 465      47.064   3.264  20.935  1.00115.92           C
ANISOU 2982  CD2 TRP A 465    18357   9261  16426   2279  -3321    321       C
ATOM   2983  NE1 TRP A 465      45.077   4.214  21.354  1.00118.26           N
ANISOU 2983  NE1 TRP A 465    18954   9643  16337   2323  -2907    397       N
ATOM   2984  CE2 TRP A 465      45.829   3.641  20.360  1.00118.35           C
ANISOU 2984  CE2 TRP A 465    18584   9715  16667   2206  -2967    349       C
ATOM   2985  CE3 TRP A 465      48.033   2.659  20.116  1.00116.45           C
ANISOU 2985  CE3 TRP A 465    18076   9343  16825   2185  -3434    273       C
ATOM   2986  CZ2 TRP A 465      45.531   3.422  19.008  1.00115.18           C
ANISOU 2986  CZ2 TRP A 465    17789   9474  16501   2048  -2745    328       C
ATOM   2987  CZ3 TRP A 465      47.740   2.453  18.774  1.00115.70           C
ANISOU 2987  CZ3 TRP A 465    17600   9407  16954   2028  -3191    255       C
ATOM   2988  CH2 TRP A 465      46.503   2.836  18.232  1.00114.67           C
ANISOU 2988  CH2 TRP A 465    17416   9420  16733   1963  -2862    279       C
ATOM   2989  N   THR A 466      46.548   0.428  24.123  1.00121.70           N
ANISOU 2989  N   THR A 466    20124   9575  16541   2702  -3285    585       N
ATOM   2990  CA  THR A 466      46.077  -0.854  23.618  1.00120.22           C
ANISOU 2990  CA  THR A 466    19755   9447  16478   2642  -3002    651       C
ATOM   2991  C   THR A 466      44.801  -0.685  22.757  1.00119.86           C
ANISOU 2991  C   THR A 466    19507   9570  16465   2528  -2573    682       C
ATOM   2992  O   THR A 466      43.695  -0.650  23.311  1.00119.67           O
ANISOU 2992  O   THR A 466    19740   9515  16214   2602  -2307    764       O
ATOM   2993  CB  THR A 466      45.971  -1.906  24.767  1.00135.37           C
ANISOU 2993  CB  THR A 466    22057  11190  18187   2806  -3006    747       C
ATOM   2994  OG1 THR A 466      47.088  -1.799  25.646  1.00140.47           O
ANISOU 2994  OG1 THR A 466    22923  11669  18781   2920  -3444    708       O
ATOM   2995  CG2 THR A 466      45.919  -3.333  24.260  1.00133.28           C
ANISOU 2995  CG2 THR A 466    21581  10959  18101   2748  -2806    802       C
ATOM   2996  N   PRO A 467      44.917  -0.574  21.407  1.00112.52           N
ANISOU 2996  N   PRO A 467    18127   8804  15821   2354  -2501    617       N
ATOM   2997  CA  PRO A 467      43.694  -0.476  20.588  1.00109.91           C
ANISOU 2997  CA  PRO A 467    17609   8619  15531   2251  -2124    642       C
ATOM   2998  C   PRO A 467      42.931  -1.801  20.550  1.00112.13           C
ANISOU 2998  C   PRO A 467    17879   8892  15835   2253  -1826    734       C
ATOM   2999  O   PRO A 467      43.543  -2.881  20.498  1.00111.75           O
ANISOU 2999  O   PRO A 467    17751   8797  15910   2252  -1897    747       O
ATOM   3000  CB  PRO A 467      44.212  -0.093  19.200  1.00109.63           C
ANISOU 3000  CB  PRO A 467    17131   8731  15793   2081  -2178    544       C
ATOM   3001  CG  PRO A 467      45.610  -0.562  19.170  1.00114.59           C
ANISOU 3001  CG  PRO A 467    17652   9287  16599   2080  -2485    496       C
ATOM   3002  CD  PRO A 467      46.137  -0.588  20.566  1.00112.68           C
ANISOU 3002  CD  PRO A 467    17802   8865  16144   2249  -2748    521       C
ATOM   3003  N   LYS A 468      41.595  -1.718  20.602  1.00106.88           N
ANISOU 3003  N   LYS A 468    17289   8258  15064   2257  -1491    799       N
ATOM   3004  CA  LYS A 468      40.742  -2.900  20.579  1.00106.08           C
ANISOU 3004  CA  LYS A 468    17172   8136  14998   2260  -1179    888       C
ATOM   3005  C   LYS A 468      39.883  -2.973  19.314  1.00107.02           C
ANISOU 3005  C   LYS A 468    16920   8408  15334   2103   -915    868       C
ATOM   3006  O   LYS A 468      39.368  -1.947  18.854  1.00105.14           O
ANISOU 3006  O   LYS A 468    16593   8261  15095   2043   -850    830       O
ATOM   3007  CB  LYS A 468      39.880  -2.976  21.850  1.00109.75           C
ANISOU 3007  CB  LYS A 468    18068   8455  15176   2421   -988    997       C
ATOM   3008  CG  LYS A 468      40.567  -3.673  23.022  1.00118.11           C
ANISOU 3008  CG  LYS A 468    19489   9333  16053   2584  -1165   1049       C
ATOM   3009  CD  LYS A 468      40.145  -5.147  23.151  1.00127.55           C
ANISOU 3009  CD  LYS A 468    20700  10460  17304   2616   -946   1140       C
ATOM   3010  CE  LYS A 468      39.255  -5.403  24.343  1.00130.30           C
ANISOU 3010  CE  LYS A 468    21470  10646  17391   2777   -683   1264       C
ATOM   3011  NZ  LYS A 468      39.048  -6.853  24.571  1.00129.01           N
ANISOU 3011  NZ  LYS A 468    21352  10393  17274   2825   -517   1350       N
ATOM   3012  N   ASN A 469      39.733  -4.201  18.765  1.00102.11           N
ANISOU 3012  N   ASN A 469    16095   7806  14897   2041   -776    892       N
ATOM   3013  CA  ASN A 469      38.923  -4.478  17.577  1.00 99.62           C
ANISOU 3013  CA  ASN A 469    15440   7611  14799   1900   -543    874       C
ATOM   3014  C   ASN A 469      37.434  -4.311  17.865  1.00104.28           C
ANISOU 3014  C   ASN A 469    16128   8179  15317   1928   -214    948       C
ATOM   3015  O   ASN A 469      37.009  -4.436  19.013  1.00105.42           O
ANISOU 3015  O   ASN A 469    16601   8191  15262   2063   -102   1037       O
ATOM   3016  CB  ASN A 469      39.215  -5.868  17.033  1.00 96.51           C
ANISOU 3016  CB  ASN A 469    14848   7217  14606   1846   -499    884       C
ATOM   3017  CG  ASN A 469      40.657  -6.092  16.645  1.00108.38           C
ANISOU 3017  CG  ASN A 469    16211   8735  16232   1806   -792    813       C
ATOM   3018  OD1 ASN A 469      41.402  -5.159  16.311  1.00 99.31           O
ANISOU 3018  OD1 ASN A 469    14983   7641  15112   1766  -1011    732       O
ATOM   3019  ND2 ASN A 469      41.082  -7.349  16.681  1.00 94.67           N
ANISOU 3019  ND2 ASN A 469    14436   6943  14593   1817   -793    845       N
ATOM   3020  N   SER A 470      36.656  -4.005  16.814  1.00 99.91           N
ANISOU 3020  N   SER A 470    15291   7740  14929   1803    -61    910       N
ATOM   3021  CA  SER A 470      35.210  -3.756  16.816  1.00 99.69           C
ANISOU 3021  CA  SER A 470    15263   7705  14911   1798    241    962       C
ATOM   3022  C   SER A 470      34.389  -4.671  17.753  1.00103.77           C
ANISOU 3022  C   SER A 470    15996   8066  15366   1908    516   1086       C
ATOM   3023  O   SER A 470      33.609  -4.178  18.579  1.00104.07           O
ANISOU 3023  O   SER A 470    16267   8019  15258   1996    692   1155       O
ATOM   3024  CB  SER A 470      34.675  -3.826  15.386  1.00101.94           C
ANISOU 3024  CB  SER A 470    15161   8116  15454   1638    329    899       C
ATOM   3025  OG  SER A 470      35.200  -4.924  14.650  1.00108.34           O
ANISOU 3025  OG  SER A 470    15758   8957  16450   1567    283    870       O
ATOM   3026  N   ASP A 471      34.602  -5.995  17.635  1.00 99.20           N
ANISOU 3026  N   ASP A 471    15346   7444  14902   1905    560   1117       N
ATOM   3027  CA  ASP A 471      33.923  -7.040  18.410  1.00 99.76           C
ANISOU 3027  CA  ASP A 471    15588   7364  14952   2001    824   1234       C
ATOM   3028  C   ASP A 471      34.667  -7.431  19.687  1.00102.89           C
ANISOU 3028  C   ASP A 471    16364   7620  15110   2162    715   1298       C
ATOM   3029  O   ASP A 471      34.284  -8.405  20.346  1.00103.39           O
ANISOU 3029  O   ASP A 471    16585   7551  15150   2250    909   1394       O
ATOM   3030  CB  ASP A 471      33.676  -8.283  17.523  1.00100.87           C
ANISOU 3030  CB  ASP A 471    15419   7535  15372   1901    943   1229       C
ATOM   3031  CG  ASP A 471      34.914  -8.956  16.934  1.00111.55           C
ANISOU 3031  CG  ASP A 471    16609   8953  16820   1840    696   1163       C
ATOM   3032  OD1 ASP A 471      36.007  -8.343  16.972  1.00110.46           O
ANISOU 3032  OD1 ASP A 471    16509   8870  16592   1838    407   1097       O
ATOM   3033  OD2 ASP A 471      34.784 -10.090  16.420  1.00120.83           O
ANISOU 3033  OD2 ASP A 471    17609  10120  18181   1790    796   1175       O
ATOM   3034  N   GLY A 472      35.721  -6.679  20.014  1.00 98.28           N
ANISOU 3034  N   GLY A 472    15922   7056  14362   2200    400   1242       N
ATOM   3035  CA  GLY A 472      36.584  -6.920  21.167  1.00 99.27           C
ANISOU 3035  CA  GLY A 472    16408   7049  14259   2351    212   1281       C
ATOM   3036  C   GLY A 472      37.252  -8.281  21.128  1.00102.39           C
ANISOU 3036  C   GLY A 472    16743   7401  14760   2357    155   1302       C
ATOM   3037  O   GLY A 472      37.620  -8.824  22.176  1.00104.70           O
ANISOU 3037  O   GLY A 472    17361   7541  14878   2502    132   1376       O
ATOM   3038  N   ARG A 473      37.403  -8.844  19.912  1.00 95.11           N
ANISOU 3038  N   ARG A 473    15416   6602  14118   2205    138   1239       N
ATOM   3039  CA  ARG A 473      37.981 -10.165  19.686  1.00 94.37           C
ANISOU 3039  CA  ARG A 473    15207   6483  14166   2187    103   1252       C
ATOM   3040  C   ARG A 473      39.253 -10.089  18.850  1.00 93.80           C
ANISOU 3040  C   ARG A 473    14877   6515  14249   2085   -211   1144       C
ATOM   3041  O   ARG A 473      39.591  -9.026  18.327  1.00 93.01           O
ANISOU 3041  O   ARG A 473    14660   6513  14168   2017   -372   1059       O
ATOM   3042  CB  ARG A 473      36.938 -11.084  19.011  1.00 95.51           C
ANISOU 3042  CB  ARG A 473    15115   6647  14528   2108    431   1290       C
ATOM   3043  CG  ARG A 473      35.728 -11.395  19.889  1.00113.35           C
ANISOU 3043  CG  ARG A 473    17622   8764  16683   2220    771   1413       C
ATOM   3044  CD  ARG A 473      34.506 -11.823  19.092  1.00132.09           C
ANISOU 3044  CD  ARG A 473    19714  11172  19300   2119   1083   1426       C
ATOM   3045  NE  ARG A 473      33.605 -12.669  19.879  1.00151.56           N
ANISOU 3045  NE  ARG A 473    22357  13474  21756   2220   1415   1551       N
ATOM   3046  CZ  ARG A 473      32.523 -13.276  19.397  1.00169.01           C
ANISOU 3046  CZ  ARG A 473    24353  15664  24199   2158   1708   1582       C
ATOM   3047  NH1 ARG A 473      32.183 -13.131  18.121  1.00154.84           N
ANISOU 3047  NH1 ARG A 473    22176  14007  22650   1996   1695   1495       N
ATOM   3048  NH2 ARG A 473      31.770 -14.029  20.188  1.00158.54           N
ANISOU 3048  NH2 ARG A 473    23202  14167  22869   2261   2016   1700       N
ATOM   3049  N   TYR A 474      39.967 -11.212  18.754  1.00 87.91           N
ANISOU 3049  N   TYR A 474    14050   5732  13618   2080   -286   1153       N
ATOM   3050  CA  TYR A 474      41.174 -11.375  17.943  1.00 86.01           C
ANISOU 3050  CA  TYR A 474    13550   5563  13567   1985   -540   1064       C
ATOM   3051  C   TYR A 474      40.978 -12.613  17.063  1.00 89.27           C
ANISOU 3051  C   TYR A 474    13680   6015  14225   1885   -375   1067       C
ATOM   3052  O   TYR A 474      40.011 -13.341  17.276  1.00 90.55           O
ANISOU 3052  O   TYR A 474    13893   6125  14385   1915   -107   1145       O
ATOM   3053  CB  TYR A 474      42.433 -11.459  18.829  1.00 88.06           C
ANISOU 3053  CB  TYR A 474    14031   5710  13720   2096   -860   1066       C
ATOM   3054  CG  TYR A 474      42.596 -10.225  19.689  1.00 89.49           C
ANISOU 3054  CG  TYR A 474    14502   5841  13658   2196  -1036   1056       C
ATOM   3055  CD1 TYR A 474      43.103  -9.045  19.158  1.00 90.77           C
ANISOU 3055  CD1 TYR A 474    14525   6094  13870   2124  -1233    958       C
ATOM   3056  CD2 TYR A 474      42.147 -10.205  21.006  1.00 91.73           C
ANISOU 3056  CD2 TYR A 474    15211   5984  13659   2364   -977   1145       C
ATOM   3057  CE1 TYR A 474      43.169  -7.879  19.918  1.00 93.10           C
ANISOU 3057  CE1 TYR A 474    15082   6345  13946   2211  -1383    946       C
ATOM   3058  CE2 TYR A 474      42.240  -9.055  21.787  1.00 93.36           C
ANISOU 3058  CE2 TYR A 474    15705   6138  13629   2459  -1131   1134       C
ATOM   3059  CZ  TYR A 474      42.751  -7.891  21.239  1.00100.91           C
ANISOU 3059  CZ  TYR A 474    16502   7193  14647   2379  -1340   1032       C
ATOM   3060  OH  TYR A 474      42.847  -6.744  21.995  1.00101.42           O
ANISOU 3060  OH  TYR A 474    16846   7204  14485   2471  -1497   1016       O
ATOM   3061  N   LEU A 475      41.812 -12.831  16.046  1.00 83.43           N
ANISOU 3061  N   LEU A 475    12640   5357  13701   1767   -508    985       N
ATOM   3062  CA  LEU A 475      41.595 -13.978  15.164  1.00 82.19           C
ANISOU 3062  CA  LEU A 475    12227   5235  13768   1672   -348    983       C
ATOM   3063  C   LEU A 475      42.860 -14.779  14.905  1.00 86.77           C
ANISOU 3063  C   LEU A 475    12688   5785  14498   1650   -534    957       C
ATOM   3064  O   LEU A 475      42.780 -15.899  14.401  1.00 85.14           O
ANISOU 3064  O   LEU A 475    12323   5576  14452   1598   -412    971       O
ATOM   3065  CB  LEU A 475      40.956 -13.522  13.831  1.00 80.39           C
ANISOU 3065  CB  LEU A 475    11706   5145  13694   1523   -222    910       C
ATOM   3066  CG  LEU A 475      39.681 -12.665  13.915  1.00 85.06           C
ANISOU 3066  CG  LEU A 475    12368   5771  14178   1528    -47    926       C
ATOM   3067  CD1 LEU A 475      39.494 -11.844  12.674  1.00 83.51           C
ANISOU 3067  CD1 LEU A 475    11923   5711  14097   1396    -58    829       C
ATOM   3068  CD2 LEU A 475      38.453 -13.509  14.190  1.00 89.17           C
ANISOU 3068  CD2 LEU A 475    12936   6227  14718   1561    254   1012       C
ATOM   3069  N   GLY A 476      44.007 -14.192  15.247  1.00 85.32           N
ANISOU 3069  N   GLY A 476    12577   5566  14274   1691   -829    919       N
ATOM   3070  CA  GLY A 476      45.323 -14.776  15.024  1.00 85.70           C
ANISOU 3070  CA  GLY A 476    12503   5568  14489   1673  -1039    888       C
ATOM   3071  C   GLY A 476      45.820 -14.508  13.616  1.00 88.99           C
ANISOU 3071  C   GLY A 476    12575   6091  15147   1521  -1074    789       C
ATOM   3072  O   GLY A 476      45.519 -13.456  13.037  1.00 88.28           O
ANISOU 3072  O   GLY A 476    12403   6094  15046   1458  -1067    729       O
ATOM   3073  N   MET A 477      46.574 -15.460  13.051  1.00 85.63           N
ANISOU 3073  N   MET A 477    11957   5643  14937   1465  -1098    774       N
ATOM   3074  CA  MET A 477      47.091 -15.335  11.698  1.00 84.06           C
ANISOU 3074  CA  MET A 477    11449   5519  14971   1328  -1105    686       C
ATOM   3075  C   MET A 477      45.964 -15.461  10.668  1.00 84.98           C
ANISOU 3075  C   MET A 477    11409   5747  15131   1222   -836    663       C
ATOM   3076  O   MET A 477      45.215 -16.441  10.687  1.00 85.07           O
ANISOU 3076  O   MET A 477    11424   5749  15151   1222   -644    714       O
ATOM   3077  CB  MET A 477      48.211 -16.337  11.445  1.00 87.06           C
ANISOU 3077  CB  MET A 477    11689   5821  15569   1309  -1200    683       C
ATOM   3078  CG  MET A 477      49.296 -15.767  10.609  1.00 90.85           C
ANISOU 3078  CG  MET A 477    11954   6308  16256   1230  -1348    597       C
ATOM   3079  SD  MET A 477      50.246 -14.447  11.400  1.00 97.37           S
ANISOU 3079  SD  MET A 477    12897   7070  17030   1305  -1681    561       S
ATOM   3080  CE  MET A 477      51.938 -14.961  10.939  1.00 95.19           C
ANISOU 3080  CE  MET A 477    12390   6677  17101   1268  -1873    522       C
ATOM   3081  N   ILE A 478      45.808 -14.427   9.826  1.00 78.45           N
ANISOU 3081  N   ILE A 478    10462   5016  14328   1141   -832    588       N
ATOM   3082  CA  ILE A 478      44.792 -14.332   8.768  1.00 76.81           C
ANISOU 3082  CA  ILE A 478    10112   4912  14162   1040   -625    549       C
ATOM   3083  C   ILE A 478      45.406 -13.655   7.533  1.00 82.85           C
ANISOU 3083  C   ILE A 478    10671   5740  15069    934   -681    451       C
ATOM   3084  O   ILE A 478      46.317 -12.847   7.711  1.00 83.30           O
ANISOU 3084  O   ILE A 478    10737   5776  15138    953   -867    418       O
ATOM   3085  CB  ILE A 478      43.484 -13.605   9.226  1.00 78.55           C
ANISOU 3085  CB  ILE A 478    10476   5179  14190   1076   -508    579       C
ATOM   3086  CG1 ILE A 478      43.767 -12.234   9.880  1.00 77.99           C
ANISOU 3086  CG1 ILE A 478    10555   5116  13963   1134   -676    563       C
ATOM   3087  CG2 ILE A 478      42.611 -14.500  10.117  1.00 79.23           C
ANISOU 3087  CG2 ILE A 478    10719   5199  14185   1157   -348    677       C
ATOM   3088  CD1 ILE A 478      42.571 -11.342  10.044  1.00 73.38           C
ANISOU 3088  CD1 ILE A 478    10072   4589  13221   1148   -557    575       C
ATOM   3089  N   PRO A 479      44.966 -13.950   6.279  1.00 79.79           N
ANISOU 3089  N   PRO A 479    10108   5413  14793    829   -531    402       N
ATOM   3090  CA  PRO A 479      45.566 -13.247   5.124  1.00 79.09           C
ANISOU 3090  CA  PRO A 479     9864   5370  14818    742   -571    312       C
ATOM   3091  C   PRO A 479      45.184 -11.774   5.112  1.00 81.09           C
ANISOU 3091  C   PRO A 479    10175   5694  14941    743   -619    276       C
ATOM   3092  O   PRO A 479      44.128 -11.412   5.642  1.00 79.14           O
ANISOU 3092  O   PRO A 479    10048   5486  14538    780   -557    310       O
ATOM   3093  CB  PRO A 479      45.021 -13.989   3.899  1.00 80.49           C
ANISOU 3093  CB  PRO A 479     9898   5582  15102    648   -394    276       C
ATOM   3094  CG  PRO A 479      43.799 -14.672   4.365  1.00 84.74           C
ANISOU 3094  CG  PRO A 479    10510   6126  15561    676   -257    334       C
ATOM   3095  CD  PRO A 479      43.913 -14.895   5.854  1.00 81.21           C
ANISOU 3095  CD  PRO A 479    10238   5613  15004    790   -324    422       C
ATOM   3096  N   LEU A 480      46.067 -10.933   4.534  1.00 77.51           N
ANISOU 3096  N   LEU A 480     9635   5248  14569    705   -721    210       N
ATOM   3097  CA  LEU A 480      45.938  -9.486   4.421  1.00 77.01           C
ANISOU 3097  CA  LEU A 480     9603   5244  14413    700   -782    167       C
ATOM   3098  C   LEU A 480      44.560  -9.038   3.954  1.00 78.74           C
ANISOU 3098  C   LEU A 480     9842   5560  14514    663   -638    153       C
ATOM   3099  O   LEU A 480      44.033  -8.039   4.464  1.00 77.04           O
ANISOU 3099  O   LEU A 480     9735   5387  14149    701   -671    161       O
ATOM   3100  CB  LEU A 480      47.021  -8.956   3.468  1.00 77.31           C
ANISOU 3100  CB  LEU A 480     9493   5264  14616    640   -840     93       C
ATOM   3101  CG  LEU A 480      47.232  -7.455   3.437  1.00 82.53           C
ANISOU 3101  CG  LEU A 480    10175   5963  15220    642   -933     48       C
ATOM   3102  CD1 LEU A 480      48.698  -7.128   3.436  1.00 83.86           C
ANISOU 3102  CD1 LEU A 480    10262   6039  15560    651  -1090     19       C
ATOM   3103  CD2 LEU A 480      46.515  -6.813   2.223  1.00 84.67           C
ANISOU 3103  CD2 LEU A 480    10380   6324  15465    562   -796    -12       C
ATOM   3104  N   ARG A 481      44.000  -9.760   2.967  1.00 74.17           N
ANISOU 3104  N   ARG A 481     9159   5008  14015    591   -489    130       N
ATOM   3105  CA  ARG A 481      42.693  -9.434   2.421  1.00 73.07           C
ANISOU 3105  CA  ARG A 481     9016   4944  13805    551   -368    109       C
ATOM   3106  C   ARG A 481      41.565  -9.577   3.434  1.00 78.11           C
ANISOU 3106  C   ARG A 481     9776   5583  14318    612   -300    182       C
ATOM   3107  O   ARG A 481      40.689  -8.710   3.467  1.00 77.91           O
ANISOU 3107  O   ARG A 481     9795   5613  14195    613   -264    175       O
ATOM   3108  CB  ARG A 481      42.419 -10.136   1.076  1.00 70.96           C
ANISOU 3108  CB  ARG A 481     8618   4684  13658    463   -255     57       C
ATOM   3109  CG  ARG A 481      42.485 -11.641   1.086  1.00 76.65           C
ANISOU 3109  CG  ARG A 481     9293   5344  14487    458   -181     91       C
ATOM   3110  CD  ARG A 481      42.139 -12.178  -0.274  1.00 86.71           C
ANISOU 3110  CD  ARG A 481    10466   6627  15854    374    -81     30       C
ATOM   3111  NE  ARG A 481      41.945 -13.625  -0.219  1.00 99.72           N
ANISOU 3111  NE  ARG A 481    12072   8219  17599    368      2     63       N
ATOM   3112  CZ  ARG A 481      41.136 -14.307  -1.021  1.00110.75           C
ANISOU 3112  CZ  ARG A 481    13410   9611  19059    316     99     33       C
ATOM   3113  NH1 ARG A 481      40.439 -13.682  -1.963  1.00 87.92           N
ANISOU 3113  NH1 ARG A 481    10502   6765  16140    267    116    -33       N
ATOM   3114  NH2 ARG A 481      41.029 -15.625  -0.899  1.00101.93           N
ANISOU 3114  NH2 ARG A 481    12253   8437  18038    315    170     66       N
ATOM   3115  N   ARG A 482      41.624 -10.617   4.303  1.00 75.83           N
ANISOU 3115  N   ARG A 482     9551   5225  14035    671   -277    255       N
ATOM   3116  CA  ARG A 482      40.614 -10.884   5.339  1.00 76.51           C
ANISOU 3116  CA  ARG A 482     9773   5285  14015    743   -182    336       C
ATOM   3117  C   ARG A 482      40.640  -9.757   6.367  1.00 80.03           C
ANISOU 3117  C   ARG A 482    10395   5731  14280    825   -275    366       C
ATOM   3118  O   ARG A 482      39.591  -9.207   6.715  1.00 79.16           O
ANISOU 3118  O   ARG A 482    10366   5643  14068    849   -187    392       O
ATOM   3119  CB  ARG A 482      40.868 -12.254   6.007  1.00 79.65           C
ANISOU 3119  CB  ARG A 482    10208   5593  14461    792   -142    406       C
ATOM   3120  CG  ARG A 482      39.676 -13.212   5.958  1.00 90.11           C
ANISOU 3120  CG  ARG A 482    11508   6893  15837    785     56    450       C
ATOM   3121  CD  ARG A 482      40.013 -14.567   5.319  1.00 94.46           C
ANISOU 3121  CD  ARG A 482    11924   7408  16559    734    112    441       C
ATOM   3122  NE  ARG A 482      39.950 -14.536   3.850  1.00 91.61           N
ANISOU 3122  NE  ARG A 482    11386   7100  16320    623    127    349       N
ATOM   3123  CZ  ARG A 482      39.793 -15.599   3.060  1.00 93.91           C
ANISOU 3123  CZ  ARG A 482    11555   7369  16758    563    209    325       C
ATOM   3124  NH1 ARG A 482      39.668 -16.815   3.583  1.00 82.95           N
ANISOU 3124  NH1 ARG A 482    10176   5910  15430    596    293    389       N
ATOM   3125  NH2 ARG A 482      39.741 -15.452   1.746  1.00 71.21           N
ANISOU 3125  NH2 ARG A 482     8561   4533  13962    474    210    238       N
ATOM   3126  N   ALA A 483      41.867  -9.367   6.771  1.00 76.52           N
ANISOU 3126  N   ALA A 483    10001   5257  13818    863   -460    354       N
ATOM   3127  CA  ALA A 483      42.191  -8.304   7.726  1.00 76.13           C
ANISOU 3127  CA  ALA A 483    10122   5192  13611    943   -602    369       C
ATOM   3128  C   ALA A 483      41.591  -6.979   7.320  1.00 78.61           C
ANISOU 3128  C   ALA A 483    10427   5593  13849    908   -585    322       C
ATOM   3129  O   ALA A 483      41.094  -6.237   8.170  1.00 78.51           O
ANISOU 3129  O   ALA A 483    10583   5577  13671    976   -590    358       O
ATOM   3130  CB  ALA A 483      43.692  -8.164   7.823  1.00 77.26           C
ANISOU 3130  CB  ALA A 483    10240   5285  13830    958   -817    337       C
ATOM   3131  N   LEU A 484      41.649  -6.681   6.011  1.00 73.42           N
ANISOU 3131  N   LEU A 484     9585   5004  13306    806   -561    245       N
ATOM   3132  CA  LEU A 484      41.117  -5.466   5.446  1.00 71.84           C
ANISOU 3132  CA  LEU A 484     9358   4887  13053    765   -544    194       C
ATOM   3133  C   LEU A 484      39.616  -5.544   5.475  1.00 77.86           C
ANISOU 3133  C   LEU A 484    10147   5677  13759    761   -373    229       C
ATOM   3134  O   LEU A 484      38.993  -4.612   5.971  1.00 79.10           O
ANISOU 3134  O   LEU A 484    10410   5858  13788    798   -359    246       O
ATOM   3135  CB  LEU A 484      41.644  -5.244   4.012  1.00 70.64           C
ANISOU 3135  CB  LEU A 484     9023   4779  13037    666   -557    106       C
ATOM   3136  CG  LEU A 484      41.255  -3.946   3.309  1.00 74.27           C
ANISOU 3136  CG  LEU A 484     9454   5319  13446    623   -556     46       C
ATOM   3137  CD1 LEU A 484      41.484  -2.766   4.210  1.00 75.22           C
ANISOU 3137  CD1 LEU A 484     9703   5445  13433    688   -672     58       C
ATOM   3138  CD2 LEU A 484      42.058  -3.721   2.081  1.00 74.53           C
ANISOU 3138  CD2 LEU A 484     9351   5365  13601    551   -581    -32       C
ATOM   3139  N   TYR A 485      39.036  -6.651   4.982  1.00 73.89           N
ANISOU 3139  N   TYR A 485     9551   5159  13366    721   -242    240       N
ATOM   3140  CA  TYR A 485      37.591  -6.820   4.970  1.00 73.34           C
ANISOU 3140  CA  TYR A 485     9477   5093  13295    714    -78    271       C
ATOM   3141  C   TYR A 485      36.947  -6.693   6.354  1.00 77.68           C
ANISOU 3141  C   TYR A 485    10215   5588  13710    815     -7    363       C
ATOM   3142  O   TYR A 485      35.977  -5.945   6.484  1.00 80.11           O
ANISOU 3142  O   TYR A 485    10560   5916  13961    823     72    375       O
ATOM   3143  CB  TYR A 485      37.170  -8.116   4.254  1.00 74.55           C
ANISOU 3143  CB  TYR A 485     9496   5219  13610    658     31    266       C
ATOM   3144  CG  TYR A 485      35.684  -8.387   4.335  1.00 76.98           C
ANISOU 3144  CG  TYR A 485     9787   5504  13959    657    196    302       C
ATOM   3145  CD1 TYR A 485      34.760  -7.500   3.787  1.00 77.75           C
ANISOU 3145  CD1 TYR A 485     9834   5651  14057    617    225    263       C
ATOM   3146  CD2 TYR A 485      35.198  -9.533   4.958  1.00 79.54           C
ANISOU 3146  CD2 TYR A 485    10136   5744  14341    698    325    377       C
ATOM   3147  CE1 TYR A 485      33.391  -7.728   3.888  1.00 79.44           C
ANISOU 3147  CE1 TYR A 485    10014   5824  14346    617    371    297       C
ATOM   3148  CE2 TYR A 485      33.828  -9.785   5.045  1.00 81.03           C
ANISOU 3148  CE2 TYR A 485    10290   5890  14606    698    489    413       C
ATOM   3149  CZ  TYR A 485      32.927  -8.878   4.514  1.00 86.55           C
ANISOU 3149  CZ  TYR A 485    10929   6632  15324    657    507    372       C
ATOM   3150  OH  TYR A 485      31.575  -9.124   4.607  1.00 86.05           O
ANISOU 3150  OH  TYR A 485    10813   6508  15374    657    664    408       O
ATOM   3151  N   LEU A 486      37.481  -7.370   7.380  1.00 72.51           N
ANISOU 3151  N   LEU A 486     9693   4855  13002    897    -32    429       N
ATOM   3152  CA  LEU A 486      36.897  -7.291   8.723  1.00 73.23           C
ANISOU 3152  CA  LEU A 486    10006   4874  12945   1008     50    522       C
ATOM   3153  C   LEU A 486      37.310  -6.034   9.503  1.00 80.60           C
ANISOU 3153  C   LEU A 486    11124   5814  13688   1077    -83    523       C
ATOM   3154  O   LEU A 486      36.793  -5.775  10.604  1.00 81.08           O
ANISOU 3154  O   LEU A 486    11401   5810  13596   1175    -14    596       O
ATOM   3155  CB  LEU A 486      37.180  -8.562   9.538  1.00 73.73           C
ANISOU 3155  CB  LEU A 486    10168   4834  13012   1080     95    600       C
ATOM   3156  CG  LEU A 486      36.801  -9.919   8.937  1.00 76.57           C
ANISOU 3156  CG  LEU A 486    10364   5170  13558   1023    228    607       C
ATOM   3157  CD1 LEU A 486      37.235 -11.026   9.845  1.00 77.49           C
ANISOU 3157  CD1 LEU A 486    10600   5186  13657   1104    241    682       C
ATOM   3158  CD2 LEU A 486      35.312 -10.039   8.696  1.00 75.22           C
ANISOU 3158  CD2 LEU A 486    10130   4986  13465    999    446    633       C
ATOM   3159  N   SER A 487      38.213  -5.235   8.898  1.00 78.65           N
ANISOU 3159  N   SER A 487    10793   5634  13455   1027   -261    441       N
ATOM   3160  CA  SER A 487      38.785  -3.995   9.436  1.00 79.03           C
ANISOU 3160  CA  SER A 487    10973   5694  13360   1075   -423    420       C
ATOM   3161  C   SER A 487      39.369  -4.224  10.849  1.00 86.22           C
ANISOU 3161  C   SER A 487    12137   6497  14125   1203   -528    485       C
ATOM   3162  O   SER A 487      38.933  -3.616  11.849  1.00 87.40           O
ANISOU 3162  O   SER A 487    12514   6604  14089   1293   -515    532       O
ATOM   3163  CB  SER A 487      37.781  -2.848   9.384  1.00 80.17           C
ANISOU 3163  CB  SER A 487    11153   5893  13414   1068   -336    415       C
ATOM   3164  OG  SER A 487      37.201  -2.700   8.100  1.00 82.03           O
ANISOU 3164  OG  SER A 487    11174   6212  13780    959   -251    357       O
ATOM   3165  N   ARG A 488      40.332  -5.173  10.915  1.00 82.47           N
ANISOU 3165  N   ARG A 488    11631   5967  13737   1214   -628    490       N
ATOM   3166  CA  ARG A 488      40.997  -5.544  12.156  1.00 82.98           C
ANISOU 3166  CA  ARG A 488    11927   5917  13685   1335   -757    546       C
ATOM   3167  C   ARG A 488      42.023  -4.479  12.506  1.00 85.06           C
ANISOU 3167  C   ARG A 488    12267   6168  13885   1369  -1023    494       C
ATOM   3168  O   ARG A 488      43.064  -4.371  11.851  1.00 82.38           O
ANISOU 3168  O   ARG A 488    11752   5848  13702   1307  -1178    425       O
ATOM   3169  CB  ARG A 488      41.602  -6.972  12.096  1.00 82.42           C
ANISOU 3169  CB  ARG A 488    11788   5783  13744   1335   -767    572       C
ATOM   3170  CG  ARG A 488      40.672  -8.072  11.580  1.00 87.55           C
ANISOU 3170  CG  ARG A 488    12313   6449  14505   1282   -516    607       C
ATOM   3171  CD  ARG A 488      39.328  -8.155  12.309  1.00 91.39           C
ANISOU 3171  CD  ARG A 488    12966   6893  14864   1348   -290    691       C
ATOM   3172  NE  ARG A 488      39.436  -8.657  13.678  1.00 88.36           N
ANISOU 3172  NE  ARG A 488    12872   6380  14321   1489   -294    783       N
ATOM   3173  CZ  ARG A 488      38.436  -8.665  14.552  1.00 94.87           C
ANISOU 3173  CZ  ARG A 488    13910   7133  15004   1578   -105    869       C
ATOM   3174  NH1 ARG A 488      37.245  -8.184  14.216  1.00 79.96           N
ANISOU 3174  NH1 ARG A 488    11956   5289  13137   1536     97    874       N
ATOM   3175  NH2 ARG A 488      38.620  -9.144  15.771  1.00 76.56           N
ANISOU 3175  NH2 ARG A 488    11880   4683  12526   1715   -113    951       N
ATOM   3176  N   ASN A 489      41.663  -3.635  13.497  1.00 82.35           N
ANISOU 3176  N   ASN A 489    12182   5785  13323   1465  -1059    526       N
ATOM   3177  CA  ASN A 489      42.427  -2.499  14.005  1.00 82.13           C
ANISOU 3177  CA  ASN A 489    12276   5732  13198   1515  -1305    483       C
ATOM   3178  C   ASN A 489      43.856  -2.836  14.441  1.00 89.25           C
ANISOU 3178  C   ASN A 489    13208   6535  14166   1563  -1590    461       C
ATOM   3179  O   ASN A 489      44.766  -2.024  14.231  1.00 88.78           O
ANISOU 3179  O   ASN A 489    13069   6479  14184   1539  -1806    388       O
ATOM   3180  CB  ASN A 489      41.662  -1.837  15.138  1.00 82.08           C
ANISOU 3180  CB  ASN A 489    12592   5672  12924   1629  -1256    541       C
ATOM   3181  CG  ASN A 489      40.364  -1.184  14.713  1.00101.64           C
ANISOU 3181  CG  ASN A 489    15025   8237  15355   1581  -1014    550       C
ATOM   3182  OD1 ASN A 489      40.185  -0.710  13.575  1.00 94.28           O
ANISOU 3182  OD1 ASN A 489    13841   7421  14559   1464   -966    486       O
ATOM   3183  ND2 ASN A 489      39.448  -1.083  15.658  1.00 93.19           N
ANISOU 3183  ND2 ASN A 489    14219   7099  14090   1679   -863    630       N
ATOM   3184  N   THR A 490      44.059  -4.047  15.009  1.00 87.32           N
ANISOU 3184  N   THR A 490    13067   6196  13915   1629  -1588    524       N
ATOM   3185  CA  THR A 490      45.358  -4.521  15.491  1.00 87.88           C
ANISOU 3185  CA  THR A 490    13179   6154  14057   1685  -1857    515       C
ATOM   3186  C   THR A 490      46.328  -4.833  14.354  1.00 90.20           C
ANISOU 3186  C   THR A 490    13132   6486  14655   1568  -1937    444       C
ATOM   3187  O   THR A 490      47.544  -4.670  14.523  1.00 89.97           O
ANISOU 3187  O   THR A 490    13068   6378  14739   1588  -2205    401       O
ATOM   3188  CB  THR A 490      45.174  -5.697  16.433  1.00 97.70           C
ANISOU 3188  CB  THR A 490    14643   7285  15192   1792  -1803    609       C
ATOM   3189  OG1 THR A 490      44.413  -6.688  15.755  1.00101.51           O
ANISOU 3189  OG1 THR A 490    14959   7830  15780   1718  -1521    645       O
ATOM   3190  CG2 THR A 490      44.480  -5.307  17.733  1.00 94.82           C
ANISOU 3190  CG2 THR A 490    14677   6837  14512   1936  -1769    680       C
ATOM   3191  N   VAL A 491      45.802  -5.298  13.206  1.00 85.43           N
ANISOU 3191  N   VAL A 491    12282   5984  14193   1452  -1708    431       N
ATOM   3192  CA  VAL A 491      46.642  -5.582  12.040  1.00 84.60           C
ANISOU 3192  CA  VAL A 491    11869   5910  14366   1341  -1741    365       C
ATOM   3193  C   VAL A 491      47.073  -4.262  11.386  1.00 87.94           C
ANISOU 3193  C   VAL A 491    12161   6391  14862   1277  -1838    279       C
ATOM   3194  O   VAL A 491      48.215  -4.131  10.944  1.00 87.84           O
ANISOU 3194  O   VAL A 491    11986   6336  15054   1240  -1993    223       O
ATOM   3195  CB  VAL A 491      46.077  -6.642  11.051  1.00 87.43           C
ANISOU 3195  CB  VAL A 491    12033   6332  14853   1248  -1492    377       C
ATOM   3196  CG1 VAL A 491      44.577  -6.591  10.927  1.00 86.83           C
ANISOU 3196  CG1 VAL A 491    12004   6340  14646   1229  -1239    410       C
ATOM   3197  CG2 VAL A 491      46.747  -6.551   9.691  1.00 86.04           C
ANISOU 3197  CG2 VAL A 491    11564   6202  14926   1128  -1492    298       C
ATOM   3198  N   SER A 492      46.180  -3.269  11.406  1.00 83.94           N
ANISOU 3198  N   SER A 492    11736   5964  14194   1275  -1751    272       N
ATOM   3199  CA  SER A 492      46.436  -1.935  10.874  1.00 83.28           C
ANISOU 3199  CA  SER A 492    11559   5938  14146   1225  -1826    197       C
ATOM   3200  C   SER A 492      47.615  -1.276  11.585  1.00 89.67           C
ANISOU 3200  C   SER A 492    12446   6643  14983   1293  -2133    163       C
ATOM   3201  O   SER A 492      48.540  -0.832  10.912  1.00 91.19           O
ANISOU 3201  O   SER A 492    12443   6823  15382   1234  -2240     95       O
ATOM   3202  CB  SER A 492      45.192  -1.061  10.968  1.00 85.14           C
ANISOU 3202  CB  SER A 492    11904   6263  14182   1228  -1679    209       C
ATOM   3203  OG  SER A 492      44.143  -1.628  10.203  1.00 94.67           O
ANISOU 3203  OG  SER A 492    13011   7553  15407   1160  -1417    231       O
ATOM   3204  N   VAL A 493      47.627  -1.289  12.933  1.00 85.84           N
ANISOU 3204  N   VAL A 493    12247   6062  14306   1420  -2278    211       N
ATOM   3205  CA  VAL A 493      48.710  -0.727  13.758  1.00 85.91           C
ANISOU 3205  CA  VAL A 493    12371   5946  14326   1502  -2609    180       C
ATOM   3206  C   VAL A 493      50.029  -1.492  13.510  1.00 88.84           C
ANISOU 3206  C   VAL A 493    12560   6216  14981   1483  -2781    155       C
ATOM   3207  O   VAL A 493      51.100  -0.877  13.455  1.00 89.69           O
ANISOU 3207  O   VAL A 493    12563   6251  15266   1477  -3012     91       O
ATOM   3208  CB  VAL A 493      48.299  -0.659  15.250  1.00 90.94           C
ANISOU 3208  CB  VAL A 493    13399   6492  14660   1654  -2707    243       C
ATOM   3209  CG1 VAL A 493      49.438  -0.151  16.129  1.00 92.13           C
ANISOU 3209  CG1 VAL A 493    13687   6496  14823   1746  -3086    205       C
ATOM   3210  CG2 VAL A 493      47.070   0.221  15.427  1.00 90.40           C
ANISOU 3210  CG2 VAL A 493    13488   6514  14348   1667  -2528    263       C
ATOM   3211  N   ARG A 494      49.928  -2.816  13.298  1.00 83.50           N
ANISOU 3211  N   ARG A 494    11823   5531  14371   1467  -2651    204       N
ATOM   3212  CA  ARG A 494      51.054  -3.688  12.980  1.00 83.29           C
ANISOU 3212  CA  ARG A 494    11610   5414  14622   1440  -2761    190       C
ATOM   3213  C   ARG A 494      51.621  -3.383  11.588  1.00 86.59           C
ANISOU 3213  C   ARG A 494    11688   5882  15331   1309  -2691    117       C
ATOM   3214  O   ARG A 494      52.835  -3.314  11.419  1.00 86.76           O
ANISOU 3214  O   ARG A 494    11557   5801  15608   1297  -2878     73       O
ATOM   3215  CB  ARG A 494      50.652  -5.157  13.144  1.00 82.09           C
ANISOU 3215  CB  ARG A 494    11501   5249  14439   1458  -2609    266       C
ATOM   3216  CG  ARG A 494      50.809  -5.628  14.579  1.00 93.81           C
ANISOU 3216  CG  ARG A 494    13296   6602  15744   1607  -2789    329       C
ATOM   3217  CD  ARG A 494      50.537  -7.111  14.747  1.00100.46           C
ANISOU 3217  CD  ARG A 494    14171   7414  16585   1629  -2653    404       C
ATOM   3218  NE  ARG A 494      50.896  -7.569  16.092  1.00106.61           N
ANISOU 3218  NE  ARG A 494    15242   8041  17224   1777  -2864    459       N
ATOM   3219  CZ  ARG A 494      50.079  -7.567  17.142  1.00117.85           C
ANISOU 3219  CZ  ARG A 494    17012   9431  18334   1894  -2817    527       C
ATOM   3220  NH1 ARG A 494      48.821  -7.169  17.010  1.00103.45           N
ANISOU 3220  NH1 ARG A 494    15264   7716  16327   1875  -2552    554       N
ATOM   3221  NH2 ARG A 494      50.513  -7.970  18.329  1.00104.19           N
ANISOU 3221  NH2 ARG A 494    15564   7546  16479   2036  -3029    572       N
ATOM   3222  N   LEU A 495      50.737  -3.141  10.611  1.00 83.31           N
ANISOU 3222  N   LEU A 495    11166   5610  14876   1218  -2424    104       N
ATOM   3223  CA  LEU A 495      51.107  -2.745   9.248  1.00 82.09           C
ANISOU 3223  CA  LEU A 495    10737   5508  14944   1101  -2322     37       C
ATOM   3224  C   LEU A 495      51.676  -1.324   9.239  1.00 86.68           C
ANISOU 3224  C   LEU A 495    11288   6069  15577   1102  -2487    -29       C
ATOM   3225  O   LEU A 495      52.551  -1.050   8.432  1.00 86.69           O
ANISOU 3225  O   LEU A 495    11070   6029  15839   1039  -2509    -85       O
ATOM   3226  CB  LEU A 495      49.917  -2.826   8.279  1.00 79.88           C
ANISOU 3226  CB  LEU A 495    10394   5377  14578   1017  -2019     39       C
ATOM   3227  CG  LEU A 495      49.382  -4.219   7.950  1.00 83.01           C
ANISOU 3227  CG  LEU A 495    10753   5797  14989    988  -1828     87       C
ATOM   3228  CD1 LEU A 495      48.241  -4.129   6.988  1.00 81.13           C
ANISOU 3228  CD1 LEU A 495    10452   5691  14684    907  -1574     75       C
ATOM   3229  CD2 LEU A 495      50.432  -5.098   7.336  1.00 84.86           C
ANISOU 3229  CD2 LEU A 495    10790   5948  15503    943  -1846     71       C
ATOM   3230  N   LEU A 496      51.187  -0.433  10.139  1.00 83.33           N
ANISOU 3230  N   LEU A 496    11087   5660  14914   1176  -2591    -22       N
ATOM   3231  CA  LEU A 496      51.675   0.943  10.278  1.00 84.14           C
ANISOU 3231  CA  LEU A 496    11187   5736  15047   1188  -2766    -83       C
ATOM   3232  C   LEU A 496      53.097   0.955  10.843  1.00 90.99           C
ANISOU 3232  C   LEU A 496    12011   6426  16136   1240  -3084   -113       C
ATOM   3233  O   LEU A 496      53.923   1.750  10.387  1.00 89.96           O
ANISOU 3233  O   LEU A 496    11708   6246  16227   1201  -3184   -179       O
ATOM   3234  CB  LEU A 496      50.727   1.828  11.109  1.00 84.39           C
ANISOU 3234  CB  LEU A 496    11484   5825  14757   1257  -2783    -64       C
ATOM   3235  CG  LEU A 496      51.140   3.315  11.287  1.00 89.91           C
ANISOU 3235  CG  LEU A 496    12194   6504  15464   1269  -2957   -129       C
ATOM   3236  CD1 LEU A 496      51.230   4.035   9.980  1.00 88.77           C
ANISOU 3236  CD1 LEU A 496    11796   6442  15490   1156  -2811   -190       C
ATOM   3237  CD2 LEU A 496      50.173   4.059  12.137  1.00 92.45           C
ANISOU 3237  CD2 LEU A 496    12793   6875  15460   1341  -2952   -103       C
ATOM   3238  N   GLN A 497      53.386   0.050  11.801  1.00 91.04           N
ANISOU 3238  N   GLN A 497    12164   6326  16102   1328  -3238    -65       N
ATOM   3239  CA  GLN A 497      54.717  -0.150  12.383  1.00 93.75           C
ANISOU 3239  CA  GLN A 497    12470   6482  16670   1384  -3559    -87       C
ATOM   3240  C   GLN A 497      55.676  -0.687  11.291  1.00 98.91           C
ANISOU 3240  C   GLN A 497    12777   7083  17723   1288  -3495   -119       C
ATOM   3241  O   GLN A 497      56.836  -0.270  11.223  1.00100.31           O
ANISOU 3241  O   GLN A 497    12795   7126  18190   1284  -3701   -173       O
ATOM   3242  CB  GLN A 497      54.646  -1.177  13.531  1.00 96.56           C
ANISOU 3242  CB  GLN A 497    13069   6748  16872   1496  -3684    -17       C
ATOM   3243  CG  GLN A 497      54.112  -0.645  14.858  1.00112.03           C
ANISOU 3243  CG  GLN A 497    15407   8675  18482   1627  -3841     12       C
ATOM   3244  CD  GLN A 497      54.312  -1.627  15.999  1.00134.37           C
ANISOU 3244  CD  GLN A 497    18482  11378  21194   1748  -3999     75       C
ATOM   3245  OE1 GLN A 497      54.287  -2.860  15.827  1.00132.01           O
ANISOU 3245  OE1 GLN A 497    18113  11072  20971   1732  -3882    124       O
ATOM   3246  NE2 GLN A 497      54.512  -1.100  17.198  1.00123.58           N
ANISOU 3246  NE2 GLN A 497    17428   9900  19626   1880  -4270     78       N
ATOM   3247  N   THR A 498      55.168  -1.590  10.426  1.00 94.29           N
ANISOU 3247  N   THR A 498    12078   6590  17158   1212  -3204    -87       N
ATOM   3248  CA  THR A 498      55.916  -2.219   9.330  1.00 93.99           C
ANISOU 3248  CA  THR A 498    11743   6509  17458   1121  -3083   -108       C
ATOM   3249  C   THR A 498      56.217  -1.238   8.177  1.00 97.15           C
ANISOU 3249  C   THR A 498    11925   6942  18046   1028  -2966   -176       C
ATOM   3250  O   THR A 498      57.333  -1.222   7.657  1.00 97.77           O
ANISOU 3250  O   THR A 498    11778   6897  18472    991  -3018   -214       O
ATOM   3251  CB  THR A 498      55.182  -3.484   8.856  1.00 99.53           C
ANISOU 3251  CB  THR A 498    12437   7299  18081   1079  -2817    -53       C
ATOM   3252  OG1 THR A 498      54.840  -4.295   9.983  1.00 97.77           O
ANISOU 3252  OG1 THR A 498    12443   7047  17657   1174  -2907     15       O
ATOM   3253  CG2 THR A 498      56.013  -4.310   7.898  1.00 99.43           C
ANISOU 3253  CG2 THR A 498    12162   7213  18405   1006  -2719    -64       C
ATOM   3254  N   VAL A 499      55.194  -0.439   7.783  1.00 91.99           N
ANISOU 3254  N   VAL A 499    11343   6445  17165    994  -2795   -189       N
ATOM   3255  CA  VAL A 499      55.199   0.553   6.696  1.00 90.38           C
ANISOU 3255  CA  VAL A 499    10989   6300  17052    913  -2649   -247       C
ATOM   3256  C   VAL A 499      55.929   1.850   7.077  1.00 96.04           C
ANISOU 3256  C   VAL A 499    11679   6930  17880    944  -2875   -303       C
ATOM   3257  O   VAL A 499      56.567   2.461   6.215  1.00 95.81           O
ANISOU 3257  O   VAL A 499    11453   6860  18091    884  -2812   -354       O
ATOM   3258  CB  VAL A 499      53.749   0.810   6.185  1.00 92.04           C
ANISOU 3258  CB  VAL A 499    11303   6704  16963    873  -2398   -233       C
ATOM   3259  CG1 VAL A 499      53.626   2.102   5.381  1.00 91.32           C
ANISOU 3259  CG1 VAL A 499    11146   6679  16874    824  -2318   -290       C
ATOM   3260  CG2 VAL A 499      53.231  -0.368   5.374  1.00 90.65           C
ANISOU 3260  CG2 VAL A 499    11057   6593  16793    810  -2142   -205       C
ATOM   3261  N   GLY A 500      55.820   2.251   8.345  1.00 93.89           N
ANISOU 3261  N   GLY A 500    11618   6623  17435   1040  -3127   -292       N
ATOM   3262  CA  GLY A 500      56.401   3.478   8.877  1.00 94.81           C
ANISOU 3262  CA  GLY A 500    11755   6654  17615   1083  -3377   -346       C
ATOM   3263  C   GLY A 500      55.406   4.617   8.804  1.00 99.25           C
ANISOU 3263  C   GLY A 500    12440   7363  17908   1073  -3274   -362       C
ATOM   3264  O   GLY A 500      54.766   4.813   7.767  1.00 98.11           O
ANISOU 3264  O   GLY A 500    12206   7346  17724    992  -3000   -369       O
ATOM   3265  N   ILE A 501      55.253   5.364   9.916  1.00 96.63           N
ANISOU 3265  N   ILE A 501    12329   7006  17381   1161  -3499   -367       N
ATOM   3266  CA  ILE A 501      54.339   6.505  10.056  1.00 95.45           C
ANISOU 3266  CA  ILE A 501    12328   6976  16964   1169  -3439   -380       C
ATOM   3267  C   ILE A 501      54.554   7.615   9.002  1.00 99.03           C
ANISOU 3267  C   ILE A 501    12574   7471  17582   1085  -3326   -444       C
ATOM   3268  O   ILE A 501      53.566   8.229   8.578  1.00 97.15           O
ANISOU 3268  O   ILE A 501    12388   7382  17142   1049  -3131   -442       O
ATOM   3269  CB  ILE A 501      54.233   7.037  11.523  1.00 99.80           C
ANISOU 3269  CB  ILE A 501    13178   7460  17281   1291  -3720   -374       C
ATOM   3270  CG1 ILE A 501      55.624   7.139  12.210  1.00102.70           C
ANISOU 3270  CG1 ILE A 501    13505   7613  17905   1353  -4098   -419       C
ATOM   3271  CG2 ILE A 501      53.272   6.182  12.339  1.00100.12           C
ANISOU 3271  CG2 ILE A 501    13497   7548  16998   1362  -3656   -292       C
ATOM   3272  CD1 ILE A 501      55.699   7.694  13.703  1.00112.14           C
ANISOU 3272  CD1 ILE A 501    15015   8702  18890   1486  -4440   -428       C
ATOM   3273  N   GLU A 502      55.830   7.814   8.542  1.00 95.93           N
ANISOU 3273  N   GLU A 502    11940   6937  17571   1054  -3432   -497       N
ATOM   3274  CA  GLU A 502      56.269   8.794   7.523  1.00 95.12           C
ANISOU 3274  CA  GLU A 502    11620   6828  17693    981  -3329   -557       C
ATOM   3275  C   GLU A 502      55.640   8.563   6.136  1.00 94.48           C
ANISOU 3275  C   GLU A 502    11424   6883  17591    884  -2957   -547       C
ATOM   3276  O   GLU A 502      55.061   9.488   5.560  1.00 93.59           O
ANISOU 3276  O   GLU A 502    11318   6877  17365    847  -2812   -569       O
ATOM   3277  CB  GLU A 502      57.822   8.870   7.413  1.00 98.84           C
ANISOU 3277  CB  GLU A 502    11853   7082  18621    977  -3512   -605       C
ATOM   3278  CG  GLU A 502      58.533   7.540   7.111  1.00117.14           C
ANISOU 3278  CG  GLU A 502    14030   9295  21182    962  -3492   -575       C
ATOM   3279  CD  GLU A 502      59.933   7.607   6.517  1.00141.30           C
ANISOU 3279  CD  GLU A 502    16793  12151  24744    930  -3549   -617       C
ATOM   3280  OE1 GLU A 502      60.058   7.966   5.322  1.00136.55           O
ANISOU 3280  OE1 GLU A 502    16002  11556  24324    852  -3299   -640       O
ATOM   3281  OE2 GLU A 502      60.900   7.241   7.227  1.00129.46           O
ANISOU 3281  OE2 GLU A 502    15254  10474  23463    984  -3833   -622       O
ATOM   3282  N   ARG A 503      55.765   7.334   5.611  1.00 88.27           N
ANISOU 3282  N   ARG A 503    10544   6083  16911    848  -2817   -514       N
ATOM   3283  CA  ARG A 503      55.243   6.912   4.315  1.00 85.38           C
ANISOU 3283  CA  ARG A 503    10087   5818  16536    764  -2489   -505       C
ATOM   3284  C   ARG A 503      53.701   7.070   4.228  1.00 86.95           C
ANISOU 3284  C   ARG A 503    10467   6217  16354    754  -2324   -477       C
ATOM   3285  O   ARG A 503      53.176   7.513   3.200  1.00 85.63           O
ANISOU 3285  O   ARG A 503    10253   6143  16139    694  -2109   -497       O
ATOM   3286  CB  ARG A 503      55.698   5.461   4.020  1.00 80.30           C
ANISOU 3286  CB  ARG A 503     9347   5106  16059    744  -2420   -471       C
ATOM   3287  CG  ARG A 503      55.255   4.922   2.660  1.00 76.33           C
ANISOU 3287  CG  ARG A 503     8758   4680  15562    662  -2096   -466       C
ATOM   3288  CD  ARG A 503      55.893   5.639   1.483  1.00 78.42           C
ANISOU 3288  CD  ARG A 503     8845   4886  16064    604  -1944   -517       C
ATOM   3289  NE  ARG A 503      55.287   5.218   0.224  1.00 81.30           N
ANISOU 3289  NE  ARG A 503     9197   5338  16357    538  -1644   -514       N
ATOM   3290  CZ  ARG A 503      54.384   5.922  -0.451  1.00 96.12           C
ANISOU 3290  CZ  ARG A 503    11149   7345  18027    508  -1490   -532       C
ATOM   3291  NH1 ARG A 503      53.968   7.097   0.008  1.00 76.67           N
ANISOU 3291  NH1 ARG A 503     8771   4949  15409    534  -1590   -550       N
ATOM   3292  NH2 ARG A 503      53.879   5.451  -1.583  1.00 85.59           N
ANISOU 3292  NH2 ARG A 503     9815   6068  16636    455  -1246   -533       N
ATOM   3293  N   THR A 504      53.001   6.717   5.320  1.00 82.05           N
ANISOU 3293  N   THR A 504    10055   5643  15476    819  -2427   -430       N
ATOM   3294  CA  THR A 504      51.550   6.806   5.476  1.00 79.72           C
ANISOU 3294  CA  THR A 504     9939   5508  14844    825  -2293   -394       C
ATOM   3295  C   THR A 504      51.138   8.289   5.344  1.00 81.65           C
ANISOU 3295  C   THR A 504    10224   5823  14975    819  -2286   -433       C
ATOM   3296  O   THR A 504      50.309   8.629   4.493  1.00 80.64           O
ANISOU 3296  O   THR A 504    10084   5815  14740    766  -2081   -438       O
ATOM   3297  CB  THR A 504      51.169   6.171   6.823  1.00 84.04           C
ANISOU 3297  CB  THR A 504    10702   6035  15193    914  -2429   -335       C
ATOM   3298  OG1 THR A 504      51.744   4.863   6.883  1.00 84.75           O
ANISOU 3298  OG1 THR A 504    10727   6044  15429    917  -2445   -305       O
ATOM   3299  CG2 THR A 504      49.667   6.091   7.042  1.00 78.33           C
ANISOU 3299  CG2 THR A 504    10157   5449  14155    926  -2270   -287       C
ATOM   3300  N   ARG A 505      51.791   9.170   6.121  1.00 76.82           N
ANISOU 3300  N   ARG A 505     9652   5126  14412    872  -2520   -464       N
ATOM   3301  CA  ARG A 505      51.562  10.624   6.107  1.00 74.92           C
ANISOU 3301  CA  ARG A 505     9446   4931  14090    872  -2544   -505       C
ATOM   3302  C   ARG A 505      51.821  11.258   4.712  1.00 77.11           C
ANISOU 3302  C   ARG A 505     9517   5232  14550    787  -2366   -555       C
ATOM   3303  O   ARG A 505      51.114  12.198   4.330  1.00 75.67           O
ANISOU 3303  O   ARG A 505     9371   5151  14228    764  -2260   -572       O
ATOM   3304  CB  ARG A 505      52.386  11.307   7.216  1.00 73.05           C
ANISOU 3304  CB  ARG A 505     9284   4567  13904    951  -2861   -534       C
ATOM   3305  CG  ARG A 505      51.866  11.006   8.625  1.00 74.32           C
ANISOU 3305  CG  ARG A 505     9730   4724  13784   1049  -3013   -486       C
ATOM   3306  CD  ARG A 505      52.540  11.784   9.741  1.00 66.78           C
ANISOU 3306  CD  ARG A 505     8901   3644  12829   1136  -3338   -520       C
ATOM   3307  NE  ARG A 505      51.954  13.116   9.831  1.00 72.28           N
ANISOU 3307  NE  ARG A 505     9685   4415  13362   1139  -3321   -548       N
ATOM   3308  CZ  ARG A 505      52.540  14.216   9.380  1.00 82.27           C
ANISOU 3308  CZ  ARG A 505    10801   5644  14811   1106  -3377   -615       C
ATOM   3309  NH1 ARG A 505      53.774  14.166   8.887  1.00 60.55           N
ANISOU 3309  NH1 ARG A 505     7811   2767  12429   1072  -3466   -660       N
ATOM   3310  NH2 ARG A 505      51.915  15.379   9.445  1.00 79.95           N
ANISOU 3310  NH2 ARG A 505    10597   5430  14352   1108  -3343   -635       N
ATOM   3311  N   GLN A 506      52.799  10.698   3.944  1.00 73.45           N
ANISOU 3311  N   GLN A 506     8850   4665  14392    744  -2315   -573       N
ATOM   3312  CA  GLN A 506      53.155  11.133   2.590  1.00 72.14           C
ANISOU 3312  CA  GLN A 506     8503   4487  14418    672  -2120   -614       C
ATOM   3313  C   GLN A 506      52.024  10.874   1.598  1.00 73.92           C
ANISOU 3313  C   GLN A 506     8770   4864  14453    617  -1846   -597       C
ATOM   3314  O   GLN A 506      51.748  11.751   0.773  1.00 73.86           O
ANISOU 3314  O   GLN A 506     8739   4913  14414    582  -1716   -628       O
ATOM   3315  CB  GLN A 506      54.439  10.451   2.105  1.00 74.76           C
ANISOU 3315  CB  GLN A 506     8632   4655  15118    649  -2115   -626       C
ATOM   3316  CG  GLN A 506      55.261  11.331   1.158  1.00 96.24           C
ANISOU 3316  CG  GLN A 506    11168   7281  18118    608  -2014   -678       C
ATOM   3317  CD  GLN A 506      55.645  10.632  -0.128  1.00115.73           C
ANISOU 3317  CD  GLN A 506    13500   9698  20776    549  -1760   -675       C
ATOM   3318  OE1 GLN A 506      56.377   9.624  -0.138  1.00105.49           O
ANISOU 3318  OE1 GLN A 506    12100   8285  19696    547  -1777   -659       O
ATOM   3319  NE2 GLN A 506      55.195  11.192  -1.250  1.00111.48           N
ANISOU 3319  NE2 GLN A 506    12963   9230  20163    504  -1519   -694       N
ATOM   3320  N   LEU A 507      51.378   9.669   1.669  1.00 67.71           N
ANISOU 3320  N   LEU A 507     8048   4135  13545    612  -1769   -550       N
ATOM   3321  CA  LEU A 507      50.256   9.286   0.799  1.00 64.19           C
ANISOU 3321  CA  LEU A 507     7645   3817  12926    564  -1542   -535       C
ATOM   3322  C   LEU A 507      49.037  10.173   1.067  1.00 66.73           C
ANISOU 3322  C   LEU A 507     8111   4276  12967    577  -1521   -529       C
ATOM   3323  O   LEU A 507      48.402  10.646   0.129  1.00 62.90           O
ANISOU 3323  O   LEU A 507     7622   3872  12404    534  -1362   -548       O
ATOM   3324  CB  LEU A 507      49.907   7.805   0.980  1.00 62.97           C
ANISOU 3324  CB  LEU A 507     7522   3671  12731    566  -1501   -486       C
ATOM   3325  CG  LEU A 507      48.951   7.201  -0.044  1.00 64.30           C
ANISOU 3325  CG  LEU A 507     7701   3933  12797    512  -1280   -478       C
ATOM   3326  CD1 LEU A 507      49.529   7.194  -1.454  1.00 63.14           C
ANISOU 3326  CD1 LEU A 507     7426   3734  12832    453  -1118   -520       C
ATOM   3327  CD2 LEU A 507      48.605   5.816   0.321  1.00 67.53           C
ANISOU 3327  CD2 LEU A 507     8150   4346  13163    523  -1267   -428       C
ATOM   3328  N   PHE A 508      48.744  10.389   2.356  1.00 66.28           N
ANISOU 3328  N   PHE A 508     8193   4230  12761    642  -1685   -501       N
ATOM   3329  CA  PHE A 508      47.698  11.253   2.882  1.00 67.63           C
ANISOU 3329  CA  PHE A 508     8515   4501  12679    670  -1692   -488       C
ATOM   3330  C   PHE A 508      47.810  12.690   2.399  1.00 72.89           C
ANISOU 3330  C   PHE A 508     9141   5194  13361    650  -1680   -540       C
ATOM   3331  O   PHE A 508      46.787  13.316   2.112  1.00 70.90           O
ANISOU 3331  O   PHE A 508     8955   5049  12933    635  -1578   -537       O
ATOM   3332  CB  PHE A 508      47.825  11.303   4.389  1.00 71.14           C
ANISOU 3332  CB  PHE A 508     9114   4895  13021    756  -1902   -458       C
ATOM   3333  CG  PHE A 508      47.021  10.252   5.067  1.00 72.76           C
ANISOU 3333  CG  PHE A 508     9456   5128  13060    792  -1865   -390       C
ATOM   3334  CD1 PHE A 508      47.544   8.987   5.272  1.00 75.94           C
ANISOU 3334  CD1 PHE A 508     9826   5459  13570    802  -1896   -362       C
ATOM   3335  CD2 PHE A 508      45.740  10.528   5.524  1.00 75.26           C
ANISOU 3335  CD2 PHE A 508     9935   5533  13126    819  -1789   -351       C
ATOM   3336  CE1 PHE A 508      46.793   7.998   5.900  1.00 78.01           C
ANISOU 3336  CE1 PHE A 508    10215   5739  13684    839  -1846   -296       C
ATOM   3337  CE2 PHE A 508      44.996   9.549   6.169  1.00 78.83           C
ANISOU 3337  CE2 PHE A 508    10513   5994  13446    857  -1732   -283       C
ATOM   3338  CZ  PHE A 508      45.533   8.287   6.362  1.00 77.26           C
ANISOU 3338  CZ  PHE A 508    10283   5724  13349    868  -1762   -256       C
ATOM   3339  N   MET A 509      49.042  13.238   2.393  1.00 72.49           N
ANISOU 3339  N   MET A 509     8982   5033  13530    654  -1795   -584       N
ATOM   3340  CA  MET A 509      49.301  14.598   1.936  1.00 73.29           C
ANISOU 3340  CA  MET A 509     9027   5135  13685    637  -1784   -635       C
ATOM   3341  C   MET A 509      49.019  14.730   0.426  1.00 74.51           C
ANISOU 3341  C   MET A 509     9089   5341  13879    568  -1541   -657       C
ATOM   3342  O   MET A 509      48.474  15.763  -0.000  1.00 73.13           O
ANISOU 3342  O   MET A 509     8945   5242  13601    552  -1465   -679       O
ATOM   3343  CB  MET A 509      50.716  15.031   2.324  1.00 77.84           C
ANISOU 3343  CB  MET A 509     9495   5554  14525    663  -1972   -675       C
ATOM   3344  CG  MET A 509      50.753  15.822   3.627  1.00 82.91           C
ANISOU 3344  CG  MET A 509    10270   6173  15059    733  -2212   -681       C
ATOM   3345  SD  MET A 509      52.265  15.587   4.596  1.00 89.62           S
ANISOU 3345  SD  MET A 509    11060   6816  16176    791  -2527   -703       S
ATOM   3346  CE  MET A 509      53.379  16.630   3.703  1.00 87.04           C
ANISOU 3346  CE  MET A 509    10492   6377  16204    747  -2500   -774       C
ATOM   3347  N   ASP A 510      49.294  13.636  -0.347  1.00 69.68           N
ANISOU 3347  N   ASP A 510     8393   4690  13393    531  -1422   -649       N
ATOM   3348  CA  ASP A 510      49.032  13.463  -1.787  1.00 68.55           C
ANISOU 3348  CA  ASP A 510     8199   4575  13274    474  -1193   -666       C
ATOM   3349  C   ASP A 510      47.524  13.453  -2.155  1.00 70.43           C
ANISOU 3349  C   ASP A 510     8553   4962  13243    455  -1079   -649       C
ATOM   3350  O   ASP A 510      47.183  13.556  -3.336  1.00 70.06           O
ANISOU 3350  O   ASP A 510     8498   4944  13177    417   -917   -671       O
ATOM   3351  CB  ASP A 510      49.700  12.177  -2.310  1.00 70.98           C
ANISOU 3351  CB  ASP A 510     8413   4791  13766    451  -1119   -656       C
ATOM   3352  CG  ASP A 510      51.201  12.251  -2.427  1.00 86.11           C
ANISOU 3352  CG  ASP A 510    10176   6538  16005    454  -1166   -680       C
ATOM   3353  OD1 ASP A 510      51.712  13.326  -2.786  1.00 86.62           O
ANISOU 3353  OD1 ASP A 510    10176   6549  16185    450  -1144   -718       O
ATOM   3354  OD2 ASP A 510      51.867  11.212  -2.208  1.00 96.47           O
ANISOU 3354  OD2 ASP A 510    11422   7760  17473    460  -1215   -661       O
ATOM   3355  N   PHE A 511      46.636  13.302  -1.154  1.00 65.34           N
ANISOU 3355  N   PHE A 511     8025   4397  12406    488  -1161   -608       N
ATOM   3356  CA  PHE A 511      45.174  13.313  -1.312  1.00 63.38           C
ANISOU 3356  CA  PHE A 511     7875   4273  11936    476  -1070   -587       C
ATOM   3357  C   PHE A 511      44.576  14.709  -1.035  1.00 70.02           C
ANISOU 3357  C   PHE A 511     8787   5185  12633    492  -1098   -598       C
ATOM   3358  O   PHE A 511      43.360  14.928  -1.156  1.00 69.21           O
ANISOU 3358  O   PHE A 511     8755   5177  12363    484  -1028   -583       O
ATOM   3359  CB  PHE A 511      44.541  12.254  -0.405  1.00 64.09           C
ANISOU 3359  CB  PHE A 511     8043   4384  11924    504  -1107   -528       C
ATOM   3360  CG  PHE A 511      45.013  10.843  -0.663  1.00 65.02           C
ANISOU 3360  CG  PHE A 511     8097   4439  12169    488  -1076   -513       C
ATOM   3361  CD1 PHE A 511      45.575  10.487  -1.889  1.00 68.18           C
ANISOU 3361  CD1 PHE A 511     8394   4794  12716    439   -964   -547       C
ATOM   3362  CD2 PHE A 511      44.891   9.864   0.314  1.00 66.80           C
ANISOU 3362  CD2 PHE A 511     8378   4642  12360    526  -1145   -461       C
ATOM   3363  CE1 PHE A 511      46.013   9.175  -2.125  1.00 68.56           C
ANISOU 3363  CE1 PHE A 511     8387   4780  12884    424   -928   -532       C
ATOM   3364  CE2 PHE A 511      45.324   8.557   0.072  1.00 69.64           C
ANISOU 3364  CE2 PHE A 511     8676   4944  12840    511  -1113   -445       C
ATOM   3365  CZ  PHE A 511      45.864   8.220  -1.152  1.00 67.41           C
ANISOU 3365  CZ  PHE A 511     8282   4623  12708    457  -1005   -482       C
ATOM   3366  N   GLY A 512      45.461  15.647  -0.707  1.00 68.49           N
ANISOU 3366  N   GLY A 512     8562   4935  12526    514  -1201   -628       N
ATOM   3367  CA  GLY A 512      45.104  17.020  -0.417  1.00 68.44           C
ANISOU 3367  CA  GLY A 512     8613   4981  12411    531  -1239   -644       C
ATOM   3368  C   GLY A 512      45.279  17.410   1.031  1.00 75.14           C
ANISOU 3368  C   GLY A 512     9553   5802  13193    594  -1424   -627       C
ATOM   3369  O   GLY A 512      45.029  18.565   1.378  1.00 75.83           O
ANISOU 3369  O   GLY A 512     9694   5920  13198    613  -1470   -643       O
ATOM   3370  N   LEU A 513      45.699  16.475   1.889  1.00 73.14           N
ANISOU 3370  N   LEU A 513     9336   5486  12969    631  -1537   -596       N
ATOM   3371  CA  LEU A 513      45.876  16.800   3.297  1.00 74.30           C
ANISOU 3371  CA  LEU A 513     9610   5590  13033    704  -1729   -580       C
ATOM   3372  C   LEU A 513      47.072  17.702   3.615  1.00 81.35           C
ANISOU 3372  C   LEU A 513    10443   6380  14088    726  -1905   -632       C
ATOM   3373  O   LEU A 513      48.045  17.774   2.851  1.00 82.38           O
ANISOU 3373  O   LEU A 513    10405   6437  14459    690  -1889   -674       O
ATOM   3374  CB  LEU A 513      45.782  15.579   4.208  1.00 74.67           C
ANISOU 3374  CB  LEU A 513     9755   5597  13019    750  -1798   -525       C
ATOM   3375  CG  LEU A 513      44.354  15.151   4.439  1.00 78.60           C
ANISOU 3375  CG  LEU A 513    10380   6189  13294    759  -1667   -466       C
ATOM   3376  CD1 LEU A 513      44.197  13.676   4.275  1.00 79.73           C
ANISOU 3376  CD1 LEU A 513    10514   6311  13468    756  -1614   -423       C
ATOM   3377  CD2 LEU A 513      43.809  15.664   5.761  1.00 80.51           C
ANISOU 3377  CD2 LEU A 513    10831   6436  13323    834  -1749   -434       C
ATOM   3378  N   GLN A 514      46.947  18.441   4.724  1.00 77.48           N
ANISOU 3378  N   GLN A 514    10098   5875  13465    789  -2061   -630       N
ATOM   3379  CA  GLN A 514      47.954  19.377   5.200  1.00 77.84           C
ANISOU 3379  CA  GLN A 514    10117   5819  13638    820  -2261   -682       C
ATOM   3380  C   GLN A 514      48.811  18.687   6.238  1.00 82.44           C
ANISOU 3380  C   GLN A 514    10757   6270  14298    885  -2499   -674       C
ATOM   3381  O   GLN A 514      48.357  17.749   6.909  1.00 82.06           O
ANISOU 3381  O   GLN A 514    10850   6230  14098    925  -2515   -620       O
ATOM   3382  CB  GLN A 514      47.306  20.648   5.799  1.00 79.24           C
ANISOU 3382  CB  GLN A 514    10442   6054  13612    855  -2302   -690       C
ATOM   3383  CG  GLN A 514      46.037  21.166   5.074  1.00 92.45           C
ANISOU 3383  CG  GLN A 514    12132   7878  15115    809  -2069   -673       C
ATOM   3384  CD  GLN A 514      44.753  20.370   5.328  1.00 96.49           C
ANISOU 3384  CD  GLN A 514    12779   8480  15402    820  -1939   -603       C
ATOM   3385  OE1 GLN A 514      44.705  19.423   6.115  1.00 82.27           O
ANISOU 3385  OE1 GLN A 514    11071   6639  13547    861  -1993   -560       O
ATOM   3386  NE2 GLN A 514      43.696  20.699   4.601  1.00 89.61           N
ANISOU 3386  NE2 GLN A 514    11906   7722  14417    781  -1757   -591       N
ATOM   3387  N   GLU A 515      50.057  19.171   6.375  1.00 79.95           N
ANISOU 3387  N   GLU A 515    10329   5818  14231    896  -2686   -729       N
ATOM   3388  CA  GLU A 515      51.050  18.691   7.325  1.00 80.87           C
ANISOU 3388  CA  GLU A 515    10477   5778  14474    960  -2962   -738       C
ATOM   3389  C   GLU A 515      50.432  18.705   8.734  1.00 86.48           C
ANISOU 3389  C   GLU A 515    11488   6495  14875   1053  -3113   -702       C
ATOM   3390  O   GLU A 515      50.489  17.704   9.452  1.00 85.14           O
ANISOU 3390  O   GLU A 515    11441   6276  14632   1106  -3203   -659       O
ATOM   3391  CB  GLU A 515      52.289  19.597   7.242  1.00 82.82           C
ANISOU 3391  CB  GLU A 515    10567   5885  15016    959  -3140   -813       C
ATOM   3392  CG  GLU A 515      53.561  18.977   7.797  1.00 95.19           C
ANISOU 3392  CG  GLU A 515    12049   7259  16860    996  -3394   -834       C
ATOM   3393  CD  GLU A 515      54.409  18.220   6.795  1.00107.24           C
ANISOU 3393  CD  GLU A 515    13309   8713  18724    931  -3270   -840       C
ATOM   3394  OE1 GLU A 515      54.919  18.850   5.839  1.00 93.39           O
ANISOU 3394  OE1 GLU A 515    11350   6925  17207    875  -3150   -882       O
ATOM   3395  OE2 GLU A 515      54.597  16.998   6.992  1.00 94.74           O
ANISOU 3395  OE2 GLU A 515    11728   7094  17174    941  -3289   -802       O
ATOM   3396  N   ASP A 516      49.756  19.824   9.075  1.00 85.63           N
ANISOU 3396  N   ASP A 516    11509   6453  14574   1073  -3105   -713       N
ATOM   3397  CA  ASP A 516      49.095  20.049  10.361  1.00 87.13           C
ANISOU 3397  CA  ASP A 516    12003   6650  14452   1161  -3205   -682       C
ATOM   3398  C   ASP A 516      47.835  19.175  10.685  1.00 91.83           C
ANISOU 3398  C   ASP A 516    12786   7336  14771   1186  -3029   -594       C
ATOM   3399  O   ASP A 516      47.446  19.111  11.855  1.00 93.17           O
ANISOU 3399  O   ASP A 516    13226   7456  14720   1280  -3139   -559       O
ATOM   3400  CB  ASP A 516      48.891  21.564  10.614  1.00 88.90           C
ANISOU 3400  CB  ASP A 516    12269   6920  14591   1160  -3207   -723       C
ATOM   3401  CG  ASP A 516      47.465  22.095  10.497  1.00103.75           C
ANISOU 3401  CG  ASP A 516    14377   8915  16130   1189  -3061   -674       C
ATOM   3402  OD1 ASP A 516      46.956  22.661  11.498  1.00106.47           O
ANISOU 3402  OD1 ASP A 516    14963   9202  16289   1274  -3220   -674       O
ATOM   3403  OD2 ASP A 516      46.867  21.969   9.397  1.00109.19           O
ANISOU 3403  OD2 ASP A 516    14996   9740  16750   1126  -2791   -640       O
ATOM   3404  N   GLN A 517      47.213  18.502   9.683  1.00 86.61           N
ANISOU 3404  N   GLN A 517    11992   6785  14129   1111  -2764   -560       N
ATOM   3405  CA  GLN A 517      46.007  17.700   9.949  1.00 85.76           C
ANISOU 3405  CA  GLN A 517    12032   6752  13800   1129  -2588   -480       C
ATOM   3406  C   GLN A 517      46.206  16.178  10.043  1.00 90.62           C
ANISOU 3406  C   GLN A 517    12635   7320  14477   1139  -2582   -436       C
ATOM   3407  O   GLN A 517      45.233  15.435  10.218  1.00 90.70           O
ANISOU 3407  O   GLN A 517    12753   7380  14329   1154  -2425   -369       O
ATOM   3408  CB  GLN A 517      44.820  18.116   9.061  1.00 85.46           C
ANISOU 3408  CB  GLN A 517    11932   6866  13673   1061  -2311   -463       C
ATOM   3409  CG  GLN A 517      44.360  19.586   9.253  1.00101.86           C
ANISOU 3409  CG  GLN A 517    14083   8994  15625   1068  -2302   -488       C
ATOM   3410  CD  GLN A 517      43.279  19.800  10.301  1.00121.39           C
ANISOU 3410  CD  GLN A 517    16831  11480  17809   1144  -2260   -430       C
ATOM   3411  OE1 GLN A 517      42.129  20.146   9.987  1.00114.68           O
ANISOU 3411  OE1 GLN A 517    16004  10729  16841   1119  -2060   -399       O
ATOM   3412  NE2 GLN A 517      43.636  19.681  11.577  1.00114.42           N
ANISOU 3412  NE2 GLN A 517    16176  10485  16813   1244  -2452   -416       N
ATOM   3413  N   ILE A 518      47.469  15.718   9.975  1.00 86.81           N
ANISOU 3413  N   ILE A 518    12019   6729  14236   1135  -2750   -472       N
ATOM   3414  CA  ILE A 518      47.812  14.302  10.123  1.00 86.41           C
ANISOU 3414  CA  ILE A 518    11953   6619  14259   1149  -2769   -434       C
ATOM   3415  C   ILE A 518      48.807  14.197  11.297  1.00 93.41           C
ANISOU 3415  C   ILE A 518    12978   7340  15173   1246  -3091   -445       C
ATOM   3416  O   ILE A 518      49.916  14.729  11.187  1.00 94.57           O
ANISOU 3416  O   ILE A 518    12999   7389  15544   1241  -3288   -510       O
ATOM   3417  CB  ILE A 518      48.393  13.617   8.841  1.00 87.89           C
ANISOU 3417  CB  ILE A 518    11852   6815  14728   1054  -2654   -456       C
ATOM   3418  CG1 ILE A 518      47.941  14.264   7.517  1.00 86.17           C
ANISOU 3418  CG1 ILE A 518    11462   6714  14566    959  -2432   -487       C
ATOM   3419  CG2 ILE A 518      48.114  12.121   8.861  1.00 88.25           C
ANISOU 3419  CG2 ILE A 518    11914   6863  14753   1056  -2557   -395       C
ATOM   3420  CD1 ILE A 518      48.999  14.229   6.435  1.00 87.50           C
ANISOU 3420  CD1 ILE A 518    11369   6825  15051    891  -2417   -540       C
ATOM   3421  N   PRO A 519      48.462  13.536  12.427  1.00 89.95           N
ANISOU 3421  N   PRO A 519    12802   6851  14524   1340  -3155   -385       N
ATOM   3422  CA  PRO A 519      49.446  13.407  13.510  1.00 90.92           C
ANISOU 3422  CA  PRO A 519    13073   6801  14670   1439  -3487   -400       C
ATOM   3423  C   PRO A 519      50.491  12.339  13.174  1.00 93.32           C
ANISOU 3423  C   PRO A 519    13187   7013  15259   1416  -3585   -409       C
ATOM   3424  O   PRO A 519      50.261  11.527  12.281  1.00 90.58           O
ANISOU 3424  O   PRO A 519    12663   6739  15012   1339  -3368   -383       O
ATOM   3425  CB  PRO A 519      48.589  13.018  14.714  1.00 93.60           C
ANISOU 3425  CB  PRO A 519    13776   7123  14664   1548  -3466   -323       C
ATOM   3426  CG  PRO A 519      47.425  12.303  14.136  1.00 96.66           C
ANISOU 3426  CG  PRO A 519    14117   7647  14962   1491  -3119   -257       C
ATOM   3427  CD  PRO A 519      47.198  12.838  12.753  1.00 90.83           C
ANISOU 3427  CD  PRO A 519    13085   7040  14386   1364  -2932   -300       C
ATOM   3428  N   ARG A 520      51.636  12.350  13.868  1.00 91.86           N
ANISOU 3428  N   ARG A 520    13034   6655  15212   1481  -3919   -447       N
ATOM   3429  CA  ARG A 520      52.695  11.360  13.656  1.00 92.94           C
ANISOU 3429  CA  ARG A 520    12997   6678  15640   1469  -4043   -455       C
ATOM   3430  C   ARG A 520      52.337  10.003  14.264  1.00 98.74           C
ANISOU 3430  C   ARG A 520    13909   7390  16218   1531  -4012   -375       C
ATOM   3431  O   ARG A 520      52.723   8.979  13.715  1.00 98.63           O
ANISOU 3431  O   ARG A 520    13716   7359  16401   1485  -3947   -359       O
ATOM   3432  CB  ARG A 520      54.038  11.847  14.231  1.00 94.16           C
ANISOU 3432  CB  ARG A 520    13124   6635  16018   1525  -4437   -525       C
ATOM   3433  CG  ARG A 520      54.991  12.420  13.186  1.00 96.42           C
ANISOU 3433  CG  ARG A 520    13044   6879  16713   1430  -4449   -599       C
ATOM   3434  CD  ARG A 520      55.079  13.928  13.255  1.00 88.56           C
ANISOU 3434  CD  ARG A 520    12048   5877  15724   1430  -4548   -665       C
ATOM   3435  NE  ARG A 520      55.502  14.485  11.973  1.00 88.25           N
ANISOU 3435  NE  ARG A 520    11671   5870  15989   1319  -4382   -713       N
ATOM   3436  CZ  ARG A 520      55.250  15.727  11.571  1.00110.47           C
ANISOU 3436  CZ  ARG A 520    14435   8749  18789   1282  -4308   -756       C
ATOM   3437  NH1 ARG A 520      54.574  16.565  12.355  1.00103.29           N
ANISOU 3437  NH1 ARG A 520    13780   7883  17581   1343  -4388   -759       N
ATOM   3438  NH2 ARG A 520      55.667  16.142  10.383  1.00 99.19           N
ANISOU 3438  NH2 ARG A 520    12713   7334  17641   1188  -4140   -793       N
ATOM   3439  N   ASN A 521      51.595  10.000  15.385  1.00 96.56           N
ANISOU 3439  N   ASN A 521    13990   7105  15591   1636  -4044   -324       N
ATOM   3440  CA  ASN A 521      51.199   8.813  16.150  1.00 97.67           C
ANISOU 3440  CA  ASN A 521    14358   7204  15549   1717  -4018   -243       C
ATOM   3441  C   ASN A 521      50.500   7.660  15.385  1.00100.61           C
ANISOU 3441  C   ASN A 521    14600   7693  15936   1644  -3686   -179       C
ATOM   3442  O   ASN A 521      49.941   7.864  14.299  1.00 97.46           O
ANISOU 3442  O   ASN A 521    14004   7440  15588   1538  -3420   -185       O
ATOM   3443  CB  ASN A 521      50.424   9.224  17.409  1.00 99.74           C
ANISOU 3443  CB  ASN A 521    15048   7426  15424   1848  -4077   -200       C
ATOM   3444  CG  ASN A 521      49.267  10.148  17.144  1.00126.69           C
ANISOU 3444  CG  ASN A 521    18533  10978  18626   1820  -3836   -188       C
ATOM   3445  OD1 ASN A 521      48.573  10.034  16.133  1.00122.52           O
ANISOU 3445  OD1 ASN A 521    17799  10603  18151   1714  -3537   -175       O
ATOM   3446  ND2 ASN A 521      49.017  11.071  18.060  1.00120.82           N
ANISOU 3446  ND2 ASN A 521    18097  10175  17635   1919  -3964   -192       N
ATOM   3447  N   TYR A 522      50.512   6.453  16.005  1.00 98.77           N
ANISOU 3447  N   TYR A 522    14496   7384  15648   1709  -3714   -117       N
ATOM   3448  CA  TYR A 522      49.934   5.207  15.492  1.00 98.04           C
ANISOU 3448  CA  TYR A 522    14312   7367  15570   1659  -3442    -53       C
ATOM   3449  C   TYR A 522      48.399   5.170  15.413  1.00100.41           C
ANISOU 3449  C   TYR A 522    14733   7801  15618   1648  -3110     11       C
ATOM   3450  O   TYR A 522      47.816   4.124  15.118  1.00 99.06           O
ANISOU 3450  O   TYR A 522    14512   7681  15445   1618  -2886     67       O
ATOM   3451  CB  TYR A 522      50.523   3.982  16.228  1.00101.36           C
ANISOU 3451  CB  TYR A 522    14847   7653  16015   1741  -3590     -8       C
ATOM   3452  CG  TYR A 522      51.994   3.771  15.939  1.00105.04           C
ANISOU 3452  CG  TYR A 522    15085   8001  16825   1715  -3850    -67       C
ATOM   3453  CD1 TYR A 522      52.410   3.098  14.797  1.00106.27           C
ANISOU 3453  CD1 TYR A 522    14901   8199  17278   1601  -3713    -83       C
ATOM   3454  CD2 TYR A 522      52.972   4.267  16.795  1.00108.36           C
ANISOU 3454  CD2 TYR A 522    15632   8252  17288   1808  -4233   -110       C
ATOM   3455  CE1 TYR A 522      53.765   2.928  14.508  1.00108.73           C
ANISOU 3455  CE1 TYR A 522    14990   8387  17937   1577  -3928   -134       C
ATOM   3456  CE2 TYR A 522      54.332   4.088  16.526  1.00110.37           C
ANISOU 3456  CE2 TYR A 522    15653   8378  17903   1784  -4476   -165       C
ATOM   3457  CZ  TYR A 522      54.725   3.415  15.381  1.00115.82           C
ANISOU 3457  CZ  TYR A 522    15993   9112  18901   1667  -4309   -174       C
ATOM   3458  OH  TYR A 522      56.063   3.248  15.105  1.00115.70           O
ANISOU 3458  OH  TYR A 522    15738   8955  19267   1643  -4525   -223       O
ATOM   3459  N   THR A 523      47.765   6.335  15.613  1.00 97.28           N
ANISOU 3459  N   THR A 523    14471   7455  15037   1668  -3077     -2       N
ATOM   3460  CA  THR A 523      46.314   6.552  15.571  1.00 96.08           C
ANISOU 3460  CA  THR A 523    14428   7412  14665   1661  -2780     52       C
ATOM   3461  C   THR A 523      45.831   6.694  14.127  1.00 97.68           C
ANISOU 3461  C   THR A 523    14313   7772  15028   1516  -2535     24       C
ATOM   3462  O   THR A 523      44.636   6.528  13.862  1.00 98.11           O
ANISOU 3462  O   THR A 523    14382   7916  14981   1488  -2266     72       O
ATOM   3463  CB  THR A 523      45.929   7.819  16.362  1.00102.07           C
ANISOU 3463  CB  THR A 523    15443   8151  15188   1736  -2857     42       C
ATOM   3464  OG1 THR A 523      46.265   8.982  15.596  1.00101.72           O
ANISOU 3464  OG1 THR A 523    15194   8173  15283   1656  -2922    -42       O
ATOM   3465  CG2 THR A 523      46.523   7.861  17.776  1.00 99.84           C
ANISOU 3465  CG2 THR A 523    15508   7694  14733   1889  -3141     56       C
ATOM   3466  N   ILE A 524      46.752   7.062  13.209  1.00 90.22           N
ANISOU 3466  N   ILE A 524    13093   6847  14338   1429  -2631    -55       N
ATOM   3467  CA  ILE A 524      46.472   7.215  11.777  1.00 85.90           C
ANISOU 3467  CA  ILE A 524    12259   6428  13949   1298  -2427    -90       C
ATOM   3468  C   ILE A 524      46.121   5.853  11.105  1.00 84.99           C
ANISOU 3468  C   ILE A 524    12017   6353  13921   1243  -2223    -48       C
ATOM   3469  O   ILE A 524      45.444   5.835  10.071  1.00 82.55           O
ANISOU 3469  O   ILE A 524    11571   6156  13639   1159  -2000    -51       O
ATOM   3470  CB  ILE A 524      47.563   8.055  11.040  1.00 88.03           C
ANISOU 3470  CB  ILE A 524    12300   6685  14464   1233  -2564   -180       C
ATOM   3471  CG1 ILE A 524      48.975   7.409  11.111  1.00 88.55           C
ANISOU 3471  CG1 ILE A 524    12250   6615  14778   1244  -2777   -206       C
ATOM   3472  CG2 ILE A 524      47.579   9.479  11.580  1.00 89.34           C
ANISOU 3472  CG2 ILE A 524    12582   6841  14520   1274  -2701   -220       C
ATOM   3473  CD1 ILE A 524      50.071   8.011  10.191  1.00 85.81           C
ANISOU 3473  CD1 ILE A 524    11630   6234  14741   1170  -2860   -287       C
ATOM   3474  N   ALA A 525      46.523   4.725  11.746  1.00 80.55           N
ANISOU 3474  N   ALA A 525    11526   5694  13386   1299  -2306     -6       N
ATOM   3475  CA  ALA A 525      46.243   3.354  11.293  1.00 79.40           C
ANISOU 3475  CA  ALA A 525    11283   5566  13319   1260  -2135     38       C
ATOM   3476  C   ALA A 525      44.784   3.009  11.547  1.00 83.36           C
ANISOU 3476  C   ALA A 525    11921   6129  13622   1279  -1890    109       C
ATOM   3477  O   ALA A 525      44.265   2.099  10.911  1.00 80.91           O
ANISOU 3477  O   ALA A 525    11494   5863  13385   1224  -1703    135       O
ATOM   3478  CB  ALA A 525      47.125   2.359  12.032  1.00 81.18           C
ANISOU 3478  CB  ALA A 525    11576   5659  13610   1329  -2308     66       C
ATOM   3479  N   LEU A 526      44.124   3.752  12.470  1.00 81.72           N
ANISOU 3479  N   LEU A 526    11957   5914  13179   1357  -1887    141       N
ATOM   3480  CA  LEU A 526      42.736   3.539  12.902  1.00 81.42           C
ANISOU 3480  CA  LEU A 526    12075   5902  12958   1393  -1650    217       C
ATOM   3481  C   LEU A 526      41.714   4.532  12.321  1.00 86.09           C
ANISOU 3481  C   LEU A 526    12604   6608  13500   1333  -1483    198       C
ATOM   3482  O   LEU A 526      40.515   4.419  12.607  1.00 86.43           O
ANISOU 3482  O   LEU A 526    12745   6665  13428   1354  -1274    259       O
ATOM   3483  CB  LEU A 526      42.685   3.527  14.444  1.00 82.68           C
ANISOU 3483  CB  LEU A 526    12596   5940  12880   1542  -1739    281       C
ATOM   3484  CG  LEU A 526      42.756   2.172  15.160  1.00 88.11           C
ANISOU 3484  CG  LEU A 526    13425   6522  13531   1620  -1727    355       C
ATOM   3485  CD1 LEU A 526      43.857   1.282  14.615  1.00 87.71           C
ANISOU 3485  CD1 LEU A 526    13162   6448  13716   1569  -1860    320       C
ATOM   3486  CD2 LEU A 526      42.925   2.359  16.653  1.00 91.27           C
ANISOU 3486  CD2 LEU A 526    14206   6784  13689   1777  -1879    399       C
ATOM   3487  N   GLY A 527      42.194   5.472  11.504  1.00 81.98           N
ANISOU 3487  N   GLY A 527    11913   6152  13083   1260  -1568    117       N
ATOM   3488  CA  GLY A 527      41.366   6.491  10.869  1.00 80.16           C
ANISOU 3488  CA  GLY A 527    11610   6028  12820   1201  -1442     89       C
ATOM   3489  C   GLY A 527      40.776   7.505  11.827  1.00 84.55           C
ANISOU 3489  C   GLY A 527    12409   6565  13152   1282  -1449    116       C
ATOM   3490  O   GLY A 527      39.586   7.830  11.745  1.00 83.29           O
ANISOU 3490  O   GLY A 527    12283   6456  12906   1272  -1255    150       O
ATOM   3491  N   THR A 528      41.605   8.006  12.745  1.00 82.66           N
ANISOU 3491  N   THR A 528    12341   6239  12826   1364  -1679    101       N
ATOM   3492  CA  THR A 528      41.210   9.041  13.699  1.00 83.06           C
ANISOU 3492  CA  THR A 528    12650   6255  12655   1450  -1723    117       C
ATOM   3493  C   THR A 528      41.478  10.459  13.163  1.00 86.04           C
ANISOU 3493  C   THR A 528    12922   6701  13070   1398  -1809     38       C
ATOM   3494  O   THR A 528      40.620  11.306  13.401  1.00 85.04           O
ANISOU 3494  O   THR A 528    12903   6611  12798   1415  -1701     55       O
ATOM   3495  CB  THR A 528      41.763   8.775  15.080  1.00 92.08           C
ANISOU 3495  CB  THR A 528    14095   7250  13643   1586  -1910    152       C
ATOM   3496  OG1 THR A 528      43.146   8.450  14.951  1.00 93.97           O
ANISOU 3496  OG1 THR A 528    14224   7430  14050   1577  -2166     97       O
ATOM   3497  CG2 THR A 528      41.017   7.662  15.786  1.00 90.53           C
ANISOU 3497  CG2 THR A 528    14086   6987  13324   1659  -1737    252       C
ATOM   3498  N   PRO A 529      42.577  10.775  12.407  1.00 82.68           N
ANISOU 3498  N   PRO A 529    12281   6290  12844   1332  -1973    -45       N
ATOM   3499  CA  PRO A 529      42.720  12.147  11.876  1.00 81.91           C
ANISOU 3499  CA  PRO A 529    12086   6256  12780   1284  -2017   -113       C
ATOM   3500  C   PRO A 529      41.510  12.610  11.062  1.00 85.22           C
ANISOU 3500  C   PRO A 529    12409   6803  13168   1212  -1767   -104       C
ATOM   3501  O   PRO A 529      40.845  11.796  10.425  1.00 85.86           O
ANISOU 3501  O   PRO A 529    12377   6937  13308   1159  -1580    -74       O
ATOM   3502  CB  PRO A 529      43.974  12.069  10.991  1.00 83.10           C
ANISOU 3502  CB  PRO A 529    11977   6397  13202   1212  -2148   -187       C
ATOM   3503  CG  PRO A 529      44.201  10.642  10.755  1.00 87.81           C
ANISOU 3503  CG  PRO A 529    12491   6962  13910   1196  -2104   -156       C
ATOM   3504  CD  PRO A 529      43.726   9.946  11.993  1.00 84.66           C
ANISOU 3504  CD  PRO A 529    12365   6490  13314   1301  -2108    -77       C
ATOM   3505  N   GLN A 530      41.211  13.904  11.121  1.00 79.79           N
ANISOU 3505  N   GLN A 530    11774   6155  12389   1215  -1774   -131       N
ATOM   3506  CA  GLN A 530      40.096  14.518  10.415  1.00 77.94           C
ANISOU 3506  CA  GLN A 530    11460   6031  12123   1155  -1568   -127       C
ATOM   3507  C   GLN A 530      40.418  14.631   8.918  1.00 76.48           C
ANISOU 3507  C   GLN A 530    10984   5929  12144   1041  -1529   -192       C
ATOM   3508  O   GLN A 530      41.475  15.152   8.545  1.00 75.75           O
ANISOU 3508  O   GLN A 530    10787   5820  12174   1017  -1676   -258       O
ATOM   3509  CB  GLN A 530      39.804  15.941  10.982  1.00 80.24           C
ANISOU 3509  CB  GLN A 530    11902   6327  12257   1198  -1610   -140       C
ATOM   3510  CG  GLN A 530      39.460  16.033  12.482  1.00 94.73           C
ANISOU 3510  CG  GLN A 530    14071   8066  13857   1323  -1646    -80       C
ATOM   3511  CD  GLN A 530      38.043  15.614  12.808  1.00107.36           C
ANISOU 3511  CD  GLN A 530    15788   9672  15333   1350  -1387      9       C
ATOM   3512  OE1 GLN A 530      37.719  14.425  12.864  1.00103.86           O
ANISOU 3512  OE1 GLN A 530    15337   9203  14923   1356  -1279     63       O
ATOM   3513  NE2 GLN A 530      37.177  16.581  13.071  1.00 91.11           N
ANISOU 3513  NE2 GLN A 530    13841   7634  13142   1373  -1277     30       N
ATOM   3514  N   VAL A 531      39.487  14.162   8.072  1.00 68.65           N
ANISOU 3514  N   VAL A 531     9875   5013  11195    976  -1328   -173       N
ATOM   3515  CA  VAL A 531      39.541  14.250   6.606  1.00 65.25           C
ANISOU 3515  CA  VAL A 531     9212   4658  10921    875  -1258   -228       C
ATOM   3516  C   VAL A 531      38.271  14.945   6.079  1.00 64.34           C
ANISOU 3516  C   VAL A 531     9073   4631  10742    838  -1097   -222       C
ATOM   3517  O   VAL A 531      37.234  14.946   6.753  1.00 62.92           O
ANISOU 3517  O   VAL A 531     9019   4449  10440    879   -996   -162       O
ATOM   3518  CB  VAL A 531      39.692  12.858   5.906  1.00 68.19           C
ANISOU 3518  CB  VAL A 531     9452   5022  11436    828  -1194   -222       C
ATOM   3519  CG1 VAL A 531      40.958  12.139   6.331  1.00 68.32           C
ANISOU 3519  CG1 VAL A 531     9471   4946  11541    861  -1348   -226       C
ATOM   3520  CG2 VAL A 531      38.462  11.976   6.120  1.00 68.31           C
ANISOU 3520  CG2 VAL A 531     9512   5048  11395    835  -1026   -154       C
ATOM   3521  N   LEU A 532      38.338  15.493   4.855  1.00 57.79           N
ANISOU 3521  N   LEU A 532     8087   3867  10005    764  -1066   -281       N
ATOM   3522  CA  LEU A 532      37.172  15.984   4.138  1.00 55.22           C
ANISOU 3522  CA  LEU A 532     7712   3618   9652    720   -927   -282       C
ATOM   3523  C   LEU A 532      36.856  14.823   3.174  1.00 59.56           C
ANISOU 3523  C   LEU A 532     8134   4178  10318    662   -834   -284       C
ATOM   3524  O   LEU A 532      37.778  14.169   2.674  1.00 60.40           O
ANISOU 3524  O   LEU A 532     8155   4257  10539    636   -883   -314       O
ATOM   3525  CB  LEU A 532      37.451  17.254   3.311  1.00 53.95           C
ANISOU 3525  CB  LEU A 532     7475   3512   9514    679   -954   -348       C
ATOM   3526  CG  LEU A 532      37.995  18.497   4.013  1.00 57.77           C
ANISOU 3526  CG  LEU A 532     8044   3982   9923    722  -1067   -370       C
ATOM   3527  CD1 LEU A 532      38.554  19.463   3.017  1.00 56.72           C
ANISOU 3527  CD1 LEU A 532     7796   3884   9871    673  -1090   -441       C
ATOM   3528  CD2 LEU A 532      36.950  19.173   4.819  1.00 58.32           C
ANISOU 3528  CD2 LEU A 532     8254   4072   9832    765  -1011   -325       C
ATOM   3529  N   PRO A 533      35.568  14.519   2.933  1.00 55.80           N
ANISOU 3529  N   PRO A 533     7643   3729   9831    644   -704   -251       N
ATOM   3530  CA  PRO A 533      35.203  13.428   1.994  1.00 54.93           C
ANISOU 3530  CA  PRO A 533     7416   3620   9837    589   -631   -259       C
ATOM   3531  C   PRO A 533      35.824  13.545   0.579  1.00 54.58           C
ANISOU 3531  C   PRO A 533     7249   3603   9888    524   -658   -336       C
ATOM   3532  O   PRO A 533      36.125  12.519  -0.055  1.00 52.61           O
ANISOU 3532  O   PRO A 533     6926   3328   9736    491   -641   -351       O
ATOM   3533  CB  PRO A 533      33.674  13.525   1.947  1.00 56.43           C
ANISOU 3533  CB  PRO A 533     7604   3828  10010    582   -511   -223       C
ATOM   3534  CG  PRO A 533      33.298  14.177   3.245  1.00 60.59           C
ANISOU 3534  CG  PRO A 533     8278   4335  10407    652   -491   -167       C
ATOM   3535  CD  PRO A 533      34.369  15.165   3.499  1.00 56.78           C
ANISOU 3535  CD  PRO A 533     7852   3868   9854    673   -617   -206       C
ATOM   3536  N   ILE A 534      36.022  14.801   0.092  1.00 48.76           N
ANISOU 3536  N   ILE A 534     6502   2907   9118    510   -688   -383       N
ATOM   3537  CA  ILE A 534      36.633  15.093  -1.206  1.00 48.09           C
ANISOU 3537  CA  ILE A 534     6333   2835   9105    460   -694   -452       C
ATOM   3538  C   ILE A 534      38.068  14.500  -1.291  1.00 53.65           C
ANISOU 3538  C   ILE A 534     6992   3479   9915    458   -750   -474       C
ATOM   3539  O   ILE A 534      38.476  13.978  -2.336  1.00 50.59           O
ANISOU 3539  O   ILE A 534     6534   3068   9618    419   -714   -511       O
ATOM   3540  CB  ILE A 534      36.519  16.598  -1.588  1.00 51.08           C
ANISOU 3540  CB  ILE A 534     6724   3262   9422    455   -701   -489       C
ATOM   3541  CG1 ILE A 534      37.130  16.895  -2.966  1.00 51.45           C
ANISOU 3541  CG1 ILE A 534     6707   3305   9535    413   -683   -556       C
ATOM   3542  CG2 ILE A 534      37.058  17.561  -0.516  1.00 53.55           C
ANISOU 3542  CG2 ILE A 534     7107   3572   9669    503   -781   -478       C
ATOM   3543  CD1 ILE A 534      36.171  17.260  -3.937  1.00 64.12           C
ANISOU 3543  CD1 ILE A 534     8308   4951  11104    383   -628   -580       C
ATOM   3544  N   GLN A 535      38.786  14.530  -0.147  1.00 52.89           N
ANISOU 3544  N   GLN A 535     6946   3342   9808    507   -842   -449       N
ATOM   3545  CA  GLN A 535      40.122  13.976   0.067  1.00 52.29           C
ANISOU 3545  CA  GLN A 535     6830   3191   9847    518   -923   -460       C
ATOM   3546  C   GLN A 535      40.069  12.467   0.004  1.00 55.20           C
ANISOU 3546  C   GLN A 535     7169   3526  10281    507   -882   -431       C
ATOM   3547  O   GLN A 535      40.976  11.859  -0.555  1.00 54.38           O
ANISOU 3547  O   GLN A 535     6983   3370  10310    483   -885   -456       O
ATOM   3548  CB  GLN A 535      40.675  14.436   1.417  1.00 53.80           C
ANISOU 3548  CB  GLN A 535     7112   3342   9988    583  -1058   -438       C
ATOM   3549  CG  GLN A 535      40.894  15.926   1.465  1.00 53.77           C
ANISOU 3549  CG  GLN A 535     7126   3359   9945    593  -1112   -474       C
ATOM   3550  CD  GLN A 535      41.377  16.420   2.793  1.00 73.21           C
ANISOU 3550  CD  GLN A 535     9701   5775  12340    662  -1260   -458       C
ATOM   3551  OE1 GLN A 535      41.141  15.809   3.858  1.00 67.26           O
ANISOU 3551  OE1 GLN A 535     9064   4989  11501    716  -1302   -405       O
ATOM   3552  NE2 GLN A 535      42.048  17.570   2.740  1.00 64.01           N
ANISOU 3552  NE2 GLN A 535     8516   4598  11209    666  -1341   -504       N
ATOM   3553  N   MET A 536      38.999  11.862   0.545  1.00 53.82           N
ANISOU 3553  N   MET A 536     7054   3369  10025    525   -828   -376       N
ATOM   3554  CA  MET A 536      38.770  10.403   0.470  1.00 55.38           C
ANISOU 3554  CA  MET A 536     7222   3536  10284    514   -773   -345       C
ATOM   3555  C   MET A 536      38.501   9.986  -0.984  1.00 59.39           C
ANISOU 3555  C   MET A 536     7632   4060  10873    446   -689   -390       C
ATOM   3556  O   MET A 536      39.062   9.000  -1.420  1.00 61.50           O
ANISOU 3556  O   MET A 536     7842   4284  11243    425   -675   -400       O
ATOM   3557  CB  MET A 536      37.608   9.929   1.378  1.00 58.27           C
ANISOU 3557  CB  MET A 536     7674   3904  10563    552   -711   -274       C
ATOM   3558  CG  MET A 536      37.851  10.090   2.876  1.00 63.51           C
ANISOU 3558  CG  MET A 536     8479   4526  11126    632   -782   -221       C
ATOM   3559  SD  MET A 536      39.433   9.476   3.476  1.00 69.44           S
ANISOU 3559  SD  MET A 536     9245   5192  11948    670   -929   -221       S
ATOM   3560  CE  MET A 536      39.269   7.783   3.062  1.00 67.29           C
ANISOU 3560  CE  MET A 536     8894   4890  11785    640   -838   -196       C
ATOM   3561  N   ALA A 537      37.686  10.749  -1.737  1.00 54.69           N
ANISOU 3561  N   ALA A 537     7030   3520  10229    418   -641   -420       N
ATOM   3562  CA  ALA A 537      37.395  10.484  -3.154  1.00 53.26           C
ANISOU 3562  CA  ALA A 537     6792   3344  10099    363   -583   -470       C
ATOM   3563  C   ALA A 537      38.678  10.598  -3.994  1.00 57.34           C
ANISOU 3563  C   ALA A 537     7268   3821  10700    342   -590   -523       C
ATOM   3564  O   ALA A 537      38.888   9.800  -4.903  1.00 56.93           O
ANISOU 3564  O   ALA A 537     7180   3730  10720    310   -543   -550       O
ATOM   3565  CB  ALA A 537      36.335  11.452  -3.659  1.00 52.50           C
ANISOU 3565  CB  ALA A 537     6716   3304   9926    349   -559   -490       C
ATOM   3566  N   THR A 538      39.562  11.551  -3.642  1.00 54.36           N
ANISOU 3566  N   THR A 538     6894   3436  10324    364   -645   -536       N
ATOM   3567  CA  THR A 538      40.872  11.742  -4.285  1.00 53.94           C
ANISOU 3567  CA  THR A 538     6788   3321  10386    351   -642   -579       C
ATOM   3568  C   THR A 538      41.774  10.522  -4.032  1.00 57.37           C
ANISOU 3568  C   THR A 538     7169   3677  10952    353   -657   -562       C
ATOM   3569  O   THR A 538      42.450  10.055  -4.955  1.00 56.18           O
ANISOU 3569  O   THR A 538     6969   3466  10911    326   -593   -593       O
ATOM   3570  CB  THR A 538      41.541  13.027  -3.796  1.00 55.51           C
ANISOU 3570  CB  THR A 538     6990   3518  10584    377   -711   -593       C
ATOM   3571  OG1 THR A 538      40.589  14.102  -3.833  1.00 61.90           O
ANISOU 3571  OG1 THR A 538     7856   4406  11258    380   -702   -599       O
ATOM   3572  CG2 THR A 538      42.774  13.381  -4.617  1.00 47.44           C
ANISOU 3572  CG2 THR A 538     5901   2421   9703    361   -676   -641       C
ATOM   3573  N   GLY A 539      41.752  10.037  -2.787  1.00 53.52           N
ANISOU 3573  N   GLY A 539     6707   3184  10445    391   -734   -510       N
ATOM   3574  CA  GLY A 539      42.517   8.893  -2.316  1.00 53.29           C
ANISOU 3574  CA  GLY A 539     6640   3082  10525    403   -771   -484       C
ATOM   3575  C   GLY A 539      42.110   7.580  -2.932  1.00 57.58           C
ANISOU 3575  C   GLY A 539     7156   3613  11108    370   -681   -476       C
ATOM   3576  O   GLY A 539      42.969   6.762  -3.249  1.00 59.19           O
ANISOU 3576  O   GLY A 539     7298   3746  11446    356   -664   -483       O
ATOM   3577  N   TYR A 540      40.805   7.342  -3.061  1.00 51.87           N
ANISOU 3577  N   TYR A 540     6473   2950  10286    359   -626   -460       N
ATOM   3578  CA  TYR A 540      40.254   6.120  -3.659  1.00 51.04           C
ANISOU 3578  CA  TYR A 540     6342   2831  10220    328   -551   -458       C
ATOM   3579  C   TYR A 540      40.425   6.075  -5.166  1.00 55.82           C
ANISOU 3579  C   TYR A 540     6921   3415  10873    280   -479   -521       C
ATOM   3580  O   TYR A 540      40.478   4.996  -5.737  1.00 57.64           O
ANISOU 3580  O   TYR A 540     7126   3603  11173    255   -429   -529       O
ATOM   3581  CB  TYR A 540      38.778   5.929  -3.270  1.00 50.50           C
ANISOU 3581  CB  TYR A 540     6313   2811  10063    334   -522   -421       C
ATOM   3582  CG  TYR A 540      38.647   5.180  -1.972  1.00 50.17           C
ANISOU 3582  CG  TYR A 540     6302   2747  10014    379   -539   -350       C
ATOM   3583  CD1 TYR A 540      38.390   3.809  -1.960  1.00 49.64           C
ANISOU 3583  CD1 TYR A 540     6205   2642  10016    369   -489   -322       C
ATOM   3584  CD2 TYR A 540      38.909   5.806  -0.755  1.00 51.62           C
ANISOU 3584  CD2 TYR A 540     6559   2933  10122    436   -609   -310       C
ATOM   3585  CE1 TYR A 540      38.334   3.095  -0.772  1.00 47.44           C
ANISOU 3585  CE1 TYR A 540     5969   2330   9728    417   -494   -253       C
ATOM   3586  CE2 TYR A 540      38.890   5.092   0.440  1.00 54.03           C
ANISOU 3586  CE2 TYR A 540     6926   3198  10404    488   -626   -243       C
ATOM   3587  CZ  TYR A 540      38.602   3.735   0.424  1.00 60.11           C
ANISOU 3587  CZ  TYR A 540     7664   3932  11242    480   -562   -213       C
ATOM   3588  OH  TYR A 540      38.501   3.040   1.601  1.00 68.06           O
ANISOU 3588  OH  TYR A 540     8748   4894  12217    538   -561   -142       O
ATOM   3589  N   ALA A 541      40.543   7.243  -5.793  1.00 51.21           N
ANISOU 3589  N   ALA A 541     6358   2852  10248    273   -471   -564       N
ATOM   3590  CA  ALA A 541      40.763   7.469  -7.214  1.00 50.55           C
ANISOU 3590  CA  ALA A 541     6288   2736  10182    242   -398   -624       C
ATOM   3591  C   ALA A 541      42.074   6.898  -7.612  1.00 53.64           C
ANISOU 3591  C   ALA A 541     6632   3032  10716    234   -350   -638       C
ATOM   3592  O   ALA A 541      42.257   6.600  -8.783  1.00 53.19           O
ANISOU 3592  O   ALA A 541     6601   2922  10685    211   -263   -679       O
ATOM   3593  CB  ALA A 541      40.746   8.971  -7.508  1.00 51.18           C
ANISOU 3593  CB  ALA A 541     6405   2853  10189    250   -403   -655       C
ATOM   3594  N   THR A 542      42.998   6.761  -6.628  1.00 51.09           N
ANISOU 3594  N   THR A 542     6249   2674  10490    258   -410   -604       N
ATOM   3595  CA  THR A 542      44.337   6.210  -6.790  1.00 51.31           C
ANISOU 3595  CA  THR A 542     6205   2595  10696    255   -381   -608       C
ATOM   3596  C   THR A 542      44.235   4.767  -7.188  1.00 55.19           C
ANISOU 3596  C   THR A 542     6684   3045  11240    233   -320   -600       C
ATOM   3597  O   THR A 542      45.021   4.332  -8.008  1.00 59.29           O
ANISOU 3597  O   THR A 542     7177   3474  11874    215   -230   -624       O
ATOM   3598  CB  THR A 542      45.165   6.403  -5.510  1.00 63.55           C
ANISOU 3598  CB  THR A 542     7701   4117  12329    292   -503   -573       C
ATOM   3599  OG1 THR A 542      44.991   7.744  -5.048  1.00 64.48           O
ANISOU 3599  OG1 THR A 542     7851   4288  12360    315   -575   -580       O
ATOM   3600  CG2 THR A 542      46.666   6.106  -5.704  1.00 62.36           C
ANISOU 3600  CG2 THR A 542     7452   3836  12404    291   -486   -584       C
ATOM   3601  N   PHE A 543      43.273   4.021  -6.635  1.00 48.87           N
ANISOU 3601  N   PHE A 543     5903   2298  10366    235   -355   -565       N
ATOM   3602  CA  PHE A 543      43.073   2.619  -6.980  1.00 49.13           C
ANISOU 3602  CA  PHE A 543     5923   2294  10451    213   -301   -557       C
ATOM   3603  C   PHE A 543      42.483   2.524  -8.360  1.00 52.56           C
ANISOU 3603  C   PHE A 543     6415   2722  10833    180   -216   -611       C
ATOM   3604  O   PHE A 543      43.100   1.928  -9.228  1.00 52.22           O
ANISOU 3604  O   PHE A 543     6372   2598  10872    161   -133   -638       O
ATOM   3605  CB  PHE A 543      42.212   1.892  -5.937  1.00 51.29           C
ANISOU 3605  CB  PHE A 543     6199   2613  10675    231   -353   -501       C
ATOM   3606  CG  PHE A 543      42.659   2.114  -4.516  1.00 53.47           C
ANISOU 3606  CG  PHE A 543     6468   2895  10955    278   -451   -448       C
ATOM   3607  CD1 PHE A 543      43.985   1.929  -4.151  1.00 56.46           C
ANISOU 3607  CD1 PHE A 543     6791   3196  11464    295   -496   -439       C
ATOM   3608  CD2 PHE A 543      41.756   2.524  -3.548  1.00 56.45           C
ANISOU 3608  CD2 PHE A 543     6902   3337  11208    311   -501   -408       C
ATOM   3609  CE1 PHE A 543      44.404   2.167  -2.852  1.00 58.14           C
ANISOU 3609  CE1 PHE A 543     7018   3399  11673    346   -617   -397       C
ATOM   3610  CE2 PHE A 543      42.170   2.757  -2.240  1.00 59.42           C
ANISOU 3610  CE2 PHE A 543     7311   3704  11563    365   -598   -362       C
ATOM   3611  CZ  PHE A 543      43.490   2.557  -1.899  1.00 57.91           C
ANISOU 3611  CZ  PHE A 543     7075   3437  11492    384   -668   -359       C
ATOM   3612  N   ALA A 544      41.362   3.234  -8.579  1.00 50.32           N
ANISOU 3612  N   ALA A 544     6191   2511  10417    177   -241   -629       N
ATOM   3613  CA  ALA A 544      40.587   3.353  -9.815  1.00 50.53           C
ANISOU 3613  CA  ALA A 544     6296   2537  10366    155   -203   -684       C
ATOM   3614  C   ALA A 544      41.396   3.729 -11.053  1.00 55.84           C
ANISOU 3614  C   ALA A 544     7031   3134  11053    148   -114   -738       C
ATOM   3615  O   ALA A 544      41.030   3.315 -12.150  1.00 53.83           O
ANISOU 3615  O   ALA A 544     6859   2835  10761    133    -70   -782       O
ATOM   3616  CB  ALA A 544      39.448   4.351  -9.618  1.00 50.46           C
ANISOU 3616  CB  ALA A 544     6324   2616  10234    163   -265   -686       C
ATOM   3617  N   ASN A 545      42.486   4.506 -10.880  1.00 56.40           N
ANISOU 3617  N   ASN A 545     7070   3176  11183    164    -86   -735       N
ATOM   3618  CA  ASN A 545      43.326   5.034 -11.964  1.00 57.54           C
ANISOU 3618  CA  ASN A 545     7270   3233  11359    166     27   -778       C
ATOM   3619  C   ASN A 545      44.720   4.411 -12.145  1.00 65.08           C
ANISOU 3619  C   ASN A 545     8165   4064  12499    165    126   -770       C
ATOM   3620  O   ASN A 545      45.443   4.800 -13.074  1.00 65.75           O
ANISOU 3620  O   ASN A 545     8302   4053  12627    170    252   -801       O
ATOM   3621  CB  ASN A 545      43.381   6.570 -11.884  1.00 55.77           C
ANISOU 3621  CB  ASN A 545     7064   3050  11074    185      9   -789       C
ATOM   3622  CG  ASN A 545      44.282   7.122 -10.812  1.00 69.80           C
ANISOU 3622  CG  ASN A 545     8731   4829  12963    202    -43   -755       C
ATOM   3623  OD1 ASN A 545      45.148   6.420 -10.253  1.00 58.83           O
ANISOU 3623  OD1 ASN A 545     7249   3380  11725    204    -51   -727       O
ATOM   3624  ND2 ASN A 545      44.075   8.401 -10.484  1.00 57.68           N
ANISOU 3624  ND2 ASN A 545     7205   3355  11357    218    -93   -759       N
ATOM   3625  N   GLY A 546      45.092   3.496 -11.245  1.00 63.93           N
ANISOU 3625  N   GLY A 546     7915   3910  12467    162     77   -726       N
ATOM   3626  CA  GLY A 546      46.362   2.771 -11.295  1.00 65.28           C
ANISOU 3626  CA  GLY A 546     8006   3958  12838    160    154   -713       C
ATOM   3627  C   GLY A 546      47.530   3.360 -10.528  1.00 72.82           C
ANISOU 3627  C   GLY A 546     8842   4864  13963    180    114   -688       C
ATOM   3628  O   GLY A 546      48.687   3.081 -10.862  1.00 73.70           O
ANISOU 3628  O   GLY A 546     8887   4846  14271    179    205   -688       O
ATOM   3629  N   GLY A 547      47.235   4.154  -9.495  1.00 69.86           N
ANISOU 3629  N   GLY A 547     8439   4578  13526    199    -24   -668       N
ATOM   3630  CA  GLY A 547      48.244   4.727  -8.605  1.00 68.98           C
ANISOU 3630  CA  GLY A 547     8223   4421  13565    224   -112   -649       C
ATOM   3631  C   GLY A 547      48.745   6.101  -8.953  1.00 70.58           C
ANISOU 3631  C   GLY A 547     8417   4591  13808    234    -79   -680       C
ATOM   3632  O   GLY A 547      49.911   6.415  -8.713  1.00 70.09           O
ANISOU 3632  O   GLY A 547     8250   4425  13955    246    -91   -678       O
ATOM   3633  N   TYR A 548      47.866   6.932  -9.496  1.00 66.15           N
ANISOU 3633  N   TYR A 548     7960   4110  13063    231    -44   -708       N
ATOM   3634  CA  TYR A 548      48.213   8.292  -9.878  1.00 64.56           C
ANISOU 3634  CA  TYR A 548     7767   3887  12876    242     -1   -737       C
ATOM   3635  C   TYR A 548      47.518   9.268  -8.973  1.00 65.49           C
ANISOU 3635  C   TYR A 548     7904   4128  12852    259   -147   -729       C
ATOM   3636  O   TYR A 548      46.460   8.968  -8.408  1.00 61.51           O
ANISOU 3636  O   TYR A 548     7450   3735  12186    259   -234   -707       O
ATOM   3637  CB  TYR A 548      47.882   8.569 -11.351  1.00 65.45           C
ANISOU 3637  CB  TYR A 548     8003   3970  12893    232    170   -779       C
ATOM   3638  CG  TYR A 548      48.794   7.844 -12.314  1.00 69.13           C
ANISOU 3638  CG  TYR A 548     8468   4280  13517    225    349   -790       C
ATOM   3639  CD1 TYR A 548      49.964   8.436 -12.776  1.00 72.05           C
ANISOU 3639  CD1 TYR A 548     8786   4508  14083    237    481   -801       C
ATOM   3640  CD2 TYR A 548      48.495   6.555 -12.754  1.00 70.44           C
ANISOU 3640  CD2 TYR A 548     8684   4427  13652    208    398   -787       C
ATOM   3641  CE1 TYR A 548      50.818   7.763 -13.648  1.00 74.62           C
ANISOU 3641  CE1 TYR A 548     9114   4670  14568    235    672   -805       C
ATOM   3642  CE2 TYR A 548      49.332   5.880 -13.640  1.00 71.81           C
ANISOU 3642  CE2 TYR A 548     8871   4447  13966    204    576   -796       C
ATOM   3643  CZ  TYR A 548      50.495   6.487 -14.083  1.00 78.24           C
ANISOU 3643  CZ  TYR A 548     9639   5116  14973    219    720   -803       C
ATOM   3644  OH  TYR A 548      51.315   5.835 -14.968  1.00 75.33           O
ANISOU 3644  OH  TYR A 548     9292   4580  14751    219    923   -806       O
ATOM   3645  N   ARG A 549      48.143  10.459  -8.852  1.00 63.31           N
ANISOU 3645  N   ARG A 549     7585   3818  12652    275   -161   -745       N
ATOM   3646  CA  ARG A 549      47.707  11.581  -8.044  1.00 62.95           C
ANISOU 3646  CA  ARG A 549     7555   3864  12497    295   -287   -742       C
ATOM   3647  C   ARG A 549      46.970  12.568  -8.912  1.00 66.58           C
ANISOU 3647  C   ARG A 549     8115   4386  12795    290   -202   -774       C
ATOM   3648  O   ARG A 549      47.601  13.353  -9.617  1.00 67.24           O
ANISOU 3648  O   ARG A 549     8190   4396  12964    294   -101   -803       O
ATOM   3649  CB  ARG A 549      48.928  12.249  -7.370  1.00 63.50           C
ANISOU 3649  CB  ARG A 549     7509   3842  12776    317   -370   -746       C
ATOM   3650  CG  ARG A 549      48.631  13.365  -6.375  1.00 61.19           C
ANISOU 3650  CG  ARG A 549     7234   3628  12388    344   -527   -743       C
ATOM   3651  CD  ARG A 549      49.425  14.595  -6.756  1.00 84.62           C
ANISOU 3651  CD  ARG A 549    10144   6520  15487    351   -486   -779       C
ATOM   3652  NE  ARG A 549      50.741  14.681  -6.113  1.00108.23           N
ANISOU 3652  NE  ARG A 549    12995   9373  18755    369   -583   -782       N
ATOM   3653  CZ  ARG A 549      51.768  15.385  -6.594  1.00131.66           C
ANISOU 3653  CZ  ARG A 549    15860  12207  21956    369   -503   -811       C
ATOM   3654  NH1 ARG A 549      51.665  16.011  -7.762  1.00123.28           N
ANISOU 3654  NH1 ARG A 549    14842  11132  20869    356   -302   -835       N
ATOM   3655  NH2 ARG A 549      52.918  15.433  -5.931  1.00119.85           N
ANISOU 3655  NH2 ARG A 549    14224  10577  20739    386   -619   -815       N
ATOM   3656  N   VAL A 550      45.627  12.536  -8.851  1.00 62.22           N
ANISOU 3656  N   VAL A 550     7657   3958  12025    284   -242   -767       N
ATOM   3657  CA  VAL A 550      44.778  13.504  -9.547  1.00 60.38           C
ANISOU 3657  CA  VAL A 550     7522   3792  11629    283   -196   -795       C
ATOM   3658  C   VAL A 550      44.307  14.563  -8.543  1.00 63.60           C
ANISOU 3658  C   VAL A 550     7927   4295  11943    302   -317   -781       C
ATOM   3659  O   VAL A 550      44.183  14.243  -7.346  1.00 62.75           O
ANISOU 3659  O   VAL A 550     7788   4224  11831    315   -438   -745       O
ATOM   3660  CB  VAL A 550      43.615  12.891 -10.354  1.00 62.67           C
ANISOU 3660  CB  VAL A 550     7916   4130  11767    265   -153   -807       C
ATOM   3661  CG1 VAL A 550      44.139  12.017 -11.482  1.00 62.97           C
ANISOU 3661  CG1 VAL A 550     7987   4057  11880    253    -20   -829       C
ATOM   3662  CG2 VAL A 550      42.636  12.136  -9.455  1.00 62.20           C
ANISOU 3662  CG2 VAL A 550     7849   4158  11627    260   -260   -769       C
ATOM   3663  N   GLN A 551      44.088  15.824  -9.014  1.00 58.73           N
ANISOU 3663  N   GLN A 551     7357   3706  11252    309   -281   -808       N
ATOM   3664  CA  GLN A 551      43.611  16.887  -8.129  1.00 58.26           C
ANISOU 3664  CA  GLN A 551     7306   3734  11098    326   -385   -797       C
ATOM   3665  C   GLN A 551      42.136  17.152  -8.431  1.00 61.91           C
ANISOU 3665  C   GLN A 551     7862   4302  11360    319   -384   -797       C
ATOM   3666  O   GLN A 551      41.834  17.426  -9.597  1.00 63.41           O
ANISOU 3666  O   GLN A 551     8118   4480  11494    311   -294   -829       O
ATOM   3667  CB  GLN A 551      44.406  18.202  -8.312  1.00 60.29           C
ANISOU 3667  CB  GLN A 551     7531   3944  11434    340   -357   -826       C
ATOM   3668  CG  GLN A 551      45.909  18.079  -8.637  1.00 88.07           C
ANISOU 3668  CG  GLN A 551    10951   7314  15197    343   -294   -841       C
ATOM   3669  CD  GLN A 551      46.678  19.356  -8.331  1.00109.32           C
ANISOU 3669  CD  GLN A 551    13579   9958  17999    361   -320   -861       C
ATOM   3670  OE1 GLN A 551      46.814  19.763  -7.173  1.00103.53           O
ANISOU 3670  OE1 GLN A 551    12809   9255  17274    379   -473   -850       O
ATOM   3671  NE2 GLN A 551      47.236  20.001  -9.352  1.00103.55           N
ANISOU 3671  NE2 GLN A 551    12842   9139  17363    362   -168   -891       N
ATOM   3672  N   PRO A 552      41.193  17.098  -7.445  1.00 56.27           N
ANISOU 3672  N   PRO A 552     7164   3676  10541    328   -478   -760       N
ATOM   3673  CA  PRO A 552      39.786  17.435  -7.756  1.00 54.65           C
ANISOU 3673  CA  PRO A 552     7028   3554  10184    321   -474   -760       C
ATOM   3674  C   PRO A 552      39.638  18.872  -8.243  1.00 57.52           C
ANISOU 3674  C   PRO A 552     7430   3944  10479    328   -448   -790       C
ATOM   3675  O   PRO A 552      40.270  19.782  -7.718  1.00 56.50           O
ANISOU 3675  O   PRO A 552     7274   3812  10380    345   -476   -792       O
ATOM   3676  CB  PRO A 552      39.035  17.170  -6.448  1.00 56.05           C
ANISOU 3676  CB  PRO A 552     7203   3790  10302    336   -555   -707       C
ATOM   3677  CG  PRO A 552      40.052  17.251  -5.403  1.00 61.53           C
ANISOU 3677  CG  PRO A 552     7860   4450  11068    362   -624   -689       C
ATOM   3678  CD  PRO A 552      41.369  16.825  -6.007  1.00 57.79           C
ANISOU 3678  CD  PRO A 552     7325   3880  10751    351   -586   -717       C
ATOM   3679  N   HIS A 553      38.828  19.046  -9.278  1.00 54.80           N
ANISOU 3679  N   HIS A 553     7155   3617  10050    317   -402   -816       N
ATOM   3680  CA  HIS A 553      38.622  20.310  -9.942  1.00 55.06           C
ANISOU 3680  CA  HIS A 553     7244   3669  10009    325   -368   -847       C
ATOM   3681  C   HIS A 553      37.176  20.454 -10.434  1.00 53.74           C
ANISOU 3681  C   HIS A 553     7144   3556   9719    319   -394   -853       C
ATOM   3682  O   HIS A 553      36.618  19.478 -10.917  1.00 52.13           O
ANISOU 3682  O   HIS A 553     6965   3331   9510    305   -401   -859       O
ATOM   3683  CB  HIS A 553      39.720  20.520 -11.036  1.00 58.09           C
ANISOU 3683  CB  HIS A 553     7656   3953  10463    330   -255   -887       C
ATOM   3684  CG  HIS A 553      39.527  19.794 -12.338  1.00 63.37           C
ANISOU 3684  CG  HIS A 553     8415   4560  11103    323   -183   -917       C
ATOM   3685  ND1 HIS A 553      39.938  18.472 -12.506  1.00 67.04           N
ANISOU 3685  ND1 HIS A 553     8860   4965  11648    310   -160   -912       N
ATOM   3686  CD2 HIS A 553      39.047  20.254 -13.519  1.00 66.36           C
ANISOU 3686  CD2 HIS A 553     8920   4916  11379    334   -133   -953       C
ATOM   3687  CE1 HIS A 553      39.639  18.157 -13.761  1.00 67.21           C
ANISOU 3687  CE1 HIS A 553     9000   4932  11607    312    -99   -947       C
ATOM   3688  NE2 HIS A 553      39.118  19.206 -14.416  1.00 67.44           N
ANISOU 3688  NE2 HIS A 553     9128   4976  11520    329    -85   -974       N
ATOM   3689  N   PHE A 554      36.559  21.659 -10.289  1.00 47.96           N
ANISOU 3689  N   PHE A 554     6434   2886   8903    330   -418   -852       N
ATOM   3690  CA  PHE A 554      35.168  21.861 -10.696  1.00 46.99           C
ANISOU 3690  CA  PHE A 554     6358   2805   8691    326   -458   -855       C
ATOM   3691  C   PHE A 554      34.953  22.782 -11.902  1.00 50.93           C
ANISOU 3691  C   PHE A 554     6954   3289   9108    337   -428   -900       C
ATOM   3692  O   PHE A 554      33.841  22.870 -12.389  1.00 50.32           O
ANISOU 3692  O   PHE A 554     6921   3226   8970    336   -477   -910       O
ATOM   3693  CB  PHE A 554      34.244  22.212  -9.501  1.00 48.30           C
ANISOU 3693  CB  PHE A 554     6476   3046   8829    329   -515   -807       C
ATOM   3694  CG  PHE A 554      34.479  23.564  -8.874  1.00 50.15           C
ANISOU 3694  CG  PHE A 554     6707   3326   9020    348   -515   -798       C
ATOM   3695  CD1 PHE A 554      33.903  24.716  -9.416  1.00 52.42           C
ANISOU 3695  CD1 PHE A 554     7041   3646   9232    355   -511   -817       C
ATOM   3696  CD2 PHE A 554      35.229  23.687  -7.717  1.00 51.99           C
ANISOU 3696  CD2 PHE A 554     6901   3566   9288    362   -532   -771       C
ATOM   3697  CE1 PHE A 554      34.121  25.967  -8.834  1.00 52.68           C
ANISOU 3697  CE1 PHE A 554     7070   3719   9228    372   -508   -809       C
ATOM   3698  CE2 PHE A 554      35.462  24.945  -7.146  1.00 54.39           C
ANISOU 3698  CE2 PHE A 554     7210   3902   9553    382   -544   -769       C
ATOM   3699  CZ  PHE A 554      34.891  26.073  -7.697  1.00 52.53           C
ANISOU 3699  CZ  PHE A 554     7011   3702   9245    384   -525   -787       C
ATOM   3700  N   ILE A 555      35.994  23.455 -12.385  1.00 50.09           N
ANISOU 3700  N   ILE A 555     6882   3139   9012    352   -348   -925       N
ATOM   3701  CA  ILE A 555      35.882  24.389 -13.514  1.00 51.84           C
ANISOU 3701  CA  ILE A 555     7215   3333   9146    373   -300   -964       C
ATOM   3702  C   ILE A 555      36.502  23.789 -14.753  1.00 59.82           C
ANISOU 3702  C   ILE A 555     8331   4236  10162    383   -213  -1001       C
ATOM   3703  O   ILE A 555      37.661  23.392 -14.695  1.00 62.27           O
ANISOU 3703  O   ILE A 555     8602   4483  10575    382   -130   -999       O
ATOM   3704  CB  ILE A 555      36.539  25.785 -13.191  1.00 54.98           C
ANISOU 3704  CB  ILE A 555     7590   3750   9551    390   -249   -963       C
ATOM   3705  CG1 ILE A 555      35.901  26.465 -11.960  1.00 54.68           C
ANISOU 3705  CG1 ILE A 555     7474   3812   9490    386   -331   -927       C
ATOM   3706  CG2 ILE A 555      36.490  26.707 -14.396  1.00 56.79           C
ANISOU 3706  CG2 ILE A 555     7948   3938   9692    417   -180  -1000       C
ATOM   3707  CD1 ILE A 555      36.471  27.848 -11.569  1.00 65.54           C
ANISOU 3707  CD1 ILE A 555     8826   5206  10872    402   -300   -930       C
ATOM   3708  N   GLN A 556      35.780  23.775 -15.886  1.00 57.88           N
ANISOU 3708  N   GLN A 556     8227   3954   9809    398   -229  -1035       N
ATOM   3709  CA  GLN A 556      36.331  23.293 -17.172  1.00 59.16           C
ANISOU 3709  CA  GLN A 556     8541   3996   9943    421   -135  -1074       C
ATOM   3710  C   GLN A 556      36.820  24.504 -17.965  1.00 63.71           C
ANISOU 3710  C   GLN A 556     9236   4520  10452    461    -23  -1096       C
ATOM   3711  O   GLN A 556      37.921  24.485 -18.520  1.00 62.65           O
ANISOU 3711  O   GLN A 556     9159   4281  10363    481    131  -1107       O
ATOM   3712  CB  GLN A 556      35.317  22.460 -17.995  1.00 61.10           C
ANISOU 3712  CB  GLN A 556     8905   4206  10105    423   -230  -1104       C
ATOM   3713  CG  GLN A 556      35.777  21.030 -18.270  1.00 94.18           C
ANISOU 3713  CG  GLN A 556    13114   8315  14353    411   -195  -1114       C
ATOM   3714  CD  GLN A 556      37.136  20.885 -18.958  1.00124.91           C
ANISOU 3714  CD  GLN A 556    17094  12088  18278    435    -11  -1128       C
ATOM   3715  OE1 GLN A 556      37.502  21.645 -19.871  1.00122.64           O
ANISOU 3715  OE1 GLN A 556    16960  11727  17909    477     91  -1152       O
ATOM   3716  NE2 GLN A 556      37.904  19.874 -18.547  1.00114.57           N
ANISOU 3716  NE2 GLN A 556    15693  10744  17096    413     44  -1110       N
ATOM   3717  N   ARG A 557      35.995  25.557 -18.017  1.00 62.63           N
ANISOU 3717  N   ARG A 557     9135   4445  10216    474    -88  -1100       N
ATOM   3718  CA  ARG A 557      36.386  26.807 -18.665  1.00 64.42           C
ANISOU 3718  CA  ARG A 557     9469   4632  10377    514     16  -1116       C
ATOM   3719  C   ARG A 557      35.637  28.018 -18.097  1.00 69.02           C
ANISOU 3719  C   ARG A 557     9995   5320  10910    513    -63  -1101       C
ATOM   3720  O   ARG A 557      34.524  27.883 -17.583  1.00 69.81           O
ANISOU 3720  O   ARG A 557    10035   5503  10985    491   -207  -1088       O
ATOM   3721  CB  ARG A 557      36.275  26.731 -20.216  1.00 67.86           C
ANISOU 3721  CB  ARG A 557    10161   4946  10677    563     73  -1159       C
ATOM   3722  CG  ARG A 557      34.869  26.947 -20.763  1.00 80.89           C
ANISOU 3722  CG  ARG A 557    11935   6623  12178    580    -86  -1183       C
ATOM   3723  CD  ARG A 557      34.748  26.763 -22.266  1.00 88.59           C
ANISOU 3723  CD  ARG A 557    13191   7463  13004    636    -60  -1230       C
ATOM   3724  NE  ARG A 557      33.380  27.041 -22.712  1.00 93.22           N
ANISOU 3724  NE  ARG A 557    13883   8069  13468    655   -247  -1256       N
ATOM   3725  CZ  ARG A 557      32.385  26.157 -22.712  1.00104.36           C
ANISOU 3725  CZ  ARG A 557    15279   9490  14883    634   -434  -1273       C
ATOM   3726  NH1 ARG A 557      32.595  24.906 -22.311  1.00100.34           N
ANISOU 3726  NH1 ARG A 557    14669   8980  14477    595   -449  -1266       N
ATOM   3727  NH2 ARG A 557      31.174  26.514 -23.117  1.00 76.05           N
ANISOU 3727  NH2 ARG A 557    11774   5907  11217    653   -610  -1298       N
ATOM   3728  N   ILE A 558      36.258  29.192 -18.185  1.00 65.43           N
ANISOU 3728  N   ILE A 558     9554   4850  10455    536     43  -1102       N
ATOM   3729  CA  ILE A 558      35.618  30.453 -17.834  1.00 65.07           C
ANISOU 3729  CA  ILE A 558     9486   4889  10350    543     -7  -1093       C
ATOM   3730  C   ILE A 558      35.666  31.343 -19.080  1.00 72.43           C
ANISOU 3730  C   ILE A 558    10615   5743  11162    596     85  -1122       C
ATOM   3731  O   ILE A 558      36.715  31.458 -19.729  1.00 73.68           O
ANISOU 3731  O   ILE A 558    10854   5791  11349    626    253  -1134       O
ATOM   3732  CB  ILE A 558      36.225  31.183 -16.606  1.00 67.00           C
ANISOU 3732  CB  ILE A 558     9554   5199  10703    523     15  -1064       C
ATOM   3733  CG1 ILE A 558      36.295  30.279 -15.366  1.00 67.23           C
ANISOU 3733  CG1 ILE A 558     9420   5286  10837    482    -69  -1034       C
ATOM   3734  CG2 ILE A 558      35.470  32.492 -16.309  1.00 64.82           C
ANISOU 3734  CG2 ILE A 558     9271   5006  10351    531    -34  -1056       C
ATOM   3735  CD1 ILE A 558      37.283  30.796 -14.287  1.00 72.21           C
ANISOU 3735  CD1 ILE A 558     9910   5932  11595    473    -40  -1016       C
ATOM   3736  N   GLU A 559      34.529  31.957 -19.415  1.00 69.72           N
ANISOU 3736  N   GLU A 559    10353   5442  10694    612    -20  -1131       N
ATOM   3737  CA  GLU A 559      34.435  32.935 -20.497  1.00 70.41           C
ANISOU 3737  CA  GLU A 559    10636   5467  10651    669     44  -1154       C
ATOM   3738  C   GLU A 559      34.109  34.282 -19.857  1.00 74.15           C
ANISOU 3738  C   GLU A 559    11014   6034  11124    664     27  -1134       C
ATOM   3739  O   GLU A 559      33.434  34.319 -18.832  1.00 70.56           O
ANISOU 3739  O   GLU A 559    10399   5691  10719    623    -89  -1109       O
ATOM   3740  CB  GLU A 559      33.309  32.582 -21.475  1.00 72.28           C
ANISOU 3740  CB  GLU A 559    11057   5665  10742    697    -95  -1185       C
ATOM   3741  CG  GLU A 559      33.459  31.262 -22.201  1.00 82.19           C
ANISOU 3741  CG  GLU A 559    12429   6825  11975    705   -115  -1212       C
ATOM   3742  CD  GLU A 559      32.344  30.987 -23.189  1.00102.50           C
ANISOU 3742  CD  GLU A 559    15202   9341  14404    741   -277  -1251       C
ATOM   3743  OE1 GLU A 559      31.192  31.399 -22.923  1.00 89.31           O
ANISOU 3743  OE1 GLU A 559    13476   7741  12717    730   -444  -1249       O
ATOM   3744  OE2 GLU A 559      32.628  30.371 -24.241  1.00 99.02           O
ANISOU 3744  OE2 GLU A 559    14980   8771  13872    784   -240  -1286       O
ATOM   3745  N   ASP A 560      34.542  35.388 -20.472  1.00 75.35           N
ANISOU 3745  N   ASP A 560    11277   6136  11218    709    149  -1144       N
ATOM   3746  CA  ASP A 560      34.177  36.736 -20.011  1.00 76.03           C
ANISOU 3746  CA  ASP A 560    11298   6302  11286    711    134  -1129       C
ATOM   3747  C   ASP A 560      32.749  37.029 -20.507  1.00 83.59           C
ANISOU 3747  C   ASP A 560    12362   7292  12105    729    -23  -1139       C
ATOM   3748  O   ASP A 560      32.221  36.256 -21.305  1.00 85.17           O
ANISOU 3748  O   ASP A 560    12700   7433  12228    747   -109  -1163       O
ATOM   3749  CB  ASP A 560      35.201  37.795 -20.463  1.00 78.32           C
ANISOU 3749  CB  ASP A 560    11649   6517  11591    752    334  -1133       C
ATOM   3750  CG  ASP A 560      35.426  37.979 -21.958  1.00 92.33           C
ANISOU 3750  CG  ASP A 560    13694   8149  13239    824    460  -1159       C
ATOM   3751  OD1 ASP A 560      34.538  37.595 -22.747  1.00 93.68           O
ANISOU 3751  OD1 ASP A 560    14041   8291  13261    851    351  -1179       O
ATOM   3752  OD2 ASP A 560      36.472  38.579 -22.337  1.00 98.95           O
ANISOU 3752  OD2 ASP A 560    14576   8893  14128    857    667  -1159       O
ATOM   3753  N   ALA A 561      32.056  38.008 -19.930  1.00 82.01           N
ANISOU 3753  N   ALA A 561    12079   7185  11896    719    -87  -1120       N
ATOM   3754  CA  ALA A 561      30.671  38.266 -20.350  1.00 83.59           C
ANISOU 3754  CA  ALA A 561    12353   7406  12000    734   -247  -1127       C
ATOM   3755  C   ALA A 561      30.509  38.291 -21.890  1.00 93.03           C
ANISOU 3755  C   ALA A 561    13828   8478  13040    803   -250  -1167       C
ATOM   3756  O   ALA A 561      29.526  37.746 -22.407  1.00 94.11           O
ANISOU 3756  O   ALA A 561    14053   8586  13119    814   -419  -1187       O
ATOM   3757  CB  ALA A 561      30.159  39.556 -19.742  1.00 83.61           C
ANISOU 3757  CB  ALA A 561    12265   7498  12006    728   -262  -1103       C
ATOM   3758  N   TYR A 562      31.512  38.854 -22.608  1.00 91.74           N
ANISOU 3758  N   TYR A 562    13811   8226  12821    852    -59  -1178       N
ATOM   3759  CA  TYR A 562      31.553  38.968 -24.070  1.00 93.66           C
ANISOU 3759  CA  TYR A 562    14358   8329  12898    932    -13  -1211       C
ATOM   3760  C   TYR A 562      31.365  37.627 -24.781  1.00 96.84           C
ANISOU 3760  C   TYR A 562    14911   8640  13244    947    -97  -1243       C
ATOM   3761  O   TYR A 562      30.453  37.498 -25.594  1.00 97.40           O
ANISOU 3761  O   TYR A 562    15169   8654  13185    989   -252  -1273       O
ATOM   3762  CB  TYR A 562      32.856  39.666 -24.533  1.00 96.43           C
ANISOU 3762  CB  TYR A 562    14805   8589  13244    978    257  -1207       C
ATOM   3763  CG  TYR A 562      32.777  41.178 -24.648  1.00 99.31           C
ANISOU 3763  CG  TYR A 562    15215   8970  13549   1015    321  -1197       C
ATOM   3764  CD1 TYR A 562      33.425  41.852 -25.679  1.00102.89           C
ANISOU 3764  CD1 TYR A 562    15920   9287  13886   1098    498  -1208       C
ATOM   3765  CD2 TYR A 562      32.073  41.936 -23.712  1.00 98.97           C
ANISOU 3765  CD2 TYR A 562    14971   9068  13564    970    219  -1174       C
ATOM   3766  CE1 TYR A 562      33.367  43.242 -25.783  1.00104.98           C
ANISOU 3766  CE1 TYR A 562    16226   9562  14098   1134    565  -1197       C
ATOM   3767  CE2 TYR A 562      32.004  43.324 -23.809  1.00 99.80           C
ANISOU 3767  CE2 TYR A 562    15115   9187  13617   1003    279  -1165       C
ATOM   3768  CZ  TYR A 562      32.656  43.974 -24.844  1.00111.15           C
ANISOU 3768  CZ  TYR A 562    16794  10494  14943   1084    448  -1177       C
ATOM   3769  OH  TYR A 562      32.587  45.342 -24.944  1.00116.79           O
ANISOU 3769  OH  TYR A 562    17548  11220  15608   1118    513  -1166       O
ATOM   3770  N   GLY A 563      32.206  36.654 -24.437  1.00 92.31           N
ANISOU 3770  N   GLY A 563    14250   8048  12775    913    -10  -1238       N
ATOM   3771  CA  GLY A 563      32.209  35.299 -24.987  1.00 92.25           C
ANISOU 3771  CA  GLY A 563    14356   7955  12740    919    -61  -1265       C
ATOM   3772  C   GLY A 563      33.599  34.704 -25.141  1.00 94.19           C
ANISOU 3772  C   GLY A 563    14621   8111  13057    923    161  -1261       C
ATOM   3773  O   GLY A 563      33.728  33.570 -25.604  1.00 94.02           O
ANISOU 3773  O   GLY A 563    14691   8014  13021    926    146  -1281       O
ATOM   3774  N   LYS A 564      34.652  35.462 -24.750  1.00 89.49           N
ANISOU 3774  N   LYS A 564    13930   7514  12557    921    369  -1235       N
ATOM   3775  CA  LYS A 564      36.053  35.041 -24.836  1.00 89.45           C
ANISOU 3775  CA  LYS A 564    13910   7409  12668    925    599  -1227       C
ATOM   3776  C   LYS A 564      36.445  34.095 -23.702  1.00 92.10           C
ANISOU 3776  C   LYS A 564    13977   7821  13195    848    554  -1208       C
ATOM   3777  O   LYS A 564      36.260  34.421 -22.525  1.00 91.95           O
ANISOU 3777  O   LYS A 564    13720   7936  13280    794    466  -1184       O
ATOM   3778  CB  LYS A 564      36.992  36.262 -24.855  1.00 91.73           C
ANISOU 3778  CB  LYS A 564    14179   7652  13023    954    821  -1209       C
ATOM   3779  CG  LYS A 564      38.448  35.937 -25.203  1.00110.54           C
ANISOU 3779  CG  LYS A 564    16580   9882  15538    975   1091  -1202       C
ATOM   3780  CD  LYS A 564      39.398  36.927 -24.543  1.00123.15           C
ANISOU 3780  CD  LYS A 564    17979  11487  17326    960   1242  -1178       C
ATOM   3781  CE  LYS A 564      40.835  36.685 -24.924  1.00135.58           C
ANISOU 3781  CE  LYS A 564    19562  12884  19069    985   1521  -1169       C
ATOM   3782  NZ  LYS A 564      41.226  37.522 -26.089  1.00146.65           N
ANISOU 3782  NZ  LYS A 564    21216  14125  20379   1074   1759  -1171       N
ATOM   3783  N   VAL A 565      37.020  32.940 -24.070  1.00 86.28           N
ANISOU 3783  N   VAL A 565    13298   6989  12497    849    623  -1217       N
ATOM   3784  CA  VAL A 565      37.532  31.939 -23.141  1.00 84.46           C
ANISOU 3784  CA  VAL A 565    12844   6802  12445    785    603  -1199       C
ATOM   3785  C   VAL A 565      38.819  32.523 -22.531  1.00 86.01           C
ANISOU 3785  C   VAL A 565    12869   6973  12838    773    782  -1175       C
ATOM   3786  O   VAL A 565      39.786  32.788 -23.247  1.00 86.96           O
ANISOU 3786  O   VAL A 565    13095   6948  12999    817   1006  -1177       O
ATOM   3787  CB  VAL A 565      37.741  30.576 -23.852  1.00 88.59           C
ANISOU 3787  CB  VAL A 565    13503   7214  12942    797    630  -1219       C
ATOM   3788  CG1 VAL A 565      38.430  29.563 -22.943  1.00 88.25           C
ANISOU 3788  CG1 VAL A 565    13236   7198  13097    737    640  -1198       C
ATOM   3789  CG2 VAL A 565      36.414  30.023 -24.352  1.00 88.40           C
ANISOU 3789  CG2 VAL A 565    13622   7215  12751    805    413  -1249       C
ATOM   3790  N   ILE A 566      38.776  32.799 -21.217  1.00 78.43           N
ANISOU 3790  N   ILE A 566    11656   6144  11999    718    680  -1152       N
ATOM   3791  CA  ILE A 566      39.860  33.391 -20.427  1.00 75.82           C
ANISOU 3791  CA  ILE A 566    11134   5806  11870    700    783  -1133       C
ATOM   3792  C   ILE A 566      40.562  32.339 -19.572  1.00 77.84           C
ANISOU 3792  C   ILE A 566    11201   6062  12313    653    756  -1119       C
ATOM   3793  O   ILE A 566      41.698  32.538 -19.147  1.00 77.89           O
ANISOU 3793  O   ILE A 566    11072   6003  12519    647    859  -1110       O
ATOM   3794  CB  ILE A 566      39.339  34.585 -19.600  1.00 77.22           C
ANISOU 3794  CB  ILE A 566    11199   6110  12031    685    686  -1122       C
ATOM   3795  CG1 ILE A 566      38.263  34.133 -18.588  1.00 76.48           C
ANISOU 3795  CG1 ILE A 566    10992   6175  11891    637    455  -1108       C
ATOM   3796  CG2 ILE A 566      38.831  35.692 -20.535  1.00 77.35           C
ANISOU 3796  CG2 ILE A 566    11404   6099  11887    739    750  -1135       C
ATOM   3797  CD1 ILE A 566      37.956  35.057 -17.570  1.00 86.81           C
ANISOU 3797  CD1 ILE A 566    12161   7595  13230    615    374  -1091       C
ATOM   3798  N   TYR A 567      39.885  31.209 -19.343  1.00 72.74           N
ANISOU 3798  N   TYR A 567    10546   5476  11615    623    612  -1117       N
ATOM   3799  CA  TYR A 567      40.429  30.080 -18.604  1.00 71.56           C
ANISOU 3799  CA  TYR A 567    10246   5326  11617    583    576  -1102       C
ATOM   3800  C   TYR A 567      39.946  28.788 -19.255  1.00 75.54           C
ANISOU 3800  C   TYR A 567    10870   5797  12035    582    538  -1115       C
ATOM   3801  O   TYR A 567      38.815  28.722 -19.721  1.00 74.73           O
ANISOU 3801  O   TYR A 567    10892   5739  11763    591    432  -1129       O
ATOM   3802  CB  TYR A 567      40.065  30.145 -17.100  1.00 71.24           C
ANISOU 3802  CB  TYR A 567    10004   5429  11635    538    402  -1077       C
ATOM   3803  CG  TYR A 567      40.517  28.926 -16.315  1.00 72.36           C
ANISOU 3803  CG  TYR A 567    10012   5571  11909    503    344  -1060       C
ATOM   3804  CD1 TYR A 567      41.850  28.765 -15.940  1.00 74.42           C
ANISOU 3804  CD1 TYR A 567    10151   5744  12380    498    427  -1054       C
ATOM   3805  CD2 TYR A 567      39.619  27.909 -15.988  1.00 71.65           C
ANISOU 3805  CD2 TYR A 567     9919   5556  11750    477    210  -1049       C
ATOM   3806  CE1 TYR A 567      42.274  27.627 -15.252  1.00 74.19           C
ANISOU 3806  CE1 TYR A 567    10010   5708  12472    470    367  -1038       C
ATOM   3807  CE2 TYR A 567      40.028  26.780 -15.288  1.00 71.93           C
ANISOU 3807  CE2 TYR A 567     9843   5586  11899    449    164  -1031       C
ATOM   3808  CZ  TYR A 567      41.355  26.643 -14.918  1.00 79.68           C
ANISOU 3808  CZ  TYR A 567    10715   6487  13073    447    238  -1026       C
ATOM   3809  OH  TYR A 567      41.753  25.526 -14.220  1.00 81.76           O
ANISOU 3809  OH  TYR A 567    10875   6743  13448    423    182  -1007       O
ATOM   3810  N   GLU A 568      40.823  27.782 -19.311  1.00 72.47           N
ANISOU 3810  N   GLU A 568    10442   5318  11777    572    622  -1111       N
ATOM   3811  CA  GLU A 568      40.551  26.466 -19.857  1.00 72.87           C
ANISOU 3811  CA  GLU A 568    10589   5321  11775    568    600  -1123       C
ATOM   3812  C   GLU A 568      41.370  25.490 -19.020  1.00 74.53           C
ANISOU 3812  C   GLU A 568    10613   5519  12184    529    600  -1100       C
ATOM   3813  O   GLU A 568      42.612  25.509 -19.073  1.00 74.14           O
ANISOU 3813  O   GLU A 568    10505   5357  12307    537    756  -1093       O
ATOM   3814  CB  GLU A 568      40.944  26.403 -21.345  1.00 76.02           C
ANISOU 3814  CB  GLU A 568    11237   5554  12092    625    784  -1149       C
ATOM   3815  CG  GLU A 568      40.486  25.147 -22.079  1.00 90.28           C
ANISOU 3815  CG  GLU A 568    13200   7307  13798    631    743  -1171       C
ATOM   3816  CD  GLU A 568      39.148  25.265 -22.787  1.00119.13           C
ANISOU 3816  CD  GLU A 568    17047  10996  17221    655    593  -1202       C
ATOM   3817  OE1 GLU A 568      39.104  25.853 -23.894  1.00125.66           O
ANISOU 3817  OE1 GLU A 568    18116  11727  17902    716    680  -1227       O
ATOM   3818  OE2 GLU A 568      38.147  24.740 -22.249  1.00108.39           O
ANISOU 3818  OE2 GLU A 568    15602   9746  15836    616    387  -1202       O
ATOM   3819  N   ALA A 569      40.668  24.668 -18.214  1.00 68.51           N
ANISOU 3819  N   ALA A 569     9753   4865  11413    489    425  -1086       N
ATOM   3820  CA  ALA A 569      41.273  23.692 -17.318  1.00 67.36           C
ANISOU 3820  CA  ALA A 569     9440   4725  11430    454    390  -1061       C
ATOM   3821  C   ALA A 569      42.257  22.773 -18.017  1.00 72.63           C
ANISOU 3821  C   ALA A 569    10149   5243  12205    462    542  -1068       C
ATOM   3822  O   ALA A 569      41.952  22.223 -19.078  1.00 72.85           O
ANISOU 3822  O   ALA A 569    10354   5200  12126    482    597  -1092       O
ATOM   3823  CB  ALA A 569      40.205  22.874 -16.628  1.00 67.23           C
ANISOU 3823  CB  ALA A 569     9372   4820  11350    421    210  -1047       C
ATOM   3824  N   LYS A 570      43.459  22.662 -17.435  1.00 69.33           N
ANISOU 3824  N   LYS A 570     9574   4764  12007    452    609  -1049       N
ATOM   3825  CA  LYS A 570      44.542  21.801 -17.884  1.00 69.82           C
ANISOU 3825  CA  LYS A 570     9624   4675  12230    455    759  -1047       C
ATOM   3826  C   LYS A 570      44.839  20.826 -16.723  1.00 72.44           C
ANISOU 3826  C   LYS A 570     9765   5050  12709    416    638  -1020       C
ATOM   3827  O   LYS A 570      45.808  21.056 -15.985  1.00 71.87           O
ANISOU 3827  O   LYS A 570     9526   4936  12843    410    642  -1004       O
ATOM   3828  CB  LYS A 570      45.782  22.642 -18.279  1.00 73.75           C
ANISOU 3828  CB  LYS A 570    10099   5026  12898    485    963  -1050       C
ATOM   3829  CG  LYS A 570      45.693  23.278 -19.674  1.00 97.61           C
ANISOU 3829  CG  LYS A 570    13361   7949  15779    536   1145  -1073       C
ATOM   3830  CD  LYS A 570      47.006  23.145 -20.461  1.00113.35           C
ANISOU 3830  CD  LYS A 570    15387   9720  17960    569   1424  -1070       C
ATOM   3831  CE  LYS A 570      46.791  23.114 -21.966  1.00126.10           C
ANISOU 3831  CE  LYS A 570    17304  11209  19401    622   1606  -1091       C
ATOM   3832  NZ  LYS A 570      46.784  21.721 -22.500  1.00131.99           N
ANISOU 3832  NZ  LYS A 570    18128  11887  20134    615   1635  -1094       N
ATOM   3833  N   PRO A 571      43.982  19.786 -16.476  1.00 67.05           N
ANISOU 3833  N   PRO A 571     9100   4448  11929    392    513  -1014       N
ATOM   3834  CA  PRO A 571      44.239  18.916 -15.318  1.00 65.28           C
ANISOU 3834  CA  PRO A 571     8709   4263  11831    362    401   -983       C
ATOM   3835  C   PRO A 571      45.380  17.953 -15.534  1.00 67.85           C
ANISOU 3835  C   PRO A 571     8978   4450  12351    358    515   -976       C
ATOM   3836  O   PRO A 571      45.827  17.776 -16.661  1.00 67.07           O
ANISOU 3836  O   PRO A 571     8992   4225  12266    376    690   -995       O
ATOM   3837  CB  PRO A 571      42.905  18.190 -15.101  1.00 65.87           C
ANISOU 3837  CB  PRO A 571     8830   4453  11743    343    259   -978       C
ATOM   3838  CG  PRO A 571      42.239  18.207 -16.412  1.00 70.57           C
ANISOU 3838  CG  PRO A 571     9623   5015  12177    360    320  -1014       C
ATOM   3839  CD  PRO A 571      42.774  19.350 -17.220  1.00 67.38           C
ANISOU 3839  CD  PRO A 571     9311   4532  11759    395    463  -1035       C
ATOM   3840  N   GLU A 572      45.862  17.359 -14.434  1.00 65.90           N
ANISOU 3840  N   GLU A 572     8566   4217  12255    338    419   -948       N
ATOM   3841  CA  GLU A 572      46.896  16.318 -14.427  1.00 66.87           C
ANISOU 3841  CA  GLU A 572     8603   4218  12585    329    491   -935       C
ATOM   3842  C   GLU A 572      46.149  15.007 -14.695  1.00 70.94           C
ANISOU 3842  C   GLU A 572     9195   4771  12988    311    458   -932       C
ATOM   3843  O   GLU A 572      45.267  14.636 -13.919  1.00 70.58           O
ANISOU 3843  O   GLU A 572     9125   4850  12841    295    299   -915       O
ATOM   3844  CB  GLU A 572      47.607  16.244 -13.059  1.00 68.32           C
ANISOU 3844  CB  GLU A 572     8592   4408  12958    321    359   -907       C
ATOM   3845  CG  GLU A 572      48.492  17.430 -12.720  1.00 80.57           C
ANISOU 3845  CG  GLU A 572    10042   5900  14670    338    368   -913       C
ATOM   3846  CD  GLU A 572      49.199  17.272 -11.390  1.00110.27           C
ANISOU 3846  CD  GLU A 572    13630   9647  18620    336    207   -892       C
ATOM   3847  OE1 GLU A 572      48.742  17.888 -10.400  1.00 96.26           O
ANISOU 3847  OE1 GLU A 572    11836   7983  16756    342     35   -885       O
ATOM   3848  OE2 GLU A 572      50.187  16.503 -11.328  1.00117.09           O
ANISOU 3848  OE2 GLU A 572    14390  10383  19717    332    247   -882       O
ATOM   3849  N   TYR A 573      46.451  14.352 -15.822  1.00 68.35           N
ANISOU 3849  N   TYR A 573     8974   4326  12671    318    616   -949       N
ATOM   3850  CA  TYR A 573      45.795  13.116 -16.212  1.00 68.40           C
ANISOU 3850  CA  TYR A 573     9066   4345  12578    303    593   -955       C
ATOM   3851  C   TYR A 573      46.516  11.903 -15.709  1.00 74.22           C
ANISOU 3851  C   TYR A 573     9680   5025  13497    283    596   -928       C
ATOM   3852  O   TYR A 573      47.742  11.804 -15.830  1.00 74.05           O
ANISOU 3852  O   TYR A 573     9583   4868  13686    289    723   -919       O
ATOM   3853  CB  TYR A 573      45.626  13.038 -17.734  1.00 70.63           C
ANISOU 3853  CB  TYR A 573     9571   4527  12737    327    747   -994       C
ATOM   3854  CG  TYR A 573      44.636  14.048 -18.277  1.00 72.51           C
ANISOU 3854  CG  TYR A 573     9962   4833  12754    349    703  -1024       C
ATOM   3855  CD1 TYR A 573      43.266  13.798 -18.246  1.00 74.22           C
ANISOU 3855  CD1 TYR A 573    10244   5166  12791    336    540  -1037       C
ATOM   3856  CD2 TYR A 573      45.064  15.269 -18.790  1.00 73.46           C
ANISOU 3856  CD2 TYR A 573    10152   4893  12864    382    825  -1036       C
ATOM   3857  CE1 TYR A 573      42.347  14.738 -18.709  1.00 75.76           C
ANISOU 3857  CE1 TYR A 573    10567   5416  12802    357    484  -1064       C
ATOM   3858  CE2 TYR A 573      44.155  16.210 -19.272  1.00 74.16           C
ANISOU 3858  CE2 TYR A 573    10384   5044  12749    404    779  -1062       C
ATOM   3859  CZ  TYR A 573      42.797  15.936 -19.237  1.00 83.93           C
ANISOU 3859  CZ  TYR A 573    11683   6397  13811    392    602  -1076       C
ATOM   3860  OH  TYR A 573      41.888  16.853 -19.708  1.00 89.30           O
ANISOU 3860  OH  TYR A 573    12495   7128  14307    414    542  -1101       O
ATOM   3861  N   ALA A 574      45.750  10.961 -15.158  1.00 72.48           N
ANISOU 3861  N   ALA A 574     9434   4895  13211    260    464   -913       N
ATOM   3862  CA  ALA A 574      46.271   9.677 -14.697  1.00 73.65           C
ANISOU 3862  CA  ALA A 574     9481   4999  13504    242    455   -886       C
ATOM   3863  C   ALA A 574      46.757   8.908 -15.930  1.00 81.81           C
ANISOU 3863  C   ALA A 574    10621   5886  14577    245    637   -909       C
ATOM   3864  O   ALA A 574      47.905   8.461 -15.978  1.00 81.83           O
ANISOU 3864  O   ALA A 574    10543   5763  14785    246    748   -894       O
ATOM   3865  CB  ALA A 574      45.175   8.901 -13.989  1.00 73.73           C
ANISOU 3865  CB  ALA A 574     9474   5133  13409    222    297   -868       C
ATOM   3866  N   CYS A 575      45.897   8.836 -16.956  1.00 82.77           N
ANISOU 3866  N   CYS A 575    10936   6010  14504    253    668   -947       N
ATOM   3867  CA  CYS A 575      46.158   8.160 -18.218  1.00 86.15           C
ANISOU 3867  CA  CYS A 575    11527   6299  14908    266    829   -976       C
ATOM   3868  C   CYS A 575      45.724   9.065 -19.365  1.00 89.73           C
ANISOU 3868  C   CYS A 575    12204   6716  15176    302    904  -1019       C
ATOM   3869  O   CYS A 575      44.522   9.243 -19.586  1.00 88.24           O
ANISOU 3869  O   CYS A 575    12120   6617  14788    304    775  -1046       O
ATOM   3870  CB  CYS A 575      45.437   6.813 -18.240  1.00 88.75           C
ANISOU 3870  CB  CYS A 575    11885   6659  15177    242    744   -982       C
ATOM   3871  SG  CYS A 575      45.305   6.044 -19.877  1.00 95.24           S
ANISOU 3871  SG  CYS A 575    12976   7332  15880    264    885  -1034       S
ATOM   3872  N   ILE A 576      46.702   9.680 -20.060  1.00 87.93           N
ANISOU 3872  N   ILE A 576    12041   6344  15023    335   1112  -1024       N
ATOM   3873  CA  ILE A 576      46.417  10.592 -21.181  1.00 88.66           C
ANISOU 3873  CA  ILE A 576    12368   6379  14938    380   1210  -1061       C
ATOM   3874  C   ILE A 576      45.735   9.861 -22.373  1.00 95.83           C
ANISOU 3874  C   ILE A 576    13550   7217  15643    403   1233  -1106       C
ATOM   3875  O   ILE A 576      44.679  10.321 -22.807  1.00 95.47           O
ANISOU 3875  O   ILE A 576    13658   7235  15381    420   1117  -1141       O
ATOM   3876  CB  ILE A 576      47.581  11.555 -21.584  1.00 91.73           C
ANISOU 3876  CB  ILE A 576    12762   6632  15461    416   1435  -1050       C
ATOM   3877  CG1 ILE A 576      48.287  12.144 -20.338  1.00 91.10           C
ANISOU 3877  CG1 ILE A 576    12392   6603  15617    390   1378  -1011       C
ATOM   3878  CG2 ILE A 576      47.053  12.674 -22.488  1.00 92.33           C
ANISOU 3878  CG2 ILE A 576    13056   6703  15321    461   1472  -1082       C
ATOM   3879  CD1 ILE A 576      49.648  12.807 -20.580  1.00 95.68           C
ANISOU 3879  CD1 ILE A 576    12906   7016  16433    416   1603   -995       C
ATOM   3880  N   PRO A 577      46.225   8.688 -22.853  1.00 94.27           N
ANISOU 3880  N   PRO A 577    13415   6895  15509    403   1348  -1109       N
ATOM   3881  CA  PRO A 577      45.511   7.992 -23.947  1.00 95.44           C
ANISOU 3881  CA  PRO A 577    13837   6975  15450    428   1336  -1158       C
ATOM   3882  C   PRO A 577      44.022   7.689 -23.680  1.00100.20           C
ANISOU 3882  C   PRO A 577    14447   7731  15894    402   1056  -1187       C
ATOM   3883  O   PRO A 577      43.210   7.668 -24.607  1.00101.24           O
ANISOU 3883  O   PRO A 577    14821   7822  15821    432    992  -1239       O
ATOM   3884  CB  PRO A 577      46.298   6.688 -24.092  1.00 97.78           C
ANISOU 3884  CB  PRO A 577    14112   7147  15893    415   1472  -1145       C
ATOM   3885  CG  PRO A 577      47.660   7.011 -23.587  1.00102.06           C
ANISOU 3885  CG  PRO A 577    14457   7617  16703    410   1648  -1094       C
ATOM   3886  CD  PRO A 577      47.456   7.960 -22.468  1.00 96.19           C
ANISOU 3886  CD  PRO A 577    13493   7038  16018    384   1490  -1069       C
ATOM   3887  N   CYS A 578      43.672   7.482 -22.402  1.00 95.19           N
ANISOU 3887  N   CYS A 578    13550   7255  15362    351    889  -1152       N
ATOM   3888  CA  CYS A 578      42.342   7.135 -21.912  1.00 93.59           C
ANISOU 3888  CA  CYS A 578    13295   7191  15076    321    646  -1165       C
ATOM   3889  C   CYS A 578      41.220   8.093 -22.275  1.00 99.80           C
ANISOU 3889  C   CYS A 578    14204   8044  15670    342    507  -1201       C
ATOM   3890  O   CYS A 578      40.060   7.690 -22.172  1.00100.02           O
ANISOU 3890  O   CYS A 578    14230   8140  15631    324    319  -1222       O
ATOM   3891  CB  CYS A 578      42.382   6.882 -20.409  1.00 91.75           C
ANISOU 3891  CB  CYS A 578    12770   7090  15002    274    545  -1109       C
ATOM   3892  SG  CYS A 578      43.359   5.438 -19.921  1.00 95.27           S
ANISOU 3892  SG  CYS A 578    13070   7469  15660    244    632  -1071       S
ATOM   3893  N   ILE A 579      41.531   9.345 -22.687  1.00 97.34           N
ANISOU 3893  N   ILE A 579    13992   7706  15287    380    597  -1207       N
ATOM   3894  CA  ILE A 579      40.510  10.358 -23.006  1.00 96.99           C
ANISOU 3894  CA  ILE A 579    14061   7723  15066    404    467  -1238       C
ATOM   3895  C   ILE A 579      39.529   9.958 -24.162  1.00104.77           C
ANISOU 3895  C   ILE A 579    15319   8630  15859    436    365  -1305       C
ATOM   3896  O   ILE A 579      38.598  10.692 -24.465  1.00104.24           O
ANISOU 3896  O   ILE A 579    15372   8590  15645    462    247  -1337       O
ATOM   3897  CB  ILE A 579      41.062  11.827 -22.976  1.00 99.08           C
ANISOU 3897  CB  ILE A 579    14324   7999  15322    432    572  -1221       C
ATOM   3898  CG1 ILE A 579      42.038  12.018 -21.770  1.00 98.13           C
ANISOU 3898  CG1 ILE A 579    13933   7929  15423    400    651  -1162       C
ATOM   3899  CG2 ILE A 579      39.924  12.870 -22.889  1.00 98.95           C
ANISOU 3899  CG2 ILE A 579    14323   8101  15173    437    396  -1235       C
ATOM   3900  CD1 ILE A 579      43.138  13.059 -21.958  1.00 98.92           C
ANISOU 3900  CD1 ILE A 579    14045   7949  15593    432    848  -1148       C
ATOM   3901  N   ASN A 580      39.626   8.709 -24.676  1.00105.16           N
ANISOU 3901  N   ASN A 580    15443   8590  15921    430    372  -1328       N
ATOM   3902  CA  ASN A 580      38.689   8.117 -25.652  1.00107.02           C
ANISOU 3902  CA  ASN A 580    15916   8744  16002    456    238  -1396       C
ATOM   3903  C   ASN A 580      37.919   6.927 -24.992  1.00111.34           C
ANISOU 3903  C   ASN A 580    16294   9358  16652    401     59  -1397       C
ATOM   3904  O   ASN A 580      38.535   6.098 -24.310  1.00110.66           O
ANISOU 3904  O   ASN A 580    16034   9288  16724    362    136  -1357       O
ATOM   3905  CB  ASN A 580      39.409   7.661 -26.936  1.00110.45           C
ANISOU 3905  CB  ASN A 580    16655   8975  16337    512    422  -1431       C
ATOM   3906  CG  ASN A 580      38.470   7.184 -28.033  1.00140.41           C
ANISOU 3906  CG  ASN A 580    20746  12664  19939    553    266  -1511       C
ATOM   3907  OD1 ASN A 580      38.254   5.975 -28.235  1.00134.79           O
ANISOU 3907  OD1 ASN A 580    20064  11898  19250    536    197  -1539       O
ATOM   3908  ND2 ASN A 580      37.886   8.129 -28.763  1.00134.09           N
ANISOU 3908  ND2 ASN A 580    20173  11827  18947    609    192  -1551       N
ATOM   3909  N   ALA A 581      36.579   6.858 -25.194  1.00107.94           N
ANISOU 3909  N   ALA A 581    15909   8957  16147    400   -180  -1441       N
ATOM   3910  CA  ALA A 581      35.712   5.816 -24.630  1.00123.47           C
ANISOU 3910  CA  ALA A 581    17720  10971  18222    352   -358  -1447       C
ATOM   3911  C   ALA A 581      35.511   4.646 -25.592  1.00128.92           C
ANISOU 3911  C   ALA A 581    18612  11514  18858    369   -403  -1510       C
ATOM   3912  O   ALA A 581      35.699   3.493 -25.204  1.00 86.38           O
ANISOU 3912  O   ALA A 581    13110   6116  13594    333   -378  -1495       O
ATOM   3913  CB  ALA A 581      34.369   6.408 -24.227  1.00123.80           C
ANISOU 3913  CB  ALA A 581    17674  11106  18258    341   -586  -1458       C
ATOM   3914  N   TYR A 627      47.097  16.592 -22.439  1.00 94.03           N
ANISOU 3914  N   TYR A 627    13291   6970  15466    531   1568  -1085       N
ATOM   3915  CA  TYR A 627      48.439  17.178 -22.368  1.00 95.70           C
ANISOU 3915  CA  TYR A 627    13385   7040  15938    546   1779  -1060       C
ATOM   3916  C   TYR A 627      49.223  16.856 -21.093  1.00 95.54           C
ANISOU 3916  C   TYR A 627    13041   7049  16213    499   1698  -1027       C
ATOM   3917  O   TYR A 627      50.269  16.211 -21.202  1.00 96.55           O
ANISOU 3917  O   TYR A 627    13086   7022  16575    498   1855  -1008       O
ATOM   3918  CB  TYR A 627      48.463  18.713 -22.643  1.00 99.70           C
ANISOU 3918  CB  TYR A 627    13954   7533  16395    585   1860  -1067       C
ATOM   3919  CG  TYR A 627      49.625  19.148 -23.525  1.00106.93           C
ANISOU 3919  CG  TYR A 627    14955   8210  17465    637   2194  -1058       C
ATOM   3920  CD1 TYR A 627      50.942  18.815 -23.201  1.00110.73           C
ANISOU 3920  CD1 TYR A 627    15228   8547  18297    624   2345  -1028       C
ATOM   3921  CD2 TYR A 627      49.405  19.859 -24.703  1.00109.26           C
ANISOU 3921  CD2 TYR A 627    15543   8404  17566    704   2367  -1076       C
ATOM   3922  CE1 TYR A 627      52.005  19.144 -24.043  1.00113.83           C
ANISOU 3922  CE1 TYR A 627    15694   8696  18862    674   2679  -1015       C
ATOM   3923  CE2 TYR A 627      50.465  20.210 -25.546  1.00112.17           C
ANISOU 3923  CE2 TYR A 627    16009   8532  18078    760   2708  -1062       C
ATOM   3924  CZ  TYR A 627      51.764  19.847 -25.212  1.00122.33           C
ANISOU 3924  CZ  TYR A 627    17074   9673  19734    743   2873  -1030       C
ATOM   3925  OH  TYR A 627      52.823  20.173 -26.032  1.00126.43           O
ANISOU 3925  OH  TYR A 627    17675   9933  20431    798   3233  -1010       O
ATOM   3926  N   ARG A 628      48.760  17.347 -19.907  1.00 87.21           N
ANISOU 3926  N   ARG A 628    11812   6173  15151    465   1460  -1019       N
ATOM   3927  CA  ARG A 628      49.411  17.173 -18.589  1.00 84.97           C
ANISOU 3927  CA  ARG A 628    11246   5924  15115    429   1339   -990       C
ATOM   3928  C   ARG A 628      49.350  15.741 -18.007  1.00 86.39           C
ANISOU 3928  C   ARG A 628    11335   6143  15346    393   1222   -973       C
ATOM   3929  O   ARG A 628      48.321  15.073 -18.129  1.00 85.67           O
ANISOU 3929  O   ARG A 628    11351   6153  15048    380   1118   -983       O
ATOM   3930  CB  ARG A 628      48.834  18.160 -17.583  1.00 82.11           C
ANISOU 3930  CB  ARG A 628    10783   5727  14689    417   1136   -989       C
ATOM   3931  CG  ARG A 628      49.191  19.603 -17.883  1.00 88.35           C
ANISOU 3931  CG  ARG A 628    11590   6463  15516    448   1247  -1000       C
ATOM   3932  CD  ARG A 628      49.896  20.245 -16.708  1.00 90.06           C
ANISOU 3932  CD  ARG A 628    11569   6690  15958    434   1142   -987       C
ATOM   3933  NE  ARG A 628      48.960  20.702 -15.679  1.00 94.54           N
ANISOU 3933  NE  ARG A 628    12093   7458  16370    416    892   -985       N
ATOM   3934  CZ  ARG A 628      49.202  20.662 -14.371  1.00108.72           C
ANISOU 3934  CZ  ARG A 628    13712   9311  18286    397    704   -970       C
ATOM   3935  NH1 ARG A 628      50.351  20.175 -13.914  1.00 89.30           N
ANISOU 3935  NH1 ARG A 628    11087   6728  16115    391    713   -958       N
ATOM   3936  NH2 ARG A 628      48.293  21.102 -13.508  1.00 98.88           N
ANISOU 3936  NH2 ARG A 628    12463   8234  16874    388    507   -965       N
ATOM   3937  N   GLN A 629      50.440  15.276 -17.361  1.00 80.37           N
ANISOU 3937  N   GLN A 629    10371   5291  14873    378   1235   -948       N
ATOM   3938  CA  GLN A 629      50.490  13.917 -16.792  1.00 78.46           C
ANISOU 3938  CA  GLN A 629    10040   5071  14701    348   1137   -928       C
ATOM   3939  C   GLN A 629      50.577  13.974 -15.278  1.00 79.11           C
ANISOU 3939  C   GLN A 629     9918   5257  14885    326    901   -905       C
ATOM   3940  O   GLN A 629      51.403  14.722 -14.746  1.00 79.92           O
ANISOU 3940  O   GLN A 629     9874   5301  15190    334    884   -900       O
ATOM   3941  CB  GLN A 629      51.654  13.100 -17.412  1.00 80.68           C
ANISOU 3941  CB  GLN A 629    10290   5140  15226    354   1354   -917       C
ATOM   3942  CG  GLN A 629      51.994  11.734 -16.771  1.00 86.83           C
ANISOU 3942  CG  GLN A 629    10942   5908  16141    324   1273   -891       C
ATOM   3943  CD  GLN A 629      50.911  10.674 -16.847  1.00 91.44           C
ANISOU 3943  CD  GLN A 629    11645   6612  16487    305   1173   -897       C
ATOM   3944  OE1 GLN A 629      50.309  10.303 -15.835  1.00 83.63           O
ANISOU 3944  OE1 GLN A 629    10575   5768  15432    283    956   -882       O
ATOM   3945  NE2 GLN A 629      50.683  10.112 -18.027  1.00 76.49           N
ANISOU 3945  NE2 GLN A 629     9948   4641  14475    318   1331   -917       N
ATOM   3946  N   ALA A 630      49.698  13.211 -14.592  1.00 72.39           N
ANISOU 3946  N   ALA A 630     9067   4548  13888    304    720   -892       N
ATOM   3947  CA  ALA A 630      49.641  13.132 -13.133  1.00 70.89           C
ANISOU 3947  CA  ALA A 630     8731   4456  13746    293    495   -866       C
ATOM   3948  C   ALA A 630      50.831  12.321 -12.625  1.00 75.86           C
ANISOU 3948  C   ALA A 630     9196   4963  14666    288    491   -843       C
ATOM   3949  O   ALA A 630      51.225  11.339 -13.256  1.00 75.59           O
ANISOU 3949  O   ALA A 630     9176   4826  14718    280    621   -839       O
ATOM   3950  CB  ALA A 630      48.335  12.483 -12.685  1.00 70.28           C
ANISOU 3950  CB  ALA A 630     8723   4541  13439    278    349   -855       C
ATOM   3951  N   GLN A 631      51.437  12.758 -11.516  1.00 72.61           N
ANISOU 3951  N   GLN A 631     8634   4544  14410    295    339   -830       N
ATOM   3952  CA  GLN A 631      52.544  12.009 -10.951  1.00 73.49           C
ANISOU 3952  CA  GLN A 631     8582   4533  14808    294    294   -809       C
ATOM   3953  C   GLN A 631      52.013  10.716 -10.296  1.00 76.26           C
ANISOU 3953  C   GLN A 631     8942   4968  15066    281    167   -779       C
ATOM   3954  O   GLN A 631      50.896  10.698  -9.759  1.00 74.38           O
ANISOU 3954  O   GLN A 631     8786   4890  14585    281     39   -770       O
ATOM   3955  CB  GLN A 631      53.416  12.880 -10.014  1.00 75.87           C
ANISOU 3955  CB  GLN A 631     8728   4774  15326    312    154   -811       C
ATOM   3956  CG  GLN A 631      53.081  12.854  -8.511  1.00100.20           C
ANISOU 3956  CG  GLN A 631    11770   7959  18341    325   -132   -792       C
ATOM   3957  CD  GLN A 631      54.224  12.375  -7.624  1.00122.99           C
ANISOU 3957  CD  GLN A 631    14486  10710  21534    337   -269   -779       C
ATOM   3958  OE1 GLN A 631      55.191  11.743  -8.072  1.00119.52           O
ANISOU 3958  OE1 GLN A 631    13940  10107  21363    329   -153   -775       O
ATOM   3959  NE2 GLN A 631      54.114  12.623  -6.325  1.00113.17           N
ANISOU 3959  NE2 GLN A 631    13225   9521  20253    362   -525   -770       N
ATOM   3960  N   ARG A 632      52.779   9.628 -10.427  1.00 73.02           N
ANISOU 3960  N   ARG A 632     8452   4437  14854    273    229   -762       N
ATOM   3961  CA  ARG A 632      52.458   8.320  -9.865  1.00 71.69           C
ANISOU 3961  CA  ARG A 632     8279   4318  14643    262    135   -732       C
ATOM   3962  C   ARG A 632      52.781   8.364  -8.372  1.00 76.67           C
ANISOU 3962  C   ARG A 632     8805   4970  15357    283   -112   -707       C
ATOM   3963  O   ARG A 632      53.866   8.828  -8.013  1.00 77.64           O
ANISOU 3963  O   ARG A 632     8793   4969  15739    298   -163   -711       O
ATOM   3964  CB  ARG A 632      53.294   7.249 -10.564  1.00 69.91           C
ANISOU 3964  CB  ARG A 632     8002   3936  14626    249    299   -724       C
ATOM   3965  CG  ARG A 632      53.144   5.867  -9.946  1.00 73.93           C
ANISOU 3965  CG  ARG A 632     8478   4472  15138    240    203   -690       C
ATOM   3966  CD  ARG A 632      53.790   4.776 -10.772  1.00 65.40           C
ANISOU 3966  CD  ARG A 632     7373   3250  14224    223    386   -684       C
ATOM   3967  NE  ARG A 632      52.995   4.376 -11.937  1.00 67.19           N
ANISOU 3967  NE  ARG A 632     7770   3510  14249    207    554   -705       N
ATOM   3968  CZ  ARG A 632      51.883   3.645 -11.877  1.00 82.48           C
ANISOU 3968  CZ  ARG A 632     9809   5573  15958    193    496   -702       C
ATOM   3969  NH1 ARG A 632      51.380   3.284 -10.704  1.00 62.32           N
ANISOU 3969  NH1 ARG A 632     7213   3132  13334    196    298   -672       N
ATOM   3970  NH2 ARG A 632      51.250   3.294 -12.992  1.00 70.92           N
ANISOU 3970  NH2 ARG A 632     8499   4111  14337    182    633   -729       N
ATOM   3971  N   ILE A 633      51.834   7.922  -7.507  1.00 72.21           N
ANISOU 3971  N   ILE A 633     8309   4547  14579    289   -264   -681       N
ATOM   3972  CA  ILE A 633      51.992   7.917  -6.041  1.00 71.76           C
ANISOU 3972  CA  ILE A 633     8209   4514  14541    321   -502   -654       C
ATOM   3973  C   ILE A 633      51.967   6.535  -5.413  1.00 77.07           C
ANISOU 3973  C   ILE A 633     8870   5182  15233    325   -574   -613       C
ATOM   3974  O   ILE A 633      52.326   6.396  -4.236  1.00 77.91           O
ANISOU 3974  O   ILE A 633     8942   5265  15395    360   -767   -589       O
ATOM   3975  CB  ILE A 633      51.041   8.896  -5.310  1.00 73.68           C
ANISOU 3975  CB  ILE A 633     8553   4902  14541    343   -632   -654       C
ATOM   3976  CG1 ILE A 633      49.562   8.608  -5.641  1.00 73.12           C
ANISOU 3976  CG1 ILE A 633     8619   4981  14182    326   -565   -645       C
ATOM   3977  CG2 ILE A 633      51.441  10.353  -5.569  1.00 73.46           C
ANISOU 3977  CG2 ILE A 633     8495   4844  14572    350   -622   -692       C
ATOM   3978  CD1 ILE A 633      48.564   9.152  -4.647  1.00 76.31           C
ANISOU 3978  CD1 ILE A 633     9118   5516  14361    352   -699   -626       C
ATOM   3979  N   LEU A 634      51.512   5.528  -6.172  1.00 73.17           N
ANISOU 3979  N   LEU A 634     8418   4704  14679    296   -429   -607       N
ATOM   3980  CA  LEU A 634      51.423   4.154  -5.701  1.00 73.55           C
ANISOU 3980  CA  LEU A 634     8457   4748  14740    296   -468   -568       C
ATOM   3981  C   LEU A 634      51.760   3.203  -6.858  1.00 78.38           C
ANISOU 3981  C   LEU A 634     9043   5272  15466    260   -268   -578       C
ATOM   3982  O   LEU A 634      51.328   3.459  -7.987  1.00 78.24           O
ANISOU 3982  O   LEU A 634     9100   5271  15356    237   -108   -610       O
ATOM   3983  CB  LEU A 634      50.010   3.905  -5.149  1.00 72.86           C
ANISOU 3983  CB  LEU A 634     8493   4817  14371    303   -530   -543       C
ATOM   3984  CG  LEU A 634      49.801   2.682  -4.255  1.00 77.79           C
ANISOU 3984  CG  LEU A 634     9126   5452  14980    321   -616   -493       C
ATOM   3985  CD1 LEU A 634      50.288   2.956  -2.827  1.00 78.32           C
ANISOU 3985  CD1 LEU A 634     9181   5492  15084    376   -831   -464       C
ATOM   3986  CD2 LEU A 634      48.326   2.272  -4.256  1.00 78.10           C
ANISOU 3986  CD2 LEU A 634     9275   5620  14780    312   -578   -476       C
ATOM   3987  N   LYS A 635      52.557   2.143  -6.597  1.00 74.94           N
ANISOU 3987  N   LYS A 635     8514   4733  15228    261   -280   -552       N
ATOM   3988  CA  LYS A 635      52.969   1.221  -7.657  1.00 75.80           C
ANISOU 3988  CA  LYS A 635     8597   4741  15461    230    -85   -558       C
ATOM   3989  C   LYS A 635      51.781   0.517  -8.333  1.00 80.98           C
ANISOU 3989  C   LYS A 635     9386   5497  15885    204     15   -565       C
ATOM   3990  O   LYS A 635      50.852   0.096  -7.648  1.00 80.13           O
ANISOU 3990  O   LYS A 635     9335   5507  15605    211    -91   -541       O
ATOM   3991  CB  LYS A 635      54.059   0.254  -7.183  1.00 79.28           C
ANISOU 3991  CB  LYS A 635     8903   5049  16173    238   -130   -525       C
ATOM   3992  CG  LYS A 635      54.955  -0.233  -8.321  1.00 97.96           C
ANISOU 3992  CG  LYS A 635    11200   7247  18773    213     91   -538       C
ATOM   3993  CD  LYS A 635      54.511  -1.609  -8.877  1.00105.75           C
ANISOU 3993  CD  LYS A 635    12249   8241  19689    187    215   -527       C
ATOM   3994  CE  LYS A 635      54.958  -1.837 -10.300  1.00105.54           C
ANISOU 3994  CE  LYS A 635    12247   8083  19768    164    482   -553       C
ATOM   3995  NZ  LYS A 635      54.266  -2.991 -10.913  1.00102.50           N
ANISOU 3995  NZ  LYS A 635    11971   7733  19240    140    588   -556       N
ATOM   3996  N   SER A 636      51.805   0.439  -9.686  1.00 79.11           N
ANISOU 3996  N   SER A 636     9210   5199  15648    180    219   -599       N
ATOM   3997  CA  SER A 636      50.744  -0.105 -10.550  1.00 78.97           C
ANISOU 3997  CA  SER A 636     9332   5246  15425    158    313   -621       C
ATOM   3998  C   SER A 636      50.125  -1.368  -9.991  1.00 81.44           C
ANISOU 3998  C   SER A 636     9645   5621  15680    149    239   -589       C
ATOM   3999  O   SER A 636      48.900  -1.448  -9.913  1.00 80.93           O
ANISOU 3999  O   SER A 636     9666   5676  15409    143    186   -593       O
ATOM   4000  CB  SER A 636      51.263  -0.382 -11.963  1.00 86.25           C
ANISOU 4000  CB  SER A 636    10313   6034  16425    143    541   -653       C
ATOM   4001  OG  SER A 636      52.337   0.468 -12.335  1.00102.71           O
ANISOU 4001  OG  SER A 636    12339   7992  18695    156    643   -664       O
ATOM   4002  N   SER A 637      50.983  -2.338  -9.576  1.00 77.02           N
ANISOU 4002  N   SER A 637     8977   4967  15319    150    236   -555       N
ATOM   4003  CA  SER A 637      50.628  -3.642  -9.003  1.00 75.05           C
ANISOU 4003  CA  SER A 637     8709   4747  15060    146    181   -518       C
ATOM   4004  C   SER A 637      49.843  -3.476  -7.715  1.00 74.47           C
ANISOU 4004  C   SER A 637     8648   4801  14845    172     -3   -482       C
ATOM   4005  O   SER A 637      48.821  -4.133  -7.571  1.00 71.64           O
ANISOU 4005  O   SER A 637     8348   4522  14349    165    -16   -469       O
ATOM   4006  CB  SER A 637      51.885  -4.468  -8.730  1.00 79.09           C
ANISOU 4006  CB  SER A 637     9091   5120  15842    149    199   -486       C
ATOM   4007  OG  SER A 637      52.661  -3.909  -7.679  1.00 87.40           O
ANISOU 4007  OG  SER A 637    10038   6138  17030    182     45   -460       O
ATOM   4008  N   SER A 638      50.321  -2.589  -6.784  1.00 70.48           N
ANISOU 4008  N   SER A 638     8096   4301  14383    206   -140   -466       N
ATOM   4009  CA  SER A 638      49.679  -2.315  -5.487  1.00 70.10           C
ANISOU 4009  CA  SER A 638     8086   4352  14195    243   -312   -429       C
ATOM   4010  C   SER A 638      48.318  -1.660  -5.647  1.00 74.54           C
ANISOU 4010  C   SER A 638     8760   5050  14512    238   -306   -445       C
ATOM   4011  O   SER A 638      47.399  -2.005  -4.898  1.00 75.23           O
ANISOU 4011  O   SER A 638     8901   5218  14465    256   -369   -410       O
ATOM   4012  CB  SER A 638      50.559  -1.448  -4.595  1.00 74.44           C
ANISOU 4012  CB  SER A 638     8578   4855  14850    283   -463   -420       C
ATOM   4013  OG  SER A 638      51.838  -2.024  -4.398  1.00 90.51           O
ANISOU 4013  OG  SER A 638    10494   6749  17146    291   -490   -405       O
ATOM   4014  N   ALA A 639      48.182  -0.717  -6.617  1.00 69.61           N
ANISOU 4014  N   ALA A 639     8171   4439  13837    217   -225   -496       N
ATOM   4015  CA  ALA A 639      46.917  -0.028  -6.885  1.00 68.38           C
ANISOU 4015  CA  ALA A 639     8115   4400  13467    210   -222   -517       C
ATOM   4016  C   ALA A 639      45.929  -0.981  -7.510  1.00 71.23           C
ANISOU 4016  C   ALA A 639     8529   4791  13742    182   -147   -525       C
ATOM   4017  O   ALA A 639      44.781  -1.024  -7.069  1.00 70.77           O
ANISOU 4017  O   ALA A 639     8517   4822  13550    187   -195   -507       O
ATOM   4018  CB  ALA A 639      47.136   1.190  -7.772  1.00 69.27           C
ANISOU 4018  CB  ALA A 639     8257   4501  13561    201   -157   -568       C
ATOM   4019  N   TYR A 640      46.395  -1.805  -8.482  1.00 67.69           N
ANISOU 4019  N   TYR A 640     8072   4255  13393    154    -30   -549       N
ATOM   4020  CA  TYR A 640      45.591  -2.838  -9.147  1.00 67.24           C
ANISOU 4020  CA  TYR A 640     8065   4201  13283    126     34   -564       C
ATOM   4021  C   TYR A 640      45.164  -3.956  -8.172  1.00 64.85           C
ANISOU 4021  C   TYR A 640     7718   3924  12999    134    -24   -509       C
ATOM   4022  O   TYR A 640      44.048  -4.464  -8.286  1.00 64.37           O
ANISOU 4022  O   TYR A 640     7696   3911  12853    121    -24   -512       O
ATOM   4023  CB  TYR A 640      46.349  -3.425 -10.356  1.00 70.26           C
ANISOU 4023  CB  TYR A 640     8464   4462  13770    103    179   -601       C
ATOM   4024  CG  TYR A 640      45.579  -4.479 -11.123  1.00 72.90           C
ANISOU 4024  CG  TYR A 640     8865   4783  14050     77    235   -626       C
ATOM   4025  CD1 TYR A 640      44.698  -4.124 -12.142  1.00 75.17           C
ANISOU 4025  CD1 TYR A 640     9276   5091  14192     64    258   -683       C
ATOM   4026  CD2 TYR A 640      45.739  -5.829 -10.837  1.00 74.12           C
ANISOU 4026  CD2 TYR A 640     8963   4896  14303     66    252   -596       C
ATOM   4027  CE1 TYR A 640      43.972  -5.089 -12.840  1.00 77.43           C
ANISOU 4027  CE1 TYR A 640     9628   5352  14438     43    280   -713       C
ATOM   4028  CE2 TYR A 640      45.027  -6.802 -11.533  1.00 76.24           C
ANISOU 4028  CE2 TYR A 640     9290   5146  14533     42    294   -624       C
ATOM   4029  CZ  TYR A 640      44.133  -6.426 -12.525  1.00 87.69           C
ANISOU 4029  CZ  TYR A 640    10863   6613  15843     30    300   -684       C
ATOM   4030  OH  TYR A 640      43.415  -7.387 -13.202  1.00 96.06           O
ANISOU 4030  OH  TYR A 640    11982   7640  16874      9    316   -718       O
ATOM   4031  N   ASP A 641      46.059  -4.335  -7.242  1.00 57.85           N
ANISOU 4031  N   ASP A 641     6753   2993  12235    158    -75   -462       N
ATOM   4032  CA  ASP A 641      45.807  -5.371  -6.243  1.00 57.29           C
ANISOU 4032  CA  ASP A 641     6653   2931  12183    177   -127   -403       C
ATOM   4033  C   ASP A 641      44.798  -4.938  -5.230  1.00 58.55           C
ANISOU 4033  C   ASP A 641     6863   3188  12196    209   -215   -367       C
ATOM   4034  O   ASP A 641      43.864  -5.700  -4.960  1.00 57.68           O
ANISOU 4034  O   ASP A 641     6771   3107  12037    209   -198   -340       O
ATOM   4035  CB  ASP A 641      47.095  -5.853  -5.561  1.00 60.49           C
ANISOU 4035  CB  ASP A 641     6976   3249  12761    201   -174   -364       C
ATOM   4036  CG  ASP A 641      47.930  -6.852  -6.368  1.00 68.69           C
ANISOU 4036  CG  ASP A 641     7952   4176  13971    171    -65   -377       C
ATOM   4037  OD1 ASP A 641      47.351  -7.550  -7.257  1.00 66.22           O
ANISOU 4037  OD1 ASP A 641     7675   3862  13624    136     38   -403       O
ATOM   4038  OD2 ASP A 641      49.157  -6.945  -6.109  1.00 76.84           O
ANISOU 4038  OD2 ASP A 641     8900   5113  15184    184    -87   -362       O
ATOM   4039  N   MET A 642      44.943  -3.698  -4.701  1.00 54.64           N
ANISOU 4039  N   MET A 642     6393   2733  11637    237   -296   -366       N
ATOM   4040  CA  MET A 642      43.980  -3.123  -3.769  1.00 54.43           C
ANISOU 4040  CA  MET A 642     6432   2790  11459    272   -365   -333       C
ATOM   4041  C   MET A 642      42.611  -2.998  -4.435  1.00 57.15           C
ANISOU 4041  C   MET A 642     6819   3202  11695    242   -301   -359       C
ATOM   4042  O   MET A 642      41.596  -3.392  -3.851  1.00 57.15           O
ANISOU 4042  O   MET A 642     6846   3237  11633    257   -297   -320       O
ATOM   4043  CB  MET A 642      44.439  -1.776  -3.279  1.00 58.13           C
ANISOU 4043  CB  MET A 642     6922   3279  11885    302   -457   -340       C
ATOM   4044  CG  MET A 642      43.565  -1.237  -2.152  1.00 62.95           C
ANISOU 4044  CG  MET A 642     7617   3958  12342    350   -527   -296       C
ATOM   4045  SD  MET A 642      43.236  -2.509  -0.895  1.00 67.68           S
ANISOU 4045  SD  MET A 642     8258   4530  12926    398   -544   -212       S
ATOM   4046  CE  MET A 642      44.811  -2.577  -0.094  1.00 65.97           C
ANISOU 4046  CE  MET A 642     8020   4221  12826    444   -680   -191       C
ATOM   4047  N   ALA A 643      42.594  -2.541  -5.696  1.00 52.61           N
ANISOU 4047  N   ALA A 643     6250   2624  11114    202   -246   -425       N
ATOM   4048  CA  ALA A 643      41.360  -2.445  -6.456  1.00 51.67           C
ANISOU 4048  CA  ALA A 643     6175   2549  10910    174   -210   -460       C
ATOM   4049  C   ALA A 643      40.596  -3.775  -6.421  1.00 55.53           C
ANISOU 4049  C   ALA A 643     6643   3020  11438    161   -175   -439       C
ATOM   4050  O   ALA A 643      39.405  -3.776  -6.102  1.00 57.93           O
ANISOU 4050  O   ALA A 643     6959   3366  11688    165   -185   -422       O
ATOM   4051  CB  ALA A 643      41.662  -2.035  -7.889  1.00 52.04           C
ANISOU 4051  CB  ALA A 643     6255   2563  10955    142   -153   -534       C
ATOM   4052  N   ASN A 644      41.283  -4.898  -6.705  1.00 50.16           N
ANISOU 4052  N   ASN A 644     5923   2267  10868    145   -128   -438       N
ATOM   4053  CA  ASN A 644      40.659  -6.223  -6.742  1.00 50.43           C
ANISOU 4053  CA  ASN A 644     5931   2272  10958    130    -88   -423       C
ATOM   4054  C   ASN A 644      40.242  -6.748  -5.362  1.00 54.90           C
ANISOU 4054  C   ASN A 644     6476   2855  11528    169   -108   -341       C
ATOM   4055  O   ASN A 644      39.212  -7.411  -5.247  1.00 51.85           O
ANISOU 4055  O   ASN A 644     6078   2469  11155    163    -78   -325       O
ATOM   4056  CB  ASN A 644      41.514  -7.203  -7.500  1.00 48.49           C
ANISOU 4056  CB  ASN A 644     5660   1942  10823    103    -24   -447       C
ATOM   4057  CG  ASN A 644      41.511  -7.007  -8.995  1.00 68.71           C
ANISOU 4057  CG  ASN A 644     8278   4466  13362     67     24   -528       C
ATOM   4058  OD1 ASN A 644      40.475  -6.794  -9.638  1.00 54.90           O
ANISOU 4058  OD1 ASN A 644     6580   2739  11539     50      7   -572       O
ATOM   4059  ND2 ASN A 644      42.658  -7.244  -9.592  1.00 67.23           N
ANISOU 4059  ND2 ASN A 644     8089   4201  13253     58     90   -548       N
ATOM   4060  N   ILE A 645      41.001  -6.386  -4.313  1.00 55.45           N
ANISOU 4060  N   ILE A 645     6553   2929  11587    214   -161   -292       N
ATOM   4061  CA  ILE A 645      40.648  -6.718  -2.933  1.00 57.10           C
ANISOU 4061  CA  ILE A 645     6787   3144  11764    268   -182   -212       C
ATOM   4062  C   ILE A 645      39.302  -6.000  -2.657  1.00 62.49           C
ANISOU 4062  C   ILE A 645     7516   3888  12341    279   -173   -202       C
ATOM   4063  O   ILE A 645      38.337  -6.640  -2.252  1.00 62.47           O
ANISOU 4063  O   ILE A 645     7510   3875  12351    288   -118   -164       O
ATOM   4064  CB  ILE A 645      41.769  -6.267  -1.947  1.00 60.75           C
ANISOU 4064  CB  ILE A 645     7278   3589  12217    321   -275   -175       C
ATOM   4065  CG1 ILE A 645      43.038  -7.159  -2.100  1.00 61.62           C
ANISOU 4065  CG1 ILE A 645     7323   3617  12473    314   -282   -173       C
ATOM   4066  CG2 ILE A 645      41.251  -6.272  -0.501  1.00 62.17           C
ANISOU 4066  CG2 ILE A 645     7541   3777  12304    390   -305    -96       C
ATOM   4067  CD1 ILE A 645      44.284  -6.675  -1.446  1.00 69.10           C
ANISOU 4067  CD1 ILE A 645     8269   4521  13463    355   -394   -156       C
ATOM   4068  N   LEU A 646      39.230  -4.693  -2.977  1.00 59.20           N
ANISOU 4068  N   LEU A 646     7129   3523  11840    273   -215   -241       N
ATOM   4069  CA  LEU A 646      38.024  -3.848  -2.832  1.00 58.74           C
ANISOU 4069  CA  LEU A 646     7107   3521  11691    280   -210   -239       C
ATOM   4070  C   LEU A 646      36.814  -4.351  -3.615  1.00 63.55           C
ANISOU 4070  C   LEU A 646     7675   4122  12351    238   -155   -268       C
ATOM   4071  O   LEU A 646      35.688  -4.249  -3.120  1.00 63.64           O
ANISOU 4071  O   LEU A 646     7690   4142  12349    254   -124   -234       O
ATOM   4072  CB  LEU A 646      38.305  -2.354  -3.093  1.00 56.72           C
ANISOU 4072  CB  LEU A 646     6887   3318  11345    280   -268   -279       C
ATOM   4073  CG  LEU A 646      39.235  -1.727  -2.078  1.00 60.22           C
ANISOU 4073  CG  LEU A 646     7376   3764  11741    331   -341   -245       C
ATOM   4074  CD1 LEU A 646      39.502  -0.265  -2.408  1.00 59.57           C
ANISOU 4074  CD1 LEU A 646     7317   3728  11591    326   -392   -290       C
ATOM   4075  CD2 LEU A 646      38.711  -1.921  -0.646  1.00 60.86           C
ANISOU 4075  CD2 LEU A 646     7530   3841  11755    395   -342   -162       C
ATOM   4076  N   ARG A 647      37.055  -4.941  -4.798  1.00 60.08           N
ANISOU 4076  N   ARG A 647     7198   3649  11981    189   -143   -329       N
ATOM   4077  CA  ARG A 647      36.004  -5.549  -5.611  1.00 60.78           C
ANISOU 4077  CA  ARG A 647     7252   3709  12134    150   -120   -368       C
ATOM   4078  C   ARG A 647      35.543  -6.861  -4.938  1.00 65.89           C
ANISOU 4078  C   ARG A 647     7847   4305  12883    161    -60   -310       C
ATOM   4079  O   ARG A 647      34.358  -7.154  -4.943  1.00 64.66           O
ANISOU 4079  O   ARG A 647     7654   4128  12786    154    -35   -304       O
ATOM   4080  CB  ARG A 647      36.497  -5.799  -7.049  1.00 61.26           C
ANISOU 4080  CB  ARG A 647     7324   3733  12219    104   -127   -452       C
ATOM   4081  CG  ARG A 647      35.516  -6.601  -7.912  1.00 62.73           C
ANISOU 4081  CG  ARG A 647     7486   3868  12479     68   -128   -498       C
ATOM   4082  CD  ARG A 647      35.654  -6.349  -9.396  1.00 65.34           C
ANISOU 4082  CD  ARG A 647     7885   4170  12773     35   -161   -592       C
ATOM   4083  NE  ARG A 647      36.938  -6.795  -9.930  1.00 76.42           N
ANISOU 4083  NE  ARG A 647     9319   5527  14189     26   -113   -614       N
ATOM   4084  CZ  ARG A 647      37.177  -7.025 -11.219  1.00 94.04           C
ANISOU 4084  CZ  ARG A 647    11627   7698  16407      2   -105   -688       C
ATOM   4085  NH1 ARG A 647      38.385  -7.407 -11.619  1.00 86.01           N
ANISOU 4085  NH1 ARG A 647    10635   6627  15416     -2    -34   -697       N
ATOM   4086  NH2 ARG A 647      36.209  -6.876 -12.119  1.00 74.89           N
ANISOU 4086  NH2 ARG A 647     9261   5251  13944    -13   -169   -753       N
ATOM   4087  N   ASP A 648      36.498  -7.644  -4.373  1.00 64.69           N
ANISOU 4087  N   ASP A 648     7690   4123  12768    181    -35   -267       N
ATOM   4088  CA  ASP A 648      36.284  -8.887  -3.619  1.00 65.59           C
ANISOU 4088  CA  ASP A 648     7769   4184  12968    202     29   -203       C
ATOM   4089  C   ASP A 648      35.419  -8.540  -2.396  1.00 69.25           C
ANISOU 4089  C   ASP A 648     8267   4659  13387    256     66   -126       C
ATOM   4090  O   ASP A 648      34.472  -9.253  -2.099  1.00 70.80           O
ANISOU 4090  O   ASP A 648     8425   4809  13667    262    141    -90       O
ATOM   4091  CB  ASP A 648      37.653  -9.413  -3.134  1.00 68.34           C
ANISOU 4091  CB  ASP A 648     8127   4507  13333    225     20   -170       C
ATOM   4092  CG  ASP A 648      37.879 -10.907  -3.122  1.00 82.57           C
ANISOU 4092  CG  ASP A 648     9878   6241  15254    216     78   -147       C
ATOM   4093  OD1 ASP A 648      37.911 -11.506  -4.213  1.00 83.82           O
ANISOU 4093  OD1 ASP A 648     9992   6368  15489    164     97   -206       O
ATOM   4094  OD2 ASP A 648      38.179 -11.450  -2.038  1.00 91.26           O
ANISOU 4094  OD2 ASP A 648    10998   7314  16362    266     97    -71       O
ATOM   4095  N   VAL A 649      35.731  -7.419  -1.722  1.00 64.75           N
ANISOU 4095  N   VAL A 649     7772   4138  12692    297     21   -102       N
ATOM   4096  CA  VAL A 649      35.038  -6.870  -0.544  1.00 64.42           C
ANISOU 4096  CA  VAL A 649     7801   4103  12574    358     58    -30       C
ATOM   4097  C   VAL A 649      33.556  -6.584  -0.838  1.00 66.80           C
ANISOU 4097  C   VAL A 649     8058   4401  12921    338    114    -38       C
ATOM   4098  O   VAL A 649      32.712  -6.828   0.017  1.00 65.87           O
ANISOU 4098  O   VAL A 649     7958   4240  12831    379    209     32       O
ATOM   4099  CB  VAL A 649      35.810  -5.633   0.063  1.00 67.41           C
ANISOU 4099  CB  VAL A 649     8275   4532  12805    400    -27    -22       C
ATOM   4100  CG1 VAL A 649      35.001  -4.897   1.130  1.00 66.68           C
ANISOU 4100  CG1 VAL A 649     8276   4446  12613    460     14     41       C
ATOM   4101  CG2 VAL A 649      37.166  -6.060   0.645  1.00 67.65           C
ANISOU 4101  CG2 VAL A 649     8346   4534  12825    435    -87      5       C
ATOM   4102  N   ILE A 650      33.247  -6.078  -2.037  1.00 64.20           N
ANISOU 4102  N   ILE A 650     7678   4103  12611    280     59   -122       N
ATOM   4103  CA  ILE A 650      31.883  -5.702  -2.435  1.00 64.03           C
ANISOU 4103  CA  ILE A 650     7607   4072  12651    258     77   -143       C
ATOM   4104  C   ILE A 650      31.084  -6.835  -3.059  1.00 67.45           C
ANISOU 4104  C   ILE A 650     7937   4429  13263    218    111   -167       C
ATOM   4105  O   ILE A 650      29.884  -6.915  -2.824  1.00 67.59           O
ANISOU 4105  O   ILE A 650     7899   4397  13386    224    169   -140       O
ATOM   4106  CB  ILE A 650      31.875  -4.379  -3.259  1.00 66.00           C
ANISOU 4106  CB  ILE A 650     7878   4388  12811    230    -16   -217       C
ATOM   4107  CG1 ILE A 650      30.560  -3.577  -3.059  1.00 66.77           C
ANISOU 4107  CG1 ILE A 650     7959   4487  12922    239      5   -202       C
ATOM   4108  CG2 ILE A 650      32.202  -4.620  -4.726  1.00 66.16           C
ANISOU 4108  CG2 ILE A 650     7869   4400  12867    170    -86   -313       C
ATOM   4109  CD1 ILE A 650      30.571  -2.116  -3.602  1.00 67.11           C
ANISOU 4109  CD1 ILE A 650     8044   4603  12850    227    -79   -256       C
ATOM   4110  N   GLU A 651      31.747  -7.697  -3.849  1.00 64.65           N
ANISOU 4110  N   GLU A 651     7556   4054  12956    180     77   -217       N
ATOM   4111  CA  GLU A 651      31.144  -8.849  -4.535  1.00 65.30           C
ANISOU 4111  CA  GLU A 651     7550   4057  13204    140     90   -252       C
ATOM   4112  C   GLU A 651      31.021 -10.063  -3.617  1.00 73.87           C
ANISOU 4112  C   GLU A 651     8595   5076  14396    169    203   -171       C
ATOM   4113  O   GLU A 651      30.125 -10.891  -3.802  1.00 75.06           O
ANISOU 4113  O   GLU A 651     8656   5147  14716    151    244   -172       O
ATOM   4114  CB  GLU A 651      31.990  -9.258  -5.756  1.00 65.76           C
ANISOU 4114  CB  GLU A 651     7623   4111  13249     94     21   -336       C
ATOM   4115  CG  GLU A 651      31.957  -8.329  -6.966  1.00 71.15           C
ANISOU 4115  CG  GLU A 651     8353   4823  13856     61    -82   -430       C
ATOM   4116  CD  GLU A 651      32.813  -8.752  -8.156  1.00 87.43           C
ANISOU 4116  CD  GLU A 651    10462   6860  15897     26   -119   -507       C
ATOM   4117  OE1 GLU A 651      33.810  -9.487  -7.958  1.00 90.67           O
ANISOU 4117  OE1 GLU A 651    10874   7256  16321     29    -67   -483       O
ATOM   4118  OE2 GLU A 651      32.504  -8.323  -9.291  1.00 68.87           O
ANISOU 4118  OE2 GLU A 651     8159   4495  13514      0   -198   -591       O
ATOM   4119  N   HIS A 652      31.959 -10.227  -2.677  1.00 73.22           N
ANISOU 4119  N   HIS A 652     8578   5013  14227    216    244   -104       N
ATOM   4120  CA  HIS A 652      31.966 -11.419  -1.818  1.00 74.75           C
ANISOU 4120  CA  HIS A 652     8757   5139  14504    251    350    -25       C
ATOM   4121  C   HIS A 652      31.614 -11.158  -0.364  1.00 85.52           C
ANISOU 4121  C   HIS A 652    10196   6486  15813    329    449     81       C
ATOM   4122  O   HIS A 652      31.268 -12.088   0.361  1.00 85.63           O
ANISOU 4122  O   HIS A 652    10201   6423  15913    365    565    152       O
ATOM   4123  CB  HIS A 652      33.256 -12.238  -2.020  1.00 73.86           C
ANISOU 4123  CB  HIS A 652     8655   5024  14383    241    325    -35       C
ATOM   4124  CG  HIS A 652      33.604 -12.409  -3.472  1.00 75.52           C
ANISOU 4124  CG  HIS A 652     8822   5240  14633    171    248   -138       C
ATOM   4125  ND1 HIS A 652      32.658 -12.814  -4.403  1.00 76.54           N
ANISOU 4125  ND1 HIS A 652     8876   5320  14884    122    236   -200       N
ATOM   4126  CD2 HIS A 652      34.770 -12.176  -4.114  1.00 76.31           C
ANISOU 4126  CD2 HIS A 652     8958   5372  14665    149    185   -188       C
ATOM   4127  CE1 HIS A 652      33.277 -12.818  -5.569  1.00 75.45           C
ANISOU 4127  CE1 HIS A 652     8756   5190  14721     77    165   -285       C
ATOM   4128  NE2 HIS A 652      34.549 -12.446  -5.447  1.00 75.73           N
ANISOU 4128  NE2 HIS A 652     8853   5271  14648     91    148   -278       N
ATOM   4129  N   GLY A 653      31.661  -9.889   0.020  1.00 87.00           N
ANISOU 4129  N   GLY A 653    10465   6734  15858    358    410     89       N
ATOM   4130  CA  GLY A 653      31.259  -9.403   1.334  1.00 89.95           C
ANISOU 4130  CA  GLY A 653    10941   7087  16148    437    498    182       C
ATOM   4131  C   GLY A 653      30.127  -8.396   1.199  1.00 99.57           C
ANISOU 4131  C   GLY A 653    12135   8314  17381    429    521    171       C
ATOM   4132  O   GLY A 653      30.131  -7.579   0.267  1.00 99.15           O
ANISOU 4132  O   GLY A 653    12045   8326  17300    378    414     90       O
ATOM   4133  N   THR A 654      29.153  -8.436   2.138  1.00 99.93           N
ANISOU 4133  N   THR A 654    12209   8285  17475    483    672    256       N
ATOM   4134  CA  THR A 654      27.949  -7.578   2.176  1.00101.19           C
ANISOU 4134  CA  THR A 654    12337   8422  17689    486    732    265       C
ATOM   4135  C   THR A 654      26.845  -8.089   1.202  1.00107.09           C
ANISOU 4135  C   THR A 654    12894   9101  18693    420    747    216       C
ATOM   4136  O   THR A 654      26.846  -7.747   0.011  1.00106.64           O
ANISOU 4136  O   THR A 654    12759   9093  18668    352    607    118       O
ATOM   4137  CB  THR A 654      28.255  -6.037   2.116  1.00113.09           C
ANISOU 4137  CB  THR A 654    13925  10030  19015    489    629    231       C
ATOM   4138  OG1 THR A 654      28.446  -5.615   0.761  1.00112.82           O
ANISOU 4138  OG1 THR A 654    13800  10066  18998    409    477    121       O
ATOM   4139  CG2 THR A 654      29.460  -5.612   2.983  1.00112.53           C
ANISOU 4139  CG2 THR A 654    14031  10012  18714    551    581    267       C
ATOM   4140  N   GLY A 655      25.942  -8.924   1.727  1.00104.63           N
ANISOU 4140  N   GLY A 655    12522   8665  18566    446    912    284       N
ATOM   4141  CA  GLY A 655      24.827  -9.499   0.979  1.00127.52           C
ANISOU 4141  CA  GLY A 655    15233  11468  21751    393    934    247       C
ATOM   4142  C   GLY A 655      24.792 -11.014   1.014  1.00161.78           C
ANISOU 4142  C   GLY A 655    19495  15716  26256    387   1010    267       C
ATOM   4143  O   GLY A 655      23.954 -11.641   0.361  1.00126.07           O
ANISOU 4143  O   GLY A 655    14809  11107  21983    338   1002    224       O
ATOM   4144  N   LYS A 660      24.096  -5.387  -4.588  1.00105.18           N
ANISOU 4144  N   LYS A 660    12259   8913  18791    133     71   -255       N
ATOM   4145  CA  LYS A 660      22.692  -5.151  -4.948  1.00105.79           C
ANISOU 4145  CA  LYS A 660    12211   8896  19087    115     31   -279       C
ATOM   4146  C   LYS A 660      22.531  -4.570  -6.377  1.00109.02           C
ANISOU 4146  C   LYS A 660    12629   9324  19469     69   -189   -401       C
ATOM   4147  O   LYS A 660      21.399  -4.286  -6.805  1.00109.37           O
ANISOU 4147  O   LYS A 660    12573   9286  19696     53   -266   -435       O
ATOM   4148  CB  LYS A 660      21.998  -4.239  -3.912  1.00108.12           C
ANISOU 4148  CB  LYS A 660    12503   9184  19396    160    161   -193       C
ATOM   4149  CG  LYS A 660      21.584  -4.926  -2.612  1.00114.68           C
ANISOU 4149  CG  LYS A 660    13296   9922  20355    209    389    -75       C
ATOM   4150  CD  LYS A 660      20.576  -4.066  -1.841  1.00120.72           C
ANISOU 4150  CD  LYS A 660    14035  10634  21199    248    515     -3       C
ATOM   4151  CE  LYS A 660      20.998  -3.796  -0.416  1.00124.91           C
ANISOU 4151  CE  LYS A 660    14706  11184  21571    324    715    114       C
ATOM   4152  NZ  LYS A 660      20.661  -2.408   0.008  1.00124.93           N
ANISOU 4152  NZ  LYS A 660    14780  11228  21460    356    751    145       N
ATOM   4153  N   ILE A 661      23.671  -4.383  -7.104  1.00103.00           N
ANISOU 4153  N   ILE A 661    11995   8656  18486     54   -286   -464       N
ATOM   4154  CA  ILE A 661      23.705  -3.869  -8.489  1.00100.81           C
ANISOU 4154  CA  ILE A 661    11776   8392  18137     22   -478   -577       C
ATOM   4155  C   ILE A 661      24.182  -4.987  -9.454  1.00100.46           C
ANISOU 4155  C   ILE A 661    11758   8297  18115    -10   -561   -653       C
ATOM   4156  O   ILE A 661      24.811  -5.968  -9.025  1.00 99.97           O
ANISOU 4156  O   ILE A 661    11691   8233  18059     -7   -465   -615       O
ATOM   4157  CB  ILE A 661      24.557  -2.556  -8.647  1.00102.28           C
ANISOU 4157  CB  ILE A 661    12104   8706  18051     36   -509   -592       C
ATOM   4158  CG1 ILE A 661      24.367  -1.578  -7.466  1.00101.84           C
ANISOU 4158  CG1 ILE A 661    12042   8708  17945     74   -402   -506       C
ATOM   4159  CG2 ILE A 661      24.249  -1.856  -9.973  1.00102.83           C
ANISOU 4159  CG2 ILE A 661    12239   8767  18065     15   -692   -699       C
ATOM   4160  CD1 ILE A 661      25.547  -0.602  -7.179  1.00102.79           C
ANISOU 4160  CD1 ILE A 661    12295   8956  17804     97   -375   -489       C
ATOM   4161  N   GLY A 662      23.833  -4.829 -10.732  1.00 93.21           N
ANISOU 4161  N   GLY A 662    10877   7328  17211    -35   -741   -758       N
ATOM   4162  CA  GLY A 662      24.236  -5.718 -11.816  1.00 90.80           C
ANISOU 4162  CA  GLY A 662    10638   6964  16897    -60   -842   -845       C
ATOM   4163  C   GLY A 662      25.429  -5.151 -12.560  1.00 87.43           C
ANISOU 4163  C   GLY A 662    10401   6619  16199    -55   -875   -895       C
ATOM   4164  O   GLY A 662      25.326  -4.772 -13.734  1.00 87.42           O
ANISOU 4164  O   GLY A 662    10511   6584  16120    -60  -1024   -987       O
ATOM   4165  N   ARG A 663      26.559  -5.034 -11.841  1.00 77.13           N
ANISOU 4165  N   ARG A 663     9138   5410  14756    -40   -733   -830       N
ATOM   4166  CA  ARG A 663      27.835  -4.536 -12.334  1.00 72.82           C
ANISOU 4166  CA  ARG A 663     8745   4935  13988    -32   -718   -857       C
ATOM   4167  C   ARG A 663      28.921  -5.344 -11.682  1.00 71.96           C
ANISOU 4167  C   ARG A 663     8624   4854  13864    -29   -584   -799       C
ATOM   4168  O   ARG A 663      28.782  -5.726 -10.519  1.00 70.28           O
ANISOU 4168  O   ARG A 663     8312   4657  13735    -16   -485   -714       O
ATOM   4169  CB  ARG A 663      28.008  -3.059 -11.998  1.00 69.71           C
ANISOU 4169  CB  ARG A 663     8398   4639  13450    -10   -705   -832       C
ATOM   4170  CG  ARG A 663      27.139  -2.144 -12.842  1.00 74.57           C
ANISOU 4170  CG  ARG A 663     9064   5230  14040    -11   -849   -901       C
ATOM   4171  CD  ARG A 663      27.685  -0.744 -12.922  1.00 68.90           C
ANISOU 4171  CD  ARG A 663     8445   4605  13131     10   -841   -902       C
ATOM   4172  NE  ARG A 663      28.810  -0.632 -13.853  1.00 70.80           N
ANISOU 4172  NE  ARG A 663     8845   4849  13206     13   -838   -957       N
ATOM   4173  CZ  ARG A 663      28.698  -0.305 -15.137  1.00 82.71           C
ANISOU 4173  CZ  ARG A 663    10495   6303  14627     16   -947  -1045       C
ATOM   4174  NH1 ARG A 663      29.781  -0.175 -15.891  1.00 62.37           N
ANISOU 4174  NH1 ARG A 663     8073   3721  11903     26   -903  -1083       N
ATOM   4175  NH2 ARG A 663      27.500  -0.095 -15.676  1.00 70.01           N
ANISOU 4175  NH2 ARG A 663     8881   4632  13087     13  -1098  -1096       N
ATOM   4176  N   SER A 664      29.998  -5.614 -12.423  1.00 67.34           N
ANISOU 4176  N   SER A 664     8148   4262  13177    -35   -574   -843       N
ATOM   4177  CA  SER A 664      31.131  -6.410 -11.934  1.00 67.33           C
ANISOU 4177  CA  SER A 664     8136   4273  13175    -33   -459   -796       C
ATOM   4178  C   SER A 664      32.423  -5.599 -11.902  1.00 67.64           C
ANISOU 4178  C   SER A 664     8261   4380  13058    -16   -403   -783       C
ATOM   4179  O   SER A 664      33.509  -6.161 -11.717  1.00 66.45           O
ANISOU 4179  O   SER A 664     8116   4226  12908    -14   -323   -758       O
ATOM   4180  CB  SER A 664      31.316  -7.642 -12.820  1.00 75.33           C
ANISOU 4180  CB  SER A 664     9182   5190  14251    -58   -475   -853       C
ATOM   4181  OG  SER A 664      31.618  -7.270 -14.158  1.00 86.74           O
ANISOU 4181  OG  SER A 664    10782   6593  15580    -62   -546   -946       O
ATOM   4182  N   ASP A 665      32.301  -4.274 -12.121  1.00 62.96           N
ANISOU 4182  N   ASP A 665     7729   3840  12352     -3   -447   -803       N
ATOM   4183  CA  ASP A 665      33.416  -3.342 -12.225  1.00 60.24           C
ANISOU 4183  CA  ASP A 665     7466   3547  11876     13   -405   -803       C
ATOM   4184  C   ASP A 665      33.477  -2.406 -11.041  1.00 61.26           C
ANISOU 4184  C   ASP A 665     7543   3767  11965     39   -379   -733       C
ATOM   4185  O   ASP A 665      34.084  -1.354 -11.158  1.00 61.31           O
ANISOU 4185  O   ASP A 665     7609   3817  11869     52   -373   -742       O
ATOM   4186  CB  ASP A 665      33.282  -2.560 -13.548  1.00 61.61           C
ANISOU 4186  CB  ASP A 665     7778   3692  11937     12   -472   -890       C
ATOM   4187  CG  ASP A 665      32.044  -1.675 -13.654  1.00 66.94           C
ANISOU 4187  CG  ASP A 665     8452   4392  12591     17   -577   -911       C
ATOM   4188  OD1 ASP A 665      32.067  -0.724 -14.455  1.00 66.80           O
ANISOU 4188  OD1 ASP A 665     8550   4376  12455     28   -622   -963       O
ATOM   4189  OD2 ASP A 665      31.055  -1.935 -12.929  1.00 68.96           O
ANISOU 4189  OD2 ASP A 665     8590   4655  12957     12   -605   -873       O
ATOM   4190  N   LEU A 666      32.858  -2.784  -9.912  1.00 56.45           N
ANISOU 4190  N   LEU A 666     6835   3174  11438     49   -357   -663       N
ATOM   4191  CA  LEU A 666      32.767  -1.963  -8.700  1.00 55.45           C
ANISOU 4191  CA  LEU A 666     6682   3118  11267     81   -331   -592       C
ATOM   4192  C   LEU A 666      33.597  -2.475  -7.566  1.00 56.11           C
ANISOU 4192  C   LEU A 666     6739   3213  11366    107   -264   -518       C
ATOM   4193  O   LEU A 666      33.530  -3.659  -7.258  1.00 54.69           O
ANISOU 4193  O   LEU A 666     6510   2987  11284    104   -223   -488       O
ATOM   4194  CB  LEU A 666      31.320  -1.805  -8.214  1.00 55.97           C
ANISOU 4194  CB  LEU A 666     6684   3179  11403     87   -343   -563       C
ATOM   4195  CG  LEU A 666      30.351  -1.147  -9.157  1.00 61.17           C
ANISOU 4195  CG  LEU A 666     7358   3823  12061     69   -434   -629       C
ATOM   4196  CD1 LEU A 666      28.940  -1.482  -8.759  1.00 62.49           C
ANISOU 4196  CD1 LEU A 666     7424   3939  12381     66   -438   -603       C
ATOM   4197  CD2 LEU A 666      30.524   0.347  -9.156  1.00 62.40           C
ANISOU 4197  CD2 LEU A 666     7576   4053  12079     85   -459   -636       C
ATOM   4198  N   GLY A 667      34.374  -1.573  -6.968  1.00 50.95           N
ANISOU 4198  N   GLY A 667     6123   2615  10620    135   -263   -491       N
ATOM   4199  CA  GLY A 667      35.208  -1.827  -5.801  1.00 50.25           C
ANISOU 4199  CA  GLY A 667     6031   2534  10528    171   -233   -421       C
ATOM   4200  C   GLY A 667      34.777  -0.890  -4.693  1.00 53.49           C
ANISOU 4200  C   GLY A 667     6471   2994  10861    214   -239   -366       C
ATOM   4201  O   GLY A 667      34.417   0.252  -4.982  1.00 54.49           O
ANISOU 4201  O   GLY A 667     6625   3165  10913    212   -271   -394       O
ATOM   4202  N   GLY A 668      34.798  -1.341  -3.440  1.00 48.19           N
ANISOU 4202  N   GLY A 668     5808   2308  10195    258   -203   -287       N
ATOM   4203  CA  GLY A 668      34.408  -0.459  -2.345  1.00 47.69           C
ANISOU 4203  CA  GLY A 668     5803   2276  10039    307   -199   -232       C
ATOM   4204  C   GLY A 668      34.746  -0.937  -0.957  1.00 52.13           C
ANISOU 4204  C   GLY A 668     6422   2807  10576    369   -171   -148       C
ATOM   4205  O   GLY A 668      34.990  -2.113  -0.752  1.00 49.20           O
ANISOU 4205  O   GLY A 668     6027   2385  10280    374   -136   -120       O
ATOM   4206  N   LYS A 669      34.759  -0.004  -0.003  1.00 54.23           N
ANISOU 4206  N   LYS A 669     6780   3098  10728    422   -190   -108       N
ATOM   4207  CA  LYS A 669      35.066  -0.219   1.414  1.00 56.61           C
ANISOU 4207  CA  LYS A 669     7187   3362  10960    498   -182    -29       C
ATOM   4208  C   LYS A 669      34.096   0.575   2.298  1.00 63.75           C
ANISOU 4208  C   LYS A 669     8185   4270  11769    549   -123     25       C
ATOM   4209  O   LYS A 669      33.846   1.760   2.034  1.00 64.25           O
ANISOU 4209  O   LYS A 669     8258   4387  11768    538   -154     -7       O
ATOM   4210  CB  LYS A 669      36.506   0.271   1.703  1.00 60.03           C
ANISOU 4210  CB  LYS A 669     7670   3805  11332    522   -308    -47       C
ATOM   4211  CG  LYS A 669      36.983   0.068   3.144  1.00 67.88           C
ANISOU 4211  CG  LYS A 669     8800   4749  12245    609   -345     25       C
ATOM   4212  CD  LYS A 669      37.494  -1.339   3.419  1.00 66.33           C
ANISOU 4212  CD  LYS A 669     8588   4484  12129    624   -333     60       C
ATOM   4213  CE  LYS A 669      37.773  -1.498   4.892  1.00 70.39           C
ANISOU 4213  CE  LYS A 669     9270   4936  12537    723   -366    137       C
ATOM   4214  NZ  LYS A 669      36.544  -1.909   5.600  1.00 75.24           N
ANISOU 4214  NZ  LYS A 669     9967   5514  13109    767   -214    213       N
ATOM   4215  N   THR A 670      33.600  -0.058   3.372  1.00 61.66           N
ANISOU 4215  N   THR A 670     8000   3939  11491    611    -27    110       N
ATOM   4216  CA  THR A 670      32.740   0.586   4.373  1.00 62.91           C
ANISOU 4216  CA  THR A 670     8277   4072  11555    675     59    176       C
ATOM   4217  C   THR A 670      33.633   1.101   5.510  1.00 71.03           C
ANISOU 4217  C   THR A 670     9489   5087  12413    756    -27    210       C
ATOM   4218  O   THR A 670      34.749   0.616   5.698  1.00 71.64           O
ANISOU 4218  O   THR A 670     9591   5148  12481    772   -129    203       O
ATOM   4219  CB  THR A 670      31.708  -0.395   4.964  1.00 58.44           C
ANISOU 4219  CB  THR A 670     7722   3414  11071    709    235    257       C
ATOM   4220  OG1 THR A 670      32.387  -1.505   5.542  1.00 54.84           O
ANISOU 4220  OG1 THR A 670     7321   2899  10616    749    235    299       O
ATOM   4221  CG2 THR A 670      30.702  -0.851   3.967  1.00 51.02           C
ANISOU 4221  CG2 THR A 670     6605   2463  10316    637    310    226       C
ATOM   4222  N   GLY A 671      33.109   2.030   6.287  1.00 68.86           N
ANISOU 4222  N   GLY A 671     9345   4803  12014    813     14    249       N
ATOM   4223  CA  GLY A 671      33.806   2.572   7.442  1.00 69.81           C
ANISOU 4223  CA  GLY A 671     9673   4895  11958    901    -71    283       C
ATOM   4224  C   GLY A 671      32.843   2.935   8.545  1.00 75.63           C
ANISOU 4224  C   GLY A 671    10589   5566  12580    985     70    366       C
ATOM   4225  O   GLY A 671      31.744   3.424   8.272  1.00 74.98           O
ANISOU 4225  O   GLY A 671    10452   5497  12540    960    193    374       O
ATOM   4226  N   THR A 672      33.237   2.652   9.796  1.00 75.24           N
ANISOU 4226  N   THR A 672    10764   5431  12393   1089     60    432       N
ATOM   4227  CA  THR A 672      32.488   2.972  11.013  1.00 77.50           C
ANISOU 4227  CA  THR A 672    11286   5627  12532   1193    198    520       C
ATOM   4228  C   THR A 672      33.496   3.390  12.094  1.00 83.86           C
ANISOU 4228  C   THR A 672    12350   6386  13126   1293     32    533       C
ATOM   4229  O   THR A 672      34.429   2.648  12.377  1.00 85.02           O
ANISOU 4229  O   THR A 672    12544   6496  13266   1322    -89    534       O
ATOM   4230  CB  THR A 672      31.545   1.818  11.437  1.00 87.77           C
ANISOU 4230  CB  THR A 672    12611   6823  13914   1230    435    611       C
ATOM   4231  OG1 THR A 672      30.920   1.256  10.288  1.00 89.73           O
ANISOU 4231  OG1 THR A 672    12586   7112  14393   1126    514    577       O
ATOM   4232  CG2 THR A 672      30.464   2.271  12.385  1.00 87.12           C
ANISOU 4232  CG2 THR A 672    12714   6649  13740   1313    643    697       C
ATOM   4233  N   THR A 673      33.334   4.576  12.667  1.00 81.33           N
ANISOU 4233  N   THR A 673    12196   6061  12646   1345     12    538       N
ATOM   4234  CA  THR A 673      34.250   5.061  13.709  1.00 82.65           C
ANISOU 4234  CA  THR A 673    12627   6170  12606   1446   -169    543       C
ATOM   4235  C   THR A 673      33.809   4.554  15.090  1.00 89.19           C
ANISOU 4235  C   THR A 673    13773   6848  13269   1584    -33    652       C
ATOM   4236  O   THR A 673      32.737   3.951  15.200  1.00 87.96           O
ANISOU 4236  O   THR A 673    13611   6638  13174   1594    226    724       O
ATOM   4237  CB  THR A 673      34.347   6.607  13.664  1.00 84.27           C
ANISOU 4237  CB  THR A 673    12872   6436  12711   1438   -269    490       C
ATOM   4238  OG1 THR A 673      33.051   7.154  13.867  1.00 83.53           O
ANISOU 4238  OG1 THR A 673    12842   6324  12571   1457    -44    542       O
ATOM   4239  CG2 THR A 673      34.910   7.121  12.372  1.00 74.87           C
ANISOU 4239  CG2 THR A 673    11402   5377  11669   1317   -402    386       C
ATOM   4240  N   ASN A 674      34.616   4.822  16.142  1.00 89.24           N
ANISOU 4240  N   ASN A 674    14064   6772  13070   1694   -204    663       N
ATOM   4241  CA  ASN A 674      34.271   4.434  17.505  1.00 92.22           C
ANISOU 4241  CA  ASN A 674    14800   6990  13249   1842    -89    765       C
ATOM   4242  C   ASN A 674      32.904   4.956  17.889  1.00 97.27           C
ANISOU 4242  C   ASN A 674    15555   7582  13820   1881    199    834       C
ATOM   4243  O   ASN A 674      32.606   6.123  17.657  1.00 95.28           O
ANISOU 4243  O   ASN A 674    15273   7394  13536   1849    189    797       O
ATOM   4244  CB  ASN A 674      35.351   4.841  18.510  1.00 99.52           C
ANISOU 4244  CB  ASN A 674    16028   7832  13953   1956   -360    750       C
ATOM   4245  CG  ASN A 674      36.446   3.811  18.551  1.00144.13           C
ANISOU 4245  CG  ASN A 674    21654  13444  19663   1969   -548    737       C
ATOM   4246  OD1 ASN A 674      36.378   2.841  19.311  1.00140.96           O
ANISOU 4246  OD1 ASN A 674    21452  12922  19183   2064   -466    817       O
ATOM   4247  ND2 ASN A 674      37.408   3.923  17.655  1.00141.18           N
ANISOU 4247  ND2 ASN A 674    21014  13169  19458   1869   -769    643       N
ATOM   4248  N   ASP A 675      32.060   4.054  18.429  1.00 96.18           N
ANISOU 4248  N   ASP A 675    15530   7327  13688   1945    472    938       N
ATOM   4249  CA  ASP A 675      30.675   4.294  18.852  1.00 96.61           C
ANISOU 4249  CA  ASP A 675    15688   7294  13724   1990    804   1025       C
ATOM   4250  C   ASP A 675      29.783   4.795  17.709  1.00 96.03           C
ANISOU 4250  C   ASP A 675    15272   7335  13880   1856    927    985       C
ATOM   4251  O   ASP A 675      28.909   5.625  17.921  1.00 96.29           O
ANISOU 4251  O   ASP A 675    15367   7340  13879   1875   1090   1016       O
ATOM   4252  CB  ASP A 675      30.593   5.146  20.145  1.00100.82           C
ANISOU 4252  CB  ASP A 675    16649   7706  13952   2138    825   1076       C
ATOM   4253  CG  ASP A 675      30.670   4.346  21.452  1.00120.61           C
ANISOU 4253  CG  ASP A 675    19552  10019  16255   2304    913   1177       C
ATOM   4254  OD1 ASP A 675      31.316   4.833  22.409  1.00123.25           O
ANISOU 4254  OD1 ASP A 675    20234  10278  16320   2419    732   1175       O
ATOM   4255  OD2 ASP A 675      30.079   3.232  21.517  1.00129.16           O
ANISOU 4255  OD2 ASP A 675    20606  11018  17453   2322   1160   1257       O
ATOM   4256  N   ALA A 676      30.020   4.263  16.488  1.00 88.96           N
ANISOU 4256  N   ALA A 676    14023   6558  13219   1725    842    916       N
ATOM   4257  CA  ALA A 676      29.315   4.574  15.243  1.00 86.17           C
ANISOU 4257  CA  ALA A 676    13328   6315  13099   1591    904    863       C
ATOM   4258  C   ALA A 676      29.014   6.058  15.123  1.00 88.73           C
ANISOU 4258  C   ALA A 676    13662   6703  13348   1571    871    825       C
ATOM   4259  O   ALA A 676      27.884   6.464  14.845  1.00 88.55           O
ANISOU 4259  O   ALA A 676    13532   6674  13439   1537   1059    846       O
ATOM   4260  CB  ALA A 676      28.044   3.749  15.137  1.00 87.33           C
ANISOU 4260  CB  ALA A 676    13362   6373  13446   1580   1208    938       C
ATOM   4261  N   LYS A 677      30.034   6.873  15.373  1.00 84.43           N
ANISOU 4261  N   LYS A 677    13248   6208  12622   1597    628    769       N
ATOM   4262  CA  LYS A 677      29.895   8.325  15.314  1.00 84.03           C
ANISOU 4262  CA  LYS A 677    13228   6219  12482   1585    573    728       C
ATOM   4263  C   LYS A 677      29.904   8.826  13.858  1.00 85.61           C
ANISOU 4263  C   LYS A 677    13083   6577  12868   1440    478    630       C
ATOM   4264  O   LYS A 677      29.598  10.003  13.606  1.00 84.48           O
ANISOU 4264  O   LYS A 677    12910   6492  12695   1413    467    597       O
ATOM   4265  CB  LYS A 677      30.984   9.012  16.169  1.00 87.12           C
ANISOU 4265  CB  LYS A 677    13895   6587  12622   1672    340    702       C
ATOM   4266  CG  LYS A 677      30.690   8.958  17.667  1.00 98.16           C
ANISOU 4266  CG  LYS A 677    15698   7813  13784   1832    465    801       C
ATOM   4267  CD  LYS A 677      31.725   9.729  18.474  1.00106.79           C
ANISOU 4267  CD  LYS A 677    17072   8874  14629   1920    206    765       C
ATOM   4268  CE  LYS A 677      31.225  10.117  19.846  1.00116.94           C
ANISOU 4268  CE  LYS A 677    18776  10001  15656   2071    351    852       C
ATOM   4269  NZ  LYS A 677      30.989   8.939  20.724  1.00125.78           N
ANISOU 4269  NZ  LYS A 677    20135  10960  16697   2183    512    954       N
ATOM   4270  N   ASP A 678      30.265   7.912  12.907  1.00 79.10           N
ANISOU 4270  N   ASP A 678    12015   5813  12227   1353    412    586       N
ATOM   4271  CA  ASP A 678      30.361   8.136  11.465  1.00 75.65           C
ANISOU 4271  CA  ASP A 678    11271   5508  11965   1222    321    494       C
ATOM   4272  C   ASP A 678      30.176   6.815  10.717  1.00 73.98           C
ANISOU 4272  C   ASP A 678    10853   5295  11960   1158    380    492       C
ATOM   4273  O   ASP A 678      30.802   5.822  11.075  1.00 73.66           O
ANISOU 4273  O   ASP A 678    10869   5207  11913   1191    343    514       O
ATOM   4274  CB  ASP A 678      31.740   8.735  11.086  1.00 76.57           C
ANISOU 4274  CB  ASP A 678    11359   5713  12022   1191     47    401       C
ATOM   4275  CG  ASP A 678      32.099  10.032  11.775  1.00 86.38           C
ANISOU 4275  CG  ASP A 678    12794   6956  13070   1251    -55    388       C
ATOM   4276  OD1 ASP A 678      31.567  11.075  11.376  1.00 87.13           O
ANISOU 4276  OD1 ASP A 678    12830   7111  13166   1214    -22    362       O
ATOM   4277  OD2 ASP A 678      32.905   9.996  12.720  1.00 93.22           O
ANISOU 4277  OD2 ASP A 678    13878   7756  13787   1338   -176    405       O
ATOM   4278  N   ALA A 679      29.324   6.823   9.672  1.00 66.86           N
ANISOU 4278  N   ALA A 679     9718   4441  11243   1067    458    460       N
ATOM   4279  CA  ALA A 679      29.062   5.729   8.736  1.00 65.05           C
ANISOU 4279  CA  ALA A 679     9267   4221  11229    990    491    438       C
ATOM   4280  C   ALA A 679      29.576   6.204   7.382  1.00 67.97           C
ANISOU 4280  C   ALA A 679     9447   4714  11663    888    321    328       C
ATOM   4281  O   ALA A 679      29.178   7.270   6.922  1.00 67.87           O
ANISOU 4281  O   ALA A 679     9388   4761  11640    856    300    290       O
ATOM   4282  CB  ALA A 679      27.577   5.448   8.648  1.00 66.16           C
ANISOU 4282  CB  ALA A 679     9311   4289  11536    978    711    489       C
ATOM   4283  N   TRP A 680      30.508   5.455   6.778  1.00 63.62           N
ANISOU 4283  N   TRP A 680     8805   4196  11171    845    204    279       N
ATOM   4284  CA  TRP A 680      31.144   5.803   5.503  1.00 61.01           C
ANISOU 4284  CA  TRP A 680     8322   3963  10896    759     57    178       C
ATOM   4285  C   TRP A 680      31.093   4.663   4.492  1.00 62.46           C
ANISOU 4285  C   TRP A 680     8332   4144  11254    689     65    143       C
ATOM   4286  O   TRP A 680      31.099   3.480   4.859  1.00 61.82           O
ANISOU 4286  O   TRP A 680     8256   3998  11233    709    128    188       O
ATOM   4287  CB  TRP A 680      32.639   6.077   5.729  1.00 58.97           C
ANISOU 4287  CB  TRP A 680     8140   3731  10532    781   -116    143       C
ATOM   4288  CG  TRP A 680      33.037   7.310   6.487  1.00 59.58           C
ANISOU 4288  CG  TRP A 680     8374   3823  10441    837   -195    145       C
ATOM   4289  CD1 TRP A 680      33.292   7.398   7.826  1.00 63.32           C
ANISOU 4289  CD1 TRP A 680     9064   4228  10767    935   -206    206       C
ATOM   4290  CD2 TRP A 680      33.512   8.537   5.908  1.00 58.85           C
ANISOU 4290  CD2 TRP A 680     8240   3808  10311    801   -308     74       C
ATOM   4291  NE1 TRP A 680      33.807   8.639   8.134  1.00 62.99           N
ANISOU 4291  NE1 TRP A 680     9116   4216  10599    961   -324    175       N
ATOM   4292  CE2 TRP A 680      33.970   9.356   6.971  1.00 63.55           C
ANISOU 4292  CE2 TRP A 680     9021   4380  10746    877   -384     94       C
ATOM   4293  CE3 TRP A 680      33.529   9.060   4.593  1.00 58.84           C
ANISOU 4293  CE3 TRP A 680     8079   3886  10393    717   -345     -4       C
ATOM   4294  CZ2 TRP A 680      34.438  10.674   6.759  1.00 61.67           C
ANISOU 4294  CZ2 TRP A 680     8789   4198  10445    866   -493     38       C
ATOM   4295  CZ3 TRP A 680      34.015  10.350   4.386  1.00 59.57           C
ANISOU 4295  CZ3 TRP A 680     8185   4032  10415    709   -441    -55       C
ATOM   4296  CH2 TRP A 680      34.459  11.143   5.459  1.00 60.40           C
ANISOU 4296  CH2 TRP A 680     8454   4117  10380    780   -512    -35       C
ATOM   4297  N   PHE A 681      31.159   5.037   3.213  1.00 57.35           N
ANISOU 4297  N   PHE A 681     7550   3565  10674    610     -9     59       N
ATOM   4298  CA  PHE A 681      31.318   4.137   2.070  1.00 56.19           C
ANISOU 4298  CA  PHE A 681     7260   3423  10666    540    -38      4       C
ATOM   4299  C   PHE A 681      32.037   4.872   0.955  1.00 57.39           C
ANISOU 4299  C   PHE A 681     7358   3650  10797    486   -158    -88       C
ATOM   4300  O   PHE A 681      31.594   5.933   0.518  1.00 54.19           O
ANISOU 4300  O   PHE A 681     6942   3291  10357    467   -177   -121       O
ATOM   4301  CB  PHE A 681      30.037   3.434   1.584  1.00 57.69           C
ANISOU 4301  CB  PHE A 681     7336   3564  11021    506     63     13       C
ATOM   4302  CG  PHE A 681      30.380   2.221   0.733  1.00 58.51           C
ANISOU 4302  CG  PHE A 681     7336   3647  11248    455     35    -27       C
ATOM   4303  CD1 PHE A 681      30.755   1.015   1.323  1.00 61.24           C
ANISOU 4303  CD1 PHE A 681     7702   3935  11632    483     84     22       C
ATOM   4304  CD2 PHE A 681      30.428   2.310  -0.655  1.00 59.91           C
ANISOU 4304  CD2 PHE A 681     7420   3858  11485    386    -45   -116       C
ATOM   4305  CE1 PHE A 681      31.160  -0.080   0.540  1.00 60.26           C
ANISOU 4305  CE1 PHE A 681     7489   3792  11616    437     57    -17       C
ATOM   4306  CE2 PHE A 681      30.812   1.201  -1.440  1.00 61.53           C
ANISOU 4306  CE2 PHE A 681     7555   4037  11788    344    -69   -156       C
ATOM   4307  CZ  PHE A 681      31.174   0.018  -0.833  1.00 58.97           C
ANISOU 4307  CZ  PHE A 681     7236   3660  11511    367    -16   -106       C
ATOM   4308  N   ALA A 682      33.192   4.323   0.562  1.00 53.15           N
ANISOU 4308  N   ALA A 682     6799   3115  10281    468   -230   -122       N
ATOM   4309  CA  ALA A 682      34.054   4.829  -0.484  1.00 51.18           C
ANISOU 4309  CA  ALA A 682     6505   2908  10031    422   -318   -203       C
ATOM   4310  C   ALA A 682      34.142   3.732  -1.523  1.00 60.68           C
ANISOU 4310  C   ALA A 682     7617   4083  11355    369   -304   -243       C
ATOM   4311  O   ALA A 682      34.583   2.622  -1.223  1.00 63.64           O
ANISOU 4311  O   ALA A 682     7980   4412  11789    378   -288   -216       O
ATOM   4312  CB  ALA A 682      35.413   5.140   0.089  1.00 50.66           C
ANISOU 4312  CB  ALA A 682     6499   2841   9908    457   -402   -201       C
ATOM   4313  N   GLY A 683      33.633   4.010  -2.709  1.00 58.78           N
ANISOU 4313  N   GLY A 683     7325   3860  11148    320   -311   -305       N
ATOM   4314  CA  GLY A 683      33.592   3.036  -3.791  1.00 59.16           C
ANISOU 4314  CA  GLY A 683     7309   3872  11298    272   -306   -352       C
ATOM   4315  C   GLY A 683      33.754   3.631  -5.168  1.00 65.71           C
ANISOU 4315  C   GLY A 683     8140   4721  12108    231   -352   -437       C
ATOM   4316  O   GLY A 683      33.509   4.824  -5.382  1.00 68.99           O
ANISOU 4316  O   GLY A 683     8585   5180  12447    233   -380   -460       O
ATOM   4317  N   PHE A 684      34.125   2.795  -6.120  1.00 60.76           N
ANISOU 4317  N   PHE A 684     7492   4050  11543    197   -352   -483       N
ATOM   4318  CA  PHE A 684      34.384   3.247  -7.481  1.00 59.54           C
ANISOU 4318  CA  PHE A 684     7374   3891  11357    168   -381   -564       C
ATOM   4319  C   PHE A 684      34.204   2.149  -8.548  1.00 62.49           C
ANISOU 4319  C   PHE A 684     7742   4198  11806    133   -380   -613       C
ATOM   4320  O   PHE A 684      33.974   0.981  -8.254  1.00 61.44           O
ANISOU 4320  O   PHE A 684     7558   4024  11764    127   -355   -587       O
ATOM   4321  CB  PHE A 684      35.849   3.776  -7.566  1.00 60.30           C
ANISOU 4321  CB  PHE A 684     7502   3993  11415    178   -374   -578       C
ATOM   4322  CG  PHE A 684      36.900   2.742  -7.188  1.00 61.63           C
ANISOU 4322  CG  PHE A 684     7638   4115  11666    181   -345   -551       C
ATOM   4323  CD1 PHE A 684      37.388   1.837  -8.128  1.00 64.31           C
ANISOU 4323  CD1 PHE A 684     7974   4389  12071    154   -309   -591       C
ATOM   4324  CD2 PHE A 684      37.368   2.645  -5.883  1.00 63.61           C
ANISOU 4324  CD2 PHE A 684     7870   4375  11925    217   -357   -487       C
ATOM   4325  CE1 PHE A 684      38.317   0.844  -7.762  1.00 64.96           C
ANISOU 4325  CE1 PHE A 684     8015   4421  12245    156   -278   -563       C
ATOM   4326  CE2 PHE A 684      38.283   1.639  -5.515  1.00 66.40           C
ANISOU 4326  CE2 PHE A 684     8189   4675  12364    223   -343   -460       C
ATOM   4327  CZ  PHE A 684      38.756   0.752  -6.458  1.00 63.90           C
ANISOU 4327  CZ  PHE A 684     7849   4299  12129    191   -301   -498       C
ATOM   4328  N   ASN A 685      34.377   2.572  -9.790  1.00 58.64           N
ANISOU 4328  N   ASN A 685     7322   3691  11268    117   -403   -685       N
ATOM   4329  CA  ASN A 685      34.499   1.811 -11.019  1.00 58.24           C
ANISOU 4329  CA  ASN A 685     7321   3566  11241     93   -405   -749       C
ATOM   4330  C   ASN A 685      35.623   2.598 -11.757  1.00 62.23           C
ANISOU 4330  C   ASN A 685     7916   4063  11666    100   -367   -788       C
ATOM   4331  O   ASN A 685      36.110   3.602 -11.213  1.00 61.66           O
ANISOU 4331  O   ASN A 685     7837   4043  11547    119   -356   -764       O
ATOM   4332  CB  ASN A 685      33.149   1.708 -11.768  1.00 54.30           C
ANISOU 4332  CB  ASN A 685     6841   3035  10755     77   -487   -797       C
ATOM   4333  CG  ASN A 685      32.889   2.629 -12.933  1.00 65.90           C
ANISOU 4333  CG  ASN A 685     8428   4491  12121     80   -546   -870       C
ATOM   4334  OD1 ASN A 685      32.918   3.852 -12.834  1.00 62.24           O
ANISOU 4334  OD1 ASN A 685     7994   4082  11572     95   -554   -868       O
ATOM   4335  ND2 ASN A 685      32.555   2.046 -14.052  1.00 57.08           N
ANISOU 4335  ND2 ASN A 685     7388   3292  11008     68   -597   -937       N
ATOM   4336  N   GLY A 686      36.044   2.148 -12.932  1.00 56.39           N
ANISOU 4336  N   GLY A 686     7263   3246  10918     90   -338   -845       N
ATOM   4337  CA  GLY A 686      37.107   2.820 -13.664  1.00 54.99           C
ANISOU 4337  CA  GLY A 686     7176   3034  10684    102   -268   -877       C
ATOM   4338  C   GLY A 686      36.841   4.249 -14.068  1.00 57.74           C
ANISOU 4338  C   GLY A 686     7603   3419  10917    119   -294   -906       C
ATOM   4339  O   GLY A 686      37.800   4.989 -14.303  1.00 60.75           O
ANISOU 4339  O   GLY A 686     8025   3785  11271    135   -222   -913       O
ATOM   4340  N   LYS A 687      35.546   4.660 -14.121  1.00 50.10           N
ANISOU 4340  N   LYS A 687     6645   2491   9899    118   -394   -921       N
ATOM   4341  CA  LYS A 687      35.120   5.995 -14.567  1.00 49.37           C
ANISOU 4341  CA  LYS A 687     6633   2430   9695    135   -435   -951       C
ATOM   4342  C   LYS A 687      34.540   6.947 -13.481  1.00 51.66           C
ANISOU 4342  C   LYS A 687     6832   2822   9974    142   -478   -902       C
ATOM   4343  O   LYS A 687      34.349   8.140 -13.758  1.00 50.96           O
ANISOU 4343  O   LYS A 687     6800   2767   9797    157   -497   -921       O
ATOM   4344  CB  LYS A 687      34.128   5.874 -15.748  1.00 50.82           C
ANISOU 4344  CB  LYS A 687     6935   2554   9822    134   -527  -1020       C
ATOM   4345  CG  LYS A 687      34.617   5.006 -16.917  1.00 57.85           C
ANISOU 4345  CG  LYS A 687     7961   3329  10691    136   -490  -1076       C
ATOM   4346  CD  LYS A 687      35.486   5.721 -17.937  1.00 73.95           C
ANISOU 4346  CD  LYS A 687    10171   5308  12617    165   -397  -1115       C
ATOM   4347  CE  LYS A 687      36.263   4.757 -18.801  1.00 91.58           C
ANISOU 4347  CE  LYS A 687    12527   7419  14850    170   -310  -1151       C
ATOM   4348  NZ  LYS A 687      37.404   5.419 -19.474  1.00 99.25           N
ANISOU 4348  NZ  LYS A 687    13619   8328  15764    199   -154  -1160       N
ATOM   4349  N   LEU A 688      34.278   6.438 -12.267  1.00 46.51           N
ANISOU 4349  N   LEU A 688     6057   2211   9403    136   -483   -840       N
ATOM   4350  CA  LEU A 688      33.632   7.215 -11.234  1.00 46.34           C
ANISOU 4350  CA  LEU A 688     5972   2267   9368    149   -512   -791       C
ATOM   4351  C   LEU A 688      33.928   6.736  -9.828  1.00 51.50           C
ANISOU 4351  C   LEU A 688     6536   2950  10083    159   -477   -716       C
ATOM   4352  O   LEU A 688      33.665   5.563  -9.512  1.00 52.44           O
ANISOU 4352  O   LEU A 688     6601   3035  10290    149   -466   -691       O
ATOM   4353  CB  LEU A 688      32.103   7.148 -11.484  1.00 46.74           C
ANISOU 4353  CB  LEU A 688     6004   2307   9446    139   -591   -806       C
ATOM   4354  CG  LEU A 688      31.193   8.225 -10.858  1.00 49.86           C
ANISOU 4354  CG  LEU A 688     6364   2764   9816    152   -621   -775       C
ATOM   4355  CD1 LEU A 688      31.657   9.619 -11.205  1.00 48.59           C
ANISOU 4355  CD1 LEU A 688     6280   2648   9533    168   -621   -800       C
ATOM   4356  CD2 LEU A 688      29.761   8.025 -11.312  1.00 52.76           C
ANISOU 4356  CD2 LEU A 688     6699   3089  10257    139   -703   -797       C
ATOM   4357  N   VAL A 689      34.402   7.678  -8.961  1.00 45.61           N
ANISOU 4357  N   VAL A 689     5783   2260   9287    183   -466   -679       N
ATOM   4358  CA  VAL A 689      34.676   7.445  -7.540  1.00 44.67           C
ANISOU 4358  CA  VAL A 689     5617   2163   9192    207   -451   -608       C
ATOM   4359  C   VAL A 689      33.598   8.168  -6.752  1.00 49.73           C
ANISOU 4359  C   VAL A 689     6251   2852   9791    226   -464   -567       C
ATOM   4360  O   VAL A 689      33.442   9.366  -6.926  1.00 48.40           O
ANISOU 4360  O   VAL A 689     6117   2726   9548    233   -485   -586       O
ATOM   4361  CB  VAL A 689      36.099   7.901  -7.097  1.00 47.63           C
ANISOU 4361  CB  VAL A 689     6000   2541   9556    227   -445   -600       C
ATOM   4362  CG1 VAL A 689      36.330   7.612  -5.617  1.00 47.54           C
ANISOU 4362  CG1 VAL A 689     5969   2537   9558    261   -458   -529       C
ATOM   4363  CG2 VAL A 689      37.188   7.242  -7.935  1.00 47.01           C
ANISOU 4363  CG2 VAL A 689     5920   2396   9544    208   -409   -638       C
ATOM   4364  N   THR A 690      32.880   7.453  -5.862  1.00 49.60           N
ANISOU 4364  N   THR A 690     6197   2821   9828    239   -438   -508       N
ATOM   4365  CA  THR A 690      31.849   8.052  -4.999  1.00 49.92           C
ANISOU 4365  CA  THR A 690     6236   2885   9845    264   -418   -458       C
ATOM   4366  C   THR A 690      32.107   7.733  -3.534  1.00 53.47           C
ANISOU 4366  C   THR A 690     6710   3327  10279    309   -375   -378       C
ATOM   4367  O   THR A 690      32.313   6.563  -3.180  1.00 52.28           O
ANISOU 4367  O   THR A 690     6539   3132  10194    314   -345   -347       O
ATOM   4368  CB  THR A 690      30.434   7.660  -5.436  1.00 54.72           C
ANISOU 4368  CB  THR A 690     6786   3457  10549    242   -413   -463       C
ATOM   4369  OG1 THR A 690      30.292   8.050  -6.799  1.00 58.74           O
ANISOU 4369  OG1 THR A 690     7306   3965  11045    210   -479   -543       O
ATOM   4370  CG2 THR A 690      29.330   8.328  -4.567  1.00 51.94           C
ANISOU 4370  CG2 THR A 690     6424   3113  10199    268   -369   -407       C
ATOM   4371  N   VAL A 691      32.105   8.785  -2.694  1.00 47.99           N
ANISOU 4371  N   VAL A 691     6076   2671   9489    347   -375   -346       N
ATOM   4372  CA  VAL A 691      32.270   8.689  -1.245  1.00 47.11           C
ANISOU 4372  CA  VAL A 691     6033   2543   9326    404   -344   -270       C
ATOM   4373  C   VAL A 691      31.017   9.240  -0.592  1.00 55.48           C
ANISOU 4373  C   VAL A 691     7119   3598  10363    431   -273   -220       C
ATOM   4374  O   VAL A 691      30.630  10.373  -0.873  1.00 56.84           O
ANISOU 4374  O   VAL A 691     7299   3813  10486    424   -289   -243       O
ATOM   4375  CB  VAL A 691      33.574   9.364  -0.729  1.00 47.71           C
ANISOU 4375  CB  VAL A 691     6178   2640   9308    435   -418   -278       C
ATOM   4376  CG1 VAL A 691      33.612   9.414   0.804  1.00 47.57           C
ANISOU 4376  CG1 VAL A 691     6271   2595   9206    507   -406   -204       C
ATOM   4377  CG2 VAL A 691      34.807   8.640  -1.260  1.00 46.39           C
ANISOU 4377  CG2 VAL A 691     5970   2448   9206    414   -466   -314       C
ATOM   4378  N   THR A 692      30.362   8.436   0.235  1.00 53.80           N
ANISOU 4378  N   THR A 692     6917   3324  10199    462   -181   -149       N
ATOM   4379  CA  THR A 692      29.177   8.854   0.990  1.00 54.82           C
ANISOU 4379  CA  THR A 692     7079   3422  10331    497    -76    -86       C
ATOM   4380  C   THR A 692      29.508   8.852   2.502  1.00 61.48           C
ANISOU 4380  C   THR A 692     8075   4228  11058    579    -23     -6       C
ATOM   4381  O   THR A 692      30.413   8.133   2.947  1.00 61.35           O
ANISOU 4381  O   THR A 692     8112   4189  11011    604    -57      9       O
ATOM   4382  CB  THR A 692      27.925   8.014   0.627  1.00 62.99           C
ANISOU 4382  CB  THR A 692     8000   4388  11548    471     12    -67       C
ATOM   4383  OG1 THR A 692      28.154   6.639   0.933  1.00 66.47           O
ANISOU 4383  OG1 THR A 692     8426   4769  12060    480     54    -35       O
ATOM   4384  CG2 THR A 692      27.514   8.161  -0.827  1.00 59.58           C
ANISOU 4384  CG2 THR A 692     7448   3978  11212    402    -67   -149       C
ATOM   4385  N   TRP A 693      28.818   9.689   3.277  1.00 58.61           N
ANISOU 4385  N   TRP A 693     7797   3849  10624    624     53     42       N
ATOM   4386  CA  TRP A 693      29.021   9.753   4.718  1.00 59.43           C
ANISOU 4386  CA  TRP A 693     8084   3900  10596    712    109    118       C
ATOM   4387  C   TRP A 693      27.706  10.073   5.371  1.00 65.40           C
ANISOU 4387  C   TRP A 693     8884   4590  11373    751    281    191       C
ATOM   4388  O   TRP A 693      26.908  10.816   4.807  1.00 66.04           O
ANISOU 4388  O   TRP A 693     8878   4696  11518    714    307    169       O
ATOM   4389  CB  TRP A 693      30.123  10.769   5.094  1.00 57.87           C
ANISOU 4389  CB  TRP A 693     8007   3756  10225    742    -26     87       C
ATOM   4390  CG  TRP A 693      30.109  11.229   6.530  1.00 60.07           C
ANISOU 4390  CG  TRP A 693     8504   3978  10340    838     20    157       C
ATOM   4391  CD1 TRP A 693      30.842  10.725   7.565  1.00 63.94           C
ANISOU 4391  CD1 TRP A 693     9163   4407  10726    913    -16    199       C
ATOM   4392  CD2 TRP A 693      29.344  12.319   7.077  1.00 60.23           C
ANISOU 4392  CD2 TRP A 693     8620   3990  10276    875    103    189       C
ATOM   4393  NE1 TRP A 693      30.568  11.419   8.729  1.00 64.74           N
ANISOU 4393  NE1 TRP A 693     9477   4456  10667    999     38    255       N
ATOM   4394  CE2 TRP A 693      29.641  12.394   8.461  1.00 65.80           C
ANISOU 4394  CE2 TRP A 693     9567   4621  10813    976    123    252       C
ATOM   4395  CE3 TRP A 693      28.398  13.205   6.544  1.00 60.40           C
ANISOU 4395  CE3 TRP A 693     8552   4046  10349    836    165    174       C
ATOM   4396  CZ2 TRP A 693      29.015  13.315   9.318  1.00 65.27           C
ANISOU 4396  CZ2 TRP A 693     9663   4513  10624   1039    220    301       C
ATOM   4397  CZ3 TRP A 693      27.766  14.091   7.396  1.00 62.13           C
ANISOU 4397  CZ3 TRP A 693     8909   4229  10468    893    264    226       C
ATOM   4398  CH2 TRP A 693      28.080  14.146   8.764  1.00 63.87           C
ANISOU 4398  CH2 TRP A 693     9377   4374  10516    994    298    289       C
ATOM   4399  N   VAL A 694      27.469   9.496   6.554  1.00 62.50           N
ANISOU 4399  N   VAL A 694     8659   4126  10963    829    408    280       N
ATOM   4400  CA  VAL A 694      26.271   9.709   7.379  1.00 62.96           C
ANISOU 4400  CA  VAL A 694     8794   4087  11040    885    615    368       C
ATOM   4401  C   VAL A 694      26.752   9.885   8.836  1.00 71.50           C
ANISOU 4401  C   VAL A 694    10158   5106  11904    996    654    437       C
ATOM   4402  O   VAL A 694      27.617   9.137   9.305  1.00 70.80           O
ANISOU 4402  O   VAL A 694    10168   4993  11739   1035    591    449       O
ATOM   4403  CB  VAL A 694      25.206   8.578   7.242  1.00 65.14           C
ANISOU 4403  CB  VAL A 694     8941   4262  11546    870    786    417       C
ATOM   4404  CG1 VAL A 694      23.989   8.849   8.119  1.00 65.58           C
ANISOU 4404  CG1 VAL A 694     9071   4198  11648    931   1024    512       C
ATOM   4405  CG2 VAL A 694      24.777   8.384   5.789  1.00 63.39           C
ANISOU 4405  CG2 VAL A 694     8463   4091  11531    765    708    339       C
ATOM   4406  N   GLY A 695      26.211  10.894   9.512  1.00 71.44           N
ANISOU 4406  N   GLY A 695    10283   5066  11794   1048    746    477       N
ATOM   4407  CA  GLY A 695      26.535  11.201  10.903  1.00 73.04           C
ANISOU 4407  CA  GLY A 695    10789   5193  11772   1163    789    542       C
ATOM   4408  C   GLY A 695      25.899  12.478  11.385  1.00 78.83           C
ANISOU 4408  C   GLY A 695    11637   5906  12408   1202    881    569       C
ATOM   4409  O   GLY A 695      25.345  13.230  10.580  1.00 79.00           O
ANISOU 4409  O   GLY A 695    11489   5992  12535   1133    881    528       O
ATOM   4410  N   PHE A 696      25.980  12.733  12.703  1.00 76.43           N
ANISOU 4410  N   PHE A 696    11637   5504  11898   1317    958    638       N
ATOM   4411  CA  PHE A 696      25.459  13.959  13.326  1.00 75.74           C
ANISOU 4411  CA  PHE A 696    11711   5382  11684   1370   1052    670       C
ATOM   4412  C   PHE A 696      26.510  15.047  13.309  1.00 78.60           C
ANISOU 4412  C   PHE A 696    12161   5844  11861   1369    805    591       C
ATOM   4413  O   PHE A 696      27.690  14.745  13.467  1.00 76.70           O
ANISOU 4413  O   PHE A 696    11999   5628  11517   1389    605    551       O
ATOM   4414  CB  PHE A 696      25.007  13.689  14.770  1.00 79.18           C
ANISOU 4414  CB  PHE A 696    12466   5641  11980   1506   1274    786       C
ATOM   4415  CG  PHE A 696      23.779  12.817  14.828  1.00 81.32           C
ANISOU 4415  CG  PHE A 696    12642   5789  12467   1511   1569    874       C
ATOM   4416  CD1 PHE A 696      22.528  13.338  14.539  1.00 84.77           C
ANISOU 4416  CD1 PHE A 696    12940   6188  13081   1478   1767    904       C
ATOM   4417  CD2 PHE A 696      23.880  11.461  15.111  1.00 83.07           C
ANISOU 4417  CD2 PHE A 696    12891   5929  12745   1543   1642    922       C
ATOM   4418  CE1 PHE A 696      21.395  12.527  14.551  1.00 86.66           C
ANISOU 4418  CE1 PHE A 696    13062   6299  13568   1478   2033    982       C
ATOM   4419  CE2 PHE A 696      22.742  10.649  15.128  1.00 86.53           C
ANISOU 4419  CE2 PHE A 696    13218   6243  13415   1544   1919   1001       C
ATOM   4420  CZ  PHE A 696      21.510  11.184  14.834  1.00 85.16           C
ANISOU 4420  CZ  PHE A 696    12894   6026  13437   1509   2108   1028       C
ATOM   4421  N   ASP A 697      26.087  16.318  13.152  1.00 78.04           N
ANISOU 4421  N   ASP A 697    12073   5818  11760   1350    818    568       N
ATOM   4422  CA  ASP A 697      27.021  17.440  13.137  1.00 77.82           C
ANISOU 4422  CA  ASP A 697    12119   5878  11573   1349    596    493       C
ATOM   4423  C   ASP A 697      27.774  17.604  14.458  1.00 83.66           C
ANISOU 4423  C   ASP A 697    13209   6528  12049   1470    517    520       C
ATOM   4424  O   ASP A 697      28.981  17.848  14.433  1.00 81.41           O
ANISOU 4424  O   ASP A 697    12962   6294  11675   1471    264    450       O
ATOM   4425  CB  ASP A 697      26.361  18.719  12.634  1.00 78.64           C
ANISOU 4425  CB  ASP A 697    12119   6046  11713   1300    635    465       C
ATOM   4426  CG  ASP A 697      26.087  18.740  11.135  1.00 84.52           C
ANISOU 4426  CG  ASP A 697    12526   6907  12681   1174    587    398       C
ATOM   4427  OD1 ASP A 697      26.885  18.142  10.367  1.00 86.45           O
ANISOU 4427  OD1 ASP A 697    12626   7223  12996   1115    428    334       O
ATOM   4428  OD2 ASP A 697      25.126  19.414  10.721  1.00 85.39           O
ANISOU 4428  OD2 ASP A 697    12528   7031  12885   1138    695    404       O
ATOM   4429  N   GLN A 698      27.078  17.394  15.594  1.00 84.56           N
ANISOU 4429  N   GLN A 698    13582   6493  12055   1578    734    623       N
ATOM   4430  CA  GLN A 698      27.659  17.370  16.942  1.00 87.85           C
ANISOU 4430  CA  GLN A 698    14385   6789  12206   1714    687    664       C
ATOM   4431  C   GLN A 698      27.814  15.861  17.198  1.00 93.49           C
ANISOU 4431  C   GLN A 698    15127   7427  12970   1747    736    714       C
ATOM   4432  O   GLN A 698      26.788  15.176  17.318  1.00 94.04           O
ANISOU 4432  O   GLN A 698    15172   7409  13151   1762   1010    798       O
ATOM   4433  CB  GLN A 698      26.710  18.047  17.957  1.00 91.78           C
ANISOU 4433  CB  GLN A 698    15158   7155  12560   1814    934    751       C
ATOM   4434  CG  GLN A 698      27.328  18.346  19.327  1.00120.59           C
ANISOU 4434  CG  GLN A 698    19253  10675  15890   1964    860    781       C
ATOM   4435  CD  GLN A 698      27.734  19.791  19.491  1.00146.36           C
ANISOU 4435  CD  GLN A 698    22639  13983  18990   1979    694    719       C
ATOM   4436  OE1 GLN A 698      26.897  20.701  19.563  1.00145.39           O
ANISOU 4436  OE1 GLN A 698    22539  13848  18853   1980    859    743       O
ATOM   4437  NE2 GLN A 698      29.031  20.015  19.618  1.00138.96           N
ANISOU 4437  NE2 GLN A 698    21794  13077  17929   1999    367    640       N
ATOM   4438  N   PRO A 699      29.060  15.304  17.086  1.00 90.11           N
ANISOU 4438  N   PRO A 699    14685   7038  12514   1740    475    656       N
ATOM   4439  CA  PRO A 699      29.229  13.840  17.111  1.00 90.31           C
ANISOU 4439  CA  PRO A 699    14676   7013  12624   1749    511    694       C
ATOM   4440  C   PRO A 699      28.600  13.049  18.240  1.00 96.70           C
ANISOU 4440  C   PRO A 699    15765   7643  13335   1872    754    814       C
ATOM   4441  O   PRO A 699      28.974  13.191  19.403  1.00 97.68           O
ANISOU 4441  O   PRO A 699    16257   7649  13209   2002    718    853       O
ATOM   4442  CB  PRO A 699      30.743  13.636  16.994  1.00 91.65           C
ANISOU 4442  CB  PRO A 699    14844   7232  12744   1742    176    613       C
ATOM   4443  CG  PRO A 699      31.246  14.872  16.373  1.00 94.59           C
ANISOU 4443  CG  PRO A 699    15088   7726  13125   1673    -14    516       C
ATOM   4444  CD  PRO A 699      30.355  15.975  16.858  1.00 90.90           C
ANISOU 4444  CD  PRO A 699    14768   7226  12543   1715    144    552       C
ATOM   4445  N   THR A 700      27.615  12.224  17.861  1.00 94.25           N
ANISOU 4445  N   THR A 700    15278   7301  13233   1832   1006    872       N
ATOM   4446  CA  THR A 700      26.837  11.319  18.713  1.00 96.05           C
ANISOU 4446  CA  THR A 700    15690   7354  13452   1928   1299    994       C
ATOM   4447  C   THR A 700      26.787   9.991  17.994  1.00 97.45           C
ANISOU 4447  C   THR A 700    15601   7557  13868   1855   1334    994       C
ATOM   4448  O   THR A 700      27.098   9.928  16.805  1.00 96.62           O
ANISOU 4448  O   THR A 700    15169   7599  13944   1727   1182    908       O
ATOM   4449  CB  THR A 700      25.379  11.814  18.895  1.00110.87           C
ANISOU 4449  CB  THR A 700    17565   9145  15415   1942   1636   1070       C
ATOM   4450  OG1 THR A 700      25.260  13.217  18.634  1.00112.94           O
ANISOU 4450  OG1 THR A 700    17803   9488  15619   1908   1564   1018       O
ATOM   4451  CG2 THR A 700      24.800  11.456  20.268  1.00112.60           C
ANISOU 4451  CG2 THR A 700    18159   9140  15483   2100   1926   1201       C
ATOM   4452  N   THR A 701      26.347   8.946  18.687  1.00 92.82           N
ANISOU 4452  N   THR A 701    15160   6819  13288   1937   1549   1093       N
ATOM   4453  CA  THR A 701      26.191   7.618  18.111  1.00 90.92           C
ANISOU 4453  CA  THR A 701    14688   6578  13279   1878   1617   1105       C
ATOM   4454  C   THR A 701      25.010   7.571  17.161  1.00 92.87           C
ANISOU 4454  C   THR A 701    14592   6853  13840   1771   1806   1106       C
ATOM   4455  O   THR A 701      23.976   8.195  17.412  1.00 93.49           O
ANISOU 4455  O   THR A 701    14701   6857  13962   1794   2030   1158       O
ATOM   4456  CB  THR A 701      26.124   6.546  19.209  1.00 92.68           C
ANISOU 4456  CB  THR A 701    15192   6618  13403   2009   1792   1213       C
ATOM   4457  OG1 THR A 701      26.328   5.266  18.606  1.00 93.93           O
ANISOU 4457  OG1 THR A 701    15125   6803  13761   1946   1774   1203       O
ATOM   4458  CG2 THR A 701      24.812   6.568  20.010  1.00 86.09           C
ANISOU 4458  CG2 THR A 701    14538   5594  12579   2103   2189   1339       C
ATOM   4459  N   LEU A 702      25.177   6.833  16.068  1.00 87.44           N
ANISOU 4459  N   LEU A 702    13583   6263  13378   1657   1706   1045       N
ATOM   4460  CA  LEU A 702      24.138   6.632  15.070  1.00 86.35           C
ANISOU 4460  CA  LEU A 702    13107   6145  13557   1552   1835   1032       C
ATOM   4461  C   LEU A 702      23.215   5.468  15.483  1.00 93.69           C
ANISOU 4461  C   LEU A 702    14028   6902  14667   1597   2137   1136       C
ATOM   4462  O   LEU A 702      22.122   5.310  14.937  1.00 93.21           O
ANISOU 4462  O   LEU A 702    13736   6794  14886   1541   2310   1153       O
ATOM   4463  CB  LEU A 702      24.785   6.314  13.711  1.00 83.91           C
ANISOU 4463  CB  LEU A 702    12491   6001  13391   1419   1584    917       C
ATOM   4464  CG  LEU A 702      25.385   7.460  12.923  1.00 85.48           C
ANISOU 4464  CG  LEU A 702    12589   6366  13524   1342   1335    809       C
ATOM   4465  CD1 LEU A 702      26.103   6.936  11.724  1.00 84.04           C
ANISOU 4465  CD1 LEU A 702    12162   6308  13460   1236   1124    712       C
ATOM   4466  CD2 LEU A 702      24.330   8.425  12.476  1.00 84.71           C
ANISOU 4466  CD2 LEU A 702    12360   6283  13543   1296   1437    801       C
ATOM   4467  N   GLY A 703      23.685   4.669  16.432  1.00 92.84           N
ANISOU 4467  N   GLY A 703    14173   6694  14409   1701   2188   1201       N
ATOM   4468  CA  GLY A 703      23.027   3.460  16.895  1.00 94.63           C
ANISOU 4468  CA  GLY A 703    14426   6753  14777   1756   2461   1301       C
ATOM   4469  C   GLY A 703      24.026   2.333  16.840  1.00 99.21           C
ANISOU 4469  C   GLY A 703    15008   7367  15321   1754   2303   1279       C
ATOM   4470  O   GLY A 703      25.089   2.502  16.234  1.00 97.43           O
ANISOU 4470  O   GLY A 703    14689   7300  15032   1686   1994   1179       O
ATOM   4471  N   ARG A 704      23.738   1.204  17.499  1.00 97.64           N
ANISOU 4471  N   ARG A 704    14925   7011  15163   1834   2516   1374       N
ATOM   4472  CA  ARG A 704      24.716   0.123  17.498  1.00 97.87           C
ANISOU 4472  CA  ARG A 704    14970   7064  15151   1839   2367   1358       C
ATOM   4473  C   ARG A 704      24.774  -0.581  16.149  1.00101.82           C
ANISOU 4473  C   ARG A 704    15065   7680  15941   1690   2253   1275       C
ATOM   4474  O   ARG A 704      25.824  -0.556  15.500  1.00 99.56           O
ANISOU 4474  O   ARG A 704    14678   7545  15607   1620   1959   1178       O
ATOM   4475  CB  ARG A 704      24.538  -0.835  18.685  1.00 99.28           C
ANISOU 4475  CB  ARG A 704    15435   7040  15245   1981   2610   1485       C
ATOM   4476  CG  ARG A 704      24.765  -0.170  20.049  1.00107.56           C
ANISOU 4476  CG  ARG A 704    16953   7974  15943   2144   2666   1557       C
ATOM   4477  CD  ARG A 704      25.275  -1.106  21.141  1.00120.33           C
ANISOU 4477  CD  ARG A 704    18912   9443  17364   2287   2723   1642       C
ATOM   4478  NE  ARG A 704      24.460  -2.313  21.311  1.00128.96           N
ANISOU 4478  NE  ARG A 704    19939  10386  18675   2313   3042   1736       N
ATOM   4479  CZ  ARG A 704      24.855  -3.537  20.972  1.00145.37           C
ANISOU 4479  CZ  ARG A 704    21855  12487  20891   2269   2982   1723       C
ATOM   4480  NH1 ARG A 704      26.059  -3.733  20.446  1.00126.83           N
ANISOU 4480  NH1 ARG A 704    19397  10303  18491   2199   2624   1623       N
ATOM   4481  NH2 ARG A 704      24.049  -4.576  21.156  1.00141.04           N
ANISOU 4481  NH2 ARG A 704    21248  11789  20551   2296   3289   1811       N
ATOM   4482  N   ARG A 705      23.615  -1.086  15.676  1.00 99.96           N
ANISOU 4482  N   ARG A 705    14594   7370  16018   1639   2479   1305       N
ATOM   4483  CA  ARG A 705      23.446  -1.795  14.397  1.00 98.80           C
ANISOU 4483  CA  ARG A 705    14071   7299  16170   1504   2399   1230       C
ATOM   4484  C   ARG A 705      23.509  -0.819  13.204  1.00 99.43           C
ANISOU 4484  C   ARG A 705    13919   7549  16310   1381   2178   1111       C
ATOM   4485  O   ARG A 705      22.911  -1.091  12.158  1.00 98.59           O
ANISOU 4485  O   ARG A 705    13513   7466  16480   1279   2178   1061       O
ATOM   4486  CB  ARG A 705      22.095  -2.563  14.375  1.00101.81           C
ANISOU 4486  CB  ARG A 705    14290   7513  16880   1500   2713   1304       C
ATOM   4487  CG  ARG A 705      21.826  -3.502  15.563  1.00114.65           C
ANISOU 4487  CG  ARG A 705    16143   8940  18480   1628   2995   1435       C
ATOM   4488  CD  ARG A 705      20.352  -3.899  15.709  1.00126.83           C
ANISOU 4488  CD  ARG A 705    17554  10285  20350   1642   3353   1522       C
ATOM   4489  NE  ARG A 705      19.416  -2.770  15.590  1.00137.18           N
ANISOU 4489  NE  ARG A 705    18793  11567  21763   1624   3460   1526       N
ATOM   4490  CZ  ARG A 705      19.059  -1.957  16.585  1.00150.86           C
ANISOU 4490  CZ  ARG A 705    20797  13195  23328   1731   3653   1609       C
ATOM   4491  NH1 ARG A 705      19.563  -2.123  17.802  1.00141.12           N
ANISOU 4491  NH1 ARG A 705    19954  11870  21795   1873   3755   1695       N
ATOM   4492  NH2 ARG A 705      18.201  -0.967  16.367  1.00131.37           N
ANISOU 4492  NH2 ARG A 705    18224  10704  20985   1701   3741   1607       N
ATOM   4493  N   GLU A 706      24.239   0.300  13.353  1.00 94.13           N
ANISOU 4493  N   GLU A 706    13393   6988  15384   1395   1985   1064       N
ATOM   4494  CA  GLU A 706      24.347   1.345  12.336  1.00 92.15           C
ANISOU 4494  CA  GLU A 706    12969   6892  15152   1295   1788    958       C
ATOM   4495  C   GLU A 706      25.777   1.548  11.843  1.00 96.55           C
ANISOU 4495  C   GLU A 706    13532   7604  15547   1254   1473    863       C
ATOM   4496  O   GLU A 706      26.479   2.443  12.315  1.00 96.05           O
ANISOU 4496  O   GLU A 706    13662   7587  15246   1302   1348    850       O
ATOM   4497  CB  GLU A 706      23.740   2.660  12.867  1.00 93.33           C
ANISOU 4497  CB  GLU A 706    13252   7014  15197   1342   1886    991       C
ATOM   4498  CG  GLU A 706      22.222   2.686  12.828  1.00 98.65           C
ANISOU 4498  CG  GLU A 706    13788   7566  16129   1332   2156   1049       C
ATOM   4499  CD  GLU A 706      21.628   2.981  11.463  1.00102.95           C
ANISOU 4499  CD  GLU A 706    13992   8194  16930   1201   2059    960       C
ATOM   4500  OE1 GLU A 706      20.411   2.751  11.282  1.00 81.30           O
ANISOU 4500  OE1 GLU A 706    11084   5339  14466   1181   2249    997       O
ATOM   4501  OE2 GLU A 706      22.369   3.477  10.585  1.00 92.38           O
ANISOU 4501  OE2 GLU A 706    12562   7020  15517   1125   1794    854       O
ATOM   4502  N   TYR A 707      26.209   0.713  10.891  1.00 93.73           N
ANISOU 4502  N   TYR A 707    12962   7315  15335   1166   1349    797       N
ATOM   4503  CA  TYR A 707      27.555   0.792  10.319  1.00 92.70           C
ANISOU 4503  CA  TYR A 707    12801   7314  15108   1119   1075    707       C
ATOM   4504  C   TYR A 707      27.550   1.463   8.918  1.00 91.47           C
ANISOU 4504  C   TYR A 707    12408   7290  15056    999    925    595       C
ATOM   4505  O   TYR A 707      26.474   1.749   8.379  1.00 91.28           O
ANISOU 4505  O   TYR A 707    12237   7254  15190    952   1018    587       O
ATOM   4506  CB  TYR A 707      28.200  -0.612  10.263  1.00 94.86           C
ANISOU 4506  CB  TYR A 707    13037   7558  15448   1116   1047    714       C
ATOM   4507  CG  TYR A 707      28.042  -1.456  11.506  1.00100.10           C
ANISOU 4507  CG  TYR A 707    13909   8075  16049   1230   1223    827       C
ATOM   4508  CD1 TYR A 707      28.607  -1.064  12.717  1.00103.19           C
ANISOU 4508  CD1 TYR A 707    14610   8416  16181   1346   1195    881       C
ATOM   4509  CD2 TYR A 707      27.402  -2.693  11.454  1.00102.24           C
ANISOU 4509  CD2 TYR A 707    14078   8250  16518   1225   1402    877       C
ATOM   4510  CE1 TYR A 707      28.491  -1.859  13.859  1.00106.50           C
ANISOU 4510  CE1 TYR A 707    15255   8689  16521   1462   1355    986       C
ATOM   4511  CE2 TYR A 707      27.289  -3.501  12.585  1.00104.73           C
ANISOU 4511  CE2 TYR A 707    14597   8423  16774   1335   1576    985       C
ATOM   4512  CZ  TYR A 707      27.835  -3.081  13.786  1.00113.87           C
ANISOU 4512  CZ  TYR A 707    16082   9528  17653   1456   1555   1041       C
ATOM   4513  OH  TYR A 707      27.727  -3.894  14.894  1.00116.70           O
ANISOU 4513  OH  TYR A 707    16671   9733  17935   1574   1729   1149       O
ATOM   4514  N   GLY A 708      28.742   1.690   8.349  1.00 83.00           N
ANISOU 4514  N   GLY A 708    11306   6326  13906    956    700    514       N
ATOM   4515  CA  GLY A 708      28.899   2.240   7.006  1.00 79.79           C
ANISOU 4515  CA  GLY A 708    10707   6033  13577    853    560    409       C
ATOM   4516  C   GLY A 708      28.040   1.519   5.981  1.00 81.51           C
ANISOU 4516  C   GLY A 708    10700   6234  14037    773    624    380       C
ATOM   4517  O   GLY A 708      27.307   2.159   5.225  1.00 79.29           O
ANISOU 4517  O   GLY A 708    10298   5985  13843    718    616    335       O
ATOM   4518  N   GLY A 709      28.074   0.182   6.022  1.00 79.10           N
ANISOU 4518  N   GLY A 709    10347   5863  13843    774    686    408       N
ATOM   4519  CA  GLY A 709      27.298  -0.712   5.163  1.00 78.89           C
ANISOU 4519  CA  GLY A 709    10120   5795  14061    707    744    385       C
ATOM   4520  C   GLY A 709      25.791  -0.643   5.336  1.00 84.03           C
ANISOU 4520  C   GLY A 709    10699   6349  14879    715    924    435       C
ATOM   4521  O   GLY A 709      25.052  -1.098   4.450  1.00 85.01           O
ANISOU 4521  O   GLY A 709    10631   6443  15224    649    928    394       O
ATOM   4522  N   ILE A 710      25.324  -0.046   6.466  1.00 78.86           N
ANISOU 4522  N   ILE A 710    10200   5632  14130    798   1070    521       N
ATOM   4523  CA  ILE A 710      23.910   0.105   6.819  1.00 79.00           C
ANISOU 4523  CA  ILE A 710    10169   5534  14312    820   1277    584       C
ATOM   4524  C   ILE A 710      23.367   1.514   6.548  1.00 79.15           C
ANISOU 4524  C   ILE A 710    10166   5603  14306    799   1244    554       C
ATOM   4525  O   ILE A 710      22.287   1.656   5.969  1.00 79.27           O
ANISOU 4525  O   ILE A 710    10006   5570  14542    753   1292    538       O
ATOM   4526  CB  ILE A 710      23.677  -0.391   8.283  1.00 84.27           C
ANISOU 4526  CB  ILE A 710    11035   6063  14922    935   1512    713       C
ATOM   4527  CG1 ILE A 710      23.612  -1.927   8.336  1.00 85.56           C
ANISOU 4527  CG1 ILE A 710    11128   6133  15247    937   1607    749       C
ATOM   4528  CG2 ILE A 710      22.437   0.204   8.948  1.00 86.33           C
ANISOU 4528  CG2 ILE A 710    11330   6204  15267    985   1744    793       C
ATOM   4529  CD1 ILE A 710      24.935  -2.615   8.700  1.00 94.82           C
ANISOU 4529  CD1 ILE A 710    12445   7347  16237    974   1505    753       C
ATOM   4530  N   ALA A 711      24.095   2.547   6.974  1.00 72.30           N
ANISOU 4530  N   ALA A 711     9469   4818  13183    836   1157    546       N
ATOM   4531  CA  ALA A 711      23.638   3.915   6.806  1.00 70.29           C
ANISOU 4531  CA  ALA A 711     9212   4611  12885    823   1134    523       C
ATOM   4532  C   ALA A 711      24.108   4.600   5.502  1.00 70.87           C
ANISOU 4532  C   ALA A 711     9161   4828  12940    733    902    403       C
ATOM   4533  O   ALA A 711      23.274   5.172   4.781  1.00 71.10           O
ANISOU 4533  O   ALA A 711     9053   4863  13098    683    888    366       O
ATOM   4534  CB  ALA A 711      24.010   4.737   8.028  1.00 71.17           C
ANISOU 4534  CB  ALA A 711     9586   4712  12743    919   1190    585       C
ATOM   4535  N   ALA A 712      25.433   4.554   5.220  1.00 63.15           N
ANISOU 4535  N   ALA A 712     8237   3948  11809    719    727    346       N
ATOM   4536  CA  ALA A 712      26.077   5.172   4.059  1.00 60.18           C
ANISOU 4536  CA  ALA A 712     7779   3696  11391    646    527    239       C
ATOM   4537  C   ALA A 712      25.948   4.357   2.759  1.00 64.68           C
ANISOU 4537  C   ALA A 712     8159   4274  12143    563    449    166       C
ATOM   4538  O   ALA A 712      25.578   4.927   1.724  1.00 62.88           O
ANISOU 4538  O   ALA A 712     7827   4089  11974    504    362     96       O
ATOM   4539  CB  ALA A 712      27.540   5.453   4.365  1.00 59.85           C
ANISOU 4539  CB  ALA A 712     7870   3727  11143    672    395    216       C
ATOM   4540  N   LEU A 713      26.256   3.026   2.806  1.00 61.99           N
ANISOU 4540  N   LEU A 713     7788   3885  11881    561    475    182       N
ATOM   4541  CA  LEU A 713      26.192   2.158   1.627  1.00 61.60           C
ANISOU 4541  CA  LEU A 713     7581   3830  11993    488    402    114       C
ATOM   4542  C   LEU A 713      24.902   2.280   0.797  1.00 66.16           C
ANISOU 4542  C   LEU A 713     8001   4361  12775    438    407     78       C
ATOM   4543  O   LEU A 713      25.038   2.508  -0.409  1.00 64.62           O
ANISOU 4543  O   LEU A 713     7734   4217  12600    377    263    -14       O
ATOM   4544  CB  LEU A 713      26.538   0.713   1.969  1.00 62.42           C
ANISOU 4544  CB  LEU A 713     7680   3871  12164    503    461    151       C
ATOM   4545  CG  LEU A 713      26.613  -0.346   0.856  1.00 66.08           C
ANISOU 4545  CG  LEU A 713     8004   4319  12784    435    393     85       C
ATOM   4546  CD1 LEU A 713      27.555   0.070  -0.306  1.00 65.44           C
ANISOU 4546  CD1 LEU A 713     7913   4336  12614    379    215    -18       C
ATOM   4547  CD2 LEU A 713      27.016  -1.659   1.430  1.00 63.84           C
ANISOU 4547  CD2 LEU A 713     7738   3973  12546    463    472    139       C
ATOM   4548  N   PRO A 714      23.673   2.233   1.389  1.00 64.81           N
ANISOU 4548  N   PRO A 714     7783   4086  12758    465    562    147       N
ATOM   4549  CA  PRO A 714      22.450   2.378   0.565  1.00 65.22           C
ANISOU 4549  CA  PRO A 714     7664   4077  13038    416    539    108       C
ATOM   4550  C   PRO A 714      22.351   3.649  -0.307  1.00 68.85           C
ANISOU 4550  C   PRO A 714     8109   4621  13430    379    392     31       C
ATOM   4551  O   PRO A 714      21.767   3.584  -1.395  1.00 67.51           O
ANISOU 4551  O   PRO A 714     7813   4426  13411    324    281    -41       O
ATOM   4552  CB  PRO A 714      21.317   2.294   1.596  1.00 68.33           C
ANISOU 4552  CB  PRO A 714     8037   4338  13587    468    762    212       C
ATOM   4553  CG  PRO A 714      21.950   2.522   2.921  1.00 72.30           C
ANISOU 4553  CG  PRO A 714     8745   4857  13869    550    884    298       C
ATOM   4554  CD  PRO A 714      23.315   1.960   2.801  1.00 67.55           C
ANISOU 4554  CD  PRO A 714     8227   4341  13099    546    770    264       C
ATOM   4555  N   ILE A 715      22.939   4.788   0.147  1.00 64.37           N
ANISOU 4555  N   ILE A 715     7677   4146  12634    410    379     42       N
ATOM   4556  CA  ILE A 715      22.965   6.023  -0.643  1.00 62.88           C
ANISOU 4556  CA  ILE A 715     7489   4043  12360    380    248    -28       C
ATOM   4557  C   ILE A 715      23.906   5.805  -1.843  1.00 66.14           C
ANISOU 4557  C   ILE A 715     7899   4533  12700    328     71   -129       C
ATOM   4558  O   ILE A 715      23.540   6.145  -2.979  1.00 65.94           O
ANISOU 4558  O   ILE A 715     7809   4517  12730    283    -50   -206       O
ATOM   4559  CB  ILE A 715      23.380   7.263   0.204  1.00 65.19           C
ANISOU 4559  CB  ILE A 715     7928   4403  12437    429    288     12       C
ATOM   4560  CG1 ILE A 715      22.426   7.492   1.376  1.00 66.83           C
ANISOU 4560  CG1 ILE A 715     8165   4518  12709    487    484    114       C
ATOM   4561  CG2 ILE A 715      23.508   8.535  -0.655  1.00 63.41           C
ANISOU 4561  CG2 ILE A 715     7704   4270  12120    397    153    -63       C
ATOM   4562  CD1 ILE A 715      23.064   8.106   2.546  1.00 69.66           C
ANISOU 4562  CD1 ILE A 715     8718   4908  12842    557    555    175       C
ATOM   4563  N   TRP A 716      25.116   5.236  -1.570  1.00 61.33           N
ANISOU 4563  N   TRP A 716     7369   3964  11970    341     61   -125       N
ATOM   4564  CA  TRP A 716      26.147   4.945  -2.565  1.00 60.62           C
ANISOU 4564  CA  TRP A 716     7290   3930  11814    301    -68   -206       C
ATOM   4565  C   TRP A 716      25.604   4.018  -3.654  1.00 63.33           C
ANISOU 4565  C   TRP A 716     7521   4209  12333    250   -129   -265       C
ATOM   4566  O   TRP A 716      25.734   4.339  -4.834  1.00 61.56           O
ANISOU 4566  O   TRP A 716     7294   4011  12085    212   -252   -351       O
ATOM   4567  CB  TRP A 716      27.382   4.325  -1.897  1.00 59.65           C
ANISOU 4567  CB  TRP A 716     7248   3828  11589    329    -43   -174       C
ATOM   4568  CG  TRP A 716      28.541   4.118  -2.836  1.00 60.06           C
ANISOU 4568  CG  TRP A 716     7312   3926  11582    294   -150   -250       C
ATOM   4569  CD1 TRP A 716      29.569   4.981  -3.064  1.00 62.23           C
ANISOU 4569  CD1 TRP A 716     7658   4274  11713    295   -220   -288       C
ATOM   4570  CD2 TRP A 716      28.789   2.967  -3.670  1.00 60.41           C
ANISOU 4570  CD2 TRP A 716     7299   3931  11722    255   -183   -294       C
ATOM   4571  NE1 TRP A 716      30.439   4.453  -3.992  1.00 62.04           N
ANISOU 4571  NE1 TRP A 716     7625   4253  11697    260   -279   -349       N
ATOM   4572  CE2 TRP A 716      29.998   3.209  -4.367  1.00 64.48           C
ANISOU 4572  CE2 TRP A 716     7864   4495  12140    236   -259   -354       C
ATOM   4573  CE3 TRP A 716      28.137   1.727  -3.852  1.00 62.29           C
ANISOU 4573  CE3 TRP A 716     7451   4087  12130    236   -147   -287       C
ATOM   4574  CZ2 TRP A 716      30.541   2.283  -5.281  1.00 64.12           C
ANISOU 4574  CZ2 TRP A 716     7797   4419  12147    201   -293   -407       C
ATOM   4575  CZ3 TRP A 716      28.655   0.827  -4.780  1.00 63.86           C
ANISOU 4575  CZ3 TRP A 716     7625   4263  12376    198   -201   -346       C
ATOM   4576  CH2 TRP A 716      29.853   1.099  -5.471  1.00 64.18           C
ANISOU 4576  CH2 TRP A 716     7730   4353  12302    182   -268   -403       C
ATOM   4577  N   ILE A 717      24.993   2.884  -3.265  1.00 61.25           N
ANISOU 4577  N   ILE A 717     7179   3852  12243    254    -44   -221       N
ATOM   4578  CA  ILE A 717      24.405   1.935  -4.219  1.00 62.31           C
ANISOU 4578  CA  ILE A 717     7200   3906  12570    208   -107   -276       C
ATOM   4579  C   ILE A 717      23.394   2.643  -5.104  1.00 68.14           C
ANISOU 4579  C   ILE A 717     7871   4616  13402    179   -214   -337       C
ATOM   4580  O   ILE A 717      23.485   2.554  -6.331  1.00 69.15           O
ANISOU 4580  O   ILE A 717     8000   4743  13530    141   -359   -429       O
ATOM   4581  CB  ILE A 717      23.729   0.745  -3.508  1.00 66.25           C
ANISOU 4581  CB  ILE A 717     7608   4291  13272    224     25   -206       C
ATOM   4582  CG1 ILE A 717      24.748  -0.136  -2.796  1.00 66.78           C
ANISOU 4582  CG1 ILE A 717     7744   4373  13255    251    106   -156       C
ATOM   4583  CG2 ILE A 717      22.891  -0.078  -4.489  1.00 67.99           C
ANISOU 4583  CG2 ILE A 717     7691   4410  13730    176    -56   -267       C
ATOM   4584  CD1 ILE A 717      24.147  -0.861  -1.637  1.00 72.21           C
ANISOU 4584  CD1 ILE A 717     8403   4964  14069    296    288    -53       C
ATOM   4585  N   ASN A 718      22.433   3.335  -4.464  1.00 63.84           N
ANISOU 4585  N   ASN A 718     7281   4038  12937    202   -138   -283       N
ATOM   4586  CA  ASN A 718      21.342   4.038  -5.115  1.00 63.58           C
ANISOU 4586  CA  ASN A 718     7168   3961  13029    181   -226   -325       C
ATOM   4587  C   ASN A 718      21.849   5.077  -6.147  1.00 64.65           C
ANISOU 4587  C   ASN A 718     7394   4191  12981    162   -389   -412       C
ATOM   4588  O   ASN A 718      21.273   5.193  -7.229  1.00 64.89           O
ANISOU 4588  O   ASN A 718     7382   4176  13095    132   -539   -490       O
ATOM   4589  CB  ASN A 718      20.430   4.641  -4.046  1.00 67.30           C
ANISOU 4589  CB  ASN A 718     7594   4383  13594    218    -74   -234       C
ATOM   4590  CG  ASN A 718      19.049   5.049  -4.485  1.00 91.27           C
ANISOU 4590  CG  ASN A 718    10495   7323  16861    200   -126   -254       C
ATOM   4591  OD1 ASN A 718      18.289   4.305  -5.110  1.00 96.17           O
ANISOU 4591  OD1 ASN A 718    10984   7833  17725    170   -206   -296       O
ATOM   4592  ND2 ASN A 718      18.665   6.242  -4.090  1.00 77.95           N
ANISOU 4592  ND2 ASN A 718     8833   5664  15121    223    -77   -220       N
ATOM   4593  N   PHE A 719      22.958   5.774  -5.837  1.00 57.63           N
ANISOU 4593  N   PHE A 719     6634   3418  11847    182   -364   -401       N
ATOM   4594  CA  PHE A 719      23.597   6.742  -6.731  1.00 55.48           C
ANISOU 4594  CA  PHE A 719     6457   3231  11392    170   -483   -475       C
ATOM   4595  C   PHE A 719      24.299   6.045  -7.897  1.00 57.65           C
ANISOU 4595  C   PHE A 719     6776   3500  11629    140   -592   -559       C
ATOM   4596  O   PHE A 719      23.960   6.315  -9.045  1.00 56.21           O
ANISOU 4596  O   PHE A 719     6612   3291  11454    119   -725   -638       O
ATOM   4597  CB  PHE A 719      24.602   7.591  -5.961  1.00 56.00           C
ANISOU 4597  CB  PHE A 719     6632   3402  11246    202   -414   -435       C
ATOM   4598  CG  PHE A 719      25.432   8.480  -6.855  1.00 57.13           C
ANISOU 4598  CG  PHE A 719     6870   3622  11215    191   -512   -507       C
ATOM   4599  CD1 PHE A 719      24.905   9.663  -7.368  1.00 58.89           C
ANISOU 4599  CD1 PHE A 719     7108   3868  11399    189   -579   -540       C
ATOM   4600  CD2 PHE A 719      26.749   8.139  -7.177  1.00 59.79           C
ANISOU 4600  CD2 PHE A 719     7280   3996  11440    187   -527   -537       C
ATOM   4601  CE1 PHE A 719      25.655  10.459  -8.223  1.00 59.50           C
ANISOU 4601  CE1 PHE A 719     7282   4004  11321    184   -653   -604       C
ATOM   4602  CE2 PHE A 719      27.500   8.934  -8.038  1.00 62.22           C
ANISOU 4602  CE2 PHE A 719     7676   4355  11611    180   -591   -601       C
ATOM   4603  CZ  PHE A 719      26.953  10.100  -8.538  1.00 60.60           C
ANISOU 4603  CZ  PHE A 719     7495   4172  11358    181   -649   -632       C
ATOM   4604  N   MET A 720      25.279   5.157  -7.583  1.00 53.23           N
ANISOU 4604  N   MET A 720     6247   2953  11025    142   -532   -540       N
ATOM   4605  CA  MET A 720      26.101   4.397  -8.522  1.00 52.89           C
ANISOU 4605  CA  MET A 720     6254   2899  10943    119   -595   -605       C
ATOM   4606  C   MET A 720      25.298   3.577  -9.525  1.00 62.48           C
ANISOU 4606  C   MET A 720     7416   4011  12312     88   -700   -670       C
ATOM   4607  O   MET A 720      25.657   3.567 -10.706  1.00 64.08           O
ANISOU 4607  O   MET A 720     7704   4201  12444     73   -803   -753       O
ATOM   4608  CB  MET A 720      27.098   3.487  -7.784  1.00 54.27           C
ANISOU 4608  CB  MET A 720     6439   3088  11095    129   -497   -556       C
ATOM   4609  CG  MET A 720      28.189   4.251  -7.055  1.00 55.56           C
ANISOU 4609  CG  MET A 720     6682   3339  11089    159   -443   -518       C
ATOM   4610  SD  MET A 720      29.218   5.311  -8.109  1.00 56.96           S
ANISOU 4610  SD  MET A 720     6970   3579  11091    150   -517   -596       S
ATOM   4611  CE  MET A 720      30.469   4.231  -8.557  1.00 53.54           C
ANISOU 4611  CE  MET A 720     6567   3118  10657    137   -499   -621       C
ATOM   4612  N   GLY A 721      24.242   2.891  -9.057  1.00 58.56           N
ANISOU 4612  N   GLY A 721     6790   3431  12029     84   -670   -633       N
ATOM   4613  CA  GLY A 721      23.362   2.109  -9.917  1.00 58.63           C
ANISOU 4613  CA  GLY A 721     6726   3324  12228     56   -786   -695       C
ATOM   4614  C   GLY A 721      22.764   2.973 -11.013  1.00 64.38           C
ANISOU 4614  C   GLY A 721     7497   4029  12936     48   -958   -777       C
ATOM   4615  O   GLY A 721      22.897   2.661 -12.197  1.00 66.53           O
ANISOU 4615  O   GLY A 721     7848   4256  13176     34  -1097   -867       O
ATOM   4616  N   GLN A 722      22.189   4.116 -10.626  1.00 59.70           N
ANISOU 4616  N   GLN A 722     6878   3467  12337     63   -948   -747       N
ATOM   4617  CA  GLN A 722      21.567   5.073 -11.533  1.00 59.82           C
ANISOU 4617  CA  GLN A 722     6932   3464  12335     62  -1108   -815       C
ATOM   4618  C   GLN A 722      22.558   5.840 -12.407  1.00 65.90           C
ANISOU 4618  C   GLN A 722     7890   4313  12836     70  -1171   -877       C
ATOM   4619  O   GLN A 722      22.289   6.061 -13.600  1.00 64.71           O
ANISOU 4619  O   GLN A 722     7825   4111  12651     68  -1337   -964       O
ATOM   4620  CB  GLN A 722      20.698   6.046 -10.741  1.00 60.64           C
ANISOU 4620  CB  GLN A 722     6943   3575  12524     77  -1051   -753       C
ATOM   4621  CG  GLN A 722      19.380   5.454 -10.299  1.00 69.89           C
ANISOU 4621  CG  GLN A 722     7923   4615  14015     69  -1032   -717       C
ATOM   4622  CD  GLN A 722      18.679   6.358  -9.330  1.00 88.75           C
ANISOU 4622  CD  GLN A 722    10232   7011  16476     90   -913   -635       C
ATOM   4623  OE1 GLN A 722      18.670   6.112  -8.124  1.00 77.90           O
ANISOU 4623  OE1 GLN A 722     8815   5645  15139    110   -717   -540       O
ATOM   4624  NE2 GLN A 722      18.100   7.442  -9.832  1.00 88.55           N
ANISOU 4624  NE2 GLN A 722    10205   6977  16462     91  -1026   -670       N
ATOM   4625  N   ALA A 723      23.686   6.291 -11.799  1.00 64.38           N
ANISOU 4625  N   ALA A 723     7768   4234  12459     85  -1039   -830       N
ATOM   4626  CA  ALA A 723      24.741   7.037 -12.485  1.00 63.86           C
ANISOU 4626  CA  ALA A 723     7866   4238  12161     96  -1056   -875       C
ATOM   4627  C   ALA A 723      25.466   6.147 -13.500  1.00 70.16           C
ANISOU 4627  C   ALA A 723     8769   4987  12903     86  -1102   -943       C
ATOM   4628  O   ALA A 723      25.756   6.593 -14.604  1.00 70.35           O
ANISOU 4628  O   ALA A 723     8938   4994  12796     95  -1183  -1014       O
ATOM   4629  CB  ALA A 723      25.719   7.610 -11.474  1.00 63.41           C
ANISOU 4629  CB  ALA A 723     7826   4290  11977    113   -911   -807       C
ATOM   4630  N   LEU A 724      25.701   4.879 -13.151  1.00 68.63           N
ANISOU 4630  N   LEU A 724     8511   4756  12808     71  -1047   -921       N
ATOM   4631  CA  LEU A 724      26.400   3.946 -14.032  1.00 68.64           C
ANISOU 4631  CA  LEU A 724     8607   4703  12769     61  -1072   -979       C
ATOM   4632  C   LEU A 724      25.498   3.148 -14.988  1.00 73.36           C
ANISOU 4632  C   LEU A 724     9211   5174  13488     46  -1230  -1055       C
ATOM   4633  O   LEU A 724      26.023   2.380 -15.801  1.00 72.71           O
ANISOU 4633  O   LEU A 724     9233   5034  13361     42  -1259  -1111       O
ATOM   4634  CB  LEU A 724      27.351   3.022 -13.242  1.00 67.80           C
ANISOU 4634  CB  LEU A 724     8456   4626  12680     55   -930   -922       C
ATOM   4635  CG  LEU A 724      28.448   3.668 -12.366  1.00 71.29           C
ANISOU 4635  CG  LEU A 724     8914   5172  13001     73   -800   -859       C
ATOM   4636  CD1 LEU A 724      29.349   2.604 -11.802  1.00 71.61           C
ANISOU 4636  CD1 LEU A 724     8925   5211  13072     69   -701   -820       C
ATOM   4637  CD2 LEU A 724      29.322   4.657 -13.142  1.00 71.16           C
ANISOU 4637  CD2 LEU A 724     9041   5191  12804     87   -807   -905       C
ATOM   4638  N   GLN A 725      24.161   3.351 -14.915  1.00 70.75           N
ANISOU 4638  N   GLN A 725     8775   4788  13319     42  -1336  -1061       N
ATOM   4639  CA  GLN A 725      23.144   2.716 -15.775  1.00 72.38           C
ANISOU 4639  CA  GLN A 725     8964   4856  13681     31  -1524  -1137       C
ATOM   4640  C   GLN A 725      23.429   2.989 -17.257  1.00 78.65           C
ANISOU 4640  C   GLN A 725     9984   5596  14302     48  -1677  -1243       C
ATOM   4641  O   GLN A 725      23.638   4.134 -17.640  1.00 77.95           O
ANISOU 4641  O   GLN A 725    10014   5555  14050     71  -1703  -1261       O
ATOM   4642  CB  GLN A 725      21.738   3.246 -15.419  1.00 74.24           C
ANISOU 4642  CB  GLN A 725     9046   5046  14115     29  -1605  -1118       C
ATOM   4643  CG  GLN A 725      20.571   2.562 -16.128  1.00 98.38           C
ANISOU 4643  CG  GLN A 725    12032   7941  17406     17  -1808  -1188       C
ATOM   4644  CD  GLN A 725      20.226   1.231 -15.512  1.00131.73           C
ANISOU 4644  CD  GLN A 725    16081  12093  21878     -8  -1739  -1149       C
ATOM   4645  OE1 GLN A 725      19.708   0.324 -16.180  1.00132.79           O
ANISOU 4645  OE1 GLN A 725    16182  12093  22179    -21  -1887  -1214       O
ATOM   4646  NE2 GLN A 725      20.450   1.091 -14.212  1.00126.00           N
ANISOU 4646  NE2 GLN A 725    15241  11442  21191     -9  -1518  -1043       N
ATOM   4647  N   GLY A 726      23.437   1.932 -18.067  1.00 78.38           N
ANISOU 4647  N   GLY A 726    10022   5456  14304     41  -1770  -1311       N
ATOM   4648  CA  GLY A 726      23.685   2.015 -19.504  1.00 79.48           C
ANISOU 4648  CA  GLY A 726    10410   5514  14275     66  -1914  -1414       C
ATOM   4649  C   GLY A 726      25.050   2.572 -19.855  1.00 83.10           C
ANISOU 4649  C   GLY A 726    11067   6046  14461     90  -1776  -1412       C
ATOM   4650  O   GLY A 726      25.167   3.511 -20.658  1.00 83.37           O
ANISOU 4650  O   GLY A 726    11289   6070  14317    124  -1840  -1460       O
ATOM   4651  N   THR A 727      26.079   2.055 -19.164  1.00 78.03           N
ANISOU 4651  N   THR A 727    10370   5476  13802     75  -1576  -1350       N
ATOM   4652  CA  THR A 727      27.490   2.403 -19.344  1.00 76.23           C
ANISOU 4652  CA  THR A 727    10284   5304  13376     92  -1415  -1337       C
ATOM   4653  C   THR A 727      28.255   1.089 -19.313  1.00 79.63           C
ANISOU 4653  C   THR A 727    10709   5696  13852     74  -1317  -1330       C
ATOM   4654  O   THR A 727      27.924   0.213 -18.503  1.00 78.67           O
ANISOU 4654  O   THR A 727    10404   5579  13908     46  -1293  -1286       O
ATOM   4655  CB  THR A 727      28.025   3.436 -18.321  1.00 75.74           C
ANISOU 4655  CB  THR A 727    10132   5381  13263     95  -1270  -1254       C
ATOM   4656  OG1 THR A 727      28.298   2.826 -17.059  1.00 74.78           O
ANISOU 4656  OG1 THR A 727     9823   5324  13267     71  -1147  -1170       O
ATOM   4657  CG2 THR A 727      27.136   4.639 -18.165  1.00 71.25           C
ANISOU 4657  CG2 THR A 727     9530   4853  12687    106  -1359  -1250       C
ATOM   4658  N   PRO A 728      29.248   0.902 -20.207  1.00 76.36           N
ANISOU 4658  N   PRO A 728    10497   5228  13288     94  -1251  -1372       N
ATOM   4659  CA  PRO A 728      29.967  -0.372 -20.218  1.00 75.95           C
ANISOU 4659  CA  PRO A 728    10439   5129  13289     77  -1156  -1367       C
ATOM   4660  C   PRO A 728      30.834  -0.541 -18.987  1.00 79.49           C
ANISOU 4660  C   PRO A 728    10719   5681  13803     57   -972  -1270       C
ATOM   4661  O   PRO A 728      31.191   0.449 -18.346  1.00 77.96           O
ANISOU 4661  O   PRO A 728    10476   5585  13560     66   -899  -1219       O
ATOM   4662  CB  PRO A 728      30.799  -0.298 -21.501  1.00 78.15           C
ANISOU 4662  CB  PRO A 728    10998   5315  13381    111  -1115  -1432       C
ATOM   4663  CG  PRO A 728      31.027   1.148 -21.722  1.00 83.16           C
ANISOU 4663  CG  PRO A 728    11736   5999  13862    144  -1087  -1431       C
ATOM   4664  CD  PRO A 728      29.774   1.831 -21.231  1.00 78.47           C
ANISOU 4664  CD  PRO A 728    11010   5464  13339    136  -1239  -1421       C
ATOM   4665  N   ALA A 729      31.146  -1.802 -18.646  1.00 77.60           N
ANISOU 4665  N   ALA A 729    10394   5413  13677     34   -909  -1248       N
ATOM   4666  CA  ALA A 729      32.021  -2.139 -17.530  1.00 76.70           C
ANISOU 4666  CA  ALA A 729    10138   5375  13629     21   -751  -1160       C
ATOM   4667  C   ALA A 729      33.365  -1.447 -17.753  1.00 80.98           C
ANISOU 4667  C   ALA A 729    10785   5940  14044     42   -617  -1150       C
ATOM   4668  O   ALA A 729      33.891  -1.460 -18.872  1.00 82.25           O
ANISOU 4668  O   ALA A 729    11134   6016  14103     59   -588  -1208       O
ATOM   4669  CB  ALA A 729      32.209  -3.642 -17.442  1.00 77.65           C
ANISOU 4669  CB  ALA A 729    10198   5434  13872     -2   -714  -1154       C
ATOM   4670  N   ALA A 730      33.863  -0.764 -16.713  1.00 75.64           N
ANISOU 4670  N   ALA A 730     9999   5366  13377     45   -539  -1078       N
ATOM   4671  CA  ALA A 730      35.126  -0.029 -16.735  1.00 74.20           C
ANISOU 4671  CA  ALA A 730     9869   5204  13119     63   -417  -1060       C
ATOM   4672  C   ALA A 730      35.860  -0.352 -15.460  1.00 78.27           C
ANISOU 4672  C   ALA A 730    10224   5779  13735     55   -333   -977       C
ATOM   4673  O   ALA A 730      35.348  -0.094 -14.368  1.00 80.48           O
ANISOU 4673  O   ALA A 730    10382   6141  14056     54   -370   -923       O
ATOM   4674  CB  ALA A 730      34.864   1.459 -16.822  1.00 73.64           C
ANISOU 4674  CB  ALA A 730     9852   5191  12938     84   -454  -1069       C
ATOM   4675  N   TRP A 731      37.032  -0.951 -15.588  1.00 71.16           N
ANISOU 4675  N   TRP A 731     9332   4825  12879     53   -223   -967       N
ATOM   4676  CA  TRP A 731      37.822  -1.333 -14.432  1.00 69.81           C
ANISOU 4676  CA  TRP A 731     9020   4691  12812     51   -160   -893       C
ATOM   4677  C   TRP A 731      39.250  -0.818 -14.579  1.00 79.44           C
ANISOU 4677  C   TRP A 731    10267   5878  14039     65    -49   -886       C
ATOM   4678  O   TRP A 731      39.631  -0.371 -15.663  1.00 80.37           O
ANISOU 4678  O   TRP A 731    10520   5929  14088     76      9   -937       O
ATOM   4679  CB  TRP A 731      37.764  -2.865 -14.263  1.00 67.17           C
ANISOU 4679  CB  TRP A 731     8622   4308  12590     30   -146   -878       C
ATOM   4680  CG  TRP A 731      38.354  -3.381 -12.983  1.00 66.25           C
ANISOU 4680  CG  TRP A 731     8367   4226  12579     33   -108   -799       C
ATOM   4681  CD1 TRP A 731      39.480  -4.137 -12.856  1.00 69.08           C
ANISOU 4681  CD1 TRP A 731     8688   4529  13030     30    -24   -775       C
ATOM   4682  CD2 TRP A 731      37.912  -3.088 -11.641  1.00 65.15           C
ANISOU 4682  CD2 TRP A 731     8125   4173  12456     46   -154   -732       C
ATOM   4683  NE1 TRP A 731      39.750  -4.370 -11.523  1.00 68.17           N
ANISOU 4683  NE1 TRP A 731     8456   4461  12986     42    -34   -700       N
ATOM   4684  CE2 TRP A 731      38.797  -3.746 -10.756  1.00 68.79           C
ANISOU 4684  CE2 TRP A 731     8504   4623  13008     55   -109   -672       C
ATOM   4685  CE3 TRP A 731      36.857  -2.325 -11.100  1.00 65.46           C
ANISOU 4685  CE3 TRP A 731     8144   4286  12442     56   -224   -715       C
ATOM   4686  CZ2 TRP A 731      38.636  -3.704  -9.360  1.00 67.36           C
ANISOU 4686  CZ2 TRP A 731     8249   4500  12846     79   -138   -598       C
ATOM   4687  CZ3 TRP A 731      36.696  -2.287  -9.719  1.00 66.29           C
ANISOU 4687  CZ3 TRP A 731     8169   4446  12574     78   -230   -639       C
ATOM   4688  CH2 TRP A 731      37.583  -2.962  -8.866  1.00 67.15           C
ANISOU 4688  CH2 TRP A 731     8223   4541  12752     92   -190   -582       C
ATOM   4689  N   VAL A 732      40.026  -0.865 -13.489  1.00 79.61           N
ANISOU 4689  N   VAL A 732    10166   5931  14151     71    -22   -823       N
ATOM   4690  CA  VAL A 732      41.420  -0.438 -13.417  1.00 82.79           C
ANISOU 4690  CA  VAL A 732    10545   6291  14619     83     67   -808       C
ATOM   4691  C   VAL A 732      42.300  -1.130 -14.457  1.00 96.09           C
ANISOU 4691  C   VAL A 732    12299   7846  16365     78    195   -839       C
ATOM   4692  O   VAL A 732      42.053  -2.289 -14.819  1.00 98.07           O
ANISOU 4692  O   VAL A 732    12566   8048  16648     61    210   -851       O
ATOM   4693  CB  VAL A 732      41.968  -0.533 -11.973  1.00 86.81           C
ANISOU 4693  CB  VAL A 732    10911   6846  15228     93     29   -736       C
ATOM   4694  CG1 VAL A 732      40.994   0.097 -10.999  1.00 86.21           C
ANISOU 4694  CG1 VAL A 732    10802   6882  15070    106    -78   -705       C
ATOM   4695  CG2 VAL A 732      42.224  -1.969 -11.557  1.00 87.45           C
ANISOU 4695  CG2 VAL A 732    10920   6888  15421     82     45   -702       C
ATOM   4696  N   ARG A 733      43.233  -0.360 -15.019  1.00 97.12           N
ANISOU 4696  N   ARG A 733    12484   7913  16504     94    295   -858       N
ATOM   4697  CA  ARG A 733      44.115  -0.847 -16.064  1.00 99.24           C
ANISOU 4697  CA  ARG A 733    12841   8039  16829     97    452   -885       C
ATOM   4698  C   ARG A 733      45.498  -1.142 -15.513  1.00105.36           C
ANISOU 4698  C   ARG A 733    13480   8744  17808     98    541   -840       C
ATOM   4699  O   ARG A 733      46.202  -0.226 -15.093  1.00105.57           O
ANISOU 4699  O   ARG A 733    13442   8767  17902    113    560   -822       O
ATOM   4700  CB  ARG A 733      44.135   0.136 -17.267  1.00101.06           C
ANISOU 4700  CB  ARG A 733    13257   8210  16932    122    532   -940       C
ATOM   4701  CG  ARG A 733      42.815   0.184 -18.068  1.00114.03           C
ANISOU 4701  CG  ARG A 733    15062   9881  18382    124    437   -997       C
ATOM   4702  CD  ARG A 733      42.453  -1.153 -18.738  1.00127.89           C
ANISOU 4702  CD  ARG A 733    16910  11559  20124    112    440  -1031       C
ATOM   4703  NE  ARG A 733      41.041  -1.520 -18.551  1.00130.52           N
ANISOU 4703  NE  ARG A 733    17237  11969  20385     95    264  -1051       N
ATOM   4704  CZ  ARG A 733      40.587  -2.769 -18.455  1.00134.17           C
ANISOU 4704  CZ  ARG A 733    17653  12419  20908     72    213  -1051       C
ATOM   4705  NH1 ARG A 733      41.428  -3.796 -18.509  1.00105.20           N
ANISOU 4705  NH1 ARG A 733    13945   8674  17354     61    321  -1032       N
ATOM   4706  NH2 ARG A 733      39.290  -2.999 -18.292  1.00122.71           N
ANISOU 4706  NH2 ARG A 733    16183  11022  19419     59     58  -1070       N
ATOM   4707  N   LEU A 734      45.864  -2.427 -15.452  1.00103.67           N
ANISOU 4707  N   LEU A 734    13212   8470  17709     82    581   -821       N
ATOM   4708  CA  LEU A 734      47.190  -2.826 -14.991  1.00104.57           C
ANISOU 4708  CA  LEU A 734    13193   8496  18042     83    660   -778       C
ATOM   4709  C   LEU A 734      48.151  -2.567 -16.153  1.00110.14           C
ANISOU 4709  C   LEU A 734    13992   9042  18813     96    865   -807       C
ATOM   4710  O   LEU A 734      48.208  -3.356 -17.105  1.00111.40           O
ANISOU 4710  O   LEU A 734    14270   9103  18953     92    980   -836       O
ATOM   4711  CB  LEU A 734      47.211  -4.308 -14.558  1.00104.79           C
ANISOU 4711  CB  LEU A 734    13138   8510  18167     64    640   -747       C
ATOM   4712  CG  LEU A 734      48.526  -4.873 -13.987  1.00109.90           C
ANISOU 4712  CG  LEU A 734    13634   9064  19059     65    695   -699       C
ATOM   4713  CD1 LEU A 734      49.036  -4.064 -12.790  1.00109.92           C
ANISOU 4713  CD1 LEU A 734    13499   9115  19151     84    583   -658       C
ATOM   4714  CD2 LEU A 734      48.361  -6.323 -13.598  1.00112.55           C
ANISOU 4714  CD2 LEU A 734    13909   9397  19458     48    668   -670       C
ATOM   4715  N   GLU A 735      48.840  -1.419 -16.103  1.00105.74           N
ANISOU 4715  N   GLU A 735    13399   8450  18326    116    916   -802       N
ATOM   4716  CA  GLU A 735      49.765  -0.975 -17.141  1.00132.19           C
ANISOU 4716  CA  GLU A 735    16834  11636  21755    136   1133   -823       C
ATOM   4717  C   GLU A 735      51.181  -0.907 -16.578  1.00154.19           C
ANISOU 4717  C   GLU A 735    19428  14315  24840    140   1203   -780       C
ATOM   4718  O   GLU A 735      51.570  -1.774 -15.794  1.00112.07           O
ANISOU 4718  O   GLU A 735    13943   8978  19660    124   1137   -741       O
ATOM   4719  CB  GLU A 735      49.316   0.389 -17.721  1.00133.36           C
ANISOU 4719  CB  GLU A 735    17125  11814  21732    160   1152   -861       C
ATOM   4720  CG  GLU A 735      48.066   0.313 -18.598  1.00142.83           C
ANISOU 4720  CG  GLU A 735    18542  13068  22658    164   1103   -913       C
ATOM   4721  CD  GLU A 735      47.326   1.612 -18.889  1.00154.75           C
ANISOU 4721  CD  GLU A 735    20167  14653  23978    185   1046   -944       C
ATOM   4722  OE1 GLU A 735      47.271   2.011 -20.076  1.00137.47           O
ANISOU 4722  OE1 GLU A 735    18189  12368  21675    216   1173   -985       O
ATOM   4723  OE2 GLU A 735      46.749   2.196 -17.943  1.00143.27           O
ANISOU 4723  OE2 GLU A 735    18608  13348  22478    175    875   -928       O
TER    4724      GLU A 735



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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.