CNRS Nantes University US2B US2B
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***    ***

elNémo ID: 23020803493855475

Job options:

ID        	=	 23020803493855475
JOBID     	=	 
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:


CRYST1  222.120   52.170  109.900  90.00 111.58  90.00 C 1 2 1       8
ATOM      1  N   ALA A   2     -24.308  34.601  12.229  1.00 89.07      A    N  
ANISOU    1  N   ALA A   2    10024   9120  14700   3618   6316   6527  A    N  
ATOM      2  CA  ALA A   2     -23.197  34.350  11.317  1.00 87.80      A    C  
ANISOU    2  CA  ALA A   2     9930   8928  14502   3483   6241   6448  A    C  
ATOM      3  C   ALA A   2     -21.847  34.651  11.987  1.00 88.46      A    C  
ANISOU    3  C   ALA A   2    10320   8308  14981   3225   6383   6040  A    C  
ATOM      4  O   ALA A   2     -21.604  35.771  12.445  1.00 90.79      A    O  
ANISOU    4  O   ALA A   2    10772   8079  15645   3369   6809   6097  A    O  
ATOM      5  CB  ALA A   2     -23.357  35.185  10.051  1.00 92.53      A    C  
ANISOU    5  CB  ALA A   2    10412   9719  15026   3909   6537   6999  A    C  
ATOM      6  N   ASP A   3     -20.974  33.641  12.032  1.00 79.28      A    N  
ANISOU    6  N   ASP A   3     9234   7158  13731   2844   6040   5621  A    N  
ATOM      7  CA  ASP A   3     -19.634  33.716  12.616  1.00 75.69      A    C  
ANISOU    7  CA  ASP A   3     9020   6164  13574   2568   6094   5187  A    C  
ATOM      8  C   ASP A   3     -18.705  34.515  11.698  1.00 80.20      A    C  
ANISOU    8  C   ASP A   3     9669   6478  14326   2687   6415   5350  A    C  
ATOM      9  O   ASP A   3     -18.595  34.145  10.525  1.00 80.62      A    O  
ANISOU    9  O   ASP A   3     9610   6887  14134   2752   6295   5554  A    O  
ATOM     10  CB  ASP A   3     -19.095  32.285  12.821  1.00 72.81      A    C  
ANISOU   10  CB  ASP A   3     8685   5988  12992   2185   5614   4751  A    C  
ATOM     11  CG  ASP A   3     -17.914  32.139  13.757  1.00 69.96      A    C  
ANISOU   11  CG  ASP A   3     8535   5175  12873   1890   5583   4244  A    C  
ATOM     12  OD1 ASP A   3     -17.049  33.039  13.765  1.00 67.63      A    O  
ANISOU   12  OD1 ASP A   3     8355   4458  12885   1909   5902   4188  A    O  
ATOM     13  OD2 ASP A   3     -17.823  31.088  14.437  1.00 71.17      A    O1-
ANISOU   13  OD2 ASP A   3     8732   5421  12887   1638   5245   3898  A    O1-
ATOM     14  N   PRO A   4     -17.997  35.576  12.181  1.00 76.50      A    N  
ANISOU   14  N   PRO A   4     9389   5404  14272   2689   6829   5240  A    N  
ATOM     15  CA  PRO A   4     -17.109  36.323  11.267  1.00 77.43      A    C  
ANISOU   15  CA  PRO A   4     9588   5269  14563   2784   7166   5394  A    C  
ATOM     16  C   PRO A   4     -15.811  35.575  10.917  1.00 76.04      A    C  
ANISOU   16  C   PRO A   4     9468   5083  14341   2456   6919   5021  A    C  
ATOM     17  O   PRO A   4     -15.104  35.992   9.993  1.00 75.01      A    O  
ANISOU   17  O   PRO A   4     9373   4847  14280   2516   7129   5156  A    O  
ATOM     18  CB  PRO A   4     -16.806  37.606  12.040  1.00 81.50      A    C  
ANISOU   18  CB  PRO A   4    10293   5136  15537   2831   7697   5327  A    C  
ATOM     19  CG  PRO A   4     -16.918  37.226  13.469  1.00 83.55      A    C  
ANISOU   19  CG  PRO A   4    10604   5263  15878   2579   7510   4887  A    C  
ATOM     20  CD  PRO A   4     -18.017  36.190  13.531  1.00 77.81      A    C  
ANISOU   20  CD  PRO A   4     9697   5106  14764   2609   7048   4982  A    C  
ATOM     21  N   SER A   5     -15.508  34.466  11.650  1.00 67.34      A    N  
ANISOU   21  N   SER A   5     8377   4095  13113   2131   6489   4566  A    N  
ATOM     22  CA  SER A   5     -14.305  33.648  11.450  1.00 64.17      A    C  
ANISOU   22  CA  SER A   5     8027   3711  12645   1835   6226   4189  A    C  
ATOM     23  C   SER A   5     -14.525  32.538  10.421  1.00 65.43      A    C  
ANISOU   23  C   SER A   5     8052   4415  12391   1825   5844   4320  A    C  
ATOM     24  O   SER A   5     -13.563  31.921   9.986  1.00 62.85      A    O  
ANISOU   24  O   SER A   5     7759   4135  11988   1641   5668   4099  A    O  
ATOM     25  CB  SER A   5     -13.856  33.027  12.768  1.00 63.80      A    C  
ANISOU   25  CB  SER A   5     8072   3511  12659   1534   5992   3656  A    C  
ATOM     26  OG  SER A   5     -13.991  33.932  13.849  1.00 69.22      A    O  
ANISOU   26  OG  SER A   5     8845   3799  13658   1545   6294   3540  A    O  
ATOM     27  N   SER A   6     -15.784  32.305  10.027  1.00 62.17      A    N  
ANISOU   27  N   SER A   6     7480   4432  11712   2019   5735   4668  A    N  
ATOM     28  CA  SER A   6     -16.203  31.271   9.087  1.00 60.66      A    C  
ANISOU   28  CA  SER A   6     7130   4818  11099   1999   5392   4791  A    C  
ATOM     29  C   SER A   6     -16.814  31.897   7.816  1.00 69.67      A    C  
ANISOU   29  C   SER A   6     8100   6284  12088   2349   5592   5346  A    C  
ATOM     30  O   SER A   6     -17.228  33.056   7.834  1.00 72.54      A    O  
ANISOU   30  O   SER A   6     8457   6464  12639   2650   5971   5681  A    O  
ATOM     31  CB  SER A   6     -17.206  30.344   9.784  1.00 60.43      A    C  
ANISOU   31  CB  SER A   6     7027   5099  10837   1881   5065   4665  A    C  
ATOM     32  OG  SER A   6     -17.900  29.464   8.917  1.00 61.56      A    O  
ANISOU   32  OG  SER A   6     6985   5841  10564   1870   4789   4810  A    O  
ATOM     33  N   PHE A   7     -16.864  31.127   6.717  1.00 67.78      A    N  
ANISOU   33  N   PHE A   7     7722   6536  11495   2322   5351   5444  A    N  
ATOM     34  CA  PHE A   7     -17.484  31.508   5.434  1.00 71.34      A    C  
ANISOU   34  CA  PHE A   7     7966   7442  11699   2645   5465   5955  A    C  
ATOM     35  C   PHE A   7     -18.884  30.929   5.363  1.00 77.78      A    C  
ANISOU   35  C   PHE A   7     8534   8875  12142   2715   5227   6119  A    C  
ATOM     36  O   PHE A   7     -19.698  31.357   4.550  1.00 81.80      A    O  
ANISOU   36  O   PHE A   7     8828   9811  12441   3044   5343   6576  A    O  
ATOM     37  CB  PHE A   7     -16.673  30.976   4.239  1.00 72.97      A    C  
ANISOU   37  CB  PHE A   7     8142   7878  11704   2550   5334   5934  A    C  
ATOM     38  CG  PHE A   7     -15.408  31.710   3.879  1.00 75.56      A    C  
ANISOU   38  CG  PHE A   7     8640   7740  12328   2573   5633   5925  A    C  
ATOM     39  CD1 PHE A   7     -15.456  32.897   3.158  1.00 83.02      A    C  
ANISOU   39  CD1 PHE A   7     9570   8581  13391   2936   6060   6389  A    C  
ATOM     40  CD2 PHE A   7     -14.165  31.171   4.180  1.00 75.30      A    C  
ANISOU   40  CD2 PHE A   7     8772   7413  12425   2243   5494   5465  A    C  
ATOM     41  CE1 PHE A   7     -14.279  33.558   2.785  1.00 84.84      A    C  
ANISOU   41  CE1 PHE A   7     9963   8378  13894   2929   6363   6369  A    C  
ATOM     42  CE2 PHE A   7     -12.991  31.827   3.805  1.00 78.93      A    C  
ANISOU   42  CE2 PHE A   7     9361   7488  13139   2240   5770   5437  A    C  
ATOM     43  CZ  PHE A   7     -13.055  33.022   3.118  1.00 80.98      A    C  
ANISOU   43  CZ  PHE A   7     9618   7614  13538   2564   6210   5878  A    C  
ATOM     44  N   ALA A   8     -19.140  29.907   6.187  1.00 72.17      A    N  
ANISOU   44  N   ALA A   8     7847   8245  11328   2400   4895   5736  A    N  
ATOM     45  CA  ALA A   8     -20.398  29.181   6.239  1.00 72.83      A    C  
ANISOU   45  CA  ALA A   8     7713   8899  11061   2360   4641   5776  A    C  
ATOM     46  C   ALA A   8     -21.493  29.995   6.926  1.00 78.25      A    C  
ANISOU   46  C   ALA A   8     8309   9572  11851   2628   4840   6035  A    C  
ATOM     47  O   ALA A   8     -21.198  30.841   7.780  1.00 76.86      A    O  
ANISOU   47  O   ALA A   8     8314   8828  12060   2713   5104   6006  A    O  
ATOM     48  CB  ALA A   8     -20.194  27.865   6.963  1.00 70.19      A    C  
ANISOU   48  CB  ALA A   8     7494   8538  10636   1928   4287   5266  A    C  
ATOM     49  N   SER A   9     -22.751  29.758   6.527  1.00 77.47      A    N  
ANISOU   49  N   SER A   9     7916  10122  11398   2758   4727   6279  A    N  
ATOM     50  CA  SER A   9     -23.896  30.445   7.106  1.00 80.12      A    C  
ANISOU   50  CA  SER A   9     8121  10550  11772   3032   4892   6545  A    C  
ATOM     51  C   SER A   9     -24.717  29.450   7.949  1.00 82.32      A    C  
ANISOU   51  C   SER A   9     8330  11075  11874   2735   4587   6236  A    C  
ATOM     52  O   SER A   9     -25.414  28.596   7.385  1.00 82.64      A    O  
ANISOU   52  O   SER A   9     8127  11771  11503   2609   4329   6221  A    O  
ATOM     53  CB  SER A   9     -24.745  31.101   6.020  1.00 89.44      A    C  
ANISOU   53  CB  SER A   9     8988  12315  12682   3480   5050   7116  A    C  
ATOM     54  OG  SER A   9     -24.017  32.117   5.348  1.00103.62      A    O  
ANISOU   54  OG  SER A   9    10885  13809  14678   3793   5399   7437  A    O  
ATOM     55  N   PRO A  10     -24.623  29.517   9.300  1.00 76.72      A    N  
ANISOU   55  N   PRO A  10     7831   9856  11462   2598   4623   5967  A    N  
ATOM     56  CA  PRO A  10     -25.393  28.575  10.138  1.00 75.03      A    C  
ANISOU   56  CA  PRO A  10     7573   9847  11088   2320   4361   5683  A    C  
ATOM     57  C   PRO A  10     -26.899  28.854  10.123  1.00 83.31      A    C  
ANISOU   57  C   PRO A  10     8304  11437  11912   2559   4400   6001  A    C  
ATOM     58  O   PRO A  10     -27.674  27.984  10.509  1.00 82.14      A    O  
ANISOU   58  O   PRO A  10     8036  11650  11524   2323   4167   5812  A    O  
ATOM     59  CB  PRO A  10     -24.819  28.776  11.538  1.00 73.81      A    C  
ANISOU   59  CB  PRO A  10     7726   8992  11328   2186   4444   5370  A    C  
ATOM     60  CG  PRO A  10     -23.674  29.706  11.403  1.00 78.32      A    C  
ANISOU   60  CG  PRO A  10     8495   9017  12247   2323   4717   5419  A    C  
ATOM     61  CD  PRO A  10     -23.830  30.450  10.125  1.00 77.25      A    C  
ANISOU   61  CD  PRO A  10     8178   9165  12009   2678   4918   5895  A    C  
ATOM     62  N   GLU A  11     -27.305  30.060   9.674  1.00 84.59      A    N  
ANISOU   62  N   GLU A  11     8332  11660  12148   3033   4714   6486  A    N  
ATOM     63  CA  GLU A  11     -28.703  30.504   9.555  1.00 88.51      A    C  
ANISOU   63  CA  GLU A  11     8498  12701  12429   3364   4801   6869  A    C  
ATOM     64  C   GLU A  11     -29.360  29.939   8.279  1.00 93.67      A    C  
ANISOU   64  C   GLU A  11     8771  14259  12559   3403   4598   7062  A    C  
ATOM     65  O   GLU A  11     -30.589  29.914   8.183  1.00 95.79      A    O  
ANISOU   65  O   GLU A  11     8706  15155  12534   3547   4549   7256  A    O  
ATOM     66  CB  GLU A  11     -28.784  32.045   9.571  1.00 93.12      A    C  
ANISOU   66  CB  GLU A  11     9121  12957  13304   3894   5261   7332  A    C  
ATOM     67  CG  GLU A  11     -27.910  32.735   8.533  1.00109.60      A    C  
ANISOU   67  CG  GLU A  11    11283  14880  15479   4146   5495   7617  A    C  
ATOM     68  CD  GLU A  11     -27.446  34.142   8.865  1.00142.70      A    C  
ANISOU   68  CD  GLU A  11    15711  18383  20125   4495   5994   7869  A    C  
ATOM     69  OE1 GLU A  11     -26.272  34.453   8.558  1.00139.14      A    O  
ANISOU   69  OE1 GLU A  11    15493  17466  19909   4449   6150   7810  A    O  
ATOM     70  OE2 GLU A  11     -28.251  34.942   9.398  1.00143.87      A    O1-
ANISOU   70  OE2 GLU A  11    15812  18457  20395   4811   6252   8122  A    O1-
ATOM     71  N   LYS A  12     -28.539  29.498   7.306  1.00 88.17      A    N  
ANISOU   71  N   LYS A  12     8108  13659  11735   3272   4487   6997  A    N  
ATOM     72  CA  LYS A  12     -29.019  28.944   6.039  1.00 89.78      A    C  
ANISOU   72  CA  LYS A  12     7962  14714  11435   3276   4298   7138  A    C  
ATOM     73  C   LYS A  12     -29.141  27.427   6.137  1.00 89.41      A    C  
ANISOU   73  C   LYS A  12     7880  14983  11111   2715   3913   6640  A    C  
ATOM     74  O   LYS A  12     -30.143  26.874   5.697  1.00 90.62      A    O  
ANISOU   74  O   LYS A  12     7680  15913  10839   2644   3745   6663  A    O  
ATOM     75  CB  LYS A  12     -28.101  29.347   4.870  1.00 93.14      A    C  
ANISOU   75  CB  LYS A  12     8435  15097  11857   3458   4415   7359  A    C  
ATOM     76  CG  LYS A  12     -28.295  30.789   4.421  1.00114.88      A    C  
ANISOU   76  CG  LYS A  12    11104  17830  14715   4079   4810   7966  A    C  
ATOM     77  CD  LYS A  12     -27.390  31.160   3.250  1.00126.13      A    C  
ANISOU   77  CD  LYS A  12    12574  19236  16112   4252   4937   8193  A    C  
ATOM     78  CE  LYS A  12     -27.684  32.549   2.734  1.00141.43      A    C  
ANISOU   78  CE  LYS A  12    14426  21198  18114   4899   5360   8836  A    C  
ATOM     79  NZ  LYS A  12     -26.881  32.869   1.527  1.00153.15      A    N1+
ANISOU   79  NZ  LYS A  12    15938  22723  19530   5079   5492   9084  A    N1+
ATOM     80  N   PHE A  13     -28.125  26.764   6.736  1.00 81.54      A    N  
ANISOU   80  N   PHE A  13     7248  13385  10349   2321   3797   6187  A    N  
ATOM     81  CA  PHE A  13     -28.084  25.310   6.910  1.00 78.96      A    C  
ANISOU   81  CA  PHE A  13     6978  13207   9815   1789   3486   5698  A    C  
ATOM     82  C   PHE A  13     -27.182  24.892   8.080  1.00 74.76      A    C  
ANISOU   82  C   PHE A  13     6879  11882   9644   1495   3446   5275  A    C  
ATOM     83  O   PHE A  13     -26.459  25.719   8.643  1.00 70.85      A    O  
ANISOU   83  O   PHE A  13     6623  10752   9546   1672   3640   5330  A    O  
ATOM     84  CB  PHE A  13     -27.654  24.589   5.614  1.00 82.09      A    C  
ANISOU   84  CB  PHE A  13     7265  14045   9880   1617   3324   5625  A    C  
ATOM     85  CG  PHE A  13     -26.286  24.929   5.073  1.00 83.39      A    C  
ANISOU   85  CG  PHE A  13     7665  13761  10260   1700   3416   5659  A    C  
ATOM     86  CD1 PHE A  13     -25.208  24.075   5.277  1.00 83.95      A    C  
ANISOU   86  CD1 PHE A  13     8052  13394  10453   1336   3282   5235  A    C  
ATOM     87  CD2 PHE A  13     -26.087  26.068   4.299  1.00 88.70      A    C  
ANISOU   87  CD2 PHE A  13     8233  14483  10988   2151   3652   6124  A    C  
ATOM     88  CE1 PHE A  13     -23.944  24.377   4.751  1.00 84.13      A    C  
ANISOU   88  CE1 PHE A  13     8264  13043  10658   1406   3366   5255  A    C  
ATOM     89  CE2 PHE A  13     -24.820  26.374   3.784  1.00 90.79      A    C  
ANISOU   89  CE2 PHE A  13     8711  14336  11450   2203   3755   6141  A    C  
ATOM     90  CZ  PHE A  13     -23.760  25.525   4.014  1.00 85.17      A    C  
ANISOU   90  CZ  PHE A  13     8290  13211  10859   1821   3602   5697  A    C  
ATOM     91  N   ASN A  14     -27.261  23.597   8.444  1.00 69.31      A    N  
ANISOU   91  N   ASN A  14     6279  11261   8796   1046   3212   4851  A    N  
ATOM     92  CA  ASN A  14     -26.510  22.969   9.532  1.00 65.46      A    C  
ANISOU   92  CA  ASN A  14     6178  10135   8560    754   3141   4437  A    C  
ATOM     93  C   ASN A  14     -26.095  21.535   9.191  1.00 66.33      A    C  
ANISOU   93  C   ASN A  14     6410  10351   8441    318   2918   4045  A    C  
ATOM     94  O   ASN A  14     -26.875  20.778   8.606  1.00 66.28      A    O  
ANISOU   94  O   ASN A  14     6181  10942   8062    112   2793   3978  A    O  
ATOM     95  CB  ASN A  14     -27.342  22.941  10.836  1.00 68.15      A    C  
ANISOU   95  CB  ASN A  14     6555  10334   9003    701   3159   4338  A    C  
ATOM     96  CG  ASN A  14     -27.518  24.246  11.589  1.00 96.84      A    C  
ANISOU   96  CG  ASN A  14    10199  13633  12962   1071   3401   4608  A    C  
ATOM     97  ND2 ASN A  14     -28.549  24.301  12.415  1.00 89.85      A    N  
ANISOU   97  ND2 ASN A  14     9202  12885  12051   1092   3425   4637  A    N  
ATOM     98  OD1 ASN A  14     -26.705  25.174  11.518  1.00 96.48      A    O  
ANISOU   98  OD1 ASN A  14    10285  13164  13209   1311   3585   4754  A    O  
ATOM     99  N   ILE A  15     -24.860  21.166   9.580  1.00 60.34      A    N  
ANISOU   99  N   ILE A  15     6006   9017   7905    179   2888   3773  A    N  
ATOM    100  CA  ILE A  15     -24.341  19.796   9.472  1.00 57.28      A    C  
ANISOU  100  CA  ILE A  15     5819   8583   7363   -210   2716   3383  A    C  
ATOM    101  C   ILE A  15     -24.784  19.110  10.756  1.00 60.12      A    C  
ANISOU  101  C   ILE A  15     6358   8720   7763   -439   2666   3107  A    C  
ATOM    102  O   ILE A  15     -24.496  19.603  11.854  1.00 56.86      A    O  
ANISOU  102  O   ILE A  15     6124   7828   7650   -319   2743   3084  A    O  
ATOM    103  CB  ILE A  15     -22.804  19.673   9.207  1.00 56.45      A    C  
ANISOU  103  CB  ILE A  15     5987   8023   7439   -219   2710   3239  A    C  
ATOM    104  CG1 ILE A  15     -22.389  20.379   7.893  1.00 57.38      A    C  
ANISOU  104  CG1 ILE A  15     5922   8374   7507      8   2780   3528  A    C  
ATOM    105  CG2 ILE A  15     -22.380  18.182   9.189  1.00 53.70      A    C  
ANISOU  105  CG2 ILE A  15     5867   7612   6924   -601   2556   2836  A    C  
ATOM    106  CD1 ILE A  15     -20.896  20.775   7.819  1.00 57.14      A    C  
ANISOU  106  CD1 ILE A  15     6123   7823   7766    115   2854   3483  A    C  
ATOM    107  N   LYS A  16     -25.514  17.999  10.609  1.00 58.73      A    N  
ANISOU  107  N   LYS A  16     6126   8912   7278   -775   2557   2896  A    N  
ATOM    108  CA  LYS A  16     -26.074  17.265  11.726  1.00 58.05      A    C  
ANISOU  108  CA  LYS A  16     6197   8675   7185  -1016   2533   2647  A    C  
ATOM    109  C   LYS A  16     -25.284  15.983  12.047  1.00 59.84      A    C  
ANISOU  109  C   LYS A  16     6804   8536   7397  -1329   2465   2258  A    C  
ATOM    110  O   LYS A  16     -25.313  15.504  13.190  1.00 59.45      A    O  
ANISOU  110  O   LYS A  16     7007   8130   7452  -1442   2477   2063  A    O  
ATOM    111  CB  LYS A  16     -27.549  16.944  11.429  1.00 63.71      A    C  
ANISOU  111  CB  LYS A  16     6581  10053   7572  -1183   2507   2678  A    C  
ATOM    112  CG  LYS A  16     -28.453  18.190  11.387  1.00 78.18      A    C  
ANISOU  112  CG  LYS A  16     8052  12229   9424   -830   2592   3073  A    C  
ATOM    113  CD  LYS A  16     -28.781  18.717  12.792  1.00 85.70      A    C  
ANISOU  113  CD  LYS A  16     9122  12786  10654   -688   2683   3111  A    C  
ATOM    114  CE  LYS A  16     -29.129  20.182  12.777  1.00 95.97      A    C  
ANISOU  114  CE  LYS A  16    10192  14159  12113   -234   2825   3529  A    C  
ATOM    115  NZ  LYS A  16     -29.312  20.706  14.153  1.00101.75      A    N1+
ANISOU  115  NZ  LYS A  16    11065  14461  13132   -108   2929   3535  A    N1+
ATOM    116  N   HIS A  17     -24.592  15.428  11.053  1.00 53.92      A    N  
ANISOU  116  N   HIS A  17     6100   7878   6509  -1449   2411   2158  A    N  
ATOM    117  CA  HIS A  17     -23.806  14.204  11.205  1.00 51.01      A    C  
ANISOU  117  CA  HIS A  17     6090   7184   6107  -1713   2373   1814  A    C  
ATOM    118  C   HIS A  17     -22.729  14.132  10.140  1.00 56.56      A    C  
ANISOU  118  C   HIS A  17     6835   7865   6791  -1665   2339   1812  A    C  
ATOM    119  O   HIS A  17     -22.921  14.615   9.024  1.00 58.36      A    O  
ANISOU  119  O   HIS A  17     6771   8518   6886  -1569   2328   2016  A    O  
ATOM    120  CB  HIS A  17     -24.706  12.960  11.118  1.00 51.70      A    C  
ANISOU  120  CB  HIS A  17     6183   7577   5885  -2133   2364   1555  A    C  
ATOM    121  CG  HIS A  17     -24.018  11.654  11.410  1.00 53.03      A    C  
ANISOU  121  CG  HIS A  17     6766   7354   6027  -2396   2381   1208  A    C  
ATOM    122  CD2 HIS A  17     -23.633  10.669  10.568  1.00 54.95      A    C  
ANISOU  122  CD2 HIS A  17     7125   7680   6075  -2652   2381    991  A    C  
ATOM    123  ND1 HIS A  17     -23.734  11.258  12.708  1.00 52.24      A    N  
ANISOU  123  ND1 HIS A  17     7013   6732   6103  -2393   2426   1067  A    N  
ATOM    124  CE1 HIS A  17     -23.157  10.071  12.613  1.00 50.77      A    C  
ANISOU  124  CE1 HIS A  17     7150   6310   5828  -2613   2460    797  A    C  
ATOM    125  NE2 HIS A  17     -23.098   9.661  11.353  1.00 53.11      A    N  
ANISOU  125  NE2 HIS A  17     7329   6941   5908  -2789   2442    729  A    N  
ATOM    126  N   MET A  18     -21.614  13.487  10.487  1.00 51.62      A    N  
ANISOU  126  N   MET A  18     6568   6767   6277  -1720   2329   1585  A    N  
ATOM    127  CA  MET A  18     -20.497  13.241   9.609  1.00 50.57      A    C  
ANISOU  127  CA  MET A  18     6530   6552   6132  -1701   2301   1528  A    C  
ATOM    128  C   MET A  18     -20.054  11.800   9.689  1.00 51.56      A    C  
ANISOU  128  C   MET A  18     6989   6471   6133  -1984   2297   1184  A    C  
ATOM    129  O   MET A  18     -19.856  11.273  10.779  1.00 48.83      A    O  
ANISOU  129  O   MET A  18     6940   5722   5890  -2018   2325   1019  A    O  
ATOM    130  CB  MET A  18     -19.309  14.148   9.975  1.00 51.64      A    C  
ANISOU  130  CB  MET A  18     6766   6256   6598  -1378   2323   1638  A    C  
ATOM    131  CG  MET A  18     -19.427  15.573   9.499  1.00 56.68      A    C  
ANISOU  131  CG  MET A  18     7107   7066   7362  -1087   2378   1986  A    C  
ATOM    132  SD  MET A  18     -17.816  16.393   9.625  1.00 60.05      A    S  
ANISOU  132  SD  MET A  18     7674   7012   8129   -815   2433   2025  A    S  
ATOM    133  CE  MET A  18     -18.284  18.054   9.276  1.00 57.94      A    C  
ANISOU  133  CE  MET A  18     7093   6901   8019   -498   2570   2441  A    C  
ATOM    134  N   HIS A  19     -19.889  11.166   8.535  1.00 50.37      A    N  
ANISOU  134  N   HIS A  19     6796   6590   5751  -2171   2281   1083  A    N  
ATOM    135  CA  HIS A  19     -19.284   9.844   8.426  1.00 50.21      A    C  
ANISOU  135  CA  HIS A  19     7111   6344   5625  -2408   2313    769  A    C  
ATOM    136  C   HIS A  19     -17.907  10.107   7.791  1.00 51.84      A    C  
ANISOU  136  C   HIS A  19     7387   6371   5938  -2211   2282    805  A    C  
ATOM    137  O   HIS A  19     -17.855  10.638   6.686  1.00 51.85      A    O  
ANISOU  137  O   HIS A  19     7128   6727   5847  -2160   2248    953  A    O  
ATOM    138  CB  HIS A  19     -20.150   8.842   7.637  1.00 53.23      A    C  
ANISOU  138  CB  HIS A  19     7413   7156   5658  -2819   2351    569  A    C  
ATOM    139  CG  HIS A  19     -19.538   7.476   7.577  1.00 56.88      A    C  
ANISOU  139  CG  HIS A  19     8261   7320   6030  -3061   2436    241  A    C  
ATOM    140  CD2 HIS A  19     -19.741   6.404   8.373  1.00 59.40      A    C  
ANISOU  140  CD2 HIS A  19     8926   7319   6325  -3277   2553     -6  A    C  
ATOM    141  ND1 HIS A  19     -18.566   7.159   6.647  1.00 59.00      A    N  
ANISOU  141  ND1 HIS A  19     8605   7571   6241  -3060   2429    166  A    N  
ATOM    142  CE1 HIS A  19     -18.223   5.906   6.892  1.00 58.89      A    C  
ANISOU  142  CE1 HIS A  19     8976   7231   6167  -3269   2546   -125  A    C  
ATOM    143  NE2 HIS A  19     -18.909   5.407   7.917  1.00 59.68      A    N  
ANISOU  143  NE2 HIS A  19     9259   7132   6285  -3402   2633   -231  A    N  
ATOM    144  N   LEU A  20     -16.809   9.833   8.523  1.00 46.17      A    N  
ANISOU  144  N   LEU A  20     6995   5135   5414  -2072   2294    693  A    N  
ATOM    145  CA  LEU A  20     -15.455  10.137   8.061  1.00 43.88      A    C  
ANISOU  145  CA  LEU A  20     6764   4660   5250  -1869   2269    716  A    C  
ATOM    146  C   LEU A  20     -14.615   8.910   7.718  1.00 48.20      A    C  
ANISOU  146  C   LEU A  20     7616   5017   5680  -2002   2303    455  A    C  
ATOM    147  O   LEU A  20     -14.276   8.122   8.592  1.00 47.57      A    O  
ANISOU  147  O   LEU A  20     7867   4575   5633  -2017   2352    278  A    O  
ATOM    148  CB  LEU A  20     -14.695  10.968   9.109  1.00 41.57      A    C  
ANISOU  148  CB  LEU A  20     6550   3972   5272  -1560   2258    794  A    C  
ATOM    149  CG  LEU A  20     -15.245  12.342   9.494  1.00 46.54      A    C  
ANISOU  149  CG  LEU A  20     6918   4678   6087  -1367   2261   1053  A    C  
ATOM    150  CD1 LEU A  20     -14.524  12.879  10.718  1.00 45.74      A    C  
ANISOU  150  CD1 LEU A  20     6958   4154   6266  -1144   2272   1024  A    C  
ATOM    151  CD2 LEU A  20     -15.084  13.341   8.385  1.00 48.57      A    C  
ANISOU  151  CD2 LEU A  20     6881   5202   6372  -1232   2270   1295  A    C  
ATOM    152  N   LYS A  21     -14.226   8.791   6.444  1.00 45.55      A    N  
ANISOU  152  N   LYS A  21     7175   4920   5211  -2064   2291    449  A    N  
ATOM    153  CA  LYS A  21     -13.316   7.760   5.962  1.00 45.16      A    C  
ANISOU  153  CA  LYS A  21     7390   4702   5065  -2152   2335    225  A    C  
ATOM    154  C   LYS A  21     -11.961   8.451   5.749  1.00 47.62      A    C  
ANISOU  154  C   LYS A  21     7686   4836   5572  -1851   2290    318  A    C  
ATOM    155  O   LYS A  21     -11.770   9.122   4.736  1.00 48.20      A    O  
ANISOU  155  O   LYS A  21     7511   5181   5620  -1797   2257    462  A    O  
ATOM    156  CB  LYS A  21     -13.869   7.099   4.688  1.00 50.27      A    C  
ANISOU  156  CB  LYS A  21     7925   5770   5403  -2471   2367    114  A    C  
ATOM    157  CG  LYS A  21     -14.934   6.041   4.976  1.00 68.99      A    C  
ANISOU  157  CG  LYS A  21    10440   8199   7574  -2834   2466   -111  A    C  
ATOM    158  CD  LYS A  21     -15.993   5.887   3.881  1.00 83.40      A    C  
ANISOU  158  CD  LYS A  21    11964  10632   9092  -3157   2469   -154  A    C  
ATOM    159  CE  LYS A  21     -16.976   7.022   3.750  1.00 96.82      A    C  
ANISOU  159  CE  LYS A  21    13226  12797  10765  -3076   2374    121  A    C  
ATOM    160  NZ  LYS A  21     -18.020   6.719   2.741  1.00109.80      A    N1+
ANISOU  160  NZ  LYS A  21    14568  15090  12059  -3393   2377     47  A    N1+
ATOM    161  N   LEU A  22     -11.061   8.377   6.753  1.00 41.19      A    N  
ANISOU  161  N   LEU A  22     7106   3595   4948  -1643   2293    249  A    N  
ATOM    162  CA  LEU A  22      -9.768   9.052   6.696  1.00 38.66      A    C  
ANISOU  162  CA  LEU A  22     6753   3115   4820  -1371   2257    302  A    C  
ATOM    163  C   LEU A  22      -8.625   8.096   6.346  1.00 41.74      A    C  
ANISOU  163  C   LEU A  22     7398   3324   5139  -1346   2289    104  A    C  
ATOM    164  O   LEU A  22      -8.429   7.091   7.033  1.00 41.40      A    O  
ANISOU  164  O   LEU A  22     7671   3018   5040  -1360   2343    -69  A    O  
ATOM    165  CB  LEU A  22      -9.429   9.777   8.010  1.00 36.80      A    C  
ANISOU  165  CB  LEU A  22     6540   2603   4839  -1133   2235    351  A    C  
ATOM    166  CG  LEU A  22     -10.504  10.610   8.702  1.00 40.95      A    C  
ANISOU  166  CG  LEU A  22     6889   3206   5464  -1126   2228    515  A    C  
ATOM    167  CD1 LEU A  22     -10.054  10.988  10.107  1.00 39.44      A    C  
ANISOU  167  CD1 LEU A  22     6812   2698   5475   -933   2221    470  A    C  
ATOM    168  CD2 LEU A  22     -10.833  11.864   7.918  1.00 40.94      A    C  
ANISOU  168  CD2 LEU A  22     6543   3464   5549  -1055   2230    768  A    C  
ATOM    169  N   HIS A  23      -7.865   8.429   5.274  1.00 36.55      A    N  
ANISOU  169  N   HIS A  23     6605   2804   4478  -1291   2273    146  A    N  
ATOM    170  CA  HIS A  23      -6.699   7.675   4.838  1.00 35.95      A    C  
ANISOU  170  CA  HIS A  23     6723   2589   4347  -1235   2302    -19  A    C  
ATOM    171  C   HIS A  23      -5.464   8.460   5.265  1.00 36.36      A    C  
ANISOU  171  C   HIS A  23     6714   2472   4631   -939   2263     18  A    C  
ATOM    172  O   HIS A  23      -5.206   9.542   4.725  1.00 32.93      A    O  
ANISOU  172  O   HIS A  23     6015   2185   4314   -865   2242    173  A    O  
ATOM    173  CB  HIS A  23      -6.742   7.423   3.318  1.00 39.43      A    C  
ANISOU  173  CB  HIS A  23     7051   3339   4591  -1415   2323    -29  A    C  
ATOM    174  CG  HIS A  23      -5.559   6.659   2.799  1.00 44.36      A    C  
ANISOU  174  CG  HIS A  23     7866   3832   5156  -1358   2366   -196  A    C  
ATOM    175  CD2 HIS A  23      -4.339   7.104   2.415  1.00 45.14      A    C  
ANISOU  175  CD2 HIS A  23     7888   3901   5360  -1163   2344   -172  A    C  
ATOM    176  ND1 HIS A  23      -5.582   5.265   2.687  1.00 48.07      A    N  
ANISOU  176  ND1 HIS A  23     8653   4167   5444  -1512   2467   -422  A    N  
ATOM    177  CE1 HIS A  23      -4.385   4.922   2.230  1.00 47.10      A    C  
ANISOU  177  CE1 HIS A  23     8631   3947   5318  -1381   2494   -512  A    C  
ATOM    178  NE2 HIS A  23      -3.603   5.990   2.054  1.00 45.99      A    N  
ANISOU  178  NE2 HIS A  23     8250   3881   5343  -1175   2412   -372  A    N  
ATOM    179  N   VAL A  24      -4.742   7.951   6.280  1.00 33.46      A    N  
ANISOU  179  N   VAL A  24     6583   1810   4322   -768   2268   -121  A    N  
ATOM    180  CA  VAL A  24      -3.539   8.602   6.838  1.00 32.46      A    C  
ANISOU  180  CA  VAL A  24     6393   1553   4388   -497   2231   -141  A    C  
ATOM    181  C   VAL A  24      -2.301   8.060   6.132  1.00 37.39      A    C  
ANISOU  181  C   VAL A  24     7102   2162   4943   -405   2250   -264  A    C  
ATOM    182  O   VAL A  24      -2.019   6.870   6.250  1.00 36.58      A    O  
ANISOU  182  O   VAL A  24     7285   1920   4692   -385   2300   -407  A    O  
ATOM    183  CB  VAL A  24      -3.450   8.400   8.386  1.00 35.19      A    C  
ANISOU  183  CB  VAL A  24     6904   1663   4804   -332   2215   -218  A    C  
ATOM    184  CG1 VAL A  24      -2.158   9.002   8.953  1.00 34.02      A    C  
ANISOU  184  CG1 VAL A  24     6666   1446   4813    -69   2176   -287  A    C  
ATOM    185  CG2 VAL A  24      -4.670   8.978   9.093  1.00 33.99      A    C  
ANISOU  185  CG2 VAL A  24     6658   1527   4729   -421   2202    -98  A    C  
ATOM    186  N   ASP A  25      -1.562   8.924   5.400  1.00 34.98      A    N  
ANISOU  186  N   ASP A  25     6561   1985   4747   -343   2236   -203  A    N  
ATOM    187  CA  ASP A  25      -0.357   8.518   4.661  1.00 34.62      A    C  
ANISOU  187  CA  ASP A  25     6553   1955   4644   -254   2256   -313  A    C  
ATOM    188  C   ASP A  25       0.878   9.297   5.138  1.00 35.45      A    C  
ANISOU  188  C   ASP A  25     6512   2014   4942    -27   2231   -363  A    C  
ATOM    189  O   ASP A  25       1.027  10.469   4.808  1.00 32.66      A    O  
ANISOU  189  O   ASP A  25     5899   1757   4755    -37   2243   -256  A    O  
ATOM    190  CB  ASP A  25      -0.573   8.702   3.148  1.00 37.90      A    C  
ANISOU  190  CB  ASP A  25     6821   2614   4965   -427   2284   -221  A    C  
ATOM    191  CG  ASP A  25       0.427   7.951   2.290  1.00 56.69      A    C  
ANISOU  191  CG  ASP A  25     9304   5009   7226   -386   2320   -357  A    C  
ATOM    192  OD1 ASP A  25       1.590   8.419   2.181  1.00 56.07      A    O  
ANISOU  192  OD1 ASP A  25     9111   4927   7265   -220   2315   -388  A    O  
ATOM    193  OD2 ASP A  25       0.047   6.890   1.720  1.00 68.27      A    O1-
ANISOU  193  OD2 ASP A  25    10965   6493   8481   -533   2370   -449  A    O1-
ATOM    194  N   PHE A  26       1.772   8.635   5.899  1.00 33.74      A    N  
ANISOU  194  N   PHE A  26     6461   1667   4690    181   2218   -530  A    N  
ATOM    195  CA  PHE A  26       2.976   9.275   6.446  1.00 33.28      A    C  
ANISOU  195  CA  PHE A  26     6249   1621   4775    393   2190   -627  A    C  
ATOM    196  C   PHE A  26       4.018   9.613   5.386  1.00 37.40      A    C  
ANISOU  196  C   PHE A  26     6606   2277   5326    410   2219   -662  A    C  
ATOM    197  O   PHE A  26       4.752  10.576   5.583  1.00 39.66      A    O  
ANISOU  197  O   PHE A  26     6665   2621   5784    480   2223   -705  A    O  
ATOM    198  CB  PHE A  26       3.617   8.412   7.540  1.00 35.25      A    C  
ANISOU  198  CB  PHE A  26     6704   1762   4927    644   2164   -781  A    C  
ATOM    199  CG  PHE A  26       2.882   8.494   8.857  1.00 35.05      A    C  
ANISOU  199  CG  PHE A  26     6752   1627   4937    682   2131   -761  A    C  
ATOM    200  CD1 PHE A  26       3.242   9.435   9.816  1.00 35.38      A    C  
ANISOU  200  CD1 PHE A  26     6594   1710   5139    787   2086   -812  A    C  
ATOM    201  CD2 PHE A  26       1.841   7.619   9.145  1.00 36.37      A    C  
ANISOU  201  CD2 PHE A  26     7188   1656   4973    595   2163   -709  A    C  
ATOM    202  CE1 PHE A  26       2.561   9.510  11.035  1.00 35.28      A    C  
ANISOU  202  CE1 PHE A  26     6648   1609   5148    823   2059   -799  A    C  
ATOM    203  CE2 PHE A  26       1.157   7.705  10.357  1.00 37.44      A    C  
ANISOU  203  CE2 PHE A  26     7391   1695   5139    629   2142   -685  A    C  
ATOM    204  CZ  PHE A  26       1.516   8.657  11.289  1.00 34.17      A    C  
ANISOU  204  CZ  PHE A  26     6762   1353   4869    742   2080   -711  A    C  
ATOM    205  N   THR A  27       4.082   8.851   4.270  1.00 31.79      A    N  
ANISOU  205  N   THR A  27     6005   1620   4453    327   2256   -659  A    N  
ATOM    206  CA  THR A  27       5.015   9.113   3.183  1.00 31.35      A    C  
ANISOU  206  CA  THR A  27     5804   1701   4408    332   2291   -683  A    C  
ATOM    207  C   THR A  27       4.616  10.425   2.474  1.00 34.02      A    C  
ANISOU  207  C   THR A  27     5861   2162   4903    177   2328   -502  A    C  
ATOM    208  O   THR A  27       5.466  11.275   2.218  1.00 32.74      A    O  
ANISOU  208  O   THR A  27     5491   2062   4887    224   2369   -517  A    O  
ATOM    209  CB  THR A  27       5.093   7.905   2.232  1.00 42.72      A    C  
ANISOU  209  CB  THR A  27     7457   3158   5618    279   2334   -739  A    C  
ATOM    210  CG2 THR A  27       6.072   8.119   1.084  1.00 40.90      A    C  
ANISOU  210  CG2 THR A  27     7085   3076   5381    293   2373   -771  A    C  
ATOM    211  OG1 THR A  27       5.508   6.761   2.980  1.00 44.60      A    O  
ANISOU  211  OG1 THR A  27     7977   3237   5731    464   2343   -883  A    O  
ATOM    212  N   SER A  28       3.320  10.607   2.223  1.00 31.51      A    N  
ANISOU  212  N   SER A  28     5537   1883   4552      5   2331   -329  A    N  
ATOM    213  CA  SER A  28       2.779  11.800   1.585  1.00 31.24      A    C  
ANISOU  213  CA  SER A  28     5261   1972   4636   -100   2385   -109  A    C  
ATOM    214  C   SER A  28       2.510  12.952   2.568  1.00 31.91      A    C  
ANISOU  214  C   SER A  28     5205   1951   4969    -52   2410    -36  A    C  
ATOM    215  O   SER A  28       2.356  14.098   2.118  1.00 27.66      A    O  
ANISOU  215  O   SER A  28     4465   1465   4581    -84   2503    139  A    O  
ATOM    216  CB  SER A  28       1.474  11.448   0.891  1.00 35.92      A    C  
ANISOU  216  CB  SER A  28     5885   2718   5047   -284   2378     43  A    C  
ATOM    217  OG  SER A  28       1.713  10.718  -0.301  1.00 48.84      A    O  
ANISOU  217  OG  SER A  28     7579   4506   6473   -370   2392     -3  A    O  
ATOM    218  N   ARG A  29       2.445  12.648   3.910  1.00 29.56      A    N  
ANISOU  218  N   ARG A  29     5026   1498   4708     33   2348   -163  A    N  
ATOM    219  CA  ARG A  29       2.064  13.619   4.954  1.00 28.41      A    C  
ANISOU  219  CA  ARG A  29     4776   1247   4772     62   2370   -124  A    C  
ATOM    220  C   ARG A  29       0.689  14.138   4.551  1.00 34.62      A    C  
ANISOU  220  C   ARG A  29     5489   2099   5567    -67   2409    136  A    C  
ATOM    221  O   ARG A  29       0.494  15.342   4.331  1.00 34.32      A    O  
ANISOU  221  O   ARG A  29     5261   2066   5712    -77   2514    296  A    O  
ATOM    222  CB  ARG A  29       3.090  14.765   5.130  1.00 27.70      A    C  
ANISOU  222  CB  ARG A  29     4475   1127   4924    127   2460   -199  A    C  
ATOM    223  CG  ARG A  29       4.360  14.313   5.820  1.00 34.34      A    C  
ANISOU  223  CG  ARG A  29     5346   1955   5748    274   2404   -479  A    C  
ATOM    224  CD  ARG A  29       5.350  15.444   6.098  1.00 29.23      A    C  
ANISOU  224  CD  ARG A  29     4464   1311   5331    292   2504   -605  A    C  
ATOM    225  NE  ARG A  29       6.484  14.887   6.845  1.00 36.01      A    N  
ANISOU  225  NE  ARG A  29     5329   2234   6118    451   2425   -885  A    N  
ATOM    226  CZ  ARG A  29       7.276  15.556   7.675  1.00 45.74      A    C  
ANISOU  226  CZ  ARG A  29     6387   3502   7490    492   2460  -1093  A    C  
ATOM    227  NH1 ARG A  29       7.096  16.854   7.874  1.00 35.24      A    N1+
ANISOU  227  NH1 ARG A  29     4884   2095   6412    364   2601  -1070  A    N1+
ATOM    228  NH2 ARG A  29       8.262  14.933   8.304  1.00 36.37      A    N  
ANISOU  228  NH2 ARG A  29     5193   2445   6180    666   2370  -1333  A    N  
ATOM    229  N   ALA A  30      -0.246  13.199   4.346  1.00 30.48      A    N  
ANISOU  229  N   ALA A  30     5112   1643   4827   -168   2346    178  A    N  
ATOM    230  CA  ALA A  30      -1.562  13.588   3.883  1.00 30.31      A    C  
ANISOU  230  CA  ALA A  30     4991   1767   4758   -289   2370    414  A    C  
ATOM    231  C   ALA A  30      -2.675  12.868   4.579  1.00 34.59      A    C  
ANISOU  231  C   ALA A  30     5683   2286   5174   -376   2306    396  A    C  
ATOM    232  O   ALA A  30      -2.509  11.732   5.042  1.00 34.65      A    O  
ANISOU  232  O   ALA A  30     5926   2189   5052   -385   2256    211  A    O  
ATOM    233  CB  ALA A  30      -1.668  13.317   2.389  1.00 32.01      A    C  
ANISOU  233  CB  ALA A  30     5142   2232   4787   -390   2388    514  A    C  
ATOM    234  N   ILE A  31      -3.836  13.519   4.624  1.00 29.57      A    N  
ANISOU  234  N   ILE A  31     4914   1751   4569   -434   2330    599  A    N  
ATOM    235  CA  ILE A  31      -5.034  12.850   5.089  1.00 28.68      A    C  
ANISOU  235  CA  ILE A  31     4906   1681   4312   -558   2283    598  A    C  
ATOM    236  C   ILE A  31      -6.056  13.021   3.987  1.00 34.83      A    C  
ANISOU  236  C   ILE A  31     5508   2801   4926   -693   2299    801  A    C  
ATOM    237  O   ILE A  31      -6.529  14.134   3.737  1.00 35.40      A    O  
ANISOU  237  O   ILE A  31     5355   2994   5101   -628   2356   1044  A    O  
ATOM    238  CB  ILE A  31      -5.580  13.245   6.481  1.00 30.90      A    C  
ANISOU  238  CB  ILE A  31     5214   1782   4745   -497   2278    604  A    C  
ATOM    239  CG1 ILE A  31      -4.481  13.155   7.572  1.00 30.65      A    C  
ANISOU  239  CG1 ILE A  31     5314   1478   4853   -340   2258    397  A    C  
ATOM    240  CG2 ILE A  31      -6.805  12.341   6.831  1.00 30.78      A    C  
ANISOU  240  CG2 ILE A  31     5329   1829   4539   -660   2239    579  A    C  
ATOM    241  CD1 ILE A  31      -4.960  13.549   9.034  1.00 34.27      A    C  
ANISOU  241  CD1 ILE A  31     5797   1769   5455   -273   2254    378  A    C  
ATOM    242  N   ALA A  32      -6.338  11.925   3.281  1.00 32.55      A    N  
ANISOU  242  N   ALA A  32     5316   2683   4369   -871   2268    699  A    N  
ATOM    243  CA  ALA A  32      -7.318  11.911   2.209  1.00 34.26      A    C  
ANISOU  243  CA  ALA A  32     5352   3303   4363  -1028   2270    841  A    C  
ATOM    244  C   ALA A  32      -8.629  11.527   2.840  1.00 39.13      A    C  
ANISOU  244  C   ALA A  32     5992   3999   4876  -1175   2246    833  A    C  
ATOM    245  O   ALA A  32      -8.744  10.452   3.438  1.00 40.43      A    O  
ANISOU  245  O   ALA A  32     6409   3999   4955  -1301   2236    611  A    O  
ATOM    246  CB  ALA A  32      -6.899  10.944   1.108  1.00 36.20      A    C  
ANISOU  246  CB  ALA A  32     5676   3710   4367  -1176   2266    691  A    C  
ATOM    247  N   ALA A  33      -9.582  12.458   2.839  1.00 35.78      A    N  
ANISOU  247  N   ALA A  33     5322   3788   4485  -1130   2258   1081  A    N  
ATOM    248  CA  ALA A  33     -10.858  12.227   3.517  1.00 35.55      A    C  
ANISOU  248  CA  ALA A  33     5279   3851   4376  -1253   2240   1087  A    C  
ATOM    249  C   ALA A  33     -12.028  12.155   2.569  1.00 45.64      A    C  
ANISOU  249  C   ALA A  33     6310   5659   5370  -1420   2228   1205  A    C  
ATOM    250  O   ALA A  33     -12.179  12.988   1.670  1.00 45.99      A    O  
ANISOU  250  O   ALA A  33     6085   6019   5370  -1310   2248   1454  A    O  
ATOM    251  CB  ALA A  33     -11.114  13.308   4.552  1.00 34.06      A    C  
ANISOU  251  CB  ALA A  33     5015   3470   4457  -1057   2269   1253  A    C  
ATOM    252  N   SER A  34     -12.871  11.143   2.807  1.00 45.76      A    N  
ANISOU  252  N   SER A  34     6418   5787   5181  -1686   2211   1019  A    N  
ATOM    253  CA  SER A  34     -14.128  10.902   2.125  1.00 48.57      A    C  
ANISOU  253  CA  SER A  34     6539   6681   5235  -1905   2198   1055  A    C  
ATOM    254  C   SER A  34     -15.195  11.213   3.155  1.00 50.59      A    C  
ANISOU  254  C   SER A  34     6733   6933   5555  -1905   2198   1131  A    C  
ATOM    255  O   SER A  34     -15.513  10.357   3.983  1.00 51.43      A    O  
ANISOU  255  O   SER A  34     7066   6835   5639  -2091   2215    907  A    O  
ATOM    256  CB  SER A  34     -14.189   9.462   1.617  1.00 56.02      A    C  
ANISOU  256  CB  SER A  34     7653   7728   5902  -2255   2216    726  A    C  
ATOM    257  OG  SER A  34     -15.249   9.276   0.693  1.00 72.67      A    O  
ANISOU  257  OG  SER A  34     9481  10450   7681  -2490   2203    731  A    O  
ATOM    258  N   THR A  35     -15.646  12.481   3.205  1.00 45.32      A    N  
ANISOU  258  N   THR A  35     5796   6421   5004  -1663   2205   1457  A    N  
ATOM    259  CA  THR A  35     -16.611  12.922   4.211  1.00 45.17      A    C  
ANISOU  259  CA  THR A  35     5704   6381   5078  -1613   2216   1561  A    C  
ATOM    260  C   THR A  35     -18.053  12.901   3.673  1.00 53.33      A    C  
ANISOU  260  C   THR A  35     6415   8042   5808  -1764   2197   1657  A    C  
ATOM    261  O   THR A  35     -18.323  13.445   2.605  1.00 54.81      A    O  
ANISOU  261  O   THR A  35     6297   8702   5828  -1675   2192   1876  A    O  
ATOM    262  CB  THR A  35     -16.247  14.312   4.744  1.00 51.33      A    C  
ANISOU  262  CB  THR A  35     6406   6913   6185  -1255   2272   1840  A    C  
ATOM    263  CG2 THR A  35     -14.793  14.442   5.086  1.00 42.98      A    C  
ANISOU  263  CG2 THR A  35     5590   5344   5396  -1114   2293   1741  A    C  
ATOM    264  OG1 THR A  35     -16.575  15.272   3.759  1.00 61.95      A    O  
ANISOU  264  OG1 THR A  35     7427   8661   7450  -1080   2310   2164  A    O  
ATOM    265  N   SER A  36     -18.968  12.256   4.420  1.00 50.88      A    N  
ANISOU  265  N   SER A  36     6164   7755   5411  -1988   2195   1491  A    N  
ATOM    266  CA  SER A  36     -20.400  12.158   4.107  1.00 52.88      A    C  
ANISOU  266  CA  SER A  36     6108   8607   5376  -2166   2181   1530  A    C  
ATOM    267  C   SER A  36     -21.138  13.047   5.093  1.00 56.39      A    C  
ANISOU  267  C   SER A  36     6438   8986   6001  -1957   2205   1751  A    C  
ATOM    268  O   SER A  36     -21.237  12.697   6.276  1.00 53.88      A    O  
ANISOU  268  O   SER A  36     6358   8280   5834  -2030   2227   1600  A    O  
ATOM    269  CB  SER A  36     -20.875  10.708   4.179  1.00 56.66      A    C  
ANISOU  269  CB  SER A  36     6751   9160   5617  -2621   2196   1139  A    C  
ATOM    270  OG  SER A  36     -19.972   9.834   3.518  1.00 69.14      A    O  
ANISOU  270  OG  SER A  36     8536  10633   7100  -2791   2207    905  A    O  
ATOM    271  N   LEU A  37     -21.568  14.249   4.635  1.00 55.30      A    N  
ANISOU  271  N   LEU A  37     5958   9185   5866  -1658   2221   2128  A    N  
ATOM    272  CA  LEU A  37     -22.219  15.236   5.511  1.00 56.21      A    C  
ANISOU  272  CA  LEU A  37     5956   9228   6175  -1403   2275   2380  A    C  
ATOM    273  C   LEU A  37     -23.765  15.295   5.387  1.00 64.81      A    C  
ANISOU  273  C   LEU A  37     6682  10958   6985  -1480   2261   2485  A    C  
ATOM    274  O   LEU A  37     -24.298  15.615   4.319  1.00 67.61      A    O  
ANISOU  274  O   LEU A  37     6679  11947   7061  -1419   2243   2675  A    O  
ATOM    275  CB  LEU A  37     -21.668  16.659   5.285  1.00 55.98      A    C  
ANISOU  275  CB  LEU A  37     5824   9058   6389   -967   2362   2757  A    C  
ATOM    276  CG  LEU A  37     -20.226  16.855   4.840  1.00 59.91      A    C  
ANISOU  276  CG  LEU A  37     6516   9177   7068   -856   2387   2738  A    C  
ATOM    277  CD1 LEU A  37     -20.005  18.283   4.443  1.00 60.91      A    C  
ANISOU  277  CD1 LEU A  37     6468   9318   7358   -463   2514   3139  A    C  
ATOM    278  CD2 LEU A  37     -19.233  16.463   5.925  1.00 60.39      A    C  
ANISOU  278  CD2 LEU A  37     6969   8547   7428   -906   2387   2475  A    C  
ATOM    279  N   THR A  38     -24.469  15.071   6.509  1.00 61.43      A    N  
ANISOU  279  N   THR A  38     6328  10383   6631  -1581   2276   2382  A    N  
ATOM    280  CA  THR A  38     -25.931  15.172   6.575  1.00 63.78      A    C  
ANISOU  280  CA  THR A  38     6287  11250   6698  -1644   2273   2471  A    C  
ATOM    281  C   THR A  38     -26.243  16.653   6.760  1.00 68.88      A    C  
ANISOU  281  C   THR A  38     6713  11932   7527  -1175   2353   2912  A    C  
ATOM    282  O   THR A  38     -25.947  17.229   7.812  1.00 65.91      A    O  
ANISOU  282  O   THR A  38     6535  11014   7492   -990   2423   2973  A    O  
ATOM    283  CB  THR A  38     -26.493  14.266   7.673  1.00 72.84      A    C  
ANISOU  283  CB  THR A  38     7633  12199   7843  -1975   2277   2152  A    C  
ATOM    284  CG2 THR A  38     -28.033  14.327   7.772  1.00 72.83      A    C  
ANISOU  284  CG2 THR A  38     7263  12825   7585  -2086   2277   2203  A    C  
ATOM    285  OG1 THR A  38     -26.056  12.929   7.416  1.00 75.76      A    O  
ANISOU  285  OG1 THR A  38     8267  12438   8080  -2369   2255   1765  A    O  
ATOM    286  N   VAL A  39     -26.778  17.279   5.711  1.00 69.61      A    N  
ANISOU  286  N   VAL A  39     6407  12653   7388   -966   2361   3224  A    N  
ATOM    287  CA  VAL A  39     -27.054  18.716   5.694  1.00 70.31      A    C  
ANISOU  287  CA  VAL A  39     6285  12805   7624   -474   2481   3692  A    C  
ATOM    288  C   VAL A  39     -28.558  18.988   5.886  1.00 77.54      A    C  
ANISOU  288  C   VAL A  39     6823  14320   8318   -408   2490   3858  A    C  
ATOM    289  O   VAL A  39     -29.380  18.451   5.145  1.00 79.83      A    O  
ANISOU  289  O   VAL A  39     6788  15353   8191   -599   2403   3798  A    O  
ATOM    290  CB  VAL A  39     -26.507  19.360   4.388  1.00 74.22      A    C  
ANISOU  290  CB  VAL A  39     6619  13546   8035   -191   2524   3997  A    C  
ATOM    291  CG1 VAL A  39     -26.807  20.854   4.334  1.00 75.29      A    C  
ANISOU  291  CG1 VAL A  39     6561  13728   8319    342   2701   4510  A    C  
ATOM    292  CG2 VAL A  39     -25.006  19.124   4.247  1.00 71.05      A    C  
ANISOU  292  CG2 VAL A  39     6583  12545   7869   -252   2524   3827  A    C  
ATOM    293  N   ARG A  40     -28.897  19.843   6.865  1.00 73.96      A    N  
ANISOU  293  N   ARG A  40     6400  13563   8138   -137   2606   4055  A    N  
ATOM    294  CA  ARG A  40     -30.276  20.241   7.132  1.00 77.28      A    C  
ANISOU  294  CA  ARG A  40     6472  14493   8396     -5   2641   4251  A    C  
ATOM    295  C   ARG A  40     -30.477  21.696   6.710  1.00 84.72      A    C  
ANISOU  295  C   ARG A  40     7181  15592   9418    574   2810   4798  A    C  
ATOM    296  O   ARG A  40     -29.835  22.592   7.264  1.00 82.60      A    O  
ANISOU  296  O   ARG A  40     7147  14685   9551    862   2971   4966  A    O  
ATOM    297  CB  ARG A  40     -30.653  20.034   8.616  1.00 74.93      A    C  
ANISOU  297  CB  ARG A  40     6386  13761   8324   -151   2663   4047  A    C  
ATOM    298  CG  ARG A  40     -32.119  20.368   8.921  1.00 84.21      A    C  
ANISOU  298  CG  ARG A  40     7194  15479   9323    -39   2698   4222  A    C  
ATOM    299  CD  ARG A  40     -32.724  19.419   9.918  1.00 88.71      A    C  
ANISOU  299  CD  ARG A  40     7870  15988   9847   -455   2633   3846  A    C  
ATOM    300  NE  ARG A  40     -32.753  19.969  11.273  1.00 92.35      A    N  
ANISOU  300  NE  ARG A  40     8549  15870  10668   -301   2740   3883  A    N  
ATOM    301  CZ  ARG A  40     -32.554  19.256  12.378  1.00 98.21      A    C  
ANISOU  301  CZ  ARG A  40     9632  16110  11572   -598   2717   3541  A    C  
ATOM    302  NH1 ARG A  40     -32.270  17.960  12.300  1.00 80.29      A    N1+
ANISOU  302  NH1 ARG A  40     7561  13786   9159  -1054   2613   3148  A    N1+
ATOM    303  NH2 ARG A  40     -32.613  19.839  13.570  1.00 78.75      A    N  
ANISOU  303  NH2 ARG A  40     7329  13182   9412   -429   2818   3596  A    N  
ATOM    304  N   SER A  41     -31.377  21.922   5.738  1.00 86.35      A    N  
ANISOU  304  N   SER A  41     6922  16658   9228    744   2792   5067  A    N  
ATOM    305  CA  SER A  41     -31.720  23.254   5.229  1.00 89.46      A    C  
ANISOU  305  CA  SER A  41     7054  17314   9621   1335   2974   5633  A    C  
ATOM    306  C   SER A  41     -32.576  24.023   6.250  1.00 95.07      A    C  
ANISOU  306  C   SER A  41     7690  17923  10508   1607   3118   5842  A    C  
ATOM    307  O   SER A  41     -33.549  23.483   6.766  1.00 95.44      A    O  
ANISOU  307  O   SER A  41     7562  18332  10371   1385   3022   5665  A    O  
ATOM    308  CB  SER A  41     -32.456  23.140   3.896  1.00 97.60      A    C  
ANISOU  308  CB  SER A  41     7586  19385  10113   1426   2891   5834  A    C  
ATOM    309  OG  SER A  41     -32.966  24.386   3.447  1.00113.58      A    O  
ANISOU  309  OG  SER A  41     9315  21765  12077   2035   3076   6414  A    O  
ATOM    310  N   LEU A  42     -32.191  25.272   6.546  1.00 92.21      A    N  
ANISOU  310  N   LEU A  42     7477  17046  10513   2069   3369   6198  A    N  
ATOM    311  CA  LEU A  42     -32.879  26.162   7.484  1.00 93.37      A    C  
ANISOU  311  CA  LEU A  42     7593  17005  10878   2388   3562   6434  A    C  
ATOM    312  C   LEU A  42     -33.631  27.277   6.729  1.00104.90      A    C  
ANISOU  312  C   LEU A  42     8674  19024  12159   2993   3760   7038  A    C  
ATOM    313  O   LEU A  42     -34.494  27.940   7.308  1.00106.86      A    O  
ANISOU  313  O   LEU A  42     8781  19358  12465   3291   3910   7279  A    O  
ATOM    314  CB  LEU A  42     -31.866  26.768   8.476  1.00 89.87      A    C  
ANISOU  314  CB  LEU A  42     7626  15518  11005   2454   3747   6360  A    C  
ATOM    315  CG  LEU A  42     -31.688  26.070   9.837  1.00 90.93      A    C  
ANISOU  315  CG  LEU A  42     8068  15116  11365   2047   3643   5891  A    C  
ATOM    316  CD1 LEU A  42     -31.071  24.690   9.695  1.00 88.55      A    C  
ANISOU  316  CD1 LEU A  42     7951  14752  10941   1515   3383   5412  A    C  
ATOM    317  CD2 LEU A  42     -30.813  26.898  10.752  1.00 90.54      A    C  
ANISOU  317  CD2 LEU A  42     8393  14170  11839   2209   3866   5895  A    C  
ATOM    318  N   GLN A  43     -33.280  27.490   5.447  1.00105.53      A    N  
ANISOU  318  N   GLN A  43     8603  19470  12023   3196   3778   7294  A    N  
ATOM    319  CA  GLN A  43     -33.867  28.487   4.547  1.00110.53      A    C  
ANISOU  319  CA  GLN A  43     8885  20675  12435   3802   3971   7900  A    C  
ATOM    320  C   GLN A  43     -34.612  27.779   3.414  1.00118.50      A    C  
ANISOU  320  C   GLN A  43     9394  22821  12809   3706   3735   7914  A    C  
ATOM    321  O   GLN A  43     -34.133  26.766   2.898  1.00116.62      A    O  
ANISOU  321  O   GLN A  43     9186  22746  12379   3249   3498   7541  A    O  
ATOM    322  CB  GLN A  43     -32.764  29.407   3.980  1.00111.89      A    C  
ANISOU  322  CB  GLN A  43     9313  20312  12888   4152   4230   8213  A    C  
ATOM    323  CG  GLN A  43     -33.277  30.726   3.395  1.00134.94      A    C  
ANISOU  323  CG  GLN A  43    12018  23493  15760   4886   4567   8904  A    C  
ATOM    324  CD  GLN A  43     -32.304  31.380   2.436  1.00154.68      A    C  
ANISOU  324  CD  GLN A  43    14657  25765  18347   5185   4776   9220  A    C  
ATOM    325  NE2 GLN A  43     -32.795  31.761   1.265  1.00152.20      A    N  
ANISOU  325  NE2 GLN A  43    13969  26241  17618   5611   4835   9689  A    N  
ATOM    326  OE1 GLN A  43     -31.125  31.595   2.743  1.00145.76      A    O  
ANISOU  326  OE1 GLN A  43    13958  23775  17648   5060   4906   9064  A    O  
ATOM    327  N   ASP A  44     -35.771  28.317   3.021  1.00120.81      A    N  
ANISOU  327  N   ASP A  44     9221  23915  12767   4143   3812   8340  A    N  
ATOM    328  CA  ASP A  44     -36.585  27.747   1.949  1.00125.30      A    C  
ANISOU  328  CA  ASP A  44     9240  25681  12686   4097   3603   8378  A    C  
ATOM    329  C   ASP A  44     -35.927  27.960   0.576  1.00132.53      A    C  
ANISOU  329  C   ASP A  44    10073  26898  13385   4327   3631   8647  A    C  
ATOM    330  O   ASP A  44     -35.344  29.020   0.327  1.00133.13      A    O  
ANISOU  330  O   ASP A  44    10319  26558  13706   4842   3917   9105  A    O  
ATOM    331  CB  ASP A  44     -37.994  28.349   1.967  1.00132.17      A    C  
ANISOU  331  CB  ASP A  44     9618  27341  13261   4550   3691   8777  A    C  
ATOM    332  CG  ASP A  44     -38.722  28.185   3.289  1.00140.44      A    C  
ANISOU  332  CG  ASP A  44    10710  28157  14493   4347   3675   8536  A    C  
ATOM    333  OD1 ASP A  44     -38.990  29.211   3.948  1.00141.37      A    O  
ANISOU  333  OD1 ASP A  44    10933  27860  14922   4799   3943   8877  A    O  
ATOM    334  OD2 ASP A  44     -39.024  27.029   3.663  1.00144.77      A    O1-
ANISOU  334  OD2 ASP A  44    11202  28925  14878   3731   3415   8002  A    O1-
ATOM    335  N   SER A  45     -36.020  26.931  -0.300  1.00130.38      A    N  
ANISOU  335  N   SER A  45     9549  27340  12651   3919   3351   8339  A    N  
ATOM    336  CA  SER A  45     -35.503  26.857  -1.679  1.00132.10      A    C  
ANISOU  336  CA  SER A  45     9623  28019  12551   4011   3304   8484  A    C  
ATOM    337  C   SER A  45     -34.005  27.261  -1.795  1.00132.26      A    C  
ANISOU  337  C   SER A  45    10167  27053  13032   4085   3467   8543  A    C  
ATOM    338  O   SER A  45     -33.629  28.048  -2.670  1.00134.05      A    O  
ANISOU  338  O   SER A  45    10351  27366  13214   4573   3657   9019  A    O  
ATOM    339  CB  SER A  45     -36.372  27.673  -2.639  1.00141.89      A    C  
ANISOU  339  CB  SER A  45    10320  30268  13323   4660   3413   9102  A    C  
ATOM    340  OG  SER A  45     -36.365  29.060  -2.345  1.00149.38      A    O  
ANISOU  340  OG  SER A  45    11699  30298  14762   5133   3664   9312  A    O  
ATOM    341  N   LEU A  46     -33.155  26.678  -0.924  1.00123.50      A    N  
ANISOU  341  N   LEU A  46     9538  25044  12342   3592   3394   8048  A    N  
ATOM    342  CA  LEU A  46     -31.709  26.917  -0.916  1.00119.54      A    C  
ANISOU  342  CA  LEU A  46     9527  23615  12278   3568   3516   7998  A    C  
ATOM    343  C   LEU A  46     -31.058  26.233  -2.122  1.00122.85      A    C  
ANISOU  343  C   LEU A  46     9883  24402  12391   3351   3360   7859  A    C  
ATOM    344  O   LEU A  46     -31.238  25.031  -2.315  1.00121.87      A    O  
ANISOU  344  O   LEU A  46     9648  24689  11968   2828   3086   7400  A    O  
ATOM    345  CB  LEU A  46     -31.077  26.405   0.395  1.00114.26      A    C  
ANISOU  345  CB  LEU A  46     9336  21997  12082   3107   3456   7491  A    C  
ATOM    346  CG  LEU A  46     -30.262  27.400   1.239  1.00116.64      A    C  
ANISOU  346  CG  LEU A  46    10077  21240  13001   3355   3742   7632  A    C  
ATOM    347  CD1 LEU A  46     -29.578  26.688   2.383  1.00111.83      A    C  
ANISOU  347  CD1 LEU A  46     9881  19859  12749   2856   3624   7080  A    C  
ATOM    348  CD2 LEU A  46     -29.188  28.109   0.418  1.00120.04      A    C  
ANISOU  348  CD2 LEU A  46    10691  21316  13603   3637   3946   7908  A    C  
ATOM    349  N   ALA A  47     -30.299  26.994  -2.926  1.00119.57      A    N  
ANISOU  349  N   ALA A  47     9552  23825  12054   3740   3557   8243  A    N  
ATOM    350  CA  ALA A  47     -29.663  26.477  -4.135  1.00119.72      A    C  
ANISOU  350  CA  ALA A  47     9510  24194  11785   3590   3438   8160  A    C  
ATOM    351  C   ALA A  47     -28.179  26.138  -3.946  1.00117.24      A    C  
ANISOU  351  C   ALA A  47     9705  22960  11881   3252   3432   7803  A    C  
ATOM    352  O   ALA A  47     -27.688  25.210  -4.597  1.00115.16      A    O  
ANISOU  352  O   ALA A  47     9447  22910  11399   2859   3228   7457  A    O  
ATOM    353  CB  ALA A  47     -29.816  27.481  -5.265  1.00125.29      A    C  
ANISOU  353  CB  ALA A  47     9962  25385  12259   4230   3655   8812  A    C  
ATOM    354  N   SER A  48     -27.473  26.883  -3.070  1.00110.63      A    N  
ANISOU  354  N   SER A  48     9276  21139  11619   3403   3664   7875  A    N  
ATOM    355  CA  SER A  48     -26.039  26.710  -2.843  1.00106.30      A    C  
ANISOU  355  CA  SER A  48     9188  19724  11478   3156   3696   7585  A    C  
ATOM    356  C   SER A  48     -25.695  26.196  -1.434  1.00104.48      A    C  
ANISOU  356  C   SER A  48     9307  18759  11631   2743   3601   7090  A    C  
ATOM    357  O   SER A  48     -26.499  26.308  -0.513  1.00103.84      A    O  
ANISOU  357  O   SER A  48     9167  18684  11603   2734   3587   7053  A    O  
ATOM    358  CB  SER A  48     -25.309  28.027  -3.101  1.00111.04      A    C  
ANISOU  358  CB  SER A  48     9980  19784  12425   3641   4071   8039  A    C  
ATOM    359  OG  SER A  48     -25.832  29.071  -2.300  1.00121.95      A    O  
ANISOU  359  OG  SER A  48    11415  20817  14104   3996   4334   8331  A    O  
ATOM    360  N   LEU A  49     -24.471  25.650  -1.283  1.00 96.60      A    N  
ANISOU  360  N   LEU A  49     8668  17150  10887   2425   3542   6723  A    N  
ATOM    361  CA  LEU A  49     -23.929  25.116  -0.034  1.00 91.14      A    C  
ANISOU  361  CA  LEU A  49     8336  15746  10549   2059   3458   6256  A    C  
ATOM    362  C   LEU A  49     -22.485  25.618   0.166  1.00 89.89      A    C  
ANISOU  362  C   LEU A  49     8556  14759  10840   2096   3626   6196  A    C  
ATOM    363  O   LEU A  49     -21.582  25.187  -0.553  1.00 87.99      A    O  
ANISOU  363  O   LEU A  49     8411  14482  10542   1940   3556   6047  A    O  
ATOM    364  CB  LEU A  49     -23.982  23.579  -0.078  1.00 89.71      A    C  
ANISOU  364  CB  LEU A  49     8154  15844  10086   1517   3139   5745  A    C  
ATOM    365  CG  LEU A  49     -24.511  22.871   1.155  1.00 91.98      A    C  
ANISOU  365  CG  LEU A  49     8570  15905  10472   1196   3014   5377  A    C  
ATOM    366  CD1 LEU A  49     -26.025  23.014   1.272  1.00 95.60      A    C  
ANISOU  366  CD1 LEU A  49     8670  16985  10667   1303   2993   5558  A    C  
ATOM    367  CD2 LEU A  49     -24.161  21.408   1.112  1.00 91.28      A    C  
ANISOU  367  CD2 LEU A  49     8631  15828  10225    669   2782   4855  A    C  
ATOM    368  N   ILE A  50     -22.279  26.540   1.133  1.00 84.12      A    N  
ANISOU  368  N   ILE A  50     8025  13389  10546   2295   3861   6301  A    N  
ATOM    369  CA  ILE A  50     -20.978  27.151   1.448  1.00 81.35      A    C  
ANISOU  369  CA  ILE A  50     8006  12256  10646   2335   4067   6238  A    C  
ATOM    370  C   ILE A  50     -20.311  26.490   2.674  1.00 78.29      A    C  
ANISOU  370  C   ILE A  50     7932  11276  10540   1958   3930   5716  A    C  
ATOM    371  O   ILE A  50     -20.847  26.539   3.783  1.00 77.15      A    O  
ANISOU  371  O   ILE A  50     7841  10930  10542   1921   3931   5614  A    O  
ATOM    372  CB  ILE A  50     -21.072  28.692   1.635  1.00 87.36      A    C  
ANISOU  372  CB  ILE A  50     8796  12678  11718   2801   4477   6686  A    C  
ATOM    373  CG1 ILE A  50     -22.349  29.111   2.445  1.00 90.36      A    C  
ANISOU  373  CG1 ILE A  50     9035  13198  12102   2990   4544   6866  A    C  
ATOM    374  CG2 ILE A  50     -21.001  29.390   0.288  1.00 91.37      A    C  
ANISOU  374  CG2 ILE A  50     9143  13515  12058   3169   4680   7163  A    C  
ATOM    375  CD1 ILE A  50     -22.440  30.572   2.909  1.00102.94      A    C  
ANISOU  375  CD1 ILE A  50    10729  14313  14070   3399   4972   7220  A    C  
ATOM    376  N   LEU A  51     -19.124  25.895   2.465  1.00 69.29      A    N  
ANISOU  376  N   LEU A  51     6992   9872   9464   1705   3826   5400  A    N  
ATOM    377  CA  LEU A  51     -18.342  25.261   3.530  1.00 63.88      A    C  
ANISOU  377  CA  LEU A  51     6602   8654   9017   1392   3705   4924  A    C  
ATOM    378  C   LEU A  51     -16.948  25.874   3.625  1.00 64.84      A    C  
ANISOU  378  C   LEU A  51     6952   8180   9502   1435   3892   4847  A    C  
ATOM    379  O   LEU A  51     -16.437  26.401   2.633  1.00 64.95      A    O  
ANISOU  379  O   LEU A  51     6917   8251   9510   1601   4042   5078  A    O  
ATOM    380  CB  LEU A  51     -18.220  23.746   3.310  1.00 62.00      A    C  
ANISOU  380  CB  LEU A  51     6398   8676   8483   1009   3385   4544  A    C  
ATOM    381  CG  LEU A  51     -19.491  22.924   3.272  1.00 67.65      A    C  
ANISOU  381  CG  LEU A  51     6913   9961   8830    852   3191   4499  A    C  
ATOM    382  CD1 LEU A  51     -19.196  21.532   2.807  1.00 66.69      A    C  
ANISOU  382  CD1 LEU A  51     6836  10082   8420    492   2956   4159  A    C  
ATOM    383  CD2 LEU A  51     -20.169  22.876   4.629  1.00 69.50      A    C  
ANISOU  383  CD2 LEU A  51     7230   9967   9209    775   3167   4355  A    C  
ATOM    384  N   ASP A  52     -16.322  25.766   4.814  1.00 58.00      A    N  
ANISOU  384  N   ASP A  52     6326   6778   8935   1276   3882   4508  A    N  
ATOM    385  CA  ASP A  52     -14.972  26.271   5.078  1.00 55.75      A    C  
ANISOU  385  CA  ASP A  52     6244   5945   8995   1263   4045   4350  A    C  
ATOM    386  C   ASP A  52     -13.886  25.263   4.701  1.00 57.92      A    C  
ANISOU  386  C   ASP A  52     6639   6195   9173   1010   3839   4011  A    C  
ATOM    387  O   ASP A  52     -13.995  24.085   5.045  1.00 55.08      A    O  
ANISOU  387  O   ASP A  52     6346   5945   8636    771   3572   3715  A    O  
ATOM    388  CB  ASP A  52     -14.798  26.633   6.558  1.00 54.22      A    C  
ANISOU  388  CB  ASP A  52     6217   5246   9137   1215   4131   4124  A    C  
ATOM    389  CG  ASP A  52     -15.646  27.781   7.017  1.00 52.87      A    C  
ANISOU  389  CG  ASP A  52     5976   4970   9144   1474   4399   4429  A    C  
ATOM    390  OD1 ASP A  52     -15.335  28.933   6.647  1.00 51.30      A    O  
ANISOU  390  OD1 ASP A  52     5787   4525   9179   1693   4738   4672  A    O  
ATOM    391  OD2 ASP A  52     -16.622  27.530   7.738  1.00 58.19      A    O1-
ANISOU  391  OD2 ASP A  52     6591   5793   9725   1460   4296   4428  A    O1-
ATOM    392  N   THR A  53     -12.839  25.745   3.987  1.00 56.17      A    N  
ANISOU  392  N   THR A  53     6456   5812   9076   1074   3994   4063  A    N  
ATOM    393  CA  THR A  53     -11.641  24.987   3.584  1.00 54.22      A    C  
ANISOU  393  CA  THR A  53     6322   5495   8786    880   3858   3767  A    C  
ATOM    394  C   THR A  53     -10.415  25.877   3.735  1.00 56.55      A    C  
ANISOU  394  C   THR A  53     6728   5318   9442    931   4112   3699  A    C  
ATOM    395  O   THR A  53     -10.530  27.092   3.607  1.00 58.18      A    O  
ANISOU  395  O   THR A  53     6893   5356   9856   1141   4428   3984  A    O  
ATOM    396  CB  THR A  53     -11.713  24.421   2.143  1.00 64.12      A    C  
ANISOU  396  CB  THR A  53     7443   7234   9688    869   3747   3909  A    C  
ATOM    397  CG2 THR A  53     -12.941  23.552   1.876  1.00 62.17      A    C  
ANISOU  397  CG2 THR A  53     7056   7511   9053    773   3511   3936  A    C  
ATOM    398  OG1 THR A  53     -11.599  25.473   1.192  1.00 71.78      A    O  
ANISOU  398  OG1 THR A  53     8294   8279  10700   1127   4012   4306  A    O  
ATOM    399  N   LYS A  54      -9.250  25.281   4.011  1.00 51.12      A    N  
ANISOU  399  N   LYS A  54     6177   4422   8823    741   3997   3318  A    N  
ATOM    400  CA  LYS A  54      -7.976  26.001   4.129  1.00 51.12      A    C  
ANISOU  400  CA  LYS A  54     6259   4031   9133    734   4214   3179  A    C  
ATOM    401  C   LYS A  54      -6.864  25.054   3.698  1.00 52.50      A    C  
ANISOU  401  C   LYS A  54     6498   4265   9183    566   4021   2883  A    C  
ATOM    402  O   LYS A  54      -6.633  24.039   4.363  1.00 49.70      A    O  
ANISOU  402  O   LYS A  54     6243   3900   8741    413   3775   2554  A    O  
ATOM    403  CB  LYS A  54      -7.753  26.516   5.566  1.00 53.42      A    C  
ANISOU  403  CB  LYS A  54     6649   3907   9741    689   4322   2942  A    C  
ATOM    404  CG  LYS A  54      -6.689  27.599   5.671  1.00 63.95      A    C  
ANISOU  404  CG  LYS A  54     8023   4853  11422    692   4643   2852  A    C  
ATOM    405  CD  LYS A  54      -6.263  27.863   7.113  1.00 75.87      A    C  
ANISOU  405  CD  LYS A  54     9620   6024  13184    571   4678   2482  A    C  
ATOM    406  CE  LYS A  54      -5.129  28.872   7.151  1.00 84.81      A    C  
ANISOU  406  CE  LYS A  54    10771   6812  14639    518   5003   2332  A    C  
ATOM    407  NZ  LYS A  54      -4.565  29.053   8.522  1.00 88.88      A    N1+
ANISOU  407  NZ  LYS A  54    11340   7065  15366    372   5026   1916  A    N1+
ATOM    408  N   ASP A  55      -6.239  25.343   2.536  1.00 49.35      A    N  
ANISOU  408  N   ASP A  55     6045   3953   8752    617   4141   3027  A    N  
ATOM    409  CA  ASP A  55      -5.148  24.555   1.924  1.00 48.32      A    C  
ANISOU  409  CA  ASP A  55     5957   3901   8500    490   4002   2797  A    C  
ATOM    410  C   ASP A  55      -5.585  23.087   1.697  1.00 48.14      A    C  
ANISOU  410  C   ASP A  55     5958   4222   8112    364   3658   2668  A    C  
ATOM    411  O   ASP A  55      -4.807  22.157   1.894  1.00 43.93      A    O  
ANISOU  411  O   ASP A  55     5532   3653   7509    228   3483   2344  A    O  
ATOM    412  CB  ASP A  55      -3.859  24.628   2.780  1.00 49.82      A    C  
ANISOU  412  CB  ASP A  55     6249   3732   8947    375   4037   2402  A    C  
ATOM    413  CG  ASP A  55      -3.351  26.038   3.038  1.00 60.40      A    C  
ANISOU  413  CG  ASP A  55     7574   4719  10656    435   4406   2456  A    C  
ATOM    414  OD1 ASP A  55      -3.171  26.792   2.059  1.00 64.87      A    O  
ANISOU  414  OD1 ASP A  55     8082   5286  11280    536   4655   2726  A    O  
ATOM    415  OD2 ASP A  55      -3.103  26.374   4.220  1.00 63.56      A    O1-
ANISOU  415  OD2 ASP A  55     8025   4841  11284    374   4464   2215  A    O1-
ATOM    416  N   LEU A  56      -6.864  22.911   1.320  1.00 45.02      A    N  
ANISOU  416  N   LEU A  56     5460   4162   7484    415   3589   2922  A    N  
ATOM    417  CA  LEU A  56      -7.524  21.648   1.029  1.00 43.52      A    C  
ANISOU  417  CA  LEU A  56     5267   4333   6937    275   3322   2833  A    C  
ATOM    418  C   LEU A  56      -7.724  21.488  -0.462  1.00 52.03      A    C  
ANISOU  418  C   LEU A  56     6199   5844   7726    304   3315   3054  A    C  
ATOM    419  O   LEU A  56      -8.032  22.458  -1.157  1.00 54.42      A    O  
ANISOU  419  O   LEU A  56     6353   6279   8046    499   3507   3418  A    O  
ATOM    420  CB  LEU A  56      -8.907  21.590   1.713  1.00 43.06      A    C  
ANISOU  420  CB  LEU A  56     5155   4407   6800    283   3256   2934  A    C  
ATOM    421  CG  LEU A  56      -9.105  20.804   3.003  1.00 43.03      A    C  
ANISOU  421  CG  LEU A  56     5311   4225   6816    132   3087   2621  A    C  
ATOM    422  CD1 LEU A  56     -10.575  20.700   3.302  1.00 42.98      A    C  
ANISOU  422  CD1 LEU A  56     5204   4464   6663    132   3034   2773  A    C  
ATOM    423  CD2 LEU A  56      -8.566  19.396   2.895  1.00 42.33      A    C  
ANISOU  423  CD2 LEU A  56     5368   4200   6515    -72   2878   2301  A    C  
ATOM    424  N   THR A  57      -7.594  20.255  -0.950  1.00 49.11      A    N  
ANISOU  424  N   THR A  57     5877   5707   7077    120   3110   2840  A    N  
ATOM    425  CA  THR A  57      -7.828  19.942  -2.349  1.00 50.32      A    C  
ANISOU  425  CA  THR A  57     5885   6327   6905    105   3075   2993  A    C  
ATOM    426  C   THR A  57      -9.117  19.122  -2.406  1.00 54.35      A    C  
ANISOU  426  C   THR A  57     6308   7257   7084    -33   2903   2978  A    C  
ATOM    427  O   THR A  57      -9.189  18.051  -1.802  1.00 52.63      A    O  
ANISOU  427  O   THR A  57     6244   6962   6791   -245   2745   2659  A    O  
ATOM    428  CB  THR A  57      -6.603  19.249  -2.968  1.00 52.01      A    C  
ANISOU  428  CB  THR A  57     6210   6488   7062    -10   3019   2748  A    C  
ATOM    429  CG2 THR A  57      -6.770  19.004  -4.459  1.00 49.80      A    C  
ANISOU  429  CG2 THR A  57     5776   6697   6449    -24   3002   2902  A    C  
ATOM    430  OG1 THR A  57      -5.442  20.059  -2.746  1.00 49.37      A    O  
ANISOU  430  OG1 THR A  57     5940   5761   7057    100   3189   2734  A    O  
ATOM    431  N   ILE A  58     -10.140  19.646  -3.093  1.00 53.31      A    N  
ANISOU  431  N   ILE A  58     5928   7574   6755     96   2955   3324  A    N  
ATOM    432  CA  ILE A  58     -11.419  18.958  -3.238  1.00 55.10      A    C  
ANISOU  432  CA  ILE A  58     6009   8288   6637    -42   2808   3317  A    C  
ATOM    433  C   ILE A  58     -11.397  18.244  -4.593  1.00 59.52      A    C  
ANISOU  433  C   ILE A  58     6447   9360   6807   -175   2721   3277  A    C  
ATOM    434  O   ILE A  58     -11.257  18.889  -5.633  1.00 59.64      A    O  
ANISOU  434  O   ILE A  58     6290   9651   6720      8   2823   3568  A    O  
ATOM    435  CB  ILE A  58     -12.631  19.925  -3.047  1.00 60.75      A    C  
ANISOU  435  CB  ILE A  58     6497   9240   7347    190   2908   3702  A    C  
ATOM    436  CG1 ILE A  58     -12.663  20.489  -1.611  1.00 59.85      A    C  
ANISOU  436  CG1 ILE A  58     6529   8599   7614    275   2989   3675  A    C  
ATOM    437  CG2 ILE A  58     -13.967  19.247  -3.363  1.00 62.81      A    C  
ANISOU  437  CG2 ILE A  58     6542  10122   7202     46   2759   3701  A    C  
ATOM    438  CD1 ILE A  58     -12.177  21.918  -1.518  1.00 68.66      A    C  
ANISOU  438  CD1 ILE A  58     7648   9372   9069    579   3257   3969  A    C  
ATOM    439  N   LYS A  59     -11.478  16.902  -4.558  1.00 55.66      A    N  
ANISOU  439  N   LYS A  59     6071   8967   6109   -497   2557   2904  A    N  
ATOM    440  CA  LYS A  59     -11.444  16.053  -5.752  1.00 56.73      A    C  
ANISOU  440  CA  LYS A  59     6124   9563   5869   -691   2477   2775  A    C  
ATOM    441  C   LYS A  59     -12.826  16.005  -6.412  1.00 64.65      A    C  
ANISOU  441  C   LYS A  59     6794  11296   6475   -734   2425   2943  A    C  
ATOM    442  O   LYS A  59     -12.945  16.386  -7.575  1.00 65.89      A    O  
ANISOU  442  O   LYS A  59     6709  11936   6391   -612   2460   3183  A    O  
ATOM    443  CB  LYS A  59     -10.944  14.637  -5.418  1.00 55.79      A    C  
ANISOU  443  CB  LYS A  59     6286   9210   5700  -1019   2373   2296  A    C  
ATOM    444  CG  LYS A  59      -9.535  14.579  -4.843  1.00 46.54      A    C  
ANISOU  444  CG  LYS A  59     5412   7414   4856   -962   2409   2116  A    C  
ATOM    445  CD  LYS A  59      -9.229  13.162  -4.452  1.00 52.32      A    C  
ANISOU  445  CD  LYS A  59     6425   7941   5514  -1241   2328   1686  A    C  
ATOM    446  CE  LYS A  59      -8.143  13.010  -3.424  1.00 47.67      A    C  
ANISOU  446  CE  LYS A  59     6131   6731   5249  -1164   2343   1497  A    C  
ATOM    447  NZ  LYS A  59      -7.851  11.568  -3.194  1.00 43.20      A    N1+
ANISOU  447  NZ  LYS A  59     5849   5996   4569  -1396   2295   1116  A    N1+
ATOM    448  N   LYS A  60     -13.867  15.546  -5.674  1.00 62.85      A    N  
ANISOU  448  N   LYS A  60     6538  11181   6162   -900   2348   2818  A    N  
ATOM    449  CA  LYS A  60     -15.232  15.506  -6.188  1.00 66.61      A    C  
ANISOU  449  CA  LYS A  60     6665  12388   6254   -954   2295   2949  A    C  
ATOM    450  C   LYS A  60     -16.255  15.671  -5.066  1.00 72.99      A    C  
ANISOU  450  C   LYS A  60     7440  13138   7156   -957   2278   2976  A    C  
ATOM    451  O   LYS A  60     -15.970  15.372  -3.907  1.00 70.43      A    O  
ANISOU  451  O   LYS A  60     7403  12248   7111  -1051   2271   2759  A    O  
ATOM    452  CB  LYS A  60     -15.515  14.241  -7.024  1.00 71.19      A    C  
ANISOU  452  CB  LYS A  60     7178  13467   6405  -1345   2191   2613  A    C  
ATOM    453  CG  LYS A  60     -15.728  12.942  -6.261  1.00 87.19      A    C  
ANISOU  453  CG  LYS A  60     9465  15244   8417  -1757   2128   2131  A    C  
ATOM    454  CD  LYS A  60     -16.585  11.981  -7.089  1.00104.65      A    C  
ANISOU  454  CD  LYS A  60    11471  18152  10141  -2134   2065   1880  A    C  
ATOM    455  CE  LYS A  60     -16.810  10.639  -6.434  1.00119.58      A    C  
ANISOU  455  CE  LYS A  60    13622  19817  11997  -2569   2055   1405  A    C  
ATOM    456  NZ  LYS A  60     -15.619   9.758  -6.556  1.00129.12      A    N1+
ANISOU  456  NZ  LYS A  60    15212  20547  13301  -2743   2094   1072  A    N1+
ATOM    457  N   VAL A  61     -17.439  16.184  -5.430  1.00 74.08      A    N  
ANISOU  457  N   VAL A  61     7209  13893   7044   -824   2279   3262  A    N  
ATOM    458  CA  VAL A  61     -18.586  16.395  -4.552  1.00 74.74      A    C  
ANISOU  458  CA  VAL A  61     7175  14079   7143   -805   2266   3333  A    C  
ATOM    459  C   VAL A  61     -19.771  15.665  -5.177  1.00 85.68      A    C  
ANISOU  459  C   VAL A  61     8233  16294   8025  -1072   2160   3208  A    C  
ATOM    460  O   VAL A  61     -20.020  15.828  -6.370  1.00 88.58      A    O  
ANISOU  460  O   VAL A  61     8284  17324   8046   -985   2147   3390  A    O  
ATOM    461  CB  VAL A  61     -18.895  17.896  -4.290  1.00 78.60      A    C  
ANISOU  461  CB  VAL A  61     7514  14503   7847   -323   2409   3840  A    C  
ATOM    462  CG1 VAL A  61     -20.065  18.054  -3.318  1.00 78.58      A    C  
ANISOU  462  CG1 VAL A  61     7403  14585   7867   -311   2397   3888  A    C  
ATOM    463  CG2 VAL A  61     -17.674  18.635  -3.757  1.00 75.44      A    C  
ANISOU  463  CG2 VAL A  61     7420  13313   7932   -104   2543   3922  A    C  
ATOM    464  N   ALA A  62     -20.487  14.853  -4.377  1.00 84.76      A    N  
ANISOU  464  N   ALA A  62     8187  16160   7856  -1406   2095   2886  A    N  
ATOM    465  CA  ALA A  62     -21.657  14.089  -4.813  1.00 88.71      A    C  
ANISOU  465  CA  ALA A  62     8388  17420   7897  -1735   2013   2690  A    C  
ATOM    466  C   ALA A  62     -22.818  14.242  -3.830  1.00 94.24      A    C  
ANISOU  466  C   ALA A  62     8972  18212   8625  -1754   2007   2720  A    C  
ATOM    467  O   ALA A  62     -22.671  13.943  -2.645  1.00 91.65      A    O  
ANISOU  467  O   ALA A  62     8963  17256   8604  -1857   2029   2539  A    O  
ATOM    468  CB  ALA A  62     -21.293  12.620  -4.974  1.00 89.28      A    C  
ANISOU  468  CB  ALA A  62     8701  17395   7828  -2250   1973   2150  A    C  
ATOM    469  N   VAL A  63     -23.976  14.705  -4.332  1.00 95.34      A    N  
ANISOU  469  N   VAL A  63     8636  19166   8422  -1638   1981   2957  A    N  
ATOM    470  CA  VAL A  63     -25.197  14.891  -3.543  1.00 96.57      A    C  
ANISOU  470  CA  VAL A  63     8600  19550   8540  -1640   1976   3011  A    C  
ATOM    471  C   VAL A  63     -26.255  13.920  -4.094  1.00105.32      A    C  
ANISOU  471  C   VAL A  63     9384  21498   9134  -2090   1891   2686  A    C  
ATOM    472  O   VAL A  63     -26.736  14.099  -5.216  1.00108.67      A    O  
ANISOU  472  O   VAL A  63     9384  22771   9135  -2029   1846   2824  A    O  
ATOM    473  CB  VAL A  63     -25.686  16.371  -3.519  1.00101.79      A    C  
ANISOU  473  CB  VAL A  63     8976  20424   9275  -1059   2050   3601  A    C  
ATOM    474  CG1 VAL A  63     -26.869  16.550  -2.573  1.00102.59      A    C  
ANISOU  474  CG1 VAL A  63     8888  20743   9349  -1056   2050   3645  A    C  
ATOM    475  CG2 VAL A  63     -24.559  17.325  -3.138  1.00 98.38      A    C  
ANISOU  475  CG2 VAL A  63     8873  19156   9350   -669   2174   3872  A    C  
ATOM    476  N   ASN A  64     -26.572  12.871  -3.305  1.00101.91      A    N  
ANISOU  476  N   ASN A  64     9165  20821   8734  -2555   1887   2237  A    N  
ATOM    477  CA  ASN A  64     -27.522  11.785  -3.601  1.00105.29      A    C  
ANISOU  477  CA  ASN A  64     9376  21891   8740  -3094   1852   1817  A    C  
ATOM    478  C   ASN A  64     -27.104  10.952  -4.859  1.00110.67      A    C  
ANISOU  478  C   ASN A  64    10002  22977   9070  -3430   1826   1513  A    C  
ATOM    479  O   ASN A  64     -27.962  10.385  -5.544  1.00114.61      A    O  
ANISOU  479  O   ASN A  64    10139  24305   9102  -3778   1793   1273  A    O  
ATOM    480  CB  ASN A  64     -28.977  12.297  -3.716  1.00111.61      A    C  
ANISOU  480  CB  ASN A  64     9608  23592   9205  -2983   1811   2030  A    C  
ATOM    481  CG  ASN A  64     -29.680  12.582  -2.399  1.00141.96      A    C  
ANISOU  481  CG  ASN A  64    13504  27140  13293  -2902   1848   2108  A    C  
ATOM    482  ND2 ASN A  64     -30.840  13.216  -2.482  1.00137.72      A    N  
ANISOU  482  ND2 ASN A  64    12476  27341  12509  -2693   1821   2377  A    N  
ATOM    483  OD1 ASN A  64     -29.225  12.221  -1.304  1.00137.37      A    O  
ANISOU  483  OD1 ASN A  64    13383  25712  13097  -3019   1904   1928  A    O  
ATOM    484  N   GLY A  65     -25.791  10.860  -5.099  1.00103.59      A    N  
ANISOU  484  N   GLY A  65     9466  21488   8404  -3347   1851   1494  A    N  
ATOM    485  CA  GLY A  65     -25.183  10.060  -6.159  1.00104.27      A    C  
ANISOU  485  CA  GLY A  65     9599  21776   8243  -3641   1848   1200  A    C  
ATOM    486  C   GLY A  65     -25.359  10.498  -7.599  1.00111.08      A    C  
ANISOU  486  C   GLY A  65     9991  23529   8684  -3472   1782   1427  A    C  
ATOM    487  O   GLY A  65     -26.155   9.900  -8.325  1.00114.99      A    O  
ANISOU  487  O   GLY A  65    10127  24868   8696  -3814   1746   1183  A    O  
ATOM    488  N   LYS A  66     -24.569  11.493  -8.048  1.00105.83      A    N  
ANISOU  488  N   LYS A  66     9332  22693   8184  -2965   1782   1871  A    N  
ATOM    489  CA  LYS A  66     -24.577  11.984  -9.434  1.00108.70      A    C  
ANISOU  489  CA  LYS A  66     9297  23833   8174  -2734   1741   2145  A    C  
ATOM    490  C   LYS A  66     -23.266  12.709  -9.771  1.00110.51      A    C  
ANISOU  490  C   LYS A  66     9773  23509   8707  -2332   1792   2454  A    C  
ATOM    491  O   LYS A  66     -22.638  12.399 -10.788  1.00111.10      A    O  
ANISOU  491  O   LYS A  66     9851  23768   8594  -2429   1784   2345  A    O  
ATOM    492  CB  LYS A  66     -25.791  12.910  -9.709  1.00114.31      A    C  
ANISOU  492  CB  LYS A  66     9444  25402   8588  -2380   1702   2579  A    C  
ATOM    493  CG  LYS A  66     -25.839  13.541 -11.117  1.00121.31      A    C  
ANISOU  493  CG  LYS A  66     9901  27123   9070  -2044   1675   2947  A    C  
ATOM    494  CD  LYS A  66     -26.256  12.568 -12.229  1.00127.91      A    C  
ANISOU  494  CD  LYS A  66    10413  28878   9310  -2500   1593   2554  A    C  
ATOM    495  CE  LYS A  66     -25.797  13.021 -13.599  1.00132.74      A    C  
ANISOU  495  CE  LYS A  66    10782  30033   9621  -2203   1582   2847  A    C  
ATOM    496  NZ  LYS A  66     -26.602  14.158 -14.122  1.00142.00      A    N1+
ANISOU  496  NZ  LYS A  66    11420  32055  10480  -1659   1568   3428  A    N1+
ATOM    497  N   ASP A  67     -22.889  13.683  -8.910  1.00103.94      A    N  
ANISOU  497  N   ASP A  67     9133  22025   8335  -1898   1860   2825  A    N  
ATOM    498  CA  ASP A  67     -21.755  14.618  -8.935  1.00100.96      A    C  
ANISOU  498  CA  ASP A  67     8986  21038   8334  -1467   1949   3171  A    C  
ATOM    499  C   ASP A  67     -22.309  16.029  -9.029  1.00105.66      A    C  
ANISOU  499  C   ASP A  67     9280  21922   8945   -898   2023   3784  A    C  
ATOM    500  O   ASP A  67     -23.009  16.362  -9.987  1.00110.02      A    O  
ANISOU  500  O   ASP A  67     9402  23322   9079   -712   2006   4051  A    O  
ATOM    501  CB  ASP A  67     -20.713  14.340 -10.040  1.00103.27      A    C  
ANISOU  501  CB  ASP A  67     9362  21368   8510  -1522   1953   3085  A    C  
ATOM    502  CG  ASP A  67     -19.628  13.352  -9.646  1.00112.13      A    C  
ANISOU  502  CG  ASP A  67    10958  21789   9859  -1890   1952   2604  A    C  
ATOM    503  OD1 ASP A  67     -19.888  12.498  -8.765  1.00110.79      A    O  
ANISOU  503  OD1 ASP A  67    11052  21158   9887  -2153   1945   2295  A    O  
ATOM    504  OD2 ASP A  67     -18.519  13.425 -10.227  1.00118.24      A    O1-
ANISOU  504  OD2 ASP A  67    11842  22478  10607  -1895   1971   2551  A    O1-
ATOM    505  N   ALA A  68     -22.052  16.832  -7.992  1.00 98.30      A    N  
ANISOU  505  N   ALA A  68     8568  20304   8478   -623   2119   3997  A    N  
ATOM    506  CA  ALA A  68     -22.524  18.208  -7.872  1.00 98.92      A    C  
ANISOU  506  CA  ALA A  68     8446  20475   8664    -73   2244   4568  A    C  
ATOM    507  C   ALA A  68     -21.453  19.199  -8.308  1.00100.02      A    C  
ANISOU  507  C   ALA A  68     8734  20203   9064    334   2407   4934  A    C  
ATOM    508  O   ALA A  68     -20.258  18.943  -8.139  1.00 96.99      A    O  
ANISOU  508  O   ALA A  68     8720  19151   8982    207   2431   4722  A    O  
ATOM    509  CB  ALA A  68     -22.945  18.487  -6.439  1.00 97.46      A    C  
ANISOU  509  CB  ALA A  68     8432  19753   8845    -31   2287   4562  A    C  
ATOM    510  N   THR A  69     -21.886  20.331  -8.878  1.00 97.75      A    N  
ANISOU  510  N   THR A  69     8157  20333   8651    834   2538   5490  A    N  
ATOM    511  CA  THR A  69     -20.981  21.369  -9.365  1.00 96.62      A    C  
ANISOU  511  CA  THR A  69     8129  19850   8730   1251   2746   5892  A    C  
ATOM    512  C   THR A  69     -20.445  22.160  -8.164  1.00 94.85      A    C  
ANISOU  512  C   THR A  69     8258  18666   9116   1443   2929   5997  A    C  
ATOM    513  O   THR A  69     -21.224  22.791  -7.442  1.00 95.33      A    O  
ANISOU  513  O   THR A  69     8236  18693   9295   1675   3017   6230  A    O  
ATOM    514  CB  THR A  69     -21.689  22.252 -10.410  1.00107.72      A    C  
ANISOU  514  CB  THR A  69     9107  22065   9754   1732   2851   6463  A    C  
ATOM    515  CG2 THR A  69     -20.725  23.105 -11.199  1.00107.02      A    C  
ANISOU  515  CG2 THR A  69     9126  21737   9799   2100   3069   6839  A    C  
ATOM    516  OG1 THR A  69     -22.422  21.419 -11.311  1.00110.21      A    O  
ANISOU  516  OG1 THR A  69     9041  23370   9464   1495   2648   6292  A    O  
ATOM    517  N   PHE A  70     -19.123  22.073  -7.924  1.00 85.66      A    N  
ANISOU  517  N   PHE A  70     7475  16747   8324   1322   2983   5789  A    N  
ATOM    518  CA  PHE A  70     -18.482  22.788  -6.826  1.00 81.64      A    C  
ANISOU  518  CA  PHE A  70     7296  15342   8381   1456   3159   5825  A    C  
ATOM    519  C   PHE A  70     -17.552  23.886  -7.346  1.00 86.19      A    C  
ANISOU  519  C   PHE A  70     7979  15567   9203   1817   3435   6186  A    C  
ATOM    520  O   PHE A  70     -17.051  23.809  -8.481  1.00 85.83      A    O  
ANISOU  520  O   PHE A  70     7856  15812   8942   1858   3447   6277  A    O  
ATOM    521  CB  PHE A  70     -17.752  21.844  -5.858  1.00 78.71      A    C  
ANISOU  521  CB  PHE A  70     7282  14342   8282   1030   3019   5269  A    C  
ATOM    522  CG  PHE A  70     -16.646  21.001  -6.435  1.00 78.45      A    C  
ANISOU  522  CG  PHE A  70     7429  14174   8206    753   2924   4937  A    C  
ATOM    523  CD1 PHE A  70     -15.325  21.430  -6.384  1.00 79.40      A    C  
ANISOU  523  CD1 PHE A  70     7815  13668   8685    833   3061   4921  A    C  
ATOM    524  CD2 PHE A  70     -16.916  19.755  -6.988  1.00 81.15      A    C  
ANISOU  524  CD2 PHE A  70     7677  15001   8153    391   2712   4609  A    C  
ATOM    525  CE1 PHE A  70     -14.298  20.644  -6.905  1.00 78.99      A    C  
ANISOU  525  CE1 PHE A  70     7919  13505   8588    595   2975   4617  A    C  
ATOM    526  CE2 PHE A  70     -15.886  18.959  -7.493  1.00 82.76      A    C  
ANISOU  526  CE2 PHE A  70     8066  15052   8327    146   2644   4297  A    C  
ATOM    527  CZ  PHE A  70     -14.584  19.413  -7.456  1.00 78.99      A    C  
ANISOU  527  CZ  PHE A  70     7839  13973   8199    267   2769   4317  A    C  
ATOM    528  N   ALA A  71     -17.355  24.930  -6.513  1.00 83.05      A    N  
ANISOU  528  N   ALA A  71     7757  14548   9251   2073   3681   6390  A    N  
ATOM    529  CA  ALA A  71     -16.537  26.089  -6.857  1.00 84.38      A    C  
ANISOU  529  CA  ALA A  71     8053  14298   9708   2408   4011   6731  A    C  
ATOM    530  C   ALA A  71     -15.890  26.737  -5.630  1.00 86.81      A    C  
ANISOU  530  C   ALA A  71     8685  13706  10593   2416   4208   6620  A    C  
ATOM    531  O   ALA A  71     -16.582  27.144  -4.695  1.00 85.08      A    O  
ANISOU  531  O   ALA A  71     8472  13316  10538   2505   4267   6678  A    O  
ATOM    532  CB  ALA A  71     -17.379  27.120  -7.599  1.00 89.71      A    C  
ANISOU  532  CB  ALA A  71     8450  15463  10174   2921   4238   7362  A    C  
ATOM    533  N   LEU A  72     -14.550  26.859  -5.668  1.00 83.83      A    N  
ANISOU  533  N   LEU A  72     8558  12785  10508   2322   4322   6457  A    N  
ATOM    534  CA  LEU A  72     -13.743  27.510  -4.638  1.00 81.83      A    C  
ANISOU  534  CA  LEU A  72     8595  11708  10788   2304   4533   6316  A    C  
ATOM    535  C   LEU A  72     -13.642  29.011  -4.943  1.00 87.41      A    C  
ANISOU  535  C   LEU A  72     9322  12158  11731   2728   4986   6811  A    C  
ATOM    536  O   LEU A  72     -13.463  29.388  -6.098  1.00 89.31      A    O  
ANISOU  536  O   LEU A  72     9470  12655  11808   2943   5136   7135  A    O  
ATOM    537  CB  LEU A  72     -12.352  26.868  -4.558  1.00 79.34      A    C  
ANISOU  537  CB  LEU A  72     8507  11004  10636   1979   4429   5867  A    C  
ATOM    538  CG  LEU A  72     -12.198  25.629  -3.663  1.00 81.53      A    C  
ANISOU  538  CG  LEU A  72     8909  11166  10902   1578   4094   5321  A    C  
ATOM    539  CD1 LEU A  72     -12.651  24.355  -4.373  1.00 82.32      A    C  
ANISOU  539  CD1 LEU A  72     8861  11887  10528   1361   3776   5163  A    C  
ATOM    540  CD2 LEU A  72     -10.748  25.445  -3.277  1.00 82.35      A    C  
ANISOU  540  CD2 LEU A  72     9266  10718  11306   1379   4110   4954  A    C  
ATOM    541  N   GLY A  73     -13.784  29.838  -3.913  1.00 83.50      A    N  
ANISOU  541  N   GLY A  73     8956  11163  11608   2846   5218   6868  A    N  
ATOM    542  CA  GLY A  73     -13.753  31.290  -4.041  1.00 86.23      A    C  
ANISOU  542  CA  GLY A  73     9363  11178  12223   3240   5704   7318  A    C  
ATOM    543  C   GLY A  73     -12.369  31.879  -3.904  1.00 89.82      A    C  
ANISOU  543  C   GLY A  73    10085  10939  13104   3148   5995   7162  A    C  
ATOM    544  O   GLY A  73     -11.373  31.198  -4.168  1.00 87.54      A    O  
ANISOU  544  O   GLY A  73     9874  10581  12806   2857   5824   6817  A    O  
ATOM    545  N   THR A  74     -12.295  33.168  -3.519  1.00 88.48      A    N  
ANISOU  545  N   THR A  74    10053  10257  13308   3395   6464   7415  A    N  
ATOM    546  CA  THR A  74     -11.006  33.853  -3.356  1.00 87.63      A    C  
ANISOU  546  CA  THR A  74    10193   9469  13632   3294   6811   7260  A    C  
ATOM    547  C   THR A  74     -10.439  33.475  -1.986  1.00 86.19      A    C  
ANISOU  547  C   THR A  74    10174   8817  13757   2902   6657   6666  A    C  
ATOM    548  O   THR A  74     -11.159  33.485  -0.985  1.00 83.80      A    O  
ANISOU  548  O   THR A  74     9874   8432  13535   2889   6587   6580  A    O  
ATOM    549  CB  THR A  74     -11.112  35.381  -3.571  1.00 94.39      A    C  
ANISOU  549  CB  THR A  74    11151   9948  14764   3693   7426   7751  A    C  
ATOM    550  CG2 THR A  74     -11.638  35.746  -4.934  1.00 94.90      A    C  
ANISOU  550  CG2 THR A  74    11061  10492  14506   4117   7594   8360  A    C  
ATOM    551  OG1 THR A  74     -11.959  35.950  -2.585  1.00100.39      A    O  
ANISOU  551  OG1 THR A  74    11929  10528  15686   3845   7557   7854  A    O  
ATOM    552  N   THR A  75      -9.151  33.143  -1.954  1.00 80.89      A    N  
ANISOU  552  N   THR A  75     9625   7875  13234   2600   6604   6266  A    N  
ATOM    553  CA  THR A  75      -8.468  32.728  -0.740  1.00 77.73      A    C  
ANISOU  553  CA  THR A  75     9357   7098  13079   2241   6443   5692  A    C  
ATOM    554  C   THR A  75      -8.242  33.941   0.165  1.00 83.51      A    C  
ANISOU  554  C   THR A  75    10251   7193  14284   2273   6888   5654  A    C  
ATOM    555  O   THR A  75      -7.549  34.883  -0.209  1.00 85.47      A    O  
ANISOU  555  O   THR A  75    10605   7077  14792   2330   7314   5755  A    O  
ATOM    556  CB  THR A  75      -7.172  31.968  -1.098  1.00 81.07      A    C  
ANISOU  556  CB  THR A  75     9824   7517  13464   1947   6244   5303  A    C  
ATOM    557  CG2 THR A  75      -6.404  31.486   0.133  1.00 74.23      A    C  
ANISOU  557  CG2 THR A  75     9063   6359  12780   1608   6034   4714  A    C  
ATOM    558  OG1 THR A  75      -7.517  30.844  -1.914  1.00 79.15      A    O  
ANISOU  558  OG1 THR A  75     9436   7864  12774   1934   5878   5368  A    O  
ATOM    559  N   HIS A  76      -8.858  33.905   1.349  1.00 79.79      A    N  
ANISOU  559  N   HIS A  76     9804   6595  13919   2224   6804   5497  A    N  
ATOM    560  CA  HIS A  76      -8.742  34.928   2.381  1.00 81.75      A    C  
ANISOU  560  CA  HIS A  76    10200   6266  14595   2213   7183   5390  A    C  
ATOM    561  C   HIS A  76      -7.385  34.802   3.084  1.00 85.90      A    C  
ANISOU  561  C   HIS A  76    10845   6405  15388   1841   7182   4815  A    C  
ATOM    562  O   HIS A  76      -6.780  33.728   3.077  1.00 83.59      A    O  
ANISOU  562  O   HIS A  76    10515   6326  14919   1602   6787   4470  A    O  
ATOM    563  CB  HIS A  76      -9.897  34.795   3.385  1.00 82.11      A    C  
ANISOU  563  CB  HIS A  76    10208   6378  14612   2268   7038   5388  A    C  
ATOM    564  CG  HIS A  76     -10.061  35.983   4.274  1.00 87.82      A    C  
ANISOU  564  CG  HIS A  76    11064   6570  15735   2360   7497   5426  A    C  
ATOM    565  CD2 HIS A  76     -10.865  37.062   4.134  1.00 93.25      A    C  
ANISOU  565  CD2 HIS A  76    11772   7125  16535   2720   7915   5900  A    C  
ATOM    566  ND1 HIS A  76      -9.321  36.122   5.432  1.00 88.38      A    N  
ANISOU  566  ND1 HIS A  76    11263   6192  16124   2064   7571   4927  A    N  
ATOM    567  CE1 HIS A  76      -9.696  37.276   5.958  1.00 90.50      A    C  
ANISOU  567  CE1 HIS A  76    11634   6053  16699   2220   8036   5088  A    C  
ATOM    568  NE2 HIS A  76     -10.628  37.874   5.217  1.00 93.80      A    N  
ANISOU  568  NE2 HIS A  76    12003   6621  17014   2627   8265   5681  A    N  
ATOM    569  N   SER A  77      -6.928  35.900   3.703  1.00 85.54      A    N  
ANISOU  569  N   SER A  77    10936   5807  15757   1796   7640   4706  A    N  
ATOM    570  CA  SER A  77      -5.652  36.045   4.415  1.00 84.93      A    C  
ANISOU  570  CA  SER A  77    10949   5352  15968   1450   7736   4162  A    C  
ATOM    571  C   SER A  77      -5.471  35.019   5.561  1.00 85.10      A    C  
ANISOU  571  C   SER A  77    10936   5501  15897   1174   7262   3640  A    C  
ATOM    572  O   SER A  77      -4.338  34.591   5.806  1.00 84.30      A    O  
ANISOU  572  O   SER A  77    10832   5377  15822    908   7116   3209  A    O  
ATOM    573  CB  SER A  77      -5.526  37.469   4.961  1.00 91.61      A    C  
ANISOU  573  CB  SER A  77    11939   5610  17258   1463   8340   4161  A    C  
ATOM    574  OG  SER A  77      -4.198  37.776   5.350  1.00100.88      A    O  
ANISOU  574  OG  SER A  77    13173   6452  18704   1121   8505   3650  A    O  
ATOM    575  N   PHE A  78      -6.568  34.616   6.243  1.00 78.47      A    N  
ANISOU  575  N   PHE A  78    10065   4811  14937   1253   7035   3692  A    N  
ATOM    576  CA  PHE A  78      -6.492  33.647   7.352  1.00 74.95      A    C  
ANISOU  576  CA  PHE A  78     9607   4476  14394   1029   6615   3246  A    C  
ATOM    577  C   PHE A  78      -7.696  32.672   7.417  1.00 71.91      A    C  
ANISOU  577  C   PHE A  78     9143   4520  13659   1135   6200   3416  A    C  
ATOM    578  O   PHE A  78      -7.546  31.560   7.924  1.00 68.63      A    O  
ANISOU  578  O   PHE A  78     8720   4296  13061    963   5795   3100  A    O  
ATOM    579  CB  PHE A  78      -6.354  34.378   8.705  1.00 78.02      A    C  
ANISOU  579  CB  PHE A  78    10077   4449  15117    905   6857   2941  A    C  
ATOM    580  CG  PHE A  78      -7.386  35.458   8.961  1.00 82.31      A    C  
ANISOU  580  CG  PHE A  78    10668   4764  15844   1139   7230   3292  A    C  
ATOM    581  CD1 PHE A  78      -8.608  35.150   9.551  1.00 84.08      A    C  
ANISOU  581  CD1 PHE A  78    10854   5166  15925   1261   7026   3423  A    C  
ATOM    582  CD2 PHE A  78      -7.129  36.781   8.622  1.00 88.17      A    C  
ANISOU  582  CD2 PHE A  78    11500   5097  16903   1241   7812   3489  A    C  
ATOM    583  CE1 PHE A  78      -9.562  36.141   9.777  1.00 87.61      A    C  
ANISOU  583  CE1 PHE A  78    11335   5418  16533   1503   7377   3756  A    C  
ATOM    584  CE2 PHE A  78      -8.081  37.772   8.854  1.00 93.58      A    C  
ANISOU  584  CE2 PHE A  78    12246   5552  17757   1492   8187   3831  A    C  
ATOM    585  CZ  PHE A  78      -9.297  37.441   9.414  1.00 90.42      A    C  
ANISOU  585  CZ  PHE A  78    11789   5368  17198   1634   7955   3971  A    C  
ATOM    586  N   LYS A  79      -8.868  33.091   6.904  1.00 67.41      A    N  
ANISOU  586  N   LYS A  79     8513   4109  12992   1420   6322   3909  A    N  
ATOM    587  CA  LYS A  79     -10.121  32.331   6.920  1.00 64.85      A    C  
ANISOU  587  CA  LYS A  79     8083   4212  12345   1524   5995   4095  A    C  
ATOM    588  C   LYS A  79     -10.105  31.116   5.975  1.00 65.27      A    C  
ANISOU  588  C   LYS A  79     8039   4763  11998   1466   5602   4119  A    C  
ATOM    589  O   LYS A  79     -10.892  30.177   6.148  1.00 63.46      A    O  
ANISOU  589  O   LYS A  79     7740   4884  11488   1425   5264   4099  A    O  
ATOM    590  CB  LYS A  79     -11.313  33.243   6.572  1.00 69.69      A    C  
ANISOU  590  CB  LYS A  79     8629   4882  12969   1874   6286   4627  A    C  
ATOM    591  CG  LYS A  79     -11.682  34.252   7.651  1.00 76.96      A    C  
ANISOU  591  CG  LYS A  79     9637   5397  14208   1937   6585   4600  A    C  
ATOM    592  CD  LYS A  79     -13.135  34.673   7.543  1.00 87.55      A    C  
ANISOU  592  CD  LYS A  79    10877   6939  15448   2283   6718   5091  A    C  
ATOM    593  CE  LYS A  79     -13.304  36.112   7.145  1.00106.82      A    C  
ANISOU  593  CE  LYS A  79    13392   9024  18171   2582   7306   5474  A    C  
ATOM    594  NZ  LYS A  79     -14.727  36.538   7.226  1.00117.76      A    N1+
ANISOU  594  NZ  LYS A  79    14680  10594  19469   2947   7444   5934  A    N1+
ATOM    595  N   GLY A  80      -9.173  31.111   5.037  1.00 61.60      A    N  
ANISOU  595  N   GLY A  80     7579   4308  11517   1432   5663   4122  A    N  
ATOM    596  CA  GLY A  80      -9.033  30.049   4.053  1.00 59.71      A    C  
ANISOU  596  CA  GLY A  80     7259   4507  10920   1372   5346   4134  A    C  
ATOM    597  C   GLY A  80      -9.810  30.361   2.795  1.00 64.85      A    C  
ANISOU  597  C   GLY A  80     7765   5533  11343   1647   5449   4657  A    C  
ATOM    598  O   GLY A  80     -10.016  31.533   2.463  1.00 66.72      A    O  
ANISOU  598  O   GLY A  80     7999   5599  11752   1899   5844   5016  A    O  
ATOM    599  N   THR A  81     -10.281  29.322   2.110  1.00 60.13      A    N  
ANISOU  599  N   THR A  81     7045   5459  10344   1611   5113   4705  A    N  
ATOM    600  CA  THR A  81     -11.016  29.482   0.859  1.00 62.42      A    C  
ANISOU  600  CA  THR A  81     7153   6226  10338   1857   5157   5170  A    C  
ATOM    601  C   THR A  81     -12.441  28.987   0.997  1.00 66.58      A    C  
ANISOU  601  C   THR A  81     7515   7220  10564   1922   4936   5316  A    C  
ATOM    602  O   THR A  81     -12.645  27.887   1.496  1.00 64.66      A    O  
ANISOU  602  O   THR A  81     7280   7131  10155   1672   4595   4993  A    O  
ATOM    603  CB  THR A  81     -10.300  28.709  -0.252  1.00 63.57      A    C  
ANISOU  603  CB  THR A  81     7261   6661  10232   1736   4978   5087  A    C  
ATOM    604  CG2 THR A  81     -10.788  29.077  -1.645  1.00 62.01      A    C  
ANISOU  604  CG2 THR A  81     6878   6926   9755   2010   5091   5574  A    C  
ATOM    605  OG1 THR A  81      -8.902  28.933  -0.128  1.00 61.84      A    O  
ANISOU  605  OG1 THR A  81     7199   6000  10297   1603   5120   4832  A    O  
ATOM    606  N   PRO A  82     -13.447  29.720   0.500  1.00 66.20      A    N  
ANISOU  606  N   PRO A  82     7303   7443  10406   2259   5126   5805  A    N  
ATOM    607  CA  PRO A  82     -14.808  29.179   0.566  1.00 66.70      A    C  
ANISOU  607  CA  PRO A  82     7162   8042  10138   2304   4898   5925  A    C  
ATOM    608  C   PRO A  82     -15.066  28.162  -0.552  1.00 72.21      A    C  
ANISOU  608  C   PRO A  82     7668   9412  10356   2206   4603   5936  A    C  
ATOM    609  O   PRO A  82     -14.605  28.351  -1.674  1.00 73.31      A    O  
ANISOU  609  O   PRO A  82     7749   9732  10374   2322   4695   6137  A    O  
ATOM    610  CB  PRO A  82     -15.687  30.424   0.417  1.00 71.87      A    C  
ANISOU  610  CB  PRO A  82     7706   8743  10859   2742   5248   6460  A    C  
ATOM    611  CG  PRO A  82     -14.854  31.391  -0.399  1.00 77.98      A    C  
ANISOU  611  CG  PRO A  82     8564   9249  11816   2960   5622   6732  A    C  
ATOM    612  CD  PRO A  82     -13.406  31.051  -0.155  1.00 70.93      A    C  
ANISOU  612  CD  PRO A  82     7892   7898  11161   2627   5574   6278  A    C  
ATOM    613  N   LEU A  83     -15.806  27.090  -0.248  1.00 69.21      A    N  
ANISOU  613  N   LEU A  83     7198   9396   9703   1975   4267   5702  A    N  
ATOM    614  CA  LEU A  83     -16.215  26.085  -1.229  1.00 70.52      A    C  
ANISOU  614  CA  LEU A  83     7166  10235   9393   1837   3997   5666  A    C  
ATOM    615  C   LEU A  83     -17.756  26.114  -1.362  1.00 80.78      A    C  
ANISOU  615  C   LEU A  83     8162  12161  10370   1996   3937   5942  A    C  
ATOM    616  O   LEU A  83     -18.474  25.912  -0.376  1.00 79.07      A    O  
ANISOU  616  O   LEU A  83     7946  11894  10202   1911   3856   5817  A    O  
ATOM    617  CB  LEU A  83     -15.694  24.678  -0.869  1.00 66.89      A    C  
ANISOU  617  CB  LEU A  83     6861   9699   8856   1391   3682   5119  A    C  
ATOM    618  CG  LEU A  83     -16.376  23.485  -1.562  1.00 71.75      A    C  
ANISOU  618  CG  LEU A  83     7291  10986   8987   1163   3398   4984  A    C  
ATOM    619  CD1 LEU A  83     -15.891  23.319  -2.995  1.00 73.73      A    C  
ANISOU  619  CD1 LEU A  83     7442  11591   8982   1172   3381   5070  A    C  
ATOM    620  CD2 LEU A  83     -16.177  22.208  -0.771  1.00 69.60      A    C  
ANISOU  620  CD2 LEU A  83     7210  10527   8708    762   3157   4474  A    C  
ATOM    621  N   GLU A  84     -18.244  26.400  -2.586  1.00 83.54      A    N  
ANISOU  621  N   GLU A  84     8238  13121  10382   2245   3990   6328  A    N  
ATOM    622  CA  GLU A  84     -19.670  26.470  -2.923  1.00 87.24      A    C  
ANISOU  622  CA  GLU A  84     8353  14314  10479   2439   3939   6627  A    C  
ATOM    623  C   GLU A  84     -20.089  25.221  -3.688  1.00 94.50      A    C  
ANISOU  623  C   GLU A  84     9051  15961  10894   2136   3616   6397  A    C  
ATOM    624  O   GLU A  84     -19.437  24.861  -4.667  1.00 94.42      A    O  
ANISOU  624  O   GLU A  84     9025  16148  10704   2055   3561   6352  A    O  
ATOM    625  CB  GLU A  84     -19.996  27.726  -3.758  1.00 92.59      A    C  
ANISOU  625  CB  GLU A  84     8846  15243  11090   2983   4250   7258  A    C  
ATOM    626  CG  GLU A  84     -19.724  29.049  -3.068  1.00102.02      A    C  
ANISOU  626  CG  GLU A  84    10243  15753  12765   3312   4639   7530  A    C  
ATOM    627  CD  GLU A  84     -20.051  30.267  -3.906  1.00126.85      A    C  
ANISOU  627  CD  GLU A  84    13235  19129  15834   3876   4988   8179  A    C  
ATOM    628  OE1 GLU A  84     -21.175  30.799  -3.759  1.00119.73      A    O  
ANISOU  628  OE1 GLU A  84    12118  18574  14800   4207   5086   8534  A    O  
ATOM    629  OE2 GLU A  84     -19.187  30.687  -4.710  1.00123.35      A    O1-
ANISOU  629  OE2 GLU A  84    12882  18537  15446   4001   5173   8344  A    O1-
ATOM    630  N   ILE A  85     -21.170  24.563  -3.243  1.00 93.48      A    N  
ANISOU  630  N   ILE A  85     8753  16228  10537   1951   3421   6234  A    N  
ATOM    631  CA  ILE A  85     -21.722  23.373  -3.889  1.00 95.06      A    C  
ANISOU  631  CA  ILE A  85     8725  17146  10248   1619   3143   5978  A    C  
ATOM    632  C   ILE A  85     -23.136  23.671  -4.391  1.00104.63      A    C  
ANISOU  632  C   ILE A  85     9476  19240  11038   1863   3132   6322  A    C  
ATOM    633  O   ILE A  85     -23.998  24.075  -3.612  1.00104.83      A    O  
ANISOU  633  O   ILE A  85     9410  19281  11138   2004   3184   6452  A    O  
ATOM    634  CB  ILE A  85     -21.703  22.129  -2.961  1.00 94.98      A    C  
ANISOU  634  CB  ILE A  85     8923  16866  10299   1105   2925   5402  A    C  
ATOM    635  CG1 ILE A  85     -20.267  21.769  -2.526  1.00 91.51      A    C  
ANISOU  635  CG1 ILE A  85     8909  15644  10215    893   2923   5066  A    C  
ATOM    636  CG2 ILE A  85     -22.399  20.921  -3.624  1.00 97.61      A    C  
ANISOU  636  CG2 ILE A  85     9008  17960  10118    737   2688   5126  A    C  
ATOM    637  CD1 ILE A  85     -20.169  21.173  -1.124  1.00 96.25      A    C  
ANISOU  637  CD1 ILE A  85     9803  15670  11097    621   2847   4679  A    C  
ATOM    638  N   THR A  86     -23.356  23.409  -5.695  1.00105.53      A    N  
ANISOU  638  N   THR A  86     9288  20124  10686   1894   3053   6440  A    N  
ATOM    639  CA  THR A  86     -24.636  23.525  -6.382  1.00110.08      A    C  
ANISOU  639  CA  THR A  86     9364  21709  10753   2091   3002   6723  A    C  
ATOM    640  C   THR A  86     -25.383  22.215  -6.155  1.00115.04      A    C  
ANISOU  640  C   THR A  86     9840  22807  11062   1560   2726   6226  A    C  
ATOM    641  O   THR A  86     -24.902  21.151  -6.558  1.00113.48      A    O  
ANISOU  641  O   THR A  86     9740  22655  10721   1114   2564   5793  A    O  
ATOM    642  CB  THR A  86     -24.430  23.849  -7.872  1.00117.07      A    C  
ANISOU  642  CB  THR A  86    10002  23201  11276   2360   3053   7056  A    C  
ATOM    643  CG2 THR A  86     -25.744  24.006  -8.627  1.00120.63      A    C  
ANISOU  643  CG2 THR A  86     9895  24778  11159   2623   3006   7384  A    C  
ATOM    644  OG1 THR A  86     -23.668  25.049  -7.987  1.00115.26      A    O  
ANISOU  644  OG1 THR A  86     9986  22403  11403   2809   3351   7479  A    O  
ATOM    645  N   LEU A  87     -26.542  22.294  -5.490  1.00113.43      A    N  
ANISOU  645  N   LEU A  87     9415  22920  10763   1602   2699   6280  A    N  
ATOM    646  CA  LEU A  87     -27.379  21.134  -5.192  1.00113.57      A    C  
ANISOU  646  CA  LEU A  87     9272  23391  10490   1104   2481   5826  A    C  
ATOM    647  C   LEU A  87     -28.233  20.761  -6.412  1.00122.17      A    C  
ANISOU  647  C   LEU A  87     9825  25679  10913   1054   2353   5866  A    C  
ATOM    648  O   LEU A  87     -28.711  21.675  -7.090  1.00125.32      A    O  
ANISOU  648  O   LEU A  87     9882  26655  11079   1559   2449   6383  A    O  
ATOM    649  CB  LEU A  87     -28.276  21.430  -3.983  1.00113.25      A    C  
ANISOU  649  CB  LEU A  87     9203  23201  10627   1177   2522   5872  A    C  
ATOM    650  CG  LEU A  87     -27.576  21.488  -2.628  1.00113.18      A    C  
ANISOU  650  CG  LEU A  87     9702  22101  11200   1051   2588   5655  A    C  
ATOM    651  CD1 LEU A  87     -27.310  22.925  -2.209  1.00112.94      A    C  
ANISOU  651  CD1 LEU A  87     9810  21517  11584   1601   2845   6130  A    C  
ATOM    652  CD2 LEU A  87     -28.395  20.779  -1.572  1.00114.39      A    C  
ANISOU  652  CD2 LEU A  87     9854  22269  11341    692   2480   5306  A    C  
ATOM    653  N   PRO A  88     -28.455  19.447  -6.709  1.00119.04      A    N  
ANISOU  653  N   PRO A  88     9343  25698  10189    465   2158   5330  A    N  
ATOM    654  CA  PRO A  88     -29.303  19.082  -7.863  1.00123.82      A    C  
ANISOU  654  CA  PRO A  88     9401  27515  10129    379   2038   5321  A    C  
ATOM    655  C   PRO A  88     -30.742  19.588  -7.714  1.00132.02      A    C  
ANISOU  655  C   PRO A  88     9941  29350  10869    644   2037   5606  A    C  
ATOM    656  O   PRO A  88     -31.365  19.934  -8.719  1.00136.39      A    O  
ANISOU  656  O   PRO A  88     9999  30889  10934    929   2016   5913  A    O  
ATOM    657  CB  PRO A  88     -29.247  17.548  -7.881  1.00124.48      A    C  
ANISOU  657  CB  PRO A  88     9590  27667  10038   -374   1881   4613  A    C  
ATOM    658  CG  PRO A  88     -28.032  17.195  -7.099  1.00123.38      A    C  
ANISOU  658  CG  PRO A  88    10085  26340  10456   -578   1928   4343  A    C  
ATOM    659  CD  PRO A  88     -27.966  18.236  -6.021  1.00116.77      A    C  
ANISOU  659  CD  PRO A  88     9445  24820  10102   -144   2064   4710  A    C  
ATOM    660  N   PHE A  89     -31.249  19.666  -6.461  1.00127.44      A    N  
ANISOU  660  N   PHE A  89     9488  28358  10577    586   2065   5526  A    N  
ATOM    661  CA  PHE A  89     -32.581  20.182  -6.125  1.00130.78      A    C  
ANISOU  661  CA  PHE A  89     9487  29410  10792    846   2082   5787  A    C  
ATOM    662  C   PHE A  89     -32.485  21.164  -4.940  1.00132.47      A    C  
ANISOU  662  C   PHE A  89     9999  28771  11564   1248   2264   6111  A    C  
ATOM    663  O   PHE A  89     -31.626  21.010  -4.067  1.00126.83      A    O  
ANISOU  663  O   PHE A  89     9809  27020  11360   1071   2311   5894  A    O  
ATOM    664  CB  PHE A  89     -33.598  19.053  -5.870  1.00134.22      A    C  
ANISOU  664  CB  PHE A  89     9664  30451  10884    248   1918   5260  A    C  
ATOM    665  CG  PHE A  89     -33.295  18.061  -4.771  1.00131.54      A    C  
ANISOU  665  CG  PHE A  89     9786  29306  10887   -348   1881   4682  A    C  
ATOM    666  CD1 PHE A  89     -34.017  18.074  -3.584  1.00133.64      A    C  
ANISOU  666  CD1 PHE A  89    10091  29347  11340   -432   1907   4594  A    C  
ATOM    667  CD2 PHE A  89     -32.348  17.058  -4.957  1.00131.08      A    C  
ANISOU  667  CD2 PHE A  89    10100  28786  10919   -831   1828   4218  A    C  
ATOM    668  CE1 PHE A  89     -33.763  17.132  -2.581  1.00130.98      A    C  
ANISOU  668  CE1 PHE A  89    10178  28302  11285   -967   1888   4077  A    C  
ATOM    669  CE2 PHE A  89     -32.089  16.123  -3.951  1.00130.38      A    C  
ANISOU  669  CE2 PHE A  89    10442  27978  11120  -1343   1819   3713  A    C  
ATOM    670  CZ  PHE A  89     -32.799  16.165  -2.770  1.00127.56      A    C  
ANISOU  670  CZ  PHE A  89    10130  27392  10946  -1405   1850   3651  A    C  
ATOM    671  N   SER A  90     -33.358  22.191  -4.947  1.00133.60      A    N  
ANISOU  671  N   SER A  90     9792  29385  11586   1812   2378   6639  A    N  
ATOM    672  CA  SER A  90     -33.409  23.307  -3.992  1.00132.64      A    C  
ANISOU  672  CA  SER A  90     9867  28606  11923   2297   2598   7040  A    C  
ATOM    673  C   SER A  90     -33.909  22.957  -2.549  1.00134.79      A    C  
ANISOU  673  C   SER A  90    10326  28397  12491   2000   2574   6724  A    C  
ATOM    674  O   SER A  90     -33.868  23.837  -1.680  1.00132.80      A    O  
ANISOU  674  O   SER A  90    10297  27495  12666   2347   2762   6993  A    O  
ATOM    675  CB  SER A  90     -34.250  24.450  -4.560  1.00141.34      A    C  
ANISOU  675  CB  SER A  90    10501  30469  12733   2998   2741   7703  A    C  
ATOM    676  OG  SER A  90     -35.473  24.004  -5.126  1.00152.88      A    O  
ANISOU  676  OG  SER A  90    11475  32945  13667   2842   2557   7520  A    O  
ATOM    677  N   LEU A  91     -34.350  21.697  -2.292  1.00131.47      A    N  
ANISOU  677  N   LEU A  91     9832  28267  11853   1363   2372   6157  A    N  
ATOM    678  CA  LEU A  91     -34.831  21.186  -0.986  1.00129.23      A    C  
ANISOU  678  CA  LEU A  91     9720  27590  11791   1010   2340   5805  A    C  
ATOM    679  C   LEU A  91     -36.100  21.911  -0.465  1.00136.95      A    C  
ANISOU  679  C   LEU A  91    10339  29013  12684   1381   2422   6138  A    C  
ATOM    680  O   LEU A  91     -36.587  22.856  -1.090  1.00140.75      A    O  
ANISOU  680  O   LEU A  91    10475  30028  12976   1967   2527   6681  A    O  
ATOM    681  CB  LEU A  91     -33.734  21.258   0.111  1.00123.52      A    C  
ANISOU  681  CB  LEU A  91     9652  25562  11716    924   2431   5649  A    C  
ATOM    682  CG  LEU A  91     -32.413  20.527  -0.111  1.00124.58      A    C  
ANISOU  682  CG  LEU A  91    10218  25087  12031    574   2370   5301  A    C  
ATOM    683  CD1 LEU A  91     -31.318  21.183   0.688  1.00120.39      A    C  
ANISOU  683  CD1 LEU A  91    10203  23432  12106    781   2517   5398  A    C  
ATOM    684  CD2 LEU A  91     -32.510  19.069   0.296  1.00125.75      A    C  
ANISOU  684  CD2 LEU A  91    10505  25212  12063   -132   2214   4661  A    C  
ATOM    685  N   THR A  92     -36.632  21.448   0.686  1.00132.09      A    N  
ANISOU  685  N   THR A  92     9813  28176  12199   1048   2387   5817  A    N  
ATOM    686  CA  THR A  92     -37.793  22.037   1.365  1.00134.48      A    C  
ANISOU  686  CA  THR A  92     9829  28796  12470   1334   2464   6062  A    C  
ATOM    687  C   THR A  92     -37.511  22.047   2.883  1.00133.88      A    C  
ANISOU  687  C   THR A  92    10242  27682  12945   1194   2547   5871  A    C  
ATOM    688  O   THR A  92     -37.841  21.082   3.572  1.00132.48      A    O  
ANISOU  688  O   THR A  92    10160  27422  12756    655   2447   5393  A    O  
ATOM    689  CB  THR A  92     -39.124  21.317   0.996  1.00147.16      A    C  
ANISOU  689  CB  THR A  92    10847  31587  13482   1029   2311   5841  A    C  
ATOM    690  CG2 THR A  92     -39.671  21.729  -0.368  1.00151.20      A    C  
ANISOU  690  CG2 THR A  92    10767  33260  13424   1369   2267   6184  A    C  
ATOM    691  OG1 THR A  92     -38.961  19.898   1.058  1.00145.13      A    O  
ANISOU  691  OG1 THR A  92    10745  31271  13127    251   2161   5172  A    O  
ATOM    692  N   ARG A  93     -36.882  23.141   3.389  1.00127.64      A    N  
ANISOU  692  N   ARG A  93     9767  26101  12629   1672   2749   6236  A    N  
ATOM    693  CA  ARG A  93     -36.482  23.376   4.800  1.00122.64      A    C  
ANISOU  693  CA  ARG A  93     9605  24447  12545   1634   2858   6117  A    C  
ATOM    694  C   ARG A  93     -37.571  22.914   5.798  1.00124.12      A    C  
ANISOU  694  C   ARG A  93     9663  24834  12665   1361   2804   5869  A    C  
ATOM    695  O   ARG A  93     -38.735  23.240   5.573  1.00127.73      A    O  
ANISOU  695  O   ARG A  93     9637  26096  12799   1583   2815   6100  A    O  
ATOM    696  CB  ARG A  93     -36.177  24.878   5.020  1.00123.75      A    C  
ANISOU  696  CB  ARG A  93     9869  24097  13054   2307   3134   6664  A    C  
ATOM    697  CG  ARG A  93     -36.338  25.360   6.471  1.00131.50      A    C  
ANISOU  697  CG  ARG A  93    11120  24370  14475   2390   3280   6648  A    C  
ATOM    698  CD  ARG A  93     -37.447  26.374   6.666  1.00144.85      A    C  
ANISOU  698  CD  ARG A  93    12469  26474  16094   2918   3458   7110  A    C  
ATOM    699  NE  ARG A  93     -37.491  26.841   8.053  1.00152.12      A    N  
ANISOU  699  NE  ARG A  93    13685  26654  17460   2985   3613   7074  A    N  
ATOM    700  CZ  ARG A  93     -37.590  28.116   8.419  1.00169.14      A    C  
ANISOU  700  CZ  ARG A  93    15900  28462  19904   3537   3909   7505  A    C  
ATOM    701  NH1 ARG A  93     -37.666  29.074   7.504  1.00162.58      A    N1+
ANISOU  701  NH1 ARG A  93    14865  27938  18968   4105   4100   8043  A    N1+
ATOM    702  NH2 ARG A  93     -37.616  28.442   9.705  1.00153.51      A    N  
ANISOU  702  NH2 ARG A  93    14193  25822  18314   3532   4037   7405  A    N  
ATOM    703  N   GLY A  94     -37.244  22.191   6.880  1.00114.80      A    N  
ANISOU  703  N   GLY A  94     8881  22978  11759    914   2757   5425  A    N  
ATOM    704  CA  GLY A  94     -35.927  21.722   7.288  1.00108.63      A    C  
ANISOU  704  CA  GLY A  94     8661  21273  11341    644   2737   5122  A    C  
ATOM    705  C   GLY A  94     -35.661  20.307   6.833  1.00109.74      A    C  
ANISOU  705  C   GLY A  94     8876  21589  11232     31   2554   4621  A    C  
ATOM    706  O   GLY A  94     -35.661  19.377   7.646  1.00106.48      A    O  
ANISOU  706  O   GLY A  94     8726  20822  10909   -421   2502   4196  A    O  
ATOM    707  N   GLN A  95     -35.472  20.148   5.509  1.00107.90      A    N  
ANISOU  707  N   GLN A  95     8406  21926  10665     29   2477   4681  A    N  
ATOM    708  CA  GLN A  95     -35.183  18.893   4.817  1.00107.39      A    C  
ANISOU  708  CA  GLN A  95     8371  22113  10321   -512   2330   4242  A    C  
ATOM    709  C   GLN A  95     -33.702  18.547   4.945  1.00106.03      A    C  
ANISOU  709  C   GLN A  95     8745  21049  10493   -646   2331   4045  A    C  
ATOM    710  O   GLN A  95     -32.841  19.435   4.934  1.00103.29      A    O  
ANISOU  710  O   GLN A  95     8589  20204  10453   -246   2425   4345  A    O  
ATOM    711  CB  GLN A  95     -35.581  18.975   3.330  1.00113.09      A    C  
ANISOU  711  CB  GLN A  95     8588  23846  10535   -405   2258   4421  A    C  
ATOM    712  CG  GLN A  95     -35.914  17.621   2.704  1.00128.62      A    C  
ANISOU  712  CG  GLN A  95    10412  26376  12080  -1034   2117   3919  A    C  
ATOM    713  CD  GLN A  95     -36.429  17.727   1.291  1.00152.51      A    C  
ANISOU  713  CD  GLN A  95    12880  30507  14561   -929   2042   4082  A    C  
ATOM    714  NE2 GLN A  95     -37.583  17.132   1.039  1.00149.43      A    N  
ANISOU  714  NE2 GLN A  95    12046  31020  13711  -1265   1964   3841  A    N  
ATOM    715  OE1 GLN A  95     -35.782  18.288   0.402  1.00147.83      A    O  
ANISOU  715  OE1 GLN A  95    12245  29988  13935   -577   2056   4395  A    O  
ATOM    716  N   GLU A  96     -33.418  17.247   5.062  1.00100.70      A    N  
ANISOU  716  N   GLU A  96     8316  20188   9756  -1212   2249   3534  A    N  
ATOM    717  CA  GLU A  96     -32.066  16.727   5.196  1.00 96.05      A    C  
ANISOU  717  CA  GLU A  96     8233  18818   9443  -1380   2241   3297  A    C  
ATOM    718  C   GLU A  96     -31.646  15.987   3.928  1.00101.12      A    C  
ANISOU  718  C   GLU A  96     8798  19858   9766  -1644   2156   3104  A    C  
ATOM    719  O   GLU A  96     -32.470  15.323   3.293  1.00103.69      A    O  
ANISOU  719  O   GLU A  96     8792  20946   9659  -1964   2091   2907  A    O  
ATOM    720  CB  GLU A  96     -31.944  15.825   6.433  1.00 94.19      A    C  
ANISOU  720  CB  GLU A  96     8418  17945   9427  -1765   2253   2887  A    C  
ATOM    721  CG  GLU A  96     -31.867  16.607   7.736  1.00 95.20      A    C  
ANISOU  721  CG  GLU A  96     8762  17437   9974  -1467   2345   3065  A    C  
ATOM    722  CD  GLU A  96     -31.447  15.850   8.982  1.00 97.61      A    C  
ANISOU  722  CD  GLU A  96     9543  17003  10543  -1750   2365   2716  A    C  
ATOM    723  OE1 GLU A  96     -31.268  14.614   8.903  1.00 60.70      A    O  
ANISOU  723  OE1 GLU A  96     5064  12267   5730  -2202   2328   2320  A    O  
ATOM    724  OE2 GLU A  96     -31.315  16.492  10.049  1.00 92.05      A    O1-
ANISOU  724  OE2 GLU A  96     9016  15788  10172  -1512   2437   2841  A    O1-
ATOM    725  N   VAL A  97     -30.361  16.139   3.550  1.00 94.88      A    N  
ANISOU  725  N   VAL A  97     8294  18572   9185  -1510   2166   3153  A    N  
ATOM    726  CA  VAL A  97     -29.758  15.519   2.369  1.00 95.27      A    C  
ANISOU  726  CA  VAL A  97     8328  18878   8990  -1714   2101   2990  A    C  
ATOM    727  C   VAL A  97     -28.336  15.048   2.727  1.00 94.44      A    C  
ANISOU  727  C   VAL A  97     8773  17881   9231  -1824   2117   2763  A    C  
ATOM    728  O   VAL A  97     -27.760  15.545   3.698  1.00 91.28      A    O  
ANISOU  728  O   VAL A  97     8679  16757   9246  -1610   2180   2855  A    O  
ATOM    729  CB  VAL A  97     -29.794  16.486   1.147  1.00101.95      A    C  
ANISOU  729  CB  VAL A  97     8781  20336   9621  -1290   2102   3436  A    C  
ATOM    730  CG1 VAL A  97     -28.738  17.594   1.241  1.00 99.32      A    C  
ANISOU  730  CG1 VAL A  97     8673  19373   9692   -794   2207   3813  A    C  
ATOM    731  CG2 VAL A  97     -29.689  15.724  -0.170  1.00104.22      A    C  
ANISOU  731  CG2 VAL A  97     8884  21232   9485  -1579   2013   3228  A    C  
ATOM    732  N   ILE A  98     -27.784  14.085   1.966  1.00 90.13      A    N  
ANISOU  732  N   ILE A  98     8340  17405   8499  -2161   2069   2452  A    N  
ATOM    733  CA  ILE A  98     -26.423  13.591   2.210  1.00 86.06      A    C  
ANISOU  733  CA  ILE A  98     8318  16116   8266  -2251   2086   2238  A    C  
ATOM    734  C   ILE A  98     -25.483  14.108   1.112  1.00 86.84      A    C  
ANISOU  734  C   ILE A  98     8371  16263   8362  -1989   2078   2457  A    C  
ATOM    735  O   ILE A  98     -25.713  13.858  -0.073  1.00 88.44      A    O  
ANISOU  735  O   ILE A  98     8287  17120   8196  -2086   2031   2454  A    O  
ATOM    736  CB  ILE A  98     -26.342  12.043   2.345  1.00 89.36      A    C  
ANISOU  736  CB  ILE A  98     9002  16406   8543  -2818   2084   1701  A    C  
ATOM    737  CG1 ILE A  98     -27.477  11.452   3.231  1.00 90.85      A    C  
ANISOU  737  CG1 ILE A  98     9173  16693   8651  -3132   2117   1473  A    C  
ATOM    738  CG2 ILE A  98     -24.928  11.575   2.777  1.00 86.22      A    C  
ANISOU  738  CG2 ILE A  98     9134  15168   8456  -2844   2116   1510  A    C  
ATOM    739  CD1 ILE A  98     -27.536  11.896   4.712  1.00 94.75      A    C  
ANISOU  739  CD1 ILE A  98     9908  16569   9525  -2939   2164   1572  A    C  
ATOM    740  N   VAL A  99     -24.428  14.825   1.530  1.00 79.05      A    N  
ANISOU  740  N   VAL A  99     7658  14599   7778  -1672   2133   2632  A    N  
ATOM    741  CA  VAL A  99     -23.410  15.396   0.648  1.00 78.02      A    C  
ANISOU  741  CA  VAL A  99     7541  14381   7721  -1408   2158   2843  A    C  
ATOM    742  C   VAL A  99     -22.088  14.657   0.890  1.00 77.56      A    C  
ANISOU  742  C   VAL A  99     7932  13665   7873  -1589   2151   2524  A    C  
ATOM    743  O   VAL A  99     -21.506  14.755   1.972  1.00 73.03      A    O  
ANISOU  743  O   VAL A  99     7680  12413   7654  -1526   2187   2447  A    O  
ATOM    744  CB  VAL A  99     -23.266  16.935   0.830  1.00 81.23      A    C  
ANISOU  744  CB  VAL A  99     7861  14589   8413   -878   2270   3325  A    C  
ATOM    745  CG1 VAL A  99     -22.255  17.518  -0.158  1.00 80.88      A    C  
ANISOU  745  CG1 VAL A  99     7826  14476   8430   -626   2328   3544  A    C  
ATOM    746  CG2 VAL A  99     -24.621  17.640   0.705  1.00 84.04      A    C  
ANISOU  746  CG2 VAL A  99     7790  15580   8563   -659   2298   3657  A    C  
ATOM    747  N   GLU A 100     -21.648  13.893  -0.113  1.00 75.53      A    N  
ANISOU  747  N   GLU A 100     7678  13647   7371  -1811   2107   2330  A    N  
ATOM    748  CA  GLU A 100     -20.395  13.132  -0.082  1.00 73.28      A    C  
ANISOU  748  CA  GLU A 100     7786  12831   7227  -1968   2108   2036  A    C  
ATOM    749  C   GLU A 100     -19.275  13.979  -0.712  1.00 71.40      A    C  
ANISOU  749  C   GLU A 100     7563  12406   7160  -1635   2145   2288  A    C  
ATOM    750  O   GLU A 100     -19.453  14.467  -1.827  1.00 72.88      A    O  
ANISOU  750  O   GLU A 100     7450  13118   7124  -1503   2144   2521  A    O  
ATOM    751  CB  GLU A 100     -20.581  11.810  -0.834  1.00 77.31      A    C  
ANISOU  751  CB  GLU A 100     8299  13704   7371  -2418   2071   1660  A    C  
ATOM    752  CG  GLU A 100     -19.809  10.636  -0.259  1.00 92.50      A    C  
ANISOU  752  CG  GLU A 100    10688  15040   9417  -2709   2104   1242  A    C  
ATOM    753  CD  GLU A 100     -19.812   9.457  -1.212  1.00127.43      A    C  
ANISOU  753  CD  GLU A 100    15135  19782  13500  -3123   2115    888  A    C  
ATOM    754  OE1 GLU A 100     -19.002   9.461  -2.168  1.00123.22      A    O  
ANISOU  754  OE1 GLU A 100    14626  19282  12910  -3078   2109    882  A    O  
ATOM    755  OE2 GLU A 100     -20.649   8.542  -1.026  1.00129.55      A    O1-
ANISOU  755  OE2 GLU A 100    15397  20269  13556  -3509   2149    603  A    O1-
ATOM    756  N   ILE A 101     -18.156  14.204   0.008  1.00 61.97      A    N  
ANISOU  756  N   ILE A 101     6694  10500   6350  -1488   2188   2254  A    N  
ATOM    757  CA  ILE A 101     -17.043  15.005  -0.520  1.00 60.12      A    C  
ANISOU  757  CA  ILE A 101     6488  10048   6305  -1203   2247   2459  A    C  
ATOM    758  C   ILE A 101     -15.720  14.246  -0.379  1.00 61.03      A    C  
ANISOU  758  C   ILE A 101     6965   9657   6565  -1328   2234   2148  A    C  
ATOM    759  O   ILE A 101     -15.376  13.789   0.712  1.00 58.43      A    O  
ANISOU  759  O   ILE A 101     6927   8832   6443  -1398   2228   1930  A    O  
ATOM    760  CB  ILE A 101     -16.927  16.439   0.098  1.00 61.52      A    C  
ANISOU  760  CB  ILE A 101     6624   9919   6832   -810   2361   2809  A    C  
ATOM    761  CG1 ILE A 101     -18.248  17.223   0.002  1.00 63.42      A    C  
ANISOU  761  CG1 ILE A 101     6515  10646   6936   -631   2399   3149  A    C  
ATOM    762  CG2 ILE A 101     -15.773  17.237  -0.572  1.00 60.44      A    C  
ANISOU  762  CG2 ILE A 101     6511   9581   6872   -558   2460   2999  A    C  
ATOM    763  CD1 ILE A 101     -18.316  18.432   0.888  1.00 66.96      A    C  
ANISOU  763  CD1 ILE A 101     6979  10726   7736   -309   2533   3417  A    C  
ATOM    764  N   ASP A 102     -14.965  14.157  -1.486  1.00 56.71      A    N  
ANISOU  764  N   ASP A 102     6388   9255   5902  -1322   2237   2150  A    N  
ATOM    765  CA  ASP A 102     -13.646  13.535  -1.508  1.00 54.26      A    C  
ANISOU  765  CA  ASP A 102     6380   8521   5713  -1391   2236   1896  A    C  
ATOM    766  C   ASP A 102     -12.591  14.640  -1.545  1.00 52.37      A    C  
ANISOU  766  C   ASP A 102     6156   7960   5783  -1067   2320   2120  A    C  
ATOM    767  O   ASP A 102     -12.517  15.395  -2.516  1.00 52.47      A    O  
ANISOU  767  O   ASP A 102     5948   8263   5727   -895   2377   2397  A    O  
ATOM    768  CB  ASP A 102     -13.500  12.565  -2.696  1.00 58.74      A    C  
ANISOU  768  CB  ASP A 102     6926   9454   5941  -1643   2198   1696  A    C  
ATOM    769  CG  ASP A 102     -14.347  11.312  -2.588  1.00 81.37      A    C  
ANISOU  769  CG  ASP A 102     9857  12526   8534  -2032   2157   1372  A    C  
ATOM    770  OD1 ASP A 102     -14.269  10.626  -1.540  1.00 82.58      A    O  
ANISOU  770  OD1 ASP A 102    10308  12243   8826  -2156   2167   1131  A    O  
ATOM    771  OD2 ASP A 102     -15.054  10.988  -3.567  1.00 93.82      A    O1-
ANISOU  771  OD2 ASP A 102    11192  14705   9748  -2222   2133   1343  A    O1-
ATOM    772  N   SER A 103     -11.822  14.764  -0.457  1.00 43.42      A    N  
ANISOU  772  N   SER A 103     5271   6247   4981   -983   2344   2002  A    N  
ATOM    773  CA  SER A 103     -10.779  15.772  -0.304  1.00 40.08      A    C  
ANISOU  773  CA  SER A 103     4879   5470   4878   -726   2444   2139  A    C  
ATOM    774  C   SER A 103      -9.433  15.154   0.085  1.00 40.39      A    C  
ANISOU  774  C   SER A 103     5203   5074   5070   -770   2421   1835  A    C  
ATOM    775  O   SER A 103      -9.338  13.944   0.285  1.00 38.79      A    O  
ANISOU  775  O   SER A 103     5198   4810   4731   -968   2339   1545  A    O  
ATOM    776  CB  SER A 103     -11.200  16.807   0.735  1.00 41.08      A    C  
ANISOU  776  CB  SER A 103     4961   5364   5282   -534   2526   2326  A    C  
ATOM    777  OG  SER A 103     -11.142  16.315   2.065  1.00 45.18      A    O  
ANISOU  777  OG  SER A 103     5705   5512   5951   -614   2473   2080  A    O  
ATOM    778  N   VAL A 104      -8.385  15.994   0.141  1.00 36.51      A    N  
ANISOU  778  N   VAL A 104     4725   4299   4848   -579   2515   1907  A    N  
ATOM    779  CA  VAL A 104      -7.032  15.643   0.576  1.00 34.19      A    C  
ANISOU  779  CA  VAL A 104     4644   3622   4723   -565   2506   1648  A    C  
ATOM    780  C   VAL A 104      -6.394  16.918   1.152  1.00 37.77      A    C  
ANISOU  780  C   VAL A 104     5054   3764   5535   -361   2639   1758  A    C  
ATOM    781  O   VAL A 104      -6.553  18.007   0.589  1.00 38.38      A    O  
ANISOU  781  O   VAL A 104     4948   3937   5696   -226   2777   2046  A    O  
ATOM    782  CB  VAL A 104      -6.139  14.923  -0.496  1.00 38.33      A    C  
ANISOU  782  CB  VAL A 104     5225   4261   5079   -644   2479   1510  A    C  
ATOM    783  CG1 VAL A 104      -5.822  15.801  -1.705  1.00 39.39      A    C  
ANISOU  783  CG1 VAL A 104     5150   4616   5202   -530   2584   1768  A    C  
ATOM    784  CG2 VAL A 104      -4.859  14.371   0.124  1.00 36.33      A    C  
ANISOU  784  CG2 VAL A 104     5200   3639   4965   -621   2454   1217  A    C  
ATOM    785  N   THR A 105      -5.715  16.775   2.299  1.00 34.36      A    N  
ANISOU  785  N   THR A 105     4787   2969   5298   -340   2617   1524  A    N  
ATOM    786  CA  THR A 105      -5.015  17.858   2.999  1.00 34.43      A    C  
ANISOU  786  CA  THR A 105     4769   2670   5641   -201   2744   1528  A    C  
ATOM    787  C   THR A 105      -3.709  18.198   2.287  1.00 40.13      A    C  
ANISOU  787  C   THR A 105     5460   3331   6457   -151   2830   1479  A    C  
ATOM    788  O   THR A 105      -3.251  17.464   1.410  1.00 42.09      A    O  
ANISOU  788  O   THR A 105     5743   3733   6515   -214   2764   1402  A    O  
ATOM    789  CB  THR A 105      -4.723  17.472   4.484  1.00 41.08      A    C  
ANISOU  789  CB  THR A 105     5780   3223   6604   -205   2669   1258  A    C  
ATOM    790  CG2 THR A 105      -5.957  17.108   5.262  1.00 35.12      A    C  
ANISOU  790  CG2 THR A 105     5075   2500   5770   -260   2596   1288  A    C  
ATOM    791  OG1 THR A 105      -3.773  16.402   4.549  1.00 40.34      A    O  
ANISOU  791  OG1 THR A 105     5856   3068   6403   -247   2560    978  A    O  
ATOM    792  N   SER A 106      -3.110  19.315   2.679  1.00 35.42      A    N  
ANISOU  792  N   SER A 106     4798   2503   6158    -55   2998   1505  A    N  
ATOM    793  CA  SER A 106      -1.801  19.727   2.227  1.00 35.50      A    C  
ANISOU  793  CA  SER A 106     4774   2411   6303    -27   3108   1414  A    C  
ATOM    794  C   SER A 106      -0.809  19.295   3.310  1.00 39.15      A    C  
ANISOU  794  C   SER A 106     5347   2657   6871    -43   3027   1046  A    C  
ATOM    795  O   SER A 106      -1.216  19.273   4.474  1.00 37.64      A    O  
ANISOU  795  O   SER A 106     5213   2332   6757    -36   2982    954  A    O  
ATOM    796  CB  SER A 106      -1.770  21.237   1.984  1.00 40.58      A    C  
ANISOU  796  CB  SER A 106     5280   2935   7205     66   3385   1654  A    C  
ATOM    797  OG  SER A 106      -0.470  21.697   1.660  1.00 55.09      A    O  
ANISOU  797  OG  SER A 106     7086   4643   9204     64   3524   1532  A    O  
ATOM    798  N   PRO A 107       0.474  18.940   3.006  1.00 37.71      A    N  
ANISOU  798  N   PRO A 107     5184   2463   6680    -47   3008    832  A    N  
ATOM    799  CA  PRO A 107       1.403  18.566   4.097  1.00 37.53      A    C  
ANISOU  799  CA  PRO A 107     5231   2296   6731    -24   2930    492  A    C  
ATOM    800  C   PRO A 107       1.667  19.722   5.084  1.00 43.17      A    C  
ANISOU  800  C   PRO A 107     5849   2803   7748     -9   3083    410  A    C  
ATOM    801  O   PRO A 107       2.163  19.493   6.186  1.00 42.47      A    O  
ANISOU  801  O   PRO A 107     5797   2637   7703     14   3010    145  A    O  
ATOM    802  CB  PRO A 107       2.694  18.186   3.354  1.00 39.77      A    C  
ANISOU  802  CB  PRO A 107     5499   2659   6953    -16   2924    334  A    C  
ATOM    803  CG  PRO A 107       2.301  18.006   1.926  1.00 44.45      A    C  
ANISOU  803  CG  PRO A 107     6070   3442   7378    -55   2944    566  A    C  
ATOM    804  CD  PRO A 107       1.151  18.913   1.691  1.00 39.98      A    C  
ANISOU  804  CD  PRO A 107     5412   2895   6883    -57   3062    890  A    C  
ATOM    805  N   LYS A 108       1.322  20.954   4.678  1.00 42.05      A    N  
ANISOU  805  N   LYS A 108     5591   2583   7802    -14   3313    640  A    N  
ATOM    806  CA  LYS A 108       1.492  22.188   5.449  1.00 43.35      A    C  
ANISOU  806  CA  LYS A 108     5673   2521   8278    -26   3531    587  A    C  
ATOM    807  C   LYS A 108       0.259  22.497   6.325  1.00 47.80      A    C  
ANISOU  807  C   LYS A 108     6272   2989   8901      0   3537    717  A    C  
ATOM    808  O   LYS A 108       0.269  23.502   7.032  1.00 49.12      A    O  
ANISOU  808  O   LYS A 108     6386   2952   9326    -11   3737    686  A    O  
ATOM    809  CB  LYS A 108       1.776  23.371   4.503  1.00 46.63      A    C  
ANISOU  809  CB  LYS A 108     5977   2855   8886    -31   3838    788  A    C  
ATOM    810  CG  LYS A 108       3.011  23.195   3.618  1.00 62.94      A    C  
ANISOU  810  CG  LYS A 108     7991   5004  10918    -68   3870    662  A    C  
ATOM    811  CD  LYS A 108       4.273  23.818   4.178  1.00 68.06      A    C  
ANISOU  811  CD  LYS A 108     8550   5507  11802   -151   4027    331  A    C  
ATOM    812  CE  LYS A 108       5.435  23.452   3.294  1.00 65.85      A    C  
ANISOU  812  CE  LYS A 108     8218   5365  11435   -179   4007    198  A    C  
ATOM    813  NZ  LYS A 108       6.733  23.895   3.864  1.00 71.90      A    N1+
ANISOU  813  NZ  LYS A 108     8866   6064  12388   -277   4135   -171  A    N1+
ATOM    814  N   SER A 109      -0.808  21.654   6.255  1.00 43.34      A    N  
ANISOU  814  N   SER A 109     5794   2571   8102     20   3341    850  A    N  
ATOM    815  CA  SER A 109      -2.073  21.794   7.005  1.00 42.06      A    C  
ANISOU  815  CA  SER A 109     5663   2368   7950     42   3320    981  A    C  
ATOM    816  C   SER A 109      -1.833  22.403   8.411  1.00 46.64      A    C  
ANISOU  816  C   SER A 109     6244   2718   8761     35   3396    759  A    C  
ATOM    817  O   SER A 109      -1.096  21.825   9.216  1.00 45.56      A    O  
ANISOU  817  O   SER A 109     6162   2565   8583     17   3261    446  A    O  
ATOM    818  CB  SER A 109      -2.785  20.443   7.123  1.00 42.01      A    C  
ANISOU  818  CB  SER A 109     5782   2536   7645     13   3060    962  A    C  
ATOM    819  OG  SER A 109      -3.900  20.468   8.003  1.00 40.96      A    O  
ANISOU  819  OG  SER A 109     5684   2365   7514     18   3024   1029  A    O  
ATOM    820  N   SER A 110      -2.431  23.583   8.677  1.00 43.03      A    N  
ANISOU  820  N   SER A 110     5719   2097   8533     63   3629    925  A    N  
ATOM    821  CA  SER A 110      -2.304  24.289   9.948  1.00 43.06      A    C  
ANISOU  821  CA  SER A 110     5712   1879   8769     37   3748    725  A    C  
ATOM    822  C   SER A 110      -2.794  23.446  11.161  1.00 45.00      A    C  
ANISOU  822  C   SER A 110     6056   2162   8880     37   3514    559  A    C  
ATOM    823  O   SER A 110      -2.257  23.586  12.261  1.00 45.57      A    O  
ANISOU  823  O   SER A 110     6127   2135   9054      6   3517    269  A    O  
ATOM    824  CB  SER A 110      -3.043  25.623   9.896  1.00 47.55      A    C  
ANISOU  824  CB  SER A 110     6221   2260   9584     86   4062    988  A    C  
ATOM    825  OG  SER A 110      -4.415  25.490   9.550  1.00 49.80      A    O  
ANISOU  825  OG  SER A 110     6514   2670   9737    181   4017   1340  A    O  
ATOM    826  N   ALA A 111      -3.748  22.532  10.952  1.00 39.51      A    N  
ANISOU  826  N   ALA A 111     5442   1631   7937     61   3319    721  A    N  
ATOM    827  CA  ALA A 111      -4.272  21.677  12.019  1.00 36.41      A    C  
ANISOU  827  CA  ALA A 111     5168   1265   7401     58   3122    594  A    C  
ATOM    828  C   ALA A 111      -3.327  20.546  12.434  1.00 35.89      A    C  
ANISOU  828  C   ALA A 111     5212   1262   7162     59   2918    295  A    C  
ATOM    829  O   ALA A 111      -3.431  20.050  13.560  1.00 32.81      A    O  
ANISOU  829  O   ALA A 111     4825   1019   6623     80   2809    121  A    O  
ATOM    830  CB  ALA A 111      -5.587  21.062  11.574  1.00 36.57      A    C  
ANISOU  830  CB  ALA A 111     5233   1447   7216     52   3020    854  A    C  
ATOM    831  N   LEU A 112      -2.455  20.095  11.533  1.00 33.40      A    N  
ANISOU  831  N   LEU A 112     4891   1050   6748     56   2873    246  A    N  
ATOM    832  CA  LEU A 112      -1.655  18.907  11.835  1.00 33.36      A    C  
ANISOU  832  CA  LEU A 112     5011   1114   6549     96   2689      8  A    C  
ATOM    833  C   LEU A 112      -0.162  19.176  11.985  1.00 37.30      A    C  
ANISOU  833  C   LEU A 112     5417   1619   7137    128   2724   -260  A    C  
ATOM    834  O   LEU A 112       0.339  20.166  11.488  1.00 36.53      A    O  
ANISOU  834  O   LEU A 112     5169   1475   7237     80   2899   -250  A    O  
ATOM    835  CB  LEU A 112      -1.867  17.836  10.737  1.00 32.89      A    C  
ANISOU  835  CB  LEU A 112     5058   1198   6242     71   2580    128  A    C  
ATOM    836  CG  LEU A 112      -3.295  17.566  10.244  1.00 35.24      A    C  
ANISOU  836  CG  LEU A 112     5395   1578   6416     -2   2559    391  A    C  
ATOM    837  CD1 LEU A 112      -3.281  16.879   8.891  1.00 34.98      A    C  
ANISOU  837  CD1 LEU A 112     5382   1722   6189    -60   2519    495  A    C  
ATOM    838  CD2 LEU A 112      -4.095  16.800  11.242  1.00 35.76      A    C  
ANISOU  838  CD2 LEU A 112     5623   1610   6355    -10   2449    336  A    C  
ATOM    839  N   GLN A 113       0.538  18.260  12.671  1.00 34.79      A    N  
ANISOU  839  N   GLN A 113     5189   1371   6659    218   2572   -498  A    N  
ATOM    840  CA  GLN A 113       1.982  18.297  12.862  1.00 36.13      A    C  
ANISOU  840  CA  GLN A 113     5257   1628   6842    276   2566   -778  A    C  
ATOM    841  C   GLN A 113       2.519  16.895  12.559  1.00 37.15      A    C  
ANISOU  841  C   GLN A 113     5541   1878   6696    395   2400   -841  A    C  
ATOM    842  O   GLN A 113       2.128  15.948  13.233  1.00 33.93      A    O  
ANISOU  842  O   GLN A 113     5317   1468   6108    491   2279   -859  A    O  
ATOM    843  CB  GLN A 113       2.352  18.795  14.287  1.00 39.30      A    C  
ANISOU  843  CB  GLN A 113     5567   2030   7335    309   2578  -1036  A    C  
ATOM    844  CG  GLN A 113       3.755  18.416  14.788  1.00 55.80      A    C  
ANISOU  844  CG  GLN A 113     7568   4312   9323    419   2498  -1363  A    C  
ATOM    845  CD  GLN A 113       4.819  19.413  14.477  1.00 74.14      A    C  
ANISOU  845  CD  GLN A 113     9646   6689  11837    316   2655  -1550  A    C  
ATOM    846  NE2 GLN A 113       5.569  19.793  15.482  1.00 58.59      A    N  
ANISOU  846  NE2 GLN A 113     7510   4842   9909    318   2675  -1866  A    N  
ATOM    847  OE1 GLN A 113       5.049  19.778  13.328  1.00 81.18      A    O  
ANISOU  847  OE1 GLN A 113    10490   7542  12815    234   2760  -1434  A    O  
ATOM    848  N   TRP A 114       3.369  16.764  11.494  1.00 33.86      A    N  
ANISOU  848  N   TRP A 114     5068   1548   6250    390   2424   -857  A    N  
ATOM    849  CA  TRP A 114       4.006  15.504  11.096  1.00 32.88      A    C  
ANISOU  849  CA  TRP A 114     5084   1527   5882    511   2305   -925  A    C  
ATOM    850  C   TRP A 114       5.426  15.443  11.663  1.00 40.99      A    C  
ANISOU  850  C   TRP A 114     5991   2704   6880    652   2271  -1218  A    C  
ATOM    851  O   TRP A 114       6.215  16.351  11.425  1.00 42.34      A    O  
ANISOU  851  O   TRP A 114     5935   2938   7214    583   2373  -1339  A    O  
ATOM    852  CB  TRP A 114       4.026  15.343   9.559  1.00 30.64      A    C  
ANISOU  852  CB  TRP A 114     4765   1360   5516    383   2337   -722  A    C  
ATOM    853  CG  TRP A 114       2.654  15.338   8.946  1.00 29.70      A    C  
ANISOU  853  CG  TRP A 114     4728   1181   5375    268   2367   -459  A    C  
ATOM    854  CD1 TRP A 114       1.929  16.426   8.540  1.00 32.09      A    C  
ANISOU  854  CD1 TRP A 114     4938   1359   5897    182   2496   -286  A    C  
ATOM    855  CD2 TRP A 114       1.825  14.187   8.714  1.00 28.45      A    C  
ANISOU  855  CD2 TRP A 114     4754   1101   4953    229   2279   -344  A    C  
ATOM    856  CE2 TRP A 114       0.606  14.652   8.173  1.00 30.90      A    C  
ANISOU  856  CE2 TRP A 114     5100   1261   5381    132   2339   -146  A    C  
ATOM    857  CE3 TRP A 114       1.999  12.800   8.907  1.00 29.22      A    C  
ANISOU  857  CE3 TRP A 114     5101   1173   4827    315   2187   -440  A    C  
ATOM    858  NE1 TRP A 114       0.708  16.020   8.047  1.00 30.93      A    N  
ANISOU  858  NE1 TRP A 114     4886   1239   5626    105   2465    -65  A    N  
ATOM    859  CZ2 TRP A 114      -0.415  13.779   7.780  1.00 29.55      A    C  
ANISOU  859  CZ2 TRP A 114     5082   1135   5010     38   2288    -33  A    C  
ATOM    860  CZ3 TRP A 114       0.961  11.939   8.577  1.00 29.79      A    C  
ANISOU  860  CZ3 TRP A 114     5407   1145   4767    241   2173   -362  A    C  
ATOM    861  CH2 TRP A 114      -0.218  12.422   8.000  1.00 29.99      A    C  
ANISOU  861  CH2 TRP A 114     5383   1159   4855     78   2213   -170  A    C  
ATOM    862  N   LEU A 115       5.729  14.402  12.455  1.00 39.32      A    N  
ANISOU  862  N   LEU A 115     5924   2563   6454    856   2145  -1334  A    N  
ATOM    863  CA  LEU A 115       7.050  14.216  13.057  1.00 40.40      A    C  
ANISOU  863  CA  LEU A 115     5935   2914   6501   1043   2092  -1603  A    C  
ATOM    864  C   LEU A 115       7.675  12.938  12.571  1.00 46.24      A    C  
ANISOU  864  C   LEU A 115     6844   3734   6993   1243   2020  -1609  A    C  
ATOM    865  O   LEU A 115       7.038  11.881  12.624  1.00 44.33      A    O  
ANISOU  865  O   LEU A 115     6892   3372   6578   1329   1975  -1479  A    O  
ATOM    866  CB  LEU A 115       7.001  14.181  14.599  1.00 40.87      A    C  
ANISOU  866  CB  LEU A 115     5985   3045   6500   1179   2022  -1745  A    C  
ATOM    867  CG  LEU A 115       6.328  15.325  15.321  1.00 46.05      A    C  
ANISOU  867  CG  LEU A 115     6516   3603   7378   1005   2097  -1756  A    C  
ATOM    868  CD1 LEU A 115       4.948  14.918  15.806  1.00 44.71      A    C  
ANISOU  868  CD1 LEU A 115     6586   3248   7152   1005   2056  -1560  A    C  
ATOM    869  CD2 LEU A 115       7.151  15.743  16.505  1.00 53.35      A    C  
ANISOU  869  CD2 LEU A 115     7208   4750   8313   1073   2085  -2064  A    C  
ATOM    870  N   ASN A 116       8.946  13.027  12.127  1.00 45.36      A    N  
ANISOU  870  N   ASN A 116     6553   3820   6862   1315   2031  -1774  A    N  
ATOM    871  CA  ASN A 116       9.729  11.867  11.723  1.00 46.41      A    C  
ANISOU  871  CA  ASN A 116     6816   4057   6761   1545   1980  -1808  A    C  
ATOM    872  C   ASN A 116      10.144  11.151  12.995  1.00 55.46      A    C  
ANISOU  872  C   ASN A 116     8030   5349   7694   1865   1886  -1930  A    C  
ATOM    873  O   ASN A 116      10.104  11.759  14.062  1.00 56.08      A    O  
ANISOU  873  O   ASN A 116     7959   5523   7826   1874   1856  -2048  A    O  
ATOM    874  CB  ASN A 116      10.957  12.293  10.895  1.00 43.90      A    C  
ANISOU  874  CB  ASN A 116     6248   3934   6497   1521   2029  -1952  A    C  
ATOM    875  CG  ASN A 116      10.635  13.132   9.685  1.00 64.21      A    C  
ANISOU  875  CG  ASN A 116     8728   6388   9281   1228   2145  -1828  A    C  
ATOM    876  ND2 ASN A 116      11.224  14.312   9.606  1.00 50.19      A    N  
ANISOU  876  ND2 ASN A 116     6654   4708   7709   1082   2241  -1968  A    N  
ATOM    877  OD1 ASN A 116       9.865  12.736   8.805  1.00 67.22      A    O  
ANISOU  877  OD1 ASN A 116     9300   6606   9634   1129   2167  -1612  A    O  
ATOM    878  N   LYS A 117      10.541   9.879  12.898  1.00 56.48      A    N  
ANISOU  878  N   LYS A 117     8385   5499   7575   2138   1856  -1898  A    N  
ATOM    879  CA  LYS A 117      10.994   9.077  14.035  1.00 58.87      A    C  
ANISOU  879  CA  LYS A 117     8783   5952   7634   2514   1790  -1969  A    C  
ATOM    880  C   LYS A 117      12.150   9.781  14.758  1.00 68.81      A    C  
ANISOU  880  C   LYS A 117     9652   7614   8878   2643   1730  -2240  A    C  
ATOM    881  O   LYS A 117      12.191   9.765  15.986  1.00 70.60      A    O  
ANISOU  881  O   LYS A 117     9835   7997   8994   2825   1666  -2321  A    O  
ATOM    882  CB  LYS A 117      11.383   7.667  13.587  1.00 61.78      A    C  
ANISOU  882  CB  LYS A 117     9449   6266   7760   2794   1822  -1885  A    C  
ATOM    883  CG  LYS A 117      12.410   7.602  12.454  1.00 68.11      A    C  
ANISOU  883  CG  LYS A 117    10122   7198   8558   2800   1856  -1958  A    C  
ATOM    884  CD  LYS A 117      12.401   6.267  11.748  1.00 66.12      A    C  
ANISOU  884  CD  LYS A 117    10234   6767   8122   2968   1934  -1835  A    C  
ATOM    885  CE  LYS A 117      13.164   6.341  10.450  1.00 66.61      A    C  
ANISOU  885  CE  LYS A 117    10176   6918   8217   2896   1978  -1889  A    C  
ATOM    886  NZ  LYS A 117      13.460   4.990   9.921  1.00 69.79      A    N1+
ANISOU  886  NZ  LYS A 117    10919   7182   8415   3112   2070  -1812  A    N1+
ATOM    887  N   GLU A 118      13.019  10.483  13.995  1.00 67.88      A    N  
ANISOU  887  N   GLU A 118     9236   7676   8880   2509   1763  -2392  A    N  
ATOM    888  CA  GLU A 118      14.156  11.267  14.494  1.00 70.37      A    C  
ANISOU  888  CA  GLU A 118     9132   8399   9205   2545   1736  -2697  A    C  
ATOM    889  C   GLU A 118      13.686  12.360  15.477  1.00 73.73      A    C  
ANISOU  889  C   GLU A 118     9364   8854   9795   2344   1739  -2825  A    C  
ATOM    890  O   GLU A 118      14.379  12.641  16.458  1.00 75.12      A    O  
ANISOU  890  O   GLU A 118     9283   9391   9866   2475   1683  -3073  A    O  
ATOM    891  CB  GLU A 118      14.943  11.904  13.329  1.00 72.38      A    C  
ANISOU  891  CB  GLU A 118     9144   8744   9615   2340   1819  -2807  A    C  
ATOM    892  CG  GLU A 118      15.564  10.910  12.359  1.00 86.32      A    C  
ANISOU  892  CG  GLU A 118    11055  10522  11220   2530   1824  -2721  A    C  
ATOM    893  CD  GLU A 118      14.719  10.538  11.153  1.00114.03      A    C  
ANISOU  893  CD  GLU A 118    14855  13648  14824   2337   1897  -2458  A    C  
ATOM    894  OE1 GLU A 118      14.166  11.454  10.501  1.00110.86      A    O  
ANISOU  894  OE1 GLU A 118    14368  13081  14674   1990   1978  -2399  A    O  
ATOM    895  OE2 GLU A 118      14.673   9.333  10.814  1.00113.07      A    O1-
ANISOU  895  OE2 GLU A 118    15036  13413  14514   2540   1892  -2321  A    O1-
ATOM    896  N   GLN A 119      12.502  12.948  15.216  1.00 67.95      A    N  
ANISOU  896  N   GLN A 119     8750   7764   9302   2038   1812  -2659  A    N  
ATOM    897  CA  GLN A 119      11.892  13.971  16.064  1.00 67.27      A    C  
ANISOU  897  CA  GLN A 119     8535   7626   9397   1835   1848  -2740  A    C  
ATOM    898  C   GLN A 119      11.286  13.354  17.339  1.00 71.70      A    C  
ANISOU  898  C   GLN A 119     9277   8194   9773   2056   1747  -2688  A    C  
ATOM    899  O   GLN A 119      11.431  13.941  18.407  1.00 72.96      A    O  
ANISOU  899  O   GLN A 119     9238   8546   9937   2051   1727  -2888  A    O  
ATOM    900  CB  GLN A 119      10.809  14.752  15.289  1.00 66.55      A    C  
ANISOU  900  CB  GLN A 119     8528   7155   9602   1489   1973  -2534  A    C  
ATOM    901  CG  GLN A 119      11.341  15.750  14.257  1.00 72.74      A    C  
ANISOU  901  CG  GLN A 119     9092   7925  10621   1232   2121  -2597  A    C  
ATOM    902  CD  GLN A 119      10.245  16.376  13.412  1.00 77.00      A    C  
ANISOU  902  CD  GLN A 119     9746   8114  11397    969   2247  -2329  A    C  
ATOM    903  NE2 GLN A 119       9.540  17.362  13.979  1.00 66.91      A    N  
ANISOU  903  NE2 GLN A 119     8406   6691  10326    794   2342  -2328  A    N  
ATOM    904  OE1 GLN A 119      10.039  16.017  12.236  1.00 61.92      A    O  
ANISOU  904  OE1 GLN A 119     7963   6083   9480    928   2272  -2126  A    O  
ATOM    905  N   THR A 120      10.626  12.169  17.231  1.00 67.34      A    N  
ANISOU  905  N   THR A 120     9102   7434   9051   2239   1703  -2434  A    N  
ATOM    906  CA  THR A 120       9.930  11.476  18.336  1.00 66.51      A    C  
ANISOU  906  CA  THR A 120     9239   7264   8767   2447   1642  -2331  A    C  
ATOM    907  C   THR A 120      10.893  10.893  19.401  1.00 73.88      A    C  
ANISOU  907  C   THR A 120    10078   8594   9397   2854   1547  -2496  A    C  
ATOM    908  O   THR A 120      12.111  10.896  19.212  1.00 75.34      A    O  
ANISOU  908  O   THR A 120    10031   9115   9480   3002   1518  -2676  A    O  
ATOM    909  CB  THR A 120       8.983  10.359  17.823  1.00 63.34      A    C  
ANISOU  909  CB  THR A 120     9277   6514   8275   2494   1670  -2035  A    C  
ATOM    910  CG2 THR A 120       8.164  10.762  16.613  1.00 54.38      A    C  
ANISOU  910  CG2 THR A 120     8214   5075   7374   2132   1750  -1868  A    C  
ATOM    911  OG1 THR A 120       9.703   9.156  17.574  1.00 67.12      A    O  
ANISOU  911  OG1 THR A 120     9911   7076   8513   2804   1662  -2008  A    O  
ATOM    912  N   ALA A 121      10.318  10.371  20.508  1.00 70.88      A    N  
ANISOU  912  N   ALA A 121     9880   8195   8857   3049   1504  -2419  A    N  
ATOM    913  CA  ALA A 121      11.047   9.784  21.632  1.00 73.29      A    C  
ANISOU  913  CA  ALA A 121    10128   8881   8839   3477   1420  -2522  A    C  
ATOM    914  C   ALA A 121      11.486   8.321  21.370  1.00 78.49      A    C  
ANISOU  914  C   ALA A 121    11092   9525   9208   3898   1433  -2347  A    C  
ATOM    915  O   ALA A 121      12.624   7.975  21.689  1.00 81.54      A    O  
ANISOU  915  O   ALA A 121    11308  10320   9353   4250   1379  -2470  A    O  
ATOM    916  CB  ALA A 121      10.205   9.868  22.899  1.00 73.91      A    C  
ANISOU  916  CB  ALA A 121    10295   8924   8864   3514   1393  -2487  A    C  
ATOM    917  N   GLY A 122      10.598   7.496  20.801  1.00 72.60      A    N  
ANISOU  917  N   GLY A 122    10776   8325   8483   3855   1520  -2077  A    N  
ATOM    918  CA  GLY A 122      10.856   6.086  20.491  1.00 72.78      A    C  
ANISOU  918  CA  GLY A 122    11162   8223   8269   4204   1594  -1899  A    C  
ATOM    919  C   GLY A 122      11.888   5.852  19.403  1.00 76.86      A    C  
ANISOU  919  C   GLY A 122    11586   8857   8762   4278   1614  -1958  A    C  
ATOM    920  O   GLY A 122      12.498   4.775  19.340  1.00 78.66      A    O  
ANISOU  920  O   GLY A 122    12014   9130   8745   4674   1667  -1876  A    O  
ATOM    921  N   LYS A 123      12.062   6.859  18.510  1.00 70.21      A    N  
ANISOU  921  N   LYS A 123    10457   8041   8179   3899   1596  -2087  A    N  
ATOM    922  CA  LYS A 123      13.030   6.934  17.404  1.00 69.15      A    C  
ANISOU  922  CA  LYS A 123    10154   8040   8079   3875   1613  -2180  A    C  
ATOM    923  C   LYS A 123      12.837   5.859  16.304  1.00 71.46      A    C  
ANISOU  923  C   LYS A 123    10828   8005   8320   3914   1724  -1985  A    C  
ATOM    924  O   LYS A 123      13.547   5.915  15.293  1.00 72.12      A    O  
ANISOU  924  O   LYS A 123    10793   8164   8445   3862   1747  -2047  A    O  
ATOM    925  CB  LYS A 123      14.493   6.895  17.926  1.00 73.65      A    C  
ANISOU  925  CB  LYS A 123    10404   9157   8422   4252   1536  -2390  A    C  
ATOM    926  CG  LYS A 123      14.826   7.867  19.069  1.00 74.91      A    C  
ANISOU  926  CG  LYS A 123    10150   9730   8584   4223   1434  -2643  A    C  
ATOM    927  CD  LYS A 123      14.984   9.317  18.613  1.00 79.57      A    C  
ANISOU  927  CD  LYS A 123    10354  10394   9486   3756   1443  -2868  A    C  
ATOM    928  CE  LYS A 123      15.276  10.247  19.765  1.00 86.93      A    C  
ANISOU  928  CE  LYS A 123    10897  11711  10422   3692   1378  -3153  A    C  
ATOM    929  NZ  LYS A 123      14.960  11.657  19.424  1.00 91.52      A    N1+
ANISOU  929  NZ  LYS A 123    11238  12168  11369   3175   1453  -3306  A    N1+
ATOM    930  N   ILE A 124      11.890   4.911  16.466  1.00 66.35      A    N  
ANISOU  930  N   ILE A 124    10628   6995   7587   3978   1811  -1772  A    N  
ATOM    931  CA  ILE A 124      11.628   3.856  15.466  1.00 65.62      A    C  
ANISOU  931  CA  ILE A 124    10919   6573   7440   3977   1951  -1621  A    C  
ATOM    932  C   ILE A 124      10.443   4.262  14.560  1.00 66.80      A    C  
ANISOU  932  C   ILE A 124    11160   6392   7829   3464   1994  -1535  A    C  
ATOM    933  O   ILE A 124      10.448   3.957  13.363  1.00 66.78      A    O  
ANISOU  933  O   ILE A 124    11250   6259   7863   3312   2067  -1504  A    O  
ATOM    934  CB  ILE A 124      11.372   2.465  16.134  1.00 70.62      A    C  
ANISOU  934  CB  ILE A 124    12018   6999   7817   4358   2076  -1457  A    C  
ATOM    935  CG1 ILE A 124      12.529   2.061  17.089  1.00 74.45      A    C  
ANISOU  935  CG1 ILE A 124    12398   7865   8024   4932   2036  -1507  A    C  
ATOM    936  CG2 ILE A 124      11.130   1.356  15.082  1.00 71.43      A    C  
ANISOU  936  CG2 ILE A 124    12533   6738   7870   4326   2265  -1340  A    C  
ATOM    937  CD1 ILE A 124      12.207   0.914  18.121  1.00 81.60      A    C  
ANISOU  937  CD1 ILE A 124    13723   8610   8669   5360   2159  -1322  A    C  
ATOM    938  N   HIS A 125       9.428   4.940  15.129  1.00 60.08      A    N  
ANISOU  938  N   HIS A 125    10269   5436   7121   3214   1952  -1495  A    N  
ATOM    939  CA  HIS A 125       8.228   5.275  14.377  1.00 56.70      A    C  
ANISOU  939  CA  HIS A 125     9922   4742   6881   2777   1993  -1390  A    C  
ATOM    940  C   HIS A 125       7.918   6.754  14.300  1.00 55.06      A    C  
ANISOU  940  C   HIS A 125     9351   4636   6935   2457   1916  -1444  A    C  
ATOM    941  O   HIS A 125       8.177   7.480  15.260  1.00 52.55      A    O  
ANISOU  941  O   HIS A 125     8801   4503   6663   2528   1841  -1551  A    O  
ATOM    942  CB  HIS A 125       7.019   4.568  14.999  1.00 57.27      A    C  
ANISOU  942  CB  HIS A 125    10360   4519   6880   2744   2068  -1246  A    C  
ATOM    943  CG  HIS A 125       7.066   3.082  14.825  1.00 62.24      A    C  
ANISOU  943  CG  HIS A 125    11424   4932   7292   2961   2220  -1167  A    C  
ATOM    944  CD2 HIS A 125       6.820   2.335  13.727  1.00 64.14      A    C  
ANISOU  944  CD2 HIS A 125    11908   4963   7497   2820   2350  -1124  A    C  
ATOM    945  ND1 HIS A 125       7.418   2.246  15.866  1.00 65.75      A    N  
ANISOU  945  ND1 HIS A 125    12095   5363   7523   3374   2274  -1129  A    N  
ATOM    946  CE1 HIS A 125       7.352   1.023  15.378  1.00 66.80      A    C  
ANISOU  946  CE1 HIS A 125    12627   5237   7518   3471   2458  -1055  A    C  
ATOM    947  NE2 HIS A 125       7.010   1.028  14.090  1.00 66.23      A    N  
ANISOU  947  NE2 HIS A 125    12575   5044   7548   3131   2508  -1068  A    N  
ATOM    948  N   PRO A 126       7.274   7.191  13.179  1.00 49.03      A    N  
ANISOU  948  N   PRO A 126     8553   3743   6334   2103   1954  -1360  A    N  
ATOM    949  CA  PRO A 126       6.811   8.594  13.090  1.00 46.08      A    C  
ANISOU  949  CA  PRO A 126     7883   3410   6217   1815   1927  -1361  A    C  
ATOM    950  C   PRO A 126       5.583   8.871  13.989  1.00 48.04      A    C  
ANISOU  950  C   PRO A 126     8210   3515   6529   1701   1917  -1270  A    C  
ATOM    951  O   PRO A 126       5.037   7.961  14.612  1.00 47.96      A    O  
ANISOU  951  O   PRO A 126     8489   3366   6366   1814   1933  -1202  A    O  
ATOM    952  CB  PRO A 126       6.456   8.745  11.609  1.00 46.74      A    C  
ANISOU  952  CB  PRO A 126     7955   3417   6388   1545   1986  -1257  A    C  
ATOM    953  CG  PRO A 126       6.022   7.390  11.191  1.00 52.03      A    C  
ANISOU  953  CG  PRO A 126     8992   3916   6863   1577   2043  -1170  A    C  
ATOM    954  CD  PRO A 126       6.876   6.417  11.977  1.00 49.18      A    C  
ANISOU  954  CD  PRO A 126     8808   3584   6294   1958   2043  -1257  A    C  
ATOM    955  N   TYR A 127       5.144  10.132  14.048  1.00 43.89      A    N  
ANISOU  955  N   TYR A 127     7436   3008   6234   1481   1916  -1263  A    N  
ATOM    956  CA  TYR A 127       4.010  10.555  14.873  1.00 41.94      A    C  
ANISOU  956  CA  TYR A 127     7216   2645   6073   1367   1915  -1183  A    C  
ATOM    957  C   TYR A 127       3.223  11.661  14.180  1.00 43.46      A    C  
ANISOU  957  C   TYR A 127     7240   2772   6501   1065   1972  -1061  A    C  
ATOM    958  O   TYR A 127       3.801  12.509  13.492  1.00 43.00      A    O  
ANISOU  958  O   TYR A 127     6948   2796   6593    974   2014  -1101  A    O  
ATOM    959  CB  TYR A 127       4.547  11.072  16.219  1.00 43.50      A    C  
ANISOU  959  CB  TYR A 127     7244   2994   6290   1526   1863  -1358  A    C  
ATOM    960  CG  TYR A 127       3.583  11.116  17.388  1.00 44.10      A    C  
ANISOU  960  CG  TYR A 127     7420   2976   6360   1529   1849  -1311  A    C  
ATOM    961  CD1 TYR A 127       2.702  12.187  17.555  1.00 44.12      A    C  
ANISOU  961  CD1 TYR A 127     7294   2888   6583   1293   1890  -1248  A    C  
ATOM    962  CD2 TYR A 127       3.663  10.180  18.413  1.00 45.39      A    C  
ANISOU  962  CD2 TYR A 127     7784   3163   6298   1798   1807  -1337  A    C  
ATOM    963  CE1 TYR A 127       1.877  12.281  18.677  1.00 42.67      A    C  
ANISOU  963  CE1 TYR A 127     7180   2636   6396   1301   1879  -1222  A    C  
ATOM    964  CE2 TYR A 127       2.851  10.269  19.541  1.00 46.08      A    C  
ANISOU  964  CE2 TYR A 127     7946   3188   6376   1809   1797  -1306  A    C  
ATOM    965  CZ  TYR A 127       1.973  11.332  19.677  1.00 51.61      A    C  
ANISOU  965  CZ  TYR A 127     8503   3805   7302   1552   1826  -1265  A    C  
ATOM    966  OH  TYR A 127       1.157  11.413  20.779  1.00 55.43      A    O  
ANISOU  966  OH  TYR A 127     9060   4227   7772   1562   1822  -1237  A    O  
ATOM    967  N   LEU A 128       1.901  11.667  14.405  1.00 39.34      A    N  
ANISOU  967  N   LEU A 128     6831   2110   6005    927   1989   -909  A    N  
ATOM    968  CA  LEU A 128       0.957  12.670  13.911  1.00 37.67      A    C  
ANISOU  968  CA  LEU A 128     6476   1850   5989    690   2050   -754  A    C  
ATOM    969  C   LEU A 128      -0.043  13.026  14.998  1.00 37.91      A    C  
ANISOU  969  C   LEU A 128     6527   1794   6083    655   2051   -707  A    C  
ATOM    970  O   LEU A 128      -0.551  12.137  15.683  1.00 36.65      A    O  
ANISOU  970  O   LEU A 128     6596   1564   5766    721   2014   -694  A    O  
ATOM    971  CB  LEU A 128       0.205  12.170  12.658  1.00 37.86      A    C  
ANISOU  971  CB  LEU A 128     6609   1848   5928    525   2078   -574  A    C  
ATOM    972  CG  LEU A 128      -1.092  12.929  12.275  1.00 41.22      A    C  
ANISOU  972  CG  LEU A 128     6937   2257   6468    319   2131   -364  A    C  
ATOM    973  CD1 LEU A 128      -0.782  14.287  11.636  1.00 40.56      A    C  
ANISOU  973  CD1 LEU A 128     6572   2227   6611    255   2216   -295  A    C  
ATOM    974  CD2 LEU A 128      -1.993  12.077  11.400  1.00 43.46      A    C  
ANISOU  974  CD2 LEU A 128     7372   2567   6574    171   2132   -236  A    C  
ATOM    975  N   PHE A 129      -0.335  14.332  15.139  1.00 32.56      A    N  
ANISOU  975  N   PHE A 129     5538   1280   5555    491   2105   -612  A    N  
ATOM    976  CA  PHE A 129      -1.339  14.821  16.055  1.00 31.56      A    C  
ANISOU  976  CA  PHE A 129     5341   1198   5453    409   2123   -519  A    C  
ATOM    977  C   PHE A 129      -1.964  16.082  15.483  1.00 33.02      A    C  
ANISOU  977  C   PHE A 129     5422   1164   5961    316   2260   -428  A    C  
ATOM    978  O   PHE A 129      -1.318  16.814  14.737  1.00 31.18      A    O  
ANISOU  978  O   PHE A 129     4947   1106   5796    242   2339   -401  A    O  
ATOM    979  CB  PHE A 129      -0.792  15.018  17.474  1.00 33.46      A    C  
ANISOU  979  CB  PHE A 129     5597   1358   5759    569   2088   -755  A    C  
ATOM    980  CG  PHE A 129       0.170  16.170  17.698  1.00 34.55      A    C  
ANISOU  980  CG  PHE A 129     5515   1468   6143    596   2164   -987  A    C  
ATOM    981  CD1 PHE A 129      -0.295  17.417  18.105  1.00 35.69      A    C  
ANISOU  981  CD1 PHE A 129     5543   1446   6571    515   2298  -1028  A    C  
ATOM    982  CD2 PHE A 129       1.542  15.980  17.591  1.00 36.05      A    C  
ANISOU  982  CD2 PHE A 129     5657   1734   6308    747   2138  -1238  A    C  
ATOM    983  CE1 PHE A 129       0.591  18.486  18.314  1.00 38.77      A    C  
ANISOU  983  CE1 PHE A 129     5694   1883   7152    466   2406  -1242  A    C  
ATOM    984  CE2 PHE A 129       2.428  17.041  17.826  1.00 40.33      A    C  
ANISOU  984  CE2 PHE A 129     5931   2369   7023    699   2221  -1459  A    C  
ATOM    985  CZ  PHE A 129       1.948  18.292  18.171  1.00 38.55      A    C  
ANISOU  985  CZ  PHE A 129     5561   2033   7053    541   2365  -1468  A    C  
ATOM    986  N   SER A 130      -3.237  16.295  15.806  1.00 32.08      A    N  
ANISOU  986  N   SER A 130     5276   1103   5811    228   2287   -257  A    N  
ATOM    987  CA  SER A 130      -4.028  17.427  15.352  1.00 32.52      A    C  
ANISOU  987  CA  SER A 130     5192   1079   6087    148   2422    -84  A    C  
ATOM    988  C   SER A 130      -4.303  18.437  16.466  1.00 37.86      A    C  
ANISOU  988  C   SER A 130     5874   1443   7068    179   2515   -161  A    C  
ATOM    989  O   SER A 130      -4.276  18.091  17.647  1.00 39.22      A    O  
ANISOU  989  O   SER A 130     6129   1593   7178    241   2445   -316  A    O  
ATOM    990  CB  SER A 130      -5.360  16.940  14.787  1.00 33.65      A    C  
ANISOU  990  CB  SER A 130     5495   1106   6184     75   2399    141  A    C  
ATOM    991  OG  SER A 130      -6.259  16.629  15.836  1.00 37.93      A    O  
ANISOU  991  OG  SER A 130     6164   1558   6689     72   2359    141  A    O  
ATOM    992  N   GLN A 131      -4.581  19.685  16.061  1.00 34.92      A    N  
ANISOU  992  N   GLN A 131     5311   1054   6903    123   2692    -24  A    N  
ATOM    993  CA  GLN A 131      -4.987  20.820  16.881  1.00 35.49      A    C  
ANISOU  993  CA  GLN A 131     5267   1032   7187    109   2845    -38  A    C  
ATOM    994  C   GLN A 131      -5.972  21.642  16.054  1.00 37.85      A    C  
ANISOU  994  C   GLN A 131     5520   1200   7661     87   3010    286  A    C  
ATOM    995  O   GLN A 131      -5.546  22.464  15.241  1.00 39.08      A    O  
ANISOU  995  O   GLN A 131     5563   1309   7978     78   3179    366  A    O  
ATOM    996  CB  GLN A 131      -3.786  21.649  17.361  1.00 37.32      A    C  
ANISOU  996  CB  GLN A 131     5417   1109   7652    106   2960   -324  A    C  
ATOM    997  CG  GLN A 131      -4.151  22.846  18.276  1.00 41.79      A    C  
ANISOU  997  CG  GLN A 131     5894   1515   8470     67   3157   -389  A    C  
ATOM    998  CD  GLN A 131      -5.171  22.533  19.359  1.00 51.29      A    C  
ANISOU  998  CD  GLN A 131     7192   2701   9597     99   3078   -362  A    C  
ATOM    999  NE2 GLN A 131      -6.247  23.285  19.390  1.00 49.54      A    N  
ANISOU  999  NE2 GLN A 131     6943   2363   9518     85   3228   -140  A    N  
ATOM   1000  OE1 GLN A 131      -5.003  21.629  20.174  1.00 42.46      A    O  
ANISOU 1000  OE1 GLN A 131     6173   1676   8286    153   2896   -527  A    O  
ATOM   1001  N   CYS A 132      -7.275  21.358  16.201  1.00 33.66      A    N  
ANISOU 1001  N   CYS A 132     4887   1013   6889    107   2964    442  A    N  
ATOM   1002  CA  CYS A 132      -8.269  22.034  15.381  1.00 35.13      A    C  
ANISOU 1002  CA  CYS A 132     5032   1113   7204    126   3097    778  A    C  
ATOM   1003  C   CYS A 132      -8.754  23.353  15.957  1.00 39.47      A    C  
ANISOU 1003  C   CYS A 132     5578   1313   8106    145   3337    909  A    C  
ATOM   1004  O   CYS A 132      -9.117  24.225  15.164  1.00 40.63      A    O  
ANISOU 1004  O   CYS A 132     5620   1444   8375    202   3530   1175  A    O  
ATOM   1005  CB  CYS A 132      -9.429  21.115  15.043  1.00 35.53      A    C  
ANISOU 1005  CB  CYS A 132     5191   1257   7051     78   2952    979  A    C  
ATOM   1006  SG  CYS A 132      -8.976  19.798  13.889  1.00 39.40      A    S  
ANISOU 1006  SG  CYS A 132     5800   1891   7281    -10   2774    979  A    S  
ATOM   1007  N   GLN A 133      -8.724  23.542  17.299  1.00 36.24      A    N  
ANISOU 1007  N   GLN A 133     5083   1024   7663    161   3343    642  A    N  
ATOM   1008  CA  GLN A 133      -9.163  24.817  17.910  1.00 36.07      A    C  
ANISOU 1008  CA  GLN A 133     4929    922   7854    203   3595    666  A    C  
ATOM   1009  C   GLN A 133      -8.155  25.941  17.548  1.00 39.73      A    C  
ANISOU 1009  C   GLN A 133     5457    902   8735    157   3862    641  A    C  
ATOM   1010  O   GLN A 133      -6.954  25.711  17.650  1.00 37.27      A    O  
ANISOU 1010  O   GLN A 133     5042    805   8316     99   3805    343  A    O  
ATOM   1011  CB  GLN A 133      -9.347  24.687  19.437  1.00 35.83      A    C  
ANISOU 1011  CB  GLN A 133     4937    876   7801    164   3540    448  A    C  
ATOM   1012  CG  GLN A 133     -10.265  25.774  20.039  1.00 37.10      A    C  
ANISOU 1012  CG  GLN A 133     5072    822   8204    206   3773    567  A    C  
ATOM   1013  CD  GLN A 133     -10.429  25.748  21.535  1.00 45.65      A    C  
ANISOU 1013  CD  GLN A 133     6394   1462   9490    160   3744    373  A    C  
ATOM   1014  NE2 GLN A 133     -11.237  26.669  22.030  1.00 42.98      A    N  
ANISOU 1014  NE2 GLN A 133     6017    978   9334    197   3955    477  A    N  
ATOM   1015  OE1 GLN A 133      -9.918  24.870  22.255  1.00 41.81      A    O  
ANISOU 1015  OE1 GLN A 133     5985   1066   8836    129   3537    113  A    O  
ATOM   1016  N   ALA A 134      -8.625  27.121  17.059  1.00 40.62      A    N  
ANISOU 1016  N   ALA A 134     5473    912   9048    230   4165    882  A    N  
ATOM   1017  CA  ALA A 134     -10.045  27.470  16.957  1.00 41.57      A    C  
ANISOU 1017  CA  ALA A 134     5593   1009   9193    341   4252   1239  A    C  
ATOM   1018  C   ALA A 134     -10.680  27.156  15.596  1.00 46.86      A    C  
ANISOU 1018  C   ALA A 134     6240   1851   9714    422   4198   1645  A    C  
ATOM   1019  O   ALA A 134     -11.778  26.590  15.558  1.00 46.23      A    O  
ANISOU 1019  O   ALA A 134     6144   1988   9433    460   4049   1828  A    O  
ATOM   1020  CB  ALA A 134     -10.240  28.947  17.274  1.00 44.09      A    C  
ANISOU 1020  CB  ALA A 134     5912    959   9881    389   4651   1336  A    C  
ATOM   1021  N   THR A 135     -10.029  27.573  14.500  1.00 45.17      A    N  
ANISOU 1021  N   THR A 135     5978   1619   9567    453   4338   1763  A    N  
ATOM   1022  CA  THR A 135     -10.542  27.440  13.132  1.00 46.55      A    C  
ANISOU 1022  CA  THR A 135     6072   2043   9573    558   4325   2134  A    C  
ATOM   1023  C   THR A 135      -9.606  26.613  12.222  1.00 49.70      A    C  
ANISOU 1023  C   THR A 135     6483   2604   9795    471   4142   2028  A    C  
ATOM   1024  O   THR A 135      -9.406  26.981  11.062  1.00 50.90      A    O  
ANISOU 1024  O   THR A 135     6569   2828   9943    544   4266   2255  A    O  
ATOM   1025  CB  THR A 135     -10.756  28.850  12.510  1.00 54.57      A    C  
ANISOU 1025  CB  THR A 135     7016   2895  10823    733   4725   2470  A    C  
ATOM   1026  CG2 THR A 135     -11.887  29.613  13.147  1.00 55.31      A    C  
ANISOU 1026  CG2 THR A 135     7086   2885  11045    872   4918   2669  A    C  
ATOM   1027  OG1 THR A 135      -9.559  29.589  12.660  1.00 55.20      A    O  
ANISOU 1027  OG1 THR A 135     7140   2654  11179    659   4963   2251  A    O  
ATOM   1028  N   HIS A 136      -9.057  25.495  12.712  1.00 45.36      A    N  
ANISOU 1028  N   HIS A 136     6025   2125   9086    338   3862   1711  A    N  
ATOM   1029  CA  HIS A 136      -8.161  24.693  11.866  1.00 44.77      A    C  
ANISOU 1029  CA  HIS A 136     5973   2194   8845    272   3707   1610  A    C  
ATOM   1030  C   HIS A 136      -8.787  23.391  11.369  1.00 46.71      A    C  
ANISOU 1030  C   HIS A 136     6253   2752   8743    224   3431   1676  A    C  
ATOM   1031  O   HIS A 136      -8.157  22.715  10.573  1.00 46.15      A    O  
ANISOU 1031  O   HIS A 136     6205   2810   8520    174   3320   1618  A    O  
ATOM   1032  CB  HIS A 136      -6.822  24.414  12.555  1.00 44.30      A    C  
ANISOU 1032  CB  HIS A 136     5982   1989   8859    180   3642   1200  A    C  
ATOM   1033  CG  HIS A 136      -6.114  25.664  12.969  1.00 48.63      A    C  
ANISOU 1033  CG  HIS A 136     6478   2262   9736    172   3930   1077  A    C  
ATOM   1034  CD2 HIS A 136      -5.862  26.151  14.195  1.00 50.22      A    C  
ANISOU 1034  CD2 HIS A 136     6690   2269  10122    127   4024    828  A    C  
ATOM   1035  ND1 HIS A 136      -5.596  26.540  12.021  1.00 51.80      A    N  
ANISOU 1035  ND1 HIS A 136     6809   2576  10299    194   4180   1209  A    N  
ATOM   1036  CE1 HIS A 136      -5.021  27.507  12.706  1.00 52.65      A    C  
ANISOU 1036  CE1 HIS A 136     6895   2414  10695    143   4433   1020  A    C  
ATOM   1037  NE2 HIS A 136      -5.158  27.317  14.020  1.00 52.21      A    N  
ANISOU 1037  NE2 HIS A 136     6877   2301  10659     96   4344    778  A    N  
ATOM   1038  N   CYS A 137     -10.035  23.074  11.745  1.00 43.70      A    N  
ANISOU 1038  N   CYS A 137     5868   2502   8234    227   3350   1800  A    N  
ATOM   1039  CA  CYS A 137     -10.686  21.847  11.263  1.00 42.02      A    C  
ANISOU 1039  CA  CYS A 137     5684   2593   7690    137   3126   1835  A    C  
ATOM   1040  C   CYS A 137     -10.863  21.891   9.735  1.00 45.69      A    C  
ANISOU 1040  C   CYS A 137     6016   3342   8002    168   3152   2095  A    C  
ATOM   1041  O   CYS A 137     -10.831  20.852   9.080  1.00 45.56      A    O  
ANISOU 1041  O   CYS A 137     6036   3546   7728     58   2986   2032  A    O  
ATOM   1042  CB  CYS A 137     -12.013  21.609  11.972  1.00 42.20      A    C  
ANISOU 1042  CB  CYS A 137     5700   2715   7620    117   3068   1910  A    C  
ATOM   1043  SG  CYS A 137     -12.685  19.945  11.736  1.00 44.92      A    S  
ANISOU 1043  SG  CYS A 137     6135   3356   7578    -71   2815   1817  A    S  
ATOM   1044  N   ARG A 138     -10.995  23.106   9.183  1.00 41.78      A    N  
ANISOU 1044  N   ARG A 138     5381   2828   7667    324   3384   2380  A    N  
ATOM   1045  CA  ARG A 138     -11.121  23.397   7.757  1.00 42.42      A    C  
ANISOU 1045  CA  ARG A 138     5318   3171   7627    411   3461   2676  A    C  
ATOM   1046  C   ARG A 138      -9.850  22.977   6.977  1.00 42.47      A    C  
ANISOU 1046  C   ARG A 138     5381   3161   7595    338   3412   2520  A    C  
ATOM   1047  O   ARG A 138      -9.950  22.749   5.774  1.00 41.50      A    O  
ANISOU 1047  O   ARG A 138     5165   3333   7270    351   3385   2689  A    O  
ATOM   1048  CB  ARG A 138     -11.444  24.896   7.519  1.00 43.06      A    C  
ANISOU 1048  CB  ARG A 138     5280   3146   7935    638   3780   3020  A    C  
ATOM   1049  CG  ARG A 138     -10.439  25.899   8.096  1.00 42.13      A    C  
ANISOU 1049  CG  ARG A 138     5245   2565   8197    673   4030   2891  A    C  
ATOM   1050  CD  ARG A 138     -10.970  27.331   8.045  1.00 48.39      A    C  
ANISOU 1050  CD  ARG A 138     5962   3201   9222    894   4387   3228  A    C  
ATOM   1051  NE  ARG A 138     -12.144  27.492   8.912  1.00 49.14      A    N  
ANISOU 1051  NE  ARG A 138     6033   3308   9331    957   4387   3310  A    N  
ATOM   1052  CZ  ARG A 138     -12.840  28.615   9.060  1.00 52.41      A    C  
ANISOU 1052  CZ  ARG A 138     6392   3601   9921   1166   4679   3601  A    C  
ATOM   1053  NH1 ARG A 138     -12.493  29.716   8.397  1.00 45.72      A    N1+
ANISOU 1053  NH1 ARG A 138     5525   2584   9262   1341   5025   3856  A    N1+
ATOM   1054  NH2 ARG A 138     -13.888  28.647   9.866  1.00 39.33      A    N  
ANISOU 1054  NH2 ARG A 138     4544   2183   8215   1393   4529   3350  A    N  
ATOM   1055  N   SER A 139      -8.681  22.855   7.671  1.00 37.72      A    N  
ANISOU 1055  N   SER A 139     4912   2256   7162    265   3397   2191  A    N  
ATOM   1056  CA  SER A 139      -7.398  22.365   7.140  1.00 36.93      A    C  
ANISOU 1056  CA  SER A 139     4872   2129   7029    195   3336   1987  A    C  
ATOM   1057  C   SER A 139      -7.360  20.819   7.066  1.00 39.20      A    C  
ANISOU 1057  C   SER A 139     5276   2598   7019     57   3059   1781  A    C  
ATOM   1058  O   SER A 139      -6.391  20.271   6.534  1.00 39.43      A    O  
ANISOU 1058  O   SER A 139     5357   2651   6972     10   2996   1632  A    O  
ATOM   1059  CB  SER A 139      -6.221  22.871   7.972  1.00 38.32      A    C  
ANISOU 1059  CB  SER A 139     5110   1966   7484    182   3437   1709  A    C  
ATOM   1060  OG  SER A 139      -6.138  24.281   7.917  1.00 51.34      A    O  
ANISOU 1060  OG  SER A 139     6672   3419   9415    275   3744   1872  A    O  
ATOM   1061  N   ILE A 140      -8.405  20.118   7.576  1.00 35.29      A    N  
ANISOU 1061  N   ILE A 140     4830   2221   6357    -10   2923   1771  A    N  
ATOM   1062  CA  ILE A 140      -8.472  18.656   7.500  1.00 33.97      A    C  
ANISOU 1062  CA  ILE A 140     4802   2191   5914   -156   2716   1583  A    C  
ATOM   1063  C   ILE A 140      -9.614  18.243   6.560  1.00 40.97      A    C  
ANISOU 1063  C   ILE A 140     5577   3466   6521   -235   2664   1784  A    C  
ATOM   1064  O   ILE A 140      -9.373  17.522   5.588  1.00 42.20      A    O  
ANISOU 1064  O   ILE A 140     5743   3827   6463   -328   2593   1744  A    O  
ATOM   1065  CB  ILE A 140      -8.598  17.957   8.885  1.00 35.35      A    C  
ANISOU 1065  CB  ILE A 140     5161   2179   6091   -207   2611   1340  A    C  
ATOM   1066  CG1 ILE A 140      -7.557  18.503   9.894  1.00 34.57      A    C  
ANISOU 1066  CG1 ILE A 140     5120   1769   6247   -117   2665   1140  A    C  
ATOM   1067  CG2 ILE A 140      -8.525  16.409   8.748  1.00 32.24      A    C  
ANISOU 1067  CG2 ILE A 140     4956   1870   5422   -348   2454   1146  A    C  
ATOM   1068  CD1 ILE A 140      -7.699  17.976  11.327  1.00 34.65      A    C  
ANISOU 1068  CD1 ILE A 140     5285   1621   6261   -124   2581    937  A    C  
ATOM   1069  N   ILE A 141     -10.853  18.670   6.867  1.00 37.61      A    N  
ANISOU 1069  N   ILE A 141     5037   3169   6084   -206   2699   1977  A    N  
ATOM   1070  CA  ILE A 141     -12.056  18.302   6.107  1.00 38.32      A    C  
ANISOU 1070  CA  ILE A 141     4978   3695   5886   -287   2645   2148  A    C  
ATOM   1071  C   ILE A 141     -12.909  19.544   5.748  1.00 45.23      A    C  
ANISOU 1071  C   ILE A 141     5601   4765   6820    -95   2793   2534  A    C  
ATOM   1072  O   ILE A 141     -12.877  20.526   6.494  1.00 43.49      A    O  
ANISOU 1072  O   ILE A 141     5376   4272   6875     58   2931   2624  A    O  
ATOM   1073  CB  ILE A 141     -12.907  17.264   6.912  1.00 40.67      A    C  
ANISOU 1073  CB  ILE A 141     5394   4036   6025   -472   2520   1965  A    C  
ATOM   1074  CG1 ILE A 141     -13.319  17.800   8.319  1.00 39.51      A    C  
ANISOU 1074  CG1 ILE A 141     5296   3617   6099   -389   2568   1958  A    C  
ATOM   1075  CG2 ILE A 141     -12.204  15.880   6.993  1.00 38.94      A    C  
ANISOU 1075  CG2 ILE A 141     5430   3697   5668   -654   2404   1632  A    C  
ATOM   1076  CD1 ILE A 141     -14.428  17.122   8.933  1.00 45.94      A    C  
ANISOU 1076  CD1 ILE A 141     6152   4542   6760   -535   2493   1885  A    C  
ATOM   1077  N   PRO A 142     -13.671  19.530   4.620  1.00 47.34      A    N  
ANISOU 1077  N   PRO A 142     5652   5514   6820    -88   2782   2764  A    N  
ATOM   1078  CA  PRO A 142     -14.579  20.659   4.340  1.00 50.42      A    C  
ANISOU 1078  CA  PRO A 142     5799   6127   7233    142   2930   3160  A    C  
ATOM   1079  C   PRO A 142     -15.767  20.597   5.308  1.00 53.56      A    C  
ANISOU 1079  C   PRO A 142     6156   6583   7611    115   2896   3169  A    C  
ATOM   1080  O   PRO A 142     -16.377  19.538   5.465  1.00 52.20      A    O  
ANISOU 1080  O   PRO A 142     6002   6632   7200   -114   2736   2985  A    O  
ATOM   1081  CB  PRO A 142     -14.995  20.443   2.881  1.00 55.04      A    C  
ANISOU 1081  CB  PRO A 142     6161   7278   7473    142   2890   3352  A    C  
ATOM   1082  CG  PRO A 142     -14.862  18.976   2.658  1.00 58.70      A    C  
ANISOU 1082  CG  PRO A 142     6736   7889   7679   -176   2688   3010  A    C  
ATOM   1083  CD  PRO A 142     -13.842  18.441   3.632  1.00 50.91      A    C  
ANISOU 1083  CD  PRO A 142     6066   6363   6915   -289   2642   2661  A    C  
ATOM   1084  N   CYS A 143     -16.044  21.703   6.012  1.00 51.21      A    N  
ANISOU 1084  N   CYS A 143     5829   6047   7582    327   3066   3352  A    N  
ATOM   1085  CA  CYS A 143     -17.089  21.738   7.041  1.00 51.58      A    C  
ANISOU 1085  CA  CYS A 143     5853   6093   7653    319   3054   3353  A    C  
ATOM   1086  C   CYS A 143     -17.594  23.150   7.297  1.00 54.92      A    C  
ANISOU 1086  C   CYS A 143     6150   6421   8297    625   3294   3694  A    C  
ATOM   1087  O   CYS A 143     -17.048  24.119   6.773  1.00 54.16      A    O  
ANISOU 1087  O   CYS A 143     6025   6181   8374    837   3496   3908  A    O  
ATOM   1088  CB  CYS A 143     -16.536  21.138   8.336  1.00 49.71      A    C  
ANISOU 1088  CB  CYS A 143     5892   5418   7578    149   2966   2975  A    C  
ATOM   1089  SG  CYS A 143     -14.996  21.911   8.909  1.00 52.42      A    S  
ANISOU 1089  SG  CYS A 143     6427   5161   8329    256   3112   2836  A    S  
ATOM   1090  N   GLN A 144     -18.615  23.257   8.171  1.00 50.88      A    N  
ANISOU 1090  N   GLN A 144     5588   5946   7797    645   3298   3728  A    N  
ATOM   1091  CA  GLN A 144     -19.103  24.519   8.694  1.00 51.02      A    C  
ANISOU 1091  CA  GLN A 144     5538   5790   8057    919   3538   3993  A    C  
ATOM   1092  C   GLN A 144     -18.243  24.740   9.928  1.00 49.97      A    C  
ANISOU 1092  C   GLN A 144     5664   5049   8274    853   3600   3706  A    C  
ATOM   1093  O   GLN A 144     -18.623  24.360  11.027  1.00 47.37      A    O  
ANISOU 1093  O   GLN A 144     5425   4596   7979    739   3519   3509  A    O  
ATOM   1094  CB  GLN A 144     -20.608  24.457   8.999  1.00 53.85      A    C  
ANISOU 1094  CB  GLN A 144     5699   6530   8230    962   3499   4149  A    C  
ATOM   1095  CG  GLN A 144     -21.525  24.531   7.778  1.00 65.35      A    C  
ANISOU 1095  CG  GLN A 144     6831   8655   9342   1100   3486   4489  A    C  
ATOM   1096  CD  GLN A 144     -22.972  24.569   8.200  1.00 69.75      A    C  
ANISOU 1096  CD  GLN A 144     7177   9585   9739   1155   3466   4626  A    C  
ATOM   1097  NE2 GLN A 144     -23.681  25.614   7.804  1.00 54.74      A    N  
ANISOU 1097  NE2 GLN A 144     5047   7923   7828   1520   3664   5060  A    N  
ATOM   1098  OE1 GLN A 144     -23.463  23.675   8.899  1.00 62.34      A    O  
ANISOU 1098  OE1 GLN A 144     6281   8721   8682    883   3292   4351  A    O  
ATOM   1099  N   ASP A 145     -17.020  25.235   9.729  1.00 46.79      A    N  
ANISOU 1099  N   ASP A 145     5379   4300   8099    894   3727   3641  A    N  
ATOM   1100  CA  ASP A 145     -16.052  25.375  10.811  1.00 45.15      A    C  
ANISOU 1100  CA  ASP A 145     5387   3583   8183    803   3769   3317  A    C  
ATOM   1101  C   ASP A 145     -16.375  26.570  11.716  1.00 53.09      A    C  
ANISOU 1101  C   ASP A 145     6403   4269   9501    969   4037   3416  A    C  
ATOM   1102  O   ASP A 145     -15.618  27.543  11.801  1.00 56.85      A    O  
ANISOU 1102  O   ASP A 145     6941   4385  10273   1057   4289   3414  A    O  
ATOM   1103  CB  ASP A 145     -14.626  25.440  10.251  1.00 45.74      A    C  
ANISOU 1103  CB  ASP A 145     5555   3455   8368    759   3810   3179  A    C  
ATOM   1104  CG  ASP A 145     -13.536  25.180  11.271  1.00 47.91      A    C  
ANISOU 1104  CG  ASP A 145     6026   3350   8828    609   3757   2764  A    C  
ATOM   1105  OD1 ASP A 145     -13.806  24.468  12.270  1.00 47.67      A    O  
ANISOU 1105  OD1 ASP A 145     6091   3285   8736    489   3591   2536  A    O  
ATOM   1106  OD2 ASP A 145     -12.406  25.646  11.053  1.00 47.16      A    O1-
ANISOU 1106  OD2 ASP A 145     5979   3025   8915    612   3881   2665  A    O1-
ATOM   1107  N   THR A 146     -17.518  26.470  12.393  1.00 49.29      A    N  
ANISOU 1107  N   THR A 146     5861   3922   8945    992   3994   3481  A    N  
ATOM   1108  CA  THR A 146     -18.054  27.437  13.351  1.00 49.42      A    C  
ANISOU 1108  CA  THR A 146     5882   3689   9208   1137   4219   3564  A    C  
ATOM   1109  C   THR A 146     -18.631  26.656  14.549  1.00 49.03      A    C  
ANISOU 1109  C   THR A 146     5903   3654   9073    968   4020   3314  A    C  
ATOM   1110  O   THR A 146     -19.397  25.717  14.343  1.00 48.84      A    O  
ANISOU 1110  O   THR A 146     5806   4003   8749    861   3799   3323  A    O  
ATOM   1111  CB  THR A 146     -19.065  28.416  12.705  1.00 56.52      A    C  
ANISOU 1111  CB  THR A 146     6581   4797  10098   1449   4458   4050  A    C  
ATOM   1112  CG2 THR A 146     -20.179  27.723  11.924  1.00 52.36      A    C  
ANISOU 1112  CG2 THR A 146     5831   4891   9172   1470   4259   4272  A    C  
ATOM   1113  OG1 THR A 146     -19.645  29.196  13.735  1.00 60.94      A    O  
ANISOU 1113  OG1 THR A 146     7161   5117  10875   1568   4657   4094  A    O  
ATOM   1114  N   PRO A 147     -18.276  27.029  15.800  1.00 43.93      A    N  
ANISOU 1114  N   PRO A 147     5396   2616   8677    932   4111   3080  A    N  
ATOM   1115  CA  PRO A 147     -18.794  26.294  16.980  1.00 42.59      A    C  
ANISOU 1115  CA  PRO A 147     5309   2452   8421    786   3935   2848  A    C  
ATOM   1116  C   PRO A 147     -20.330  26.333  17.145  1.00 51.47      A    C  
ANISOU 1116  C   PRO A 147     6281   3866   9408    872   3940   3088  A    C  
ATOM   1117  O   PRO A 147     -20.886  25.629  17.990  1.00 49.88      A    O  
ANISOU 1117  O   PRO A 147     6134   3725   9094    738   3790   2925  A    O  
ATOM   1118  CB  PRO A 147     -18.094  26.986  18.156  1.00 43.11      A    C  
ANISOU 1118  CB  PRO A 147     5514   2067   8799    778   4092   2596  A    C  
ATOM   1119  CG  PRO A 147     -17.730  28.335  17.642  1.00 49.07      A    C  
ANISOU 1119  CG  PRO A 147     6217   2599   9830    960   4431   2792  A    C  
ATOM   1120  CD  PRO A 147     -17.357  28.105  16.212  1.00 45.30      A    C  
ANISOU 1120  CD  PRO A 147     5662   2339   9212    997   4388   2984  A    C  
ATOM   1121  N   SER A 148     -21.005  27.103  16.292  1.00 53.98      A    N  
ANISOU 1121  N   SER A 148     6404   4397   9711   1102   4110   3482  A    N  
ATOM   1122  CA  SER A 148     -22.456  27.267  16.222  1.00 56.86      A    C  
ANISOU 1122  CA  SER A 148     6562   5121   9921   1239   4139   3769  A    C  
ATOM   1123  C   SER A 148     -23.133  26.008  15.686  1.00 58.84      A    C  
ANISOU 1123  C   SER A 148     6694   5890   9770   1052   3846   3742  A    C  
ATOM   1124  O   SER A 148     -24.325  25.812  15.922  1.00 57.01      A    O  
ANISOU 1124  O   SER A 148     6314   5975   9372   1056   3800   3841  A    O  
ATOM   1125  CB  SER A 148     -22.784  28.449  15.310  1.00 65.59      A    C  
ANISOU 1125  CB  SER A 148     7493   6324  11105   1582   4421   4218  A    C  
ATOM   1126  OG  SER A 148     -24.165  28.484  14.981  1.00 81.97      A    O  
ANISOU 1126  OG  SER A 148     9316   8875  12954   1741   4417   4526  A    O  
ATOM   1127  N   VAL A 149     -22.390  25.203  14.899  1.00 55.37      A    N  
ANISOU 1127  N   VAL A 149     6308   5556   9174    887   3676   3611  A    N  
ATOM   1128  CA  VAL A 149     -22.893  23.966  14.295  1.00 54.75      A    C  
ANISOU 1128  CA  VAL A 149     6142   5941   8719    666   3429   3538  A    C  
ATOM   1129  C   VAL A 149     -22.291  22.788  15.065  1.00 53.12      A    C  
ANISOU 1129  C   VAL A 149     6203   5502   8479    363   3236   3114  A    C  
ATOM   1130  O   VAL A 149     -21.073  22.620  15.112  1.00 52.02      A    O  
ANISOU 1130  O   VAL A 149     6255   5049   8460    307   3209   2917  A    O  
ATOM   1131  CB  VAL A 149     -22.614  23.905  12.759  1.00 60.66      A    C  
ANISOU 1131  CB  VAL A 149     6743   7028   9277    714   3400   3720  A    C  
ATOM   1132  CG1 VAL A 149     -23.078  22.586  12.160  1.00 60.78      A    C  
ANISOU 1132  CG1 VAL A 149     6677   7515   8902    438   3161   3584  A    C  
ATOM   1133  CG2 VAL A 149     -23.267  25.087  12.023  1.00 63.49      A    C  
ANISOU 1133  CG2 VAL A 149     6840   7637   9648   1070   3615   4185  A    C  
ATOM   1134  N   LYS A 150     -23.155  22.003  15.712  1.00 47.42      A    N  
ANISOU 1134  N   LYS A 150     5493   4932   7593    187   3125   2985  A    N  
ATOM   1135  CA  LYS A 150     -22.738  20.841  16.490  1.00 42.73      A    C  
ANISOU 1135  CA  LYS A 150     5165   4129   6939    -73   2976   2621  A    C  
ATOM   1136  C   LYS A 150     -23.286  19.612  15.846  1.00 44.19      A    C  
ANISOU 1136  C   LYS A 150     5310   4705   6777   -336   2823   2529  A    C  
ATOM   1137  O   LYS A 150     -24.471  19.544  15.539  1.00 44.87      A    O  
ANISOU 1137  O   LYS A 150     5168   5216   6664   -380   2817   2663  A    O  
ATOM   1138  CB  LYS A 150     -23.149  20.959  17.953  1.00 42.26      A    C  
ANISOU 1138  CB  LYS A 150     5218   3825   7015    -74   3018   2508  A    C  
ATOM   1139  CG  LYS A 150     -22.264  21.936  18.721  1.00 38.68      A    C  
ANISOU 1139  CG  LYS A 150     4880   2909   6908    108   3157   2463  A    C  
ATOM   1140  CD  LYS A 150     -22.049  21.523  20.168  1.00 52.03      A    C  
ANISOU 1140  CD  LYS A 150     6803   4291   8674     15   3113   2177  A    C  
ATOM   1141  CE  LYS A 150     -23.136  22.011  21.091  1.00 53.34      A    C  
ANISOU 1141  CE  LYS A 150     6898   4465   8906     77   3208   2253  A    C  
ATOM   1142  NZ  LYS A 150     -22.756  21.883  22.515  1.00 43.84      A    N1+
ANISOU 1142  NZ  LYS A 150     5912   2931   7816     38   3200   1991  A    N1+
ATOM   1143  N   PHE A 151     -22.403  18.659  15.597  1.00 39.11      A    N  
ANISOU 1143  N   PHE A 151     4875   3935   6049   -510   2716   2293  A    N  
ATOM   1144  CA  PHE A 151     -22.745  17.443  14.879  1.00 39.52      A    C  
ANISOU 1144  CA  PHE A 151     4925   4311   5780   -789   2604   2165  A    C  
ATOM   1145  C   PHE A 151     -22.175  16.197  15.543  1.00 43.33      A    C  
ANISOU 1145  C   PHE A 151     5759   4493   6213  -1009   2533   1827  A    C  
ATOM   1146  O   PHE A 151     -21.125  16.243  16.199  1.00 42.29      A    O  
ANISOU 1146  O   PHE A 151     5859   3941   6270   -913   2533   1699  A    O  
ATOM   1147  CB  PHE A 151     -22.184  17.564  13.424  1.00 41.01      A    C  
ANISOU 1147  CB  PHE A 151     4981   4733   5869   -749   2581   2279  A    C  
ATOM   1148  CG  PHE A 151     -20.692  17.791  13.348  1.00 39.36      A    C  
ANISOU 1148  CG  PHE A 151     4963   4126   5865   -635   2591   2199  A    C  
ATOM   1149  CD1 PHE A 151     -20.163  19.074  13.417  1.00 41.35      A    C  
ANISOU 1149  CD1 PHE A 151     5152   4162   6398   -357   2713   2381  A    C  
ATOM   1150  CD2 PHE A 151     -19.813  16.719  13.202  1.00 39.67      A    C  
ANISOU 1150  CD2 PHE A 151     5246   4010   5816   -809   2501   1934  A    C  
ATOM   1151  CE1 PHE A 151     -18.783  19.281  13.389  1.00 40.48      A    C  
ANISOU 1151  CE1 PHE A 151     5199   3708   6473   -283   2732   2273  A    C  
ATOM   1152  CE2 PHE A 151     -18.430  16.927  13.180  1.00 41.08      A    C  
ANISOU 1152  CE2 PHE A 151     5578   3857   6174   -695   2507   1850  A    C  
ATOM   1153  CZ  PHE A 151     -17.926  18.210  13.255  1.00 39.14      A    C  
ANISOU 1153  CZ  PHE A 151     5242   3432   6200   -446   2616   2011  A    C  
ATOM   1154  N   THR A 152     -22.850  15.079  15.322  1.00 40.96      A    N  
ANISOU 1154  N   THR A 152     5489   4433   5641  -1301   2489   1682  A    N  
ATOM   1155  CA  THR A 152     -22.433  13.754  15.746  1.00 39.26      A    C  
ANISOU 1155  CA  THR A 152     5615   3977   5325  -1530   2463   1383  A    C  
ATOM   1156  C   THR A 152     -21.514  13.209  14.653  1.00 41.91      A    C  
ANISOU 1156  C   THR A 152     6028   4335   5560  -1599   2418   1295  A    C  
ATOM   1157  O   THR A 152     -21.613  13.650  13.495  1.00 40.17      A    O  
ANISOU 1157  O   THR A 152     5550   4457   5258  -1565   2397   1450  A    O  
ATOM   1158  CB  THR A 152     -23.693  12.939  15.964  1.00 50.09      A    C  
ANISOU 1158  CB  THR A 152     6959   5605   6468  -1826   2489   1280  A    C  
ATOM   1159  CG2 THR A 152     -23.502  11.481  15.865  1.00 49.37      A    C  
ANISOU 1159  CG2 THR A 152     7163   5404   6192  -2130   2508    996  A    C  
ATOM   1160  OG1 THR A 152     -24.214  13.279  17.243  1.00 54.00      A    O  
ANISOU 1160  OG1 THR A 152     7497   5925   7097  -1745   2535   1306  A    O  
ATOM   1161  N   TYR A 153     -20.617  12.267  14.996  1.00 37.30      A    N  
ANISOU 1161  N   TYR A 153     5795   3404   4973  -1670   2412   1062  A    N  
ATOM   1162  CA  TYR A 153     -19.782  11.690  13.953  1.00 37.43      A    C  
ANISOU 1162  CA  TYR A 153     5892   3444   4884  -1741   2382    968  A    C  
ATOM   1163  C   TYR A 153     -19.394  10.242  14.215  1.00 40.96      A    C  
ANISOU 1163  C   TYR A 153     6718   3643   5201  -1939   2421    690  A    C  
ATOM   1164  O   TYR A 153     -19.427   9.749  15.339  1.00 38.90      A    O  
ANISOU 1164  O   TYR A 153     6715   3083   4982  -1940   2467    579  A    O  
ATOM   1165  CB  TYR A 153     -18.520  12.549  13.651  1.00 38.12      A    C  
ANISOU 1165  CB  TYR A 153     5948   3352   5186  -1455   2350   1068  A    C  
ATOM   1166  CG  TYR A 153     -17.321  12.395  14.571  1.00 37.92      A    C  
ANISOU 1166  CG  TYR A 153     6212   2864   5333  -1293   2343    924  A    C  
ATOM   1167  CD1 TYR A 153     -16.383  11.383  14.365  1.00 40.05      A    C  
ANISOU 1167  CD1 TYR A 153     6750   2953   5514  -1345   2332    730  A    C  
ATOM   1168  CD2 TYR A 153     -17.031  13.357  15.531  1.00 36.66      A    C  
ANISOU 1168  CD2 TYR A 153     6024   2484   5421  -1064   2357    990  A    C  
ATOM   1169  CE1 TYR A 153     -15.238  11.280  15.159  1.00 39.07      A    C  
ANISOU 1169  CE1 TYR A 153     6850   2475   5519  -1156   2320    614  A    C  
ATOM   1170  CE2 TYR A 153     -15.884  13.270  16.325  1.00 36.22      A    C  
ANISOU 1170  CE2 TYR A 153     6181   2086   5494   -910   2342    844  A    C  
ATOM   1171  CZ  TYR A 153     -14.985  12.238  16.130  1.00 40.87      A    C  
ANISOU 1171  CZ  TYR A 153     7018   2541   5971   -942   2315    666  A    C  
ATOM   1172  OH  TYR A 153     -13.843  12.198  16.897  1.00 40.01      A    O  
ANISOU 1172  OH  TYR A 153     7078   2161   5963   -754   2295    537  A    O  
ATOM   1173  N   TYR A 154     -19.034   9.572  13.123  1.00 39.50      A    N  
ANISOU 1173  N   TYR A 154     6566   3593   4850  -2095   2421    590  A    N  
ATOM   1174  CA  TYR A 154     -18.497   8.224  13.054  1.00 39.07      A    C  
ANISOU 1174  CA  TYR A 154     6868   3309   4667  -2263   2489    340  A    C  
ATOM   1175  C   TYR A 154     -17.317   8.269  12.116  1.00 42.05      A    C  
ANISOU 1175  C   TYR A 154     7254   3660   5062  -2149   2443    335  A    C  
ATOM   1176  O   TYR A 154     -17.436   8.833  11.028  1.00 42.78      A    O  
ANISOU 1176  O   TYR A 154     7051   4104   5099  -2158   2390    459  A    O  
ATOM   1177  CB  TYR A 154     -19.543   7.208  12.566  1.00 42.36      A    C  
ANISOU 1177  CB  TYR A 154     7298   3986   4810  -2677   2583    172  A    C  
ATOM   1178  CG  TYR A 154     -19.088   5.780  12.777  1.00 45.11      A    C  
ANISOU 1178  CG  TYR A 154     8091   3990   5058  -2849   2721    -92  A    C  
ATOM   1179  CD1 TYR A 154     -19.464   5.069  13.914  1.00 47.35      A    C  
ANISOU 1179  CD1 TYR A 154     8680   3969   5342  -2929   2847   -204  A    C  
ATOM   1180  CD2 TYR A 154     -18.241   5.153  11.864  1.00 46.60      A    C  
ANISOU 1180  CD2 TYR A 154     8417   4132   5159  -2902   2750   -215  A    C  
ATOM   1181  CE1 TYR A 154     -19.017   3.771  14.134  1.00 48.46      A    C  
ANISOU 1181  CE1 TYR A 154     9264   3749   5398  -3043   3017   -416  A    C  
ATOM   1182  CE2 TYR A 154     -17.779   3.857  12.078  1.00 48.61      A    C  
ANISOU 1182  CE2 TYR A 154     9108   4027   5334  -3018   2912   -440  A    C  
ATOM   1183  CZ  TYR A 154     -18.184   3.165  13.206  1.00 57.11      A    C  
ANISOU 1183  CZ  TYR A 154    10495   4791   6412  -3085   3056   -533  A    C  
ATOM   1184  OH  TYR A 154     -17.742   1.885  13.408  1.00 61.12      A    O  
ANISOU 1184  OH  TYR A 154    11461   4923   6841  -3172   3259   -729  A    O  
ATOM   1185  N   SER A 155     -16.186   7.684  12.508  1.00 37.55      A    N  
ANISOU 1185  N   SER A 155     7009   2704   4553  -2022   2468    206  A    N  
ATOM   1186  CA  SER A 155     -15.024   7.686  11.631  1.00 36.49      A    C  
ANISOU 1186  CA  SER A 155     6887   2545   4433  -1911   2430    187  A    C  
ATOM   1187  C   SER A 155     -14.347   6.331  11.538  1.00 41.47      A    C  
ANISOU 1187  C   SER A 155     7898   2920   4940  -1996   2525    -39  A    C  
ATOM   1188  O   SER A 155     -14.374   5.540  12.476  1.00 41.67      A    O  
ANISOU 1188  O   SER A 155     8242   2643   4947  -1999   2618   -153  A    O  
ATOM   1189  CB  SER A 155     -14.004   8.738  12.060  1.00 36.77      A    C  
ANISOU 1189  CB  SER A 155     6845   2405   4723  -1559   2351    307  A    C  
ATOM   1190  OG  SER A 155     -13.359   8.377  13.268  1.00 45.46      A    O  
ANISOU 1190  OG  SER A 155     8228   3133   5913  -1388   2370    205  A    O  
ATOM   1191  N   GLN A 156     -13.743   6.083  10.381  1.00 40.48      A    N  
ANISOU 1191  N   GLN A 156     7739   2916   4724  -2049   2520    -89  A    N  
ATOM   1192  CA  GLN A 156     -12.896   4.937  10.074  1.00 41.86      A    C  
ANISOU 1192  CA  GLN A 156     8244   2863   4798  -2082   2616   -283  A    C  
ATOM   1193  C   GLN A 156     -11.554   5.526   9.667  1.00 43.49      A    C  
ANISOU 1193  C   GLN A 156     8373   3018   5132  -1795   2524   -216  A    C  
ATOM   1194  O   GLN A 156     -11.527   6.381   8.779  1.00 43.45      A    O  
ANISOU 1194  O   GLN A 156     8051   3305   5151  -1786   2439    -88  A    O  
ATOM   1195  CB  GLN A 156     -13.509   4.042   8.981  1.00 45.62      A    C  
ANISOU 1195  CB  GLN A 156     8736   3577   5021  -2469   2719   -443  A    C  
ATOM   1196  CG  GLN A 156     -14.846   3.431   9.386  1.00 64.15      A    C  
ANISOU 1196  CG  GLN A 156    11159   5983   7232  -2797   2839   -552  A    C  
ATOM   1197  CD  GLN A 156     -15.423   2.535   8.329  1.00 84.18      A    C  
ANISOU 1197  CD  GLN A 156    13698   8778   9509  -3218   2960   -761  A    C  
ATOM   1198  NE2 GLN A 156     -15.908   1.384   8.755  1.00 82.41      A    N  
ANISOU 1198  NE2 GLN A 156    13806   8333   9174  -3483   3172   -982  A    N  
ATOM   1199  OE1 GLN A 156     -15.486   2.877   7.139  1.00 76.83      A    O  
ANISOU 1199  OE1 GLN A 156    12465   8262   8463  -3324   2882   -732  A    O  
ATOM   1200  N   VAL A 157     -10.456   5.154  10.368  1.00 37.92      A    N  
ANISOU 1200  N   VAL A 157     7932   1965   4508  -1539   2544   -285  A    N  
ATOM   1201  CA  VAL A 157      -9.117   5.706  10.094  1.00 34.70      A    C  
ANISOU 1201  CA  VAL A 157     7443   1518   4225  -1263   2462   -249  A    C  
ATOM   1202  C   VAL A 157      -8.141   4.630   9.667  1.00 37.12      A    C  
ANISOU 1202  C   VAL A 157     8035   1650   4417  -1216   2548   -410  A    C  
ATOM   1203  O   VAL A 157      -7.764   3.794  10.477  1.00 36.54      A    O  
ANISOU 1203  O   VAL A 157     8293   1283   4308  -1090   2639   -504  A    O  
ATOM   1204  CB  VAL A 157      -8.544   6.504  11.293  1.00 35.41      A    C  
ANISOU 1204  CB  VAL A 157     7492   1441   4523   -950   2385   -183  A    C  
ATOM   1205  CG1 VAL A 157      -7.260   7.219  10.894  1.00 34.44      A    C  
ANISOU 1205  CG1 VAL A 157     7209   1347   4529   -724   2309   -161  A    C  
ATOM   1206  CG2 VAL A 157      -9.554   7.485  11.818  1.00 33.54      A    C  
ANISOU 1206  CG2 VAL A 157     7020   1322   4400   -993   2336    -38  A    C  
ATOM   1207  N   SER A 158      -7.657   4.723   8.413  1.00 35.51      A    N  
ANISOU 1207  N   SER A 158     7698   1634   4163  -1275   2528   -420  A    N  
ATOM   1208  CA  SER A 158      -6.699   3.809   7.812  1.00 36.38      A    C  
ANISOU 1208  CA  SER A 158     8034   1620   4167  -1232   2611   -564  A    C  
ATOM   1209  C   SER A 158      -5.288   4.282   8.143  1.00 41.82      A    C  
ANISOU 1209  C   SER A 158     8689   2197   5002   -864   2532   -539  A    C  
ATOM   1210  O   SER A 158      -4.938   5.419   7.833  1.00 41.13      A    O  
ANISOU 1210  O   SER A 158     8289   2284   5054   -776   2419   -427  A    O  
ATOM   1211  CB  SER A 158      -6.921   3.749   6.299  1.00 41.04      A    C  
ANISOU 1211  CB  SER A 158     8463   2509   4619  -1486   2623   -592  A    C  
ATOM   1212  OG  SER A 158      -5.994   2.885   5.664  1.00 48.51      A    O  
ANISOU 1212  OG  SER A 158     9624   3340   5469  -1450   2713   -738  A    O  
ATOM   1213  N   VAL A 159      -4.486   3.427   8.800  1.00 39.06      A    N  
ANISOU 1213  N   VAL A 159     8658   1569   4615   -643   2610   -643  A    N  
ATOM   1214  CA  VAL A 159      -3.119   3.769   9.217  1.00 37.80      A    C  
ANISOU 1214  CA  VAL A 159     8461   1345   4556   -280   2539   -648  A    C  
ATOM   1215  C   VAL A 159      -2.147   2.580   8.997  1.00 44.98      A    C  
ANISOU 1215  C   VAL A 159     9687   2074   5328   -117   2662   -776  A    C  
ATOM   1216  O   VAL A 159      -2.614   1.435   8.887  1.00 45.93      A    O  
ANISOU 1216  O   VAL A 159    10132   2021   5297   -259   2833   -859  A    O  
ATOM   1217  CB  VAL A 159      -3.065   4.231  10.716  1.00 40.01      A    C  
ANISOU 1217  CB  VAL A 159     8739   1517   4947    -45   2476   -603  A    C  
ATOM   1218  CG1 VAL A 159      -3.897   5.477  10.970  1.00 37.81      A    C  
ANISOU 1218  CG1 VAL A 159     8143   1395   4828   -162   2371   -479  A    C  
ATOM   1219  CG2 VAL A 159      -3.427   3.103  11.689  1.00 40.93      A    C  
ANISOU 1219  CG2 VAL A 159     9249   1365   4938     11   2610   -651  A    C  
ATOM   1220  N   PRO A 160      -0.794   2.801   9.000  1.00 41.70      A    N  
ANISOU 1220  N   PRO A 160     9200   1684   4960    189   2603   -804  A    N  
ATOM   1221  CA  PRO A 160       0.118   1.645   8.937  1.00 42.88      A    C  
ANISOU 1221  CA  PRO A 160     9667   1657   4970    405   2735   -905  A    C  
ATOM   1222  C   PRO A 160      -0.165   0.757  10.146  1.00 49.08      A    C  
ANISOU 1222  C   PRO A 160    10818   2163   5667    570   2861   -909  A    C  
ATOM   1223  O   PRO A 160      -0.307   1.277  11.255  1.00 46.11      A    O  
ANISOU 1223  O   PRO A 160    10363   1791   5365    719   2773   -846  A    O  
ATOM   1224  CB  PRO A 160       1.514   2.275   8.977  1.00 44.03      A    C  
ANISOU 1224  CB  PRO A 160     9585   1947   5196    719   2617   -919  A    C  
ATOM   1225  CG  PRO A 160       1.309   3.725   8.613  1.00 46.94      A    C  
ANISOU 1225  CG  PRO A 160     9525   2562   5749    566   2459   -844  A    C  
ATOM   1226  CD  PRO A 160      -0.045   4.070   9.143  1.00 41.34      A    C  
ANISOU 1226  CD  PRO A 160     8796   1822   5090    358   2443   -756  A    C  
ATOM   1227  N   LYS A 161      -0.312  -0.564   9.912  1.00 49.40      A    N  
ANISOU 1227  N   LYS A 161    11265   1956   5549    522   3091   -983  A    N  
ATOM   1228  CA  LYS A 161      -0.679  -1.599  10.881  1.00 52.19      A    C  
ANISOU 1228  CA  LYS A 161    12047   1987   5797    637   3292   -981  A    C  
ATOM   1229  C   LYS A 161       0.111  -1.587  12.211  1.00 58.66      A    C  
ANISOU 1229  C   LYS A 161    12936   2745   6607   1130   3250   -907  A    C  
ATOM   1230  O   LYS A 161      -0.452  -1.987  13.227  1.00 60.93      A    O  
ANISOU 1230  O   LYS A 161    13453   2846   6851   1198   3345   -855  A    O  
ATOM   1231  CB  LYS A 161      -0.594  -3.008  10.246  1.00 57.80      A    C  
ANISOU 1231  CB  LYS A 161    13189   2424   6350    568   3589  -1091  A    C  
ATOM   1232  CG  LYS A 161       0.749  -3.391   9.607  1.00 64.11      A    C  
ANISOU 1232  CG  LYS A 161    14042   3226   7090    857   3631  -1140  A    C  
ATOM   1233  CD  LYS A 161       0.835  -4.889   9.340  1.00 74.31      A    C  
ANISOU 1233  CD  LYS A 161    15857   4150   8226    880   3986  -1228  A    C  
ATOM   1234  CE  LYS A 161       1.664  -5.261   8.128  1.00 93.12      A    C  
ANISOU 1234  CE  LYS A 161    18261   6570  10551    876   4063  -1336  A    C  
ATOM   1235  NZ  LYS A 161       3.044  -4.701   8.158  1.00105.62      A    N1+
ANISOU 1235  NZ  LYS A 161    19611   8355  12164   1313   3889  -1282  A    N1+
ATOM   1236  N   GLU A 162       1.374  -1.135  12.222  1.00 55.16      A    N  
ANISOU 1236  N   GLU A 162    12285   2486   6188   1464   3115   -910  A    N  
ATOM   1237  CA  GLU A 162       2.207  -1.116  13.437  1.00 55.81      A    C  
ANISOU 1237  CA  GLU A 162    12382   2603   6222   1946   3063   -862  A    C  
ATOM   1238  C   GLU A 162       1.911   0.085  14.334  1.00 58.99      A    C  
ANISOU 1238  C   GLU A 162    12445   3212   6757   1945   2845   -820  A    C  
ATOM   1239  O   GLU A 162       2.512   0.222  15.404  1.00 59.34      A    O  
ANISOU 1239  O   GLU A 162    12450   3345   6752   2309   2781   -800  A    O  
ATOM   1240  CB  GLU A 162       3.709  -1.144  13.070  1.00 58.18      A    C  
ANISOU 1240  CB  GLU A 162    12566   3071   6470   2295   3015   -912  A    C  
ATOM   1241  CG  GLU A 162       4.270   0.134  12.458  1.00 66.44      A    C  
ANISOU 1241  CG  GLU A 162    13112   4459   7672   2191   2784   -968  A    C  
ATOM   1242  CD  GLU A 162       4.003   0.441  10.993  1.00 82.58      A    C  
ANISOU 1242  CD  GLU A 162    15016   6561   9799   1802   2776  -1009  A    C  
ATOM   1243  OE1 GLU A 162       3.403  -0.409  10.292  1.00 56.82      A    O  
ANISOU 1243  OE1 GLU A 162    12035   3098   6456   1576   2948  -1027  A    O  
ATOM   1244  OE2 GLU A 162       4.407   1.542  10.546  1.00 72.69      A    O1-
ANISOU 1244  OE2 GLU A 162    13368   5566   8685   1722   2612  -1030  A    O1-
ATOM   1245  N   LEU A 163       1.025   0.974  13.887  1.00 54.20      A    N  
ANISOU 1245  N   LEU A 163    11581   2706   6305   1555   2740   -810  A    N  
ATOM   1246  CA  LEU A 163       0.728   2.176  14.641  1.00 51.94      A    C  
ANISOU 1246  CA  LEU A 163    10972   2594   6168   1530   2562   -777  A    C  
ATOM   1247  C   LEU A 163      -0.691   2.173  15.202  1.00 54.50      A    C  
ANISOU 1247  C   LEU A 163    11404   2785   6519   1288   2607   -708  A    C  
ATOM   1248  O   LEU A 163      -1.601   1.520  14.673  1.00 53.52      A    O  
ANISOU 1248  O   LEU A 163    11489   2506   6341   1002   2742   -700  A    O  
ATOM   1249  CB  LEU A 163       0.976   3.434  13.786  1.00 49.99      A    C  
ANISOU 1249  CB  LEU A 163    10292   2599   6104   1343   2408   -798  A    C  
ATOM   1250  CG  LEU A 163       2.420   3.664  13.288  1.00 55.02      A    C  
ANISOU 1250  CG  LEU A 163    10744   3415   6744   1561   2346   -882  A    C  
ATOM   1251  CD1 LEU A 163       2.497   4.896  12.384  1.00 54.40      A    C  
ANISOU 1251  CD1 LEU A 163    10279   3535   6855   1326   2245   -883  A    C  
ATOM   1252  CD2 LEU A 163       3.411   3.828  14.445  1.00 56.54      A    C  
ANISOU 1252  CD2 LEU A 163    10846   3741   6895   1958   2270   -942  A    C  
ATOM   1253  N   MET A 164      -0.835   2.878  16.328  1.00 51.05      A    N  
ANISOU 1253  N   MET A 164    10816   2428   6153   1406   2502   -679  A    N  
ATOM   1254  CA  MET A 164      -2.081   3.106  17.048  1.00 50.66      A    C  
ANISOU 1254  CA  MET A 164    10802   2299   6149   1223   2515   -614  A    C  
ATOM   1255  C   MET A 164      -2.669   4.439  16.557  1.00 50.08      A    C  
ANISOU 1255  C   MET A 164    10334   2412   6283    937   2383   -584  A    C  
ATOM   1256  O   MET A 164      -1.902   5.367  16.270  1.00 49.21      A    O  
ANISOU 1256  O   MET A 164     9912   2490   6296   1006   2265   -619  A    O  
ATOM   1257  CB  MET A 164      -1.782   3.130  18.572  1.00 54.73      A    C  
ANISOU 1257  CB  MET A 164    11378   2813   6605   1557   2486   -603  A    C  
ATOM   1258  CG  MET A 164      -3.000   3.412  19.490  1.00 59.31      A    C  
ANISOU 1258  CG  MET A 164    11984   3319   7231   1407   2495   -538  A    C  
ATOM   1259  SD  MET A 164      -4.162   2.036  19.446  1.00 66.60      A    S  
ANISOU 1259  SD  MET A 164    13381   3912   8013   1189   2746   -484  A    S  
ATOM   1260  CE  MET A 164      -5.364   2.610  20.475  1.00 62.14      A    C  
ANISOU 1260  CE  MET A 164    12746   3344   7520   1056   2715   -422  A    C  
ATOM   1261  N   ALA A 165      -4.011   4.518  16.427  1.00 44.09      A    N  
ANISOU 1261  N   ALA A 165     9590   1606   5555    622   2425   -518  A    N  
ATOM   1262  CA  ALA A 165      -4.765   5.728  16.070  1.00 41.59      A    C  
ANISOU 1262  CA  ALA A 165     8930   1457   5415    383   2332   -448  A    C  
ATOM   1263  C   ALA A 165      -5.834   6.019  17.130  1.00 42.44      A    C  
ANISOU 1263  C   ALA A 165     9049   1513   5562    317   2337   -388  A    C  
ATOM   1264  O   ALA A 165      -6.482   5.086  17.596  1.00 39.59      A    O  
ANISOU 1264  O   ALA A 165     8985    986   5072    266   2451   -388  A    O  
ATOM   1265  CB  ALA A 165      -5.410   5.580  14.708  1.00 42.26      A    C  
ANISOU 1265  CB  ALA A 165     8962   1623   5472     62   2374   -414  A    C  
ATOM   1266  N   LEU A 166      -6.006   7.306  17.525  1.00 37.94      A    N  
ANISOU 1266  N   LEU A 166     8168   1074   5175    318   2240   -344  A    N  
ATOM   1267  CA  LEU A 166      -7.030   7.691  18.511  1.00 37.29      A    C  
ANISOU 1267  CA  LEU A 166     8013   1058   5097    246   2243   -271  A    C  
ATOM   1268  C   LEU A 166      -7.767   8.930  18.062  1.00 38.54      A    C  
ANISOU 1268  C   LEU A 166     7891   1262   5491     70   2202   -184  A    C  
ATOM   1269  O   LEU A 166      -7.158   9.815  17.467  1.00 38.81      A    O  
ANISOU 1269  O   LEU A 166     7677   1407   5662    100   2154   -175  A    O  
ATOM   1270  CB  LEU A 166      -6.457   7.903  19.934  1.00 37.29      A    C  
ANISOU 1270  CB  LEU A 166     7999   1099   5071    511   2198   -315  A    C  
ATOM   1271  CG  LEU A 166      -5.858   6.681  20.660  1.00 42.67      A    C  
ANISOU 1271  CG  LEU A 166     9116   1465   5631    803   2262   -412  A    C  
ATOM   1272  CD1 LEU A 166      -4.985   7.116  21.811  1.00 42.33      A    C  
ANISOU 1272  CD1 LEU A 166     8975   1518   5590   1119   2181   -495  A    C  
ATOM   1273  CD2 LEU A 166      -6.934   5.756  21.157  1.00 46.14      A    C  
ANISOU 1273  CD2 LEU A 166     9870   1719   5944    698   2391   -355  A    C  
ATOM   1274  N   MET A 167      -9.081   9.010  18.371  1.00 34.43      A    N  
ANISOU 1274  N   MET A 167     7226   1023   4832   -104   2240    -92  A    N  
ATOM   1275  CA  MET A 167      -9.895  10.187  18.018  1.00 32.29      A    C  
ANISOU 1275  CA  MET A 167     6585   1024   4660   -214   2220     11  A    C  
ATOM   1276  C   MET A 167     -10.700  10.703  19.233  1.00 34.14      A    C  
ANISOU 1276  C   MET A 167     6842   1091   5039   -204   2232     52  A    C  
ATOM   1277  O   MET A 167     -10.789  10.031  20.265  1.00 33.25      A    O  
ANISOU 1277  O   MET A 167     6849   1060   4723   -129   2256    -10  A    O  
ATOM   1278  CB  MET A 167     -10.827   9.884  16.824  1.00 33.57      A    C  
ANISOU 1278  CB  MET A 167     6816   1094   4847   -489   2254    101  A    C  
ATOM   1279  CG  MET A 167     -10.086   9.815  15.503  1.00 35.92      A    C  
ANISOU 1279  CG  MET A 167     7112   1347   5190   -542   2239    119  A    C  
ATOM   1280  SD  MET A 167     -11.043  10.069  13.983  1.00 39.67      A    S  
ANISOU 1280  SD  MET A 167     7349   2134   5589   -810   2252    263  A    S  
ATOM   1281  CE  MET A 167     -11.421  11.816  14.116  1.00 34.41      A    C  
ANISOU 1281  CE  MET A 167     6317   1586   5170   -710   2237    468  A    C  
ATOM   1282  N   SER A 168     -11.277  11.912  19.118  1.00 32.08      A    N  
ANISOU 1282  N   SER A 168     6216   1104   4869   -222   2230    134  A    N  
ATOM   1283  CA  SER A 168     -12.083  12.515  20.188  1.00 31.16      A    C  
ANISOU 1283  CA  SER A 168     5970   1084   4784   -191   2254    154  A    C  
ATOM   1284  C   SER A 168     -13.486  11.854  20.216  1.00 34.96      A    C  
ANISOU 1284  C   SER A 168     6738   1226   5319   -431   2300    269  A    C  
ATOM   1285  O   SER A 168     -14.533  12.508  20.092  1.00 34.82      A    O  
ANISOU 1285  O   SER A 168     6537   1314   5378   -523   2325    395  A    O  
ATOM   1286  CB  SER A 168     -12.168  14.025  20.005  1.00 32.47      A    C  
ANISOU 1286  CB  SER A 168     5916   1138   5283   -169   2281    269  A    C  
ATOM   1287  OG  SER A 168     -12.537  14.378  18.683  1.00 38.15      A    O  
ANISOU 1287  OG  SER A 168     6656   1631   6207   -331   2308    495  A    O  
ATOM   1288  N   ALA A 169     -13.470  10.533  20.393  1.00 33.55      A    N  
ANISOU 1288  N   ALA A 169     6755   1159   4833   -449   2325    141  A    N  
ATOM   1289  CA  ALA A 169     -14.625   9.656  20.390  1.00 33.77      A    C  
ANISOU 1289  CA  ALA A 169     6942   1178   4712   -661   2395    138  A    C  
ATOM   1290  C   ALA A 169     -14.318   8.339  21.111  1.00 38.38      A    C  
ANISOU 1290  C   ALA A 169     8104   1165   5313   -713   2484     97  A    C  
ATOM   1291  O   ALA A 169     -13.161   8.054  21.453  1.00 38.46      A    O  
ANISOU 1291  O   ALA A 169     8240   1091   5284   -473   2461     15  A    O  
ATOM   1292  CB  ALA A 169     -15.018   9.374  18.945  1.00 34.29      A    C  
ANISOU 1292  CB  ALA A 169     6980   1297   4752   -913   2405    192  A    C  
ATOM   1293  N   LEU A 170     -15.355   7.514  21.305  1.00 36.31      A    N  
ANISOU 1293  N   LEU A 170     7889   1126   4782   -866   2586     31  A    N  
ATOM   1294  CA  LEU A 170     -15.188   6.210  21.909  1.00 37.12      A    C  
ANISOU 1294  CA  LEU A 170     8380   1029   4694   -843   2718    -59  A    C  
ATOM   1295  C   LEU A 170     -14.648   5.259  20.852  1.00 41.61      A    C  
ANISOU 1295  C   LEU A 170     9284   1232   5293  -1004   2794   -101  A    C  
ATOM   1296  O   LEU A 170     -15.064   5.345  19.698  1.00 40.72      A    O  
ANISOU 1296  O   LEU A 170     8998   1320   5153  -1247   2783   -100  A    O  
ATOM   1297  CB  LEU A 170     -16.516   5.670  22.495  1.00 37.46      A    C  
ANISOU 1297  CB  LEU A 170     8554   1038   4639  -1059   2850    -77  A    C  
ATOM   1298  CG  LEU A 170     -17.267   6.507  23.526  1.00 39.69      A    C  
ANISOU 1298  CG  LEU A 170     8799   1121   5158  -1082   2819     45  A    C  
ATOM   1299  CD1 LEU A 170     -18.544   5.809  23.953  1.00 39.27      A    C  
ANISOU 1299  CD1 LEU A 170     8865   1106   4949  -1320   2970      0  A    C  
ATOM   1300  CD2 LEU A 170     -16.425   6.776  24.753  1.00 44.05      A    C  
ANISOU 1300  CD2 LEU A 170     9487   1450   5800   -745   2774     52  A    C  
ATOM   1301  N   ARG A 171     -13.715   4.378  21.231  1.00 40.32      A    N  
ANISOU 1301  N   ARG A 171     9405    932   4984   -777   2870   -172  A    N  
ATOM   1302  CA  ARG A 171     -13.159   3.371  20.331  1.00 42.15      A    C  
ANISOU 1302  CA  ARG A 171     9923    948   5144   -853   2976   -255  A    C  
ATOM   1303  C   ARG A 171     -14.280   2.430  19.921  1.00 47.01      A    C  
ANISOU 1303  C   ARG A 171    10722   1518   5620  -1249   3174   -332  A    C  
ATOM   1304  O   ARG A 171     -15.075   2.064  20.787  1.00 47.61      A    O  
ANISOU 1304  O   ARG A 171    10964   1473   5652  -1335   3295   -332  A    O  
ATOM   1305  CB  ARG A 171     -12.021   2.587  21.025  1.00 47.25      A    C  
ANISOU 1305  CB  ARG A 171    10918   1326   5708   -493   3052   -284  A    C  
ATOM   1306  CG  ARG A 171     -10.813   3.466  21.392  1.00 61.35      A    C  
ANISOU 1306  CG  ARG A 171    12493   3217   7602   -123   2858   -256  A    C  
ATOM   1307  CD  ARG A 171      -9.922   2.732  22.380  1.00 72.35      A    C  
ANISOU 1307  CD  ARG A 171    14196   4417   8878    265   2928   -264  A    C  
ATOM   1308  NE  ARG A 171      -9.624   3.502  23.594  1.00 77.05      A    N  
ANISOU 1308  NE  ARG A 171    14647   5097   9532    529   2806   -232  A    N  
ATOM   1309  CZ  ARG A 171     -10.410   3.561  24.664  1.00 90.77      A    C  
ANISOU 1309  CZ  ARG A 171    16467   6770  11250    519   2857   -189  A    C  
ATOM   1310  NH1 ARG A 171     -11.582   2.939  24.673  1.00 82.43      A    N1+
ANISOU 1310  NH1 ARG A 171    15624   5566  10129    244   3029   -170  A    N1+
ATOM   1311  NH2 ARG A 171     -10.036   4.251  25.727  1.00 79.61      A    N  
ANISOU 1311  NH2 ARG A 171    14912   5459   9876    766   2747   -184  A    N  
ATOM   1312  N   ASP A 172     -14.397   2.085  18.616  1.00 43.73      A    N  
ANISOU 1312  N   ASP A 172    10254   1229   5133  -1515   3214   -412  A    N  
ATOM   1313  CA  ASP A 172     -15.476   1.210  18.153  1.00 46.26      A    C  
ANISOU 1313  CA  ASP A 172    10709   1561   5307  -1947   3412   -534  A    C  
ATOM   1314  C   ASP A 172     -14.932   0.012  17.366  1.00 53.25      A    C  
ANISOU 1314  C   ASP A 172    11919   2258   6057  -2052   3605   -686  A    C  
ATOM   1315  O   ASP A 172     -15.633  -0.550  16.518  1.00 54.43      A    O  
ANISOU 1315  O   ASP A 172    12074   2522   6086  -2455   3735   -827  A    O  
ATOM   1316  CB  ASP A 172     -16.542   1.994  17.339  1.00 47.93      A    C  
ANISOU 1316  CB  ASP A 172    10473   2213   5523  -2263   3297   -508  A    C  
ATOM   1317  CG  ASP A 172     -17.823   1.205  17.063  1.00 58.54      A    C  
ANISOU 1317  CG  ASP A 172    11885   3652   6706  -2734   3489   -652  A    C  
ATOM   1318  OD1 ASP A 172     -18.329   0.544  17.989  1.00 58.48      A    O  
ANISOU 1318  OD1 ASP A 172    12151   3410   6660  -2808   3664   -698  A    O  
ATOM   1319  OD2 ASP A 172     -18.285   1.214  15.915  1.00 67.26      A    O1-
ANISOU 1319  OD2 ASP A 172    12772   5074   7708  -3033   3479   -731  A    O1-
ATOM   1320  N   GLY A 173     -13.704  -0.396  17.683  1.00 50.95      A    N  
ANISOU 1320  N   GLY A 173    11895   1692   5770  -1690   3639   -670  A    N  
ATOM   1321  CA  GLY A 173     -13.079  -1.552  17.057  1.00 52.78      A    C  
ANISOU 1321  CA  GLY A 173    12481   1691   5884  -1718   3850   -797  A    C  
ATOM   1322  C   GLY A 173     -12.124  -1.296  15.910  1.00 57.23      A    C  
ANISOU 1322  C   GLY A 173    12870   2411   6463  -1637   3722   -820  A    C  
ATOM   1323  O   GLY A 173     -12.118  -0.225  15.293  1.00 56.11      A    O  
ANISOU 1323  O   GLY A 173    12296   2614   6409  -1665   3483   -754  A    O  
ATOM   1324  N   GLU A 174     -11.308  -2.312  15.639  1.00 55.11      A    N  
ANISOU 1324  N   GLU A 174    12965   1869   6106  -1521   3911   -905  A    N  
ATOM   1325  CA  GLU A 174     -10.306  -2.370  14.589  1.00 56.04      A    C  
ANISOU 1325  CA  GLU A 174    13028   2056   6209  -1429   3859   -953  A    C  
ATOM   1326  C   GLU A 174     -10.852  -3.207  13.442  1.00 64.96      A    C  
ANISOU 1326  C   GLU A 174    14274   3205   7204  -1882   4065  -1152  A    C  
ATOM   1327  O   GLU A 174     -11.606  -4.154  13.671  1.00 66.60      A    O  
ANISOU 1327  O   GLU A 174    14806   3185   7313  -2148   4350  -1275  A    O  
ATOM   1328  CB  GLU A 174      -8.976  -2.953  15.113  1.00 57.97      A    C  
ANISOU 1328  CB  GLU A 174    13599   1995   6430   -949   3944   -912  A    C  
ATOM   1329  CG  GLU A 174      -8.402  -2.212  16.317  1.00 67.22      A    C  
ANISOU 1329  CG  GLU A 174    14661   3185   7696   -503   3758   -751  A    C  
ATOM   1330  CD  GLU A 174      -7.146  -2.797  16.946  1.00 89.17      A    C  
ANISOU 1330  CD  GLU A 174    17731   5737  10411      4   3837   -701  A    C  
ATOM   1331  OE1 GLU A 174      -6.485  -3.638  16.292  1.00 83.28      A    O  
ANISOU 1331  OE1 GLU A 174    17229   4835   9578     75   4000   -770  A    O  
ATOM   1332  OE2 GLU A 174      -6.810  -2.397  18.085  1.00 80.36      A    O1-
ANISOU 1332  OE2 GLU A 174    16581   4631   9322    347   3736   -593  A    O1-
ATOM   1333  N   LEU A 175     -10.493  -2.827  12.211  1.00 62.88      A    N  
ANISOU 1333  N   LEU A 175    13734   3226   6931  -1988   3933  -1195  A    N  
ATOM   1334  CA  LEU A 175     -10.920  -3.473  10.967  1.00 65.30      A    C  
ANISOU 1334  CA  LEU A 175    14066   3652   7094  -2422   4086  -1400  A    C  
ATOM   1335  C   LEU A 175      -9.701  -3.758  10.077  1.00 67.75      A    C  
ANISOU 1335  C   LEU A 175    14444   3922   7375  -2256   4096  -1453  A    C  
ATOM   1336  O   LEU A 175      -8.684  -3.071  10.173  1.00 63.98      A    O  
ANISOU 1336  O   LEU A 175    13801   3503   7004  -1873   3889  -1313  A    O  
ATOM   1337  CB  LEU A 175     -11.925  -2.532  10.250  1.00 64.76      A    C  
ANISOU 1337  CB  LEU A 175    13487   4108   7010  -2759   3884  -1382  A    C  
ATOM   1338  CG  LEU A 175     -12.944  -3.137   9.272  1.00 71.96      A    C  
ANISOU 1338  CG  LEU A 175    14358   5252   7731  -3321   4046  -1613  A    C  
ATOM   1339  CD1 LEU A 175     -13.873  -4.142   9.968  1.00 74.74      A    C  
ANISOU 1339  CD1 LEU A 175    15043   5351   8004  -3620   4341  -1767  A    C  
ATOM   1340  CD2 LEU A 175     -13.794  -2.042   8.646  1.00 72.26      A    C  
ANISOU 1340  CD2 LEU A 175    13832   5881   7742  -3517   3798  -1530  A    C  
ATOM   1341  N   SER A 176      -9.795  -4.782   9.237  1.00 67.82      A    N  
ANISOU 1341  N   SER A 176    14701   3826   7239  -2554   4355  -1675  A    N  
ATOM   1342  CA  SER A 176      -8.717  -5.157   8.317  1.00 68.37      A    C  
ANISOU 1342  CA  SER A 176    14861   3853   7265  -2439   4402  -1753  A    C  
ATOM   1343  C   SER A 176      -8.903  -4.445   6.985  1.00 72.92      A    C  
ANISOU 1343  C   SER A 176    14981   4934   7789  -2700   4202  -1793  A    C  
ATOM   1344  O   SER A 176     -10.007  -4.470   6.428  1.00 73.93      A    O  
ANISOU 1344  O   SER A 176    14939   5346   7804  -3157   4235  -1918  A    O  
ATOM   1345  CB  SER A 176      -8.685  -6.670   8.106  1.00 74.46      A    C  
ANISOU 1345  CB  SER A 176    16168   4218   7906  -2617   4826  -1981  A    C  
ATOM   1346  OG  SER A 176      -9.906  -7.135   7.552  1.00 84.01      A    O  
ANISOU 1346  OG  SER A 176    17372   5564   8984  -3210   5004  -2213  A    O  
ATOM   1347  N   GLU A 177      -7.841  -3.774   6.494  1.00 67.95      A    N  
ANISOU 1347  N   GLU A 177    14134   4453   7232  -2403   3997  -1683  A    N  
ATOM   1348  CA  GLU A 177      -7.879  -3.123   5.197  1.00 66.53      A    C  
ANISOU 1348  CA  GLU A 177    13551   4732   6996  -2595   3830  -1695  A    C  
ATOM   1349  C   GLU A 177      -7.587  -4.221   4.201  1.00 73.24      A    C  
ANISOU 1349  C   GLU A 177    14656   5494   7680  -2822   4074  -1945  A    C  
ATOM   1350  O   GLU A 177      -6.463  -4.720   4.154  1.00 72.20      A    O  
ANISOU 1350  O   GLU A 177    14777   5087   7569  -2542   4169  -1969  A    O  
ATOM   1351  CB  GLU A 177      -6.887  -1.943   5.116  1.00 64.61      A    C  
ANISOU 1351  CB  GLU A 177    12982   4659   6909  -2205   3545  -1479  A    C  
ATOM   1352  CG  GLU A 177      -6.940  -1.214   3.785  1.00 71.92      A    C  
ANISOU 1352  CG  GLU A 177    13493   6057   7775  -2376   3389  -1452  A    C  
ATOM   1353  CD  GLU A 177      -6.938   0.300   3.861  1.00 86.02      A    C  
ANISOU 1353  CD  GLU A 177    14831   8135   9717  -2190   3112  -1198  A    C  
ATOM   1354  OE1 GLU A 177      -5.898   0.914   3.528  1.00 80.45      A    O  
ANISOU 1354  OE1 GLU A 177    13987   7466   9114  -1917   2996  -1102  A    O  
ATOM   1355  OE2 GLU A 177      -8.000   0.875   4.183  1.00 72.73      A    O1-
ANISOU 1355  OE2 GLU A 177    12929   6656   8047  -2334   3032  -1101  A    O1-
ATOM   1356  N   GLN A 178      -8.623  -4.662   3.478  1.00 74.20      A    N  
ANISOU 1356  N   GLN A 178    14728   5841   7625  -3335   4202  -2152  A    N  
ATOM   1357  CA  GLN A 178      -8.537  -5.756   2.507  1.00 78.05      A    C  
ANISOU 1357  CA  GLN A 178    15452   6272   7932  -3652   4473  -2448  A    C  
ATOM   1358  C   GLN A 178      -7.684  -5.376   1.289  1.00 82.58      A    C  
ANISOU 1358  C   GLN A 178    15786   7131   8459  -3568   4333  -2439  A    C  
ATOM   1359  O   GLN A 178      -7.113  -6.266   0.654  1.00 84.35      A    O  
ANISOU 1359  O   GLN A 178    16282   7176   8591  -3636   4551  -2638  A    O  
ATOM   1360  CB  GLN A 178      -9.940  -6.202   2.061  1.00 82.24      A    C  
ANISOU 1360  CB  GLN A 178    15904   7075   8269  -4262   4619  -2692  A    C  
ATOM   1361  CG  GLN A 178     -10.243  -7.672   2.356  1.00107.20      A    C  
ANISOU 1361  CG  GLN A 178    19609   9783  11339  -4559   5069  -2998  A    C  
ATOM   1362  CD  GLN A 178     -10.571  -7.927   3.811  1.00128.53      A    C  
ANISOU 1362  CD  GLN A 178    22648  12027  14162  -4411   5215  -2911  A    C  
ATOM   1363  NE2 GLN A 178      -9.652  -8.560   4.528  1.00122.41      A    N  
ANISOU 1363  NE2 GLN A 178    22392  10659  13459  -4102   5469  -2904  A    N  
ATOM   1364  OE1 GLN A 178     -11.651  -7.583   4.302  1.00123.50      A    O  
ANISOU 1364  OE1 GLN A 178    21816  11569  13538  -4564   5119  -2847  A    O  
ATOM   1365  N   SER A 179      -7.587  -4.064   0.982  1.00 77.01      A    N  
ANISOU 1365  N   SER A 179    14592   6844   7823  -3413   3996  -2206  A    N  
ATOM   1366  CA  SER A 179      -6.798  -3.524  -0.137  1.00 76.31      A    C  
ANISOU 1366  CA  SER A 179    14229   7059   7705  -3308   3842  -2149  A    C  
ATOM   1367  C   SER A 179      -5.299  -3.431   0.198  1.00 77.40      A    C  
ANISOU 1367  C   SER A 179    14522   6878   8010  -2807   3801  -2031  A    C  
ATOM   1368  O   SER A 179      -4.466  -3.679  -0.677  1.00 77.03      A    O  
ANISOU 1368  O   SER A 179    14489   6876   7904  -2756   3834  -2106  A    O  
ATOM   1369  CB  SER A 179      -7.316  -2.147  -0.541  1.00 79.32      A    C  
ANISOU 1369  CB  SER A 179    14058   7977   8104  -3318   3545  -1922  A    C  
ATOM   1370  OG  SER A 179      -8.666  -2.208  -0.971  1.00 93.88      A    O  
ANISOU 1370  OG  SER A 179    15694  10232   9745  -3768   3568  -2035  A    O  
ATOM   1371  N   ASP A 180      -4.955  -3.052   1.449  1.00 72.09      A    N  
ANISOU 1371  N   ASP A 180    13937   5926   7527  -2441   3724  -1856  A    N  
ATOM   1372  CA  ASP A 180      -3.559  -2.926   1.878  1.00 70.37      A    C  
ANISOU 1372  CA  ASP A 180    13827   5465   7447  -1956   3675  -1755  A    C  
ATOM   1373  C   ASP A 180      -3.314  -3.685   3.187  1.00 74.61      A    C  
ANISOU 1373  C   ASP A 180    14793   5517   8040  -1699   3841  -1758  A    C  
ATOM   1374  O   ASP A 180      -3.761  -3.263   4.256  1.00 74.43      A    O  
ANISOU 1374  O   ASP A 180    14742   5427   8113  -1608   3764  -1636  A    O  
ATOM   1375  CB  ASP A 180      -3.138  -1.450   2.004  1.00 68.89      A    C  
ANISOU 1375  CB  ASP A 180    13205   5537   7432  -1695   3369  -1510  A    C  
ATOM   1376  CG  ASP A 180      -1.644  -1.196   1.895  1.00 77.08      A    C  
ANISOU 1376  CG  ASP A 180    14217   6505   8563  -1302   3301  -1459  A    C  
ATOM   1377  OD1 ASP A 180      -0.858  -2.085   2.279  1.00 77.14      A    O  
ANISOU 1377  OD1 ASP A 180    14576   6188   8546  -1076   3458  -1548  A    O  
ATOM   1378  OD2 ASP A 180      -1.261  -0.091   1.455  1.00 86.38      A    O1-
ANISOU 1378  OD2 ASP A 180    15024   7956   9839  -1207   3106  -1323  A    O1-
ATOM   1379  N   SER A 181      -2.574  -4.802   3.081  1.00 71.80      A    N  
ANISOU 1379  N   SER A 181    14836   4830   7614  -1561   4085  -1888  A    N  
ATOM   1380  CA  SER A 181      -2.182  -5.718   4.163  1.00 71.27      A    C  
ANISOU 1380  CA  SER A 181    15241   4281   7558  -1264   4309  -1886  A    C  
ATOM   1381  C   SER A 181      -1.245  -5.036   5.161  1.00 70.02      A    C  
ANISOU 1381  C   SER A 181    14976   4090   7540   -722   4110  -1676  A    C  
ATOM   1382  O   SER A 181      -1.191  -5.443   6.325  1.00 69.85      A    O  
ANISOU 1382  O   SER A 181    15233   3773   7534   -458   4215  -1609  A    O  
ATOM   1383  CB  SER A 181      -1.509  -6.953   3.576  1.00 75.70      A    C  
ANISOU 1383  CB  SER A 181    16216   4548   8000  -1236   4630  -2065  A    C  
ATOM   1384  OG  SER A 181      -2.313  -7.462   2.527  1.00 85.64      A    O  
ANISOU 1384  OG  SER A 181    17500   5916   9121  -1775   4791  -2296  A    O  
ATOM   1385  N   ASN A 182      -0.516  -3.993   4.692  1.00 62.48      A    N  
ANISOU 1385  N   ASN A 182    13610   3456   6674   -569   3839  -1584  A    N  
ATOM   1386  CA  ASN A 182       0.370  -3.149   5.498  1.00 59.35      A    C  
ANISOU 1386  CA  ASN A 182    13012   3126   6411   -125   3626  -1425  A    C  
ATOM   1387  C   ASN A 182      -0.433  -2.160   6.336  1.00 56.41      A    C  
ANISOU 1387  C   ASN A 182    12382   2887   6163   -177   3431  -1291  A    C  
ATOM   1388  O   ASN A 182       0.177  -1.379   7.070  1.00 52.86      A    O  
ANISOU 1388  O   ASN A 182    11739   2515   5831    137   3257  -1183  A    O  
ATOM   1389  CB  ASN A 182       1.361  -2.358   4.609  1.00 58.80      A    C  
ANISOU 1389  CB  ASN A 182    12595   3349   6399    -11   3448  -1406  A    C  
ATOM   1390  CG  ASN A 182       2.468  -3.162   3.963  1.00 78.83      A    C  
ANISOU 1390  CG  ASN A 182    15338   5775   8838    175   3600  -1511  A    C  
ATOM   1391  ND2 ASN A 182       2.964  -2.674   2.829  1.00 64.03      A    N  
ANISOU 1391  ND2 ASN A 182    13198   4162   6968     82   3507  -1542  A    N  
ATOM   1392  OD1 ASN A 182       2.945  -4.171   4.501  1.00 75.85      A    O  
ANISOU 1392  OD1 ASN A 182    15346   5088   8384    442   3802  -1546  A    O  
ATOM   1393  N   ARG A 183      -1.790  -2.189   6.234  1.00 52.20      A    N  
ANISOU 1393  N   ARG A 183    11833   2401   5598   -578   3468  -1313  A    N  
ATOM   1394  CA  ARG A 183      -2.638  -1.233   6.929  1.00 50.59      A    C  
ANISOU 1394  CA  ARG A 183    11371   2344   5508   -654   3297  -1184  A    C  
ATOM   1395  C   ARG A 183      -3.758  -1.816   7.811  1.00 56.59      A    C  
ANISOU 1395  C   ARG A 183    12387   2893   6221   -820   3441  -1203  A    C  
ATOM   1396  O   ARG A 183      -4.322  -2.877   7.534  1.00 58.93      A    O  
ANISOU 1396  O   ARG A 183    12995   3013   6383  -1078   3685  -1346  A    O  
ATOM   1397  CB  ARG A 183      -3.259  -0.258   5.915  1.00 50.24      A    C  
ANISOU 1397  CB  ARG A 183    10899   2699   5493   -958   3135  -1136  A    C  
ATOM   1398  CG  ARG A 183      -2.285   0.856   5.528  1.00 50.32      A    C  
ANISOU 1398  CG  ARG A 183    10560   2930   5630   -738   2939  -1036  A    C  
ATOM   1399  CD  ARG A 183      -2.726   1.673   4.342  1.00 52.83      A    C  
ANISOU 1399  CD  ARG A 183    10509   3621   5941   -998   2834   -974  A    C  
ATOM   1400  NE  ARG A 183      -1.779   2.763   4.094  1.00 57.86      A    N  
ANISOU 1400  NE  ARG A 183    10837   4419   6730   -776   2681   -863  A    N  
ATOM   1401  CZ  ARG A 183      -1.855   3.969   4.648  1.00 62.28      A    C  
ANISOU 1401  CZ  ARG A 183    11127   5064   7471   -661   2544   -714  A    C  
ATOM   1402  NH1 ARG A 183      -2.845   4.264   5.479  1.00 46.54      A    N1+
ANISOU 1402  NH1 ARG A 183     9123   3032   5529   -727   2519   -644  A    N1+
ATOM   1403  NH2 ARG A 183      -0.939   4.887   4.380  1.00 52.52      A    N  
ANISOU 1403  NH2 ARG A 183     9638   3944   6373   -490   2453   -646  A    N  
ATOM   1404  N   LYS A 184      -4.117  -1.034   8.850  1.00 50.51      A    N  
ANISOU 1404  N   LYS A 184    11460   2161   5570   -702   3296  -1070  A    N  
ATOM   1405  CA  LYS A 184      -5.195  -1.315   9.803  1.00 49.95      A    C  
ANISOU 1405  CA  LYS A 184    11554   1939   5484   -834   3388  -1054  A    C  
ATOM   1406  C   LYS A 184      -6.217  -0.183   9.718  1.00 50.48      A    C  
ANISOU 1406  C   LYS A 184    11216   2325   5640  -1070   3201   -959  A    C  
ATOM   1407  O   LYS A 184      -5.858   0.909   9.277  1.00 47.83      A    O  
ANISOU 1407  O   LYS A 184    10508   2250   5415   -989   2997   -862  A    O  
ATOM   1408  CB  LYS A 184      -4.615  -1.421  11.229  1.00 51.73      A    C  
ANISOU 1408  CB  LYS A 184    11977   1922   5755   -407   3395   -970  A    C  
ATOM   1409  CG  LYS A 184      -5.408  -2.311  12.166  1.00 65.87      A    C  
ANISOU 1409  CG  LYS A 184    14150   3408   7468   -473   3617   -989  A    C  
ATOM   1410  CD  LYS A 184      -4.930  -2.216  13.614  1.00 75.73      A    C  
ANISOU 1410  CD  LYS A 184    15517   4505   8752    -37   3583   -873  A    C  
ATOM   1411  CE  LYS A 184      -3.646  -2.954  13.923  1.00 92.65      A    C  
ANISOU 1411  CE  LYS A 184    17944   6447  10811    417   3693   -866  A    C  
ATOM   1412  NZ  LYS A 184      -3.114  -2.605  15.267  1.00100.63      A    N1+
ANISOU 1412  NZ  LYS A 184    18939   7456  11839    858   3592   -749  A    N1+
ATOM   1413  N   ILE A 185      -7.474  -0.432  10.132  1.00 46.23      A    N  
ANISOU 1413  N   ILE A 185    10749   1763   5052  -1352   3290   -981  A    N  
ATOM   1414  CA  ILE A 185      -8.539   0.577  10.147  1.00 44.07      A    C  
ANISOU 1414  CA  ILE A 185    10106   1793   4844  -1555   3137   -879  A    C  
ATOM   1415  C   ILE A 185      -9.138   0.665  11.557  1.00 47.36      A    C  
ANISOU 1415  C   ILE A 185    10629   2041   5326  -1466   3153   -809  A    C  
ATOM   1416  O   ILE A 185      -9.806  -0.271  11.999  1.00 48.60      A    O  
ANISOU 1416  O   ILE A 185    11092   1993   5382  -1641   3354   -901  A    O  
ATOM   1417  CB  ILE A 185      -9.631   0.288   9.074  1.00 48.05      A    C  
ANISOU 1417  CB  ILE A 185    10490   2571   5195  -2035   3208   -984  A    C  
ATOM   1418  CG1 ILE A 185      -9.074   0.492   7.659  1.00 47.95      A    C  
ANISOU 1418  CG1 ILE A 185    10278   2817   5123  -2101   3145  -1017  A    C  
ATOM   1419  CG2 ILE A 185     -10.915   1.138   9.318  1.00 47.77      A    C  
ANISOU 1419  CG2 ILE A 185    10122   2834   5194  -2223   3093   -872  A    C  
ATOM   1420  CD1 ILE A 185      -9.894  -0.169   6.579  1.00 59.72      A    C  
ANISOU 1420  CD1 ILE A 185    11756   4533   6401  -2559   3274  -1195  A    C  
ATOM   1421  N   TYR A 186      -8.894   1.774  12.262  1.00 41.66      A    N  
ANISOU 1421  N   TYR A 186     9664   1396   4770  -1211   2964   -660  A    N  
ATOM   1422  CA  TYR A 186      -9.472   1.990  13.594  1.00 40.75      A    C  
ANISOU 1422  CA  TYR A 186     9600   1164   4719  -1123   2958   -590  A    C  
ATOM   1423  C   TYR A 186     -10.810   2.694  13.422  1.00 44.33      A    C  
ANISOU 1423  C   TYR A 186     9755   1890   5200  -1418   2893   -521  A    C  
ATOM   1424  O   TYR A 186     -10.966   3.482  12.494  1.00 44.95      A    O  
ANISOU 1424  O   TYR A 186     9489   2277   5314  -1522   2775   -456  A    O  
ATOM   1425  CB  TYR A 186      -8.519   2.787  14.506  1.00 40.16      A    C  
ANISOU 1425  CB  TYR A 186     9419   1045   4794   -709   2808   -500  A    C  
ATOM   1426  CG  TYR A 186      -7.272   2.029  14.913  1.00 42.08      A    C  
ANISOU 1426  CG  TYR A 186     9961   1052   4975   -369   2880   -557  A    C  
ATOM   1427  CD1 TYR A 186      -7.223   1.321  16.112  1.00 45.26      A    C  
ANISOU 1427  CD1 TYR A 186    10693   1196   5309   -164   2996   -556  A    C  
ATOM   1428  CD2 TYR A 186      -6.152   1.982  14.078  1.00 41.25      A    C  
ANISOU 1428  CD2 TYR A 186     9813    999   4861   -234   2845   -602  A    C  
ATOM   1429  CE1 TYR A 186      -6.091   0.584  16.473  1.00 46.58      A    C  
ANISOU 1429  CE1 TYR A 186    11133   1177   5387    194   3078   -582  A    C  
ATOM   1430  CE2 TYR A 186      -4.997   1.297  14.456  1.00 42.17      A    C  
ANISOU 1430  CE2 TYR A 186    10182    937   4904    112   2912   -643  A    C  
ATOM   1431  CZ  TYR A 186      -4.973   0.598  15.657  1.00 50.65      A    C  
ANISOU 1431  CZ  TYR A 186    11576   1771   5897    340   3029   -626  A    C  
ATOM   1432  OH  TYR A 186      -3.853  -0.107  16.034  1.00 50.75      A    O  
ANISOU 1432  OH  TYR A 186    11836   1637   5808    726   3110   -641  A    O  
ATOM   1433  N   ARG A 187     -11.795   2.363  14.245  1.00 41.92      A    N  
ANISOU 1433  N   ARG A 187     9584   1489   4856  -1555   2989   -532  A    N  
ATOM   1434  CA  ARG A 187     -13.125   2.964  14.134  1.00 41.13      A    C  
ANISOU 1434  CA  ARG A 187     9201   1667   4758  -1829   2943   -472  A    C  
ATOM   1435  C   ARG A 187     -13.510   3.602  15.432  1.00 42.95      A    C  
ANISOU 1435  C   ARG A 187     9376   1826   5117  -1660   2881   -361  A    C  
ATOM   1436  O   ARG A 187     -13.118   3.124  16.504  1.00 41.93      A    O  
ANISOU 1436  O   ARG A 187     9540   1396   4995  -1455   2952   -382  A    O  
ATOM   1437  CB  ARG A 187     -14.189   1.958  13.711  1.00 43.48      A    C  
ANISOU 1437  CB  ARG A 187     9657   1998   4864  -2254   3137   -627  A    C  
ATOM   1438  CG  ARG A 187     -13.873   1.206  12.432  1.00 48.98      A    C  
ANISOU 1438  CG  ARG A 187    10443   2756   5410  -2469   3237   -785  A    C  
ATOM   1439  CD  ARG A 187     -14.638  -0.093  12.417  1.00 61.01      A    C  
ANISOU 1439  CD  ARG A 187    12282   4139   6758  -2844   3511   -995  A    C  
ATOM   1440  NE  ARG A 187     -15.977   0.083  11.860  1.00 72.85      A    N  
ANISOU 1440  NE  ARG A 187    13482   6057   8140  -3266   3505  -1054  A    N  
ATOM   1441  CZ  ARG A 187     -16.831  -0.908  11.628  1.00 94.14      A    C  
ANISOU 1441  CZ  ARG A 187    16340   8766  10661  -3699   3736  -1278  A    C  
ATOM   1442  NH1 ARG A 187     -16.503  -2.161  11.925  1.00 88.03      A    N1+
ANISOU 1442  NH1 ARG A 187    16070   7546   9831  -3767   4022  -1450  A    N1+
ATOM   1443  NH2 ARG A 187     -18.020  -0.656  11.105  1.00 81.08      A    N  
ANISOU 1443  NH2 ARG A 187    14346   7581   8880  -4066   3704  -1334  A    N  
ATOM   1444  N   PHE A 188     -14.242   4.732  15.323  1.00 37.52      A    N  
ANISOU 1444  N   PHE A 188     8304   1430   4525  -1716   2753   -229  A    N  
ATOM   1445  CA  PHE A 188     -14.630   5.582  16.439  1.00 35.00      A    C  
ANISOU 1445  CA  PHE A 188     7790   1238   4269  -1493   2671   -155  A    C  
ATOM   1446  C   PHE A 188     -16.049   6.093  16.305  1.00 39.75      A    C  
ANISOU 1446  C   PHE A 188     8191   1980   4934  -1803   2674    -32  A    C  
ATOM   1447  O   PHE A 188     -16.500   6.408  15.200  1.00 39.33      A    O  
ANISOU 1447  O   PHE A 188     7874   2255   4814  -1985   2638      8  A    O  
ATOM   1448  CB  PHE A 188     -13.664   6.777  16.538  1.00 33.43      A    C  
ANISOU 1448  CB  PHE A 188     7325   1144   4235  -1158   2517    -66  A    C  
ATOM   1449  CG  PHE A 188     -12.211   6.379  16.590  1.00 33.18      A    C  
ANISOU 1449  CG  PHE A 188     7451    984   4171   -914   2514   -133  A    C  
ATOM   1450  CD1 PHE A 188     -11.596   6.101  17.801  1.00 34.54      A    C  
ANISOU 1450  CD1 PHE A 188     7862    883   4377   -690   2537   -151  A    C  
ATOM   1451  CD2 PHE A 188     -11.464   6.259  15.423  1.00 34.80      A    C  
ANISOU 1451  CD2 PHE A 188     7716   1048   4458   -982   2496   -134  A    C  
ATOM   1452  CE1 PHE A 188     -10.268   5.679  17.843  1.00 35.46      A    C  
ANISOU 1452  CE1 PHE A 188     8153    845   4477   -460   2533   -204  A    C  
ATOM   1453  CE2 PHE A 188     -10.134   5.847  15.464  1.00 36.90      A    C  
ANISOU 1453  CE2 PHE A 188     8195   1068   4757   -764   2497   -205  A    C  
ATOM   1454  CZ  PHE A 188      -9.547   5.547  16.673  1.00 35.02      A    C  
ANISOU 1454  CZ  PHE A 188     8052    849   4403   -478   2514   -236  A    C  
ATOM   1455  N   LYS A 189     -16.731   6.221  17.456  1.00 37.66      A    N  
ANISOU 1455  N   LYS A 189     7972   1621   4715  -1780   2704      0  A    N  
ATOM   1456  CA  LYS A 189     -18.101   6.718  17.529  1.00 38.41      A    C  
ANISOU 1456  CA  LYS A 189     7815   1983   4795  -1974   2704     81  A    C  
ATOM   1457  C   LYS A 189     -18.215   7.892  18.476  1.00 41.44      A    C  
ANISOU 1457  C   LYS A 189     8020   2345   5378  -1733   2622    227  A    C  
ATOM   1458  O   LYS A 189     -17.783   7.821  19.634  1.00 41.08      A    O  
ANISOU 1458  O   LYS A 189     8178   2022   5407  -1540   2637    197  A    O  
ATOM   1459  CB  LYS A 189     -19.092   5.612  17.927  1.00 43.02      A    C  
ANISOU 1459  CB  LYS A 189     8634   2504   5207  -2279   2874    -56  A    C  
ATOM   1460  CG  LYS A 189     -18.669   4.770  19.128  1.00 55.10      A    C  
ANISOU 1460  CG  LYS A 189    10606   3598   6731  -2150   2996   -143  A    C  
ATOM   1461  CD  LYS A 189     -19.632   3.648  19.408  1.00 59.38      A    C  
ANISOU 1461  CD  LYS A 189    11400   4052   7108  -2479   3211   -280  A    C  
ATOM   1462  CE  LYS A 189     -19.346   2.969  20.735  1.00 68.11      A    C  
ANISOU 1462  CE  LYS A 189    12934   4734   8212  -2304   3350   -312  A    C  
ATOM   1463  NZ  LYS A 189     -18.096   2.158  20.718  1.00 70.71      A    N1+
ANISOU 1463  NZ  LYS A 189    13629   4745   8493  -2116   3436   -381  A    N1+
ATOM   1464  N   GLN A 190     -18.785   8.987  17.968  1.00 37.60      A    N  
ANISOU 1464  N   GLN A 190     7151   2166   4971  -1731   2549    388  A    N  
ATOM   1465  CA  GLN A 190     -19.071  10.173  18.754  1.00 35.71      A    C  
ANISOU 1465  CA  GLN A 190     6716   1929   4923  -1538   2509    532  A    C  
ATOM   1466  C   GLN A 190     -20.558  10.504  18.556  1.00 42.07      A    C  
ANISOU 1466  C   GLN A 190     7256   3074   5655  -1724   2537    640  A    C  
ATOM   1467  O   GLN A 190     -20.936  11.150  17.569  1.00 41.06      A    O  
ANISOU 1467  O   GLN A 190     6812   3282   5507  -1747   2500    782  A    O  
ATOM   1468  CB  GLN A 190     -18.139  11.344  18.405  1.00 34.37      A    C  
ANISOU 1468  CB  GLN A 190     6348   1753   4959  -1277   2434    648  A    C  
ATOM   1469  CG  GLN A 190     -18.349  12.605  19.276  1.00 31.42      A    C  
ANISOU 1469  CG  GLN A 190     5721   1483   4733   -969   2390    656  A    C  
ATOM   1470  CD  GLN A 190     -18.351  12.325  20.771  1.00 43.31      A    C  
ANISOU 1470  CD  GLN A 190     7527   2576   6352  -1005   2462    664  A    C  
ATOM   1471  NE2 GLN A 190     -17.213  12.515  21.433  1.00 29.30      A    N  
ANISOU 1471  NE2 GLN A 190     5582   1151   4401   -555   2369    321  A    N  
ATOM   1472  OE1 GLN A 190     -19.375  11.945  21.349  1.00 40.40      A    O  
ANISOU 1472  OE1 GLN A 190     7208   2245   5899  -1137   2511    659  A    O  
ATOM   1473  N   ASN A 191     -21.391  10.024  19.497  1.00 39.40      A    N  
ANISOU 1473  N   ASN A 191     7047   2667   5257  -1846   2610    575  A    N  
ATOM   1474  CA  ASN A 191     -22.851  10.113  19.472  1.00 40.75      A    C  
ANISOU 1474  CA  ASN A 191     7001   3158   5325  -2055   2653    632  A    C  
ATOM   1475  C   ASN A 191     -23.376  11.343  20.199  1.00 45.62      A    C  
ANISOU 1475  C   ASN A 191     7387   3826   6122  -1850   2634    812  A    C  
ATOM   1476  O   ASN A 191     -24.597  11.565  20.256  1.00 47.03      A    O  
ANISOU 1476  O   ASN A 191     7350   4288   6230  -1971   2668    886  A    O  
ATOM   1477  CB  ASN A 191     -23.452   8.832  20.079  1.00 42.18      A    C  
ANISOU 1477  CB  ASN A 191     7474   3214   5338  -2330   2778    441  A    C  
ATOM   1478  CG  ASN A 191     -23.223   7.595  19.243  1.00 56.79      A    C  
ANISOU 1478  CG  ASN A 191     9528   5063   6986  -2603   2853    252  A    C  
ATOM   1479  ND2 ASN A 191     -22.962   6.472  19.897  1.00 49.56      A    N  
ANISOU 1479  ND2 ASN A 191     9031   3794   6006  -2689   2986     85  A    N  
ATOM   1480  OD1 ASN A 191     -23.294   7.624  18.014  1.00 50.31      A    O  
ANISOU 1480  OD1 ASN A 191     8500   4559   6059  -2736   2813    256  A    O  
ATOM   1481  N   VAL A 192     -22.463  12.140  20.765  1.00 40.53      A    N  
ANISOU 1481  N   VAL A 192     6778   2918   5704  -1550   2596    867  A    N  
ATOM   1482  CA  VAL A 192     -22.821  13.396  21.403  1.00 39.60      A    C  
ANISOU 1482  CA  VAL A 192     6455   2806   5786  -1346   2609   1023  A    C  
ATOM   1483  C   VAL A 192     -22.482  14.491  20.398  1.00 45.13      A    C  
ANISOU 1483  C   VAL A 192     6869   3672   6607  -1181   2583   1213  A    C  
ATOM   1484  O   VAL A 192     -21.346  14.505  19.913  1.00 45.53      A    O  
ANISOU 1484  O   VAL A 192     6996   3587   6718  -1090   2543   1171  A    O  
ATOM   1485  CB  VAL A 192     -22.131  13.610  22.778  1.00 41.31      A    C  
ANISOU 1485  CB  VAL A 192     6886   2643   6167  -1151   2619    931  A    C  
ATOM   1486  CG1 VAL A 192     -22.520  14.957  23.384  1.00 40.77      A    C  
ANISOU 1486  CG1 VAL A 192     6600   2576   6312   -964   2661   1072  A    C  
ATOM   1487  CG2 VAL A 192     -22.444  12.465  23.742  1.00 41.13      A    C  
ANISOU 1487  CG2 VAL A 192     7172   2456   6000  -1287   2665    771  A    C  
ATOM   1488  N   PRO A 193     -23.422  15.395  20.026  1.00 42.57      A    N  
ANISOU 1488  N   PRO A 193     6219   3649   6309  -1126   2621   1434  A    N  
ATOM   1489  CA  PRO A 193     -23.075  16.445  19.054  1.00 41.63      A    C  
ANISOU 1489  CA  PRO A 193     5854   3665   6299   -936   2634   1646  A    C  
ATOM   1490  C   PRO A 193     -21.935  17.313  19.557  1.00 40.51      A    C  
ANISOU 1490  C   PRO A 193     5800   3147   6446   -694   2671   1636  A    C  
ATOM   1491  O   PRO A 193     -21.942  17.744  20.702  1.00 38.36      A    O  
ANISOU 1491  O   PRO A 193     5603   2639   6334   -596   2722   1588  A    O  
ATOM   1492  CB  PRO A 193     -24.382  17.239  18.902  1.00 45.18      A    C  
ANISOU 1492  CB  PRO A 193     5977   4460   6728   -870   2700   1892  A    C  
ATOM   1493  CG  PRO A 193     -25.446  16.318  19.339  1.00 50.45      A    C  
ANISOU 1493  CG  PRO A 193     6672   5315   7179  -1128   2683   1775  A    C  
ATOM   1494  CD  PRO A 193     -24.829  15.521  20.452  1.00 44.75      A    C  
ANISOU 1494  CD  PRO A 193     6330   4168   6506  -1209   2670   1516  A    C  
ATOM   1495  N   ILE A 194     -20.927  17.505  18.709  1.00 35.73      A    N  
ANISOU 1495  N   ILE A 194     5190   2496   5889   -624   2651   1648  A    N  
ATOM   1496  CA  ILE A 194     -19.757  18.319  19.007  1.00 33.82      A    C  
ANISOU 1496  CA  ILE A 194     4963   2006   5878   -366   2662   1531  A    C  
ATOM   1497  C   ILE A 194     -19.558  19.394  17.930  1.00 38.43      A    C  
ANISOU 1497  C   ILE A 194     5358   2636   6607   -277   2790   1850  A    C  
ATOM   1498  O   ILE A 194     -19.908  19.164  16.766  1.00 39.14      A    O  
ANISOU 1498  O   ILE A 194     5306   3044   6521   -332   2757   1988  A    O  
ATOM   1499  CB  ILE A 194     -18.448  17.452  19.105  1.00 34.40      A    C  
ANISOU 1499  CB  ILE A 194     5315   1834   5922   -448   2591   1315  A    C  
ATOM   1500  CG1 ILE A 194     -18.058  16.779  17.760  1.00 34.56      A    C  
ANISOU 1500  CG1 ILE A 194     5349   1998   5783   -576   2535   1350  A    C  
ATOM   1501  CG2 ILE A 194     -18.431  16.499  20.270  1.00 33.41      A    C  
ANISOU 1501  CG2 ILE A 194     5412   1613   5670   -486   2523   1048  A    C  
ATOM   1502  CD1 ILE A 194     -16.570  16.614  17.571  1.00 38.83      A    C  
ANISOU 1502  CD1 ILE A 194     6030   2321   6400   -509   2502   1206  A    C  
ATOM   1503  N   PRO A 195     -18.844  20.490  18.260  1.00 34.30      A    N  
ANISOU 1503  N   PRO A 195     4762   1937   6334    -20   2872   1774  A    N  
ATOM   1504  CA  PRO A 195     -18.468  21.449  17.216  1.00 35.12      A    C  
ANISOU 1504  CA  PRO A 195     4714   2061   6571    109   3000   2008  A    C  
ATOM   1505  C   PRO A 195     -17.190  20.948  16.513  1.00 39.36      A    C  
ANISOU 1505  C   PRO A 195     5397   2468   7092     -6   2952   1941  A    C  
ATOM   1506  O   PRO A 195     -16.489  20.098  17.067  1.00 38.06      A    O  
ANISOU 1506  O   PRO A 195     5435   2152   6873   -104   2835   1669  A    O  
ATOM   1507  CB  PRO A 195     -18.245  22.734  17.996  1.00 36.49      A    C  
ANISOU 1507  CB  PRO A 195     4877   1916   7072    256   3218   2063  A    C  
ATOM   1508  CG  PRO A 195     -17.863  22.280  19.364  1.00 38.84      A    C  
ANISOU 1508  CG  PRO A 195     5403   1919   7434    141   3166   1808  A    C  
ATOM   1509  CD  PRO A 195     -18.358  20.912  19.591  1.00 34.73      A    C  
ANISOU 1509  CD  PRO A 195     4930   1681   6585     39   2940   1594  A    C  
ATOM   1510  N   SER A 196     -16.878  21.467  15.325  1.00 35.86      A    N  
ANISOU 1510  N   SER A 196     4805   2161   6660     95   3014   2107  A    N  
ATOM   1511  CA  SER A 196     -15.728  21.046  14.508  1.00 35.41      A    C  
ANISOU 1511  CA  SER A 196     4812   2089   6554     51   2947   1996  A    C  
ATOM   1512  C   SER A 196     -14.407  21.255  15.205  1.00 38.54      A    C  
ANISOU 1512  C   SER A 196     5371   2105   7168     56   2986   1767  A    C  
ATOM   1513  O   SER A 196     -13.488  20.524  14.934  1.00 37.03      A    O  
ANISOU 1513  O   SER A 196     5293   1887   6888    -15   2876   1583  A    O  
ATOM   1514  CB  SER A 196     -15.702  21.813  13.189  1.00 41.34      A    C  
ANISOU 1514  CB  SER A 196     5386   2995   7327    153   3078   2314  A    C  
ATOM   1515  OG  SER A 196     -15.645  23.212  13.430  1.00 50.94      A    O  
ANISOU 1515  OG  SER A 196     6519   4004   8832    347   3319   2483  A    O  
ATOM   1516  N   TYR A 197     -14.281  22.259  16.077  1.00 36.61      A    N  
ANISOU 1516  N   TYR A 197     5097   1637   7177    168   3136   1718  A    N  
ATOM   1517  CA  TYR A 197     -12.993  22.499  16.723  1.00 36.03      A    C  
ANISOU 1517  CA  TYR A 197     5070   1379   7240    198   3161   1395  A    C  
ATOM   1518  C   TYR A 197     -12.619  21.380  17.696  1.00 37.18      A    C  
ANISOU 1518  C   TYR A 197     5472   1353   7300     71   2981   1157  A    C  
ATOM   1519  O   TYR A 197     -11.454  21.273  18.084  1.00 35.59      A    O  
ANISOU 1519  O   TYR A 197     5262   1179   7081    102   2946    860  A    O  
ATOM   1520  CB  TYR A 197     -12.952  23.882  17.411  1.00 37.57      A    C  
ANISOU 1520  CB  TYR A 197     5212   1301   7763    281   3415   1424  A    C  
ATOM   1521  CG  TYR A 197     -13.705  23.999  18.724  1.00 38.48      A    C  
ANISOU 1521  CG  TYR A 197     5399   1270   7953    268   3435   1379  A    C  
ATOM   1522  CD1 TYR A 197     -13.074  23.743  19.939  1.00 38.68      A    C  
ANISOU 1522  CD1 TYR A 197     5536   1152   8011    216   3371   1053  A    C  
ATOM   1523  CD2 TYR A 197     -15.012  24.488  18.760  1.00 39.41      A    C  
ANISOU 1523  CD2 TYR A 197     5444   1420   8109    333   3541   1666  A    C  
ATOM   1524  CE1 TYR A 197     -13.731  23.945  21.153  1.00 38.68      A    C  
ANISOU 1524  CE1 TYR A 197     5542   1116   8040    229   3404    973  A    C  
ATOM   1525  CE2 TYR A 197     -15.677  24.689  19.968  1.00 39.42      A    C  
ANISOU 1525  CE2 TYR A 197     5476   1328   8175    342   3579   1597  A    C  
ATOM   1526  CZ  TYR A 197     -15.047  24.382  21.161  1.00 45.56      A    C  
ANISOU 1526  CZ  TYR A 197     6384   1943   8985    274   3506   1262  A    C  
ATOM   1527  OH  TYR A 197     -15.726  24.523  22.351  1.00 44.65      A    O  
ANISOU 1527  OH  TYR A 197     6301   1756   8909    280   3537   1193  A    O  
ATOM   1528  N   LEU A 198     -13.590  20.519  18.049  1.00 35.92      A    N  
ANISOU 1528  N   LEU A 198     5360   1372   6915     15   2857   1161  A    N  
ATOM   1529  CA  LEU A 198     -13.378  19.437  19.003  1.00 35.00      A    C  
ANISOU 1529  CA  LEU A 198     5413   1268   6618    -29   2709    899  A    C  
ATOM   1530  C   LEU A 198     -13.064  18.094  18.324  1.00 39.77      A    C  
ANISOU 1530  C   LEU A 198     6222   1868   7022   -152   2568    874  A    C  
ATOM   1531  O   LEU A 198     -12.916  17.067  19.002  1.00 37.73      A    O  
ANISOU 1531  O   LEU A 198     6168   1554   6615   -184   2473    704  A    O  
ATOM   1532  CB  LEU A 198     -14.584  19.328  19.945  1.00 35.34      A    C  
ANISOU 1532  CB  LEU A 198     5492   1312   6624    -59   2712    943  A    C  
ATOM   1533  CG  LEU A 198     -14.681  20.408  21.042  1.00 38.82      A    C  
ANISOU 1533  CG  LEU A 198     5932   1466   7352      4   2849    940  A    C  
ATOM   1534  CD1 LEU A 198     -15.847  20.111  21.994  1.00 39.43      A    C  
ANISOU 1534  CD1 LEU A 198     6062   1571   7348    -33   2832    963  A    C  
ATOM   1535  CD2 LEU A 198     -13.405  20.484  21.858  1.00 36.83      A    C  
ANISOU 1535  CD2 LEU A 198     5751   1066   7176     57   2832    642  A    C  
ATOM   1536  N   ILE A 199     -12.918  18.114  16.996  1.00 38.49      A    N  
ANISOU 1536  N   ILE A 199     5962   1855   6807   -182   2573   1004  A    N  
ATOM   1537  CA  ILE A 199     -12.501  16.952  16.238  1.00 38.51      A    C  
ANISOU 1537  CA  ILE A 199     6088   1955   6588   -274   2464    924  A    C  
ATOM   1538  C   ILE A 199     -10.967  16.838  16.447  1.00 38.95      A    C  
ANISOU 1538  C   ILE A 199     6241   1845   6712   -182   2433    706  A    C  
ATOM   1539  O   ILE A 199     -10.250  17.849  16.324  1.00 38.37      A    O  
ANISOU 1539  O   ILE A 199     6036   1696   6845    -95   2517    705  A    O  
ATOM   1540  CB  ILE A 199     -12.939  17.106  14.756  1.00 43.80      A    C  
ANISOU 1540  CB  ILE A 199     6588   2889   7165   -336   2485   1141  A    C  
ATOM   1541  CG1 ILE A 199     -14.297  16.418  14.548  1.00 45.72      A    C  
ANISOU 1541  CG1 ILE A 199     6808   3376   7187   -490   2447   1237  A    C  
ATOM   1542  CG2 ILE A 199     -11.881  16.547  13.775  1.00 45.90      A    C  
ANISOU 1542  CG2 ILE A 199     6918   3192   7329   -365   2429   1049  A    C  
ATOM   1543  CD1 ILE A 199     -14.850  16.449  13.100  1.00 56.47      A    C  
ANISOU 1543  CD1 ILE A 199     7974   5095   8387   -564   2450   1432  A    C  
ATOM   1544  N   ALA A 200     -10.486  15.635  16.807  1.00 32.41      A    N  
ANISOU 1544  N   ALA A 200     5540   1161   5612   -158   2329    471  A    N  
ATOM   1545  CA  ALA A 200      -9.065  15.380  17.045  1.00 31.65      A    C  
ANISOU 1545  CA  ALA A 200     5469   1089   5466    -51   2290    270  A    C  
ATOM   1546  C   ALA A 200      -8.643  14.001  16.576  1.00 35.40      A    C  
ANISOU 1546  C   ALA A 200     6323   1262   5866   -109   2219    224  A    C  
ATOM   1547  O   ALA A 200      -9.425  13.050  16.621  1.00 33.38      A    O  
ANISOU 1547  O   ALA A 200     6159   1167   5356   -197   2204    221  A    O  
ATOM   1548  CB  ALA A 200      -8.741  15.522  18.515  1.00 32.10      A    C  
ANISOU 1548  CB  ALA A 200     5567   1066   5564     41   2282    131  A    C  
ATOM   1549  N   LEU A 201      -7.368  13.897  16.193  1.00 33.56      A    N  
ANISOU 1549  N   LEU A 201     6038   1126   5586    -12   2195    104  A    N  
ATOM   1550  CA  LEU A 201      -6.735  12.681  15.713  1.00 33.41      A    C  
ANISOU 1550  CA  LEU A 201     6214   1120   5362      1   2150     11  A    C  
ATOM   1551  C   LEU A 201      -5.252  12.626  16.116  1.00 37.30      A    C  
ANISOU 1551  C   LEU A 201     6786   1454   5934    201   2114   -176  A    C  
ATOM   1552  O   LEU A 201      -4.530  13.597  15.928  1.00 36.03      A    O  
ANISOU 1552  O   LEU A 201     6414   1334   5943    247   2134   -212  A    O  
ATOM   1553  CB  LEU A 201      -6.858  12.619  14.164  1.00 33.15      A    C  
ANISOU 1553  CB  LEU A 201     6136   1145   5315   -134   2168    122  A    C  
ATOM   1554  CG  LEU A 201      -6.116  11.471  13.435  1.00 36.93      A    C  
ANISOU 1554  CG  LEU A 201     6813   1595   5622   -136   2147     21  A    C  
ATOM   1555  CD1 LEU A 201      -6.611  10.076  13.891  1.00 35.92      A    C  
ANISOU 1555  CD1 LEU A 201     7004   1365   5279   -193   2161    -52  A    C  
ATOM   1556  CD2 LEU A 201      -6.215  11.625  11.937  1.00 37.33      A    C  
ANISOU 1556  CD2 LEU A 201     6727   1821   5636   -268   2166    127  A    C  
ATOM   1557  N   VAL A 202      -4.818  11.467  16.644  1.00 36.38      A    N  
ANISOU 1557  N   VAL A 202     6923   1269   5630    322   2080   -291  A    N  
ATOM   1558  CA  VAL A 202      -3.426  11.138  16.981  1.00 37.09      A    C  
ANISOU 1558  CA  VAL A 202     7053   1375   5663    549   2040   -461  A    C  
ATOM   1559  C   VAL A 202      -3.115   9.766  16.372  1.00 40.06      A    C  
ANISOU 1559  C   VAL A 202     7697   1704   5819    587   2055   -481  A    C  
ATOM   1560  O   VAL A 202      -3.920   8.848  16.521  1.00 40.56      A    O  
ANISOU 1560  O   VAL A 202     8012   1659   5741    514   2102   -433  A    O  
ATOM   1561  CB  VAL A 202      -3.048  11.210  18.494  1.00 41.12      A    C  
ANISOU 1561  CB  VAL A 202     7588   1875   6159    755   2004   -588  A    C  
ATOM   1562  CG1 VAL A 202      -3.863  10.245  19.339  1.00 41.49      A    C  
ANISOU 1562  CG1 VAL A 202     7922   1799   6042    787   2023   -543  A    C  
ATOM   1563  CG2 VAL A 202      -1.552  10.970  18.715  1.00 41.35      A    C  
ANISOU 1563  CG2 VAL A 202     7592   2012   6109   1002   1955   -764  A    C  
ATOM   1564  N   VAL A 203      -1.975   9.658  15.649  1.00 35.13      A    N  
ANISOU 1564  N   VAL A 203     6987   1215   5146    664   2036   -539  A    N  
ATOM   1565  CA  VAL A 203      -1.472   8.421  15.044  1.00 35.22      A    C  
ANISOU 1565  CA  VAL A 203     7227   1205   4949    725   2067   -565  A    C  
ATOM   1566  C   VAL A 203       0.035   8.312  15.365  1.00 42.98      A    C  
ANISOU 1566  C   VAL A 203     8212   2191   5928   1049   2031   -744  A    C  
ATOM   1567  O   VAL A 203       0.831   9.137  14.918  1.00 45.12      A    O  
ANISOU 1567  O   VAL A 203     8216   2604   6325   1057   1995   -806  A    O  
ATOM   1568  CB  VAL A 203      -1.752   8.288  13.520  1.00 37.32      A    C  
ANISOU 1568  CB  VAL A 203     7508   1432   5240    523   2112   -525  A    C  
ATOM   1569  CG1 VAL A 203      -1.224   6.944  12.980  1.00 38.52      A    C  
ANISOU 1569  CG1 VAL A 203     7946   1504   5186    593   2176   -592  A    C  
ATOM   1570  CG2 VAL A 203      -3.235   8.442  13.199  1.00 35.86      A    C  
ANISOU 1570  CG2 VAL A 203     7305   1249   5071    240   2143   -388  A    C  
ATOM   1571  N   GLY A 204       0.404   7.290  16.128  1.00 40.22      A    N  
ANISOU 1571  N   GLY A 204     8122   1770   5391   1296   2052   -793  A    N  
ATOM   1572  CA  GLY A 204       1.790   7.059  16.513  1.00 41.81      A    C  
ANISOU 1572  CA  GLY A 204     8287   2102   5496   1626   2013   -920  A    C  
ATOM   1573  C   GLY A 204       1.992   5.779  17.291  1.00 49.79      A    C  
ANISOU 1573  C   GLY A 204     9646   3007   6266   1924   2075   -912  A    C  
ATOM   1574  O   GLY A 204       1.049   5.005  17.474  1.00 49.37      A    O  
ANISOU 1574  O   GLY A 204     9895   2732   6130   1841   2172   -817  A    O  
ATOM   1575  N   ALA A 205       3.240   5.532  17.733  1.00 49.68      A    N  
ANISOU 1575  N   ALA A 205     9590   3161   6126   2281   2039  -1009  A    N  
ATOM   1576  CA  ALA A 205       3.561   4.354  18.547  1.00 51.97      A    C  
ANISOU 1576  CA  ALA A 205    10202   3380   6165   2651   2114   -975  A    C  
ATOM   1577  C   ALA A 205       3.147   4.659  19.988  1.00 56.44      A    C  
ANISOU 1577  C   ALA A 205    10739   4003   6702   2769   2065   -970  A    C  
ATOM   1578  O   ALA A 205       3.935   5.207  20.769  1.00 58.05      A    O  
ANISOU 1578  O   ALA A 205    10689   4496   6873   2989   1958  -1085  A    O  
ATOM   1579  CB  ALA A 205       5.046   4.016  18.445  1.00 54.67      A    C  
ANISOU 1579  CB  ALA A 205    10474   3939   6361   3019   2091  -1064  A    C  
ATOM   1580  N   LEU A 206       1.870   4.381  20.306  1.00 51.09      A    N  
ANISOU 1580  N   LEU A 206    10291   3078   6043   2582   2143   -856  A    N  
ATOM   1581  CA  LEU A 206       1.298   4.715  21.604  1.00 50.97      A    C  
ANISOU 1581  CA  LEU A 206    10256   3091   6018   2638   2107   -840  A    C  
ATOM   1582  C   LEU A 206       1.065   3.506  22.490  1.00 56.11      A    C  
ANISOU 1582  C   LEU A 206    11321   3569   6430   2919   2240   -733  A    C  
ATOM   1583  O   LEU A 206       0.744   2.426  22.014  1.00 54.83      A    O  
ANISOU 1583  O   LEU A 206    11527   3132   6173   2900   2410   -641  A    O  
ATOM   1584  CB  LEU A 206      -0.037   5.488  21.436  1.00 48.68      A    C  
ANISOU 1584  CB  LEU A 206     9867   2685   5946   2216   2097   -790  A    C  
ATOM   1585  CG  LEU A 206      -0.009   6.784  20.608  1.00 50.79      A    C  
ANISOU 1585  CG  LEU A 206     9746   3084   6467   1934   2006   -850  A    C  
ATOM   1586  CD1 LEU A 206      -1.411   7.298  20.361  1.00 48.99      A    C  
ANISOU 1586  CD1 LEU A 206     9492   2723   6401   1570   2035   -747  A    C  
ATOM   1587  CD2 LEU A 206       0.821   7.857  21.277  1.00 52.60      A    C  
ANISOU 1587  CD2 LEU A 206     9617   3586   6781   2057   1893  -1005  A    C  
ATOM   1588  N   GLU A 207       1.194   3.730  23.806  1.00 56.05      A    N  
ANISOU 1588  N   GLU A 207    11249   3723   6326   3167   2182   -751  A    N  
ATOM   1589  CA  GLU A 207       0.952   2.753  24.868  1.00 58.54      A    C  
ANISOU 1589  CA  GLU A 207    11922   3913   6407   3472   2306   -632  A    C  
ATOM   1590  C   GLU A 207       0.042   3.411  25.908  1.00 62.53      A    C  
ANISOU 1590  C   GLU A 207    12341   4438   6982   3340   2256   -625  A    C  
ATOM   1591  O   GLU A 207       0.189   4.606  26.190  1.00 61.62      A    O  
ANISOU 1591  O   GLU A 207    11833   4571   7009   3230   2097   -755  A    O  
ATOM   1592  CB  GLU A 207       2.271   2.261  25.489  1.00 62.65      A    C  
ANISOU 1592  CB  GLU A 207    12439   4702   6663   4026   2284   -651  A    C  
ATOM   1593  CG  GLU A 207       3.130   1.421  24.557  1.00 77.21      A    C  
ANISOU 1593  CG  GLU A 207    14454   6482   8400   4222   2382   -622  A    C  
ATOM   1594  CD  GLU A 207       2.986  -0.085  24.676  1.00105.30      A    C  
ANISOU 1594  CD  GLU A 207    18568   9692  11748   4476   2649   -438  A    C  
ATOM   1595  OE1 GLU A 207       3.232  -0.627  25.779  1.00106.33      A    O  
ANISOU 1595  OE1 GLU A 207    18880   9875  11645   4896   2721   -335  A    O  
ATOM   1596  OE2 GLU A 207       2.698  -0.731  23.642  1.00 94.93      A    O1-
ANISOU 1596  OE2 GLU A 207    17508   8067  10493   4271   2805   -403  A    O1-
ATOM   1597  N   GLY A 208      -0.960   2.660  26.356  1.00 59.64      A    N  
ANISOU 1597  N   GLY A 208    12343   3776   6540   3297   2418   -485  A    N  
ATOM   1598  CA  GLY A 208      -1.949   3.118  27.317  1.00 58.92      A    C  
ANISOU 1598  CA  GLY A 208    12231   3658   6500   3164   2405   -458  A    C  
ATOM   1599  C   GLY A 208      -2.245   2.138  28.427  1.00 67.17      A    C  
ANISOU 1599  C   GLY A 208    13656   4566   7301   3467   2561   -322  A    C  
ATOM   1600  O   GLY A 208      -2.357   0.929  28.187  1.00 67.14      A    O  
ANISOU 1600  O   GLY A 208    14077   4275   7159   3576   2777   -201  A    O  
ATOM   1601  N   ARG A 209      -2.393   2.668  29.655  1.00 66.46      A    N  
ANISOU 1601  N   ARG A 209    13425   4669   7157   3598   2477   -345  A    N  
ATOM   1602  CA  ARG A 209      -2.729   1.878  30.839  1.00 69.40      A    C  
ANISOU 1602  CA  ARG A 209    14126   4950   7293   3893   2618   -207  A    C  
ATOM   1603  C   ARG A 209      -3.805   2.578  31.657  1.00 71.11      A    C  
ANISOU 1603  C   ARG A 209    14241   5163   7615   3656   2580   -218  A    C  
ATOM   1604  O   ARG A 209      -3.782   3.804  31.787  1.00 68.45      A    O  
ANISOU 1604  O   ARG A 209    13492   5065   7450   3479   2394   -367  A    O  
ATOM   1605  CB  ARG A 209      -1.488   1.597  31.705  1.00 75.70      A    C  
ANISOU 1605  CB  ARG A 209    14868   6097   7799   4476   2560   -209  A    C  
ATOM   1606  CG  ARG A 209      -1.602   0.303  32.513  1.00 91.37      A    C  
ANISOU 1606  CG  ARG A 209    17337   7898   9482   4887   2795     10  A    C  
ATOM   1607  CD  ARG A 209      -0.681   0.291  33.721  1.00109.09      A    C  
ANISOU 1607  CD  ARG A 209    19446  10586  11419   5446   2703     15  A    C  
ATOM   1608  NE  ARG A 209      -1.215  -0.538  34.808  1.00121.28      A    N  
ANISOU 1608  NE  ARG A 209    21386  11974  12722   5741   2907    227  A    N  
ATOM   1609  CZ  ARG A 209      -0.570  -1.554  35.378  1.00133.78      A    C  
ANISOU 1609  CZ  ARG A 209    23271  13591  13969   6320   3069    416  A    C  
ATOM   1610  NH1 ARG A 209       0.653  -1.884  34.978  1.00123.89      A    N1+
ANISOU 1610  NH1 ARG A 209    21952  12547  12572   6682   3040    413  A    N1+
ATOM   1611  NH2 ARG A 209      -1.140  -2.242  36.357  1.00117.63      A    N  
ANISOU 1611  NH2 ARG A 209    21593  11379  11721   6562   3276    622  A    N  
ATOM   1612  N   LYS A 210      -4.764   1.780  32.178  1.00 69.18      A    N  
ANISOU 1612  N   LYS A 210    14389   4621   7274   3641   2786    -65  A    N  
ATOM   1613  CA  LYS A 210      -5.899   2.186  33.015  1.00 68.41      A    C  
ANISOU 1613  CA  LYS A 210    14285   4468   7239   3442   2803    -42  A    C  
ATOM   1614  C   LYS A 210      -5.402   2.876  34.301  1.00 73.47      A    C  
ANISOU 1614  C   LYS A 210    14662   5495   7759   3739   2645   -119  A    C  
ATOM   1615  O   LYS A 210      -4.491   2.372  34.950  1.00 76.22      A    O  
ANISOU 1615  O   LYS A 210    15085   6039   7835   4214   2649    -80  A    O  
ATOM   1616  CB  LYS A 210      -6.769   0.946  33.347  1.00 72.45      A    C  
ANISOU 1616  CB  LYS A 210    15330   4585   7613   3447   3102    142  A    C  
ATOM   1617  CG  LYS A 210      -7.977   1.241  34.236  1.00 86.28      A    C  
ANISOU 1617  CG  LYS A 210    17108   6260   9414   3236   3149    176  A    C  
ATOM   1618  CD  LYS A 210      -8.950   0.066  34.373  1.00 96.88      A    C  
ANISOU 1618  CD  LYS A 210    18968   7181  10662   3137   3474    330  A    C  
ATOM   1619  CE  LYS A 210      -9.960   0.300  35.479  1.00102.57      A    C  
ANISOU 1619  CE  LYS A 210    19717   7879  11374   3032   3522    373  A    C  
ATOM   1620  NZ  LYS A 210     -11.217  -0.472  35.281  1.00106.18      A    N1+
ANISOU 1620  NZ  LYS A 210    20539   7940  11863   2685   3806    448  A    N1+
ATOM   1621  N   VAL A 211      -5.974   4.044  34.634  1.00 68.49      A    N  
ANISOU 1621  N   VAL A 211    13705   4997   7322   3464   2512   -236  A    N  
ATOM   1622  CA  VAL A 211      -5.638   4.847  35.826  1.00 68.79      A    C  
ANISOU 1622  CA  VAL A 211    13454   5403   7281   3649   2371   -359  A    C  
ATOM   1623  C   VAL A 211      -6.978   5.216  36.547  1.00 70.89      A    C  
ANISOU 1623  C   VAL A 211    13763   5530   7641   3401   2431   -320  A    C  
ATOM   1624  O   VAL A 211      -7.002   6.000  37.507  1.00 70.64      A    O  
ANISOU 1624  O   VAL A 211    13504   5751   7583   3462   2338   -429  A    O  
ATOM   1625  CB  VAL A 211      -4.754   6.096  35.462  1.00 71.87      A    C  
ANISOU 1625  CB  VAL A 211    13332   6139   7836   3564   2154   -607  A    C  
ATOM   1626  CG1 VAL A 211      -4.299   6.862  36.706  1.00 72.95      A    C  
ANISOU 1626  CG1 VAL A 211    13170   6695   7855   3760   2029   -782  A    C  
ATOM   1627  CG2 VAL A 211      -3.530   5.693  34.636  1.00 72.49      A    C  
ANISOU 1627  CG2 VAL A 211    13376   6323   7842   3759   2111   -639  A    C  
ATOM   1628  N   GLY A 212      -8.065   4.590  36.096  1.00 65.06      A    N  
ANISOU 1628  N   GLY A 212    13322   4410   6989   3127   2600   -176  A    N  
ATOM   1629  CA  GLY A 212      -9.407   4.800  36.627  1.00 63.45      A    C  
ANISOU 1629  CA  GLY A 212    13186   4049   6873   2865   2683   -122  A    C  
ATOM   1630  C   GLY A 212     -10.453   4.018  35.856  1.00 64.38      A    C  
ANISOU 1630  C   GLY A 212    13620   3779   7063   2547   2881      7  A    C  
ATOM   1631  O   GLY A 212     -10.185   3.597  34.732  1.00 61.97      A    O  
ANISOU 1631  O   GLY A 212    13396   3344   6807   2446   2918     19  A    O  
ATOM   1632  N   PRO A 213     -11.687   3.861  36.402  1.00 61.54      A    N  
ANISOU 1632  N   PRO A 213    13415   3251   6716   2350   3014     83  A    N  
ATOM   1633  CA  PRO A 213     -12.727   3.075  35.697  1.00 60.79      A    C  
ANISOU 1633  CA  PRO A 213    13607   2820   6668   2008   3224    171  A    C  
ATOM   1634  C   PRO A 213     -13.119   3.610  34.306  1.00 60.59      A    C  
ANISOU 1634  C   PRO A 213    13339   2791   6892   1592   3145    103  A    C  
ATOM   1635  O   PRO A 213     -13.758   2.905  33.537  1.00 59.15      A    O  
ANISOU 1635  O   PRO A 213    13361   2390   6721   1316   3305    139  A    O  
ATOM   1636  CB  PRO A 213     -13.922   3.128  36.661  1.00 62.89      A    C  
ANISOU 1636  CB  PRO A 213    13963   3011   6920   1873   3332    224  A    C  
ATOM   1637  CG  PRO A 213     -13.657   4.300  37.550  1.00 66.95      A    C  
ANISOU 1637  CG  PRO A 213    14121   3836   7481   2020   3129    135  A    C  
ATOM   1638  CD  PRO A 213     -12.172   4.321  37.717  1.00 63.37      A    C  
ANISOU 1638  CD  PRO A 213    13579   3606   6894   2430   2996     78  A    C  
ATOM   1639  N   ARG A 214     -12.707   4.830  33.965  1.00 56.54      A    N  
ANISOU 1639  N   ARG A 214    12395   2526   6562   1554   2921      0  A    N  
ATOM   1640  CA  ARG A 214     -13.027   5.435  32.664  1.00 54.18      A    C  
ANISOU 1640  CA  ARG A 214    11837   2261   6488   1214   2843    -39  A    C  
ATOM   1641  C   ARG A 214     -11.858   6.308  32.161  1.00 56.26      A    C  
ANISOU 1641  C   ARG A 214    11768   2746   6863   1347   2647   -144  A    C  
ATOM   1642  O   ARG A 214     -12.067   7.203  31.342  1.00 56.54      A    O  
ANISOU 1642  O   ARG A 214    11502   2867   7112   1118   2559   -177  A    O  
ATOM   1643  CB  ARG A 214     -14.345   6.235  32.766  1.00 51.58      A    C  
ANISOU 1643  CB  ARG A 214    11299   1969   6331    892   2838    -23  A    C  
ATOM   1644  CG  ARG A 214     -14.518   6.969  34.091  1.00 58.58      A    C  
ANISOU 1644  CG  ARG A 214    12047   2979   7232   1038   2781    -55  A    C  
ATOM   1645  CD  ARG A 214     -15.874   7.621  34.198  1.00 62.35      A    C  
ANISOU 1645  CD  ARG A 214    12385   3455   7849    742   2821    -16  A    C  
ATOM   1646  NE  ARG A 214     -15.963   8.469  35.383  1.00 62.42      A    N  
ANISOU 1646  NE  ARG A 214    12224   3593   7901    872   2762    -70  A    N  
ATOM   1647  CZ  ARG A 214     -17.085   9.026  35.824  1.00 73.02      A    C  
ANISOU 1647  CZ  ARG A 214    13447   4951   9347    694   2800    -43  A    C  
ATOM   1648  NH1 ARG A 214     -18.236   8.806  35.199  1.00 57.14      A    N1+
ANISOU 1648  NH1 ARG A 214    11452   2867   7391    384   2891     43  A    N1+
ATOM   1649  NH2 ARG A 214     -17.069   9.794  36.903  1.00 63.14      A    N  
ANISOU 1649  NH2 ARG A 214    12048   3813   8129    822   2756   -114  A    N  
ATOM   1650  N   THR A 215     -10.627   6.025  32.640  1.00 50.72      A    N  
ANISOU 1650  N   THR A 215    11121   2147   6002   1725   2597   -192  A    N  
ATOM   1651  CA  THR A 215      -9.428   6.769  32.286  1.00 48.44      A    C  
ANISOU 1651  CA  THR A 215    10525   2093   5787   1865   2430   -319  A    C  
ATOM   1652  C   THR A 215      -8.238   5.870  32.000  1.00 52.75      A    C  
ANISOU 1652  C   THR A 215    11249   2654   6138   2173   2443   -318  A    C  
ATOM   1653  O   THR A 215      -7.750   5.155  32.878  1.00 54.15      A    O  
ANISOU 1653  O   THR A 215    11640   2864   6071   2528   2494   -280  A    O  
ATOM   1654  CB  THR A 215      -9.056   7.776  33.389  1.00 52.60      A    C  
ANISOU 1654  CB  THR A 215    10771   2879   6334   2021   2312   -449  A    C  
ATOM   1655  CG2 THR A 215      -7.827   8.640  33.015  1.00 46.50      A    C  
ANISOU 1655  CG2 THR A 215     9650   2367   5652   2113   2162   -624  A    C  
ATOM   1656  OG1 THR A 215     -10.180   8.616  33.675  1.00 49.13      A    O  
ANISOU 1656  OG1 THR A 215    10178   2406   6084   1751   2322   -444  A    O  
ATOM   1657  N   THR A 216      -7.749   5.965  30.768  1.00 47.81      A    N  
ANISOU 1657  N   THR A 216    10517   2030   5619   2059   2399   -352  A    N  
ATOM   1658  CA  THR A 216      -6.539   5.325  30.279  1.00 48.05      A    C  
ANISOU 1658  CA  THR A 216    10638   2107   5514   2320   2392   -372  A    C  
ATOM   1659  C   THR A 216      -5.570   6.455  30.000  1.00 50.71      A    C  
ANISOU 1659  C   THR A 216    10544   2738   5984   2352   2208   -536  A    C  
ATOM   1660  O   THR A 216      -6.003   7.462  29.447  1.00 46.16      A    O  
ANISOU 1660  O   THR A 216     9698   2184   5657   2049   2150   -582  A    O  
ATOM   1661  CB  THR A 216      -6.859   4.505  29.026  1.00 53.56      A    C  
ANISOU 1661  CB  THR A 216    11572   2550   6227   2110   2518   -295  A    C  
ATOM   1662  CG2 THR A 216      -5.635   3.824  28.437  1.00 48.87      A    C  
ANISOU 1662  CG2 THR A 216    11088   1979   5500   2376   2532   -312  A    C  
ATOM   1663  OG1 THR A 216      -7.904   3.575  29.305  1.00 57.75      A    O  
ANISOU 1663  OG1 THR A 216    12477   2802   6664   1996   2718   -179  A    O  
ATOM   1664  N   ILE A 217      -4.280   6.318  30.360  1.00 51.70      A    N  
ANISOU 1664  N   ILE A 217    10597   3101   5945   2715   2136   -624  A    N  
ATOM   1665  CA  ILE A 217      -3.328   7.380  30.028  1.00 52.34      A    C  
ANISOU 1665  CA  ILE A 217    10261   3469   6156   2704   1986   -813  A    C  
ATOM   1666  C   ILE A 217      -2.495   6.883  28.826  1.00 55.95      A    C  
ANISOU 1666  C   ILE A 217    10758   3904   6595   2752   1991   -808  A    C  
ATOM   1667  O   ILE A 217      -1.926   5.789  28.867  1.00 55.82      A    O  
ANISOU 1667  O   ILE A 217    11000   3864   6346   3058   2053   -739  A    O  
ATOM   1668  CB  ILE A 217      -2.498   7.912  31.240  1.00 57.73      A    C  
ANISOU 1668  CB  ILE A 217    10700   4529   6704   2990   1878   -985  A    C  
ATOM   1669  CG1 ILE A 217      -3.460   8.618  32.247  1.00 58.23      A    C  
ANISOU 1669  CG1 ILE A 217    10680   4592   6853   2844   1880  -1013  A    C  
ATOM   1670  CG2 ILE A 217      -1.399   8.887  30.772  1.00 57.93      A    C  
ANISOU 1670  CG2 ILE A 217    10310   4848   6851   2956   1760  -1212  A    C  
ATOM   1671  CD1 ILE A 217      -2.850   9.281  33.559  1.00 71.81      A    C  
ANISOU 1671  CD1 ILE A 217    12140   6705   8441   3064   1786  -1216  A    C  
ATOM   1672  N   TRP A 218      -2.504   7.673  27.730  1.00 50.88      A    N  
ANISOU 1672  N   TRP A 218     9884   3245   6202   2448   1949   -859  A    N  
ATOM   1673  CA  TRP A 218      -1.828   7.318  26.480  1.00 50.61      A    C  
ANISOU 1673  CA  TRP A 218     9861   3185   6183   2431   1955   -857  A    C  
ATOM   1674  C   TRP A 218      -0.620   8.203  26.192  1.00 57.42      A    C  
ANISOU 1674  C   TRP A 218    10342   4347   7130   2490   1840  -1048  A    C  
ATOM   1675  O   TRP A 218      -0.729   9.418  26.277  1.00 56.27      A    O  
ANISOU 1675  O   TRP A 218     9885   4306   7189   2301   1789  -1160  A    O  
ATOM   1676  CB  TRP A 218      -2.796   7.434  25.296  1.00 46.80      A    C  
ANISOU 1676  CB  TRP A 218     9418   2473   5891   2036   2015   -753  A    C  
ATOM   1677  CG  TRP A 218      -4.026   6.584  25.374  1.00 47.10      A    C  
ANISOU 1677  CG  TRP A 218     9798   2236   5861   1896   2144   -600  A    C  
ATOM   1678  CD1 TRP A 218      -5.242   6.951  25.872  1.00 49.25      A    C  
ANISOU 1678  CD1 TRP A 218    10072   2421   6218   1694   2174   -539  A    C  
ATOM   1679  CD2 TRP A 218      -4.185   5.258  24.861  1.00 47.37      A    C  
ANISOU 1679  CD2 TRP A 218    10214   2047   5739   1913   2286   -508  A    C  
ATOM   1680  CE2 TRP A 218      -5.532   4.886  25.069  1.00 50.77      A    C  
ANISOU 1680  CE2 TRP A 218    10854   2269   6169   1683   2401   -410  A    C  
ATOM   1681  CE3 TRP A 218      -3.328   4.357  24.204  1.00 49.65      A    C  
ANISOU 1681  CE3 TRP A 218    10688   2284   5894   2082   2348   -510  A    C  
ATOM   1682  NE1 TRP A 218      -6.147   5.931  25.708  1.00 48.93      A    N  
ANISOU 1682  NE1 TRP A 218    10375   2139   6077   1571   2318   -423  A    N  
ATOM   1683  CZ2 TRP A 218      -6.024   3.625  24.717  1.00 51.07      A    C  
ANISOU 1683  CZ2 TRP A 218    11289   2043   6072   1606   2591   -336  A    C  
ATOM   1684  CZ3 TRP A 218      -3.817   3.107  23.854  1.00 52.25      A    C  
ANISOU 1684  CZ3 TRP A 218    11427   2329   6095   2024   2542   -424  A    C  
ATOM   1685  CH2 TRP A 218      -5.150   2.755  24.106  1.00 52.74      A    C  
ANISOU 1685  CH2 TRP A 218    11698   2181   6160   1774   2668   -349  A    C  
ATOM   1686  N   THR A 219       0.500   7.600  25.748  1.00 58.24      A    N  
ANISOU 1686  N   THR A 219    10475   4564   7090   2724   1826  -1087  A    N  
ATOM   1687  CA  THR A 219       1.731   8.304  25.323  1.00 59.24      A    C  
ANISOU 1687  CA  THR A 219    10249   4983   7277   2772   1734  -1277  A    C  
ATOM   1688  C   THR A 219       2.798   7.266  24.869  1.00 65.68      A    C  
ANISOU 1688  C   THR A 219    11208   5877   7869   3092   1749  -1261  A    C  
ATOM   1689  O   THR A 219       2.485   6.074  24.764  1.00 66.64      A    O  
ANISOU 1689  O   THR A 219    11717   5767   7834   3225   1854  -1094  A    O  
ATOM   1690  CB  THR A 219       2.253   9.301  26.407  1.00 62.49      A    C  
ANISOU 1690  CB  THR A 219    10310   5737   7696   2851   1641  -1499  A    C  
ATOM   1691  CG2 THR A 219       2.783   8.619  27.648  1.00 63.12      A    C  
ANISOU 1691  CG2 THR A 219    10477   6055   7450   3277   1605  -1525  A    C  
ATOM   1692  OG1 THR A 219       3.255  10.144  25.841  1.00 63.56      A    O  
ANISOU 1692  OG1 THR A 219    10086   6112   7952   2776   1588  -1704  A    O  
ATOM   1693  N   GLU A 220       4.029   7.730  24.552  1.00 63.77      A    N  
ANISOU 1693  N   GLU A 220    10658   5945   7625   3195   1669  -1440  A    N  
ATOM   1694  CA  GLU A 220       5.157   6.855  24.174  1.00 66.16      A    C  
ANISOU 1694  CA  GLU A 220    11036   6389   7711   3533   1675  -1446  A    C  
ATOM   1695  C   GLU A 220       5.801   6.310  25.458  1.00 75.78      A    C  
ANISOU 1695  C   GLU A 220    12277   7908   8609   4013   1638  -1477  A    C  
ATOM   1696  O   GLU A 220       6.058   7.096  26.369  1.00 76.63      A    O  
ANISOU 1696  O   GLU A 220    12084   8330   8702   4043   1542  -1648  A    O  
ATOM   1697  CB  GLU A 220       6.200   7.614  23.325  1.00 67.03      A    C  
ANISOU 1697  CB  GLU A 220    10778   6740   7950   3428   1611  -1634  A    C  
ATOM   1698  CG  GLU A 220       5.830   7.796  21.865  1.00 72.75      A    C  
ANISOU 1698  CG  GLU A 220    11543   7198   8902   3080   1669  -1557  A    C  
ATOM   1699  CD  GLU A 220       6.973   8.317  21.017  1.00 87.84      A    C  
ANISOU 1699  CD  GLU A 220    13149   9336  10891   3044   1633  -1717  A    C  
ATOM   1700  OE1 GLU A 220       7.797   7.494  20.555  1.00 75.89      A    O  
ANISOU 1700  OE1 GLU A 220    11734   7889   9210   3284   1650  -1702  A    O  
ATOM   1701  OE2 GLU A 220       7.062   9.553  20.837  1.00 78.48      A    O1-
ANISOU 1701  OE2 GLU A 220    11630   8255   9934   2780   1609  -1862  A    O1-
ATOM   1702  N   LYS A 221       6.054   4.983  25.533  1.00 75.90      A    N  
ANISOU 1702  N   LYS A 221    12645   7833   8360   4392   1732  -1313  A    N  
ATOM   1703  CA  LYS A 221       6.643   4.241  26.670  1.00 79.03      A    C  
ANISOU 1703  CA  LYS A 221    13138   8490   8400   4936   1736  -1266  A    C  
ATOM   1704  C   LYS A 221       7.554   5.080  27.605  1.00 85.07      A    C  
ANISOU 1704  C   LYS A 221    13426   9851   9047   5116   1565  -1512  A    C  
ATOM   1705  O   LYS A 221       7.404   5.010  28.829  1.00 86.12      A    O  
ANISOU 1705  O   LYS A 221    13561  10173   8989   5346   1538  -1502  A    O  
ATOM   1706  CB  LYS A 221       7.451   3.043  26.153  1.00 83.54      A    C  
ANISOU 1706  CB  LYS A 221    13964   9028   8749   5331   1843  -1143  A    C  
ATOM   1707  CG  LYS A 221       6.596   1.879  25.688  1.00100.19      A    C  
ANISOU 1707  CG  LYS A 221    16644  10585  10838   5315   2069   -889  A    C  
ATOM   1708  CD  LYS A 221       7.447   0.778  25.082  1.00114.78      A    C  
ANISOU 1708  CD  LYS A 221    18738  12366  12507   5665   2205   -792  A    C  
ATOM   1709  CE  LYS A 221       6.619  -0.395  24.614  1.00128.36      A    C  
ANISOU 1709  CE  LYS A 221    21043  13517  14210   5619   2475   -575  A    C  
ATOM   1710  NZ  LYS A 221       7.441  -1.401  23.884  1.00139.20      A    N1+
ANISOU 1710  NZ  LYS A 221    22663  14780  15448   5908   2636   -502  A    N1+
ATOM   1711  N   GLU A 222       8.480   5.869  27.017  1.00 81.86      A    N  
ANISOU 1711  N   GLU A 222    12607   9748   8748   4991   1465  -1747  A    N  
ATOM   1712  CA  GLU A 222       9.462   6.726  27.696  1.00 83.59      A    C  
ANISOU 1712  CA  GLU A 222    12319  10565   8877   5082   1321  -2049  A    C  
ATOM   1713  C   GLU A 222       8.802   7.788  28.607  1.00 86.61      A    C  
ANISOU 1713  C   GLU A 222    12487  11027   9394   4805   1265  -2204  A    C  
ATOM   1714  O   GLU A 222       9.367   8.136  29.643  1.00 88.22      A    O  
ANISOU 1714  O   GLU A 222    12399  11723   9398   5000   1173  -2401  A    O  
ATOM   1715  CB  GLU A 222      10.388   7.419  26.677  1.00 84.71      A    C  
ANISOU 1715  CB  GLU A 222    12105  10891   9190   4869   1276  -2269  A    C  
ATOM   1716  CG  GLU A 222      11.128   6.467  25.744  1.00 97.95      A    C  
ANISOU 1716  CG  GLU A 222    13944  12534  10740   5133   1327  -2152  A    C  
ATOM   1717  CD  GLU A 222      10.385   5.944  24.525  1.00115.18      A    C  
ANISOU 1717  CD  GLU A 222    16511  14134  13117   4899   1454  -1926  A    C  
ATOM   1718  OE1 GLU A 222       9.594   6.712  23.929  1.00105.46      A    O  
ANISOU 1718  OE1 GLU A 222    15238  12621  12211   4413   1471  -1944  A    O  
ATOM   1719  OE2 GLU A 222      10.622   4.774  24.143  1.00106.45      A    O1-
ANISOU 1719  OE2 GLU A 222    15744  12873  11830   5210   1552  -1737  A    O1-
ATOM   1720  N   LEU A 223       7.621   8.296  28.214  1.00 80.43      A    N  
ANISOU 1720  N   LEU A 223    11839   9789   8931   4363   1328  -2121  A    N  
ATOM   1721  CA  LEU A 223       6.875   9.312  28.954  1.00 79.45      A    C  
ANISOU 1721  CA  LEU A 223    11555   9656   8977   4074   1309  -2240  A    C  
ATOM   1722  C   LEU A 223       5.739   8.723  29.800  1.00 81.95      A    C  
ANISOU 1722  C   LEU A 223    12230   9710   9196   4165   1363  -2014  A    C  
ATOM   1723  O   LEU A 223       5.134   9.470  30.576  1.00 81.57      A    O  
ANISOU 1723  O   LEU A 223    12063   9685   9244   3984   1349  -2106  A    O  
ATOM   1724  CB  LEU A 223       6.282  10.358  27.982  1.00 76.97      A    C  
ANISOU 1724  CB  LEU A 223    11124   9033   9088   3538   1361  -2287  A    C  
ATOM   1725  CG  LEU A 223       7.218  11.424  27.393  1.00 82.10      A    C  
ANISOU 1725  CG  LEU A 223    11340   9939   9916   3322   1338  -2579  A    C  
ATOM   1726  CD1 LEU A 223       6.618  12.028  26.130  1.00 79.70      A    C  
ANISOU 1726  CD1 LEU A 223    11067   9242   9974   2910   1428  -2489  A    C  
ATOM   1727  CD2 LEU A 223       7.537  12.524  28.407  1.00 85.09      A    C  
ANISOU 1727  CD2 LEU A 223    11336  10661  10332   3202   1307  -2903  A    C  
ATOM   1728  N   LEU A 224       5.448   7.409  29.660  1.00 77.44      A    N  
ANISOU 1728  N   LEU A 224    12101   8879   8444   4429   1450  -1732  A    N  
ATOM   1729  CA  LEU A 224       4.343   6.727  30.348  1.00 76.89      A    C  
ANISOU 1729  CA  LEU A 224    12423   8505   8286   4499   1545  -1500  A    C  
ATOM   1730  C   LEU A 224       4.485   6.708  31.880  1.00 86.02      A    C  
ANISOU 1730  C   LEU A 224    13507  10015   9160   4829   1493  -1550  A    C  
ATOM   1731  O   LEU A 224       3.575   7.178  32.569  1.00 84.68      A    O  
ANISOU 1731  O   LEU A 224    13368   9735   9072   4653   1506  -1541  A    O  
ATOM   1732  CB  LEU A 224       4.148   5.300  29.809  1.00 76.72      A    C  
ANISOU 1732  CB  LEU A 224    12894   8126   8129   4704   1696  -1221  A    C  
ATOM   1733  CG  LEU A 224       2.756   4.681  29.999  1.00 79.47      A    C  
ANISOU 1733  CG  LEU A 224    13684   8000   8511   4571   1850   -987  A    C  
ATOM   1734  CD1 LEU A 224       1.703   5.402  29.185  1.00 76.04      A    C  
ANISOU 1734  CD1 LEU A 224    13209   7246   8437   4007   1864   -992  A    C  
ATOM   1735  CD2 LEU A 224       2.752   3.232  29.600  1.00 82.81      A    C  
ANISOU 1735  CD2 LEU A 224    14588   8118   8757   4822   2037   -758  A    C  
ATOM   1736  N   GLU A 225       5.602   6.162  32.401  1.00 87.92      A    N  
ANISOU 1736  N   GLU A 225    13645  10704   9057   5318   1438  -1597  A    N  
ATOM   1737  CA  GLU A 225       5.892   6.064  33.836  1.00 91.31      A    C  
ANISOU 1737  CA  GLU A 225    13975  11569   9149   5703   1380  -1641  A    C  
ATOM   1738  C   GLU A 225       5.722   7.447  34.538  1.00 96.18      A    C  
ANISOU 1738  C   GLU A 225    14162  12476   9906   5389   1265  -1951  A    C  
ATOM   1739  O   GLU A 225       4.923   7.506  35.476  1.00 96.21      A    O  
ANISOU 1739  O   GLU A 225    14277  12426   9853   5391   1289  -1892  A    O  
ATOM   1740  CB  GLU A 225       7.295   5.474  34.065  1.00 96.47      A    C  
ANISOU 1740  CB  GLU A 225    14483  12751   9420   6261   1320  -1677  A    C  
ATOM   1741  CG  GLU A 225       7.555   4.940  35.464  1.00114.24      A    C  
ANISOU 1741  CG  GLU A 225    16776  15402  11230   6803   1308  -1591  A    C  
ATOM   1742  CD  GLU A 225       8.978   4.467  35.689  1.00148.36      A    C  
ANISOU 1742  CD  GLU A 225    20879  20339  15151   7374   1236  -1639  A    C  
ATOM   1743  OE1 GLU A 225       9.207   3.235  35.673  1.00144.84      A    O  
ANISOU 1743  OE1 GLU A 225    20803  19784  14443   7869   1366  -1337  A    O  
ATOM   1744  OE2 GLU A 225       9.868   5.328  35.877  1.00149.40      A    O1-
ANISOU 1744  OE2 GLU A 225    20467  21071  15229   7324   1069  -1986  A    O1-
ATOM   1745  N   PRO A 226       6.336   8.577  34.082  1.00 92.83      A    N  
ANISOU 1745  N   PRO A 226    13284  12296   9691   5080   1175  -2275  A    N  
ATOM   1746  CA  PRO A 226       6.109   9.857  34.790  1.00 92.93      A    C  
ANISOU 1746  CA  PRO A 226    12940  12526   9845   4771   1121  -2573  A    C  
ATOM   1747  C   PRO A 226       4.722  10.493  34.572  1.00 94.38      A    C  
ANISOU 1747  C   PRO A 226    13277  12177  10405   4299   1211  -2491  A    C  
ATOM   1748  O   PRO A 226       4.336  11.371  35.356  1.00 94.40      A    O  
ANISOU 1748  O   PRO A 226    13091  12295  10481   4115   1202  -2671  A    O  
ATOM   1749  CB  PRO A 226       7.205  10.768  34.233  1.00 95.23      A    C  
ANISOU 1749  CB  PRO A 226    12757  13163  10264   4571   1057  -2926  A    C  
ATOM   1750  CG  PRO A 226       7.510  10.220  32.895  1.00 97.81      A    C  
ANISOU 1750  CG  PRO A 226    13254  13202  10707   4559   1099  -2759  A    C  
ATOM   1751  CD  PRO A 226       7.331   8.742  32.999  1.00 94.09      A    C  
ANISOU 1751  CD  PRO A 226    13229  12574   9947   5015   1142  -2405  A    C  
ATOM   1752  N   SER A 227       3.983  10.084  33.522  1.00 88.61      A    N  
ANISOU 1752  N   SER A 227    12864  10902   9902   4103   1303  -2238  A    N  
ATOM   1753  CA  SER A 227       2.657  10.648  33.255  1.00 85.75      A    C  
ANISOU 1753  CA  SER A 227    12630  10079   9873   3683   1387  -2138  A    C  
ATOM   1754  C   SER A 227       1.601  10.090  34.203  1.00 90.92      A    C  
ANISOU 1754  C   SER A 227    13596  10555  10394   3795   1441  -1939  A    C  
ATOM   1755  O   SER A 227       0.705  10.834  34.606  1.00 89.05      A    O  
ANISOU 1755  O   SER A 227    13307  10182  10347   3521   1473  -1979  A    O  
ATOM   1756  CB  SER A 227       2.240  10.407  31.812  1.00 86.47      A    C  
ANISOU 1756  CB  SER A 227    12923   9732  10200   3450   1460  -1947  A    C  
ATOM   1757  OG  SER A 227       2.807  11.395  30.968  1.00 92.46      A    O  
ANISOU 1757  OG  SER A 227    13361  10575  11195   3202   1440  -2141  A    O  
ATOM   1758  N   VAL A 228       1.717   8.791  34.578  1.00 90.19      A    N  
ANISOU 1758  N   VAL A 228    13835  10456   9976   4208   1474  -1721  A    N  
ATOM   1759  CA  VAL A 228       0.768   8.136  35.485  1.00 90.60      A    C  
ANISOU 1759  CA  VAL A 228    14225  10325   9875   4346   1558  -1511  A    C  
ATOM   1760  C   VAL A 228       0.905   8.712  36.917  1.00 96.29      A    C  
ANISOU 1760  C   VAL A 228    14701  11465  10420   4482   1481  -1696  A    C  
ATOM   1761  O   VAL A 228      -0.115   8.843  37.586  1.00 94.87      A    O  
ANISOU 1761  O   VAL A 228    14654  11109  10282   4365   1537  -1621  A    O  
ATOM   1762  CB  VAL A 228       0.803   6.578  35.460  1.00 95.75      A    C  
ANISOU 1762  CB  VAL A 228    15346  10793  10243   4743   1674  -1211  A    C  
ATOM   1763  CG1 VAL A 228       0.668   6.046  34.033  1.00 93.65      A    C  
ANISOU 1763  CG1 VAL A 228    15320  10105  10159   4552   1769  -1064  A    C  
ATOM   1764  CG2 VAL A 228       2.040   6.007  36.147  1.00 99.01      A    C  
ANISOU 1764  CG2 VAL A 228    15673  11693  10255   5306   1613  -1244  A    C  
ATOM   1765  N   TYR A 229       2.133   9.095  37.362  1.00 96.09      A    N  
ANISOU 1765  N   TYR A 229    14295  12013  10201   4697   1356  -1960  A    N  
ATOM   1766  CA  TYR A 229       2.332   9.706  38.684  1.00 98.28      A    C  
ANISOU 1766  CA  TYR A 229    14285  12761  10295   4796   1278  -2192  A    C  
ATOM   1767  C   TYR A 229       1.735  11.120  38.705  1.00 99.89      A    C  
ANISOU 1767  C   TYR A 229    14214  12868  10869   4275   1285  -2442  A    C  
ATOM   1768  O   TYR A 229       1.029  11.471  39.654  1.00100.25      A    O  
ANISOU 1768  O   TYR A 229    14257  12934  10898   4209   1306  -2483  A    O  
ATOM   1769  CB  TYR A 229       3.826   9.748  39.113  1.00103.38      A    C  
ANISOU 1769  CB  TYR A 229    14559  14113  10606   5151   1147  -2438  A    C  
ATOM   1770  CG  TYR A 229       4.070  10.730  40.250  1.00107.80      A    C  
ANISOU 1770  CG  TYR A 229    14699  15198  11061   5085   1062  -2798  A    C  
ATOM   1771  CD1 TYR A 229       3.788  10.384  41.570  1.00112.17      A    C  
ANISOU 1771  CD1 TYR A 229    15326  16012  11283   5388   1050  -2740  A    C  
ATOM   1772  CD2 TYR A 229       4.463  12.044  39.992  1.00108.51      A    C  
ANISOU 1772  CD2 TYR A 229    14344  15474  11410   4677   1027  -3199  A    C  
ATOM   1773  CE1 TYR A 229       3.918  11.311  42.607  1.00115.12      A    C  
ANISOU 1773  CE1 TYR A 229    15316  16858  11566   5286    984  -3092  A    C  
ATOM   1774  CE2 TYR A 229       4.570  12.985  41.018  1.00111.42      A    C  
ANISOU 1774  CE2 TYR A 229    14348  16271  11714   4549    989  -3561  A    C  
ATOM   1775  CZ  TYR A 229       4.316  12.610  42.327  1.00121.12      A    C  
ANISOU 1775  CZ  TYR A 229    15633  17796  12592   4855    956  -3517  A    C  
ATOM   1776  OH  TYR A 229       4.464  13.526  43.344  1.00123.68      A    O  
ANISOU 1776  OH  TYR A 229    15580  18584  12828   4723    919  -3903  A    O  
ATOM   1777  N   GLU A 230       2.063  11.935  37.679  1.00 94.07      A    N  
ANISOU 1777  N   GLU A 230    13249  12037  10456   3931   1285  -2607  A    N  
ATOM   1778  CA  GLU A 230       1.629  13.328  37.538  1.00 92.22      A    C  
ANISOU 1778  CA  GLU A 230    12757  11681  10601   3450   1335  -2838  A    C  
ATOM   1779  C   GLU A 230       0.103  13.465  37.423  1.00 91.63      A    C  
ANISOU 1779  C   GLU A 230    12959  11067  10789   3179   1445  -2605  A    C  
ATOM   1780  O   GLU A 230      -0.453  14.454  37.906  1.00 90.23      A    O  
ANISOU 1780  O   GLU A 230    12626  10850  10806   2913   1499  -2760  A    O  
ATOM   1781  CB  GLU A 230       2.300  13.961  36.307  1.00 92.84      A    C  
ANISOU 1781  CB  GLU A 230    12612  11712  10950   3195   1348  -2983  A    C  
ATOM   1782  CG  GLU A 230       2.241  15.485  36.265  1.00104.34      A    C  
ANISOU 1782  CG  GLU A 230    13728  13173  12745   2764   1425  -3301  A    C  
ATOM   1783  CD  GLU A 230       3.184  16.252  37.177  1.00130.27      A    C  
ANISOU 1783  CD  GLU A 230    16582  17029  15884   2768   1383  -3751  A    C  
ATOM   1784  OE1 GLU A 230       2.966  17.473  37.360  1.00129.11      A    O  
ANISOU 1784  OE1 GLU A 230    16210  16841  16005   2410   1491  -4014  A    O  
ATOM   1785  OE2 GLU A 230       4.154  15.646  37.688  1.00126.57      A    O1-
ANISOU 1785  OE2 GLU A 230    15993  17067  15032   3126   1259  -3850  A    O1-
ATOM   1786  N   PHE A 231      -0.566  12.493  36.778  1.00 85.99      A    N  
ANISOU 1786  N   PHE A 231    12641   9955  10078   3237   1495  -2252  A    N  
ATOM   1787  CA  PHE A 231      -2.013  12.555  36.568  1.00 83.05      A    C  
ANISOU 1787  CA  PHE A 231    12512   9112   9933   2973   1599  -2031  A    C  
ATOM   1788  C   PHE A 231      -2.734  11.350  37.204  1.00 85.81      A    C  
ANISOU 1788  C   PHE A 231    13271   9308  10023   3224   1645  -1752  A    C  
ATOM   1789  O   PHE A 231      -3.716  10.850  36.654  1.00 84.11      A    O  
ANISOU 1789  O   PHE A 231    13360   8688   9912   3089   1735  -1502  A    O  
ATOM   1790  CB  PHE A 231      -2.320  12.677  35.059  1.00 82.54      A    C  
ANISOU 1790  CB  PHE A 231    12506   8685  10170   2688   1652  -1899  A    C  
ATOM   1791  CG  PHE A 231      -1.500  13.721  34.330  1.00 83.81      A    C  
ANISOU 1791  CG  PHE A 231    12309   8976  10559   2488   1635  -2137  A    C  
ATOM   1792  CD1 PHE A 231      -1.516  15.054  34.735  1.00 87.16      A    C  
ANISOU 1792  CD1 PHE A 231    12420   9501  11196   2251   1675  -2395  A    C  
ATOM   1793  CD2 PHE A 231      -0.710  13.371  33.244  1.00 85.57      A    C  
ANISOU 1793  CD2 PHE A 231    12520   9205  10788   2529   1606  -2113  A    C  
ATOM   1794  CE1 PHE A 231      -0.753  16.018  34.067  1.00 88.01      A    C  
ANISOU 1794  CE1 PHE A 231    12220   9697  11522   2050   1705  -2621  A    C  
ATOM   1795  CE2 PHE A 231       0.062  14.333  32.582  1.00 88.56      A    C  
ANISOU 1795  CE2 PHE A 231    12574   9702  11374   2339   1611  -2335  A    C  
ATOM   1796  CZ  PHE A 231       0.032  15.651  32.994  1.00 86.94      A    C  
ANISOU 1796  CZ  PHE A 231    12071   9576  11384   2095   1670  -2586  A    C  
ATOM   1797  N   ALA A 232      -2.271  10.928  38.397  1.00 83.17      A    N  
ANISOU 1797  N   ALA A 232    12935   9318   9347   3576   1599  -1808  A    N  
ATOM   1798  CA  ALA A 232      -2.845   9.814  39.159  1.00 83.02      A    C  
ANISOU 1798  CA  ALA A 232    13302   9192   9050   3862   1670  -1553  A    C  
ATOM   1799  C   ALA A 232      -4.243  10.137  39.714  1.00 81.86      A    C  
ANISOU 1799  C   ALA A 232    13279   8776   9047   3615   1758  -1469  A    C  
ATOM   1800  O   ALA A 232      -5.069   9.234  39.847  1.00 80.21      A    O  
ANISOU 1800  O   ALA A 232    13455   8263   8759   3668   1872  -1206  A    O  
ATOM   1801  CB  ALA A 232      -1.915   9.444  40.304  1.00 87.13      A    C  
ANISOU 1801  CB  ALA A 232    13728  10228   9149   4331   1593  -1644  A    C  
ATOM   1802  N   GLU A 233      -4.485  11.416  40.046  1.00 76.90      A    N  
ANISOU 1802  N   GLU A 233    12328   8260   8630   3345   1728  -1705  A    N  
ATOM   1803  CA  GLU A 233      -5.712  11.931  40.668  1.00 75.18      A    C  
ANISOU 1803  CA  GLU A 233    12146   7860   8558   3117   1805  -1680  A    C  
ATOM   1804  C   GLU A 233      -6.791  12.420  39.644  1.00 73.99      A    C  
ANISOU 1804  C   GLU A 233    12037   7269   8806   2693   1891  -1562  A    C  
ATOM   1805  O   GLU A 233      -7.678  13.201  40.027  1.00 72.24      A    O  
ANISOU 1805  O   GLU A 233    11728   6946   8776   2461   1949  -1604  A    O  
ATOM   1806  CB  GLU A 233      -5.338  13.079  41.630  1.00 77.94      A    C  
ANISOU 1806  CB  GLU A 233    12114   8586   8913   3067   1751  -2021  A    C  
ATOM   1807  CG  GLU A 233      -4.677  12.609  42.924  1.00 96.17      A    C  
ANISOU 1807  CG  GLU A 233    14390  11362  10788   3472   1681  -2112  A    C  
ATOM   1808  CD  GLU A 233      -3.977  13.656  43.776  1.00125.48      A    C  
ANISOU 1808  CD  GLU A 233    17667  15567  14443   3442   1609  -2520  A    C  
ATOM   1809  OE1 GLU A 233      -4.547  14.754  43.977  1.00122.63      A    O  
ANISOU 1809  OE1 GLU A 233    17132  15113  14348   3111   1672  -2698  A    O  
ATOM   1810  OE2 GLU A 233      -2.876  13.351  44.291  1.00121.83      A    O1-
ANISOU 1810  OE2 GLU A 233    17040  15604  13647   3763   1504  -2667  A    O1-
ATOM   1811  N   THR A 234      -6.750  11.918  38.377  1.00 66.69      A    N  
ANISOU 1811  N   THR A 234    11251   6108   7982   2613   1908  -1405  A    N  
ATOM   1812  CA  THR A 234      -7.698  12.293  37.312  1.00 62.93      A    C  
ANISOU 1812  CA  THR A 234    10795   5285   7830   2250   1980  -1279  A    C  
ATOM   1813  C   THR A 234      -9.160  11.948  37.673  1.00 66.20      A    C  
ANISOU 1813  C   THR A 234    11451   5437   8266   2117   2087  -1079  A    C  
ATOM   1814  O   THR A 234     -10.037  12.798  37.491  1.00 64.46      A    O  
ANISOU 1814  O   THR A 234    11099   5088   8303   1839   2137  -1074  A    O  
ATOM   1815  CB  THR A 234      -7.328  11.644  35.971  1.00 62.88      A    C  
ANISOU 1815  CB  THR A 234    10911   5129   7851   2228   1976  -1155  A    C  
ATOM   1816  CG2 THR A 234      -8.082  12.251  34.819  1.00 57.76      A    C  
ANISOU 1816  CG2 THR A 234    10178   4242   7526   1868   2024  -1073  A    C  
ATOM   1817  OG1 THR A 234      -5.940  11.812  35.705  1.00 59.93      A    O  
ANISOU 1817  OG1 THR A 234    10339   5021   7411   2393   1881  -1330  A    O  
ATOM   1818  N   GLU A 235      -9.411  10.713  38.175  1.00 63.68      A    N  
ANISOU 1818  N   GLU A 235    11483   5039   7674   2324   2143   -912  A    N  
ATOM   1819  CA  GLU A 235     -10.749  10.247  38.568  1.00 63.08      A    C  
ANISOU 1819  CA  GLU A 235    11661   4724   7581   2204   2267   -733  A    C  
ATOM   1820  C   GLU A 235     -11.329  11.121  39.683  1.00 66.80      A    C  
ANISOU 1820  C   GLU A 235    11965   5311   8104   2151   2271   -839  A    C  
ATOM   1821  O   GLU A 235     -12.484  11.544  39.586  1.00 65.83      A    O  
ANISOU 1821  O   GLU A 235    11829   5018   8168   1888   2344   -769  A    O  
ATOM   1822  CB  GLU A 235     -10.724   8.773  39.013  1.00 66.00      A    C  
ANISOU 1822  CB  GLU A 235    12453   4994   7630   2475   2363   -557  A    C  
ATOM   1823  CG  GLU A 235     -11.751   7.897  38.309  1.00 74.26      A    C  
ANISOU 1823  CG  GLU A 235    13823   5675   8716   2253   2520   -351  A    C  
ATOM   1824  CD  GLU A 235     -13.220   8.282  38.389  1.00 85.02      A    C  
ANISOU 1824  CD  GLU A 235    15173   6881  10250   1918   2602   -291  A    C  
ATOM   1825  OE1 GLU A 235     -13.942   8.011  37.403  1.00 77.53      A    O  
ANISOU 1825  OE1 GLU A 235    14303   5728   9428   1631   2676   -197  A    O  
ATOM   1826  OE2 GLU A 235     -13.661   8.822  39.431  1.00 74.69      A    O1-
ANISOU 1826  OE2 GLU A 235    13770   5676   8931   1946   2599   -341  A    O1-
ATOM   1827  N   LYS A 236     -10.506  11.417  40.717  1.00 64.74      A    N  
ANISOU 1827  N   LYS A 236    11555   5376   7669   2403   2193  -1022  A    N  
ATOM   1828  CA  LYS A 236     -10.840  12.285  41.847  1.00 65.21      A    C  
ANISOU 1828  CA  LYS A 236    11424   5609   7744   2379   2191  -1183  A    C  
ATOM   1829  C   LYS A 236     -11.305  13.645  41.315  1.00 67.21      A    C  
ANISOU 1829  C   LYS A 236    11382   5769   8385   2028   2213  -1301  A    C  
ATOM   1830  O   LYS A 236     -12.332  14.153  41.761  1.00 66.53      A    O  
ANISOU 1830  O   LYS A 236    11273   5585   8422   1868   2291  -1282  A    O  
ATOM   1831  CB  LYS A 236      -9.612  12.430  42.779  1.00 69.63      A    C  
ANISOU 1831  CB  LYS A 236    11799   6611   8044   2690   2084  -1413  A    C  
ATOM   1832  CG  LYS A 236      -9.822  13.308  44.028  1.00 70.83      A    C  
ANISOU 1832  CG  LYS A 236    11745   7006   8162   2681   2083  -1625  A    C  
ATOM   1833  CD  LYS A 236      -8.546  13.392  44.859  1.00 76.03      A    C  
ANISOU 1833  CD  LYS A 236    12132   8169   8586   2925   1965  -1913  A    C  
ATOM   1834  CE  LYS A 236      -8.503  14.600  45.759  1.00 88.09      A    C  
ANISOU 1834  CE  LYS A 236    13431   9966  10073   2884   1971  -2169  A    C  
ATOM   1835  NZ  LYS A 236      -7.216  14.679  46.496  1.00 99.71      A    N1+
ANISOU 1835  NZ  LYS A 236    14581  11986  11317   3070   1857  -2500  A    N1+
ATOM   1836  N   MET A 237     -10.575  14.193  40.321  1.00 62.80      A    N  
ANISOU 1836  N   MET A 237    10618   5227   8017   1922   2165  -1400  A    N  
ATOM   1837  CA  MET A 237     -10.896  15.479  39.703  1.00 61.47      A    C  
ANISOU 1837  CA  MET A 237    10188   4950   8219   1624   2219  -1487  A    C  
ATOM   1838  C   MET A 237     -12.208  15.391  38.912  1.00 61.18      A    C  
ANISOU 1838  C   MET A 237    10281   4592   8373   1393   2309  -1224  A    C  
ATOM   1839  O   MET A 237     -13.023  16.315  39.002  1.00 59.27      A    O  
ANISOU 1839  O   MET A 237     9905   4254   8359   1206   2398  -1227  A    O  
ATOM   1840  CB  MET A 237      -9.738  15.963  38.817  1.00 64.12      A    C  
ANISOU 1840  CB  MET A 237    10304   5382   8677   1593   2165  -1639  A    C  
ATOM   1841  CG  MET A 237      -8.652  16.676  39.598  1.00 70.35      A    C  
ANISOU 1841  CG  MET A 237    10814   6513   9404   1681   2120  -1988  A    C  
ATOM   1842  SD  MET A 237      -7.314  17.320  38.553  1.00 75.24      A    S  
ANISOU 1842  SD  MET A 237    11160   7244  10183   1602   2087  -2190  A    S  
ATOM   1843  CE  MET A 237      -6.256  15.883  38.497  1.00 72.98      A    C  
ANISOU 1843  CE  MET A 237    11042   7186   9501   1965   1934  -2122  A    C  
ATOM   1844  N   LEU A 238     -12.438  14.270  38.198  1.00 56.09      A    N  
ANISOU 1844  N   LEU A 238     9892   3803   7616   1411   2302  -1008  A    N  
ATOM   1845  CA  LEU A 238     -13.642  14.012  37.393  1.00 54.76      A    C  
ANISOU 1845  CA  LEU A 238     9842   3395   7569   1185   2380   -777  A    C  
ATOM   1846  C   LEU A 238     -14.866  13.858  38.282  1.00 57.47      A    C  
ANISOU 1846  C   LEU A 238    10310   3663   7862   1127   2468   -685  A    C  
ATOM   1847  O   LEU A 238     -15.932  14.379  37.945  1.00 55.68      A    O  
ANISOU 1847  O   LEU A 238     9997   3333   7825    910   2540   -587  A    O  
ATOM   1848  CB  LEU A 238     -13.446  12.745  36.526  1.00 55.13      A    C  
ANISOU 1848  CB  LEU A 238    10149   3337   7463   1219   2369   -629  A    C  
ATOM   1849  CG  LEU A 238     -14.474  12.442  35.421  1.00 59.55      A    C  
ANISOU 1849  CG  LEU A 238    10788   3712   8125    956   2437   -436  A    C  
ATOM   1850  CD1 LEU A 238     -14.609  13.588  34.429  1.00 59.17      A    C  
ANISOU 1850  CD1 LEU A 238    10440   3675   8368    764   2427   -431  A    C  
ATOM   1851  CD2 LEU A 238     -14.073  11.218  34.661  1.00 63.00      A    C  
ANISOU 1851  CD2 LEU A 238    11486   4060   8393    999   2443   -352  A    C  
ATOM   1852  N   LYS A 239     -14.705  13.165  39.421  1.00 55.12      A    N  
ANISOU 1852  N   LYS A 239    10204   3441   7299   1339   2469   -710  A    N  
ATOM   1853  CA  LYS A 239     -15.766  12.973  40.414  1.00 56.36      A    C  
ANISOU 1853  CA  LYS A 239    10494   3544   7375   1314   2560   -638  A    C  
ATOM   1854  C   LYS A 239     -16.145  14.326  41.070  1.00 58.99      A    C  
ANISOU 1854  C   LYS A 239    10544   3964   7904   1223   2582   -781  A    C  
ATOM   1855  O   LYS A 239     -17.332  14.668  41.140  1.00 57.59      A    O  
ANISOU 1855  O   LYS A 239    10345   3679   7859   1043   2672   -687  A    O  
ATOM   1856  CB  LYS A 239     -15.315  11.947  41.473  1.00 61.54      A    C  
ANISOU 1856  CB  LYS A 239    11419   4285   7680   1615   2565   -627  A    C  
ATOM   1857  CG  LYS A 239     -16.449  11.294  42.284  1.00 83.94      A    C  
ANISOU 1857  CG  LYS A 239    14519   6993  10380   1589   2697   -480  A    C  
ATOM   1858  CD  LYS A 239     -16.796   9.816  41.950  1.00 98.80      A    C  
ANISOU 1858  CD  LYS A 239    16807   8649  12083   1598   2815   -275  A    C  
ATOM   1859  CE  LYS A 239     -15.683   8.806  42.169  1.00116.09      A    C  
ANISOU 1859  CE  LYS A 239    19245  10888  13977   1955   2810   -245  A    C  
ATOM   1860  NZ  LYS A 239     -16.165   7.410  42.028  1.00125.67      A    N1+
ANISOU 1860  NZ  LYS A 239    20890  11825  15035   1945   2991    -50  A    N1+
ATOM   1861  N   TYR A 240     -15.125  15.107  41.488  1.00 56.13      A    N  
ANISOU 1861  N   TYR A 240     9956   3803   7567   1334   2515  -1022  A    N  
ATOM   1862  CA  TYR A 240     -15.280  16.436  42.118  1.00 56.67      A    C  
ANISOU 1862  CA  TYR A 240     9755   3952   7825   1245   2564  -1217  A    C  
ATOM   1863  C   TYR A 240     -16.018  17.410  41.185  1.00 56.69      A    C  
ANISOU 1863  C   TYR A 240     9583   3767   8190    988   2657  -1140  A    C  
ATOM   1864  O   TYR A 240     -16.859  18.184  41.635  1.00 56.38      A    O  
ANISOU 1864  O   TYR A 240     9440   3674   8308    882   2762  -1156  A    O  
ATOM   1865  CB  TYR A 240     -13.902  17.002  42.508  1.00 60.05      A    C  
ANISOU 1865  CB  TYR A 240     9966   4644   8206   1371   2488  -1521  A    C  
ATOM   1866  CG  TYR A 240     -13.399  16.629  43.892  1.00 65.62      A    C  
ANISOU 1866  CG  TYR A 240    10708   5638   8587   1617   2433  -1676  A    C  
ATOM   1867  CD1 TYR A 240     -13.602  15.347  44.417  1.00 68.12      A    C  
ANISOU 1867  CD1 TYR A 240    11331   5962   8591   1820   2420  -1492  A    C  
ATOM   1868  CD2 TYR A 240     -12.706  17.545  44.667  1.00 69.20      A    C  
ANISOU 1868  CD2 TYR A 240    10890   6376   9027   1650   2410  -2013  A    C  
ATOM   1869  CE1 TYR A 240     -13.114  14.993  45.673  1.00 71.72      A    C  
ANISOU 1869  CE1 TYR A 240    11818   6713   8719   2087   2376  -1605  A    C  
ATOM   1870  CE2 TYR A 240     -12.220  17.204  45.931  1.00 73.07      A    C  
ANISOU 1870  CE2 TYR A 240    11380   7203   9179   1890   2349  -2163  A    C  
ATOM   1871  CZ  TYR A 240     -12.423  15.925  46.429  1.00 82.43      A    C  
ANISOU 1871  CZ  TYR A 240    12871   8404  10044   2129   2327  -1939  A    C  
ATOM   1872  OH  TYR A 240     -11.949  15.580  47.673  1.00 86.57      A    O  
ANISOU 1872  OH  TYR A 240    13397   9287  10208   2406   2274  -2055  A    O  
ATOM   1873  N   ALA A 241     -15.730  17.319  39.879  1.00 50.95      A    N  
ANISOU 1873  N   ALA A 241     8831   2951   7578    910   2627  -1038  A    N  
ATOM   1874  CA  ALA A 241     -16.375  18.098  38.834  1.00 48.77      A    C  
ANISOU 1874  CA  ALA A 241     8405   2525   7600    712   2712   -913  A    C  
ATOM   1875  C   ALA A 241     -17.841  17.690  38.672  1.00 52.71      A    C  
ANISOU 1875  C   ALA A 241     9019   2909   8097    591   2777   -663  A    C  
ATOM   1876  O   ALA A 241     -18.685  18.567  38.513  1.00 52.60      A    O  
ANISOU 1876  O   ALA A 241     8855   2832   8300    476   2885   -590  A    O  
ATOM   1877  CB  ALA A 241     -15.639  17.906  37.524  1.00 48.31      A    C  
ANISOU 1877  CB  ALA A 241     8314   2445   7598    689   2649   -864  A    C  
ATOM   1878  N   GLU A 242     -18.143  16.368  38.709  1.00 49.80      A    N  
ANISOU 1878  N   GLU A 242     8919   2521   7483    618   2736   -538  A    N  
ATOM   1879  CA  GLU A 242     -19.501  15.821  38.572  1.00 50.07      A    C  
ANISOU 1879  CA  GLU A 242     9075   2475   7474    472   2808   -336  A    C  
ATOM   1880  C   GLU A 242     -20.398  16.263  39.707  1.00 57.83      A    C  
ANISOU 1880  C   GLU A 242    10029   3469   8476    460   2897   -355  A    C  
ATOM   1881  O   GLU A 242     -21.585  16.501  39.484  1.00 58.53      A    O  
ANISOU 1881  O   GLU A 242    10051   3526   8663    309   2980   -217  A    O  
ATOM   1882  CB  GLU A 242     -19.482  14.292  38.521  1.00 51.53      A    C  
ANISOU 1882  CB  GLU A 242     9587   2609   7384    502   2790   -250  A    C  
ATOM   1883  CG  GLU A 242     -19.217  13.695  37.159  1.00 54.97      A    C  
ANISOU 1883  CG  GLU A 242    10076   2996   7812    410   2753   -158  A    C  
ATOM   1884  CD  GLU A 242     -19.332  12.179  37.141  1.00 71.48      A    C  
ANISOU 1884  CD  GLU A 242    12521   4990   9648    408   2795    -80  A    C  
ATOM   1885  OE1 GLU A 242     -18.759  11.523  38.044  1.00 57.94      A    O  
ANISOU 1885  OE1 GLU A 242    11024   3261   7728    621   2797   -133  A    O  
ATOM   1886  OE2 GLU A 242     -20.007  11.645  36.228  1.00 51.23      A    O1-
ANISOU 1886  OE2 GLU A 242    10016   2372   7078    195   2847     31  A    O1-
ATOM   1887  N   ASP A 243     -19.830  16.379  40.926  1.00 56.24      A    N  
ANISOU 1887  N   ASP A 243     9857   3347   8166    625   2879   -532  A    N  
ATOM   1888  CA  ASP A 243     -20.522  16.849  42.130  1.00 56.66      A    C  
ANISOU 1888  CA  ASP A 243     9877   3432   8221    635   2962   -592  A    C  
ATOM   1889  C   ASP A 243     -20.993  18.297  41.944  1.00 61.08      A    C  
ANISOU 1889  C   ASP A 243    10149   3958   9100    526   3059   -628  A    C  
ATOM   1890  O   ASP A 243     -22.068  18.675  42.410  1.00 61.50      A    O  
ANISOU 1890  O   ASP A 243    10159   3983   9225    456   3164   -567  A    O  
ATOM   1891  CB  ASP A 243     -19.579  16.755  43.353  1.00 59.61      A    C  
ANISOU 1891  CB  ASP A 243    10300   3959   8392    851   2908   -807  A    C  
ATOM   1892  CG  ASP A 243     -19.166  15.359  43.793  1.00 70.41      A    C  
ANISOU 1892  CG  ASP A 243    11972   5367   9414   1033   2852   -748  A    C  
ATOM   1893  OD1 ASP A 243     -18.444  15.248  44.810  1.00 72.65      A    O  
ANISOU 1893  OD1 ASP A 243    12282   5827   9493   1247   2805   -898  A    O  
ATOM   1894  OD2 ASP A 243     -19.580  14.377  43.136  1.00 76.79      A    O1-
ANISOU 1894  OD2 ASP A 243    12992   6040  10145    965   2874   -555  A    O1-
ATOM   1895  N   LEU A 244     -20.184  19.087  41.226  1.00 57.27      A    N  
ANISOU 1895  N   LEU A 244     9483   3467   8812    518   3046   -717  A    N  
ATOM   1896  CA  LEU A 244     -20.396  20.502  40.946  1.00 57.16      A    C  
ANISOU 1896  CA  LEU A 244     9218   3381   9118    443   3177   -756  A    C  
ATOM   1897  C   LEU A 244     -21.265  20.761  39.715  1.00 57.72      A    C  
ANISOU 1897  C   LEU A 244     9200   3363   9368    328   3242   -489  A    C  
ATOM   1898  O   LEU A 244     -22.175  21.585  39.788  1.00 57.73      A    O  
ANISOU 1898  O   LEU A 244     9074   3312   9549    284   3385   -403  A    O  
ATOM   1899  CB  LEU A 244     -19.027  21.170  40.729  1.00 58.27      A    C  
ANISOU 1899  CB  LEU A 244     9219   3553   9369    483   3160   -991  A    C  
ATOM   1900  CG  LEU A 244     -18.261  21.761  41.930  1.00 66.86      A    C  
ANISOU 1900  CG  LEU A 244    10219   4755  10429    546   3188  -1331  A    C  
ATOM   1901  CD1 LEU A 244     -18.229  20.823  43.141  1.00 68.62      A    C  
ANISOU 1901  CD1 LEU A 244    10615   5145  10314    678   3086  -1402  A    C  
ATOM   1902  CD2 LEU A 244     -16.838  22.047  41.538  1.00 71.13      A    C  
ANISOU 1902  CD2 LEU A 244    10645   5380  11002    569   3134  -1552  A    C  
ATOM   1903  N   ALA A 245     -20.971  20.102  38.577  1.00 51.78      A    N  
ANISOU 1903  N   ALA A 245     8498   2617   8558    294   3147   -360  A    N  
ATOM   1904  CA  ALA A 245     -21.644  20.386  37.308  1.00 49.65      A    C  
ANISOU 1904  CA  ALA A 245     8107   2327   8430    199   3196   -122  A    C  
ATOM   1905  C   ALA A 245     -22.798  19.461  36.939  1.00 51.59      A    C  
ANISOU 1905  C   ALA A 245     8445   2640   8516     89   3172     93  A    C  
ATOM   1906  O   ALA A 245     -23.675  19.872  36.182  1.00 50.26      A    O  
ANISOU 1906  O   ALA A 245     8124   2521   8451     19   3239    288  A    O  
ATOM   1907  CB  ALA A 245     -20.631  20.371  36.195  1.00 49.30      A    C  
ANISOU 1907  CB  ALA A 245     8020   2274   8437    206   3128   -127  A    C  
ATOM   1908  N   GLY A 246     -22.779  18.235  37.433  1.00 48.68      A    N  
ANISOU 1908  N   GLY A 246     8318   2288   7890     77   3095     55  A    N  
ATOM   1909  CA  GLY A 246     -23.782  17.231  37.099  1.00 48.24      A    C  
ANISOU 1909  CA  GLY A 246     8381   2282   7667    -69   3098    209  A    C  
ATOM   1910  C   GLY A 246     -23.152  16.038  36.412  1.00 50.63      A    C  
ANISOU 1910  C   GLY A 246     8886   2566   7783   -105   3006    209  A    C  
ATOM   1911  O   GLY A 246     -21.923  15.962  36.355  1.00 50.06      A    O  
ANISOU 1911  O   GLY A 246     8872   2453   7694     21   2928     93  A    O  
ATOM   1912  N   PRO A 247     -23.951  15.100  35.849  1.00 47.12      A    N  
ANISOU 1912  N   PRO A 247     8544   2163   7195   -286   3028    322  A    N  
ATOM   1913  CA  PRO A 247     -23.358  13.886  35.251  1.00 46.44      A    C  
ANISOU 1913  CA  PRO A 247     8694   2023   6927   -330   2980    302  A    C  
ATOM   1914  C   PRO A 247     -22.459  14.101  34.039  1.00 47.24      A    C  
ANISOU 1914  C   PRO A 247     8690   2150   7111   -307   2894    309  A    C  
ATOM   1915  O   PRO A 247     -22.676  15.019  33.243  1.00 46.44      A    O  
ANISOU 1915  O   PRO A 247     8317   2143   7185   -342   2890    394  A    O  
ATOM   1916  CB  PRO A 247     -24.581  13.062  34.843  1.00 49.29      A    C  
ANISOU 1916  CB  PRO A 247     9126   2445   7155   -588   3062    397  A    C  
ATOM   1917  CG  PRO A 247     -25.690  13.566  35.702  1.00 54.13      A    C  
ANISOU 1917  CG  PRO A 247     9627   3121   7817   -629   3145    438  A    C  
ATOM   1918  CD  PRO A 247     -25.429  15.024  35.839  1.00 49.07      A    C  
ANISOU 1918  CD  PRO A 247     8712   2515   7418   -468   3118    442  A    C  
ATOM   1919  N   TYR A 248     -21.435  13.221  33.918  1.00 42.33      A    N  
ANISOU 1919  N   TYR A 248     8295   1439   6347   -227   2840    230  A    N  
ATOM   1920  CA  TYR A 248     -20.485  13.178  32.804  1.00 40.26      A    C  
ANISOU 1920  CA  TYR A 248     7988   1190   6120   -203   2761    219  A    C  
ATOM   1921  C   TYR A 248     -21.157  12.363  31.711  1.00 43.07      A    C  
ANISOU 1921  C   TYR A 248     8403   1593   6367   -441   2795    311  A    C  
ATOM   1922  O   TYR A 248     -21.466  11.198  31.934  1.00 44.36      A    O  
ANISOU 1922  O   TYR A 248     8844   1672   6338   -530   2864    292  A    O  
ATOM   1923  CB  TYR A 248     -19.137  12.573  33.261  1.00 40.32      A    C  
ANISOU 1923  CB  TYR A 248     8206   1108   6004     16   2701     89  A    C  
ATOM   1924  CG  TYR A 248     -18.050  12.573  32.205  1.00 38.47      A    C  
ANISOU 1924  CG  TYR A 248     7885    962   5769     65   2620     56  A    C  
ATOM   1925  CD1 TYR A 248     -17.423  13.755  31.822  1.00 38.63      A    C  
ANISOU 1925  CD1 TYR A 248     7660    990   6029    128   2568     15  A    C  
ATOM   1926  CD2 TYR A 248     -17.606  11.383  31.632  1.00 38.87      A    C  
ANISOU 1926  CD2 TYR A 248     8184    939   5646     55   2621     57  A    C  
ATOM   1927  CE1 TYR A 248     -16.407  13.760  30.867  1.00 38.09      A    C  
ANISOU 1927  CE1 TYR A 248     7517    990   5965    167   2503    -17  A    C  
ATOM   1928  CE2 TYR A 248     -16.586  11.376  30.679  1.00 39.00      A    C  
ANISOU 1928  CE2 TYR A 248     8163    957   5699    110   2549     25  A    C  
ATOM   1929  CZ  TYR A 248     -15.987  12.567  30.304  1.00 42.07      A    C  
ANISOU 1929  CZ  TYR A 248     8281   1390   6314    168   2481    -13  A    C  
ATOM   1930  OH  TYR A 248     -14.996  12.580  29.362  1.00 41.23      A    O  
ANISOU 1930  OH  TYR A 248     8121   1312   6234    212   2421    -48  A    O  
ATOM   1931  N   VAL A 249     -21.444  12.985  30.560  1.00 38.53      A    N  
ANISOU 1931  N   VAL A 249     7566   1166   5908   -551   2772    408  A    N  
ATOM   1932  CA  VAL A 249     -22.203  12.352  29.472  1.00 39.39      A    C  
ANISOU 1932  CA  VAL A 249     7650   1409   5906   -803   2801    483  A    C  
ATOM   1933  C   VAL A 249     -21.337  11.747  28.357  1.00 43.06      A    C  
ANISOU 1933  C   VAL A 249     8201   1862   6299   -832   2749    447  A    C  
ATOM   1934  O   VAL A 249     -21.865  11.062  27.485  1.00 46.77      A    O  
ANISOU 1934  O   VAL A 249     8692   2437   6640  -1058   2783    464  A    O  
ATOM   1935  CB  VAL A 249     -23.220  13.356  28.855  1.00 43.33      A    C  
ANISOU 1935  CB  VAL A 249     7786   2152   6527   -891   2815    638  A    C  
ATOM   1936  CG1 VAL A 249     -24.246  13.829  29.882  1.00 43.19      A    C  
ANISOU 1936  CG1 VAL A 249     7689   2165   6555   -893   2889    679  A    C  
ATOM   1937  CG2 VAL A 249     -22.522  14.538  28.199  1.00 42.01      A    C  
ANISOU 1937  CG2 VAL A 249     7375   2020   6568   -726   2764    706  A    C  
ATOM   1938  N   TRP A 250     -20.035  11.960  28.404  1.00 38.03      A    N  
ANISOU 1938  N   TRP A 250     7568   1196   5687   -600   2674    357  A    N  
ATOM   1939  CA  TRP A 250     -19.095  11.572  27.361  1.00 37.94      A    C  
ANISOU 1939  CA  TRP A 250     7591   1196   5627   -584   2619    321  A    C  
ATOM   1940  C   TRP A 250     -18.600  10.108  27.436  1.00 43.88      A    C  
ANISOU 1940  C   TRP A 250     8770   1689   6214   -614   2666    249  A    C  
ATOM   1941  O   TRP A 250     -17.856   9.674  26.549  1.00 41.58      A    O  
ANISOU 1941  O   TRP A 250     8540   1383   5874   -608   2636    215  A    O  
ATOM   1942  CB  TRP A 250     -17.917  12.530  27.394  1.00 36.29      A    C  
ANISOU 1942  CB  TRP A 250     7158   1117   5515   -340   2539    257  A    C  
ATOM   1943  CG  TRP A 250     -18.361  13.946  27.174  1.00 36.89      A    C  
ANISOU 1943  CG  TRP A 250     6954   1192   5870   -347   2552    374  A    C  
ATOM   1944  CD1 TRP A 250     -18.672  14.872  28.129  1.00 39.20      A    C  
ANISOU 1944  CD1 TRP A 250     7203   1313   6377   -283   2596    401  A    C  
ATOM   1945  CD2 TRP A 250     -18.666  14.551  25.909  1.00 36.35      A    C  
ANISOU 1945  CD2 TRP A 250     6650   1259   5901   -428   2553    511  A    C  
ATOM   1946  CE2 TRP A 250     -19.079  15.878  26.169  1.00 40.59      A    C  
ANISOU 1946  CE2 TRP A 250     7003   1710   6709   -381   2617    640  A    C  
ATOM   1947  CE3 TRP A 250     -18.635  14.095  24.577  1.00 36.68      A    C  
ANISOU 1947  CE3 TRP A 250     6706   1333   5898   -576   2529    601  A    C  
ATOM   1948  NE1 TRP A 250     -19.056  16.054  27.532  1.00 39.14      A    N  
ANISOU 1948  NE1 TRP A 250     6909   1398   6566   -287   2642    532  A    N  
ATOM   1949  CZ2 TRP A 250     -19.438  16.762  25.142  1.00 39.84      A    C  
ANISOU 1949  CZ2 TRP A 250     6642   1760   6735   -390   2659    820  A    C  
ATOM   1950  CZ3 TRP A 250     -18.948  14.989  23.561  1.00 38.22      A    C  
ANISOU 1950  CZ3 TRP A 250     6624   1687   6210   -597   2546    773  A    C  
ATOM   1951  CH2 TRP A 250     -19.326  16.307  23.846  1.00 39.04      A    C  
ANISOU 1951  CH2 TRP A 250     6501   1807   6525   -485   2615    890  A    C  
ATOM   1952  N   GLY A 251     -19.012   9.389  28.476  1.00 42.71      A    N  
ANISOU 1952  N   GLY A 251     8876   1410   5942   -615   2756    216  A    N  
ATOM   1953  CA  GLY A 251     -18.652   7.997  28.687  1.00 44.86      A    C  
ANISOU 1953  CA  GLY A 251     9548   1485   6011   -597   2856    152  A    C  
ATOM   1954  C   GLY A 251     -17.246   7.729  29.185  1.00 49.36      A    C  
ANISOU 1954  C   GLY A 251    10294   1932   6531   -265   2808     88  A    C  
ATOM   1955  O   GLY A 251     -17.078   7.020  30.175  1.00 53.31      A    O  
ANISOU 1955  O   GLY A 251    11081   2282   6892   -106   2889     70  A    O  
ATOM   1956  N   GLN A 252     -16.232   8.272  28.518  1.00 42.16      A    N  
ANISOU 1956  N   GLN A 252     9207   1101   5712   -145   2688     59  A    N  
ATOM   1957  CA  GLN A 252     -14.824   7.970  28.793  1.00 40.66      A    C  
ANISOU 1957  CA  GLN A 252     9077    987   5386    155   2636    -11  A    C  
ATOM   1958  C   GLN A 252     -14.009   9.249  28.937  1.00 41.54      A    C  
ANISOU 1958  C   GLN A 252     8929   1113   5739    327   2493    -72  A    C  
ATOM   1959  O   GLN A 252     -14.266  10.220  28.217  1.00 41.76      A    O  
ANISOU 1959  O   GLN A 252     8665   1249   5952    187   2446    -38  A    O  
ATOM   1960  CB  GLN A 252     -14.317   7.071  27.626  1.00 41.13      A    C  
ANISOU 1960  CB  GLN A 252     9304    962   5360     92   2674    -25  A    C  
ATOM   1961  CG  GLN A 252     -12.816   6.965  27.309  1.00 42.29      A    C  
ANISOU 1961  CG  GLN A 252     9525   1009   5535    362   2595    -94  A    C  
ATOM   1962  CD  GLN A 252     -12.619   6.656  25.829  1.00 53.68      A    C  
ANISOU 1962  CD  GLN A 252    10939   2471   6986    194   2597    -95  A    C  
ATOM   1963  NE2 GLN A 252     -11.836   7.467  25.096  1.00 37.80      A    N  
ANISOU 1963  NE2 GLN A 252     8634    653   5075    254   2473   -120  A    N  
ATOM   1964  OE1 GLN A 252     -13.221   5.727  25.293  1.00 55.76      A    O  
ANISOU 1964  OE1 GLN A 252    11406   2636   7145    -24   2723    -82  A    O  
ATOM   1965  N   TYR A 253     -13.044   9.266  29.872  1.00 37.89      A    N  
ANISOU 1965  N   TYR A 253     8338   1025   5032    566   2438   -115  A    N  
ATOM   1966  CA  TYR A 253     -12.161  10.427  30.019  1.00 37.72      A    C  
ANISOU 1966  CA  TYR A 253     8040   1105   5188    691   2323   -214  A    C  
ATOM   1967  C   TYR A 253     -10.715   9.950  29.930  1.00 41.19      A    C  
ANISOU 1967  C   TYR A 253     8701   1299   5651   1015   2270   -370  A    C  
ATOM   1968  O   TYR A 253     -10.148   9.544  30.934  1.00 42.37      A    O  
ANISOU 1968  O   TYR A 253     8971   1495   5631   1277   2259   -431  A    O  
ATOM   1969  CB  TYR A 253     -12.423  11.252  31.315  1.00 38.09      A    C  
ANISOU 1969  CB  TYR A 253     7995   1135   5343    781   2313   -291  A    C  
ATOM   1970  CG  TYR A 253     -11.628  12.540  31.323  1.00 39.22      A    C  
ANISOU 1970  CG  TYR A 253     7890   1247   5763    872   2248   -470  A    C  
ATOM   1971  CD1 TYR A 253     -12.072  13.658  30.628  1.00 40.03      A    C  
ANISOU 1971  CD1 TYR A 253     7753   1309   6149    692   2275   -442  A    C  
ATOM   1972  CD2 TYR A 253     -10.388  12.616  31.952  1.00 40.95      A    C  
ANISOU 1972  CD2 TYR A 253     8077   1569   5912   1128   2179   -658  A    C  
ATOM   1973  CE1 TYR A 253     -11.306  14.821  30.560  1.00 42.86      A    C  
ANISOU 1973  CE1 TYR A 253     7837   1751   6698    717   2261   -579  A    C  
ATOM   1974  CE2 TYR A 253      -9.606  13.771  31.878  1.00 41.78      A    C  
ANISOU 1974  CE2 TYR A 253     7873   1808   6195   1128   2142   -827  A    C  
ATOM   1975  CZ  TYR A 253     -10.072  14.875  31.186  1.00 49.38      A    C  
ANISOU 1975  CZ  TYR A 253     8612   2710   7442    911   2198   -790  A    C  
ATOM   1976  OH  TYR A 253      -9.336  16.041  31.151  1.00 50.31      A    O  
ANISOU 1976  OH  TYR A 253     8451   2915   7752    890   2213   -966  A    O  
ATOM   1977  N   ASP A 254     -10.131   9.970  28.729  1.00 37.29      A    N  
ANISOU 1977  N   ASP A 254     7968   1142   5058    872   2221   -293  A    N  
ATOM   1978  CA  ASP A 254      -8.751   9.523  28.549  1.00 37.29      A    C  
ANISOU 1978  CA  ASP A 254     8016   1209   4943   1097   2159   -365  A    C  
ATOM   1979  C   ASP A 254      -7.819  10.719  28.455  1.00 42.73      A    C  
ANISOU 1979  C   ASP A 254     8502   1779   5956   1250   2085   -612  A    C  
ATOM   1980  O   ASP A 254      -8.274  11.828  28.178  1.00 38.60      A    O  
ANISOU 1980  O   ASP A 254     7700   1334   5632   1035   2084   -587  A    O  
ATOM   1981  CB  ASP A 254      -8.633   8.668  27.282  1.00 37.75      A    C  
ANISOU 1981  CB  ASP A 254     8248   1150   4944   1020   2210   -310  A    C  
ATOM   1982  CG  ASP A 254      -9.064   7.214  27.396  1.00 48.41      A    C  
ANISOU 1982  CG  ASP A 254    10165   2002   6227   1133   2359   -310  A    C  
ATOM   1983  OD1 ASP A 254      -9.632   6.834  28.451  1.00 49.32      A    O  
ANISOU 1983  OD1 ASP A 254    10460   2039   6240   1198   2429   -272  A    O  
ATOM   1984  OD2 ASP A 254      -8.828   6.454  26.431  1.00 49.71      A    O1-
ANISOU 1984  OD2 ASP A 254    10488   2076   6324   1077   2417   -287  A    O1-
ATOM   1985  N   LEU A 255      -6.507  10.491  28.665  1.00 44.49      A    N  
ANISOU 1985  N   LEU A 255     8698   2151   6056   1511   2020   -740  A    N  
ATOM   1986  CA  LEU A 255      -5.494  11.548  28.532  1.00 44.84      A    C  
ANISOU 1986  CA  LEU A 255     8404   2398   6237   1541   1947   -922  A    C  
ATOM   1987  C   LEU A 255      -4.432  11.116  27.550  1.00 48.03      A    C  
ANISOU 1987  C   LEU A 255     8806   2858   6584   1628   1912   -952  A    C  
ATOM   1988  O   LEU A 255      -4.086   9.946  27.505  1.00 45.87      A    O  
ANISOU 1988  O   LEU A 255     8794   2544   6089   1816   1924   -893  A    O  
ATOM   1989  CB  LEU A 255      -4.827  11.919  29.871  1.00 46.48      A    C  
ANISOU 1989  CB  LEU A 255     8481   2839   6342   1765   1891  -1115  A    C  
ATOM   1990  CG  LEU A 255      -5.677  12.477  31.003  1.00 51.84      A    C  
ANISOU 1990  CG  LEU A 255     9118   3512   7067   1708   1921  -1138  A    C  
ATOM   1991  CD1 LEU A 255      -4.868  12.550  32.263  1.00 54.88      A    C  
ANISOU 1991  CD1 LEU A 255     9413   4180   7260   1975   1858  -1332  A    C  
ATOM   1992  CD2 LEU A 255      -6.119  13.874  30.718  1.00 53.18      A    C  
ANISOU 1992  CD2 LEU A 255     9007   3644   7556   1440   1967  -1199  A    C  
ATOM   1993  N   LEU A 256      -3.889  12.066  26.792  1.00 46.82      A    N  
ANISOU 1993  N   LEU A 256     8368   2789   6631   1505   1892  -1045  A    N  
ATOM   1994  CA  LEU A 256      -2.815  11.799  25.847  1.00 47.69      A    C  
ANISOU 1994  CA  LEU A 256     8431   2980   6709   1574   1860  -1095  A    C  
ATOM   1995  C   LEU A 256      -1.718  12.851  26.019  1.00 54.14      A    C  
ANISOU 1995  C   LEU A 256     8898   4035   7639   1603   1821  -1335  A    C  
ATOM   1996  O   LEU A 256      -1.994  14.044  25.891  1.00 53.71      A    O  
ANISOU 1996  O   LEU A 256     8615   3954   7837   1391   1874  -1387  A    O  
ATOM   1997  CB  LEU A 256      -3.356  11.776  24.408  1.00 46.57      A    C  
ANISOU 1997  CB  LEU A 256     8324   2673   6697   1329   1910   -935  A    C  
ATOM   1998  CG  LEU A 256      -2.335  11.507  23.312  1.00 51.46      A    C  
ANISOU 1998  CG  LEU A 256     8903   3358   7293   1370   1889   -971  A    C  
ATOM   1999  CD1 LEU A 256      -2.369  10.078  22.879  1.00 52.03      A    C  
ANISOU 1999  CD1 LEU A 256     9308   3315   7144   1463   1914   -865  A    C  
ATOM   2000  CD2 LEU A 256      -2.608  12.363  22.129  1.00 52.59      A    C  
ANISOU 2000  CD2 LEU A 256     8857   3458   7668   1112   1931   -901  A    C  
ATOM   2001  N   ILE A 257      -0.485  12.409  26.324  1.00 53.12      A    N  
ANISOU 2001  N   ILE A 257     8724   4143   7315   1868   1751  -1486  A    N  
ATOM   2002  CA  ILE A 257       0.636  13.336  26.488  1.00 54.33      A    C  
ANISOU 2002  CA  ILE A 257     8525   4575   7542   1881   1720  -1758  A    C  
ATOM   2003  C   ILE A 257       1.418  13.344  25.166  1.00 55.29      A    C  
ANISOU 2003  C   ILE A 257     8560   4708   7738   1823   1727  -1766  A    C  
ATOM   2004  O   ILE A 257       1.971  12.335  24.732  1.00 53.73      A    O  
ANISOU 2004  O   ILE A 257     8515   4552   7347   2020   1688  -1710  A    O  
ATOM   2005  CB  ILE A 257       1.496  13.073  27.761  1.00 60.56      A    C  
ANISOU 2005  CB  ILE A 257     9227   5718   8066   2194   1635  -1960  A    C  
ATOM   2006  CG1 ILE A 257       0.674  13.398  29.050  1.00 61.66      A    C  
ANISOU 2006  CG1 ILE A 257     9382   5858   8186   2185   1645  -1986  A    C  
ATOM   2007  CG2 ILE A 257       2.792  13.915  27.762  1.00 63.06      A    C  
ANISOU 2007  CG2 ILE A 257     9154   6381   8427   2187   1606  -2279  A    C  
ATOM   2008  CD1 ILE A 257      -0.242  12.268  29.571  1.00 70.38      A    C  
ANISOU 2008  CD1 ILE A 257    10873   6776   9093   2343   1654  -1740  A    C  
ATOM   2009  N   LEU A 258       1.387  14.510  24.510  1.00 50.18      A    N  
ANISOU 2009  N   LEU A 258     7688   3996   7383   1548   1805  -1816  A    N  
ATOM   2010  CA  LEU A 258       1.956  14.756  23.192  1.00 48.74      A    C  
ANISOU 2010  CA  LEU A 258     7399   3791   7327   1431   1844  -1805  A    C  
ATOM   2011  C   LEU A 258       3.454  15.075  23.207  1.00 54.01      A    C  
ANISOU 2011  C   LEU A 258     7797   4770   7954   1526   1815  -2088  A    C  
ATOM   2012  O   LEU A 258       4.004  15.313  24.279  1.00 55.52      A    O  
ANISOU 2012  O   LEU A 258     7829   5217   8050   1639   1773  -2320  A    O  
ATOM   2013  CB  LEU A 258       1.208  15.950  22.572  1.00 46.75      A    C  
ANISOU 2013  CB  LEU A 258     7021   3336   7404   1120   1976  -1720  A    C  
ATOM   2014  CG  LEU A 258      -0.152  15.724  21.931  1.00 47.23      A    C  
ANISOU 2014  CG  LEU A 258     7281   3134   7531    982   2018  -1411  A    C  
ATOM   2015  CD1 LEU A 258      -0.134  14.612  20.920  1.00 44.35      A    C  
ANISOU 2015  CD1 LEU A 258     7124   2721   7004   1033   1969  -1251  A    C  
ATOM   2016  CD2 LEU A 258      -1.233  15.615  22.960  1.00 47.29      A    C  
ANISOU 2016  CD2 LEU A 258     7417   3049   7502    987   2012  -1336  A    C  
ATOM   2017  N   PRO A 259       4.115  15.171  22.027  1.00 50.43      A    N  
ANISOU 2017  N   PRO A 259     7257   4331   7572   1461   1845  -2093  A    N  
ATOM   2018  CA  PRO A 259       5.528  15.587  22.008  1.00 52.40      A    C  
ANISOU 2018  CA  PRO A 259     7211   4897   7803   1512   1836  -2387  A    C  
ATOM   2019  C   PRO A 259       5.662  17.043  22.491  1.00 57.19      A    C  
ANISOU 2019  C   PRO A 259     7511   5557   8661   1268   1955  -2631  A    C  
ATOM   2020  O   PRO A 259       4.631  17.727  22.576  1.00 55.67      A    O  
ANISOU 2020  O   PRO A 259     7365   5105   8681   1073   2057  -2515  A    O  
ATOM   2021  CB  PRO A 259       5.916  15.422  20.523  1.00 53.71      A    C  
ANISOU 2021  CB  PRO A 259     7395   4987   8026   1449   1870  -2284  A    C  
ATOM   2022  CG  PRO A 259       4.849  14.521  19.917  1.00 56.01      A    C  
ANISOU 2022  CG  PRO A 259     8034   4985   8263   1448   1857  -1949  A    C  
ATOM   2023  CD  PRO A 259       3.622  14.931  20.652  1.00 50.79      A    C  
ANISOU 2023  CD  PRO A 259     7445   4143   7709   1327   1893  -1849  A    C  
ATOM   2024  N   PRO A 260       6.874  17.563  22.830  1.00 55.84      A    N  
ANISOU 2024  N   PRO A 260     7024   5717   8475   1263   1968  -2978  A    N  
ATOM   2025  CA  PRO A 260       6.959  18.955  23.343  1.00 56.28      A    C  
ANISOU 2025  CA  PRO A 260     6809   5795   8778    992   2126  -3246  A    C  
ATOM   2026  C   PRO A 260       6.475  20.041  22.373  1.00 57.81      A    C  
ANISOU 2026  C   PRO A 260     6982   5633   9350    671   2351  -3130  A    C  
ATOM   2027  O   PRO A 260       6.249  21.171  22.804  1.00 58.43      A    O  
ANISOU 2027  O   PRO A 260     6921   5617   9663    448   2528  -3283  A    O  
ATOM   2028  CB  PRO A 260       8.449  19.141  23.652  1.00 60.77      A    C  
ANISOU 2028  CB  PRO A 260     7041   6825   9224   1037   2100  -3646  A    C  
ATOM   2029  CG  PRO A 260       9.002  17.766  23.768  1.00 66.08      A    C  
ANISOU 2029  CG  PRO A 260     7819   7770   9520   1424   1888  -3579  A    C  
ATOM   2030  CD  PRO A 260       8.203  16.914  22.824  1.00 59.15      A    C  
ANISOU 2030  CD  PRO A 260     7307   6528   8638   1501   1856  -3164  A    C  
ATOM   2031  N   SER A 261       6.268  19.692  21.095  1.00 51.94      A    N  
ANISOU 2031  N   SER A 261     6389   4691   8655    661   2362  -2850  A    N  
ATOM   2032  CA  SER A 261       5.823  20.607  20.044  1.00 50.67      A    C  
ANISOU 2032  CA  SER A 261     6222   4225   8807    417   2571  -2680  A    C  
ATOM   2033  C   SER A 261       4.311  20.951  20.123  1.00 54.77      A    C  
ANISOU 2033  C   SER A 261     6918   4414   9479    331   2651  -2390  A    C  
ATOM   2034  O   SER A 261       3.874  21.840  19.387  1.00 56.15      A    O  
ANISOU 2034  O   SER A 261     7076   4349   9911    159   2849  -2232  A    O  
ATOM   2035  CB  SER A 261       6.172  20.040  18.669  1.00 51.36      A    C  
ANISOU 2035  CB  SER A 261     6391   4284   8841    460   2537  -2489  A    C  
ATOM   2036  OG  SER A 261       5.575  18.780  18.408  1.00 52.60      A    O  
ANISOU 2036  OG  SER A 261     6824   4390   8774    643   2364  -2225  A    O  
ATOM   2037  N   PHE A 262       3.521  20.300  21.021  1.00 48.88      A    N  
ANISOU 2037  N   PHE A 262     6332   3666   8574    461   2517  -2313  A    N  
ATOM   2038  CA  PHE A 262       2.088  20.616  21.176  1.00 46.66      A    C  
ANISOU 2038  CA  PHE A 262     6195   3116   8419    387   2586  -2060  A    C  
ATOM   2039  C   PHE A 262       1.943  22.123  21.528  1.00 50.87      A    C  
ANISOU 2039  C   PHE A 262     6551   3505   9271    175   2841  -2194  A    C  
ATOM   2040  O   PHE A 262       2.623  22.596  22.445  1.00 51.26      A    O  
ANISOU 2040  O   PHE A 262     6425   3712   9337    131   2882  -2541  A    O  
ATOM   2041  CB  PHE A 262       1.414  19.697  22.221  1.00 47.50      A    C  
ANISOU 2041  CB  PHE A 262     6483   3274   8289    555   2414  -2012  A    C  
ATOM   2042  CG  PHE A 262      -0.054  19.943  22.519  1.00 47.36      A    C  
ANISOU 2042  CG  PHE A 262     6601   3026   8368    488   2469  -1778  A    C  
ATOM   2043  CD1 PHE A 262      -0.976  20.088  21.492  1.00 48.75      A    C  
ANISOU 2043  CD1 PHE A 262     6868   2997   8656    396   2542  -1456  A    C  
ATOM   2044  CD2 PHE A 262      -0.522  19.945  23.826  1.00 48.72      A    C  
ANISOU 2044  CD2 PHE A 262     6803   3228   8479    537   2437  -1873  A    C  
ATOM   2045  CE1 PHE A 262      -2.323  20.338  21.768  1.00 48.24      A    C  
ANISOU 2045  CE1 PHE A 262     6893   2768   8666    345   2595  -1245  A    C  
ATOM   2046  CE2 PHE A 262      -1.873  20.164  24.099  1.00 50.54      A    C  
ANISOU 2046  CE2 PHE A 262     7147   3261   8795    478   2492  -1660  A    C  
ATOM   2047  CZ  PHE A 262      -2.763  20.362  23.066  1.00 47.27      A    C  
ANISOU 2047  CZ  PHE A 262     6801   2654   8504    383   2570  -1349  A    C  
ATOM   2048  N   PRO A 263       1.149  22.894  20.733  1.00 46.86      A    N  
ANISOU 2048  N   PRO A 263     6077   2719   9011     46   3037  -1933  A    N  
ATOM   2049  CA  PRO A 263       1.107  24.361  20.916  1.00 47.97      A    C  
ANISOU 2049  CA  PRO A 263     6074   2674   9478   -144   3343  -2046  A    C  
ATOM   2050  C   PRO A 263       0.403  24.873  22.167  1.00 50.86      A    C  
ANISOU 2050  C   PRO A 263     6443   2959   9923   -180   3413  -2145  A    C  
ATOM   2051  O   PRO A 263       0.442  26.076  22.399  1.00 49.45      A    O  
ANISOU 2051  O   PRO A 263     6156   2618  10015   -343   3693  -2283  A    O  
ATOM   2052  CB  PRO A 263       0.352  24.850  19.675  1.00 49.61      A    C  
ANISOU 2052  CB  PRO A 263     6352   2628   9871   -192   3517  -1663  A    C  
ATOM   2053  CG  PRO A 263      -0.480  23.691  19.273  1.00 52.54      A    C  
ANISOU 2053  CG  PRO A 263     6909   3049  10005    -49   3281  -1350  A    C  
ATOM   2054  CD  PRO A 263       0.372  22.491  19.542  1.00 47.24      A    C  
ANISOU 2054  CD  PRO A 263     6274   2636   9038     74   3013  -1538  A    C  
ATOM   2055  N   TYR A 264      -0.259  23.999  22.937  1.00 48.24      A    N  
ANISOU 2055  N   TYR A 264     6247   2715   9367    -37   3195  -2073  A    N  
ATOM   2056  CA  TYR A 264      -0.982  24.413  24.142  1.00 47.86      A    C  
ANISOU 2056  CA  TYR A 264     6211   2604   9370    -59   3248  -2153  A    C  
ATOM   2057  C   TYR A 264      -0.594  23.531  25.322  1.00 50.06      A    C  
ANISOU 2057  C   TYR A 264     6498   3173   9348     83   3010  -2386  A    C  
ATOM   2058  O   TYR A 264       0.252  22.654  25.181  1.00 46.69      A    O  
ANISOU 2058  O   TYR A 264     6065   2986   8689    210   2825  -2478  A    O  
ATOM   2059  CB  TYR A 264      -2.513  24.419  23.905  1.00 47.17      A    C  
ANISOU 2059  CB  TYR A 264     6293   2285   9344    -30   3282  -1755  A    C  
ATOM   2060  CG  TYR A 264      -2.923  25.365  22.799  1.00 48.77      A    C  
ANISOU 2060  CG  TYR A 264     6467   2236   9825   -125   3541  -1506  A    C  
ATOM   2061  CD1 TYR A 264      -3.044  24.919  21.488  1.00 49.61      A    C  
ANISOU 2061  CD1 TYR A 264     6632   2337   9880    -82   3490  -1216  A    C  
ATOM   2062  CD2 TYR A 264      -3.113  26.725  23.048  1.00 50.21      A    C  
ANISOU 2062  CD2 TYR A 264     6565   2195  10318   -249   3863  -1572  A    C  
ATOM   2063  CE1 TYR A 264      -3.344  25.797  20.451  1.00 49.92      A    C  
ANISOU 2063  CE1 TYR A 264     6635   2184  10148   -135   3737   -974  A    C  
ATOM   2064  CE2 TYR A 264      -3.432  27.609  22.020  1.00 50.77      A    C  
ANISOU 2064  CE2 TYR A 264     6625   2027  10639   -295   4138  -1319  A    C  
ATOM   2065  CZ  TYR A 264      -3.540  27.138  20.721  1.00 53.62      A    C  
ANISOU 2065  CZ  TYR A 264     7032   2418  10922   -225   4066  -1010  A    C  
ATOM   2066  OH  TYR A 264      -3.892  27.974  19.699  1.00 52.30      A    O  
ANISOU 2066  OH  TYR A 264     6855   2051  10967   -231   4334   -724  A    O  
ATOM   2067  N   GLY A 265      -1.138  23.847  26.491  1.00 48.63      A    N  
ANISOU 2067  N   GLY A 265     6316   2982   9178     69   3043  -2495  A    N  
ATOM   2068  CA  GLY A 265      -0.887  23.089  27.709  1.00 48.72      A    C  
ANISOU 2068  CA  GLY A 265     6339   3275   8898    223   2841  -2691  A    C  
ATOM   2069  C   GLY A 265      -1.872  21.951  27.864  1.00 48.69      A    C  
ANISOU 2069  C   GLY A 265     6598   3224   8676    400   2657  -2381  A    C  
ATOM   2070  O   GLY A 265      -1.517  20.872  28.344  1.00 46.20      A    O  
ANISOU 2070  O   GLY A 265     6372   3128   8054    602   2454  -2417  A    O  
ATOM   2071  N   GLY A 266      -3.120  22.230  27.472  1.00 44.90      A    N  
ANISOU 2071  N   GLY A 266     6240   2464   8357    326   2754  -2078  A    N  
ATOM   2072  CA  GLY A 266      -4.235  21.292  27.507  1.00 42.85      A    C  
ANISOU 2072  CA  GLY A 266     6217   2127   7937    426   2631  -1778  A    C  
ATOM   2073  C   GLY A 266      -5.257  21.573  26.421  1.00 44.53      A    C  
ANISOU 2073  C   GLY A 266     6494   2104   8320    330   2733  -1429  A    C  
ATOM   2074  O   GLY A 266      -5.426  22.721  26.001  1.00 39.97      A    O  
ANISOU 2074  O   GLY A 266     5786   1385   8016    201   2943  -1388  A    O  
ATOM   2075  N   MET A 267      -5.892  20.496  25.909  1.00 41.86      A    N  
ANISOU 2075  N   MET A 267     6348   1758   7799    394   2600  -1173  A    N  
ATOM   2076  CA  MET A 267      -6.933  20.560  24.883  1.00 40.77      A    C  
ANISOU 2076  CA  MET A 267     6260   1488   7743    316   2660   -841  A    C  
ATOM   2077  C   MET A 267      -8.011  19.523  25.234  1.00 42.84      A    C  
ANISOU 2077  C   MET A 267     6728   1754   7795    353   2545   -670  A    C  
ATOM   2078  O   MET A 267      -7.740  18.328  25.257  1.00 42.81      A    O  
ANISOU 2078  O   MET A 267     6893   1827   7547    433   2402   -680  A    O  
ATOM   2079  CB  MET A 267      -6.353  20.368  23.459  1.00 42.21      A    C  
ANISOU 2079  CB  MET A 267     6415   1695   7929    291   2648   -740  A    C  
ATOM   2080  CG  MET A 267      -7.382  20.511  22.349  1.00 44.26      A    C  
ANISOU 2080  CG  MET A 267     6682   1886   8249    219   2713   -404  A    C  
ATOM   2081  SD  MET A 267      -8.264  22.080  22.337  1.00 48.16      A    S  
ANISOU 2081  SD  MET A 267     7017   2216   9065    154   2976   -243  A    S  
ATOM   2082  CE  MET A 267      -9.893  21.490  21.968  1.00 43.76      A    C  
ANISOU 2082  CE  MET A 267     6548   1709   8368    142   2916     97  A    C  
ATOM   2083  N   GLU A 268      -9.227  20.025  25.524  1.00 38.65      A    N  
ANISOU 2083  N   GLU A 268     6141   1219   7327    276   2636   -501  A    N  
ATOM   2084  CA  GLU A 268     -10.426  19.324  25.987  1.00 36.83      A    C  
ANISOU 2084  CA  GLU A 268     5976   1157   6861    245   2579   -329  A    C  
ATOM   2085  C   GLU A 268     -11.102  18.444  24.917  1.00 39.44      A    C  
ANISOU 2085  C   GLU A 268     6541   1267   7178    220   2521   -131  A    C  
ATOM   2086  O   GLU A 268     -12.328  18.303  24.946  1.00 40.03      A    O  
ANISOU 2086  O   GLU A 268     6649   1344   7217    153   2544     39  A    O  
ATOM   2087  CB  GLU A 268     -11.445  20.375  26.517  1.00 37.57      A    C  
ANISOU 2087  CB  GLU A 268     5979   1132   7164    208   2732   -260  A    C  
ATOM   2088  CG  GLU A 268     -12.052  21.292  25.458  1.00 42.68      A    C  
ANISOU 2088  CG  GLU A 268     6594   1486   8136    179   2889    -46  A    C  
ATOM   2089  CD  GLU A 268     -11.435  22.669  25.291  1.00 58.15      A    C  
ANISOU 2089  CD  GLU A 268     8380   3328  10384    172   3088   -128  A    C  
ATOM   2090  OE1 GLU A 268     -10.205  22.801  25.476  1.00 49.85      A    O  
ANISOU 2090  OE1 GLU A 268     7295   2288   9360    177   3074   -382  A    O  
ATOM   2091  OE2 GLU A 268     -12.190  23.623  24.996  1.00 45.75      A    O1-
ANISOU 2091  OE2 GLU A 268     6710   1661   9013    166   3278     61  A    O1-
ATOM   2092  N   ASN A 269     -10.347  17.824  24.005  1.00 36.06      A    N  
ANISOU 2092  N   ASN A 269     6029   1154   6519    200   2447   -117  A    N  
ATOM   2093  CA  ASN A 269     -10.986  16.979  23.001  1.00 36.04      A    C  
ANISOU 2093  CA  ASN A 269     6147   1153   6392    126   2403     50  A    C  
ATOM   2094  C   ASN A 269     -11.880  15.936  23.703  1.00 39.60      A    C  
ANISOU 2094  C   ASN A 269     6916   1388   6742    102   2356     73  A    C  
ATOM   2095  O   ASN A 269     -11.416  15.293  24.648  1.00 39.80      A    O  
ANISOU 2095  O   ASN A 269     7108   1372   6641    208   2303    -77  A    O  
ATOM   2096  CB  ASN A 269      -9.969  16.319  22.049  1.00 37.91      A    C  
ANISOU 2096  CB  ASN A 269     6534   1250   6619    153   2334      0  A    C  
ATOM   2097  CG  ASN A 269      -8.972  17.292  21.475  1.00 45.77      A    C  
ANISOU 2097  CG  ASN A 269     7345   2233   7813    190   2388    -66  A    C  
ATOM   2098  ND2 ASN A 269      -9.414  18.170  20.590  1.00 29.72      A    N  
ANISOU 2098  ND2 ASN A 269     4757    977   5559     99   2493     99  A    N  
ATOM   2099  OD1 ASN A 269      -7.796  17.262  21.829  1.00 40.78      A    O  
ANISOU 2099  OD1 ASN A 269     6712   1613   7169    287   2348   -273  A    O  
ATOM   2100  N   PRO A 270     -13.188  15.845  23.338  1.00 35.53      A    N  
ANISOU 2100  N   PRO A 270     6285   1117   6097    -25   2392    240  A    N  
ATOM   2101  CA  PRO A 270     -14.101  14.909  24.041  1.00 34.72      A    C  
ANISOU 2101  CA  PRO A 270     6342   1072   5777    -82   2380    236  A    C  
ATOM   2102  C   PRO A 270     -13.575  13.486  24.059  1.00 37.54      A    C  
ANISOU 2102  C   PRO A 270     7109   1134   6022    -82   2328    161  A    C  
ATOM   2103  O   PRO A 270     -13.046  13.055  23.048  1.00 37.96      A    O  
ANISOU 2103  O   PRO A 270     7200   1198   6026   -115   2301    164  A    O  
ATOM   2104  CB  PRO A 270     -15.397  15.001  23.234  1.00 35.69      A    C  
ANISOU 2104  CB  PRO A 270     6436   1158   5966   -263   2422    446  A    C  
ATOM   2105  CG  PRO A 270     -15.343  16.309  22.564  1.00 40.57      A    C  
ANISOU 2105  CG  PRO A 270     6821   1749   6843   -237   2481    593  A    C  
ATOM   2106  CD  PRO A 270     -13.892  16.578  22.268  1.00 35.91      A    C  
ANISOU 2106  CD  PRO A 270     6183   1150   6312   -117   2456    458  A    C  
ATOM   2107  N   CYS A 271     -13.651  12.782  25.202  1.00 35.53      A    N  
ANISOU 2107  N   CYS A 271     6926   1089   5486     -5   2332     69  A    N  
ATOM   2108  CA  CYS A 271     -13.156  11.388  25.380  1.00 37.67      A    C  
ANISOU 2108  CA  CYS A 271     7592   1120   5599     54   2328      3  A    C  
ATOM   2109  C   CYS A 271     -11.608  11.266  25.368  1.00 42.31      A    C  
ANISOU 2109  C   CYS A 271     8304   1520   6253    283   2262   -127  A    C  
ATOM   2110  O   CYS A 271     -11.116  10.203  25.717  1.00 44.20      A    O  
ANISOU 2110  O   CYS A 271     8810   1680   6303    415   2273   -183  A    O  
ATOM   2111  CB  CYS A 271     -13.767  10.407  24.375  1.00 38.46      A    C  
ANISOU 2111  CB  CYS A 271     7871   1145   5596   -155   2378     64  A    C  
ATOM   2112  SG  CYS A 271     -15.552  10.577  24.146  1.00 42.50      A    S  
ANISOU 2112  SG  CYS A 271     8324   1659   6166   -455   2448    203  A    S  
ATOM   2113  N   LEU A 272     -10.851  12.308  24.973  1.00 38.46      A    N  
ANISOU 2113  N   LEU A 272     7545   1133   5934    332   2216   -171  A    N  
ATOM   2114  CA  LEU A 272      -9.391  12.232  24.935  1.00 37.62      A    C  
ANISOU 2114  CA  LEU A 272     7386   1149   5759    510   2153   -298  A    C  
ATOM   2115  C   LEU A 272      -8.756  13.634  25.102  1.00 38.61      A    C  
ANISOU 2115  C   LEU A 272     7249   1263   6159    569   2144   -416  A    C  
ATOM   2116  O   LEU A 272      -8.553  14.354  24.124  1.00 37.84      A    O  
ANISOU 2116  O   LEU A 272     6960   1196   6221    475   2166   -375  A    O  
ATOM   2117  CB  LEU A 272      -8.964  11.562  23.620  1.00 37.52      A    C  
ANISOU 2117  CB  LEU A 272     7456   1120   5678    459   2146   -265  A    C  
ATOM   2118  CG  LEU A 272      -7.491  11.227  23.370  1.00 40.38      A    C  
ANISOU 2118  CG  LEU A 272     7878   1458   6008    668   2094   -405  A    C  
ATOM   2119  CD1 LEU A 272      -7.000  10.110  24.256  1.00 39.27      A    C  
ANISOU 2119  CD1 LEU A 272     8016   1272   5634    907   2090   -475  A    C  
ATOM   2120  CD2 LEU A 272      -7.315  10.815  21.945  1.00 40.69      A    C  
ANISOU 2120  CD2 LEU A 272     7942   1502   6016    555   2104   -347  A    C  
ATOM   2121  N   THR A 273      -8.454  14.014  26.348  1.00 35.64      A    N  
ANISOU 2121  N   THR A 273     6698   1185   5658    629   2118   -483  A    N  
ATOM   2122  CA  THR A 273      -7.799  15.281  26.625  1.00 36.04      A    C  
ANISOU 2122  CA  THR A 273     6488   1280   5925    643   2136   -633  A    C  
ATOM   2123  C   THR A 273      -6.315  15.200  26.152  1.00 38.93      A    C  
ANISOU 2123  C   THR A 273     6887   1537   6369    830   2095   -870  A    C  
ATOM   2124  O   THR A 273      -5.626  14.241  26.470  1.00 37.63      A    O  
ANISOU 2124  O   THR A 273     6847   1496   5955    997   2013   -919  A    O  
ATOM   2125  CB  THR A 273      -7.964  15.677  28.111  1.00 38.13      A    C  
ANISOU 2125  CB  THR A 273     6806   1414   6266    773   2156   -819  A    C  
ATOM   2126  CG2 THR A 273      -6.924  16.717  28.563  1.00 34.82      A    C  
ANISOU 2126  CG2 THR A 273     6000   1379   5853    701   2136   -946  A    C  
ATOM   2127  OG1 THR A 273      -9.281  16.233  28.309  1.00 37.24      A    O  
ANISOU 2127  OG1 THR A 273     6590   1341   6220    586   2235   -638  A    O  
ATOM   2128  N   PHE A 274      -5.846  16.200  25.383  1.00 37.55      A    N  
ANISOU 2128  N   PHE A 274     6435   1459   6371    696   2144   -875  A    N  
ATOM   2129  CA  PHE A 274      -4.451  16.270  24.930  1.00 38.06      A    C  
ANISOU 2129  CA  PHE A 274     6403   1604   6452    786   2113  -1059  A    C  
ATOM   2130  C   PHE A 274      -3.680  17.150  25.938  1.00 46.46      A    C  
ANISOU 2130  C   PHE A 274     7270   2770   7613    848   2142  -1364  A    C  
ATOM   2131  O   PHE A 274      -4.157  18.240  26.254  1.00 45.52      A    O  
ANISOU 2131  O   PHE A 274     7009   2572   7714    715   2258  -1397  A    O  
ATOM   2132  CB  PHE A 274      -4.397  16.847  23.500  1.00 38.55      A    C  
ANISOU 2132  CB  PHE A 274     6362   1565   6719    648   2194   -959  A    C  
ATOM   2133  CG  PHE A 274      -4.809  15.951  22.353  1.00 38.79      A    C  
ANISOU 2133  CG  PHE A 274     6557   1548   6635    603   2158   -746  A    C  
ATOM   2134  CD1 PHE A 274      -5.435  14.731  22.584  1.00 42.04      A    C  
ANISOU 2134  CD1 PHE A 274     7233   1916   6824    645   2098   -648  A    C  
ATOM   2135  CD2 PHE A 274      -4.584  16.333  21.038  1.00 40.77      A    C  
ANISOU 2135  CD2 PHE A 274     6699   1798   6996    504   2206   -655  A    C  
ATOM   2136  CE1 PHE A 274      -5.810  13.906  21.522  1.00 42.40      A    C  
ANISOU 2136  CE1 PHE A 274     7423   1926   6760    563   2090   -496  A    C  
ATOM   2137  CE2 PHE A 274      -4.978  15.516  19.974  1.00 43.01      A    C  
ANISOU 2137  CE2 PHE A 274     7115   2073   7155    444   2176   -484  A    C  
ATOM   2138  CZ  PHE A 274      -5.575  14.300  20.224  1.00 41.31      A    C  
ANISOU 2138  CZ  PHE A 274     7154   1823   6719    462   2118   -423  A    C  
ATOM   2139  N   VAL A 275      -2.560  16.654  26.513  1.00 46.39      A    N  
ANISOU 2139  N   VAL A 275     7239   2983   7405   1042   2044  -1574  A    N  
ATOM   2140  CA  VAL A 275      -1.774  17.390  27.530  1.00 48.67      A    C  
ANISOU 2140  CA  VAL A 275     7296   3489   7708   1082   2052  -1892  A    C  
ATOM   2141  C   VAL A 275      -0.300  17.542  27.093  1.00 53.09      A    C  
ANISOU 2141  C   VAL A 275     7651   4276   8244   1129   2025  -2118  A    C  
ATOM   2142  O   VAL A 275       0.262  16.631  26.496  1.00 50.14      A    O  
ANISOU 2142  O   VAL A 275     7380   3970   7701   1275   1937  -2051  A    O  
ATOM   2143  CB  VAL A 275      -1.852  16.744  28.939  1.00 54.45      A    C  
ANISOU 2143  CB  VAL A 275     8132   4384   8172   1298   1957  -1972  A    C  
ATOM   2144  CG1 VAL A 275      -1.414  17.730  30.020  1.00 55.93      A    C  
ANISOU 2144  CG1 VAL A 275     8059   4772   8420   1256   2000  -2289  A    C  
ATOM   2145  CG2 VAL A 275      -3.254  16.223  29.243  1.00 53.72      A    C  
ANISOU 2145  CG2 VAL A 275     8310   4069   8031   1289   1967  -1710  A    C  
ATOM   2146  N   THR A 276       0.310  18.701  27.411  1.00 52.58      A    N  
ANISOU 2146  N   THR A 276     7298   4329   8353    993   2123  -2403  A    N  
ATOM   2147  CA  THR A 276       1.715  19.035  27.112  1.00 54.07      A    C  
ANISOU 2147  CA  THR A 276     7235   4768   8540    988   2127  -2680  A    C  
ATOM   2148  C   THR A 276       2.673  18.272  28.050  1.00 60.48      A    C  
ANISOU 2148  C   THR A 276     7981   5996   9001   1269   1962  -2899  A    C  
ATOM   2149  O   THR A 276       2.326  18.079  29.215  1.00 61.15      A    O  
ANISOU 2149  O   THR A 276     8107   6194   8935   1383   1909  -2954  A    O  
ATOM   2150  CB  THR A 276       1.946  20.580  27.228  1.00 59.00      A    C  
ANISOU 2150  CB  THR A 276     7583   5355   9481    705   2337  -2936  A    C  
ATOM   2151  CG2 THR A 276       1.765  21.117  28.644  1.00 53.26      A    C  
ANISOU 2151  CG2 THR A 276     6736   4766   8735    672   2372  -3195  A    C  
ATOM   2152  OG1 THR A 276       3.252  20.928  26.761  1.00 64.05      A    O  
ANISOU 2152  OG1 THR A 276     7985   6202  10150    646   2373  -3190  A    O  
ATOM   2153  N   PRO A 277       3.902  17.895  27.628  1.00 58.79      A    N  
ANISOU 2153  N   PRO A 277     7643   6053   8643   1398   1888  -3036  A    N  
ATOM   2154  CA  PRO A 277       4.819  17.277  28.595  1.00 60.86      A    C  
ANISOU 2154  CA  PRO A 277     7798   6773   8552   1698   1743  -3247  A    C  
ATOM   2155  C   PRO A 277       5.492  18.340  29.495  1.00 67.57      A    C  
ANISOU 2155  C   PRO A 277     8266   7971   9437   1563   1796  -3687  A    C  
ATOM   2156  O   PRO A 277       6.187  17.978  30.445  1.00 68.48      A    O  
ANISOU 2156  O   PRO A 277     8237   8538   9245   1799   1678  -3895  A    O  
ATOM   2157  CB  PRO A 277       5.824  16.533  27.708  1.00 62.73      A    C  
ANISOU 2157  CB  PRO A 277     8036   7159   8641   1878   1666  -3213  A    C  
ATOM   2158  CG  PRO A 277       5.829  17.273  26.430  1.00 65.63      A    C  
ANISOU 2158  CG  PRO A 277     8329   7272   9335   1574   1799  -3179  A    C  
ATOM   2159  CD  PRO A 277       4.529  18.012  26.290  1.00 59.86      A    C  
ANISOU 2159  CD  PRO A 277     7713   6127   8905   1302   1935  -3005  A    C  
ATOM   2160  N   THR A 278       5.256  19.654  29.215  1.00 65.70      A    N  
ANISOU 2160  N   THR A 278     7868   7530   9565   1188   1994  -3831  A    N  
ATOM   2161  CA  THR A 278       5.826  20.780  29.975  1.00 69.37      A    C  
ANISOU 2161  CA  THR A 278     7981   8260  10116    977   2108  -4284  A    C  
ATOM   2162  C   THR A 278       5.183  20.920  31.381  1.00 76.60      A    C  
ANISOU 2162  C   THR A 278     8905   9278  10923   1018   2086  -4385  A    C  
ATOM   2163  O   THR A 278       5.730  21.639  32.225  1.00 79.28      A    O  
ANISOU 2163  O   THR A 278     8945   9942  11234    895   2144  -4800  A    O  
ATOM   2164  CB  THR A 278       5.753  22.118  29.193  1.00 81.13      A    C  
ANISOU 2164  CB  THR A 278     9347   9432  12046    570   2385  -4383  A    C  
ATOM   2165  CG2 THR A 278       6.319  22.018  27.784  1.00 79.90      A    C  
ANISOU 2165  CG2 THR A 278     9200   9155  12005    524   2422  -4253  A    C  
ATOM   2166  OG1 THR A 278       4.425  22.644  29.172  1.00 79.98      A    O  
ANISOU 2166  OG1 THR A 278     9395   8829  12164    415   2531  -4152  A    O  
ATOM   2167  N   VAL A 279       4.042  20.245  31.638  1.00 72.17      A    N  
ANISOU 2167  N   VAL A 279     8669   8458  10292   1170   2016  -4033  A    N  
ATOM   2168  CA  VAL A 279       3.394  20.289  32.958  1.00 73.00      A    C  
ANISOU 2168  CA  VAL A 279     8810   8651  10277   1232   1992  -4094  A    C  
ATOM   2169  C   VAL A 279       3.971  19.187  33.874  1.00 80.43      A    C  
ANISOU 2169  C   VAL A 279     9754  10066  10740   1639   1773  -4137  A    C  
ATOM   2170  O   VAL A 279       3.690  19.206  35.076  1.00 81.91      A    O  
ANISOU 2170  O   VAL A 279     9906  10458  10757   1726   1738  -4253  A    O  
ATOM   2171  CB  VAL A 279       1.840  20.234  32.923  1.00 73.93      A    C  
ANISOU 2171  CB  VAL A 279     9245   8283  10562   1169   2055  -3730  A    C  
ATOM   2172  CG1 VAL A 279       1.253  21.522  32.367  1.00 72.73      A    C  
ANISOU 2172  CG1 VAL A 279     9033   7748  10853    802   2301  -3737  A    C  
ATOM   2173  CG2 VAL A 279       1.318  19.010  32.168  1.00 71.54      A    C  
ANISOU 2173  CG2 VAL A 279     9286   7750  10145   1369   1945  -3298  A    C  
ATOM   2174  N   LEU A 280       4.786  18.248  33.315  1.00 77.82      A    N  
ANISOU 2174  N   LEU A 280     9464   9919  10185   1906   1642  -4037  A    N  
ATOM   2175  CA  LEU A 280       5.405  17.155  34.071  1.00 79.97      A    C  
ANISOU 2175  CA  LEU A 280     9755  10639   9992   2354   1461  -4032  A    C  
ATOM   2176  C   LEU A 280       6.582  17.712  34.900  1.00 90.04      A    C  
ANISOU 2176  C   LEU A 280    10574  12571  11068   2377   1416  -4517  A    C  
ATOM   2177  O   LEU A 280       7.751  17.609  34.507  1.00 91.91      A    O  
ANISOU 2177  O   LEU A 280    10574  13167  11181   2466   1360  -4698  A    O  
ATOM   2178  CB  LEU A 280       5.846  15.988  33.149  1.00 79.07      A    C  
ANISOU 2178  CB  LEU A 280     9850  10469   9724   2634   1375  -3758  A    C  
ATOM   2179  CG  LEU A 280       4.793  15.380  32.189  1.00 80.11      A    C  
ANISOU 2179  CG  LEU A 280    10406  10005  10028   2583   1426  -3321  A    C  
ATOM   2180  CD1 LEU A 280       5.450  14.523  31.128  1.00 79.66      A    C  
ANISOU 2180  CD1 LEU A 280    10460   9923   9883   2756   1382  -3168  A    C  
ATOM   2181  CD2 LEU A 280       3.763  14.553  32.928  1.00 81.91      A    C  
ANISOU 2181  CD2 LEU A 280    10988  10053  10083   2786   1402  -3041  A    C  
ATOM   2182  N   ALA A 281       6.238  18.337  36.045  1.00 89.38      A    N  
ANISOU 2182  N   ALA A 281    10350  12656  10955   2273   1450  -4746  A    N  
ATOM   2183  CA  ALA A 281       7.163  18.975  36.990  1.00 92.92      A    C  
ANISOU 2183  CA  ALA A 281    10350  13743  11212   2232   1428  -5252  A    C  
ATOM   2184  C   ALA A 281       7.513  18.038  38.168  1.00 99.02      A    C  
ANISOU 2184  C   ALA A 281    11095  15086  11444   2724   1235  -5244  A    C  
ATOM   2185  O   ALA A 281       8.312  18.410  39.032  1.00102.11      A    O  
ANISOU 2185  O   ALA A 281    11091  16128  11578   2765   1180  -5654  A    O  
ATOM   2186  CB  ALA A 281       6.554  20.278  37.505  1.00 93.81      A    C  
ANISOU 2186  CB  ALA A 281    10332  13689  11624   1805   1613  -5524  A    C  
ATOM   2187  N   GLY A 282       6.919  16.839  38.172  1.00 93.72      A    N  
ANISOU 2187  N   GLY A 282    10838  14176  10595   3087   1155  -4784  A    N  
ATOM   2188  CA  GLY A 282       7.138  15.800  39.174  1.00 95.64      A    C  
ANISOU 2188  CA  GLY A 282    11157  14853  10330   3614   1009  -4662  A    C  
ATOM   2189  C   GLY A 282       6.556  16.041  40.555  1.00100.70      A    C  
ANISOU 2189  C   GLY A 282    11763  15696  10802   3651   1003  -4767  A    C  
ATOM   2190  O   GLY A 282       6.883  15.301  41.486  1.00103.34      A    O  
ANISOU 2190  O   GLY A 282    12086  16503  10675   4099    888  -4722  A    O  
ATOM   2191  N   ASP A 283       5.677  17.049  40.703  1.00 95.04      A    N  
ANISOU 2191  N   ASP A 283    11042  14627  10443   3211   1138  -4888  A    N  
ATOM   2192  CA  ASP A 283       5.073  17.404  41.989  1.00 95.55      A    C  
ANISOU 2192  CA  ASP A 283    11063  14853  10388   3191   1155  -5020  A    C  
ATOM   2193  C   ASP A 283       3.563  17.701  41.877  1.00 95.09      A    C  
ANISOU 2193  C   ASP A 283    11341  14092  10695   2919   1295  -4766  A    C  
ATOM   2194  O   ASP A 283       2.932  18.022  42.890  1.00 95.21      A    O  
ANISOU 2194  O   ASP A 283    11352  14164  10660   2869   1331  -4854  A    O  
ATOM   2195  CB  ASP A 283       5.813  18.617  42.596  1.00100.48      A    C  
ANISOU 2195  CB  ASP A 283    11160  16006  11011   2898   1195  -5630  A    C  
ATOM   2196  CG  ASP A 283       5.871  19.885  41.743  1.00109.25      A    C  
ANISOU 2196  CG  ASP A 283    12093  16785  12633   2331   1389  -5905  A    C  
ATOM   2197  OD1 ASP A 283       5.359  19.865  40.600  1.00105.58      A    O  
ANISOU 2197  OD1 ASP A 283    11887  15706  12523   2180   1475  -5608  A    O  
ATOM   2198  OD2 ASP A 283       6.427  20.900  42.224  1.00119.67      A    O1-
ANISOU 2198  OD2 ASP A 283    13014  18467  13987   2038   1475  -6422  A    O1-
ATOM   2199  N   ARG A 284       2.997  17.602  40.651  1.00 87.41      A    N  
ANISOU 2199  N   ARG A 284    10639  12501  10072   2749   1374  -4462  A    N  
ATOM   2200  CA  ARG A 284       1.584  17.834  40.320  1.00 83.54      A    C  
ANISOU 2200  CA  ARG A 284    10454  11358   9931   2502   1505  -4185  A    C  
ATOM   2201  C   ARG A 284       1.158  19.311  40.641  1.00 86.72      A    C  
ANISOU 2201  C   ARG A 284    10631  11645  10674   2059   1677  -4504  A    C  
ATOM   2202  O   ARG A 284      -0.033  19.592  40.824  1.00 84.50      A    O  
ANISOU 2202  O   ARG A 284    10541  10971  10594   1909   1780  -4341  A    O  
ATOM   2203  CB  ARG A 284       0.656  16.790  41.009  1.00 82.70      A    C  
ANISOU 2203  CB  ARG A 284    10725  11111   9585   2800   1457  -3823  A    C  
ATOM   2204  CG  ARG A 284       1.083  15.327  40.793  1.00 91.32      A    C  
ANISOU 2204  CG  ARG A 284    12081  12274  10345   3247   1346  -3510  A    C  
ATOM   2205  CD  ARG A 284       0.019  14.321  41.206  1.00 96.39      A    C  
ANISOU 2205  CD  ARG A 284    13163  12618  10842   3460   1370  -3116  A    C  
ATOM   2206  NE  ARG A 284       0.100  13.952  42.622  1.00105.34      A    N  
ANISOU 2206  NE  ARG A 284    14278  14178  11570   3794   1311  -3168  A    N  
ATOM   2207  CZ  ARG A 284       0.071  12.701  43.079  1.00120.28      A    C  
ANISOU 2207  CZ  ARG A 284    16468  16140  13095   4243   1283  -2881  A    C  
ATOM   2208  NH1 ARG A 284      -0.020  11.679  42.235  1.00104.44      A    N1+
ANISOU 2208  NH1 ARG A 284    14811  13786  11086   4393   1319  -2543  A    N1+
ATOM   2209  NH2 ARG A 284       0.136  12.464  44.383  1.00109.66      A    N  
ANISOU 2209  NH2 ARG A 284    15082  15210  11376   4549   1240  -2929  A    N  
ATOM   2210  N   SER A 285       2.135  20.255  40.656  1.00 84.69      A    N  
ANISOU 2210  N   SER A 285     9973  11715  10492   1840   1732  -4962  A    N  
ATOM   2211  CA  SER A 285       1.903  21.694  40.924  1.00 84.81      A    C  
ANISOU 2211  CA  SER A 285     9766  11622  10837   1404   1947  -5316  A    C  
ATOM   2212  C   SER A 285       1.251  22.396  39.719  1.00 85.40      A    C  
ANISOU 2212  C   SER A 285     9982  11042  11425   1074   2150  -5129  A    C  
ATOM   2213  O   SER A 285       0.630  23.451  39.877  1.00 84.61      A    O  
ANISOU 2213  O   SER A 285     9845  10659  11642    764   2366  -5251  A    O  
ATOM   2214  CB  SER A 285       3.209  22.399  41.292  1.00 91.43      A    C  
ANISOU 2214  CB  SER A 285    10136  13033  11570   1262   1968  -5887  A    C  
ATOM   2215  OG  SER A 285       4.151  22.391  40.230  1.00 97.30      A    O  
ANISOU 2215  OG  SER A 285    10751  13823  12396   1213   1961  -5940  A    O  
ATOM   2216  N   LEU A 286       1.397  21.794  38.517  1.00 80.02      A    N  
ANISOU 2216  N   LEU A 286     9463  10136  10807   1164   2090  -4823  A    N  
ATOM   2217  CA  LEU A 286       0.863  22.285  37.244  1.00 76.74      A    C  
ANISOU 2217  CA  LEU A 286     9181   9164  10812    920   2252  -4592  A    C  
ATOM   2218  C   LEU A 286      -0.230  21.336  36.702  1.00 76.95      A    C  
ANISOU 2218  C   LEU A 286     9610   8797  10833   1089   2174  -4055  A    C  
ATOM   2219  O   LEU A 286      -0.606  21.436  35.536  1.00 74.64      A    O  
ANISOU 2219  O   LEU A 286     9442   8124  10793    968   2250  -3805  A    O  
ATOM   2220  CB  LEU A 286       2.015  22.458  36.221  1.00 77.11      A    C  
ANISOU 2220  CB  LEU A 286     9041   9317  10942    835   2269  -4733  A    C  
ATOM   2221  CG  LEU A 286       3.220  23.342  36.647  1.00 84.61      A    C  
ANISOU 2221  CG  LEU A 286     9565  10699  11883    637   2356  -5302  A    C  
ATOM   2222  CD1 LEU A 286       4.297  23.365  35.570  1.00 84.81      A    C  
ANISOU 2222  CD1 LEU A 286     9439  10818  11968    581   2362  -5388  A    C  
ATOM   2223  CD2 LEU A 286       2.789  24.781  37.008  1.00 86.93      A    C  
ANISOU 2223  CD2 LEU A 286     9734  10762  12535    237   2655  -5579  A    C  
ATOM   2224  N   ALA A 287      -0.768  20.454  37.573  1.00 73.76      A    N  
ANISOU 2224  N   ALA A 287     9398   8493  10136   1350   2044  -3893  A    N  
ATOM   2225  CA  ALA A 287      -1.803  19.456  37.262  1.00 71.75      A    C  
ANISOU 2225  CA  ALA A 287     9525   7915   9822   1503   1984  -3434  A    C  
ATOM   2226  C   ALA A 287      -3.257  20.013  37.309  1.00 73.25      A    C  
ANISOU 2226  C   ALA A 287     9859   7678  10293   1289   2133  -3246  A    C  
ATOM   2227  O   ALA A 287      -4.198  19.253  37.051  1.00 72.79      A    O  
ANISOU 2227  O   ALA A 287    10092   7361  10201   1365   2104  -2891  A    O  
ATOM   2228  CB  ALA A 287      -1.683  18.272  38.207  1.00 73.87      A    C  
ANISOU 2228  CB  ALA A 287     9943   8475   9649   1880   1822  -3354  A    C  
ATOM   2229  N   SER A 288      -3.440  21.330  37.572  1.00 67.85      A    N  
ANISOU 2229  N   SER A 288     8972   6914   9892   1014   2314  -3483  A    N  
ATOM   2230  CA  SER A 288      -4.767  21.966  37.561  1.00 65.37      A    C  
ANISOU 2230  CA  SER A 288     8763   6209   9866    826   2483  -3311  A    C  
ATOM   2231  C   SER A 288      -5.301  22.029  36.117  1.00 62.89      A    C  
ANISOU 2231  C   SER A 288     8574   5505   9816    713   2558  -2977  A    C  
ATOM   2232  O   SER A 288      -6.502  22.227  35.897  1.00 61.16      A    O  
ANISOU 2232  O   SER A 288     8489   4981   9769    631   2653  -2719  A    O  
ATOM   2233  CB  SER A 288      -4.720  23.353  38.201  1.00 70.97      A    C  
ANISOU 2233  CB  SER A 288     9230   6928  10805    582   2694  -3668  A    C  
ATOM   2234  OG  SER A 288      -3.817  24.217  37.531  1.00 82.89      A    O  
ANISOU 2234  OG  SER A 288    10520   8441  12534    386   2826  -3907  A    O  
ATOM   2235  N   VAL A 289      -4.391  21.807  35.145  1.00 56.66      A    N  
ANISOU 2235  N   VAL A 289     7727   4773   9028    727   2505  -2983  A    N  
ATOM   2236  CA  VAL A 289      -4.628  21.722  33.701  1.00 53.70      A    C  
ANISOU 2236  CA  VAL A 289     7445   4122   8835    653   2544  -2695  A    C  
ATOM   2237  C   VAL A 289      -5.638  20.589  33.435  1.00 53.02      A    C  
ANISOU 2237  C   VAL A 289     7661   3884   8601    781   2432  -2304  A    C  
ATOM   2238  O   VAL A 289      -6.471  20.732  32.551  1.00 50.64      A    O  
ANISOU 2238  O   VAL A 289     7444   3315   8481    671   2510  -2033  A    O  
ATOM   2239  CB  VAL A 289      -3.284  21.547  32.915  1.00 57.59      A    C  
ANISOU 2239  CB  VAL A 289     7809   4790   9284    680   2483  -2830  A    C  
ATOM   2240  CG1 VAL A 289      -2.604  20.200  33.174  1.00 57.57      A    C  
ANISOU 2240  CG1 VAL A 289     7904   5082   8889    969   2250  -2824  A    C  
ATOM   2241  CG2 VAL A 289      -3.440  21.802  31.416  1.00 55.70      A    C  
ANISOU 2241  CG2 VAL A 289     7607   4274   9283    554   2574  -2590  A    C  
ATOM   2242  N   ILE A 290      -5.607  19.508  34.246  1.00 49.43      A    N  
ANISOU 2242  N   ILE A 290     7361   3608   7810   1006   2275  -2284  A    N  
ATOM   2243  CA  ILE A 290      -6.536  18.383  34.134  1.00 48.17      A    C  
ANISOU 2243  CA  ILE A 290     7508   3301   7493   1107   2205  -1959  A    C  
ATOM   2244  C   ILE A 290      -7.922  18.816  34.609  1.00 52.10      A    C  
ANISOU 2244  C   ILE A 290     8070   3600   8125    984   2311  -1826  A    C  
ATOM   2245  O   ILE A 290      -8.878  18.638  33.855  1.00 51.37      A    O  
ANISOU 2245  O   ILE A 290     8100   3283   8134    885   2353  -1552  A    O  
ATOM   2246  CB  ILE A 290      -6.018  17.120  34.877  1.00 52.79      A    C  
ANISOU 2246  CB  ILE A 290     8262   4113   7683   1408   2057  -1971  A    C  
ATOM   2247  CG1 ILE A 290      -4.580  16.730  34.413  1.00 54.06      A    C  
ANISOU 2247  CG1 ILE A 290     8330   4513   7699   1565   1957  -2108  A    C  
ATOM   2248  CG2 ILE A 290      -6.992  15.924  34.750  1.00 53.05      A    C  
ANISOU 2248  CG2 ILE A 290     8646   3945   7567   1481   2038  -1649  A    C  
ATOM   2249  CD1 ILE A 290      -4.339  16.562  32.845  1.00 52.58      A    C  
ANISOU 2249  CD1 ILE A 290     8173   4155   7650   1467   1965  -1959  A    C  
ATOM   2250  N   ALA A 291      -8.027  19.400  35.830  1.00 48.76      A    N  
ANISOU 2250  N   ALA A 291     7545   3288   7695    986   2357  -2032  A    N  
ATOM   2251  CA  ALA A 291      -9.289  19.892  36.388  1.00 48.58      A    C  
ANISOU 2251  CA  ALA A 291     7562   3098   7800    881   2470  -1938  A    C  
ATOM   2252  C   ALA A 291      -9.926  20.913  35.461  1.00 49.89      A    C  
ANISOU 2252  C   ALA A 291     7628   2999   8330    665   2640  -1811  A    C  
ATOM   2253  O   ALA A 291     -11.151  21.014  35.420  1.00 50.37      A    O  
ANISOU 2253  O   ALA A 291     7771   2885   8483    598   2714  -1592  A    O  
ATOM   2254  CB  ALA A 291      -9.058  20.517  37.759  1.00 51.34      A    C  
ANISOU 2254  CB  ALA A 291     7769   3638   8100    900   2509  -2245  A    C  
ATOM   2255  N   HIS A 292      -9.094  21.671  34.728  1.00 43.03      A    N  
ANISOU 2255  N   HIS A 292     6576   2117   7655    570   2716  -1942  A    N  
ATOM   2256  CA  HIS A 292      -9.555  22.686  33.783  1.00 41.09      A    C  
ANISOU 2256  CA  HIS A 292     6216   1664   7732    385   2901  -1782  A    C  
ATOM   2257  C   HIS A 292     -10.170  21.980  32.564  1.00 43.48      A    C  
ANISOU 2257  C   HIS A 292     6681   1812   8027    411   2843  -1439  A    C  
ATOM   2258  O   HIS A 292     -11.319  22.257  32.211  1.00 40.70      A    O  
ANISOU 2258  O   HIS A 292     6346   1329   7790    340   2935  -1178  A    O  
ATOM   2259  CB  HIS A 292      -8.405  23.649  33.394  1.00 40.73      A    C  
ANISOU 2259  CB  HIS A 292     5926   1686   7863    255   3015  -2011  A    C  
ATOM   2260  CG  HIS A 292      -8.760  24.587  32.282  1.00 41.58      A    C  
ANISOU 2260  CG  HIS A 292     5993   1489   8316    148   3240  -1865  A    C  
ATOM   2261  CD2 HIS A 292      -8.602  24.436  30.945  1.00 40.31      A    C  
ANISOU 2261  CD2 HIS A 292     5813   1312   8191    116   3230  -1624  A    C  
ATOM   2262  ND1 HIS A 292      -9.347  25.808  32.530  1.00 43.78      A    N  
ANISOU 2262  ND1 HIS A 292     6220   1514   8902     57   3514  -1913  A    N  
ATOM   2263  CE1 HIS A 292      -9.536  26.353  31.342  1.00 42.34      A    C  
ANISOU 2263  CE1 HIS A 292     5968   1215   8905    -20   3661  -1651  A    C  
ATOM   2264  NE2 HIS A 292      -9.110  25.547  30.354  1.00 40.37      A    N  
ANISOU 2264  NE2 HIS A 292     5725   1129   8487     10   3487  -1473  A    N  
ATOM   2265  N   GLU A 293      -9.414  21.057  31.942  1.00 41.12      A    N  
ANISOU 2265  N   GLU A 293     6457   1621   7548    491   2688  -1416  A    N  
ATOM   2266  CA  GLU A 293      -9.902  20.307  30.776  1.00 40.03      A    C  
ANISOU 2266  CA  GLU A 293     6447   1409   7352    477   2626  -1112  A    C  
ATOM   2267  C   GLU A 293     -11.149  19.468  31.141  1.00 42.60      A    C  
ANISOU 2267  C   GLU A 293     6977   1687   7520    496   2575   -903  A    C  
ATOM   2268  O   GLU A 293     -12.112  19.482  30.376  1.00 42.89      A    O  
ANISOU 2268  O   GLU A 293     7036   1633   7627    403   2621   -652  A    O  
ATOM   2269  CB  GLU A 293      -8.799  19.442  30.128  1.00 40.60      A    C  
ANISOU 2269  CB  GLU A 293     6577   1594   7255    567   2488  -1162  A    C  
ATOM   2270  CG  GLU A 293      -7.591  20.210  29.587  1.00 44.98      A    C  
ANISOU 2270  CG  GLU A 293     6925   2204   7961    528   2543  -1357  A    C  
ATOM   2271  CD  GLU A 293      -7.785  21.593  28.981  1.00 69.59      A    C  
ANISOU 2271  CD  GLU A 293     9863   5157  11421    368   2755  -1320  A    C  
ATOM   2272  OE1 GLU A 293      -8.812  21.823  28.300  1.00 68.83      A    O  
ANISOU 2272  OE1 GLU A 293     9801   4913  11437    305   2832  -1033  A    O  
ATOM   2273  OE2 GLU A 293      -6.876  22.440  29.153  1.00 61.58      A    O1-
ANISOU 2273  OE2 GLU A 293     8670   4176  10552    310   2860  -1580  A    O1-
ATOM   2274  N   ILE A 294     -11.165  18.831  32.334  1.00 38.62      A    N  
ANISOU 2274  N   ILE A 294     6553   1358   6762    577   2492   -973  A    N  
ATOM   2275  CA  ILE A 294     -12.304  18.048  32.841  1.00 38.04      A    C  
ANISOU 2275  CA  ILE A 294     6663   1274   6515    575   2472   -797  A    C  
ATOM   2276  C   ILE A 294     -13.583  18.913  32.851  1.00 42.26      A    C  
ANISOU 2276  C   ILE A 294     7164   1569   7325    478   2619   -703  A    C  
ATOM   2277  O   ILE A 294     -14.616  18.474  32.349  1.00 43.20      A    O  
ANISOU 2277  O   ILE A 294     7366   1635   7414    395   2631   -473  A    O  
ATOM   2278  CB  ILE A 294     -12.005  17.452  34.252  1.00 41.07      A    C  
ANISOU 2278  CB  ILE A 294     7237   1654   6715    785   2414   -999  A    C  
ATOM   2279  CG1 ILE A 294     -11.129  16.222  34.132  1.00 41.27      A    C  
ANISOU 2279  CG1 ILE A 294     7445   1771   6466    959   2293  -1012  A    C  
ATOM   2280  CG2 ILE A 294     -13.290  17.136  35.028  1.00 41.60      A    C  
ANISOU 2280  CG2 ILE A 294     7446   1651   6710    756   2461   -873  A    C  
ATOM   2281  CD1 ILE A 294     -10.760  15.535  35.376  1.00 55.27      A    C  
ANISOU 2281  CD1 ILE A 294     9350   3690   7960   1185   2233  -1121  A    C  
ATOM   2282  N   SER A 295     -13.488  20.143  33.391  1.00 39.12      A    N  
ANISOU 2282  N   SER A 295     6531   1244   7090    423   2732   -819  A    N  
ATOM   2283  CA  SER A 295     -14.569  21.114  33.525  1.00 39.03      A    C  
ANISOU 2283  CA  SER A 295     6393   1160   7277    328   2898   -703  A    C  
ATOM   2284  C   SER A 295     -15.160  21.531  32.154  1.00 41.50      A    C  
ANISOU 2284  C   SER A 295     6694   1244   7832    281   2987   -471  A    C  
ATOM   2285  O   SER A 295     -16.377  21.731  32.067  1.00 41.82      A    O  
ANISOU 2285  O   SER A 295     6717   1248   7926    240   3064   -263  A    O  
ATOM   2286  CB  SER A 295     -14.077  22.324  34.307  1.00 42.24      A    C  
ANISOU 2286  CB  SER A 295     6706   1395   7948    350   3045  -1007  A    C  
ATOM   2287  OG  SER A 295     -13.620  21.901  35.584  1.00 45.89      A    O  
ANISOU 2287  OG  SER A 295     7225   2001   8208    435   2957  -1247  A    O  
ATOM   2288  N   HIS A 296     -14.328  21.556  31.079  1.00 37.35      A    N  
ANISOU 2288  N   HIS A 296     5936   1079   7176    210   2955   -396  A    N  
ATOM   2289  CA  HIS A 296     -14.785  21.802  29.712  1.00 36.57      A    C  
ANISOU 2289  CA  HIS A 296     5725   1025   7143    169   3016   -153  A    C  
ATOM   2290  C   HIS A 296     -15.817  20.770  29.255  1.00 38.24      A    C  
ANISOU 2290  C   HIS A 296     6194   1040   7297    165   2918     44  A    C  
ATOM   2291  O   HIS A 296     -16.639  21.087  28.406  1.00 38.39      A    O  
ANISOU 2291  O   HIS A 296     6137   1045   7407    130   2987    277  A    O  
ATOM   2292  CB  HIS A 296     -13.624  21.804  28.719  1.00 37.08      A    C  
ANISOU 2292  CB  HIS A 296     5766   1060   7264    172   2981   -205  A    C  
ATOM   2293  CG  HIS A 296     -13.006  23.152  28.515  1.00 40.24      A    C  
ANISOU 2293  CG  HIS A 296     6118   1092   8080    184   3178   -328  A    C  
ATOM   2294  CD2 HIS A 296     -11.722  23.544  28.675  1.00 41.27      A    C  
ANISOU 2294  CD2 HIS A 296     6231   1115   8337    191   3207   -617  A    C  
ATOM   2295  ND1 HIS A 296     -13.771  24.247  28.142  1.00 42.85      A    N  
ANISOU 2295  ND1 HIS A 296     6399   1166   8717    188   3400   -151  A    N  
ATOM   2296  CE1 HIS A 296     -12.935  25.272  28.103  1.00 43.09      A    C  
ANISOU 2296  CE1 HIS A 296     6323   1073   8977    162   3580   -318  A    C  
ATOM   2297  NE2 HIS A 296     -11.687  24.896  28.417  1.00 42.93      A    N  
ANISOU 2297  NE2 HIS A 296     6311   1135   8864    145   3467   -621  A    N  
ATOM   2298  N   SER A 297     -15.809  19.554  29.826  1.00 34.85      A    N  
ANISOU 2298  N   SER A 297     5799    999   6443    151   2779    -11  A    N  
ATOM   2299  CA  SER A 297     -16.816  18.535  29.509  1.00 34.55      A    C  
ANISOU 2299  CA  SER A 297     5904    994   6230     93   2724    131  A    C  
ATOM   2300  C   SER A 297     -18.244  19.081  29.644  1.00 39.76      A    C  
ANISOU 2300  C   SER A 297     6677   1233   7197     34   2830    326  A    C  
ATOM   2301  O   SER A 297     -19.136  18.584  28.968  1.00 39.12      A    O  
ANISOU 2301  O   SER A 297     6591   1260   7012    -70   2816    502  A    O  
ATOM   2302  CB  SER A 297     -16.643  17.319  30.399  1.00 34.43      A    C  
ANISOU 2302  CB  SER A 297     6163    940   5978    121   2630     32  A    C  
ATOM   2303  OG  SER A 297     -15.360  16.779  30.148  1.00 35.04      A    O  
ANISOU 2303  OG  SER A 297     6377    937   6000    198   2537    -80  A    O  
ATOM   2304  N   TRP A 298     -18.424  20.169  30.447  1.00 38.62      A    N  
ANISOU 2304  N   TRP A 298     6396   1056   7221     94   2950    268  A    N  
ATOM   2305  CA  TRP A 298     -19.694  20.860  30.668  1.00 37.60      A    C  
ANISOU 2305  CA  TRP A 298     6114    998   7173     82   3079    421  A    C  
ATOM   2306  C   TRP A 298     -19.678  22.194  29.954  1.00 40.41      A    C  
ANISOU 2306  C   TRP A 298     6308   1192   7853    132   3245    558  A    C  
ATOM   2307  O   TRP A 298     -20.374  22.365  28.955  1.00 39.06      A    O  
ANISOU 2307  O   TRP A 298     6017   1128   7695    121   3285    810  A    O  
ATOM   2308  CB  TRP A 298     -19.978  21.028  32.169  1.00 36.17      A    C  
ANISOU 2308  CB  TRP A 298     5925    901   6918    116   3122    264  A    C  
ATOM   2309  CG  TRP A 298     -20.331  19.731  32.825  1.00 36.06      A    C  
ANISOU 2309  CG  TRP A 298     6153    897   6653     73   3006    225  A    C  
ATOM   2310  CD1 TRP A 298     -21.569  19.163  32.906  1.00 38.05      A    C  
ANISOU 2310  CD1 TRP A 298     6555   1024   6880    -25   3015    382  A    C  
ATOM   2311  CD2 TRP A 298     -19.419  18.789  33.402  1.00 35.69      A    C  
ANISOU 2311  CD2 TRP A 298     6291    882   6389    116   2889     54  A    C  
ATOM   2312  CE2 TRP A 298     -20.176  17.673  33.819  1.00 38.38      A    C  
ANISOU 2312  CE2 TRP A 298     6956    999   6629     65   2855    109  A    C  
ATOM   2313  CE3 TRP A 298     -18.030  18.774  33.604  1.00 36.45      A    C  
ANISOU 2313  CE3 TRP A 298     6446    902   6499    211   2821   -137  A    C  
ATOM   2314  NE1 TRP A 298     -21.486  17.932  33.510  1.00 37.44      A    N  
ANISOU 2314  NE1 TRP A 298     6727    940   6560    -50   2933    293  A    N  
ATOM   2315  CZ2 TRP A 298     -19.600  16.583  34.462  1.00 37.52      A    C  
ANISOU 2315  CZ2 TRP A 298     7085    899   6274    136   2779     -6  A    C  
ATOM   2316  CZ3 TRP A 298     -17.462  17.689  34.244  1.00 36.93      A    C  
ANISOU 2316  CZ3 TRP A 298     6763    921   6349    300   2718   -252  A    C  
ATOM   2317  CH2 TRP A 298     -18.245  16.614  34.668  1.00 37.53      A    C  
ANISOU 2317  CH2 TRP A 298     7098    915   6248    280   2707   -177  A    C  
ATOM   2318  N   THR A 299     -18.852  23.126  30.439  1.00 39.24      A    N  
ANISOU 2318  N   THR A 299     6076    958   7874    190   3358    370  A    N  
ATOM   2319  CA  THR A 299     -18.731  24.501  29.922  1.00 39.76      A    C  
ANISOU 2319  CA  THR A 299     5968    913   8227    244   3584    451  A    C  
ATOM   2320  C   THR A 299     -17.731  24.553  28.757  1.00 44.86      A    C  
ANISOU 2320  C   THR A 299     6619   1465   8959    242   3563    476  A    C  
ATOM   2321  O   THR A 299     -16.520  24.680  28.945  1.00 45.67      A    O  
ANISOU 2321  O   THR A 299     6743   1494   9115    227   3553    227  A    O  
ATOM   2322  CB  THR A 299     -18.380  25.412  31.075  1.00 42.55      A    C  
ANISOU 2322  CB  THR A 299     6348   1007   8813    264   3746    212  A    C  
ATOM   2323  CG2 THR A 299     -19.533  25.552  32.041  1.00 39.38      A    C  
ANISOU 2323  CG2 THR A 299     5854    810   8298    268   3810    251  A    C  
ATOM   2324  OG1 THR A 299     -17.270  24.842  31.770  1.00 41.47      A    O  
ANISOU 2324  OG1 THR A 299     6298    912   8548    231   3602   -112  A    O  
ATOM   2325  N   GLY A 300     -18.271  24.406  27.556  1.00 41.67      A    N  
ANISOU 2325  N   GLY A 300     6147   1183   8503    250   3548    763  A    N  
ATOM   2326  CA  GLY A 300     -17.507  24.367  26.324  1.00 40.82      A    C  
ANISOU 2326  CA  GLY A 300     6000   1108   8402    248   3521    828  A    C  
ATOM   2327  C   GLY A 300     -17.928  23.243  25.404  1.00 43.10      A    C  
ANISOU 2327  C   GLY A 300     6318   1631   8428    188   3334    991  A    C  
ATOM   2328  O   GLY A 300     -18.372  23.502  24.285  1.00 44.04      A    O  
ANISOU 2328  O   GLY A 300     6312   1873   8548    218   3384   1249  A    O  
ATOM   2329  N   ASN A 301     -17.786  21.983  25.864  1.00 37.87      A    N  
ANISOU 2329  N   ASN A 301     5793   1099   7496    113   3134    820  A    N  
ATOM   2330  CA  ASN A 301     -18.085  20.771  25.088  1.00 36.24      A    C  
ANISOU 2330  CA  ASN A 301     5628   1140   7002     30   2972    882  A    C  
ATOM   2331  C   ASN A 301     -19.582  20.416  25.103  1.00 42.31      A    C  
ANISOU 2331  C   ASN A 301     6412   1971   7692    -67   2975   1102  A    C  
ATOM   2332  O   ASN A 301     -20.125  20.010  24.074  1.00 44.17      A    O  
ANISOU 2332  O   ASN A 301     6567   2425   7789   -141   2934   1267  A    O  
ATOM   2333  CB  ASN A 301     -17.244  19.588  25.581  1.00 32.51      A    C  
ANISOU 2333  CB  ASN A 301     5173   1040   6141     45   2807    553  A    C  
ATOM   2334  CG  ASN A 301     -15.738  19.797  25.616  1.00 45.76      A    C  
ANISOU 2334  CG  ASN A 301     7151   2070   8164     42   2798    479  A    C  
ATOM   2335  ND2 ASN A 301     -15.005  18.740  26.002  1.00 31.14      A    N  
ANISOU 2335  ND2 ASN A 301     5110    969   5752     77   2665    233  A    N  
ATOM   2336  OD1 ASN A 301     -15.206  20.881  25.294  1.00 36.06      A    O  
ANISOU 2336  OD1 ASN A 301     5639   1036   7026    106   2914    443  A    O  
ATOM   2337  N   LEU A 302     -20.239  20.540  26.255  1.00 38.60      A    N  
ANISOU 2337  N   LEU A 302     5978   1444   7244    -58   3018   1054  A    N  
ATOM   2338  CA  LEU A 302     -21.681  20.286  26.381  1.00 38.58      A    C  
ANISOU 2338  CA  LEU A 302     5911   1623   7126   -130   3035   1206  A    C  
ATOM   2339  C   LEU A 302     -22.453  21.583  26.033  1.00 42.16      A    C  
ANISOU 2339  C   LEU A 302     6110   2145   7764     -5   3206   1455  A    C  
ATOM   2340  O   LEU A 302     -23.402  21.544  25.246  1.00 41.27      A    O  
ANISOU 2340  O   LEU A 302     5832   2303   7545    -28   3215   1677  A    O  
ATOM   2341  CB  LEU A 302     -22.008  19.780  27.804  1.00 37.04      A    C  
ANISOU 2341  CB  LEU A 302     5887   1331   6857   -169   3013   1041  A    C  
ATOM   2342  CG  LEU A 302     -23.382  19.191  28.058  1.00 41.49      A    C  
ANISOU 2342  CG  LEU A 302     6438   2071   7254   -292   3014   1132  A    C  
ATOM   2343  CD1 LEU A 302     -23.682  18.022  27.128  1.00 41.66      A    C  
ANISOU 2343  CD1 LEU A 302     6510   2296   7025   -481   2918   1164  A    C  
ATOM   2344  CD2 LEU A 302     -23.491  18.750  29.506  1.00 40.89      A    C  
ANISOU 2344  CD2 LEU A 302     6556   1854   7127   -303   3012    961  A    C  
ATOM   2345  N   VAL A 303     -22.034  22.712  26.614  1.00 41.21      A    N  
ANISOU 2345  N   VAL A 303     5957   1795   7908    131   3359   1409  A    N  
ATOM   2346  CA  VAL A 303     -22.602  24.028  26.311  1.00 44.66      A    C  
ANISOU 2346  CA  VAL A 303     6195   2217   8556    289   3579   1643  A    C  
ATOM   2347  C   VAL A 303     -21.488  24.826  25.611  1.00 48.22      A    C  
ANISOU 2347  C   VAL A 303     6613   2499   9210    377   3690   1649  A    C  
ATOM   2348  O   VAL A 303     -20.486  25.157  26.228  1.00 47.94      A    O  
ANISOU 2348  O   VAL A 303     6672   2215   9329    374   3739   1407  A    O  
ATOM   2349  CB  VAL A 303     -23.283  24.760  27.502  1.00 51.59      A    C  
ANISOU 2349  CB  VAL A 303     7064   2954   9585    360   3732   1605  A    C  
ATOM   2350  CG1 VAL A 303     -22.357  25.068  28.667  1.00 52.29      A    C  
ANISOU 2350  CG1 VAL A 303     7285   2739   9846    362   3791   1297  A    C  
ATOM   2351  CG2 VAL A 303     -24.004  26.010  27.020  1.00 52.89      A    C  
ANISOU 2351  CG2 VAL A 303     7024   3151   9920    545   3972   1913  A    C  
ATOM   2352  N   THR A 304     -21.625  25.024  24.290  1.00 44.72      A    N  
ANISOU 2352  N   THR A 304     6033   2227   8733    437   3718   1906  A    N  
ATOM   2353  CA  THR A 304     -20.603  25.627  23.427  1.00 45.03      A    C  
ANISOU 2353  CA  THR A 304     6045   2143   8923    505   3816   1941  A    C  
ATOM   2354  C   THR A 304     -20.865  27.114  23.138  1.00 50.60      A    C  
ANISOU 2354  C   THR A 304     6620   2709   9898    712   4138   2186  A    C  
ATOM   2355  O   THR A 304     -22.016  27.542  23.066  1.00 50.39      A    O  
ANISOU 2355  O   THR A 304     6461   2825   9860    840   4246   2453  A    O  
ATOM   2356  CB  THR A 304     -20.548  24.811  22.108  1.00 50.88      A    C  
ANISOU 2356  CB  THR A 304     6734   3175   9425    443   3647   2071  A    C  
ATOM   2357  CG2 THR A 304     -19.350  25.160  21.211  1.00 43.87      A    C  
ANISOU 2357  CG2 THR A 304     5848   2177   8644    479   3701   2065  A    C  
ATOM   2358  OG1 THR A 304     -20.510  23.421  22.437  1.00 44.47      A    O  
ANISOU 2358  OG1 THR A 304     6064   2470   8362    256   3399   1865  A    O  
ATOM   2359  N   ASN A 305     -19.780  27.898  22.967  1.00 47.89      A    N  
ANISOU 2359  N   ASN A 305     6316   2085   9794    748   4313   2093  A    N  
ATOM   2360  CA  ASN A 305     -19.866  29.313  22.580  1.00 50.02      A    C  
ANISOU 2360  CA  ASN A 305     6505   2159  10342    941   4675   2323  A    C  
ATOM   2361  C   ASN A 305     -20.358  29.375  21.132  1.00 55.01      A    C  
ANISOU 2361  C   ASN A 305     6986   3069  10847   1090   4696   2729  A    C  
ATOM   2362  O   ASN A 305     -19.899  28.581  20.318  1.00 53.91      A    O  
ANISOU 2362  O   ASN A 305     6842   3123  10517    999   4489   2712  A    O  
ATOM   2363  CB  ASN A 305     -18.511  30.019  22.751  1.00 53.64      A    C  
ANISOU 2363  CB  ASN A 305     7055   2255  11070    884   4861   2067  A    C  
ATOM   2364  CG  ASN A 305     -17.286  29.388  22.101  1.00 70.13      A    C  
ANISOU 2364  CG  ASN A 305     9191   4386  13070    756   4685   1894  A    C  
ATOM   2365  ND2 ASN A 305     -17.430  28.404  21.235  1.00 65.95      A    N  
ANISOU 2365  ND2 ASN A 305     8627   4165  12265    727   4430   2020  A    N  
ATOM   2366  OD1 ASN A 305     -16.163  29.773  22.389  1.00 62.36      A    O  
ANISOU 2366  OD1 ASN A 305     8267   3167  12259    669   4784   1617  A    O  
ATOM   2367  N   GLU A 306     -21.331  30.235  20.828  1.00 54.47      A    N  
ANISOU 2367  N   GLU A 306     6787   3060  10849   1329   4934   3093  A    N  
ATOM   2368  CA  GLU A 306     -21.914  30.360  19.490  1.00 56.34      A    C  
ANISOU 2368  CA  GLU A 306     6844   3629  10932   1521   4969   3516  A    C  
ATOM   2369  C   GLU A 306     -20.843  30.709  18.430  1.00 60.07      A    C  
ANISOU 2369  C   GLU A 306     7344   3986  11495   1556   5077   3578  A    C  
ATOM   2370  O   GLU A 306     -20.834  30.137  17.338  1.00 59.71      A    O  
ANISOU 2370  O   GLU A 306     7202   4273  11211   1555   4912   3727  A    O  
ATOM   2371  CB  GLU A 306     -23.014  31.425  19.511  1.00 60.87      A    C  
ANISOU 2371  CB  GLU A 306     7292   4218  11618   1829   5278   3890  A    C  
ATOM   2372  CG  GLU A 306     -23.833  31.544  18.235  1.00 75.96      A    C  
ANISOU 2372  CG  GLU A 306     8973   6576  13311   2078   5305   4362  A    C  
ATOM   2373  CD  GLU A 306     -24.843  30.440  17.988  1.00 96.73      A    C  
ANISOU 2373  CD  GLU A 306    11419   9790  15544   1991   4975   4424  A    C  
ATOM   2374  OE1 GLU A 306     -25.286  29.787  18.960  1.00 90.35      A    O  
ANISOU 2374  OE1 GLU A 306    10654   9016  14661   1804   4799   4184  A    O  
ATOM   2375  OE2 GLU A 306     -25.218  30.252  16.811  1.00 92.28      A    O1-
ANISOU 2375  OE2 GLU A 306    10660   9667  14734   2106   4910   4710  A    O1-
ATOM   2376  N   THR A 307     -19.961  31.654  18.761  1.00 55.47      A    N  
ANISOU 2376  N   THR A 307     6886   2941  11250   1573   5371   3449  A    N  
ATOM   2377  CA  THR A 307     -18.853  32.126  17.931  1.00 54.47      A    C  
ANISOU 2377  CA  THR A 307     6808   2620  11268   1583   5536   3459  A    C  
ATOM   2378  C   THR A 307     -17.630  32.336  18.852  1.00 55.46      A    C  
ANISOU 2378  C   THR A 307     7099   2331  11642   1360   5604   2986  A    C  
ATOM   2379  O   THR A 307     -17.755  32.201  20.069  1.00 52.77      A    O  
ANISOU 2379  O   THR A 307     6824   1877  11350   1244   5543   2709  A    O  
ATOM   2380  CB  THR A 307     -19.240  33.436  17.163  1.00 61.60      A    C  
ANISOU 2380  CB  THR A 307     7652   3399  12356   1911   5976   3908  A    C  
ATOM   2381  CG2 THR A 307     -20.532  33.332  16.347  1.00 60.04      A    C  
ANISOU 2381  CG2 THR A 307     7247   3679  11887   2177   5924   4392  A    C  
ATOM   2382  OG1 THR A 307     -19.355  34.500  18.091  1.00 60.97      A    O  
ANISOU 2382  OG1 THR A 307     7664   2900  12602   1984   6337   3851  A    O  
ATOM   2383  N   TRP A 308     -16.469  32.713  18.285  1.00 52.75      A    N  
ANISOU 2383  N   TRP A 308     6809   1785  11448   1305   5749   2894  A    N  
ATOM   2384  CA  TRP A 308     -15.260  33.011  19.058  1.00 52.14      A    C  
ANISOU 2384  CA  TRP A 308     6847   1364  11600   1092   5848   2439  A    C  
ATOM   2385  C   TRP A 308     -15.337  34.413  19.704  1.00 60.49      A    C  
ANISOU 2385  C   TRP A 308     7967   1984  13033   1158   6330   2416  A    C  
ATOM   2386  O   TRP A 308     -14.504  34.762  20.545  1.00 60.40      A    O  
ANISOU 2386  O   TRP A 308     8030   1699  13219    964   6449   2003  A    O  
ATOM   2387  CB  TRP A 308     -14.019  32.840  18.186  1.00 50.31      A    C  
ANISOU 2387  CB  TRP A 308     6628   1121  11368    988   5817   2331  A    C  
ATOM   2388  CG  TRP A 308     -13.946  31.448  17.657  1.00 49.01      A    C  
ANISOU 2388  CG  TRP A 308     6425   1352  10845    910   5365   2311  A    C  
ATOM   2389  CD1 TRP A 308     -14.122  31.051  16.363  1.00 52.15      A    C  
ANISOU 2389  CD1 TRP A 308     6746   2029  11040   1003   5259   2612  A    C  
ATOM   2390  CD2 TRP A 308     -13.880  30.252  18.441  1.00 46.38      A    C  
ANISOU 2390  CD2 TRP A 308     6135   1194  10294    746   4982   2010  A    C  
ATOM   2391  CE2 TRP A 308     -13.968  29.162  17.550  1.00 49.43      A    C  
ANISOU 2391  CE2 TRP A 308     6488   1925  10371    726   4678   2124  A    C  
ATOM   2392  CE3 TRP A 308     -13.738  29.995  19.818  1.00 46.50      A    C  
ANISOU 2392  CE3 TRP A 308     6222   1110  10336    619   4884   1653  A    C  
ATOM   2393  NE1 TRP A 308     -14.086  29.680  16.284  1.00 49.82      A    N  
ANISOU 2393  NE1 TRP A 308     6452   2044  10432    872   4844   2473  A    N  
ATOM   2394  CZ2 TRP A 308     -13.899  27.834  17.985  1.00 46.36      A    C  
ANISOU 2394  CZ2 TRP A 308     6160   1732   9723    585   4314   1896  A    C  
ATOM   2395  CZ3 TRP A 308     -13.698  28.676  20.250  1.00 45.69      A    C  
ANISOU 2395  CZ3 TRP A 308     6171   1232   9958    508   4506   1458  A    C  
ATOM   2396  CH2 TRP A 308     -13.753  27.617  19.338  1.00 44.96      A    C  
ANISOU 2396  CH2 TRP A 308     6069   1428   9584    491   4240   1578  A    C  
ATOM   2397  N   GLU A 309     -16.366  35.191  19.346  1.00 59.93      A    N  
ANISOU 2397  N   GLU A 309     7858   1870  13042   1434   6614   2848  A    N  
ATOM   2398  CA  GLU A 309     -16.639  36.479  19.970  1.00 63.56      A    C  
ANISOU 2398  CA  GLU A 309     8395   1911  13844   1533   7097   2872  A    C  
ATOM   2399  C   GLU A 309     -17.183  36.201  21.396  1.00 65.70      A    C  
ANISOU 2399  C   GLU A 309     8683   2182  14096   1428   6958   2601  A    C  
ATOM   2400  O   GLU A 309     -16.885  36.940  22.325  1.00 66.42      A    O  
ANISOU 2400  O   GLU A 309     8864   1918  14455   1329   7240   2324  A    O  
ATOM   2401  CB  GLU A 309     -17.632  37.289  19.118  1.00 68.05      A    C  
ANISOU 2401  CB  GLU A 309     8913   2486  14456   1916   7424   3463  A    C  
ATOM   2402  CG  GLU A 309     -17.116  37.555  17.711  1.00 80.28      A    C  
ANISOU 2402  CG  GLU A 309    10444   4066  15994   2046   7564   3761  A    C  
ATOM   2403  CD  GLU A 309     -18.039  38.329  16.789  1.00109.04      A    C  
ANISOU 2403  CD  GLU A 309    14026   7767  19637   2473   7888   4382  A    C  
ATOM   2404  OE1 GLU A 309     -17.550  39.266  16.118  1.00104.59      A    O  
ANISOU 2404  OE1 GLU A 309    13551   6890  19300   2608   8328   4574  A    O  
ATOM   2405  OE2 GLU A 309     -19.239  37.979  16.704  1.00106.93      A    O1-
ANISOU 2405  OE2 GLU A 309    13616   7883  19128   2680   7709   4683  A    O1-
ATOM   2406  N   ASN A 310     -17.904  35.076  21.552  1.00 59.41      A    N  
ANISOU 2406  N   ASN A 310     7806   1797  12971   1422   6523   2651  A    N  
ATOM   2407  CA  ASN A 310     -18.531  34.581  22.784  1.00 58.58      A    C  
ANISOU 2407  CA  ASN A 310     7708   1780  12770   1336   6325   2447  A    C  
ATOM   2408  C   ASN A 310     -17.658  33.533  23.520  1.00 56.94      A    C  
ANISOU 2408  C   ASN A 310     7558   1665  12414   1042   5954   1963  A    C  
ATOM   2409  O   ASN A 310     -18.168  32.847  24.401  1.00 53.58      A    O  
ANISOU 2409  O   ASN A 310     7140   1393  11825    973   5712   1824  A    O  
ATOM   2410  CB  ASN A 310     -19.898  33.955  22.455  1.00 58.61      A    C  
ANISOU 2410  CB  ASN A 310     7585   2197  12486   1505   6102   2811  A    C  
ATOM   2411  CG  ASN A 310     -20.909  34.941  21.930  1.00 75.89      A    C  
ANISOU 2411  CG  ASN A 310     9689   4373  14774   1842   6445   3299  A    C  
ATOM   2412  ND2 ASN A 310     -21.147  34.913  20.631  1.00 67.68      A    N  
ANISOU 2412  ND2 ASN A 310     8540   3584  13593   2023   6438   3683  A    N  
ATOM   2413  OD1 ASN A 310     -21.510  35.707  22.678  1.00 65.39      A    O  
ANISOU 2413  OD1 ASN A 310     8382   2839  13624   1961   6716   3347  A    O  
ATOM   2414  N   PHE A 311     -16.341  33.478  23.201  1.00 52.37      A    N  
ANISOU 2414  N   PHE A 311     7019    983  11898    888   5943   1711  A    N  
ATOM   2415  CA  PHE A 311     -15.340  32.558  23.754  1.00 50.08      A    C  
ANISOU 2415  CA  PHE A 311     6758    819  11452    655   5624   1270  A    C  
ATOM   2416  C   PHE A 311     -15.241  32.601  25.289  1.00 53.63      A    C  
ANISOU 2416  C   PHE A 311     7269   1142  11966    523   5612    878  A    C  
ATOM   2417  O   PHE A 311     -14.884  31.579  25.886  1.00 52.64      A    O  
ANISOU 2417  O   PHE A 311     7171   1212  11616    407   5274    618  A    O  
ATOM   2418  CB  PHE A 311     -13.947  32.804  23.124  1.00 52.16      A    C  
ANISOU 2418  CB  PHE A 311     7040    937  11840    541   5715   1090  A    C  
ATOM   2419  CG  PHE A 311     -12.864  31.797  23.470  1.00 52.12      A    C  
ANISOU 2419  CG  PHE A 311     7051   1102  11649    353   5377    696  A    C  
ATOM   2420  CD1 PHE A 311     -13.114  30.418  23.410  1.00 52.25      A    C  
ANISOU 2420  CD1 PHE A 311     7083   1445  11325    351   4953    729  A    C  
ATOM   2421  CD2 PHE A 311     -11.591  32.219  23.833  1.00 54.22      A    C  
ANISOU 2421  CD2 PHE A 311     7313   1215  12071    184   5504    296  A    C  
ATOM   2422  CE1 PHE A 311     -12.115  29.488  23.742  1.00 51.00      A    C  
ANISOU 2422  CE1 PHE A 311     6957   1431  10989    225   4671    395  A    C  
ATOM   2423  CE2 PHE A 311     -10.590  31.287  24.154  1.00 55.37      A    C  
ANISOU 2423  CE2 PHE A 311     7452   1567  12021     54   5193    -47  A    C  
ATOM   2424  CZ  PHE A 311     -10.854  29.928  24.096  1.00 51.20      A    C  
ANISOU 2424  CZ  PHE A 311     6959   1338  11157     97   4782     24  A    C  
ATOM   2425  N   TRP A 312     -15.598  33.726  25.932  1.00 50.40      A    N  
ANISOU 2425  N   TRP A 312     6804    591  11756    549   5983    830  A    N  
ATOM   2426  CA  TRP A 312     -15.550  33.854  27.395  1.00 50.42      A    C  
ANISOU 2426  CA  TRP A 312     6824    544  11789    414   6001    457  A    C  
ATOM   2427  C   TRP A 312     -16.561  32.908  28.086  1.00 53.02      A    C  
ANISOU 2427  C   TRP A 312     7253    951  11943    478   5681    530  A    C  
ATOM   2428  O   TRP A 312     -16.321  32.502  29.219  1.00 50.82      A    O  
ANISOU 2428  O   TRP A 312     7006    730  11574    359   5535    189  A    O  
ATOM   2429  CB  TRP A 312     -15.769  35.312  27.841  1.00 52.78      A    C  
ANISOU 2429  CB  TRP A 312     7142    469  12441    433   6514    421  A    C  
ATOM   2430  CG  TRP A 312     -17.210  35.728  27.928  1.00 54.22      A    C  
ANISOU 2430  CG  TRP A 312     7372    511  12718    666   6674    795  A    C  
ATOM   2431  CD1 TRP A 312     -17.979  36.241  26.925  1.00 57.99      A    C  
ANISOU 2431  CD1 TRP A 312     7878    830  13326    931   6888   1299  A    C  
ATOM   2432  CD2 TRP A 312     -18.064  35.620  29.077  1.00 53.74      A    C  
ANISOU 2432  CD2 TRP A 312     7315    509  12596    675   6623    718  A    C  
ATOM   2433  CE2 TRP A 312     -19.345  36.069  28.691  1.00 58.17      A    C  
ANISOU 2433  CE2 TRP A 312     7907    928  13268    953   6805   1181  A    C  
ATOM   2434  CE3 TRP A 312     -17.869  35.194  30.402  1.00 53.15      A    C  
ANISOU 2434  CE3 TRP A 312     7274    486  12432    507   6446    314  A    C  
ATOM   2435  NE1 TRP A 312     -19.259  36.463  27.377  1.00 57.96      A    N  
ANISOU 2435  NE1 TRP A 312     7854    852  13316   1107   6971   1532  A    N  
ATOM   2436  CZ2 TRP A 312     -20.424  36.124  29.594  1.00 56.91      A    C  
ANISOU 2436  CZ2 TRP A 312     7741    800  13081   1032   6825   1227  A    C  
ATOM   2437  CZ3 TRP A 312     -18.934  35.249  31.291  1.00 53.71      A    C  
ANISOU 2437  CZ3 TRP A 312     7389    504  12513    592   6468    361  A    C  
ATOM   2438  CH2 TRP A 312     -20.197  35.690  30.881  1.00 55.27      A    C  
ANISOU 2438  CH2 TRP A 312     7572    639  12790    841   6651    810  A    C  
ATOM   2439  N   LEU A 313     -17.689  32.581  27.426  1.00 50.98      A    N  
ANISOU 2439  N   LEU A 313     6953    869  11547    649   5591    961  A    N  
ATOM   2440  CA  LEU A 313     -18.690  31.665  27.986  1.00 51.09      A    C  
ANISOU 2440  CA  LEU A 313     6967   1142  11302    671   5311   1037  A    C  
ATOM   2441  C   LEU A 313     -18.071  30.285  28.196  1.00 54.49      A    C  
ANISOU 2441  C   LEU A 313     7456   1811  11438    525   4900    803  A    C  
ATOM   2442  O   LEU A 313     -18.356  29.607  29.180  1.00 55.27      A    O  
ANISOU 2442  O   LEU A 313     7610   2016  11373    466   4712    637  A    O  
ATOM   2443  CB  LEU A 313     -19.908  31.556  27.063  1.00 51.64      A    C  
ANISOU 2443  CB  LEU A 313     6943   1417  11259    857   5298   1524  A    C  
ATOM   2444  CG  LEU A 313     -20.755  32.807  26.915  1.00 57.00      A    C  
ANISOU 2444  CG  LEU A 313     7561   1921  12175   1073   5694   1830  A    C  
ATOM   2445  CD1 LEU A 313     -21.707  32.663  25.763  1.00 57.67      A    C  
ANISOU 2445  CD1 LEU A 313     7513   2290  12107   1275   5659   2313  A    C  
ATOM   2446  CD2 LEU A 313     -21.534  33.076  28.177  1.00 57.62      A    C  
ANISOU 2446  CD2 LEU A 313     7661   1921  12310   1085   5783   1727  A    C  
ATOM   2447  N   ASN A 314     -17.196  29.903  27.264  1.00 48.53      A    N  
ANISOU 2447  N   ASN A 314     6698   1120  10622    484   4789    797  A    N  
ATOM   2448  CA  ASN A 314     -16.412  28.686  27.264  1.00 45.90      A    C  
ANISOU 2448  CA  ASN A 314     6429    975  10038    376   4451    592  A    C  
ATOM   2449  C   ASN A 314     -15.355  28.744  28.373  1.00 48.31      A    C  
ANISOU 2449  C   ASN A 314     6778   1193  10384    261   4436    133  A    C  
ATOM   2450  O   ASN A 314     -15.413  27.975  29.335  1.00 47.51      A    O  
ANISOU 2450  O   ASN A 314     6745   1214  10091    226   4234    -50  A    O  
ATOM   2451  CB  ASN A 314     -15.709  28.558  25.888  1.00 46.45      A    C  
ANISOU 2451  CB  ASN A 314     6463   1095  10092    380   4420    718  A    C  
ATOM   2452  CG  ASN A 314     -16.026  27.360  25.057  1.00 62.44      A    C  
ANISOU 2452  CG  ASN A 314     8504   3398  11821    381   4133    906  A    C  
ATOM   2453  ND2 ASN A 314     -17.237  27.303  24.536  1.00 56.74      A    N  
ANISOU 2453  ND2 ASN A 314     7718   2826  11016    464   4137   1244  A    N  
ATOM   2454  OD1 ASN A 314     -15.143  26.559  24.744  1.00 49.73      A    O  
ANISOU 2454  OD1 ASN A 314     6949   1881  10067    311   3937    756  A    O  
ATOM   2455  N   GLU A 315     -14.389  29.671  28.232  1.00 44.91      A    N  
ANISOU 2455  N   GLU A 315     6213    745  10107    186   4670    -45  A    N  
ATOM   2456  CA  GLU A 315     -13.243  29.721  29.118  1.00 44.50      A    C  
ANISOU 2456  CA  GLU A 315     6124    748  10037     42   4648   -485  A    C  
ATOM   2457  C   GLU A 315     -13.497  30.354  30.485  1.00 48.40      A    C  
ANISOU 2457  C   GLU A 315     6731    900  10758     23   4810   -776  A    C  
ATOM   2458  O   GLU A 315     -12.943  29.841  31.447  1.00 47.57      A    O  
ANISOU 2458  O   GLU A 315     6634    952  10489    -39   4634  -1106  A    O  
ATOM   2459  CB  GLU A 315     -11.994  30.314  28.437  1.00 46.09      A    C  
ANISOU 2459  CB  GLU A 315     6301    753  10456    -35   4812   -659  A    C  
ATOM   2460  CG  GLU A 315     -11.358  29.334  27.431  1.00 48.15      A    C  
ANISOU 2460  CG  GLU A 315     6645   1062  10586      3   4549   -598  A    C  
ATOM   2461  CD  GLU A 315     -10.833  28.016  27.975  1.00 63.64      A    C  
ANISOU 2461  CD  GLU A 315     8659   3300  12221     -2   4176   -804  A    C  
ATOM   2462  OE1 GLU A 315     -10.796  27.924  29.228  1.00 41.67      A    O  
ANISOU 2462  OE1 GLU A 315     5679    983   9171   -109   4109   -960  A    O  
ATOM   2463  OE2 GLU A 315     -10.549  27.065  27.188  1.00 44.05      A    O1-
ANISOU 2463  OE2 GLU A 315     6220    974   9543     37   3951   -683  A    O1-
ATOM   2464  N   GLY A 316     -14.334  31.386  30.585  1.00 47.28      A    N  
ANISOU 2464  N   GLY A 316     6496    685  10782     42   5129   -595  A    N  
ATOM   2465  CA  GLY A 316     -14.653  32.025  31.860  1.00 48.24      A    C  
ANISOU 2465  CA  GLY A 316     6628    675  11028    -11   5310   -830  A    C  
ATOM   2466  C   GLY A 316     -15.372  31.117  32.843  1.00 50.06      A    C  
ANISOU 2466  C   GLY A 316     6986    968  11067     58   5042   -882  A    C  
ATOM   2467  O   GLY A 316     -15.017  31.089  34.023  1.00 49.21      A    O  
ANISOU 2467  O   GLY A 316     6876    923  10899    -26   5010  -1240  A    O  
ATOM   2468  N   HIS A 317     -16.385  30.362  32.368  1.00 46.44      A    N  
ANISOU 2468  N   HIS A 317     6514    753  10380    157   4853   -490  A    N  
ATOM   2469  CA  HIS A 317     -17.140  29.413  33.191  1.00 46.00      A    C  
ANISOU 2469  CA  HIS A 317     6565    811  10101    201   4611   -482  A    C  
ATOM   2470  C   HIS A 317     -16.266  28.202  33.580  1.00 50.66      A    C  
ANISOU 2470  C   HIS A 317     7240   1601  10409    161   4276   -725  A    C  
ATOM   2471  O   HIS A 317     -16.365  27.724  34.714  1.00 51.18      A    O  
ANISOU 2471  O   HIS A 317     7363   1779  10305    156   4156   -905  A    O  
ATOM   2472  CB  HIS A 317     -18.435  28.944  32.487  1.00 45.29      A    C  
ANISOU 2472  CB  HIS A 317     6498    786   9926    313   4534    -46  A    C  
ATOM   2473  CG  HIS A 317     -19.442  30.027  32.264  1.00 49.69      A    C  
ANISOU 2473  CG  HIS A 317     6981   1178  10719    418   4844    219  A    C  
ATOM   2474  CD2 HIS A 317     -20.628  30.284  32.844  1.00 51.31      A    C  
ANISOU 2474  CD2 HIS A 317     7171   1385  10939    493   4936    369  A    C  
ATOM   2475  ND1 HIS A 317     -19.208  30.996  31.311  1.00 53.25      A    N  
ANISOU 2475  ND1 HIS A 317     7369   1437  11425    477   5119    369  A    N  
ATOM   2476  CE1 HIS A 317     -20.247  31.814  31.341  1.00 53.95      A    C  
ANISOU 2476  CE1 HIS A 317     7414   1412  11673    610   5378    617  A    C  
ATOM   2477  NE2 HIS A 317     -21.124  31.436  32.236  1.00 53.08      A    N  
ANISOU 2477  NE2 HIS A 317     7318   1423  11427    624   5273    625  A    N  
ATOM   2478  N   THR A 318     -15.412  27.728  32.657  1.00 46.33      A    N  
ANISOU 2478  N   THR A 318     6689   1126   9788    148   4145   -713  A    N  
ATOM   2479  CA  THR A 318     -14.498  26.595  32.878  1.00 45.07      A    C  
ANISOU 2479  CA  THR A 318     6596   1179   9349    143   3854   -908  A    C  
ATOM   2480  C   THR A 318     -13.470  26.985  33.950  1.00 50.97      A    C  
ANISOU 2480  C   THR A 318     7282   1977  10108     84   3892  -1355  A    C  
ATOM   2481  O   THR A 318     -13.239  26.196  34.866  1.00 50.53      A    O  
ANISOU 2481  O   THR A 318     7288   2115   9798    126   3698  -1527  A    O  
ATOM   2482  CB  THR A 318     -13.835  26.169  31.557  1.00 46.01      A    C  
ANISOU 2482  CB  THR A 318     6709   1343   9428    146   3754   -783  A    C  
ATOM   2483  CG2 THR A 318     -12.826  25.065  31.736  1.00 39.28      A    C  
ANISOU 2483  CG2 THR A 318     5792    957   8175    106   3477   -897  A    C  
ATOM   2484  OG1 THR A 318     -14.843  25.753  30.642  1.00 43.31      A    O  
ANISOU 2484  OG1 THR A 318     6380   1071   9007    181   3706   -389  A    O  
ATOM   2485  N   VAL A 319     -12.889  28.214  33.851  1.00 48.55      A    N  
ANISOU 2485  N   VAL A 319     6853   1508  10087    -15   4166  -1545  A    N  
ATOM   2486  CA  VAL A 319     -11.928  28.732  34.835  1.00 50.44      A    C  
ANISOU 2486  CA  VAL A 319     6991   1817  10357   -120   4248  -2016  A    C  
ATOM   2487  C   VAL A 319     -12.646  28.845  36.207  1.00 55.76      A    C  
ANISOU 2487  C   VAL A 319     7693   2524  10971   -111   4277  -2142  A    C  
ATOM   2488  O   VAL A 319     -12.049  28.505  37.227  1.00 57.01      A    O  
ANISOU 2488  O   VAL A 319     7817   2917  10926   -119   4148  -2467  A    O  
ATOM   2489  CB  VAL A 319     -11.267  30.074  34.391  1.00 55.79      A    C  
ANISOU 2489  CB  VAL A 319     7548   2268  11383   -270   4599  -2194  A    C  
ATOM   2490  CG1 VAL A 319     -10.580  30.782  35.551  1.00 57.92      A    C  
ANISOU 2490  CG1 VAL A 319     7701   2590  11716   -424   4758  -2702  A    C  
ATOM   2491  CG2 VAL A 319     -10.271  29.838  33.261  1.00 53.99      A    C  
ANISOU 2491  CG2 VAL A 319     7274   2088  11150   -291   4529  -2176  A    C  
ATOM   2492  N   TYR A 320     -13.934  29.239  36.220  1.00 51.01      A    N  
ANISOU 2492  N   TYR A 320     7146   1728  10506    -70   4428  -1868  A    N  
ATOM   2493  CA  TYR A 320     -14.711  29.318  37.455  1.00 50.73      A    C  
ANISOU 2493  CA  TYR A 320     7144   1717  10414    -54   4459  -1952  A    C  
ATOM   2494  C   TYR A 320     -14.870  27.925  38.082  1.00 52.27      A    C  
ANISOU 2494  C   TYR A 320     7449   2191  10222     48   4115  -1922  A    C  
ATOM   2495  O   TYR A 320     -14.568  27.761  39.260  1.00 52.09      A    O  
ANISOU 2495  O   TYR A 320     7417   2338  10038     46   4052  -2208  A    O  
ATOM   2496  CB  TYR A 320     -16.079  29.988  37.218  1.00 52.27      A    C  
ANISOU 2496  CB  TYR A 320     7366   1667  10827     -6   4691  -1626  A    C  
ATOM   2497  CG  TYR A 320     -16.865  30.194  38.492  1.00 54.19      A    C  
ANISOU 2497  CG  TYR A 320     7633   1914  11043      0   4764  -1734  A    C  
ATOM   2498  CD1 TYR A 320     -16.758  31.379  39.220  1.00 59.21      A    C  
ANISOU 2498  CD1 TYR A 320     8201   2379  11916    -99   5082  -2018  A    C  
ATOM   2499  CD2 TYR A 320     -17.685  29.191  38.995  1.00 52.88      A    C  
ANISOU 2499  CD2 TYR A 320     7564   1917  10612     88   4535  -1572  A    C  
ATOM   2500  CE1 TYR A 320     -17.466  31.563  40.409  1.00 61.61      A    C  
ANISOU 2500  CE1 TYR A 320     8525   2697  12186    -96   5152  -2131  A    C  
ATOM   2501  CE2 TYR A 320     -18.373  29.351  40.192  1.00 54.77      A    C  
ANISOU 2501  CE2 TYR A 320     7824   2174  10811     93   4599  -1677  A    C  
ATOM   2502  CZ  TYR A 320     -18.267  30.540  40.892  1.00 65.73      A    C  
ANISOU 2502  CZ  TYR A 320     9136   3408  12431      8   4898  -1952  A    C  
ATOM   2503  OH  TYR A 320     -18.977  30.682  42.052  1.00 66.41      A    O  
ANISOU 2503  OH  TYR A 320     9243   3519  12469     15   4963  -2051  A    O  
ATOM   2504  N   LEU A 321     -15.326  26.932  37.297  1.00 48.83      A    N  
ANISOU 2504  N   LEU A 321     7120   1803   9629    134   3916  -1586  A    N  
ATOM   2505  CA  LEU A 321     -15.491  25.532  37.720  1.00 47.86      A    C  
ANISOU 2505  CA  LEU A 321     7145   1888   9151    228   3633  -1519  A    C  
ATOM   2506  C   LEU A 321     -14.180  24.915  38.220  1.00 49.89      A    C  
ANISOU 2506  C   LEU A 321     7401   2386   9169    275   3449  -1821  A    C  
ATOM   2507  O   LEU A 321     -14.187  24.252  39.259  1.00 48.01      A    O  
ANISOU 2507  O   LEU A 321     7242   2325   8673    360   3321  -1928  A    O  
ATOM   2508  CB  LEU A 321     -16.042  24.676  36.573  1.00 47.07      A    C  
ANISOU 2508  CB  LEU A 321     7148   1775   8963    263   3505  -1146  A    C  
ATOM   2509  CG  LEU A 321     -17.518  24.850  36.193  1.00 53.27      A    C  
ANISOU 2509  CG  LEU A 321     7943   2452   9845    255   3606   -810  A    C  
ATOM   2510  CD1 LEU A 321     -17.927  23.771  35.184  1.00 52.69      A    C  
ANISOU 2510  CD1 LEU A 321     7960   2452   9610    261   3445   -518  A    C  
ATOM   2511  CD2 LEU A 321     -18.446  24.789  37.431  1.00 55.39      A    C  
ANISOU 2511  CD2 LEU A 321     8271   2748  10027    273   3630   -838  A    C  
ATOM   2512  N   GLU A 322     -13.067  25.145  37.482  1.00 46.84      A    N  
ANISOU 2512  N   GLU A 322     6915   2024   8857    237   3447  -1947  A    N  
ATOM   2513  CA  GLU A 322     -11.710  24.687  37.809  1.00 47.95      A    C  
ANISOU 2513  CA  GLU A 322     7002   2429   8787    289   3291  -2243  A    C  
ATOM   2514  C   GLU A 322     -11.310  25.186  39.201  1.00 55.45      A    C  
ANISOU 2514  C   GLU A 322     7836   3560   9673    265   3346  -2636  A    C  
ATOM   2515  O   GLU A 322     -10.874  24.394  40.037  1.00 56.20      A    O  
ANISOU 2515  O   GLU A 322     7966   3942   9446    399   3161  -2772  A    O  
ATOM   2516  CB  GLU A 322     -10.704  25.187  36.742  1.00 49.77      A    C  
ANISOU 2516  CB  GLU A 322     7102   2618   9189    206   3355  -2328  A    C  
ATOM   2517  CG  GLU A 322      -9.232  24.842  36.972  1.00 59.78      A    C  
ANISOU 2517  CG  GLU A 322     8262   4190  10263    248   3217  -2657  A    C  
ATOM   2518  CD  GLU A 322      -8.199  25.705  36.261  1.00 81.24      A    C  
ANISOU 2518  CD  GLU A 322    10789   6879  13201    101   3362  -2874  A    C  
ATOM   2519  OE1 GLU A 322      -8.594  26.628  35.511  1.00 71.72      A    O  
ANISOU 2519  OE1 GLU A 322     9549   5374  12328    -34   3605  -2764  A    O  
ATOM   2520  OE2 GLU A 322      -6.987  25.439  36.432  1.00 77.75      A    O1-
ANISOU 2520  OE2 GLU A 322    10231   6724  12589    134   3245  -3145  A    O1-
ATOM   2521  N   ARG A 323     -11.517  26.491  39.457  1.00 54.18      A    N  
ANISOU 2521  N   ARG A 323     7547   3232   9808    104   3619  -2807  A    N  
ATOM   2522  CA  ARG A 323     -11.165  27.117  40.726  1.00 55.74      A    C  
ANISOU 2522  CA  ARG A 323     7612   3589   9977     30   3717  -3222  A    C  
ATOM   2523  C   ARG A 323     -12.103  26.664  41.869  1.00 57.75      A    C  
ANISOU 2523  C   ARG A 323     7982   3923  10037    131   3647  -3156  A    C  
ATOM   2524  O   ARG A 323     -11.686  26.695  43.028  1.00 58.66      A    O  
ANISOU 2524  O   ARG A 323     8014   4309   9966    144   3612  -3482  A    O  
ATOM   2525  CB  ARG A 323     -11.083  28.638  40.590  1.00 56.92      A    C  
ANISOU 2525  CB  ARG A 323     7618   3489  10519   -193   4077  -3433  A    C  
ATOM   2526  CG  ARG A 323      -9.735  29.076  39.999  1.00 64.73      A    C  
ANISOU 2526  CG  ARG A 323     8439   4549  11604   -321   4141  -3712  A    C  
ATOM   2527  CD  ARG A 323      -9.731  30.525  39.552  1.00 70.22      A    C  
ANISOU 2527  CD  ARG A 323     9052   4896  12733   -540   4548  -3825  A    C  
ATOM   2528  NE  ARG A 323      -8.534  30.837  38.774  1.00 68.91      A    N  
ANISOU 2528  NE  ARG A 323     8756   4762  12665   -661   4610  -4015  A    N  
ATOM   2529  CZ  ARG A 323      -8.367  31.944  38.055  1.00 79.76      A    C  
ANISOU 2529  CZ  ARG A 323    10086   5810  14410   -834   4962  -4051  A    C  
ATOM   2530  NH1 ARG A 323      -9.319  32.863  38.009  1.00 67.04      A    N1+
ANISOU 2530  NH1 ARG A 323     8554   3808  13109   -882   5293  -3899  A    N1+
ATOM   2531  NH2 ARG A 323      -7.247  32.135  37.367  1.00 66.12      A    N  
ANISOU 2531  NH2 ARG A 323     8242   4139  12742   -946   5004  -4230  A    N  
ATOM   2532  N   ARG A 324     -13.309  26.166  41.552  1.00 51.91      A    N  
ANISOU 2532  N   ARG A 324     7421   3000   9302    207   3613  -2750  A    N  
ATOM   2533  CA  ARG A 324     -14.191  25.601  42.569  1.00 51.99      A    C  
ANISOU 2533  CA  ARG A 324     7558   3089   9106    304   3539  -2665  A    C  
ATOM   2534  C   ARG A 324     -13.686  24.200  42.968  1.00 59.25      A    C  
ANISOU 2534  C   ARG A 324     8604   4304   9606    497   3253  -2643  A    C  
ATOM   2535  O   ARG A 324     -13.770  23.843  44.141  1.00 61.54      A    O  
ANISOU 2535  O   ARG A 324     8934   4795   9653    593   3189  -2761  A    O  
ATOM   2536  CB  ARG A 324     -15.646  25.554  42.089  1.00 50.65      A    C  
ANISOU 2536  CB  ARG A 324     7513   2656   9077    300   3618  -2262  A    C  
ATOM   2537  CG  ARG A 324     -16.329  26.913  42.049  1.00 57.07      A    C  
ANISOU 2537  CG  ARG A 324     8223   3204  10255    178   3927  -2267  A    C  
ATOM   2538  CD  ARG A 324     -16.622  27.464  43.425  1.00 66.14      A    C  
ANISOU 2538  CD  ARG A 324     9327   4405  11397    143   4055  -2532  A    C  
ATOM   2539  NE  ARG A 324     -18.011  27.233  43.816  1.00 70.75      A    N  
ANISOU 2539  NE  ARG A 324    10020   4908  11955    197   4083  -2271  A    N  
ATOM   2540  CZ  ARG A 324     -18.409  26.252  44.612  1.00 74.39      A    C  
ANISOU 2540  CZ  ARG A 324    10610   5548  12108    294   3905  -2212  A    C  
ATOM   2541  NH1 ARG A 324     -17.526  25.395  45.112  1.00 51.56      A    N1+
ANISOU 2541  NH1 ARG A 324     7765   2927   8898    385   3689  -2371  A    N1+
ATOM   2542  NH2 ARG A 324     -19.692  26.119  44.919  1.00 63.61      A    N  
ANISOU 2542  NH2 ARG A 324     9327   4100  10744    316   3959  -1985  A    N  
ATOM   2543  N   ILE A 325     -13.100  23.436  42.001  1.00 55.12      A    N  
ANISOU 2543  N   ILE A 325     8142   3809   8992    569   3102  -2500  A    N  
ATOM   2544  CA  ILE A 325     -12.501  22.107  42.228  1.00 55.14      A    C  
ANISOU 2544  CA  ILE A 325     8281   4057   8613    780   2867  -2461  A    C  
ATOM   2545  C   ILE A 325     -11.251  22.310  43.099  1.00 63.71      A    C  
ANISOU 2545  C   ILE A 325     9184   5517   9506    853   2805  -2871  A    C  
ATOM   2546  O   ILE A 325     -11.030  21.534  44.022  1.00 65.21      A    O  
ANISOU 2546  O   ILE A 325     9451   5975   9351   1053   2675  -2917  A    O  
ATOM   2547  CB  ILE A 325     -12.217  21.334  40.889  1.00 55.97      A    C  
ANISOU 2547  CB  ILE A 325     8495   4065   8705    819   2760  -2212  A    C  
ATOM   2548  CG1 ILE A 325     -13.540  20.983  40.160  1.00 53.62      A    C  
ANISOU 2548  CG1 ILE A 325     8371   3487   8514    751   2802  -1823  A    C  
ATOM   2549  CG2 ILE A 325     -11.343  20.056  41.096  1.00 56.53      A    C  
ANISOU 2549  CG2 ILE A 325     8691   4391   8397   1059   2555  -2220  A    C  
ATOM   2550  CD1 ILE A 325     -13.396  20.677  38.680  1.00 56.40      A    C  
ANISOU 2550  CD1 ILE A 325     8756   3709   8966    701   2768  -1612  A    C  
ATOM   2551  N   ASP A 326     -10.512  23.411  42.871  1.00 63.63      A    N  
ANISOU 2551  N   ASP A 326     8925   5534   9719    683   2928  -3176  A    N  
ATOM   2552  CA  ASP A 326      -9.348  23.813  43.669  1.00 67.58      A    C  
ANISOU 2552  CA  ASP A 326     9184   6420  10073    680   2908  -3635  A    C  
ATOM   2553  C   ASP A 326      -9.762  24.154  45.102  1.00 78.25      A    C  
ANISOU 2553  C   ASP A 326    10484   7938  11308    676   2969  -3852  A    C  
ATOM   2554  O   ASP A 326      -8.967  23.972  46.025  1.00 81.04      A    O  
ANISOU 2554  O   ASP A 326    10697   8729  11367    777   2872  -4159  A    O  
ATOM   2555  CB  ASP A 326      -8.632  25.023  43.036  1.00 69.93      A    C  
ANISOU 2555  CB  ASP A 326     9241   6630  10697    427   3095  -3913  A    C  
ATOM   2556  CG  ASP A 326      -7.447  24.695  42.141  1.00 77.80      A    C  
ANISOU 2556  CG  ASP A 326    10152   7765  11645    463   2984  -3959  A    C  
ATOM   2557  OD1 ASP A 326      -7.062  23.501  42.066  1.00 78.83      A    O  
ANISOU 2557  OD1 ASP A 326    10392   8103  11456    710   2748  -3809  A    O  
ATOM   2558  OD2 ASP A 326      -6.904  25.627  41.513  1.00 80.83      A    O1-
ANISOU 2558  OD2 ASP A 326    10369   8035  12308    250   3155  -4145  A    O1-
ATOM   2559  N   GLY A 327     -10.996  24.651  45.256  1.00 76.24      A    N  
ANISOU 2559  N   GLY A 327    10330   7365  11275    569   3132  -3691  A    N  
ATOM   2560  CA  GLY A 327     -11.595  25.017  46.533  1.00 78.04      A    C  
ANISOU 2560  CA  GLY A 327    10537   7680  11434    550   3219  -3851  A    C  
ATOM   2561  C   GLY A 327     -11.822  23.810  47.415  1.00 84.78      A    C  
ANISOU 2561  C   GLY A 327    11561   8791  11862    818   3017  -3712  A    C  
ATOM   2562  O   GLY A 327     -11.312  23.762  48.537  1.00 86.40      A    O  
ANISOU 2562  O   GLY A 327    11656   9379  11792    904   2964  -3997  A    O  
ATOM   2563  N   ARG A 328     -12.542  22.795  46.891  1.00 81.98      A    N  
ANISOU 2563  N   ARG A 328    11474   8245  11430    952   2916  -3279  A    N  
ATOM   2564  CA  ARG A 328     -12.811  21.541  47.606  1.00 82.95      A    C  
ANISOU 2564  CA  ARG A 328    11819   8536  11162   1212   2766  -3091  A    C  
ATOM   2565  C   ARG A 328     -11.489  20.756  47.819  1.00 89.43      A    C  
ANISOU 2565  C   ARG A 328    12600   9769  11610   1464   2571  -3216  A    C  
ATOM   2566  O   ARG A 328     -11.410  19.915  48.719  1.00 90.13      A    O  
ANISOU 2566  O   ARG A 328    12812  10113  11321   1723   2470  -3164  A    O  
ATOM   2567  CB  ARG A 328     -13.876  20.699  46.857  1.00 81.66      A    C  
ANISOU 2567  CB  ARG A 328    11949   8027  11052   1230   2758  -2628  A    C  
ATOM   2568  CG  ARG A 328     -14.493  19.487  47.608  1.00 93.29      A    C  
ANISOU 2568  CG  ARG A 328    13706   9556  12184   1444   2686  -2395  A    C  
ATOM   2569  CD  ARG A 328     -14.701  19.634  49.119  1.00105.05      A    C  
ANISOU 2569  CD  ARG A 328    15172  11285  13456   1537   2714  -2564  A    C  
ATOM   2570  NE  ARG A 328     -15.658  20.680  49.483  1.00113.62      A    N  
ANISOU 2570  NE  ARG A 328    16158  12198  14813   1319   2888  -2639  A    N  
ATOM   2571  CZ  ARG A 328     -15.689  21.290  50.666  1.00129.45      A    C  
ANISOU 2571  CZ  ARG A 328    18029  14410  16746   1308   2953  -2914  A    C  
ATOM   2572  NH1 ARG A 328     -14.800  20.981  51.604  1.00117.21      A    N1+
ANISOU 2572  NH1 ARG A 328    16399  13292  14844   1499   2844  -3151  A    N1+
ATOM   2573  NH2 ARG A 328     -16.599  22.221  50.916  1.00116.58      A    N  
ANISOU 2573  NH2 ARG A 328    16332  12582  15384   1116   3134  -2958  A    N  
ATOM   2574  N   LEU A 329     -10.441  21.094  47.044  1.00 87.07      A    N  
ANISOU 2574  N   LEU A 329    12115   9557  11412   1401   2537  -3389  A    N  
ATOM   2575  CA  LEU A 329      -9.131  20.468  47.168  1.00 89.19      A    C  
ANISOU 2575  CA  LEU A 329    12296  10244  11348   1636   2363  -3526  A    C  
ATOM   2576  C   LEU A 329      -8.280  21.163  48.260  1.00 97.26      A    C  
ANISOU 2576  C   LEU A 329    12991  11772  12190   1632   2355  -4015  A    C  
ATOM   2577  O   LEU A 329      -8.405  20.827  49.442  1.00 98.51      A    O  
ANISOU 2577  O   LEU A 329    13166  12246  12016   1826   2297  -4077  A    O  
ATOM   2578  CB  LEU A 329      -8.404  20.467  45.814  1.00 88.10      A    C  
ANISOU 2578  CB  LEU A 329    12108   9982  11386   1568   2330  -3478  A    C  
ATOM   2579  CG  LEU A 329      -8.178  19.099  45.202  1.00 92.06      A    C  
ANISOU 2579  CG  LEU A 329    12865  10451  11665   1831   2185  -3146  A    C  
ATOM   2580  CD1 LEU A 329      -8.774  19.017  43.816  1.00 89.41      A    C  
ANISOU 2580  CD1 LEU A 329    12696   9641  11634   1666   2244  -2833  A    C  
ATOM   2581  CD2 LEU A 329      -6.703  18.761  45.166  1.00 97.04      A    C  
ANISOU 2581  CD2 LEU A 329    13322  11494  12052   2022   2046  -3343  A    C  
ATOM   2582  N   TYR A 330      -7.461  22.154  47.857  1.00 95.14      A    N  
ANISOU 2582  N   TYR A 330    12425  11581  12142   1394   2435  -4368  A    N  
ATOM   2583  CA  TYR A 330      -6.486  22.895  48.664  1.00 98.36      A    C  
ANISOU 2583  CA  TYR A 330    12470  12489  12413   1315   2449  -4901  A    C  
ATOM   2584  C   TYR A 330      -7.074  23.901  49.681  1.00102.25      A    C  
ANISOU 2584  C   TYR A 330    12842  12996  13012   1099   2629  -5194  A    C  
ATOM   2585  O   TYR A 330      -6.333  24.353  50.559  1.00105.21      A    O  
ANISOU 2585  O   TYR A 330    12933  13868  13176   1066   2622  -5643  A    O  
ATOM   2586  CB  TYR A 330      -5.508  23.636  47.734  1.00100.76      A    C  
ANISOU 2586  CB  TYR A 330    12526  12791  12968   1080   2520  -5166  A    C  
ATOM   2587  CG  TYR A 330      -4.979  22.779  46.602  1.00101.81      A    C  
ANISOU 2587  CG  TYR A 330    12773  12853  13058   1249   2374  -4886  A    C  
ATOM   2588  CD1 TYR A 330      -3.892  21.929  46.792  1.00105.67      A    C  
ANISOU 2588  CD1 TYR A 330    13161  13849  13140   1545   2164  -4960  A    C  
ATOM   2589  CD2 TYR A 330      -5.573  22.808  45.343  1.00 99.88      A    C  
ANISOU 2589  CD2 TYR A 330    12728  12059  13162   1129   2452  -4543  A    C  
ATOM   2590  CE1 TYR A 330      -3.410  21.128  45.756  1.00105.37      A    C  
ANISOU 2590  CE1 TYR A 330    13239  13731  13066   1707   2049  -4706  A    C  
ATOM   2591  CE2 TYR A 330      -5.098  22.013  44.300  1.00 99.52      A    C  
ANISOU 2591  CE2 TYR A 330    12788  11953  13071   1270   2328  -4302  A    C  
ATOM   2592  CZ  TYR A 330      -4.014  21.177  44.509  1.00109.52      A    C  
ANISOU 2592  CZ  TYR A 330    13972  13689  13953   1553   2132  -4388  A    C  
ATOM   2593  OH  TYR A 330      -3.539  20.403  43.474  1.00110.45      A    O  
ANISOU 2593  OH  TYR A 330    14202  13733  14033   1694   2029  -4159  A    O  
ATOM   2594  N   GLY A 331      -8.360  24.240  49.565  1.00 95.32      A    N  
ANISOU 2594  N   GLY A 331    12161  11619  12439    956   2790  -4960  A    N  
ATOM   2595  CA  GLY A 331      -9.010  25.183  50.475  1.00 95.47      A    C  
ANISOU 2595  CA  GLY A 331    12098  11588  12588    759   2988  -5201  A    C  
ATOM   2596  C   GLY A 331      -9.424  26.506  49.859  1.00 96.42      A    C  
ANISOU 2596  C   GLY A 331    12151  11248  13238    396   3291  -5314  A    C  
ATOM   2597  O   GLY A 331      -8.841  26.947  48.865  1.00 95.37      A    O  
ANISOU 2597  O   GLY A 331    11925  10961  13351    246   3365  -5373  A    O  
ATOM   2598  N   GLU A 332     -10.419  27.162  50.486  1.00 92.44      A    N  
ANISOU 2598  N   GLU A 332    11693  10527  12903    267   3489  -5347  A    N  
ATOM   2599  CA  GLU A 332     -11.005  28.444  50.080  1.00 91.22      A    C  
ANISOU 2599  CA  GLU A 332    11512   9906  13243    -33   3828  -5421  A    C  
ATOM   2600  C   GLU A 332      -9.954  29.563  49.988  1.00 96.16      A    C  
ANISOU 2600  C   GLU A 332    11850  10633  14055   -324   4033  -5950  A    C  
ATOM   2601  O   GLU A 332     -10.094  30.429  49.127  1.00 94.99      A    O  
ANISOU 2601  O   GLU A 332    11705  10054  14332   -531   4292  -5924  A    O  
ATOM   2602  CB  GLU A 332     -12.145  28.825  51.036  1.00 92.98      A    C  
ANISOU 2602  CB  GLU A 332    11815  10002  13511    -66   3981  -5416  A    C  
ATOM   2603  CG  GLU A 332     -13.004  30.020  50.626  1.00103.35      A    C  
ANISOU 2603  CG  GLU A 332    13164  10781  15325   -297   4346  -5376  A    C  
ATOM   2604  CD  GLU A 332     -13.673  30.045  49.260  1.00112.10      A    C  
ANISOU 2604  CD  GLU A 332    14440  11390  16762   -281   4420  -4894  A    C  
ATOM   2605  OE1 GLU A 332     -13.842  28.968  48.643  1.00 96.68      A    O  
ANISOU 2605  OE1 GLU A 332    12643   9440  14650    -84   4172  -4494  A    O  
ATOM   2606  OE2 GLU A 332     -14.066  31.152  48.824  1.00 98.88      A    O1-
ANISOU 2606  OE2 GLU A 332    12746   9323  15499   -461   4748  -4915  A    O1-
ATOM   2607  N   GLU A 333      -8.894  29.525  50.829  1.00 94.80      A    N  
ANISOU 2607  N   GLU A 333    11426  11041  13553   -333   3927  -6419  A    N  
ATOM   2608  CA  GLU A 333      -7.811  30.521  50.797  1.00 97.15      A    C  
ANISOU 2608  CA  GLU A 333    11418  11516  13979   -640   4116  -6984  A    C  
ATOM   2609  C   GLU A 333      -7.000  30.435  49.500  1.00 98.16      A    C  
ANISOU 2609  C   GLU A 333    11506  11533  14257   -676   4080  -6893  A    C  
ATOM   2610  O   GLU A 333      -6.591  31.474  48.980  1.00 98.34      A    O  
ANISOU 2610  O   GLU A 333    11406  11330  14628   -985   4369  -7161  A    O  
ATOM   2611  CB  GLU A 333      -6.871  30.380  52.001  1.00102.09      A    C  
ANISOU 2611  CB  GLU A 333    11751  12892  14145   -614   3970  -7495  A    C  
ATOM   2612  CG  GLU A 333      -7.455  30.912  53.298  1.00113.31      A    C  
ANISOU 2612  CG  GLU A 333    13116  14439  15498   -722   4121  -7790  A    C  
ATOM   2613  CD  GLU A 333      -8.276  29.934  54.117  1.00131.96      A    C  
ANISOU 2613  CD  GLU A 333    15687  16910  17543   -394   3913  -7440  A    C  
ATOM   2614  OE1 GLU A 333      -8.505  30.232  55.312  1.00130.78      A    O  
ANISOU 2614  OE1 GLU A 333    15453  16992  17246   -453   3994  -7724  A    O  
ATOM   2615  OE2 GLU A 333      -8.689  28.878  53.581  1.00120.93      A    O1-
ANISOU 2615  OE2 GLU A 333    14540  15367  16040    -93   3690  -6900  A    O1-
ATOM   2616  N   PHE A 334      -6.785  29.204  48.976  1.00 92.28      A    N  
ANISOU 2616  N   PHE A 334    10883  10923  13257   -364   3753  -6515  A    N  
ATOM   2617  CA  PHE A 334      -6.068  28.937  47.722  1.00 90.56      A    C  
ANISOU 2617  CA  PHE A 334    10656  10615  13137   -348   3679  -6369  A    C  
ATOM   2618  C   PHE A 334      -6.926  29.366  46.526  1.00 88.97      A    C  
ANISOU 2618  C   PHE A 334    10673   9725  13407   -454   3883  -5969  A    C  
ATOM   2619  O   PHE A 334      -6.399  29.909  45.547  1.00 88.60      A    O  
ANISOU 2619  O   PHE A 334    10556   9477  13633   -624   4029  -6023  A    O  
ATOM   2620  CB  PHE A 334      -5.689  27.445  47.618  1.00 91.30      A    C  
ANISOU 2620  CB  PHE A 334    10848  11038  12802     40   3294  -6069  A    C  
ATOM   2621  CG  PHE A 334      -4.952  27.062  46.355  1.00 92.02      A    C  
ANISOU 2621  CG  PHE A 334    10940  11064  12959     83   3200  -5912  A    C  
ATOM   2622  CD1 PHE A 334      -3.586  27.314  46.217  1.00 98.15      A    C  
ANISOU 2622  CD1 PHE A 334    11413  12233  13645    -14   3180  -6320  A    C  
ATOM   2623  CD2 PHE A 334      -5.616  26.440  45.308  1.00 91.05      A    C  
ANISOU 2623  CD2 PHE A 334    11103  10521  12972    210   3136  -5376  A    C  
ATOM   2624  CE1 PHE A 334      -2.901  26.960  45.042  1.00 97.86      A    C  
ANISOU 2624  CE1 PHE A 334    11376  12136  13669     26   3100  -6174  A    C  
ATOM   2625  CE2 PHE A 334      -4.930  26.085  44.139  1.00 92.96      A    C  
ANISOU 2625  CE2 PHE A 334    11344  10712  13266    245   3055  -5242  A    C  
ATOM   2626  CZ  PHE A 334      -3.579  26.346  44.015  1.00 93.40      A    C  
ANISOU 2626  CZ  PHE A 334    11113  11133  13243    161   3037  -5633  A    C  
ATOM   2627  N   ARG A 335      -8.252  29.123  46.619  1.00 81.13      A    N  
ANISOU 2627  N   ARG A 335     9933   8403  12491   -343   3898  -5568  A    N  
ATOM   2628  CA  ARG A 335      -9.234  29.497  45.603  1.00 77.57      A    C  
ANISOU 2628  CA  ARG A 335     9675   7364  12436   -399   4082  -5159  A    C  
ATOM   2629  C   ARG A 335      -9.207  31.017  45.400  1.00 82.86      A    C  
ANISOU 2629  C   ARG A 335    10231   7705  13546   -718   4504  -5433  A    C  
ATOM   2630  O   ARG A 335      -9.123  31.485  44.262  1.00 82.42      A    O  
ANISOU 2630  O   ARG A 335    10204   7311  13802   -812   4669  -5279  A    O  
ATOM   2631  CB  ARG A 335     -10.633  29.013  46.009  1.00 72.69      A    C  
ANISOU 2631  CB  ARG A 335     9287   6570  11762   -240   4030  -4777  A    C  
ATOM   2632  CG  ARG A 335     -11.692  29.328  44.973  1.00 73.48      A    C  
ANISOU 2632  CG  ARG A 335     9555   6148  12216   -264   4195  -4337  A    C  
ATOM   2633  CD  ARG A 335     -13.059  28.784  45.328  1.00 76.45      A    C  
ANISOU 2633  CD  ARG A 335    10132   6405  12512   -117   4129  -3971  A    C  
ATOM   2634  NE  ARG A 335     -14.079  29.438  44.507  1.00 85.78      A    N  
ANISOU 2634  NE  ARG A 335    11399   7136  14057   -171   4357  -3640  A    N  
ATOM   2635  CZ  ARG A 335     -14.854  30.446  44.909  1.00 97.02      A    C  
ANISOU 2635  CZ  ARG A 335    12810   8309  15744   -271   4658  -3684  A    C  
ATOM   2636  NH1 ARG A 335     -14.771  30.906  46.151  1.00 91.67      A    N1+
ANISOU 2636  NH1 ARG A 335    12047   7770  15012   -357   4768  -4065  A    N1+
ATOM   2637  NH2 ARG A 335     -15.724  30.994  44.072  1.00 73.44      A    N  
ANISOU 2637  NH2 ARG A 335     9890   4951  13062   -269   4859  -3344  A    N  
ATOM   2638  N   GLN A 336      -9.220  31.771  46.518  1.00 80.75      A    N  
ANISOU 2638  N   GLN A 336     9840   7552  13290   -883   4693  -5854  A    N  
ATOM   2639  CA  GLN A 336      -9.170  33.234  46.571  1.00 82.31      A    C  
ANISOU 2639  CA  GLN A 336     9940   7453  13882  -1205   5145  -6197  A    C  
ATOM   2640  C   GLN A 336      -7.865  33.757  45.975  1.00 87.39      A    C  
ANISOU 2640  C   GLN A 336    10380   8180  14643  -1433   5270  -6560  A    C  
ATOM   2641  O   GLN A 336      -7.884  34.794  45.315  1.00 86.45      A    O  
ANISOU 2641  O   GLN A 336    10277   7628  14942  -1648   5651  -6605  A    O  
ATOM   2642  CB  GLN A 336      -9.307  33.718  48.023  1.00 86.13      A    C  
ANISOU 2642  CB  GLN A 336    10312   8162  14253  -1329   5266  -6637  A    C  
ATOM   2643  CG  GLN A 336     -10.698  33.536  48.646  1.00 84.29      A    C  
ANISOU 2643  CG  GLN A 336    10274   7747  14005  -1173   5268  -6330  A    C  
ATOM   2644  CD  GLN A 336     -11.738  34.511  48.152  1.00 94.28      A    C  
ANISOU 2644  CD  GLN A 336    11692   8386  15744  -1263   5662  -6093  A    C  
ATOM   2645  NE2 GLN A 336     -12.972  34.048  48.032  1.00 77.63      A    N  
ANISOU 2645  NE2 GLN A 336     9786   6070  13639  -1048   5579  -5598  A    N  
ATOM   2646  OE1 GLN A 336     -11.462  35.691  47.912  1.00 91.32      A    O  
ANISOU 2646  OE1 GLN A 336    11254   7717  15726  -1519   6064  -6357  A    O  
ATOM   2647  N   PHE A 337      -6.740  33.024  46.191  1.00 85.96      A    N  
ANISOU 2647  N   PHE A 337    10013   8560  14087  -1367   4963  -6801  A    N  
ATOM   2648  CA  PHE A 337      -5.415  33.380  45.688  1.00 88.32      A    C  
ANISOU 2648  CA  PHE A 337    10082   9044  14430  -1570   5032  -7171  A    C  
ATOM   2649  C   PHE A 337      -5.340  33.186  44.182  1.00 90.53      A    C  
ANISOU 2649  C   PHE A 337    10495   8974  14930  -1503   5024  -6753  A    C  
ATOM   2650  O   PHE A 337      -4.774  34.048  43.505  1.00 91.90      A    O  
ANISOU 2650  O   PHE A 337    10583   8923  15411  -1758   5319  -6946  A    O  
ATOM   2651  CB  PHE A 337      -4.303  32.584  46.397  1.00 92.26      A    C  
ANISOU 2651  CB  PHE A 337    10330  10303  14421  -1462   4685  -7511  A    C  
ATOM   2652  CG  PHE A 337      -2.890  32.863  45.885  1.00 96.73      A    C  
ANISOU 2652  CG  PHE A 337    10625  11141  14989  -1658   4724  -7901  A    C  
ATOM   2653  CD1 PHE A 337      -2.316  34.127  46.018  1.00104.12      A    C  
ANISOU 2653  CD1 PHE A 337    11346  12028  16185  -2087   5118  -8465  A    C  
ATOM   2654  CD2 PHE A 337      -2.140  31.864  45.260  1.00 98.19      A    C  
ANISOU 2654  CD2 PHE A 337    10772  11618  14918  -1425   4393  -7714  A    C  
ATOM   2655  CE1 PHE A 337      -1.019  34.386  45.530  1.00107.35      A    C  
ANISOU 2655  CE1 PHE A 337    11493  12698  16595  -2293   5170  -8842  A    C  
ATOM   2656  CE2 PHE A 337      -0.844  32.126  44.776  1.00103.41      A    C  
ANISOU 2656  CE2 PHE A 337    11167  12547  15577  -1605   4433  -8076  A    C  
ATOM   2657  CZ  PHE A 337      -0.293  33.385  44.915  1.00105.13      A    C  
ANISOU 2657  CZ  PHE A 337    11159  12734  16051  -2045   4817  -8641  A    C  
ATOM   2658  N   LYS A 338      -5.918  32.079  43.649  1.00 83.25      A    N  
ANISOU 2658  N   LYS A 338     9783   7996  13851  -1179   4712  -6194  A    N  
ATOM   2659  CA  LYS A 338      -5.930  31.829  42.209  1.00 80.27      A    C  
ANISOU 2659  CA  LYS A 338     9538   7313  13650  -1101   4685  -5775  A    C  
ATOM   2660  C   LYS A 338      -6.820  32.878  41.518  1.00 83.86      A    C  
ANISOU 2660  C   LYS A 338    10134   7138  14589  -1237   5085  -5541  A    C  
ATOM   2661  O   LYS A 338      -6.501  33.307  40.408  1.00 82.72      A    O  
ANISOU 2661  O   LYS A 338     9999   6727  14704  -1326   5255  -5432  A    O  
ATOM   2662  CB  LYS A 338      -6.372  30.394  41.887  1.00 79.11      A    C  
ANISOU 2662  CB  LYS A 338     9584   7268  13208   -753   4289  -5279  A    C  
ATOM   2663  CG  LYS A 338      -5.245  29.366  41.994  1.00 86.59      A    C  
ANISOU 2663  CG  LYS A 338    10417   8738  13747   -585   3941  -5406  A    C  
ATOM   2664  CD  LYS A 338      -4.514  29.130  40.663  1.00 91.25      A    C  
ANISOU 2664  CD  LYS A 338    10998   9251  14423   -579   3891  -5256  A    C  
ATOM   2665  CE  LYS A 338      -3.877  27.745  40.604  1.00104.47      A    C  
ANISOU 2665  CE  LYS A 338    12682  11337  15676   -292   3506  -5152  A    C  
ATOM   2666  NZ  LYS A 338      -3.461  27.347  39.230  1.00114.05      A    N1+
ANISOU 2666  NZ  LYS A 338    13948  12416  16969   -249   3441  -4908  A    N1+
ATOM   2667  N   ALA A 339      -7.887  33.340  42.219  1.00 81.18      A    N  
ANISOU 2667  N   ALA A 339     9895   6582  14368  -1245   5259  -5485  A    N  
ATOM   2668  CA  ALA A 339      -8.800  34.406  41.779  1.00 81.67      A    C  
ANISOU 2668  CA  ALA A 339    10086   6076  14868  -1336   5675  -5281  A    C  
ATOM   2669  C   ALA A 339      -8.070  35.745  41.645  1.00 87.84      A    C  
ANISOU 2669  C   ALA A 339    10742   6638  15995  -1669   6138  -5713  A    C  
ATOM   2670  O   ALA A 339      -8.305  36.473  40.677  1.00 87.11      A    O  
ANISOU 2670  O   ALA A 339    10745   6085  16265  -1719   6459  -5487  A    O  
ATOM   2671  CB  ALA A 339      -9.950  34.555  42.768  1.00 82.69      A    C  
ANISOU 2671  CB  ALA A 339    10312   6124  14984  -1270   5738  -5216  A    C  
ATOM   2672  N   LEU A 340      -7.192  36.063  42.623  1.00 87.08      A    N  
ANISOU 2672  N   LEU A 340    10428   6887  15770  -1898   6188  -6338  A    N  
ATOM   2673  CA  LEU A 340      -6.399  37.292  42.666  1.00 90.54      A    C  
ANISOU 2673  CA  LEU A 340    10719   7188  16495  -2276   6637  -6864  A    C  
ATOM   2674  C   LEU A 340      -5.262  37.245  41.641  1.00 93.44      A    C  
ANISOU 2674  C   LEU A 340    10975   7623  16904  -2374   6618  -6938  A    C  
ATOM   2675  O   LEU A 340      -4.962  38.277  41.038  1.00 94.75      A    O  
ANISOU 2675  O   LEU A 340    11148   7408  17446  -2616   7060  -7068  A    O  
ATOM   2676  CB  LEU A 340      -5.856  37.549  44.080  1.00 94.09      A    C  
ANISOU 2676  CB  LEU A 340    10940   8073  16737  -2498   6662  -7533  A    C  
ATOM   2677  CG  LEU A 340      -4.991  38.814  44.327  1.00103.96      A    C  
ANISOU 2677  CG  LEU A 340    12005   9248  18247  -2959   7149  -8198  A    C  
ATOM   2678  CD1 LEU A 340      -5.652  40.083  43.832  1.00105.60      A    C  
ANISOU 2678  CD1 LEU A 340    12418   8701  19003  -3117   7749  -8072  A    C  
ATOM   2679  CD2 LEU A 340      -4.762  39.000  45.771  1.00109.19      A    C  
ANISOU 2679  CD2 LEU A 340    12467  10339  18681  -3141   7158  -8787  A    C  
ATOM   2680  N   GLY A 341      -4.672  36.062  41.442  1.00 87.24      A    N  
ANISOU 2680  N   GLY A 341    10107   7297  15741  -2176   6138  -6840  A    N  
ATOM   2681  CA  GLY A 341      -3.632  35.822  40.449  1.00 86.71      A    C  
ANISOU 2681  CA  GLY A 341     9940   7344  15661  -2212   6052  -6855  A    C  
ATOM   2682  C   GLY A 341      -4.184  35.965  39.045  1.00 89.11      A    C  
ANISOU 2682  C   GLY A 341    10467   7119  16272  -2103   6191  -6294  A    C  
ATOM   2683  O   GLY A 341      -3.452  36.336  38.123  1.00 89.31      A    O  
ANISOU 2683  O   GLY A 341    10438   7023  16473  -2238   6353  -6344  A    O  
ATOM   2684  N   GLY A 342      -5.482  35.684  38.898  1.00 84.22      A    N  
ANISOU 2684  N   GLY A 342    10082   6217  15702  -1861   6134  -5768  A    N  
ATOM   2685  CA  GLY A 342      -6.203  35.820  37.640  1.00 82.53      A    C  
ANISOU 2685  CA  GLY A 342    10068   5546  15742  -1721   6259  -5198  A    C  
ATOM   2686  C   GLY A 342      -6.303  37.271  37.217  1.00 89.85      A    C  
ANISOU 2686  C   GLY A 342    11046   5947  17147  -1937   6852  -5266  A    C  
ATOM   2687  O   GLY A 342      -6.018  37.614  36.063  1.00 89.52      A    O  
ANISOU 2687  O   GLY A 342    11050   5647  17318  -1957   7034  -5065  A    O  
ATOM   2688  N   TRP A 343      -6.641  38.149  38.187  1.00 89.35      A    N  
ANISOU 2688  N   TRP A 343    10977   5724  17249  -2109   7185  -5579  A    N  
ATOM   2689  CA  TRP A 343      -6.724  39.593  37.995  1.00 92.45      A    C  
ANISOU 2689  CA  TRP A 343    11436   5590  18102  -2337   7821  -5718  A    C  
ATOM   2690  C   TRP A 343      -5.385  40.130  37.473  1.00 98.43      A    C  
ANISOU 2690  C   TRP A 343    12052   6344  19004  -2642   8061  -6116  A    C  
ATOM   2691  O   TRP A 343      -5.372  40.938  36.546  1.00100.12      A    O  
ANISOU 2691  O   TRP A 343    12379   6088  19574  -2705   8482  -5942  A    O  
ATOM   2692  CB  TRP A 343      -7.117  40.280  39.312  1.00 94.34      A    C  
ANISOU 2692  CB  TRP A 343    11655   5777  18412  -2506   8080  -6114  A    C  
ATOM   2693  CG  TRP A 343      -7.318  41.762  39.190  1.00 99.47      A    C  
ANISOU 2693  CG  TRP A 343    12417   5831  19546  -2721   8780  -6241  A    C  
ATOM   2694  CD1 TRP A 343      -6.388  42.739  39.382  1.00106.59      A    C  
ANISOU 2694  CD1 TRP A 343    13217   6609  20674  -3126   9231  -6825  A    C  
ATOM   2695  CD2 TRP A 343      -8.536  42.427  38.861  1.00 99.91      A    C  
ANISOU 2695  CD2 TRP A 343    12714   5336  19913  -2534   9137  -5776  A    C  
ATOM   2696  CE2 TRP A 343      -8.275  43.814  38.879  1.00108.47      A    C  
ANISOU 2696  CE2 TRP A 343    13860   5936  21417  -2822   9824  -6090  A    C  
ATOM   2697  CE3 TRP A 343      -9.833  41.985  38.555  1.00 98.47      A    C  
ANISOU 2697  CE3 TRP A 343    12692   5038  19684  -2150   8957  -5128  A    C  
ATOM   2698  NE1 TRP A 343      -6.949  43.973  39.178  1.00109.33      A    N  
ANISOU 2698  NE1 TRP A 343    13760   6307  21472  -3204   9874  -6742  A    N  
ATOM   2699  CZ2 TRP A 343      -9.250  44.760  38.562  1.00109.51      A    C  
ANISOU 2699  CZ2 TRP A 343    14229   5453  21926  -2691  10341  -5734  A    C  
ATOM   2700  CZ3 TRP A 343     -10.807  42.926  38.273  1.00101.51      A    C  
ANISOU 2700  CZ3 TRP A 343    13272   4875  20422  -2027   9439  -4796  A    C  
ATOM   2701  CH2 TRP A 343     -10.514  44.294  38.281  1.00106.59      A    C  
ANISOU 2701  CH2 TRP A 343    13992   5025  21481  -2274  10125  -5081  A    C  
ATOM   2702  N   LYS A 344      -4.263  39.646  38.040  1.00 94.76      A    N  
ANISOU 2702  N   LYS A 344    11334   6427  18244  -2810   7792  -6627  A    N  
ATOM   2703  CA  LYS A 344      -2.921  40.062  37.641  1.00 96.73      A    C  
ANISOU 2703  CA  LYS A 344    11397   6780  18575  -3120   7976  -7069  A    C  
ATOM   2704  C   LYS A 344      -2.565  39.571  36.230  1.00 97.01      A    C  
ANISOU 2704  C   LYS A 344    11484   6757  18618  -2960   7819  -6654  A    C  
ATOM   2705  O   LYS A 344      -1.877  40.299  35.506  1.00 98.68      A    O  
ANISOU 2705  O   LYS A 344    11667   6733  19093  -3188   8180  -6804  A    O  
ATOM   2706  CB  LYS A 344      -1.873  39.600  38.661  1.00100.92      A    C  
ANISOU 2706  CB  LYS A 344    11608   8008  18730  -3295   7688  -7706  A    C  
ATOM   2707  CG  LYS A 344      -1.792  40.481  39.914  1.00119.74      A    C  
ANISOU 2707  CG  LYS A 344    13870  10439  21188  -3629   8021  -8331  A    C  
ATOM   2708  CD  LYS A 344      -0.966  41.758  39.715  1.00132.96      A    C  
ANISOU 2708  CD  LYS A 344    15451  11840  23228  -4108   8629  -8857  A    C  
ATOM   2709  CE  LYS A 344      -1.144  42.720  40.868  1.00146.27      A    C  
ANISOU 2709  CE  LYS A 344    17075  13457  25043  -4442   9032  -9424  A    C  
ATOM   2710  NZ  LYS A 344      -0.513  44.038  40.597  1.00152.43      A    N1+
ANISOU 2710  NZ  LYS A 344    18021  14126  25770  -4552   9043  -9299  A    N1+
ATOM   2711  N   GLU A 345      -3.047  38.367  35.833  1.00 86.88      A    N  
ANISOU 2711  N   GLU A 345    10285   5672  17053  -2587   7313  -6147  A    N  
ATOM   2712  CA  GLU A 345      -2.809  37.828  34.500  1.00 83.27      A    C  
ANISOU 2712  CA  GLU A 345     9888   5175  16575  -2415   7140  -5728  A    C  
ATOM   2713  C   GLU A 345      -3.627  38.622  33.472  1.00 86.17      A    C  
ANISOU 2713  C   GLU A 345    10490   4915  17337  -2337   7547  -5238  A    C  
ATOM   2714  O   GLU A 345      -3.158  38.864  32.362  1.00 85.40      A    O  
ANISOU 2714  O   GLU A 345    10416   4637  17397  -2368   7704  -5086  A    O  
ATOM   2715  CB  GLU A 345      -3.131  36.323  34.448  1.00 80.45      A    C  
ANISOU 2715  CB  GLU A 345     9567   5198  15803  -2066   6525  -5369  A    C  
ATOM   2716  CG  GLU A 345      -2.590  35.590  33.228  1.00 87.39      A    C  
ANISOU 2716  CG  GLU A 345    10451   6180  16573  -1928   6283  -5080  A    C  
ATOM   2717  CD  GLU A 345      -1.262  36.022  32.632  1.00113.96      A    C  
ANISOU 2717  CD  GLU A 345    13647   9611  20042  -2170   6457  -5416  A    C  
ATOM   2718  OE1 GLU A 345      -1.289  36.709  31.586  1.00112.11      A    O  
ANISOU 2718  OE1 GLU A 345    13508   8966  20124  -2236   6799  -5204  A    O  
ATOM   2719  OE2 GLU A 345      -0.199  35.670  33.194  1.00112.36      A    O1-
ANISOU 2719  OE2 GLU A 345    13212   9891  19589  -2275   6253  -5869  A    O1-
ATOM   2720  N   LEU A 346      -4.839  39.047  33.863  1.00 84.20      A    N  
ANISOU 2720  N   LEU A 346    10405   4354  17235  -2221   7731  -4991  A    N  
ATOM   2721  CA  LEU A 346      -5.720  39.896  33.059  1.00 85.18      A    C  
ANISOU 2721  CA  LEU A 346    10743   3901  17722  -2108   8161  -4529  A    C  
ATOM   2722  C   LEU A 346      -5.048  41.256  32.878  1.00 94.39      A    C  
ANISOU 2722  C   LEU A 346    11909   4666  19289  -2435   8804  -4879  A    C  
ATOM   2723  O   LEU A 346      -5.017  41.779  31.763  1.00 95.47      A    O  
ANISOU 2723  O   LEU A 346    12159   4441  19675  -2392   9114  -4574  A    O  
ATOM   2724  CB  LEU A 346      -7.101  40.035  33.733  1.00 84.54      A    C  
ANISOU 2724  CB  LEU A 346    10798   3650  17674  -1921   8208  -4274  A    C  
ATOM   2725  CG  LEU A 346      -8.109  40.989  33.089  1.00 90.25      A    C  
ANISOU 2725  CG  LEU A 346    11728   3801  18761  -1768   8692  -3812  A    C  
ATOM   2726  CD1 LEU A 346      -8.490  40.538  31.686  1.00 88.35      A    C  
ANISOU 2726  CD1 LEU A 346    11574   3504  18492  -1477   8553  -3175  A    C  
ATOM   2727  CD2 LEU A 346      -9.333  41.114  33.943  1.00 91.58      A    C  
ANISOU 2727  CD2 LEU A 346    11984   3883  18928  -1618   8719  -3669  A    C  
ATOM   2728  N   GLN A 347      -4.456  41.787  33.969  1.00 94.37      A    N  
ANISOU 2728  N   GLN A 347    11771   4762  19325  -2776   9002  -5543  A    N  
ATOM   2729  CA  GLN A 347      -3.681  43.036  33.989  1.00 99.01      A    C  
ANISOU 2729  CA  GLN A 347    12328   5025  20265  -3176   9623  -6023  A    C  
ATOM   2730  C   GLN A 347      -2.447  42.863  33.092  1.00103.60      A    C  
ANISOU 2730  C   GLN A 347    12778   5763  20824  -3331   9582  -6168  A    C  
ATOM   2731  O   GLN A 347      -2.107  43.775  32.340  1.00106.85      A    O  
ANISOU 2731  O   GLN A 347    13276   5738  21584  -3503  10108  -6182  A    O  
ATOM   2732  CB  GLN A 347      -3.287  43.385  35.436  1.00103.31      A    C  
ANISOU 2732  CB  GLN A 347    12704   5800  20751  -3512   9725  -6747  A    C  
ATOM   2733  CG  GLN A 347      -2.816  44.813  35.659  1.00129.89      A    C  
ANISOU 2733  CG  GLN A 347    16092   8730  24529  -3944  10470  -7247  A    C  
ATOM   2734  CD  GLN A 347      -2.596  45.082  37.129  1.00151.46      A    C  
ANISOU 2734  CD  GLN A 347    18691  11867  26989  -4150  10290  -7782  A    C  
ATOM   2735  NE2 GLN A 347      -3.628  45.561  37.809  1.00143.25      A    N  
ANISOU 2735  NE2 GLN A 347    17778  10373  26277  -4190  10791  -7861  A    N  
ATOM   2736  OE1 GLN A 347      -1.512  44.852  37.675  1.00150.04      A    O  
ANISOU 2736  OE1 GLN A 347    18218  12195  26596  -4440  10137  -8396  A    O  
ATOM   2737  N   ASN A 348      -1.829  41.660  33.124  1.00 96.75      A    N  
ANISOU 2737  N   ASN A 348    11720   5497  19544  -3238   8971  -6230  A    N  
ATOM   2738  CA  ASN A 348      -0.671  41.293  32.307  1.00 96.24      A    C  
ANISOU 2738  CA  ASN A 348    11508   5667  19390  -3333   8839  -6342  A    C  
ATOM   2739  C   ASN A 348      -1.047  41.189  30.820  1.00 97.16      A    C  
ANISOU 2739  C   ASN A 348    11822   5452  19643  -3070   8879  -5672  A    C  
ATOM   2740  O   ASN A 348      -0.208  41.470  29.965  1.00 98.83      A    O  
ANISOU 2740  O   ASN A 348    11992   5572  19985  -3216   9077  -5736  A    O  
ATOM   2741  CB  ASN A 348      -0.058  39.965  32.795  1.00 93.67      A    C  
ANISOU 2741  CB  ASN A 348    10950   6075  18564  -3231   8169  -6531  A    C  
ATOM   2742  CG  ASN A 348       1.170  39.506  32.037  1.00112.74      A    C  
ANISOU 2742  CG  ASN A 348    13187   8799  20850  -3313   8002  -6680  A    C  
ATOM   2743  ND2 ASN A 348       1.062  38.345  31.391  1.00 97.64      A    N  
ANISOU 2743  ND2 ASN A 348    11314   7114  18670  -2983   7519  -6243  A    N  
ATOM   2744  OD1 ASN A 348       2.222  40.169  32.033  1.00108.27      A    O  
ANISOU 2744  OD1 ASN A 348    12442   8284  20414  -3682   8309  -7204  A    O  
ATOM   2745  N   SER A 349      -2.289  40.778  30.513  1.00 89.02      A    N  
ANISOU 2745  N   SER A 349    10985   4278  18562  -2692   8692  -5047  A    N  
ATOM   2746  CA  SER A 349      -2.740  40.633  29.129  1.00 86.12      A    C  
ANISOU 2746  CA  SER A 349    10780   3670  18272  -2417   8697  -4398  A    C  
ATOM   2747  C   SER A 349      -3.223  41.952  28.552  1.00 93.24      A    C  
ANISOU 2747  C   SER A 349    11884   3919  19623  -2436   9374  -4158  A    C  
ATOM   2748  O   SER A 349      -2.957  42.223  27.378  1.00 92.45      A    O  
ANISOU 2748  O   SER A 349    11856   3604  19667  -2385   9575  -3874  A    O  
ATOM   2749  CB  SER A 349      -3.833  39.579  29.014  1.00 82.82      A    C  
ANISOU 2749  CB  SER A 349    10452   3439  17578  -2023   8208  -3859  A    C  
ATOM   2750  OG  SER A 349      -3.302  38.325  29.394  1.00 85.42      A    O  
ANISOU 2750  OG  SER A 349    10628   4331  17498  -1985   7623  -4046  A    O  
ATOM   2751  N   VAL A 350      -3.922  42.781  29.365  1.00 93.51      A    N  
ANISOU 2751  N   VAL A 350    12020   3631  19877  -2494   9750  -4261  A    N  
ATOM   2752  CA  VAL A 350      -4.425  44.068  28.879  1.00 96.81      A    C  
ANISOU 2752  CA  VAL A 350    12660   3390  20733  -2476  10450  -4019  A    C  
ATOM   2753  C   VAL A 350      -3.258  44.977  28.498  1.00105.31      A    C  
ANISOU 2753  C   VAL A 350    13713   4198  22100  -2856  10980  -4431  A    C  
ATOM   2754  O   VAL A 350      -3.401  45.692  27.522  1.00107.24      A    O  
ANISOU 2754  O   VAL A 350    14139   3976  22633  -2768  11446  -4077  A    O  
ATOM   2755  CB  VAL A 350      -5.454  44.798  29.786  1.00102.52      A    C  
ANISOU 2755  CB  VAL A 350    13521   3786  21647  -2431  10784  -4013  A    C  
ATOM   2756  CG1 VAL A 350      -6.723  43.969  29.974  1.00 98.21      A    C  
ANISOU 2756  CG1 VAL A 350    13018   3453  20844  -2028  10322  -3515  A    C  
ATOM   2757  CG2 VAL A 350      -4.858  45.221  31.124  1.00105.06      A    C  
ANISOU 2757  CG2 VAL A 350    13713   4199  22007  -2847  10942  -4790  A    C  
ATOM   2758  N   ASN A 351      -2.104  44.921  29.206  1.00104.06      A    N  
ANISOU 2758  N   ASN A 351    13325   4360  21852  -3264  10912  -5155  A    N  
ATOM   2759  CA  ASN A 351      -0.940  45.759  28.864  1.00108.18      A    C  
ANISOU 2759  CA  ASN A 351    13798   4666  22640  -3673  11422  -5600  A    C  
ATOM   2760  C   ASN A 351      -0.249  45.277  27.582  1.00110.49      A    C  
ANISOU 2760  C   ASN A 351    14041   5095  22843  -3592  11238  -5347  A    C  
ATOM   2761  O   ASN A 351       0.254  46.104  26.813  1.00113.70      A    O  
ANISOU 2761  O   ASN A 351    14535   5113  23552  -3767  11767  -5370  A    O  
ATOM   2762  CB  ASN A 351       0.081  45.849  30.014  1.00112.95      A    C  
ANISOU 2762  CB  ASN A 351    14131   5627  23156  -4152  11425  -6485  A    C  
ATOM   2763  CG  ASN A 351       0.759  44.563  30.449  1.00139.06      A    C  
ANISOU 2763  CG  ASN A 351    17131   9732  25972  -4139  10679  -6758  A    C  
ATOM   2764  ND2 ASN A 351       0.829  44.356  31.753  1.00134.73      A    N  
ANISOU 2764  ND2 ASN A 351    16420   9542  25229  -4274  10485  -7222  A    N  
ATOM   2765  OD1 ASN A 351       1.337  43.815  29.652  1.00131.21      A    O  
ANISOU 2765  OD1 ASN A 351    16032   9045  24776  -4037  10320  -6613  A    O  
ATOM   2766  N   THR A 352      -0.210  43.944  27.368  1.00101.43      A    N  
ANISOU 2766  N   THR A 352    12767   4486  21285  -3335  10515  -5118  A    N  
ATOM   2767  CA  THR A 352       0.423  43.335  26.198  1.00 99.39      A    C  
ANISOU 2767  CA  THR A 352    12454   4419  20891  -3231  10267  -4874  A    C  
ATOM   2768  C   THR A 352      -0.339  43.750  24.930  1.00102.73      A    C  
ANISOU 2768  C   THR A 352    13141   4362  21531  -2924  10566  -4149  A    C  
ATOM   2769  O   THR A 352       0.291  44.164  23.950  1.00103.40      A    O  
ANISOU 2769  O   THR A 352    13261   4243  21784  -3012  10870  -4080  A    O  
ATOM   2770  CB  THR A 352       0.508  41.799  26.357  1.00100.69      A    C  
ANISOU 2770  CB  THR A 352    12457   5234  20566  -3007   9455  -4791  A    C  
ATOM   2771  CG2 THR A 352       1.363  41.139  25.272  1.00 95.88      A    C  
ANISOU 2771  CG2 THR A 352    11755   4877  19797  -2957   9196  -4666  A    C  
ATOM   2772  OG1 THR A 352       1.055  41.489  27.640  1.00101.45      A    O  
ANISOU 2772  OG1 THR A 352    12326   5767  20453  -3230   9217  -5412  A    O  
ATOM   2773  N   PHE A 353      -1.688  43.667  24.971  1.00 96.97      A    N  
ANISOU 2773  N   PHE A 353    12581   3476  20788  -2563  10496  -3621  A    N  
ATOM   2774  CA  PHE A 353      -2.560  44.014  23.851  1.00 96.73      A    C  
ANISOU 2774  CA  PHE A 353    12773   3076  20905  -2208  10738  -2894  A    C  
ATOM   2775  C   PHE A 353      -2.848  45.519  23.776  1.00104.55      A    C  
ANISOU 2775  C   PHE A 353    13984   3375  22364  -2281  11575  -2841  A    C  
ATOM   2776  O   PHE A 353      -3.018  46.060  22.681  1.00105.02      A    O  
ANISOU 2776  O   PHE A 353    14207   3086  22612  -2104  11949  -2386  A    O  
ATOM   2777  CB  PHE A 353      -3.878  43.233  23.949  1.00 95.43      A    C  
ANISOU 2777  CB  PHE A 353    12658   3113  20490  -1793  10290  -2377  A    C  
ATOM   2778  CG  PHE A 353      -3.827  41.827  23.396  1.00 93.11      A    C  
ANISOU 2778  CG  PHE A 353    12248   3345  19783  -1597   9593  -2138  A    C  
ATOM   2779  CD1 PHE A 353      -4.403  41.524  22.167  1.00 95.00      A    C  
ANISOU 2779  CD1 PHE A 353    12570   3587  19938  -1262   9493  -1497  A    C  
ATOM   2780  CD2 PHE A 353      -3.216  40.800  24.107  1.00 93.24      A    C  
ANISOU 2780  CD2 PHE A 353    12076   3867  19485  -1735   9056  -2554  A    C  
ATOM   2781  CE1 PHE A 353      -4.360  40.221  21.654  1.00 91.73      A    C  
ANISOU 2781  CE1 PHE A 353    12060   3646  19148  -1110   8880  -1309  A    C  
ATOM   2782  CE2 PHE A 353      -3.156  39.501  23.585  1.00 91.73      A    C  
ANISOU 2782  CE2 PHE A 353    11809   4116  18926  -1551   8462  -2336  A    C  
ATOM   2783  CZ  PHE A 353      -3.734  39.219  22.364  1.00 88.19      A    C  
ANISOU 2783  CZ  PHE A 353    11454   3637  18417  -1259   8384  -1730  A    C  
ATOM   2784  N   GLY A 354      -2.888  46.175  24.933  1.00103.65      A    N  
ANISOU 2784  N   GLY A 354    13881   3075  22426  -2532  11877  -3302  A    N  
ATOM   2785  CA  GLY A 354      -3.207  47.590  25.063  1.00107.58      A    C  
ANISOU 2785  CA  GLY A 354    14608   2895  23373  -2622  12697  -3315  A    C  
ATOM   2786  C   GLY A 354      -4.514  47.774  25.809  1.00109.39      A    C  
ANISOU 2786  C   GLY A 354    14958   2973  23633  -2372  12737  -3079  A    C  
ATOM   2787  O   GLY A 354      -5.511  47.121  25.483  1.00106.30      A    O  
ANISOU 2787  O   GLY A 354    14592   2773  23025  -1944  12343  -2505  A    O  
ATOM   2788  N   ALA A 355      -4.510  48.657  26.836  1.00107.68      A    N  
ANISOU 2788  N   ALA A 355    14803   2433  23677  -2659  13218  -3551  A    N  
ATOM   2789  CA  ALA A 355      -5.652  48.988  27.700  1.00106.77      A    C  
ANISOU 2789  CA  ALA A 355    14804   2131  23634  -2486  13345  -3435  A    C  
ATOM   2790  C   ALA A 355      -6.845  49.533  26.899  1.00108.22      A    C  
ANISOU 2790  C   ALA A 355    15250   1872  23997  -1987  13696  -2628  A    C  
ATOM   2791  O   ALA A 355      -7.979  49.518  27.391  1.00105.61      A    O  
ANISOU 2791  O   ALA A 355    14982   1525  23620  -1702  13619  -2342  A    O  
ATOM   2792  CB  ALA A 355      -5.226  50.008  28.741  1.00111.90      A    C  
ANISOU 2792  CB  ALA A 355    15493   2438  24586  -2938  13930  -4123  A    C  
ATOM   2793  N   THR A 356      -6.579  49.964  25.656  1.00104.53      A    N  
ANISOU 2793  N   THR A 356    14915   1103  23700  -1862  14053  -2251  A    N  
ATOM   2794  CA  THR A 356      -7.546  50.529  24.726  1.00105.63      A    C  
ANISOU 2794  CA  THR A 356    15288    853  23993  -1367  14431  -1463  A    C  
ATOM   2795  C   THR A 356      -7.899  49.589  23.552  1.00105.70      A    C  
ANISOU 2795  C   THR A 356    15212   1277  23671   -953  13885   -811  A    C  
ATOM   2796  O   THR A 356      -8.814  49.914  22.791  1.00107.45      A    O  
ANISOU 2796  O   THR A 356    15578   1310  23937   -488  14099   -116  A    O  
ATOM   2797  CB  THR A 356      -7.019  51.859  24.185  1.00115.61      A    C  
ANISOU 2797  CB  THR A 356    16764   1893  25269  -1451  14647  -1414  A    C  
ATOM   2798  CG2 THR A 356      -5.752  51.694  23.278  1.00114.26      A    C  
ANISOU 2798  CG2 THR A 356    16537   1732  25144  -1644  14737  -1489  A    C  
ATOM   2799  OG1 THR A 356      -8.092  52.468  23.482  1.00116.27      A    O  
ANISOU 2799  OG1 THR A 356    17055   1863  25261   -931  14662   -672  A    O  
ATOM   2800  N   ASN A 357      -7.174  48.467  23.386  1.00 97.99      A    N  
ANISOU 2800  N   ASN A 357    14004    863  22366  -1112  13224  -1032  A    N  
ATOM   2801  CA  ASN A 357      -7.387  47.507  22.291  1.00 94.44      A    C  
ANISOU 2801  CA  ASN A 357    13462    829  21591   -788  12701   -503  A    C  
ATOM   2802  C   ASN A 357      -8.789  46.893  22.337  1.00 97.07      A    C  
ANISOU 2802  C   ASN A 357    13771   1444  21666   -342  12295     35  A    C  
ATOM   2803  O   ASN A 357      -9.125  46.270  23.343  1.00 92.16      A    O  
ANISOU 2803  O   ASN A 357    13040   1117  20859   -415  11882   -220  A    O  
ATOM   2804  CB  ASN A 357      -6.334  46.396  22.317  1.00 87.51      A    C  
ANISOU 2804  CB  ASN A 357    12323    540  20387  -1064  12078   -928  A    C  
ATOM   2805  CG  ASN A 357      -6.073  45.719  20.984  1.00103.04      A    C  
ANISOU 2805  CG  ASN A 357    14253   2741  22156   -875  11757   -518  A    C  
ATOM   2806  ND2 ASN A 357      -4.819  45.393  20.723  1.00 94.27      A    N  
ANISOU 2806  ND2 ASN A 357    13020   1807  20990  -1180  11622   -907  A    N  
ATOM   2807  OD1 ASN A 357      -6.974  45.463  20.179  1.00 94.72      A    O  
ANISOU 2807  OD1 ASN A 357    13243   1789  20959   -456  11616    128  A    O  
ATOM   2808  N   PRO A 358      -9.607  47.027  21.251  1.00 97.68      A    N  
ANISOU 2808  N   PRO A 358    13933   1477  21705    121  12398    772  A    N  
ATOM   2809  CA  PRO A 358     -10.959  46.424  21.257  1.00 94.97      A    C  
ANISOU 2809  CA  PRO A 358    13529   1466  21091    531  12008   1269  A    C  
ATOM   2810  C   PRO A 358     -10.934  44.905  21.398  1.00 89.31      A    C  
ANISOU 2810  C   PRO A 358    12589   1416  19928    471  11153   1150  A    C  
ATOM   2811  O   PRO A 358     -11.959  44.313  21.741  1.00 83.78      A    O  
ANISOU 2811  O   PRO A 358    11821   1008  19002    686  10797   1376  A    O  
ATOM   2812  CB  PRO A 358     -11.553  46.844  19.906  1.00 99.74      A    C  
ANISOU 2812  CB  PRO A 358    14221   1971  21704    991  12280   2024  A    C  
ATOM   2813  CG  PRO A 358     -10.366  47.184  19.047  1.00106.62      A    C  
ANISOU 2813  CG  PRO A 358    15148   2640  22721    802  12556   1916  A    C  
ATOM   2814  CD  PRO A 358      -9.364  47.770  19.993  1.00103.82      A    C  
ANISOU 2814  CD  PRO A 358    14854   1923  22671    298  12898   1187  A    C  
ATOM   2815  N   LEU A 359      -9.754  44.286  21.182  1.00 83.28      A    N  
ANISOU 2815  N   LEU A 359    11719    879  19044    170  10852    773  A    N  
ATOM   2816  CA  LEU A 359      -9.541  42.857  21.366  1.00 78.20      A    C  
ANISOU 2816  CA  LEU A 359    10892    819  17999     83  10095    596  A    C  
ATOM   2817  C   LEU A 359      -9.638  42.477  22.850  1.00 80.26      A    C  
ANISOU 2817  C   LEU A 359    11090   1218  18185   -125   9844    114  A    C  
ATOM   2818  O   LEU A 359      -9.892  41.306  23.156  1.00 74.16      A    O  
ANISOU 2818  O   LEU A 359    10204    900  17071    -95   9247     85  A    O  
ATOM   2819  CB  LEU A 359      -8.179  42.424  20.814  1.00 77.28      A    C  
ANISOU 2819  CB  LEU A 359    10690    866  17808   -175   9921    294  A    C  
ATOM   2820  CG  LEU A 359      -8.046  42.144  19.317  1.00 80.97      A    C  
ANISOU 2820  CG  LEU A 359    11151   1450  18163     23   9862    746  A    C  
ATOM   2821  CD1 LEU A 359      -6.640  41.773  18.998  1.00 80.32      A    C  
ANISOU 2821  CD1 LEU A 359    10982   1496  18041   -281   9730    344  A    C  
ATOM   2822  CD2 LEU A 359      -9.032  41.099  18.831  1.00 80.08      A    C  
ANISOU 2822  CD2 LEU A 359    10960   1796  17673    344   9335   1226  A    C  
ATOM   2823  N   THR A 360      -9.480  43.480  23.770  1.00 80.87      A    N  
ANISOU 2823  N   THR A 360    11251    896  18579   -331  10328   -260  A    N  
ATOM   2824  CA  THR A 360      -9.563  43.276  25.227  1.00 79.83      A    C  
ANISOU 2824  CA  THR A 360    11061    875  18395   -536  10160   -741  A    C  
ATOM   2825  C   THR A 360     -11.010  43.392  25.770  1.00 81.99      A    C  
ANISOU 2825  C   THR A 360    11398   1103  18651   -250  10174   -407  A    C  
ATOM   2826  O   THR A 360     -11.211  43.261  26.983  1.00 79.91      A    O  
ANISOU 2826  O   THR A 360    11100    917  18345   -384  10061   -756  A    O  
ATOM   2827  CB  THR A 360      -8.591  44.173  26.003  1.00 91.28      A    C  
ANISOU 2827  CB  THR A 360    12529   2011  20142   -951  10618  -1389  A    C  
ATOM   2828  CG2 THR A 360      -7.130  43.891  25.649  1.00 89.61      A    C  
ANISOU 2828  CG2 THR A 360    12195   1974  19880  -1267  10503  -1805  A    C  
ATOM   2829  OG1 THR A 360      -8.922  45.548  25.809  1.00 94.53      A    O  
ANISOU 2829  OG1 THR A 360    13140   1814  20964   -892  11369  -1221  A    O  
ATOM   2830  N   ASN A 361     -12.010  43.600  24.884  1.00 79.03      A    N  
ANISOU 2830  N   ASN A 361    11095    654  18280    151  10293    260  A    N  
ATOM   2831  CA  ASN A 361     -13.423  43.577  25.286  1.00 78.17      A    C  
ANISOU 2831  CA  ASN A 361    11006    597  18099    454  10243    619  A    C  
ATOM   2832  C   ASN A 361     -13.774  42.149  25.607  1.00 78.51      A    C  
ANISOU 2832  C   ASN A 361    10898   1214  17719    471   9510    605  A    C  
ATOM   2833  O   ASN A 361     -13.257  41.259  24.926  1.00 76.40      A    O  
ANISOU 2833  O   ASN A 361    10543   1274  17211    439   9108    644  A    O  
ATOM   2834  CB  ASN A 361     -14.336  44.061  24.161  1.00 78.29      A    C  
ANISOU 2834  CB  ASN A 361    11060    547  18140    896  10519   1338  A    C  
ATOM   2835  CG  ASN A 361     -14.244  45.507  23.792  1.00 94.00      A    C  
ANISOU 2835  CG  ASN A 361    13271   1871  20575    991  11307   1499  A    C  
ATOM   2836  ND2 ASN A 361     -15.248  45.959  23.062  1.00 83.84      A    N  
ANISOU 2836  ND2 ASN A 361    11948    685  19221   1434  11557   2123  A    N  
ATOM   2837  OD1 ASN A 361     -13.282  46.213  24.110  1.00 91.40      A    O  
ANISOU 2837  OD1 ASN A 361    13035   1163  20531    671  11707   1055  A    O  
ATOM   2838  N   LEU A 362     -14.656  41.916  26.601  1.00 73.64      A    N  
ANISOU 2838  N   LEU A 362    10263    710  17009    524   9356    560  A    N  
ATOM   2839  CA  LEU A 362     -15.074  40.568  26.967  1.00 69.20      A    C  
ANISOU 2839  CA  LEU A 362     9584    656  16051    541   8707    557  A    C  
ATOM   2840  C   LEU A 362     -15.713  39.887  25.770  1.00 71.57      A    C  
ANISOU 2840  C   LEU A 362     9821   1267  16104    825   8423   1119  A    C  
ATOM   2841  O   LEU A 362     -15.438  38.723  25.532  1.00 66.89      A    O  
ANISOU 2841  O   LEU A 362     9147   1064  15205    757   7919   1071  A    O  
ATOM   2842  CB  LEU A 362     -16.037  40.577  28.163  1.00 68.74      A    C  
ANISOU 2842  CB  LEU A 362     9535    618  15967    585   8679    484  A    C  
ATOM   2843  CG  LEU A 362     -16.291  39.234  28.838  1.00 68.80      A    C  
ANISOU 2843  CG  LEU A 362     9452   1090  15598    521   8067    341  A    C  
ATOM   2844  CD1 LEU A 362     -15.022  38.667  29.444  1.00 67.09      A    C  
ANISOU 2844  CD1 LEU A 362     9193   1029  15269    195   7802   -230  A    C  
ATOM   2845  CD2 LEU A 362     -17.348  39.361  29.893  1.00 71.98      A    C  
ANISOU 2845  CD2 LEU A 362     9871   1479  16000    598   8107    338  A    C  
ATOM   2846  N   VAL A 363     -16.539  40.625  25.007  1.00 71.98      A    N  
ANISOU 2846  N   VAL A 363     9910   1156  16283   1148   8770   1644  A    N  
ATOM   2847  CA  VAL A 363     -17.172  40.131  23.788  1.00 70.78      A    C  
ANISOU 2847  CA  VAL A 363     9673   1321  15900   1439   8570   2199  A    C  
ATOM   2848  C   VAL A 363     -16.538  40.979  22.655  1.00 76.01      A    C  
ANISOU 2848  C   VAL A 363    10407   1693  16782   1533   8998   2420  A    C  
ATOM   2849  O   VAL A 363     -17.041  42.053  22.337  1.00 78.28      A    O  
ANISOU 2849  O   VAL A 363    10777   1666  17301   1792   9507   2762  A    O  
ATOM   2850  CB  VAL A 363     -18.734  40.159  23.831  1.00 74.89      A    C  
ANISOU 2850  CB  VAL A 363    10130   2019  16305   1777   8564   2657  A    C  
ATOM   2851  CG1 VAL A 363     -19.333  39.402  22.653  1.00 73.76      A    C  
ANISOU 2851  CG1 VAL A 363     9843   2354  15829   2003   8232   3126  A    C  
ATOM   2852  CG2 VAL A 363     -19.272  39.597  25.148  1.00 72.06      A    C  
ANISOU 2852  CG2 VAL A 363     9745   1801  15832   1649   8297   2370  A    C  
ATOM   2853  N   PRO A 364     -15.370  40.560  22.104  1.00 71.61      A    N  
ANISOU 2853  N   PRO A 364     9834   1202  16174   1321   8838   2205  A    N  
ATOM   2854  CA  PRO A 364     -14.714  41.396  21.090  1.00 74.16      A    C  
ANISOU 2854  CA  PRO A 364    10237   1221  16719   1382   9275   2382  A    C  
ATOM   2855  C   PRO A 364     -15.283  41.250  19.685  1.00 80.69      A    C  
ANISOU 2855  C   PRO A 364    10999   2298  17360   1733   9225   3007  A    C  
ATOM   2856  O   PRO A 364     -15.935  40.256  19.367  1.00 78.32      A    O  
ANISOU 2856  O   PRO A 364    10562   2488  16708   1847   8748   3218  A    O  
ATOM   2857  CB  PRO A 364     -13.269  40.907  21.126  1.00 73.65      A    C  
ANISOU 2857  CB  PRO A 364    10152   1194  16638   1004   9078   1872  A    C  
ATOM   2858  CG  PRO A 364     -13.365  39.470  21.510  1.00 74.49      A    C  
ANISOU 2858  CG  PRO A 364    10133   1805  16364    900   8398   1699  A    C  
ATOM   2859  CD  PRO A 364     -14.586  39.331  22.377  1.00 68.93      A    C  
ANISOU 2859  CD  PRO A 364     9413   1203  15575   1035   8286   1802  A    C  
ATOM   2860  N   ASN A 365     -15.022  42.258  18.844  1.00 82.52      A    N  
ANISOU 2860  N   ASN A 365    11333   2195  17826   1897   9744   3291  A    N  
ATOM   2861  CA  ASN A 365     -15.393  42.247  17.442  1.00 84.14      A    C  
ANISOU 2861  CA  ASN A 365    11480   2623  17866   2236   9761   3876  A    C  
ATOM   2862  C   ASN A 365     -14.257  41.541  16.697  1.00 87.91      A    C  
ANISOU 2862  C   ASN A 365    11907   3290  18203   2005   9471   3683  A    C  
ATOM   2863  O   ASN A 365     -13.106  41.997  16.722  1.00 89.63      A    O  
ANISOU 2863  O   ASN A 365    12225   3163  18666   1754   9741   3356  A    O  
ATOM   2864  CB  ASN A 365     -15.636  43.667  16.927  1.00 91.32      A    C  
ANISOU 2864  CB  ASN A 365    12544   3067  19086   2553  10489   4295  A    C  
ATOM   2865  CG  ASN A 365     -16.412  43.724  15.633  1.00117.24      A    C  
ANISOU 2865  CG  ASN A 365    15740   6653  22152   3025  10523   5004  A    C  
ATOM   2866  ND2 ASN A 365     -17.297  44.704  15.527  1.00110.81      A    N  
ANISOU 2866  ND2 ASN A 365    14997   5628  21477   3438  11003   5472  A    N  
ATOM   2867  OD1 ASN A 365     -16.230  42.908  14.716  1.00111.40      A    O  
ANISOU 2867  OD1 ASN A 365    14867   6348  21111   3038  10141   5143  A    O  
ATOM   2868  N   LEU A 366     -14.562  40.391  16.096  1.00 80.75      A    N  
ANISOU 2868  N   LEU A 366    10841   2940  16900   2059   8922   3838  A    N  
ATOM   2869  CA  LEU A 366     -13.532  39.632  15.410  1.00 77.90      A    C  
ANISOU 2869  CA  LEU A 366    10431   2788  16380   1852   8619   3653  A    C  
ATOM   2870  C   LEU A 366     -13.693  39.687  13.886  1.00 84.79      A    C  
ANISOU 2870  C   LEU A 366    11245   3876  17093   2138   8681   4184  A    C  
ATOM   2871  O   LEU A 366     -13.114  38.849  13.188  1.00 83.33      A    O  
ANISOU 2871  O   LEU A 366    10984   3996  16682   2022   8338   4118  A    O  
ATOM   2872  CB  LEU A 366     -13.485  38.181  15.928  1.00 72.63      A    C  
ANISOU 2872  CB  LEU A 366     9654   2554  15388   1625   7956   3323  A    C  
ATOM   2873  CG  LEU A 366     -13.084  38.009  17.402  1.00 74.37      A    C  
ANISOU 2873  CG  LEU A 366     9923   2613  15722   1323   7852   2753  A    C  
ATOM   2874  CD1 LEU A 366     -13.380  36.618  17.880  1.00 70.56      A    C  
ANISOU 2874  CD1 LEU A 366     9351   2567  14891   1214   7250   2578  A    C  
ATOM   2875  CD2 LEU A 366     -11.611  38.341  17.640  1.00 75.79      A    C  
ANISOU 2875  CD2 LEU A 366    10168   2503  16126   1007   8022   2267  A    C  
ATOM   2876  N   HIS A 367     -14.417  40.707  13.364  1.00 85.39      A    N  
ANISOU 2876  N   HIS A 367    11366   3785  17293   2520   9149   4705  A    N  
ATOM   2877  CA  HIS A 367     -14.548  40.909  11.918  1.00 87.71      A    C  
ANISOU 2877  CA  HIS A 367    11611   4273  17444   2834   9279   5241  A    C  
ATOM   2878  C   HIS A 367     -13.164  41.244  11.366  1.00 91.72      A    C  
ANISOU 2878  C   HIS A 367    12230   4472  18146   2631   9521   5048  A    C  
ATOM   2879  O   HIS A 367     -12.517  42.167  11.859  1.00 91.43      A    O  
ANISOU 2879  O   HIS A 367    12369   3872  18499   2487  10000   4813  A    O  
ATOM   2880  CB  HIS A 367     -15.592  41.988  11.552  1.00 92.93      A    C  
ANISOU 2880  CB  HIS A 367    12305   4807  18197   3331   9772   5852  A    C  
ATOM   2881  CG  HIS A 367     -15.589  42.357  10.091  1.00100.04      A    C  
ANISOU 2881  CG  HIS A 367    13177   5855  18979   3678   9995   6407  A    C  
ATOM   2882  CD2 HIS A 367     -15.633  41.562   8.992  1.00101.04      A    C  
ANISOU 2882  CD2 HIS A 367    13125   6547  18719   3768   9622   6640  A    C  
ATOM   2883  ND1 HIS A 367     -15.521  43.681   9.672  1.00106.98      A    N  
ANISOU 2883  ND1 HIS A 367    14233   6263  20152   3976  10696   6775  A    N  
ATOM   2884  CE1 HIS A 367     -15.520  43.643   8.346  1.00107.89      A    C  
ANISOU 2884  CE1 HIS A 367    14267   6686  20040   4254  10713   7234  A    C  
ATOM   2885  NE2 HIS A 367     -15.579  42.393   7.892  1.00104.77      A    N  
ANISOU 2885  NE2 HIS A 367    13650   6928  19231   4130  10070   7157  A    N  
ATOM   2886  N   GLU A 368     -12.689  40.421  10.414  1.00 88.36      A    N  
ANISOU 2886  N   GLU A 368    11698   4432  17443   2573   9170   5084  A    N  
ATOM   2887  CA  GLU A 368     -11.379  40.488   9.750  1.00 88.25      A    C  
ANISOU 2887  CA  GLU A 368    11745   4260  17526   2372   9284   4904  A    C  
ATOM   2888  C   GLU A 368     -10.235  40.365  10.793  1.00 89.75      A    C  
ANISOU 2888  C   GLU A 368    12009   4147  17946   1897   9240   4193  A    C  
ATOM   2889  O   GLU A 368      -9.231  41.068  10.696  1.00 91.86      A    O  
ANISOU 2889  O   GLU A 368    12390   4012  18501   1725   9633   3990  A    O  
ATOM   2890  CB  GLU A 368     -11.240  41.765   8.879  1.00 94.81      A    C  
ANISOU 2890  CB  GLU A 368    12714   4714  18598   2648   9956   5338  A    C  
ATOM   2891  CG  GLU A 368     -12.081  41.768   7.607  1.00108.52      A    C  
ANISOU 2891  CG  GLU A 368    14343   6853  20037   3115   9958   6031  A    C  
ATOM   2892  CD  GLU A 368     -11.652  40.818   6.500  1.00130.83      A    C  
ANISOU 2892  CD  GLU A 368    17024  10175  22509   3071   9549   6095  A    C  
ATOM   2893  OE1 GLU A 368     -10.429  40.659   6.279  1.00128.68      A    O  
ANISOU 2893  OE1 GLU A 368    16810   9742  22339   2774   9552   5762  A    O  
ATOM   2894  OE2 GLU A 368     -12.551  40.248   5.840  1.00125.19      A    O1-
ANISOU 2894  OE2 GLU A 368    16128  10029  21409   3334   9243   6475  A    O1-
ATOM   2895  N   VAL A 369     -10.386  39.441  11.778  1.00 82.57      A    N  
ANISOU 2895  N   VAL A 369    11022   3466  16886   1687   8760   3812  A    N  
ATOM   2896  CA  VAL A 369      -9.386  39.214  12.834  1.00 80.63      A    C  
ANISOU 2896  CA  VAL A 369    10805   3045  16784   1275   8653   3147  A    C  
ATOM   2897  C   VAL A 369      -8.978  37.721  12.889  1.00 81.08      A    C  
ANISOU 2897  C   VAL A 369    10740   3573  16494   1081   7992   2856  A    C  
ATOM   2898  O   VAL A 369      -9.840  36.845  13.021  1.00 79.11      A    O  
ANISOU 2898  O   VAL A 369    10409   3701  15949   1184   7580   2993  A    O  
ATOM   2899  CB  VAL A 369      -9.882  39.715  14.226  1.00 85.10      A    C  
ANISOU 2899  CB  VAL A 369    11435   3343  17557   1210   8813   2915  A    C  
ATOM   2900  CG1 VAL A 369      -8.881  39.378  15.330  1.00 83.10      A    C  
ANISOU 2900  CG1 VAL A 369    11172   3019  17383    799   8647   2221  A    C  
ATOM   2901  CG2 VAL A 369     -10.179  41.225  14.215  1.00 89.25      A    C  
ANISOU 2901  CG2 VAL A 369    12115   3335  18461   1381   9529   3157  A    C  
ATOM   2902  N   ASP A 370      -7.657  37.455  12.815  1.00 76.47      A    N  
ANISOU 2902  N   ASP A 370    10149   2952  15953    798   7923   2445  A    N  
ATOM   2903  CA  ASP A 370      -7.041  36.131  12.919  1.00 72.93      A    C  
ANISOU 2903  CA  ASP A 370     9612   2876  15220    608   7373   2117  A    C  
ATOM   2904  C   ASP A 370      -7.152  35.688  14.387  1.00 74.13      A    C  
ANISOU 2904  C   ASP A 370     9757   3059  15350    443   7130   1702  A    C  
ATOM   2905  O   ASP A 370      -6.500  36.266  15.253  1.00 73.51      A    O  
ANISOU 2905  O   ASP A 370     9707   2710  15514    234   7352   1297  A    O  
ATOM   2906  CB  ASP A 370      -5.563  36.194  12.428  1.00 75.72      A    C  
ANISOU 2906  CB  ASP A 370     9953   3149  15666    387   7467   1819  A    C  
ATOM   2907  CG  ASP A 370      -4.913  34.863  12.032  1.00 86.74      A    C  
ANISOU 2907  CG  ASP A 370    11264   4953  16741    291   6960   1652  A    C  
ATOM   2908  OD1 ASP A 370      -5.300  33.813  12.601  1.00 83.45      A    O  
ANISOU 2908  OD1 ASP A 370    10814   4823  16072    275   6512   1528  A    O  
ATOM   2909  OD2 ASP A 370      -3.981  34.882  11.190  1.00 94.91      A    O1-
ANISOU 2909  OD2 ASP A 370    12278   5994  17790    221   7040   1617  A    O1-
ATOM   2910  N   VAL A 371      -8.012  34.694  14.664  1.00 70.67      A    N  
ANISOU 2910  N   VAL A 371     9278   2957  14616    532   6699   1803  A    N  
ATOM   2911  CA  VAL A 371      -8.318  34.203  16.022  1.00 69.05      A    C  
ANISOU 2911  CA  VAL A 371     9077   2815  14345    427   6453   1492  A    C  
ATOM   2912  C   VAL A 371      -7.076  33.679  16.781  1.00 69.10      A    C  
ANISOU 2912  C   VAL A 371     9060   2865  14328    152   6255    915  A    C  
ATOM   2913  O   VAL A 371      -6.988  33.881  17.996  1.00 67.74      A    O  
ANISOU 2913  O   VAL A 371     8898   2588  14253     30   6283    579  A    O  
ATOM   2914  CB  VAL A 371      -9.469  33.167  16.075  1.00 71.71      A    C  
ANISOU 2914  CB  VAL A 371     9383   3515  14350    561   6043   1722  A    C  
ATOM   2915  CG1 VAL A 371     -10.797  33.810  15.703  1.00 73.43      A    C  
ANISOU 2915  CG1 VAL A 371     9589   3705  14605    827   6260   2212  A    C  
ATOM   2916  CG2 VAL A 371      -9.194  31.954  15.191  1.00 70.35      A    C  
ANISOU 2916  CG2 VAL A 371     9166   3709  13855    555   5664   1795  A    C  
ATOM   2917  N   ASP A 372      -6.133  33.026  16.083  1.00 65.12      A    N  
ANISOU 2917  N   ASP A 372     8515   2542  13685     72   6063    803  A    N  
ATOM   2918  CA  ASP A 372      -4.913  32.491  16.707  1.00 65.44      A    C  
ANISOU 2918  CA  ASP A 372     8508   2688  13669   -144   5868    286  A    C  
ATOM   2919  C   ASP A 372      -4.008  33.627  17.200  1.00 74.84      A    C  
ANISOU 2919  C   ASP A 372     9671   3575  15189   -348   6275    -79  A    C  
ATOM   2920  O   ASP A 372      -3.383  33.501  18.260  1.00 74.89      A    O  
ANISOU 2920  O   ASP A 372     9622   3640  15192   -522   6185   -546  A    O  
ATOM   2921  CB  ASP A 372      -4.155  31.582  15.724  1.00 66.53      A    C  
ANISOU 2921  CB  ASP A 372     8609   3088  13583   -151   5602    297  A    C  
ATOM   2922  CG  ASP A 372      -5.029  30.538  15.053  1.00 79.05      A    C  
ANISOU 2922  CG  ASP A 372    10223   4961  14851     14   5257    643  A    C  
ATOM   2923  OD1 ASP A 372      -5.820  29.870  15.770  1.00 76.02      A    O  
ANISOU 2923  OD1 ASP A 372     9874   4710  14299     54   5004    636  A    O  
ATOM   2924  OD2 ASP A 372      -4.951  30.411  13.809  1.00 90.33      A    O1-
ANISOU 2924  OD2 ASP A 372    11637   6487  16197     90   5261    914  A    O1-
ATOM   2925  N   ALA A 373      -3.989  34.747  16.447  1.00 74.75      A    N  
ANISOU 2925  N   ALA A 373     9699   3250  15452   -323   6743    138  A    N  
ATOM   2926  CA  ALA A 373      -3.229  35.950  16.750  1.00 78.26      A    C  
ANISOU 2926  CA  ALA A 373    10147   3341  16249   -531   7233   -163  A    C  
ATOM   2927  C   ALA A 373      -3.973  36.850  17.745  1.00 86.69      A    C  
ANISOU 2927  C   ALA A 373    11286   4098  17556   -536   7556   -202  A    C  
ATOM   2928  O   ALA A 373      -3.386  37.813  18.253  1.00 90.21      A    O  
ANISOU 2928  O   ALA A 373    11739   4242  18294   -752   7969   -536  A    O  
ATOM   2929  CB  ALA A 373      -2.941  36.715  15.467  1.00 81.21      A    C  
ANISOU 2929  CB  ALA A 373    10565   3488  16803   -483   7624    124  A    C  
ATOM   2930  N   ALA A 374      -5.258  36.533  18.021  1.00 81.47      A    N  
ANISOU 2930  N   ALA A 374    10672   3517  16766   -313   7381    119  A    N  
ATOM   2931  CA  ALA A 374      -6.135  37.280  18.923  1.00 82.44      A    C  
ANISOU 2931  CA  ALA A 374    10864   3382  17076   -267   7644    145  A    C  
ATOM   2932  C   ALA A 374      -6.281  36.610  20.310  1.00 83.35      A    C  
ANISOU 2932  C   ALA A 374    10932   3707  17032   -373   7299   -226  A    C  
ATOM   2933  O   ALA A 374      -6.958  37.165  21.178  1.00 84.24      A    O  
ANISOU 2933  O   ALA A 374    11091   3629  17285   -366   7493   -276  A    O  
ATOM   2934  CB  ALA A 374      -7.506  37.437  18.283  1.00 83.48      A    C  
ANISOU 2934  CB  ALA A 374    11061   3492  17166     74   7708    771  A    C  
ATOM   2935  N   PHE A 375      -5.641  35.436  20.521  1.00 76.37      A    N  
ANISOU 2935  N   PHE A 375     9963   3205  15851   -454   6814   -475  A    N  
ATOM   2936  CA  PHE A 375      -5.699  34.667  21.774  1.00 73.37      A    C  
ANISOU 2936  CA  PHE A 375     9541   3069  15266   -521   6459   -801  A    C  
ATOM   2937  C   PHE A 375      -5.053  35.439  22.946  1.00 75.92      A    C  
ANISOU 2937  C   PHE A 375     9812   3244  15791   -773   6714  -1341  A    C  
ATOM   2938  O   PHE A 375      -3.963  36.002  22.794  1.00 77.91      A    O  
ANISOU 2938  O   PHE A 375     9996   3402  16204   -984   6953  -1658  A    O  
ATOM   2939  CB  PHE A 375      -5.039  33.287  21.587  1.00 72.61      A    C  
ANISOU 2939  CB  PHE A 375     9385   3381  14821   -523   5956   -922  A    C  
ATOM   2940  CG  PHE A 375      -5.051  32.390  22.808  1.00 72.71      A    C  
ANISOU 2940  CG  PHE A 375     9374   3666  14587   -546   5589  -1215  A    C  
ATOM   2941  CD1 PHE A 375      -6.212  31.725  23.193  1.00 74.30      A    C  
ANISOU 2941  CD1 PHE A 375     9653   3974  14604   -388   5348   -973  A    C  
ATOM   2942  CD2 PHE A 375      -3.901  32.207  23.569  1.00 75.29      A    C  
ANISOU 2942  CD2 PHE A 375     9590   4168  14849   -718   5497  -1731  A    C  
ATOM   2943  CE1 PHE A 375      -6.224  30.908  24.332  1.00 74.05      A    C  
ANISOU 2943  CE1 PHE A 375     9621   4172  14344   -396   5043  -1225  A    C  
ATOM   2944  CE2 PHE A 375      -3.910  31.380  24.700  1.00 76.92      A    C  
ANISOU 2944  CE2 PHE A 375     9776   4646  14802   -697   5172  -1971  A    C  
ATOM   2945  CZ  PHE A 375      -5.068  30.727  25.066  1.00 73.47      A    C  
ANISOU 2945  CZ  PHE A 375     9449   4268  14196   -533   4954  -1706  A    C  
ATOM   2946  N   SER A 376      -5.754  35.470  24.106  1.00 68.35      A    N  
ANISOU 2946  N   SER A 376     8875   2282  14814   -765   6674  -1455  A    N  
ATOM   2947  CA  SER A 376      -5.345  36.174  25.328  1.00 69.08      A    C  
ANISOU 2947  CA  SER A 376     8914   2267  15065   -996   6904  -1963  A    C  
ATOM   2948  C   SER A 376      -6.003  35.588  26.582  1.00 71.94      A    C  
ANISOU 2948  C   SER A 376     9276   2833  15226   -944   6617  -2084  A    C  
ATOM   2949  O   SER A 376      -6.869  34.718  26.472  1.00 68.70      A    O  
ANISOU 2949  O   SER A 376     8926   2590  14587   -731   6289  -1744  A    O  
ATOM   2950  CB  SER A 376      -5.704  37.654  25.223  1.00 72.95      A    C  
ANISOU 2950  CB  SER A 376     9495   2255  15969  -1050   7526  -1888  A    C  
ATOM   2951  OG  SER A 376      -7.099  37.823  25.032  1.00 75.11      A    O  
ANISOU 2951  OG  SER A 376     9890   2364  16285   -782   7604  -1382  A    O  
ATOM   2952  N   SER A 377      -5.613  36.102  27.772  1.00 71.10      A    N  
ANISOU 2952  N   SER A 377     9099   2712  15204  -1155   6771  -2579  A    N  
ATOM   2953  CA  SER A 377      -6.161  35.699  29.071  1.00 70.01      A    C  
ANISOU 2953  CA  SER A 377     8953   2752  14894  -1129   6560  -2749  A    C  
ATOM   2954  C   SER A 377      -7.439  36.472  29.411  1.00 73.93      A    C  
ANISOU 2954  C   SER A 377     9573   2908  15608  -1036   6866  -2502  A    C  
ATOM   2955  O   SER A 377      -8.033  36.232  30.463  1.00 73.10      A    O  
ANISOU 2955  O   SER A 377     9477   2909  15389  -1006   6737  -2602  A    O  
ATOM   2956  CB  SER A 377      -5.133  35.908  30.177  1.00 75.85      A    C  
ANISOU 2956  CB  SER A 377     9533   3693  15594  -1396   6583  -3409  A    C  
ATOM   2957  OG  SER A 377      -3.912  35.246  29.896  1.00 86.60      A    O  
ANISOU 2957  OG  SER A 377    10756   5402  16747  -1464   6318  -3649  A    O  
ATOM   2958  N   VAL A 378      -7.847  37.422  28.533  1.00 72.09      A    N  
ANISOU 2958  N   VAL A 378     9435   2271  15683   -972   7291  -2175  A    N  
ATOM   2959  CA  VAL A 378      -9.052  38.242  28.705  1.00 72.41      A    C  
ANISOU 2959  CA  VAL A 378     9597   1966  15950   -835   7638  -1883  A    C  
ATOM   2960  C   VAL A 378     -10.318  37.332  28.809  1.00 72.33      A    C  
ANISOU 2960  C   VAL A 378     9629   2175  15679   -559   7259  -1467  A    C  
ATOM   2961  O   VAL A 378     -10.996  37.448  29.824  1.00 71.69      A    O  
ANISOU 2961  O   VAL A 378     9570   2076  15594   -547   7279  -1558  A    O  
ATOM   2962  CB  VAL A 378      -9.214  39.327  27.612  1.00 78.50      A    C  
ANISOU 2962  CB  VAL A 378    10469   2299  17060   -754   8157  -1543  A    C  
ATOM   2963  CG1 VAL A 378     -10.535  40.082  27.777  1.00 79.83      A    C  
ANISOU 2963  CG1 VAL A 378    10760   2153  17420   -538   8491  -1180  A    C  
ATOM   2964  CG2 VAL A 378      -8.031  40.295  27.619  1.00 81.62      A    C  
ANISOU 2964  CG2 VAL A 378    10843   2427  17742  -1066   8604  -1990  A    C  
ATOM   2965  N   PRO A 379     -10.651  36.412  27.849  1.00 65.44      A    N  
ANISOU 2965  N   PRO A 379     8760   1528  14577   -364   6920  -1055  A    N  
ATOM   2966  CA  PRO A 379     -11.872  35.607  28.020  1.00 63.73      A    C  
ANISOU 2966  CA  PRO A 379     8573   1518  14122   -156   6607   -719  A    C  
ATOM   2967  C   PRO A 379     -11.851  34.730  29.281  1.00 64.87      A    C  
ANISOU 2967  C   PRO A 379     8693   1946  14007   -236   6245  -1045  A    C  
ATOM   2968  O   PRO A 379     -12.896  34.492  29.892  1.00 64.02      A    O  
ANISOU 2968  O   PRO A 379     8622   1891  13811   -131   6156   -906  A    O  
ATOM   2969  CB  PRO A 379     -11.925  34.756  26.751  1.00 64.08      A    C  
ANISOU 2969  CB  PRO A 379     8606   1782  13958    -17   6322   -347  A    C  
ATOM   2970  CG  PRO A 379     -10.561  34.831  26.152  1.00 68.20      A    C  
ANISOU 2970  CG  PRO A 379     9083   2299  14528   -172   6353   -585  A    C  
ATOM   2971  CD  PRO A 379      -9.986  36.114  26.560  1.00 66.01      A    C  
ANISOU 2971  CD  PRO A 379     8809   1671  14600   -340   6838   -882  A    C  
ATOM   2972  N   TYR A 380     -10.649  34.296  29.676  1.00 60.07      A    N  
ANISOU 2972  N   TYR A 380     8018   1530  13277   -411   6064  -1477  A    N  
ATOM   2973  CA  TYR A 380     -10.351  33.488  30.851  1.00 58.19      A    C  
ANISOU 2973  CA  TYR A 380     7743   1594  12771   -476   5739  -1826  A    C  
ATOM   2974  C   TYR A 380     -10.613  34.265  32.151  1.00 62.64      A    C  
ANISOU 2974  C   TYR A 380     8293   2035  13471   -584   5976  -2143  A    C  
ATOM   2975  O   TYR A 380     -11.505  33.907  32.911  1.00 61.36      A    O  
ANISOU 2975  O   TYR A 380     8179   1951  13182   -491   5845  -2058  A    O  
ATOM   2976  CB  TYR A 380      -8.862  33.064  30.800  1.00 59.06      A    C  
ANISOU 2976  CB  TYR A 380     7750   1937  12752   -617   5571  -2207  A    C  
ATOM   2977  CG  TYR A 380      -8.522  32.039  29.741  1.00 59.50      A    C  
ANISOU 2977  CG  TYR A 380     7823   2191  12594   -510   5256  -1968  A    C  
ATOM   2978  CD1 TYR A 380      -8.600  32.350  28.384  1.00 61.44      A    C  
ANISOU 2978  CD1 TYR A 380     8095   2266  12985   -455   5400  -1628  A    C  
ATOM   2979  CD2 TYR A 380      -8.073  30.768  30.094  1.00 58.50      A    C  
ANISOU 2979  CD2 TYR A 380     7689   2423  12114   -457   4838  -2093  A    C  
ATOM   2980  CE1 TYR A 380      -8.282  31.406  27.405  1.00 60.28      A    C  
ANISOU 2980  CE1 TYR A 380     7959   2310  12633   -372   5120  -1433  A    C  
ATOM   2981  CE2 TYR A 380      -7.779  29.812  29.127  1.00 57.28      A    C  
ANISOU 2981  CE2 TYR A 380     7570   2426  11769   -363   4577  -1885  A    C  
ATOM   2982  CZ  TYR A 380      -7.867  30.140  27.782  1.00 65.25      A    C  
ANISOU 2982  CZ  TYR A 380     8593   3270  12927   -336   4714  -1572  A    C  
ATOM   2983  OH  TYR A 380      -7.564  29.212  26.816  1.00 66.63      A    O  
ANISOU 2983  OH  TYR A 380     8799   3609  12910   -259   4468  -1391  A    O  
ATOM   2984  N   GLU A 381      -9.815  35.315  32.410  1.00 60.88      A    N  
ANISOU 2984  N   GLU A 381     8004   1625  13503   -801   6339  -2528  A    N  
ATOM   2985  CA  GLU A 381      -9.791  36.063  33.662  1.00 62.27      A    C  
ANISOU 2985  CA  GLU A 381     8142   1720  13799   -969   6580  -2949  A    C  
ATOM   2986  C   GLU A 381     -10.805  37.201  33.777  1.00 65.18      A    C  
ANISOU 2986  C   GLU A 381     8614   1654  14499   -929   7043  -2763  A    C  
ATOM   2987  O   GLU A 381     -11.252  37.464  34.901  1.00 65.34      A    O  
ANISOU 2987  O   GLU A 381     8637   1666  14522   -976   7119  -2971  A    O  
ATOM   2988  CB  GLU A 381      -8.376  36.589  33.924  1.00 66.40      A    C  
ANISOU 2988  CB  GLU A 381     8522   2300  14406  -1265   6751  -3522  A    C  
ATOM   2989  CG  GLU A 381      -7.303  35.500  33.934  1.00 72.54      A    C  
ANISOU 2989  CG  GLU A 381     9170   3552  14838  -1286   6308  -3750  A    C  
ATOM   2990  CD  GLU A 381      -7.534  34.290  34.822  1.00 85.34      A    C  
ANISOU 2990  CD  GLU A 381    10781   5594  16052  -1140   5831  -3779  A    C  
ATOM   2991  OE1 GLU A 381      -8.228  34.418  35.858  1.00 93.25      A    O  
ANISOU 2991  OE1 GLU A 381    11811   6602  17017  -1126   5854  -3862  A    O  
ATOM   2992  OE2 GLU A 381      -7.014  33.204  34.477  1.00 71.28      A    O1-
ANISOU 2992  OE2 GLU A 381     8973   4126  13984  -1033   5453  -3716  A    O1-
ATOM   2993  N   LYS A 382     -11.180  37.869  32.662  1.00 61.48      A    N  
ANISOU 2993  N   LYS A 382     8204    889  14268   -828   7357  -2350  A    N  
ATOM   2994  CA  LYS A 382     -12.221  38.906  32.727  1.00 63.72      A    C  
ANISOU 2994  CA  LYS A 382     8584    794  14832   -721   7803  -2095  A    C  
ATOM   2995  C   LYS A 382     -13.579  38.200  32.820  1.00 64.94      A    C  
ANISOU 2995  C   LYS A 382     8820   1036  14817   -433   7518  -1677  A    C  
ATOM   2996  O   LYS A 382     -14.482  38.673  33.495  1.00 64.74      A    O  
ANISOU 2996  O   LYS A 382     8845    863  14892   -362   7709  -1624  A    O  
ATOM   2997  CB  LYS A 382     -12.163  39.887  31.539  1.00 66.82      A    C  
ANISOU 2997  CB  LYS A 382     9089    718  15583   -645   8268  -1817  A    C  
ATOM   2998  CG  LYS A 382     -13.141  41.059  31.686  1.00 69.41      A    C  
ANISOU 2998  CG  LYS A 382     9523    634  16217   -520   8805  -1582  A    C  
ATOM   2999  CD  LYS A 382     -13.273  41.911  30.420  1.00 76.98      A    C  
ANISOU 2999  CD  LYS A 382    10608   1167  17476   -348   9246  -1165  A    C  
ATOM   3000  CE  LYS A 382     -12.197  42.963  30.310  1.00 79.40      A    C  
ANISOU 3000  CE  LYS A 382    10960   1092  18116   -625   9770  -1537  A    C  
ATOM   3001  NZ  LYS A 382     -12.489  43.965  29.249  1.00 88.07      A    N1+
ANISOU 3001  NZ  LYS A 382    12207   1726  19531   -426  10326  -1096  A    N1+
ATOM   3002  N   GLY A 383     -13.674  37.053  32.159  1.00 61.06      A    N  
ANISOU 3002  N   GLY A 383     8305    860  14035   -301   7070  -1400  A    N  
ATOM   3003  CA  GLY A 383     -14.838  36.174  32.177  1.00 58.23      A    C  
ANISOU 3003  CA  GLY A 383     7968    728  13428    -88   6743  -1029  A    C  
ATOM   3004  C   GLY A 383     -15.037  35.596  33.557  1.00 59.80      A    C  
ANISOU 3004  C   GLY A 383     8158   1144  13420   -160   6503  -1330  A    C  
ATOM   3005  O   GLY A 383     -16.154  35.595  34.061  1.00 57.77      A    O  
ANISOU 3005  O   GLY A 383     7935    875  13139    -42   6518  -1152  A    O  
ATOM   3006  N   PHE A 384     -13.942  35.119  34.183  1.00 57.18      A    N  
ANISOU 3006  N   PHE A 384     7768   1029  12928   -342   6293  -1787  A    N  
ATOM   3007  CA  PHE A 384     -13.977  34.581  35.540  1.00 56.15      A    C  
ANISOU 3007  CA  PHE A 384     7621   1141  12573   -400   6072  -2103  A    C  
ATOM   3008  C   PHE A 384     -14.351  35.672  36.551  1.00 62.39      A    C  
ANISOU 3008  C   PHE A 384     8414   1697  13593   -494   6449  -2349  A    C  
ATOM   3009  O   PHE A 384     -15.183  35.423  37.430  1.00 62.24      A    O  
ANISOU 3009  O   PHE A 384     8427   1763  13457   -427   6360  -2326  A    O  
ATOM   3010  CB  PHE A 384     -12.639  33.928  35.935  1.00 57.05      A    C  
ANISOU 3010  CB  PHE A 384     7647   1571  12459   -541   5803  -2534  A    C  
ATOM   3011  CG  PHE A 384     -12.542  33.685  37.427  1.00 58.88      A    C  
ANISOU 3011  CG  PHE A 384     7838   2034  12501   -612   5684  -2925  A    C  
ATOM   3012  CD1 PHE A 384     -13.181  32.598  38.015  1.00 58.66      A    C  
ANISOU 3012  CD1 PHE A 384     7875   2261  12153   -467   5336  -2786  A    C  
ATOM   3013  CD2 PHE A 384     -11.912  34.606  38.259  1.00 63.32      A    C  
ANISOU 3013  CD2 PHE A 384     8303   2544  13213   -829   5963  -3425  A    C  
ATOM   3014  CE1 PHE A 384     -13.135  32.402  39.400  1.00 60.10      A    C  
ANISOU 3014  CE1 PHE A 384     8025   2663  12148   -507   5245  -3119  A    C  
ATOM   3015  CE2 PHE A 384     -11.869  34.410  39.638  1.00 66.58      A    C  
ANISOU 3015  CE2 PHE A 384     8661   3207  13428   -885   5858  -3782  A    C  
ATOM   3016  CZ  PHE A 384     -12.474  33.311  40.201  1.00 62.37      A    C  
ANISOU 3016  CZ  PHE A 384     8195   2941  12563   -708   5494  -3613  A    C  
ATOM   3017  N   ALA A 385     -13.694  36.855  36.458  1.00 61.35      A    N  
ANISOU 3017  N   ALA A 385     8255   1274  13782   -669   6883  -2617  A    N  
ATOM   3018  CA  ALA A 385     -13.895  38.007  37.353  1.00 63.25      A    C  
ANISOU 3018  CA  ALA A 385     8508   1241  14284   -805   7322  -2915  A    C  
ATOM   3019  C   ALA A 385     -15.361  38.425  37.415  1.00 67.44      A    C  
ANISOU 3019  C   ALA A 385     9143   1529  14952   -593   7525  -2510  A    C  
ATOM   3020  O   ALA A 385     -15.860  38.739  38.496  1.00 66.79      A    O  
ANISOU 3020  O   ALA A 385     9073   1416  14889   -633   7640  -2705  A    O  
ATOM   3021  CB  ALA A 385     -13.039  39.193  36.906  1.00 67.02      A    C  
ANISOU 3021  CB  ALA A 385     8974   1375  15115  -1014   7809  -3167  A    C  
ATOM   3022  N   LEU A 386     -16.054  38.395  36.267  1.00 63.63      A    N  
ANISOU 3022  N   LEU A 386     8717    923  14536   -357   7553  -1949  A    N  
ATOM   3023  CA  LEU A 386     -17.463  38.736  36.181  1.00 64.09      A    C  
ANISOU 3023  CA  LEU A 386     8842    820  14690   -111   7721  -1508  A    C  
ATOM   3024  C   LEU A 386     -18.292  37.726  36.961  1.00 67.71      A    C  
ANISOU 3024  C   LEU A 386     9284   1614  14828    -24   7318  -1438  A    C  
ATOM   3025  O   LEU A 386     -19.171  38.124  37.714  1.00 68.95      A    O  
ANISOU 3025  O   LEU A 386     9470   1674  15053     39   7485  -1418  A    O  
ATOM   3026  CB  LEU A 386     -17.888  38.792  34.704  1.00 63.86      A    C  
ANISOU 3026  CB  LEU A 386     8833    706  14727    126   7776   -938  A    C  
ATOM   3027  CG  LEU A 386     -19.378  38.921  34.367  1.00 69.07      A    C  
ANISOU 3027  CG  LEU A 386     9512   1329  15404    437   7866   -394  A    C  
ATOM   3028  CD1 LEU A 386     -19.997  40.209  34.929  1.00 73.19      A    C  
ANISOU 3028  CD1 LEU A 386    10108   1440  16259    503   8423   -404  A    C  
ATOM   3029  CD2 LEU A 386     -19.581  38.828  32.875  1.00 70.89      A    C  
ANISOU 3029  CD2 LEU A 386     9720   1595  15619    650   7845    114  A    C  
ATOM   3030  N   LEU A 387     -17.986  36.425  36.807  1.00 61.67      A    N  
ANISOU 3030  N   LEU A 387     8484   1228  13718    -26   6815  -1415  A    N  
ATOM   3031  CA  LEU A 387     -18.707  35.349  37.481  1.00 59.04      A    C  
ANISOU 3031  CA  LEU A 387     8161   1210  13062     46   6434  -1340  A    C  
ATOM   3032  C   LEU A 387     -18.409  35.329  38.981  1.00 62.99      A    C  
ANISOU 3032  C   LEU A 387     8652   1816  13466   -105   6400  -1821  A    C  
ATOM   3033  O   LEU A 387     -19.301  35.046  39.777  1.00 61.50      A    O  
ANISOU 3033  O   LEU A 387     8491   1720  13158    -37   6323  -1764  A    O  
ATOM   3034  CB  LEU A 387     -18.376  34.004  36.835  1.00 56.33      A    C  
ANISOU 3034  CB  LEU A 387     7814   1188  12400     79   5972  -1196  A    C  
ATOM   3035  CG  LEU A 387     -18.740  33.860  35.344  1.00 59.99      A    C  
ANISOU 3035  CG  LEU A 387     8270   1632  12890    224   5947   -721  A    C  
ATOM   3036  CD1 LEU A 387     -18.109  32.627  34.753  1.00 55.85      A    C  
ANISOU 3036  CD1 LEU A 387     7751   1390  12080    197   5539   -701  A    C  
ATOM   3037  CD2 LEU A 387     -20.256  33.829  35.139  1.00 63.23      A    C  
ANISOU 3037  CD2 LEU A 387     8677   2067  13279    420   5979   -275  A    C  
ATOM   3038  N   PHE A 388     -17.186  35.686  39.367  1.00 61.45      A    N  
ANISOU 3038  N   PHE A 388     8403   1624  13322   -313   6482  -2298  A    N  
ATOM   3039  CA  PHE A 388     -16.791  35.741  40.766  1.00 62.48      A    C  
ANISOU 3039  CA  PHE A 388     8489   1907  13342   -468   6465  -2796  A    C  
ATOM   3040  C   PHE A 388     -17.366  37.006  41.431  1.00 70.37      A    C  
ANISOU 3040  C   PHE A 388     9511   2581  14644   -528   6937  -2937  A    C  
ATOM   3041  O   PHE A 388     -17.757  36.950  42.597  1.00 71.17      A    O  
ANISOU 3041  O   PHE A 388     9609   2800  14632   -557   6909  -3144  A    O  
ATOM   3042  CB  PHE A 388     -15.272  35.670  40.873  1.00 64.82      A    C  
ANISOU 3042  CB  PHE A 388     8681   2385  13563   -671   6388  -3265  A    C  
ATOM   3043  CG  PHE A 388     -14.715  35.590  42.270  1.00 67.71      A    C  
ANISOU 3043  CG  PHE A 388     8957   3034  13734   -821   6308  -3800  A    C  
ATOM   3044  CD1 PHE A 388     -15.033  34.522  43.104  1.00 69.51      A    C  
ANISOU 3044  CD1 PHE A 388     9204   3619  13588   -706   5931  -3785  A    C  
ATOM   3045  CD2 PHE A 388     -13.810  36.541  42.728  1.00 73.32      A    C  
ANISOU 3045  CD2 PHE A 388     9555   3691  14610  -1084   6607  -4333  A    C  
ATOM   3046  CE1 PHE A 388     -14.492  34.430  44.389  1.00 71.80      A    C  
ANISOU 3046  CE1 PHE A 388     9397   4224  13660   -814   5850  -4265  A    C  
ATOM   3047  CE2 PHE A 388     -13.258  36.444  44.005  1.00 77.84      A    C  
ANISOU 3047  CE2 PHE A 388    10008   4606  14960  -1225   6515  -4849  A    C  
ATOM   3048  CZ  PHE A 388     -13.605  35.389  44.830  1.00 74.31      A    C  
ANISOU 3048  CZ  PHE A 388     9575   4533  14127  -1070   6129  -4798  A    C  
ATOM   3049  N   TYR A 389     -17.479  38.118  40.679  1.00 67.93      A    N  
ANISOU 3049  N   TYR A 389     9242   1856  14714   -524   7386  -2797  A    N  
ATOM   3050  CA  TYR A 389     -18.100  39.340  41.178  1.00 70.31      A    C  
ANISOU 3050  CA  TYR A 389     9599   1785  15332   -544   7890  -2869  A    C  
ATOM   3051  C   TYR A 389     -19.630  39.108  41.348  1.00 73.30      A    C  
ANISOU 3051  C   TYR A 389    10035   2158  15656   -279   7842  -2418  A    C  
ATOM   3052  O   TYR A 389     -20.191  39.519  42.367  1.00 72.54      A    O  
ANISOU 3052  O   TYR A 389     9961   1988  15614   -300   8023  -2579  A    O  
ATOM   3053  CB  TYR A 389     -17.771  40.542  40.265  1.00 73.85      A    C  
ANISOU 3053  CB  TYR A 389    10099   1767  16193   -587   8416  -2815  A    C  
ATOM   3054  CG  TYR A 389     -18.715  41.725  40.340  1.00 77.80      A    C  
ANISOU 3054  CG  TYR A 389    10709   1812  17041   -463   8961  -2618  A    C  
ATOM   3055  CD1 TYR A 389     -18.757  42.541  41.468  1.00 82.68      A    C  
ANISOU 3055  CD1 TYR A 389    11353   2248  17812   -626   9306  -3028  A    C  
ATOM   3056  CD2 TYR A 389     -19.485  42.087  39.247  1.00 78.72      A    C  
ANISOU 3056  CD2 TYR A 389    10897   1682  17330   -177   9164  -2034  A    C  
ATOM   3057  CE1 TYR A 389     -19.608  43.649  41.526  1.00 87.26      A    C  
ANISOU 3057  CE1 TYR A 389    12052   2374  18728   -498   9853  -2848  A    C  
ATOM   3058  CE2 TYR A 389     -20.321  43.190  39.285  1.00 83.02      A    C  
ANISOU 3058  CE2 TYR A 389    11547   1809  18189    -18   9694  -1826  A    C  
ATOM   3059  CZ  TYR A 389     -20.405  43.952  40.436  1.00 94.12      A    C  
ANISOU 3059  CZ  TYR A 389    12999   3005  19757   -172  10039  -2226  A    C  
ATOM   3060  OH  TYR A 389     -21.244  45.030  40.450  1.00100.62      A    O  
ANISOU 3060  OH  TYR A 389    13943   3393  20896     10  10588  -2003  A    O  
ATOM   3061  N   LEU A 390     -20.274  38.385  40.399  1.00 69.02      A    N  
ANISOU 3061  N   LEU A 390     9501   1744  14979    -52   7580  -1891  A    N  
ATOM   3062  CA  LEU A 390     -21.705  38.045  40.474  1.00 68.24      A    C  
ANISOU 3062  CA  LEU A 390     9420   1725  14784    183   7490  -1468  A    C  
ATOM   3063  C   LEU A 390     -21.988  37.157  41.687  1.00 69.78      A    C  
ANISOU 3063  C   LEU A 390     9605   2246  14662    127   7153  -1674  A    C  
ATOM   3064  O   LEU A 390     -22.955  37.402  42.401  1.00 70.43      A    O  
ANISOU 3064  O   LEU A 390     9705   2290  14766    206   7273  -1611  A    O  
ATOM   3065  CB  LEU A 390     -22.194  37.342  39.188  1.00 65.83      A    C  
ANISOU 3065  CB  LEU A 390     9092   1571  14351    386   7248   -931  A    C  
ATOM   3066  CG  LEU A 390     -22.407  38.233  37.954  1.00 71.36      A    C  
ANISOU 3066  CG  LEU A 390     9799   1978  15336    561   7607   -546  A    C  
ATOM   3067  CD1 LEU A 390     -22.727  37.408  36.727  1.00 67.72      A    C  
ANISOU 3067  CD1 LEU A 390     9286   1765  14680    718   7302    -95  A    C  
ATOM   3068  CD2 LEU A 390     -23.500  39.278  38.189  1.00 74.49      A    C  
ANISOU 3068  CD2 LEU A 390    10224   2106  15974    757   8039   -316  A    C  
ATOM   3069  N   GLU A 391     -21.101  36.171  41.943  1.00 63.68      A    N  
ANISOU 3069  N   GLU A 391     8809   1787  13600      1   6762  -1928  A    N  
ATOM   3070  CA  GLU A 391     -21.155  35.242  43.077  1.00 62.43      A    C  
ANISOU 3070  CA  GLU A 391     8656   1960  13104    -42   6433  -2138  A    C  
ATOM   3071  C   GLU A 391     -21.248  36.002  44.422  1.00 68.99      A    C  
ANISOU 3071  C   GLU A 391     9478   2712  14023   -153   6690  -2534  A    C  
ATOM   3072  O   GLU A 391     -22.098  35.676  45.246  1.00 66.97      A    O  
ANISOU 3072  O   GLU A 391     9250   2572  13625    -86   6612  -2482  A    O  
ATOM   3073  CB  GLU A 391     -19.916  34.325  43.055  1.00 62.05      A    C  
ANISOU 3073  CB  GLU A 391     8581   2208  12787   -143   6077  -2387  A    C  
ATOM   3074  CG  GLU A 391     -19.736  33.455  44.288  1.00 72.71      A    C  
ANISOU 3074  CG  GLU A 391     9938   3904  13783   -174   5785  -2659  A    C  
ATOM   3075  CD  GLU A 391     -18.304  33.058  44.584  1.00 92.69      A    C  
ANISOU 3075  CD  GLU A 391    12401   6699  16118   -290   5587  -3060  A    C  
ATOM   3076  OE1 GLU A 391     -17.733  32.288  43.783  1.00 82.34      A    O  
ANISOU 3076  OE1 GLU A 391    11099   5507  14678   -245   5343  -2921  A    O  
ATOM   3077  OE2 GLU A 391     -17.752  33.507  45.615  1.00100.47      A    O1-
ANISOU 3077  OE2 GLU A 391    13310   7802  17062   -421   5676  -3520  A    O1-
ATOM   3078  N   GLN A 392     -20.375  37.006  44.623  1.00 69.59      A    N  
ANISOU 3078  N   GLN A 392     9514   2596  14333   -341   7011  -2941  A    N  
ATOM   3079  CA  GLN A 392     -20.302  37.823  45.837  1.00 72.60      A    C  
ANISOU 3079  CA  GLN A 392     9874   2895  14817   -500   7302  -3396  A    C  
ATOM   3080  C   GLN A 392     -21.557  38.694  45.988  1.00 80.17      A    C  
ANISOU 3080  C   GLN A 392    10903   3515  16045   -375   7690  -3158  A    C  
ATOM   3081  O   GLN A 392     -22.070  38.876  47.102  1.00 81.44      A    O  
ANISOU 3081  O   GLN A 392    11070   3717  16156   -402   7772  -3348  A    O  
ATOM   3082  CB  GLN A 392     -19.037  38.702  45.805  1.00 76.13      A    C  
ANISOU 3082  CB  GLN A 392    10255   3200  15472   -763   7591  -3882  A    C  
ATOM   3083  CG  GLN A 392     -17.738  37.897  45.806  1.00 77.20      A    C  
ANISOU 3083  CG  GLN A 392    10284   3727  15321   -890   7225  -4184  A    C  
ATOM   3084  CD  GLN A 392     -16.494  38.727  45.571  1.00102.85      A    C  
ANISOU 3084  CD  GLN A 392    13445   6854  18780  -1156   7507  -4623  A    C  
ATOM   3085  NE2 GLN A 392     -15.345  38.122  45.814  1.00 94.15      A    N  
ANISOU 3085  NE2 GLN A 392    12212   6150  17410  -1279   7213  -4968  A    N  
ATOM   3086  OE1 GLN A 392     -16.536  39.901  45.172  1.00102.81      A    O  
ANISOU 3086  OE1 GLN A 392    13487   6406  19170  -1250   8003  -4657  A    O  
ATOM   3087  N   LEU A 393     -22.067  39.194  44.851  1.00 76.35      A    N  
ANISOU 3087  N   LEU A 393    10466   2724  15821   -211   7921  -2722  A    N  
ATOM   3088  CA  LEU A 393     -23.257  40.038  44.758  1.00 77.04      A    C  
ANISOU 3088  CA  LEU A 393    10614   2486  16173    -24   8313  -2405  A    C  
ATOM   3089  C   LEU A 393     -24.556  39.279  44.987  1.00 75.81      A    C  
ANISOU 3089  C   LEU A 393    10451   2558  15794    195   8053  -2017  A    C  
ATOM   3090  O   LEU A 393     -25.505  39.878  45.481  1.00 74.62      A    O  
ANISOU 3090  O   LEU A 393    10327   2247  15779    305   8329  -1921  A    O  
ATOM   3091  CB  LEU A 393     -23.300  40.644  43.346  1.00 78.43      A    C  
ANISOU 3091  CB  LEU A 393    10823   2346  16629    125   8588  -2014  A    C  
ATOM   3092  CG  LEU A 393     -23.434  42.152  43.214  1.00 88.81      A    C  
ANISOU 3092  CG  LEU A 393    12225   3135  18385    158   9254  -2024  A    C  
ATOM   3093  CD1 LEU A 393     -22.293  42.895  43.908  1.00 91.99      A    C  
ANISOU 3093  CD1 LEU A 393    12647   3335  18969   -187   9566  -2670  A    C  
ATOM   3094  CD2 LEU A 393     -23.467  42.538  41.763  1.00 92.58      A    C  
ANISOU 3094  CD2 LEU A 393    12737   3375  19063    373   9460  -1540  A    C  
ATOM   3095  N   LEU A 394     -24.627  37.979  44.600  1.00 69.02      A    N  
ANISOU 3095  N   LEU A 394     9560   2060  14603    255   7554  -1794  A    N  
ATOM   3096  CA  LEU A 394     -25.887  37.233  44.641  1.00 67.52      A    C  
ANISOU 3096  CA  LEU A 394     9359   2088  14207    438   7326  -1405  A    C  
ATOM   3097  C   LEU A 394     -26.073  36.270  45.836  1.00 75.17      A    C  
ANISOU 3097  C   LEU A 394    10341   3384  14835    358   7001  -1620  A    C  
ATOM   3098  O   LEU A 394     -27.111  35.598  45.909  1.00 74.41      A    O  
ANISOU 3098  O   LEU A 394    10242   3469  14562    478   6827  -1327  A    O  
ATOM   3099  CB  LEU A 394     -26.099  36.476  43.323  1.00 64.53      A    C  
ANISOU 3099  CB  LEU A 394     8947   1868  13702    568   7056   -958  A    C  
ATOM   3100  CG  LEU A 394     -26.229  37.349  42.066  1.00 69.26      A    C  
ANISOU 3100  CG  LEU A 394     9524   2201  14593    732   7368   -605  A    C  
ATOM   3101  CD1 LEU A 394     -25.818  36.589  40.832  1.00 66.38      A    C  
ANISOU 3101  CD1 LEU A 394     9124   2012  14085    763   7076   -352  A    C  
ATOM   3102  CD2 LEU A 394     -27.631  37.940  41.912  1.00 70.57      A    C  
ANISOU 3102  CD2 LEU A 394     9651   2282  14880    987   7624   -206  A    C  
ATOM   3103  N   GLY A 395     -25.128  36.237  46.775  1.00 74.02      A    N  
ANISOU 3103  N   GLY A 395    10203   3328  14594    165   6947  -2120  A    N  
ATOM   3104  CA  GLY A 395     -25.291  35.393  47.959  1.00 72.86      A    C  
ANISOU 3104  CA  GLY A 395    10076   3492  14116    121   6678  -2316  A    C  
ATOM   3105  C   GLY A 395     -24.282  34.302  48.260  1.00 72.88      A    C  
ANISOU 3105  C   GLY A 395    10087   3837  13768     34   6273  -2541  A    C  
ATOM   3106  O   GLY A 395     -24.512  33.518  49.179  1.00 72.57      A    O  
ANISOU 3106  O   GLY A 395    10084   4059  13428     48   6049  -2616  A    O  
ATOM   3107  N   GLY A 396     -23.177  34.247  47.525  1.00 67.35      A    N  
ANISOU 3107  N   GLY A 396     9355   3140  13095    -37   6195  -2642  A    N  
ATOM   3108  CA  GLY A 396     -22.134  33.255  47.770  1.00 65.58      A    C  
ANISOU 3108  CA  GLY A 396     9127   3248  12540    -90   5833  -2858  A    C  
ATOM   3109  C   GLY A 396     -21.960  32.165  46.724  1.00 67.18      A    C  
ANISOU 3109  C   GLY A 396     9378   3574  12572      1   5508  -2530  A    C  
ATOM   3110  O   GLY A 396     -22.697  32.126  45.731  1.00 64.93      A    O  
ANISOU 3110  O   GLY A 396     9117   3148  12407     95   5537  -2115  A    O  
ATOM   3111  N   PRO A 397     -20.974  31.247  46.943  1.00 63.27      A    N  
ANISOU 3111  N   PRO A 397     8893   3373  11774    -15   5200  -2715  A    N  
ATOM   3112  CA  PRO A 397     -20.699  30.191  45.950  1.00 60.23      A    C  
ANISOU 3112  CA  PRO A 397     8570   3090  11226     63   4912  -2438  A    C  
ATOM   3113  C   PRO A 397     -21.811  29.156  45.806  1.00 62.61      A    C  
ANISOU 3113  C   PRO A 397     8994   3464  11330    179   4723  -2042  A    C  
ATOM   3114  O   PRO A 397     -22.085  28.726  44.690  1.00 60.06      A    O  
ANISOU 3114  O   PRO A 397     8702   3094  11024    221   4632  -1716  A    O  
ATOM   3115  CB  PRO A 397     -19.419  29.529  46.477  1.00 62.15      A    C  
ANISOU 3115  CB  PRO A 397     8793   3642  11178     45   4674  -2770  A    C  
ATOM   3116  CG  PRO A 397     -18.841  30.470  47.461  1.00 69.54      A    C  
ANISOU 3116  CG  PRO A 397     9606   4628  12190    -82   4871  -3251  A    C  
ATOM   3117  CD  PRO A 397     -20.014  31.181  48.064  1.00 66.28      A    C  
ANISOU 3117  CD  PRO A 397     9214   4024  11945    -93   5122  -3194  A    C  
ATOM   3118  N   GLU A 398     -22.431  28.751  46.928  1.00 60.72      A    N  
ANISOU 3118  N   GLU A 398     8819   3355  10898    214   4677  -2088  A    N  
ATOM   3119  CA  GLU A 398     -23.515  27.773  46.985  1.00 59.07      A    C  
ANISOU 3119  CA  GLU A 398     8731   3223  10490    289   4534  -1766  A    C  
ATOM   3120  C   GLU A 398     -24.717  28.238  46.154  1.00 62.64      A    C  
ANISOU 3120  C   GLU A 398     9137   3488  11177    307   4697  -1403  A    C  
ATOM   3121  O   GLU A 398     -25.246  27.450  45.363  1.00 61.02      A    O  
ANISOU 3121  O   GLU A 398     8983   3334  10870    334   4557  -1089  A    O  
ATOM   3122  CB  GLU A 398     -23.931  27.515  48.442  1.00 61.84      A    C  
ANISOU 3122  CB  GLU A 398     9143   3724  10627    313   4520  -1925  A    C  
ATOM   3123  CG  GLU A 398     -22.999  26.576  49.195  1.00 79.18      A    C  
ANISOU 3123  CG  GLU A 398    11427   6199  12460    368   4281  -2135  A    C  
ATOM   3124  CD  GLU A 398     -23.680  25.594  50.136  1.00103.76      A    C  
ANISOU 3124  CD  GLU A 398    14696   9470  15260    447   4173  -2044  A    C  
ATOM   3125  OE1 GLU A 398     -23.389  25.640  51.354  1.00 93.19      A    O  
ANISOU 3125  OE1 GLU A 398    13349   8309  13748    480   4178  -2313  A    O  
ATOM   3126  OE2 GLU A 398     -24.469  24.749  49.654  1.00 97.81      A    O1-
ANISOU 3126  OE2 GLU A 398    14070   8678  14416    469   4091  -1716  A    O1-
ATOM   3127  N   ILE A 399     -25.113  29.528  46.296  1.00 59.74      A    N  
ANISOU 3127  N   ILE A 399     8667   2917  11114    299   5008  -1452  A    N  
ATOM   3128  CA  ILE A 399     -26.220  30.132  45.550  1.00 59.10      A    C  
ANISOU 3128  CA  ILE A 399     8517   2678  11262    367   5205  -1104  A    C  
ATOM   3129  C   ILE A 399     -25.847  30.257  44.056  1.00 61.73      A    C  
ANISOU 3129  C   ILE A 399     8797   2924  11732    392   5197   -879  A    C  
ATOM   3130  O   ILE A 399     -26.671  29.891  43.207  1.00 61.59      A    O  
ANISOU 3130  O   ILE A 399     8751   2967  11682    457   5139   -513  A    O  
ATOM   3131  CB  ILE A 399     -26.664  31.491  46.166  1.00 64.76      A    C  
ANISOU 3131  CB  ILE A 399     9164   3176  12267    383   5580  -1226  A    C  
ATOM   3132  CG1 ILE A 399     -27.209  31.281  47.604  1.00 65.70      A    C  
ANISOU 3132  CG1 ILE A 399     9330   3413  12222    367   5576  -1401  A    C  
ATOM   3133  CG2 ILE A 399     -27.712  32.205  45.273  1.00 66.87      A    C  
ANISOU 3133  CG2 ILE A 399     9346   3280  12781    511   5815   -833  A    C  
ATOM   3134  CD1 ILE A 399     -27.807  32.497  48.325  1.00 73.78      A    C  
ANISOU 3134  CD1 ILE A 399    10301   4236  13498    377   5946  -1539  A    C  
ATOM   3135  N   PHE A 400     -24.609  30.733  43.735  1.00 56.87      A    N  
ANISOU 3135  N   PHE A 400     8157   2204  11248    332   5252  -1107  A    N  
ATOM   3136  CA  PHE A 400     -24.159  30.883  42.343  1.00 54.67      A    C  
ANISOU 3136  CA  PHE A 400     7834   1838  11099    353   5259   -916  A    C  
ATOM   3137  C   PHE A 400     -24.001  29.534  41.623  1.00 54.35      A    C  
ANISOU 3137  C   PHE A 400     7853   2017  10780    355   4907   -734  A    C  
ATOM   3138  O   PHE A 400     -24.202  29.488  40.411  1.00 52.15      A    O  
ANISOU 3138  O   PHE A 400     7531   1723  10561    400   4895   -445  A    O  
ATOM   3139  CB  PHE A 400     -22.850  31.679  42.229  1.00 57.42      A    C  
ANISOU 3139  CB  PHE A 400     8144   2030  11644    260   5414  -1236  A    C  
ATOM   3140  CG  PHE A 400     -22.665  32.280  40.850  1.00 59.33      A    C  
ANISOU 3140  CG  PHE A 400     8332   2087  12124    305   5572  -1002  A    C  
ATOM   3141  CD1 PHE A 400     -23.499  33.308  40.400  1.00 63.22      A    C  
ANISOU 3141  CD1 PHE A 400     8778   2343  12898    417   5910   -739  A    C  
ATOM   3142  CD2 PHE A 400     -21.666  31.814  39.997  1.00 60.48      A    C  
ANISOU 3142  CD2 PHE A 400     8477   2302  12202    259   5396  -1026  A    C  
ATOM   3143  CE1 PHE A 400     -23.343  33.849  39.118  1.00 64.76      A    C  
ANISOU 3143  CE1 PHE A 400     8933   2384  13291    492   6070   -489  A    C  
ATOM   3144  CE2 PHE A 400     -21.490  32.375  38.722  1.00 63.36      A    C  
ANISOU 3144  CE2 PHE A 400     8795   2503  12775    306   5552   -802  A    C  
ATOM   3145  CZ  PHE A 400     -22.329  33.392  38.292  1.00 62.81      A    C  
ANISOU 3145  CZ  PHE A 400     8685   2205  12973    426   5890   -529  A    C  
ATOM   3146  N   LEU A 401     -23.642  28.455  42.352  1.00 50.22      A    N  
ANISOU 3146  N   LEU A 401     7436   1694   9950    317   4646   -898  A    N  
ATOM   3147  CA  LEU A 401     -23.501  27.104  41.782  1.00 48.17      A    C  
ANISOU 3147  CA  LEU A 401     7273   1610   9418    316   4349   -746  A    C  
ATOM   3148  C   LEU A 401     -24.855  26.590  41.252  1.00 50.77      A    C  
ANISOU 3148  C   LEU A 401     7606   2011   9674    338   4314   -374  A    C  
ATOM   3149  O   LEU A 401     -24.889  25.981  40.186  1.00 49.93      A    O  
ANISOU 3149  O   LEU A 401     7505   1975   9491    326   4188   -165  A    O  
ATOM   3150  CB  LEU A 401     -22.903  26.120  42.801  1.00 47.89      A    C  
ANISOU 3150  CB  LEU A 401     7373   1752   9072    312   4136   -984  A    C  
ATOM   3151  CG  LEU A 401     -22.447  24.752  42.241  1.00 51.87      A    C  
ANISOU 3151  CG  LEU A 401     8009   2391   9307    324   3867   -889  A    C  
ATOM   3152  CD1 LEU A 401     -21.237  24.892  41.318  1.00 52.62      A    C  
ANISOU 3152  CD1 LEU A 401     8050   2465   9480    316   3815   -985  A    C  
ATOM   3153  CD2 LEU A 401     -22.131  23.800  43.351  1.00 53.18      A    C  
ANISOU 3153  CD2 LEU A 401     8333   2719   9155    373   3712  -1041  A    C  
ATOM   3154  N   GLY A 402     -25.946  26.898  41.968  1.00 48.38      A    N  
ANISOU 3154  N   GLY A 402     7278   1707   9399    361   4441   -311  A    N  
ATOM   3155  CA  GLY A 402     -27.312  26.558  41.575  1.00 47.21      A    C  
ANISOU 3155  CA  GLY A 402     7085   1665   9189    374   4443     12  A    C  
ATOM   3156  C   GLY A 402     -27.631  27.100  40.196  1.00 48.84      A    C  
ANISOU 3156  C   GLY A 402     7141   1853   9564    431   4534    304  A    C  
ATOM   3157  O   GLY A 402     -28.178  26.391  39.351  1.00 47.66      A    O  
ANISOU 3157  O   GLY A 402     6963   1875   9271    402   4408    540  A    O  
ATOM   3158  N   PHE A 403     -27.239  28.356  39.954  1.00 45.97      A    N  
ANISOU 3158  N   PHE A 403     6685   1284   9497    508   4769    275  A    N  
ATOM   3159  CA  PHE A 403     -27.375  29.006  38.649  1.00 45.53      A    C  
ANISOU 3159  CA  PHE A 403     6499   1182   9620    604   4898    554  A    C  
ATOM   3160  C   PHE A 403     -26.562  28.255  37.564  1.00 48.92      A    C  
ANISOU 3160  C   PHE A 403     6958   1702   9926    544   4679    599  A    C  
ATOM   3161  O   PHE A 403     -27.088  27.994  36.485  1.00 48.85      A    O  
ANISOU 3161  O   PHE A 403     6859   1848   9854    580   4625    893  A    O  
ATOM   3162  CB  PHE A 403     -26.930  30.471  38.717  1.00 47.28      A    C  
ANISOU 3162  CB  PHE A 403     6672   1103  10189    684   5234    462  A    C  
ATOM   3163  CG  PHE A 403     -26.525  31.045  37.377  1.00 48.13      A    C  
ANISOU 3163  CG  PHE A 403     6704   1114  10468    765   5351    665  A    C  
ATOM   3164  CD1 PHE A 403     -27.479  31.308  36.395  1.00 50.78      A    C  
ANISOU 3164  CD1 PHE A 403     6906   1554  10832    924   5439   1083  A    C  
ATOM   3165  CD2 PHE A 403     -25.188  31.299  37.086  1.00 48.37      A    C  
ANISOU 3165  CD2 PHE A 403     6783    987  10608    690   5370    441  A    C  
ATOM   3166  CE1 PHE A 403     -27.097  31.798  35.142  1.00 51.69      A    C  
ANISOU 3166  CE1 PHE A 403     6957   1606  11076   1020   5546   1292  A    C  
ATOM   3167  CE2 PHE A 403     -24.814  31.812  35.841  1.00 51.69      A    C  
ANISOU 3167  CE2 PHE A 403     7145   1314  11182    763   5491    637  A    C  
ATOM   3168  CZ  PHE A 403     -25.768  32.046  34.874  1.00 50.41      A    C  
ANISOU 3168  CZ  PHE A 403     6868   1246  11038    935   5577   1071  A    C  
ATOM   3169  N   LEU A 404     -25.285  27.965  37.842  1.00 44.57      A    N  
ANISOU 3169  N   LEU A 404     6514   1081   9339    463   4567    304  A    N  
ATOM   3170  CA  LEU A 404     -24.401  27.309  36.888  1.00 45.41      A    C  
ANISOU 3170  CA  LEU A 404     6656   1253   9344    416   4379    313  A    C  
ATOM   3171  C   LEU A 404     -24.917  25.934  36.501  1.00 43.85      A    C  
ANISOU 3171  C   LEU A 404     6526   1292   8844    353   4126    466  A    C  
ATOM   3172  O   LEU A 404     -24.849  25.593  35.318  1.00 40.76      A    O  
ANISOU 3172  O   LEU A 404     6090    993   8403    343   4044    650  A    O  
ATOM   3173  CB  LEU A 404     -22.970  27.203  37.414  1.00 46.59      A    C  
ANISOU 3173  CB  LEU A 404     6893   1332   9476    355   4303    -54  A    C  
ATOM   3174  CG  LEU A 404     -22.237  28.515  37.563  1.00 54.24      A    C  
ANISOU 3174  CG  LEU A 404     7788   2076  10745    359   4564   -255  A    C  
ATOM   3175  CD1 LEU A 404     -21.026  28.326  38.403  1.00 54.86      A    C  
ANISOU 3175  CD1 LEU A 404     7921   2181  10741    283   4477   -669  A    C  
ATOM   3176  CD2 LEU A 404     -21.841  29.087  36.213  1.00 59.02      A    C  
ANISOU 3176  CD2 LEU A 404     8314   2574  11536    389   4674    -94  A    C  
ATOM   3177  N   LYS A 405     -25.466  25.177  37.489  1.00 38.84      A    N  
ANISOU 3177  N   LYS A 405     5961    825   7972    298   4031    383  A    N  
ATOM   3178  CA ALYS A 405     -26.061  23.855  37.282  0.50 37.24      A    C  
ANISOU 3178  CA ALYS A 405     5831    853   7466    214   3846    487  A    C  
ATOM   3179  CA BLYS A 405     -26.053  23.854  37.271  0.50 37.46      A    C  
ANISOU 3179  CA BLYS A 405     5868    861   7503    213   3845    489  A    C  
ATOM   3180  C   LYS A 405     -27.265  23.956  36.335  1.00 40.90      A    C  
ANISOU 3180  C   LYS A 405     6186   1366   7989    204   3897    824  A    C  
ATOM   3181  O   LYS A 405     -27.377  23.174  35.402  1.00 39.83      A    O  
ANISOU 3181  O   LYS A 405     6050   1386   7698    122   3770    947  A    O  
ATOM   3182  CB ALYS A 405     -26.504  23.238  38.630  0.50 38.53      A    C  
ANISOU 3182  CB ALYS A 405     6198    929   7514    171   3810    367  A    C  
ATOM   3183  CB BLYS A 405     -26.473  23.213  38.612  0.50 39.48      A    C  
ANISOU 3183  CB BLYS A 405     6322   1049   7631    170   3805    364  A    C  
ATOM   3184  CG ALYS A 405     -25.366  22.779  39.531  0.50 36.64      A    C  
ANISOU 3184  CG ALYS A 405     6023    859   7039    173   3705     81  A    C  
ATOM   3185  CG BLYS A 405     -25.425  22.304  39.237  0.50 45.59      A    C  
ANISOU 3185  CG BLYS A 405     7313   1807   8201    156   3642    135  A    C  
ATOM   3186  CD ALYS A 405     -25.857  22.419  40.933  0.50 34.09      A    C  
ANISOU 3186  CD ALYS A 405     5731    735   6487    154   3718    -15  A    C  
ATOM   3187  CD BLYS A 405     -25.961  21.630  40.512  0.50 47.58      A    C  
ANISOU 3187  CD BLYS A 405     7720   2102   8256    139   3626     52  A    C  
ATOM   3188  CE ALYS A 405     -24.944  21.393  41.555  0.50 40.74      A    C  
ANISOU 3188  CE ALYS A 405     6989   1210   7279    220   3565   -226  A    C  
ATOM   3189  CE BLYS A 405     -25.363  20.258  40.771  0.50 40.32      A    C  
ANISOU 3189  CE BLYS A 405     7053   1220   7047    126   3466    -27  A    C  
ATOM   3190  NZ ALYS A 405     -24.773  21.604  43.011  0.50 50.46      A    N1+
ANISOU 3190  NZ ALYS A 405     8279   2458   8437    284   3606   -435  A    N1+
ATOM   3191  NZ BLYS A 405     -25.864  19.229  39.817  0.50 35.17      A    N1+
ANISOU 3191  NZ BLYS A 405     6467    657   6238      4   3398    158  A    N1+
ATOM   3192  N   SER A 406     -28.176  24.920  36.584  1.00 39.62      A    N  
ANISOU 3192  N   SER A 406     5868   1196   7989    298   4094    955  A    N  
ATOM   3193  CA  SER A 406     -29.378  25.105  35.753  1.00 40.87      A    C  
ANISOU 3193  CA  SER A 406     5821   1575   8132    338   4158   1273  A    C  
ATOM   3194  C   SER A 406     -29.013  25.600  34.359  1.00 44.68      A    C  
ANISOU 3194  C   SER A 406     6167   2092   8717    424   4191   1470  A    C  
ATOM   3195  O   SER A 406     -29.694  25.238  33.402  1.00 44.63      A    O  
ANISOU 3195  O   SER A 406     6022   2362   8575    405   4131   1698  A    O  
ATOM   3196  CB  SER A 406     -30.363  26.077  36.391  1.00 44.35      A    C  
ANISOU 3196  CB  SER A 406     6134   1988   8729    467   4384   1369  A    C  
ATOM   3197  OG  SER A 406     -30.538  25.778  37.762  1.00 60.62      A    O  
ANISOU 3197  OG  SER A 406     8328   3984  10719    400   4374   1161  A    O  
ATOM   3198  N   TYR A 407     -27.933  26.408  34.254  1.00 40.55      A    N  
ANISOU 3198  N   TYR A 407     5677   1311   8418    507   4294   1366  A    N  
ATOM   3199  CA  TYR A 407     -27.420  26.964  32.997  1.00 40.26      A    C  
ANISOU 3199  CA  TYR A 407     5541   1249   8506    598   4360   1532  A    C  
ATOM   3200  C   TYR A 407     -26.908  25.821  32.100  1.00 43.64      A    C  
ANISOU 3200  C   TYR A 407     6025   1848   8708    465   4106   1527  A    C  
ATOM   3201  O   TYR A 407     -27.284  25.763  30.929  1.00 46.05      A    O  
ANISOU 3201  O   TYR A 407     6188   2363   8945    499   4085   1776  A    O  
ATOM   3202  CB  TYR A 407     -26.342  28.035  33.283  1.00 41.85      A    C  
ANISOU 3202  CB  TYR A 407     5794   1106   9001    667   4556   1353  A    C  
ATOM   3203  CG  TYR A 407     -25.449  28.343  32.110  1.00 43.48      A    C  
ANISOU 3203  CG  TYR A 407     5966   1247   9306    704   4584   1430  A    C  
ATOM   3204  CD1 TYR A 407     -25.926  29.056  31.012  1.00 47.76      A    C  
ANISOU 3204  CD1 TYR A 407     6349   1846   9952    871   4754   1777  A    C  
ATOM   3205  CD2 TYR A 407     -24.125  27.916  32.088  1.00 41.80      A    C  
ANISOU 3205  CD2 TYR A 407     5874    941   9066    593   4447   1170  A    C  
ATOM   3206  CE1 TYR A 407     -25.115  29.308  29.906  1.00 48.85      A    C  
ANISOU 3206  CE1 TYR A 407     6463   1933  10166    909   4786   1863  A    C  
ATOM   3207  CE2 TYR A 407     -23.298  28.182  30.999  1.00 42.15      A    C  
ANISOU 3207  CE2 TYR A 407     5885    934   9196    618   4476   1237  A    C  
ATOM   3208  CZ  TYR A 407     -23.795  28.886  29.912  1.00 52.84      A    C  
ANISOU 3208  CZ  TYR A 407     7094   2325  10659    769   4651   1582  A    C  
ATOM   3209  OH  TYR A 407     -22.998  29.161  28.821  1.00 56.41      A    O  
ANISOU 3209  OH  TYR A 407     7518   2727  11189    800   4695   1663  A    O  
ATOM   3210  N   ILE A 408     -26.098  24.903  32.665  1.00 37.30      A    N  
ANISOU 3210  N   ILE A 408     5374   1071   7727    350   3920   1214  A    N  
ATOM   3211  CA  ILE A 408     -25.566  23.708  31.990  1.00 36.33      A    C  
ANISOU 3211  CA  ILE A 408     5324   1126   7353    242   3690   1141  A    C  
ATOM   3212  C   ILE A 408     -26.732  22.818  31.482  1.00 39.50      A    C  
ANISOU 3212  C   ILE A 408     5745   1683   7581     86   3607   1386  A    C  
ATOM   3213  O   ILE A 408     -26.697  22.383  30.328  1.00 39.00      A    O  
ANISOU 3213  O   ILE A 408     5618   1794   7405     30   3522   1505  A    O  
ATOM   3214  CB  ILE A 408     -24.601  22.918  32.934  1.00 36.91      A    C  
ANISOU 3214  CB  ILE A 408     5658   1036   7330    150   3562    856  A    C  
ATOM   3215  CG1 ILE A 408     -23.248  23.658  33.067  1.00 36.02      A    C  
ANISOU 3215  CG1 ILE A 408     5469    899   7320    226   3619    637  A    C  
ATOM   3216  CG2 ILE A 408     -24.377  21.481  32.447  1.00 36.52      A    C  
ANISOU 3216  CG2 ILE A 408     5771   1085   7019     19   3360    835  A    C  
ATOM   3217  CD1 ILE A 408     -22.506  23.418  34.395  1.00 37.75      A    C  
ANISOU 3217  CD1 ILE A 408     5929    839   7575    201   3574    367  A    C  
ATOM   3218  N   GLN A 409     -27.753  22.589  32.331  1.00 36.52      A    N  
ANISOU 3218  N   GLN A 409     5358   1410   7110     52   3631   1372  A    N  
ATOM   3219  CA AGLN A 409     -28.939  21.782  32.004  0.50 36.55      A    C  
ANISOU 3219  CA AGLN A 409     5297   1698   6891   -104   3577   1514  A    C  
ATOM   3220  CA BGLN A 409     -28.930  21.780  31.990  0.50 36.41      A    C  
ANISOU 3220  CA BGLN A 409     5280   1682   6873   -105   3575   1515  A    C  
ATOM   3221  C   GLN A 409     -29.789  22.461  30.929  1.00 42.20      A    C  
ANISOU 3221  C   GLN A 409     5704   2697   7634    -11   3658   1816  A    C  
ATOM   3222  O   GLN A 409     -30.250  21.793  29.998  1.00 42.70      A    O  
ANISOU 3222  O   GLN A 409     5666   3067   7493   -137   3566   1914  A    O  
ATOM   3223  CB AGLN A 409     -29.790  21.516  33.256  0.50 37.63      A    C  
ANISOU 3223  CB AGLN A 409     5503   1835   6960   -163   3621   1435  A    C  
ATOM   3224  CB BGLN A 409     -29.778  21.465  33.233  0.50 37.33      A    C  
ANISOU 3224  CB BGLN A 409     5469   1803   6910   -172   3613   1432  A    C  
ATOM   3225  CG AGLN A 409     -29.177  20.506  34.220  0.50 45.40      A    C  
ANISOU 3225  CG AGLN A 409     6798   2645   7807   -275   3523   1180  A    C  
ATOM   3226  CG BGLN A 409     -29.207  20.347  34.102  0.50 41.72      A    C  
ANISOU 3226  CG BGLN A 409     6339   2204   7310   -300   3508   1185  A    C  
ATOM   3227  CD AGLN A 409     -29.660  20.666  35.643  0.50 61.53      A    C  
ANISOU 3227  CD AGLN A 409     8920   4593   9864   -250   3604   1079  A    C  
ATOM   3228  CD BGLN A 409     -29.073  19.037  33.356  0.50 51.50      A    C  
ANISOU 3228  CD BGLN A 409     7702   3556   8309   -497   3378   1157  A    C  
ATOM   3229  NE2AGLN A 409     -30.969  20.716  35.854  0.50 60.28      A    N  
ANISOU 3229  NE2AGLN A 409     8638   4626   9642   -312   3676   1193  A    N  
ATOM   3230  NE2BGLN A 409     -27.864  18.503  33.330  0.50 46.41      A    N  
ANISOU 3230  NE2BGLN A 409     7275   2731   7628   -490   3285   1006  A    N  
ATOM   3231  OE1AGLN A 409     -28.868  20.683  36.587  0.50 53.60      A    O  
ANISOU 3231  OE1AGLN A 409     8085   3377   8904   -182   3597    885  A    O  
ATOM   3232  OE1BGLN A 409     -30.048  18.474  32.840  0.50 42.63      A    O  
ANISOU 3232  OE1BGLN A 409     6483   2692   7023   -664   3374   1251  A    O  
ATOM   3233  N   MET A 410     -29.992  23.783  31.058  1.00 39.60      A    N  
ANISOU 3233  N   MET A 410     5225   2277   7544    216   3848   1960  A    N  
ATOM   3234  CA  MET A 410     -30.778  24.566  30.110  1.00 41.84      A    C  
ANISOU 3234  CA  MET A 410     5215   2819   7863    385   3966   2289  A    C  
ATOM   3235  C   MET A 410     -30.214  24.474  28.690  1.00 44.61      A    C  
ANISOU 3235  C   MET A 410     5485   3304   8160    401   3894   2417  A    C  
ATOM   3236  O   MET A 410     -30.976  24.206  27.763  1.00 45.17      A    O  
ANISOU 3236  O   MET A 410     5342   3782   8041    385   3846   2617  A    O  
ATOM   3237  CB  MET A 410     -30.857  26.054  30.549  1.00 45.76      A    C  
ANISOU 3237  CB  MET A 410     5637   3080   8668    656   4234   2403  A    C  
ATOM   3238  CG  MET A 410     -31.674  26.943  29.617  1.00 52.67      A    C  
ANISOU 3238  CG  MET A 410     6223   4204   9585    904   4400   2786  A    C  
ATOM   3239  SD  MET A 410     -33.449  26.574  29.590  1.00 60.95      A    S  
ANISOU 3239  SD  MET A 410     6996   5790  10373    894   4372   2991  A    S  
ATOM   3240  CE  MET A 410     -33.805  26.958  27.875  1.00 60.32      A    C  
ANISOU 3240  CE  MET A 410     6595   6139  10183   1105   4406   3393  A    C  
ATOM   3241  N   PHE A 411     -28.896  24.673  28.523  1.00 40.20      A    N  
ANISOU 3241  N   PHE A 411     5081   2444   7748    425   3886   2289  A    N  
ATOM   3242  CA  PHE A 411     -28.302  24.747  27.198  1.00 40.51      A    C  
ANISOU 3242  CA  PHE A 411     5046   2575   7770    467   3851   2419  A    C  
ATOM   3243  C   PHE A 411     -27.448  23.545  26.775  1.00 42.70      A    C  
ANISOU 3243  C   PHE A 411     5493   2863   7867    249   3626   2217  A    C  
ATOM   3244  O   PHE A 411     -26.720  23.654  25.785  1.00 42.19      A    O  
ANISOU 3244  O   PHE A 411     5405   2802   7821    284   3603   2276  A    O  
ATOM   3245  CB  PHE A 411     -27.467  26.035  27.100  1.00 43.25      A    C  
ANISOU 3245  CB  PHE A 411     5405   2589   8440    680   4063   2470  A    C  
ATOM   3246  CG  PHE A 411     -28.239  27.315  27.308  1.00 47.70      A    C  
ANISOU 3246  CG  PHE A 411     5814   3107   9204    934   4342   2710  A    C  
ATOM   3247  CD1 PHE A 411     -28.976  27.879  26.271  1.00 52.90      A    C  
ANISOU 3247  CD1 PHE A 411     6227   4049   9825   1143   4456   3090  A    C  
ATOM   3248  CD2 PHE A 411     -28.204  27.973  28.529  1.00 50.51      A    C  
ANISOU 3248  CD2 PHE A 411     6270   3147   9776    984   4508   2561  A    C  
ATOM   3249  CE1 PHE A 411     -29.676  29.071  26.452  1.00 56.75      A    C  
ANISOU 3249  CE1 PHE A 411     6587   4480  10495   1423   4746   3340  A    C  
ATOM   3250  CE2 PHE A 411     -28.897  29.170  28.710  1.00 56.55      A    C  
ANISOU 3250  CE2 PHE A 411     6914   3833  10738   1229   4802   2781  A    C  
ATOM   3251  CZ  PHE A 411     -29.633  29.713  27.669  1.00 56.72      A    C  
ANISOU 3251  CZ  PHE A 411     6707   4117  10728   1461   4927   3182  A    C  
ATOM   3252  N   ALA A 412     -27.562  22.400  27.476  1.00 39.51      A    N  
ANISOU 3252  N   ALA A 412     5263   2466   7281     36   3484   2000  A    N  
ATOM   3253  CA  ALA A 412     -26.819  21.176  27.159  1.00 38.10      A    C  
ANISOU 3253  CA  ALA A 412     5280   2275   6921   -158   3305   1812  A    C  
ATOM   3254  C   ALA A 412     -27.060  20.742  25.721  1.00 43.00      A    C  
ANISOU 3254  C   ALA A 412     5748   3235   7356   -242   3228   1960  A    C  
ATOM   3255  O   ALA A 412     -28.211  20.747  25.264  1.00 43.03      A    O  
ANISOU 3255  O   ALA A 412     5525   3603   7223   -272   3247   2137  A    O  
ATOM   3256  CB  ALA A 412     -27.220  20.061  28.108  1.00 38.67      A    C  
ANISOU 3256  CB  ALA A 412     5549   2331   6812   -350   3228   1622  A    C  
ATOM   3257  N   PHE A 413     -25.961  20.391  25.005  1.00 39.88      A    N  
ANISOU 3257  N   PHE A 413     5457   2751   6946   -273   3143   1881  A    N  
ATOM   3258  CA  PHE A 413     -25.910  19.929  23.611  1.00 40.30      A    C  
ANISOU 3258  CA  PHE A 413     5402   3086   6823   -361   3062   1973  A    C  
ATOM   3259  C   PHE A 413     -26.194  21.082  22.607  1.00 45.12      A    C  
ANISOU 3259  C   PHE A 413     5713   3905   7524   -147   3168   2289  A    C  
ATOM   3260  O   PHE A 413     -26.274  20.852  21.397  1.00 44.73      A    O  
ANISOU 3260  O   PHE A 413     5520   4162   7314   -186   3114   2408  A    O  
ATOM   3261  CB  PHE A 413     -26.865  18.724  23.374  1.00 42.76      A    C  
ANISOU 3261  CB  PHE A 413     5698   3726   6823   -635   2975   1916  A    C  
ATOM   3262  CG  PHE A 413     -26.732  17.598  24.375  1.00 43.02      A    C  
ANISOU 3262  CG  PHE A 413     6044   3542   6760   -828   2924   1648  A    C  
ATOM   3263  CD1 PHE A 413     -27.663  17.436  25.393  1.00 46.33      A    C  
ANISOU 3263  CD1 PHE A 413     6487   3973   7144   -895   2976   1610  A    C  
ATOM   3264  CD2 PHE A 413     -25.674  16.703  24.303  1.00 44.35      A    C  
ANISOU 3264  CD2 PHE A 413     6487   3498   6866   -919   2844   1451  A    C  
ATOM   3265  CE1 PHE A 413     -27.525  16.411  26.335  1.00 46.86      A    C  
ANISOU 3265  CE1 PHE A 413     6863   3825   7117  -1047   2957   1387  A    C  
ATOM   3266  CE2 PHE A 413     -25.555  15.657  25.226  1.00 46.87      A    C  
ANISOU 3266  CE2 PHE A 413     7114   3611   7084  -1052   2829   1239  A    C  
ATOM   3267  CZ  PHE A 413     -26.474  15.525  26.245  1.00 45.38      A    C  
ANISOU 3267  CZ  PHE A 413     6959   3421   6864  -1113   2891   1214  A    C  
ATOM   3268  N   LYS A 414     -26.275  22.321  23.101  1.00 43.17      A    N  
ANISOU 3268  N   LYS A 414     5392   3477   7535     90   3340   2419  A    N  
ATOM   3269  CA  LYS A 414     -26.537  23.503  22.267  1.00 45.34      A    C  
ANISOU 3269  CA  LYS A 414     5422   3883   7922    346   3501   2747  A    C  
ATOM   3270  C   LYS A 414     -25.377  24.515  22.334  1.00 50.28      A    C  
ANISOU 3270  C   LYS A 414     6146   4090   8867    522   3657   2734  A    C  
ATOM   3271  O   LYS A 414     -24.449  24.351  23.131  1.00 48.31      A    O  
ANISOU 3271  O   LYS A 414     6119   3493   8745    445   3629   2455  A    O  
ATOM   3272  CB  LYS A 414     -27.862  24.172  22.678  1.00 48.95      A    C  
ANISOU 3272  CB  LYS A 414     5674   4530   8396    495   3637   2964  A    C  
ATOM   3273  CG  LYS A 414     -29.101  23.323  22.361  1.00 61.46      A    C  
ANISOU 3273  CG  LYS A 414     7075   6632   9646    330   3512   3016  A    C  
ATOM   3274  CD  LYS A 414     -30.356  23.702  23.166  1.00 73.89      A    C  
ANISOU 3274  CD  LYS A 414     8506   8344  11226    412   3615   3120  A    C  
ATOM   3275  CE  LYS A 414     -31.194  24.816  22.594  1.00 91.75      A    C  
ANISOU 3275  CE  LYS A 414    10453  10884  13523    740   3794   3513  A    C  
ATOM   3276  NZ  LYS A 414     -32.404  25.063  23.436  1.00104.01      A    N1+
ANISOU 3276  NZ  LYS A 414    11872  12587  15060    804   3881   3586  A    N1+
ATOM   3277  N   SER A 415     -25.429  25.536  21.452  1.00 47.89      A    N  
ANISOU 3277  N   SER A 415     5670   3853   8674    758   3833   3037  A    N  
ATOM   3278  CA  SER A 415     -24.489  26.650  21.380  1.00 48.04      A    C  
ANISOU 3278  CA  SER A 415     5754   3492   9008    932   4054   3071  A    C  
ATOM   3279  C   SER A 415     -25.159  27.882  21.974  1.00 55.71      A    C  
ANISOU 3279  C   SER A 415     6652   4304  10213   1168   4343   3253  A    C  
ATOM   3280  O   SER A 415     -26.390  27.973  21.916  1.00 58.26      A    O  
ANISOU 3280  O   SER A 415     6792   4935  10411   1274   4371   3484  A    O  
ATOM   3281  CB  SER A 415     -24.030  26.886  19.951  1.00 49.85      A    C  
ANISOU 3281  CB  SER A 415     5879   3863   9197   1033   4089   3288  A    C  
ATOM   3282  OG  SER A 415     -22.978  25.985  19.657  1.00 47.28      A    O  
ANISOU 3282  OG  SER A 415     5697   3499   8770    822   3883   3037  A    O  
ATOM   3283  N   VAL A 416     -24.375  28.785  22.612  1.00 51.78      A    N  
ANISOU 3283  N   VAL A 416     6293   3338  10043   1231   4564   3119  A    N  
ATOM   3284  CA  VAL A 416     -24.929  29.918  23.352  1.00 54.20      A    C  
ANISOU 3284  CA  VAL A 416     6580   3415  10597   1421   4868   3221  A    C  
ATOM   3285  C   VAL A 416     -24.197  31.246  23.068  1.00 58.33      A    C  
ANISOU 3285  C   VAL A 416     7152   3549  11461   1600   5234   3313  A    C  
ATOM   3286  O   VAL A 416     -22.979  31.265  22.872  1.00 55.42      A    O  
ANISOU 3286  O   VAL A 416     6901   2951  11204   1487   5236   3109  A    O  
ATOM   3287  CB  VAL A 416     -24.978  29.587  24.896  1.00 58.11      A    C  
ANISOU 3287  CB  VAL A 416     7223   3716  11141   1253   4797   2868  A    C  
ATOM   3288  CG1 VAL A 416     -23.610  29.287  25.513  1.00 56.66      A    C  
ANISOU 3288  CG1 VAL A 416     7245   3235  11047   1051   4702   2451  A    C  
ATOM   3289  CG2 VAL A 416     -25.748  30.629  25.688  1.00 59.58      A    C  
ANISOU 3289  CG2 VAL A 416     7379   3712  11547   1432   5096   2965  A    C  
ATOM   3290  N   THR A 417     -24.989  32.356  23.023  1.00 57.51      A    N  
ANISOU 3290  N   THR A 417     6954   3381  11515   1887   5566   3633  A    N  
ATOM   3291  CA  THR A 417     -24.535  33.746  22.889  1.00 59.13      A    C  
ANISOU 3291  CA  THR A 417     7229   3166  12074   2087   6012   3755  A    C  
ATOM   3292  C   THR A 417     -24.521  34.379  24.277  1.00 63.19      A    C  
ANISOU 3292  C   THR A 417     7876   3277  12858   2038   6232   3491  A    C  
ATOM   3293  O   THR A 417     -25.167  33.867  25.201  1.00 62.38      A    O  
ANISOU 3293  O   THR A 417     7763   3295  12643   1944   6065   3347  A    O  
ATOM   3294  CB  THR A 417     -25.410  34.577  21.917  1.00 64.70      A    C  
ANISOU 3294  CB  THR A 417     7764   4047  12773   2480   6284   4308  A    C  
ATOM   3295  CG2 THR A 417     -25.286  34.148  20.476  1.00 59.95      A    C  
ANISOU 3295  CG2 THR A 417     7030   3813  11934   2550   6133   4569  A    C  
ATOM   3296  OG1 THR A 417     -26.778  34.561  22.327  1.00 63.57      A    O  
ANISOU 3296  OG1 THR A 417     7468   4192  12495   2633   6267   4508  A    O  
ATOM   3297  N   THR A 418     -23.768  35.474  24.425  1.00 60.43      A    N  
ANISOU 3297  N   THR A 418     7652   2450  12857   2081   6621   3408  A    N  
ATOM   3298  CA  THR A 418     -23.666  36.242  25.660  1.00 61.16      A    C  
ANISOU 3298  CA  THR A 418     7871   2129  13236   2028   6904   3140  A    C  
ATOM   3299  C   THR A 418     -25.070  36.778  26.052  1.00 67.09      A    C  
ANISOU 3299  C   THR A 418     8536   2947  14007   2295   7100   3441  A    C  
ATOM   3300  O   THR A 418     -25.353  36.895  27.235  1.00 66.34      A    O  
ANISOU 3300  O   THR A 418     8499   2714  13991   2209   7141   3202  A    O  
ATOM   3301  CB  THR A 418     -22.630  37.359  25.455  1.00 67.69      A    C  
ANISOU 3301  CB  THR A 418     8833   2461  14424   2024   7336   3041  A    C  
ATOM   3302  CG2 THR A 418     -22.674  38.420  26.545  1.00 66.38      A    C  
ANISOU 3302  CG2 THR A 418     8787   1843  14589   2014   7752   2830  A    C  
ATOM   3303  OG1 THR A 418     -21.338  36.755  25.421  1.00 64.69      A    O  
ANISOU 3303  OG1 THR A 418     8518   2058  14004   1729   7106   2662  A    O  
ATOM   3304  N   GLU A 419     -25.927  37.080  25.050  1.00 66.53      A    N  
ANISOU 3304  N   GLU A 419     8312   3128  13839   2628   7210   3962  A    N  
ATOM   3305  CA  GLU A 419     -27.290  37.554  25.240  1.00 69.31      A    C  
ANISOU 3305  CA  GLU A 419     8537   3636  14163   2934   7383   4310  A    C  
ATOM   3306  C   GLU A 419     -28.162  36.460  25.856  1.00 70.06      A    C  
ANISOU 3306  C   GLU A 419     8508   4163  13947   2791   6970   4202  A    C  
ATOM   3307  O   GLU A 419     -28.906  36.774  26.787  1.00 71.24      A    O  
ANISOU 3307  O   GLU A 419     8655   4243  14168   2855   7095   4172  A    O  
ATOM   3308  CB  GLU A 419     -27.904  38.066  23.926  1.00 74.00      A    C  
ANISOU 3308  CB  GLU A 419     8963   4486  14666   3340   7562   4898  A    C  
ATOM   3309  CG  GLU A 419     -28.443  39.495  24.010  1.00 93.88      A    C  
ANISOU 3309  CG  GLU A 419    11520   6681  17468   3742   8139   5238  A    C  
ATOM   3310  CD  GLU A 419     -29.604  39.779  24.956  1.00129.09      A    C  
ANISOU 3310  CD  GLU A 419    15915  11186  21947   3897   8255   5307  A    C  
ATOM   3311  OE1 GLU A 419     -29.710  40.937  25.423  1.00128.93      A    O  
ANISOU 3311  OE1 GLU A 419    16022  10715  22249   4114   8761   5399  A    O  
ATOM   3312  OE2 GLU A 419     -30.406  38.856  25.230  1.00125.72      A    O1-
ANISOU 3312  OE2 GLU A 419    15318  11232  21219   3799   7868   5267  A    O1-
ATOM   3313  N   GLU A 420     -28.062  35.183  25.366  1.00 61.84      A    N  
ANISOU 3313  N   GLU A 420     7381   3545  12571   2587   6510   4130  A    N  
ATOM   3314  CA  GLU A 420     -28.819  34.030  25.916  1.00 59.25      A    C  
ANISOU 3314  CA  GLU A 420     6963   3610  11940   2402   6131   3998  A    C  
ATOM   3315  C   GLU A 420     -28.416  33.769  27.365  1.00 59.04      A    C  
ANISOU 3315  C   GLU A 420     7125   3286  12020   2138   6063   3530  A    C  
ATOM   3316  O   GLU A 420     -29.282  33.547  28.206  1.00 58.78      A    O  
ANISOU 3316  O   GLU A 420     7052   3373  11910   2120   6012   3487  A    O  
ATOM   3317  CB  GLU A 420     -28.627  32.753  25.086  1.00 58.68      A    C  
ANISOU 3317  CB  GLU A 420     6810   3960  11524   2205   5716   3969  A    C  
ATOM   3318  CG  GLU A 420     -29.285  32.791  23.722  1.00 74.06      A    C  
ANISOU 3318  CG  GLU A 420     8510   6372  13258   2441   5707   4418  A    C  
ATOM   3319  CD  GLU A 420     -28.874  31.645  22.827  1.00 93.19      A    C  
ANISOU 3319  CD  GLU A 420    10886   9135  15387   2222   5350   4343  A    C  
ATOM   3320  OE1 GLU A 420     -29.713  30.745  22.592  1.00 98.50      A    O  
ANISOU 3320  OE1 GLU A 420    11389  10307  15730   2120   5092   4385  A    O  
ATOM   3321  OE2 GLU A 420     -27.702  31.630  22.388  1.00 82.44      A    O1-
ANISOU 3321  OE2 GLU A 420     9662   7535  14125   2129   5340   4213  A    O1-
ATOM   3322  N   TRP A 421     -27.106  33.844  27.654  1.00 54.57      A    N  
ANISOU 3322  N   TRP A 421     6750   2356  11628   1947   6082   3186  A    N  
ATOM   3323  CA  TRP A 421     -26.555  33.683  28.996  1.00 52.57      A    C  
ANISOU 3323  CA  TRP A 421     6665   1836  11472   1714   6038   2725  A    C  
ATOM   3324  C   TRP A 421     -27.129  34.742  29.954  1.00 56.89      A    C  
ANISOU 3324  C   TRP A 421     7242   2101  12270   1849   6399   2715  A    C  
ATOM   3325  O   TRP A 421     -27.476  34.391  31.078  1.00 57.32      A    O  
ANISOU 3325  O   TRP A 421     7337   2175  12265   1730   6297   2488  A    O  
ATOM   3326  CB  TRP A 421     -25.005  33.747  28.967  1.00 50.08      A    C  
ANISOU 3326  CB  TRP A 421     6499   1229  11302   1528   6044   2392  A    C  
ATOM   3327  CG  TRP A 421     -24.369  33.766  30.336  1.00 50.74      A    C  
ANISOU 3327  CG  TRP A 421     6723   1066  11489   1319   6046   1914  A    C  
ATOM   3328  CD1 TRP A 421     -24.028  32.686  31.097  1.00 51.11      A    C  
ANISOU 3328  CD1 TRP A 421     6839   1258  11321   1100   5702   1592  A    C  
ATOM   3329  CD2 TRP A 421     -24.047  34.930  31.121  1.00 52.76      A    C  
ANISOU 3329  CD2 TRP A 421     7061    913  12071   1322   6430   1707  A    C  
ATOM   3330  CE2 TRP A 421     -23.520  34.473  32.351  1.00 54.92      A    C  
ANISOU 3330  CE2 TRP A 421     7424   1158  12286   1091   6266   1247  A    C  
ATOM   3331  CE3 TRP A 421     -24.158  36.317  30.902  1.00 57.40      A    C  
ANISOU 3331  CE3 TRP A 421     7665   1153  12990   1500   6924   1865  A    C  
ATOM   3332  NE1 TRP A 421     -23.487  33.101  32.295  1.00 50.85      A    N  
ANISOU 3332  NE1 TRP A 421     6905    980  11437    980   5822   1205  A    N  
ATOM   3333  CZ2 TRP A 421     -23.087  35.349  33.351  1.00 55.76      A    C  
ANISOU 3333  CZ2 TRP A 421     7607    940  12640   1004   6556    909  A    C  
ATOM   3334  CZ3 TRP A 421     -23.765  37.185  31.911  1.00 60.80      A    C  
ANISOU 3334  CZ3 TRP A 421     8199   1209  13691   1403   7240   1529  A    C  
ATOM   3335  CH2 TRP A 421     -23.215  36.702  33.108  1.00 59.87      A    C  
ANISOU 3335  CH2 TRP A 421     8143   1108  13497   1142   7046   1039  A    C  
ATOM   3336  N   LYS A 422     -27.201  36.028  29.518  1.00 55.41      A    N  
ANISOU 3336  N   LYS A 422     7053   1636  12366   2100   6844   2959  A    N  
ATOM   3337  CA  LYS A 422     -27.694  37.133  30.341  1.00 58.02      A    C  
ANISOU 3337  CA  LYS A 422     7434   1640  12969   2249   7260   2963  A    C  
ATOM   3338  C   LYS A 422     -29.192  37.002  30.561  1.00 62.17      A    C  
ANISOU 3338  C   LYS A 422     7803   2486  13333   2451   7224   3256  A    C  
ATOM   3339  O   LYS A 422     -29.642  37.238  31.679  1.00 61.80      A    O  
ANISOU 3339  O   LYS A 422     7800   2313  13367   2423   7329   3087  A    O  
ATOM   3340  CB  LYS A 422     -27.335  38.493  29.726  1.00 64.10      A    C  
ANISOU 3340  CB  LYS A 422     8271   2007  14077   2474   7779   3171  A    C  
ATOM   3341  CG  LYS A 422     -27.370  39.629  30.747  1.00 75.30      A    C  
ANISOU 3341  CG  LYS A 422     9828   2939  15842   2501   8245   2981  A    C  
ATOM   3342  CD  LYS A 422     -26.758  40.920  30.200  1.00 82.80      A    C  
ANISOU 3342  CD  LYS A 422    10903   3402  17155   2645   8795   3093  A    C  
ATOM   3343  CE  LYS A 422     -27.768  42.043  30.135  1.00101.42      A    C  
ANISOU 3343  CE  LYS A 422    13259   5566  19708   3048   9295   3500  A    C  
ATOM   3344  NZ  LYS A 422     -28.732  41.868  29.016  1.00116.67      A    N1+
ANISOU 3344  NZ  LYS A 422    14993   7926  21410   3431   9207   4109  A    N1+
ATOM   3345  N   LYS A 423     -29.953  36.582  29.526  1.00 60.51      A    N  
ANISOU 3345  N   LYS A 423     7392   2727  12874   2634   7065   3666  A    N  
ATOM   3346  CA  LYS A 423     -31.394  36.326  29.637  1.00 62.68      A    C  
ANISOU 3346  CA  LYS A 423     7464   3416  12936   2803   6985   3938  A    C  
ATOM   3347  C   LYS A 423     -31.651  35.182  30.626  1.00 65.63      A    C  
ANISOU 3347  C   LYS A 423     7856   3994  13087   2492   6612   3602  A    C  
ATOM   3348  O   LYS A 423     -32.612  35.259  31.396  1.00 67.46      A    O  
ANISOU 3348  O   LYS A 423     8024   4317  13290   2556   6667   3628  A    O  
ATOM   3349  CB  LYS A 423     -31.993  35.974  28.266  1.00 66.73      A    C  
ANISOU 3349  CB  LYS A 423     7734   4446  13175   2998   6839   4374  A    C  
ATOM   3350  CG  LYS A 423     -32.410  37.162  27.418  1.00 90.23      A    C  
ANISOU 3350  CG  LYS A 423    10609   7383  16292   3456   7251   4868  A    C  
ATOM   3351  CD  LYS A 423     -32.953  36.706  26.062  1.00106.66      A    C  
ANISOU 3351  CD  LYS A 423    12418  10069  18040   3630   7056   5269  A    C  
ATOM   3352  CE  LYS A 423     -33.877  37.722  25.415  1.00127.05      A    C  
ANISOU 3352  CE  LYS A 423    14813  12818  20642   4158   7416   5830  A    C  
ATOM   3353  NZ  LYS A 423     -33.144  38.868  24.812  1.00139.18      A    N1+
ANISOU 3353  NZ  LYS A 423    16503  13903  22476   4417   7845   6044  A    N1+
ATOM   3354  N   PHE A 424     -30.782  34.127  30.621  1.00 58.12      A    N  
ANISOU 3354  N   PHE A 424     7003   3100  11979   2169   6255   3294  A    N  
ATOM   3355  CA  PHE A 424     -30.945  33.001  31.542  1.00 54.90      A    C  
ANISOU 3355  CA  PHE A 424     6652   2853  11355   1888   5930   2989  A    C  
ATOM   3356  C   PHE A 424     -30.579  33.412  32.962  1.00 57.45      A    C  
ANISOU 3356  C   PHE A 424     7153   2794  11881   1784   6074   2626  A    C  
ATOM   3357  O   PHE A 424     -31.263  33.009  33.907  1.00 55.55      A    O  
ANISOU 3357  O   PHE A 424     6914   2662  11531   1706   5985   2512  A    O  
ATOM   3358  CB  PHE A 424     -30.133  31.769  31.118  1.00 53.97      A    C  
ANISOU 3358  CB  PHE A 424     6607   2890  11010   1618   5550   2793  A    C  
ATOM   3359  CG  PHE A 424     -30.465  30.573  31.982  1.00 52.84      A    C  
ANISOU 3359  CG  PHE A 424     6527   2931  10619   1372   5254   2551  A    C  
ATOM   3360  CD1 PHE A 424     -31.672  29.895  31.825  1.00 56.07      A    C  
ANISOU 3360  CD1 PHE A 424     6777   3764  10765   1354   5108   2727  A    C  
ATOM   3361  CD2 PHE A 424     -29.615  30.177  33.010  1.00 53.40      A    C  
ANISOU 3361  CD2 PHE A 424     6811   2762  10718   1169   5154   2147  A    C  
ATOM   3362  CE1 PHE A 424     -32.026  28.854  32.692  1.00 55.80      A    C  
ANISOU 3362  CE1 PHE A 424     6825   3853  10522   1126   4895   2507  A    C  
ATOM   3363  CE2 PHE A 424     -29.965  29.123  33.864  1.00 55.02      A    C  
ANISOU 3363  CE2 PHE A 424     7097   3114  10696    981   4927   1956  A    C  
ATOM   3364  CZ  PHE A 424     -31.166  28.473  33.698  1.00 53.67      A    C  
ANISOU 3364  CZ  PHE A 424     6796   3307  10289    954   4812   2139  A    C  
ATOM   3365  N   LEU A 425     -29.498  34.226  33.104  1.00 55.21      A    N  
ANISOU 3365  N   LEU A 425     7011   2082  11884   1768   6308   2432  A    N  
ATOM   3366  CA  LEU A 425     -29.056  34.745  34.406  1.00 55.08      A    C  
ANISOU 3366  CA  LEU A 425     7144   1714  12070   1657   6485   2052  A    C  
ATOM   3367  C   LEU A 425     -30.200  35.538  35.106  1.00 60.01      A    C  
ANISOU 3367  C   LEU A 425     7715   2262  12824   1851   6784   2192  A    C  
ATOM   3368  O   LEU A 425     -30.412  35.368  36.306  1.00 58.40      A    O  
ANISOU 3368  O   LEU A 425     7574   2018  12596   1733   6753   1927  A    O  
ATOM   3369  CB  LEU A 425     -27.796  35.619  34.227  1.00 55.41      A    C  
ANISOU 3369  CB  LEU A 425     7303   1342  12407   1613   6748   1856  A    C  
ATOM   3370  CG  LEU A 425     -27.232  36.317  35.468  1.00 58.67      A    C  
ANISOU 3370  CG  LEU A 425     7849   1391  13052   1478   6990   1428  A    C  
ATOM   3371  CD1 LEU A 425     -26.449  35.345  36.364  1.00 55.86      A    C  
ANISOU 3371  CD1 LEU A 425     7577   1149  12500   1185   6641    971  A    C  
ATOM   3372  CD2 LEU A 425     -26.372  37.485  35.073  1.00 56.96      A    C  
ANISOU 3372  CD2 LEU A 425     7707    755  13179   1504   7400   1360  A    C  
ATOM   3373  N   TYR A 426     -30.940  36.357  34.343  1.00 59.93      A    N  
ANISOU 3373  N   TYR A 426     7585   2262  12925   2168   7067   2621  A    N  
ATOM   3374  CA  TYR A 426     -32.060  37.164  34.830  1.00 63.33      A    C  
ANISOU 3374  CA  TYR A 426     7947   2640  13476   2417   7382   2823  A    C  
ATOM   3375  C   TYR A 426     -33.282  36.301  35.077  1.00 68.17      A    C  
ANISOU 3375  C   TYR A 426     8394   3730  13779   2426   7106   2965  A    C  
ATOM   3376  O   TYR A 426     -34.062  36.600  35.979  1.00 68.47      A    O  
ANISOU 3376  O   TYR A 426     8418   3738  13859   2485   7243   2928  A    O  
ATOM   3377  CB  TYR A 426     -32.389  38.270  33.831  1.00 67.35      A    C  
ANISOU 3377  CB  TYR A 426     8382   3029  14179   2796   7781   3274  A    C  
ATOM   3378  CG  TYR A 426     -31.599  39.536  34.041  1.00 70.50      A    C  
ANISOU 3378  CG  TYR A 426     8973   2827  14986   2842   8269   3131  A    C  
ATOM   3379  CD1 TYR A 426     -30.287  39.649  33.581  1.00 71.48      A    C  
ANISOU 3379  CD1 TYR A 426     9226   2695  15240   2670   8294   2928  A    C  
ATOM   3380  CD2 TYR A 426     -32.178  40.645  34.647  1.00 73.80      A    C  
ANISOU 3380  CD2 TYR A 426     9443   2933  15666   3057   8740   3203  A    C  
ATOM   3381  CE1 TYR A 426     -29.564  40.828  33.748  1.00 75.09      A    C  
ANISOU 3381  CE1 TYR A 426     9855   2598  16077   2677   8780   2773  A    C  
ATOM   3382  CE2 TYR A 426     -31.464  41.823  34.825  1.00 76.84      A    C  
ANISOU 3382  CE2 TYR A 426    10022   2737  16438   3072   9240   3051  A    C  
ATOM   3383  CZ  TYR A 426     -30.166  41.920  34.355  1.00 82.96      A    C  
ANISOU 3383  CZ  TYR A 426    10918   3267  17337   2874   9266   2836  A    C  
ATOM   3384  OH  TYR A 426     -29.473  43.090  34.540  1.00 86.04      A    O  
ANISOU 3384  OH  TYR A 426    11496   3081  18113   2850   9793   2655  A    O  
ATOM   3385  N   SER A 427     -33.462  35.237  34.266  1.00 63.89      A    N  
ANISOU 3385  N   SER A 427     7723   3630  12923   2348   6736   3108  A    N  
ATOM   3386  CA  SER A 427     -34.590  34.316  34.433  1.00 62.94      A    C  
ANISOU 3386  CA  SER A 427     7437   3993  12485   2297   6471   3207  A    C  
ATOM   3387  C   SER A 427     -34.443  33.544  35.741  1.00 63.94      A    C  
ANISOU 3387  C   SER A 427     7715   4065  12515   1993   6267   2793  A    C  
ATOM   3388  O   SER A 427     -35.407  33.457  36.502  1.00 63.73      A    O  
ANISOU 3388  O   SER A 427     7622   4177  12414   2013   6289   2801  A    O  
ATOM   3389  CB  SER A 427     -34.698  33.362  33.247  1.00 64.58      A    C  
ANISOU 3389  CB  SER A 427     7493   4655  12390   2233   6154   3394  A    C  
ATOM   3390  OG  SER A 427     -36.066  33.131  32.950  1.00 72.51      A    O  
ANISOU 3390  OG  SER A 427     8235   6154  13163   2354   6095   3677  A    O  
ATOM   3391  N   TYR A 428     -33.216  33.036  36.020  1.00 57.66      A    N  
ANISOU 3391  N   TYR A 428     7119   3067  11720   1739   6091   2439  A    N  
ATOM   3392  CA  TYR A 428     -32.871  32.282  37.231  1.00 54.25      A    C  
ANISOU 3392  CA  TYR A 428     6853   2578  11181   1478   5899   2043  A    C  
ATOM   3393  C   TYR A 428     -32.950  33.202  38.470  1.00 58.60      A    C  
ANISOU 3393  C   TYR A 428     7487   2814  11964   1529   6191   1842  A    C  
ATOM   3394  O   TYR A 428     -33.642  32.860  39.417  1.00 56.61      A    O  
ANISOU 3394  O   TYR A 428     7244   2667  11599   1467   6139   1743  A    O  
ATOM   3395  CB  TYR A 428     -31.464  31.647  37.090  1.00 51.76      A    C  
ANISOU 3395  CB  TYR A 428     6705   2144  10818   1264   5679   1753  A    C  
ATOM   3396  CG  TYR A 428     -31.123  30.706  38.227  1.00 50.67      A    C  
ANISOU 3396  CG  TYR A 428     6727   2025  10498   1034   5448   1398  A    C  
ATOM   3397  CD1 TYR A 428     -31.474  29.360  38.176  1.00 50.89      A    C  
ANISOU 3397  CD1 TYR A 428     6776   2353  10205    884   5138   1411  A    C  
ATOM   3398  CD2 TYR A 428     -30.477  31.170  39.370  1.00 51.22      A    C  
ANISOU 3398  CD2 TYR A 428     6928   1829  10705    974   5567   1051  A    C  
ATOM   3399  CE1 TYR A 428     -31.228  28.504  39.256  1.00 48.78      A    C  
ANISOU 3399  CE1 TYR A 428     6677   2094   9763    714   4967   1126  A    C  
ATOM   3400  CE2 TYR A 428     -30.227  30.327  40.454  1.00 50.82      A    C  
ANISOU 3400  CE2 TYR A 428     7012   1840  10457    809   5367    757  A    C  
ATOM   3401  CZ  TYR A 428     -30.590  28.991  40.387  1.00 54.49      A    C  
ANISOU 3401  CZ  TYR A 428     7518   2579  10608    696   5071    814  A    C  
ATOM   3402  OH  TYR A 428     -30.316  28.174  41.455  1.00 51.87      A    O  
ANISOU 3402  OH  TYR A 428     7343   2287  10079    568   4908    554  A    O  
ATOM   3403  N   PHE A 429     -32.251  34.362  38.462  1.00 58.29      A    N  
ANISOU 3403  N   PHE A 429     7516   2386  12246   1624   6517   1768  A    N  
ATOM   3404  CA  PHE A 429     -32.275  35.289  39.594  1.00 61.40      A    C  
ANISOU 3404  CA  PHE A 429     7998   2456  12876   1645   6834   1536  A    C  
ATOM   3405  C   PHE A 429     -33.384  36.356  39.424  1.00 71.90      A    C  
ANISOU 3405  C   PHE A 429     9213   3717  14390   1957   7217   1872  A    C  
ATOM   3406  O   PHE A 429     -33.123  37.546  39.549  1.00 74.11      A    O  
ANISOU 3406  O   PHE A 429     9567   3609  14984   2063   7627   1809  A    O  
ATOM   3407  CB  PHE A 429     -30.902  35.944  39.833  1.00 62.97      A    C  
ANISOU 3407  CB  PHE A 429     8342   2262  13323   1532   7018   1205  A    C  
ATOM   3408  CG  PHE A 429     -29.786  34.984  40.169  1.00 61.10      A    C  
ANISOU 3408  CG  PHE A 429     8209   2106  12899   1251   6671    826  A    C  
ATOM   3409  CD1 PHE A 429     -29.686  34.414  41.438  1.00 62.30      A    C  
ANISOU 3409  CD1 PHE A 429     8442   2315  12915   1086   6536    477  A    C  
ATOM   3410  CD2 PHE A 429     -28.807  34.682  39.234  1.00 60.55      A    C  
ANISOU 3410  CD2 PHE A 429     8155   2072  12778   1176   6492    827  A    C  
ATOM   3411  CE1 PHE A 429     -28.638  33.530  41.742  1.00 61.22      A    C  
ANISOU 3411  CE1 PHE A 429     8398   2282  12581    878   6228    156  A    C  
ATOM   3412  CE2 PHE A 429     -27.759  33.804  39.546  1.00 60.28      A    C  
ANISOU 3412  CE2 PHE A 429     8214   2127  12563    955   6186    491  A    C  
ATOM   3413  CZ  PHE A 429     -27.669  33.248  40.799  1.00 57.62      A    C  
ANISOU 3413  CZ  PHE A 429     7953   1858  12081    821   6059    167  A    C  
ATOM   3414  N   LYS A 430     -34.632  35.902  39.208  1.00 71.47      A    N  
ANISOU 3414  N   LYS A 430     8978   4049  14127   2091   7096   2201  A    N  
ATOM   3415  CA  LYS A 430     -35.818  36.745  39.022  1.00 75.19      A    C  
ANISOU 3415  CA  LYS A 430     9292   4578  14697   2426   7406   2573  A    C  
ATOM   3416  C   LYS A 430     -36.166  37.555  40.271  1.00 81.00      A    C  
ANISOU 3416  C   LYS A 430    10113   5021  15641   2478   7733   2390  A    C  
ATOM   3417  O   LYS A 430     -36.667  38.674  40.139  1.00 84.51      A    O  
ANISOU 3417  O   LYS A 430    10520   5271  16318   2779   8149   2626  A    O  
ATOM   3418  CB  LYS A 430     -37.023  35.892  38.613  1.00 78.58      A    C  
ANISOU 3418  CB  LYS A 430     9489   5571  14798   2479   7142   2866  A    C  
ATOM   3419  CG  LYS A 430     -37.777  36.482  37.436  1.00104.22      A    C  
ANISOU 3419  CG  LYS A 430    12508   9042  18050   2845   7315   3379  A    C  
ATOM   3420  CD  LYS A 430     -38.893  35.562  36.966  1.00120.03      A    C  
ANISOU 3420  CD  LYS A 430    14241  11678  19688   2849   7029   3617  A    C  
ATOM   3421  CE  LYS A 430     -39.394  35.945  35.592  1.00137.96      A    C  
ANISOU 3421  CE  LYS A 430    16249  14271  21899   3209   7149   4120  A    C  
ATOM   3422  NZ  LYS A 430     -38.388  35.668  34.525  1.00147.40      A    N1+
ANISOU 3422  NZ  LYS A 430    17471  15465  23069   3176   7027   4198  A    N1+
ATOM   3423  N   ASP A 431     -35.944  36.991  41.474  1.00 74.90      A    N  
ANISOU 3423  N   ASP A 431     9459   4221  14777   2208   7568   1983  A    N  
ATOM   3424  CA  ASP A 431     -36.216  37.680  42.741  1.00 76.01      A    C  
ANISOU 3424  CA  ASP A 431     9685   4107  15087   2215   7854   1750  A    C  
ATOM   3425  C   ASP A 431     -35.073  38.637  43.114  1.00 80.49      A    C  
ANISOU 3425  C   ASP A 431    10440   4167  15977   2132   8171   1414  A    C  
ATOM   3426  O   ASP A 431     -35.295  39.592  43.868  1.00 83.57      A    O  
ANISOU 3426  O   ASP A 431    10891   4253  16606   2219   8567   1305  A    O  
ATOM   3427  CB  ASP A 431     -36.446  36.667  43.877  1.00 76.06      A    C  
ANISOU 3427  CB  ASP A 431     9733   4334  14831   1968   7549   1461  A    C  
ATOM   3428  CG  ASP A 431     -37.637  35.758  43.661  1.00 89.08      A    C  
ANISOU 3428  CG  ASP A 431    11207   6458  16180   2006   7298   1737  A    C  
ATOM   3429  OD1 ASP A 431     -37.425  34.539  43.451  1.00 88.68      A    O  
ANISOU 3429  OD1 ASP A 431    11165   6681  15850   1801   6908   1687  A    O  
ATOM   3430  OD2 ASP A 431     -38.783  36.257  43.720  1.00 98.20      A    O1-
ANISOU 3430  OD2 ASP A 431    12218   7718  17377   2234   7508   1993  A    O1-
ATOM   3431  N   LYS A 432     -33.859  38.370  42.576  1.00 74.22      A    N  
ANISOU 3431  N   LYS A 432     9728   3291  15180   1951   8009   1234  A    N  
ATOM   3432  CA  LYS A 432     -32.611  39.111  42.793  1.00 74.12      A    C  
ANISOU 3432  CA  LYS A 432     9869   2865  15428   1804   8249    869  A    C  
ATOM   3433  C   LYS A 432     -32.256  40.001  41.571  1.00 78.58      A    C  
ANISOU 3433  C   LYS A 432    10439   3157  16259   1994   8571   1140  A    C  
ATOM   3434  O   LYS A 432     -31.135  40.501  41.480  1.00 77.78      A    O  
ANISOU 3434  O   LYS A 432    10453   2741  16360   1851   8751    868  A    O  
ATOM   3435  CB  LYS A 432     -31.457  38.117  43.083  1.00 72.95      A    C  
ANISOU 3435  CB  LYS A 432     9791   2856  15069   1482   7842    482  A    C  
ATOM   3436  CG  LYS A 432     -31.539  37.418  44.440  1.00 77.43      A    C  
ANISOU 3436  CG  LYS A 432    10402   3611  15408   1290   7604    141  A    C  
ATOM   3437  CD  LYS A 432     -30.393  36.428  44.639  1.00 75.37      A    C  
ANISOU 3437  CD  LYS A 432    10207   3514  14918   1039   7216   -178  A    C  
ATOM   3438  CE  LYS A 432     -30.457  35.696  45.959  1.00 82.83      A    C  
ANISOU 3438  CE  LYS A 432    11204   4659  15608    888   6990   -483  A    C  
ATOM   3439  NZ  LYS A 432     -30.043  36.560  47.101  1.00 94.30      A    N1+
ANISOU 3439  NZ  LYS A 432    12714   5894  17221    779   7267   -922  A    N1+
ATOM   3440  N   VAL A 433     -33.222  40.191  40.646  1.00 76.07      A    N  
ANISOU 3440  N   VAL A 433     9988   2991  15924   2320   8654   1675  A    N  
ATOM   3441  CA  VAL A 433     -33.136  40.989  39.416  1.00 77.70      A    C  
ANISOU 3441  CA  VAL A 433    10177   3014  16331   2587   8959   2052  A    C  
ATOM   3442  C   VAL A 433     -32.698  42.458  39.729  1.00 83.45      A    C  
ANISOU 3442  C   VAL A 433    11078   3136  17493   2656   9586   1908  A    C  
ATOM   3443  O   VAL A 433     -32.039  43.084  38.894  1.00 82.62      A    O  
ANISOU 3443  O   VAL A 433    11044   2753  17595   2735   9850   2022  A    O  
ATOM   3444  CB  VAL A 433     -34.492  40.885  38.647  1.00 82.81      A    C  
ANISOU 3444  CB  VAL A 433    10608   4038  16817   2955   8927   2638  A    C  
ATOM   3445  CG1 VAL A 433     -35.014  42.224  38.136  1.00 86.51      A    C  
ANISOU 3445  CG1 VAL A 433    11075   4223  17571   3378   9495   3035  A    C  
ATOM   3446  CG2 VAL A 433     -34.403  39.858  37.522  1.00 80.13      A    C  
ANISOU 3446  CG2 VAL A 433    10129   4139  16178   2923   8486   2863  A    C  
ATOM   3447  N   ASP A 434     -33.009  42.967  40.947  1.00 82.18      A    N  
ANISOU 3447  N   ASP A 434    10998   2763  17465   2596   9831   1625  A    N  
ATOM   3448  CA  ASP A 434     -32.607  44.309  41.385  1.00 85.68      A    C  
ANISOU 3448  CA  ASP A 434    11620   2619  18314   2603  10447   1411  A    C  
ATOM   3449  C   ASP A 434     -31.080  44.388  41.600  1.00 88.13      A    C  
ANISOU 3449  C   ASP A 434    12068   2672  18746   2211  10458    872  A    C  
ATOM   3450  O   ASP A 434     -30.487  45.433  41.357  1.00 90.60      A    O  
ANISOU 3450  O   ASP A 434    12521   2504  19398   2206  10957    775  A    O  
ATOM   3451  CB  ASP A 434     -33.359  44.720  42.662  1.00 89.40      A    C  
ANISOU 3451  CB  ASP A 434    12124   2984  18859   2621  10676   1228  A    C  
ATOM   3452  CG  ASP A 434     -32.998  43.933  43.900  1.00 97.61      A    C  
ANISOU 3452  CG  ASP A 434    13175   4221  19693   2244  10317    695  A    C  
ATOM   3453  OD1 ASP A 434     -33.519  42.800  44.058  1.00 98.69      A    O  
ANISOU 3453  OD1 ASP A 434    13184   4833  19482   2213   9824    785  A    O  
ATOM   3454  OD2 ASP A 434     -32.204  44.448  44.718  1.00 99.01      A    O1-
ANISOU 3454  OD2 ASP A 434    13485   4090  20046   1979  10545    183  A    O1-
ATOM   3455  N   ILE A 435     -30.456  43.284  42.037  1.00 81.08      A    N  
ANISOU 3455  N   ILE A 435    11133   2106  17570   1893   9931    530  A    N  
ATOM   3456  CA  ILE A 435     -29.016  43.201  42.274  1.00 80.71      A    C  
ANISOU 3456  CA  ILE A 435    11166   1935  17565   1528   9866     12  A    C  
ATOM   3457  C   ILE A 435     -28.287  43.100  40.898  1.00 84.49      A    C  
ANISOU 3457  C   ILE A 435    11637   2390  18075   1562   9803    232  A    C  
ATOM   3458  O   ILE A 435     -27.176  43.623  40.752  1.00 85.21      A    O  
ANISOU 3458  O   ILE A 435    11817   2191  18367   1363  10024    -73  A    O  
ATOM   3459  CB  ILE A 435     -28.667  42.015  43.235  1.00 80.85      A    C  
ANISOU 3459  CB  ILE A 435    11135   2349  17233   1239   9329   -387  A    C  
ATOM   3460  CG1 ILE A 435     -29.497  42.057  44.529  1.00 81.80      A    C  
ANISOU 3460  CG1 ILE A 435    11252   2547  17283   1244   9363   -528  A    C  
ATOM   3461  CG2 ILE A 435     -27.177  41.986  43.570  1.00 82.44      A    C  
ANISOU 3461  CG2 ILE A 435    11391   2465  17467    883   9295   -956  A    C  
ATOM   3462  CD1 ILE A 435     -29.664  40.667  45.259  1.00 89.32      A    C  
ANISOU 3462  CD1 ILE A 435    12141   3984  17812   1098   8784   -676  A    C  
ATOM   3463  N   LEU A 436     -28.925  42.442  39.902  1.00 78.90      A    N  
ANISOU 3463  N   LEU A 436    10812   2005  17163   1802   9515    745  A    N  
ATOM   3464  CA  LEU A 436     -28.386  42.289  38.554  1.00 78.00      A    C  
ANISOU 3464  CA  LEU A 436    10671   1927  17038   1872   9432   1011  A    C  
ATOM   3465  C   LEU A 436     -28.324  43.659  37.827  1.00 89.23      A    C  
ANISOU 3465  C   LEU A 436    12191   2870  18842   2103  10058   1264  A    C  
ATOM   3466  O   LEU A 436     -27.315  43.963  37.182  1.00 90.22      A    O  
ANISOU 3466  O   LEU A 436    12385   2787  19107   2000  10185   1183  A    O  
ATOM   3467  CB  LEU A 436     -29.207  41.267  37.743  1.00 75.14      A    C  
ANISOU 3467  CB  LEU A 436    10141   2070  16339   2063   8990   1476  A    C  
ATOM   3468  CG  LEU A 436     -29.179  39.775  38.218  1.00 74.61      A    C  
ANISOU 3468  CG  LEU A 436    10004   2468  15877   1832   8369   1276  A    C  
ATOM   3469  CD1 LEU A 436     -30.097  38.918  37.385  1.00 72.50      A    C  
ANISOU 3469  CD1 LEU A 436     9574   2658  15316   2012   8039   1732  A    C  
ATOM   3470  CD2 LEU A 436     -27.776  39.174  38.172  1.00 71.62      A    C  
ANISOU 3470  CD2 LEU A 436     9686   2108  15417   1526   8098    897  A    C  
ATOM   3471  N   ASP A 437     -29.367  44.499  37.991  1.00 88.31      A    N  
ANISOU 3471  N   ASP A 437    12094   2562  18897   2414  10475   1557  A    N  
ATOM   3472  CA  ASP A 437     -29.469  45.821  37.373  1.00 92.37      A    C  
ANISOU 3472  CA  ASP A 437    12727   2598  19771   2701  11130   1854  A    C  
ATOM   3473  C   ASP A 437     -28.450  46.829  37.957  1.00 99.25      A    C  
ANISOU 3473  C   ASP A 437    13815   2874  21021   2424  11644   1346  A    C  
ATOM   3474  O   ASP A 437     -28.329  47.952  37.449  1.00100.29      A    O  
ANISOU 3474  O   ASP A 437    14094   2526  21487   2600  12243   1524  A    O  
ATOM   3475  CB  ASP A 437     -30.909  46.358  37.514  1.00 96.47      A    C  
ANISOU 3475  CB  ASP A 437    13198   3121  20334   3129  11416   2293  A    C  
ATOM   3476  CG  ASP A 437     -31.924  45.616  36.656  1.00105.68      A    C  
ANISOU 3476  CG  ASP A 437    14131   4854  21170   3460  11043   2869  A    C  
ATOM   3477  OD1 ASP A 437     -31.520  45.025  35.623  1.00103.50      A    O  
ANISOU 3477  OD1 ASP A 437    13769   4834  20721   3462  10745   3063  A    O  
ATOM   3478  OD2 ASP A 437     -33.121  45.651  36.995  1.00115.09      A    O1-
ANISOU 3478  OD2 ASP A 437    15214   6243  22271   3715  11071   3121  A    O1-
ATOM   3479  N   LYS A 438     -27.691  46.410  38.988  1.00 95.39      A    N  
ANISOU 3479  N   LYS A 438    13341   2438  20465   1988  11419    713  A    N  
ATOM   3480  CA  LYS A 438     -26.656  47.234  39.621  1.00 97.52      A    C  
ANISOU 3480  CA  LYS A 438    13769   2252  21034   1644  11837    131  A    C  
ATOM   3481  C   LYS A 438     -25.313  47.108  38.884  1.00 98.75      A    C  
ANISOU 3481  C   LYS A 438    13943   2355  21224   1392  11758    -77  A    C  
ATOM   3482  O   LYS A 438     -24.483  48.016  38.972  1.00102.20      A    O  
ANISOU 3482  O   LYS A 438    14518   2341  21974   1178  12243   -419  A    O  
ATOM   3483  CB  LYS A 438     -26.460  46.827  41.091  1.00 98.71      A    C  
ANISOU 3483  CB  LYS A 438    13887   2568  21049   1305  11616   -465  A    C  
ATOM   3484  CG  LYS A 438     -27.623  47.111  42.021  1.00109.31      A    C  
ANISOU 3484  CG  LYS A 438    15239   3881  22411   1474  11785   -399  A    C  
ATOM   3485  CD  LYS A 438     -27.344  46.476  43.376  1.00113.33      A    C  
ANISOU 3485  CD  LYS A 438    15688   4684  22690   1141  11429   -952  A    C  
ATOM   3486  CE  LYS A 438     -28.204  47.045  44.466  1.00120.41      A    C  
ANISOU 3486  CE  LYS A 438    16634   5422  23693   1201  11742  -1072  A    C  
ATOM   3487  NZ  LYS A 438     -27.392  47.358  45.667  1.00125.21      A    N1+
ANISOU 3487  NZ  LYS A 438    17291   5928  24357    780  11868  -1809  A    N1+
ATOM   3488  N   VAL A 439     -25.098  45.985  38.181  1.00 89.07      A    N  
ANISOU 3488  N   VAL A 439    12579   1587  19677   1399  11170    107  A    N  
ATOM   3489  CA  VAL A 439     -23.836  45.694  37.489  1.00 86.61      A    C  
ANISOU 3489  CA  VAL A 439    12260   1300  19347   1168  11019    -81  A    C  
ATOM   3490  C   VAL A 439     -23.754  46.563  36.218  1.00 90.63      A    C  
ANISOU 3490  C   VAL A 439    12870   1439  20128   1414  11490    346  A    C  
ATOM   3491  O   VAL A 439     -24.765  46.809  35.550  1.00 90.46      A    O  
ANISOU 3491  O   VAL A 439    12838   1414  20116   1835  11629    944  A    O  
ATOM   3492  CB  VAL A 439     -23.667  44.167  37.197  1.00 85.61      A    C  
ANISOU 3492  CB  VAL A 439    11972   1775  18781   1103  10251    -31  A    C  
ATOM   3493  CG1 VAL A 439     -22.386  43.808  36.433  1.00 83.52      A    C  
ANISOU 3493  CG1 VAL A 439    11691   1560  18484    913  10088   -166  A    C  
ATOM   3494  CG2 VAL A 439     -23.852  43.286  38.428  1.00 83.31      A    C  
ANISOU 3494  CG2 VAL A 439    11609   1831  18214    894   9823   -417  A    C  
ATOM   3495  N   ASP A 440     -22.538  47.037  35.919  1.00 88.03      A    N  
ANISOU 3495  N   ASP A 440    12626    816  20005   1149  11747     25  A    N  
ATOM   3496  CA  ASP A 440     -22.227  47.857  34.749  1.00 90.80      A    C  
ANISOU 3496  CA  ASP A 440    13095    784  20622   1316  12216    351  A    C  
ATOM   3497  C   ASP A 440     -21.903  46.888  33.589  1.00 89.33      A    C  
ANISOU 3497  C   ASP A 440    12777   1014  20151   1402  11703    666  A    C  
ATOM   3498  O   ASP A 440     -20.742  46.590  33.306  1.00 86.98      A    O  
ANISOU 3498  O   ASP A 440    12458    764  19826   1113  11550    359  A    O  
ATOM   3499  CB  ASP A 440     -21.070  48.833  35.085  1.00 96.00      A    C  
ANISOU 3499  CB  ASP A 440    13907    930  21640    935  12761   -208  A    C  
ATOM   3500  CG  ASP A 440     -20.568  49.760  33.988  1.00110.29      A    C  
ANISOU 3500  CG  ASP A 440    15877   2261  23766   1034  13332     33  A    C  
ATOM   3501  OD1 ASP A 440     -20.985  49.590  32.820  1.00108.86      A    O  
ANISOU 3501  OD1 ASP A 440    15675   2188  23499   1413  13260    660  A    O  
ATOM   3502  OD2 ASP A 440     -19.751  50.655  34.298  1.00122.38      A    O1-
ANISOU 3502  OD2 ASP A 440    17552   3325  25622    722  13865   -418  A    O1-
ATOM   3503  N   TRP A 441     -22.959  46.410  32.923  1.00 84.39      A    N  
ANISOU 3503  N   TRP A 441    12032    749  19286   1784  11453   1273  A    N  
ATOM   3504  CA  TRP A 441     -22.905  45.455  31.826  1.00 81.83      A    C  
ANISOU 3504  CA  TRP A 441    11587    827  18679   1917  10965   1617  A    C  
ATOM   3505  C   TRP A 441     -22.094  45.936  30.627  1.00 88.30      A    C  
ANISOU 3505  C   TRP A 441    12480   1407  19662   1957  11241   1792  A    C  
ATOM   3506  O   TRP A 441     -21.332  45.142  30.093  1.00 86.38      A    O  
ANISOU 3506  O   TRP A 441    12156   1441  19226   1790  10839   1698  A    O  
ATOM   3507  CB  TRP A 441     -24.313  45.068  31.385  1.00 80.01      A    C  
ANISOU 3507  CB  TRP A 441    11224    960  18215   2343  10765   2223  A    C  
ATOM   3508  CG  TRP A 441     -25.051  44.279  32.428  1.00 78.36      A    C  
ANISOU 3508  CG  TRP A 441    10909   1105  17761   2268  10356   2060  A    C  
ATOM   3509  CD1 TRP A 441     -26.091  44.709  33.209  1.00 82.69      A    C  
ANISOU 3509  CD1 TRP A 441    11465   1580  18374   2442  10563   2148  A    C  
ATOM   3510  CD2 TRP A 441     -24.752  42.943  32.854  1.00 73.65      A    C  
ANISOU 3510  CD2 TRP A 441    10201    961  16821   1994   9704   1766  A    C  
ATOM   3511  CE2 TRP A 441     -25.673  42.612  33.869  1.00 76.75      A    C  
ANISOU 3511  CE2 TRP A 441    10541   1539  17081   2016   9546   1705  A    C  
ATOM   3512  CE3 TRP A 441     -23.796  41.984  32.469  1.00 71.59      A    C  
ANISOU 3512  CE3 TRP A 441     9892    960  16351   1748   9257   1558  A    C  
ATOM   3513  NE1 TRP A 441     -26.468  43.714  34.076  1.00 78.65      A    N  
ANISOU 3513  NE1 TRP A 441    10848   1459  17578   2281  10071   1927  A    N  
ATOM   3514  CZ2 TRP A 441     -25.660  41.367  34.512  1.00 72.59      A    C  
ANISOU 3514  CZ2 TRP A 441     9932   1426  16224   1798   8978   1450  A    C  
ATOM   3515  CZ3 TRP A 441     -23.777  40.762  33.118  1.00 69.29      A    C  
ANISOU 3515  CZ3 TRP A 441     9521   1068  15736   1549   8702   1308  A    C  
ATOM   3516  CH2 TRP A 441     -24.714  40.457  34.113  1.00 69.16      A    C  
ANISOU 3516  CH2 TRP A 441     9469   1214  15595   1578   8573   1266  A    C  
ATOM   3517  N   LYS A 442     -22.238  47.201  30.222  1.00 89.60      A    N  
ANISOU 3517  N   LYS A 442    12811   1056  20177   2177  11935   2041  A    N  
ATOM   3518  CA  LYS A 442     -21.506  47.825  29.114  1.00 91.32      A    C  
ANISOU 3518  CA  LYS A 442    13138    966  20594   2235  12311   2228  A    C  
ATOM   3519  C   LYS A 442     -19.991  47.865  29.427  1.00 93.61      A    C  
ANISOU 3519  C   LYS A 442    13489   1053  21026   1711  12350   1564  A    C  
ATOM   3520  O   LYS A 442     -19.181  47.476  28.582  1.00 90.54      A    O  
ANISOU 3520  O   LYS A 442    13058    793  20552   1614  12165   1579  A    O  
ATOM   3521  CB  LYS A 442     -22.069  49.223  28.825  1.00 99.15      A    C  
ANISOU 3521  CB  LYS A 442    14331   1396  21947   2599  13117   2620  A    C  
ATOM   3522  CG  LYS A 442     -21.471  49.948  27.611  1.00128.58      A    C  
ANISOU 3522  CG  LYS A 442    18193   4838  25823   2724  13485   2897  A    C  
ATOM   3523  CD  LYS A 442     -22.171  49.595  26.291  1.00139.74      A    C  
ANISOU 3523  CD  LYS A 442    19445   7108  26541   3080  12571   3465  A    C  
ATOM   3524  CE  LYS A 442     -21.325  49.939  25.093  1.00149.42      A    C  
ANISOU 3524  CE  LYS A 442    20706   8824  27245   2905  11780   3382  A    C  
ATOM   3525  NZ  LYS A 442     -21.454  48.916  24.017  1.00152.45      A    N1+
ANISOU 3525  NZ  LYS A 442    20899   9631  27393   3102  11486   3792  A    N1+
ATOM   3526  N   GLY A 443     -19.653  48.276  30.653  1.00 91.89      A    N  
ANISOU 3526  N   GLY A 443    13329    611  20975   1372  12559    982  A    N  
ATOM   3527  CA  GLY A 443     -18.285  48.314  31.157  1.00 91.89      A    C  
ANISOU 3527  CA  GLY A 443    13321    534  21057    842  12583    281  A    C  
ATOM   3528  C   GLY A 443     -17.655  46.936  31.226  1.00 89.86      A    C  
ANISOU 3528  C   GLY A 443    12892    807  20444    622  11808     11  A    C  
ATOM   3529  O   GLY A 443     -16.469  46.772  30.931  1.00 88.11      A    O  
ANISOU 3529  O   GLY A 443    12639    610  20229    330  11739   -317  A    O  
ATOM   3530  N   TRP A 444     -18.457  45.924  31.577  1.00 84.26      A    N  
ANISOU 3530  N   TRP A 444    12046    579  19389    765  11238    173  A    N  
ATOM   3531  CA  TRP A 444     -17.997  44.529  31.651  1.00 79.63      A    C  
ANISOU 3531  CA  TRP A 444    11291    555  18408    599  10504    -13  A    C  
ATOM   3532  C   TRP A 444     -17.909  43.839  30.289  1.00 82.43      A    C  
ANISOU 3532  C   TRP A 444    11574   1187  18559    788  10186    432  A    C  
ATOM   3533  O   TRP A 444     -16.964  43.085  30.074  1.00 78.37      A    O  
ANISOU 3533  O   TRP A 444    10981    924  17871    570   9822    183  A    O  
ATOM   3534  CB  TRP A 444     -18.915  43.697  32.561  1.00 75.86      A    C  
ANISOU 3534  CB  TRP A 444    10681    540  17602    648  10063     -1  A    C  
ATOM   3535  CG  TRP A 444     -18.581  43.786  34.018  1.00 76.61      A    C  
ANISOU 3535  CG  TRP A 444    10789    583  17737    342  10076   -616  A    C  
ATOM   3536  CD1 TRP A 444     -19.225  44.525  34.960  1.00 81.07      A    C  
ANISOU 3536  CD1 TRP A 444    11459    830  18515    372  10434   -750  A    C  
ATOM   3537  CD2 TRP A 444     -17.525  43.103  34.698  1.00 74.90      A    C  
ANISOU 3537  CD2 TRP A 444    10483    643  17335    -11   9716  -1188  A    C  
ATOM   3538  CE2 TRP A 444     -17.591  43.479  36.060  1.00 80.05      A    C  
ANISOU 3538  CE2 TRP A 444    11177   1158  18082   -189   9873  -1659  A    C  
ATOM   3539  CE3 TRP A 444     -16.526  42.209  34.292  1.00 73.72      A    C  
ANISOU 3539  CE3 TRP A 444    10264    767  16981   -154   9285  -1368  A    C  
ATOM   3540  NE1 TRP A 444     -18.627  44.362  36.186  1.00 79.98      A    N  
ANISOU 3540  NE1 TRP A 444    11278    799  18313     28  10320  -1383  A    N  
ATOM   3541  CZ2 TRP A 444     -16.699  42.982  37.018  1.00 79.10      A    C  
ANISOU 3541  CZ2 TRP A 444    10957   1319  17779   -517   9595  -2265  A    C  
ATOM   3542  CZ3 TRP A 444     -15.646  41.715  35.241  1.00 74.64      A    C  
ANISOU 3542  CZ3 TRP A 444    10290   1142  16928   -460   9021  -1955  A    C  
ATOM   3543  CH2 TRP A 444     -15.742  42.095  36.588  1.00 76.94      A    C  
ANISOU 3543  CH2 TRP A 444    10580   1389  17266   -632   9167  -2390  A    C  
ATOM   3544  N   MET A 445     -18.889  44.053  29.390  1.00 83.94      A    N  
ANISOU 3544  N   MET A 445    11774   1378  18742   1198  10306   1079  A    N  
ATOM   3545  CA  MET A 445     -18.970  43.334  28.113  1.00 85.02      A    C  
ANISOU 3545  CA  MET A 445    11816   1855  18634   1395   9973   1522  A    C  
ATOM   3546  C   MET A 445     -18.292  43.996  26.923  1.00 93.59      A    C  
ANISOU 3546  C   MET A 445    12978   2664  19915   1465  10342   1732  A    C  
ATOM   3547  O   MET A 445     -17.712  43.282  26.100  1.00 90.91      A    O  
ANISOU 3547  O   MET A 445    12562   2595  19384   1411  10010   1787  A    O  
ATOM   3548  CB  MET A 445     -20.438  43.099  27.711  1.00 88.62      A    C  
ANISOU 3548  CB  MET A 445    12187   2584  18902   1813   9850   2124  A    C  
ATOM   3549  CG  MET A 445     -21.251  42.310  28.715  1.00 91.94      A    C  
ANISOU 3549  CG  MET A 445    12513   3339  19079   1780   9446   2008  A    C  
ATOM   3550  SD  MET A 445     -20.754  40.603  28.787  1.00 93.33      A    S  
ANISOU 3550  SD  MET A 445    12562   4075  18826   1518   8660   1747  A    S  
ATOM   3551  CE  MET A 445     -21.900  39.997  30.013  1.00 88.62      A    C  
ANISOU 3551  CE  MET A 445    11905   3739  18028   1535   8383   1678  A    C  
ATOM   3552  N   HIS A 446     -18.439  45.330  26.766  1.00 95.18      A    N  
ANISOU 3552  N   HIS A 446    13342   2335  20486   1618  11039   1899  A    N  
ATOM   3553  CA  HIS A 446     -17.944  46.007  25.572  1.00 97.52      A    C  
ANISOU 3553  CA  HIS A 446    13734   2352  20966   1752  11445   2195  A    C  
ATOM   3554  C   HIS A 446     -17.042  47.205  25.851  1.00102.00      A    C  
ANISOU 3554  C   HIS A 446    14503   2279  21975   1501  12124   1824  A    C  
ATOM   3555  O   HIS A 446     -17.084  48.192  25.111  1.00104.83      A    O  
ANISOU 3555  O   HIS A 446    15018   2222  22592   1723  12712   2168  A    O  
ATOM   3556  CB  HIS A 446     -19.132  46.450  24.707  1.00101.10      A    C  
ANISOU 3556  CB  HIS A 446    14198   2817  21398   2307  11685   2957  A    C  
ATOM   3557  CG  HIS A 446     -20.053  45.335  24.344  1.00101.44      A    C  
ANISOU 3557  CG  HIS A 446    14023   3514  21006   2537  11065   3321  A    C  
ATOM   3558  CD2 HIS A 446     -19.937  44.400  23.374  1.00101.30      A    C  
ANISOU 3558  CD2 HIS A 446    13857   3968  20667   2587  10598   3540  A    C  
ATOM   3559  ND1 HIS A 446     -21.214  45.105  25.050  1.00102.77      A    N  
ANISOU 3559  ND1 HIS A 446    14108   3898  21041   2705  10905   3445  A    N  
ATOM   3560  CE1 HIS A 446     -21.774  44.046  24.491  1.00 99.76      A    C  
ANISOU 3560  CE1 HIS A 446    13528   4112  20264   2837  10357   3726  A    C  
ATOM   3561  NE2 HIS A 446     -21.045  43.589  23.473  1.00 99.11      A    N  
ANISOU 3561  NE2 HIS A 446    13403   4200  20055   2772  10158   3791  A    N  
ATOM   3562  N   THR A 447     -16.195  47.105  26.873  1.00 96.33      A    N  
ANISOU 3562  N   THR A 447    13776   1502  21324   1036  12054   1121  A    N  
ATOM   3563  CA  THR A 447     -15.253  48.169  27.177  1.00 99.46      A    C  
ANISOU 3563  CA  THR A 447    14329   1347  22113    714  12673    671  A    C  
ATOM   3564  C   THR A 447     -13.840  47.543  27.253  1.00 99.41      A    C  
ANISOU 3564  C   THR A 447    14202   1576  21995    253  12333     95  A    C  
ATOM   3565  O   THR A 447     -13.662  46.556  27.960  1.00 93.35      A    O  
ANISOU 3565  O   THR A 447    13269   1261  20939     67  11747   -241  A    O  
ATOM   3566  CB  THR A 447     -15.682  48.938  28.429  1.00109.25      A    C  
ANISOU 3566  CB  THR A 447    15677   2238  23593    606  13077    351  A    C  
ATOM   3567  CG2 THR A 447     -14.759  50.111  28.745  1.00111.25      A    C  
ANISOU 3567  CG2 THR A 447    16106   1892  24272    245  13792   -140  A    C  
ATOM   3568  OG1 THR A 447     -17.012  49.432  28.225  1.00114.39      A    O  
ANISOU 3568  OG1 THR A 447    16422   2727  24313   1092  13355    953  A    O  
ATOM   3569  N   PRO A 448     -12.823  48.114  26.544  1.00 98.49      A    N  
ANISOU 3569  N   PRO A 448    14165   1158  22097     77  12717    -20  A    N  
ATOM   3570  CA  PRO A 448     -11.454  47.554  26.634  1.00 96.71      A    C  
ANISOU 3570  CA  PRO A 448    13800   1181  21763   -358  12415   -586  A    C  
ATOM   3571  C   PRO A 448     -10.814  47.754  28.014  1.00100.96      A    C  
ANISOU 3571  C   PRO A 448    14286   1684  22391   -825  12489  -1379  A    C  
ATOM   3572  O   PRO A 448     -11.294  48.566  28.804  1.00103.41      A    O  
ANISOU 3572  O   PRO A 448    14714   1640  22936   -862  12926  -1526  A    O  
ATOM   3573  CB  PRO A 448     -10.667  48.345  25.570  1.00101.42      A    C  
ANISOU 3573  CB  PRO A 448    14523   1380  22631   -410  12943   -480  A    C  
ATOM   3574  CG  PRO A 448     -11.421  49.580  25.367  1.00109.95      A    C  
ANISOU 3574  CG  PRO A 448    15852   1858  24066   -146  13689   -105  A    C  
ATOM   3575  CD  PRO A 448     -12.869  49.284  25.639  1.00103.92      A    C  
ANISOU 3575  CD  PRO A 448    15073   1277  23133    279  13458    364  A    C  
ATOM   3576  N   GLY A 449      -9.735  47.017  28.277  1.00 94.61      A    N  
ANISOU 3576  N   GLY A 449    13295   1272  21381  -1164  12067  -1882  A    N  
ATOM   3577  CA  GLY A 449      -8.952  47.153  29.496  1.00 95.44      A    C  
ANISOU 3577  CA  GLY A 449    13296   1454  21514  -1625  12097  -2672  A    C  
ATOM   3578  C   GLY A 449      -9.464  46.436  30.715  1.00 97.27      A    C  
ANISOU 3578  C   GLY A 449    13407   2082  21470  -1629  11622  -2890  A    C  
ATOM   3579  O   GLY A 449     -10.084  45.370  30.612  1.00 93.48      A    O  
ANISOU 3579  O   GLY A 449    12853   2009  20656  -1354  11035  -2540  A    O  
ATOM   3580  N   MET A 450      -9.184  47.020  31.887  1.00 96.31      A    N  
ANISOU 3580  N   MET A 450    13266   1847  21482  -1962  11895  -3497  A    N  
ATOM   3581  CA  MET A 450      -9.546  46.425  33.170  1.00 94.38      A    C  
ANISOU 3581  CA  MET A 450    12900   1977  20982  -2016  11499  -3797  A    C  
ATOM   3582  C   MET A 450     -11.047  46.557  33.475  1.00 98.46      A    C  
ANISOU 3582  C   MET A 450    13552   2331  21526  -1656  11553  -3333  A    C  
ATOM   3583  O   MET A 450     -11.680  47.521  33.036  1.00100.46      A    O  
ANISOU 3583  O   MET A 450    14006   2060  22106  -1475  12116  -2987  A    O  
ATOM   3584  CB  MET A 450      -8.683  46.980  34.311  1.00 99.86      A    C  
ANISOU 3584  CB  MET A 450    13497   2668  21777  -2509  11767  -4633  A    C  
ATOM   3585  CG  MET A 450      -7.216  46.521  34.229  1.00103.44      A    C  
ANISOU 3585  CG  MET A 450    13724   3522  22057  -2854  11511  -5152  A    C  
ATOM   3586  SD  MET A 450      -6.987  44.737  33.994  1.00101.94      A    S  
ANISOU 3586  SD  MET A 450    13327   4096  21307  -2632  10542  -4946  A    S  
ATOM   3587  CE  MET A 450      -7.202  44.188  35.613  1.00 97.51      A    C  
ANISOU 3587  CE  MET A 450    12618   3993  20436  -2717  10164  -5378  A    C  
ATOM   3588  N   PRO A 451     -11.625  45.544  34.185  1.00 93.00      A    N  
ANISOU 3588  N   PRO A 451    12752   2106  20480  -1529  10967  -3297  A    N  
ATOM   3589  CA  PRO A 451     -13.063  45.564  34.494  1.00 92.81      A    C  
ANISOU 3589  CA  PRO A 451    12823   1997  20444  -1196  10967  -2871  A    C  
ATOM   3590  C   PRO A 451     -13.498  46.782  35.311  1.00103.61      A    C  
ANISOU 3590  C   PRO A 451    14327   2887  22151  -1294  11603  -3099  A    C  
ATOM   3591  O   PRO A 451     -12.671  47.370  36.018  1.00106.22      A    O  
ANISOU 3591  O   PRO A 451    14630   3101  22628  -1695  11901  -3742  A    O  
ATOM   3592  CB  PRO A 451     -13.259  44.282  35.305  1.00 90.43      A    C  
ANISOU 3592  CB  PRO A 451    12365   2291  19704  -1183  10265  -3002  A    C  
ATOM   3593  CG  PRO A 451     -12.153  43.401  34.925  1.00 91.86      A    C  
ANISOU 3593  CG  PRO A 451    12399   2870  19633  -1326   9823  -3192  A    C  
ATOM   3594  CD  PRO A 451     -11.001  44.318  34.723  1.00 91.18      A    C  
ANISOU 3594  CD  PRO A 451    12310   2502  19831  -1662  10293  -3624  A    C  
ATOM   3595  N   PRO A 452     -14.793  47.175  35.228  1.00101.97      A    N  
ANISOU 3595  N   PRO A 452    14257   2422  22064   -936  11831  -2594  A    N  
ATOM   3596  CA  PRO A 452     -15.247  48.387  35.947  1.00106.62      A    C  
ANISOU 3596  CA  PRO A 452    15005   2505  23002   -996  12494  -2776  A    C  
ATOM   3597  C   PRO A 452     -15.124  48.309  37.473  1.00112.23      A    C  
ANISOU 3597  C   PRO A 452    15624   3413  23607  -1302  12387  -3412  A    C  
ATOM   3598  O   PRO A 452     -14.774  49.310  38.095  1.00116.28      A    O  
ANISOU 3598  O   PRO A 452    16217   3559  24406  -1595  12943  -3890  A    O  
ATOM   3599  CB  PRO A 452     -16.716  48.532  35.528  1.00108.12      A    C  
ANISOU 3599  CB  PRO A 452    15307   2544  23231   -481  12594  -2043  A    C  
ATOM   3600  CG  PRO A 452     -17.095  47.211  34.972  1.00107.51      A    C  
ANISOU 3600  CG  PRO A 452    15078   3027  22744   -232  11859  -1624  A    C  
ATOM   3601  CD  PRO A 452     -15.870  46.613  34.389  1.00100.81      A    C  
ANISOU 3601  CD  PRO A 452    14124   2423  21756   -460  11550  -1835  A    C  
ATOM   3602  N   VAL A 453     -15.390  47.132  38.063  1.00104.86      A    N  
ANISOU 3602  N   VAL A 453    14529   3053  22261  -1243  11701  -3429  A    N  
ATOM   3603  CA  VAL A 453     -15.334  46.887  39.508  1.00104.84      A    C  
ANISOU 3603  CA  VAL A 453    14422   3334  22080  -1477  11512  -3973  A    C  
ATOM   3604  C   VAL A 453     -14.419  45.670  39.789  1.00106.01      A    C  
ANISOU 3604  C   VAL A 453    14348   4122  21807  -1657  10835  -4298  A    C  
ATOM   3605  O   VAL A 453     -14.366  44.746  38.976  1.00102.58      A    O  
ANISOU 3605  O   VAL A 453    13863   3963  21149  -1466  10382  -3923  A    O  
ATOM   3606  CB  VAL A 453     -16.776  46.696  40.073  1.00107.76      A    C  
ANISOU 3606  CB  VAL A 453    14843   3740  22360  -1162  11409  -3617  A    C  
ATOM   3607  CG1 VAL A 453     -17.600  45.726  39.221  1.00103.18      A    C  
ANISOU 3607  CG1 VAL A 453    14235   3443  21524   -754  10914  -2921  A    C  
ATOM   3608  CG2 VAL A 453     -16.783  46.288  41.552  1.00107.27      A    C  
ANISOU 3608  CG2 VAL A 453    14670   4021  22065  -1369  11161  -4131  A    C  
ATOM   3609  N   GLN A 454     -13.687  45.695  40.921  1.00103.61      A    N  
ANISOU 3609  N   GLN A 454    13914   4060  21394  -2017  10797  -4998  A    N  
ATOM   3610  CA  GLN A 454     -12.810  44.605  41.342  1.00100.77      A    C  
ANISOU 3610  CA  GLN A 454    13335   4335  20619  -2165  10200  -5347  A    C  
ATOM   3611  C   GLN A 454     -13.490  43.775  42.441  1.00102.24      A    C  
ANISOU 3611  C   GLN A 454    13458   4937  20453  -2043   9759  -5372  A    C  
ATOM   3612  O   GLN A 454     -13.938  44.355  43.438  1.00103.92      A    O  
ANISOU 3612  O   GLN A 454    13699   5028  20757  -2143  10030  -5642  A    O  
ATOM   3613  CB  GLN A 454     -11.440  45.126  41.827  1.00105.22      A    C  
ANISOU 3613  CB  GLN A 454    13749   4987  21242  -2640  10431  -6122  A    C  
ATOM   3614  CG  GLN A 454     -10.424  44.007  42.089  1.00117.45      A    C  
ANISOU 3614  CG  GLN A 454    15052   7219  22354  -2747   9828  -6436  A    C  
ATOM   3615  CD  GLN A 454      -9.146  44.486  42.732  1.00137.48      A    C  
ANISOU 3615  CD  GLN A 454    17386   9964  24886  -3213  10020  -7250  A    C  
ATOM   3616  NE2 GLN A 454      -8.287  45.133  41.955  1.00134.07      A    N  
ANISOU 3616  NE2 GLN A 454    16945   9275  24720  -3453  10389  -7434  A    N  
ATOM   3617  OE1 GLN A 454      -8.895  44.250  43.914  1.00131.09      A    O  
ANISOU 3617  OE1 GLN A 454    16409   9589  23810  -3364   9829  -7726  A    O  
ATOM   3618  N   PRO A 455     -13.553  42.423  42.296  1.00 94.08      A    N  
ANISOU 3618  N   PRO A 455    12348   4380  19016  -1840   9108  -5112  A    N  
ATOM   3619  CA  PRO A 455     -14.153  41.596  43.361  1.00 91.88      A    C  
ANISOU 3619  CA  PRO A 455    12027   4491  18393  -1728   8711  -5138  A    C  
ATOM   3620  C   PRO A 455     -13.327  41.614  44.652  1.00 97.71      A    C  
ANISOU 3620  C   PRO A 455    12593   5598  18932  -2028   8652  -5858  A    C  
ATOM   3621  O   PRO A 455     -12.115  41.826  44.595  1.00100.47      A    O  
ANISOU 3621  O   PRO A 455    12803   6086  19284  -2301   8718  -6315  A    O  
ATOM   3622  CB  PRO A 455     -14.165  40.180  42.754  1.00 88.80      A    C  
ANISOU 3622  CB  PRO A 455    11612   4483  17646  -1484   8095  -4735  A    C  
ATOM   3623  CG  PRO A 455     -13.942  40.365  41.305  1.00 92.82      A    C  
ANISOU 3623  CG  PRO A 455    12177   4734  18355  -1405   8207  -4376  A    C  
ATOM   3624  CD  PRO A 455     -13.089  41.583  41.177  1.00 92.24      A    C  
ANISOU 3624  CD  PRO A 455    12084   4338  18627  -1705   8735  -4788  A    C  
ATOM   3625  N   LYS A 456     -13.977  41.371  45.809  1.00 92.46      A    N  
ANISOU 3625  N   LYS A 456    11922   5137  18074  -1976   8521  -5961  A    N  
ATOM   3626  CA  LYS A 456     -13.304  41.311  47.113  1.00 93.66      A    C  
ANISOU 3626  CA  LYS A 456    11897   5719  17973  -2216   8426  -6612  A    C  
ATOM   3627  C   LYS A 456     -12.516  39.991  47.241  1.00 94.01      A    C  
ANISOU 3627  C   LYS A 456    11784   6400  17535  -2141   7815  -6682  A    C  
ATOM   3628  O   LYS A 456     -13.113  38.917  47.136  1.00 89.23      A    O  
ANISOU 3628  O   LYS A 456    11250   5988  16665  -1844   7391  -6242  A    O  
ATOM   3629  CB  LYS A 456     -14.309  41.456  48.278  1.00 96.44      A    C  
ANISOU 3629  CB  LYS A 456    12305   6079  18261  -2151   8488  -6651  A    C  
ATOM   3630  CG  LYS A 456     -15.099  42.764  48.265  1.00116.75      A    C  
ANISOU 3630  CG  LYS A 456    15035   8033  21294  -2200   9114  -6600  A    C  
ATOM   3631  CD  LYS A 456     -15.676  43.140  49.637  1.00129.66      A    C  
ANISOU 3631  CD  LYS A 456    16657   9730  22880  -2303   9284  -6957  A    C  
ATOM   3632  CE  LYS A 456     -14.883  44.208  50.366  1.00138.68      A    C  
ANISOU 3632  CE  LYS A 456    17701  10784  24207  -2736   9761  -7705  A    C  
ATOM   3633  NZ  LYS A 456     -14.880  45.510  49.646  1.00148.58      A    N1+
ANISOU 3633  NZ  LYS A 456    19110  11342  26000  -2859  10431  -7673  A    N1+
ATOM   3634  N   TYR A 457     -11.178  40.079  47.430  1.00 92.11      A    N  
ANISOU 3634  N   TYR A 457    11333   6481  17185  -2407   7796  -7229  A    N  
ATOM   3635  CA  TYR A 457     -10.311  38.907  47.561  1.00 90.26      A    C  
ANISOU 3635  CA  TYR A 457    10931   6871  16492  -2323   7260  -7329  A    C  
ATOM   3636  C   TYR A 457      -9.669  38.776  48.930  1.00 98.18      A    C  
ANISOU 3636  C   TYR A 457    11701   8460  17144  -2483   7127  -7949  A    C  
ATOM   3637  O   TYR A 457      -9.372  39.784  49.572  1.00102.00      A    O  
ANISOU 3637  O   TYR A 457    12076   8895  17786  -2810   7513  -8496  A    O  
ATOM   3638  CB  TYR A 457      -9.155  38.937  46.540  1.00 91.54      A    C  
ANISOU 3638  CB  TYR A 457    10990   7057  16735  -2448   7264  -7422  A    C  
ATOM   3639  CG  TYR A 457      -9.519  39.162  45.098  1.00 91.41      A    C  
ANISOU 3639  CG  TYR A 457    11159   6515  17055  -2331   7424  -6889  A    C  
ATOM   3640  CD1 TYR A 457     -10.030  38.129  44.319  1.00 88.51      A    C  
ANISOU 3640  CD1 TYR A 457    10919   6174  16536  -1993   7039  -6276  A    C  
ATOM   3641  CD2 TYR A 457      -9.222  40.364  44.472  1.00 95.50      A    C  
ANISOU 3641  CD2 TYR A 457    11711   6558  18016  -2573   7958  -7027  A    C  
ATOM   3642  CE1 TYR A 457     -10.309  38.315  42.969  1.00 86.45      A    C  
ANISOU 3642  CE1 TYR A 457    10798   5505  16545  -1886   7169  -5803  A    C  
ATOM   3643  CE2 TYR A 457      -9.486  40.559  43.123  1.00 95.24      A    C  
ANISOU 3643  CE2 TYR A 457    11837   6090  18261  -2441   8103  -6528  A    C  
ATOM   3644  CZ  TYR A 457     -10.027  39.530  42.373  1.00 95.96      A    C  
ANISOU 3644  CZ  TYR A 457    12029   6255  18175  -2094   7692  -5919  A    C  
ATOM   3645  OH  TYR A 457     -10.282  39.731  41.044  1.00 94.09      A    O  
ANISOU 3645  OH  TYR A 457    11925   5643  18183  -1964   7831  -5440  A    O  
ATOM   3646  N   ASP A 458      -9.375  37.524  49.335  1.00 95.09      A    N  
ANISOU 3646  N   ASP A 458    11225   8644  16261  -2255   6595  -7877  A    N  
ATOM   3647  CA  ASP A 458      -8.591  37.229  50.532  1.00 98.72      A    C  
ANISOU 3647  CA  ASP A 458    11426   9785  16299  -2342   6396  -8428  A    C  
ATOM   3648  C   ASP A 458      -7.126  37.436  50.121  1.00108.07      A    C  
ANISOU 3648  C   ASP A 458    12350  11263  17448  -2579   6416  -8873  A    C  
ATOM   3649  O   ASP A 458      -6.727  36.953  49.063  1.00105.68      A    O  
ANISOU 3649  O   ASP A 458    12083  10907  17164  -2458   6246  -8577  A    O  
ATOM   3650  CB  ASP A 458      -8.871  35.812  51.063  1.00 98.18      A    C  
ANISOU 3650  CB  ASP A 458    11399  10178  15725  -1959   5863  -8117  A    C  
ATOM   3651  CG  ASP A 458      -7.892  35.353  52.133  1.00114.86      A    C  
ANISOU 3651  CG  ASP A 458    13226  13084  17334  -1966   5598  -8614  A    C  
ATOM   3652  OD1 ASP A 458      -8.019  35.811  53.291  1.00118.10      A    O  
ANISOU 3652  OD1 ASP A 458    13513  13722  17639  -2119   5736  -9043  A    O  
ATOM   3653  OD2 ASP A 458      -6.995  34.544  51.809  1.00124.34      A    O1-
ANISOU 3653  OD2 ASP A 458    14318  14696  18229  -1802   5258  -8568  A    O1-
ATOM   3654  N   MET A 459      -6.353  38.202  50.905  1.00111.94      A    N  
ANISOU 3654  N   MET A 459    12578  12046  17909  -2939   6654  -9595  A    N  
ATOM   3655  CA  MET A 459      -4.967  38.585  50.575  1.00115.97      A    C  
ANISOU 3655  CA  MET A 459    12807  12835  18423  -3245   6756 -10113  A    C  
ATOM   3656  C   MET A 459      -3.902  37.801  51.352  1.00120.89      A    C  
ANISOU 3656  C   MET A 459    13086  14387  18459  -3180   6336 -10507  A    C  
ATOM   3657  O   MET A 459      -2.715  38.126  51.233  1.00121.76      A    O  
ANISOU 3657  O   MET A 459    12906  14842  18518  -3449   6408 -11010  A    O  
ATOM   3658  CB  MET A 459      -4.771  40.094  50.861  1.00123.98      A    C  
ANISOU 3658  CB  MET A 459    13736  13551  19819  -3753   7375 -10723  A    C  
ATOM   3659  CG  MET A 459      -5.813  41.000  50.223  1.00127.96      A    C  
ANISOU 3659  CG  MET A 459    14573  13144  20901  -3805   7866 -10375  A    C  
ATOM   3660  SD  MET A 459      -5.511  41.259  48.462  1.00131.30      A    S  
ANISOU 3660  SD  MET A 459    15149  12997  21740  -3809   8056  -9973  A    S  
ATOM   3661  CE  MET A 459      -6.926  42.278  48.063  1.00128.08      A    C  
ANISOU 3661  CE  MET A 459    15118  11636  21910  -3784   8620  -9561  A    C  
ATOM   3662  N   THR A 460      -4.318  36.786  52.143  1.00117.56      A    N  
ANISOU 3662  N   THR A 460    12692  14383  17592  -2818   5921 -10279  A    N  
ATOM   3663  CA  THR A 460      -3.442  35.972  52.999  1.00119.61      A    C  
ANISOU 3663  CA  THR A 460    12650  15555  17241  -2664   5517 -10580  A    C  
ATOM   3664  C   THR A 460      -2.200  35.447  52.239  1.00121.97      A    C  
ANISOU 3664  C   THR A 460    12749  16233  17363  -2604   5280 -10628  A    C  
ATOM   3665  O   THR A 460      -1.078  35.690  52.688  1.00125.90      A    O  
ANISOU 3665  O   THR A 460    12862  17359  17614  -2811   5270 -11236  A    O  
ATOM   3666  CB  THR A 460      -4.230  34.806  53.649  1.00130.24      A    C  
ANISOU 3666  CB  THR A 460    14175  17116  18195  -2191   5119 -10109  A    C  
ATOM   3667  CG2 THR A 460      -3.404  34.032  54.672  1.00133.29      A    C  
ANISOU 3667  CG2 THR A 460    14261  18456  17928  -1994   4749 -10412  A    C  
ATOM   3668  OG1 THR A 460      -5.407  35.311  54.282  1.00130.62      A    O  
ANISOU 3668  OG1 THR A 460    14409  16789  18430  -2252   5351 -10049  A    O  
ATOM   3669  N   LEU A 461      -2.397  34.763  51.100  1.00112.84      A    N  
ANISOU 3669  N   LEU A 461    11831  14720  16324  -2338   5104 -10016  A    N  
ATOM   3670  CA  LEU A 461      -1.294  34.172  50.337  1.00111.26      A    C  
ANISOU 3670  CA  LEU A 461    11475  14848  15952  -2236   4866  -9998  A    C  
ATOM   3671  C   LEU A 461      -0.588  35.167  49.405  1.00114.95      A    C  
ANISOU 3671  C   LEU A 461    11828  15008  16839  -2645   5228 -10295  A    C  
ATOM   3672  O   LEU A 461       0.583  34.957  49.072  1.00116.74      A    O  
ANISOU 3672  O   LEU A 461    11796  15668  16891  -2687   5099 -10538  A    O  
ATOM   3673  CB  LEU A 461      -1.797  32.970  49.522  1.00106.30      A    C  
ANISOU 3673  CB  LEU A 461    11156  13992  15242  -1779   4525  -9235  A    C  
ATOM   3674  CG  LEU A 461      -2.234  31.740  50.332  1.00109.58      A    C  
ANISOU 3674  CG  LEU A 461    11669  14803  15161  -1327   4123  -8929  A    C  
ATOM   3675  CD1 LEU A 461      -3.172  30.852  49.531  1.00104.84      A    C  
ANISOU 3675  CD1 LEU A 461    11472  13711  14650   -995   3954  -8168  A    C  
ATOM   3676  CD2 LEU A 461      -1.027  30.943  50.817  1.00114.39      A    C  
ANISOU 3676  CD2 LEU A 461    11974  16275  15214  -1112   3782  -9181  A    C  
ATOM   3677  N   ALA A 462      -1.286  36.238  48.992  1.00108.78      A    N  
ANISOU 3677  N   ALA A 462    11241  13493  16599  -2931   5695 -10268  A    N  
ATOM   3678  CA  ALA A 462      -0.760  37.229  48.055  1.00109.14      A    C  
ANISOU 3678  CA  ALA A 462    11249  13127  17094  -3307   6109 -10481  A    C  
ATOM   3679  C   ALA A 462       0.150  38.275  48.687  1.00117.60      A    C  
ANISOU 3679  C   ALA A 462    11974  14500  18210  -3823   6465 -11342  A    C  
ATOM   3680  O   ALA A 462       1.065  38.751  48.007  1.00119.15      A    O  
ANISOU 3680  O   ALA A 462    12016  14668  18587  -4109   6675 -11629  A    O  
ATOM   3681  CB  ALA A 462      -1.907  37.931  47.367  1.00107.77      A    C  
ANISOU 3681  CB  ALA A 462    11448  12037  17463  -3343   6485 -10044  A    C  
ATOM   3682  N   ASN A 463      -0.119  38.671  49.953  1.00115.91      A    N  
ANISOU 3682  N   ASN A 463    11640  14554  17846  -3968   6564 -11766  A    N  
ATOM   3683  CA  ASN A 463       0.615  39.717  50.676  1.00120.82      A    C  
ANISOU 3683  CA  ASN A 463    11937  15465  18504  -4499   6939 -12634  A    C  
ATOM   3684  C   ASN A 463       2.148  39.573  50.569  1.00127.16      A    C  
ANISOU 3684  C   ASN A 463    12300  16992  19023  -4689   6805 -13166  A    C  
ATOM   3685  O   ASN A 463       2.822  40.559  50.274  1.00129.67      A    O  
ANISOU 3685  O   ASN A 463    12460  17180  19628  -5182   7240 -13690  A    O  
ATOM   3686  CB  ASN A 463       0.180  39.779  52.145  1.00123.36      A    C  
ANISOU 3686  CB  ASN A 463    12151  16188  18533  -4514   6897 -12966  A    C  
ATOM   3687  CG  ASN A 463      -1.108  40.542  52.391  1.00144.73      A    C  
ANISOU 3687  CG  ASN A 463    15189  18154  21647  -4602   7294 -12799  A    C  
ATOM   3688  ND2 ASN A 463      -1.764  40.241  53.503  1.00137.08      A    N  
ANISOU 3688  ND2 ASN A 463    14238  17450  20396  -4425   7124 -12790  A    N  
ATOM   3689  OD1 ASN A 463      -1.519  41.417  51.614  1.00136.11      A    O  
ANISOU 3689  OD1 ASN A 463    14336  16266  21114  -4813   7771 -12679  A    O  
ATOM   3690  N   ALA A 464       2.683  38.350  50.737  1.00122.88      A    N  
ANISOU 3690  N   ALA A 464    11579  17173  17938  -4290   6234 -13002  A    N  
ATOM   3691  CA  ALA A 464       4.120  38.071  50.647  1.00125.12      A    C  
ANISOU 3691  CA  ALA A 464    11428  18223  17890  -4383   6048 -13444  A    C  
ATOM   3692  C   ALA A 464       4.672  38.318  49.232  1.00127.62      A    C  
ANISOU 3692  C   ALA A 464    11808  18108  18573  -4525   6220 -13296  A    C  
ATOM   3693  O   ALA A 464       5.817  38.771  49.109  1.00131.30      A    O  
ANISOU 3693  O   ALA A 464    11915  18966  19007  -4881   6366 -13878  A    O  
ATOM   3694  CB  ALA A 464       4.405  36.640  51.076  1.00124.19      A    C  
ANISOU 3694  CB  ALA A 464    11181  18878  17127  -3826   5415 -13168  A    C  
ATOM   3695  N   CYS A 465       3.854  38.053  48.181  1.00118.21      A    N  
ANISOU 3695  N   CYS A 465    11056  16133  17724  -4268   6222 -12545  A    N  
ATOM   3696  CA  CYS A 465       4.221  38.217  46.767  1.00115.75      A    C  
ANISOU 3696  CA  CYS A 465    10861  15355  17762  -4341   6372 -12293  A    C  
ATOM   3697  C   CYS A 465       4.332  39.696  46.383  1.00121.64      A    C  
ANISOU 3697  C   CYS A 465    11633  15516  19069  -4916   7050 -12700  A    C  
ATOM   3698  O   CYS A 465       5.291  40.076  45.703  1.00123.96      A    O  
ANISOU 3698  O   CYS A 465    11746  15861  19495  -5200   7236 -12997  A    O  
ATOM   3699  CB  CYS A 465       3.229  37.497  45.857  1.00110.26      A    C  
ANISOU 3699  CB  CYS A 465    10611  14061  17221  -3890   6170 -11387  A    C  
ATOM   3700  SG  CYS A 465       2.910  35.770  46.298  1.00110.33      A    S  
ANISOU 3700  SG  CYS A 465    10688  14602  16631  -3223   5459 -10857  A    S  
ATOM   3701  N   ILE A 466       3.328  40.511  46.785  1.00116.83      A    N  
ANISOU 3701  N   ILE A 466    11270  14323  18799  -5072   7441 -12687  A    N  
ATOM   3702  CA  ILE A 466       3.239  41.954  46.505  1.00118.99      A    C  
ANISOU 3702  CA  ILE A 466    11646  13928  19637  -5580   8157 -13017  A    C  
ATOM   3703  C   ILE A 466       4.425  42.690  47.162  1.00125.73      A    C  
ANISOU 3703  C   ILE A 466    12175  15326  20270  -5995   8243 -13723  A    C  
ATOM   3704  O   ILE A 466       5.023  43.573  46.536  1.00125.00      A    O  
ANISOU 3704  O   ILE A 466    12230  14916  20348  -6174   8410 -13608  A    O  
ATOM   3705  CB  ILE A 466       1.862  42.526  46.967  1.00121.20      A    C  
ANISOU 3705  CB  ILE A 466    12280  13546  20227  -5543   8467 -12766  A    C  
ATOM   3706  CG1 ILE A 466       0.685  41.693  46.410  1.00115.38      A    C  
ANISOU 3706  CG1 ILE A 466    11924  12411  19504  -4971   8132 -11824  A    C  
ATOM   3707  CG2 ILE A 466       1.701  44.011  46.591  1.00124.72      A    C  
ANISOU 3707  CG2 ILE A 466    12925  13201  21263  -5969   9208 -12947  A    C  
ATOM   3708  CD1 ILE A 466      -0.562  41.652  47.307  1.00122.83      A    C  
ANISOU 3708  CD1 ILE A 466    13072  13174  20423  -4778   8112 -11604  A    C  
ATOM   3709  N   THR A 467       4.773  42.291  48.405  1.00123.52      A    N  
ANISOU 3709  N   THR A 467    11560  15890  19482  -5983   7937 -14169  A    N  
ATOM   3710  CA  THR A 467       5.863  42.864  49.212  1.00123.58      A    C  
ANISOU 3710  CA  THR A 467    11455  16489  19012  -6057   7639 -14322  A    C  
ATOM   3711  C   THR A 467       7.235  42.634  48.538  1.00123.18      A    C  
ANISOU 3711  C   THR A 467    11161  16871  18770  -6101   7433 -14403  A    C  
ATOM   3712  O   THR A 467       7.931  43.604  48.242  1.00121.64      A    O  
ANISOU 3712  O   THR A 467    11067  16478  18672  -6332   7565 -14391  A    O  
ATOM   3713  CB  THR A 467       5.829  42.305  50.650  1.00133.60      A    C  
ANISOU 3713  CB  THR A 467    12829  18431  19502  -5510   6870 -13852  A    C  
ATOM   3714  CG2 THR A 467       4.738  42.909  51.461  1.00132.09      A    C  
ANISOU 3714  CG2 THR A 467    12828  17884  19477  -5600   7133 -13932  A    C  
ATOM   3715  OG1 THR A 467       5.601  40.898  50.634  1.00140.04      A    O  
ANISOU 3715  OG1 THR A 467    13564  19647  19999  -5057   6433 -13559  A    O  
ATOM   3716  N   LEU A 468       7.586  41.366  48.251  1.00120.60      A    N  
ANISOU 3716  N   LEU A 468    10387  17160  18275  -6012   7274 -14757  A    N  
ATOM   3717  CA  LEU A 468       8.853  40.983  47.611  1.00120.29      A    C  
ANISOU 3717  CA  LEU A 468    10080  17606  18019  -5999   7046 -14834  A    C  
ATOM   3718  C   LEU A 468       9.077  41.703  46.263  1.00121.18      A    C  
ANISOU 3718  C   LEU A 468    10463  16947  18632  -6194   7381 -14547  A    C  
ATOM   3719  O   LEU A 468      10.159  42.265  46.054  1.00120.91      A    O  
ANISOU 3719  O   LEU A 468    10390  17079  18472  -6326   7303 -14544  A    O  
ATOM   3720  CB  LEU A 468       8.930  39.458  47.440  1.00119.72      A    C  
ANISOU 3720  CB  LEU A 468     9678  18176  17636  -5639   6667 -14890  A    C  
ATOM   3721  CG  LEU A 468      10.262  38.857  46.946  1.00124.03      A    C  
ANISOU 3721  CG  LEU A 468    10011  19319  17797  -5431   6250 -14753  A    C  
ATOM   3722  CD1 LEU A 468      11.466  39.385  47.727  1.00125.05      A    C  
ANISOU 3722  CD1 LEU A 468    10079  19996  17440  -5438   5947 -14720  A    C  
ATOM   3723  CD2 LEU A 468      10.216  37.350  47.007  1.00125.15      A    C  
ANISOU 3723  CD2 LEU A 468    10024  20025  17501  -4861   5718 -14473  A    C  
ATOM   3724  N   GLY A 469       8.051  41.725  45.410  1.00117.66      A    N  
ANISOU 3724  N   GLY A 469    10174  15693  18837  -6344   7919 -14559  A    N  
ATOM   3725  CA  GLY A 469       8.095  42.397  44.113  1.00117.23      A    C  
ANISOU 3725  CA  GLY A 469    10384  14840  19316  -6529   8338 -14305  A    C  
ATOM   3726  C   GLY A 469       8.403  43.876  44.224  1.00121.40      A    C  
ANISOU 3726  C   GLY A 469    11316  14965  19848  -6615   8363 -13904  A    C  
ATOM   3727  O   GLY A 469       9.269  44.389  43.505  1.00121.55      A    O  
ANISOU 3727  O   GLY A 469    11365  14906  19915  -6742   8395 -13812  A    O  
ATOM   3728  N   GLN A 470       7.720  44.563  45.159  1.00119.14      A    N  
ANISOU 3728  N   GLN A 470    11175  14465  19626  -6727   8558 -14027  A    N  
ATOM   3729  CA  GLN A 470       7.922  45.977  45.437  1.00119.42      A    C  
ANISOU 3729  CA  GLN A 470    11507  14157  19709  -6881   8674 -13864  A    C  
ATOM   3730  C   GLN A 470       9.363  46.203  45.886  1.00123.80      A    C  
ANISOU 3730  C   GLN A 470    11954  15395  19690  -6797   8105 -13757  A    C  
ATOM   3731  O   GLN A 470      10.031  47.095  45.358  1.00123.60      A    O  
ANISOU 3731  O   GLN A 470    12064  15110  19787  -6961   8212 -13633  A    O  
ATOM   3732  CB  GLN A 470       6.922  46.460  46.512  1.00120.61      A    C  
ANISOU 3732  CB  GLN A 470    11886  14113  19828  -6799   8699 -13780  A    C  
ATOM   3733  CG  GLN A 470       6.366  47.854  46.254  1.00125.07      A    C  
ANISOU 3733  CG  GLN A 470    13062  13873  20586  -6636   8736 -13034  A    C  
ATOM   3734  CD  GLN A 470       7.110  48.963  46.957  1.00138.76      A    C  
ANISOU 3734  CD  GLN A 470    15190  15820  21714  -6238   7911 -12214  A    C  
ATOM   3735  NE2 GLN A 470       6.585  50.175  46.846  1.00132.58      A    N  
ANISOU 3735  NE2 GLN A 470    14607  14380  21386  -6544   8490 -12386  A    N  
ATOM   3736  OE1 GLN A 470       8.142  48.759  47.610  1.00137.11      A    O  
ANISOU 3736  OE1 GLN A 470    14679  16265  21151  -6363   7691 -12590  A    O  
ATOM   3737  N   LYS A 471       9.863  45.352  46.816  1.00123.02      A    N  
ANISOU 3737  N   LYS A 471    11473  16183  19085  -6703   7721 -14097  A    N  
ATOM   3738  CA  LYS A 471      11.229  45.445  47.343  1.00124.11      A    C  
ANISOU 3738  CA  LYS A 471    11414  17019  18725  -6683   7301 -14158  A    C  
ATOM   3739  C   LYS A 471      12.245  45.384  46.211  1.00127.52      A    C  
ANISOU 3739  C   LYS A 471    11845  17450  19159  -6632   7152 -13860  A    C  
ATOM   3740  O   LYS A 471      13.179  46.180  46.211  1.00127.74      A    O  
ANISOU 3740  O   LYS A 471    11907  17533  19095  -6768   7082 -13813  A    O  
ATOM   3741  CB  LYS A 471      11.506  44.345  48.386  1.00126.85      A    C  
ANISOU 3741  CB  LYS A 471    11499  18247  18449  -6337   6749 -14186  A    C  
ATOM   3742  CG  LYS A 471      10.939  44.667  49.771  1.00141.92      A    C  
ANISOU 3742  CG  LYS A 471    14121  19974  19827  -5599   5977 -12956  A    C  
ATOM   3743  CD  LYS A 471      11.165  43.542  50.782  1.00150.16      A    C  
ANISOU 3743  CD  LYS A 471    15293  21593  20167  -4922   5196 -12282  A    C  
ATOM   3744  CE  LYS A 471      10.737  43.946  52.178  1.00155.68      A    C  
ANISOU 3744  CE  LYS A 471    16510  22144  20498  -4466   4733 -11519  A    C  
ATOM   3745  NZ  LYS A 471      10.935  42.849  53.163  1.00160.61      A    N1+
ANISOU 3745  NZ  LYS A 471    17270  23216  20538  -3898   4144 -10949  A    N1+
ATOM   3746  N   TRP A 472      12.018  44.498  45.212  1.00125.01      A    N  
ANISOU 3746  N   TRP A 472    11334  17080  19084  -6647   7343 -14021  A    N  
ATOM   3747  CA  TRP A 472      12.917  44.336  44.073  1.00125.01      A    C  
ANISOU 3747  CA  TRP A 472    11223  17116  19159  -6703   7341 -13961  A    C  
ATOM   3748  C   TRP A 472      12.899  45.528  43.094  1.00127.01      A    C  
ANISOU 3748  C   TRP A 472    11925  16525  19809  -6801   7590 -13464  A    C  
ATOM   3749  O   TRP A 472      13.966  45.893  42.598  1.00126.53      A    O  
ANISOU 3749  O   TRP A 472    11791  16586  19698  -6924   7543 -13453  A    O  
ATOM   3750  CB  TRP A 472      12.628  43.030  43.319  1.00124.01      A    C  
ANISOU 3750  CB  TRP A 472    10843  17144  19132  -6575   7366 -14111  A    C  
ATOM   3751  CG  TRP A 472      13.408  41.856  43.840  1.00125.34      A    C  
ANISOU 3751  CG  TRP A 472    10603  18315  18704  -6292   6829 -14268  A    C  
ATOM   3752  CD1 TRP A 472      12.916  40.783  44.527  1.00127.46      A    C  
ANISOU 3752  CD1 TRP A 472    10734  19049  18647  -5950   6506 -14273  A    C  
ATOM   3753  CD2 TRP A 472      14.832  41.670  43.767  1.00125.70      A    C  
ANISOU 3753  CD2 TRP A 472    10396  19003  18362  -6241   6498 -14298  A    C  
ATOM   3754  CE2 TRP A 472      15.126  40.443  44.401  1.00128.75      A    C  
ANISOU 3754  CE2 TRP A 472    10539  20195  18184  -5808   5965 -14236  A    C  
ATOM   3755  CE3 TRP A 472      15.888  42.409  43.196  1.00126.77      A    C  
ANISOU 3755  CE3 TRP A 472    10608  19033  18526  -6388   6497 -14120  A    C  
ATOM   3756  NE1 TRP A 472      13.942  39.935  44.877  1.00127.60      A    N  
ANISOU 3756  NE1 TRP A 472    10382  19990  18108  -5715   6047 -14393  A    N  
ATOM   3757  CZ2 TRP A 472      16.434  39.958  44.521  1.00128.89      A    C  
ANISOU 3757  CZ2 TRP A 472    10263  20973  17737  -5648   5584 -14259  A    C  
ATOM   3758  CZ3 TRP A 472      17.182  41.920  43.302  1.00128.38      A    C  
ANISOU 3758  CZ3 TRP A 472    10557  19954  18268  -6210   6074 -14071  A    C  
ATOM   3759  CH2 TRP A 472      17.446  40.713  43.964  1.00129.27      A    C  
ANISOU 3759  CH2 TRP A 472    10370  20880  17866  -5845   5637 -14138  A    C  
ATOM   3760  N   VAL A 473      11.717  46.119  42.805  1.00124.46      A    N  
ANISOU 3760  N   VAL A 473    11914  15402  19974  -6908   8055 -13364  A    N  
ATOM   3761  CA  VAL A 473      11.617  47.256  41.871  1.00124.16      A    C  
ANISOU 3761  CA  VAL A 473    12238  14582  20354  -7047   8408 -13030  A    C  
ATOM   3762  C   VAL A 473      12.118  48.571  42.513  1.00126.01      A    C  
ANISOU 3762  C   VAL A 473    12730  14766  20382  -7055   8190 -12758  A    C  
ATOM   3763  O   VAL A 473      12.539  49.476  41.786  1.00125.25      A    O  
ANISOU 3763  O   VAL A 473    12804  14281  20505  -7211   8386 -12600  A    O  
ATOM   3764  CB  VAL A 473      10.207  47.459  41.239  1.00126.48      A    C  
ANISOU 3764  CB  VAL A 473    12938  14019  21100  -6889   8726 -12573  A    C  
ATOM   3765  CG1 VAL A 473       9.870  46.351  40.268  1.00125.88      A    C  
ANISOU 3765  CG1 VAL A 473    12736  13842  21252  -6795   8860 -12564  A    C  
ATOM   3766  CG2 VAL A 473       9.111  47.621  42.284  1.00126.50      A    C  
ANISOU 3766  CG2 VAL A 473    13080  13876  21110  -6811   8781 -12601  A    C  
ATOM   3767  N   LYS A 474      12.065  48.681  43.853  1.00123.71      A    N  
ANISOU 3767  N   LYS A 474    12345  14855  19806  -7074   8026 -13022  A    N  
ATOM   3768  CA  LYS A 474      12.495  49.900  44.543  1.00123.97      A    C  
ANISOU 3768  CA  LYS A 474    12556  14835  19713  -7166   7929 -12942  A    C  
ATOM   3769  C   LYS A 474      13.906  49.762  45.150  1.00127.35      A    C  
ANISOU 3769  C   LYS A 474    12813  15997  19578  -7020   7320 -12832  A    C  
ATOM   3770  O   LYS A 474      14.409  50.719  45.751  1.00127.52      A    O  
ANISOU 3770  O   LYS A 474    12937  16026  19487  -7113   7225 -12808  A    O  
ATOM   3771  CB  LYS A 474      11.468  50.324  45.610  1.00125.70      A    C  
ANISOU 3771  CB  LYS A 474    13013  14861  19886  -7033   7897 -12832  A    C  
ATOM   3772  CG  LYS A 474      10.155  50.835  45.014  1.00133.45      A    C  
ANISOU 3772  CG  LYS A 474    14596  15040  21066  -6574   7774 -11875  A    C  
ATOM   3773  CD  LYS A 474       9.462  51.859  45.898  1.00140.61      A    C  
ANISOU 3773  CD  LYS A 474    15969  15681  21774  -6217   7386 -11239  A    C  
ATOM   3774  CE  LYS A 474       9.473  53.246  45.304  1.00144.17      A    C  
ANISOU 3774  CE  LYS A 474    16857  15644  22279  -6019   7171 -10529  A    C  
ATOM   3775  NZ  LYS A 474       9.021  54.268  46.285  1.00147.23      A    N1+
ANISOU 3775  NZ  LYS A 474    17559  15878  22502  -5805   6892 -10189  A    N1+
ATOM   3776  N   ALA A 475      14.567  48.608  44.938  1.00124.97      A    N  
ANISOU 3776  N   ALA A 475    12121  16301  19060  -6990   7161 -13090  A    N  
ATOM   3777  CA  ALA A 475      15.919  48.380  45.448  1.00125.50      A    C  
ANISOU 3777  CA  ALA A 475    11931  17077  18678  -6948   6752 -13169  A    C  
ATOM   3778  C   ALA A 475      16.967  49.084  44.601  1.00127.79      A    C  
ANISOU 3778  C   ALA A 475    12345  17185  19025  -6987   6660 -12821  A    C  
ATOM   3779  O   ALA A 475      16.860  49.111  43.373  1.00126.86      A    O  
ANISOU 3779  O   ALA A 475    12285  16672  19244  -7082   6935 -12741  A    O  
ATOM   3780  CB  ALA A 475      16.224  46.892  45.496  1.00126.18      A    C  
ANISOU 3780  CB  ALA A 475    11668  17842  18432  -6714   6454 -13286  A    C  
ATOM   3781  N   THR A 476      17.992  49.638  45.256  1.00125.96      A    N  
ANISOU 3781  N   THR A 476    11999  17302  18557  -7113   6491 -12961  A    N  
ATOM   3782  CA  THR A 476      19.129  50.260  44.578  1.00125.89      A    C  
ANISOU 3782  CA  THR A 476    11984  17251  18600  -7255   6468 -12844  A    C  
ATOM   3783  C   THR A 476      20.259  49.213  44.572  1.00128.45      A    C  
ANISOU 3783  C   THR A 476    12018  18275  18512  -7018   6021 -12745  A    C  
ATOM   3784  O   THR A 476      19.996  48.049  44.893  1.00128.07      A    O  
ANISOU 3784  O   THR A 476    11748  18679  18235  -6832   5874 -12897  A    O  
ATOM   3785  CB  THR A 476      19.508  51.600  45.248  1.00132.10      A    C  
ANISOU 3785  CB  THR A 476    13163  17762  19267  -7122   6152 -12318  A    C  
ATOM   3786  CG2 THR A 476      18.478  52.698  44.999  1.00129.65      A    C  
ANISOU 3786  CG2 THR A 476    13188  16709  19366  -7285   6545 -12269  A    C  
ATOM   3787  OG1 THR A 476      19.691  51.398  46.650  1.00133.29      A    O  
ANISOU 3787  OG1 THR A 476    13231  18374  19041  -6999   5848 -12416  A    O  
ATOM   3788  N   GLU A 477      21.499  49.599  44.202  1.00126.08      A    N  
ANISOU 3788  N   GLU A 477    11560  18154  18193  -7213   6012 -12842  A    N  
ATOM   3789  CA  GLU A 477      22.634  48.672  44.230  1.00126.08      A    C  
ANISOU 3789  CA  GLU A 477    11212  18851  17841  -7081   5694 -12904  A    C  
ATOM   3790  C   GLU A 477      23.038  48.384  45.690  1.00128.60      A    C  
ANISOU 3790  C   GLU A 477    11484  19688  17688  -6832   5249 -12810  A    C  
ATOM   3791  O   GLU A 477      23.479  47.272  45.989  1.00128.58      A    O  
ANISOU 3791  O   GLU A 477    11195  20309  17349  -6628   4990 -12890  A    O  
ATOM   3792  CB  GLU A 477      23.824  49.211  43.417  1.00127.36      A    C  
ANISOU 3792  CB  GLU A 477    11381  18933  18078  -7179   5651 -12693  A    C  
ATOM   3793  CG  GLU A 477      23.712  48.918  41.929  1.00133.23      A    C  
ANISOU 3793  CG  GLU A 477    12376  19221  19023  -6927   5604 -12079  A    C  
ATOM   3794  CD  GLU A 477      24.934  49.280  41.107  1.00143.78      A    C  
ANISOU 3794  CD  GLU A 477    14077  20336  20216  -6470   5031 -10979  A    C  
ATOM   3795  OE1 GLU A 477      25.180  50.490  40.900  1.00139.54      A    O  
ANISOU 3795  OE1 GLU A 477    13574  19514  19931  -6848   5323 -11193  A    O  
ATOM   3796  OE2 GLU A 477      25.632  48.349  40.646  1.00137.13      A    O1-
ANISOU 3796  OE2 GLU A 477    12832  19984  19286  -6548   5085 -11334  A    O1-
ATOM   3797  N   SER A 478      22.833  49.374  46.595  1.00125.69      A    N  
ANISOU 3797  N   SER A 478    11235  19164  17356  -7035   5357 -12993  A    N  
ATOM   3798  CA  SER A 478      23.117  49.297  48.029  1.00125.91      A    C  
ANISOU 3798  CA  SER A 478    11199  19636  17007  -6918   5063 -13057  A    C  
ATOM   3799  C   SER A 478      22.160  48.342  48.788  1.00128.07      A    C  
ANISOU 3799  C   SER A 478    11473  20136  17053  -6611   4910 -13025  A    C  
ATOM   3800  O   SER A 478      22.547  47.817  49.835  1.00129.11      A    O  
ANISOU 3800  O   SER A 478    11461  20809  16785  -6417   4602 -13044  A    O  
ATOM   3801  CB  SER A 478      23.057  50.694  48.646  1.00128.24      A    C  
ANISOU 3801  CB  SER A 478    11862  19464  17399  -6989   5042 -12820  A    C  
ATOM   3802  OG  SER A 478      22.764  50.677  50.033  1.00134.98      A    O  
ANISOU 3802  OG  SER A 478    12995  20360  17931  -6600   4625 -12395  A    O  
ATOM   3803  N   ASP A 479      20.923  48.146  48.292  1.00123.52      A    N  
ANISOU 3803  N   ASP A 479    10889  19261  16783  -6762   5306 -13324  A    N  
ATOM   3804  CA  ASP A 479      19.906  47.293  48.927  1.00122.78      A    C  
ANISOU 3804  CA  ASP A 479    10725  19379  16547  -6580   5279 -13467  A    C  
ATOM   3805  C   ASP A 479      20.023  45.809  48.530  1.00124.12      A    C  
ANISOU 3805  C   ASP A 479    10647  20024  16488  -6273   5054 -13403  A    C  
ATOM   3806  O   ASP A 479      19.472  44.945  49.216  1.00122.92      A    O  
ANISOU 3806  O   ASP A 479    10350  20257  16096  -6084   4939 -13554  A    O  
ATOM   3807  CB  ASP A 479      18.502  47.797  48.563  1.00123.40      A    C  
ANISOU 3807  CB  ASP A 479    11122  18728  17039  -6650   5621 -13382  A    C  
ATOM   3808  CG  ASP A 479      18.145  49.158  49.123  1.00131.17      A    C  
ANISOU 3808  CG  ASP A 479    12685  19060  18094  -6505   5474 -12764  A    C  
ATOM   3809  OD1 ASP A 479      17.919  49.252  50.348  1.00132.33      A    O  
ANISOU 3809  OD1 ASP A 479    12898  19390  17992  -6391   5291 -12760  A    O  
ATOM   3810  OD2 ASP A 479      17.993  50.107  48.322  1.00134.53      A    O1-
ANISOU 3810  OD2 ASP A 479    13444  18829  18841  -6543   5598 -12392  A    O1-
ATOM   3811  N   LEU A 480      20.743  45.518  47.430  1.00121.77      A    N  
ANISOU 3811  N   LEU A 480    10115  19851  16302  -6397   5151 -13540  A    N  
ATOM   3812  CA  LEU A 480      20.927  44.169  46.883  1.00121.50      A    C  
ANISOU 3812  CA  LEU A 480     9780  20285  16098  -6173   5008 -13602  A    C  
ATOM   3813  C   LEU A 480      21.415  43.164  47.931  1.00125.09      A    C  
ANISOU 3813  C   LEU A 480    10093  21455  15982  -5748   4510 -13422  A    C  
ATOM   3814  O   LEU A 480      20.986  42.013  47.895  1.00124.64      A    O  
ANISOU 3814  O   LEU A 480     9842  21755  15760  -5507   4412 -13516  A    O  
ATOM   3815  CB  LEU A 480      21.882  44.178  45.680  1.00121.33      A    C  
ANISOU 3815  CB  LEU A 480     9657  20237  16208  -6261   5045 -13522  A    C  
ATOM   3816  CG  LEU A 480      21.393  44.887  44.416  1.00123.89      A    C  
ANISOU 3816  CG  LEU A 480    10321  19715  17038  -6403   5354 -13231  A    C  
ATOM   3817  CD1 LEU A 480      22.492  44.954  43.377  1.00124.04      A    C  
ANISOU 3817  CD1 LEU A 480    10239  19771  17121  -6481   5344 -13129  A    C  
ATOM   3818  CD2 LEU A 480      20.169  44.200  43.825  1.00125.55      A    C  
ANISOU 3818  CD2 LEU A 480    10631  19611  17462  -6250   5493 -13144  A    C  
ATOM   3819  N   GLY A 481      22.255  43.621  48.863  1.00123.49      A    N  
ANISOU 3819  N   GLY A 481     9793  21602  15523  -5828   4358 -13529  A    N  
ATOM   3820  CA  GLY A 481      22.800  42.811  49.948  1.00124.13      A    C  
ANISOU 3820  CA  GLY A 481     9692  22387  15085  -5515   3969 -13478  A    C  
ATOM   3821  C   GLY A 481      21.786  42.343  50.976  1.00126.72      A    C  
ANISOU 3821  C   GLY A 481    10168  22771  15208  -5240   3833 -13357  A    C  
ATOM   3822  O   GLY A 481      22.035  41.361  51.683  1.00126.67      A    O  
ANISOU 3822  O   GLY A 481     9973  23378  14779  -4925   3544 -13332  A    O  
ATOM   3823  N   SER A 482      20.638  43.040  51.071  1.00124.17      A    N  
ANISOU 3823  N   SER A 482     9981  22004  15192  -5506   4172 -13621  A    N  
ATOM   3824  CA  SER A 482      19.559  42.721  52.009  1.00124.01      A    C  
ANISOU 3824  CA  SER A 482    10025  22055  15038  -5363   4153 -13694  A    C  
ATOM   3825  C   SER A 482      18.796  41.454  51.593  1.00126.09      A    C  
ANISOU 3825  C   SER A 482    10223  22440  15247  -5039   4077 -13591  A    C  
ATOM   3826  O   SER A 482      18.278  40.753  52.464  1.00126.28      A    O  
ANISOU 3826  O   SER A 482    10184  22821  14976  -4792   3918 -13621  A    O  
ATOM   3827  CB  SER A 482      18.590  43.895  52.135  1.00126.02      A    C  
ANISOU 3827  CB  SER A 482    10708  21513  15661  -5550   4408 -13553  A    C  
ATOM   3828  OG  SER A 482      19.240  45.072  52.587  1.00133.44      A    O  
ANISOU 3828  OG  SER A 482    12110  22004  16586  -5477   4182 -12946  A    O  
ATOM   3829  N   PHE A 483      18.720  41.169  50.275  1.00122.73      A    N  
ANISOU 3829  N   PHE A 483     9599  21913  15119  -5197   4318 -13837  A    N  
ATOM   3830  CA  PHE A 483      18.011  40.007  49.728  1.00122.19      A    C  
ANISOU 3830  CA  PHE A 483     9357  22011  15060  -4983   4321 -13937  A    C  
ATOM   3831  C   PHE A 483      18.764  38.707  50.005  1.00126.34      A    C  
ANISOU 3831  C   PHE A 483     9742  23211  15050  -4453   3823 -13592  A    C  
ATOM   3832  O   PHE A 483      19.987  38.659  49.870  1.00126.46      A    O  
ANISOU 3832  O   PHE A 483     9633  23537  14877  -4414   3646 -13493  A    O  
ATOM   3833  CB  PHE A 483      17.768  40.166  48.220  1.00122.37      A    C  
ANISOU 3833  CB  PHE A 483     9454  21467  15575  -5168   4620 -13918  A    C  
ATOM   3834  CG  PHE A 483      16.857  41.313  47.840  1.00122.58      A    C  
ANISOU 3834  CG  PHE A 483     9836  20592  16147  -5496   5047 -13887  A    C  
ATOM   3835  CD1 PHE A 483      15.475  41.150  47.818  1.00123.92      A    C  
ANISOU 3835  CD1 PHE A 483    10197  20327  16562  -5430   5218 -13828  A    C  
ATOM   3836  CD2 PHE A 483      17.380  42.548  47.480  1.00123.60      A    C  
ANISOU 3836  CD2 PHE A 483    10217  20222  16523  -5758   5201 -13706  A    C  
ATOM   3837  CE1 PHE A 483      14.634  42.208  47.455  1.00123.70      A    C  
ANISOU 3837  CE1 PHE A 483    10505  19451  17043  -5706   5631 -13768  A    C  
ATOM   3838  CE2 PHE A 483      16.537  43.605  47.119  1.00124.86      A    C  
ANISOU 3838  CE2 PHE A 483    10767  19526  17148  -5960   5543 -13539  A    C  
ATOM   3839  CZ  PHE A 483      15.171  43.428  47.105  1.00122.83      A    C  
ANISOU 3839  CZ  PHE A 483    10575  18926  17170  -6003   5832 -13709  A    C  
ATOM   3840  N   SER A 484      18.025  37.656  50.398  1.00124.98      A    N  
ANISOU 3840  N   SER A 484     9383  23457  14648  -4172   3713 -13749  A    N  
ATOM   3841  CA  SER A 484      18.576  36.339  50.723  1.00125.88      A    C  
ANISOU 3841  CA  SER A 484     9272  24318  14239  -3677   3307 -13585  A    C  
ATOM   3842  C   SER A 484      17.621  35.224  50.276  1.00129.45      A    C  
ANISOU 3842  C   SER A 484     9779  24712  14693  -3299   3218 -13389  A    C  
ATOM   3843  O   SER A 484      16.548  35.522  49.744  1.00128.85      A    O  
ANISOU 3843  O   SER A 484     9790  24123  15045  -3517   3524 -13579  A    O  
ATOM   3844  CB  SER A 484      18.850  36.242  52.224  1.00129.45      A    C  
ANISOU 3844  CB  SER A 484     9906  25037  14242  -3395   2992 -13229  A    C  
ATOM   3845  OG  SER A 484      17.659  36.358  52.987  1.00136.28      A    O  
ANISOU 3845  OG  SER A 484    11240  25386  15154  -3227   2970 -12816  A    O  
ATOM   3846  N   ALA A 485      18.002  33.942  50.498  1.00128.13      A    N  
ANISOU 3846  N   ALA A 485     9321  25321  14043  -2837   2890 -13374  A    N  
ATOM   3847  CA  ALA A 485      17.178  32.774  50.144  1.00128.03      A    C  
ANISOU 3847  CA  ALA A 485     9185  25527  13934  -2456   2785 -13398  A    C  
ATOM   3848  C   ALA A 485      15.852  32.766  50.917  1.00131.18      A    C  
ANISOU 3848  C   ALA A 485     9850  25621  14370  -2364   2824 -13278  A    C  
ATOM   3849  O   ALA A 485      14.854  32.243  50.417  1.00130.54      A    O  
ANISOU 3849  O   ALA A 485     9711  25426  14464  -2263   2905 -13428  A    O  
ATOM   3850  CB  ALA A 485      17.945  31.489  50.414  1.00129.09      A    C  
ANISOU 3850  CB  ALA A 485     9181  26373  13496  -1858   2360 -13074  A    C  
ATOM   3851  N   ASP A 486      15.849  33.397  52.112  1.00129.62      A    N  
ANISOU 3851  N   ASP A 486     9687  25550  14011  -2514   2842 -13395  A    N  
ATOM   3852  CA  ASP A 486      14.721  33.538  53.036  1.00129.92      A    C  
ANISOU 3852  CA  ASP A 486     9861  25469  14034  -2506   2910 -13462  A    C  
ATOM   3853  C   ASP A 486      13.479  34.167  52.383  1.00133.19      A    C  
ANISOU 3853  C   ASP A 486    10542  25003  15062  -2815   3277 -13506  A    C  
ATOM   3854  O   ASP A 486      12.361  33.886  52.813  1.00133.34      A    O  
ANISOU 3854  O   ASP A 486    10609  24953  15101  -2710   3323 -13575  A    O  
ATOM   3855  CB  ASP A 486      15.140  34.402  54.244  1.00131.54      A    C  
ANISOU 3855  CB  ASP A 486    10304  25591  14083  -2644   2867 -13278  A    C  
ATOM   3856  CG  ASP A 486      16.376  33.934  55.002  1.00135.77      A    C  
ANISOU 3856  CG  ASP A 486    11085  26353  14149  -2234   2444 -12564  A    C  
ATOM   3857  OD1 ASP A 486      16.671  32.716  54.973  1.00135.29      A    O  
ANISOU 3857  OD1 ASP A 486    10873  26803  13727  -1787   2184 -12393  A    O  
ATOM   3858  OD2 ASP A 486      17.027  34.781  55.651  1.00138.98      A    O1-
ANISOU 3858  OD2 ASP A 486    11812  26429  14564  -2366   2394 -12225  A    O1-
ATOM   3859  N   ASP A 487      13.683  35.019  51.365  1.00130.81      A    N  
ANISOU 3859  N   ASP A 487    10183  24260  15258  -3297   3630 -13809  A    N  
ATOM   3860  CA  ASP A 487      12.637  35.737  50.630  1.00130.12      A    C  
ANISOU 3860  CA  ASP A 487    10261  23351  15827  -3691   4091 -13998  A    C  
ATOM   3861  C   ASP A 487      11.684  34.815  49.850  1.00132.94      A    C  
ANISOU 3861  C   ASP A 487    10640  23478  16393  -3454   4103 -13899  A    C  
ATOM   3862  O   ASP A 487      10.496  35.134  49.727  1.00131.73      A    O  
ANISOU 3862  O   ASP A 487    10629  22743  16680  -3656   4430 -14028  A    O  
ATOM   3863  CB  ASP A 487      13.279  36.722  49.638  1.00130.96      A    C  
ANISOU 3863  CB  ASP A 487    10536  22877  16347  -4061   4339 -13899  A    C  
ATOM   3864  CG  ASP A 487      14.270  37.724  50.210  1.00138.19      A    C  
ANISOU 3864  CG  ASP A 487    11900  23526  17078  -4028   4113 -13236  A    C  
ATOM   3865  OD1 ASP A 487      14.336  37.860  51.455  1.00139.81      A    O  
ANISOU 3865  OD1 ASP A 487    12216  23953  16953  -3891   3916 -13093  A    O  
ATOM   3866  OD2 ASP A 487      14.979  38.372  49.414  1.00140.17      A    O1-
ANISOU 3866  OD2 ASP A 487    12317  23403  17540  -4178   4169 -12987  A    O1-
ATOM   3867  N   VAL A 488      12.209  33.705  49.290  1.00131.44      A    N  
ANISOU 3867  N   VAL A 488    10107  23895  15939  -3141   3852 -14003  A    N  
ATOM   3868  CA  VAL A 488      11.425  32.785  48.452  1.00128.20      A    C  
ANISOU 3868  CA  VAL A 488     9909  23098  15704  -2793   3754 -13592  A    C  
ATOM   3869  C   VAL A 488      11.248  31.394  49.112  1.00131.44      A    C  
ANISOU 3869  C   VAL A 488    10380  24049  15512  -2069   3242 -13135  A    C  
ATOM   3870  O   VAL A 488      10.336  30.660  48.720  1.00126.44      A    O  
ANISOU 3870  O   VAL A 488    10236  22823  14984  -1677   3096 -12408  A    O  
ATOM   3871  CB  VAL A 488      12.014  32.668  47.010  1.00130.13      A    C  
ANISOU 3871  CB  VAL A 488    10215  23010  16218  -2822   3792 -13369  A    C  
ATOM   3872  CG1 VAL A 488      12.031  34.022  46.304  1.00130.96      A    C  
ANISOU 3872  CG1 VAL A 488    10360  22439  16961  -3494   4341 -13707  A    C  
ATOM   3873  CG2 VAL A 488      13.407  32.032  46.999  1.00132.98      A    C  
ANISOU 3873  CG2 VAL A 488    10091  24366  16068  -2616   3495 -13639  A    C  
ATOM   3874  N   LYS A 489      12.065  31.098  50.160  1.00132.59      A    N  
ANISOU 3874  N   LYS A 489    10032  25313  15033  -1916   3011 -13585  A    N  
ATOM   3875  CA  LYS A 489      12.120  29.861  50.959  1.00132.35      A    C  
ANISOU 3875  CA  LYS A 489     9959  25986  14342  -1232   2560 -13271  A    C  
ATOM   3876  C   LYS A 489      10.746  29.426  51.504  1.00132.03      A    C  
ANISOU 3876  C   LYS A 489    10403  25437  14326   -930   2490 -12734  A    C  
ATOM   3877  O   LYS A 489      10.424  28.236  51.447  1.00128.85      A    O  
ANISOU 3877  O   LYS A 489    10288  25003  13664   -323   2186 -12098  A    O  
ATOM   3878  CB  LYS A 489      13.098  30.044  52.137  1.00136.35      A    C  
ANISOU 3878  CB  LYS A 489    10416  27050  14340  -1149   2363 -13161  A    C  
ATOM   3879  CG  LYS A 489      13.641  28.737  52.716  1.00143.74      A    C  
ANISOU 3879  CG  LYS A 489    11796  28116  14703   -367   1881 -12110  A    C  
ATOM   3880  CD  LYS A 489      13.409  28.637  54.224  1.00147.53      A    C  
ANISOU 3880  CD  LYS A 489    12748  28414  14894   -159   1739 -11501  A    C  
ATOM   3881  CE  LYS A 489      14.516  29.248  55.050  1.00150.92      A    C  
ANISOU 3881  CE  LYS A 489    13602  28481  15260   -294   1663 -10912  A    C  
ATOM   3882  NZ  LYS A 489      14.217  29.169  56.504  1.00156.24      A    N1+
ANISOU 3882  NZ  LYS A 489    14725  28926  15715   -124   1554 -10384  A    N1+
ATOM   3883  N   ASP A 490       9.956  30.381  52.037  1.00128.01      A    N  
ANISOU 3883  N   ASP A 490     9981  24533  14123  -1356   2792 -13001  A    N  
ATOM   3884  CA  ASP A 490       8.631  30.126  52.612  1.00124.63      A    C  
ANISOU 3884  CA  ASP A 490     9975  23633  13747  -1147   2773 -12572  A    C  
ATOM   3885  C   ASP A 490       7.500  30.276  51.573  1.00122.27      A    C  
ANISOU 3885  C   ASP A 490    10257  22106  14094  -1231   2970 -11983  A    C  
ATOM   3886  O   ASP A 490       6.327  30.268  51.959  1.00119.39      A    O  
ANISOU 3886  O   ASP A 490    10236  21246  13882  -1177   3037 -11687  A    O  
ATOM   3887  CB  ASP A 490       8.382  31.081  53.799  1.00130.43      A    C  
ANISOU 3887  CB  ASP A 490    10472  24648  14439  -1547   2999 -13195  A    C  
ATOM   3888  CG  ASP A 490       9.321  30.919  54.982  1.00144.42      A    C  
ANISOU 3888  CG  ASP A 490    12244  27050  15578  -1282   2688 -12954  A    C  
ATOM   3889  OD1 ASP A 490       8.945  31.339  56.101  1.00145.52      A    O  
ANISOU 3889  OD1 ASP A 490    12563  27147  15582  -1322   2704 -12870  A    O  
ATOM   3890  OD2 ASP A 490      10.444  30.399  54.787  1.00150.26      A    O1-
ANISOU 3890  OD2 ASP A 490    13155  27897  16040   -973   2401 -12377  A    O1-
ATOM   3891  N   LEU A 491       7.834  30.370  50.264  1.00116.56      A    N  
ANISOU 3891  N   LEU A 491     9638  20930  13721  -1336   3051 -11796  A    N  
ATOM   3892  CA  LEU A 491       6.810  30.564  49.235  1.00111.21      A    C  
ANISOU 3892  CA  LEU A 491     9467  19158  13629  -1418   3245 -11259  A    C  
ATOM   3893  C   LEU A 491       6.541  29.301  48.431  1.00111.62      A    C  
ANISOU 3893  C   LEU A 491     9871  18945  13596   -893   2942 -10505  A    C  
ATOM   3894  O   LEU A 491       7.469  28.557  48.120  1.00112.70      A    O  
ANISOU 3894  O   LEU A 491     9833  19581  13408   -612   2693 -10465  A    O  
ATOM   3895  CB  LEU A 491       7.183  31.707  48.265  1.00111.59      A    C  
ANISOU 3895  CB  LEU A 491     9447  18723  14229  -1978   3648 -11564  A    C  
ATOM   3896  CG  LEU A 491       7.397  33.127  48.817  1.00120.34      A    C  
ANISOU 3896  CG  LEU A 491    10275  19882  15567  -2606   4074 -12321  A    C  
ATOM   3897  CD1 LEU A 491       7.808  34.068  47.712  1.00120.75      A    C  
ANISOU 3897  CD1 LEU A 491    10310  19429  16142  -3079   4466 -12523  A    C  
ATOM   3898  CD2 LEU A 491       6.137  33.677  49.474  1.00122.71      A    C  
ANISOU 3898  CD2 LEU A 491    10852  19664  16108  -2728   4298 -12243  A    C  
ATOM   3899  N   SER A 492       5.272  29.080  48.067  1.00103.71      A    N  
ANISOU 3899  N   SER A 492     9357  17159  12890   -774   2985  -9923  A    N  
ATOM   3900  CA  SER A 492       4.866  27.961  47.218  1.00 99.32      A    C  
ANISOU 3900  CA  SER A 492     9179  16237  12321   -350   2758  -9212  A    C  
ATOM   3901  C   SER A 492       5.201  28.296  45.762  1.00101.90      A    C  
ANISOU 3901  C   SER A 492     9573  16075  13068   -564   2911  -9096  A    C  
ATOM   3902  O   SER A 492       5.540  29.446  45.475  1.00103.02      A    O  
ANISOU 3902  O   SER A 492     9530  16062  13552  -1040   3228  -9516  A    O  
ATOM   3903  CB  SER A 492       3.373  27.685  47.380  1.00 99.31      A    C  
ANISOU 3903  CB  SER A 492     9632  15630  12472   -197   2770  -8695  A    C  
ATOM   3904  OG  SER A 492       2.602  28.818  47.017  1.00107.13      A    O  
ANISOU 3904  OG  SER A 492    10764  15924  14015   -617   3133  -8734  A    O  
ATOM   3905  N   SER A 493       5.109  27.309  44.847  1.00 95.97      A    N  
ANISOU 3905  N   SER A 493     9094  15079  12291   -224   2711  -8539  A    N  
ATOM   3906  CA  SER A 493       5.373  27.504  43.418  1.00 94.18      A    C  
ANISOU 3906  CA  SER A 493     8962  14397  12426   -371   2825  -8358  A    C  
ATOM   3907  C   SER A 493       4.452  28.592  42.820  1.00 96.17      A    C  
ANISOU 3907  C   SER A 493     9428  13833  13279   -770   3201  -8273  A    C  
ATOM   3908  O   SER A 493       4.934  29.448  42.077  1.00 96.49      A    O  
ANISOU 3908  O   SER A 493     9344  13664  13652  -1121   3461  -8504  A    O  
ATOM   3909  CB  SER A 493       5.210  26.186  42.659  1.00 95.37      A    C  
ANISOU 3909  CB  SER A 493     9423  14389  12426     80   2552  -7741  A    C  
ATOM   3910  OG  SER A 493       3.878  25.708  42.756  1.00104.92      A    O  
ANISOU 3910  OG  SER A 493    11046  15108  13710    258   2516  -7238  A    O  
ATOM   3911  N   HIS A 494       3.151  28.594  43.201  1.00 91.03      A    N  
ANISOU 3911  N   HIS A 494     9080  12756  12752   -709   3251  -7962  A    N  
ATOM   3912  CA  HIS A 494       2.145  29.575  42.750  1.00 89.00      A    C  
ANISOU 3912  CA  HIS A 494     9040  11750  13024  -1009   3603  -7826  A    C  
ATOM   3913  C   HIS A 494       2.454  30.968  43.288  1.00 92.56      A    C  
ANISOU 3913  C   HIS A 494     9230  12230  13707  -1482   3976  -8445  A    C  
ATOM   3914  O   HIS A 494       2.202  31.961  42.605  1.00 91.25      A    O  
ANISOU 3914  O   HIS A 494     9141  11515  14014  -1799   4343  -8466  A    O  
ATOM   3915  CB  HIS A 494       0.728  29.129  43.143  1.00 87.67      A    C  
ANISOU 3915  CB  HIS A 494     9217  11241  12854   -791   3531  -7369  A    C  
ATOM   3916  CG  HIS A 494       0.295  27.889  42.416  1.00 88.26      A    C  
ANISOU 3916  CG  HIS A 494     9594  11141  12797   -411   3255  -6752  A    C  
ATOM   3917  CD2 HIS A 494      -0.256  27.757  41.187  1.00 87.56      A    C  
ANISOU 3917  CD2 HIS A 494     9770  10507  12993   -390   3303  -6285  A    C  
ATOM   3918  ND1 HIS A 494       0.518  26.618  42.938  1.00 90.33      A    N  
ANISOU 3918  ND1 HIS A 494     9893  11854  12575     -8   2907  -6602  A    N  
ATOM   3919  CE1 HIS A 494       0.059  25.764  42.032  1.00 86.66      A    C  
ANISOU 3919  CE1 HIS A 494     9731  11061  12137    215   2776  -6069  A    C  
ATOM   3920  NE2 HIS A 494      -0.411  26.398  40.958  1.00 85.18      A    N  
ANISOU 3920  NE2 HIS A 494     9672  10300  12392     -9   2990  -5872  A    N  
ATOM   3921  N   GLN A 495       3.040  31.036  44.490  1.00 91.50      A    N  
ANISOU 3921  N   GLN A 495     8783  12754  13228  -1526   3901  -8957  A    N  
ATOM   3922  CA  GLN A 495       3.473  32.292  45.095  1.00 95.36      A    C  
ANISOU 3922  CA  GLN A 495     8977  13384  13871  -2002   4249  -9640  A    C  
ATOM   3923  C   GLN A 495       4.696  32.843  44.341  1.00 99.53      A    C  
ANISOU 3923  C   GLN A 495     9226  14049  14543  -2315   4421 -10033  A    C  
ATOM   3924  O   GLN A 495       4.771  34.050  44.111  1.00 99.97      A    O  
ANISOU 3924  O   GLN A 495     9223  13757  15003  -2774   4861 -10376  A    O  
ATOM   3925  CB  GLN A 495       3.773  32.116  46.590  1.00100.29      A    C  
ANISOU 3925  CB  GLN A 495     9318  14766  14023  -1940   4084 -10079  A    C  
ATOM   3926  CG  GLN A 495       2.522  32.198  47.462  1.00117.38      A    C  
ANISOU 3926  CG  GLN A 495    11715  16676  16209  -1864   4130  -9906  A    C  
ATOM   3927  CD  GLN A 495       2.820  31.990  48.923  1.00143.10      A    C  
ANISOU 3927  CD  GLN A 495    14696  20707  18967  -1775   3956 -10311  A    C  
ATOM   3928  NE2 GLN A 495       2.382  32.917  49.753  1.00139.30      A    N  
ANISOU 3928  NE2 GLN A 495    14163  20147  18619  -2076   4232 -10679  A    N  
ATOM   3929  OE1 GLN A 495       3.418  30.990  49.329  1.00141.10      A    O  
ANISOU 3929  OE1 GLN A 495    14288  21127  18196  -1411   3584 -10277  A    O  
ATOM   3930  N   LEU A 496       5.619  31.956  43.912  1.00 96.18      A    N  
ANISOU 3930  N   LEU A 496     8653  14088  13802  -2060   4103  -9957  A    N  
ATOM   3931  CA  LEU A 496       6.794  32.348  43.131  1.00 97.79      A    C  
ANISOU 3931  CA  LEU A 496     8592  14454  14111  -2315   4229 -10284  A    C  
ATOM   3932  C   LEU A 496       6.379  32.811  41.722  1.00 97.21      A    C  
ANISOU 3932  C   LEU A 496     8820  13537  14577  -2464   4502  -9902  A    C  
ATOM   3933  O   LEU A 496       6.991  33.746  41.200  1.00 98.86      A    O  
ANISOU 3933  O   LEU A 496     8878  13594  15091  -2876   4850 -10258  A    O  
ATOM   3934  CB  LEU A 496       7.846  31.222  43.061  1.00 98.43      A    C  
ANISOU 3934  CB  LEU A 496     8443  15269  13689  -1949   3806 -10264  A    C  
ATOM   3935  CG  LEU A 496       9.248  31.575  42.474  1.00106.40      A    C  
ANISOU 3935  CG  LEU A 496     9072  16659  14696  -2206   3895 -10713  A    C  
ATOM   3936  CD1 LEU A 496       9.804  32.899  43.012  1.00111.83      A    C  
ANISOU 3936  CD1 LEU A 496     9391  17566  15533  -2796   4280 -11510  A    C  
ATOM   3937  CD2 LEU A 496      10.247  30.470  42.736  1.00109.83      A    C  
ANISOU 3937  CD2 LEU A 496     9232  17949  14550  -1795   3466 -10745  A    C  
ATOM   3938  N   ILE A 497       5.324  32.195  41.131  1.00 88.34      A    N  
ANISOU 3938  N   ILE A 497     8116  11880  13568  -2147   4372  -9196  A    N  
ATOM   3939  CA  ILE A 497       4.805  32.586  39.811  1.00 86.26      A    C  
ANISOU 3939  CA  ILE A 497     8147  10851  13778  -2235   4611  -8776  A    C  
ATOM   3940  C   ILE A 497       4.270  34.041  39.883  1.00 93.97      A    C  
ANISOU 3940  C   ILE A 497     9189  11272  15245  -2666   5146  -9001  A    C  
ATOM   3941  O   ILE A 497       4.625  34.868  39.035  1.00 95.11      A    O  
ANISOU 3941  O   ILE A 497     9324  11056  15758  -2963   5501  -9105  A    O  
ATOM   3942  CB  ILE A 497       3.731  31.583  39.284  1.00 84.67      A    C  
ANISOU 3942  CB  ILE A 497     8345  10285  13539  -1810   4346  -8014  A    C  
ATOM   3943  CG1 ILE A 497       4.376  30.245  38.880  1.00 83.37      A    C  
ANISOU 3943  CG1 ILE A 497     8158  10531  12987  -1430   3918  -7776  A    C  
ATOM   3944  CG2 ILE A 497       2.934  32.166  38.103  1.00 83.80      A    C  
ANISOU 3944  CG2 ILE A 497     8535   9380  13925  -1916   4639  -7589  A    C  
ATOM   3945  CD1 ILE A 497       3.458  29.020  39.007  1.00 89.17      A    C  
ANISOU 3945  CD1 ILE A 497     9207  11193  13479   -984   3586  -7208  A    C  
ATOM   3946  N   GLU A 498       3.475  34.343  40.936  1.00 91.74      A    N  
ANISOU 3946  N   GLU A 498     8967  10943  14946  -2692   5220  -9095  A    N  
ATOM   3947  CA  GLU A 498       2.832  35.626  41.190  1.00 93.36      A    C  
ANISOU 3947  CA  GLU A 498     9267  10630  15574  -3039   5717  -9284  A    C  
ATOM   3948  C   GLU A 498       3.853  36.767  41.362  1.00 99.33      A    C  
ANISOU 3948  C   GLU A 498     9713  11518  16509  -3563   6131 -10021  A    C  
ATOM   3949  O   GLU A 498       3.685  37.806  40.724  1.00 99.78      A    O  
ANISOU 3949  O   GLU A 498     9899  10969  17044  -3858   6616 -10041  A    O  
ATOM   3950  CB  GLU A 498       1.900  35.507  42.416  1.00 95.36      A    C  
ANISOU 3950  CB  GLU A 498     9601  10967  15664  -2915   5629  -9278  A    C  
ATOM   3951  CG  GLU A 498       1.160  36.778  42.805  1.00114.65      A    C  
ANISOU 3951  CG  GLU A 498    12160  12885  18517  -3231   6135  -9459  A    C  
ATOM   3952  CD  GLU A 498       0.097  37.307  41.866  1.00147.13      A    C  
ANISOU 3952  CD  GLU A 498    16643  16147  23112  -3197   6443  -8918  A    C  
ATOM   3953  OE1 GLU A 498      -0.384  36.549  40.992  1.00138.39      A    O  
ANISOU 3953  OE1 GLU A 498    15754  14840  21988  -2866   6196  -8295  A    O  
ATOM   3954  OE2 GLU A 498      -0.304  38.476  42.064  1.00153.75      A    O1-
ANISOU 3954  OE2 GLU A 498    17554  16535  24327  -3488   6942  -9119  A    O1-
ATOM   3955  N   VAL A 499       4.900  36.584  42.191  1.00 97.43      A    N  
ANISOU 3955  N   VAL A 499     9067  12068  15883  -3676   5963 -10617  A    N  
ATOM   3956  CA  VAL A 499       5.925  37.621  42.403  1.00102.08      A    C  
ANISOU 3956  CA  VAL A 499     9314  12876  16596  -4213   6347 -11388  A    C  
ATOM   3957  C   VAL A 499       6.679  37.914  41.066  1.00107.50      A    C  
ANISOU 3957  C   VAL A 499     9983  13301  17559  -4389   6547 -11350  A    C  
ATOM   3958  O   VAL A 499       6.974  39.080  40.792  1.00111.28      A    O  
ANISOU 3958  O   VAL A 499    10424  13427  18429  -4860   7081 -11727  A    O  
ATOM   3959  CB  VAL A 499       6.883  37.322  43.602  1.00109.37      A    C  
ANISOU 3959  CB  VAL A 499     9759  14810  16988  -4278   6093 -12044  A    C  
ATOM   3960  CG1 VAL A 499       7.524  35.949  43.510  1.00107.67      A    C  
ANISOU 3960  CG1 VAL A 499     9377  15275  16258  -3832   5518 -11834  A    C  
ATOM   3961  CG2 VAL A 499       7.948  38.402  43.777  1.00114.78      A    C  
ANISOU 3961  CG2 VAL A 499    10070  15735  17805  -4890   6521 -12890  A    C  
ATOM   3962  N   LEU A 500       6.927  36.881  40.220  1.00100.05      A    N  
ANISOU 3962  N   LEU A 500     9104  12475  16434  -4013   6158 -10877  A    N  
ATOM   3963  CA  LEU A 500       7.600  37.058  38.928  1.00 99.56      A    C  
ANISOU 3963  CA  LEU A 500     9042  12183  16604  -4131   6308 -10785  A    C  
ATOM   3964  C   LEU A 500       6.702  37.815  37.942  1.00102.12      A    C  
ANISOU 3964  C   LEU A 500     9771  11540  17490  -4212   6730 -10329  A    C  
ATOM   3965  O   LEU A 500       7.182  38.720  37.254  1.00102.81      A    O  
ANISOU 3965  O   LEU A 500     9838  11290  17934  -4566   7173 -10531  A    O  
ATOM   3966  CB  LEU A 500       8.045  35.707  38.334  1.00 96.54      A    C  
ANISOU 3966  CB  LEU A 500     8634  12190  15858  -3683   5776 -10392  A    C  
ATOM   3967  CG  LEU A 500       9.270  35.042  38.978  1.00103.24      A    C  
ANISOU 3967  CG  LEU A 500     9030  14021  16176  -3611   5425 -10856  A    C  
ATOM   3968  CD1 LEU A 500       9.436  33.629  38.485  1.00 99.96      A    C  
ANISOU 3968  CD1 LEU A 500     8692  13888  15402  -3073   4905 -10353  A    C  
ATOM   3969  CD2 LEU A 500      10.558  35.844  38.723  1.00108.51      A    C  
ANISOU 3969  CD2 LEU A 500     9319  14965  16947  -4085   5726 -11506  A    C  
ATOM   3970  N   ALA A 501       5.399  37.449  37.902  1.00 97.34      A    N  
ANISOU 3970  N   ALA A 501     9523  10514  16947  -3879   6608  -9722  A    N  
ATOM   3971  CA  ALA A 501       4.356  38.072  37.082  1.00 96.22      A    C  
ANISOU 3971  CA  ALA A 501     9767   9518  17276  -3863   6960  -9217  A    C  
ATOM   3972  C   ALA A 501       4.216  39.568  37.415  1.00106.86      A    C  
ANISOU 3972  C   ALA A 501    11136  10410  19055  -4323   7620  -9630  A    C  
ATOM   3973  O   ALA A 501       4.072  40.374  36.493  1.00107.49      A    O  
ANISOU 3973  O   ALA A 501    11403   9875  19565  -4471   8065  -9452  A    O  
ATOM   3974  CB  ALA A 501       3.024  37.362  37.303  1.00 92.68      A    C  
ANISOU 3974  CB  ALA A 501     9610   8883  16720  -3443   6669  -8615  A    C  
ATOM   3975  N   ILE A 502       4.302  39.949  38.717  1.00107.96      A    N  
ANISOU 3975  N   ILE A 502    11086  10857  19077  -4552   7711 -10193  A    N  
ATOM   3976  CA  ILE A 502       4.187  41.355  39.121  1.00112.64      A    C  
ANISOU 3976  CA  ILE A 502    11704  11025  20069  -5012   8364 -10642  A    C  
ATOM   3977  C   ILE A 502       5.482  42.114  38.763  1.00121.22      A    C  
ANISOU 3977  C   ILE A 502    12532  12209  21316  -5506   8747 -11251  A    C  
ATOM   3978  O   ILE A 502       5.417  43.316  38.490  1.00123.55      A    O  
ANISOU 3978  O   ILE A 502    12962  11906  22077  -5864   9391 -11428  A    O  
ATOM   3979  CB  ILE A 502       3.745  41.577  40.600  1.00118.70      A    C  
ANISOU 3979  CB  ILE A 502    12381  12032  20686  -5115   8383 -11037  A    C  
ATOM   3980  CG1 ILE A 502       4.822  41.195  41.630  1.00122.33      A    C  
ANISOU 3980  CG1 ILE A 502    12375  13439  20667  -5278   8090 -11736  A    C  
ATOM   3981  CG2 ILE A 502       2.387  40.915  40.906  1.00115.85      A    C  
ANISOU 3981  CG2 ILE A 502    12307  11490  20220  -4652   8075 -10412  A    C  
ATOM   3982  CD1 ILE A 502       4.747  41.992  42.895  1.00132.02      A    C  
ANISOU 3982  CD1 ILE A 502    13453  14821  21887  -5625   8375 -12372  A    C  
ATOM   3983  N   LEU A 503       6.643  41.412  38.735  1.00119.14      A    N  
ANISOU 3983  N   LEU A 503    11913  12678  20675  -5512   8375 -11549  A    N  
ATOM   3984  CA  LEU A 503       7.925  42.001  38.326  1.00122.87      A    C  
ANISOU 3984  CA  LEU A 503    12106  13325  21255  -5962   8682 -12112  A    C  
ATOM   3985  C   LEU A 503       7.949  42.247  36.823  1.00127.16      A    C  
ANISOU 3985  C   LEU A 503    12900  13247  22169  -5929   8930 -11648  A    C  
ATOM   3986  O   LEU A 503       8.545  43.223  36.373  1.00129.31      A    O  
ANISOU 3986  O   LEU A 503    13189  13252  22693  -6282   9346 -11855  A    O  
ATOM   3987  CB  LEU A 503       9.115  41.116  38.726  1.00123.44      A    C  
ANISOU 3987  CB  LEU A 503    11712  14406  20782  -5912   8180 -12510  A    C  
ATOM   3988  CG  LEU A 503       9.606  41.266  40.144  1.00130.35      A    C  
ANISOU 3988  CG  LEU A 503    12279  16013  21234  -6052   7984 -13064  A    C  
ATOM   3989  CD1 LEU A 503      10.517  40.138  40.521  1.00130.89      A    C  
ANISOU 3989  CD1 LEU A 503    11890  17085  20759  -5866   7474 -13370  A    C  
ATOM   3990  CD2 LEU A 503      10.319  42.576  40.331  1.00132.33      A    C  
ANISOU 3990  CD2 LEU A 503    12735  16202  21340  -6189   7926 -12864  A    C  
ATOM   3991  N   LEU A 504       7.293  41.361  36.049  1.00120.58      A    N  
ANISOU 3991  N   LEU A 504    12325  12229  21262  -5416   8546 -10861  A    N  
ATOM   3992  CA  LEU A 504       7.199  41.468  34.593  1.00119.22      A    C  
ANISOU 3992  CA  LEU A 504    12402  11509  21388  -5309   8716 -10335  A    C  
ATOM   3993  C   LEU A 504       6.236  42.590  34.175  1.00126.98      A    C  
ANISOU 3993  C   LEU A 504    13764  11571  22911  -5411   9336 -10043  A    C  
ATOM   3994  O   LEU A 504       6.436  43.202  33.124  1.00128.66      A    O  
ANISOU 3994  O   LEU A 504    14118  11300  23466  -5539   9742  -9885  A    O  
ATOM   3995  CB  LEU A 504       6.759  40.132  33.981  1.00113.10      A    C  
ANISOU 3995  CB  LEU A 504    11771  10871  20329  -4740   8107  -9621  A    C  
ATOM   3996  CG  LEU A 504       7.848  39.064  33.875  1.00116.20      A    C  
ANISOU 3996  CG  LEU A 504    11858  12020  20271  -4593   7584  -9763  A    C  
ATOM   3997  CD1 LEU A 504       7.242  37.703  33.759  1.00110.87      A    C  
ANISOU 3997  CD1 LEU A 504    11338  11527  19261  -4038   6984  -9160  A    C  
ATOM   3998  CD2 LEU A 504       8.777  39.327  32.695  1.00119.32      A    C  
ANISOU 3998  CD2 LEU A 504    12182  12323  20832  -4762   7775  -9794  A    C  
ATOM   3999  N   LEU A 505       5.196  42.850  35.008  1.00124.14      A    N  
ANISOU 3999  N   LEU A 505    13571  10986  22611  -5326   9412  -9955  A    N  
ATOM   4000  CA  LEU A 505       4.161  43.879  34.817  1.00125.46      A    C  
ANISOU 4000  CA  LEU A 505    14096  10325  23248  -5360   9981  -9670  A    C  
ATOM   4001  C   LEU A 505       4.695  45.312  35.068  1.00132.20      A    C  
ANISOU 4001  C   LEU A 505    15004  10969  24256  -5746  10396  -9996  A    C  
ATOM   4002  O   LEU A 505       4.065  46.277  34.628  1.00131.85      A    O  
ANISOU 4002  O   LEU A 505    15320  10297  24480  -5666  10707  -9547  A    O  
ATOM   4003  CB  LEU A 505       2.965  43.603  35.750  1.00123.94      A    C  
ANISOU 4003  CB  LEU A 505    14034  10121  22936  -5106   9781  -9468  A    C  
ATOM   4004  CG  LEU A 505       1.569  43.948  35.208  1.00127.42      A    C  
ANISOU 4004  CG  LEU A 505    14886   9834  23694  -4807  10025  -8766  A    C  
ATOM   4005  CD1 LEU A 505       0.544  42.931  35.666  1.00123.28      A    C  
ANISOU 4005  CD1 LEU A 505    14449   9535  22857  -4350   9464  -8300  A    C  
ATOM   4006  CD2 LEU A 505       1.124  45.339  35.632  1.00135.01      A    C  
ANISOU 4006  CD2 LEU A 505    16004  10209  25084  -5113  10754  -9039  A    C  
ATOM   4007  N   GLU A 506       5.834  45.450  35.776  1.00129.53      A    N  
ANISOU 4007  N   GLU A 506    14362  11260  23594  -6033  10193 -10584  A    N  
ATOM   4008  CA  GLU A 506       6.444  46.752  36.051  1.00129.16      A    C  
ANISOU 4008  CA  GLU A 506    14446  11226  23404  -6199  10162 -10580  A    C  
ATOM   4009  C   GLU A 506       7.534  47.077  35.022  1.00130.52      A    C  
ANISOU 4009  C   GLU A 506    14605  11499  23486  -6252  10037 -10414  A    C  
ATOM   4010  O   GLU A 506       7.620  46.396  33.999  1.00129.40      A    O  
ANISOU 4010  O   GLU A 506    14377  11243  23547  -6225  10188 -10364  A    O  
ATOM   4011  CB  GLU A 506       6.987  46.814  37.487  1.00130.85      A    C  
ANISOU 4011  CB  GLU A 506    14463  12140  23115  -6267   9714 -10947  A    C  
ATOM   4012  CG  GLU A 506       5.931  47.217  38.505  1.00140.16      A    C  
ANISOU 4012  CG  GLU A 506    15984  13281  23989  -5857   9258 -10386  A    C  
ATOM   4013  CD  GLU A 506       5.313  48.589  38.303  1.00159.54      A    C  
ANISOU 4013  CD  GLU A 506    19128  15524  25966  -5170   8389  -8984  A    C  
ATOM   4014  OE1 GLU A 506       4.282  48.681  37.598  1.00161.02      A    O  
ANISOU 4014  OE1 GLU A 506    19539  15140  26502  -5039   8695  -8635  A    O  
ATOM   4015  OE2 GLU A 506       5.857  49.571  38.856  1.00158.20      A    O1-
ANISOU 4015  OE2 GLU A 506    18963  15400  25746  -5393   8463  -9243  A    O1-
ATOM   4016  N   LYS A 507       8.326  48.146  35.262  1.00128.27      A    N  
ANISOU 4016  N   LYS A 507    14345  11281  23109  -6492  10070 -10569  A    N  
ATOM   4017  CA  LYS A 507       9.399  48.579  34.357  1.00128.13      A    C  
ANISOU 4017  CA  LYS A 507    14302  11316  23065  -6621  10057 -10500  A    C  
ATOM   4018  C   LYS A 507      10.596  47.587  34.369  1.00130.21      A    C  
ANISOU 4018  C   LYS A 507    14165  12385  22924  -6626   9588 -10771  A    C  
ATOM   4019  O   LYS A 507      10.801  46.913  35.378  1.00130.13      A    O  
ANISOU 4019  O   LYS A 507    13867  12971  22604  -6630   9300 -11159  A    O  
ATOM   4020  CB  LYS A 507       9.867  50.015  34.695  1.00130.25      A    C  
ANISOU 4020  CB  LYS A 507    14783  11555  23151  -6683   9892 -10313  A    C  
ATOM   4021  CG  LYS A 507      10.563  50.191  36.050  1.00140.56      A    C  
ANISOU 4021  CG  LYS A 507    16057  13694  23657  -6394   8880 -10077  A    C  
ATOM   4022  CD  LYS A 507      11.480  51.418  36.083  1.00146.10      A    C  
ANISOU 4022  CD  LYS A 507    16952  14541  24020  -6293   8390  -9636  A    C  
ATOM   4023  CE  LYS A 507      12.916  51.097  35.727  1.00150.45      A    C  
ANISOU 4023  CE  LYS A 507    17360  15692  24113  -6124   7749  -9360  A    C  
ATOM   4024  NZ  LYS A 507      13.815  52.262  35.942  1.00154.27      A    N1+
ANISOU 4024  NZ  LYS A 507    18022  16308  24286  -6005   7256  -8923  A    N1+
ATOM   4025  N   PRO A 508      11.407  47.509  33.281  1.00127.62      A    N  
ANISOU 4025  N   PRO A 508    13730  12021  22740  -6776   9769 -10827  A    N  
ATOM   4026  CA  PRO A 508      12.545  46.567  33.257  1.00127.65      A    C  
ANISOU 4026  CA  PRO A 508    13307  12761  22432  -6834   9449 -11194  A    C  
ATOM   4027  C   PRO A 508      13.597  46.835  34.343  1.00129.76      A    C  
ANISOU 4027  C   PRO A 508    13372  13775  22156  -6874   8936 -11401  A    C  
ATOM   4028  O   PRO A 508      14.017  47.973  34.570  1.00129.86      A    O  
ANISOU 4028  O   PRO A 508    13532  13688  22120  -7004   8936 -11313  A    O  
ATOM   4029  CB  PRO A 508      13.129  46.774  31.858  1.00128.90      A    C  
ANISOU 4029  CB  PRO A 508    13569  12675  22732  -6832   9547 -10864  A    C  
ATOM   4030  CG  PRO A 508      11.985  47.267  31.046  1.00131.46      A    C  
ANISOU 4030  CG  PRO A 508    14356  12191  23401  -6609   9806 -10212  A    C  
ATOM   4031  CD  PRO A 508      11.274  48.194  31.979  1.00128.50      A    C  
ANISOU 4031  CD  PRO A 508    14168  11507  23150  -6718  10039 -10308  A    C  
ATOM   4032  N   LEU A 509      13.995  45.756  35.024  1.00126.24      A    N  
ANISOU 4032  N   LEU A 509    12470  14029  21467  -6932   8771 -11983  A    N  
ATOM   4033  CA  LEU A 509      14.959  45.769  36.120  1.00125.82      A    C  
ANISOU 4033  CA  LEU A 509    12133  14748  20927  -6990   8375 -12310  A    C  
ATOM   4034  C   LEU A 509      16.398  45.917  35.635  1.00126.73      A    C  
ANISOU 4034  C   LEU A 509    12096  15250  20807  -7041   8136 -12260  A    C  
ATOM   4035  O   LEU A 509      16.726  45.385  34.578  1.00126.71      A    O  
ANISOU 4035  O   LEU A 509    12006  15211  20928  -7023   8213 -12207  A    O  
ATOM   4036  CB  LEU A 509      14.850  44.454  36.917  1.00125.80      A    C  
ANISOU 4036  CB  LEU A 509    11779  15430  20589  -6807   8049 -12635  A    C  
ATOM   4037  CG  LEU A 509      13.632  44.257  37.802  1.00128.11      A    C  
ANISOU 4037  CG  LEU A 509    12251  15576  20850  -6595   7964 -12494  A    C  
ATOM   4038  CD1 LEU A 509      13.394  42.795  38.042  1.00127.82      A    C  
ANISOU 4038  CD1 LEU A 509    11898  16037  20631  -6388   7748 -12738  A    C  
ATOM   4039  CD2 LEU A 509      13.795  44.960  39.136  1.00130.64      A    C  
ANISOU 4039  CD2 LEU A 509    12664  16172  20803  -6549   7656 -12435  A    C  
ATOM   4040  N   PRO A 510      17.299  46.538  36.432  1.00122.93      A    N  
ANISOU 4040  N   PRO A 510    11426  15181  20102  -7283   8065 -12615  A    N  
ATOM   4041  CA  PRO A 510      18.725  46.594  36.039  1.00122.48      A    C  
ANISOU 4041  CA  PRO A 510    11146  15543  19849  -7384   7898 -12688  A    C  
ATOM   4042  C   PRO A 510      19.382  45.205  35.949  1.00122.68      A    C  
ANISOU 4042  C   PRO A 510    10737  16323  19551  -7222   7586 -12931  A    C  
ATOM   4043  O   PRO A 510      18.909  44.260  36.592  1.00121.39      A    O  
ANISOU 4043  O   PRO A 510    10360  16552  19212  -7076   7442 -13189  A    O  
ATOM   4044  CB  PRO A 510      19.378  47.402  37.171  1.00124.45      A    C  
ANISOU 4044  CB  PRO A 510    11438  16084  19764  -7400   7584 -12630  A    C  
ATOM   4045  CG  PRO A 510      18.260  48.105  37.851  1.00127.66      A    C  
ANISOU 4045  CG  PRO A 510    12230  16022  20251  -7281   7597 -12336  A    C  
ATOM   4046  CD  PRO A 510      17.073  47.211  37.725  1.00124.19      A    C  
ANISOU 4046  CD  PRO A 510    11705  15434  20047  -7265   7887 -12608  A    C  
ATOM   4047  N   VAL A 511      20.498  45.095  35.169  1.00119.71      A    N  
ANISOU 4047  N   VAL A 511    10081  16217  19186  -7419   7674 -13175  A    N  
ATOM   4048  CA  VAL A 511      21.276  43.851  34.947  1.00119.32      A    C  
ANISOU 4048  CA  VAL A 511     9592  16911  18831  -7272   7391 -13416  A    C  
ATOM   4049  C   VAL A 511      21.825  43.336  36.304  1.00121.29      A    C  
ANISOU 4049  C   VAL A 511     9564  18015  18506  -7066   6886 -13573  A    C  
ATOM   4050  O   VAL A 511      21.885  42.127  36.513  1.00121.13      A    O  
ANISOU 4050  O   VAL A 511     9230  18589  18206  -6825   6629 -13764  A    O  
ATOM   4051  CB  VAL A 511      22.409  44.018  33.873  1.00122.40      A    C  
ANISOU 4051  CB  VAL A 511    10005  17310  19190  -7248   7282 -13086  A    C  
ATOM   4052  CG1 VAL A 511      23.184  42.715  33.641  1.00122.21      A    C  
ANISOU 4052  CG1 VAL A 511     9566  18025  18844  -7033   6970 -13259  A    C  
ATOM   4053  CG2 VAL A 511      21.851  44.524  32.545  1.00121.82      A    C  
ANISOU 4053  CG2 VAL A 511    10244  16392  19652  -7410   7762 -12855  A    C  
ATOM   4054  N   SER A 512      22.161  44.253  37.228  1.00118.38      A    N  
ANISOU 4054  N   SER A 512     9166  17761  18053  -7322   6939 -13814  A    N  
ATOM   4055  CA  SER A 512      22.667  43.959  38.572  1.00118.37      A    C  
ANISOU 4055  CA  SER A 512     8920  18506  17549  -7187   6541 -13992  A    C  
ATOM   4056  C   SER A 512      21.631  43.240  39.462  1.00120.05      A    C  
ANISOU 4056  C   SER A 512     9123  18887  17603  -6946   6399 -14061  A    C  
ATOM   4057  O   SER A 512      22.007  42.411  40.292  1.00119.80      A    O  
ANISOU 4057  O   SER A 512     8797  19614  17108  -6703   6023 -14204  A    O  
ATOM   4058  CB  SER A 512      23.093  45.255  39.253  1.00120.69      A    C  
ANISOU 4058  CB  SER A 512     9486  18584  17787  -7295   6457 -13731  A    C  
ATOM   4059  OG  SER A 512      21.971  46.100  39.463  1.00125.46      A    O  
ANISOU 4059  OG  SER A 512    10625  18409  18636  -7231   6558 -13280  A    O  
ATOM   4060  N   HIS A 513      20.344  43.584  39.308  1.00117.40      A    N  
ANISOU 4060  N   HIS A 513     8960  17926  17721  -7170   6872 -14263  A    N  
ATOM   4061  CA  HIS A 513      19.253  43.032  40.114  1.00117.30      A    C  
ANISOU 4061  CA  HIS A 513     8930  17986  17654  -7028   6848 -14417  A    C  
ATOM   4062  C   HIS A 513      18.920  41.600  39.732  1.00119.15      A    C  
ANISOU 4062  C   HIS A 513     8946  18551  17775  -6709   6660 -14446  A    C  
ATOM   4063  O   HIS A 513      18.716  40.779  40.628  1.00119.45      A    O  
ANISOU 4063  O   HIS A 513     8774  19180  17432  -6446   6341 -14581  A    O  
ATOM   4064  CB  HIS A 513      18.008  43.922  40.007  1.00117.52      A    C  
ANISOU 4064  CB  HIS A 513     9395  17081  18176  -7197   7285 -14255  A    C  
ATOM   4065  CG  HIS A 513      18.109  45.180  40.807  1.00120.35      A    C  
ANISOU 4065  CG  HIS A 513    10077  17190  18460  -7260   7214 -13985  A    C  
ATOM   4066  CD2 HIS A 513      17.178  45.788  41.576  1.00121.74      A    C  
ANISOU 4066  CD2 HIS A 513    10549  16981  18724  -7247   7299 -13858  A    C  
ATOM   4067  ND1 HIS A 513      19.278  45.926  40.841  1.00122.20      A    N  
ANISOU 4067  ND1 HIS A 513    10347  17566  18517  -7325   7024 -13804  A    N  
ATOM   4068  CE1 HIS A 513      19.021  46.954  41.631  1.00122.18      A    C  
ANISOU 4068  CE1 HIS A 513    10574  17303  18546  -7447   7091 -13766  A    C  
ATOM   4069  NE2 HIS A 513      17.769  46.913  42.098  1.00122.10      A    N  
ANISOU 4069  NE2 HIS A 513    10733  16976  18682  -7393   7246 -13782  A    N  
ATOM   4070  N   VAL A 514      18.859  41.294  38.417  1.00115.64      A    N  
ANISOU 4070  N   VAL A 514     8377  17826  17734  -6888   7023 -14661  A    N  
ATOM   4071  CA  VAL A 514      18.567  39.941  37.930  1.00115.11      A    C  
ANISOU 4071  CA  VAL A 514     8030  18079  17627  -6646   6911 -14830  A    C  
ATOM   4072  C   VAL A 514      19.779  39.018  38.201  1.00118.63      A    C  
ANISOU 4072  C   VAL A 514     8167  19500  17409  -6245   6274 -14706  A    C  
ATOM   4073  O   VAL A 514      19.602  37.807  38.345  1.00118.74      A    O  
ANISOU 4073  O   VAL A 514     7909  20062  17143  -5906   5985 -14832  A    O  
ATOM   4074  CB  VAL A 514      18.091  39.877  36.454  1.00116.89      A    C  
ANISOU 4074  CB  VAL A 514     8506  17533  18376  -6674   7238 -14539  A    C  
ATOM   4075  CG1 VAL A 514      16.687  40.466  36.307  1.00115.97      A    C  
ANISOU 4075  CG1 VAL A 514     8781  16451  18831  -6832   7736 -14413  A    C  
ATOM   4076  CG2 VAL A 514      19.076  40.548  35.494  1.00116.89      A    C  
ANISOU 4076  CG2 VAL A 514     8578  17323  18512  -6884   7387 -14387  A    C  
ATOM   4077  N   LYS A 515      20.993  39.605  38.302  1.00116.45      A    N  
ANISOU 4077  N   LYS A 515     7749  19540  16957  -6435   6224 -14804  A    N  
ATOM   4078  CA  LYS A 515      22.228  38.902  38.653  1.00116.90      A    C  
ANISOU 4078  CA  LYS A 515     7456  20520  16440  -6159   5743 -14814  A    C  
ATOM   4079  C   LYS A 515      22.180  38.523  40.129  1.00119.82      A    C  
ANISOU 4079  C   LYS A 515     7806  21438  16284  -5812   5300 -14674  A    C  
ATOM   4080  O   LYS A 515      22.623  37.436  40.505  1.00119.22      A    O  
ANISOU 4080  O   LYS A 515     7404  22159  15735  -5436   4914 -14740  A    O  
ATOM   4081  CB  LYS A 515      23.463  39.776  38.361  1.00118.79      A    C  
ANISOU 4081  CB  LYS A 515     7820  20660  16655  -6316   5708 -14531  A    C  
ATOM   4082  CG  LYS A 515      23.991  39.661  36.942  1.00122.85      A    C  
ANISOU 4082  CG  LYS A 515     8684  20705  17287  -6053   5554 -13733  A    C  
ATOM   4083  CD  LYS A 515      25.163  40.596  36.689  1.00128.00      A    C  
ANISOU 4083  CD  LYS A 515     9760  21001  17874  -5964   5310 -12919  A    C  
ATOM   4084  CE  LYS A 515      25.838  40.307  35.370  1.00133.66      A    C  
ANISOU 4084  CE  LYS A 515    10847  21392  18545  -5528   4967 -11937  A    C  
ATOM   4085  NZ  LYS A 515      27.054  41.143  35.170  1.00141.04      A    N1+
ANISOU 4085  NZ  LYS A 515    12231  21956  19403  -5351   4648 -11025  A    N1+
ATOM   4086  N   ARG A 516      21.622  39.433  40.961  1.00118.68      A    N  
ANISOU 4086  N   ARG A 516     7838  20993  16261  -6065   5493 -14793  A    N  
ATOM   4087  CA  ARG A 516      21.457  39.253  42.400  1.00119.26      A    C  
ANISOU 4087  CA  ARG A 516     7859  21539  15914  -5862   5200 -14818  A    C  
ATOM   4088  C   ARG A 516      20.378  38.194  42.672  1.00123.56      A    C  
ANISOU 4088  C   ARG A 516     8474  22142  16333  -5437   4998 -14635  A    C  
ATOM   4089  O   ARG A 516      20.532  37.417  43.615  1.00124.24      A    O  
ANISOU 4089  O   ARG A 516     8387  22909  15911  -5070   4608 -14605  A    O  
ATOM   4090  CB  ARG A 516      21.123  40.592  43.072  1.00119.54      A    C  
ANISOU 4090  CB  ARG A 516     8226  21045  16147  -6167   5415 -14759  A    C  
ATOM   4091  CG  ARG A 516      21.137  40.572  44.605  1.00128.07      A    C  
ANISOU 4091  CG  ARG A 516     9684  22256  16722  -5674   4850 -14044  A    C  
ATOM   4092  CD  ARG A 516      22.534  40.466  45.196  1.00136.15      A    C  
ANISOU 4092  CD  ARG A 516    11005  23460  17265  -5197   4219 -13134  A    C  
ATOM   4093  NE  ARG A 516      22.493  40.449  46.657  1.00141.67      A    N  
ANISOU 4093  NE  ARG A 516    12165  24079  17586  -4737   3746 -12375  A    N  
ATOM   4094  CZ  ARG A 516      22.880  39.430  47.415  1.00151.59      A    C  
ANISOU 4094  CZ  ARG A 516    13856  25352  18389  -3989   3123 -11323  A    C  
ATOM   4095  NH1 ARG A 516      23.379  38.332  46.861  1.00143.67      A    N1+
ANISOU 4095  NH1 ARG A 516    12320  25056  17210  -3938   3118 -11779  A    N1+
ATOM   4096  NH2 ARG A 516      22.798  39.511  48.737  1.00140.91      A    N  
ANISOU 4096  NH2 ARG A 516    12146  24620  16774  -4170   3169 -11976  A    N  
ATOM   4097  N   MET A 517      19.309  38.147  41.833  1.00121.13      A    N  
ANISOU 4097  N   MET A 517     8197  21288  16539  -5643   5414 -14892  A    N  
ATOM   4098  CA  MET A 517      18.230  37.154  41.936  1.00121.16      A    C  
ANISOU 4098  CA  MET A 517     8108  21388  16539  -5382   5360 -15014  A    C  
ATOM   4099  C   MET A 517      18.774  35.745  41.751  1.00122.61      A    C  
ANISOU 4099  C   MET A 517     7970  22361  16255  -4877   4897 -14953  A    C  
ATOM   4100  O   MET A 517      18.436  34.852  42.523  1.00121.97      A    O  
ANISOU 4100  O   MET A 517     7708  22863  15773  -4495   4582 -15018  A    O  
ATOM   4101  CB  MET A 517      17.128  37.407  40.898  1.00122.25      A    C  
ANISOU 4101  CB  MET A 517     8564  20537  17349  -5568   5804 -14892  A    C  
ATOM   4102  CG  MET A 517      16.237  38.541  41.249  1.00125.05      A    C  
ANISOU 4102  CG  MET A 517     9407  20044  18063  -5786   6110 -14625  A    C  
ATOM   4103  SD  MET A 517      14.923  38.761  40.043  1.00127.51      A    S  
ANISOU 4103  SD  MET A 517    10160  19167  19120  -5879   6587 -14288  A    S  
ATOM   4104  CE  MET A 517      14.221  40.217  40.665  1.00125.23      A    C  
ANISOU 4104  CE  MET A 517    10204  18201  19177  -6253   7032 -14336  A    C  
ATOM   4105  N   GLN A 518      19.627  35.557  40.729  1.00119.84      A    N  
ANISOU 4105  N   GLN A 518     7369  22195  15970  -4968   4951 -15125  A    N  
ATOM   4106  CA  GLN A 518      20.259  34.281  40.420  1.00119.30      A    C  
ANISOU 4106  CA  GLN A 518     6947  22907  15473  -4507   4552 -15134  A    C  
ATOM   4107  C   GLN A 518      21.166  33.848  41.567  1.00122.71      A    C  
ANISOU 4107  C   GLN A 518     7333  24099  15192  -4065   4016 -14777  A    C  
ATOM   4108  O   GLN A 518      21.170  32.674  41.929  1.00123.07      A    O  
ANISOU 4108  O   GLN A 518     7177  24810  14774  -3530   3631 -14708  A    O  
ATOM   4109  CB  GLN A 518      21.046  34.377  39.101  1.00119.90      A    C  
ANISOU 4109  CB  GLN A 518     7008  22767  15782  -4642   4679 -15046  A    C  
ATOM   4110  CG  GLN A 518      21.643  33.047  38.598  1.00123.56      A    C  
ANISOU 4110  CG  GLN A 518     7368  23742  15837  -4027   4204 -14665  A    C  
ATOM   4111  CD  GLN A 518      20.746  31.839  38.798  1.00135.33      A    C  
ANISOU 4111  CD  GLN A 518     9386  24947  17086  -3251   3734 -13718  A    C  
ATOM   4112  NE2 GLN A 518      21.313  30.760  39.310  1.00130.00      A    N  
ANISOU 4112  NE2 GLN A 518     8289  25292  15812  -2780   3340 -13902  A    N  
ATOM   4113  OE1 GLN A 518      19.549  31.850  38.490  1.00127.64      A    O  
ANISOU 4113  OE1 GLN A 518     8709  23296  16491  -3285   3908 -13568  A    O  
ATOM   4114  N   GLU A 519      21.888  34.807  42.156  1.00120.07      A    N  
ANISOU 4114  N   GLU A 519     6994  23823  14804  -4387   4098 -14874  A    N  
ATOM   4115  CA  GLU A 519      22.813  34.605  43.264  1.00120.94      A    C  
ANISOU 4115  CA  GLU A 519     7022  24587  14344  -4106   3704 -14659  A    C  
ATOM   4116  C   GLU A 519      22.107  34.041  44.520  1.00124.46      A    C  
ANISOU 4116  C   GLU A 519     7630  25238  14423  -3685   3407 -14377  A    C  
ATOM   4117  O   GLU A 519      22.593  33.055  45.071  1.00124.94      A    O  
ANISOU 4117  O   GLU A 519     7527  25989  13955  -3190   3015 -14192  A    O  
ATOM   4118  CB  GLU A 519      23.533  35.939  43.579  1.00122.17      A    C  
ANISOU 4118  CB  GLU A 519     7410  24365  14646  -4502   3840 -14515  A    C  
ATOM   4119  CG  GLU A 519      24.518  35.932  44.740  1.00128.11      A    C  
ANISOU 4119  CG  GLU A 519     8460  25286  14931  -4122   3367 -13774  A    C  
ATOM   4120  CD  GLU A 519      25.838  35.208  44.558  1.00135.94      A    C  
ANISOU 4120  CD  GLU A 519    10041  25950  15661  -3437   2808 -12377  A    C  
ATOM   4121  OE1 GLU A 519      26.150  34.766  43.427  1.00136.39      A    O  
ANISOU 4121  OE1 GLU A 519    10131  25847  15843  -3320   2801 -12152  A    O  
ATOM   4122  OE2 GLU A 519      26.571  35.093  45.566  1.00123.19      A    O1-
ANISOU 4122  OE2 GLU A 519     8061  25090  13654  -3417   2657 -12702  A    O1-
ATOM   4123  N   VAL A 520      20.977  34.629  44.957  1.00121.87      A    N  
ANISOU 4123  N   VAL A 520     7386  24555  14364  -3978   3689 -14692  A    N  
ATOM   4124  CA  VAL A 520      20.320  34.171  46.188  1.00121.85      A    C  
ANISOU 4124  CA  VAL A 520     7383  24906  14009  -3684   3479 -14676  A    C  
ATOM   4125  C   VAL A 520      19.145  33.198  45.955  1.00125.18      A    C  
ANISOU 4125  C   VAL A 520     7919  25198  14446  -3281   3371 -14484  A    C  
ATOM   4126  O   VAL A 520      18.873  32.393  46.848  1.00125.76      A    O  
ANISOU 4126  O   VAL A 520     7916  25818  14049  -2818   3050 -14364  A    O  
ATOM   4127  CB  VAL A 520      19.879  35.331  47.121  1.00123.92      A    C  
ANISOU 4127  CB  VAL A 520     8012  24625  14446  -3995   3655 -14569  A    C  
ATOM   4128  CG1 VAL A 520      21.077  35.963  47.815  1.00124.33      A    C  
ANISOU 4128  CG1 VAL A 520     8096  24886  14257  -4093   3516 -14423  A    C  
ATOM   4129  CG2 VAL A 520      19.047  36.381  46.386  1.00122.85      A    C  
ANISOU 4129  CG2 VAL A 520     8099  23583  14995  -4518   4174 -14769  A    C  
ATOM   4130  N   TYR A 521      18.443  33.268  44.810  1.00122.36      A    N  
ANISOU 4130  N   TYR A 521     7502  24368  14623  -3558   3726 -14826  A    N  
ATOM   4131  CA  TYR A 521      17.280  32.395  44.600  1.00120.04      A    C  
ANISOU 4131  CA  TYR A 521     7359  23851  14399  -3193   3631 -14616  A    C  
ATOM   4132  C   TYR A 521      17.575  31.180  43.717  1.00121.67      A    C  
ANISOU 4132  C   TYR A 521     7724  24086  14420  -2600   3267 -13986  A    C  
ATOM   4133  O   TYR A 521      16.779  30.237  43.725  1.00118.07      A    O  
ANISOU 4133  O   TYR A 521     7674  23340  13846  -2050   2988 -13304  A    O  
ATOM   4134  CB  TYR A 521      16.080  33.173  44.011  1.00117.32      A    C  
ANISOU 4134  CB  TYR A 521     7575  22240  14762  -3511   4027 -14293  A    C  
ATOM   4135  CG  TYR A 521      15.686  34.453  44.728  1.00121.76      A    C  
ANISOU 4135  CG  TYR A 521     8071  22581  15611  -4117   4470 -14862  A    C  
ATOM   4136  CD1 TYR A 521      15.798  34.565  46.110  1.00124.67      A    C  
ANISOU 4136  CD1 TYR A 521     8413  23417  15538  -3996   4254 -14864  A    C  
ATOM   4137  CD2 TYR A 521      15.114  35.514  44.035  1.00121.33      A    C  
ANISOU 4137  CD2 TYR A 521     8328  21537  16234  -4605   4987 -14859  A    C  
ATOM   4138  CE1 TYR A 521      15.418  35.730  46.775  1.00125.05      A    C  
ANISOU 4138  CE1 TYR A 521     8734  22978  15803  -4356   4513 -14870  A    C  
ATOM   4139  CE2 TYR A 521      14.713  36.677  44.692  1.00122.90      A    C  
ANISOU 4139  CE2 TYR A 521     8720  21317  16660  -4993   5305 -14994  A    C  
ATOM   4140  CZ  TYR A 521      14.870  36.783  46.064  1.00128.02      A    C  
ANISOU 4140  CZ  TYR A 521     9550  22288  16803  -4719   4926 -14634  A    C  
ATOM   4141  OH  TYR A 521      14.487  37.927  46.725  1.00126.72      A    O  
ANISOU 4141  OH  TYR A 521     9617  21704  16828  -5041   5183 -14692  A    O  
ATOM   4142  N   ASN A 522      18.703  31.197  42.957  1.00120.15      A    N  
ANISOU 4142  N   ASN A 522     7222  24222  14208  -2724   3290 -14221  A    N  
ATOM   4143  CA  ASN A 522      19.136  30.132  42.036  1.00117.04      A    C  
ANISOU 4143  CA  ASN A 522     6936  23875  13660  -2221   2994 -13702  A    C  
ATOM   4144  C   ASN A 522      17.972  29.662  41.124  1.00114.16      A    C  
ANISOU 4144  C   ASN A 522     7281  22408  13686  -1945   2975 -12839  A    C  
ATOM   4145  O   ASN A 522      17.668  28.464  41.027  1.00109.89      A    O  
ANISOU 4145  O   ASN A 522     7006  21873  12875  -1321   2625 -12240  A    O  
ATOM   4146  CB  ASN A 522      19.762  28.959  42.791  1.00118.36      A    C  
ANISOU 4146  CB  ASN A 522     6792  25102  13077  -1577   2519 -13651  A    C  
ATOM   4147  CG  ASN A 522      20.832  28.280  41.985  1.00138.92      A    C  
ANISOU 4147  CG  ASN A 522     9684  27565  15534  -1184   2261 -12865  A    C  
ATOM   4148  ND2 ASN A 522      22.073  28.434  42.426  1.00136.90      A    N  
ANISOU 4148  ND2 ASN A 522     9247  27798  14973  -1191   2144 -12855  A    N  
ATOM   4149  OD1 ASN A 522      20.573  27.682  40.935  1.00125.08      A    O  
ANISOU 4149  OD1 ASN A 522     7845  25758  13922  -1018   2260 -12943  A    O  
ATOM   4150  N   LEU A 523      17.332  30.629  40.454  1.00108.79      A    N  
ANISOU 4150  N   LEU A 523     6899  20799  13638  -2422   3380 -12796  A    N  
ATOM   4151  CA  LEU A 523      16.186  30.379  39.584  1.00102.50      A    C  
ANISOU 4151  CA  LEU A 523     6731  18970  13244  -2251   3419 -12050  A    C  
ATOM   4152  C   LEU A 523      16.573  29.724  38.254  1.00103.56      A    C  
ANISOU 4152  C   LEU A 523     7024  18868  13457  -2012   3303 -11610  A    C  
ATOM   4153  O   LEU A 523      15.685  29.248  37.547  1.00 98.80      A    O  
ANISOU 4153  O   LEU A 523     6916  17553  13072  -1768   3248 -10950  A    O  
ATOM   4154  CB  LEU A 523      15.410  31.684  39.340  1.00102.10      A    C  
ANISOU 4154  CB  LEU A 523     6914  18067  13814  -2817   3917 -12165  A    C  
ATOM   4155  CG  LEU A 523      14.810  32.359  40.581  1.00107.45      A    C  
ANISOU 4155  CG  LEU A 523     7552  18786  14487  -3036   4064 -12495  A    C  
ATOM   4156  CD1 LEU A 523      14.586  33.824  40.343  1.00109.14      A    C  
ANISOU 4156  CD1 LEU A 523     7784  18433  15250  -3712   4638 -12902  A    C  
ATOM   4157  CD2 LEU A 523      13.526  31.675  41.034  1.00105.04      A    C  
ANISOU 4157  CD2 LEU A 523     7706  18066  14138  -2606   3851 -11865  A    C  
ATOM   4158  N   ASN A 524      17.883  29.652  37.932  1.00103.08      A    N  
ANISOU 4158  N   ASN A 524     6536  19440  13191  -2066   3254 -11973  A    N  
ATOM   4159  CA  ASN A 524      18.383  29.019  36.711  1.00100.55      A    C  
ANISOU 4159  CA  ASN A 524     6313  18987  12902  -1839   3141 -11614  A    C  
ATOM   4160  C   ASN A 524      18.211  27.500  36.736  1.00103.19      A    C  
ANISOU 4160  C   ASN A 524     6866  19522  12819  -1098   2685 -11020  A    C  
ATOM   4161  O   ASN A 524      18.132  26.908  35.656  1.00 99.88      A    O  
ANISOU 4161  O   ASN A 524     6742  18681  12528   -875   2613 -10529  A    O  
ATOM   4162  CB  ASN A 524      19.862  29.344  36.469  1.00104.09      A    C  
ANISOU 4162  CB  ASN A 524     6206  20133  13210  -2095   3213 -12205  A    C  
ATOM   4163  CG  ASN A 524      20.146  30.597  35.669  1.00121.21      A    C  
ANISOU 4163  CG  ASN A 524     8311  21829  15912  -2773   3703 -12562  A    C  
ATOM   4164  ND2 ASN A 524      21.426  30.898  35.494  1.00119.27      A    N  
ANISOU 4164  ND2 ASN A 524     7565  22209  15544  -3040   3789 -13120  A    N  
ATOM   4165  OD1 ASN A 524      19.248  31.317  35.217  1.00108.67      A    O  
ANISOU 4165  OD1 ASN A 524     7112  19337  14839  -3059   4024 -12348  A    O  
ATOM   4166  N   ASP A 525      18.154  26.860  37.934  1.00102.44      A    N  
ANISOU 4166  N   ASP A 525     6643  20053  12225   -713   2401 -11055  A    N  
ATOM   4167  CA  ASP A 525      18.008  25.398  38.012  1.00101.49      A    C  
ANISOU 4167  CA  ASP A 525     6752  20114  11694     11   2012 -10492  A    C  
ATOM   4168  C   ASP A 525      16.567  24.934  38.381  1.00104.28      A    C  
ANISOU 4168  C   ASP A 525     7644  19852  12124    264   1939  -9940  A    C  
ATOM   4169  O   ASP A 525      16.365  23.741  38.629  1.00102.88      A    O  
ANISOU 4169  O   ASP A 525     7676  19823  11592    847   1654  -9504  A    O  
ATOM   4170  CB  ASP A 525      19.040  24.771  38.968  1.00108.05      A    C  
ANISOU 4170  CB  ASP A 525     7096  22107  11850    400   1725 -10802  A    C  
ATOM   4171  CG  ASP A 525      20.451  24.646  38.414  1.00122.25      A    C  
ANISOU 4171  CG  ASP A 525     8444  24556  13448    417   1673 -11111  A    C  
ATOM   4172  OD1 ASP A 525      20.616  24.024  37.336  1.00119.29      A    O  
ANISOU 4172  OD1 ASP A 525     8292  23872  13162    649   1607 -10707  A    O  
ATOM   4173  OD2 ASP A 525      21.400  25.094  39.100  1.00135.11      A    O1-
ANISOU 4173  OD2 ASP A 525     9481  27069  14787    231   1680 -11760  A    O1-
ATOM   4174  N   VAL A 526      15.573  25.846  38.354  1.00100.64      A    N  
ANISOU 4174  N   VAL A 526     7424  18682  12132   -161   2217  -9938  A    N  
ATOM   4175  CA  VAL A 526      14.168  25.503  38.615  1.00 97.66      A    C  
ANISOU 4175  CA  VAL A 526     7544  17691  11873     22   2180  -9432  A    C  
ATOM   4176  C   VAL A 526      13.596  24.862  37.343  1.00 99.48      A    C  
ANISOU 4176  C   VAL A 526     8256  17186  12358    214   2148  -8773  A    C  
ATOM   4177  O   VAL A 526      13.625  25.484  36.274  1.00 98.36      A    O  
ANISOU 4177  O   VAL A 526     8186  16546  12641   -123   2378  -8753  A    O  
ATOM   4178  CB  VAL A 526      13.327  26.714  39.094  1.00101.93      A    C  
ANISOU 4178  CB  VAL A 526     8139  17796  12795   -474   2497  -9681  A    C  
ATOM   4179  CG1 VAL A 526      11.835  26.384  39.113  1.00 97.48      A    C  
ANISOU 4179  CG1 VAL A 526     8106  16522  12409   -300   2478  -9106  A    C  
ATOM   4180  CG2 VAL A 526      13.786  27.190  40.472  1.00106.69      A    C  
ANISOU 4180  CG2 VAL A 526     8289  19162  13085   -625   2502 -10317  A    C  
ATOM   4181  N   LYS A 527      13.111  23.612  37.455  1.00 94.75      A    N  
ANISOU 4181  N   LYS A 527     7978  16539  11483    750   1880  -8251  A    N  
ATOM   4182  CA  LYS A 527      12.554  22.879  36.316  1.00 90.73      A    C  
ANISOU 4182  CA  LYS A 527     7920  15397  11154    951   1833  -7644  A    C  
ATOM   4183  C   LYS A 527      11.108  23.305  36.001  1.00 92.07      A    C  
ANISOU 4183  C   LYS A 527     8512  14706  11764    727   2013  -7301  A    C  
ATOM   4184  O   LYS A 527      10.702  23.179  34.841  1.00 90.04      A    O  
ANISOU 4184  O   LYS A 527     8539  13882  11790    685   2078  -6932  A    O  
ATOM   4185  CB  LYS A 527      12.626  21.356  36.534  1.00 92.39      A    C  
ANISOU 4185  CB  LYS A 527     8330  15869  10906   1592   1526  -7239  A    C  
ATOM   4186  CG  LYS A 527      14.022  20.774  36.341  1.00104.98      A    C  
ANISOU 4186  CG  LYS A 527     9609  18142  12135   1884   1363  -7397  A    C  
ATOM   4187  CD  LYS A 527      14.008  19.256  36.400  1.00112.74      A    C  
ANISOU 4187  CD  LYS A 527    10880  19227  12728   2530   1122  -6916  A    C  
ATOM   4188  CE  LYS A 527      15.368  18.642  36.158  1.00122.38      A    C  
ANISOU 4188  CE  LYS A 527    11806  21116  13578   2874    973  -7034  A    C  
ATOM   4189  NZ  LYS A 527      15.751  18.682  34.721  1.00126.43      A    N1+
ANISOU 4189  NZ  LYS A 527    12375  21290  14374   2715   1055  -6935  A    N1+
ATOM   4190  N   ASN A 528      10.345  23.810  37.012  1.00 87.98      A    N  
ANISOU 4190  N   ASN A 528     8016  14125  11287    592   2093  -7426  A    N  
ATOM   4191  CA  ASN A 528       8.943  24.262  36.908  1.00 84.41      A    C  
ANISOU 4191  CA  ASN A 528     7923  12937  11214    402   2266  -7134  A    C  
ATOM   4192  C   ASN A 528       8.779  25.320  35.794  1.00 86.27      A    C  
ANISOU 4192  C   ASN A 528     8203  12588  11988    -41   2582  -7148  A    C  
ATOM   4193  O   ASN A 528       9.154  26.481  35.969  1.00 88.60      A    O  
ANISOU 4193  O   ASN A 528     8236  12924  12504   -454   2845  -7606  A    O  
ATOM   4194  CB  ASN A 528       8.452  24.797  38.262  1.00 85.13      A    C  
ANISOU 4194  CB  ASN A 528     7914  13197  11234    287   2329  -7413  A    C  
ATOM   4195  CG  ASN A 528       6.957  25.005  38.367  1.00100.85      A    C  
ANISOU 4195  CG  ASN A 528    10284  14533  13500    219   2443  -7062  A    C  
ATOM   4196  ND2 ASN A 528       6.283  24.119  39.087  1.00 91.12      A    N  
ANISOU 4196  ND2 ASN A 528     9271  13364  11987    571   2244  -6772  A    N  
ATOM   4197  OD1 ASN A 528       6.397  25.989  37.867  1.00 90.43      A    O  
ANISOU 4197  OD1 ASN A 528     9052  12671  12636   -143   2729  -7060  A    O  
ATOM   4198  N   SER A 529       8.218  24.877  34.648  1.00 78.19      A    N  
ANISOU 4198  N   SER A 529     7520  11031  11157     58   2570  -6638  A    N  
ATOM   4199  CA  SER A 529       7.989  25.589  33.385  1.00 76.01      A    C  
ANISOU 4199  CA  SER A 529     7356  10186  11336   -237   2826  -6492  A    C  
ATOM   4200  C   SER A 529       7.416  26.998  33.533  1.00 79.31      A    C  
ANISOU 4200  C   SER A 529     7754  10203  12177   -668   3196  -6688  A    C  
ATOM   4201  O   SER A 529       7.863  27.900  32.821  1.00 80.91      A    O  
ANISOU 4201  O   SER A 529     7828  10229  12686   -998   3475  -6890  A    O  
ATOM   4202  CB  SER A 529       7.053  24.774  32.490  1.00 76.50      A    C  
ANISOU 4202  CB  SER A 529     7839   9759  11469    -11   2721  -5861  A    C  
ATOM   4203  OG  SER A 529       7.565  23.472  32.252  1.00 86.51      A    O  
ANISOU 4203  OG  SER A 529     9168  11316  12385    371   2433  -5666  A    O  
ATOM   4204  N   GLU A 530       6.409  27.177  34.410  1.00 72.56      A    N  
ANISOU 4204  N   GLU A 530     7047   9176  11348   -658   3225  -6610  A    N  
ATOM   4205  CA  GLU A 530       5.741  28.463  34.610  1.00 71.67      A    C  
ANISOU 4205  CA  GLU A 530     6958   8642  11629  -1019   3590  -6752  A    C  
ATOM   4206  C   GLU A 530       6.677  29.466  35.280  1.00 76.44      A    C  
ANISOU 4206  C   GLU A 530     7172   9604  12266  -1375   3812  -7440  A    C  
ATOM   4207  O   GLU A 530       6.643  30.654  34.948  1.00 76.31      A    O  
ANISOU 4207  O   GLU A 530     7120   9226  12648  -1758   4207  -7637  A    O  
ATOM   4208  CB  GLU A 530       4.439  28.298  35.422  1.00 71.30      A    C  
ANISOU 4208  CB  GLU A 530     7153   8382  11555   -884   3539  -6503  A    C  
ATOM   4209  CG  GLU A 530       3.306  27.641  34.648  1.00 75.58      A    C  
ANISOU 4209  CG  GLU A 530     8085   8455  12178   -656   3435  -5853  A    C  
ATOM   4210  CD  GLU A 530       2.690  28.419  33.499  1.00 89.44      A    C  
ANISOU 4210  CD  GLU A 530    10011   9587  14384   -848   3726  -5565  A    C  
ATOM   4211  OE1 GLU A 530       2.666  29.668  33.557  1.00 86.67      A    O  
ANISOU 4211  OE1 GLU A 530     9566   8999  14365  -1171   4088  -5813  A    O  
ATOM   4212  OE2 GLU A 530       2.169  27.774  32.563  1.00 81.96      A    O1-
ANISOU 4212  OE2 GLU A 530     9303   8388  13448   -667   3608  -5082  A    O1-
ATOM   4213  N   ILE A 531       7.521  28.975  36.207  1.00 73.29      A    N  
ANISOU 4213  N   ILE A 531     6480   9930  11437  -1243   3574  -7804  A    N  
ATOM   4214  CA  ILE A 531       8.507  29.777  36.935  1.00 75.97      A    C  
ANISOU 4214  CA  ILE A 531     6388  10767  11710  -1567   3733  -8512  A    C  
ATOM   4215  C   ILE A 531       9.668  30.129  35.984  1.00 77.41      A    C  
ANISOU 4215  C   ILE A 531     6337  11062  12012  -1789   3866  -8758  A    C  
ATOM   4216  O   ILE A 531      10.035  31.298  35.880  1.00 77.41      A    O  
ANISOU 4216  O   ILE A 531     6165  10929  12317  -2250   4247  -9179  A    O  
ATOM   4217  CB  ILE A 531       9.002  29.058  38.232  1.00 81.10      A    C  
ANISOU 4217  CB  ILE A 531     6778  12235  11800  -1300   3408  -8787  A    C  
ATOM   4218  CG1 ILE A 531       7.817  28.785  39.202  1.00 80.40      A    C  
ANISOU 4218  CG1 ILE A 531     6927  12006  11615  -1116   3319  -8561  A    C  
ATOM   4219  CG2 ILE A 531      10.123  29.861  38.930  1.00 86.33      A    C  
ANISOU 4219  CG2 ILE A 531     6929  13525  12348  -1653   3556  -9568  A    C  
ATOM   4220  CD1 ILE A 531       8.096  27.889  40.408  1.00 91.93      A    C  
ANISOU 4220  CD1 ILE A 531     8232  14196  12501   -746   2977  -8666  A    C  
ATOM   4221  N   ARG A 532      10.217  29.120  35.284  1.00 73.15      A    N  
ANISOU 4221  N   ARG A 532     5814  10735  11246  -1467   3581  -8489  A    N  
ATOM   4222  CA  ARG A 532      11.349  29.259  34.364  1.00 74.36      A    C  
ANISOU 4222  CA  ARG A 532     5749  11053  11453  -1607   3651  -8676  A    C  
ATOM   4223  C   ARG A 532      11.055  30.254  33.230  1.00 77.79      A    C  
ANISOU 4223  C   ARG A 532     6351  10768  12438  -1972   4061  -8565  A    C  
ATOM   4224  O   ARG A 532      11.894  31.125  32.983  1.00 79.95      A    O  
ANISOU 4224  O   ARG A 532     6357  11130  12888  -2361   4348  -9019  A    O  
ATOM   4225  CB  ARG A 532      11.770  27.896  33.796  1.00 71.88      A    C  
ANISOU 4225  CB  ARG A 532     5509  10997  10807  -1134   3271  -8304  A    C  
ATOM   4226  CG  ARG A 532      13.124  27.920  33.085  1.00 77.10      A    C  
ANISOU 4226  CG  ARG A 532     5853  12035  11404  -1228   3284  -8585  A    C  
ATOM   4227  CD  ARG A 532      13.738  26.546  33.016  1.00 73.38      A    C  
ANISOU 4227  CD  ARG A 532     5337  12080  10463   -719   2881  -8387  A    C  
ATOM   4228  NE  ARG A 532      14.682  26.424  31.915  1.00 88.90      A    N  
ANISOU 4228  NE  ARG A 532     7180  14127  12471   -747   2899  -8403  A    N  
ATOM   4229  CZ  ARG A 532      16.004  26.619  31.969  1.00106.39      A    C  
ANISOU 4229  CZ  ARG A 532     8941  16976  14506   -859   2902  -8891  A    C  
ATOM   4230  NH1 ARG A 532      16.743  26.472  30.876  1.00 89.84      A    N1+
ANISOU 4230  NH1 ARG A 532     6783  14876  12475   -872   2926  -8841  A    N1+
ATOM   4231  NH2 ARG A 532      16.596  26.920  33.120  1.00 93.21      A    N  
ANISOU 4231  NH2 ARG A 532     6863  15991  12561   -945   2869  -9434  A    N  
ATOM   4232  N   PHE A 533       9.877  30.147  32.574  1.00 71.05      A    N  
ANISOU 4232  N   PHE A 533     5922   9233  11841  -1853   4107  -7980  A    N  
ATOM   4233  CA  PHE A 533       9.483  31.036  31.472  1.00 71.06      A    C  
ANISOU 4233  CA  PHE A 533     6116   8548  12338  -2121   4491  -7781  A    C  
ATOM   4234  C   PHE A 533       9.480  32.517  31.911  1.00 78.51      A    C  
ANISOU 4234  C   PHE A 533     6937   9258  13635  -2611   4980  -8242  A    C  
ATOM   4235  O   PHE A 533      10.021  33.376  31.201  1.00 79.30      A    O  
ANISOU 4235  O   PHE A 533     6956   9134  14040  -2943   5342  -8437  A    O  
ATOM   4236  CB  PHE A 533       8.107  30.628  30.909  1.00 69.28      A    C  
ANISOU 4236  CB  PHE A 533     6332   7739  12253  -1869   4424  -7088  A    C  
ATOM   4237  CG  PHE A 533       7.340  31.703  30.169  1.00 70.84      A    C  
ANISOU 4237  CG  PHE A 533     6747   7220  12948  -2109   4854  -6867  A    C  
ATOM   4238  CD1 PHE A 533       7.784  32.178  28.937  1.00 74.76      A    C  
ANISOU 4238  CD1 PHE A 533     7256   7440  13710  -2270   5098  -6785  A    C  
ATOM   4239  CD2 PHE A 533       6.150  32.209  30.684  1.00 72.58      A    C  
ANISOU 4239  CD2 PHE A 533     7170   7047  13359  -2138   5019  -6706  A    C  
ATOM   4240  CE1 PHE A 533       7.076  33.174  28.258  1.00 75.71      A    C  
ANISOU 4240  CE1 PHE A 533     7587   6909  14269  -2443   5518  -6544  A    C  
ATOM   4241  CE2 PHE A 533       5.435  33.196  29.998  1.00 75.21      A    C  
ANISOU 4241  CE2 PHE A 533     7707   6735  14135  -2305   5432  -6467  A    C  
ATOM   4242  CZ  PHE A 533       5.908  33.678  28.795  1.00 74.08      A    C  
ANISOU 4242  CZ  PHE A 533     7575   6330  14242  -2448   5685  -6381  A    C  
ATOM   4243  N   ARG A 534       8.902  32.796  33.087  1.00 76.26      A    N  
ANISOU 4243  N   ARG A 534     6645   9027  13301  -2657   5010  -8426  A    N  
ATOM   4244  CA  ARG A 534       8.808  34.141  33.651  1.00 79.40      A    C  
ANISOU 4244  CA  ARG A 534     6952   9205  14010  -3108   5479  -8878  A    C  
ATOM   4245  C   ARG A 534      10.187  34.670  34.045  1.00 88.72      A    C  
ANISOU 4245  C   ARG A 534     7677  10936  15096  -3478   5627  -9636  A    C  
ATOM   4246  O   ARG A 534      10.492  35.837  33.785  1.00 91.30      A    O  
ANISOU 4246  O   ARG A 534     7934  10968  15786  -3933   6120  -9985  A    O  
ATOM   4247  CB  ARG A 534       7.850  34.142  34.844  1.00 80.22      A    C  
ANISOU 4247  CB  ARG A 534     7157   9298  14024  -3018   5416  -8872  A    C  
ATOM   4248  CG  ARG A 534       6.398  34.138  34.392  1.00 84.41      A    C  
ANISOU 4248  CG  ARG A 534     8126   9136  14809  -2823   5477  -8222  A    C  
ATOM   4249  CD  ARG A 534       5.396  33.985  35.517  1.00 86.60      A    C  
ANISOU 4249  CD  ARG A 534     8519   9425  14959  -2678   5361  -8149  A    C  
ATOM   4250  NE  ARG A 534       4.034  34.031  34.991  1.00 83.29      A    N  
ANISOU 4250  NE  ARG A 534     8489   8360  14798  -2514   5446  -7539  A    N  
ATOM   4251  CZ  ARG A 534       3.397  32.996  34.455  1.00 85.43      A    C  
ANISOU 4251  CZ  ARG A 534     8994   8542  14922  -2135   5116  -6954  A    C  
ATOM   4252  NH1 ARG A 534       3.985  31.807  34.391  1.00 68.22      A    N1+
ANISOU 4252  NH1 ARG A 534     6738   6830  12351  -1863   4691  -6880  A    N1+
ATOM   4253  NH2 ARG A 534       2.164  33.138  33.987  1.00 70.53      A    N  
ANISOU 4253  NH2 ARG A 534     7416   6114  13269  -2025   5224  -6448  A    N  
ATOM   4254  N   TRP A 535      11.030  33.796  34.625  1.00 85.42      A    N  
ANISOU 4254  N   TRP A 535     6949  11322  14183  -3274   5219  -9877  A    N  
ATOM   4255  CA  TRP A 535      12.389  34.112  35.048  1.00 89.07      A    C  
ANISOU 4255  CA  TRP A 535     6918  12474  14452  -3565   5274 -10596  A    C  
ATOM   4256  C   TRP A 535      13.254  34.480  33.838  1.00 94.05      A    C  
ANISOU 4256  C   TRP A 535     7454  12967  15312  -3801   5502 -10681  A    C  
ATOM   4257  O   TRP A 535      13.981  35.476  33.897  1.00 99.13      A    O  
ANISOU 4257  O   TRP A 535     7831  13697  16138  -4297   5887 -11272  A    O  
ATOM   4258  CB  TRP A 535      12.995  32.930  35.832  1.00 87.84      A    C  
ANISOU 4258  CB  TRP A 535     6488  13216  13671  -3166   4741 -10696  A    C  
ATOM   4259  CG  TRP A 535      14.488  32.960  36.030  1.00 92.99      A    C  
ANISOU 4259  CG  TRP A 535     6609  14686  14039  -3337   4694 -11319  A    C  
ATOM   4260  CD1 TRP A 535      15.376  31.978  35.701  1.00 95.79      A    C  
ANISOU 4260  CD1 TRP A 535     6767  15607  14022  -3009   4340 -11246  A    C  
ATOM   4261  CD2 TRP A 535      15.260  34.020  36.610  1.00 98.10      A    C  
ANISOU 4261  CD2 TRP A 535     6839  15693  14742  -3885   5029 -12124  A    C  
ATOM   4262  CE2 TRP A 535      16.611  33.605  36.605  1.00104.85      A    C  
ANISOU 4262  CE2 TRP A 535     7227  17384  15229  -3858   4832 -12510  A    C  
ATOM   4263  CE3 TRP A 535      14.941  35.286  37.140  1.00102.27      A    C  
ANISOU 4263  CE3 TRP A 535     7341  15924  15594  -4405   5496 -12574  A    C  
ATOM   4264  NE1 TRP A 535      16.649  32.350  36.058  1.00100.17      A    N  
ANISOU 4264  NE1 TRP A 535     6785  16897  14378  -3295   4408 -11946  A    N  
ATOM   4265  CZ2 TRP A 535      17.639  34.402  37.116  1.00109.94      A    C  
ANISOU 4265  CZ2 TRP A 535     7357  18613  15802  -4351   5071 -13344  A    C  
ATOM   4266  CZ3 TRP A 535      15.959  36.074  37.641  1.00109.56      A    C  
ANISOU 4266  CZ3 TRP A 535     7783  17381  16464  -4909   5755 -13406  A    C  
ATOM   4267  CH2 TRP A 535      17.291  35.631  37.632  1.00113.06      A    C  
ANISOU 4267  CH2 TRP A 535     7742  18694  16522  -4891   5536 -13795  A    C  
ATOM   4268  N   LEU A 536      13.161  33.702  32.743  1.00 85.27      A    N  
ANISOU 4268  N   LEU A 536     6568  11632  14198  -3471   5290 -10109  A    N  
ATOM   4269  CA  LEU A 536      13.929  33.960  31.524  1.00 84.74      A    C  
ANISOU 4269  CA  LEU A 536     6442  11421  14333  -3646   5481 -10118  A    C  
ATOM   4270  C   LEU A 536      13.474  35.266  30.858  1.00 89.85      A    C  
ANISOU 4270  C   LEU A 536     7311  11260  15567  -4060   6077 -10090  A    C  
ATOM   4271  O   LEU A 536      14.331  36.068  30.488  1.00 92.55      A    O  
ANISOU 4271  O   LEU A 536     7445  11610  16110  -4476   6440 -10517  A    O  
ATOM   4272  CB  LEU A 536      13.860  32.787  30.530  1.00 79.89      A    C  
ANISOU 4272  CB  LEU A 536     6037  10759  13561  -3179   5111  -9500  A    C  
ATOM   4273  CG  LEU A 536      14.402  31.415  30.979  1.00 82.90      A    C  
ANISOU 4273  CG  LEU A 536     6243  11880  13373  -2716   4559  -9456  A    C  
ATOM   4274  CD1 LEU A 536      14.259  30.390  29.875  1.00 78.31      A    C  
ANISOU 4274  CD1 LEU A 536     5929  11105  12721  -2317   4294  -8842  A    C  
ATOM   4275  CD2 LEU A 536      15.856  31.479  31.429  1.00 89.67      A    C  
ANISOU 4275  CD2 LEU A 536     6563  13570  13939  -2876   4511 -10117  A    C  
ATOM   4276  N   ARG A 537      12.137  35.497  30.752  1.00 84.78      A    N  
ANISOU 4276  N   ARG A 537     7081   9943  15189  -3946   6199  -9604  A    N  
ATOM   4277  CA  ARG A 537      11.538  36.710  30.171  1.00 85.84      A    C  
ANISOU 4277  CA  ARG A 537     7476   9273  15867  -4248   6775  -9485  A    C  
ATOM   4278  C   ARG A 537      11.978  37.980  30.918  1.00 95.64      A    C  
ANISOU 4278  C   ARG A 537     8498  10513  17329  -4804   7279 -10204  A    C  
ATOM   4279  O   ARG A 537      12.246  39.003  30.280  1.00 97.58      A    O  
ANISOU 4279  O   ARG A 537     8792  10309  17975  -5175   7814 -10352  A    O  
ATOM   4280  CB  ARG A 537      10.007  36.625  30.169  1.00 83.44      A    C  
ANISOU 4280  CB  ARG A 537     7593   8401  15711  -3968   6749  -8872  A    C  
ATOM   4281  CG  ARG A 537       9.425  36.332  28.803  1.00 91.47      A    C  
ANISOU 4281  CG  ARG A 537     8940   8921  16894  -3703   6724  -8160  A    C  
ATOM   4282  CD  ARG A 537       7.955  36.691  28.742  1.00 94.05      A    C  
ANISOU 4282  CD  ARG A 537     9642   8613  17479  -3565   6894  -7660  A    C  
ATOM   4283  NE  ARG A 537       7.738  38.064  28.280  1.00106.56      A    N  
ANISOU 4283  NE  ARG A 537    11365   9564  19560  -3884   7542  -7695  A    N  
ATOM   4284  CZ  ARG A 537       6.552  38.569  27.953  1.00124.58      A    C  
ANISOU 4284  CZ  ARG A 537    13975  11226  22133  -3773   7802  -7224  A    C  
ATOM   4285  NH1 ARG A 537       5.456  37.821  28.033  1.00111.76      A    N1+
ANISOU 4285  NH1 ARG A 537    12556   9554  20356  -3384   7456  -6705  A    N1+
ATOM   4286  NH2 ARG A 537       6.451  39.824  27.536  1.00115.67      A    N  
ANISOU 4286  NH2 ARG A 537    12974   9529  21446  -4042   8429  -7264  A    N  
ATOM   4287  N   LEU A 538      12.063  37.901  32.262  1.00 94.12      A    N  
ANISOU 4287  N   LEU A 538     8068  10828  16864  -4865   7127 -10657  A    N  
ATOM   4288  CA  LEU A 538      12.495  38.998  33.123  1.00 99.83      A    C  
ANISOU 4288  CA  LEU A 538     8543  11664  17724  -5400   7560 -11411  A    C  
ATOM   4289  C   LEU A 538      13.954  39.368  32.836  1.00106.91      A    C  
ANISOU 4289  C   LEU A 538     9034  12995  18594  -5806   7750 -12034  A    C  
ATOM   4290  O   LEU A 538      14.288  40.559  32.788  1.00109.90      A    O  
ANISOU 4290  O   LEU A 538     9350  13083  19324  -6343   8340 -12505  A    O  
ATOM   4291  CB  LEU A 538      12.309  38.604  34.606  1.00101.37      A    C  
ANISOU 4291  CB  LEU A 538     8541  12447  17528  -5295   7244 -11717  A    C  
ATOM   4292  CG  LEU A 538      12.421  39.703  35.658  1.00112.77      A    C  
ANISOU 4292  CG  LEU A 538     9788  13961  19098  -5807   7670 -12441  A    C  
ATOM   4293  CD1 LEU A 538      11.185  40.632  35.652  1.00112.93      A    C  
ANISOU 4293  CD1 LEU A 538    10231  13073  19605  -5929   8147 -12187  A    C  
ATOM   4294  CD2 LEU A 538      12.599  39.102  37.044  1.00117.80      A    C  
ANISOU 4294  CD2 LEU A 538    10110  15436  19213  -5669   7253 -12801  A    C  
ATOM   4295  N   CYS A 539      14.811  38.347  32.631  1.00102.15      A    N  
ANISOU 4295  N   CYS A 539     8167  13066  17580  -5547   7275 -12030  A    N  
ATOM   4296  CA  CYS A 539      16.238  38.511  32.351  1.00105.80      A    C  
ANISOU 4296  CA  CYS A 539     8202  14058  17939  -5861   7366 -12588  A    C  
ATOM   4297  C   CYS A 539      16.484  39.124  30.969  1.00111.51      A    C  
ANISOU 4297  C   CYS A 539     9108  14156  19103  -6088   7795 -12403  A    C  
ATOM   4298  O   CYS A 539      17.418  39.914  30.828  1.00114.92      A    O  
ANISOU 4298  O   CYS A 539     9276  14696  19693  -6596   8202 -12987  A    O  
ATOM   4299  CB  CYS A 539      16.971  37.183  32.492  1.00104.23      A    C  
ANISOU 4299  CB  CYS A 539     7706  14731  17165  -5433   6726 -12548  A    C  
ATOM   4300  SG  CYS A 539      17.198  36.621  34.196  1.00109.91      A    S  
ANISOU 4300  SG  CYS A 539     8030  16436  17294  -5276   6305 -13011  A    S  
ATOM   4301  N   ILE A 540      15.662  38.777  29.963  1.00105.77      A    N  
ANISOU 4301  N   ILE A 540     8821  12807  18561  -5726   7720 -11611  A    N  
ATOM   4302  CA  ILE A 540      15.828  39.283  28.595  1.00107.08      A    C  
ANISOU 4302  CA  ILE A 540     9189  12385  19112  -5865   8096 -11343  A    C  
ATOM   4303  C   ILE A 540      15.542  40.783  28.549  1.00115.52      A    C  
ANISOU 4303  C   ILE A 540    10427  12750  20717  -6370   8856 -11584  A    C  
ATOM   4304  O   ILE A 540      16.360  41.535  28.008  1.00119.64      A    O  
ANISOU 4304  O   ILE A 540    10831  13145  21483  -6793   9310 -11934  A    O  
ATOM   4305  CB  ILE A 540      14.976  38.482  27.573  1.00105.43      A    C  
ANISOU 4305  CB  ILE A 540     9388  11753  18916  -5329   7799 -10438  A    C  
ATOM   4306  CG1 ILE A 540      15.558  37.060  27.347  1.00103.57      A    C  
ANISOU 4306  CG1 ILE A 540     8976  12177  18198  -4905   7157 -10259  A    C  
ATOM   4307  CG2 ILE A 540      14.813  39.241  26.247  1.00107.18      A    C  
ANISOU 4307  CG2 ILE A 540     9906  11212  19605  -5470   8289 -10087  A    C  
ATOM   4308  CD1 ILE A 540      16.998  36.977  26.577  1.00114.96      A    C  
ANISOU 4308  CD1 ILE A 540    10096  14014  19567  -5089   7199 -10574  A    C  
ATOM   4309  N   ARG A 541      14.405  41.210  29.140  1.00111.31      A    N  
ANISOU 4309  N   ARG A 541    10167  11767  20360  -6328   9013 -11413  A    N  
ATOM   4310  CA  ARG A 541      14.010  42.615  29.232  1.00114.69      A    C  
ANISOU 4310  CA  ARG A 541    10790  11498  21287  -6760   9751 -11623  A    C  
ATOM   4311  C   ARG A 541      15.080  43.408  29.977  1.00120.63      A    C  
ANISOU 4311  C   ARG A 541    11273  12711  21850  -7171   9804 -12218  A    C  
ATOM   4312  O   ARG A 541      15.429  44.507  29.538  1.00119.93      A    O  
ANISOU 4312  O   ARG A 541    11408  12259  21900  -7343  10040 -12021  A    O  
ATOM   4313  CB  ARG A 541      12.644  42.771  29.915  1.00114.45      A    C  
ANISOU 4313  CB  ARG A 541    11068  11065  21354  -6554   9764 -11309  A    C  
ATOM   4314  CG  ARG A 541      11.468  42.449  28.993  1.00126.67      A    C  
ANISOU 4314  CG  ARG A 541    13084  11976  23070  -6075   9681 -10376  A    C  
ATOM   4315  CD  ARG A 541      10.125  42.752  29.636  1.00139.06      A    C  
ANISOU 4315  CD  ARG A 541    14955  13116  24766  -5905   9762 -10075  A    C  
ATOM   4316  NE  ARG A 541       9.938  44.184  29.891  1.00144.77      A    N  
ANISOU 4316  NE  ARG A 541    16121  13671  25216  -5733   9456  -9425  A    N  
ATOM   4317  CZ  ARG A 541       9.193  44.992  29.142  1.00151.23      A    C  
ANISOU 4317  CZ  ARG A 541    17470  14057  25932  -5315   9176  -8398  A    C  
ATOM   4318  NH1 ARG A 541       8.544  44.518  28.084  1.00140.83      A    N1+
ANISOU 4318  NH1 ARG A 541    16172  12054  25281  -5405   9942  -8448  A    N1+
ATOM   4319  NH2 ARG A 541       9.081  46.276  29.451  1.00139.42      A    N  
ANISOU 4319  NH2 ARG A 541    16057  12057  24859  -5718   9880  -8768  A    N  
ATOM   4320  N   ALA A 542      15.667  42.804  31.047  1.00118.19      A    N  
ANISOU 4320  N   ALA A 542    10503  13277  21128  -7235   9457 -12815  A    N  
ATOM   4321  CA  ALA A 542      16.744  43.416  31.835  1.00118.33      A    C  
ANISOU 4321  CA  ALA A 542    10351  13884  20723  -7383   9165 -13029  A    C  
ATOM   4322  C   ALA A 542      17.981  43.696  30.985  1.00121.05      A    C  
ANISOU 4322  C   ALA A 542    10674  14404  20915  -7400   9001 -12802  A    C  
ATOM   4323  O   ALA A 542      18.748  44.603  31.310  1.00121.78      A    O  
ANISOU 4323  O   ALA A 542    10812  14641  20817  -7526   8879 -12743  A    O  
ATOM   4324  CB  ALA A 542      17.118  42.522  33.005  1.00119.25      A    C  
ANISOU 4324  CB  ALA A 542    10065  14954  20291  -7219   8627 -13391  A    C  
ATOM   4325  N   GLY A 543      18.150  42.933  29.906  1.00117.81      A    N  
ANISOU 4325  N   GLY A 543    10072  13940  20751  -7456   9243 -12987  A    N  
ATOM   4326  CA  GLY A 543      19.269  43.078  28.984  1.00117.80      A    C  
ANISOU 4326  CA  GLY A 543     9973  14080  20704  -7553   9235 -12934  A    C  
ATOM   4327  C   GLY A 543      20.476  42.258  29.381  1.00120.69      A    C  
ANISOU 4327  C   GLY A 543     9914  15471  20470  -7378   8618 -13118  A    C  
ATOM   4328  O   GLY A 543      21.613  42.622  29.058  1.00120.90      A    O  
ANISOU 4328  O   GLY A 543     9847  15766  20324  -7474   8502 -13084  A    O  
ATOM   4329  N   TRP A 544      20.229  41.136  30.073  1.00118.08      A    N  
ANISOU 4329  N   TRP A 544     9183  15738  19946  -7274   8436 -13618  A    N  
ATOM   4330  CA  TRP A 544      21.273  40.210  30.498  1.00118.39      A    C  
ANISOU 4330  CA  TRP A 544     8738  16820  19424  -7091   7915 -13911  A    C  
ATOM   4331  C   TRP A 544      21.650  39.312  29.312  1.00121.27      A    C  
ANISOU 4331  C   TRP A 544     9013  17289  19773  -6853   7771 -13714  A    C  
ATOM   4332  O   TRP A 544      20.797  38.608  28.767  1.00117.60      A    O  
ANISOU 4332  O   TRP A 544     8732  16499  19450  -6557   7713 -13388  A    O  
ATOM   4333  CB  TRP A 544      20.812  39.383  31.723  1.00117.15      A    C  
ANISOU 4333  CB  TRP A 544     8307  17275  18929  -6888   7598 -14249  A    C  
ATOM   4334  CG  TRP A 544      21.923  38.782  32.544  1.00118.17      A    C  
ANISOU 4334  CG  TRP A 544     8028  18491  18381  -6647   7017 -14416  A    C  
ATOM   4335  CD1 TRP A 544      23.264  38.946  32.361  1.00120.54      A    C  
ANISOU 4335  CD1 TRP A 544     8239  19203  18359  -6586   6736 -14217  A    C  
ATOM   4336  CD2 TRP A 544      21.777  37.927  33.688  1.00118.07      A    C  
ANISOU 4336  CD2 TRP A 544     7738  19223  17900  -6337   6595 -14622  A    C  
ATOM   4337  CE2 TRP A 544      23.076  37.606  34.139  1.00121.47      A    C  
ANISOU 4337  CE2 TRP A 544     7976  20449  17729  -6053   6063 -14436  A    C  
ATOM   4338  CE3 TRP A 544      20.675  37.399  34.378  1.00118.14      A    C  
ANISOU 4338  CE3 TRP A 544     7771  19222  17894  -6151   6527 -14698  A    C  
ATOM   4339  NE1 TRP A 544      23.961  38.273  33.334  1.00120.61      A    N  
ANISOU 4339  NE1 TRP A 544     7900  20150  17775  -6306   6241 -14362  A    N  
ATOM   4340  CZ2 TRP A 544      23.303  36.768  35.237  1.00121.38      A    C  
ANISOU 4340  CZ2 TRP A 544     7667  21300  17151  -5692   5597 -14565  A    C  
ATOM   4341  CZ3 TRP A 544      20.899  36.575  35.470  1.00119.43      A    C  
ANISOU 4341  CZ3 TRP A 544     7674  20249  17455  -5758   5999 -14760  A    C  
ATOM   4342  CH2 TRP A 544      22.198  36.276  35.897  1.00120.80      A    C  
ANISOU 4342  CH2 TRP A 544     7594  21246  17059  -5533   5557 -14700  A    C  
ATOM   4343  N   GLU A 545      22.912  39.397  28.878  1.00119.86      A    N  
ANISOU 4343  N   GLU A 545     8602  17511  19427  -6964   7702 -13834  A    N  
ATOM   4344  CA  GLU A 545      23.446  38.611  27.769  1.00120.14      A    C  
ANISOU 4344  CA  GLU A 545     8462  17730  19454  -6830   7635 -13809  A    C  
ATOM   4345  C   GLU A 545      23.593  37.133  28.130  1.00123.32      A    C  
ANISOU 4345  C   GLU A 545     8573  18917  19365  -6319   7043 -13816  A    C  
ATOM   4346  O   GLU A 545      23.483  36.280  27.251  1.00119.20      A    O  
ANISOU 4346  O   GLU A 545     8221  18267  18802  -5918   6798 -13313  A    O  
ATOM   4347  CB  GLU A 545      24.808  39.166  27.333  1.00121.94      A    C  
ANISOU 4347  CB  GLU A 545     8659  18192  19480  -6906   7504 -13612  A    C  
ATOM   4348  CG  GLU A 545      24.711  40.385  26.434  1.00129.72      A    C  
ANISOU 4348  CG  GLU A 545    10342  18233  20712  -6859   7592 -12642  A    C  
ATOM   4349  CD  GLU A 545      25.955  41.250  26.371  1.00145.12      A    C  
ANISOU 4349  CD  GLU A 545    12918  20160  22061  -6240   6673 -11099  A    C  
ATOM   4350  OE1 GLU A 545      27.013  40.753  25.917  1.00138.34      A    O  
ANISOU 4350  OE1 GLU A 545    11757  19776  21031  -6213   6557 -11250  A    O  
ATOM   4351  OE2 GLU A 545      25.863  42.439  26.753  1.00141.89      A    O1-
ANISOU 4351  OE2 GLU A 545    12624  19438  21849  -6575   6955 -11220  A    O1-
ATOM   4352  N   ASP A 546      23.846  36.841  29.420  1.00121.75      A    N  
ANISOU 4352  N   ASP A 546     8080  19473  18707  -6191   6694 -14109  A    N  
ATOM   4353  CA  ASP A 546      24.078  35.498  29.964  1.00121.51      A    C  
ANISOU 4353  CA  ASP A 546     7720  20314  18134  -5689   6135 -14179  A    C  
ATOM   4354  C   ASP A 546      22.870  34.561  29.827  1.00118.97      A    C  
ANISOU 4354  C   ASP A 546     7926  19513  17764  -5057   5758 -13318  A    C  
ATOM   4355  O   ASP A 546      23.059  33.342  29.799  1.00116.21      A    O  
ANISOU 4355  O   ASP A 546     7545  19612  16999  -4491   5250 -12986  A    O  
ATOM   4356  CB  ASP A 546      24.483  35.589  31.448  1.00123.97      A    C  
ANISOU 4356  CB  ASP A 546     7898  21280  17924  -5545   5759 -14220  A    C  
ATOM   4357  CG  ASP A 546      25.725  36.422  31.751  1.00131.92      A    C  
ANISOU 4357  CG  ASP A 546     9218  22267  18639  -5467   5464 -13527  A    C  
ATOM   4358  OD1 ASP A 546      26.092  37.278  30.915  1.00131.71      A    O  
ANISOU 4358  OD1 ASP A 546     9371  21740  18933  -5768   5754 -13388  A    O  
ATOM   4359  OD2 ASP A 546      26.258  36.304  32.876  1.00137.60      A    O1-
ANISOU 4359  OD2 ASP A 546    10012  23403  18865  -5135   4991 -13147  A    O1-
ATOM   4360  N   VAL A 547      21.648  35.121  29.741  1.00112.75      A    N  
ANISOU 4360  N   VAL A 547     7617  17831  17393  -5151   6024 -12967  A    N  
ATOM   4361  CA  VAL A 547      20.404  34.357  29.644  1.00106.83      A    C  
ANISOU 4361  CA  VAL A 547     7363  16596  16630  -4626   5722 -12193  A    C  
ATOM   4362  C   VAL A 547      20.027  33.990  28.174  1.00106.03      A    C  
ANISOU 4362  C   VAL A 547     7679  15832  16776  -4388   5719 -11487  A    C  
ATOM   4363  O   VAL A 547      19.141  33.150  27.987  1.00102.34      A    O  
ANISOU 4363  O   VAL A 547     7576  15084  16225  -3915   5406 -10846  A    O  
ATOM   4364  CB  VAL A 547      19.260  35.124  30.357  1.00110.90      A    C  
ANISOU 4364  CB  VAL A 547     8144  16569  17425  -4822   5989 -12187  A    C  
ATOM   4365  CG1 VAL A 547      18.668  36.217  29.475  1.00110.28      A    C  
ANISOU 4365  CG1 VAL A 547     8437  15500  17966  -5172   6554 -11978  A    C  
ATOM   4366  CG2 VAL A 547      18.177  34.175  30.861  1.00106.29      A    C  
ANISOU 4366  CG2 VAL A 547     7861  15920  16606  -4271   5555 -11635  A    C  
ATOM   4367  N   ILE A 548      20.683  34.601  27.149  1.00102.21      A    N  
ANISOU 4367  N   ILE A 548     7137  15118  16580  -4721   6070 -11611  A    N  
ATOM   4368  CA  ILE A 548      20.386  34.349  25.726  1.00 97.83      A    C  
ANISOU 4368  CA  ILE A 548     6943  13972  16255  -4537   6106 -10989  A    C  
ATOM   4369  C   ILE A 548      20.442  32.821  25.407  1.00 98.92      A    C  
ANISOU 4369  C   ILE A 548     7145  14467  15973  -3905   5511 -10512  A    C  
ATOM   4370  O   ILE A 548      19.444  32.328  24.868  1.00 94.34      A    O  
ANISOU 4370  O   ILE A 548     7002  13365  15478  -3575   5371  -9850  A    O  
ATOM   4371  CB  ILE A 548      21.266  35.197  24.752  1.00103.75      A    C  
ANISOU 4371  CB  ILE A 548     7556  14547  17318  -4995   6570 -11270  A    C  
ATOM   4372  CG1 ILE A 548      21.026  36.708  24.965  1.00107.69      A    C  
ANISOU 4372  CG1 ILE A 548     8107  14521  18289  -5597   7230 -11646  A    C  
ATOM   4373  CG2 ILE A 548      21.037  34.810  23.269  1.00100.23      A    C  
ANISOU 4373  CG2 ILE A 548     7452  13592  17038  -4751   6554 -10615  A    C  
ATOM   4374  CD1 ILE A 548      22.132  37.636  24.379  1.00120.94      A    C  
ANISOU 4374  CD1 ILE A 548     9518  16224  20210  -6161   7735 -12176  A    C  
ATOM   4375  N   PRO A 549      21.508  32.038  25.762  1.00 97.48      A    N  
ANISOU 4375  N   PRO A 549     6552  15156  15328  -3707   5165 -10815  A    N  
ATOM   4376  CA  PRO A 549      21.489  30.598  25.425  1.00 93.83      A    C  
ANISOU 4376  CA  PRO A 549     6216  14937  14499  -3087   4658 -10322  A    C  
ATOM   4377  C   PRO A 549      20.460  29.770  26.217  1.00 94.59      A    C  
ANISOU 4377  C   PRO A 549     6588  14984  14368  -2637   4304  -9925  A    C  
ATOM   4378  O   PRO A 549      20.139  28.671  25.772  1.00 91.67      A    O  
ANISOU 4378  O   PRO A 549     6485  14523  13824  -2165   3986  -9391  A    O  
ATOM   4379  CB  PRO A 549      22.921  30.141  25.725  1.00 99.12      A    C  
ANISOU 4379  CB  PRO A 549     6341  16578  14741  -3016   4447 -10812  A    C  
ATOM   4380  CG  PRO A 549      23.412  31.105  26.760  1.00108.40      A    C  
ANISOU 4380  CG  PRO A 549     7098  18171  15919  -3493   4694 -11562  A    C  
ATOM   4381  CD  PRO A 549      22.795  32.417  26.396  1.00104.04      A    C  
ANISOU 4381  CD  PRO A 549     6789  16792  15948  -4027   5242 -11605  A    C  
ATOM   4382  N   LEU A 550      19.946  30.283  27.366  1.00 91.63      A    N  
ANISOU 4382  N   LEU A 550     6161  14657  13997  -2795   4380 -10190  A    N  
ATOM   4383  CA  LEU A 550      18.934  29.604  28.188  1.00 88.25      A    C  
ANISOU 4383  CA  LEU A 550     5988  14171  13373  -2416   4090  -9851  A    C  
ATOM   4384  C   LEU A 550      17.528  29.828  27.629  1.00 83.82      A    C  
ANISOU 4384  C   LEU A 550     5967  12682  13200  -2404   4240  -9271  A    C  
ATOM   4385  O   LEU A 550      16.721  28.898  27.605  1.00 77.84      A    O  
ANISOU 4385  O   LEU A 550     5531  11747  12297  -1980   3948  -8747  A    O  
ATOM   4386  CB  LEU A 550      18.979  30.071  29.658  1.00 92.31      A    C  
ANISOU 4386  CB  LEU A 550     6209  15143  13721  -2595   4118 -10386  A    C  
ATOM   4387  CG  LEU A 550      20.165  29.610  30.519  1.00101.97      A    C  
ANISOU 4387  CG  LEU A 550     6898  17432  14415  -2454   3849 -10890  A    C  
ATOM   4388  CD1 LEU A 550      20.259  30.444  31.799  1.00106.22      A    C  
ANISOU 4388  CD1 LEU A 550     7104  18359  14896  -2821   4017 -11535  A    C  
ATOM   4389  CD2 LEU A 550      20.056  28.119  30.874  1.00103.81      A    C  
ANISOU 4389  CD2 LEU A 550     7242  18045  14157  -1759   3337 -10467  A    C  
ATOM   4390  N   ALA A 551      17.239  31.077  27.205  1.00 80.26      A    N  
ANISOU 4390  N   ALA A 551     5607  11657  13232  -2870   4719  -9376  A    N  
ATOM   4391  CA  ALA A 551      15.965  31.474  26.614  1.00 76.33      A    C  
ANISOU 4391  CA  ALA A 551     5577  10300  13125  -2888   4928  -8856  A    C  
ATOM   4392  C   ALA A 551      15.773  30.773  25.263  1.00 77.57      A    C  
ANISOU 4392  C   ALA A 551     6018  10133  13323  -2607   4794  -8259  A    C  
ATOM   4393  O   ALA A 551      14.677  30.286  24.986  1.00 73.38      A    O  
ANISOU 4393  O   ALA A 551     5864   9183  12836  -2340   4665  -7701  A    O  
ATOM   4394  CB  ALA A 551      15.903  32.987  26.456  1.00 79.35      A    C  
ANISOU 4394  CB  ALA A 551     5952  10209  13987  -3434   5515  -9151  A    C  
ATOM   4395  N   LEU A 552      16.848  30.686  24.452  1.00 76.75      A    N  
ANISOU 4395  N   LEU A 552     5715  10265  13182  -2672   4818  -8398  A    N  
ATOM   4396  CA  LEU A 552      16.852  29.998  23.156  1.00 74.82      A    C  
ANISOU 4396  CA  LEU A 552     5686   9805  12938  -2424   4689  -7905  A    C  
ATOM   4397  C   LEU A 552      16.602  28.497  23.335  1.00 77.61      A    C  
ANISOU 4397  C   LEU A 552     6173  10442  12875  -1878   4175  -7545  A    C  
ATOM   4398  O   LEU A 552      15.896  27.889  22.525  1.00 73.12      A    O  
ANISOU 4398  O   LEU A 552     5948   9498  12338  -1632   4056  -6992  A    O  
ATOM   4399  CB  LEU A 552      18.186  30.207  22.416  1.00 77.57      A    C  
ANISOU 4399  CB  LEU A 552     5736  10441  13298  -2623   4824  -8218  A    C  
ATOM   4400  CG  LEU A 552      18.424  31.553  21.733  1.00 85.18      A    C  
ANISOU 4400  CG  LEU A 552     6675  10971  14719  -3127   5378  -8413  A    C  
ATOM   4401  CD1 LEU A 552      19.890  31.713  21.374  1.00 88.65      A    C  
ANISOU 4401  CD1 LEU A 552     6716  11882  15084  -3349   5475  -8880  A    C  
ATOM   4402  CD2 LEU A 552      17.568  31.706  20.481  1.00 84.22      A    C  
ANISOU 4402  CD2 LEU A 552     6977  10117  14907  -3059   5549  -7791  A    C  
ATOM   4403  N   ALA A 553      17.185  27.913  24.403  1.00 77.41      A    N  
ANISOU 4403  N   ALA A 553     5872  11090  12449  -1693   3895  -7866  A    N  
ATOM   4404  CA  ALA A 553      17.047  26.505  24.756  1.00 75.54      A    C  
ANISOU 4404  CA  ALA A 553     5742  11171  11786  -1162   3446  -7581  A    C  
ATOM   4405  C   ALA A 553      15.581  26.154  25.057  1.00 75.59      A    C  
ANISOU 4405  C   ALA A 553     6173  10706  11842   -960   3345  -7103  A    C  
ATOM   4406  O   ALA A 553      15.010  25.303  24.373  1.00 72.22      A    O  
ANISOU 4406  O   ALA A 553     6070  10005  11365   -671   3176  -6598  A    O  
ATOM   4407  CB  ALA A 553      17.929  26.176  25.953  1.00 79.76      A    C  
ANISOU 4407  CB  ALA A 553     5873  12526  11907  -1036   3241  -8055  A    C  
ATOM   4408  N   MET A 554      14.947  26.881  26.009  1.00 72.38      A    N  
ANISOU 4408  N   MET A 554     5763  10182  11557  -1153   3482  -7278  A    N  
ATOM   4409  CA  MET A 554      13.551  26.661  26.401  1.00 68.66      A    C  
ANISOU 4409  CA  MET A 554     5652   9297  11140  -1002   3414  -6883  A    C  
ATOM   4410  C   MET A 554      12.573  26.939  25.236  1.00 68.74      A    C  
ANISOU 4410  C   MET A 554     6033   8571  11514  -1076   3595  -6379  A    C  
ATOM   4411  O   MET A 554      11.551  26.258  25.124  1.00 63.77      A    O  
ANISOU 4411  O   MET A 554     5731   7669  10828   -820   3427  -5914  A    O  
ATOM   4412  CB  MET A 554      13.174  27.491  27.633  1.00 72.72      A    C  
ANISOU 4412  CB  MET A 554     6046   9855  11730  -1235   3569  -7231  A    C  
ATOM   4413  CG  MET A 554      11.938  26.954  28.355  1.00 73.74      A    C  
ANISOU 4413  CG  MET A 554     6469   9798  11750   -976   3388  -6892  A    C  
ATOM   4414  SD  MET A 554      11.412  27.926  29.780  1.00 79.67      A    S  
ANISOU 4414  SD  MET A 554     7115  10546  12609  -1246   3586  -7265  A    S  
ATOM   4415  CE  MET A 554      10.023  26.958  30.319  1.00 72.83      A    C  
ANISOU 4415  CE  MET A 554     6634   9479  11560   -844   3305  -6744  A    C  
ATOM   4416  N   ALA A 555      12.900  27.907  24.365  1.00 67.57      A    N  
ANISOU 4416  N   ALA A 555     5826   8133  11714  -1414   3942  -6470  A    N  
ATOM   4417  CA  ALA A 555      12.068  28.255  23.213  1.00 65.95      A    C  
ANISOU 4417  CA  ALA A 555     5933   7289  11835  -1471   4141  -6000  A    C  
ATOM   4418  C   ALA A 555      12.128  27.188  22.110  1.00 69.01      A    C  
ANISOU 4418  C   ALA A 555     6492   7662  12065  -1179   3901  -5582  A    C  
ATOM   4419  O   ALA A 555      11.189  27.099  21.312  1.00 67.00      A    O  
ANISOU 4419  O   ALA A 555     6537   6967  11952  -1103   3934  -5105  A    O  
ATOM   4420  CB  ALA A 555      12.494  29.602  22.650  1.00 69.35      A    C  
ANISOU 4420  CB  ALA A 555     6249   7441  12660  -1895   4613  -6231  A    C  
ATOM   4421  N   THR A 556      13.215  26.383  22.059  1.00 66.49      A    N  
ANISOU 4421  N   THR A 556     5975   7846  11441  -1011   3670  -5766  A    N  
ATOM   4422  CA  THR A 556      13.367  25.360  21.019  1.00 64.73      A    C  
ANISOU 4422  CA  THR A 556     5905   7629  11059   -742   3464  -5418  A    C  
ATOM   4423  C   THR A 556      13.162  23.922  21.541  1.00 66.05      A    C  
ANISOU 4423  C   THR A 556     6213   8059  10823   -304   3067  -5223  A    C  
ATOM   4424  O   THR A 556      12.870  23.039  20.730  1.00 62.21      A    O  
ANISOU 4424  O   THR A 556     5973   7423  10243    -82   2921  -4838  A    O  
ATOM   4425  CB  THR A 556      14.724  25.467  20.303  1.00 73.85      A    C  
ANISOU 4425  CB  THR A 556     6784   9086  12188   -843   3531  -5690  A    C  
ATOM   4426  CG2 THR A 556      14.831  26.708  19.443  1.00 71.82      A    C  
ANISOU 4426  CG2 THR A 556     6492   8459  12339  -1230   3943  -5739  A    C  
ATOM   4427  OG1 THR A 556      15.785  25.407  21.253  1.00 77.81      A    O  
ANISOU 4427  OG1 THR A 556     6914  10200  12451   -845   3438  -6203  A    O  
ATOM   4428  N   GLU A 557      13.323  23.672  22.864  1.00 64.20      A    N  
ANISOU 4428  N   GLU A 557     5833   8219  10340   -177   2911  -5487  A    N  
ATOM   4429  CA  GLU A 557      13.134  22.313  23.402  1.00 62.63      A    C  
ANISOU 4429  CA  GLU A 557     5792   8252   9753    263   2575  -5287  A    C  
ATOM   4430  C   GLU A 557      11.654  21.998  23.593  1.00 61.67      A    C  
ANISOU 4430  C   GLU A 557     6050   7691   9689    357   2528  -4875  A    C  
ATOM   4431  O   GLU A 557      11.278  20.833  23.715  1.00 60.37      A    O  
ANISOU 4431  O   GLU A 557     6120   7548   9269    693   2304  -4598  A    O  
ATOM   4432  CB  GLU A 557      13.898  22.078  24.715  1.00 67.14      A    C  
ANISOU 4432  CB  GLU A 557     6066   9456   9988    421   2420  -5683  A    C  
ATOM   4433  CG  GLU A 557      15.403  22.037  24.556  1.00 83.80      A    C  
ANISOU 4433  CG  GLU A 557     7800  12131  11910    456   2379  -6042  A    C  
ATOM   4434  CD  GLU A 557      16.162  21.760  25.836  1.00111.08      A    C  
ANISOU 4434  CD  GLU A 557    10928  16293  14983    648   2212  -6422  A    C  
ATOM   4435  OE1 GLU A 557      16.091  22.580  26.783  1.00117.40      A    O  
ANISOU 4435  OE1 GLU A 557    11496  17259  15852    386   2331  -6797  A    O  
ATOM   4436  OE2 GLU A 557      16.921  20.768  25.843  1.00101.39      A    O1-
ANISOU 4436  OE2 GLU A 557     9666  15480  13378   1068   1976  -6354  A    O1-
ATOM   4437  N   GLN A 558      10.818  23.025  23.593  1.00 56.14      A    N  
ANISOU 4437  N   GLN A 558     5417   6589   9327     65   2760  -4832  A    N  
ATOM   4438  CA  GLN A 558       9.373  22.867  23.691  1.00 52.87      A    C  
ANISOU 4438  CA  GLN A 558     5332   5755   9002    115   2748  -4446  A    C  
ATOM   4439  C   GLN A 558       8.734  23.849  22.709  1.00 58.23      A    C  
ANISOU 4439  C   GLN A 558     6108   5932  10085   -166   3035  -4244  A    C  
ATOM   4440  O   GLN A 558       9.412  24.754  22.222  1.00 61.08      A    O  
ANISOU 4440  O   GLN A 558     6276   6268  10664   -419   3271  -4460  A    O  
ATOM   4441  CB  GLN A 558       8.871  23.022  25.142  1.00 53.70      A    C  
ANISOU 4441  CB  GLN A 558     5411   5977   9015    144   2703  -4605  A    C  
ATOM   4442  CG  GLN A 558       9.214  24.338  25.829  1.00 61.55      A    C  
ANISOU 4442  CG  GLN A 558     6122   7052  10213   -186   2948  -5050  A    C  
ATOM   4443  CD  GLN A 558       8.269  25.455  25.461  1.00 67.13      A    C  
ANISOU 4443  CD  GLN A 558     6952   7211  11342   -478   3263  -4907  A    C  
ATOM   4444  NE2 GLN A 558       8.808  26.584  25.023  1.00 54.60      A    N  
ANISOU 4444  NE2 GLN A 558     5184   5516  10044   -803   3574  -5154  A    N  
ATOM   4445  OE1 GLN A 558       7.052  25.310  25.531  1.00 58.88      A    O  
ANISOU 4445  OE1 GLN A 558     6169   5836  10367   -408   3251  -4565  A    O  
ATOM   4446  N   GLY A 559       7.461  23.646  22.408  1.00 52.60      A    N  
ANISOU 4446  N   GLY A 559     5687   4845   9452   -109   3026  -3828  A    N  
ATOM   4447  CA  GLY A 559       6.732  24.460  21.444  1.00 50.93      A    C  
ANISOU 4447  CA  GLY A 559     5589   4187   9574   -297   3278  -3554  A    C  
ATOM   4448  C   GLY A 559       5.391  24.967  21.898  1.00 55.28      A    C  
ANISOU 4448  C   GLY A 559     6296   4413  10293   -353   3390  -3352  A    C  
ATOM   4449  O   GLY A 559       4.549  25.312  21.065  1.00 54.67      A    O  
ANISOU 4449  O   GLY A 559     6370   3999  10405   -398   3526  -3002  A    O  
ATOM   4450  N   ARG A 560       5.181  25.040  23.225  1.00 52.65      A    N  
ANISOU 4450  N   ARG A 560     5915   4207   9881   -338   3340  -3567  A    N  
ATOM   4451  CA  ARG A 560       3.957  25.567  23.814  1.00 51.08      A    C  
ANISOU 4451  CA  ARG A 560     5841   3729   9837   -393   3456  -3424  A    C  
ATOM   4452  C   ARG A 560       3.987  27.088  23.600  1.00 56.46      A    C  
ANISOU 4452  C   ARG A 560     6410   4129  10911   -688   3863  -3557  A    C  
ATOM   4453  O   ARG A 560       4.907  27.760  24.071  1.00 57.60      A    O  
ANISOU 4453  O   ARG A 560     6325   4430  11132   -876   4015  -3995  A    O  
ATOM   4454  CB  ARG A 560       3.851  25.160  25.291  1.00 50.67      A    C  
ANISOU 4454  CB  ARG A 560     5758   3933   9561   -285   3285  -3643  A    C  
ATOM   4455  CG  ARG A 560       2.545  25.552  25.960  1.00 62.83      A    C  
ANISOU 4455  CG  ARG A 560     7446   5210  11215   -306   3365  -3474  A    C  
ATOM   4456  CD  ARG A 560       2.516  25.077  27.395  1.00 64.24      A    C  
ANISOU 4456  CD  ARG A 560     7590   5676  11143   -187   3190  -3695  A    C  
ATOM   4457  NE  ARG A 560       1.399  25.661  28.129  1.00 59.75      A    N  
ANISOU 4457  NE  ARG A 560     7109   4872  10723   -260   3321  -3628  A    N  
ATOM   4458  CZ  ARG A 560       1.203  25.503  29.431  1.00 68.94      A    C  
ANISOU 4458  CZ  ARG A 560     8246   6226  11722   -198   3231  -3813  A    C  
ATOM   4459  NH1 ARG A 560       2.041  24.770  30.152  1.00 52.03      A    N1+
ANISOU 4459  NH1 ARG A 560     5990   4531   9246    -40   3008  -4062  A    N1+
ATOM   4460  NH2 ARG A 560       0.163  26.075  30.024  1.00 60.10      A    N  
ANISOU 4460  NH2 ARG A 560     7209   4870  10756   -271   3370  -3740  A    N  
ATOM   4461  N   MET A 561       3.038  27.593  22.788  1.00 52.94      A    N  
ANISOU 4461  N   MET A 561     6127   3286  10703   -720   4054  -3172  A    N  
ATOM   4462  CA  MET A 561       2.921  28.988  22.365  1.00 56.08      A    C  
ANISOU 4462  CA  MET A 561     6487   3333  11485   -943   4486  -3176  A    C  
ATOM   4463  C   MET A 561       2.974  29.974  23.511  1.00 58.90      A    C  
ANISOU 4463  C   MET A 561     6730   3633  12017  -1145   4731  -3557  A    C  
ATOM   4464  O   MET A 561       3.605  31.014  23.348  1.00 61.89      A    O  
ANISOU 4464  O   MET A 561     6986   3877  12653  -1391   5081  -3813  A    O  
ATOM   4465  CB  MET A 561       1.642  29.221  21.572  1.00 58.58      A    C  
ANISOU 4465  CB  MET A 561     7011   3294  11953   -854   4605  -2648  A    C  
ATOM   4466  CG  MET A 561       1.753  28.774  20.154  1.00 62.67      A    C  
ANISOU 4466  CG  MET A 561     7595   3804  12413   -760   4532  -2321  A    C  
ATOM   4467  SD  MET A 561       0.599  29.667  19.108  1.00 69.32      A    S  
ANISOU 4467  SD  MET A 561     8575   4233  13529   -733   4857  -1804  A    S  
ATOM   4468  CE  MET A 561      -0.729  28.575  19.137  1.00 63.45      A    C  
ANISOU 4468  CE  MET A 561     8001   3565  12541   -509   4537  -1419  A    C  
ATOM   4469  N   LYS A 562       2.356  29.644  24.668  1.00 51.61      A    N  
ANISOU 4469  N   LYS A 562     5845   2815  10948  -1058   4567  -3621  A    N  
ATOM   4470  CA  LYS A 562       2.383  30.481  25.872  1.00 54.14      A    C  
ANISOU 4470  CA  LYS A 562     6052   3134  11386  -1242   4766  -4014  A    C  
ATOM   4471  C   LYS A 562       3.823  30.816  26.277  1.00 60.73      A    C  
ANISOU 4471  C   LYS A 562     6597   4291  12186  -1457   4838  -4595  A    C  
ATOM   4472  O   LYS A 562       4.087  31.923  26.750  1.00 62.25      A    O  
ANISOU 4472  O   LYS A 562     6669   4371  12614  -1735   5184  -4952  A    O  
ATOM   4473  CB  LYS A 562       1.668  29.757  27.027  1.00 55.62      A    C  
ANISOU 4473  CB  LYS A 562     6312   3501  11319  -1064   4483  -3992  A    C  
ATOM   4474  CG  LYS A 562       1.465  30.589  28.282  1.00 60.85      A    C  
ANISOU 4474  CG  LYS A 562     6888   4136  12095  -1232   4684  -4337  A    C  
ATOM   4475  CD  LYS A 562       0.904  29.722  29.393  1.00 66.04      A    C  
ANISOU 4475  CD  LYS A 562     7605   5044  12444  -1032   4366  -4325  A    C  
ATOM   4476  CE  LYS A 562       0.645  30.505  30.647  1.00 67.09      A    C  
ANISOU 4476  CE  LYS A 562     7656   5166  12669  -1191   4554  -4659  A    C  
ATOM   4477  NZ  LYS A 562       0.217  29.622  31.757  1.00 69.39      A    N1+
ANISOU 4477  NZ  LYS A 562     7989   5748  12628   -987   4240  -4667  A    N1+
ATOM   4478  N   PHE A 563       4.750  29.859  26.076  1.00 56.70      A    N  
ANISOU 4478  N   PHE A 563     5973   4193  11378  -1330   4530  -4696  A    N  
ATOM   4479  CA  PHE A 563       6.141  30.036  26.445  1.00 59.79      A    C  
ANISOU 4479  CA  PHE A 563     6053   4990  11674  -1497   4548  -5240  A    C  
ATOM   4480  C   PHE A 563       7.036  30.421  25.244  1.00 65.49      A    C  
ANISOU 4480  C   PHE A 563     6683   5638  12564  -1654   4742  -5280  A    C  
ATOM   4481  O   PHE A 563       7.770  31.400  25.340  1.00 69.10      A    O  
ANISOU 4481  O   PHE A 563     6940   6096  13220  -1973   5063  -5694  A    O  
ATOM   4482  CB  PHE A 563       6.680  28.764  27.123  1.00 61.46      A    C  
ANISOU 4482  CB  PHE A 563     6162   5770  11420  -1229   4102  -5364  A    C  
ATOM   4483  CG  PHE A 563       5.931  28.180  28.307  1.00 62.44      A    C  
ANISOU 4483  CG  PHE A 563     6381   6034  11309  -1025   3870  -5310  A    C  
ATOM   4484  CD1 PHE A 563       5.321  29.004  29.245  1.00 67.12      A    C  
ANISOU 4484  CD1 PHE A 563     6962   6486  12055  -1193   4070  -5489  A    C  
ATOM   4485  CD2 PHE A 563       5.917  26.802  28.530  1.00 63.60      A    C  
ANISOU 4485  CD2 PHE A 563     6626   6469  11072   -668   3476  -5110  A    C  
ATOM   4486  CE1 PHE A 563       4.661  28.464  30.354  1.00 67.76      A    C  
ANISOU 4486  CE1 PHE A 563     7123   6716  11907  -1006   3861  -5448  A    C  
ATOM   4487  CE2 PHE A 563       5.272  26.263  29.645  1.00 65.89      A    C  
ANISOU 4487  CE2 PHE A 563     7009   6888  11137   -480   3289  -5064  A    C  
ATOM   4488  CZ  PHE A 563       4.647  27.098  30.548  1.00 65.16      A    C  
ANISOU 4488  CZ  PHE A 563     6894   6667  11196   -651   3472  -5232  A    C  
ATOM   4489  N   THR A 564       6.984  29.651  24.136  1.00 59.57      A    N  
ANISOU 4489  N   THR A 564     6076   4828  11729  -1449   4565  -4872  A    N  
ATOM   4490  CA  THR A 564       7.811  29.824  22.927  1.00 59.49      A    C  
ANISOU 4490  CA  THR A 564     5996   4780  11825  -1545   4696  -4856  A    C  
ATOM   4491  C   THR A 564       7.616  31.210  22.254  1.00 65.16      A    C  
ANISOU 4491  C   THR A 564     6763   5004  12991  -1828   5211  -4810  A    C  
ATOM   4492  O   THR A 564       8.610  31.898  22.018  1.00 66.90      A    O  
ANISOU 4492  O   THR A 564     6792   5272  13357  -2091   5472  -5158  A    O  
ATOM   4493  CB  THR A 564       7.548  28.663  21.949  1.00 62.77      A    C  
ANISOU 4493  CB  THR A 564     6598   5208  12042  -1245   4394  -4387  A    C  
ATOM   4494  CG2 THR A 564       8.305  28.803  20.636  1.00 63.56      A    C  
ANISOU 4494  CG2 THR A 564     6648   5258  12243  -1323   4522  -4324  A    C  
ATOM   4495  OG1 THR A 564       7.966  27.454  22.575  1.00 60.85      A    O  
ANISOU 4495  OG1 THR A 564     6299   5420  11401  -1000   3990  -4492  A    O  
ATOM   4496  N   ARG A 565       6.358  31.607  21.956  1.00 60.97      A    N  
ANISOU 4496  N   ARG A 565     6484   4017  12665  -1764   5372  -4384  A    N  
ATOM   4497  CA  ARG A 565       6.037  32.868  21.285  1.00 62.72      A    C  
ANISOU 4497  CA  ARG A 565     6799   3737  13296  -1952   5878  -4243  A    C  
ATOM   4498  C   ARG A 565       6.606  34.110  22.058  1.00 71.35      A    C  
ANISOU 4498  C   ARG A 565     7726   4733  14650  -2327   6309  -4789  A    C  
ATOM   4499  O   ARG A 565       7.377  34.839  21.434  1.00 75.13      A    O  
ANISOU 4499  O   ARG A 565     8122   5079  15344  -2563   6654  -4962  A    O  
ATOM   4500  CB  ARG A 565       4.521  32.976  21.044  1.00 62.11      A    C  
ANISOU 4500  CB  ARG A 565     6993   3279  13327  -1758   5929  -3696  A    C  
ATOM   4501  CG  ARG A 565       4.076  34.245  20.344  1.00 76.75      A    C  
ANISOU 4501  CG  ARG A 565     8970   4611  15579  -1870   6460  -3467  A    C  
ATOM   4502  CD  ARG A 565       3.057  33.921  19.284  1.00 79.21      A    C  
ANISOU 4502  CD  ARG A 565     9492   4733  15870  -1593   6390  -2811  A    C  
ATOM   4503  NE  ARG A 565       2.845  35.045  18.381  1.00 86.15      A    N  
ANISOU 4503  NE  ARG A 565    10476   5168  17088  -1648   6896  -2552  A    N  
ATOM   4504  CZ  ARG A 565       1.912  35.966  18.550  1.00 93.20      A    C  
ANISOU 4504  CZ  ARG A 565    11506   5670  18237  -1624   7254  -2347  A    C  
ATOM   4505  NH1 ARG A 565       1.799  36.965  17.686  1.00 76.70      A    N1+
ANISOU 4505  NH1 ARG A 565     9522   3179  16441  -1638   7739  -2090  A    N1+
ATOM   4506  NH2 ARG A 565       1.098  35.909  19.597  1.00 81.32      A    N  
ANISOU 4506  NH2 ARG A 565    10038   4167  16694  -1571   7151  -2394  A    N  
ATOM   4507  N   PRO A 566       6.315  34.363  23.374  1.00 66.69      A    N  
ANISOU 4507  N   PRO A 566     7075   4222  14041  -2414   6319  -5098  A    N  
ATOM   4508  CA  PRO A 566       6.914  35.529  24.044  1.00 70.11      A    C  
ANISOU 4508  CA  PRO A 566     7341   4583  14716  -2810   6752  -5661  A    C  
ATOM   4509  C   PRO A 566       8.444  35.474  24.146  1.00 76.64      A    C  
ANISOU 4509  C   PRO A 566     7835   5869  15415  -3048   6725  -6231  A    C  
ATOM   4510  O   PRO A 566       9.074  36.523  24.022  1.00 80.50      A    O  
ANISOU 4510  O   PRO A 566     8217   6189  16180  -3415   7187  -6593  A    O  
ATOM   4511  CB  PRO A 566       6.292  35.485  25.441  1.00 71.40      A    C  
ANISOU 4511  CB  PRO A 566     7492   4861  14774  -2788   6637  -5848  A    C  
ATOM   4512  CG  PRO A 566       5.055  34.708  25.278  1.00 71.92      A    C  
ANISOU 4512  CG  PRO A 566     7809   4809  14707  -2411   6328  -5257  A    C  
ATOM   4513  CD  PRO A 566       5.433  33.643  24.308  1.00 65.09      A    C  
ANISOU 4513  CD  PRO A 566     6957   4169  13605  -2182   5973  -4970  A    C  
ATOM   4514  N   LEU A 567       9.042  34.276  24.372  1.00 69.97      A    N  
ANISOU 4514  N   LEU A 567     6829   5601  14156  -2841   6215  -6316  A    N  
ATOM   4515  CA  LEU A 567      10.501  34.141  24.488  1.00 72.21      A    C  
ANISOU 4515  CA  LEU A 567     6763   6406  14269  -3017   6150  -6843  A    C  
ATOM   4516  C   LEU A 567      11.193  34.579  23.189  1.00 77.70      A    C  
ANISOU 4516  C   LEU A 567     7444   6900  15179  -3179   6429  -6788  A    C  
ATOM   4517  O   LEU A 567      12.163  35.320  23.260  1.00 81.54      A    O  
ANISOU 4517  O   LEU A 567     7688   7503  15791  -3542   6733  -7295  A    O  
ATOM   4518  CB  LEU A 567      10.931  32.711  24.875  1.00 70.08      A    C  
ANISOU 4518  CB  LEU A 567     6363   6763  13502  -2678   5560  -6846  A    C  
ATOM   4519  CG  LEU A 567      10.742  32.284  26.332  1.00 74.64      A    C  
ANISOU 4519  CG  LEU A 567     6817   7756  13788  -2578   5296  -7117  A    C  
ATOM   4520  CD1 LEU A 567      10.894  30.792  26.470  1.00 72.41      A    C  
ANISOU 4520  CD1 LEU A 567     6535   7930  13048  -2145   4750  -6912  A    C  
ATOM   4521  CD2 LEU A 567      11.710  32.984  27.265  1.00 80.97      A    C  
ANISOU 4521  CD2 LEU A 567     7230   8976  14559  -2935   5478  -7859  A    C  
ATOM   4522  N   TYR A 568      10.645  34.182  22.018  1.00 71.15      A    N  
ANISOU 4522  N   TYR A 568     6873   5761  14400  -2932   6359  -6185  A    N  
ATOM   4523  CA  TYR A 568      11.128  34.562  20.698  1.00 72.43      A    C  
ANISOU 4523  CA  TYR A 568     7069   5689  14760  -3035   6621  -6033  A    C  
ATOM   4524  C   TYR A 568      10.967  36.071  20.433  1.00 81.85      A    C  
ANISOU 4524  C   TYR A 568     8357   6315  16427  -3376   7286  -6107  A    C  
ATOM   4525  O   TYR A 568      11.902  36.686  19.911  1.00 86.18      A    O  
ANISOU 4525  O   TYR A 568     8774   6825  17145  -3663   7617  -6379  A    O  
ATOM   4526  CB  TYR A 568      10.402  33.758  19.608  1.00 70.24      A    C  
ANISOU 4526  CB  TYR A 568     7055   5245  14388  -2667   6369  -5353  A    C  
ATOM   4527  CG  TYR A 568      11.187  32.557  19.124  1.00 69.64      A    C  
ANISOU 4527  CG  TYR A 568     6860   5638  13963  -2462   5938  -5337  A    C  
ATOM   4528  CD1 TYR A 568      12.351  32.715  18.374  1.00 73.09      A    C  
ANISOU 4528  CD1 TYR A 568     7118   6225  14428  -2621   6065  -5548  A    C  
ATOM   4529  CD2 TYR A 568      10.765  31.263  19.408  1.00 66.86      A    C  
ANISOU 4529  CD2 TYR A 568     6588   5558  13256  -2105   5433  -5106  A    C  
ATOM   4530  CE1 TYR A 568      13.084  31.615  17.937  1.00 72.00      A    C  
ANISOU 4530  CE1 TYR A 568     6871   6516  13969  -2415   5685  -5532  A    C  
ATOM   4531  CE2 TYR A 568      11.488  30.153  18.972  1.00 66.67      A    C  
ANISOU 4531  CE2 TYR A 568     6481   5932  12917  -1898   5074  -5085  A    C  
ATOM   4532  CZ  TYR A 568      12.648  30.335  18.237  1.00 74.52      A    C  
ANISOU 4532  CZ  TYR A 568     7287   7085  13943  -2045   5197  -5297  A    C  
ATOM   4533  OH  TYR A 568      13.361  29.252  17.791  1.00 71.30      A    O  
ANISOU 4533  OH  TYR A 568     6801   7061  13229  -1826   4863  -5271  A    O  
ATOM   4534  N   ARG A 569       9.800  36.660  20.794  1.00 77.69      A    N  
ANISOU 4534  N   ARG A 569     8062   5343  16111  -3340   7502  -5867  A    N  
ATOM   4535  CA  ARG A 569       9.490  38.085  20.623  1.00 80.80      A    C  
ANISOU 4535  CA  ARG A 569     8600   5138  16960  -3606   8164  -5881  A    C  
ATOM   4536  C   ARG A 569      10.473  38.946  21.400  1.00 90.13      A    C  
ANISOU 4536  C   ARG A 569     9526   6431  18289  -4090   8533  -6637  A    C  
ATOM   4537  O   ARG A 569      11.103  39.836  20.820  1.00 93.74      A    O  
ANISOU 4537  O   ARG A 569     9965   6619  19032  -4396   9032  -6816  A    O  
ATOM   4538  CB  ARG A 569       8.060  38.392  21.089  1.00 79.41      A    C  
ANISOU 4538  CB  ARG A 569     8681   4581  16909  -3432   8247  -5532  A    C  
ATOM   4539  CG  ARG A 569       7.161  38.985  20.006  1.00 84.75      A    C  
ANISOU 4539  CG  ARG A 569     9674   4667  17862  -3256   8582  -4892  A    C  
ATOM   4540  CD  ARG A 569       5.904  39.637  20.569  1.00 87.15      A    C  
ANISOU 4540  CD  ARG A 569    10192   4553  18368  -3173   8831  -4670  A    C  
ATOM   4541  NE  ARG A 569       5.034  38.707  21.300  1.00 92.15      A    N  
ANISOU 4541  NE  ARG A 569    10849   5455  18707  -2893   8315  -4498  A    N  
ATOM   4542  CZ  ARG A 569       4.873  38.701  22.620  1.00107.02      A    C  
ANISOU 4542  CZ  ARG A 569    12641   7508  20515  -2992   8217  -4873  A    C  
ATOM   4543  NH1 ARG A 569       4.057  37.824  23.191  1.00 88.09      A    N1+
ANISOU 4543  NH1 ARG A 569    10289   5333  17848  -2718   7762  -4667  A    N1+
ATOM   4544  NH2 ARG A 569       5.524  39.572  23.380  1.00104.18      A    N  
ANISOU 4544  NH2 ARG A 569    12141   7103  20339  -3380   8589  -5470  A    N  
ATOM   4545  N   ASP A 570      10.615  38.660  22.711  1.00 86.51      A    N  
ANISOU 4545  N   ASP A 570     8860   6393  17614  -4165   8292  -7090  A    N  
ATOM   4546  CA  ASP A 570      11.524  39.345  23.622  1.00 90.53      A    C  
ANISOU 4546  CA  ASP A 570     9072   7146  18179  -4624   8563  -7873  A    C  
ATOM   4547  C   ASP A 570      12.987  39.209  23.149  1.00 97.78      A    C  
ANISOU 4547  C   ASP A 570     9674   8488  18990  -4849   8553  -8282  A    C  
ATOM   4548  O   ASP A 570      13.729  40.193  23.176  1.00102.13      A    O  
ANISOU 4548  O   ASP A 570    10082   8936  19788  -5312   9055  -8780  A    O  
ATOM   4549  CB  ASP A 570      11.348  38.796  25.047  1.00 91.50      A    C  
ANISOU 4549  CB  ASP A 570     9022   7758  17985  -4550   8177  -8185  A    C  
ATOM   4550  CG  ASP A 570      10.102  39.288  25.765  1.00104.54      A    C  
ANISOU 4550  CG  ASP A 570    10919   8997  19805  -4489   8336  -8001  A    C  
ATOM   4551  OD1 ASP A 570       9.028  39.346  25.127  1.00103.80      A    O  
ANISOU 4551  OD1 ASP A 570    11165   8384  19888  -4233   8417  -7368  A    O  
ATOM   4552  OD2 ASP A 570      10.196  39.598  26.969  1.00114.41      A    O1-
ANISOU 4552  OD2 ASP A 570    12004  10479  20987  -4685   8370  -8491  A    O1-
ATOM   4553  N   LEU A 571      13.379  38.010  22.677  1.00 91.33      A    N  
ANISOU 4553  N   LEU A 571     8763   8120  17819  -4528   8018  -8067  A    N  
ATOM   4554  CA  LEU A 571      14.728  37.743  22.180  1.00 93.08      A    C  
ANISOU 4554  CA  LEU A 571     8683   8785  17897  -4669   7950  -8394  A    C  
ATOM   4555  C   LEU A 571      15.036  38.563  20.909  1.00102.07      A    C  
ANISOU 4555  C   LEU A 571     9953   9422  19405  -4887   8462  -8245  A    C  
ATOM   4556  O   LEU A 571      16.175  39.014  20.738  1.00104.84      A    O  
ANISOU 4556  O   LEU A 571    10042   9970  19823  -5253   8723  -8739  A    O  
ATOM   4557  CB  LEU A 571      14.930  36.240  21.909  1.00 88.63      A    C  
ANISOU 4557  CB  LEU A 571     8059   8730  16887  -4214   7283  -8104  A    C  
ATOM   4558  CG  LEU A 571      15.480  35.382  23.060  1.00 92.67      A    C  
ANISOU 4558  CG  LEU A 571     8244  10025  16942  -4091   6805  -8508  A    C  
ATOM   4559  CD1 LEU A 571      15.298  33.925  22.774  1.00 88.24      A    C  
ANISOU 4559  CD1 LEU A 571     7773   9754  16000  -3568   6213  -8057  A    C  
ATOM   4560  CD2 LEU A 571      16.949  35.632  23.300  1.00 99.26      A    C  
ANISOU 4560  CD2 LEU A 571     8619  11430  17664  -4427   6900  -9207  A    C  
ATOM   4561  N   TYR A 572      14.014  38.780  20.045  1.00 98.84      A    N  
ANISOU 4561  N   TYR A 572     9940   8389  19227  -4663   8624  -7574  A    N  
ATOM   4562  CA  TYR A 572      14.135  39.559  18.807  1.00100.91      A    C  
ANISOU 4562  CA  TYR A 572    10383   8125  19834  -4794   9127  -7321  A    C  
ATOM   4563  C   TYR A 572      14.310  41.052  19.125  1.00109.28      A    C  
ANISOU 4563  C   TYR A 572    11468   8727  21328  -5286   9877  -7729  A    C  
ATOM   4564  O   TYR A 572      15.135  41.716  18.499  1.00111.37      A    O  
ANISOU 4564  O   TYR A 572    11671   8836  21810  -5607  10320  -7952  A    O  
ATOM   4565  CB  TYR A 572      12.914  39.337  17.885  1.00 99.31      A    C  
ANISOU 4565  CB  TYR A 572    10573   7458  19702  -4372   9063  -6477  A    C  
ATOM   4566  CG  TYR A 572      13.032  40.023  16.541  1.00103.51      A    C  
ANISOU 4566  CG  TYR A 572    11292   7504  20533  -4432   9540  -6147  A    C  
ATOM   4567  CD1 TYR A 572      13.720  39.427  15.491  1.00104.45      A    C  
ANISOU 4567  CD1 TYR A 572    11336   7843  20506  -4337   9360  -5996  A    C  
ATOM   4568  CD2 TYR A 572      12.449  41.268  16.318  1.00107.71      A    C  
ANISOU 4568  CD2 TYR A 572    12087   7351  21487  -4563  10190  -5968  A    C  
ATOM   4569  CE1 TYR A 572      13.850  40.063  14.258  1.00108.51      A    C  
ANISOU 4569  CE1 TYR A 572    12020   7930  21279  -4386   9808  -5690  A    C  
ATOM   4570  CE2 TYR A 572      12.574  41.916  15.090  1.00111.11      A    C  
ANISOU 4570  CE2 TYR A 572    12700   7337  22181  -4592  10660  -5645  A    C  
ATOM   4571  CZ  TYR A 572      13.273  41.307  14.060  1.00120.70      A    C  
ANISOU 4571  CZ  TYR A 572    13825   8800  23233  -4506  10459  -5504  A    C  
ATOM   4572  OH  TYR A 572      13.404  41.939  12.845  1.00127.13      A    O  
ANISOU 4572  OH  TYR A 572    14820   9194  24289  -4524  10925  -5175  A    O  
ATOM   4573  N   ASN A 573      13.536  41.571  20.097  1.00106.66      A    N  
ANISOU 4573  N   ASN A 573    11238   8168  21123  -5353  10040  -7837  A    N  
ATOM   4574  CA  ASN A 573      13.599  42.974  20.515  1.00111.54      A    C  
ANISOU 4574  CA  ASN A 573    11910   8318  22153  -5815  10772  -8240  A    C  
ATOM   4575  C   ASN A 573      14.897  43.265  21.297  1.00118.46      A    C  
ANISOU 4575  C   ASN A 573    12359   9690  22961  -6340  10899  -9160  A    C  
ATOM   4576  O   ASN A 573      15.192  44.427  21.573  1.00122.40      A    O  
ANISOU 4576  O   ASN A 573    12856   9850  23799  -6817  11554  -9608  A    O  
ATOM   4577  CB  ASN A 573      12.358  43.347  21.343  1.00112.39      A    C  
ANISOU 4577  CB  ASN A 573    12245   8076  22381  -5698  10867  -8075  A    C  
ATOM   4578  CG  ASN A 573      11.038  43.095  20.639  1.00143.67      A    C  
ANISOU 4578  CG  ASN A 573    16593  11593  26401  -5198  10766  -7203  A    C  
ATOM   4579  ND2 ASN A 573       9.960  43.046  21.410  1.00137.65      A    N  
ANISOU 4579  ND2 ASN A 573    15969  10718  25614  -5003  10640  -7028  A    N  
ATOM   4580  OD1 ASN A 573      10.961  42.937  19.409  1.00137.70      A    O  
ANISOU 4580  OD1 ASN A 573    16000  10623  25696  -4983  10799  -6687  A    O  
ATOM   4581  N   PHE A 574      15.672  42.209  21.624  1.00113.44      A    N  
ANISOU 4581  N   PHE A 574    11361   9863  21879  -6244  10294  -9436  A    N  
ATOM   4582  CA  PHE A 574      16.954  42.278  22.322  1.00117.29      A    C  
ANISOU 4582  CA  PHE A 574    11371  10997  22195  -6664  10293 -10281  A    C  
ATOM   4583  C   PHE A 574      18.077  42.289  21.259  1.00122.75      A    C  
ANISOU 4583  C   PHE A 574    11902  11822  22915  -6837  10431 -10393  A    C  
ATOM   4584  O   PHE A 574      18.464  41.241  20.725  1.00119.50      A    O  
ANISOU 4584  O   PHE A 574    11378  11841  22187  -6511   9920 -10152  A    O  
ATOM   4585  CB  PHE A 574      17.078  41.107  23.324  1.00116.85      A    C  
ANISOU 4585  CB  PHE A 574    11023  11763  21611  -6387   9561 -10458  A    C  
ATOM   4586  CG  PHE A 574      18.251  41.090  24.282  1.00122.51      A    C  
ANISOU 4586  CG  PHE A 574    11209  13277  22061  -6742   9474 -11323  A    C  
ATOM   4587  CD1 PHE A 574      19.019  42.229  24.496  1.00128.08      A    C  
ANISOU 4587  CD1 PHE A 574    11902  14014  22749  -7080   9653 -11515  A    C  
ATOM   4588  CD2 PHE A 574      18.557  39.946  25.008  1.00123.15      A    C  
ANISOU 4588  CD2 PHE A 574    10993  14181  21616  -6433   8802 -11441  A    C  
ATOM   4589  CE1 PHE A 574      20.095  42.209  25.387  1.00129.62      A    C  
ANISOU 4589  CE1 PHE A 574    11784  15043  22423  -7109   9170 -11801  A    C  
ATOM   4590  CE2 PHE A 574      19.625  39.930  25.907  1.00130.02      A    C  
ANISOU 4590  CE2 PHE A 574    11342  15860  22199  -6724   8712 -12226  A    C  
ATOM   4591  CZ  PHE A 574      20.396  41.057  26.080  1.00129.46      A    C  
ANISOU 4591  CZ  PHE A 574    11325  15809  22055  -6982   8790 -12241  A    C  
ATOM   4592  N   GLU A 575      18.550  43.509  20.934  1.00122.19      A    N  
ANISOU 4592  N   GLU A 575    11912  11397  23116  -7235  10970 -10552  A    N  
ATOM   4593  CA  GLU A 575      19.555  43.865  19.925  1.00122.25      A    C  
ANISOU 4593  CA  GLU A 575    11904  11457  23089  -7345  11029 -10433  A    C  
ATOM   4594  C   GLU A 575      20.738  42.880  19.839  1.00124.44      A    C  
ANISOU 4594  C   GLU A 575    11746  12596  22938  -7283  10513 -10712  A    C  
ATOM   4595  O   GLU A 575      21.061  42.419  18.742  1.00123.97      A    O  
ANISOU 4595  O   GLU A 575    11655  12466  22983  -7240  10627 -10595  A    O  
ATOM   4596  CB  GLU A 575      20.103  45.284  20.179  1.00123.86      A    C  
ANISOU 4596  CB  GLU A 575    12294  11642  23127  -7486  10946 -10235  A    C  
ATOM   4597  CG  GLU A 575      19.047  46.369  20.338  1.00131.31      A    C  
ANISOU 4597  CG  GLU A 575    13819  12064  24009  -7147  10740  -9376  A    C  
ATOM   4598  CD  GLU A 575      18.595  46.627  21.764  1.00138.24      A    C  
ANISOU 4598  CD  GLU A 575    14843  13315  24367  -6804   9947  -9031  A    C  
ATOM   4599  OE1 GLU A 575      19.415  47.119  22.573  1.00136.61      A    O  
ANISOU 4599  OE1 GLU A 575    14471  13531  23905  -6978   9719  -9310  A    O  
ATOM   4600  OE2 GLU A 575      17.410  46.365  22.064  1.00128.64      A    O1-
ANISOU 4600  OE2 GLU A 575    13644  11504  23729  -7011  10709  -9458  A    O1-
ATOM   4601  N   LYS A 576      21.373  42.569  20.987  1.00121.48      A    N  
ANISOU 4601  N   LYS A 576    10942  12962  22255  -7436  10236 -11353  A    N  
ATOM   4602  CA  LYS A 576      22.533  41.674  21.084  1.00121.34      A    C  
ANISOU 4602  CA  LYS A 576    10434  13829  21841  -7417   9828 -11760  A    C  
ATOM   4603  C   LYS A 576      22.194  40.234  20.666  1.00121.20      A    C  
ANISOU 4603  C   LYS A 576    10335  14035  21681  -6995   9460 -11567  A    C  
ATOM   4604  O   LYS A 576      23.044  39.546  20.094  1.00118.88      A    O  
ANISOU 4604  O   LYS A 576     9806  14227  21136  -6867   9174 -11594  A    O  
ATOM   4605  CB  LYS A 576      23.097  41.681  22.516  1.00123.53      A    C  
ANISOU 4605  CB  LYS A 576    10458  14888  21592  -7372   9285 -12009  A    C  
ATOM   4606  CG  LYS A 576      23.646  43.035  22.971  1.00134.96      A    C  
ANISOU 4606  CG  LYS A 576    12399  16330  22548  -7061   8620 -11012  A    C  
ATOM   4607  CD  LYS A 576      23.440  43.226  24.467  1.00141.00      A    C  
ANISOU 4607  CD  LYS A 576    13311  17439  22824  -6728   7958 -10664  A    C  
ATOM   4608  CE  LYS A 576      23.599  44.648  24.935  1.00143.22      A    C  
ANISOU 4608  CE  LYS A 576    14011  17505  22901  -6597   7618  -9990  A    C  
ATOM   4609  NZ  LYS A 576      23.119  44.811  26.335  1.00145.80      A    N1+
ANISOU 4609  NZ  LYS A 576    14496  18014  22886  -6324   7136  -9732  A    N1+
ATOM   4610  N   ALA A 577      20.949  39.793  20.935  1.00113.88      A    N  
ANISOU 4610  N   ALA A 577     9755  12798  20716  -6563   9177 -10996  A    N  
ATOM   4611  CA  ALA A 577      20.482  38.441  20.635  1.00108.59      A    C  
ANISOU 4611  CA  ALA A 577     9218  12340  19700  -5928   8511 -10387  A    C  
ATOM   4612  C   ALA A 577      19.857  38.290  19.235  1.00109.01      A    C  
ANISOU 4612  C   ALA A 577     9694  11772  19952  -5643   8571  -9611  A    C  
ATOM   4613  O   ALA A 577      19.926  37.199  18.683  1.00105.15      A    O  
ANISOU 4613  O   ALA A 577     9225  11545  19183  -5236   8102  -9239  A    O  
ATOM   4614  CB  ALA A 577      19.469  38.013  21.684  1.00106.85      A    C  
ANISOU 4614  CB  ALA A 577     9120  12174  19304  -5636   8169 -10222  A    C  
ATOM   4615  N   ARG A 578      19.238  39.362  18.683  1.00107.61      A    N  
ANISOU 4615  N   ARG A 578     9850  10797  20238  -5839   9152  -9369  A    N  
ATOM   4616  CA  ARG A 578      18.492  39.427  17.411  1.00105.21      A    C  
ANISOU 4616  CA  ARG A 578     9965   9852  20156  -5586   9302  -8622  A    C  
ATOM   4617  C   ARG A 578      19.026  38.529  16.289  1.00107.54      A    C  
ANISOU 4617  C   ARG A 578    10223  10397  20238  -5319   8980  -8307  A    C  
ATOM   4618  O   ARG A 578      18.230  37.819  15.677  1.00102.29      A    O  
ANISOU 4618  O   ARG A 578     9828   9568  19469  -4880   8671  -7657  A    O  
ATOM   4619  CB  ARG A 578      18.403  40.871  16.890  1.00110.13      A    C  
ANISOU 4619  CB  ARG A 578    10796   9752  21298  -5979  10114  -8653  A    C  
ATOM   4620  CG  ARG A 578      17.331  41.069  15.807  1.00120.13      A    C  
ANISOU 4620  CG  ARG A 578    12529  10319  22797  -5669  10307  -7833  A    C  
ATOM   4621  CD  ARG A 578      17.105  42.530  15.451  1.00136.79      A    C  
ANISOU 4621  CD  ARG A 578    14883  11678  25412  -6000  11140  -7825  A    C  
ATOM   4622  NE  ARG A 578      16.339  43.229  16.484  1.00140.90      A    N  
ANISOU 4622  NE  ARG A 578    15641  12183  25712  -5843  10802  -7542  A    N  
ATOM   4623  CZ  ARG A 578      15.341  44.077  16.250  1.00151.69      A    C  
ANISOU 4623  CZ  ARG A 578    17516  13345  26776  -5376  10326  -6537  A    C  
ATOM   4624  NH1 ARG A 578      14.712  44.661  17.257  1.00146.50      A    N1+
ANISOU 4624  NH1 ARG A 578    16909  12340  26415  -5585  10748  -6860  A    N1+
ATOM   4625  NH2 ARG A 578      14.971  44.352  15.004  1.00141.99      A    N  
ANISOU 4625  NH2 ARG A 578    16459  11318  26174  -5483  11249  -6404  A    N  
ATOM   4626  N   GLU A 579      20.343  38.575  16.000  1.00108.57      A    N  
ANISOU 4626  N   GLU A 579    10021  10925  20306  -5593   9070  -8772  A    N  
ATOM   4627  CA  GLU A 579      20.955  37.793  14.926  1.00107.00      A    C  
ANISOU 4627  CA  GLU A 579     9762  10975  19918  -5378   8813  -8534  A    C  
ATOM   4628  C   GLU A 579      20.834  36.281  15.159  1.00106.32      A    C  
ANISOU 4628  C   GLU A 579     9608  11436  19352  -4869   8057  -8304  A    C  
ATOM   4629  O   GLU A 579      20.308  35.579  14.294  1.00102.38      A    O  
ANISOU 4629  O   GLU A 579     9358  10782  18762  -4489   7805  -7708  A    O  
ATOM   4630  CB  GLU A 579      22.426  38.177  14.733  1.00113.04      A    C  
ANISOU 4630  CB  GLU A 579    10137  12112  20702  -5807   9074  -9160  A    C  
ATOM   4631  CG  GLU A 579      22.628  39.246  13.676  1.00126.85      A    C  
ANISOU 4631  CG  GLU A 579    12061  13267  22869  -6124   9737  -9062  A    C  
ATOM   4632  CD  GLU A 579      24.035  39.332  13.120  1.00139.81      A    C  
ANISOU 4632  CD  GLU A 579    13379  15308  24433  -6399   9839  -9451  A    C  
ATOM   4633  OE1 GLU A 579      24.738  40.320  13.434  1.00139.66      A    O  
ANISOU 4633  OE1 GLU A 579    13371  15410  24283  -6593   9812  -9459  A    O  
ATOM   4634  OE2 GLU A 579      24.429  38.420  12.359  1.00118.34      A    O1-
ANISOU 4634  OE2 GLU A 579    10562  12906  21498  -6146   9522  -9286  A    O1-
ATOM   4635  N   GLN A 580      21.293  35.797  16.330  1.00102.97      A    N  
ANISOU 4635  N   GLN A 580     8860  11644  18619  -4860   7723  -8773  A    N  
ATOM   4636  CA  GLN A 580      21.290  34.387  16.730  1.00 99.07      A    C  
ANISOU 4636  CA  GLN A 580     8278  11709  17653  -4386   7050  -8630  A    C  
ATOM   4637  C   GLN A 580      19.871  33.803  16.823  1.00 96.33      A    C  
ANISOU 4637  C   GLN A 580     8336  11008  17258  -3965   6764  -7996  A    C  
ATOM   4638  O   GLN A 580      19.681  32.645  16.468  1.00 91.71      A    O  
ANISOU 4638  O   GLN A 580     7860  10589  16396  -3541   6324  -7607  A    O  
ATOM   4639  CB  GLN A 580      22.005  34.225  18.081  1.00103.03      A    C  
ANISOU 4639  CB  GLN A 580     8349  12933  17864  -4495   6851  -9286  A    C  
ATOM   4640  CG  GLN A 580      22.545  32.817  18.346  1.00108.88      A    C  
ANISOU 4640  CG  GLN A 580     8875  14407  18087  -4055   6240  -9278  A    C  
ATOM   4641  CD  GLN A 580      23.046  32.616  19.766  1.00121.66      A    C  
ANISOU 4641  CD  GLN A 580    10098  16751  19377  -4074   6013  -9838  A    C  
ATOM   4642  NE2 GLN A 580      23.179  31.353  20.157  1.00111.79      A    N  
ANISOU 4642  NE2 GLN A 580     8770  16032  17674  -3587   5474  -9699  A    N  
ATOM   4643  OE1 GLN A 580      23.332  33.568  20.518  1.00112.35      A    O  
ANISOU 4643  OE1 GLN A 580     8678  15681  18329  -4515   6327 -10402  A    O  
ATOM   4644  N   THR A 581      18.892  34.596  17.283  1.00 92.44      A    N  
ANISOU 4644  N   THR A 581     8061  10028  17033  -4091   7034  -7906  A    N  
ATOM   4645  CA  THR A 581      17.504  34.150  17.461  1.00 87.95      A    C  
ANISOU 4645  CA  THR A 581     7848   9133  16436  -3738   6805  -7354  A    C  
ATOM   4646  C   THR A 581      16.812  33.900  16.122  1.00 88.55      A    C  
ANISOU 4646  C   THR A 581     8274   8755  16616  -3488   6809  -6660  A    C  
ATOM   4647  O   THR A 581      16.084  32.917  16.002  1.00 84.11      A    O  
ANISOU 4647  O   THR A 581     7900   8229  15829  -3092   6399  -6220  A    O  
ATOM   4648  CB  THR A 581      16.715  35.144  18.318  1.00 96.76      A    C  
ANISOU 4648  CB  THR A 581     9077   9862  17827  -3964   7145  -7478  A    C  
ATOM   4649  CG2 THR A 581      17.370  35.397  19.658  1.00 95.45      A    C  
ANISOU 4649  CG2 THR A 581     8552  10177  17539  -4233   7148  -8190  A    C  
ATOM   4650  OG1 THR A 581      16.559  36.372  17.609  1.00101.66      A    O  
ANISOU 4650  OG1 THR A 581     9867   9862  18895  -4262   7757  -7391  A    O  
ATOM   4651  N   VAL A 582      17.035  34.781  15.128  1.00 88.32      A    N  
ANISOU 4651  N   VAL A 582     8327   8319  16913  -3723   7285  -6573  A    N  
ATOM   4652  CA  VAL A 582      16.491  34.667  13.766  1.00 86.35      A    C  
ANISOU 4652  CA  VAL A 582     8372   7676  16762  -3516   7348  -5944  A    C  
ATOM   4653  C   VAL A 582      17.058  33.400  13.135  1.00 86.84      A    C  
ANISOU 4653  C   VAL A 582     8349   8179  16469  -3230   6879  -5807  A    C  
ATOM   4654  O   VAL A 582      16.303  32.598  12.595  1.00 83.15      A    O  
ANISOU 4654  O   VAL A 582     8112   7632  15850  -2879   6581  -5288  A    O  
ATOM   4655  CB  VAL A 582      16.790  35.943  12.920  1.00 94.51      A    C  
ANISOU 4655  CB  VAL A 582     9473   8231  18204  -3850   8005  -5953  A    C  
ATOM   4656  CG1 VAL A 582      16.574  35.703  11.428  1.00 92.83      A    C  
ANISOU 4656  CG1 VAL A 582     9471   7789  18010  -3637   8029  -5383  A    C  
ATOM   4657  CG2 VAL A 582      15.948  37.124  13.391  1.00 96.30      A    C  
ANISOU 4657  CG2 VAL A 582     9901   7894  18795  -4028   8484  -5909  A    C  
ATOM   4658  N   ASN A 583      18.381  33.200  13.269  1.00 85.23      A    N  
ANISOU 4658  N   ASN A 583     7800   8468  16116  -3383   6816  -6300  A    N  
ATOM   4659  CA  ASN A 583      19.104  32.043  12.751  1.00 83.70      A    C  
ANISOU 4659  CA  ASN A 583     7483   8736  15583  -3129   6412  -6254  A    C  
ATOM   4660  C   ASN A 583      18.729  30.761  13.503  1.00 83.69      A    C  
ANISOU 4660  C   ASN A 583     7503   9103  15190  -2729   5837  -6146  A    C  
ATOM   4661  O   ASN A 583      18.753  29.695  12.896  1.00 80.95      A    O  
ANISOU 4661  O   ASN A 583     7250   8908  14600  -2407   5505  -5843  A    O  
ATOM   4662  CB  ASN A 583      20.626  32.271  12.787  1.00 89.89      A    C  
ANISOU 4662  CB  ASN A 583     7858   9980  16317  -3410   6532  -6848  A    C  
ATOM   4663  CG  ASN A 583      21.140  33.317  11.816  1.00109.29      A    C  
ANISOU 4663  CG  ASN A 583    10307  12105  19112  -3765   7071  -6908  A    C  
ATOM   4664  ND2 ASN A 583      20.845  33.177  10.531  1.00100.64      A    N  
ANISOU 4664  ND2 ASN A 583     9452  10707  18081  -3608   7121  -6404  A    N  
ATOM   4665  OD1 ASN A 583      21.818  34.264  12.209  1.00101.62      A    O  
ANISOU 4665  OD1 ASN A 583     9114  11157  18341  -4194   7465  -7418  A    O  
ATOM   4666  N   THR A 584      18.366  30.855  14.794  1.00 80.71      A    N  
ANISOU 4666  N   THR A 584     7062   8849  14755  -2747   5746  -6382  A    N  
ATOM   4667  CA  THR A 584      17.933  29.690  15.583  1.00 77.95      A    C  
ANISOU 4667  CA  THR A 584     6762   8808  14048  -2367   5247  -6266  A    C  
ATOM   4668  C   THR A 584      16.544  29.242  15.101  1.00 76.75      A    C  
ANISOU 4668  C   THR A 584     7028   8209  13923  -2090   5115  -5618  A    C  
ATOM   4669  O   THR A 584      16.303  28.046  14.972  1.00 73.27      A    O  
ANISOU 4669  O   THR A 584     6710   7939  13191  -1735   4724  -5348  A    O  
ATOM   4670  CB  THR A 584      17.955  30.001  17.098  1.00 86.22      A    C  
ANISOU 4670  CB  THR A 584     7610  10117  15031  -2489   5227  -6714  A    C  
ATOM   4671  CG2 THR A 584      17.517  28.816  17.957  1.00 77.77      A    C  
ANISOU 4671  CG2 THR A 584     6599   9368  13583  -2084   4740  -6589  A    C  
ATOM   4672  OG1 THR A 584      19.286  30.371  17.468  1.00 92.37      A    O  
ANISOU 4672  OG1 THR A 584     7963  11381  15753  -2760   5345  -7338  A    O  
ATOM   4673  N   PHE A 585      15.652  30.215  14.817  1.00 73.46      A    N  
ANISOU 4673  N   PHE A 585     6824   7234  13854  -2256   5469  -5379  A    N  
ATOM   4674  CA  PHE A 585      14.290  29.967  14.338  1.00 69.74      A    C  
ANISOU 4674  CA  PHE A 585     6712   6353  13432  -2032   5401  -4780  A    C  
ATOM   4675  C   PHE A 585      14.276  29.336  12.952  1.00 71.98      A    C  
ANISOU 4675  C   PHE A 585     7142   6579  13628  -1844   5291  -4363  A    C  
ATOM   4676  O   PHE A 585      13.457  28.449  12.719  1.00 68.55      A    O  
ANISOU 4676  O   PHE A 585     6919   6122  13006  -1555   4991  -3973  A    O  
ATOM   4677  CB  PHE A 585      13.458  31.258  14.310  1.00 72.18      A    C  
ANISOU 4677  CB  PHE A 585     7177   6113  14134  -2243   5857  -4639  A    C  
ATOM   4678  CG  PHE A 585      12.128  31.137  13.593  1.00 70.74      A    C  
ANISOU 4678  CG  PHE A 585     7326   5535  14015  -2022   5847  -4000  A    C  
ATOM   4679  CD1 PHE A 585      11.108  30.345  14.109  1.00 70.28      A    C  
ANISOU 4679  CD1 PHE A 585     7431   5511  13763  -1757   5505  -3737  A    C  
ATOM   4680  CD2 PHE A 585      11.899  31.814  12.400  1.00 73.57      A    C  
ANISOU 4680  CD2 PHE A 585     7822   5520  14612  -2076   6191  -3664  A    C  
ATOM   4681  CE1 PHE A 585       9.878  30.241  13.450  1.00 68.85      A    C  
ANISOU 4681  CE1 PHE A 585     7516   5026  13619  -1572   5497  -3178  A    C  
ATOM   4682  CE2 PHE A 585      10.667  31.707  11.742  1.00 74.10      A    C  
ANISOU 4682  CE2 PHE A 585     8154   5300  14699  -1856   6175  -3079  A    C  
ATOM   4683  CZ  PHE A 585       9.667  30.918  12.272  1.00 69.03      A    C  
ANISOU 4683  CZ  PHE A 585     7642   4729  13857  -1616   5822  -2854  A    C  
ATOM   4684  N   LEU A 586      15.131  29.823  12.020  1.00 70.87      A    N  
ANISOU 4684  N   LEU A 586     6895   6404  13627  -2024   5555  -4446  A    N  
ATOM   4685  CA  LEU A 586      15.164  29.298  10.654  1.00 69.21      A    C  
ANISOU 4685  CA  LEU A 586     6809   6151  13338  -1867   5483  -4070  A    C  
ATOM   4686  C   LEU A 586      15.619  27.841  10.668  1.00 72.06      A    C  
ANISOU 4686  C   LEU A 586     7122   6958  13299  -1579   5001  -4089  A    C  
ATOM   4687  O   LEU A 586      14.973  27.018  10.020  1.00 70.17      A    O  
ANISOU 4687  O   LEU A 586     7102   6654  12905  -1332   4779  -3675  A    O  
ATOM   4688  CB  LEU A 586      16.025  30.162   9.718  1.00 72.18      A    C  
ANISOU 4688  CB  LEU A 586     7068   6417  13940  -2131   5885  -4192  A    C  
ATOM   4689  CG  LEU A 586      15.586  31.639   9.553  1.00 79.28      A    C  
ANISOU 4689  CG  LEU A 586     8064   6802  15258  -2400   6445  -4121  A    C  
ATOM   4690  CD1 LEU A 586      16.659  32.457   8.882  1.00 82.97      A    C  
ANISOU 4690  CD1 LEU A 586     8376   7221  15927  -2698   6854  -4364  A    C  
ATOM   4691  CD2 LEU A 586      14.269  31.774   8.798  1.00 79.84      A    C  
ANISOU 4691  CD2 LEU A 586     8459   6455  15420  -2204   6521  -3483  A    C  
ATOM   4692  N   LYS A 587      16.618  27.496  11.516  1.00 70.67      A    N  
ANISOU 4692  N   LYS A 587     6671   7241  12941  -1593   4841  -4564  A    N  
ATOM   4693  CA  LYS A 587      17.149  26.136  11.663  1.00 69.78      A    C  
ANISOU 4693  CA  LYS A 587     6499   7575  12439  -1287   4419  -4614  A    C  
ATOM   4694  C   LYS A 587      16.140  25.186  12.316  1.00 71.83      A    C  
ANISOU 4694  C   LYS A 587     6990   7819  12482   -981   4081  -4353  A    C  
ATOM   4695  O   LYS A 587      16.345  23.982  12.246  1.00 70.77      A    O  
ANISOU 4695  O   LYS A 587     6916   7928  12043   -688   3766  -4259  A    O  
ATOM   4696  CB  LYS A 587      18.461  26.137  12.478  1.00 75.24      A    C  
ANISOU 4696  CB  LYS A 587     6801   8800  12985  -1367   4368  -5194  A    C  
ATOM   4697  CG  LYS A 587      19.681  26.637  11.721  1.00 94.79      A    C  
ANISOU 4697  CG  LYS A 587     9023  11438  15556  -1595   4600  -5465  A    C  
ATOM   4698  CD  LYS A 587      20.900  26.718  12.642  1.00111.36      A    C  
ANISOU 4698  CD  LYS A 587    10694  14117  17500  -1702   4561  -6076  A    C  
ATOM   4699  CE  LYS A 587      22.122  27.313  11.979  1.00123.16      A    C  
ANISOU 4699  CE  LYS A 587    11899  15798  19100  -1979   4822  -6404  A    C  
ATOM   4700  NZ  LYS A 587      22.879  26.304  11.192  1.00131.56      A    N1+
ANISOU 4700  NZ  LYS A 587    12917  17170  19900  -1706   4585  -6296  A    N1+
ATOM   4701  N   ASN A 588      15.063  25.708  12.954  1.00 68.46      A    N  
ANISOU 4701  N   ASN A 588     6703   7099  12211  -1048   4168  -4238  A    N  
ATOM   4702  CA  ASN A 588      14.044  24.895  13.636  1.00 65.37      A    C  
ANISOU 4702  CA  ASN A 588     6530   6671  11637   -795   3884  -4005  A    C  
ATOM   4703  C   ASN A 588      12.621  25.059  13.039  1.00 66.37      A    C  
ANISOU 4703  C   ASN A 588     6967   6334  11915   -772   3963  -3501  A    C  
ATOM   4704  O   ASN A 588      11.702  24.360  13.469  1.00 62.64      A    O  
ANISOU 4704  O   ASN A 588     6691   5812  11298   -583   3745  -3280  A    O  
ATOM   4705  CB  ASN A 588      14.021  25.237  15.126  1.00 66.20      A    C  
ANISOU 4705  CB  ASN A 588     6492   6936  11725   -856   3865  -4347  A    C  
ATOM   4706  CG  ASN A 588      15.202  24.701  15.888  1.00 94.76      A    C  
ANISOU 4706  CG  ASN A 588     9823  11120  15063   -756   3669  -4777  A    C  
ATOM   4707  ND2 ASN A 588      16.260  25.488  15.985  1.00 90.28      A    N  
ANISOU 4707  ND2 ASN A 588     8932  10770  14600  -1017   3878  -5213  A    N  
ATOM   4708  OD1 ASN A 588      15.186  23.572  16.382  1.00 92.39      A    O  
ANISOU 4708  OD1 ASN A 588     9585  11081  14440   -437   3345  -4722  A    O  
ATOM   4709  N   ARG A 589      12.460  25.952  12.042  1.00 65.02      A    N  
ANISOU 4709  N   ARG A 589     6835   5856  12014   -950   4278  -3316  A    N  
ATOM   4710  CA  ARG A 589      11.223  26.321  11.332  1.00 64.11      A    C  
ANISOU 4710  CA  ARG A 589     6960   5345  12055   -935   4415  -2840  A    C  
ATOM   4711  C   ARG A 589      10.433  25.118  10.773  1.00 67.02      A    C  
ANISOU 4711  C   ARG A 589     7556   5742  12166   -674   4104  -2447  A    C  
ATOM   4712  O   ARG A 589       9.192  25.115  10.840  1.00 65.59      A    O  
ANISOU 4712  O   ARG A 589     7555   5361  12003   -605   4075  -2140  A    O  
ATOM   4713  CB  ARG A 589      11.578  27.265  10.171  1.00 65.28      A    C  
ANISOU 4713  CB  ARG A 589     7075   5275  12452  -1110   4783  -2729  A    C  
ATOM   4714  CG  ARG A 589      10.466  28.210   9.780  1.00 69.13      A    C  
ANISOU 4714  CG  ARG A 589     7729   5339  13197  -1157   5082  -2355  A    C  
ATOM   4715  CD  ARG A 589      10.797  28.919   8.491  1.00 74.15      A    C  
ANISOU 4715  CD  ARG A 589     8362   5785  14024  -1265   5428  -2183  A    C  
ATOM   4716  NE  ARG A 589       9.744  29.858   8.116  1.00 85.27      A    N  
ANISOU 4716  NE  ARG A 589     9932   6802  15664  -1259   5741  -1789  A    N  
ATOM   4717  CZ  ARG A 589       9.956  31.000   7.473  1.00112.94      A    C  
ANISOU 4717  CZ  ARG A 589    13445  10022  19443  -1392   6196  -1682  A    C  
ATOM   4718  NH1 ARG A 589      11.187  31.353   7.119  1.00102.16      A    N1+
ANISOU 4718  NH1 ARG A 589    11934   8715  18168  -1581   6394  -1962  A    N1+
ATOM   4719  NH2 ARG A 589       8.941  31.802   7.179  1.00108.24      A    N  
ANISOU 4719  NH2 ARG A 589    13008   9089  19031  -1326   6477  -1288  A    N  
ATOM   4720  N   SER A 590      11.144  24.114  10.218  1.00 62.78      A    N  
ANISOU 4720  N   SER A 590     7007   5458  11389   -541   3891  -2472  A    N  
ATOM   4721  CA  SER A 590      10.552  22.914   9.616  1.00 60.26      A    C  
ANISOU 4721  CA  SER A 590     6901   5177  10817   -329   3630  -2158  A    C  
ATOM   4722  C   SER A 590      10.122  21.873  10.649  1.00 64.59      A    C  
ANISOU 4722  C   SER A 590     7565   5854  11122   -135   3328  -2203  A    C  
ATOM   4723  O   SER A 590       9.264  21.039  10.349  1.00 63.92      A    O  
ANISOU 4723  O   SER A 590     7697   5712  10876     -6   3165  -1924  A    O  
ATOM   4724  CB  SER A 590      11.546  22.266   8.649  1.00 63.04      A    C  
ANISOU 4724  CB  SER A 590     7204   5730  11016   -266   3558  -2197  A    C  
ATOM   4725  OG  SER A 590      11.974  23.172   7.648  1.00 67.80      A    O  
ANISOU 4725  OG  SER A 590     7717   6217  11827   -435   3842  -2133  A    O  
ATOM   4726  N   PHE A 591      10.726  21.901  11.849  1.00 63.06      A    N  
ANISOU 4726  N   PHE A 591     7222   5852  10885   -120   3267  -2558  A    N  
ATOM   4727  CA  PHE A 591      10.478  20.928  12.923  1.00 62.83      A    C  
ANISOU 4727  CA  PHE A 591     7287   5978  10606     92   3001  -2623  A    C  
ATOM   4728  C   PHE A 591       9.423  21.399  13.956  1.00 66.67      A    C  
ANISOU 4728  C   PHE A 591     7843   6292  11199     43   3032  -2583  A    C  
ATOM   4729  O   PHE A 591       9.159  20.683  14.929  1.00 66.34      A    O  
ANISOU 4729  O   PHE A 591     7878   6370  10961    209   2837  -2640  A    O  
ATOM   4730  CB  PHE A 591      11.804  20.597  13.635  1.00 66.94      A    C  
ANISOU 4730  CB  PHE A 591     7583   6898  10952    195   2892  -3027  A    C  
ATOM   4731  CG  PHE A 591      12.960  20.319  12.694  1.00 70.17      A    C  
ANISOU 4731  CG  PHE A 591     7871   7507  11283    226   2895  -3121  A    C  
ATOM   4732  CD1 PHE A 591      13.882  21.313  12.390  1.00 75.79      A    C  
ANISOU 4732  CD1 PHE A 591     8309   8305  12182      2   3114  -3381  A    C  
ATOM   4733  CD2 PHE A 591      13.113  19.070  12.102  1.00 72.20      A    C  
ANISOU 4733  CD2 PHE A 591     8296   7852  11285    466   2706  -2959  A    C  
ATOM   4734  CE1 PHE A 591      14.935  21.066  11.507  1.00 78.03      A    C  
ANISOU 4734  CE1 PHE A 591     8474   8781  12394     26   3123  -3467  A    C  
ATOM   4735  CE2 PHE A 591      14.174  18.818  11.224  1.00 76.47      A    C  
ANISOU 4735  CE2 PHE A 591     8725   8578  11754    502   2718  -3045  A    C  
ATOM   4736  CZ  PHE A 591      15.082  19.817  10.937  1.00 76.71      A    C  
ANISOU 4736  CZ  PHE A 591     8467   8715  11965    287   2916  -3296  A    C  
ATOM   4737  N   MET A 592       8.799  22.572  13.730  1.00 62.61      A    N  
ANISOU 4737  N   MET A 592     7324   5486  10979   -158   3285  -2455  A    N  
ATOM   4738  CA  MET A 592       7.783  23.085  14.646  1.00 62.08      A    C  
ANISOU 4738  CA  MET A 592     7322   5243  11025   -202   3338  -2409  A    C  
ATOM   4739  C   MET A 592       6.366  23.043  14.037  1.00 62.98      A    C  
ANISOU 4739  C   MET A 592     7661   5082  11186   -174   3356  -1957  A    C  
ATOM   4740  O   MET A 592       6.191  22.915  12.825  1.00 62.36      A    O  
ANISOU 4740  O   MET A 592     7657   4938  11101   -165   3384  -1691  A    O  
ATOM   4741  CB  MET A 592       8.125  24.503  15.145  1.00 66.89      A    C  
ANISOU 4741  CB  MET A 592     7733   5748  11934   -446   3647  -2676  A    C  
ATOM   4742  CG  MET A 592       8.520  25.475  14.052  1.00 72.61      A    C  
ANISOU 4742  CG  MET A 592     8379   6295  12915   -631   3961  -2621  A    C  
ATOM   4743  SD  MET A 592       9.055  27.096  14.647  1.00 80.66      A    S  
ANISOU 4743  SD  MET A 592     9182   7174  14291   -953   4385  -3000  A    S  
ATOM   4744  CE  MET A 592      10.473  26.652  15.648  1.00 79.36      A    C  
ANISOU 4744  CE  MET A 592     8732   7511  13910   -972   4202  -3586  A    C  
ATOM   4745  N   HIS A 593       5.363  23.167  14.908  1.00 58.26      A    N  
ANISOU 4745  N   HIS A 593     7151   4364  10621   -159   3339  -1884  A    N  
ATOM   4746  CA  HIS A 593       3.939  23.164  14.589  1.00 55.32      A    C  
ANISOU 4746  CA  HIS A 593     6953   3781  10286   -134   3358  -1491  A    C  
ATOM   4747  C   HIS A 593       3.593  24.332  13.641  1.00 61.29      A    C  
ANISOU 4747  C   HIS A 593     7667   4305  11314   -254   3668  -1261  A    C  
ATOM   4748  O   HIS A 593       4.149  25.414  13.829  1.00 64.42      A    O  
ANISOU 4748  O   HIS A 593     7927   4595  11956   -397   3933  -1451  A    O  
ATOM   4749  CB  HIS A 593       3.140  23.260  15.885  1.00 54.24      A    C  
ANISOU 4749  CB  HIS A 593     6871   3571  10165   -116   3326  -1523  A    C  
ATOM   4750  CG  HIS A 593       1.669  23.045  15.698  1.00 54.78      A    C  
ANISOU 4750  CG  HIS A 593     7118   3518  10178    -54   3265  -1149  A    C  
ATOM   4751  CD2 HIS A 593       0.968  21.895  15.768  1.00 52.82      A    C  
ANISOU 4751  CD2 HIS A 593     7041   3355   9671     62   3026  -1003  A    C  
ATOM   4752  ND1 HIS A 593       0.833  24.041  15.275  1.00 56.18      A    N  
ANISOU 4752  ND1 HIS A 593     7295   3480  10571   -117   3490   -882  A    N  
ATOM   4753  CE1 HIS A 593      -0.357  23.465  15.137  1.00 53.05      A    C  
ANISOU 4753  CE1 HIS A 593     7037   3094  10025    -40   3354   -598  A    C  
ATOM   4754  NE2 HIS A 593      -0.311  22.189  15.417  1.00 51.76      A    N  
ANISOU 4754  NE2 HIS A 593     6986   3095   9586     45   3085   -673  A    N  
ATOM   4755  N   PRO A 594       2.711  24.151  12.618  1.00 56.00      A    N  
ANISOU 4755  N   PRO A 594     7109   3571  10597   -198   3664   -862  A    N  
ATOM   4756  CA  PRO A 594       2.431  25.258  11.675  1.00 57.06      A    C  
ANISOU 4756  CA  PRO A 594     7204   3515  10961   -260   3972   -605  A    C  
ATOM   4757  C   PRO A 594       1.854  26.541  12.299  1.00 63.37      A    C  
ANISOU 4757  C   PRO A 594     7978   4047  12054   -326   4274   -562  A    C  
ATOM   4758  O   PRO A 594       2.117  27.623  11.762  1.00 65.37      A    O  
ANISOU 4758  O   PRO A 594     8176   4109  12552   -400   4611   -487  A    O  
ATOM   4759  CB  PRO A 594       1.408  24.656  10.701  1.00 57.19      A    C  
ANISOU 4759  CB  PRO A 594     7333   3603  10793   -155   3847   -197  A    C  
ATOM   4760  CG  PRO A 594       1.530  23.226  10.833  1.00 59.14      A    C  
ANISOU 4760  CG  PRO A 594     7673   4061  10735    -85   3510   -297  A    C  
ATOM   4761  CD  PRO A 594       1.990  22.923  12.224  1.00 54.44      A    C  
ANISOU 4761  CD  PRO A 594     7070   3498  10116    -80   3396   -644  A    C  
ATOM   4762  N   VAL A 595       1.056  26.432  13.384  1.00 59.85      A    N  
ANISOU 4762  N   VAL A 595     7588   3567  11586   -294   4183   -598  A    N  
ATOM   4763  CA  VAL A 595       0.451  27.605  14.037  1.00 61.23      A    C  
ANISOU 4763  CA  VAL A 595     7752   3482  12029   -345   4468   -568  A    C  
ATOM   4764  C   VAL A 595       1.537  28.385  14.791  1.00 65.64      A    C  
ANISOU 4764  C   VAL A 595     8183   3961  12798   -523   4680  -1013  A    C  
ATOM   4765  O   VAL A 595       1.611  29.619  14.667  1.00 67.31      A    O  
ANISOU 4765  O   VAL A 595     8357   3909  13308   -629   5071  -1008  A    O  
ATOM   4766  CB  VAL A 595      -0.747  27.280  14.965  1.00 63.90      A    C  
ANISOU 4766  CB  VAL A 595     8183   3820  12275   -262   4314   -469  A    C  
ATOM   4767  CG1 VAL A 595      -1.446  28.568  15.409  1.00 65.43      A    C  
ANISOU 4767  CG1 VAL A 595     8371   3728  12762   -298   4650   -402  A    C  
ATOM   4768  CG2 VAL A 595      -1.744  26.369  14.271  1.00 62.05      A    C  
ANISOU 4768  CG2 VAL A 595     8050   3716  11809   -128   4105    -87  A    C  
ATOM   4769  N   THR A 596       2.349  27.662  15.595  1.00 58.87      A    N  
ANISOU 4769  N   THR A 596     7252   3347  11769   -550   4439  -1398  A    N  
ATOM   4770  CA  THR A 596       3.454  28.226  16.358  1.00 59.18      A    C  
ANISOU 4770  CA  THR A 596     7122   3435  11929   -725   4578  -1880  A    C  
ATOM   4771  C   THR A 596       4.416  28.910  15.375  1.00 64.18      A    C  
ANISOU 4771  C   THR A 596     7652   3993  12739   -865   4851  -1948  A    C  
ATOM   4772  O   THR A 596       4.731  30.078  15.584  1.00 65.46      A    O  
ANISOU 4772  O   THR A 596     7734   3951  13186  -1059   5220  -2142  A    O  
ATOM   4773  CB  THR A 596       4.105  27.139  17.214  1.00 58.25      A    C  
ANISOU 4773  CB  THR A 596     6940   3679  11515   -653   4221  -2201  A    C  
ATOM   4774  CG2 THR A 596       5.140  27.685  18.175  1.00 54.61      A    C  
ANISOU 4774  CG2 THR A 596     6264   3357  11127   -826   4334  -2727  A    C  
ATOM   4775  OG1 THR A 596       3.078  26.468  17.941  1.00 55.46      A    O  
ANISOU 4775  OG1 THR A 596     6724   3354  10993   -506   3993  -2059  A    O  
ATOM   4776  N   GLU A 597       4.773  28.225  14.260  1.00 60.87      A    N  
ANISOU 4776  N   GLU A 597     7254   3710  12163   -776   4704  -1771  A    N  
ATOM   4777  CA  GLU A 597       5.669  28.717  13.209  1.00 63.03      A    C  
ANISOU 4777  CA  GLU A 597     7442   3946  12560   -884   4926  -1798  A    C  
ATOM   4778  C   GLU A 597       5.158  30.025  12.581  1.00 71.48      A    C  
ANISOU 4778  C   GLU A 597     8568   4631  13960   -964   5385  -1539  A    C  
ATOM   4779  O   GLU A 597       5.917  31.000  12.535  1.00 72.69      A    O  
ANISOU 4779  O   GLU A 597     8623   4637  14360  -1169   5738  -1777  A    O  
ATOM   4780  CB  GLU A 597       5.872  27.634  12.109  1.00 62.71      A    C  
ANISOU 4780  CB  GLU A 597     7454   4114  12260   -734   4661  -1577  A    C  
ATOM   4781  CG  GLU A 597       6.973  27.927  11.089  1.00 68.15      A    C  
ANISOU 4781  CG  GLU A 597     8037   4837  13019   -834   4830  -1654  A    C  
ATOM   4782  CD  GLU A 597       6.682  28.998  10.049  1.00 86.72      A    C  
ANISOU 4782  CD  GLU A 597    10434   6887  15628   -894   5230  -1348  A    C  
ATOM   4783  OE1 GLU A 597       5.576  28.984   9.461  1.00 67.47      A    O  
ANISOU 4783  OE1 GLU A 597     8136   4330  13170   -752   5241   -900  A    O  
ATOM   4784  OE2 GLU A 597       7.545  29.884   9.858  1.00 92.53      A    O1-
ANISOU 4784  OE2 GLU A 597    11060   7514  16582  -1082   5554  -1559  A    O1-
ATOM   4785  N   MET A 598       3.899  30.039  12.071  1.00 70.32      A    N  
ANISOU 4785  N   MET A 598     8575   4338  13808   -799   5401  -1053  A    N  
ATOM   4786  CA  MET A 598       3.340  31.228  11.415  1.00 73.79      A    C  
ANISOU 4786  CA  MET A 598     9082   4430  14524   -798   5839   -730  A    C  
ATOM   4787  C   MET A 598       3.355  32.434  12.357  1.00 76.17      A    C  
ANISOU 4787  C   MET A 598     9365   4427  15151   -969   6226   -976  A    C  
ATOM   4788  O   MET A 598       3.726  33.530  11.934  1.00 79.29      A    O  
ANISOU 4788  O   MET A 598     9758   4539  15829  -1095   6681   -987  A    O  
ATOM   4789  CB  MET A 598       1.908  30.982  10.892  1.00 76.54      A    C  
ANISOU 4789  CB  MET A 598     9561   4761  14760   -561   5747   -190  A    C  
ATOM   4790  CG  MET A 598       1.417  32.115   9.962  1.00 85.15      A    C  
ANISOU 4790  CG  MET A 598    10715   5560  16079   -485   6192    221  A    C  
ATOM   4791  SD  MET A 598      -0.368  32.499   9.961  1.00 91.95      A    S  
ANISOU 4791  SD  MET A 598    11686   6308  16943   -234   6267    754  A    S  
ATOM   4792  CE  MET A 598      -0.575  33.260  11.594  1.00 89.85      A    C  
ANISOU 4792  CE  MET A 598    11438   5765  16935   -364   6460    420  A    C  
ATOM   4793  N   LEU A 599       2.964  32.219  13.628  1.00 67.89      A    N  
ANISOU 4793  N   LEU A 599     8310   3430  14055   -982   6063  -1187  A    N  
ATOM   4794  CA  LEU A 599       2.911  33.256  14.643  1.00 68.18      A    C  
ANISOU 4794  CA  LEU A 599     8329   3211  14364  -1150   6392  -1457  A    C  
ATOM   4795  C   LEU A 599       4.334  33.721  15.057  1.00 73.48      A    C  
ANISOU 4795  C   LEU A 599     8826   3929  15164  -1450   6576  -2033  A    C  
ATOM   4796  O   LEU A 599       4.543  34.925  15.179  1.00 75.28      A    O  
ANISOU 4796  O   LEU A 599     9053   3835  15715  -1647   7058  -2187  A    O  
ATOM   4797  CB  LEU A 599       2.081  32.789  15.852  1.00 66.09      A    C  
ANISOU 4797  CB  LEU A 599     8100   3042  13969  -1066   6129  -1512  A    C  
ATOM   4798  CG  LEU A 599       0.553  32.645  15.635  1.00 67.85      A    C  
ANISOU 4798  CG  LEU A 599     8478   3156  14146   -824   6072   -989  A    C  
ATOM   4799  CD1 LEU A 599      -0.107  32.155  16.864  1.00 65.79      A    C  
ANISOU 4799  CD1 LEU A 599     8239   3011  13746   -773   5811  -1099  A    C  
ATOM   4800  CD2 LEU A 599      -0.105  33.971  15.277  1.00 73.44      A    C  
ANISOU 4800  CD2 LEU A 599     9276   3439  15188   -805   6591   -713  A    C  
ATOM   4801  N   VAL A 600       5.322  32.796  15.179  1.00 68.10      A    N  
ANISOU 4801  N   VAL A 600     7997   3646  14233  -1484   6233  -2339  A    N  
ATOM   4802  CA  VAL A 600       6.696  33.169  15.541  1.00 69.24      A    C  
ANISOU 4802  CA  VAL A 600     7928   3927  14452  -1762   6377  -2899  A    C  
ATOM   4803  C   VAL A 600       7.393  33.884  14.335  1.00 77.55      A    C  
ANISOU 4803  C   VAL A 600     8967   4781  15716  -1898   6758  -2830  A    C  
ATOM   4804  O   VAL A 600       8.182  34.796  14.563  1.00 79.08      A    O  
ANISOU 4804  O   VAL A 600     9046   4857  16145  -2193   7137  -3215  A    O  
ATOM   4805  CB  VAL A 600       7.512  31.966  16.107  1.00 69.39      A    C  
ANISOU 4805  CB  VAL A 600     7779   4475  14113  -1709   5894  -3236  A    C  
ATOM   4806  CG1 VAL A 600       8.989  32.305  16.274  1.00 71.46      A    C  
ANISOU 4806  CG1 VAL A 600     7778   4959  14413  -1975   6030  -3785  A    C  
ATOM   4807  CG2 VAL A 600       6.943  31.521  17.448  1.00 67.37      A    C  
ANISOU 4807  CG2 VAL A 600     7527   4371  13698  -1623   5633  -3373  A    C  
ATOM   4808  N   ALA A 601       7.053  33.524  13.078  1.00 76.60      A    N  
ANISOU 4808  N   ALA A 601     8968   4613  15521  -1697   6695  -2344  A    N  
ATOM   4809  CA  ALA A 601       7.649  34.135  11.878  1.00 80.42      A    C  
ANISOU 4809  CA  ALA A 601     9458   4922  16175  -1785   7041  -2218  A    C  
ATOM   4810  C   ALA A 601       7.140  35.540  11.632  1.00 91.03      A    C  
ANISOU 4810  C   ALA A 601    10939   5745  17904  -1868   7643  -2022  A    C  
ATOM   4811  O   ALA A 601       7.882  36.360  11.096  1.00 94.52      A    O  
ANISOU 4811  O   ALA A 601    11355   5985  18574  -2066   8067  -2138  A    O  
ATOM   4812  CB  ALA A 601       7.381  33.282  10.651  1.00 79.26      A    C  
ANISOU 4812  CB  ALA A 601     9395   4923  15796  -1528   6773  -1756  A    C  
ATOM   4813  N   LYS A 602       5.878  35.820  11.993  1.00 89.21      A    N  
ANISOU 4813  N   LYS A 602    10865   5288  17745  -1707   7705  -1713  A    N  
ATOM   4814  CA  LYS A 602       5.284  37.148  11.829  1.00 92.67      A    C  
ANISOU 4814  CA  LYS A 602    11459   5210  18541  -1728   8295  -1483  A    C  
ATOM   4815  C   LYS A 602       5.912  38.117  12.835  1.00100.65      A    C  
ANISOU 4815  C   LYS A 602    12397   6001  19845  -2089   8699  -2047  A    C  
ATOM   4816  O   LYS A 602       6.273  39.228  12.452  1.00104.88      A    O  
ANISOU 4816  O   LYS A 602    12996   6151  20702  -2266   9279  -2086  A    O  
ATOM   4817  CB  LYS A 602       3.754  37.093  11.968  1.00 94.09      A    C  
ANISOU 4817  CB  LYS A 602    11800   5275  18677  -1427   8211   -999  A    C  
ATOM   4818  CG  LYS A 602       3.047  36.616  10.696  1.00106.97      A    C  
ANISOU 4818  CG  LYS A 602    13518   7021  20105  -1100   8028   -380  A    C  
ATOM   4819  CD  LYS A 602       1.520  36.538  10.851  1.00115.93      A    C  
ANISOU 4819  CD  LYS A 602    14768   8116  21163   -810   7927     75  A    C  
ATOM   4820  CE  LYS A 602       0.798  37.856  10.637  1.00132.56      A    C  
ANISOU 4820  CE  LYS A 602    17027   9764  23574   -687   8504    446  A    C  
ATOM   4821  NZ  LYS A 602       0.804  38.285   9.211  1.00144.40      A    N1+
ANISOU 4821  NZ  LYS A 602    18592  11183  25091   -514   8757    912  A    N1+
ATOM   4822  N   ASP A 603       6.072  37.678  14.104  1.00 95.93      A    N  
ANISOU 4822  N   ASP A 603    11664   5664  19120  -2206   8405  -2495  A    N  
ATOM   4823  CA  ASP A 603       6.717  38.399  15.211  1.00 98.39      A    C  
ANISOU 4823  CA  ASP A 603    11846   5915  19622  -2570   8680  -3126  A    C  
ATOM   4824  C   ASP A 603       8.160  38.845  14.872  1.00107.16      A    C  
ANISOU 4824  C   ASP A 603    12783   7082  20852  -2917   8955  -3581  A    C  
ATOM   4825  O   ASP A 603       8.559  39.968  15.197  1.00110.95      A    O  
ANISOU 4825  O   ASP A 603    13249   7258  21649  -3246   9495  -3931  A    O  
ATOM   4826  CB  ASP A 603       6.760  37.493  16.450  1.00 96.88      A    C  
ANISOU 4826  CB  ASP A 603    11499   6174  19139  -2559   8164  -3477  A    C  
ATOM   4827  CG  ASP A 603       5.436  37.273  17.131  1.00100.30      A    C  
ANISOU 4827  CG  ASP A 603    12077   6529  19504  -2321   7979  -3188  A    C  
ATOM   4828  OD1 ASP A 603       4.520  38.097  16.927  1.00102.23      A    O  
ANISOU 4828  OD1 ASP A 603    12517   6331  19995  -2234   8348  -2835  A    O  
ATOM   4829  OD2 ASP A 603       5.323  36.294  17.897  1.00103.28      A    O1-
ANISOU 4829  OD2 ASP A 603    12373   7290  19581  -2214   7487  -3314  A    O1-
ATOM   4830  N   LEU A 604       8.927  37.951  14.221  1.00103.05      A    N  
ANISOU 4830  N   LEU A 604    12131   6949  20076  -2851   8598  -3586  A    N  
ATOM   4831  CA  LEU A 604      10.324  38.157  13.833  1.00105.77      A    C  
ANISOU 4831  CA  LEU A 604    12277   7446  20464  -3141   8765  -3996  A    C  
ATOM   4832  C   LEU A 604      10.465  38.953  12.507  1.00114.91      A    C  
ANISOU 4832  C   LEU A 604    13587   8195  21880  -3171   9262  -3662  A    C  
ATOM   4833  O   LEU A 604      11.591  39.172  12.050  1.00116.96      A    O  
ANISOU 4833  O   LEU A 604    13703   8548  22189  -3404   9434  -3945  A    O  
ATOM   4834  CB  LEU A 604      11.010  36.774  13.703  1.00102.63      A    C  
ANISOU 4834  CB  LEU A 604    11684   7657  19652  -3000   8143  -4109  A    C  
ATOM   4835  CG  LEU A 604      11.779  36.216  14.917  1.00106.88      A    C  
ANISOU 4835  CG  LEU A 604    11932   8711  19966  -3145   7822  -4730  A    C  
ATOM   4836  CD1 LEU A 604      10.884  35.952  16.116  1.00105.00      A    C  
ANISOU 4836  CD1 LEU A 604    11744   8538  19611  -3009   7564  -4737  A    C  
ATOM   4837  CD2 LEU A 604      12.457  34.926  14.561  1.00106.46      A    C  
ANISOU 4837  CD2 LEU A 604    11721   9189  19541  -2972   7315  -4768  A    C  
ATOM   4838  N   HIS A 605       9.331  39.361  11.880  1.00112.50      A    N  
ANISOU 4838  N   HIS A 605    13561   7469  21716  -2914   9487  -3047  A    N  
ATOM   4839  CA  HIS A 605       9.260  40.099  10.599  1.00115.13      A    C  
ANISOU 4839  CA  HIS A 605    14079   7401  22264  -2845   9960  -2604  A    C  
ATOM   4840  C   HIS A 605       9.855  39.260   9.423  1.00118.63      A    C  
ANISOU 4840  C   HIS A 605    14447   8168  22460  -2716   9660  -2408  A    C  
ATOM   4841  O   HIS A 605      10.347  39.823   8.438  1.00120.67      A    O  
ANISOU 4841  O   HIS A 605    14746   8223  22879  -2811  10054  -2314  A    O  
ATOM   4842  CB  HIS A 605       9.932  41.499  10.682  1.00121.10      A    C  
ANISOU 4842  CB  HIS A 605    14872   7694  23448  -3235  10728  -2939  A    C  
ATOM   4843  CG  HIS A 605       9.462  42.357  11.822  1.00126.71      A    C  
ANISOU 4843  CG  HIS A 605    15649   8083  24411  -3411  11066  -3205  A    C  
ATOM   4844  CD2 HIS A 605       8.205  42.708  12.187  1.00128.17      A    C  
ANISOU 4844  CD2 HIS A 605    16043   7961  24694  -3179  11174  -2844  A    C  
ATOM   4845  ND1 HIS A 605      10.359  42.934  12.704  1.00131.58      A    N  
ANISOU 4845  ND1 HIS A 605    16092   8712  25192  -3881  11335  -3934  A    N  
ATOM   4846  CE1 HIS A 605       9.625  43.613  13.572  1.00132.36      A    C  
ANISOU 4846  CE1 HIS A 605    16313   8489  25488  -3927  11603  -4000  A    C  
ATOM   4847  NE2 HIS A 605       8.323  43.506  13.302  1.00130.63      A    N  
ANISOU 4847  NE2 HIS A 605    16330   8059  25243  -3504  11519  -3348  A    N  
ATOM   4848  N   ILE A 606       9.771  37.917   9.529  1.00111.67      A    N  
ANISOU 4848  N   ILE A 606    13473   7767  21191  -2493   8987  -2336  A    N  
ATOM   4849  CA  ILE A 606      10.262  36.972   8.527  1.00110.01      A    C  
ANISOU 4849  CA  ILE A 606    13194   7899  20705  -2350   8639  -2171  A    C  
ATOM   4850  C   ILE A 606       9.117  36.685   7.519  1.00113.37      A    C  
ANISOU 4850  C   ILE A 606    13827   8237  21013  -1966   8539  -1442  A    C  
ATOM   4851  O   ILE A 606       9.129  37.280   6.439  1.00115.76      A    O  
ANISOU 4851  O   ILE A 606    14230   8314  21440  -1917   8892  -1113  A    O  
ATOM   4852  CB  ILE A 606      10.870  35.702   9.214  1.00110.35      A    C  
ANISOU 4852  CB  ILE A 606    13021   8507  20399  -2346   8022  -2561  A    C  
ATOM   4853  CG1 ILE A 606      12.288  36.024   9.749  1.00113.77      A    C  
ANISOU 4853  CG1 ILE A 606    13192   9117  20917  -2725   8173  -3256  A    C  
ATOM   4854  CG2 ILE A 606      10.902  34.469   8.292  1.00107.58      A    C  
ANISOU 4854  CG2 ILE A 606    12669   8501  19706  -2087   7562  -2269  A    C  
ATOM   4855  CD1 ILE A 606      12.877  35.030  10.751  1.00121.38      A    C  
ANISOU 4855  CD1 ILE A 606    13922  10626  21572  -2729   7658  -3707  A    C  
ATOM   4856  N   SER A 607       8.115  35.843   7.895  1.00106.30      A    N  
ANISOU 4856  N   SER A 607    12989   7523  19879  -1706   8095  -1201  A    N  
ATOM   4857  CA  SER A 607       6.953  35.429   7.090  1.00119.05      A    C  
ANISOU 4857  CA  SER A 607    14752   9161  21320  -1356   7924   -569  A    C  
ATOM   4858  C   SER A 607       7.387  34.815   5.741  1.00143.22      A    C  
ANISOU 4858  C   SER A 607    17789  12459  24169  -1246   7763   -334  A    C  
ATOM   4859  O   SER A 607       8.333  34.026   5.679  1.00 95.57      A    O  
ANISOU 4859  O   SER A 607    11617   6746  17950  -1336   7460   -645  A    O  
ATOM   4860  CB  SER A 607       5.994  36.599   6.866  1.00123.74      A    C  
ANISOU 4860  CB  SER A 607    15528   9301  22186  -1238   8428   -148  A    C  
ATOM   4861  OG  SER A 607       4.857  36.221   6.107  1.00127.87      A    O  
ANISOU 4861  OG  SER A 607    16153   9923  22510   -890   8247    447  A    O  
ATOM   4862  N   ALA A   2     -36.485  -4.645  20.166  1.00116.42      B    N  
ANISOU 4862  N   ALA A   2     8971  19100  16164  -7475   6772 -10380  B    N  
ATOM   4863  CA  ALA A   2     -36.469  -4.664  21.626  1.00109.81      B    C  
ANISOU 4863  CA  ALA A   2     8774  16808  16140  -6827   6727  -9599  B    C  
ATOM   4864  C   ALA A   2     -37.888  -4.668  22.163  1.00114.42      B    C  
ANISOU 4864  C   ALA A   2     9315  17529  16630  -6731   6622  -9424  B    C  
ATOM   4865  O   ALA A   2     -38.238  -5.533  22.969  1.00114.99      B    O  
ANISOU 4865  O   ALA A   2     9468  16624  17600  -6674   7030  -9628  B    O  
ATOM   4866  CB  ALA A   2     -35.700  -3.462  22.161  1.00103.24      B    C  
ANISOU 4866  CB  ALA A   2     8564  15626  15036  -6152   6146  -8394  B    C  
ATOM   4867  N   ASP A   3     -38.710  -3.710  21.697  1.00110.66      B    N  
ANISOU 4867  N   ASP A   3     8670  18278  15097  -6703   6103  -8999  B    N  
ATOM   4868  CA  ASP A   3     -40.106  -3.562  22.078  1.00109.95      B    C  
ANISOU 4868  CA  ASP A   3     8493  18508  14776  -6619   5941  -8775  B    C  
ATOM   4869  C   ASP A   3     -40.936  -4.666  21.428  1.00120.01      B    C  
ANISOU 4869  C   ASP A   3     9065  20408  16125  -7356   6459 -10037  B    C  
ATOM   4870  O   ASP A   3     -40.998  -4.742  20.200  1.00126.04      B    O  
ANISOU 4870  O   ASP A   3     9194  22512  16182  -7948   6525 -10750  B    O  
ATOM   4871  CB  ASP A   3     -40.627  -2.161  21.684  1.00110.81      B    C  
ANISOU 4871  CB  ASP A   3     8556  19760  13787  -6352   5274  -7859  B    C  
ATOM   4872  CG  ASP A   3     -42.069  -1.831  22.049  1.00126.65      B    C  
ANISOU 4872  CG  ASP A   3    10457  22175  15489  -6216   5055  -7487  B    C  
ATOM   4873  OD1 ASP A   3     -42.561  -2.345  23.085  1.00126.40      B    O  
ANISOU 4873  OD1 ASP A   3    10730  21123  16172  -6010   5237  -7471  B    O  
ATOM   4874  OD2 ASP A   3     -42.686  -1.005  21.338  1.00135.42      B    O1-
ANISOU 4874  OD2 ASP A   3    11176  24621  15657  -6269   4694  -7100  B    O1-
ATOM   4875  N   PRO A   4     -41.571  -5.540  22.239  1.00115.68      B    N  
ANISOU 4875  N   PRO A   4     8573  18944  16435  -7352   6866 -10357  B    N  
ATOM   4876  CA  PRO A   4     -42.434  -6.593  21.670  1.00122.97      B    C  
ANISOU 4876  CA  PRO A   4     8797  20407  17520  -8074   7421 -11623  B    C  
ATOM   4877  C   PRO A   4     -43.668  -6.021  20.952  1.00129.47      B    C  
ANISOU 4877  C   PRO A   4     9119  22896  17178  -8337   7033 -11644  B    C  
ATOM   4878  O   PRO A   4     -44.368  -6.766  20.263  1.00131.27      B    O  
ANISOU 4878  O   PRO A   4     8985  23603  17289  -8575   7074 -12057  B    O  
ATOM   4879  CB  PRO A   4     -42.836  -7.416  22.901  1.00122.78      B    C  
ANISOU 4879  CB  PRO A   4     9062  18875  18714  -7816   7858 -11601  B    C  
ATOM   4880  CG  PRO A   4     -42.746  -6.459  24.033  1.00118.65      B    C  
ANISOU 4880  CG  PRO A   4     9302  17632  18148  -6963   7280 -10174  B    C  
ATOM   4881  CD  PRO A   4     -41.593  -5.566  23.713  1.00110.79      B    C  
ANISOU 4881  CD  PRO A   4     8604  16863  16629  -6700   6840  -9560  B    C  
ATOM   4882  N   SER A   5     -43.915  -4.697  21.098  1.00121.49      B    N  
ANISOU 4882  N   SER A   5     8409  22398  15355  -7798   6302 -10408  B    N  
ATOM   4883  CA  SER A   5     -45.048  -3.986  20.498  1.00124.45      B    C  
ANISOU 4883  CA  SER A   5     8323  24329  14635  -7906   5880 -10111  B    C  
ATOM   4884  C   SER A   5     -44.720  -3.449  19.091  1.00133.12      B    C  
ANISOU 4884  C   SER A   5     8814  27189  14575  -8293   5640 -10230  B    C  
ATOM   4885  O   SER A   5     -45.636  -3.053  18.366  1.00135.98      B    O  
ANISOU 4885  O   SER A   5     8718  28888  14061  -8351   5294  -9918  B    O  
ATOM   4886  CB  SER A   5     -45.503  -2.840  21.402  1.00121.30      B    C  
ANISOU 4886  CB  SER A   5     8493  23491  14104  -7113   5313  -8678  B    C  
ATOM   4887  OG  SER A   5     -45.492  -3.204  22.774  1.00125.06      B    O  
ANISOU 4887  OG  SER A   5     9617  22283  15616  -6672   5485  -8412  B    O  
ATOM   4888  N   SER A   6     -43.431  -3.461  18.709  1.00128.21      B    N  
ANISOU 4888  N   SER A   6     8322  26335  14059  -8348   5729 -10377  B    N  
ATOM   4889  CA  SER A   6     -42.928  -2.984  17.414  1.00131.86      B    C  
ANISOU 4889  CA  SER A   6     8320  28240  13542  -8606   5495 -10354  B    C  
ATOM   4890  C   SER A   6     -42.301  -4.125  16.601  1.00133.71      B    C  
ANISOU 4890  C   SER A   6     8757  27677  14370  -8529   5610 -10657  B    C  
ATOM   4891  O   SER A   6     -41.917  -5.153  17.167  1.00131.95      B    O  
ANISOU 4891  O   SER A   6     8751  26214  15172  -8659   6118 -11347  B    O  
ATOM   4892  CB  SER A   6     -41.897  -1.874  17.632  1.00129.36      B    C  
ANISOU 4892  CB  SER A   6     8525  27535  13090  -8024   5092  -9238  B    C  
ATOM   4893  OG  SER A   6     -41.198  -1.476  16.459  1.00138.01      B    O  
ANISOU 4893  OG  SER A   6     9222  29825  13389  -8254   4941  -9226  B    O  
ATOM   4894  N   PHE A   7     -42.238  -3.950  15.271  1.00132.18      B    N  
ANISOU 4894  N   PHE A   7     8313  28428  13481  -8498   5272 -10353  B    N  
ATOM   4895  CA  PHE A   7     -41.607  -4.902  14.358  1.00131.69      B    C  
ANISOU 4895  CA  PHE A   7     8333  27922  13782  -8534   5378 -10695  B    C  
ATOM   4896  C   PHE A   7     -40.219  -4.384  13.968  1.00133.64      B    C  
ANISOU 4896  C   PHE A   7     8748  28158  13871  -8441   5291 -10459  B    C  
ATOM   4897  O   PHE A   7     -39.394  -5.166  13.501  1.00132.73      B    O  
ANISOU 4897  O   PHE A   7     8755  27451  14226  -8521   5500 -10867  B    O  
ATOM   4898  CB  PHE A   7     -42.477  -5.172  13.113  1.00133.81      B    C  
ANISOU 4898  CB  PHE A   7     8467  28730  13642  -8329   5000 -10266  B    C  
ATOM   4899  CG  PHE A   7     -43.563  -6.219  13.275  1.00134.79      B    C  
ANISOU 4899  CG  PHE A   7     8633  28296  14287  -8307   5109 -10504  B    C  
ATOM   4900  CD1 PHE A   7     -43.240  -7.549  13.532  1.00136.01      B    C  
ANISOU 4900  CD1 PHE A   7     9043  27251  15385  -8329   5449 -10985  B    C  
ATOM   4901  CD2 PHE A   7     -44.901  -5.890  13.095  1.00136.86      B    C  
ANISOU 4901  CD2 PHE A   7     8758  29098  14146  -8126   4798 -10007  B    C  
ATOM   4902  CE1 PHE A   7     -44.242  -8.518  13.665  1.00136.38      B    C  
ANISOU 4902  CE1 PHE A   7     9098  26852  15869  -8307   5542 -11143  B    C  
ATOM   4903  CE2 PHE A   7     -45.897  -6.865  13.206  1.00138.66      B    C  
ANISOU 4903  CE2 PHE A   7     9058  28770  14854  -8068   4867 -10151  B    C  
ATOM   4904  CZ  PHE A   7     -45.563  -8.168  13.498  1.00136.39      B    C  
ANISOU 4904  CZ  PHE A   7     8890  27536  15396  -8253   5285 -10843  B    C  
ATOM   4905  N   ALA A   8     -39.962  -3.071  14.190  1.00131.64      B    N  
ANISOU 4905  N   ALA A   8     8308  28863  12847  -8484   5098 -10042  B    N  
ATOM   4906  CA  ALA A   8     -38.693  -2.400  13.913  1.00131.44      B    C  
ANISOU 4906  CA  ALA A   8     8321  29105  12517  -8505   5046  -9868  B    C  
ATOM   4907  C   ALA A   8     -37.586  -2.847  14.877  1.00132.18      B    C  
ANISOU 4907  C   ALA A   8     8808  27861  13555  -8631   5522 -10474  B    C  
ATOM   4908  O   ALA A   8     -37.871  -3.228  16.014  1.00131.69      B    O  
ANISOU 4908  O   ALA A   8     8917  26914  14206  -8726   5890 -10905  B    O  
ATOM   4909  CB  ALA A   8     -38.874  -0.895  14.001  1.00133.01      B    C  
ANISOU 4909  CB  ALA A   8     8341  30409  11787  -8292   4621  -8878  B    C  
ATOM   4910  N   SER A   9     -36.325  -2.813  14.403  1.00128.18      B    N  
ANISOU 4910  N   SER A   9     8275  27404  13021  -8837   5673 -10785  B    N  
ATOM   4911  CA  SER A   9     -35.139  -3.191  15.176  1.00126.22      B    C  
ANISOU 4911  CA  SER A   9     8332  25937  13690  -9021   6205 -11429  B    C  
ATOM   4912  C   SER A   9     -34.292  -1.950  15.510  1.00121.24      B    C  
ANISOU 4912  C   SER A   9     8314  24876  12876  -8283   5655 -10057  B    C  
ATOM   4913  O   SER A   9     -33.610  -1.425  14.628  1.00121.86      B    O  
ANISOU 4913  O   SER A   9     8170  25837  12295  -8392   5485  -9909  B    O  
ATOM   4914  CB  SER A   9     -34.308  -4.234  14.434  1.00127.16      B    C  
ANISOU 4914  CB  SER A   9     8604  25321  14391  -8954   6341 -11706  B    C  
ATOM   4915  OG  SER A   9     -35.047  -5.435  14.267  1.00130.58      B    O  
ANISOU 4915  OG  SER A   9     9197  24999  15420  -8684   6310 -11648  B    O  
ATOM   4916  N   PRO A  10     -34.359  -1.449  16.776  1.00109.50      B    N  
ANISOU 4916  N   PRO A  10     7564  22079  11961  -7541   5391  -9059  B    N  
ATOM   4917  CA  PRO A  10     -33.575  -0.251  17.148  1.00102.46      B    C  
ANISOU 4917  CA  PRO A  10     7228  20724  10976  -6866   4925  -7840  B    C  
ATOM   4918  C   PRO A  10     -32.064  -0.509  17.194  1.00103.59      B    C  
ANISOU 4918  C   PRO A  10     7701  19969  11689  -6825   5127  -8041  B    C  
ATOM   4919  O   PRO A  10     -31.280   0.441  17.139  1.00 99.93      B    O  
ANISOU 4919  O   PRO A  10     7510  19476  10983  -6453   4801  -7271  B    O  
ATOM   4920  CB  PRO A  10     -34.119   0.130  18.545  1.00 97.57      B    C  
ANISOU 4920  CB  PRO A  10     7220  18950  10902  -6225   4718  -7021  B    C  
ATOM   4921  CG  PRO A  10     -35.322  -0.716  18.764  1.00104.74      B    C  
ANISOU 4921  CG  PRO A  10     7836  19983  11977  -6538   4977  -7652  B    C  
ATOM   4922  CD  PRO A  10     -35.143  -1.942  17.927  1.00107.40      B    C  
ANISOU 4922  CD  PRO A  10     7614  20743  12449  -7312   5536  -9035  B    C  
ATOM   4923  N   GLU A  11     -31.663  -1.789  17.277  1.00102.21      B    N  
ANISOU 4923  N   GLU A  11     7459  19053  12325  -7210   5707  -9066  B    N  
ATOM   4924  CA  GLU A  11     -30.264  -2.241  17.314  1.00100.80      B    C  
ANISOU 4924  CA  GLU A  11     7508  17975  12819  -7232   6010  -9372  B    C  
ATOM   4925  C   GLU A  11     -29.632  -2.263  15.909  1.00108.95      B    C  
ANISOU 4925  C   GLU A  11     8007  20188  13200  -7791   6121 -10019  B    C  
ATOM   4926  O   GLU A  11     -28.401  -2.309  15.787  1.00106.61      B    O  
ANISOU 4926  O   GLU A  11     7909  19374  13223  -7741   6228 -10050  B    O  
ATOM   4927  CB  GLU A  11     -30.168  -3.641  17.964  1.00103.85      B    C  
ANISOU 4927  CB  GLU A  11     7920  17101  14438  -7424   6682 -10164  B    C  
ATOM   4928  CG  GLU A  11     -31.064  -4.700  17.324  1.00126.07      B    C  
ANISOU 4928  CG  GLU A  11    10028  20567  17307  -8182   7225 -11445  B    C  
ATOM   4929  CD  GLU A  11     -31.517  -5.832  18.229  1.00147.61      B    C  
ANISOU 4929  CD  GLU A  11    13009  21927  21148  -7873   7482 -11369  B    C  
ATOM   4930  OE1 GLU A  11     -31.285  -7.008  17.867  1.00145.90      B    O  
ANISOU 4930  OE1 GLU A  11    12734  21232  21467  -7880   7661 -11610  B    O  
ATOM   4931  OE2 GLU A  11     -32.118  -5.546  19.289  1.00139.15      B    O1-
ANISOU 4931  OE2 GLU A  11    12141  20331  20399  -7678   7555 -11110  B    O1-
ATOM   4932  N   LYS A  12     -30.474  -2.258  14.856  1.00111.23      B    N  
ANISOU 4932  N   LYS A  12     7579  22128  12556  -8341   6108 -10548  B    N  
ATOM   4933  CA  LYS A  12     -30.004  -2.296  13.472  1.00116.83      B    C  
ANISOU 4933  CA  LYS A  12     7657  24236  12497  -8946   6220 -11220  B    C  
ATOM   4934  C   LYS A  12     -29.827  -0.888  12.897  1.00116.80      B    C  
ANISOU 4934  C   LYS A  12     7620  25350  11411  -8605   5592 -10099  B    C  
ATOM   4935  O   LYS A  12     -28.796  -0.619  12.288  1.00116.42      B    O  
ANISOU 4935  O   LYS A  12     7549  25528  11158  -8663   5576 -10076  B    O  
ATOM   4936  CB  LYS A  12     -30.956  -3.130  12.590  1.00123.56      B    C  
ANISOU 4936  CB  LYS A  12     8048  25818  13081  -9216   6244 -11697  B    C  
ATOM   4937  CG  LYS A  12     -30.780  -4.635  12.767  1.00134.89      B    C  
ANISOU 4937  CG  LYS A  12    10107  25322  15823  -8624   6264 -11460  B    C  
ATOM   4938  CD  LYS A  12     -31.718  -5.433  11.863  1.00143.68      B    C  
ANISOU 4938  CD  LYS A  12    11369  26352  16869  -8112   5773 -10787  B    C  
ATOM   4939  CE  LYS A  12     -31.451  -6.916  11.938  1.00148.26      B    C  
ANISOU 4939  CE  LYS A  12    12324  25566  18441  -7812   5870 -10756  B    C  
ATOM   4940  NZ  LYS A  12     -32.291  -7.676  10.978  1.00152.19      B    N1+
ANISOU 4940  NZ  LYS A  12    12848  26182  18797  -7552   5536 -10385  B    N1+
ATOM   4941  N   PHE A  13     -30.841  -0.016  13.021  1.00111.49      B    N  
ANISOU 4941  N   PHE A  13     6866  25424  10071  -8280   5131  -9189  B    N  
ATOM   4942  CA  PHE A  13     -30.779   1.351  12.497  1.00109.80      B    C  
ANISOU 4942  CA  PHE A  13     6532  26244   8942  -7913   4607  -7999  B    C  
ATOM   4943  C   PHE A  13     -31.620   2.294  13.346  1.00105.87      B    C  
ANISOU 4943  C   PHE A  13     6386  25381   8459  -7225   4186  -6748  B    C  
ATOM   4944  O   PHE A  13     -32.528   1.846  14.056  1.00104.24      B    O  
ANISOU 4944  O   PHE A  13     6292  24695   8618  -7200   4264  -6945  B    O  
ATOM   4945  CB  PHE A  13     -31.191   1.423  11.014  1.00121.09      B    C  
ANISOU 4945  CB  PHE A  13     6961  29950   9097  -8540   4586  -8386  B    C  
ATOM   4946  CG  PHE A  13     -32.561   0.895  10.665  1.00124.52      B    C  
ANISOU 4946  CG  PHE A  13     7124  30809   9378  -8574   4517  -8517  B    C  
ATOM   4947  CD1 PHE A  13     -32.750  -0.447  10.358  1.00126.05      B    C  
ANISOU 4947  CD1 PHE A  13     7527  30042  10324  -8613   4740  -9231  B    C  
ATOM   4948  CD2 PHE A  13     -33.651   1.752  10.578  1.00127.17      B    C  
ANISOU 4948  CD2 PHE A  13     7288  31897   9132  -8179   4094  -7450  B    C  
ATOM   4949  CE1 PHE A  13     -34.014  -0.930  10.005  1.00127.06      B    C  
ANISOU 4949  CE1 PHE A  13     7574  30250  10454  -8469   4599  -9128  B    C  
ATOM   4950  CE2 PHE A  13     -34.916   1.268  10.230  1.00129.51      B    C  
ANISOU 4950  CE2 PHE A  13     7580  32080   9546  -7976   3964  -7345  B    C  
ATOM   4951  CZ  PHE A  13     -35.090  -0.071   9.953  1.00127.56      B    C  
ANISOU 4951  CZ  PHE A  13     7406  31199   9862  -8231   4242  -8303  B    C  
ATOM   4952  N   ASN A  14     -31.320   3.599  13.269  1.00 97.39      B    N  
ANISOU 4952  N   ASN A  14     5453  24505   7047  -6680   3790  -5483  B    N  
ATOM   4953  CA  ASN A  14     -31.984   4.623  14.072  1.00 91.87      B    C  
ANISOU 4953  CA  ASN A  14     5083  23344   6479  -6000   3452  -4255  B    C  
ATOM   4954  C   ASN A  14     -32.468   5.809  13.242  1.00 98.72      B    C  
ANISOU 4954  C   ASN A  14     5371  25719   6418  -5806   3134  -3151  B    C  
ATOM   4955  O   ASN A  14     -31.683   6.386  12.483  1.00102.14      B    O  
ANISOU 4955  O   ASN A  14     5587  26770   6450  -5773   3059  -2744  B    O  
ATOM   4956  CB  ASN A  14     -30.995   5.122  15.118  1.00 85.07      B    C  
ANISOU 4956  CB  ASN A  14     5082  20739   6502  -5392   3382  -3687  B    C  
ATOM   4957  CG  ASN A  14     -31.453   5.054  16.540  1.00103.52      B    C  
ANISOU 4957  CG  ASN A  14     8034  21670   9628  -4983   3363  -3474  B    C  
ATOM   4958  ND2 ASN A  14     -30.699   4.334  17.360  1.00 90.27      B    N  
ANISOU 4958  ND2 ASN A  14     6895  18626   8779  -4950   3578  -3996  B    N  
ATOM   4959  OD1 ASN A  14     -32.403   5.730  16.943  1.00102.52      B    O  
ANISOU 4959  OD1 ASN A  14     7900  21652   9399  -4649   3159  -2742  B    O  
ATOM   4960  N   ILE A  15     -33.752   6.181  13.393  1.00 95.18      B    N  
ANISOU 4960  N   ILE A  15     4645  25847   5673  -5650   2970  -2597  B    N  
ATOM   4961  CA  ILE A  15     -34.341   7.355  12.739  1.00 98.88      B    C  
ANISOU 4961  CA  ILE A  15     4527  27646   5395  -5364   2700  -1338  B    C  
ATOM   4962  C   ILE A  15     -33.913   8.533  13.584  1.00 97.39      B    C  
ANISOU 4962  C   ILE A  15     4961  26112   5929  -4568   2562   -138  B    C  
ATOM   4963  O   ILE A  15     -34.215   8.576  14.781  1.00 92.58      B    O  
ANISOU 4963  O   ILE A  15     4969  24118   6090  -4222   2563    -40  B    O  
ATOM   4964  CB  ILE A  15     -35.889   7.272  12.545  1.00106.41      B    C  
ANISOU 4964  CB  ILE A  15     4860  29811   5758  -5529   2611  -1211  B    C  
ATOM   4965  CG1 ILE A  15     -36.266   6.150  11.562  1.00113.44      B    C  
ANISOU 4965  CG1 ILE A  15     5011  32228   5862  -6410   2792  -2522  B    C  
ATOM   4966  CG2 ILE A  15     -36.478   8.629  12.088  1.00110.96      B    C  
ANISOU 4966  CG2 ILE A  15     4870  31521   5768  -5074   2357    375  B    C  
ATOM   4967  CD1 ILE A  15     -37.740   5.686  11.669  1.00112.40      B    C  
ANISOU 4967  CD1 ILE A  15     4457  32830   5419  -6662   2790  -2829  B    C  
ATOM   4968  N   LYS A  16     -33.189   9.466  12.973  1.00 95.33      B    N  
ANISOU 4968  N   LYS A  16     4510  26264   5445  -4309   2484    715  B    N  
ATOM   4969  CA  LYS A  16     -32.619  10.619  13.657  1.00 89.85      B    C  
ANISOU 4969  CA  LYS A  16     4335  24316   5486  -3613   2437   1757  B    C  
ATOM   4970  C   LYS A  16     -33.411  11.907  13.417  1.00 98.42      B    C  
ANISOU 4970  C   LYS A  16     4922  26095   6380  -3132   2332   3243  B    C  
ATOM   4971  O   LYS A  16     -33.396  12.795  14.268  1.00 94.67      B    O  
ANISOU 4971  O   LYS A  16     4866  24421   6684  -2562   2359   4014  B    O  
ATOM   4972  CB  LYS A  16     -31.149  10.798  13.227  1.00 90.46      B    C  
ANISOU 4972  CB  LYS A  16     4590  24120   5659  -3614   2501   1693  B    C  
ATOM   4973  CG  LYS A  16     -30.219   9.678  13.710  1.00 88.50      B    C  
ANISOU 4973  CG  LYS A  16     4947  22789   5888  -3945   2651    405  B    C  
ATOM   4974  CD  LYS A  16     -29.887   9.802  15.206  1.00 81.42      B    C  
ANISOU 4974  CD  LYS A  16     4954  19921   6062  -3513   2679    415  B    C  
ATOM   4975  CE  LYS A  16     -29.500   8.490  15.824  1.00 80.03      B    C  
ANISOU 4975  CE  LYS A  16     5228  18842   6339  -3848   2848   -800  B    C  
ATOM   4976  NZ  LYS A  16     -29.289   8.632  17.285  1.00 86.45      B    N1+
ANISOU 4976  NZ  LYS A  16     6807  17978   8063  -3425   2852   -683  B    N1+
ATOM   4977  N   HIS A  17     -34.107  12.002  12.280  1.00104.11      B    N  
ANISOU 4977  N   HIS A  17     4694  28766   6096  -3370   2252   3641  B    N  
ATOM   4978  CA  HIS A  17     -34.877  13.185  11.908  1.00109.49      B    C  
ANISOU 4978  CA  HIS A  17     4733  30321   6547  -2917   2189   5179  B    C  
ATOM   4979  C   HIS A  17     -35.962  12.828  10.914  1.00122.72      B    C  
ANISOU 4979  C   HIS A  17     5403  34166   7060  -3333   2077   5210  B    C  
ATOM   4980  O   HIS A  17     -35.804  11.902  10.114  1.00125.42      B    O  
ANISOU 4980  O   HIS A  17     5416  35593   6644  -3981   2070   4155  B    O  
ATOM   4981  CB  HIS A  17     -33.944  14.260  11.303  1.00112.74      B    C  
ANISOU 4981  CB  HIS A  17     4904  30926   7005  -2548   2251   6262  B    C  
ATOM   4982  CG  HIS A  17     -34.598  15.577  11.014  1.00121.33      B    C  
ANISOU 4982  CG  HIS A  17     5362  32588   8150  -1971   2291   8008  B    C  
ATOM   4983  CD2 HIS A  17     -34.972  16.114   9.828  1.00127.10      B    C  
ANISOU 4983  CD2 HIS A  17     5700  34055   8536  -1861   2278   8546  B    C  
ATOM   4984  ND1 HIS A  17     -34.862  16.486  12.020  1.00118.95      B    N  
ANISOU 4984  ND1 HIS A  17     5489  30771   8937  -1352   2432   8794  B    N  
ATOM   4985  CE1 HIS A  17     -35.406  17.533  11.421  1.00125.35      B    C  
ANISOU 4985  CE1 HIS A  17     5491  32514   9624   -943   2516  10346  B    C  
ATOM   4986  NE2 HIS A  17     -35.475  17.363  10.100  1.00126.65      B    N  
ANISOU 4986  NE2 HIS A  17     5669  33212   9241  -1216   2412   9772  B    N  
ATOM   4987  N   MET A  18     -37.051  13.597  10.955  1.00124.00      B    N  
ANISOU 4987  N   MET A  18     5089  34861   7166  -2946   2024   6397  B    N  
ATOM   4988  CA  MET A  18     -38.183  13.469  10.058  1.00125.05      B    C  
ANISOU 4988  CA  MET A  18     5213  35161   7140  -2983   1953   6108  B    C  
ATOM   4989  C   MET A  18     -38.589  14.821   9.507  1.00129.45      B    C  
ANISOU 4989  C   MET A  18     6044  34789   8354  -2302   1991   7172  B    C  
ATOM   4990  O   MET A  18     -38.756  15.775  10.266  1.00129.06      B    O  
ANISOU 4990  O   MET A  18     5960  34214   8864  -1801   2075   8271  B    O  
ATOM   4991  CB  MET A  18     -39.389  12.848  10.784  1.00126.36      B    C  
ANISOU 4991  CB  MET A  18     5381  35323   7305  -3157   1901   5633  B    C  
ATOM   4992  CG  MET A  18     -39.319  11.357  10.965  1.00128.51      B    C  
ANISOU 4992  CG  MET A  18     5812  35722   7295  -3864   1930   3968  B    C  
ATOM   4993  SD  MET A  18     -40.946  10.731  11.490  1.00131.47      B    S  
ANISOU 4993  SD  MET A  18     6287  35840   7825  -3975   1893   3412  B    S  
ATOM   4994  CE  MET A  18     -40.528   9.047  11.852  1.00128.75      B    C  
ANISOU 4994  CE  MET A  18     5921  35849   7148  -4889   2051   1542  B    C  
ATOM   4995  N   HIS A  19     -38.752  14.902   8.187  1.00128.47      B    N  
ANISOU 4995  N   HIS A  19     5930  34891   7992  -2354   1950   6972  B    N  
ATOM   4996  CA  HIS A  19     -39.317  16.067   7.518  1.00129.20      B    C  
ANISOU 4996  CA  HIS A  19     6131  34488   8472  -1884   1972   7799  B    C  
ATOM   4997  C   HIS A  19     -40.703  15.601   7.049  1.00132.41      B    C  
ANISOU 4997  C   HIS A  19     6714  34763   8831  -2006   1854   7183  B    C  
ATOM   4998  O   HIS A  19     -40.789  14.642   6.282  1.00132.00      B    O  
ANISOU 4998  O   HIS A  19     6664  35140   8349  -2397   1781   6270  B    O  
ATOM   4999  CB  HIS A  19     -38.425  16.604   6.382  1.00130.40      B    C  
ANISOU 4999  CB  HIS A  19     6459  34437   8650  -1789   2027   7908  B    C  
ATOM   5000  CG  HIS A  19     -38.991  17.831   5.738  1.00133.31      B    C  
ANISOU 5000  CG  HIS A  19     7083  34057   9513  -1360   2068   8547  B    C  
ATOM   5001  CD2 HIS A  19     -38.755  19.136   6.003  1.00134.51      B    C  
ANISOU 5001  CD2 HIS A  19     7371  33417  10319   -899   2217   9456  B    C  
ATOM   5002  ND1 HIS A  19     -39.954  17.746   4.743  1.00135.13      B    N  
ANISOU 5002  ND1 HIS A  19     7457  34280   9607  -1425   1962   8167  B    N  
ATOM   5003  CE1 HIS A  19     -40.253  18.994   4.424  1.00134.82      B    C  
ANISOU 5003  CE1 HIS A  19     7490  33769   9966  -1043   2027   8943  B    C  
ATOM   5004  NE2 HIS A  19     -39.555  19.866   5.152  1.00134.65      B    N  
ANISOU 5004  NE2 HIS A  19     7488  33216  10456   -728   2192   9686  B    N  
ATOM   5005  N   LEU A  20     -41.780  16.199   7.584  1.00130.71      B    N  
ANISOU 5005  N   LEU A  20     6379  34390   8896  -1714   1846   7846  B    N  
ATOM   5006  CA  LEU A  20     -43.144  15.762   7.284  1.00131.41      B    C  
ANISOU 5006  CA  LEU A  20     6472  34593   8864  -1832   1729   7416  B    C  
ATOM   5007  C   LEU A  20     -43.949  16.747   6.438  1.00135.36      B    C  
ANISOU 5007  C   LEU A  20     7315  34317   9800  -1485   1711   7754  B    C  
ATOM   5008  O   LEU A  20     -44.254  17.851   6.884  1.00134.39      B    O  
ANISOU 5008  O   LEU A  20     7178  33745  10139  -1083   1795   8644  B    O  
ATOM   5009  CB  LEU A  20     -43.924  15.483   8.587  1.00131.19      B    C  
ANISOU 5009  CB  LEU A  20     6312  34553   8982  -1815   1724   7524  B    C  
ATOM   5010  CG  LEU A  20     -43.406  14.405   9.543  1.00134.33      B    C  
ANISOU 5010  CG  LEU A  20     6790  34982   9267  -2169   1741   6747  B    C  
ATOM   5011  CD1 LEU A  20     -44.124  14.474  10.872  1.00134.17      B    C  
ANISOU 5011  CD1 LEU A  20     6663  34805   9512  -2017   1761   7154  B    C  
ATOM   5012  CD2 LEU A  20     -43.609  13.027   8.973  1.00136.72      B    C  
ANISOU 5012  CD2 LEU A  20     7208  35543   9196  -2707   1676   5371  B    C  
ATOM   5013  N   LYS A  21     -44.345  16.312   5.234  1.00134.73      B    N  
ANISOU 5013  N   LYS A  21     7266  34538   9388  -1686   1605   7212  B    N  
ATOM   5014  CA  LYS A  21     -45.218  17.066   4.335  1.00135.40      B    C  
ANISOU 5014  CA  LYS A  21     7475  34334   9637  -1462   1549   7509  B    C  
ATOM   5015  C   LYS A  21     -46.599  16.396   4.421  1.00138.96      B    C  
ANISOU 5015  C   LYS A  21     8066  34569  10162  -1580   1432   6922  B    C  
ATOM   5016  O   LYS A  21     -46.826  15.365   3.783  1.00138.89      B    O  
ANISOU 5016  O   LYS A  21     8039  34916   9817  -1899   1344   6154  B    O  
ATOM   5017  CB  LYS A  21     -44.647  17.094   2.905  1.00137.58      B    C  
ANISOU 5017  CB  LYS A  21     8002  34499   9772  -1535   1526   7166  B    C  
ATOM   5018  CG  LYS A  21     -43.560  18.154   2.695  1.00147.96      B    C  
ANISOU 5018  CG  LYS A  21    10119  34250  11849  -1223   1669   7241  B    C  
ATOM   5019  CD  LYS A  21     -42.431  17.730   1.721  1.00155.62      B    C  
ANISOU 5019  CD  LYS A  21    11673  34537  12916  -1361   1702   6463  B    C  
ATOM   5020  CE  LYS A  21     -42.789  17.433   0.281  1.00163.39      B    C  
ANISOU 5020  CE  LYS A  21    13266  34741  14073  -1407   1620   5714  B    C  
ATOM   5021  NZ  LYS A  21     -41.575  17.077  -0.511  1.00167.37      B    N1+
ANISOU 5021  NZ  LYS A  21    14161  34814  14619  -1515   1681   5177  B    N1+
ATOM   5022  N   LEU A  22     -47.484  16.925   5.287  1.00137.08      B    N  
ANISOU 5022  N   LEU A  22     7687  34208  10189  -1357   1444   7477  B    N  
ATOM   5023  CA  LEU A  22     -48.808  16.331   5.513  1.00137.42      B    C  
ANISOU 5023  CA  LEU A  22     7663  34356  10195  -1472   1341   7113  B    C  
ATOM   5024  C   LEU A  22     -49.922  17.072   4.775  1.00141.36      B    C  
ANISOU 5024  C   LEU A  22     8454  34215  11041  -1234   1268   7240  B    C  
ATOM   5025  O   LEU A  22     -50.087  18.280   4.956  1.00140.71      B    O  
ANISOU 5025  O   LEU A  22     8400  33752  11312   -893   1336   7996  B    O  
ATOM   5026  CB  LEU A  22     -49.159  16.268   7.015  1.00136.84      B    C  
ANISOU 5026  CB  LEU A  22     7448  34214  10331  -1401   1401   7379  B    C  
ATOM   5027  CG  LEU A  22     -48.096  15.779   8.012  1.00139.34      B    C  
ANISOU 5027  CG  LEU A  22     7868  34370  10707  -1526   1497   7128  B    C  
ATOM   5028  CD1 LEU A  22     -48.529  16.065   9.437  1.00138.79      B    C  
ANISOU 5028  CD1 LEU A  22     7699  34051  10984  -1315   1575   7681  B    C  
ATOM   5029  CD2 LEU A  22     -47.814  14.293   7.853  1.00141.10      B    C  
ANISOU 5029  CD2 LEU A  22     8136  34912  10562  -2014   1446   5982  B    C  
ATOM   5030  N   HIS A  23     -50.690  16.335   3.950  1.00140.53      B    N  
ANISOU 5030  N   HIS A  23     8294  34449  10652  -1451   1133   6685  B    N  
ATOM   5031  CA  HIS A  23     -51.842  16.862   3.221  1.00141.68      B    C  
ANISOU 5031  CA  HIS A  23     8538  34346  10949  -1294   1032   6817  B    C  
ATOM   5032  C   HIS A  23     -53.113  16.367   3.928  1.00146.45      B    C  
ANISOU 5032  C   HIS A  23     9257  34562  11825  -1329    975   6440  B    C  
ATOM   5033  O   HIS A  23     -53.391  15.165   3.912  1.00146.25      B    O  
ANISOU 5033  O   HIS A  23     9135  34876  11557  -1637    916   5765  B    O  
ATOM   5034  CB  HIS A  23     -51.807  16.436   1.737  1.00142.84      B    C  
ANISOU 5034  CB  HIS A  23     8841  34574  10859  -1449    928   6310  B    C  
ATOM   5035  CG  HIS A  23     -52.979  16.926   0.937  1.00145.87      B    C  
ANISOU 5035  CG  HIS A  23     9427  34545  11453  -1298    811   6333  B    C  
ATOM   5036  CD2 HIS A  23     -54.207  16.377   0.772  1.00147.59      B    C  
ANISOU 5036  CD2 HIS A  23     9658  34716  11704  -1389    688   5932  B    C  
ATOM   5037  ND1 HIS A  23     -52.924  18.114   0.232  1.00147.29      B    N  
ANISOU 5037  ND1 HIS A  23     9821  34299  11846  -1032    818   6794  B    N  
ATOM   5038  CE1 HIS A  23     -54.110  18.247  -0.342  1.00147.53      B    C  
ANISOU 5038  CE1 HIS A  23     9855  34296  11902   -988    688   6746  B    C  
ATOM   5039  NE2 HIS A  23     -54.917  17.228  -0.042  1.00147.94      B    N  
ANISOU 5039  NE2 HIS A  23     9797  34548  11864  -1189    605   6244  B    N  
ATOM   5040  N   VAL A  24     -53.877  17.272   4.558  1.00145.42      B    N  
ANISOU 5040  N   VAL A  24     9049  34205  11997  -1054   1001   7064  B    N  
ATOM   5041  CA  VAL A  24     -55.085  16.821   5.248  1.00146.30      B    C  
ANISOU 5041  CA  VAL A  24     9070  34302  12215  -1103    950   6870  B    C  
ATOM   5042  C   VAL A  24     -56.328  17.250   4.447  1.00151.42      B    C  
ANISOU 5042  C   VAL A  24    10014  34364  13153   -971    831   6718  B    C  
ATOM   5043  O   VAL A  24     -56.491  18.427   4.110  1.00151.23      B    O  
ANISOU 5043  O   VAL A  24    10077  34040  13344   -703    845   7252  B    O  
ATOM   5044  CB  VAL A  24     -55.167  17.200   6.763  1.00148.42      B    C  
ANISOU 5044  CB  VAL A  24     9393  34098  12902   -920   1075   7230  B    C  
ATOM   5045  CG1 VAL A  24     -53.909  16.773   7.514  1.00147.70      B    C  
ANISOU 5045  CG1 VAL A  24     9256  34157  12706  -1032   1186   7186  B    C  
ATOM   5046  CG2 VAL A  24     -55.443  18.681   6.987  1.00148.03      B    C  
ANISOU 5046  CG2 VAL A  24     9413  33535  13298   -520   1156   8052  B    C  
ATOM   5047  N   ASP A  25     -57.158  16.264   4.086  1.00150.97      B    N  
ANISOU 5047  N   ASP A  25     9835  34643  12886  -1204    710   6172  B    N  
ATOM   5048  CA  ASP A  25     -58.407  16.494   3.372  1.00152.23      B    C  
ANISOU 5048  CA  ASP A  25    10048  34644  13150  -1128    577   6123  B    C  
ATOM   5049  C   ASP A  25     -59.543  15.932   4.199  1.00156.17      B    C  
ANISOU 5049  C   ASP A  25    10602  34810  13925  -1174    553   5786  B    C  
ATOM   5050  O   ASP A  25     -59.535  14.754   4.566  1.00155.76      B    O  
ANISOU 5050  O   ASP A  25    10426  35047  13708  -1445    557   5268  B    O  
ATOM   5051  CB  ASP A  25     -58.398  15.906   1.955  1.00154.35      B    C  
ANISOU 5051  CB  ASP A  25    10496  34908  13242  -1296    455   5560  B    C  
ATOM   5052  CG  ASP A  25     -59.655  16.254   1.178  1.00163.71      B    C  
ANISOU 5052  CG  ASP A  25    12210  35058  14934  -1126    325   5272  B    C  
ATOM   5053  OD1 ASP A  25     -59.767  17.412   0.717  1.00164.82      B    O  
ANISOU 5053  OD1 ASP A  25    12513  34866  15245   -884    317   5694  B    O  
ATOM   5054  OD2 ASP A  25     -60.544  15.384   1.070  1.00167.91      B    O1-
ANISOU 5054  OD2 ASP A  25    12894  35272  15634  -1247    233   4698  B    O1-
ATOM   5055  N   PHE A  26     -60.501  16.798   4.516  1.00154.93      B    N  
ANISOU 5055  N   PHE A  26    10356  34525  13984   -940    534   6278  B    N  
ATOM   5056  CA  PHE A  26     -61.662  16.481   5.334  1.00155.32      B    C  
ANISOU 5056  CA  PHE A  26    10278  34539  14199   -948    515   6206  B    C  
ATOM   5057  C   PHE A  26     -62.754  15.732   4.566  1.00159.06      B    C  
ANISOU 5057  C   PHE A  26    10877  34842  14719  -1095    359   5573  B    C  
ATOM   5058  O   PHE A  26     -63.505  14.983   5.193  1.00159.13      B    O  
ANISOU 5058  O   PHE A  26    10739  34966  14758  -1227    347   5293  B    O  
ATOM   5059  CB  PHE A  26     -62.229  17.768   5.941  1.00156.43      B    C  
ANISOU 5059  CB  PHE A  26    10512  34155  14770   -604    581   6829  B    C  
ATOM   5060  CG  PHE A  26     -61.457  18.247   7.148  1.00156.69      B    C  
ANISOU 5060  CG  PHE A  26    10595  33899  15039   -460    763   7234  B    C  
ATOM   5061  CD1 PHE A  26     -61.814  17.840   8.426  1.00158.55      B    C  
ANISOU 5061  CD1 PHE A  26    10821  33943  15478   -483    839   7142  B    C  
ATOM   5062  CD2 PHE A  26     -60.374  19.110   7.007  1.00157.65      B    C  
ANISOU 5062  CD2 PHE A  26    10936  33655  15308   -297    863   7568  B    C  
ATOM   5063  CE1 PHE A  26     -61.104  18.286   9.544  1.00158.27      B    C  
ANISOU 5063  CE1 PHE A  26    10815  33650  15672   -337   1007   7566  B    C  
ATOM   5064  CE2 PHE A  26     -59.659  19.549   8.127  1.00158.72      B    C  
ANISOU 5064  CE2 PHE A  26    11172  33394  15741   -157   1035   7902  B    C  
ATOM   5065  CZ  PHE A  26     -60.028  19.130   9.388  1.00157.10      B    C  
ANISOU 5065  CZ  PHE A  26    10759  33317  15613   -170   1105   8017  B    C  
ATOM   5066  N   THR A  27     -62.852  15.925   3.231  1.00157.00      B    N  
ANISOU 5066  N   THR A  27    10603  34798  14253  -1098    236   5570  B    N  
ATOM   5067  CA  THR A  27     -63.850  15.247   2.397  1.00157.52      B    C  
ANISOU 5067  CA  THR A  27    10641  34954  14256  -1238     76   5123  B    C  
ATOM   5068  C   THR A  27     -63.521  13.743   2.343  1.00159.21      B    C  
ANISOU 5068  C   THR A  27    10909  35220  14363  -1569     79   4350  B    C  
ATOM   5069  O   THR A  27     -64.420  12.915   2.508  1.00159.29      B    O  
ANISOU 5069  O   THR A  27    10795  35322  14405  -1727     24   3972  B    O  
ATOM   5070  CB  THR A  27     -63.923  15.898   1.002  1.00165.42      B    C  
ANISOU 5070  CB  THR A  27    12190  35125  15539  -1069    -30   4985  B    C  
ATOM   5071  CG2 THR A  27     -64.984  15.264   0.110  1.00165.88      B    C  
ANISOU 5071  CG2 THR A  27    12204  35268  15554  -1180   -206   4613  B    C  
ATOM   5072  OG1 THR A  27     -64.199  17.291   1.148  1.00165.95      B    O  
ANISOU 5072  OG1 THR A  27    12339  34882  15833   -771     -4   5562  B    O  
ATOM   5073  N   SER A  28     -62.231  13.405   2.165  1.00155.41      B    N  
ANISOU 5073  N   SER A  28    10333  35180  13536  -1721    149   4283  B    N  
ATOM   5074  CA  SER A  28     -61.746  12.028   2.099  1.00154.55      B    C  
ANISOU 5074  CA  SER A  28    10163  35339  13219  -2064    175   3611  B    C  
ATOM   5075  C   SER A  28     -61.453  11.425   3.481  1.00154.94      B    C  
ANISOU 5075  C   SER A  28    10150  35371  13349  -2195    316   3405  B    C  
ATOM   5076  O   SER A  28     -61.395  10.195   3.595  1.00154.47      B    O  
ANISOU 5076  O   SER A  28    10018  35479  13195  -2500    344   2777  B    O  
ATOM   5077  CB  SER A  28     -60.489  11.953   1.241  1.00156.56      B    C  
ANISOU 5077  CB  SER A  28    10698  35393  13393  -2095    203   3435  B    C  
ATOM   5078  OG  SER A  28     -60.798  12.094  -0.135  1.00162.49      B    O  
ANISOU 5078  OG  SER A  28    11901  35432  14406  -1969     81   3248  B    O  
ATOM   5079  N   ARG A  29     -61.247  12.282   4.515  1.00150.91      B    N  
ANISOU 5079  N   ARG A  29     9413  35142  12785  -2028    402   4057  B    N  
ATOM   5080  CA  ARG A  29     -60.919  11.926   5.910  1.00149.62      B    C  
ANISOU 5080  CA  ARG A  29     9101  35136  12612  -2124    534   4041  B    C  
ATOM   5081  C   ARG A  29     -59.572  11.161   5.985  1.00150.00      B    C  
ANISOU 5081  C   ARG A  29     9245  35256  12493  -2364    630   3571  B    C  
ATOM   5082  O   ARG A  29     -59.437  10.207   6.757  1.00149.89      B    O  
ANISOU 5082  O   ARG A  29     9145  35379  12427  -2625    710   3079  B    O  
ATOM   5083  CB  ARG A  29     -62.056  11.124   6.587  1.00150.62      B    C  
ANISOU 5083  CB  ARG A  29     9120  35230  12878  -2272    526   3653  B    C  
ATOM   5084  CG  ARG A  29     -63.310  11.939   6.894  1.00159.64      B    C  
ANISOU 5084  CG  ARG A  29    10682  35263  14713  -1906    488   3894  B    C  
ATOM   5085  CD  ARG A  29     -64.525  11.050   7.098  1.00168.14      B    C  
ANISOU 5085  CD  ARG A  29    12067  35526  16291  -1976    459   3247  B    C  
ATOM   5086  NE  ARG A  29     -65.065  10.558   5.828  1.00175.44      B    N  
ANISOU 5086  NE  ARG A  29    13404  35712  17543  -1986    332   2720  B    N  
ATOM   5087  CZ  ARG A  29     -66.052   9.675   5.719  1.00186.19      B    C  
ANISOU 5087  CZ  ARG A  29    15241  35943  19561  -1983    296   2114  B    C  
ATOM   5088  NH1 ARG A  29     -66.622   9.167   6.806  1.00178.60      B    N1+
ANISOU 5088  NH1 ARG A  29    13698  35876  18287  -2192    361   2152  B    N1+
ATOM   5089  NH2 ARG A  29     -66.477   9.291   4.523  1.00176.74      B    N  
ANISOU 5089  NH2 ARG A  29    13579  35722  17852  -2189    146   2049  B    N  
ATOM   5090  N   ALA A  30     -58.573  11.604   5.199  1.00145.45      B    N  
ANISOU 5090  N   ALA A  30     8576  35104  11584  -2347    623   3838  B    N  
ATOM   5091  CA  ALA A  30     -57.249  10.980   5.164  1.00144.00      B    C  
ANISOU 5091  CA  ALA A  30     8393  35174  11148  -2587    708   3454  B    C  
ATOM   5092  C   ALA A  30     -56.115  12.014   5.189  1.00143.45      B    C  
ANISOU 5092  C   ALA A  30     8427  34991  11084  -2351    776   4058  B    C  
ATOM   5093  O   ALA A  30     -56.326  13.185   4.871  1.00142.70      B    O  
ANISOU 5093  O   ALA A  30     8362  34753  11102  -2039    743   4738  B    O  
ATOM   5094  CB  ALA A  30     -57.120  10.101   3.929  1.00144.99      B    C  
ANISOU 5094  CB  ALA A  30     8641  35289  11159  -2810    644   2797  B    C  
ATOM   5095  N   ILE A  31     -54.910  11.562   5.580  1.00139.40      B    N  
ANISOU 5095  N   ILE A  31     7721  35008  10238  -2578    874   3894  B    N  
ATOM   5096  CA  ILE A  31     -53.690  12.358   5.647  1.00137.95      B    C  
ANISOU 5096  CA  ILE A  31     7553  34869   9992  -2417    951   4425  B    C  
ATOM   5097  C   ILE A  31     -52.678  11.694   4.734  1.00138.00      B    C  
ANISOU 5097  C   ILE A  31     7654  35032   9749  -2665    965   3856  B    C  
ATOM   5098  O   ILE A  31     -52.222  10.578   5.004  1.00137.68      B    O  
ANISOU 5098  O   ILE A  31     7573  35180   9558  -3015   1025   3127  B    O  
ATOM   5099  CB  ILE A  31     -53.124  12.597   7.088  1.00139.42      B    C  
ANISOU 5099  CB  ILE A  31     7771  34816  10385  -2324   1076   4710  B    C  
ATOM   5100  CG1 ILE A  31     -54.196  13.179   8.036  1.00139.62      B    C  
ANISOU 5100  CG1 ILE A  31     7716  34626  10707  -2077   1077   5247  B    C  
ATOM   5101  CG2 ILE A  31     -51.869  13.513   7.030  1.00139.67      B    C  
ANISOU 5101  CG2 ILE A  31     7923  34646  10498  -2097   1159   5285  B    C  
ATOM   5102  CD1 ILE A  31     -53.720  13.481   9.496  1.00145.55      B    C  
ANISOU 5102  CD1 ILE A  31     8731  34663  11911  -1904   1210   5469  B    C  
ATOM   5103  N   ALA A  32     -52.374  12.360   3.627  1.00133.98      B    N  
ANISOU 5103  N   ALA A  32     7029  34897   8981  -2559    910   4265  B    N  
ATOM   5104  CA  ALA A  32     -51.380  11.884   2.677  1.00132.73      B    C  
ANISOU 5104  CA  ALA A  32     6914  34977   8542  -2765    925   3848  B    C  
ATOM   5105  C   ALA A  32     -50.051  12.465   3.108  1.00132.99      B    C  
ANISOU 5105  C   ALA A  32     6979  34980   8570  -2658   1039   4246  B    C  
ATOM   5106  O   ALA A  32     -49.905  13.691   3.170  1.00131.82      B    O  
ANISOU 5106  O   ALA A  32     6817  34717   8553  -2318   1059   5100  B    O  
ATOM   5107  CB  ALA A  32     -51.753  12.299   1.264  1.00133.72      B    C  
ANISOU 5107  CB  ALA A  32     7196  34939   8671  -2627    819   3963  B    C  
ATOM   5108  N   ALA A  33     -49.126  11.593   3.534  1.00130.06      B    N  
ANISOU 5108  N   ALA A  33     6404  35145   7870  -3012   1121   3736  B    N  
ATOM   5109  CA  ALA A  33     -47.846  12.050   4.053  1.00129.38      B    C  
ANISOU 5109  CA  ALA A  33     6296  35117   7746  -2946   1226   4092  B    C  
ATOM   5110  C   ALA A  33     -46.672  11.672   3.173  1.00131.60      B    C  
ANISOU 5110  C   ALA A  33     6772  35320   7909  -3104   1274   3631  B    C  
ATOM   5111  O   ALA A  33     -46.546  10.531   2.721  1.00130.96      B    O  
ANISOU 5111  O   ALA A  33     6690  35420   7650  -3465   1282   2759  B    O  
ATOM   5112  CB  ALA A  33     -47.626  11.510   5.453  1.00129.30      B    C  
ANISOU 5112  CB  ALA A  33     6187  35177   7762  -3124   1308   3837  B    C  
ATOM   5113  N   SER A  34     -45.807  12.661   2.952  1.00129.38      B    N  
ANISOU 5113  N   SER A  34     6401  35227   7532  -2890   1315   4357  B    N  
ATOM   5114  CA  SER A  34     -44.550  12.548   2.240  1.00129.15      B    C  
ANISOU 5114  CA  SER A  34     6452  35297   7323  -3003   1375   4145  B    C  
ATOM   5115  C   SER A  34     -43.484  12.684   3.317  1.00131.84      B    C  
ANISOU 5115  C   SER A  34     6844  35439   7809  -2982   1492   4286  B    C  
ATOM   5116  O   SER A  34     -43.141  13.803   3.705  1.00131.55      B    O  
ANISOU 5116  O   SER A  34     6787  35228   7967  -2638   1537   5184  B    O  
ATOM   5117  CB  SER A  34     -44.456  13.623   1.161  1.00131.87      B    C  
ANISOU 5117  CB  SER A  34     7063  35175   7866  -2653   1353   4712  B    C  
ATOM   5118  OG  SER A  34     -43.405  13.350   0.251  1.00136.99      B    O  
ANISOU 5118  OG  SER A  34     8147  35256   8648  -2699   1414   4252  B    O  
ATOM   5119  N   THR A  35     -43.068  11.552   3.905  1.00129.50      B    N  
ANISOU 5119  N   THR A  35     6356  35616   7231  -3424   1542   3504  B    N  
ATOM   5120  CA  THR A  35     -42.110  11.557   5.016  1.00129.17      B    C  
ANISOU 5120  CA  THR A  35     6244  35637   7197  -3498   1638   3570  B    C  
ATOM   5121  C   THR A  35     -40.677  11.310   4.519  1.00131.99      B    C  
ANISOU 5121  C   THR A  35     6820  35787   7545  -3625   1728   3181  B    C  
ATOM   5122  O   THR A  35     -40.428  10.345   3.796  1.00131.98      B    O  
ANISOU 5122  O   THR A  35     6889  35863   7393  -3957   1755   2296  B    O  
ATOM   5123  CB  THR A  35     -42.503  10.526   6.094  1.00135.69      B    C  
ANISOU 5123  CB  THR A  35     7350  35848   8360  -3727   1686   2702  B    C  
ATOM   5124  CG2 THR A  35     -41.669  10.657   7.354  1.00135.86      B    C  
ANISOU 5124  CG2 THR A  35     7318  35871   8433  -3751   1767   2893  B    C  
ATOM   5125  OG1 THR A  35     -43.903  10.593   6.416  1.00133.39      B    O  
ANISOU 5125  OG1 THR A  35     6897  35699   8087  -3653   1604   2894  B    O  
ATOM   5126  N   SER A  36     -39.744  12.192   4.920  1.00129.13      B    N  
ANISOU 5126  N   SER A  36     6284  35656   7124  -3429   1778   3981  B    N  
ATOM   5127  CA  SER A  36     -38.316  12.104   4.603  1.00128.51      B    C  
ANISOU 5127  CA  SER A  36     6236  35685   6906  -3567   1863   3791  B    C  
ATOM   5128  C   SER A  36     -37.595  11.709   5.886  1.00130.07      B    C  
ANISOU 5128  C   SER A  36     6458  35766   7196  -3754   1941   3492  B    C  
ATOM   5129  O   SER A  36     -37.480  12.524   6.805  1.00129.42      B    O  
ANISOU 5129  O   SER A  36     6276  35592   7304  -3449   1949   4383  B    O  
ATOM   5130  CB  SER A  36     -37.800  13.429   4.045  1.00130.59      B    C  
ANISOU 5130  CB  SER A  36     6662  35507   7450  -3079   1890   4795  B    C  
ATOM   5131  OG  SER A  36     -38.677  13.962   3.067  1.00136.17      B    O  
ANISOU 5131  OG  SER A  36     7733  35531   8475  -2790   1832   4948  B    O  
ATOM   5132  N   LEU A  37     -37.190  10.442   5.985  1.00127.02      B    N  
ANISOU 5132  N   LEU A  37     5945  35843   6474  -4361   2010   2292  B    N  
ATOM   5133  CA  LEU A  37     -36.548   9.916   7.187  1.00125.98      B    C  
ANISOU 5133  CA  LEU A  37     5741  35839   6288  -4723   2105   1752  B    C  
ATOM   5134  C   LEU A  37     -35.020   9.836   7.023  1.00127.10      B    C  
ANISOU 5134  C   LEU A  37     6015  35847   6428  -4880   2211   1448  B    C  
ATOM   5135  O   LEU A  37     -34.527   9.310   6.023  1.00126.44      B    O  
ANISOU 5135  O   LEU A  37     5991  35827   6223  -5108   2273    803  B    O  
ATOM   5136  CB  LEU A  37     -37.122   8.524   7.553  1.00125.72      B    C  
ANISOU 5136  CB  LEU A  37     5750  35753   6264  -5267   2198    385  B    C  
ATOM   5137  CG  LEU A  37     -38.654   8.395   7.718  1.00129.31      B    C  
ANISOU 5137  CG  LEU A  37     6313  35841   6976  -5073   2110    476  B    C  
ATOM   5138  CD1 LEU A  37     -39.326   7.975   6.414  1.00130.02      B    C  
ANISOU 5138  CD1 LEU A  37     6488  35832   7081  -5061   2060    152  B    C  
ATOM   5139  CD2 LEU A  37     -38.995   7.359   8.736  1.00130.18      B    C  
ANISOU 5139  CD2 LEU A  37     6506  35680   7276  -5479   2238   -517  B    C  
ATOM   5140  N   THR A  38     -34.286  10.378   8.009  1.00123.98      B    N  
ANISOU 5140  N   THR A  38     5399  35790   5917  -4865   2225   2003  B    N  
ATOM   5141  CA  THR A  38     -32.831  10.308   8.087  1.00123.48      B    C  
ANISOU 5141  CA  THR A  38     5373  35759   5783  -5090   2326   1712  B    C  
ATOM   5142  C   THR A  38     -32.522   9.048   8.881  1.00125.42      B    C  
ANISOU 5142  C   THR A  38     5892  35545   6215  -5715   2504    167  B    C  
ATOM   5143  O   THR A  38     -32.808   8.980  10.083  1.00118.11      B    O  
ANISOU 5143  O   THR A  38     5701  32973   6202  -5371   2512    147  B    O  
ATOM   5144  CB  THR A  38     -32.254  11.585   8.691  1.00129.85      B    C  
ANISOU 5144  CB  THR A  38     6335  35959   7042  -4436   2279   3130  B    C  
ATOM   5145  CG2 THR A  38     -30.724  11.556   8.787  1.00123.22      B    C  
ANISOU 5145  CG2 THR A  38     5947  34296   6576  -4449   2384   2807  B    C  
ATOM   5146  OG1 THR A  38     -32.664  12.698   7.899  1.00129.09      B    O  
ANISOU 5146  OG1 THR A  38     6178  35759   7112  -3825   2219   4351  B    O  
ATOM   5147  N   VAL A  39     -31.986   8.035   8.193  1.00122.79      B    N  
ANISOU 5147  N   VAL A  39     5606  35244   5806  -6238   2682  -1117  B    N  
ATOM   5148  CA  VAL A  39     -31.710   6.729   8.782  1.00122.06      B    C  
ANISOU 5148  CA  VAL A  39     5743  34590   6046  -6881   2974  -2739  B    C  
ATOM   5149  C   VAL A  39     -30.209   6.565   9.064  1.00121.07      B    C  
ANISOU 5149  C   VAL A  39     6296  33052   6653  -6792   3127  -3117  B    C  
ATOM   5150  O   VAL A  39     -29.392   6.719   8.159  1.00124.92      B    O  
ANISOU 5150  O   VAL A  39     6439  34386   6641  -7002   3158  -3144  B    O  
ATOM   5151  CB  VAL A  39     -32.268   5.593   7.873  1.00125.24      B    C  
ANISOU 5151  CB  VAL A  39     6344  34462   6781  -6991   3073  -3643  B    C  
ATOM   5152  CG1 VAL A  39     -31.943   4.209   8.429  1.00124.32      B    C  
ANISOU 5152  CG1 VAL A  39     6441  33582   7212  -7582   3457  -5227  B    C  
ATOM   5153  CG2 VAL A  39     -33.775   5.749   7.677  1.00125.58      B    C  
ANISOU 5153  CG2 VAL A  39     6254  34750   6712  -6709   2881  -3120  B    C  
ATOM   5154  N   ARG A  40     -29.860   6.242  10.325  1.00109.29      B    N  
ANISOU 5154  N   ARG A  40     5727  29480   6318  -6484   3224  -3385  B    N  
ATOM   5155  CA  ARG A  40     -28.480   5.990  10.736  1.00103.44      B    C  
ANISOU 5155  CA  ARG A  40     5649  27292   6359  -6385   3380  -3763  B    C  
ATOM   5156  C   ARG A  40     -28.304   4.498  10.992  1.00108.40      B    C  
ANISOU 5156  C   ARG A  40     6430  27235   7523  -6945   3778  -5296  B    C  
ATOM   5157  O   ARG A  40     -28.958   3.949  11.886  1.00104.67      B    O  
ANISOU 5157  O   ARG A  40     6275  25854   7641  -6886   3874  -5612  B    O  
ATOM   5158  CB  ARG A  40     -28.086   6.818  11.975  1.00 93.05      B    C  
ANISOU 5158  CB  ARG A  40     5191  24210   5954  -5585   3214  -2800  B    C  
ATOM   5159  CG  ARG A  40     -26.617   6.631  12.376  1.00 93.59      B    C  
ANISOU 5159  CG  ARG A  40     5890  22907   6764  -5466   3348  -3111  B    C  
ATOM   5160  CD  ARG A  40     -25.972   7.923  12.835  1.00 88.07      B    C  
ANISOU 5160  CD  ARG A  40     5615  21431   6415  -4781   3142  -1930  B    C  
ATOM   5161  NE  ARG A  40     -25.907   8.033  14.290  1.00 87.53      B    N  
ANISOU 5161  NE  ARG A  40     6318  19649   7289  -4316   3117  -1735  B    N  
ATOM   5162  CZ  ARG A  40     -26.090   9.160  14.971  1.00 93.06      B    C  
ANISOU 5162  CZ  ARG A  40     7297  19753   8309  -3725   2949   -717  B    C  
ATOM   5163  NH1 ARG A  40     -26.387  10.287  14.336  1.00 70.06      B    N1+
ANISOU 5163  NH1 ARG A  40     3953  17713   4953  -3475   2821    292  B    N1+
ATOM   5164  NH2 ARG A  40     -26.001   9.164  16.292  1.00 84.23      B    N  
ANISOU 5164  NH2 ARG A  40     6826  17198   7978  -3390   2950   -695  B    N  
ATOM   5165  N   SER A  41     -27.426   3.847  10.202  1.00109.68      B    N  
ANISOU 5165  N   SER A  41     6327  27812   7535  -7484   4055  -6225  B    N  
ATOM   5166  CA  SER A  41     -27.125   2.422  10.317  1.00111.54      B    C  
ANISOU 5166  CA  SER A  41     6603  27386   8392  -8055   4552  -7713  B    C  
ATOM   5167  C   SER A  41     -26.276   2.150  11.564  1.00111.33      B    C  
ANISOU 5167  C   SER A  41     7493  25160   9649  -7603   4675  -7653  B    C  
ATOM   5168  O   SER A  41     -25.291   2.847  11.811  1.00105.43      B    O  
ANISOU 5168  O   SER A  41     7197  23715   9148  -7152   4499  -6957  B    O  
ATOM   5169  CB  SER A  41     -26.428   1.921   9.059  1.00120.92      B    C  
ANISOU 5169  CB  SER A  41     7178  29732   9035  -8758   4836  -8666  B    C  
ATOM   5170  OG  SER A  41     -25.962   0.587   9.185  1.00125.35      B    O  
ANISOU 5170  OG  SER A  41     8035  28989  10605  -8960   5267  -9716  B    O  
ATOM   5171  N   LEU A  42     -26.694   1.155  12.366  1.00110.56      B    N  
ANISOU 5171  N   LEU A  42     7617  24033  10356  -7716   4987  -8333  B    N  
ATOM   5172  CA  LEU A  42     -26.016   0.738  13.599  1.00104.97      B    C  
ANISOU 5172  CA  LEU A  42     7658  21366  10859  -7326   5154  -8293  B    C  
ATOM   5173  C   LEU A  42     -25.274  -0.591  13.371  1.00115.32      B    C  
ANISOU 5173  C   LEU A  42     8823  22113  12881  -7873   5781  -9568  B    C  
ATOM   5174  O   LEU A  42     -24.434  -0.981  14.185  1.00110.26      B    O  
ANISOU 5174  O   LEU A  42     8690  19980  13224  -7597   5978  -9537  B    O  
ATOM   5175  CB  LEU A  42     -27.042   0.622  14.749  1.00101.02      B    C  
ANISOU 5175  CB  LEU A  42     7485  20068  10830  -6983   5081  -7966  B    C  
ATOM   5176  CG  LEU A  42     -27.197   1.830  15.683  1.00 98.67      B    C  
ANISOU 5176  CG  LEU A  42     7756  19161  10573  -6192   4587  -6625  B    C  
ATOM   5177  CD1 LEU A  42     -27.758   3.056  14.959  1.00101.07      B    C  
ANISOU 5177  CD1 LEU A  42     7707  20833   9861  -6047   4164  -5782  B    C  
ATOM   5178  CD2 LEU A  42     -28.111   1.493  16.845  1.00 97.80      B    C  
ANISOU 5178  CD2 LEU A  42     7967  18143  11049  -5935   4618  -6514  B    C  
ATOM   5179  N   GLN A  43     -25.546  -1.237  12.221  1.00122.98      B    N  
ANISOU 5179  N   GLN A  43     9035  24362  13331  -8658   6114 -10664  B    N  
ATOM   5180  CA  GLN A  43     -24.954  -2.504  11.798  1.00127.79      B    C  
ANISOU 5180  CA  GLN A  43     9397  24560  14597  -9202   6737 -11896  B    C  
ATOM   5181  C   GLN A  43     -23.968  -2.271  10.659  1.00131.62      B    C  
ANISOU 5181  C   GLN A  43     9918  25429  14662  -8999   6419 -11471  B    C  
ATOM   5182  O   GLN A  43     -24.168  -1.382   9.826  1.00132.00      B    O  
ANISOU 5182  O   GLN A  43     9714  26789  13649  -8924   5985 -10883  B    O  
ATOM   5183  CB  GLN A  43     -26.052  -3.499  11.380  1.00129.01      B    C  
ANISOU 5183  CB  GLN A  43     9451  24703  14864  -9058   6602 -11905  B    C  
ATOM   5184  CG  GLN A  43     -25.691  -4.951  11.671  1.00142.29      B    C  
ANISOU 5184  CG  GLN A  43    11772  24482  17809  -8367   6520 -11443  B    C  
ATOM   5185  CD  GLN A  43     -26.896  -5.857  11.653  1.00159.63      B    C  
ANISOU 5185  CD  GLN A  43    14412  25984  20257  -7541   5911 -10373  B    C  
ATOM   5186  NE2 GLN A  43     -27.543  -6.010  12.802  1.00154.66      B    N  
ANISOU 5186  NE2 GLN A  43    13733  24908  20124  -7749   6297 -10805  B    N  
ATOM   5187  OE1 GLN A  43     -27.248  -6.446  10.624  1.00158.16      B    O  
ANISOU 5187  OE1 GLN A  43    14042  26245  19805  -7583   5783 -10437  B    O  
ATOM   5188  N   ASP A  44     -22.906  -3.087  10.636  1.00129.32      B    N  
ANISOU 5188  N   ASP A  44     9778  24148  15209  -9103   6810 -12010  B    N  
ATOM   5189  CA  ASP A  44     -21.815  -3.034   9.676  1.00130.12      B    C  
ANISOU 5189  CA  ASP A  44     9882  24461  15097  -9061   6695 -11905  B    C  
ATOM   5190  C   ASP A  44     -22.252  -3.160   8.206  1.00134.87      B    C  
ANISOU 5190  C   ASP A  44    10369  25922  14955  -8726   6133 -11270  B    C  
ATOM   5191  O   ASP A  44     -21.671  -2.477   7.358  1.00136.01      B    O  
ANISOU 5191  O   ASP A  44    10427  26789  14460  -8648   5884 -10878  B    O  
ATOM   5192  CB  ASP A  44     -20.776  -4.115   9.995  1.00130.21      B    C  
ANISOU 5192  CB  ASP A  44    10175  22986  16312  -9017   7113 -12326  B    C  
ATOM   5193  CG  ASP A  44     -19.405  -3.550  10.296  1.00136.28      B    C  
ANISOU 5193  CG  ASP A  44    11320  23089  17372  -8772   7088 -11954  B    C  
ATOM   5194  OD1 ASP A  44     -18.961  -2.650   9.555  1.00137.51      B    O  
ANISOU 5194  OD1 ASP A  44    11376  24159  16711  -8767   6787 -11621  B    O  
ATOM   5195  OD2 ASP A  44     -18.776  -4.008  11.272  1.00139.63      B    O1-
ANISOU 5195  OD2 ASP A  44    12123  22071  18860  -8554   7372 -11932  B    O1-
ATOM   5196  N   SER A  45     -23.235  -4.028   7.900  1.00132.31      B    N  
ANISOU 5196  N   SER A  45     9893  25659  14718  -8767   6138 -11493  B    N  
ATOM   5197  CA  SER A  45     -23.699  -4.226   6.524  1.00133.08      B    C  
ANISOU 5197  CA  SER A  45     9816  26537  14211  -8620   5792 -11165  B    C  
ATOM   5198  C   SER A  45     -25.223  -4.419   6.472  1.00136.12      B    C  
ANISOU 5198  C   SER A  45    10172  27135  14411  -8396   5528 -10803  B    C  
ATOM   5199  O   SER A  45     -25.720  -5.552   6.488  1.00135.27      B    O  
ANISOU 5199  O   SER A  45    10105  26413  14878  -8444   5700 -11179  B    O  
ATOM   5200  CB  SER A  45     -22.974  -5.404   5.876  1.00135.02      B    C  
ANISOU 5200  CB  SER A  45    10245  26008  15048  -8514   5877 -11355  B    C  
ATOM   5201  OG  SER A  45     -23.224  -6.610   6.579  1.00140.29      B    O  
ANISOU 5201  OG  SER A  45    11262  25343  16699  -8258   5975 -11350  B    O  
ATOM   5202  N   LEU A  46     -25.959  -3.296   6.404  1.00134.61      B    N  
ANISOU 5202  N   LEU A  46     9725  28086  13334  -8369   5247 -10324  B    N  
ATOM   5203  CA  LEU A  46     -27.416  -3.287   6.352  1.00134.98      B    C  
ANISOU 5203  CA  LEU A  46     9637  28556  13094  -8260   5046 -10061  B    C  
ATOM   5204  C   LEU A  46     -27.937  -3.357   4.925  1.00138.52      B    C  
ANISOU 5204  C   LEU A  46    10070  29448  13114  -7925   4675  -9476  B    C  
ATOM   5205  O   LEU A  46     -27.567  -2.535   4.085  1.00138.91      B    O  
ANISOU 5205  O   LEU A  46    10030  30178  12570  -7776   4457  -8957  B    O  
ATOM   5206  CB  LEU A  46     -27.977  -2.038   7.039  1.00135.67      B    C  
ANISOU 5206  CB  LEU A  46     9619  29275  12655  -8185   4864  -9539  B    C  
ATOM   5207  CG  LEU A  46     -28.542  -2.221   8.437  1.00138.44      B    C  
ANISOU 5207  CG  LEU A  46    10183  28819  13598  -8181   5032  -9729  B    C  
ATOM   5208  CD1 LEU A  46     -28.959  -0.897   9.000  1.00139.46      B    C  
ANISOU 5208  CD1 LEU A  46    10217  29625  13148  -8094   4828  -9129  B    C  
ATOM   5209  CD2 LEU A  46     -29.755  -3.154   8.439  1.00140.06      B    C  
ANISOU 5209  CD2 LEU A  46    10415  28665  14135  -8086   5013  -9841  B    C  
ATOM   5210  N   ALA A  47     -28.819  -4.331   4.664  1.00135.99      B    N  
ANISOU 5210  N   ALA A  47     9655  29015  13001  -8035   4743  -9844  B    N  
ATOM   5211  CA  ALA A  47     -29.434  -4.516   3.356  1.00136.47      B    C  
ANISOU 5211  CA  ALA A  47     9630  29524  12697  -7875   4502  -9547  B    C  
ATOM   5212  C   ALA A  47     -30.922  -4.161   3.381  1.00139.96      B    C  
ANISOU 5212  C   ALA A  47    10070  30194  12914  -7605   4226  -9002  B    C  
ATOM   5213  O   ALA A  47     -31.435  -3.674   2.377  1.00140.93      B    O  
ANISOU 5213  O   ALA A  47    10116  30858  12573  -7404   3968  -8517  B    O  
ATOM   5214  CB  ALA A  47     -29.249  -5.951   2.890  1.00136.20      B    C  
ANISOU 5214  CB  ALA A  47     9712  28783  13255  -7966   4679 -10064  B    C  
ATOM   5215  N   SER A  48     -31.615  -4.411   4.513  1.00136.79      B    N  
ANISOU 5215  N   SER A  48     9565  29676  12734  -7824   4404  -9375  B    N  
ATOM   5216  CA  SER A  48     -33.057  -4.169   4.651  1.00136.94      B    C  
ANISOU 5216  CA  SER A  48     9454  30071  12506  -7730   4232  -9086  B    C  
ATOM   5217  C   SER A  48     -33.389  -3.087   5.688  1.00139.04      B    C  
ANISOU 5217  C   SER A  48     9723  30568  12537  -7589   4116  -8598  B    C  
ATOM   5218  O   SER A  48     -32.582  -2.805   6.571  1.00138.20      B    O  
ANISOU 5218  O   SER A  48     9666  30282  12563  -7730   4290  -8791  B    O  
ATOM   5219  CB  SER A  48     -33.777  -5.459   5.029  1.00139.15      B    C  
ANISOU 5219  CB  SER A  48     9899  29470  13500  -7746   4380  -9486  B    C  
ATOM   5220  OG  SER A  48     -33.341  -6.578   4.272  1.00145.13      B    O  
ANISOU 5220  OG  SER A  48    10987  29416  14740  -7493   4310  -9401  B    O  
ATOM   5221  N   LEU A  49     -34.598  -2.504   5.581  1.00137.19      B    N  
ANISOU 5221  N   LEU A  49     9250  31055  11820  -7517   3913  -8202  B    N  
ATOM   5222  CA  LEU A  49     -35.118  -1.462   6.470  1.00137.29      B    C  
ANISOU 5222  CA  LEU A  49     9149  31528  11488  -7427   3792  -7713  B    C  
ATOM   5223  C   LEU A  49     -36.565  -1.788   6.870  1.00140.32      B    C  
ANISOU 5223  C   LEU A  49     9579  31663  12074  -7278   3698  -7577  B    C  
ATOM   5224  O   LEU A  49     -37.464  -1.695   6.030  1.00140.66      B    O  
ANISOU 5224  O   LEU A  49     9519  32090  11834  -7104   3480  -7195  B    O  
ATOM   5225  CB  LEU A  49     -35.032  -0.099   5.757  1.00138.19      B    C  
ANISOU 5225  CB  LEU A  49     9143  32459  10905  -7106   3471  -6729  B    C  
ATOM   5226  CG  LEU A  49     -34.450   1.068   6.549  1.00141.46      B    C  
ANISOU 5226  CG  LEU A  49     9639  32950  11159  -6900   3381  -6087  B    C  
ATOM   5227  CD1 LEU A  49     -32.937   0.941   6.705  1.00140.71      B    C  
ANISOU 5227  CD1 LEU A  49     9660  32565  11238  -7099   3583  -6494  B    C  
ATOM   5228  CD2 LEU A  49     -34.782   2.381   5.883  1.00144.44      B    C  
ANISOU 5228  CD2 LEU A  49     9967  33853  11059  -6419   3049  -4897  B    C  
ATOM   5229  N   ILE A  50     -36.779  -2.196   8.144  1.00137.61      B    N  
ANISOU 5229  N   ILE A  50     9203  30996  12087  -7568   3971  -8169  B    N  
ATOM   5230  CA  ILE A  50     -38.096  -2.585   8.694  1.00137.65      B    C  
ANISOU 5230  CA  ILE A  50     9152  30882  12268  -7581   3983  -8271  B    C  
ATOM   5231  C   ILE A  50     -38.738  -1.459   9.523  1.00140.51      B    C  
ANISOU 5231  C   ILE A  50     9489  31592  12307  -7343   3776  -7554  B    C  
ATOM   5232  O   ILE A  50     -38.196  -1.043  10.550  1.00139.80      B    O  
ANISOU 5232  O   ILE A  50     9432  31410  12275  -7475   3923  -7678  B    O  
ATOM   5233  CB  ILE A  50     -38.041  -3.907   9.517  1.00138.88      B    C  
ANISOU 5233  CB  ILE A  50     9557  29851  13358  -7748   4349  -9047  B    C  
ATOM   5234  CG1 ILE A  50     -36.778  -3.974  10.427  1.00138.53      B    C  
ANISOU 5234  CG1 ILE A  50     9706  29137  13790  -7922   4676  -9496  B    C  
ATOM   5235  CG2 ILE A  50     -38.144  -5.115   8.578  1.00139.07      B    C  
ANISOU 5235  CG2 ILE A  50     9647  29455  13738  -7759   4397  -9360  B    C  
ATOM   5236  CD1 ILE A  50     -36.727  -5.097  11.475  1.00142.77      B    C  
ANISOU 5236  CD1 ILE A  50    10616  28228  15404  -7878   5001  -9918  B    C  
ATOM   5237  N   LEU A  51     -39.911  -0.990   9.075  1.00139.07      B    N  
ANISOU 5237  N   LEU A  51     9060  32132  11648  -7193   3519  -7027  B    N  
ATOM   5238  CA  LEU A  51     -40.677   0.059   9.753  1.00139.73      B    C  
ANISOU 5238  CA  LEU A  51     9004  32729  11359  -6996   3324  -6316  B    C  
ATOM   5239  C   LEU A  51     -42.089  -0.415  10.087  1.00143.04      B    C  
ANISOU 5239  C   LEU A  51     9506  32741  12099  -6859   3274  -6295  B    C  
ATOM   5240  O   LEU A  51     -42.621  -1.293   9.403  1.00142.71      B    O  
ANISOU 5240  O   LEU A  51     9474  32480  12269  -6915   3297  -6636  B    O  
ATOM   5241  CB  LEU A  51     -40.760   1.336   8.896  1.00140.62      B    C  
ANISOU 5241  CB  LEU A  51     8985  33574  10869  -6602   2976  -5217  B    C  
ATOM   5242  CG  LEU A  51     -39.460   2.035   8.519  1.00143.62      B    C  
ANISOU 5242  CG  LEU A  51     9540  33873  11157  -6399   2914  -4773  B    C  
ATOM   5243  CD1 LEU A  51     -39.722   3.100   7.493  1.00144.42      B    C  
ANISOU 5243  CD1 LEU A  51     9561  34457  10857  -5993   2635  -3787  B    C  
ATOM   5244  CD2 LEU A  51     -38.771   2.640   9.736  1.00145.14      B    C  
ANISOU 5244  CD2 LEU A  51     9803  33978  11364  -6392   2970  -4558  B    C  
ATOM   5245  N   ASP A  52     -42.710   0.203  11.107  1.00141.47      B    N  
ANISOU 5245  N   ASP A  52     9145  32905  11703  -6868   3248  -6037  B    N  
ATOM   5246  CA  ASP A  52     -44.070  -0.109  11.550  1.00141.71      B    C  
ANISOU 5246  CA  ASP A  52     9107  32858  11878  -6852   3234  -6082  B    C  
ATOM   5247  C   ASP A  52     -45.131   0.692  10.786  1.00146.09      B    C  
ANISOU 5247  C   ASP A  52     9653  33683  12173  -6351   2851  -5039  B    C  
ATOM   5248  O   ASP A  52     -44.979   1.901  10.607  1.00145.81      B    O  
ANISOU 5248  O   ASP A  52     9496  34205  11699  -6083   2643  -4175  B    O  
ATOM   5249  CB  ASP A  52     -44.220   0.165  13.057  1.00142.55      B    C  
ANISOU 5249  CB  ASP A  52     9270  32738  12153  -6920   3366  -6149  B    C  
ATOM   5250  CG  ASP A  52     -43.405  -0.710  13.987  1.00146.82      B    C  
ANISOU 5250  CG  ASP A  52    10289  31934  13562  -7026   3707  -6868  B    C  
ATOM   5251  OD1 ASP A  52     -43.099  -0.257  15.094  1.00146.94      B    O  
ANISOU 5251  OD1 ASP A  52    10369  31819  13643  -7109   3832  -6910  B    O  
ATOM   5252  OD2 ASP A  52     -43.159  -1.889  13.644  1.00149.46      B    O1-
ANISOU 5252  OD2 ASP A  52    10913  31340  14537  -7023   3862  -7358  B    O1-
ATOM   5253  N   THR A  53     -46.206   0.001  10.341  1.00145.08      B    N  
ANISOU 5253  N   THR A  53     9441  33518  12163  -6410   2836  -5297  B    N  
ATOM   5254  CA  THR A  53     -47.381   0.565   9.650  1.00146.22      B    C  
ANISOU 5254  CA  THR A  53     9479  34000  12078  -6102   2560  -4596  B    C  
ATOM   5255  C   THR A  53     -48.644  -0.123  10.160  1.00149.73      B    C  
ANISOU 5255  C   THR A  53    10045  33872  12974  -6066   2591  -4805  B    C  
ATOM   5256  O   THR A  53     -48.582  -1.292  10.540  1.00149.05      B    O  
ANISOU 5256  O   THR A  53    10039  33288  13304  -6355   2835  -5617  B    O  
ATOM   5257  CB  THR A  53     -47.306   0.446   8.102  1.00153.44      B    C  
ANISOU 5257  CB  THR A  53    10740  34351  13207  -5749   2371  -4261  B    C  
ATOM   5258  CG2 THR A  53     -46.053   1.070   7.493  1.00153.19      B    C  
ANISOU 5258  CG2 THR A  53    10749  34548  12907  -5652   2324  -3949  B    C  
ATOM   5259  OG1 THR A  53     -47.461  -0.916   7.694  1.00153.42      B    O  
ANISOU 5259  OG1 THR A  53    10823  33914  13558  -5986   2510  -5014  B    O  
ATOM   5260  N   LYS A  54     -49.785   0.582  10.147  1.00148.49      B    N  
ANISOU 5260  N   LYS A  54     9674  34198  12546  -5883   2402  -4221  B    N  
ATOM   5261  CA  LYS A  54     -51.083   0.038  10.557  1.00148.75      B    C  
ANISOU 5261  CA  LYS A  54     9652  34056  12812  -5933   2425  -4425  B    C  
ATOM   5262  C   LYS A  54     -52.170   0.727   9.741  1.00152.25      B    C  
ANISOU 5262  C   LYS A  54    10140  34504  13205  -5514   2131  -3621  B    C  
ATOM   5263  O   LYS A  54     -52.372   1.932   9.897  1.00152.12      B    O  
ANISOU 5263  O   LYS A  54    10018  34862  12919  -5244   1980  -2840  B    O  
ATOM   5264  CB  LYS A  54     -51.312   0.206  12.076  1.00150.46      B    C  
ANISOU 5264  CB  LYS A  54     9912  34040  13216  -5948   2544  -4445  B    C  
ATOM   5265  CG  LYS A  54     -52.416  -0.691  12.633  1.00160.56      B    C  
ANISOU 5265  CG  LYS A  54    11612  34098  15297  -5735   2577  -4567  B    C  
ATOM   5266  CD  LYS A  54     -52.859  -0.288  14.035  1.00166.35      B    C  
ANISOU 5266  CD  LYS A  54    12549  34336  16322  -5508   2593  -4227  B    C  
ATOM   5267  CE  LYS A  54     -54.036  -1.116  14.493  1.00172.71      B    C  
ANISOU 5267  CE  LYS A  54    13624  34247  17752  -5360   2621  -4329  B    C  
ATOM   5268  NZ  LYS A  54     -54.598  -0.637  15.780  1.00177.67      B    N1+
ANISOU 5268  NZ  LYS A  54    14433  34440  18633  -5124   2623  -3958  B    N1+
ATOM   5269  N   ASP A  55     -52.823  -0.022   8.825  1.00150.44      B    N  
ANISOU 5269  N   ASP A  55     9845  34292  13025  -5626   2095  -3939  B    N  
ATOM   5270  CA  ASP A  55     -53.885   0.459   7.926  1.00151.38      B    C  
ANISOU 5270  CA  ASP A  55     9911  34570  13037  -5374   1859  -3410  B    C  
ATOM   5271  C   ASP A  55     -53.395   1.663   7.091  1.00155.36      B    C  
ANISOU 5271  C   ASP A  55    10614  35001  13415  -4961   1663  -2603  B    C  
ATOM   5272  O   ASP A  55     -54.142   2.613   6.846  1.00155.47      B    O  
ANISOU 5272  O   ASP A  55    10548  35229  13296  -4694   1495  -1950  B    O  
ATOM   5273  CB  ASP A  55     -55.177   0.798   8.707  1.00152.97      B    C  
ANISOU 5273  CB  ASP A  55    10040  34719  13362  -5225   1796  -3084  B    C  
ATOM   5274  CG  ASP A  55     -55.722  -0.337   9.554  1.00157.66      B    C  
ANISOU 5274  CG  ASP A  55    10905  34408  14591  -5296   1949  -3600  B    C  
ATOM   5275  OD1 ASP A  55     -55.923  -1.444   9.007  1.00157.62      B    O  
ANISOU 5275  OD1 ASP A  55    10963  34103  14823  -5465   2008  -4115  B    O  
ATOM   5276  OD2 ASP A  55     -55.976  -0.110  10.755  1.00160.80      B    O1-
ANISOU 5276  OD2 ASP A  55    11422  34450  15226  -5185   2012  -3453  B    O1-
ATOM   5277  N   LEU A  56     -52.119   1.599   6.672  1.00153.76      B    N  
ANISOU 5277  N   LEU A  56    10440  34941  13040  -5076   1732  -2789  B    N  
ATOM   5278  CA  LEU A  56     -51.424   2.592   5.858  1.00154.32      B    C  
ANISOU 5278  CA  LEU A  56    10575  35190  12868  -4831   1613  -2210  B    C  
ATOM   5279  C   LEU A  56     -51.241   2.085   4.445  1.00158.42      B    C  
ANISOU 5279  C   LEU A  56    11390  35215  13586  -4748   1543  -2373  B    C  
ATOM   5280  O   LEU A  56     -50.967   0.898   4.245  1.00157.71      B    O  
ANISOU 5280  O   LEU A  56    11341  34928  13655  -5014   1657  -3056  B    O  
ATOM   5281  CB  LEU A  56     -50.034   2.887   6.451  1.00153.77      B    C  
ANISOU 5281  CB  LEU A  56    10542  35190  12692  -4890   1734  -2216  B    C  
ATOM   5282  CG  LEU A  56     -49.798   4.160   7.267  1.00157.05      B    C  
ANISOU 5282  CG  LEU A  56    11050  35502  13118  -4546   1682  -1412  B    C  
ATOM   5283  CD1 LEU A  56     -48.319   4.333   7.515  1.00156.38      B    C  
ANISOU 5283  CD1 LEU A  56    11020  35470  12927  -4627   1788  -1481  B    C  
ATOM   5284  CD2 LEU A  56     -50.301   5.405   6.552  1.00159.62      B    C  
ANISOU 5284  CD2 LEU A  56    11466  35760  13422  -4111   1497   -534  B    C  
ATOM   5285  N   THR A  57     -51.340   2.987   3.469  1.00157.63      B    N  
ANISOU 5285  N   THR A  57    11259  35400  13234  -4530   1387  -1828  B    N  
ATOM   5286  CA  THR A  57     -51.113   2.651   2.071  1.00158.34      B    C  
ANISOU 5286  CA  THR A  57    11485  35374  13303  -4523   1320  -1968  B    C  
ATOM   5287  C   THR A  57     -49.806   3.328   1.661  1.00161.93      B    C  
ANISOU 5287  C   THR A  57    12212  35553  13760  -4317   1335  -1650  B    C  
ATOM   5288  O   THR A  57     -49.703   4.553   1.735  1.00161.77      B    O  
ANISOU 5288  O   THR A  57    12165  35718  13582  -4076   1273   -999  B    O  
ATOM   5289  CB  THR A  57     -52.321   3.043   1.209  1.00165.89      B    C  
ANISOU 5289  CB  THR A  57    12778  35635  14616  -4139   1116  -1533  B    C  
ATOM   5290  CG2 THR A  57     -52.168   2.610  -0.247  1.00165.78      B    C  
ANISOU 5290  CG2 THR A  57    12867  35584  14536  -4170   1043  -1714  B    C  
ATOM   5291  OG1 THR A  57     -53.507   2.473   1.766  1.00165.95      B    O  
ANISOU 5291  OG1 THR A  57    12680  35564  14810  -4229   1104  -1745  B    O  
ATOM   5292  N   ILE A  58     -48.799   2.530   1.284  1.00160.10      B    N  
ANISOU 5292  N   ILE A  58    11986  35379  13464  -4562   1446  -2178  B    N  
ATOM   5293  CA  ILE A  58     -47.502   3.052   0.863  1.00160.32      B    C  
ANISOU 5293  CA  ILE A  58    12115  35461  13336  -4490   1483  -1994  B    C  
ATOM   5294  C   ILE A  58     -47.516   3.108  -0.668  1.00165.26      B    C  
ANISOU 5294  C   ILE A  58    13073  35622  14098  -4260   1363  -1830  B    C  
ATOM   5295  O   ILE A  58     -47.677   2.077  -1.326  1.00164.94      B    O  
ANISOU 5295  O   ILE A  58    13069  35454  14147  -4423   1368  -2309  B    O  
ATOM   5296  CB  ILE A  58     -46.319   2.227   1.458  1.00161.56      B    C  
ANISOU 5296  CB  ILE A  58    12398  35286  13702  -4699   1672  -2557  B    C  
ATOM   5297  CG1 ILE A  58     -46.293   2.327   2.997  1.00161.33      B    C  
ANISOU 5297  CG1 ILE A  58    12275  35262  13759  -4782   1777  -2610  B    C  
ATOM   5298  CG2 ILE A  58     -44.964   2.662   0.882  1.00161.84      B    C  
ANISOU 5298  CG2 ILE A  58    12549  35347  13597  -4634   1708  -2413  B    C  
ATOM   5299  CD1 ILE A  58     -46.808   1.106   3.702  1.00166.07      B    C  
ANISOU 5299  CD1 ILE A  58    13069  35133  14896  -4889   1870  -3165  B    C  
ATOM   5300  N   LYS A  59     -47.402   4.330  -1.221  1.00164.78      B    N  
ANISOU 5300  N   LYS A  59    13002  35810  13795  -4027   1274  -1208  B    N  
ATOM   5301  CA  LYS A  59     -47.417   4.578  -2.664  1.00165.93      B    C  
ANISOU 5301  CA  LYS A  59    13307  35872  13866  -3890   1173  -1045  B    C  
ATOM   5302  C   LYS A  59     -46.039   4.289  -3.268  1.00169.69      B    C  
ANISOU 5302  C   LYS A  59    14083  35930  14462  -3874   1261  -1242  B    C  
ATOM   5303  O   LYS A  59     -45.940   3.431  -4.148  1.00169.67      B    O  
ANISOU 5303  O   LYS A  59    14155  35826  14486  -3994   1254  -1638  B    O  
ATOM   5304  CB  LYS A  59     -47.865   6.015  -2.981  1.00168.35      B    C  
ANISOU 5304  CB  LYS A  59    13742  36044  14178  -3524   1061   -286  B    C  
ATOM   5305  CG  LYS A  59     -49.262   6.371  -2.497  1.00179.29      B    C  
ANISOU 5305  CG  LYS A  59    15590  36268  16263  -3151    955    -13  B    C  
ATOM   5306  CD  LYS A  59     -49.514   7.839  -2.764  1.00186.86      B    C  
ANISOU 5306  CD  LYS A  59    16981  36451  17566  -2706    893    628  B    C  
ATOM   5307  CE  LYS A  59     -50.604   8.432  -1.916  1.00194.34      B    C  
ANISOU 5307  CE  LYS A  59    18210  36586  19042  -2435    850    880  B    C  
ATOM   5308  NZ  LYS A  59     -50.879   9.833  -2.326  1.00200.49      B    N1+
ANISOU 5308  NZ  LYS A  59    19395  36646  20135  -2075    807   1358  B    N1+
ATOM   5309  N   LYS A  60     -44.980   4.989  -2.797  1.00167.69      B    N  
ANISOU 5309  N   LYS A  60    13733  35976  14004  -3866   1354  -1001  B    N  
ATOM   5310  CA  LYS A  60     -43.616   4.763  -3.271  1.00167.64      B    C  
ANISOU 5310  CA  LYS A  60    13824  35942  13928  -3945   1454  -1206  B    C  
ATOM   5311  C   LYS A  60     -42.586   5.082  -2.186  1.00170.43      B    C  
ANISOU 5311  C   LYS A  60    14269  36057  14431  -3904   1578  -1116  B    C  
ATOM   5312  O   LYS A  60     -42.852   5.868  -1.273  1.00170.00      B    O  
ANISOU 5312  O   LYS A  60    14107  36141  14343  -3793   1570   -698  B    O  
ATOM   5313  CB  LYS A  60     -43.308   5.543  -4.574  1.00170.14      B    C  
ANISOU 5313  CB  LYS A  60    14391  36058  14197  -3690   1385   -801  B    C  
ATOM   5314  CG  LYS A  60     -43.058   7.044  -4.444  1.00180.84      B    C  
ANISOU 5314  CG  LYS A  60    16328  36329  16054  -3145   1363    -42  B    C  
ATOM   5315  CD  LYS A  60     -42.197   7.534  -5.609  1.00187.76      B    C  
ANISOU 5315  CD  LYS A  60    17735  36417  17188  -2870   1382    144  B    C  
ATOM   5316  CE  LYS A  60     -41.951   9.025  -5.607  1.00194.89      B    C  
ANISOU 5316  CE  LYS A  60    19090  36502  18456  -2477   1411    727  B    C  
ATOM   5317  NZ  LYS A  60     -40.936   9.433  -4.600  1.00200.32      B    N1+
ANISOU 5317  NZ  LYS A  60    20033  36575  19505  -2355   1544    808  B    N1+
ATOM   5318  N   VAL A  61     -41.420   4.432  -2.289  1.00168.39      B    N  
ANISOU 5318  N   VAL A  61    13959  35939  14082  -4141   1704  -1574  B    N  
ATOM   5319  CA  VAL A  61     -40.270   4.603  -1.401  1.00168.10      B    C  
ANISOU 5319  CA  VAL A  61    13887  35943  14039  -4221   1835  -1620  B    C  
ATOM   5320  C   VAL A  61     -39.070   4.974  -2.279  1.00171.43      B    C  
ANISOU 5320  C   VAL A  61    14568  36077  14491  -4069   1873  -1457  B    C  
ATOM   5321  O   VAL A  61     -38.822   4.305  -3.285  1.00171.34      B    O  
ANISOU 5321  O   VAL A  61    14640  35982  14481  -4159   1882  -1806  B    O  
ATOM   5322  CB  VAL A  61     -39.987   3.355  -0.512  1.00170.08      B    C  
ANISOU 5322  CB  VAL A  61    14223  35749  14651  -4455   1961  -2322  B    C  
ATOM   5323  CG1 VAL A  61     -38.809   3.602   0.428  1.00169.33      B    C  
ANISOU 5323  CG1 VAL A  61    14089  35711  14540  -4551   2093  -2378  B    C  
ATOM   5324  CG2 VAL A  61     -41.221   2.942   0.285  1.00169.85      B    C  
ANISOU 5324  CG2 VAL A  61    14087  35688  14758  -4524   1929  -2464  B    C  
ATOM   5325  N   ALA A  62     -38.349   6.049  -1.912  1.00169.34      B    N  
ANISOU 5325  N   ALA A  62    14177  36177  13988  -3979   1907   -959  B    N  
ATOM   5326  CA  ALA A  62     -37.176   6.539  -2.637  1.00169.45      B    C  
ANISOU 5326  CA  ALA A  62    14284  36220  13880  -3903   1962   -769  B    C  
ATOM   5327  C   ALA A  62     -36.015   6.790  -1.681  1.00171.80      B    C  
ANISOU 5327  C   ALA A  62    14664  36280  14330  -3892   2078   -721  B    C  
ATOM   5328  O   ALA A  62     -36.144   7.582  -0.746  1.00171.37      B    O  
ANISOU 5328  O   ALA A  62    14501  36359  14251  -3791   2071   -282  B    O  
ATOM   5329  CB  ALA A  62     -37.518   7.812  -3.402  1.00170.70      B    C  
ANISOU 5329  CB  ALA A  62    14548  36352  13957  -3573   1874    -30  B    C  
ATOM   5330  N   VAL A  63     -34.899   6.082  -1.891  1.00169.28      B    N  
ANISOU 5330  N   VAL A  63    14291  36106  13922  -4141   2192  -1223  B    N  
ATOM   5331  CA  VAL A  63     -33.699   6.221  -1.070  1.00168.85      B    C  
ANISOU 5331  CA  VAL A  63    14199  36072  13882  -4240   2311  -1289  B    C  
ATOM   5332  C   VAL A  63     -32.647   6.960  -1.922  1.00172.40      B    C  
ANISOU 5332  C   VAL A  63    14909  36204  14390  -3984   2340   -879  B    C  
ATOM   5333  O   VAL A  63     -32.159   6.426  -2.921  1.00172.25      B    O  
ANISOU 5333  O   VAL A  63    14977  36123  14345  -4055   2373  -1193  B    O  
ATOM   5334  CB  VAL A  63     -33.210   4.875  -0.443  1.00170.69      B    C  
ANISOU 5334  CB  VAL A  63    14549  35846  14460  -4514   2429  -2136  B    C  
ATOM   5335  CG1 VAL A  63     -33.301   3.701  -1.418  1.00170.46      B    C  
ANISOU 5335  CG1 VAL A  63    14602  35625  14541  -4661   2449  -2722  B    C  
ATOM   5336  CG2 VAL A  63     -31.817   4.991   0.175  1.00170.08      B    C  
ANISOU 5336  CG2 VAL A  63    14457  35772  14395  -4641   2560  -2270  B    C  
ATOM   5337  N   ASN A  64     -32.376   8.232  -1.539  1.00170.63      B    N  
ANISOU 5337  N   ASN A  64    14555  36286  13989  -3816   2339   -174  B    N  
ATOM   5338  CA  ASN A  64     -31.472   9.219  -2.153  1.00171.16      B    C  
ANISOU 5338  CA  ASN A  64    14704  36348  13981  -3616   2383    353  B    C  
ATOM   5339  C   ASN A  64     -31.695   9.343  -3.694  1.00174.88      B    C  
ANISOU 5339  C   ASN A  64    15487  36411  14546  -3413   2343    434  B    C  
ATOM   5340  O   ASN A  64     -30.741   9.449  -4.472  1.00174.99      B    O  
ANISOU 5340  O   ASN A  64    15584  36414  14491  -3408   2414    419  B    O  
ATOM   5341  CB  ASN A  64     -29.990   8.970  -1.786  1.00171.59      B    C  
ANISOU 5341  CB  ASN A  64    14781  36329  14086  -3760   2513     78  B    C  
ATOM   5342  CG  ASN A  64     -29.366   7.704  -2.315  1.00187.57      B    C  
ANISOU 5342  CG  ASN A  64    17693  36510  17066  -3536   2559   -604  B    C  
ATOM   5343  ND2 ASN A  64     -28.732   7.796  -3.472  1.00182.37      B    N  
ANISOU 5343  ND2 ASN A  64    16862  36407  16022  -3649   2603   -628  B    N  
ATOM   5344  OD1 ASN A  64     -29.412   6.647  -1.681  1.00183.60      B    O  
ANISOU 5344  OD1 ASN A  64    16963  36298  16497  -3881   2592  -1234  B    O  
ATOM   5345  N   GLY A  65     -32.969   9.380  -4.091  1.00172.85      B    N  
ANISOU 5345  N   GLY A  65    15139  36369  14166  -3378   2227    542  B    N  
ATOM   5346  CA  GLY A  65     -33.392   9.510  -5.480  1.00173.44      B    C  
ANISOU 5346  CA  GLY A  65    15363  36366  14171  -3267   2167    622  B    C  
ATOM   5347  C   GLY A  65     -33.177   8.259  -6.304  1.00176.12      B    C  
ANISOU 5347  C   GLY A  65    15921  36335  14662  -3392   2177    -51  B    C  
ATOM   5348  O   GLY A  65     -32.340   8.241  -7.212  1.00176.06      B    O  
ANISOU 5348  O   GLY A  65    16010  36311  14573  -3394   2237   -115  B    O  
ATOM   5349  N   LYS A  66     -33.946   7.204  -5.980  1.00173.49      B    N  
ANISOU 5349  N   LYS A  66    15404  36220  14295  -3627   2128   -555  B    N  
ATOM   5350  CA  LYS A  66     -33.941   5.894  -6.641  1.00173.25      B    C  
ANISOU 5350  CA  LYS A  66    15420  36080  14325  -3825   2134  -1212  B    C  
ATOM   5351  C   LYS A  66     -35.282   5.201  -6.397  1.00175.89      B    C  
ANISOU 5351  C   LYS A  66    15836  36070  14922  -3816   2029  -1428  B    C  
ATOM   5352  O   LYS A  66     -35.771   5.214  -5.268  1.00175.24      B    O  
ANISOU 5352  O   LYS A  66    15614  36065  14904  -3878   2026  -1441  B    O  
ATOM   5353  CB  LYS A  66     -32.771   5.022  -6.129  1.00174.20      B    C  
ANISOU 5353  CB  LYS A  66    15585  35957  14645  -4016   2270  -1742  B    C  
ATOM   5354  CG  LYS A  66     -32.521   3.742  -6.936  1.00184.38      B    C  
ANISOU 5354  CG  LYS A  66    17444  36034  16577  -3853   2260  -2151  B    C  
ATOM   5355  CD  LYS A  66     -33.195   2.508  -6.317  1.00190.79      B    C  
ANISOU 5355  CD  LYS A  66    18506  36017  17968  -3822   2215  -2521  B    C  
ATOM   5356  CE  LYS A  66     -33.125   1.284  -7.201  1.00198.43      B    C  
ANISOU 5356  CE  LYS A  66    19915  36028  19450  -3661   2167  -2762  B    C  
ATOM   5357  NZ  LYS A  66     -34.064   1.366  -8.353  1.00205.28      B    N1+
ANISOU 5357  NZ  LYS A  66    21194  36238  20566  -3314   2003  -2433  B    N1+
ATOM   5358  N   ASP A  67     -35.858   4.567  -7.438  1.00173.98      B    N  
ANISOU 5358  N   ASP A  67    15571  35967  14567  -3897   1959  -1668  B    N  
ATOM   5359  CA  ASP A  67     -37.124   3.840  -7.320  1.00173.83      B    C  
ANISOU 5359  CA  ASP A  67    15496  35891  14659  -3976   1866  -1922  B    C  
ATOM   5360  C   ASP A  67     -36.872   2.508  -6.590  1.00175.80      B    C  
ANISOU 5360  C   ASP A  67    15801  35722  15274  -4170   1952  -2549  B    C  
ATOM   5361  O   ASP A  67     -36.638   1.472  -7.222  1.00175.39      B    O  
ANISOU 5361  O   ASP A  67    15801  35525  15316  -4308   1982  -2998  B    O  
ATOM   5362  CB  ASP A  67     -37.779   3.632  -8.700  1.00175.72      B    C  
ANISOU 5362  CB  ASP A  67    15930  35920  14914  -3855   1750  -1886  B    C  
ATOM   5363  CG  ASP A  67     -39.254   3.981  -8.734  1.00181.67      B    C  
ANISOU 5363  CG  ASP A  67    16969  36047  16009  -3557   1584  -1544  B    C  
ATOM   5364  OD1 ASP A  67     -40.056   3.235  -8.129  1.00181.47      B    O  
ANISOU 5364  OD1 ASP A  67    16850  35956  16146  -3670   1553  -1814  B    O  
ATOM   5365  OD2 ASP A  67     -39.609   4.988  -9.380  1.00185.83      B    O1-
ANISOU 5365  OD2 ASP A  67    17783  36206  16619  -3251   1497  -1059  B    O1-
ATOM   5366  N   ALA A  68     -36.873   2.567  -5.243  1.00172.85      B    N  
ANISOU 5366  N   ALA A  68    15172  35652  14850  -4345   2023  -2666  B    N  
ATOM   5367  CA  ALA A  68     -36.621   1.432  -4.355  1.00171.73      B    C  
ANISOU 5367  CA  ALA A  68    14949  35360  14942  -4630   2145  -3311  B    C  
ATOM   5368  C   ALA A  68     -37.787   0.448  -4.341  1.00174.21      B    C  
ANISOU 5368  C   ALA A  68    15346  35276  15569  -4652   2079  -3586  B    C  
ATOM   5369  O   ALA A  68     -38.946   0.850  -4.470  1.00174.41      B    O  
ANISOU 5369  O   ALA A  68    15325  35430  15513  -4535   1952  -3287  B    O  
ATOM   5370  CB  ALA A  68     -36.345   1.927  -2.944  1.00171.74      B    C  
ANISOU 5370  CB  ALA A  68    14866  35402  14987  -4658   2216  -3210  B    C  
ATOM   5371  N   THR A  69     -37.465  -0.845  -4.179  1.00171.16      B    N  
ANISOU 5371  N   THR A  69    14850  34860  15324  -4981   2210  -4298  B    N  
ATOM   5372  CA  THR A  69     -38.436  -1.939  -4.125  1.00170.94      B    C  
ANISOU 5372  CA  THR A  69    14790  34625  15533  -5115   2200  -4683  B    C  
ATOM   5373  C   THR A  69     -38.787  -2.227  -2.651  1.00172.94      B    C  
ANISOU 5373  C   THR A  69    15052  34536  16119  -5166   2271  -4830  B    C  
ATOM   5374  O   THR A  69     -37.889  -2.305  -1.807  1.00171.99      B    O  
ANISOU 5374  O   THR A  69    14901  34355  16091  -5304   2421  -5066  B    O  
ATOM   5375  CB  THR A  69     -37.928  -3.177  -4.906  1.00176.86      B    C  
ANISOU 5375  CB  THR A  69    15904  34530  16765  -5028   2212  -4938  B    C  
ATOM   5376  CG2 THR A  69     -36.492  -3.577  -4.559  1.00174.99      B    C  
ANISOU 5376  CG2 THR A  69    15649  34217  16622  -5217   2402  -5328  B    C  
ATOM   5377  OG1 THR A  69     -38.814  -4.279  -4.710  1.00177.10      B    O  
ANISOU 5377  OG1 THR A  69    15911  34298  17081  -5152   2219  -5282  B    O  
ATOM   5378  N   PHE A  70     -40.099  -2.348  -2.349  1.00170.55      B    N  
ANISOU 5378  N   PHE A  70    14563  34477  15760  -5249   2215  -4877  B    N  
ATOM   5379  CA  PHE A  70     -40.606  -2.592  -0.996  1.00169.81      B    C  
ANISOU 5379  CA  PHE A  70    14361  34305  15855  -5383   2303  -5090  B    C  
ATOM   5380  C   PHE A  70     -41.658  -3.714  -0.961  1.00172.23      B    C  
ANISOU 5380  C   PHE A  70    14762  34115  16564  -5406   2285  -5350  B    C  
ATOM   5381  O   PHE A  70     -42.497  -3.807  -1.862  1.00172.67      B    O  
ANISOU 5381  O   PHE A  70    14826  34237  16542  -5319   2144  -5204  B    O  
ATOM   5382  CB  PHE A  70     -41.178  -1.299  -0.380  1.00171.52      B    C  
ANISOU 5382  CB  PHE A  70    14543  34740  15884  -5152   2183  -4470  B    C  
ATOM   5383  CG  PHE A  70     -42.320  -0.646  -1.128  1.00173.50      B    C  
ANISOU 5383  CG  PHE A  70    14833  35095  15994  -4887   1970  -3934  B    C  
ATOM   5384  CD1 PHE A  70     -43.641  -0.921  -0.791  1.00175.83      B    C  
ANISOU 5384  CD1 PHE A  70    15156  35143  16507  -4817   1887  -3885  B    C  
ATOM   5385  CD2 PHE A  70     -42.074   0.283  -2.132  1.00175.58      B    C  
ANISOU 5385  CD2 PHE A  70    15234  35416  16062  -4617   1850  -3401  B    C  
ATOM   5386  CE1 PHE A  70     -44.695  -0.309  -1.474  1.00177.33      B    C  
ANISOU 5386  CE1 PHE A  70    15375  35411  16590  -4593   1701  -3431  B    C  
ATOM   5387  CE2 PHE A  70     -43.128   0.898  -2.811  1.00178.39      B    C  
ANISOU 5387  CE2 PHE A  70    15699  35684  16398  -4348   1668  -2920  B    C  
ATOM   5388  CZ  PHE A  70     -44.432   0.598  -2.477  1.00177.29      B    C  
ANISOU 5388  CZ  PHE A  70    15422  35629  16311  -4406   1602  -2994  B    C  
ATOM   5389  N   ALA A  71     -41.615  -4.548   0.101  1.00168.62      B    N  
ANISOU 5389  N   ALA A  71    14149  33587  16332  -5729   2499  -5950  B    N  
ATOM   5390  CA  ALA A  71     -42.525  -5.680   0.301  1.00167.91      B    C  
ANISOU 5390  CA  ALA A  71    14022  33211  16565  -5878   2561  -6340  B    C  
ATOM   5391  C   ALA A  71     -43.043  -5.766   1.744  1.00169.13      B    C  
ANISOU 5391  C   ALA A  71    14172  33099  16992  -5908   2650  -6412  B    C  
ATOM   5392  O   ALA A  71     -42.335  -5.397   2.685  1.00168.25      B    O  
ANISOU 5392  O   ALA A  71    14036  33004  16887  -5980   2775  -6490  B    O  
ATOM   5393  CB  ALA A  71     -41.824  -6.978  -0.072  1.00167.74      B    C  
ANISOU 5393  CB  ALA A  71    14113  32708  16912  -6033   2715  -6841  B    C  
ATOM   5394  N   LEU A  72     -44.281  -6.273   1.905  1.00166.31      B    N  
ANISOU 5394  N   LEU A  72    13629  32881  16681  -6057   2663  -6634  B    N  
ATOM   5395  CA  LEU A  72     -44.948  -6.452   3.200  1.00165.52      B    C  
ANISOU 5395  CA  LEU A  72    13439  32663  16788  -6164   2780  -6813  B    C  
ATOM   5396  C   LEU A  72     -44.996  -7.940   3.557  1.00167.13      B    C  
ANISOU 5396  C   LEU A  72    13795  32097  17608  -6272   2960  -7270  B    C  
ATOM   5397  O   LEU A  72     -45.258  -8.776   2.689  1.00166.92      B    O  
ANISOU 5397  O   LEU A  72    13790  31937  17697  -6310   2932  -7416  B    O  
ATOM   5398  CB  LEU A  72     -46.365  -5.839   3.199  1.00166.26      B    C  
ANISOU 5398  CB  LEU A  72    13421  33086  16665  -6014   2582  -6391  B    C  
ATOM   5399  CG  LEU A  72     -46.440  -4.308   3.310  1.00169.95      B    C  
ANISOU 5399  CG  LEU A  72    13960  33786  16827  -5674   2374  -5628  B    C  
ATOM   5400  CD1 LEU A  72     -46.484  -3.655   1.941  1.00170.81      B    C  
ANISOU 5400  CD1 LEU A  72    14106  34173  16621  -5469   2161  -5186  B    C  
ATOM   5401  CD2 LEU A  72     -47.646  -3.863   4.123  1.00172.10      B    C  
ANISOU 5401  CD2 LEU A  72    14193  34052  17147  -5539   2291  -5311  B    C  
ATOM   5402  N   GLY A  73     -44.706  -8.249   4.820  1.00163.74      B    N  
ANISOU 5402  N   GLY A  73    13274  31511  17428  -6520   3239  -7743  B    N  
ATOM   5403  CA  GLY A  73     -44.674  -9.615   5.336  1.00162.63      B    C  
ANISOU 5403  CA  GLY A  73    13191  30730  17873  -6706   3502  -8280  B    C  
ATOM   5404  C   GLY A  73     -46.017 -10.142   5.801  1.00165.20      B    C  
ANISOU 5404  C   GLY A  73    13554  30747  18468  -6618   3461  -8176  B    C  
ATOM   5405  O   GLY A  73     -47.062  -9.749   5.271  1.00165.97      B    O  
ANISOU 5405  O   GLY A  73    13561  31227  18273  -6507   3239  -7852  B    O  
ATOM   5406  N   THR A  74     -45.997 -11.050   6.794  1.00161.36      B    N  
ANISOU 5406  N   THR A  74    13000  29853  18455  -6881   3805  -8762  B    N  
ATOM   5407  CA  THR A  74     -47.218 -11.643   7.345  1.00160.93      B    C  
ANISOU 5407  CA  THR A  74    12881  29609  18656  -6926   3871  -8868  B    C  
ATOM   5408  C   THR A  74     -47.866 -10.640   8.303  1.00162.96      B    C  
ANISOU 5408  C   THR A  74    13117  30070  18732  -6794   3775  -8532  B    C  
ATOM   5409  O   THR A  74     -47.191 -10.079   9.173  1.00162.16      B    O  
ANISOU 5409  O   THR A  74    13029  29951  18632  -6839   3903  -8611  B    O  
ATOM   5410  CB  THR A  74     -46.950 -13.013   7.990  1.00165.57      B    C  
ANISOU 5410  CB  THR A  74    13811  29061  20036  -6791   4041  -8914  B    C  
ATOM   5411  CG2 THR A  74     -46.443 -14.040   6.988  1.00164.03      B    C  
ANISOU 5411  CG2 THR A  74    13640  28665  20018  -6880   4096  -9145  B    C  
ATOM   5412  OG1 THR A  74     -46.032 -12.877   9.078  1.00164.95      B    O  
ANISOU 5412  OG1 THR A  74    13828  28603  20243  -6841   4278  -9109  B    O  
ATOM   5413  N   THR A  75     -49.166 -10.379   8.090  1.00160.58      B    N  
ANISOU 5413  N   THR A  75    12577  30288  18150  -6843   3656  -8455  B    N  
ATOM   5414  CA  THR A  75     -49.962  -9.420   8.858  1.00160.55      B    C  
ANISOU 5414  CA  THR A  75    12444  30668  17890  -6782   3570  -8192  B    C  
ATOM   5415  C   THR A  75     -50.167  -9.886  10.318  1.00160.92      B    C  
ANISOU 5415  C   THR A  75    12577  30124  18443  -6845   3837  -8464  B    C  
ATOM   5416  O   THR A  75     -50.221 -11.089  10.593  1.00159.74      B    O  
ANISOU 5416  O   THR A  75    12490  29383  18820  -6973   4082  -8881  B    O  
ATOM   5417  CB  THR A  75     -51.297  -9.128   8.136  1.00167.91      B    C  
ANISOU 5417  CB  THR A  75    13526  31554  18717  -6374   3164  -7421  B    C  
ATOM   5418  CG2 THR A  75     -52.197 -10.367   7.977  1.00167.13      B    C  
ANISOU 5418  CG2 THR A  75    13404  31128  18969  -6481   3245  -7704  B    C  
ATOM   5419  OG1 THR A  75     -51.990  -8.080   8.817  1.00168.52      B    O  
ANISOU 5419  OG1 THR A  75    13501  31977  18553  -6263   3059  -7069  B    O  
ATOM   5420  N   HIS A  76     -50.257  -8.910  11.243  1.00157.63      B    N  
ANISOU 5420  N   HIS A  76    11969  30169  17755  -6951   3903  -8495  B    N  
ATOM   5421  CA  HIS A  76     -50.464  -9.137  12.676  1.00156.44      B    C  
ANISOU 5421  CA  HIS A  76    11841  29581  18016  -7063   4192  -8820  B    C  
ATOM   5422  C   HIS A  76     -51.860  -8.651  13.107  1.00158.19      B    C  
ANISOU 5422  C   HIS A  76    11968  30069  18069  -6928   4024  -8456  B    C  
ATOM   5423  O   HIS A  76     -52.440  -7.780  12.453  1.00159.00      B    O  
ANISOU 5423  O   HIS A  76    11924  30854  17637  -6788   3708  -7963  B    O  
ATOM   5424  CB  HIS A  76     -49.368  -8.443  13.500  1.00156.53      B    C  
ANISOU 5424  CB  HIS A  76    11959  29478  18039  -7079   4323  -8863  B    C  
ATOM   5425  CG  HIS A  76     -49.228  -8.983  14.889  1.00157.95      B    C  
ANISOU 5425  CG  HIS A  76    12371  28706  18936  -7087   4657  -9158  B    C  
ATOM   5426  CD2 HIS A  76     -48.441  -9.982  15.352  1.00158.05      B    C  
ANISOU 5426  CD2 HIS A  76    12608  27797  19647  -7128   4970  -9523  B    C  
ATOM   5427  ND1 HIS A  76     -49.969  -8.474  15.940  1.00159.28      B    N  
ANISOU 5427  ND1 HIS A  76    12556  28795  19168  -7019   4693  -9028  B    N  
ATOM   5428  CE1 HIS A  76     -49.608  -9.171  17.004  1.00157.84      B    C  
ANISOU 5428  CE1 HIS A  76    12535  27724  19714  -7121   5104  -9489  B    C  
ATOM   5429  NE2 HIS A  76     -48.694 -10.092  16.700  1.00157.30      B    N  
ANISOU 5429  NE2 HIS A  76    12602  27098  20067  -7163   5275  -9751  B    N  
ATOM   5430  N   SER A  77     -52.390  -9.227  14.207  1.00153.65      B    N  
ANISOU 5430  N   SER A  77    11286  29198  17896  -7170   4374  -9000  B    N  
ATOM   5431  CA  SER A  77     -53.712  -8.942  14.774  1.00153.20      B    C  
ANISOU 5431  CA  SER A  77    11078  29382  17749  -7148   4322  -8863  B    C  
ATOM   5432  C   SER A  77     -53.886  -7.478  15.219  1.00154.34      B    C  
ANISOU 5432  C   SER A  77    11140  30117  17383  -7005   4116  -8362  B    C  
ATOM   5433  O   SER A  77     -54.975  -6.928  15.050  1.00154.86      B    O  
ANISOU 5433  O   SER A  77    11040  30666  17135  -6896   3903  -7976  B    O  
ATOM   5434  CB  SER A  77     -53.982  -9.864  15.959  1.00154.70      B    C  
ANISOU 5434  CB  SER A  77    11486  28583  18710  -7140   4640  -9158  B    C  
ATOM   5435  OG  SER A  77     -55.355  -9.867  16.315  1.00161.90      B    O  
ANISOU 5435  OG  SER A  77    12560  29233  19720  -6791   4395  -8550  B    O  
ATOM   5436  N   PHE A  78     -52.831  -6.858  15.784  1.00149.98      B    N  
ANISOU 5436  N   PHE A  78    10512  29829  16647  -7200   4284  -8625  B    N  
ATOM   5437  CA  PHE A  78     -52.884  -5.481  16.291  1.00149.63      B    C  
ANISOU 5437  CA  PHE A  78    10328  30465  16058  -7126   4121  -8183  B    C  
ATOM   5438  C   PHE A  78     -51.602  -4.666  15.995  1.00149.99      B    C  
ANISOU 5438  C   PHE A  78    10441  30795  15753  -7059   4009  -7913  B    C  
ATOM   5439  O   PHE A  78     -51.699  -3.447  15.827  1.00150.30      B    O  
ANISOU 5439  O   PHE A  78    10324  31618  15165  -6888   3717  -7241  B    O  
ATOM   5440  CB  PHE A  78     -53.169  -5.470  17.808  1.00150.47      B    C  
ANISOU 5440  CB  PHE A  78    10560  30030  16581  -7162   4383  -8398  B    C  
ATOM   5441  CG  PHE A  78     -52.304  -6.394  18.638  1.00150.30      B    C  
ANISOU 5441  CG  PHE A  78    10843  28858  17406  -7299   4843  -9060  B    C  
ATOM   5442  CD1 PHE A  78     -51.091  -5.957  19.158  1.00151.99      B    C  
ANISOU 5442  CD1 PHE A  78    11287  28705  17759  -7274   4961  -9080  B    C  
ATOM   5443  CD2 PHE A  78     -52.712  -7.693  18.915  1.00151.27      B    C  
ANISOU 5443  CD2 PHE A  78    11136  28056  18285  -7294   5094  -9404  B    C  
ATOM   5444  CE1 PHE A  78     -50.288  -6.814  19.916  1.00151.46      B    C  
ANISOU 5444  CE1 PHE A  78    11509  27456  18583  -7357   5418  -9628  B    C  
ATOM   5445  CE2 PHE A  78     -51.909  -8.548  19.673  1.00152.01      B    C  
ANISOU 5445  CE2 PHE A  78    11551  26961  19247  -7293   5491  -9785  B    C  
ATOM   5446  CZ  PHE A  78     -50.706  -8.102  20.172  1.00150.13      B    C  
ANISOU 5446  CZ  PHE A  78    11418  26466  19159  -7399   5719 -10023  B    C  
ATOM   5447  N   LYS A  79     -50.419  -5.323  15.948  1.00144.92      B    N  
ANISOU 5447  N   LYS A  79     9822  29840  15403  -7385   4347  -8663  B    N  
ATOM   5448  CA  LYS A  79     -49.131  -4.654  15.693  1.00143.86      B    C  
ANISOU 5448  CA  LYS A  79     9703  30007  14951  -7420   4310  -8576  B    C  
ATOM   5449  C   LYS A  79     -49.069  -4.002  14.301  1.00147.45      B    C  
ANISOU 5449  C   LYS A  79    10124  31069  14831  -7115   3862  -7806  B    C  
ATOM   5450  O   LYS A  79     -48.345  -3.019  14.131  1.00147.64      B    O  
ANISOU 5450  O   LYS A  79    10110  31577  14408  -7027   3713  -7399  B    O  
ATOM   5451  CB  LYS A  79     -47.954  -5.635  15.834  1.00143.23      B    C  
ANISOU 5451  CB  LYS A  79     9892  28948  15582  -7573   4678  -9229  B    C  
ATOM   5452  CG  LYS A  79     -47.629  -6.056  17.254  1.00140.17      B    C  
ANISOU 5452  CG  LYS A  79     9746  27589  15925  -7668   5100  -9683  B    C  
ATOM   5453  CD  LYS A  79     -46.188  -6.549  17.364  1.00139.47      B    C  
ANISOU 5453  CD  LYS A  79     9937  26617  16440  -7713   5389 -10050  B    C  
ATOM   5454  CE  LYS A  79     -46.102  -8.027  17.662  1.00138.16      B    C  
ANISOU 5454  CE  LYS A  79     9989  25240  17265  -7699   5746 -10465  B    C  
ATOM   5455  NZ  LYS A  79     -44.710  -8.438  17.982  1.00140.72      B    N1+
ANISOU 5455  NZ  LYS A  79    10685  24518  18266  -7567   5958 -10517  B    N1+
ATOM   5456  N   GLY A  80     -49.751  -4.614  13.326  1.00145.31      B    N  
ANISOU 5456  N   GLY A  80     9689  31025  14496  -7173   3785  -7922  B    N  
ATOM   5457  CA  GLY A  80     -49.797  -4.178  11.932  1.00145.71      B    C  
ANISOU 5457  CA  GLY A  80     9641  31653  14071  -7003   3468  -7431  B    C  
ATOM   5458  C   GLY A  80     -48.981  -5.046  10.989  1.00147.38      B    C  
ANISOU 5458  C   GLY A  80    10056  31371  14572  -7025   3529  -7722  B    C  
ATOM   5459  O   GLY A  80     -48.364  -6.025  11.418  1.00146.28      B    O  
ANISOU 5459  O   GLY A  80    10047  30569  14962  -7239   3849  -8374  B    O  
ATOM   5460  N   THR A  81     -48.976  -4.700   9.691  1.00144.99      B    N  
ANISOU 5460  N   THR A  81     9578  31724  13789  -6994   3314  -7471  B    N  
ATOM   5461  CA  THR A  81     -48.202  -5.439   8.691  1.00144.37      B    C  
ANISOU 5461  CA  THR A  81     9592  31420  13840  -7083   3373  -7788  B    C  
ATOM   5462  C   THR A  81     -46.847  -4.713   8.520  1.00146.57      B    C  
ANISOU 5462  C   THR A  81    10016  31748  13925  -6956   3318  -7503  B    C  
ATOM   5463  O   THR A  81     -46.851  -3.492   8.337  1.00147.20      B    O  
ANISOU 5463  O   THR A  81    10002  32431  13497  -6753   3086  -6853  B    O  
ATOM   5464  CB  THR A  81     -48.992  -5.601   7.375  1.00150.91      B    C  
ANISOU 5464  CB  THR A  81    10613  32037  14689  -6723   3047  -7233  B    C  
ATOM   5465  CG2 THR A  81     -48.454  -6.733   6.508  1.00149.76      B    C  
ANISOU 5465  CG2 THR A  81    10544  31559  14800  -6883   3167  -7715  B    C  
ATOM   5466  OG1 THR A  81     -50.373  -5.844   7.659  1.00150.55      B    O  
ANISOU 5466  OG1 THR A  81    10450  32031  14721  -6724   3003  -7209  B    O  
ATOM   5467  N   PRO A  82     -45.684  -5.415   8.623  1.00142.56      B    N  
ANISOU 5467  N   PRO A  82     9521  30976  13669  -7269   3622  -8204  B    N  
ATOM   5468  CA  PRO A  82     -44.388  -4.715   8.504  1.00141.98      B    C  
ANISOU 5468  CA  PRO A  82     9477  31139  13329  -7262   3616  -8070  B    C  
ATOM   5469  C   PRO A  82     -44.093  -4.221   7.088  1.00144.46      B    C  
ANISOU 5469  C   PRO A  82     9852  31763  13273  -6999   3327  -7513  B    C  
ATOM   5470  O   PRO A  82     -44.704  -4.703   6.133  1.00144.80      B    O  
ANISOU 5470  O   PRO A  82     9892  31790  13337  -6956   3229  -7517  B    O  
ATOM   5471  CB  PRO A  82     -43.361  -5.779   8.927  1.00142.08      B    C  
ANISOU 5471  CB  PRO A  82     9715  30254  14016  -7455   3965  -8758  B    C  
ATOM   5472  CG  PRO A  82     -44.152  -6.897   9.532  1.00144.71      B    C  
ANISOU 5472  CG  PRO A  82    10212  29741  15030  -7444   4125  -9047  B    C  
ATOM   5473  CD  PRO A  82     -45.484  -6.856   8.866  1.00142.60      B    C  
ANISOU 5473  CD  PRO A  82     9694  30087  14399  -7442   3927  -8876  B    C  
ATOM   5474  N   LEU A  83     -43.156  -3.258   6.960  1.00140.87      B    N  
ANISOU 5474  N   LEU A  83     9237  31985  12302  -7039   3283  -7284  B    N  
ATOM   5475  CA  LEU A  83     -42.736  -2.687   5.678  1.00140.67      B    C  
ANISOU 5475  CA  LEU A  83     9178  32421  11849  -6876   3079  -6841  B    C  
ATOM   5476  C   LEU A  83     -41.217  -2.844   5.521  1.00141.34      B    C  
ANISOU 5476  C   LEU A  83     9429  32195  12078  -6951   3221  -7098  B    C  
ATOM   5477  O   LEU A  83     -40.445  -2.198   6.239  1.00140.89      B    O  
ANISOU 5477  O   LEU A  83     9363  32268  11901  -6982   3282  -7001  B    O  
ATOM   5478  CB  LEU A  83     -43.180  -1.204   5.557  1.00141.51      B    C  
ANISOU 5478  CB  LEU A  83     9163  33195  11410  -6553   2792  -5886  B    C  
ATOM   5479  CG  LEU A  83     -42.589  -0.342   4.413  1.00145.03      B    C  
ANISOU 5479  CG  LEU A  83     9771  33717  11617  -6189   2574  -5172  B    C  
ATOM   5480  CD1 LEU A  83     -43.056  -0.816   3.038  1.00145.66      B    C  
ANISOU 5480  CD1 LEU A  83     9903  33739  11701  -6106   2455  -5167  B    C  
ATOM   5481  CD2 LEU A  83     -42.941   1.119   4.600  1.00146.89      B    C  
ANISOU 5481  CD2 LEU A  83     9974  34295  11541  -5820   2366  -4198  B    C  
ATOM   5482  N   GLU A  84     -40.795  -3.728   4.602  1.00137.32      B    N  
ANISOU 5482  N   GLU A  84     8851  31681  11643  -7195   3349  -7663  B    N  
ATOM   5483  CA  GLU A  84     -39.376  -3.973   4.354  1.00136.02      B    C  
ANISOU 5483  CA  GLU A  84     8767  31327  11588  -7342   3516  -8018  B    C  
ATOM   5484  C   GLU A  84     -38.912  -3.178   3.132  1.00137.08      B    C  
ANISOU 5484  C   GLU A  84     8923  31902  11259  -7090   3275  -7414  B    C  
ATOM   5485  O   GLU A  84     -39.482  -3.333   2.052  1.00136.95      B    O  
ANISOU 5485  O   GLU A  84     8877  32073  11084  -6991   3125  -7245  B    O  
ATOM   5486  CB  GLU A  84     -39.086  -5.481   4.182  1.00136.27      B    C  
ANISOU 5486  CB  GLU A  84     8959  30543  12276  -7520   3758  -8724  B    C  
ATOM   5487  CG  GLU A  84     -37.600  -5.816   4.087  1.00142.75      B    C  
ANISOU 5487  CG  GLU A  84    10176  30506  13556  -7358   3834  -8724  B    C  
ATOM   5488  CD  GLU A  84     -37.234  -7.289   4.075  1.00152.56      B    C  
ANISOU 5488  CD  GLU A  84    11940  30295  15733  -7093   3881  -8771  B    C  
ATOM   5489  OE1 GLU A  84     -37.855  -8.058   3.305  1.00144.23      B    O  
ANISOU 5489  OE1 GLU A  84    10528  29776  14499  -7454   3994  -9331  B    O  
ATOM   5490  OE2 GLU A  84     -36.290  -7.665   4.808  1.00145.52      B    O1-
ANISOU 5490  OE2 GLU A  84    10894  29276  15122  -7522   4286  -9561  B    O1-
ATOM   5491  N   ILE A  85     -37.891  -2.314   3.315  1.00133.18      B    N  
ANISOU 5491  N   ILE A  85     8277  31959  10368  -7188   3316  -7303  B    N  
ATOM   5492  CA  ILE A  85     -37.311  -1.531   2.221  1.00132.84      B    C  
ANISOU 5492  CA  ILE A  85     8204  32404   9866  -7000   3143  -6775  B    C  
ATOM   5493  C   ILE A  85     -35.940  -2.145   1.955  1.00134.13      B    C  
ANISOU 5493  C   ILE A  85     8580  32017  10367  -7099   3320  -7213  B    C  
ATOM   5494  O   ILE A  85     -35.053  -2.051   2.807  1.00132.73      B    O  
ANISOU 5494  O   ILE A  85     8412  31699  10323  -7277   3504  -7504  B    O  
ATOM   5495  CB  ILE A  85     -37.273   0.004   2.512  1.00135.23      B    C  
ANISOU 5495  CB  ILE A  85     8493  33111   9775  -6660   2935  -5819  B    C  
ATOM   5496  CG1 ILE A  85     -38.692   0.569   2.748  1.00135.77      B    C  
ANISOU 5496  CG1 ILE A  85     8445  33482   9659  -6449   2739  -5262  B    C  
ATOM   5497  CG2 ILE A  85     -36.567   0.763   1.380  1.00135.76      B    C  
ANISOU 5497  CG2 ILE A  85     8598  33478   9507  -6432   2807  -5268  B    C  
ATOM   5498  CD1 ILE A  85     -38.765   1.715   3.759  1.00139.61      B    C  
ANISOU 5498  CD1 ILE A  85     9025  33887  10135  -6142   2633  -4518  B    C  
ATOM   5499  N   THR A  86     -35.795  -2.884   0.847  1.00132.20      B    N  
ANISOU 5499  N   THR A  86     8314  31783  10133  -7201   3348  -7531  B    N  
ATOM   5500  CA  THR A  86     -34.524  -3.549   0.544  1.00131.57      B    C  
ANISOU 5500  CA  THR A  86     8348  31310  10331  -7365   3544  -8029  B    C  
ATOM   5501  C   THR A  86     -33.624  -2.554  -0.223  1.00135.49      B    C  
ANISOU 5501  C   THR A  86     8988  31987  10506  -7053   3373  -7358  B    C  
ATOM   5502  O   THR A  86     -33.882  -2.229  -1.388  1.00136.11      B    O  
ANISOU 5502  O   THR A  86     9060  32397  10260  -6855   3189  -6930  B    O  
ATOM   5503  CB  THR A  86     -34.720  -4.935  -0.124  1.00134.96      B    C  
ANISOU 5503  CB  THR A  86     9047  30898  11333  -7297   3575  -8336  B    C  
ATOM   5504  CG2 THR A  86     -35.786  -4.947  -1.220  1.00133.70      B    C  
ANISOU 5504  CG2 THR A  86     8795  31152  10855  -7182   3364  -8061  B    C  
ATOM   5505  OG1 THR A  86     -33.467  -5.411  -0.627  1.00135.01      B    O  
ANISOU 5505  OG1 THR A  86     9145  30637  11516  -7400   3719  -8664  B    O  
ATOM   5506  N   LEU A  87     -32.587  -2.046   0.490  1.00132.94      B    N  
ANISOU 5506  N   LEU A  87     8579  31834  10098  -7229   3523  -7508  B    N  
ATOM   5507  CA  LEU A  87     -31.604  -1.050   0.042  1.00133.34      B    C  
ANISOU 5507  CA  LEU A  87     8628  32259   9775  -7084   3445  -7024  B    C  
ATOM   5508  C   LEU A  87     -30.800  -1.518  -1.174  1.00136.83      B    C  
ANISOU 5508  C   LEU A  87     9293  32325  10370  -6960   3440  -7068  B    C  
ATOM   5509  O   LEU A  87     -30.411  -2.688  -1.228  1.00135.86      B    O  
ANISOU 5509  O   LEU A  87     9241  31700  10680  -7188   3631  -7765  B    O  
ATOM   5510  CB  LEU A  87     -30.626  -0.680   1.179  1.00132.72      B    C  
ANISOU 5510  CB  LEU A  87     8565  32038   9824  -7241   3613  -7208  B    C  
ATOM   5511  CG  LEU A  87     -31.221  -0.076   2.456  1.00136.06      B    C  
ANISOU 5511  CG  LEU A  87     9044  32364  10288  -7082   3532  -6789  B    C  
ATOM   5512  CD1 LEU A  87     -30.264  -0.233   3.623  1.00135.23      B    C  
ANISOU 5512  CD1 LEU A  87     9019  31812  10551  -7354   3792  -7335  B    C  
ATOM   5513  CD2 LEU A  87     -31.594   1.392   2.266  1.00138.76      B    C  
ANISOU 5513  CD2 LEU A  87     9358  33220  10144  -6658   3250  -5665  B    C  
ATOM   5514  N   PRO A  88     -30.513  -0.607  -2.137  1.00135.97      B    N  
ANISOU 5514  N   PRO A  88     9089  32836   9736  -6793   3300  -6510  B    N  
ATOM   5515  CA  PRO A  88     -29.732  -1.003  -3.333  1.00136.06      B    C  
ANISOU 5515  CA  PRO A  88     9194  32757   9746  -6789   3334  -6658  B    C  
ATOM   5516  C   PRO A  88     -28.258  -1.303  -3.032  1.00137.58      B    C  
ANISOU 5516  C   PRO A  88     9531  32488  10258  -6907   3523  -7023  B    C  
ATOM   5517  O   PRO A  88     -27.666  -2.182  -3.659  1.00136.65      B    O  
ANISOU 5517  O   PRO A  88     9479  32073  10368  -7043   3643  -7500  B    O  
ATOM   5518  CB  PRO A  88     -29.854   0.215  -4.260  1.00138.51      B    C  
ANISOU 5518  CB  PRO A  88     9555  33451   9621  -6394   3110  -5737  B    C  
ATOM   5519  CG  PRO A  88     -30.956   1.062  -3.675  1.00142.10      B    C  
ANISOU 5519  CG  PRO A  88    10052  33917  10022  -6094   2928  -5056  B    C  
ATOM   5520  CD  PRO A  88     -30.914   0.812  -2.211  1.00138.12      B    C  
ANISOU 5520  CD  PRO A  88     9334  33546   9597  -6436   3081  -5543  B    C  
ATOM   5521  N   PHE A  89     -27.674  -0.559  -2.083  1.00135.14      B    N  
ANISOU 5521  N   PHE A  89     9056  32527   9762  -7055   3609  -6988  B    N  
ATOM   5522  CA  PHE A  89     -26.288  -0.706  -1.648  1.00134.38      B    C  
ANISOU 5522  CA  PHE A  89     9010  32158   9891  -7261   3820  -7401  B    C  
ATOM   5523  C   PHE A  89     -26.254  -0.909  -0.132  1.00135.36      B    C  
ANISOU 5523  C   PHE A  89     9190  31818  10421  -7439   3979  -7777  B    C  
ATOM   5524  O   PHE A  89     -27.011  -0.257   0.594  1.00135.37      B    O  
ANISOU 5524  O   PHE A  89     9089  32137  10207  -7373   3876  -7422  B    O  
ATOM   5525  CB  PHE A  89     -25.442   0.510  -2.080  1.00136.60      B    C  
ANISOU 5525  CB  PHE A  89     9331  32770   9800  -6989   3700  -6660  B    C  
ATOM   5526  CG  PHE A  89     -25.951   1.857  -1.611  1.00138.78      B    C  
ANISOU 5526  CG  PHE A  89     9556  33452   9723  -6683   3501  -5746  B    C  
ATOM   5527  CD1 PHE A  89     -26.879   2.570  -2.363  1.00142.22      B    C  
ANISOU 5527  CD1 PHE A  89    10059  34050   9928  -6262   3261  -4922  B    C  
ATOM   5528  CD2 PHE A  89     -25.479   2.427  -0.433  1.00140.19      B    C  
ANISOU 5528  CD2 PHE A  89     9764  33520   9984  -6693   3542  -5591  B    C  
ATOM   5529  CE1 PHE A  89     -27.350   3.811  -1.927  1.00143.56      B    C  
ANISOU 5529  CE1 PHE A  89    10166  34536   9843  -5974   3110  -4056  B    C  
ATOM   5530  CE2 PHE A  89     -25.944   3.673  -0.005  1.00142.89      B    C  
ANISOU 5530  CE2 PHE A  89    10086  34133  10075  -6349   3354  -4644  B    C  
ATOM   5531  CZ  PHE A  89     -26.880   4.355  -0.751  1.00142.55      B    C  
ANISOU 5531  CZ  PHE A  89     9938  34550   9676  -6056   3160  -3924  B    C  
ATOM   5532  N   SER A  90     -25.399  -1.832   0.336  1.00131.21      B    N  
ANISOU 5532  N   SER A  90     8642  30859  10352  -7870   4324  -8726  B    N  
ATOM   5533  CA  SER A  90     -25.255  -2.160   1.755  1.00129.80      B    C  
ANISOU 5533  CA  SER A  90     8504  30149  10663  -8145   4589  -9297  B    C  
ATOM   5534  C   SER A  90     -24.611  -1.009   2.532  1.00131.41      B    C  
ANISOU 5534  C   SER A  90     8739  30546  10644  -8082   4548  -8882  B    C  
ATOM   5535  O   SER A  90     -23.435  -0.687   2.327  1.00131.56      B    O  
ANISOU 5535  O   SER A  90     8809  30543  10634  -8114   4613  -8872  B    O  
ATOM   5536  CB  SER A  90     -24.450  -3.445   1.934  1.00131.84      B    C  
ANISOU 5536  CB  SER A  90     9044  29231  11816  -8249   4872  -9971  B    C  
ATOM   5537  OG  SER A  90     -23.205  -3.382   1.254  1.00140.28      B    O  
ANISOU 5537  OG  SER A  90    10468  29751  13082  -7892   4749  -9543  B    O  
ATOM   5538  N   LEU A  91     -25.409  -0.375   3.402  1.00127.97      B    N  
ANISOU 5538  N   LEU A  91     8072  30688   9863  -8208   4515  -8747  B    N  
ATOM   5539  CA  LEU A  91     -25.004   0.739   4.261  1.00127.44      B    C  
ANISOU 5539  CA  LEU A  91     7937  31004   9480  -8232   4483  -8362  B    C  
ATOM   5540  C   LEU A  91     -23.995   0.281   5.309  1.00126.80      B    C  
ANISOU 5540  C   LEU A  91     8099  29964  10114  -8533   4861  -9131  B    C  
ATOM   5541  O   LEU A  91     -24.030  -0.874   5.741  1.00125.10      B    O  
ANISOU 5541  O   LEU A  91     8006  28878  10647  -8781   5198 -10000  B    O  
ATOM   5542  CB  LEU A  91     -26.239   1.345   4.953  1.00128.14      B    C  
ANISOU 5542  CB  LEU A  91     7893  31553   9241  -8090   4284  -7819  B    C  
ATOM   5543  CG  LEU A  91     -26.475   2.846   4.756  1.00132.73      B    C  
ANISOU 5543  CG  LEU A  91     8431  32778   9224  -7555   3881  -6423  B    C  
ATOM   5544  CD1 LEU A  91     -27.024   3.145   3.369  1.00133.74      B    C  
ANISOU 5544  CD1 LEU A  91     8479  33322   9015  -7200   3628  -5794  B    C  
ATOM   5545  CD2 LEU A  91     -27.458   3.373   5.777  1.00134.56      B    C  
ANISOU 5545  CD2 LEU A  91     8635  33124   9366  -7423   3760  -5929  B    C  
ATOM   5546  N   THR A  92     -23.094   1.187   5.711  1.00123.86      B    N  
ANISOU 5546  N   THR A  92     7617  30034   9411  -8724   4927  -9020  B    N  
ATOM   5547  CA  THR A  92     -22.066   0.881   6.703  1.00122.25      B    C  
ANISOU 5547  CA  THR A  92     7640  28906   9902  -9083   5365  -9821  B    C  
ATOM   5548  C   THR A  92     -22.475   1.417   8.088  1.00123.78      B    C  
ANISOU 5548  C   THR A  92     7991  28799  10243  -9084   5401  -9657  B    C  
ATOM   5549  O   THR A  92     -23.374   2.262   8.192  1.00122.44      B    O  
ANISOU 5549  O   THR A  92     7733  29302   9486  -8719   4981  -8668  B    O  
ATOM   5550  CB  THR A  92     -20.694   1.390   6.242  1.00126.26      B    C  
ANISOU 5550  CB  THR A  92     8385  29146  10441  -8841   5273  -9401  B    C  
ATOM   5551  CG2 THR A  92     -20.587   2.910   6.235  1.00125.87      B    C  
ANISOU 5551  CG2 THR A  92     8108  30220   9499  -8709   4966  -8424  B    C  
ATOM   5552  OG1 THR A  92     -19.692   0.827   7.085  1.00125.90      B    O  
ANISOU 5552  OG1 THR A  92     8653  27854  11330  -9118   5745 -10243  B    O  
ATOM   5553  N   ARG A  93     -21.796   0.897   9.139  1.00113.04      B    N  
ANISOU 5553  N   ARG A  93     7344  25467  10141  -8801   5623  -9836  B    N  
ATOM   5554  CA AARG A  93     -22.005   1.251  10.545  0.50103.99      B    C  
ANISOU 5554  CA AARG A  93     6962  22786   9765  -8062   5385  -8961  B    C  
ATOM   5555  CA BARG A  93     -22.010   1.252  10.540  0.50104.04      B    C  
ANISOU 5555  CA BARG A  93     6964  22803   9765  -8064   5384  -8961  B    C  
ATOM   5556  C   ARG A  93     -21.634   2.718  10.771  1.00101.58      B    C  
ANISOU 5556  C   ARG A  93     7046  22374   9175  -7342   4852  -7513  B    C  
ATOM   5557  O   ARG A  93     -20.502   3.117  10.518  1.00 99.38      B    O  
ANISOU 5557  O   ARG A  93     6958  21816   8984  -7201   4820  -7276  B    O  
ATOM   5558  CB AARG A  93     -21.170   0.325  11.450  0.50 99.94      B    C  
ANISOU 5558  CB AARG A  93     6969  20439  10566  -7990   5792  -9493  B    C  
ATOM   5559  CB BARG A  93     -21.184   0.318  11.436  0.50100.13      B    C  
ANISOU 5559  CB BARG A  93     6982  20483  10579  -7998   5794  -9503  B    C  
ATOM   5560  CG AARG A  93     -21.614   0.274  12.907  0.50100.07      B    C  
ANISOU 5560  CG AARG A  93     7598  19040  11385  -7421   5686  -8928  B    C  
ATOM   5561  CG BARG A  93     -21.747   0.105  12.828  0.50101.44      B    C  
ANISOU 5561  CG BARG A  93     7675  19329  11538  -7528   5749  -9102  B    C  
ATOM   5562  CD AARG A  93     -20.502  -0.208  13.824  0.50 99.84      B    C  
ANISOU 5562  CD AARG A  93     8120  17313  12502  -7132   5927  -8938  B    C  
ATOM   5563  CD BARG A  93     -20.915   0.829  13.855  0.50 98.39      B    C  
ANISOU 5563  CD BARG A  93     8039  17625  11720  -6795   5469  -8120  B    C  
ATOM   5564  NE AARG A  93     -20.299  -1.658  13.772  0.50107.94      B    N  
ANISOU 5564  NE AARG A  93     8882  17784  14345  -7651   6617 -10119  B    N  
ATOM   5565  NE BARG A  93     -21.134   0.347  15.219  0.50 94.47      B    N  
ANISOU 5565  NE BARG A  93     8002  15758  12135  -6439   5565  -7951  B    N  
ATOM   5566  CZ AARG A  93     -19.177  -2.274  14.135  0.50118.28      B    C  
ANISOU 5566  CZ AARG A  93    10418  17917  16605  -7596   6983 -10353  B    C  
ATOM   5567  CZ BARG A  93     -21.842   0.990  16.141  0.50 92.54      B    C  
ANISOU 5567  CZ BARG A  93     8096  15207  11859  -5937   5206  -7129  B    C  
ATOM   5568  NH1AARG A  93     -18.136  -1.573  14.571  0.50 91.16      B    N1+
ANISOU 5568  NH1AARG A  93     7490  13813  13333  -7069   6680  -9536  B    N1+
ATOM   5569  NH1BARG A  93     -22.427   2.147  15.853  0.50 73.57      B    N1+
ANISOU 5569  NH1BARG A  93     5624  13678   8650  -5713   4759  -6382  B    N1+
ATOM   5570  NH2AARG A  93     -19.082  -3.594  14.057  0.50113.52      B    N  
ANISOU 5570  NH2AARG A  93     9488  16798  16845  -8076   7696 -11409  B    N  
ATOM   5571  NH2BARG A  93     -21.966   0.486  17.360  0.50 71.84      B    N  
ANISOU 5571  NH2BARG A  93     5840  11416  10040  -5650   5324  -7014  B    N  
ATOM   5572  N   GLY A  94     -22.621   3.502  11.198  1.00 95.19      B    N  
ANISOU 5572  N   GLY A  94     6294  21818   8057  -6927   4489  -6599  B    N  
ATOM   5573  CA  GLY A  94     -22.468   4.927  11.463  1.00 90.54      B    C  
ANISOU 5573  CA  GLY A  94     5992  21105   7304  -6247   4064  -5220  B    C  
ATOM   5574  C   GLY A  94     -22.705   5.826  10.266  1.00 98.57      B    C  
ANISOU 5574  C   GLY A  94     6352  23870   7231  -6307   3844  -4566  B    C  
ATOM   5575  O   GLY A  94     -22.342   7.006  10.301  1.00 95.21      B    O  
ANISOU 5575  O   GLY A  94     6078  23349   6747  -5774   3590  -3433  B    O  
ATOM   5576  N   GLN A  95     -23.323   5.289   9.199  1.00102.71      B    N  
ANISOU 5576  N   GLN A  95     6077  26053   6893  -6961   3972  -5254  B    N  
ATOM   5577  CA  GLN A  95     -23.618   6.090   8.010  1.00108.45      B    C  
ANISOU 5577  CA  GLN A  95     6040  28702   6464  -7048   3768  -4577  B    C  
ATOM   5578  C   GLN A  95     -25.080   6.503   8.000  1.00112.48      B    C  
ANISOU 5578  C   GLN A  95     6112  30226   6400  -6945   3553  -3969  B    C  
ATOM   5579  O   GLN A  95     -25.939   5.729   8.412  1.00113.03      B    O  
ANISOU 5579  O   GLN A  95     6139  30201   6605  -7230   3675  -4695  B    O  
ATOM   5580  CB  GLN A  95     -23.263   5.340   6.718  1.00117.94      B    C  
ANISOU 5580  CB  GLN A  95     6512  31393   6908  -7865   4031  -5660  B    C  
ATOM   5581  CG  GLN A  95     -22.914   6.261   5.549  1.00123.83      B    C  
ANISOU 5581  CG  GLN A  95     6890  33229   6932  -7571   3782  -4632  B    C  
ATOM   5582  CD  GLN A  95     -22.451   5.506   4.328  1.00129.81      B    C  
ANISOU 5582  CD  GLN A  95     8082  33016   8224  -7286   3815  -4932  B    C  
ATOM   5583  NE2 GLN A  95     -21.255   5.841   3.853  1.00118.45      B    N  
ANISOU 5583  NE2 GLN A  95     6220  32578   6207  -7704   3949  -5100  B    N  
ATOM   5584  OE1 GLN A  95     -23.162   4.650   3.780  1.00127.30      B    O  
ANISOU 5584  OE1 GLN A  95     7674  32763   7931  -7452   3874  -5514  B    O  
ATOM   5585  N   GLU A  96     -25.351   7.728   7.535  1.00108.78      B    N  
ANISOU 5585  N   GLU A  96     5287  30694   5352  -6522   3269  -2593  B    N  
ATOM   5586  CA  GLU A  96     -26.694   8.279   7.441  1.00111.23      B    C  
ANISOU 5586  CA  GLU A  96     5094  32070   5098  -6351   3061  -1774  B    C  
ATOM   5587  C   GLU A  96     -27.124   8.392   5.983  1.00121.21      B    C  
ANISOU 5587  C   GLU A  96     5670  34888   5496  -6485   2988  -1533  B    C  
ATOM   5588  O   GLU A  96     -26.304   8.701   5.114  1.00120.51      B    O  
ANISOU 5588  O   GLU A  96     5557  34949   5283  -6377   2994  -1274  B    O  
ATOM   5589  CB  GLU A  96     -26.790   9.636   8.152  1.00107.39      B    C  
ANISOU 5589  CB  GLU A  96     5000  30658   5146  -5465   2844   -189  B    C  
ATOM   5590  CG  GLU A  96     -26.875   9.507   9.664  1.00105.70      B    C  
ANISOU 5590  CG  GLU A  96     5727  28347   6086  -5072   2858   -324  B    C  
ATOM   5591  CD  GLU A  96     -27.298  10.733  10.458  1.00110.85      B    C  
ANISOU 5591  CD  GLU A  96     6681  28163   7275  -4303   2705   1028  B    C  
ATOM   5592  OE1 GLU A  96     -27.513  11.801   9.841  1.00109.33      B    O  
ANISOU 5592  OE1 GLU A  96     5964  28900   6677  -3987   2613   2249  B    O  
ATOM   5593  OE2 GLU A  96     -27.393  10.634  11.704  1.00 81.47      B    O1-
ANISOU 5593  OE2 GLU A  96     3679  22853   4422  -4018   2718    882  B    O1-
ATOM   5594  N   VAL A  97     -28.410   8.111   5.723  1.00119.24      B    N  
ANISOU 5594  N   VAL A  97     5279  34904   5123  -6451   2909  -1572  B    N  
ATOM   5595  CA  VAL A  97     -29.028   8.165   4.391  1.00119.85      B    C  
ANISOU 5595  CA  VAL A  97     5363  35056   5119  -6160   2806  -1261  B    C  
ATOM   5596  C   VAL A  97     -30.443   8.761   4.530  1.00124.38      B    C  
ANISOU 5596  C   VAL A  97     6006  35405   5850  -5653   2613   -376  B    C  
ATOM   5597  O   VAL A  97     -31.007   8.735   5.625  1.00123.78      B    O  
ANISOU 5597  O   VAL A  97     5832  35402   5796  -5731   2593   -359  B    O  
ATOM   5598  CB  VAL A  97     -29.018   6.768   3.697  1.00121.56      B    C  
ANISOU 5598  CB  VAL A  97     5850  34688   5649  -6495   2968  -2573  B    C  
ATOM   5599  CG1 VAL A  97     -30.085   5.825   4.265  1.00120.61      B    C  
ANISOU 5599  CG1 VAL A  97     5736  34359   5731  -6778   3039  -3372  B    C  
ATOM   5600  CG2 VAL A  97     -29.147   6.895   2.184  1.00121.98      B    C  
ANISOU 5600  CG2 VAL A  97     5937  34839   5573  -6240   2879  -2248  B    C  
ATOM   5601  N   ILE A  98     -30.997   9.317   3.443  1.00124.32      B    N  
ANISOU 5601  N   ILE A  98     5952  35564   5720  -5298   2497    304  B    N  
ATOM   5602  CA  ILE A  98     -32.346   9.891   3.466  1.00125.43      B    C  
ANISOU 5602  CA  ILE A  98     6051  35686   5921  -4923   2349   1055  B    C  
ATOM   5603  C   ILE A  98     -33.303   8.972   2.705  1.00129.95      B    C  
ANISOU 5603  C   ILE A  98     6929  35703   6745  -4986   2329    302  B    C  
ATOM   5604  O   ILE A  98     -33.080   8.683   1.524  1.00130.29      B    O  
ANISOU 5604  O   ILE A  98     7076  35688   6742  -5025   2347      4  B    O  
ATOM   5605  CB  ILE A  98     -32.405  11.352   2.931  1.00128.35      B    C  
ANISOU 5605  CB  ILE A  98     6523  35771   6472  -4281   2269   2402  B    C  
ATOM   5606  CG1 ILE A  98     -31.248  12.242   3.472  1.00128.69      B    C  
ANISOU 5606  CG1 ILE A  98     6534  35727   6638  -4051   2326   3174  B    C  
ATOM   5607  CG2 ILE A  98     -33.800  11.985   3.142  1.00128.84      B    C  
ANISOU 5607  CG2 ILE A  98     6540  35742   6672  -3925   2154   3136  B    C  
ATOM   5608  CD1 ILE A  98     -31.178  12.469   5.008  1.00134.00      B    C  
ANISOU 5608  CD1 ILE A  98     7345  35852   7718  -3903   2333   3473  B    C  
ATOM   5609  N   VAL A  99     -34.365   8.520   3.396  1.00128.14      B    N  
ANISOU 5609  N   VAL A  99     6578  35590   6520  -5119   2294     45  B    N  
ATOM   5610  CA  VAL A  99     -35.394   7.639   2.851  1.00128.55      B    C  
ANISOU 5610  CA  VAL A  99     6702  35482   6661  -5259   2271   -591  B    C  
ATOM   5611  C   VAL A  99     -36.705   8.434   2.763  1.00132.88      B    C  
ANISOU 5611  C   VAL A  99     7422  35609   7458  -4746   2101    273  B    C  
ATOM   5612  O   VAL A  99     -37.280   8.815   3.786  1.00131.95      B    O  
ANISOU 5612  O   VAL A  99     7158  35625   7351  -4651   2058    684  B    O  
ATOM   5613  CB  VAL A  99     -35.553   6.321   3.670  1.00130.62      B    C  
ANISOU 5613  CB  VAL A  99     7109  35267   7255  -5654   2411  -1714  B    C  
ATOM   5614  CG1 VAL A  99     -36.575   5.385   3.025  1.00130.47      B    C  
ANISOU 5614  CG1 VAL A  99     7121  35101   7351  -5786   2399  -2302  B    C  
ATOM   5615  CG2 VAL A  99     -34.215   5.607   3.850  1.00129.92      B    C  
ANISOU 5615  CG2 VAL A  99     7110  34972   7283  -6038   2621  -2575  B    C  
ATOM   5616  N   GLU A 100     -37.146   8.709   1.530  1.00132.32      B    N  
ANISOU 5616  N   GLU A 100     7405  35557   7316  -4565   2018    526  B    N  
ATOM   5617  CA  GLU A 100     -38.382   9.428   1.239  1.00133.08      B    C  
ANISOU 5617  CA  GLU A 100     7517  35565   7483  -4218   1878   1209  B    C  
ATOM   5618  C   GLU A 100     -39.509   8.416   1.034  1.00136.29      B    C  
ANISOU 5618  C   GLU A 100     8133  35490   8161  -4325   1833    527  B    C  
ATOM   5619  O   GLU A 100     -39.344   7.491   0.237  1.00135.75      B    O  
ANISOU 5619  O   GLU A 100     8129  35390   8059  -4558   1867   -160  B    O  
ATOM   5620  CB  GLU A 100     -38.199  10.310  -0.019  1.00134.73      B    C  
ANISOU 5620  CB  GLU A 100     7901  35582   7707  -3892   1833   1803  B    C  
ATOM   5621  CG  GLU A 100     -38.918  11.648   0.025  1.00142.25      B    C  
ANISOU 5621  CG  GLU A 100     9284  35533   9234  -3292   1771   2738  B    C  
ATOM   5622  CD  GLU A 100     -39.978  11.913  -1.031  1.00154.80      B    C  
ANISOU 5622  CD  GLU A 100    11791  35353  11674  -2855   1687   2648  B    C  
ATOM   5623  OE1 GLU A 100     -39.655  11.888  -2.240  1.00157.52      B    O  
ANISOU 5623  OE1 GLU A 100    12387  35413  12051  -2784   1684   2581  B    O  
ATOM   5624  OE2 GLU A 100     -41.139  12.159  -0.638  1.00143.50      B    O1-
ANISOU 5624  OE2 GLU A 100     9878  34726   9921  -2918   1591   2923  B    O1-
ATOM   5625  N   ILE A 101     -40.625   8.543   1.781  1.00134.88      B    N  
ANISOU 5625  N   ILE A 101     7800  35441   8008  -4277   1766    733  B    N  
ATOM   5626  CA  ILE A 101     -41.759   7.617   1.645  1.00135.36      B    C  
ANISOU 5626  CA  ILE A 101     7875  35380   8176  -4444   1723    148  B    C  
ATOM   5627  C   ILE A 101     -43.060   8.400   1.443  1.00139.32      B    C  
ANISOU 5627  C   ILE A 101     8533  35480   8923  -4038   1575    817  B    C  
ATOM   5628  O   ILE A 101     -43.380   9.295   2.230  1.00138.65      B    O  
ANISOU 5628  O   ILE A 101     8333  35484   8864  -3814   1545   1501  B    O  
ATOM   5629  CB  ILE A 101     -41.902   6.594   2.816  1.00137.01      B    C  
ANISOU 5629  CB  ILE A 101     8125  35296   8635  -4729   1829   -595  B    C  
ATOM   5630  CG1 ILE A 101     -40.592   5.813   3.068  1.00136.94      B    C  
ANISOU 5630  CG1 ILE A 101     8201  35139   8690  -5050   2005  -1335  B    C  
ATOM   5631  CG2 ILE A 101     -43.075   5.617   2.553  1.00137.86      B    C  
ANISOU 5631  CG2 ILE A 101     8267  35198   8918  -4874   1798  -1163  B    C  
ATOM   5632  CD1 ILE A 101     -40.529   5.100   4.401  1.00142.98      B    C  
ANISOU 5632  CD1 ILE A 101     9246  35104   9977  -5152   2129  -1868  B    C  
ATOM   5633  N   ASP A 102     -43.813   8.031   0.393  1.00138.22      B    N  
ANISOU 5633  N   ASP A 102     8388  35424   8704  -4077   1488    612  B    N  
ATOM   5634  CA  ASP A 102     -45.111   8.619   0.090  1.00138.97      B    C  
ANISOU 5634  CA  ASP A 102     8481  35447   8873  -3827   1348   1092  B    C  
ATOM   5635  C   ASP A 102     -46.197   7.640   0.526  1.00142.06      B    C  
ANISOU 5635  C   ASP A 102     8964  35454   9557  -3959   1325    523  B    C  
ATOM   5636  O   ASP A 102     -46.300   6.538  -0.017  1.00141.71      B    O  
ANISOU 5636  O   ASP A 102     8950  35369   9526  -4217   1344   -184  B    O  
ATOM   5637  CB  ASP A 102     -45.227   8.981  -1.402  1.00140.95      B    C  
ANISOU 5637  CB  ASP A 102     8951  35471   9133  -3646   1262   1273  B    C  
ATOM   5638  CG  ASP A 102     -44.346  10.136  -1.833  1.00147.05      B    C  
ANISOU 5638  CG  ASP A 102    10154  35517  10200  -3255   1295   1872  B    C  
ATOM   5639  OD1 ASP A 102     -44.407  11.208  -1.182  1.00147.26      B    O  
ANISOU 5639  OD1 ASP A 102    10147  35477  10328  -3002   1302   2560  B    O  
ATOM   5640  OD2 ASP A 102     -43.636   9.989  -2.849  1.00150.03      B    O1-
ANISOU 5640  OD2 ASP A 102    10842  35499  10663  -3224   1321   1673  B    O1-
ATOM   5641  N   SER A 103     -46.964   8.027   1.553  1.00140.00      B    N  
ANISOU 5641  N   SER A 103     8480  35434   9280  -3900   1298    863  B    N  
ATOM   5642  CA  SER A 103     -48.027   7.209   2.121  1.00140.07      B    C  
ANISOU 5642  CA  SER A 103     8404  35400   9418  -4076   1287    404  B    C  
ATOM   5643  C   SER A 103     -49.353   7.978   2.195  1.00143.86      B    C  
ANISOU 5643  C   SER A 103     9001  35482  10176  -3720   1157    993  B    C  
ATOM   5644  O   SER A 103     -49.409   9.163   1.865  1.00143.84      B    O  
ANISOU 5644  O   SER A 103     9020  35479  10153  -3404   1092   1745  B    O  
ATOM   5645  CB  SER A 103     -47.625   6.707   3.511  1.00141.67      B    C  
ANISOU 5645  CB  SER A 103     8633  35395   9800  -4244   1423     37  B    C  
ATOM   5646  OG  SER A 103     -47.646   7.729   4.496  1.00147.38      B    O  
ANISOU 5646  OG  SER A 103     9572  35575  10852  -3868   1418    741  B    O  
ATOM   5647  N   VAL A 104     -50.423   7.277   2.597  1.00142.20      B    N  
ANISOU 5647  N   VAL A 104     8620  35420   9991  -3897   1133    630  B    N  
ATOM   5648  CA  VAL A 104     -51.760   7.820   2.827  1.00142.66      B    C  
ANISOU 5648  CA  VAL A 104     8603  35432  10167  -3686   1024   1074  B    C  
ATOM   5649  C   VAL A 104     -52.433   6.941   3.894  1.00145.07      B    C  
ANISOU 5649  C   VAL A 104     8940  35422  10759  -3848   1087    575  B    C  
ATOM   5650  O   VAL A 104     -52.311   5.711   3.861  1.00144.22      B    O  
ANISOU 5650  O   VAL A 104     8820  35304  10671  -4184   1165   -219  B    O  
ATOM   5651  CB  VAL A 104     -52.629   8.031   1.545  1.00146.29      B    C  
ANISOU 5651  CB  VAL A 104     9293  35486  10805  -3487    874   1188  B    C  
ATOM   5652  CG1 VAL A 104     -52.970   6.722   0.837  1.00146.47      B    C  
ANISOU 5652  CG1 VAL A 104     9352  35450  10852  -3769    857    412  B    C  
ATOM   5653  CG2 VAL A 104     -53.892   8.835   1.849  1.00146.59      B    C  
ANISOU 5653  CG2 VAL A 104     9251  35473  10973  -3236    772   1738  B    C  
ATOM   5654  N   THR A 105     -53.092   7.591   4.865  1.00143.33      B    N  
ANISOU 5654  N   THR A 105     8511  35427  10520  -3711   1068   1080  B    N  
ATOM   5655  CA  THR A 105     -53.812   6.939   5.959  1.00143.27      B    C  
ANISOU 5655  CA  THR A 105     8385  35415  10635  -3882   1127    734  B    C  
ATOM   5656  C   THR A 105     -55.139   6.365   5.457  1.00146.96      B    C  
ANISOU 5656  C   THR A 105     8981  35459  11398  -3870   1037    437  B    C  
ATOM   5657  O   THR A 105     -55.586   6.675   4.347  1.00147.22      B    O  
ANISOU 5657  O   THR A 105     9059  35476  11403  -3733    908    643  B    O  
ATOM   5658  CB  THR A 105     -54.075   7.934   7.127  1.00148.43      B    C  
ANISOU 5658  CB  THR A 105     9224  35523  11650  -3504   1139   1433  B    C  
ATOM   5659  CG2 THR A 105     -52.810   8.575   7.667  1.00146.06      B    C  
ANISOU 5659  CG2 THR A 105     8864  35457  11176  -3443   1220   1833  B    C  
ATOM   5660  OG1 THR A 105     -55.003   8.945   6.724  1.00149.10      B    O  
ANISOU 5660  OG1 THR A 105     9309  35504  11838  -3161   1014   2127  B    O  
ATOM   5661  N   SER A 106     -55.769   5.540   6.289  1.00144.64      B    N  
ANISOU 5661  N   SER A 106     8483  35359  11115  -4138   1111    -36  B    N  
ATOM   5662  CA  SER A 106     -57.097   5.006   6.038  1.00145.11      B    C  
ANISOU 5662  CA  SER A 106     8485  35322  11329  -4192   1040   -272  B    C  
ATOM   5663  C   SER A 106     -58.075   5.895   6.817  1.00147.74      B    C  
ANISOU 5663  C   SER A 106     8831  35421  11884  -3873    980    367  B    C  
ATOM   5664  O   SER A 106     -57.661   6.418   7.860  1.00146.57      B    O  
ANISOU 5664  O   SER A 106     8599  35416  11675  -3809   1057    689  B    O  
ATOM   5665  CB  SER A 106     -57.173   3.546   6.482  1.00147.71      B    C  
ANISOU 5665  CB  SER A 106     8942  35213  11967  -4508   1185  -1164  B    C  
ATOM   5666  OG  SER A 106     -58.483   3.014   6.370  1.00156.45      B    O  
ANISOU 5666  OG  SER A 106    10372  35400  13674  -4347   1116  -1280  B    O  
ATOM   5667  N   PRO A 107     -59.351   6.112   6.378  1.00146.05      B    N  
ANISOU 5667  N   PRO A 107     8449  35389  11654  -3784    847    590  B    N  
ATOM   5668  CA  PRO A 107     -60.269   6.946   7.186  1.00145.88      B    C  
ANISOU 5668  CA  PRO A 107     8299  35398  11732  -3541    810   1194  B    C  
ATOM   5669  C   PRO A 107     -60.550   6.351   8.573  1.00147.43      B    C  
ANISOU 5669  C   PRO A 107     8482  35406  12127  -3681    943    875  B    C  
ATOM   5670  O   PRO A 107     -61.003   7.064   9.469  1.00147.43      B    O  
ANISOU 5670  O   PRO A 107     8386  35435  12195  -3482    950   1404  B    O  
ATOM   5671  CB  PRO A 107     -61.552   6.990   6.345  1.00147.97      B    C  
ANISOU 5671  CB  PRO A 107     8621  35410  12191  -3413    657   1250  B    C  
ATOM   5672  CG  PRO A 107     -61.145   6.560   4.977  1.00151.40      B    C  
ANISOU 5672  CG  PRO A 107     9355  35461  12709  -3441    589    909  B    C  
ATOM   5673  CD  PRO A 107     -60.028   5.596   5.171  1.00147.73      B    C  
ANISOU 5673  CD  PRO A 107     8774  35376  11982  -3812    730    304  B    C  
ATOM   5674  N   LYS A 108     -60.250   5.048   8.746  1.00143.92      B    N  
ANISOU 5674  N   LYS A 108     7897  35246  11540  -4131   1066     18  B    N  
ATOM   5675  CA  LYS A 108     -60.445   4.276   9.972  1.00143.29      B    C  
ANISOU 5675  CA  LYS A 108     7731  35151  11562  -4387   1228   -475  B    C  
ATOM   5676  C   LYS A 108     -59.222   4.336  10.909  1.00144.17      B    C  
ANISOU 5676  C   LYS A 108     7979  35122  11678  -4441   1380   -555  B    C  
ATOM   5677  O   LYS A 108     -59.264   3.739  11.989  1.00143.01      B    O  
ANISOU 5677  O   LYS A 108     7769  34973  11596  -4695   1543  -1044  B    O  
ATOM   5678  CB  LYS A 108     -60.786   2.815   9.612  1.00145.41      B    C  
ANISOU 5678  CB  LYS A 108     8136  34990  12122  -4686   1309  -1380  B    C  
ATOM   5679  CG  LYS A 108     -62.088   2.665   8.803  1.00156.73      B    C  
ANISOU 5679  CG  LYS A 108    10092  35162  14296  -4299   1140  -1197  B    C  
ATOM   5680  CD  LYS A 108     -63.295   2.366   9.714  1.00163.95      B    C  
ANISOU 5680  CD  LYS A 108    11263  35201  15830  -4135   1171  -1198  B    C  
ATOM   5681  CE  LYS A 108     -64.640   2.674   9.104  1.00173.34      B    C  
ANISOU 5681  CE  LYS A 108    12828  35435  17598  -3729    988   -808  B    C  
ATOM   5682  NZ  LYS A 108     -65.743   2.434  10.067  1.00179.71      B    N1+
ANISOU 5682  NZ  LYS A 108    13829  35503  18951  -3606   1036   -823  B    N1+
ATOM   5683  N   SER A 109     -58.160   5.086  10.512  1.00141.61      B    N  
ANISOU 5683  N   SER A 109     7598  35167  11039  -4322   1336    -89  B    N  
ATOM   5684  CA  SER A 109     -56.901   5.292  11.248  1.00140.63      B    C  
ANISOU 5684  CA  SER A 109     7493  35162  10777  -4389   1451    -60  B    C  
ATOM   5685  C   SER A 109     -57.150   5.386  12.758  1.00143.42      B    C  
ANISOU 5685  C   SER A 109     7898  35252  11344  -4347   1551     33  B    C  
ATOM   5686  O   SER A 109     -57.906   6.253  13.204  1.00143.24      B    O  
ANISOU 5686  O   SER A 109     7758  35317  11352  -4048   1469    789  B    O  
ATOM   5687  CB  SER A 109     -56.196   6.552  10.747  1.00142.32      B    C  
ANISOU 5687  CB  SER A 109     7857  35250  10968  -3978   1348    823  B    C  
ATOM   5688  OG  SER A 109     -54.894   6.705  11.284  1.00145.06      B    O  
ANISOU 5688  OG  SER A 109     8492  35171  11453  -3942   1450    797  B    O  
ATOM   5689  N   SER A 110     -56.568   4.440  13.528  1.00140.98      B    N  
ANISOU 5689  N   SER A 110     7521  35091  10955  -4790   1753   -807  B    N  
ATOM   5690  CA  SER A 110     -56.717   4.351  14.988  1.00140.63      B    C  
ANISOU 5690  CA  SER A 110     7419  35047  10968  -4902   1885   -916  B    C  
ATOM   5691  C   SER A 110     -56.196   5.612  15.719  1.00143.36      B    C  
ANISOU 5691  C   SER A 110     7857  35296  11318  -4483   1812    128  B    C  
ATOM   5692  O   SER A 110     -56.741   5.979  16.766  1.00143.76      B    O  
ANISOU 5692  O   SER A 110     7832  35360  11431  -4365   1832    515  B    O  
ATOM   5693  CB  SER A 110     -56.031   3.094  15.524  1.00142.12      B    C  
ANISOU 5693  CB  SER A 110     7842  34712  11445  -5340   2157  -2102  B    C  
ATOM   5694  OG  SER A 110     -54.671   2.995  15.135  1.00146.62      B    O  
ANISOU 5694  OG  SER A 110     8799  34695  12217  -5288   2200  -2261  B    O  
ATOM   5695  N   ALA A 111     -55.187   6.295  15.144  1.00139.82      B    N  
ANISOU 5695  N   ALA A 111     7299  35269  10556  -4360   1734    648  B    N  
ATOM   5696  CA  ALA A 111     -54.604   7.506  15.723  1.00139.30      B    C  
ANISOU 5696  CA  ALA A 111     7188  35297  10444  -3974   1680   1754  B    C  
ATOM   5697  C   ALA A 111     -55.488   8.748  15.586  1.00142.26      B    C  
ANISOU 5697  C   ALA A 111     7634  35261  11156  -3363   1553   2921  B    C  
ATOM   5698  O   ALA A 111     -55.334   9.678  16.373  1.00141.25      B    O  
ANISOU 5698  O   ALA A 111     7439  35066  11165  -3006   1561   3894  B    O  
ATOM   5699  CB  ALA A 111     -53.265   7.793  15.072  1.00139.49      B    C  
ANISOU 5699  CB  ALA A 111     7334  35311  10357  -3942   1676   1843  B    C  
ATOM   5700  N   LEU A 112     -56.366   8.801  14.580  1.00141.38      B    N  
ANISOU 5700  N   LEU A 112     7435  35273  11008  -3315   1449   2917  B    N  
ATOM   5701  CA  LEU A 112     -57.131  10.024  14.329  1.00142.11      B    C  
ANISOU 5701  CA  LEU A 112     7524  35117  11354  -2817   1355   3925  B    C  
ATOM   5702  C   LEU A 112     -58.633   9.895  14.570  1.00147.03      B    C  
ANISOU 5702  C   LEU A 112     8264  35261  12339  -2725   1325   3799  B    C  
ATOM   5703  O   LEU A 112     -59.178   8.799  14.537  1.00146.74      B    O  
ANISOU 5703  O   LEU A 112     8156  35403  12198  -3089   1341   2962  B    O  
ATOM   5704  CB  LEU A 112     -56.898  10.494  12.876  1.00142.32      B    C  
ANISOU 5704  CB  LEU A 112     7652  35086  11337  -2690   1260   4056  B    C  
ATOM   5705  CG  LEU A 112     -55.459  10.450  12.327  1.00145.00      B    C  
ANISOU 5705  CG  LEU A 112     8264  35181  11647  -2741   1298   3826  B    C  
ATOM   5706  CD1 LEU A 112     -55.456  10.445  10.823  1.00145.35      B    C  
ANISOU 5706  CD1 LEU A 112     8405  35224  11597  -2768   1205   3592  B    C  
ATOM   5707  CD2 LEU A 112     -54.611  11.576  12.885  1.00145.76      B    C  
ANISOU 5707  CD2 LEU A 112     8469  34946  11969  -2360   1358   4732  B    C  
ATOM   5708  N   GLN A 113     -59.294  11.039  14.791  1.00146.49      B    N  
ANISOU 5708  N   GLN A 113     8119  35034  12506  -2300   1292   4757  B    N  
ATOM   5709  CA  GLN A 113     -60.740  11.142  14.956  1.00147.90      B    C  
ANISOU 5709  CA  GLN A 113     8257  35021  12919  -2184   1251   4854  B    C  
ATOM   5710  C   GLN A 113     -61.237  12.277  14.060  1.00152.38      B    C  
ANISOU 5710  C   GLN A 113     9111  34905  13883  -1787   1173   5334  B    C  
ATOM   5711  O   GLN A 113     -60.812  13.424  14.220  1.00151.59      B    O  
ANISOU 5711  O   GLN A 113     9063  34535  14001  -1432   1223   6146  B    O  
ATOM   5712  CB  GLN A 113     -61.134  11.336  16.439  1.00148.69      B    C  
ANISOU 5712  CB  GLN A 113     8330  34874  13292  -2025   1354   5267  B    C  
ATOM   5713  CG  GLN A 113     -62.523  11.949  16.687  1.00162.25      B    C  
ANISOU 5713  CG  GLN A 113    10712  35001  15936  -1647   1359   5224  B    C  
ATOM   5714  CD  GLN A 113     -63.655  10.958  16.806  1.00179.33      B    C  
ANISOU 5714  CD  GLN A 113    13631  35704  18800  -1762   1362   4010  B    C  
ATOM   5715  NE2 GLN A 113     -64.424  11.085  17.872  1.00172.84      B    N  
ANISOU 5715  NE2 GLN A 113    12383  35416  17871  -1733   1412   4461  B    N  
ATOM   5716  OE1 GLN A 113     -63.909  10.135  15.917  1.00178.63      B    O  
ANISOU 5716  OE1 GLN A 113    13434  35941  18496  -2015   1283   3460  B    O  
ATOM   5717  N   TRP A 114     -62.122  11.931  13.111  1.00151.88      B    N  
ANISOU 5717  N   TRP A 114     8960  35050  13697  -1912   1053   4968  B    N  
ATOM   5718  CA  TRP A 114     -62.740  12.851  12.160  1.00152.78      B    C  
ANISOU 5718  CA  TRP A 114     9163  34902  13983  -1644    954   5356  B    C  
ATOM   5719  C   TRP A 114     -64.205  13.066  12.554  1.00156.48      B    C  
ANISOU 5719  C   TRP A 114     9735  34862  14859  -1492    930   5384  B    C  
ATOM   5720  O   TRP A 114     -65.066  12.239  12.228  1.00156.85      B    O  
ANISOU 5720  O   TRP A 114     9690  35080  14826  -1712    853   4840  B    O  
ATOM   5721  CB  TRP A 114     -62.623  12.315  10.718  1.00152.66      B    C  
ANISOU 5721  CB  TRP A 114     9180  35120  13705  -1855    834   4818  B    C  
ATOM   5722  CG  TRP A 114     -61.239  11.899  10.319  1.00153.17      B    C  
ANISOU 5722  CG  TRP A 114     9369  35276  13554  -2027    873   4489  B    C  
ATOM   5723  CD1 TRP A 114     -60.673  10.670  10.488  1.00155.08      B    C  
ANISOU 5723  CD1 TRP A 114     9698  35533  13694  -2372    931   3693  B    C  
ATOM   5724  CD2 TRP A 114     -60.257  12.707   9.660  1.00152.84      B    C  
ANISOU 5724  CD2 TRP A 114     9453  35153  13465  -1854    872   4883  B    C  
ATOM   5725  CE2 TRP A 114     -59.111  11.904   9.472  1.00155.33      B    C  
ANISOU 5725  CE2 TRP A 114     9957  35399  13661  -2097    924   4286  B    C  
ATOM   5726  CE3 TRP A 114     -60.232  14.038   9.210  1.00153.69      B    C  
ANISOU 5726  CE3 TRP A 114     9709  34890  13796  -1494    856   5553  B    C  
ATOM   5727  NE1 TRP A 114     -59.392  10.666   9.988  1.00154.45      B    N  
ANISOU 5727  NE1 TRP A 114     9700  35566  13418  -2440    957   3618  B    N  
ATOM   5728  CZ2 TRP A 114     -57.955  12.383   8.846  1.00154.56      B    C  
ANISOU 5728  CZ2 TRP A 114     9953  35336  13436  -2027    939   4500  B    C  
ATOM   5729  CZ3 TRP A 114     -59.085  14.513   8.595  1.00154.44      B    C  
ANISOU 5729  CZ3 TRP A 114     9987  34844  13849  -1418    882   5700  B    C  
ATOM   5730  CH2 TRP A 114     -57.965  13.690   8.415  1.00154.67      B    C  
ANISOU 5730  CH2 TRP A 114    10064  35080  13625  -1679    918   5203  B    C  
ATOM   5731  N   LEU A 115     -64.475  14.153  13.302  1.00153.97      B    N  
ANISOU 5731  N   LEU A 115     9323  34391  14786  -1154   1003   6222  B    N  
ATOM   5732  CA  LEU A 115     -65.821  14.489  13.766  1.00154.21      B    C  
ANISOU 5732  CA  LEU A 115     9286  34206  15100   -999    997   6443  B    C  
ATOM   5733  C   LEU A 115     -66.455  15.554  12.858  1.00157.11      B    C  
ANISOU 5733  C   LEU A 115     9908  34005  15781   -732    916   6656  B    C  
ATOM   5734  O   LEU A 115     -65.817  16.560  12.533  1.00156.32      B    O  
ANISOU 5734  O   LEU A 115     9921  33695  15778   -510    951   7133  B    O  
ATOM   5735  CB  LEU A 115     -65.851  14.911  15.254  1.00153.64      B    C  
ANISOU 5735  CB  LEU A 115     9178  33860  15336   -791   1158   6994  B    C  
ATOM   5736  CG  LEU A 115     -64.958  16.062  15.727  1.00155.97      B    C  
ANISOU 5736  CG  LEU A 115     9781  33418  16060   -447   1300   7607  B    C  
ATOM   5737  CD1 LEU A 115     -65.697  16.952  16.690  1.00155.61      B    C  
ANISOU 5737  CD1 LEU A 115     9749  32844  16530   -116   1427   8243  B    C  
ATOM   5738  CD2 LEU A 115     -63.705  15.541  16.399  1.00157.37      B    C  
ANISOU 5738  CD2 LEU A 115    10071  33563  16161   -568   1393   7447  B    C  
ATOM   5739  N   ASN A 116     -67.715  15.302  12.443  1.00155.31      B    N  
ANISOU 5739  N   ASN A 116     9483  34024  15505   -786    806   6512  B    N  
ATOM   5740  CA  ASN A 116     -68.504  16.141  11.534  1.00155.54      B    C  
ANISOU 5740  CA  ASN A 116     9573  33843  15681   -594    701   6723  B    C  
ATOM   5741  C   ASN A 116     -68.799  17.544  12.105  1.00157.97      B    C  
ANISOU 5741  C   ASN A 116    10115  33399  16509   -211    807   7316  B    C  
ATOM   5742  O   ASN A 116     -68.532  17.811  13.279  1.00156.81      B    O  
ANISOU 5742  O   ASN A 116     9926  33092  16562    -85    964   7713  B    O  
ATOM   5743  CB  ASN A 116     -69.817  15.432  11.177  1.00155.54      B    C  
ANISOU 5743  CB  ASN A 116     9444  34007  15646   -754    572   6262  B    C  
ATOM   5744  CG  ASN A 116     -69.624  14.153  10.403  1.00163.80      B    C  
ANISOU 5744  CG  ASN A 116    11141  34170  16927  -1040    491   4999  B    C  
ATOM   5745  ND2 ASN A 116     -69.883  14.202   9.107  1.00156.02      B    N  
ANISOU 5745  ND2 ASN A 116     9843  33874  15562  -1099    332   5102  B    N  
ATOM   5746  OD1 ASN A 116     -69.237  13.116  10.951  1.00159.17      B    O  
ANISOU 5746  OD1 ASN A 116    10243  34220  16014  -1312    550   4777  B    O  
ATOM   5747  N   LYS A 117     -69.348  18.438  11.248  1.00156.21      B    N  
ANISOU 5747  N   LYS A 117     9865  33146  16344    -32    726   7626  B    N  
ATOM   5748  CA  LYS A 117     -69.735  19.820  11.564  1.00155.75      B    C  
ANISOU 5748  CA  LYS A 117     9892  32589  16697    309    818   8242  B    C  
ATOM   5749  C   LYS A 117     -70.899  19.857  12.584  1.00158.51      B    C  
ANISOU 5749  C   LYS A 117    10288  32524  17414    383    872   8187  B    C  
ATOM   5750  O   LYS A 117     -71.083  20.863  13.277  1.00157.38      B    O  
ANISOU 5750  O   LYS A 117    10182  31962  17652    648   1017   8727  B    O  
ATOM   5751  CB  LYS A 117     -70.124  20.544  10.269  1.00158.13      B    C  
ANISOU 5751  CB  LYS A 117    10404  32633  17045    394    681   8139  B    C  
ATOM   5752  CG  LYS A 117     -69.982  22.058  10.321  1.00167.64      B    C  
ANISOU 5752  CG  LYS A 117    12303  32522  18869    655    765   8097  B    C  
ATOM   5753  CD  LYS A 117     -69.871  22.675   8.921  1.00174.93      B    C  
ANISOU 5753  CD  LYS A 117    13752  32844  19868    660    626   7635  B    C  
ATOM   5754  CE  LYS A 117     -71.158  22.675   8.122  1.00184.56      B    C  
ANISOU 5754  CE  LYS A 117    15410  33422  21293    599    423   6857  B    C  
ATOM   5755  NZ  LYS A 117     -72.187  23.579   8.702  1.00191.96      B    N1+
ANISOU 5755  NZ  LYS A 117    16738  33477  22719    737    434   6629  B    N1+
ATOM   5756  N   GLU A 118     -71.667  18.749  12.667  1.00156.98      B    N  
ANISOU 5756  N   GLU A 118     9815  32854  16977    159    777   7822  B    N  
ATOM   5757  CA  GLU A 118     -72.783  18.530  13.589  1.00157.14      B    C  
ANISOU 5757  CA  GLU A 118     9703  32803  17200    179    819   7824  B    C  
ATOM   5758  C   GLU A 118     -72.250  18.066  14.960  1.00159.17      B    C  
ANISOU 5758  C   GLU A 118    10049  32831  17597    133    985   7783  B    C  
ATOM   5759  O   GLU A 118     -72.908  18.290  15.979  1.00158.56      B    O  
ANISOU 5759  O   GLU A 118     9902  32544  17801    262   1094   8060  B    O  
ATOM   5760  CB  GLU A 118     -73.747  17.484  12.995  1.00159.24      B    C  
ANISOU 5760  CB  GLU A 118     9892  33319  17294    -80    645   7133  B    C  
ATOM   5761  CG  GLU A 118     -75.191  17.623  13.448  1.00167.02      B    C  
ANISOU 5761  CG  GLU A 118    11196  33475  18791     -8    631   6739  B    C  
ATOM   5762  CD  GLU A 118     -76.188  16.742  12.716  1.00180.95      B    C  
ANISOU 5762  CD  GLU A 118    13597  34216  20941   -213    464   5462  B    C  
ATOM   5763  OE1 GLU A 118     -76.363  16.928  11.489  1.00177.00      B    O  
ANISOU 5763  OE1 GLU A 118    12934  34096  20223   -209    310   5551  B    O  
ATOM   5764  OE2 GLU A 118     -76.828  15.893  13.378  1.00175.39      B    O1-
ANISOU 5764  OE2 GLU A 118    12446  34121  20074   -366    495   5472  B    O1-
ATOM   5765  N   GLN A 119     -71.052  17.424  14.970  1.00156.44      B    N  
ANISOU 5765  N   GLN A 119     9581  32960  16901    -37   1011   7736  B    N  
ATOM   5766  CA  GLN A 119     -70.348  16.902  16.153  1.00155.63      B    C  
ANISOU 5766  CA  GLN A 119     9419  32929  16783   -104   1155   7814  B    C  
ATOM   5767  C   GLN A 119     -69.502  17.976  16.854  1.00157.81      B    C  
ANISOU 5767  C   GLN A 119     9998  32457  17504    201   1339   8357  B    C  
ATOM   5768  O   GLN A 119     -69.127  17.795  18.014  1.00156.38      B    O  
ANISOU 5768  O   GLN A 119     9760  32199  17459    246   1489   8625  B    O  
ATOM   5769  CB  GLN A 119     -69.441  15.728  15.762  1.00156.51      B    C  
ANISOU 5769  CB  GLN A 119     9538  33464  16465   -456   1092   7170  B    C  
ATOM   5770  CG  GLN A 119     -70.109  14.369  15.843  1.00162.24      B    C  
ANISOU 5770  CG  GLN A 119    10533  33823  17286   -777   1060   6113  B    C  
ATOM   5771  CD  GLN A 119     -69.130  13.266  15.537  1.00170.34      B    C  
ANISOU 5771  CD  GLN A 119    12137  34181  18402  -1054   1061   5070  B    C  
ATOM   5772  NE2 GLN A 119     -68.398  12.823  16.550  1.00163.00      B    N  
ANISOU 5772  NE2 GLN A 119    10852  33927  17154  -1157   1178   5372  B    N  
ATOM   5773  OE1 GLN A 119     -69.010  12.807  14.397  1.00166.39      B    O  
ANISOU 5773  OE1 GLN A 119    11441  34236  17545  -1247    941   4802  B    O  
ATOM   5774  N   THR A 120     -69.180  19.072  16.140  1.00156.45      B    N  
ANISOU 5774  N   THR A 120     9885  32111  17449    422   1346   8805  B    N  
ATOM   5775  CA  THR A 120     -68.395  20.202  16.659  1.00155.79      B    C  
ANISOU 5775  CA  THR A 120     9964  31437  17792    723   1540   9447  B    C  
ATOM   5776  C   THR A 120     -69.313  21.170  17.416  1.00158.54      B    C  
ANISOU 5776  C   THR A 120    10522  30966  18750    981   1666   9689  B    C  
ATOM   5777  O   THR A 120     -70.535  20.999  17.372  1.00159.14      B    O  
ANISOU 5777  O   THR A 120    10503  31140  18824    943   1586   9501  B    O  
ATOM   5778  CB  THR A 120     -67.649  20.924  15.516  1.00163.13      B    C  
ANISOU 5778  CB  THR A 120    11424  31768  18790    735   1462   9063  B    C  
ATOM   5779  CG2 THR A 120     -66.564  20.070  14.890  1.00162.04      B    C  
ANISOU 5779  CG2 THR A 120    11216  32172  18179    506   1386   8783  B    C  
ATOM   5780  OG1 THR A 120     -68.585  21.354  14.523  1.00165.12      B    O  
ANISOU 5780  OG1 THR A 120    11735  31991  19013    749   1313   8861  B    O  
ATOM   5781  N   ALA A 121     -68.732  22.187  18.098  1.00155.01      B    N  
ANISOU 5781  N   ALA A 121    10084  30034  18778   1283   1903  10432  B    N  
ATOM   5782  CA  ALA A 121     -69.493  23.194  18.841  1.00154.17      B    C  
ANISOU 5782  CA  ALA A 121    10046  29255  19278   1557   2081  10852  B    C  
ATOM   5783  C   ALA A 121     -70.403  23.981  17.885  1.00157.32      B    C  
ANISOU 5783  C   ALA A 121    10625  29453  19696   1587   1938  10585  B    C  
ATOM   5784  O   ALA A 121     -69.925  24.765  17.054  1.00156.51      B    O  
ANISOU 5784  O   ALA A 121    10616  29240  19610   1674   1927  10735  B    O  
ATOM   5785  CB  ALA A 121     -68.555  24.124  19.595  1.00153.34      B    C  
ANISOU 5785  CB  ALA A 121    10141  28362  19759   1798   2356  11327  B    C  
ATOM   5786  N   GLY A 122     -71.701  23.673  17.970  1.00155.87      B    N  
ANISOU 5786  N   GLY A 122    10200  29586  19437   1561   1859  10545  B    N  
ATOM   5787  CA  GLY A 122     -72.756  24.254  17.146  1.00156.29      B    C  
ANISOU 5787  CA  GLY A 122    10246  29659  19477   1610   1729  10453  B    C  
ATOM   5788  C   GLY A 122     -72.868  23.605  15.781  1.00159.60      B    C  
ANISOU 5788  C   GLY A 122    10724  30536  19380   1365   1445   9812  B    C  
ATOM   5789  O   GLY A 122     -73.198  22.419  15.677  1.00159.96      B    O  
ANISOU 5789  O   GLY A 122    10601  31106  19070   1129   1316   9400  B    O  
ATOM   5790  N   LYS A 123     -72.583  24.395  14.724  1.00156.89      B    N  
ANISOU 5790  N   LYS A 123    10353  30288  18971   1472   1398  10082  B    N  
ATOM   5791  CA  LYS A 123     -72.616  24.021  13.304  1.00157.30      B    C  
ANISOU 5791  CA  LYS A 123    10372  30812  18584   1314   1165   9725  B    C  
ATOM   5792  C   LYS A 123     -71.802  25.071  12.530  1.00158.50      B    C  
ANISOU 5792  C   LYS A 123    10798  30589  18835   1435   1188   9868  B    C  
ATOM   5793  O   LYS A 123     -72.379  25.942  11.872  1.00158.53      B    O  
ANISOU 5793  O   LYS A 123    10874  30399  18961   1560   1135   9962  B    O  
ATOM   5794  CB  LYS A 123     -74.082  23.942  12.807  1.00159.95      B    C  
ANISOU 5794  CB  LYS A 123    10722  31142  18910   1265    988   9326  B    C  
ATOM   5795  CG  LYS A 123     -74.280  23.217  11.480  1.00168.90      B    C  
ANISOU 5795  CG  LYS A 123    12324  32025  19826    985    708   8212  B    C  
ATOM   5796  CD  LYS A 123     -75.533  23.720  10.773  1.00174.75      B    C  
ANISOU 5796  CD  LYS A 123    13396  32221  20780   1015    543   7722  B    C  
ATOM   5797  CE  LYS A 123     -75.998  22.796   9.677  1.00181.63      B    C  
ANISOU 5797  CE  LYS A 123    14555  32904  21554    775    308   6791  B    C  
ATOM   5798  NZ  LYS A 123     -76.757  21.638  10.216  1.00187.31      B    N1+
ANISOU 5798  NZ  LYS A 123    15406  33321  22444    601    280   6133  B    N1+
ATOM   5799  N   ILE A 124     -70.461  25.033  12.665  1.00154.50      B    N  
ANISOU 5799  N   ILE A 124    10174  30302  18226   1456   1307  10253  B    N  
ATOM   5800  CA  ILE A 124     -69.605  26.035  12.021  1.00153.46      B    C  
ANISOU 5800  CA  ILE A 124    10184  29934  18191   1591   1369  10558  B    C  
ATOM   5801  C   ILE A 124     -68.611  25.376  11.036  1.00154.67      B    C  
ANISOU 5801  C   ILE A 124    10406  30476  17884   1387   1236  10207  B    C  
ATOM   5802  O   ILE A 124     -68.663  25.690   9.844  1.00154.97      B    O  
ANISOU 5802  O   ILE A 124    10512  30635  17737   1369   1103  10094  B    O  
ATOM   5803  CB  ILE A 124     -68.876  26.943  13.073  1.00154.49      B    C  
ANISOU 5803  CB  ILE A 124    10548  29276  18877   1785   1639  10905  B    C  
ATOM   5804  CG1 ILE A 124     -69.831  27.483  14.189  1.00154.42      B    C  
ANISOU 5804  CG1 ILE A 124    10549  28752  19373   1958   1788  11121  B    C  
ATOM   5805  CG2 ILE A 124     -68.071  28.077  12.413  1.00154.54      B    C  
ANISOU 5805  CG2 ILE A 124    10764  28921  19034   1904   1707  11110  B    C  
ATOM   5806  CD1 ILE A 124     -70.985  28.490  13.754  1.00159.86      B    C  
ANISOU 5806  CD1 ILE A 124    11574  28882  20285   2021   1692  10780  B    C  
ATOM   5807  N   HIS A 125     -67.705  24.498  11.530  1.00150.31      B    N  
ANISOU 5807  N   HIS A 125     9575  30458  17079   1286   1307  10390  B    N  
ATOM   5808  CA  HIS A 125     -66.665  23.835  10.725  1.00149.46      B    C  
ANISOU 5808  CA  HIS A 125     9431  30848  16509   1095   1216  10169  B    C  
ATOM   5809  C   HIS A 125     -66.306  22.422  11.265  1.00149.63      B    C  
ANISOU 5809  C   HIS A 125     9330  31313  16209    833   1183   9767  B    C  
ATOM   5810  O   HIS A 125     -66.553  22.167  12.446  1.00148.62      B    O  
ANISOU 5810  O   HIS A 125     9089  31109  16271    871   1295   9929  B    O  
ATOM   5811  CB  HIS A 125     -65.392  24.711  10.702  1.00149.20      B    C  
ANISOU 5811  CB  HIS A 125     9581  30410  16698   1247   1376  10540  B    C  
ATOM   5812  CG  HIS A 125     -65.481  25.913   9.814  1.00151.66      B    C  
ANISOU 5812  CG  HIS A 125    10179  30241  17203   1381   1351  10570  B    C  
ATOM   5813  CD2 HIS A 125     -65.442  25.998   8.464  1.00153.56      B    C  
ANISOU 5813  CD2 HIS A 125    10563  30620  17163   1289   1182  10257  B    C  
ATOM   5814  ND1 HIS A 125     -65.604  27.187  10.338  1.00152.17      B    N  
ANISOU 5814  ND1 HIS A 125    10414  29589  17817   1627   1522  10940  B    N  
ATOM   5815  CE1 HIS A 125     -65.646  28.001   9.297  1.00152.11      B    C  
ANISOU 5815  CE1 HIS A 125    10509  29506  17780   1692   1458  10996  B    C  
ATOM   5816  NE2 HIS A 125     -65.551  27.332   8.148  1.00153.19      B    N  
ANISOU 5816  NE2 HIS A 125    10651  30127  17428   1500   1251  10595  B    N  
ATOM   5817  N   PRO A 126     -65.675  21.512  10.457  1.00145.97      B    N  
ANISOU 5817  N   PRO A 126     8623  31681  15157    594   1063   9556  B    N  
ATOM   5818  CA  PRO A 126     -65.286  20.188  10.997  1.00144.95      B    C  
ANISOU 5818  CA  PRO A 126     8307  32086  14683    322   1048   9197  B    C  
ATOM   5819  C   PRO A 126     -64.057  20.260  11.922  1.00143.49      B    C  
ANISOU 5819  C   PRO A 126     8119  31796  14606    388   1231   9552  B    C  
ATOM   5820  O   PRO A 126     -63.477  21.332  12.102  1.00142.04      B    O  
ANISOU 5820  O   PRO A 126     8026  31173  14770    655   1381  10142  B    O  
ATOM   5821  CB  PRO A 126     -64.985  19.371   9.736  1.00147.04      B    C  
ANISOU 5821  CB  PRO A 126     8661  32706  14504     32    867   8497  B    C  
ATOM   5822  CG  PRO A 126     -64.517  20.379   8.752  1.00150.40      B    C  
ANISOU 5822  CG  PRO A 126     9448  32598  15099    188    851   8573  B    C  
ATOM   5823  CD  PRO A 126     -65.292  21.639   9.031  1.00147.30      B    C  
ANISOU 5823  CD  PRO A 126     8952  31940  15077    515    930   9286  B    C  
ATOM   5824  N   TYR A 127     -63.660  19.118  12.509  1.00139.40      B    N  
ANISOU 5824  N   TYR A 127     7241  32047  13678    155   1235   9451  B    N  
ATOM   5825  CA  TYR A 127     -62.532  19.053  13.439  1.00138.05      B    C  
ANISOU 5825  CA  TYR A 127     7032  31838  13583    200   1396   9773  B    C  
ATOM   5826  C   TYR A 127     -61.781  17.731  13.303  1.00139.61      B    C  
ANISOU 5826  C   TYR A 127     7188  32615  13243   -198   1309   9057  B    C  
ATOM   5827  O   TYR A 127     -62.394  16.689  13.053  1.00139.55      B    O  
ANISOU 5827  O   TYR A 127     7035  33130  12857   -513   1179   8413  B    O  
ATOM   5828  CB  TYR A 127     -63.063  19.194  14.871  1.00138.69      B    C  
ANISOU 5828  CB  TYR A 127     7107  31475  14115    365   1546  10092  B    C  
ATOM   5829  CG  TYR A 127     -62.081  19.639  15.935  1.00139.17      B    C  
ANISOU 5829  CG  TYR A 127     7313  30929  14635    585   1772  10582  B    C  
ATOM   5830  CD1 TYR A 127     -62.089  20.947  16.410  1.00139.77      B    C  
ANISOU 5830  CD1 TYR A 127     7593  30061  15452    969   1978  11195  B    C  
ATOM   5831  CD2 TYR A 127     -61.281  18.714  16.605  1.00139.54      B    C  
ANISOU 5831  CD2 TYR A 127     7325  31239  14455    392   1796  10342  B    C  
ATOM   5832  CE1 TYR A 127     -61.254  21.346  17.452  1.00139.14      B    C  
ANISOU 5832  CE1 TYR A 127     7616  29347  15904   1190   2225  11677  B    C  
ATOM   5833  CE2 TYR A 127     -60.429  19.105  17.640  1.00139.19      B    C  
ANISOU 5833  CE2 TYR A 127     7379  30614  14894    624   2017  10870  B    C  
ATOM   5834  CZ  TYR A 127     -60.415  20.425  18.057  1.00142.89      B    C  
ANISOU 5834  CZ  TYR A 127     8262  29814  16216    993   2218  11240  B    C  
ATOM   5835  OH  TYR A 127     -59.588  20.820  19.081  1.00141.33      B    O  
ANISOU 5835  OH  TYR A 127     8162  28932  16606   1236   2476  11747  B    O  
ATOM   5836  N   LEU A 128     -60.452  17.782  13.495  1.00136.06      B    N  
ANISOU 5836  N   LEU A 128     6596  32456  12644   -180   1404   9428  B    N  
ATOM   5837  CA  LEU A 128     -59.545  16.635  13.475  1.00135.65      B    C  
ANISOU 5837  CA  LEU A 128     6450  33022  12070   -553   1355   8839  B    C  
ATOM   5838  C   LEU A 128     -58.542  16.750  14.608  1.00136.50      B    C  
ANISOU 5838  C   LEU A 128     6611  32830  12424   -430   1523   9226  B    C  
ATOM   5839  O   LEU A 128     -58.000  17.830  14.847  1.00135.73      B    O  
ANISOU 5839  O   LEU A 128     6608  32167  12796    -64   1674   9993  B    O  
ATOM   5840  CB  LEU A 128     -58.799  16.509  12.125  1.00136.02      B    C  
ANISOU 5840  CB  LEU A 128     6594  33322  11764   -717   1256   8451  B    C  
ATOM   5841  CG  LEU A 128     -57.529  15.618  12.110  1.00139.26      B    C  
ANISOU 5841  CG  LEU A 128     7194  33805  11914  -1022   1266   7771  B    C  
ATOM   5842  CD1 LEU A 128     -57.873  14.122  12.128  1.00139.66      B    C  
ANISOU 5842  CD1 LEU A 128     7140  34372  11551  -1498   1184   6768  B    C  
ATOM   5843  CD2 LEU A 128     -56.601  15.982  10.959  1.00141.48      B    C  
ANISOU 5843  CD2 LEU A 128     7724  33895  12136  -1004   1239   7660  B    C  
ATOM   5844  N   PHE A 129     -58.282  15.627  15.288  1.00133.09      B    N  
ANISOU 5844  N   PHE A 129     5853  33182  11534   -749   1510   8922  B    N  
ATOM   5845  CA  PHE A 129     -57.279  15.546  16.337  1.00131.77      B    C  
ANISOU 5845  CA  PHE A 129     5633  32957  11477   -683   1647   9294  B    C  
ATOM   5846  C   PHE A 129     -56.697  14.138  16.376  1.00133.06      B    C  
ANISOU 5846  C   PHE A 129     5778  33743  11036  -1235   1565   8226  B    C  
ATOM   5847  O   PHE A 129     -57.377  13.170  16.027  1.00134.18      B    O  
ANISOU 5847  O   PHE A 129     5867  34306  10809  -1634   1460   7311  B    O  
ATOM   5848  CB  PHE A 129     -57.816  15.997  17.704  1.00132.58      B    C  
ANISOU 5848  CB  PHE A 129     5776  32365  12234   -334   1815   9966  B    C  
ATOM   5849  CG  PHE A 129     -58.822  15.101  18.381  1.00134.27      B    C  
ANISOU 5849  CG  PHE A 129     5914  32804  12297   -573   1761   9445  B    C  
ATOM   5850  CD1 PHE A 129     -58.412  14.119  19.273  1.00136.37      B    C  
ANISOU 5850  CD1 PHE A 129     6212  33226  12375   -852   1781   8940  B    C  
ATOM   5851  CD2 PHE A 129     -60.185  15.286  18.183  1.00136.36      B    C  
ANISOU 5851  CD2 PHE A 129     6222  32848  12740   -507   1708   9345  B    C  
ATOM   5852  CE1 PHE A 129     -59.348  13.301  19.911  1.00137.65      B    C  
ANISOU 5852  CE1 PHE A 129     6298  33592  12413  -1088   1753   8440  B    C  
ATOM   5853  CE2 PHE A 129     -61.122  14.476  18.827  1.00138.94      B    C  
ANISOU 5853  CE2 PHE A 129     6536  33243  13010   -714   1678   8825  B    C  
ATOM   5854  CZ  PHE A 129     -60.700  13.485  19.684  1.00137.55      B    C  
ANISOU 5854  CZ  PHE A 129     6207  33536  12520  -1008   1706   8478  B    C  
ATOM   5855  N   SER A 130     -55.425  14.045  16.774  1.00127.99      B    N  
ANISOU 5855  N   SER A 130     4902  33579  10151  -1283   1631   8559  B    N  
ATOM   5856  CA  SER A 130     -54.671  12.801  16.856  1.00127.28      B    C  
ANISOU 5856  CA  SER A 130     4715  34219   9425  -1858   1584   7557  B    C  
ATOM   5857  C   SER A 130     -54.419  12.366  18.300  1.00128.64      B    C  
ANISOU 5857  C   SER A 130     4881  34288   9708  -1918   1675   7584  B    C  
ATOM   5858  O   SER A 130     -54.433  13.190  19.216  1.00125.38      B    O  
ANISOU 5858  O   SER A 130     4684  32888  10066  -1378   1809   8538  B    O  
ATOM   5859  CB  SER A 130     -53.330  12.953  16.139  1.00129.06      B    C  
ANISOU 5859  CB  SER A 130     5155  34314   9570  -1898   1590   7393  B    C  
ATOM   5860  OG  SER A 130     -52.397  13.663  16.939  1.00132.20      B    O  
ANISOU 5860  OG  SER A 130     5835  33832  10563  -1498   1728   8118  B    O  
ATOM   5861  N   GLN A 131     -54.138  11.065  18.470  1.00123.80      B    N  
ANISOU 5861  N   GLN A 131     4398  33959   8683  -2542   1658   6190  B    N  
ATOM   5862  CA  GLN A 131     -53.797  10.383  19.718  1.00114.68      B    C  
ANISOU 5862  CA  GLN A 131     4337  30819   8418  -2560   1789   5141  B    C  
ATOM   5863  C   GLN A 131     -52.860   9.233  19.339  1.00118.93      B    C  
ANISOU 5863  C   GLN A 131     5089  31458   8643  -3161   1831   3723  B    C  
ATOM   5864  O   GLN A 131     -53.329   8.156  18.951  1.00121.91      B    O  
ANISOU 5864  O   GLN A 131     5126  32707   8487  -3772   1858   2638  B    O  
ATOM   5865  CB  GLN A 131     -55.073   9.902  20.490  1.00114.53      B    C  
ANISOU 5865  CB  GLN A 131     4437  30426   8653  -2609   1818   4783  B    C  
ATOM   5866  CG  GLN A 131     -54.800   9.209  21.839  1.00115.97      B    C  
ANISOU 5866  CG  GLN A 131     5682  28636   9746  -2596   1969   3815  B    C  
ATOM   5867  CD  GLN A 131     -53.758   9.902  22.703  1.00125.37      B    C  
ANISOU 5867  CD  GLN A 131     7698  28110  11825  -2104   2059   4197  B    C  
ATOM   5868  NE2 GLN A 131     -52.717   9.174  23.079  1.00110.51      B    N  
ANISOU 5868  NE2 GLN A 131     6435  25336  10215  -2309   2137   3255  B    N  
ATOM   5869  OE1 GLN A 131     -53.868  11.085  23.045  1.00120.02      B    O  
ANISOU 5869  OE1 GLN A 131     7069  26903  11630  -1556   2096   5312  B    O  
ATOM   5870  N   CYS A 132     -51.536   9.480  19.393  1.00112.93      B    N  
ANISOU 5870  N   CYS A 132     4810  29874   8225  -3005   1877   3738  B    N  
ATOM   5871  CA  CYS A 132     -50.524   8.507  18.981  1.00112.50      B    C  
ANISOU 5871  CA  CYS A 132     4919  29887   7938  -3524   1950   2535  B    C  
ATOM   5872  C   CYS A 132     -50.220   7.468  20.051  1.00108.45      B    C  
ANISOU 5872  C   CYS A 132     5268  27751   8189  -3689   2136   1333  B    C  
ATOM   5873  O   CYS A 132     -50.254   6.278  19.731  1.00109.83      B    O  
ANISOU 5873  O   CYS A 132     5277  28353   8101  -4294   2270    102  B    O  
ATOM   5874  CB  CYS A 132     -49.252   9.202  18.520  1.00112.61      B    C  
ANISOU 5874  CB  CYS A 132     5011  29825   7951  -3301   1923   3091  B    C  
ATOM   5875  SG  CYS A 132     -49.346   9.845  16.835  1.00127.63      B    S  
ANISOU 5875  SG  CYS A 132     5670  34208   8617  -3452   1763   3971  B    S  
ATOM   5876  N   GLN A 133     -49.882   7.894  21.290  1.00 96.67      B    N  
ANISOU 5876  N   GLN A 133     4625  24457   7648  -3179   2187   1666  B    N  
ATOM   5877  CA  GLN A 133     -49.571   6.975  22.392  1.00 89.70      B    C  
ANISOU 5877  CA  GLN A 133     4525  22051   7505  -3257   2364    721  B    C  
ATOM   5878  C   GLN A 133     -50.694   5.908  22.544  1.00 94.37      B    C  
ANISOU 5878  C   GLN A 133     4893  22967   7995  -3669   2477   -125  B    C  
ATOM   5879  O   GLN A 133     -51.870   6.265  22.508  1.00 95.02      B    O  
ANISOU 5879  O   GLN A 133     4584  23689   7832  -3578   2380    365  B    O  
ATOM   5880  CB  GLN A 133     -49.353   7.747  23.703  1.00 84.39      B    C  
ANISOU 5880  CB  GLN A 133     4611  19742   7710  -2643   2374   1362  B    C  
ATOM   5881  CG  GLN A 133     -48.718   6.909  24.821  1.00 92.40      B    C  
ANISOU 5881  CG  GLN A 133     6419  19242   9446  -2661   2542    564  B    C  
ATOM   5882  CD  GLN A 133     -48.544   7.660  26.111  1.00100.93      B    C  
ANISOU 5882  CD  GLN A 133     8154  18927  11267  -2121   2551   1124  B    C  
ATOM   5883  NE2 GLN A 133     -47.759   7.096  27.012  1.00 86.53      B    N  
ANISOU 5883  NE2 GLN A 133     6955  15939   9984  -2092   2669    605  B    N  
ATOM   5884  OE1 GLN A 133     -49.112   8.735  26.324  1.00 96.27      B    O  
ANISOU 5884  OE1 GLN A 133     7467  18320  10792  -1743   2487   2012  B    O  
ATOM   5885  N   ALA A 134     -50.345   4.604  22.607  1.00 91.20      B    N  
ANISOU 5885  N   ALA A 134     4639  22230   7782  -4147   2718  -1381  B    N  
ATOM   5886  CA  ALA A 134     -48.974   4.093  22.664  1.00 88.07      B    C  
ANISOU 5886  CA  ALA A 134     4666  21051   7745  -4266   2878  -1976  B    C  
ATOM   5887  C   ALA A 134     -48.395   3.742  21.293  1.00 98.69      B    C  
ANISOU 5887  C   ALA A 134     5396  23733   8370  -4797   2919  -2527  B    C  
ATOM   5888  O   ALA A 134     -47.318   4.233  20.945  1.00 96.98      B    O  
ANISOU 5888  O   ALA A 134     5303  23469   8074  -4654   2837  -2187  B    O  
ATOM   5889  CB  ALA A 134     -48.919   2.875  23.567  1.00 85.65      B    C  
ANISOU 5889  CB  ALA A 134     4819  19522   8201  -4441   3201  -2932  B    C  
ATOM   5890  N   THR A 135     -49.094   2.890  20.524  1.00102.73      B    N  
ANISOU 5890  N   THR A 135     5223  25453   8359  -5437   3069  -3428  B    N  
ATOM   5891  CA  THR A 135     -48.597   2.410  19.238  1.00109.77      B    C  
ANISOU 5891  CA  THR A 135     5463  27692   8551  -6059   3175  -4182  B    C  
ATOM   5892  C   THR A 135     -49.502   2.822  18.068  1.00124.40      B    C  
ANISOU 5892  C   THR A 135     6290  31754   9223  -6354   2966  -3879  B    C  
ATOM   5893  O   THR A 135     -49.708   2.012  17.163  1.00130.54      B    O  
ANISOU 5893  O   THR A 135     6394  33758   9448  -7052   3147  -4913  B    O  
ATOM   5894  CB  THR A 135     -48.427   0.877  19.293  1.00119.48      B    C  
ANISOU 5894  CB  THR A 135     6680  28469  10247  -6690   3660  -5768  B    C  
ATOM   5895  CG2 THR A 135     -47.320   0.437  20.236  1.00110.40      B    C  
ANISOU 5895  CG2 THR A 135     6388  25388  10172  -6439   3896  -6012  B    C  
ATOM   5896  OG1 THR A 135     -49.668   0.304  19.709  1.00127.68      B    O  
ANISOU 5896  OG1 THR A 135     7537  29532  11444  -6874   3804  -6207  B    O  
ATOM   5897  N   HIS A 136     -49.995   4.073  18.034  1.00123.56      B    N  
ANISOU 5897  N   HIS A 136     6023  32151   8774  -5817   2619  -2446  B    N  
ATOM   5898  CA  HIS A 136     -50.865   4.472  16.920  1.00132.20      B    C  
ANISOU 5898  CA  HIS A 136     6171  35202   8858  -5984   2419  -1982  B    C  
ATOM   5899  C   HIS A 136     -50.175   5.416  15.918  1.00135.03      B    C  
ANISOU 5899  C   HIS A 136     6600  35606   9100  -5510   2190   -962  B    C  
ATOM   5900  O   HIS A 136     -50.790   5.747  14.907  1.00135.51      B    O  
ANISOU 5900  O   HIS A 136     6597  35762   9127  -5230   2026   -478  B    O  
ATOM   5901  CB  HIS A 136     -52.199   5.092  17.375  1.00133.46      B    C  
ANISOU 5901  CB  HIS A 136     6197  35467   9046  -5584   2244  -1059  B    C  
ATOM   5902  CG  HIS A 136     -52.893   4.405  18.502  1.00134.11      B    C  
ANISOU 5902  CG  HIS A 136     6652  34575   9728  -5676   2425  -1725  B    C  
ATOM   5903  CD2 HIS A 136     -53.598   3.247  18.563  1.00137.34      B    C  
ANISOU 5903  CD2 HIS A 136     7035  34804  10346  -6199   2695  -3055  B    C  
ATOM   5904  ND1 HIS A 136     -52.923   4.997  19.748  1.00128.94      B    N  
ANISOU 5904  ND1 HIS A 136     6723  32368   9902  -4990   2353   -870  B    N  
ATOM   5905  CE1 HIS A 136     -53.609   4.184  20.524  1.00126.22      B    C  
ANISOU 5905  CE1 HIS A 136     6669  31233  10056  -5153   2541  -1647  B    C  
ATOM   5906  NE2 HIS A 136     -54.022   3.113  19.864  1.00131.68      B    N  
ANISOU 5906  NE2 HIS A 136     6893  32739  10400  -5891   2771  -2972  B    N  
ATOM   5907  N   CYS A 137     -48.899   5.791  16.132  1.00132.36      B    N  
ANISOU 5907  N   CYS A 137     6206  35571   8514  -5591   2221   -790  B    N  
ATOM   5908  CA  CYS A 137     -48.198   6.657  15.175  1.00132.61      B    C  
ANISOU 5908  CA  CYS A 137     6201  35808   8375  -5220   2055    105  B    C  
ATOM   5909  C   CYS A 137     -48.050   5.959  13.804  1.00134.27      B    C  
ANISOU 5909  C   CYS A 137     6605  35711   8702  -5367   2084   -651  B    C  
ATOM   5910  O   CYS A 137     -48.044   6.645  12.778  1.00133.54      B    O  
ANISOU 5910  O   CYS A 137     6443  35826   8471  -5044   1925     68  B    O  
ATOM   5911  CB  CYS A 137     -46.852   7.116  15.717  1.00129.45      B    C  
ANISOU 5911  CB  CYS A 137     6209  34697   8280  -5014   2090    420  B    C  
ATOM   5912  SG  CYS A 137     -46.121   8.486  14.788  1.00135.50      B    S  
ANISOU 5912  SG  CYS A 137     6734  35972   8776  -4501   1910   1869  B    S  
ATOM   5913  N   ARG A 138     -48.022   4.593  13.797  1.00131.53      B    N  
ANISOU 5913  N   ARG A 138     6255  35294   8428  -5976   2323  -2101  B    N  
ATOM   5914  CA  ARG A 138     -48.013   3.728  12.602  1.00131.23      B    C  
ANISOU 5914  CA  ARG A 138     6299  35053   8511  -6169   2381  -2842  B    C  
ATOM   5915  C   ARG A 138     -49.183   4.037  11.711  1.00133.70      B    C  
ANISOU 5915  C   ARG A 138     6618  35307   8874  -5790   2156  -2232  B    C  
ATOM   5916  O   ARG A 138     -49.081   3.918  10.497  1.00133.04      B    O  
ANISOU 5916  O   ARG A 138     6550  35282   8717  -5753   2083  -2266  B    O  
ATOM   5917  CB  ARG A 138     -48.156   2.240  12.976  1.00131.62      B    C  
ANISOU 5917  CB  ARG A 138     6513  34451   9047  -6648   2697  -4231  B    C  
ATOM   5918  CG  ARG A 138     -47.134   1.674  13.900  1.00137.78      B    C  
ANISOU 5918  CG  ARG A 138     7763  34144  10444  -6794   2976  -4920  B    C  
ATOM   5919  CD  ARG A 138     -47.751   0.606  14.779  1.00140.18      B    C  
ANISOU 5919  CD  ARG A 138     8314  33507  11441  -6984   3253  -5758  B    C  
ATOM   5920  NE  ARG A 138     -46.960   0.449  15.995  1.00143.98      B    N  
ANISOU 5920  NE  ARG A 138     9180  33079  12445  -7059   3508  -6145  B    N  
ATOM   5921  CZ  ARG A 138     -46.324  -0.662  16.343  1.00150.26      B    C  
ANISOU 5921  CZ  ARG A 138    10572  32278  14244  -7029   3794  -6813  B    C  
ATOM   5922  NH1 ARG A 138     -45.597  -0.694  17.451  1.00142.55      B    N1+
ANISOU 5922  NH1 ARG A 138     9472  31345  13347  -7582   4236  -7681  B    N1+
ATOM   5923  NH2 ARG A 138     -46.420  -1.755  15.596  1.00135.54      B    N  
ANISOU 5923  NH2 ARG A 138     8227  30993  12279  -7681   4119  -7984  B    N  
ATOM   5924  N   SER A 139     -50.332   4.361  12.337  1.00131.28      B    N  
ANISOU 5924  N   SER A 139     6061  35367   8453  -5705   2082  -1838  B    N  
ATOM   5925  CA  SER A 139     -51.585   4.641  11.644  1.00131.80      B    C  
ANISOU 5925  CA  SER A 139     6037  35516   8524  -5439   1901  -1358  B    C  
ATOM   5926  C   SER A 139     -51.547   5.991  10.917  1.00134.67      B    C  
ANISOU 5926  C   SER A 139     6492  35811   8865  -4858   1679   -126  B    C  
ATOM   5927  O   SER A 139     -52.490   6.291  10.189  1.00134.90      B    O  
ANISOU 5927  O   SER A 139     6478  35859   8918  -4652   1542    223  B    O  
ATOM   5928  CB  SER A 139     -52.767   4.584  12.609  1.00134.87      B    C  
ANISOU 5928  CB  SER A 139     6460  35591   9194  -5337   1905  -1258  B    C  
ATOM   5929  OG  SER A 139     -52.910   3.294  13.180  1.00141.21      B    O  
ANISOU 5929  OG  SER A 139     7656  35383  10613  -5588   2119  -2326  B    O  
ATOM   5930  N   ILE A 140     -50.464   6.788  11.080  1.00131.94      B    N  
ANISOU 5930  N   ILE A 140     6037  35835   8258  -4735   1668    476  B    N  
ATOM   5931  CA  ILE A 140     -50.327   8.070  10.384  1.00131.91      B    C  
ANISOU 5931  CA  ILE A 140     6018  35897   8206  -4249   1522   1607  B    C  
ATOM   5932  C   ILE A 140     -49.179   7.986   9.367  1.00134.88      B    C  
ANISOU 5932  C   ILE A 140     6683  35941   8625  -4259   1544   1350  B    C  
ATOM   5933  O   ILE A 140     -49.400   8.224   8.176  1.00134.94      B    O  
ANISOU 5933  O   ILE A 140     6734  35942   8595  -4124   1452   1515  B    O  
ATOM   5934  CB  ILE A 140     -50.157   9.298  11.334  1.00133.55      B    C  
ANISOU 5934  CB  ILE A 140     6248  35877   8620  -3778   1502   2775  B    C  
ATOM   5935  CG1 ILE A 140     -51.200   9.293  12.471  1.00133.50      B    C  
ANISOU 5935  CG1 ILE A 140     6119  35846   8757  -3710   1504   2990  B    C  
ATOM   5936  CG2 ILE A 140     -50.198  10.625  10.533  1.00134.26      B    C  
ANISOU 5936  CG2 ILE A 140     6398  35749   8865  -3255   1411   3857  B    C  
ATOM   5937  CD1 ILE A 140     -51.016  10.370  13.548  1.00133.55      B    C  
ANISOU 5937  CD1 ILE A 140     6142  35545   9055  -3255   1524   4123  B    C  
ATOM   5938  N   ILE A 141     -47.957   7.679   9.844  1.00132.24      B    N  
ANISOU 5938  N   ILE A 141     6275  35885   8086  -4542   1664    985  B    N  
ATOM   5939  CA  ILE A 141     -46.744   7.635   9.021  1.00132.02      B    C  
ANISOU 5939  CA  ILE A 141     6350  35875   7937  -4622   1701    790  B    C  
ATOM   5940  C   ILE A 141     -45.928   6.336   9.246  1.00133.29      B    C  
ANISOU 5940  C   ILE A 141     6709  35702   8233  -5115   1896   -489  B    C  
ATOM   5941  O   ILE A 141     -45.978   5.779  10.346  1.00131.57      B    O  
ANISOU 5941  O   ILE A 141     6415  35528   8046  -5426   2029  -1041  B    O  
ATOM   5942  CB  ILE A 141     -45.853   8.893   9.302  1.00134.27      B    C  
ANISOU 5942  CB  ILE A 141     6735  35961   8319  -4189   1672   1851  B    C  
ATOM   5943  CG1 ILE A 141     -45.466   9.006  10.805  1.00134.35      B    C  
ANISOU 5943  CG1 ILE A 141     6686  35977   8383  -4224   1746   2026  B    C  
ATOM   5944  CG2 ILE A 141     -46.503  10.192   8.757  1.00135.29      B    C  
ANISOU 5944  CG2 ILE A 141     6883  35904   8617  -3627   1547   3016  B    C  
ATOM   5945  CD1 ILE A 141     -44.327   9.859  11.100  1.00140.63      B    C  
ANISOU 5945  CD1 ILE A 141     7751  36208   9473  -3857   1768   2755  B    C  
ATOM   5946  N   PRO A 142     -45.156   5.852   8.231  1.00131.04      B    N  
ANISOU 5946  N   PRO A 142     6432  35557   7800  -5338   1949  -1014  B    N  
ATOM   5947  CA  PRO A 142     -44.288   4.681   8.475  1.00130.39      B    C  
ANISOU 5947  CA  PRO A 142     6462  35218   7863  -5828   2182  -2199  B    C  
ATOM   5948  C   PRO A 142     -43.097   5.112   9.341  1.00132.97      B    C  
ANISOU 5948  C   PRO A 142     6945  35306   8273  -5799   2264  -2039  B    C  
ATOM   5949  O   PRO A 142     -42.456   6.120   9.044  1.00132.57      B    O  
ANISOU 5949  O   PRO A 142     6839  35533   7998  -5515   2156  -1199  B    O  
ATOM   5950  CB  PRO A 142     -43.879   4.233   7.068  1.00131.74      B    C  
ANISOU 5950  CB  PRO A 142     6800  35156   8097  -5834   2173  -2504  B    C  
ATOM   5951  CG  PRO A 142     -43.981   5.459   6.225  1.00135.30      B    C  
ANISOU 5951  CG  PRO A 142     7369  35556   8484  -5287   1953  -1381  B    C  
ATOM   5952  CD  PRO A 142     -44.966   6.400   6.868  1.00132.55      B    C  
ANISOU 5952  CD  PRO A 142     6734  35689   7939  -5043   1824   -517  B    C  
ATOM   5953  N   CYS A 143     -42.846   4.398  10.449  1.00131.18      B    N  
ANISOU 5953  N   CYS A 143     6683  35008   8151  -6239   2484  -2882  B    N  
ATOM   5954  CA  CYS A 143     -41.804   4.771  11.417  1.00131.06      B    C  
ANISOU 5954  CA  CYS A 143     6694  35016   8087  -6352   2581  -2842  B    C  
ATOM   5955  C   CYS A 143     -41.340   3.590  12.261  1.00132.43      B    C  
ANISOU 5955  C   CYS A 143     7123  34432   8762  -6864   2938  -4214  B    C  
ATOM   5956  O   CYS A 143     -41.921   2.508  12.200  1.00132.13      B    O  
ANISOU 5956  O   CYS A 143     7177  33911   9115  -7097   3115  -5083  B    O  
ATOM   5957  CB  CYS A 143     -42.337   5.884  12.323  1.00131.83      B    C  
ANISOU 5957  CB  CYS A 143     6649  35417   8024  -5965   2396  -1664  B    C  
ATOM   5958  SG  CYS A 143     -43.895   5.479  13.161  1.00134.84      B    S  
ANISOU 5958  SG  CYS A 143     7097  35418   8720  -5929   2403  -1835  B    S  
ATOM   5959  N   GLN A 144     -40.316   3.831  13.101  1.00128.38      B    N  
ANISOU 5959  N   GLN A 144     6544  34129   8106  -7182   3102  -4475  B    N  
ATOM   5960  CA  GLN A 144     -39.863   2.897  14.124  1.00121.31      B    C  
ANISOU 5960  CA  GLN A 144     6427  31311   8355  -7209   3422  -5379  B    C  
ATOM   5961  C   GLN A 144     -40.723   3.244  15.336  1.00119.59      B    C  
ANISOU 5961  C   GLN A 144     6731  29964   8742  -6645   3280  -4683  B    C  
ATOM   5962  O   GLN A 144     -40.315   4.050  16.177  1.00112.39      B    O  
ANISOU 5962  O   GLN A 144     6501  27796   8406  -5966   3102  -3730  B    O  
ATOM   5963  CB  GLN A 144     -38.358   3.040  14.395  1.00116.57      B    C  
ANISOU 5963  CB  GLN A 144     6477  29448   8368  -6942   3480  -5283  B    C  
ATOM   5964  CG  GLN A 144     -37.451   2.448  13.321  1.00121.33      B    C  
ANISOU 5964  CG  GLN A 144     6642  30890   8566  -7565   3720  -6227  B    C  
ATOM   5965  CD  GLN A 144     -35.998   2.579  13.707  1.00119.17      B    C  
ANISOU 5965  CD  GLN A 144     7058  29238   8984  -7252   3775  -6082  B    C  
ATOM   5966  NE2 GLN A 144     -35.301   1.454  13.762  1.00109.37      B    N  
ANISOU 5966  NE2 GLN A 144     5971  27233   8352  -7673   4207  -7281  B    N  
ATOM   5967  OE1 GLN A 144     -35.488   3.675  13.981  1.00104.29      B    O  
ANISOU 5967  OE1 GLN A 144     5544  26925   7158  -6637   3474  -4911  B    O  
ATOM   5968  N   ASP A 145     -41.972   2.744  15.351  1.00119.35      B    N  
ANISOU 5968  N   ASP A 145     6296  30565   8488  -6941   3347  -5112  B    N  
ATOM   5969  CA  ASP A 145     -42.943   3.097  16.378  1.00114.92      B    C  
ANISOU 5969  CA  ASP A 145     6104  29197   8364  -6456   3205  -4444  B    C  
ATOM   5970  C   ASP A 145     -42.647   2.390  17.709  1.00110.68      B    C  
ANISOU 5970  C   ASP A 145     6433  26583   9036  -6256   3455  -4923  B    C  
ATOM   5971  O   ASP A 145     -43.441   1.581  18.197  1.00110.73      B    O  
ANISOU 5971  O   ASP A 145     6447  26225   9401  -6456   3666  -5552  B    O  
ATOM   5972  CB  ASP A 145     -44.382   2.837  15.890  1.00123.91      B    C  
ANISOU 5972  CB  ASP A 145     6463  31821   8798  -6838   3178  -4687  B    C  
ATOM   5973  CG  ASP A 145     -45.468   3.561  16.673  1.00131.02      B    C  
ANISOU 5973  CG  ASP A 145     7551  32357   9874  -6279   2935  -3651  B    C  
ATOM   5974  OD1 ASP A 145     -45.173   4.616  17.266  1.00126.58      B    O  
ANISOU 5974  OD1 ASP A 145     7493  30914   9686  -5582   2716  -2467  B    O  
ATOM   5975  OD2 ASP A 145     -46.619   3.098  16.655  1.00139.57      B    O1-
ANISOU 5975  OD2 ASP A 145     8226  34085  10720  -6565   2990  -4048  B    O1-
ATOM   5976  N   THR A 146     -41.494   2.742  18.296  1.00100.05      B    N  
ANISOU 5976  N   THR A 146     5777  23938   8299  -5838   3429  -4541  B    N  
ATOM   5977  CA  THR A 146     -40.989   2.265  19.582  1.00 92.64      B    C  
ANISOU 5977  CA  THR A 146     5651  21099   8447  -5544   3615  -4728  B    C  
ATOM   5978  C   THR A 146     -40.382   3.460  20.342  1.00 89.55      B    C  
ANISOU 5978  C   THR A 146     5888  19762   8374  -4812   3322  -3552  B    C  
ATOM   5979  O   THR A 146     -39.569   4.193  19.768  1.00 88.56      B    O  
ANISOU 5979  O   THR A 146     5704  20018   7927  -4685   3167  -3068  B    O  
ATOM   5980  CB  THR A 146     -40.001   1.073  19.442  1.00101.93      B    C  
ANISOU 5980  CB  THR A 146     6903  21696  10131  -5984   4047  -5870  B    C  
ATOM   5981  CG2 THR A 146     -38.860   1.327  18.441  1.00103.96      B    C  
ANISOU 5981  CG2 THR A 146     6939  22618   9943  -6185   4020  -5964  B    C  
ATOM   5982  OG1 THR A 146     -39.450   0.778  20.732  1.00 94.44      B    O  
ANISOU 5982  OG1 THR A 146     6710  18975  10198  -5584   4179  -5755  B    O  
ATOM   5983  N   PRO A 147     -40.760   3.672  21.629  1.00 80.74      B    N  
ANISOU 5983  N   PRO A 147     5338  17443   7897  -4352   3276  -3120  B    N  
ATOM   5984  CA  PRO A 147     -40.218   4.825  22.383  1.00 75.21      B    C  
ANISOU 5984  CA  PRO A 147     5171  15890   7516  -3719   3053  -2125  B    C  
ATOM   5985  C   PRO A 147     -38.686   4.800  22.584  1.00 76.08      B    C  
ANISOU 5985  C   PRO A 147     5722  15160   8027  -3608   3120  -2227  B    C  
ATOM   5986  O   PRO A 147     -38.104   5.782  23.051  1.00 71.47      B    O  
ANISOU 5986  O   PRO A 147     5498  14006   7651  -3157   2964  -1500  B    O  
ATOM   5987  CB  PRO A 147     -40.965   4.742  23.721  1.00 72.59      B    C  
ANISOU 5987  CB  PRO A 147     5272  14550   7761  -3405   3071  -1947  B    C  
ATOM   5988  CG  PRO A 147     -41.383   3.308  23.843  1.00 78.43      B    C  
ANISOU 5988  CG  PRO A 147     5907  15138   8753  -3832   3375  -2946  B    C  
ATOM   5989  CD  PRO A 147     -41.727   2.908  22.448  1.00 81.12      B    C  
ANISOU 5989  CD  PRO A 147     5509  16927   8386  -4408   3447  -3530  B    C  
ATOM   5990  N   SER A 148     -38.041   3.693  22.177  1.00 74.93      B    N  
ANISOU 5990  N   SER A 148     5483  14985   8003  -4047   3389  -3153  B    N  
ATOM   5991  CA  SER A 148     -36.600   3.460  22.222  1.00 72.78      B    C  
ANISOU 5991  CA  SER A 148     5522  14037   8093  -4037   3506  -3383  B    C  
ATOM   5992  C   SER A 148     -35.856   4.343  21.204  1.00 80.19      B    C  
ANISOU 5992  C   SER A 148     6228  15781   8460  -4025   3318  -2967  B    C  
ATOM   5993  O   SER A 148     -34.658   4.597  21.377  1.00 77.71      B    O  
ANISOU 5993  O   SER A 148     6257  14843   8427  -3840   3309  -2817  B    O  
ATOM   5994  CB  SER A 148     -36.325   1.990  21.929  1.00 79.16      B    C  
ANISOU 5994  CB  SER A 148     6143  14713   9219  -4568   3929  -4523  B    C  
ATOM   5995  OG  SER A 148     -34.954   1.738  21.685  1.00 85.19      B    O  
ANISOU 5995  OG  SER A 148     7074  15038  10258  -4632   4071  -4785  B    O  
ATOM   5996  N   VAL A 149     -36.555   4.763  20.119  1.00 81.37      B    N  
ANISOU 5996  N   VAL A 149     5738  17386   7791  -4239   3185  -2776  B    N  
ATOM   5997  CA  VAL A 149     -36.003   5.602  19.047  1.00 83.14      B    C  
ANISOU 5997  CA  VAL A 149     5604  18596   7390  -4233   3022  -2277  B    C  
ATOM   5998  C   VAL A 149     -36.549   7.022  19.218  1.00 84.47      B    C  
ANISOU 5998  C   VAL A 149     5740  18945   7410  -3695   2751  -1011  B    C  
ATOM   5999  O   VAL A 149     -37.763   7.231  19.158  1.00 86.54      B    O  
ANISOU 5999  O   VAL A 149     5654  19862   7364  -3674   2664   -690  B    O  
ATOM   6000  CB  VAL A 149     -36.290   5.025  17.624  1.00 94.64      B    C  
ANISOU 6000  CB  VAL A 149     6239  21732   7988  -4888   3113  -2934  B    C  
ATOM   6001  CG1 VAL A 149     -35.766   5.952  16.525  1.00 98.10      B    C  
ANISOU 6001  CG1 VAL A 149     6249  23303   7721  -4843   2933  -2274  B    C  
ATOM   6002  CG2 VAL A 149     -35.694   3.636  17.457  1.00 95.55      B    C  
ANISOU 6002  CG2 VAL A 149     6352  21541   8412  -5448   3490  -4266  B    C  
ATOM   6003  N   LYS A 150     -35.652   7.986  19.450  1.00 76.63      B    N  
ANISOU 6003  N   LYS A 150     5082  17323   6711  -3266   2665   -314  B    N  
ATOM   6004  CA  LYS A 150     -36.031   9.386  19.625  1.00 76.28      B    C  
ANISOU 6004  CA  LYS A 150     4987  17272   6724  -2743   2520    880  B    C  
ATOM   6005  C   LYS A 150     -35.439  10.222  18.492  1.00 84.38      B    C  
ANISOU 6005  C   LYS A 150     5549  19247   7267  -2687   2458   1542  B    C  
ATOM   6006  O   LYS A 150     -34.250  10.118  18.179  1.00 83.66      B    O  
ANISOU 6006  O   LYS A 150     5617  18948   7223  -2772   2505   1283  B    O  
ATOM   6007  CB  LYS A 150     -35.626   9.910  21.009  1.00 72.30      B    C  
ANISOU 6007  CB  LYS A 150     5212  15169   7088  -2270   2546   1163  B    C  
ATOM   6008  CG  LYS A 150     -36.526   9.373  22.125  1.00 66.61      B    C  
ANISOU 6008  CG  LYS A 150     4815  13735   6759  -2229   2581    837  B    C  
ATOM   6009  CD  LYS A 150     -36.740  10.385  23.236  1.00 69.34      B    C  
ANISOU 6009  CD  LYS A 150     5524  13139   7684  -1718   2569   1525  B    C  
ATOM   6010  CE  LYS A 150     -35.708  10.275  24.328  1.00 65.89      B    C  
ANISOU 6010  CE  LYS A 150     5746  11409   7879  -1551   2635   1235  B    C  
ATOM   6011  NZ  LYS A 150     -36.098  11.030  25.548  1.00 64.38      B    N1+
ANISOU 6011  NZ  LYS A 150     5873  10365   8223  -1165   2665   1656  B    N1+
ATOM   6012  N   PHE A 151     -36.300  10.990  17.819  1.00 85.50      B    N  
ANISOU 6012  N   PHE A 151     5047  20528   6913  -2559   2369   2418  B    N  
ATOM   6013  CA  PHE A 151     -35.923  11.797  16.660  1.00 89.57      B    C  
ANISOU 6013  CA  PHE A 151     4955  22186   6889  -2490   2326   3216  B    C  
ATOM   6014  C   PHE A 151     -36.489  13.205  16.740  1.00 92.85      B    C  
ANISOU 6014  C   PHE A 151     5092  22639   7547  -1913   2330   4652  B    C  
ATOM   6015  O   PHE A 151     -37.505  13.441  17.398  1.00 92.55      B    O  
ANISOU 6015  O   PHE A 151     5092  22271   7801  -1692   2332   4985  B    O  
ATOM   6016  CB  PHE A 151     -36.415  11.119  15.360  1.00 99.28      B    C  
ANISOU 6016  CB  PHE A 151     5346  25356   7020  -3060   2264   2816  B    C  
ATOM   6017  CG  PHE A 151     -37.916  10.923  15.280  1.00105.16      B    C  
ANISOU 6017  CG  PHE A 151     5597  27017   7341  -3177   2192   2935  B    C  
ATOM   6018  CD1 PHE A 151     -38.510   9.761  15.761  1.00106.60      B    C  
ANISOU 6018  CD1 PHE A 151     5986  26921   7597  -3561   2246   1832  B    C  
ATOM   6019  CD2 PHE A 151     -38.734  11.902  14.726  1.00113.34      B    C  
ANISOU 6019  CD2 PHE A 151     5921  29190   7955  -2889   2102   4198  B    C  
ATOM   6020  CE1 PHE A 151     -39.899   9.588  15.702  1.00111.54      B    C  
ANISOU 6020  CE1 PHE A 151     6154  28382   7845  -3675   2185   1919  B    C  
ATOM   6021  CE2 PHE A 151     -40.125  11.743  14.700  1.00119.97      B    C  
ANISOU 6021  CE2 PHE A 151     6299  30862   8424  -2975   2031   4348  B    C  
ATOM   6022  CZ  PHE A 151     -40.697  10.580  15.174  1.00115.91      B    C  
ANISOU 6022  CZ  PHE A 151     6028  30075   7939  -3387   2058   3164  B    C  
ATOM   6023  N   THR A 152     -35.837  14.119  16.035  1.00 90.33      B    N  
ANISOU 6023  N   THR A 152     4441  22739   7141  -1679   2372   5507  B    N  
ATOM   6024  CA  THR A 152     -36.205  15.523  15.852  1.00 93.15      B    C  
ANISOU 6024  CA  THR A 152     4359  23262   7770  -1130   2474   7006  B    C  
ATOM   6025  C   THR A 152     -37.099  15.621  14.612  1.00106.37      B    C  
ANISOU 6025  C   THR A 152     4968  27015   8433  -1274   2371   7715  B    C  
ATOM   6026  O   THR A 152     -37.017  14.741  13.750  1.00108.93      B    O  
ANISOU 6026  O   THR A 152     4915  28650   7821  -1821   2239   7001  B    O  
ATOM   6027  CB  THR A 152     -34.939  16.382  15.706  1.00 93.52      B    C  
ANISOU 6027  CB  THR A 152     4568  22667   8298   -827   2626   7519  B    C  
ATOM   6028  CG2 THR A 152     -34.415  16.866  17.033  1.00 78.49      B    C  
ANISOU 6028  CG2 THR A 152     3455  18809   7560   -450   2804   7461  B    C  
ATOM   6029  OG1 THR A 152     -33.933  15.747  14.905  1.00 93.90      B    O  
ANISOU 6029  OG1 THR A 152     4644  23222   7812  -1233   2547   6782  B    O  
ATOM   6030  N   TYR A 153     -37.965  16.652  14.514  1.00108.26      B    N  
ANISOU 6030  N   TYR A 153     4661  27622   8851   -815   2461   9082  B    N  
ATOM   6031  CA  TYR A 153     -38.795  16.758  13.317  1.00117.85      B    C  
ANISOU 6031  CA  TYR A 153     4768  30971   9038   -935   2354   9870  B    C  
ATOM   6032  C   TYR A 153     -39.138  18.195  12.928  1.00126.01      B    C  
ANISOU 6032  C   TYR A 153     5486  31789  10605   -328   2543  11319  B    C  
ATOM   6033  O   TYR A 153     -39.068  19.123  13.735  1.00124.20      B    O  
ANISOU 6033  O   TYR A 153     5283  30557  11349    230   2813  12345  B    O  
ATOM   6034  CB  TYR A 153     -40.080  15.895  13.410  1.00120.14      B    C  
ANISOU 6034  CB  TYR A 153     4834  32060   8752  -1304   2183   9253  B    C  
ATOM   6035  CG  TYR A 153     -41.262  16.470  14.161  1.00121.07      B    C  
ANISOU 6035  CG  TYR A 153     4919  31627   9454   -883   2260  10018  B    C  
ATOM   6036  CD1 TYR A 153     -42.171  17.316  13.526  1.00125.55      B    C  
ANISOU 6036  CD1 TYR A 153     5224  32343  10137   -578   2292  10775  B    C  
ATOM   6037  CD2 TYR A 153     -41.577  16.029  15.441  1.00114.53      B    C  
ANISOU 6037  CD2 TYR A 153     4927  29246   9342   -875   2282   9193  B    C  
ATOM   6038  CE1 TYR A 153     -43.302  17.794  14.185  1.00125.84      B    C  
ANISOU 6038  CE1 TYR A 153     5281  31805  10728   -247   2372  11304  B    C  
ATOM   6039  CE2 TYR A 153     -42.714  16.487  16.107  1.00115.67      B    C  
ANISOU 6039  CE2 TYR A 153     5013  28971   9965   -543   2356   9805  B    C  
ATOM   6040  CZ  TYR A 153     -43.573  17.370  15.473  1.00128.15      B    C  
ANISOU 6040  CZ  TYR A 153     5683  31661  11345   -209   2418  11258  B    C  
ATOM   6041  OH  TYR A 153     -44.688  17.832  16.117  1.00126.99      B    O  
ANISOU 6041  OH  TYR A 153     5475  31042  11734    119   2522  11851  B    O  
ATOM   6042  N   TYR A 154     -39.503  18.340  11.653  1.00126.12      B    N  
ANISOU 6042  N   TYR A 154     5514  32196  10210   -474   2434  10989  B    N  
ATOM   6043  CA  TYR A 154     -39.994  19.546  11.006  1.00127.18      B    C  
ANISOU 6043  CA  TYR A 154     5822  31635  10864    -97   2537  11534  B    C  
ATOM   6044  C   TYR A 154     -41.184  19.140  10.164  1.00133.02      B    C  
ANISOU 6044  C   TYR A 154     6828  32488  11226   -375   2325  10625  B    C  
ATOM   6045  O   TYR A 154     -41.097  18.157   9.428  1.00133.68      B    O  
ANISOU 6045  O   TYR A 154     6884  33310  10597   -827   2157   9720  B    O  
ATOM   6046  CB  TYR A 154     -38.915  20.233  10.142  1.00128.06      B    C  
ANISOU 6046  CB  TYR A 154     6097  31438  11122     10   2636  11697  B    C  
ATOM   6047  CG  TYR A 154     -39.328  21.629   9.716  1.00129.05      B    C  
ANISOU 6047  CG  TYR A 154     6438  30666  11928    407   2788  12277  B    C  
ATOM   6048  CD1 TYR A 154     -38.942  22.747  10.451  1.00129.57      B    C  
ANISOU 6048  CD1 TYR A 154     6669  29550  13011    856   3085  13009  B    C  
ATOM   6049  CD2 TYR A 154     -40.152  21.829   8.609  1.00129.92      B    C  
ANISOU 6049  CD2 TYR A 154     6633  31007  11724    305   2649  11976  B    C  
ATOM   6050  CE1 TYR A 154     -39.345  24.030  10.083  1.00129.34      B    C  
ANISOU 6050  CE1 TYR A 154     6785  28794  13563   1149   3233  13448  B    C  
ATOM   6051  CE2 TYR A 154     -40.581  23.106   8.246  1.00130.07      B    C  
ANISOU 6051  CE2 TYR A 154     6804  30315  12301    624   2773  12480  B    C  
ATOM   6052  CZ  TYR A 154     -40.166  24.205   8.981  1.00132.03      B    C  
ANISOU 6052  CZ  TYR A 154     7298  29356  13510    991   3042  12999  B    C  
ATOM   6053  OH  TYR A 154     -40.584  25.466   8.631  1.00128.90      B    O  
ANISOU 6053  OH  TYR A 154     6906  28462  13606   1275   3186  13562  B    O  
ATOM   6054  N   SER A 155     -42.289  19.877  10.250  1.00131.91      B    N  
ANISOU 6054  N   SER A 155     6670  31976  11473    -90   2366  11132  B    N  
ATOM   6055  CA  SER A 155     -43.448  19.530   9.442  1.00133.23      B    C  
ANISOU 6055  CA  SER A 155     6876  32503  11242   -298   2179  10565  B    C  
ATOM   6056  C   SER A 155     -44.091  20.731   8.770  1.00138.26      B    C  
ANISOU 6056  C   SER A 155     7934  32173  12425    -14   2220  10725  B    C  
ATOM   6057  O   SER A 155     -44.033  21.851   9.278  1.00138.32      B    O  
ANISOU 6057  O   SER A 155     8040  31372  13143    363   2410  11427  B    O  
ATOM   6058  CB  SER A 155     -44.497  18.804  10.278  1.00135.54      B    C  
ANISOU 6058  CB  SER A 155     7162  32835  11501   -427   2094  10187  B    C  
ATOM   6059  OG  SER A 155     -45.110  19.682  11.207  1.00140.18      B    O  
ANISOU 6059  OG  SER A 155     8027  32285  12949    -29   2238  10692  B    O  
ATOM   6060  N   GLN A 156     -44.710  20.469   7.617  1.00136.89      B    N  
ANISOU 6060  N   GLN A 156     7711  32527  11772   -203   2060  10329  B    N  
ATOM   6061  CA  GLN A 156     -45.515  21.398   6.835  1.00137.10      B    C  
ANISOU 6061  CA  GLN A 156     7861  32218  12011    -11   2044  10577  B    C  
ATOM   6062  C   GLN A 156     -46.876  20.737   6.684  1.00140.83      B    C  
ANISOU 6062  C   GLN A 156     8470  32723  12318   -192   1865   9905  B    C  
ATOM   6063  O   GLN A 156     -46.939  19.581   6.262  1.00141.09      B    O  
ANISOU 6063  O   GLN A 156     8431  33369  11809   -541   1724   9182  B    O  
ATOM   6064  CB  GLN A 156     -44.863  21.714   5.478  1.00138.35      B    C  
ANISOU 6064  CB  GLN A 156     8209  32387  11971    -76   2018  10373  B    C  
ATOM   6065  CG  GLN A 156     -43.514  22.417   5.599  1.00144.61      B    C  
ANISOU 6065  CG  GLN A 156     9628  31952  13366     49   2180  10219  B    C  
ATOM   6066  CD  GLN A 156     -42.905  22.755   4.267  1.00151.71      B    C  
ANISOU 6066  CD  GLN A 156    11216  32085  14341    -57   2143   9483  B    C  
ATOM   6067  NE2 GLN A 156     -42.380  23.964   4.166  1.00143.12      B    N  
ANISOU 6067  NE2 GLN A 156     9859  31034  13485    226   2307  10440  B    N  
ATOM   6068  OE1 GLN A 156     -42.855  21.934   3.342  1.00148.78      B    O  
ANISOU 6068  OE1 GLN A 156    10664  32499  13368   -301   2026   9118  B    O  
ATOM   6069  N   VAL A 157     -47.953  21.420   7.081  1.00138.69      B    N  
ANISOU 6069  N   VAL A 157     8112  32185  12398     51   1894  10399  B    N  
ATOM   6070  CA  VAL A 157     -49.280  20.820   6.985  1.00139.33      B    C  
ANISOU 6070  CA  VAL A 157     8142  32525  12271    -91   1736   9978  B    C  
ATOM   6071  C   VAL A 157     -50.221  21.765   6.219  1.00142.44      B    C  
ANISOU 6071  C   VAL A 157     8845  32292  12985     87   1691  10004  B    C  
ATOM   6072  O   VAL A 157     -50.330  22.949   6.542  1.00141.48      B    O  
ANISOU 6072  O   VAL A 157     8771  31612  13374    399   1828  10646  B    O  
ATOM   6073  CB  VAL A 157     -49.850  20.344   8.362  1.00141.85      B    C  
ANISOU 6073  CB  VAL A 157     8476  32581  12840    -91   1763   9873  B    C  
ATOM   6074  CG1 VAL A 157     -49.944  21.472   9.392  1.00141.04      B    C  
ANISOU 6074  CG1 VAL A 157     8400  31725  13463    312   1964  10701  B    C  
ATOM   6075  CG2 VAL A 157     -51.183  19.610   8.209  1.00142.27      B    C  
ANISOU 6075  CG2 VAL A 157     8433  33008  12614   -287   1596   9370  B    C  
ATOM   6076  N   SER A 158     -50.858  21.221   5.170  1.00141.28      B    N  
ANISOU 6076  N   SER A 158     8641  32640  12398   -111   1513   9552  B    N  
ATOM   6077  CA  SER A 158     -51.803  21.918   4.301  1.00141.94      B    C  
ANISOU 6077  CA  SER A 158     8848  32494  12589     11   1431   9623  B    C  
ATOM   6078  C   SER A 158     -53.216  21.792   4.886  1.00145.22      B    C  
ANISOU 6078  C   SER A 158     9375  32540  13261     38   1358   9383  B    C  
ATOM   6079  O   SER A 158     -53.737  20.677   4.971  1.00145.03      B    O  
ANISOU 6079  O   SER A 158     9215  32971  12917   -202   1241   8877  B    O  
ATOM   6080  CB  SER A 158     -51.725  21.341   2.891  1.00145.20      B    C  
ANISOU 6080  CB  SER A 158     9487  33045  12637   -220   1281   8926  B    C  
ATOM   6081  OG  SER A 158     -50.450  21.558   2.306  1.00151.73      B    O  
ANISOU 6081  OG  SER A 158    10791  33265  13595   -251   1350   8599  B    O  
ATOM   6082  N   VAL A 159     -53.809  22.926   5.348  1.00143.31      B    N  
ANISOU 6082  N   VAL A 159     9098  31882  13471    341   1452  10022  B    N  
ATOM   6083  CA  VAL A 159     -55.128  22.968   6.022  1.00143.54      B    C  
ANISOU 6083  CA  VAL A 159     9055  31762  13721    422   1420  10078  B    C  
ATOM   6084  C   VAL A 159     -56.031  24.140   5.518  1.00147.52      B    C  
ANISOU 6084  C   VAL A 159     9882  31535  14635    623   1396  10139  B    C  
ATOM   6085  O   VAL A 159     -55.475  25.160   5.120  1.00146.88      B    O  
ANISOU 6085  O   VAL A 159     9918  31123  14765    787   1491  10501  B    O  
ATOM   6086  CB  VAL A 159     -54.959  23.056   7.571  1.00145.24      B    C  
ANISOU 6086  CB  VAL A 159     9330  31464  14392    544   1585  10289  B    C  
ATOM   6087  CG1 VAL A 159     -54.204  21.857   8.119  1.00144.95      B    C  
ANISOU 6087  CG1 VAL A 159     9171  31870  14032    308   1581   9957  B    C  
ATOM   6088  CG2 VAL A 159     -54.287  24.358   8.004  1.00144.34      B    C  
ANISOU 6088  CG2 VAL A 159     9325  30676  14842    851   1807  10952  B    C  
ATOM   6089  N   PRO A 160     -57.399  24.082   5.624  1.00146.38      B    N  
ANISOU 6089  N   PRO A 160     9589  31518  14510    653   1304  10143  B    N  
ATOM   6090  CA  PRO A 160     -58.226  25.235   5.185  1.00146.64      B    C  
ANISOU 6090  CA  PRO A 160     9729  31145  14844    864   1297  10424  B    C  
ATOM   6091  C   PRO A 160     -57.948  26.522   5.985  1.00149.01      B    C  
ANISOU 6091  C   PRO A 160    10270  30544  15804   1128   1510  10833  B    C  
ATOM   6092  O   PRO A 160     -57.408  26.449   7.090  1.00148.14      B    O  
ANISOU 6092  O   PRO A 160    10091  30261  15936   1191   1669  11074  B    O  
ATOM   6093  CB  PRO A 160     -59.664  24.750   5.403  1.00148.25      B    C  
ANISOU 6093  CB  PRO A 160     9883  31413  15033    802   1162  10106  B    C  
ATOM   6094  CG  PRO A 160     -59.573  23.262   5.453  1.00151.51      B    C  
ANISOU 6094  CG  PRO A 160    10332  32139  15097    492   1046   9373  B    C  
ATOM   6095  CD  PRO A 160     -58.255  22.973   6.097  1.00147.75      B    C  
ANISOU 6095  CD  PRO A 160     9661  31967  14509    466   1192   9672  B    C  
ATOM   6096  N   LYS A 161     -58.305  27.695   5.414  1.00146.87      B    N  
ANISOU 6096  N   LYS A 161    10004  30058  15741   1323   1544  11236  B    N  
ATOM   6097  CA  LYS A 161     -58.051  29.029   5.979  1.00146.13      B    C  
ANISOU 6097  CA  LYS A 161    10008  29272  16243   1583   1766  11753  B    C  
ATOM   6098  C   LYS A 161     -58.522  29.203   7.438  1.00148.29      B    C  
ANISOU 6098  C   LYS A 161    10347  28968  17027   1693   1907  11822  B    C  
ATOM   6099  O   LYS A 161     -57.688  29.513   8.290  1.00147.12      B    O  
ANISOU 6099  O   LYS A 161    10197  28468  17233   1798   2118  12134  B    O  
ATOM   6100  CB  LYS A 161     -58.666  30.132   5.108  1.00148.38      B    C  
ANISOU 6100  CB  LYS A 161    10532  29161  16686   1678   1707  11714  B    C  
ATOM   6101  CG  LYS A 161     -57.947  31.466   5.264  1.00158.65      B    C  
ANISOU 6101  CG  LYS A 161    12575  29151  18553   1714   1823  11290  B    C  
ATOM   6102  CD  LYS A 161     -58.869  32.647   5.028  1.00166.29      B    C  
ANISOU 6102  CD  LYS A 161    14058  29273  19853   1748   1748  10841  B    C  
ATOM   6103  CE  LYS A 161     -58.226  33.963   5.398  1.00173.23      B    C  
ANISOU 6103  CE  LYS A 161    15505  29094  21221   1769   1867  10532  B    C  
ATOM   6104  NZ  LYS A 161     -58.114  34.137   6.873  1.00178.41      B    N1+
ANISOU 6104  NZ  LYS A 161    16460  29009  22320   1755   1983  10217  B    N1+
ATOM   6105  N   GLU A 162     -59.830  29.032   7.722  1.00146.51      B    N  
ANISOU 6105  N   GLU A 162     9915  28933  16819   1741   1843  11907  B    N  
ATOM   6106  CA  GLU A 162     -60.355  29.203   9.081  1.00145.85      B    C  
ANISOU 6106  CA  GLU A 162     9757  28457  17203   1882   2002  12161  B    C  
ATOM   6107  C   GLU A 162     -59.988  28.019   9.998  1.00148.68      B    C  
ANISOU 6107  C   GLU A 162    10117  28928  17446   1729   2004  11857  B    C  
ATOM   6108  O   GLU A 162     -59.903  28.197  11.217  1.00147.99      B    O  
ANISOU 6108  O   GLU A 162    10007  28411  17812   1861   2198  12135  B    O  
ATOM   6109  CB  GLU A 162     -61.875  29.419   9.074  1.00147.23      B    C  
ANISOU 6109  CB  GLU A 162     9942  28548  17452   1915   1893  12009  B    C  
ATOM   6110  CG  GLU A 162     -62.332  30.566   9.967  1.00153.44      B    C  
ANISOU 6110  CG  GLU A 162    11194  28178  18927   2047   2029  11814  B    C  
ATOM   6111  CD  GLU A 162     -61.984  30.465  11.443  1.00161.86      B    C  
ANISOU 6111  CD  GLU A 162    12869  28192  20437   1946   2119  11108  B    C  
ATOM   6112  OE1 GLU A 162     -62.476  29.526  12.111  1.00154.16      B    O  
ANISOU 6112  OE1 GLU A 162    11503  27691  19380   1960   2139  11369  B    O  
ATOM   6113  OE2 GLU A 162     -61.193  31.308  11.925  1.00154.13      B    O1-
ANISOU 6113  OE2 GLU A 162    11667  27000  19896   2175   2409  11874  B    O1-
ATOM   6114  N   LEU A 163     -59.764  26.825   9.419  1.00146.52      B    N  
ANISOU 6114  N   LEU A 163     9593  29540  16538   1513   1842  11655  B    N  
ATOM   6115  CA  LEU A 163     -59.381  25.640  10.187  1.00145.84      B    C  
ANISOU 6115  CA  LEU A 163     9338  29844  16231   1363   1845  11515  B    C  
ATOM   6116  C   LEU A 163     -57.875  25.691  10.494  1.00146.90      B    C  
ANISOU 6116  C   LEU A 163     9614  29717  16485   1370   1988  11602  B    C  
ATOM   6117  O   LEU A 163     -57.061  25.219   9.696  1.00147.15      B    O  
ANISOU 6117  O   LEU A 163     9659  30160  16091   1201   1896  11347  B    O  
ATOM   6118  CB  LEU A 163     -59.768  24.347   9.447  1.00146.78      B    C  
ANISOU 6118  CB  LEU A 163     9349  30738  15683   1047   1590  10881  B    C  
ATOM   6119  CG  LEU A 163     -61.232  23.943   9.536  1.00150.60      B    C  
ANISOU 6119  CG  LEU A 163     9911  31146  16164    958   1443  10405  B    C  
ATOM   6120  CD1 LEU A 163     -61.999  24.356   8.290  1.00151.41      B    C  
ANISOU 6120  CD1 LEU A 163    10094  31281  16152    966   1286  10246  B    C  
ATOM   6121  CD2 LEU A 163     -61.358  22.462   9.737  1.00152.98      B    C  
ANISOU 6121  CD2 LEU A 163    10164  31892  16069    648   1313   9740  B    C  
ATOM   6122  N   MET A 164     -57.509  26.301  11.644  1.00142.44      B    N  
ANISOU 6122  N   MET A 164     8889  28740  16493   1637   2268  12326  B    N  
ATOM   6123  CA  MET A 164     -56.115  26.457  12.091  1.00140.82      B    C  
ANISOU 6123  CA  MET A 164     8692  28289  16524   1722   2463  12646  B    C  
ATOM   6124  C   MET A 164     -55.539  25.105  12.513  1.00140.92      B    C  
ANISOU 6124  C   MET A 164     8576  28852  16117   1505   2390  12366  B    C  
ATOM   6125  O   MET A 164     -56.253  24.278  13.074  1.00140.43      B    O  
ANISOU 6125  O   MET A 164     8359  29077  15923   1419   2332  12235  B    O  
ATOM   6126  CB  MET A 164     -55.987  27.494  13.230  1.00141.55      B    C  
ANISOU 6126  CB  MET A 164     8977  27294  17513   1999   2764  13021  B    C  
ATOM   6127  CG  MET A 164     -56.801  28.789  13.019  1.00144.34      B    C  
ANISOU 6127  CG  MET A 164     9592  26949  18303   2137   2805  12990  B    C  
ATOM   6128  SD  MET A 164     -56.591  29.629  11.419  1.00148.23      B    S  
ANISOU 6128  SD  MET A 164    10390  27371  18558   2066   2655  12670  B    S  
ATOM   6129  CE  MET A 164     -57.787  30.937  11.585  1.00145.76      B    C  
ANISOU 6129  CE  MET A 164    10037  26574  18773   2305   2771  13043  B    C  
ATOM   6130  N   ALA A 165     -54.256  24.876  12.208  1.00137.28      B    N  
ANISOU 6130  N   ALA A 165     7933  28849  15378   1456   2423  12574  B    N  
ATOM   6131  CA  ALA A 165     -53.554  23.621  12.485  1.00136.49      B    C  
ANISOU 6131  CA  ALA A 165     7665  29401  14795   1222   2348  12313  B    C  
ATOM   6132  C   ALA A 165     -52.498  23.794  13.563  1.00135.95      B    C  
ANISOU 6132  C   ALA A 165     7648  28765  15244   1395   2594  12704  B    C  
ATOM   6133  O   ALA A 165     -51.827  24.825  13.579  1.00135.38      B    O  
ANISOU 6133  O   ALA A 165     7710  28012  15716   1630   2800  13117  B    O  
ATOM   6134  CB  ALA A 165     -52.900  23.114  11.210  1.00137.73      B    C  
ANISOU 6134  CB  ALA A 165     7863  30180  14287    945   2159  11796  B    C  
ATOM   6135  N   LEU A 166     -52.337  22.796  14.460  1.00131.63      B    N  
ANISOU 6135  N   LEU A 166     6747  28765  14502   1329   2618  12886  B    N  
ATOM   6136  CA  LEU A 166     -51.316  22.830  15.520  1.00129.99      B    C  
ANISOU 6136  CA  LEU A 166     6518  28069  14802   1515   2869  13340  B    C  
ATOM   6137  C   LEU A 166     -50.642  21.478  15.682  1.00131.47      B    C  
ANISOU 6137  C   LEU A 166     6615  29010  14327   1178   2706  12827  B    C  
ATOM   6138  O   LEU A 166     -51.303  20.451  15.534  1.00131.18      B    O  
ANISOU 6138  O   LEU A 166     6391  29845  13607    858   2478  12316  B    O  
ATOM   6139  CB  LEU A 166     -51.875  23.282  16.878  1.00129.24      B    C  
ANISOU 6139  CB  LEU A 166     6470  27042  15595   1826   3141  13806  B    C  
ATOM   6140  CG  LEU A 166     -52.361  24.725  17.013  1.00131.93      B    C  
ANISOU 6140  CG  LEU A 166     7150  26188  16790   2103   3347  13969  B    C  
ATOM   6141  CD1 LEU A 166     -53.243  24.871  18.235  1.00131.60      B    C  
ANISOU 6141  CD1 LEU A 166     7128  25482  17391   2286   3534  14170  B    C  
ATOM   6142  CD2 LEU A 166     -51.188  25.717  17.090  1.00132.11      B    C  
ANISOU 6142  CD2 LEU A 166     7408  25286  17502   2311   3624  14220  B    C  
ATOM   6143  N   MET A 167     -49.331  21.474  16.011  1.00127.52      B    N  
ANISOU 6143  N   MET A 167     5956  28517  13981   1290   2873  13298  B    N  
ATOM   6144  CA  MET A 167     -48.557  20.242  16.219  1.00126.70      B    C  
ANISOU 6144  CA  MET A 167     5671  29244  13226    973   2739  12923  B    C  
ATOM   6145  C   MET A 167     -47.754  20.279  17.535  1.00127.84      B    C  
ANISOU 6145  C   MET A 167     5942  28509  14124   1231   3011  13328  B    C  
ATOM   6146  O   MET A 167     -47.620  21.343  18.146  1.00126.61      B    O  
ANISOU 6146  O   MET A 167     5911  27155  15042   1690   3368  14036  B    O  
ATOM   6147  CB  MET A 167     -47.626  19.965  15.019  1.00128.38      B    C  
ANISOU 6147  CB  MET A 167     5967  30032  12780    669   2568  12354  B    C  
ATOM   6148  CG  MET A 167     -48.382  19.473  13.794  1.00131.08      B    C  
ANISOU 6148  CG  MET A 167     6381  31037  12385    290   2282  11472  B    C  
ATOM   6149  SD  MET A 167     -47.435  18.544  12.562  1.00133.50      B    S  
ANISOU 6149  SD  MET A 167     6796  32077  11851   -208   2081  10445  B    S  
ATOM   6150  CE  MET A 167     -47.137  17.023  13.424  1.00130.82      B    C  
ANISOU 6150  CE  MET A 167     6157  32643  10907   -644   1995   9881  B    C  
ATOM   6151  N   SER A 168     -47.228  19.112  17.975  1.00125.11      B    N  
ANISOU 6151  N   SER A 168     5319  29017  13201    966   2903  13138  B    N  
ATOM   6152  CA  SER A 168     -46.427  18.996  19.199  1.00116.28      B    C  
ANISOU 6152  CA  SER A 168     5180  26043  12959   1017   3042  12332  B    C  
ATOM   6153  C   SER A 168     -45.002  19.556  18.955  1.00120.21      B    C  
ANISOU 6153  C   SER A 168     5875  25970  13828   1167   3202  12510  B    C  
ATOM   6154  O   SER A 168     -43.984  18.881  19.150  1.00113.64      B    O  
ANISOU 6154  O   SER A 168     5689  24625  12862    861   3072  11403  B    O  
ATOM   6155  CB  SER A 168     -46.393  17.555  19.690  1.00111.91      B    C  
ANISOU 6155  CB  SER A 168     5300  25299  11923    460   2751  10667  B    C  
ATOM   6156  OG  SER A 168     -46.051  16.654  18.654  1.00121.07      B    O  
ANISOU 6156  OG  SER A 168     6126  27911  11963    -45   2485  10071  B    O  
ATOM   6157  N   ALA A 169     -44.966  20.826  18.539  1.00123.50      B    N  
ANISOU 6157  N   ALA A 169     5684  26445  14793   1669   3532  13983  B    N  
ATOM   6158  CA  ALA A 169     -43.778  21.576  18.170  1.00124.66      B    C  
ANISOU 6158  CA  ALA A 169     5841  26150  15376   1888   3757  14427  B    C  
ATOM   6159  C   ALA A 169     -44.030  23.080  18.250  1.00128.01      B    C  
ANISOU 6159  C   ALA A 169     6688  25080  16868   2213   4051  14571  B    C  
ATOM   6160  O   ALA A 169     -45.173  23.518  18.390  1.00128.59      B    O  
ANISOU 6160  O   ALA A 169     6798  24886  17176   2295   4067  14621  B    O  
ATOM   6161  CB  ALA A 169     -43.378  21.198  16.752  1.00126.11      B    C  
ANISOU 6161  CB  ALA A 169     5948  27534  14433   1475   3397  13865  B    C  
ATOM   6162  N   LEU A 170     -42.965  23.873  18.147  1.00125.75      B    N  
ANISOU 6162  N   LEU A 170     6494  24081  17206   2427   4330  14890  B    N  
ATOM   6163  CA  LEU A 170     -43.083  25.325  18.151  1.00125.22      B    C  
ANISOU 6163  CA  LEU A 170     6653  22859  18065   2692   4633  15106  B    C  
ATOM   6164  C   LEU A 170     -43.561  25.781  16.787  1.00129.90      B    C  
ANISOU 6164  C   LEU A 170     7438  24002  17918   2440   4275  14611  B    C  
ATOM   6165  O   LEU A 170     -43.151  25.202  15.778  1.00130.18      B    O  
ANISOU 6165  O   LEU A 170     7358  25065  17040   2181   3987  14364  B    O  
ATOM   6166  CB  LEU A 170     -41.738  26.001  18.504  1.00124.26      B    C  
ANISOU 6166  CB  LEU A 170     6711  21659  18843   2906   5027  15275  B    C  
ATOM   6167  CG  LEU A 170     -41.048  25.620  19.821  1.00126.43      B    C  
ANISOU 6167  CG  LEU A 170     7251  20843  19944   3026   5347  15081  B    C  
ATOM   6168  CD1 LEU A 170     -39.694  26.290  19.928  1.00125.91      B    C  
ANISOU 6168  CD1 LEU A 170     7368  19829  20641   3169   5699  15099  B    C  
ATOM   6169  CD2 LEU A 170     -41.917  25.947  21.037  1.00127.61      B    C  
ANISOU 6169  CD2 LEU A 170     7648  19838  21001   3169   5627  14907  B    C  
ATOM   6170  N   ARG A 171     -44.442  26.787  16.750  1.00128.88      B    N  
ANISOU 6170  N   ARG A 171     7365  23349  18255   2596   4391  14789  B    N  
ATOM   6171  CA  ARG A 171     -44.938  27.354  15.493  1.00130.17      B    C  
ANISOU 6171  CA  ARG A 171     7572  23965  17922   2478   4167  14624  B    C  
ATOM   6172  C   ARG A 171     -43.772  27.993  14.751  1.00134.22      B    C  
ANISOU 6172  C   ARG A 171     8396  24145  18456   2411   4176  14346  B    C  
ATOM   6173  O   ARG A 171     -42.944  28.643  15.391  1.00133.02      B    O  
ANISOU 6173  O   ARG A 171     8339  23073  19131   2615   4511  14586  B    O  
ATOM   6174  CB  ARG A 171     -46.044  28.387  15.754  1.00130.21      B    C  
ANISOU 6174  CB  ARG A 171     7691  23274  18509   2642   4294  14726  B    C  
ATOM   6175  CG  ARG A 171     -47.287  27.833  16.429  1.00137.68      B    C  
ANISOU 6175  CG  ARG A 171     8904  24154  19256   2475   4077  14093  B    C  
ATOM   6176  CD  ARG A 171     -48.135  28.972  16.949  1.00143.39      B    C  
ANISOU 6176  CD  ARG A 171    10079  23786  20616   2534   4161  13705  B    C  
ATOM   6177  NE  ARG A 171     -48.452  28.825  18.372  1.00149.13      B    N  
ANISOU 6177  NE  ARG A 171    11183  23599  21883   2525   4266  13237  B    N  
ATOM   6178  CZ  ARG A 171     -47.669  29.227  19.371  1.00158.83      B    C  
ANISOU 6178  CZ  ARG A 171    13089  23599  23662   2431   4359  12433  B    C  
ATOM   6179  NH1 ARG A 171     -46.490  29.785  19.120  1.00154.07      B    N1+
ANISOU 6179  NH1 ARG A 171    12303  22771  23465   2597   4626  12921  B    N1+
ATOM   6180  NH2 ARG A 171     -48.054  29.061  20.631  1.00143.44      B    N  
ANISOU 6180  NH2 ARG A 171    10545  21279  22678   2833   4892  13478  B    N  
ATOM   6181  N   ASP A 172     -43.672  27.776  13.429  1.00134.38      B    N  
ANISOU 6181  N   ASP A 172     8343  25057  17660   2208   3908  14162  B    N  
ATOM   6182  CA  ASP A 172     -42.570  28.331  12.638  1.00135.46      B    C  
ANISOU 6182  CA  ASP A 172     8623  25070  17776   2182   3945  14111  B    C  
ATOM   6183  C   ASP A 172     -43.083  29.192  11.444  1.00141.70      B    C  
ANISOU 6183  C   ASP A 172     9792  25731  18317   2044   3750  13607  B    C  
ATOM   6184  O   ASP A 172     -42.407  29.324  10.419  1.00141.51      B    O  
ANISOU 6184  O   ASP A 172     9779  26060  17928   1950   3677  13546  B    O  
ATOM   6185  CB  ASP A 172     -41.623  27.211  12.168  1.00136.99      B    C  
ANISOU 6185  CB  ASP A 172     8773  26055  17222   1921   3749  13757  B    C  
ATOM   6186  CG  ASP A 172     -40.317  27.705  11.563  1.00141.92      B    C  
ANISOU 6186  CG  ASP A 172     9789  26221  17911   1830   3772  13369  B    C  
ATOM   6187  OD1 ASP A 172     -39.708  28.641  12.135  1.00141.43      B    O  
ANISOU 6187  OD1 ASP A 172     9864  25194  18679   2050   4063  13633  B    O  
ATOM   6188  OD2 ASP A 172     -39.922  27.181  10.505  1.00144.91      B    O1-
ANISOU 6188  OD2 ASP A 172    10276  27224  17560   1556   3538  12870  B    O1-
ATOM   6189  N   GLY A 173     -44.252  29.807  11.635  1.00141.70      B    N  
ANISOU 6189  N   GLY A 173     9828  25403  18607   2149   3770  13685  B    N  
ATOM   6190  CA  GLY A 173     -44.869  30.698  10.661  1.00143.07      B    C  
ANISOU 6190  CA  GLY A 173    10144  25532  18684   2136   3673  13581  B    C  
ATOM   6191  C   GLY A 173     -45.956  30.102   9.795  1.00149.43      B    C  
ANISOU 6191  C   GLY A 173    11172  26864  18741   1859   3293  12851  B    C  
ATOM   6192  O   GLY A 173     -46.137  28.881   9.739  1.00149.24      B    O  
ANISOU 6192  O   GLY A 173    10993  27555  18155   1687   3121  12623  B    O  
ATOM   6193  N   GLU A 174     -46.691  30.996   9.118  1.00150.03      B    N  
ANISOU 6193  N   GLU A 174    11345  26788  18870   1907   3247  12858  B    N  
ATOM   6194  CA  GLU A 174     -47.778  30.685   8.187  1.00151.96      B    C  
ANISOU 6194  CA  GLU A 174    11619  27550  18567   1763   2981  12516  B    C  
ATOM   6195  C   GLU A 174     -47.284  30.871   6.754  1.00157.72      B    C  
ANISOU 6195  C   GLU A 174    12718  28320  18890   1567   2810  11959  B    C  
ATOM   6196  O   GLU A 174     -46.414  31.715   6.520  1.00157.07      B    O  
ANISOU 6196  O   GLU A 174    12727  27869  19083   1650   2950  12166  B    O  
ATOM   6197  CB  GLU A 174     -48.999  31.586   8.454  1.00152.84      B    C  
ANISOU 6197  CB  GLU A 174    11828  27177  19069   1895   3004  12577  B    C  
ATOM   6198  CG  GLU A 174     -49.525  31.519   9.880  1.00161.05      B    C  
ANISOU 6198  CG  GLU A 174    13258  27393  20543   1858   3019  12040  B    C  
ATOM   6199  CD  GLU A 174     -50.757  32.340  10.211  1.00180.32      B    C  
ANISOU 6199  CD  GLU A 174    16700  28597  23219   1643   2782  10667  B    C  
ATOM   6200  OE1 GLU A 174     -51.226  33.124   9.352  1.00177.89      B    O  
ANISOU 6200  OE1 GLU A 174    16297  28411  22883   1727   2764  10923  B    O  
ATOM   6201  OE2 GLU A 174     -51.257  32.196  11.350  1.00178.24      B    O1-
ANISOU 6201  OE2 GLU A 174    16260  28170  23293   1762   2909  10931  B    O1-
ATOM   6202  N   LEU A 175     -47.838  30.094   5.794  1.00158.22      B    N  
ANISOU 6202  N   LEU A 175    12726  29064  18325   1389   2579  11629  B    N  
ATOM   6203  CA  LEU A 175     -47.470  30.158   4.371  1.00159.77      B    C  
ANISOU 6203  CA  LEU A 175    13071  29510  18124   1262   2461  11369  B    C  
ATOM   6204  C   LEU A 175     -48.631  29.717   3.438  1.00165.09      B    C  
ANISOU 6204  C   LEU A 175    13991  30314  18421   1092   2195  10710  B    C  
ATOM   6205  O   LEU A 175     -49.691  29.308   3.918  1.00164.54      B    O  
ANISOU 6205  O   LEU A 175    13797  30379  18340   1100   2121  10667  B    O  
ATOM   6206  CB  LEU A 175     -46.201  29.324   4.090  1.00159.99      B    C  
ANISOU 6206  CB  LEU A 175    13079  29911  17798   1099   2457  11169  B    C  
ATOM   6207  CG  LEU A 175     -44.899  30.124   3.928  1.00163.08      B    C  
ANISOU 6207  CG  LEU A 175    13761  29715  18486   1128   2600  11159  B    C  
ATOM   6208  CD1 LEU A 175     -43.693  29.289   4.296  1.00163.01      B    C  
ANISOU 6208  CD1 LEU A 175    13686  29939  18311   1018   2650  11055  B    C  
ATOM   6209  CD2 LEU A 175     -44.747  30.675   2.508  1.00165.67      B    C  
ANISOU 6209  CD2 LEU A 175    14349  29979  18619   1058   2519  10931  B    C  
ATOM   6210  N   SER A 176     -48.416  29.830   2.102  1.00165.01      B    N  
ANISOU 6210  N   SER A 176    14053  30561  18082   1016   2106  10595  B    N  
ATOM   6211  CA  SER A 176     -49.378  29.512   1.036  1.00166.40      B    C  
ANISOU 6211  CA  SER A 176    14297  31019  17909    919   1900  10254  B    C  
ATOM   6212  C   SER A 176     -48.981  28.263   0.210  1.00171.06      B    C  
ANISOU 6212  C   SER A 176    15088  31882  18023    646   1746   9519  B    C  
ATOM   6213  O   SER A 176     -47.810  27.870   0.214  1.00170.70      B    O  
ANISOU 6213  O   SER A 176    15024  31990  17845    560   1819   9469  B    O  
ATOM   6214  CB  SER A 176     -49.518  30.709   0.097  1.00169.19      B    C  
ANISOU 6214  CB  SER A 176    14966  30892  18425    989   1885  10231  B    C  
ATOM   6215  OG  SER A 176     -48.273  31.044  -0.495  1.00174.83      B    O  
ANISOU 6215  OG  SER A 176    16113  31138  19178    890   1931   9869  B    O  
ATOM   6216  N   GLU A 177     -49.963  27.671  -0.521  1.00170.11      B    N  
ANISOU 6216  N   GLU A 177    14877  32185  17573    566   1568   9301  B    N  
ATOM   6217  CA  GLU A 177     -49.785  26.486  -1.379  1.00170.86      B    C  
ANISOU 6217  CA  GLU A 177    14979  32745  17195    344   1437   8799  B    C  
ATOM   6218  C   GLU A 177     -49.863  26.833  -2.892  1.00174.67      B    C  
ANISOU 6218  C   GLU A 177    15821  32972  17574    304   1332   8476  B    C  
ATOM   6219  O   GLU A 177     -50.199  27.965  -3.250  1.00174.55      B    O  
ANISOU 6219  O   GLU A 177    15905  32660  17756    451   1340   8754  B    O  
ATOM   6220  CB  GLU A 177     -50.825  25.403  -1.029  1.00171.99      B    C  
ANISOU 6220  CB  GLU A 177    15025  33119  17203    224   1301   8396  B    C  
ATOM   6221  CG  GLU A 177     -50.263  24.228  -0.240  1.00178.52      B    C  
ANISOU 6221  CG  GLU A 177    16112  33624  18093     31   1322   7707  B    C  
ATOM   6222  CD  GLU A 177     -49.293  23.292  -0.944  1.00192.14      B    C  
ANISOU 6222  CD  GLU A 177    18685  34357  19962   -203   1291   6498  B    C  
ATOM   6223  OE1 GLU A 177     -49.325  23.211  -2.194  1.00186.94      B    O  
ANISOU 6223  OE1 GLU A 177    17875  34206  18948   -241   1210   6581  B    O  
ATOM   6224  OE2 GLU A 177     -48.537  22.592  -0.233  1.00187.77      B    O1-
ANISOU 6224  OE2 GLU A 177    17829  34294  19219   -291   1370   6597  B    O1-
ATOM   6225  N   GLN A 178     -49.547  25.847  -3.768  1.00172.96      B    N  
ANISOU 6225  N   GLN A 178    15520  33287  16911    130   1252   8185  B    N  
ATOM   6226  CA  GLN A 178     -49.536  25.988  -5.233  1.00173.69      B    C  
ANISOU 6226  CA  GLN A 178    15795  33409  16789     89   1161   8015  B    C  
ATOM   6227  C   GLN A 178     -50.852  25.467  -5.852  1.00176.75      B    C  
ANISOU 6227  C   GLN A 178    16324  33717  17115     25    960   7549  B    C  
ATOM   6228  O   GLN A 178     -51.815  26.230  -5.945  1.00176.53      B    O  
ANISOU 6228  O   GLN A 178    16309  33512  17252    154    896   7743  B    O  
ATOM   6229  CB  GLN A 178     -48.317  25.260  -5.845  1.00174.90      B    C  
ANISOU 6229  CB  GLN A 178    16061  33707  16685    -75   1204   7690  B    C  
ATOM   6230  CG  GLN A 178     -46.961  25.680  -5.277  1.00187.42      B    C  
ANISOU 6230  CG  GLN A 178    18352  34040  18818    -81   1375   7235  B    C  
ATOM   6231  CD  GLN A 178     -46.378  26.874  -5.985  1.00203.73      B    C  
ANISOU 6231  CD  GLN A 178    21482  34482  21444    -66   1410   6555  B    C  
ATOM   6232  NE2 GLN A 178     -45.261  26.662  -6.664  1.00200.10      B    N  
ANISOU 6232  NE2 GLN A 178    20900  34457  20672   -134   1472   6665  B    N  
ATOM   6233  OE1 GLN A 178     -46.893  27.996  -5.903  1.00200.66      B    O  
ANISOU 6233  OE1 GLN A 178    20974  34094  21173     79   1420   7028  B    O  
ATOM   6234  N   SER A 179     -50.885  24.180  -6.277  1.00174.66      B    N  
ANISOU 6234  N   SER A 179    15887  34011  16462   -163    871   7206  B    N  
ATOM   6235  CA  SER A 179     -52.054  23.512  -6.862  1.00175.08      B    C  
ANISOU 6235  CA  SER A 179    15918  34230  16373   -242    686   6859  B    C  
ATOM   6236  C   SER A 179     -52.917  22.906  -5.748  1.00176.90      B    C  
ANISOU 6236  C   SER A 179    16067  34350  16798   -270    649   6651  B    C  
ATOM   6237  O   SER A 179     -52.407  22.692  -4.643  1.00175.96      B    O  
ANISOU 6237  O   SER A 179    15801  34305  16752   -285    764   6761  B    O  
ATOM   6238  CB  SER A 179     -51.617  22.439  -7.856  1.00178.14      B    C  
ANISOU 6238  CB  SER A 179    16517  34621  16546   -433    627   6256  B    C  
ATOM   6239  OG  SER A 179     -52.703  22.004  -8.658  1.00185.00      B    O  
ANISOU 6239  OG  SER A 179    17774  34932  17585   -463    453   5682  B    O  
ATOM   6240  N   ASP A 180     -54.221  22.635  -6.038  1.00174.57      B    N  
ANISOU 6240  N   ASP A 180    15588  34342  16397   -278    490   6605  B    N  
ATOM   6241  CA  ASP A 180     -55.237  22.122  -5.095  1.00173.91      B    C  
ANISOU 6241  CA  ASP A 180    15293  34378  16409   -301    438   6527  B    C  
ATOM   6242  C   ASP A 180     -55.319  23.110  -3.910  1.00175.20      B    C  
ANISOU 6242  C   ASP A 180    15496  34103  16968   -113    560   6916  B    C  
ATOM   6243  O   ASP A 180     -55.187  22.729  -2.746  1.00174.15      B    O  
ANISOU 6243  O   ASP A 180    15181  34086  16904   -141    638   6968  B    O  
ATOM   6244  CB  ASP A 180     -54.937  20.666  -4.655  1.00174.84      B    C  
ANISOU 6244  CB  ASP A 180    15334  34705  16392   -528    443   6019  B    C  
ATOM   6245  CG  ASP A 180     -56.112  19.947  -4.021  1.00180.51      B    C  
ANISOU 6245  CG  ASP A 180    16239  34898  17451   -572    362   5507  B    C  
ATOM   6246  OD1 ASP A 180     -57.028  19.537  -4.766  1.00181.28      B    O  
ANISOU 6246  OD1 ASP A 180    16370  35003  17505   -623    210   5229  B    O  
ATOM   6247  OD2 ASP A 180     -56.098  19.762  -2.785  1.00183.31      B    O1-
ANISOU 6247  OD2 ASP A 180    16652  34919  18079   -562    451   5427  B    O1-
ATOM   6248  N   SER A 181     -55.518  24.402  -4.256  1.00172.45      B    N  
ANISOU 6248  N   SER A 181    15119  33695  16707     81    581   7447  B    N  
ATOM   6249  CA  SER A 181     -55.547  25.597  -3.405  1.00171.37      B    C  
ANISOU 6249  CA  SER A 181    14951  33249  16914    291    710   7978  B    C  
ATOM   6250  C   SER A 181     -56.467  25.522  -2.166  1.00172.66      B    C  
ANISOU 6250  C   SER A 181    15035  33203  17364    349    719   7983  B    C  
ATOM   6251  O   SER A 181     -56.319  26.371  -1.284  1.00171.81      B    O  
ANISOU 6251  O   SER A 181    14893  32825  17564    509    856   8404  B    O  
ATOM   6252  CB  SER A 181     -55.939  26.814  -4.236  1.00174.20      B    C  
ANISOU 6252  CB  SER A 181    15625  33086  17478    434    669   8068  B    C  
ATOM   6253  OG  SER A 181     -55.663  28.034  -3.567  1.00179.39      B    O  
ANISOU 6253  OG  SER A 181    16647  32866  18647    576    803   8147  B    O  
ATOM   6254  N   ASN A 182     -57.373  24.519  -2.068  1.00169.65      B    N  
ANISOU 6254  N   ASN A 182    14352  33358  16751    238    595   7811  B    N  
ATOM   6255  CA  ASN A 182     -58.288  24.346  -0.926  1.00168.72      B    C  
ANISOU 6255  CA  ASN A 182    14031  33261  16813    284    603   7908  B    C  
ATOM   6256  C   ASN A 182     -57.519  23.847   0.332  1.00169.04      B    C  
ANISOU 6256  C   ASN A 182    14006  33284  16940    229    748   7904  B    C  
ATOM   6257  O   ASN A 182     -57.869  22.822   0.929  1.00168.59      B    O  
ANISOU 6257  O   ASN A 182    13772  33512  16773     93    714   7646  B    O  
ATOM   6258  CB  ASN A 182     -59.438  23.397  -1.301  1.00170.28      B    C  
ANISOU 6258  CB  ASN A 182    14201  33614  16885    147    419   7413  B    C  
ATOM   6259  CG  ASN A 182     -60.812  23.973  -1.052  1.00187.75      B    C  
ANISOU 6259  CG  ASN A 182    17358  34049  19930    238    332   6554  B    C  
ATOM   6260  ND2 ASN A 182     -61.504  23.441  -0.054  1.00183.20      B    N  
ANISOU 6260  ND2 ASN A 182    16346  33963  19299    223    345   6753  B    N  
ATOM   6261  OD1 ASN A 182     -61.280  24.875  -1.758  1.00183.02      B    O  
ANISOU 6261  OD1 ASN A 182    16615  33674  19249    372    271   6969  B    O  
ATOM   6262  N   ARG A 183     -56.477  24.614   0.726  1.00164.98      B    N  
ANISOU 6262  N   ARG A 183    13363  32834  16488    358    921   8489  B    N  
ATOM   6263  CA  ARG A 183     -55.555  24.386   1.847  1.00163.50      B    C  
ANISOU 6263  CA  ARG A 183    13047  32701  16373    353   1080   8686  B    C  
ATOM   6264  C   ARG A 183     -54.706  25.665   2.126  1.00163.83      B    C  
ANISOU 6264  C   ARG A 183    13258  32204  16787    555   1260   9150  B    C  
ATOM   6265  O   ARG A 183     -54.822  26.654   1.396  1.00163.73      B    O  
ANISOU 6265  O   ARG A 183    13373  31954  16884    677   1258   9357  B    O  
ATOM   6266  CB  ARG A 183     -54.647  23.156   1.577  1.00164.40      B    C  
ANISOU 6266  CB  ARG A 183    13158  33190  16114     98   1049   8203  B    C  
ATOM   6267  CG  ARG A 183     -53.858  23.190   0.256  1.00174.18      B    C  
ANISOU 6267  CG  ARG A 183    15043  33739  17397     -1   1002   7541  B    C  
ATOM   6268  CD  ARG A 183     -53.335  21.817  -0.146  1.00182.63      B    C  
ANISOU 6268  CD  ARG A 183    16467  34559  18365   -261    945   6634  B    C  
ATOM   6269  NE  ARG A 183     -52.605  21.836  -1.417  1.00188.65      B    N  
ANISOU 6269  NE  ARG A 183    17656  34920  19102   -318    920   6250  B    N  
ATOM   6270  CZ  ARG A 183     -51.621  20.997  -1.733  1.00197.91      B    C  
ANISOU 6270  CZ  ARG A 183    19334  35468  20395   -471    951   5505  B    C  
ATOM   6271  NH1 ARG A 183     -51.205  20.089  -0.859  1.00188.59      B    N1+
ANISOU 6271  NH1 ARG A 183    17505  35366  18786   -620    996   5734  B    N1+
ATOM   6272  NH2 ARG A 183     -51.018  21.087  -2.911  1.00188.63      B    N  
ANISOU 6272  NH2 ARG A 183    17750  35264  18655   -517    930   5912  B    N  
ATOM   6273  N   LYS A 184     -53.881  25.637   3.202  1.00159.24      B    N  
ANISOU 6273  N   LYS A 184    12396  31815  16292    623   1433   9624  B    N  
ATOM   6274  CA  LYS A 184     -52.980  26.710   3.666  1.00157.59      B    C  
ANISOU 6274  CA  LYS A 184    12218  31196  16462    822   1641  10176  B    C  
ATOM   6275  C   LYS A 184     -51.901  26.084   4.559  1.00157.47      B    C  
ANISOU 6275  C   LYS A 184    12142  31241  16447    752   1753  10164  B    C  
ATOM   6276  O   LYS A 184     -52.232  25.268   5.423  1.00157.10      B    O  
ANISOU 6276  O   LYS A 184    11940  31417  16335    674   1733  10036  B    O  
ATOM   6277  CB  LYS A 184     -53.763  27.813   4.418  1.00158.89      B    C  
ANISOU 6277  CB  LYS A 184    12498  30672  17200   1049   1738  10473  B    C  
ATOM   6278  CG  LYS A 184     -52.972  29.091   4.703  1.00168.03      B    C  
ANISOU 6278  CG  LYS A 184    14323  30557  18962   1125   1873  10202  B    C  
ATOM   6279  CD  LYS A 184     -53.127  30.134   3.601  1.00175.32      B    C  
ANISOU 6279  CD  LYS A 184    15793  30810  20012   1108   1781   9760  B    C  
ATOM   6280  CE  LYS A 184     -52.365  31.398   3.914  1.00182.90      B    C  
ANISOU 6280  CE  LYS A 184    17299  30731  21462   1144   1898   9520  B    C  
ATOM   6281  NZ  LYS A 184     -52.488  32.398   2.822  1.00190.27      B    N1+
ANISOU 6281  NZ  LYS A 184    18759  31077  22459   1097   1789   9053  B    N1+
ATOM   6282  N   ILE A 185     -50.620  26.459   4.345  1.00152.89      B    N  
ANISOU 6282  N   ILE A 185    11410  30841  15842    821   1891  10625  B    N  
ATOM   6283  CA  ILE A 185     -49.475  25.896   5.071  1.00151.22      B    C  
ANISOU 6283  CA  ILE A 185    11061  30811  15584    768   2001  10720  B    C  
ATOM   6284  C   ILE A 185     -49.220  26.599   6.423  1.00150.70      B    C  
ANISOU 6284  C   ILE A 185    10989  30117  16153   1004   2222  11220  B    C  
ATOM   6285  O   ILE A 185     -49.101  27.822   6.498  1.00149.73      B    O  
ANISOU 6285  O   ILE A 185    10950  29423  16519   1228   2374  11655  B    O  
ATOM   6286  CB  ILE A 185     -48.189  25.875   4.182  1.00153.44      B    C  
ANISOU 6286  CB  ILE A 185    11556  31080  15666    652   2011  10467  B    C  
ATOM   6287  CG1 ILE A 185     -48.313  24.816   3.059  1.00154.50      B    C  
ANISOU 6287  CG1 ILE A 185    11700  31823  15181    371   1813   9837  B    C  
ATOM   6288  CG2 ILE A 185     -46.909  25.639   5.009  1.00153.22      B    C  
ANISOU 6288  CG2 ILE A 185    11502  30934  15782    655   2163  10598  B    C  
ATOM   6289  CD1 ILE A 185     -47.287  24.939   1.909  1.00159.72      B    C  
ANISOU 6289  CD1 ILE A 185    12784  32159  15744    257   1801   9382  B    C  
ATOM   6290  N   TYR A 186     -49.133  25.773   7.478  1.00146.52      B    N  
ANISOU 6290  N   TYR A 186    10097  30031  15545    991   2272  11457  B    N  
ATOM   6291  CA  TYR A 186     -48.765  26.098   8.855  1.00144.84      B    C  
ANISOU 6291  CA  TYR A 186     9802  29333  15899   1200   2496  11951  B    C  
ATOM   6292  C   TYR A 186     -47.537  25.240   9.154  1.00145.58      B    C  
ANISOU 6292  C   TYR A 186     9839  29718  15757   1057   2520  11800  B    C  
ATOM   6293  O   TYR A 186     -47.660  24.013   9.177  1.00146.03      B    O  
ANISOU 6293  O   TYR A 186     9767  30416  15301    809   2370  11366  B    O  
ATOM   6294  CB  TYR A 186     -49.925  25.799   9.834  1.00145.69      B    C  
ANISOU 6294  CB  TYR A 186     9866  29294  16197   1237   2476  11904  B    C  
ATOM   6295  CG  TYR A 186     -50.956  26.899   9.988  1.00146.91      B    C  
ANISOU 6295  CG  TYR A 186    10182  28776  16862   1440   2538  12082  B    C  
ATOM   6296  CD1 TYR A 186     -50.800  27.899  10.944  1.00147.40      B    C  
ANISOU 6296  CD1 TYR A 186    10394  27907  17706   1686   2786  12435  B    C  
ATOM   6297  CD2 TYR A 186     -52.131  26.890   9.241  1.00148.17      B    C  
ANISOU 6297  CD2 TYR A 186    10374  29177  16748   1363   2350  11803  B    C  
ATOM   6298  CE1 TYR A 186     -51.765  28.892  11.118  1.00147.64      B    C  
ANISOU 6298  CE1 TYR A 186    10522  27397  18180   1852   2852  12589  B    C  
ATOM   6299  CE2 TYR A 186     -53.105  27.875   9.408  1.00148.69      B    C  
ANISOU 6299  CE2 TYR A 186    10538  28712  17247   1544   2403  11992  B    C  
ATOM   6300  CZ  TYR A 186     -52.915  28.878  10.345  1.00152.67      B    C  
ANISOU 6300  CZ  TYR A 186    11385  28128  18494   1710   2604  12031  B    C  
ATOM   6301  OH  TYR A 186     -53.861  29.861  10.506  1.00152.49      B    O  
ANISOU 6301  OH  TYR A 186    11446  27620  18873   1864   2660  12175  B    O  
ATOM   6302  N   ARG A 187     -46.347  25.845   9.293  1.00140.82      B    N  
ANISOU 6302  N   ARG A 187     9065  29009  15430   1244   2734  12446  B    N  
ATOM   6303  CA  ARG A 187     -45.131  25.050   9.520  1.00139.88      B    C  
ANISOU 6303  CA  ARG A 187     8827  29264  15059   1122   2760  12390  B    C  
ATOM   6304  C   ARG A 187     -44.707  25.029  11.005  1.00139.86      B    C  
ANISOU 6304  C   ARG A 187     8791  28694  15654   1310   2975  12755  B    C  
ATOM   6305  O   ARG A 187     -44.953  25.987  11.742  1.00138.56      B    O  
ANISOU 6305  O   ARG A 187     8680  27681  16286   1616   3212  13256  B    O  
ATOM   6306  CB  ARG A 187     -43.967  25.490   8.606  1.00139.78      B    C  
ANISOU 6306  CB  ARG A 187     8914  29230  14968   1108   2810  12426  B    C  
ATOM   6307  CG  ARG A 187     -43.684  26.987   8.585  1.00144.95      B    C  
ANISOU 6307  CG  ARG A 187    10058  28610  16407   1321   2985  12475  B    C  
ATOM   6308  CD  ARG A 187     -42.816  27.397   7.418  1.00149.94      B    C  
ANISOU 6308  CD  ARG A 187    11060  29028  16881   1194   2936  12054  B    C  
ATOM   6309  NE  ARG A 187     -42.161  28.682   7.663  1.00153.08      B    N  
ANISOU 6309  NE  ARG A 187    11784  28389  17989   1373   3139  12197  B    N  
ATOM   6310  CZ  ARG A 187     -41.055  29.092   7.050  1.00160.80      B    C  
ANISOU 6310  CZ  ARG A 187    13271  28813  19015   1239   3130  11644  B    C  
ATOM   6311  NH1 ARG A 187     -40.462  28.319   6.147  1.00149.84      B    N1+
ANISOU 6311  NH1 ARG A 187    11277  28709  16945   1192   3108  12151  B    N1+
ATOM   6312  NH2 ARG A 187     -40.530  30.274   7.338  1.00151.64      B    N  
ANISOU 6312  NH2 ARG A 187    11729  27406  18481   1588   3454  12683  B    N  
ATOM   6313  N   PHE A 188     -44.097  23.905  11.436  1.00136.23      B    N  
ANISOU 6313  N   PHE A 188     7979  29015  14768   1172   2939  12810  B    N  
ATOM   6314  CA  PHE A 188     -43.657  23.677  12.817  1.00134.50      B    C  
ANISOU 6314  CA  PHE A 188     7651  28402  15050   1347   3140  13210  B    C  
ATOM   6315  C   PHE A 188     -42.245  23.060  12.894  1.00134.85      B    C  
ANISOU 6315  C   PHE A 188     7681  28686  14870   1216   3151  13059  B    C  
ATOM   6316  O   PHE A 188     -41.832  22.341  11.981  1.00135.07      B    O  
ANISOU 6316  O   PHE A 188     7628  29610  14081    883   2938  12559  B    O  
ATOM   6317  CB  PHE A 188     -44.661  22.768  13.550  1.00135.84      B    C  
ANISOU 6317  CB  PHE A 188     7740  28889  14984   1207   3005  12909  B    C  
ATOM   6318  CG  PHE A 188     -46.072  23.305  13.601  1.00136.96      B    C  
ANISOU 6318  CG  PHE A 188     7958  28693  15388   1323   2989  12960  B    C  
ATOM   6319  CD1 PHE A 188     -46.459  24.196  14.593  1.00138.29      B    C  
ANISOU 6319  CD1 PHE A 188     8323  27708  16513   1649   3247  13336  B    C  
ATOM   6320  CD2 PHE A 188     -47.013  22.925  12.650  1.00139.32      B    C  
ANISOU 6320  CD2 PHE A 188     8287  29599  15050   1065   2716  12386  B    C  
ATOM   6321  CE1 PHE A 188     -47.758  24.708  14.626  1.00139.18      B    C  
ANISOU 6321  CE1 PHE A 188     8497  27550  16835   1735   3227  13350  B    C  
ATOM   6322  CE2 PHE A 188     -48.310  23.442  12.680  1.00141.44      B    C  
ANISOU 6322  CE2 PHE A 188     8681  29478  15581   1166   2691  12363  B    C  
ATOM   6323  CZ  PHE A 188     -48.672  24.332  13.666  1.00139.40      B    C  
ANISOU 6323  CZ  PHE A 188     8421  28379  16166   1518   2950  12996  B    C  
ATOM   6324  N   LYS A 189     -41.526  23.331  14.004  1.00130.03      B    N  
ANISOU 6324  N   LYS A 189     6885  27509  15010   1551   3474  13834  B    N  
ATOM   6325  CA  LYS A 189     -40.186  22.805  14.265  1.00128.93      B    C  
ANISOU 6325  CA  LYS A 189     6658  27527  14803   1510   3541  13892  B    C  
ATOM   6326  C   LYS A 189     -40.054  22.223  15.697  1.00128.55      B    C  
ANISOU 6326  C   LYS A 189     6554  27066  15223   1647   3701  14105  B    C  
ATOM   6327  O   LYS A 189     -40.337  22.902  16.687  1.00126.79      B    O  
ANISOU 6327  O   LYS A 189     6409  25675  16089   2048   4058  14646  B    O  
ATOM   6328  CB  LYS A 189     -39.090  23.861  13.999  1.00130.61      B    C  
ANISOU 6328  CB  LYS A 189     7150  26776  15702   1733   3793  14107  B    C  
ATOM   6329  CG  LYS A 189     -39.336  25.248  14.598  1.00139.93      B    C  
ANISOU 6329  CG  LYS A 189     9100  26013  18053   1945   4017  13737  B    C  
ATOM   6330  CD  LYS A 189     -38.122  26.149  14.413  1.00144.01      B    C  
ANISOU 6330  CD  LYS A 189    10051  25557  19111   2002   4182  13511  B    C  
ATOM   6331  CE  LYS A 189     -38.292  27.492  15.077  1.00148.60      B    C  
ANISOU 6331  CE  LYS A 189    11136  24598  20726   2173   4420  13283  B    C  
ATOM   6332  NZ  LYS A 189     -37.040  28.292  15.018  1.00155.38      B    N1+
ANISOU 6332  NZ  LYS A 189    12476  24558  22001   2132   4516  12828  B    N1+
ATOM   6333  N   GLN A 190     -39.635  20.946  15.775  1.00122.78      B    N  
ANISOU 6333  N   GLN A 190     5691  27287  13675   1279   3456  13596  B    N  
ATOM   6334  CA  GLN A 190     -39.372  20.208  17.006  1.00111.49      B    C  
ANISOU 6334  CA  GLN A 190     5326  24369  12666   1044   3366  12134  B    C  
ATOM   6335  C   GLN A 190     -37.906  19.763  16.990  1.00108.93      B    C  
ANISOU 6335  C   GLN A 190     5593  23498  12297    799   3294  11209  B    C  
ATOM   6336  O   GLN A 190     -37.560  18.748  16.376  1.00107.70      B    O  
ANISOU 6336  O   GLN A 190     5432  24275  11215    317   3009  10389  B    O  
ATOM   6337  CB  GLN A 190     -40.347  19.029  17.190  1.00110.65      B    C  
ANISOU 6337  CB  GLN A 190     5311  24906  11824    611   3042  11218  B    C  
ATOM   6338  CG  GLN A 190     -40.181  18.272  18.511  1.00 98.76      B    C  
ANISOU 6338  CG  GLN A 190     4831  21904  10789    414   2981   9855  B    C  
ATOM   6339  CD  GLN A 190     -40.154  19.170  19.735  1.00104.78      B    C  
ANISOU 6339  CD  GLN A 190     6088  20915  12809    850   3299  10116  B    C  
ATOM   6340  NE2 GLN A 190     -41.304  19.328  20.390  1.00101.32      B    N  
ANISOU 6340  NE2 GLN A 190     5613  20176  12708   1004   3373  10341  B    N  
ATOM   6341  OE1 GLN A 190     -39.106  19.708  20.123  1.00 86.03      B    O  
ANISOU 6341  OE1 GLN A 190     4115  17465  11109   1018   3499  10046  B    O  
ATOM   6342  N   ASN A 191     -37.051  20.571  17.642  1.00102.24      B    N  
ANISOU 6342  N   ASN A 191     5188  21161  12497   1125   3599  11357  B    N  
ATOM   6343  CA  ASN A 191     -35.597  20.436  17.686  1.00 97.95      B    C  
ANISOU 6343  CA  ASN A 191     5156  19947  12112   1004   3607  10710  B    C  
ATOM   6344  C   ASN A 191     -35.111  19.603  18.871  1.00 94.85      B    C  
ANISOU 6344  C   ASN A 191     5750  18297  11993    742   3481   9276  B    C  
ATOM   6345  O   ASN A 191     -33.905  19.369  19.004  1.00 91.67      B    O  
ANISOU 6345  O   ASN A 191     5809  17317  11705    615   3464   8646  B    O  
ATOM   6346  CB  ASN A 191     -34.941  21.821  17.701  1.00 98.84      B    C  
ANISOU 6346  CB  ASN A 191     5109  19217  13228   1491   4052  11687  B    C  
ATOM   6347  CG  ASN A 191     -35.164  22.625  16.436  1.00120.78      B    C  
ANISOU 6347  CG  ASN A 191     6873  23258  15758   1773   4213  13197  B    C  
ATOM   6348  ND2 ASN A 191     -35.387  23.924  16.578  1.00118.42      B    N  
ANISOU 6348  ND2 ASN A 191     6187  22299  16509   2304   4706  14398  B    N  
ATOM   6349  OD1 ASN A 191     -35.140  22.101  15.318  1.00109.45      B    O  
ANISOU 6349  OD1 ASN A 191     4938  23427  13223   1516   3941  13321  B    O  
ATOM   6350  N   VAL A 192     -36.041  19.142  19.716  1.00 88.82      B    N  
ANISOU 6350  N   VAL A 192     5262  17170  11316    668   3399   8815  B    N  
ATOM   6351  CA  VAL A 192     -35.721  18.260  20.834  1.00 80.63      B    C  
ANISOU 6351  CA  VAL A 192     5058  15116  10460    427   3276   7560  B    C  
ATOM   6352  C   VAL A 192     -36.108  16.847  20.382  1.00 83.05      B    C  
ANISOU 6352  C   VAL A 192     5326  16414   9816    -65   2950   6738  B    C  
ATOM   6353  O   VAL A 192     -37.247  16.674  19.936  1.00 86.69      B    O  
ANISOU 6353  O   VAL A 192     5290  17853   9794   -135   2859   7053  B    O  
ATOM   6354  CB  VAL A 192     -36.401  18.676  22.169  1.00 81.72      B    C  
ANISOU 6354  CB  VAL A 192     5554  14085  11410    662   3456   7523  B    C  
ATOM   6355  CG1 VAL A 192     -36.035  17.715  23.295  1.00 74.70      B    C  
ANISOU 6355  CG1 VAL A 192     5449  12318  10614    415   3317   6309  B    C  
ATOM   6356  CG2 VAL A 192     -36.029  20.100  22.563  1.00 83.01      B    C  
ANISOU 6356  CG2 VAL A 192     5658  13285  12598   1091   3879   8246  B    C  
ATOM   6357  N   PRO A 193     -35.191  15.838  20.444  1.00 75.49      B    N  
ANISOU 6357  N   PRO A 193     4812  15258   8612   -419   2816   5700  B    N  
ATOM   6358  CA  PRO A 193     -35.566  14.478  20.017  1.00 75.59      B    C  
ANISOU 6358  CA  PRO A 193     4731  16118   7870   -920   2618   4839  B    C  
ATOM   6359  C   PRO A 193     -36.721  13.935  20.840  1.00 78.04      B    C  
ANISOU 6359  C   PRO A 193     5212  16156   8284   -975   2576   4486  B    C  
ATOM   6360  O   PRO A 193     -36.729  14.028  22.077  1.00 72.60      B    O  
ANISOU 6360  O   PRO A 193     5084  14238   8264   -783   2649   4278  B    O  
ATOM   6361  CB  PRO A 193     -34.293  13.657  20.243  1.00 72.84      B    C  
ANISOU 6361  CB  PRO A 193     4925  15133   7618  -1176   2601   3869  B    C  
ATOM   6362  CG  PRO A 193     -33.197  14.653  20.269  1.00 76.20      B    C  
ANISOU 6362  CG  PRO A 193     5493  14958   8501   -865   2720   4381  B    C  
ATOM   6363  CD  PRO A 193     -33.788  15.869  20.913  1.00 72.67      B    C  
ANISOU 6363  CD  PRO A 193     5014  13891   8706   -394   2885   5245  B    C  
ATOM   6364  N   ILE A 194     -37.735  13.438  20.126  1.00 79.02      B    N  
ANISOU 6364  N   ILE A 194     4782  17530   7714  -1238   2469   4466  B    N  
ATOM   6365  CA  ILE A 194     -38.965  12.913  20.703  1.00 78.13      B    C  
ANISOU 6365  CA  ILE A 194     4697  17393   7597  -1321   2429   4186  B    C  
ATOM   6366  C   ILE A 194     -39.269  11.502  20.166  1.00 83.88      B    C  
ANISOU 6366  C   ILE A 194     5212  19005   7653  -1912   2349   3168  B    C  
ATOM   6367  O   ILE A 194     -38.952  11.197  19.016  1.00 88.46      B    O  
ANISOU 6367  O   ILE A 194     5296  20775   7540  -2246   2305   2995  B    O  
ATOM   6368  CB  ILE A 194     -40.184  13.875  20.465  1.00 86.07      B    C  
ANISOU 6368  CB  ILE A 194     5127  19018   8556   -999   2447   5314  B    C  
ATOM   6369  CG1 ILE A 194     -40.518  14.082  18.974  1.00 94.70      B    C  
ANISOU 6369  CG1 ILE A 194     5278  21940   8762  -1132   2362   5962  B    C  
ATOM   6370  CG2 ILE A 194     -40.034  15.210  21.193  1.00 85.29      B    C  
ANISOU 6370  CG2 ILE A 194     5261  17782   9364   -435   2647   6174  B    C  
ATOM   6371  CD1 ILE A 194     -41.940  13.871  18.651  1.00104.26      B    C  
ANISOU 6371  CD1 ILE A 194     5903  24260   9451  -1254   2271   6188  B    C  
ATOM   6372  N   PRO A 195     -39.909  10.629  20.974  1.00 77.75      B    N  
ANISOU 6372  N   PRO A 195     4752  17695   7093  -2070   2371   2460  B    N  
ATOM   6373  CA  PRO A 195     -40.321   9.324  20.442  1.00 79.99      B    C  
ANISOU 6373  CA  PRO A 195     4741  18805   6846  -2651   2386   1477  B    C  
ATOM   6374  C   PRO A 195     -41.558   9.521  19.559  1.00 90.77      B    C  
ANISOU 6374  C   PRO A 195     5276  21755   7455  -2794   2286   1910  B    C  
ATOM   6375  O   PRO A 195     -42.230  10.555  19.658  1.00 92.35      B    O  
ANISOU 6375  O   PRO A 195     5258  22107   7725  -2382   2222   2967  B    O  
ATOM   6376  CB  PRO A 195     -40.606   8.508  21.702  1.00 76.20      B    C  
ANISOU 6376  CB  PRO A 195     4863  17096   6994  -2663   2488    793  B    C  
ATOM   6377  CG  PRO A 195     -40.967   9.516  22.720  1.00 77.07      B    C  
ANISOU 6377  CG  PRO A 195     5332  16276   7674  -2114   2455   1593  B    C  
ATOM   6378  CD  PRO A 195     -40.397  10.828  22.354  1.00 73.90      B    C  
ANISOU 6378  CD  PRO A 195     4805  15950   7324  -1746   2421   2552  B    C  
ATOM   6379  N   SER A 196     -41.833   8.546  18.683  1.00 91.52      B    N  
ANISOU 6379  N   SER A 196     4852  23071   6852  -3394   2309   1090  B    N  
ATOM   6380  CA  SER A 196     -42.954   8.544  17.741  1.00 98.91      B    C  
ANISOU 6380  CA  SER A 196     4888  25788   6904  -3667   2215   1296  B    C  
ATOM   6381  C   SER A 196     -44.338   8.753  18.402  1.00102.21      B    C  
ANISOU 6381  C   SER A 196     5262  26066   7506  -3435   2165   1723  B    C  
ATOM   6382  O   SER A 196     -45.206   9.356  17.772  1.00107.23      B    O  
ANISOU 6382  O   SER A 196     5187  27981   7573  -3349   2045   2547  B    O  
ATOM   6383  CB  SER A 196     -42.971   7.236  16.960  1.00107.32      B    C  
ANISOU 6383  CB  SER A 196     5531  27865   7380  -4446   2339    -43  B    C  
ATOM   6384  OG  SER A 196     -43.011   6.130  17.847  1.00113.27      B    O  
ANISOU 6384  OG  SER A 196     6843  27392   8801  -4649   2548  -1116  B    O  
ATOM   6385  N   TYR A 197     -44.539   8.296  19.661  1.00 92.39      B    N  
ANISOU 6385  N   TYR A 197     4730  23328   7045  -3313   2263   1249  B    N  
ATOM   6386  CA  TYR A 197     -45.836   8.426  20.335  1.00 92.00      B    C  
ANISOU 6386  CA  TYR A 197     4680  23072   7203  -3119   2236   1557  B    C  
ATOM   6387  C   TYR A 197     -46.148   9.883  20.725  1.00 97.92      B    C  
ANISOU 6387  C   TYR A 197     5464  23429   8311  -2455   2160   2956  B    C  
ATOM   6388  O   TYR A 197     -47.304  10.199  21.017  1.00 99.44      B    O  
ANISOU 6388  O   TYR A 197     5454  23777   8552  -2277   2131   3435  B    O  
ATOM   6389  CB  TYR A 197     -45.940   7.483  21.559  1.00 85.81      B    C  
ANISOU 6389  CB  TYR A 197     4600  20863   7139  -3187   2390    666  B    C  
ATOM   6390  CG  TYR A 197     -45.196   7.904  22.806  1.00 77.93      B    C  
ANISOU 6390  CG  TYR A 197     4461  18112   7037  -2716   2438    912  B    C  
ATOM   6391  CD1 TYR A 197     -45.810   8.699  23.771  1.00 77.06      B    C  
ANISOU 6391  CD1 TYR A 197     4642  17211   7426  -2238   2411   1620  B    C  
ATOM   6392  CD2 TYR A 197     -43.925   7.414  23.080  1.00 73.97      B    C  
ANISOU 6392  CD2 TYR A 197     4447  16764   6893  -2794   2542    338  B    C  
ATOM   6393  CE1 TYR A 197     -45.163   9.024  24.961  1.00 70.85      B    C  
ANISOU 6393  CE1 TYR A 197     4580  14941   7398  -1883   2478   1708  B    C  
ATOM   6394  CE2 TYR A 197     -43.270   7.729  24.269  1.00 67.75      B    C  
ANISOU 6394  CE2 TYR A 197     4382  14506   6852  -2407   2583    502  B    C  
ATOM   6395  CZ  TYR A 197     -43.880   8.565  25.191  1.00 71.86      B    C  
ANISOU 6395  CZ  TYR A 197     5148  14372   7782  -1967   2546   1173  B    C  
ATOM   6396  OH  TYR A 197     -43.239   8.921  26.350  1.00 67.42      B    O  
ANISOU 6396  OH  TYR A 197     5217  12522   7876  -1638   2599   1278  B    O  
ATOM   6397  N   LEU A 198     -45.131  10.766  20.686  1.00 93.88      B    N  
ANISOU 6397  N   LEU A 198     5153  22423   8093  -2111   2175   3590  B    N  
ATOM   6398  CA  LEU A 198     -45.285  12.165  21.070  1.00 93.05      B    C  
ANISOU 6398  CA  LEU A 198     5064  21779   8510  -1500   2219   4842  B    C  
ATOM   6399  C   LEU A 198     -45.552  13.126  19.878  1.00103.85      B    C  
ANISOU 6399  C   LEU A 198     5527  24602   9331  -1331   2174   6052  B    C  
ATOM   6400  O   LEU A 198     -45.696  14.331  20.111  1.00104.00      B    O  
ANISOU 6400  O   LEU A 198     5446  24187   9881   -808   2294   7185  B    O  
ATOM   6401  CB  LEU A 198     -44.075  12.625  21.899  1.00 86.58      B    C  
ANISOU 6401  CB  LEU A 198     4996  19401   8499  -1194   2336   4823  B    C  
ATOM   6402  CG  LEU A 198     -44.030  12.126  23.351  1.00 83.62      B    C  
ANISOU 6402  CG  LEU A 198     5446  17493   8834  -1136   2410   4126  B    C  
ATOM   6403  CD1 LEU A 198     -42.866  12.739  24.080  1.00 78.83      B    C  
ANISOU 6403  CD1 LEU A 198     5418  15616   8917   -837   2522   4229  B    C  
ATOM   6404  CD2 LEU A 198     -45.316  12.467  24.113  1.00 85.58      B    C  
ANISOU 6404  CD2 LEU A 198     5688  17413   9418   -898   2454   4512  B    C  
ATOM   6405  N   ILE A 199     -45.688  12.614  18.624  1.00107.27      B    N  
ANISOU 6405  N   ILE A 199     5224  26800   8736  -1771   2046   5853  B    N  
ATOM   6406  CA  ILE A 199     -46.052  13.498  17.497  1.00116.15      B    C  
ANISOU 6406  CA  ILE A 199     5371  29512   9251  -1599   1996   7124  B    C  
ATOM   6407  C   ILE A 199     -47.574  13.762  17.603  1.00124.94      B    C  
ANISOU 6407  C   ILE A 199     5969  31266  10238  -1454   1963   7777  B    C  
ATOM   6408  O   ILE A 199     -48.328  12.828  17.887  1.00123.72      B    O  
ANISOU 6408  O   ILE A 199     5880  31286   9841  -1822   1894   6882  B    O  
ATOM   6409  CB  ILE A 199     -45.613  13.020  16.065  1.00126.02      B    C  
ANISOU 6409  CB  ILE A 199     5896  32627   9359  -2102   1877   6825  B    C  
ATOM   6410  CG1 ILE A 199     -46.423  11.826  15.534  1.00130.67      B    C  
ANISOU 6410  CG1 ILE A 199     6018  34587   9043  -2794   1770   5741  B    C  
ATOM   6411  CG2 ILE A 199     -44.107  12.786  15.940  1.00122.36      B    C  
ANISOU 6411  CG2 ILE A 199     5924  31504   9062  -2225   1929   6232  B    C  
ATOM   6412  CD1 ILE A 199     -47.452  12.175  14.477  1.00137.30      B    C  
ANISOU 6412  CD1 ILE A 199     6893  35341   9935  -2640   1699   5789  B    C  
ATOM   6413  N   ALA A 200     -48.018  15.020  17.430  1.00126.43      B    N  
ANISOU 6413  N   ALA A 200     5653  31685  10699   -905   2059   9329  B    N  
ATOM   6414  CA  ALA A 200     -49.445  15.353  17.548  1.00130.25      B    C  
ANISOU 6414  CA  ALA A 200     5684  32616  11191   -713   2057  10009  B    C  
ATOM   6415  C   ALA A 200     -49.923  16.289  16.450  1.00134.04      B    C  
ANISOU 6415  C   ALA A 200     6454  32490  11987   -476   2050  10097  B    C  
ATOM   6416  O   ALA A 200     -49.123  17.041  15.901  1.00133.08      B    O  
ANISOU 6416  O   ALA A 200     6405  32068  12093   -253   2135  10545  B    O  
ATOM   6417  CB  ALA A 200     -49.723  15.986  18.898  1.00125.41      B    C  
ANISOU 6417  CB  ALA A 200     5699  30153  11796   -220   2276  10360  B    C  
ATOM   6418  N   LEU A 201     -51.239  16.258  16.149  1.00133.02      B    N  
ANISOU 6418  N   LEU A 201     6205  32614  11721   -523   1956   9960  B    N  
ATOM   6419  CA  LEU A 201     -51.846  17.138  15.149  1.00133.36      B    C  
ANISOU 6419  CA  LEU A 201     6345  32376  11948   -318   1933  10189  B    C  
ATOM   6420  C   LEU A 201     -53.316  17.419  15.474  1.00136.45      B    C  
ANISOU 6420  C   LEU A 201     6897  32213  12733   -168   1925  10177  B    C  
ATOM   6421  O   LEU A 201     -54.078  16.486  15.724  1.00136.36      B    O  
ANISOU 6421  O   LEU A 201     6745  32712  12355   -459   1812   9626  B    O  
ATOM   6422  CB  LEU A 201     -51.719  16.538  13.726  1.00134.12      B    C  
ANISOU 6422  CB  LEU A 201     6457  33136  11367   -714   1743   9327  B    C  
ATOM   6423  CG  LEU A 201     -52.430  17.277  12.577  1.00138.01      B    C  
ANISOU 6423  CG  LEU A 201     7227  33145  12065   -563   1679   9264  B    C  
ATOM   6424  CD1 LEU A 201     -51.877  18.697  12.386  1.00137.74      B    C  
ANISOU 6424  CD1 LEU A 201     7342  32420  12572   -139   1830  10092  B    C  
ATOM   6425  CD2 LEU A 201     -52.371  16.475  11.294  1.00140.69      B    C  
ANISOU 6425  CD2 LEU A 201     7698  33860  11899   -945   1514   8284  B    C  
ATOM   6426  N   VAL A 202     -53.702  18.710  15.442  1.00134.11      B    N  
ANISOU 6426  N   VAL A 202     6623  31287  13044    270   2065  11013  B    N  
ATOM   6427  CA  VAL A 202     -55.076  19.197  15.599  1.00134.24      B    C  
ANISOU 6427  CA  VAL A 202     6648  30966  13391    447   2073  11212  B    C  
ATOM   6428  C   VAL A 202     -55.351  20.184  14.462  1.00137.30      B    C  
ANISOU 6428  C   VAL A 202     7341  30858  13968    570   2031  11138  B    C  
ATOM   6429  O   VAL A 202     -54.516  21.053  14.198  1.00136.36      B    O  
ANISOU 6429  O   VAL A 202     7324  30329  14156    781   2160  11572  B    O  
ATOM   6430  CB  VAL A 202     -55.429  19.794  16.998  1.00136.26      B    C  
ANISOU 6430  CB  VAL A 202     7092  30159  14523    799   2311  11722  B    C  
ATOM   6431  CG1 VAL A 202     -54.561  21.001  17.347  1.00135.35      B    C  
ANISOU 6431  CG1 VAL A 202     7148  29069  15209   1199   2598  12444  B    C  
ATOM   6432  CG2 VAL A 202     -56.912  20.157  17.093  1.00136.26      B    C  
ANISOU 6432  CG2 VAL A 202     7064  29956  14754    914   2295  11814  B    C  
ATOM   6433  N   VAL A 203     -56.498  20.008  13.764  1.00135.97      B    N  
ANISOU 6433  N   VAL A 203     7036  31137  13490    455   1867  10882  B    N  
ATOM   6434  CA  VAL A 203     -56.973  20.874  12.676  1.00136.13      B    C  
ANISOU 6434  CA  VAL A 203     7162  30973  13587    576   1810  10973  B    C  
ATOM   6435  C   VAL A 203     -58.475  21.156  12.912  1.00139.34      B    C  
ANISOU 6435  C   VAL A 203     7703  30939  14302    663   1770  10843  B    C  
ATOM   6436  O   VAL A 203     -59.300  20.244  12.855  1.00139.38      B    O  
ANISOU 6436  O   VAL A 203     7557  31457  13945    432   1622  10379  B    O  
ATOM   6437  CB  VAL A 203     -56.705  20.321  11.243  1.00139.29      B    C  
ANISOU 6437  CB  VAL A 203     7727  31763  13434    267   1602  10189  B    C  
ATOM   6438  CG1 VAL A 203     -57.189  21.305  10.182  1.00139.38      B    C  
ANISOU 6438  CG1 VAL A 203     7853  31529  13577    431   1558  10379  B    C  
ATOM   6439  CG2 VAL A 203     -55.230  19.991  11.030  1.00138.97      B    C  
ANISOU 6439  CG2 VAL A 203     7716  31947  13141    136   1634  10064  B    C  
ATOM   6440  N   GLY A 204     -58.803  22.418  13.170  1.00136.93      B    N  
ANISOU 6440  N   GLY A 204     7399  30060  14566   1018   1932  11550  B    N  
ATOM   6441  CA  GLY A 204     -60.176  22.852  13.405  1.00137.12      B    C  
ANISOU 6441  CA  GLY A 204     7408  29814  14876   1150   1927  11661  B    C  
ATOM   6442  C   GLY A 204     -60.313  24.347  13.575  1.00140.17      B    C  
ANISOU 6442  C   GLY A 204     8144  29114  15999   1459   2101  11976  B    C  
ATOM   6443  O   GLY A 204     -59.336  25.080  13.412  1.00139.22      B    O  
ANISOU 6443  O   GLY A 204     8128  28643  16127   1596   2240  12294  B    O  
ATOM   6444  N   ALA A 205     -61.536  24.813  13.882  1.00139.13      B    N  
ANISOU 6444  N   ALA A 205     7926  28780  16157   1607   2132  12199  B    N  
ATOM   6445  CA  ALA A 205     -61.817  26.233  14.116  1.00138.99      B    C  
ANISOU 6445  CA  ALA A 205     8069  27927  16814   1903   2326  12630  B    C  
ATOM   6446  C   ALA A 205     -61.348  26.588  15.528  1.00141.81      B    C  
ANISOU 6446  C   ALA A 205     8661  27358  17862   2056   2597  12778  B    C  
ATOM   6447  O   ALA A 205     -62.121  26.501  16.488  1.00141.66      B    O  
ANISOU 6447  O   ALA A 205     8593  27076  18153   2132   2687  12870  B    O  
ATOM   6448  CB  ALA A 205     -63.304  26.514  13.933  1.00139.97      B    C  
ANISOU 6448  CB  ALA A 205     8189  28007  16987   1934   2224  12503  B    C  
ATOM   6449  N   LEU A 206     -60.053  26.919  15.660  1.00139.16      B    N  
ANISOU 6449  N   LEU A 206     8298  26813  17764   2170   2787  13178  B    N  
ATOM   6450  CA  LEU A 206     -59.434  27.188  16.957  1.00138.27      B    C  
ANISOU 6450  CA  LEU A 206     8251  25933  18351   2357   3101  13525  B    C  
ATOM   6451  C   LEU A 206     -59.112  28.655  17.182  1.00140.34      B    C  
ANISOU 6451  C   LEU A 206     8838  25112  19373   2561   3348  13650  B    C  
ATOM   6452  O   LEU A 206     -58.750  29.373  16.247  1.00140.42      B    O  
ANISOU 6452  O   LEU A 206     8925  25128  19300   2574   3311  13673  B    O  
ATOM   6453  CB  LEU A 206     -58.134  26.366  17.124  1.00138.21      B    C  
ANISOU 6453  CB  LEU A 206     8211  26197  18105   2248   3109  13476  B    C  
ATOM   6454  CG  LE