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***  3BLH_A_VS_4bcg_A  ***

elNémo ID: 22051216393486404

Job options:

ID        	=	 22051216393486404
JOBID     	=	 3BLH_A_VS_4bcg_A
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 3BLH_A_VS_4bcg_A

CRYST1  172.920  172.920   95.760  90.00  90.00 120.00 H 3           9
ATOM      1  N   VAL A   8      38.365  -4.357 -38.054  1.00115.79      A    N  
ANISOU    1  N   VAL A   8    14119  17287  12589   1000    -36  -1013  A    N  
ATOM      2  CA  VAL A   8      37.673  -3.858 -36.866  1.00115.57      A    C  
ANISOU    2  CA  VAL A   8    14029  17153  12730   1001   -102   -876  A    C  
ATOM      3  C   VAL A   8      38.654  -3.207 -35.889  1.00108.34      A    C  
ANISOU    3  C   VAL A   8    13115  16091  11958    978     36   -748  A    C  
ATOM      4  O   VAL A   8      39.592  -3.854 -35.418  1.00107.78      A    O  
ANISOU    4  O   VAL A   8    12994  15926  12033    932    120   -832  A    O  
ATOM      5  CB  VAL A   8      36.842  -4.981 -36.179  1.00 71.68      A    C  
ANISOU    5  CB  VAL A   8     8350  11529   7357    954   -233  -1002  A    C  
ATOM      6  CG1 VAL A   8      36.690  -4.735 -34.688  1.00 60.19      A    C  
ANISOU    6  CG1 VAL A   8     6819   9916   6135    929   -230   -895  A    C  
ATOM      7  CG2 VAL A   8      35.481  -5.104 -36.843  1.00 75.83      A    C  
ANISOU    7  CG2 VAL A   8     8857  12207   7749    976   -403  -1038  A    C  
ATOM      8  N   GLU A   9      38.433  -1.925 -35.599  1.00101.15      A    N  
ANISOU    8  N   GLU A   9    12269  15162  11001   1014     52   -549  A    N  
ATOM      9  CA  GLU A   9      39.327  -1.154 -34.734  1.00 98.88      A    C  
ANISOU    9  CA  GLU A   9    12007  14743  10821    980    175   -416  A    C  
ATOM     10  C   GLU A   9      39.383  -1.675 -33.298  1.00 89.71      A    C  
ANISOU   10  C   GLU A   9    10734  13417   9934    934    161   -439  A    C  
ATOM     11  O   GLU A   9      38.397  -2.191 -32.773  1.00 91.86      A    O  
ANISOU   11  O   GLU A   9    10928  13666  10307    941     43   -481  A    O  
ATOM     12  CB  GLU A   9      38.931   0.320 -34.732  1.00109.84      A    C  
ANISOU   12  CB  GLU A   9    13515  16126  12095   1033    175   -204  A    C  
ATOM     13  CG  GLU A   9      39.405   1.094 -35.944  1.00124.01      A    C  
ANISOU   13  CG  GLU A   9    15458  18029  13631   1047    251   -128  A    C  
ATOM     14  CD  GLU A   9      39.238   2.586 -35.757  1.00138.02      A    C  
ANISOU   14  CD  GLU A   9    17377  19739  15324   1087    271     95  A    C  
ATOM     15  OE1 GLU A   9      39.154   3.022 -34.588  1.00140.54      A    O  
ANISOU   15  OE1 GLU A   9    17679  19910  15811   1081    272    179  A    O  
ATOM     16  OE2 GLU A   9      39.189   3.319 -36.771  1.00144.03      A    O1-
ANISOU   16  OE2 GLU A   9    18284  20591  15849   1124    283    186  A    O1-
ATOM     17  N   CYS A  10      40.539  -1.529 -32.659  1.00 80.19      A    N  
ANISOU   17  N   CYS A  10     9519  12109   8841    878    281   -407  A    N  
ATOM     18  CA  CYS A  10      40.726  -2.086 -31.325  1.00 75.50      A    C  
ANISOU   18  CA  CYS A  10     8829  11364   8495    832    269   -433  A    C  
ATOM     19  C   CYS A  10      41.778  -1.370 -30.469  1.00 74.72      A    C  
ANISOU   19  C   CYS A  10     8745  11154   8492    779    381   -319  A    C  
ATOM     20  O   CYS A  10      42.726  -1.987 -29.995  1.00 78.98      A    O  
ANISOU   20  O   CYS A  10     9212  11632   9164    734    437   -388  A    O  
ATOM     21  CB  CYS A  10      41.058  -3.569 -31.423  1.00 66.58      A    C  
ANISOU   21  CB  CYS A  10     7611  10223   7465    811    249   -632  A    C  
ATOM     22  SG  CYS A  10      40.824  -4.391 -29.866  1.00 83.94      A    S  
ANISOU   22  SG  CYS A  10     9710  12241   9942    764    180   -662  A    S  
ATOM     23  N   PRO A  11      41.571  -0.070 -30.235  1.00 71.68      A    N  
ANISOU   23  N   PRO A  11     8457  10737   8040    788    401   -146  A    N  
ATOM     24  CA  PRO A  11      42.486   0.855 -29.557  1.00 62.50      A    C  
ANISOU   24  CA  PRO A  11     7347   9477   6924    724    503    -19  A    C  
ATOM     25  C   PRO A  11      42.965   0.388 -28.191  1.00 62.86      A    C  
ANISOU   25  C   PRO A  11     7299   9385   7201    666    504    -40  A    C  
ATOM     26  O   PRO A  11      44.059   0.757 -27.775  1.00 70.13      A    O  
ANISOU   26  O   PRO A  11     8218  10256   8172    592    596      6  A    O  
ATOM     27  CB  PRO A  11      41.622   2.107 -29.356  1.00 67.75      A    C  
ANISOU   27  CB  PRO A  11     8136  10098   7507    775    463    145  A    C  
ATOM     28  CG  PRO A  11      40.563   2.021 -30.389  1.00 69.50      A    C  
ANISOU   28  CG  PRO A  11     8388  10451   7569    871    374    118  A    C  
ATOM     29  CD  PRO A  11      40.293   0.574 -30.595  1.00 70.23      A    C  
ANISOU   29  CD  PRO A  11     8344  10607   7733    871    308    -66  A    C  
ATOM     30  N   PHE A  12      42.145  -0.384 -27.490  1.00 61.40      A    N  
ANISOU   30  N   PHE A  12     7037   9145   7147    690    402   -103  A    N  
ATOM     31  CA  PHE A  12      42.365  -0.607 -26.065  1.00 55.29      A    C  
ANISOU   31  CA  PHE A  12     6208   8229   6571    640    388    -83  A    C  
ATOM     32  C   PHE A  12      42.671  -2.060 -25.769  1.00 53.85      A    C  
ANISOU   32  C   PHE A  12     5910   8015   6536    621    352   -233  A    C  
ATOM     33  O   PHE A  12      42.691  -2.485 -24.613  1.00 51.23      A    O  
ANISOU   33  O   PHE A  12     5530   7568   6368    586    316   -232  A    O  
ATOM     34  CB  PHE A  12      41.151  -0.140 -25.250  1.00 58.58      A    C  
ANISOU   34  CB  PHE A  12     6651   8583   7023    675    309      0  A    C  
ATOM     35  CG  PHE A  12      40.795   1.295 -25.474  1.00 62.39      A    C  
ANISOU   35  CG  PHE A  12     7265   9071   7368    720    335    147  A    C  
ATOM     36  CD1 PHE A  12      41.770   2.280 -25.410  1.00 69.97      A    C  
ANISOU   36  CD1 PHE A  12     8324   9978   8284    667    433    249  A    C  
ATOM     37  CD2 PHE A  12      39.498   1.665 -25.753  1.00 64.29      A    C  
ANISOU   37  CD2 PHE A  12     7536   9370   7523    815    257    184  A    C  
ATOM     38  CE1 PHE A  12      41.452   3.612 -25.613  1.00 71.51      A    C  
ANISOU   38  CE1 PHE A  12     8672  10149   8351    706    453    388  A    C  
ATOM     39  CE2 PHE A  12      39.173   2.996 -25.958  1.00 71.60      A    C  
ANISOU   39  CE2 PHE A  12     8600  10284   8322    880    274    322  A    C  
ATOM     40  CZ  PHE A  12      40.150   3.970 -25.887  1.00 70.18      A    C  
ANISOU   40  CZ  PHE A  12     8545  10022   8098    825    372    425  A    C  
ATOM     41  N   CYS A  13      42.903  -2.826 -26.824  1.00 53.55      A    N  
ANISOU   41  N   CYS A  13     5843   8073   6431    647    360   -362  A    N  
ATOM     42  CA  CYS A  13      43.351  -4.189 -26.651  1.00 59.28      A    C  
ANISOU   42  CA  CYS A  13     6483   8755   7287    642    336   -512  A    C  
ATOM     43  C   CYS A  13      44.513  -4.422 -27.599  1.00 61.56      A    C  
ANISOU   43  C   CYS A  13     6752   9136   7501    660    437   -597  A    C  
ATOM     44  O   CYS A  13      44.310  -4.560 -28.805  1.00 63.29      A    O  
ANISOU   44  O   CYS A  13     7003   9478   7566    698    448   -671  A    O  
ATOM     45  CB  CYS A  13      42.210  -5.149 -26.950  1.00 62.45      A    C  
ANISOU   45  CB  CYS A  13     6867   9170   7691    664    220   -622  A    C  
ATOM     46  SG  CYS A  13      42.517  -6.822 -26.424  1.00 60.87      A    S  
ANISOU   46  SG  CYS A  13     6599   8848   7681    647    162   -784  A    S  
ATOM     47  N   ASP A  14      45.731  -4.441 -27.059  1.00 57.62      A    N  
ANISOU   47  N   ASP A  14     6196   8594   7103    632    511   -588  A    N  
ATOM     48  CA  ASP A  14      46.935  -4.608 -27.884  1.00 56.52      A    C  
ANISOU   48  CA  ASP A  14     6011   8564   6900    649    625   -665  A    C  
ATOM     49  C   ASP A  14      47.162  -6.069 -28.253  1.00 53.38      A    C  
ANISOU   49  C   ASP A  14     5552   8163   6567    719    596   -864  A    C  
ATOM     50  O   ASP A  14      46.776  -6.978 -27.505  1.00 54.86      A    O  
ANISOU   50  O   ASP A  14     5717   8219   6908    732    496   -923  A    O  
ATOM     51  CB  ASP A  14      48.173  -4.061 -27.162  1.00 60.34      A    C  
ANISOU   51  CB  ASP A  14     6433   9025   7469    591    712   -582  A    C  
ATOM     52  CG  ASP A  14      48.230  -2.542 -27.149  1.00 74.14      A    C  
ANISOU   52  CG  ASP A  14     8265  10800   9106    513    778   -404  A    C  
ATOM     53  OD1 ASP A  14      47.494  -1.888 -27.931  1.00 78.47      A    O  
ANISOU   53  OD1 ASP A  14     8920  11411   9484    523    779   -349  A    O  
ATOM     54  OD2 ASP A  14      49.027  -2.004 -26.348  1.00 79.61      A    O1-
ANISOU   54  OD2 ASP A  14     8924  11446   9879    440    821   -318  A    O1-
ATOM     55  N   GLU A  15      47.785  -6.293 -29.405  1.00 62.03      A    N  
ANISOU   55  N   GLU A  15     6634   9397   7538    763    685   -968  A    N  
ATOM     56  CA  GLU A  15      48.183  -7.644 -29.800  1.00 66.86      A    C  
ANISOU   56  CA  GLU A  15     7196  10003   8204    846    677  -1171  A    C  
ATOM     57  C   GLU A  15      49.356  -8.140 -28.958  1.00 60.94      A    C  
ANISOU   57  C   GLU A  15     6332   9181   7640    874    710  -1201  A    C  
ATOM     58  O   GLU A  15      50.310  -7.396 -28.710  1.00 57.50      A    O  
ANISOU   58  O   GLU A  15     5829   8809   7210    835    809  -1110  A    O  
ATOM     59  CB  GLU A  15      48.545  -7.684 -31.279  1.00 69.37      A    C  
ANISOU   59  CB  GLU A  15     7535  10506   8318    893    777  -1277  A    C  
ATOM     60  CG  GLU A  15      47.522  -7.020 -32.174  1.00 82.84      A    C  
ANISOU   60  CG  GLU A  15     9354  12310   9811    868    750  -1224  A    C  
ATOM     61  CD  GLU A  15      47.873  -7.148 -33.644  1.00103.19      A    C  
ANISOU   61  CD  GLU A  15    11964  15071  12171    913    844  -1338  A    C  
ATOM     62  OE1 GLU A  15      48.456  -8.188 -34.037  1.00107.36      A    O  
ANISOU   62  OE1 GLU A  15    12447  15618  12727    988    877  -1525  A    O  
ATOM     63  OE2 GLU A  15      47.560  -6.209 -34.408  1.00112.30      A    O1-
ANISOU   63  OE2 GLU A  15    13201  16348  13120    880    883  -1242  A    O1-
ATOM     64  N   VAL A  16      49.277  -9.399 -28.532  1.00 56.98      A    N  
ANISOU   64  N   VAL A  16     5815   8548   7288    937    622  -1327  A    N  
ATOM     65  CA  VAL A  16      50.275 -10.001 -27.644  1.00 57.10      A    C  
ANISOU   65  CA  VAL A  16     5731   8470   7494    986    620  -1357  A    C  
ATOM     66  C   VAL A  16      51.672 -10.074 -28.303  1.00 54.43      A    C  
ANISOU   66  C   VAL A  16     5279   8286   7115   1064    762  -1444  A    C  
ATOM     67  O   VAL A  16      52.691 -10.265 -27.633  1.00 56.59      A    O  
ANISOU   67  O   VAL A  16     5438   8541   7523   1101    786  -1440  A    O  
ATOM     68  CB  VAL A  16      49.810 -11.405 -27.154  1.00 54.27      A    C  
ANISOU   68  CB  VAL A  16     5413   7920   7286   1044    487  -1477  A    C  
ATOM     69  CG1 VAL A  16      50.026 -12.443 -28.227  1.00 51.28      A    C  
ANISOU   69  CG1 VAL A  16     5056   7579   6850   1158    508  -1695  A    C  
ATOM     70  CG2 VAL A  16      50.531 -11.819 -25.887  1.00 52.71      A    C  
ANISOU   70  CG2 VAL A  16     5145   7585   7297   1069    442  -1439  A    C  
ATOM     71  N   SER A  17      51.714  -9.897 -29.618  1.00 52.35      A    N  
ANISOU   71  N   SER A  17     5042   8191   6658   1088    858  -1521  A    N  
ATOM     72  CA  SER A  17      52.978  -9.841 -30.360  1.00 59.79      A    C  
ANISOU   72  CA  SER A  17     5873   9320   7526   1148   1017  -1598  A    C  
ATOM     73  C   SER A  17      53.934  -8.765 -29.838  1.00 62.89      A    C  
ANISOU   73  C   SER A  17     6151   9804   7940   1058   1116  -1440  A    C  
ATOM     74  O   SER A  17      55.116  -8.808 -30.132  1.00 74.13      A    O  
ANISOU   74  O   SER A  17     7437  11371   9359   1102   1237  -1496  A    O  
ATOM     75  CB  SER A  17      52.713  -9.594 -31.849  1.00 64.98      A    C  
ANISOU   75  CB  SER A  17     6603  10154   7931   1153   1108  -1668  A    C  
ATOM     76  OG  SER A  17      52.241  -8.267 -32.087  1.00 71.17      A    O  
ANISOU   76  OG  SER A  17     7460  11017   8564   1025   1142  -1489  A    O  
ATOM     77  N   LYS A  18      53.425  -7.797 -29.083  1.00 55.14      A    N  
ANISOU   77  N   LYS A  18     5225   8748   6977    931   1066  -1250  A    N  
ATOM     78  CA  LYS A  18      54.281  -6.781 -28.474  1.00 58.00      A    C  
ANISOU   78  CA  LYS A  18     5500   9167   7371    824   1140  -1100  A    C  
ATOM     79  C   LYS A  18      55.273  -7.431 -27.503  1.00 67.73      A    C  
ANISOU   79  C   LYS A  18     6573  10347   8813    883   1111  -1141  A    C  
ATOM     80  O   LYS A  18      56.356  -6.891 -27.216  1.00 61.61      A    O  
ANISOU   80  O   LYS A  18     5664   9678   8066    827   1195  -1081  A    O  
ATOM     81  CB  LYS A  18      53.438  -5.732 -27.728  1.00 46.88      A    C  
ANISOU   81  CB  LYS A  18     4207   7646   5958    695   1070   -906  A    C  
ATOM     82  CG  LYS A  18      52.725  -6.271 -26.501  1.00 54.66      A    C  
ANISOU   82  CG  LYS A  18     5229   8416   7124    711    909   -884  A    C  
ATOM     83  CD  LYS A  18      51.678  -5.289 -25.962  1.00 60.00      A    C  
ANISOU   83  CD  LYS A  18     6036   8998   7762    611    847   -719  A    C  
ATOM     84  CE  LYS A  18      52.321  -4.061 -25.340  1.00 54.76      A    C  
ANISOU   84  CE  LYS A  18     5358   8350   7098    487    906   -556  A    C  
ATOM     85  NZ  LYS A  18      51.301  -3.213 -24.662  1.00 58.05      A    N1+
ANISOU   85  NZ  LYS A  18     5909   8645   7501    417    835   -412  A    N1+
ATOM     86  N   TYR A  19      54.864  -8.585 -26.981  1.00 66.69      A    N  
ANISOU   86  N   TYR A  19     6465  10048   8826    988    983  -1238  A    N  
ATOM     87  CA  TYR A  19      55.681  -9.383 -26.087  1.00 58.72      A    C  
ANISOU   87  CA  TYR A  19     5332   8962   8016   1077    928  -1288  A    C  
ATOM     88  C   TYR A  19      56.268 -10.525 -26.892  1.00 62.90      A    C  
ANISOU   88  C   TYR A  19     5793   9556   8551   1257    975  -1501  A    C  
ATOM     89  O   TYR A  19      55.650 -11.024 -27.828  1.00 69.74      A    O  
ANISOU   89  O   TYR A  19     6760  10427   9313   1315    981  -1621  A    O  
ATOM     90  CB  TYR A  19      54.849  -9.909 -24.913  1.00 61.73      A    C  
ANISOU   90  CB  TYR A  19     5808   9095   8552   1071    753  -1241  A    C  
ATOM     91  CG  TYR A  19      54.247  -8.805 -24.076  1.00 62.50      A    C  
ANISOU   91  CG  TYR A  19     5977   9128   8643    910    711  -1044  A    C  
ATOM     92  CD1 TYR A  19      55.021  -8.107 -23.156  1.00 64.91      A    C  
ANISOU   92  CD1 TYR A  19     6194   9449   9021    829    721   -921  A    C  
ATOM     93  CD2 TYR A  19      52.912  -8.440 -24.222  1.00 60.76      A    C  
ANISOU   93  CD2 TYR A  19     5910   8840   8337    843    662   -986  A    C  
ATOM     94  CE1 TYR A  19      54.483  -7.081 -22.397  1.00 59.18      A    C  
ANISOU   94  CE1 TYR A  19     5551   8654   8279    688    687   -752  A    C  
ATOM     95  CE2 TYR A  19      52.358  -7.408 -23.470  1.00 54.59      A    C  
ANISOU   95  CE2 TYR A  19     5196   8001   7544    718    631   -815  A    C  
ATOM     96  CZ  TYR A  19      53.149  -6.734 -22.557  1.00 63.27      A    C  
ANISOU   96  CZ  TYR A  19     6228   9099   8714    642    647   -701  A    C  
ATOM     97  OH  TYR A  19      52.612  -5.709 -21.796  1.00 61.84      A    O  
ANISOU   97  OH  TYR A  19     6132   8848   8516    524    618   -543  A    O  
ATOM     98  N   GLU A  20      57.482 -10.920 -26.547  1.00 70.95      A    N  
ANISOU   98  N   GLU A  20     6638  10636   9683   1351   1008  -1553  A    N  
ATOM     99  CA  GLU A  20      58.135 -11.993 -27.257  1.00 69.65      A    C  
ANISOU   99  CA  GLU A  20     6397  10535   9532   1549   1059  -1762  A    C  
ATOM    100  C   GLU A  20      58.182 -13.219 -26.359  1.00 65.13      A    C  
ANISOU  100  C   GLU A  20     5836   9741   9170   1694    907  -1835  A    C  
ATOM    101  O   GLU A  20      58.767 -13.189 -25.278  1.00 62.60      A    O  
ANISOU  101  O   GLU A  20     5415   9370   9000   1696    843  -1751  A    O  
ATOM    102  CB  GLU A  20      59.527 -11.547 -27.657  1.00 79.76      A    C  
ANISOU  102  CB  GLU A  20     7453  12081  10771   1570   1225  -1780  A    C  
ATOM    103  CG  GLU A  20      60.271 -12.510 -28.543  1.00 96.78      A    C  
ANISOU  103  CG  GLU A  20     9511  14356  12906   1783   1317  -2004  A    C  
ATOM    104  CD  GLU A  20      61.737 -12.141 -28.641  1.00113.93      A    C  
ANISOU  104  CD  GLU A  20    11413  16790  15085   1811   1462  -2010  A    C  
ATOM    105  OE1 GLU A  20      62.107 -11.046 -28.148  1.00113.97      A    O  
ANISOU  105  OE1 GLU A  20    11328  16891  15083   1630   1499  -1835  A    O  
ATOM    106  OE2 GLU A  20      62.512 -12.944 -29.202  1.00119.96      A    O1-
ANISOU  106  OE2 GLU A  20    12054  17666  15859   2011   1540  -2193  A    O1-
ATOM    107  N   LYS A  21      57.532 -14.292 -26.792  1.00 62.35      A    N  
ANISOU  107  N   LYS A  21     5623   9247   8822   1805    840  -1987  A    N  
ATOM    108  CA  LYS A  21      57.463 -15.502 -25.977  1.00 70.81      A    C  
ANISOU  108  CA  LYS A  21     6751  10071  10083   1933    687  -2052  A    C  
ATOM    109  C   LYS A  21      58.836 -16.148 -25.805  1.00 78.68      A    C  
ANISOU  109  C   LYS A  21     7568  11129  11199   2139    718  -2153  A    C  
ATOM    110  O   LYS A  21      59.482 -16.522 -26.783  1.00 84.88      A    O  
ANISOU  110  O   LYS A  21     8275  12063  11914   2285    835  -2320  A    O  
ATOM    111  CB  LYS A  21      56.485 -16.506 -26.591  1.00 67.62      A    C  
ANISOU  111  CB  LYS A  21     6547   9503   9641   1991    616  -2206  A    C  
ATOM    112  CG  LYS A  21      55.047 -16.291 -26.202  1.00 57.97      A    C  
ANISOU  112  CG  LYS A  21     5502   8123   8400   1817    502  -2099  A    C  
ATOM    113  CD  LYS A  21      54.132 -17.025 -27.154  1.00 63.07      A    C  
ANISOU  113  CD  LYS A  21     6315   8700   8948   1838    470  -2258  A    C  
ATOM    114  CE  LYS A  21      52.668 -16.705 -26.861  1.00 70.46      A    C  
ANISOU  114  CE  LYS A  21     7394   9531   9847   1654    368  -2150  A    C  
ATOM    115  NZ  LYS A  21      51.782 -16.928 -28.050  1.00 73.41      A    N1+
ANISOU  115  NZ  LYS A  21     7889   9950  10054   1627    374  -2274  A    N1+
ATOM    116  N   LEU A  22      59.276 -16.284 -24.560  1.00 77.96      A    N  
ANISOU  116  N   LEU A  22     7409  10931  11282   2159    612  -2055  A    N  
ATOM    117  CA  LEU A  22      60.575 -16.887 -24.278  1.00 83.37      A    C  
ANISOU  117  CA  LEU A  22     7910  11674  12094   2367    617  -2135  A    C  
ATOM    118  C   LEU A  22      60.494 -18.370 -23.916  1.00 91.57      A    C  
ANISOU  118  C   LEU A  22     9065  12447  13281   2578    475  -2262  A    C  
ATOM    119  O   LEU A  22      61.284 -19.174 -24.405  1.00100.69      A    O  
ANISOU  119  O   LEU A  22    10140  13646  14472   2814    517  -2436  A    O  
ATOM    120  CB  LEU A  22      61.278 -16.133 -23.153  1.00 82.46      A    C  
ANISOU  120  CB  LEU A  22     7627  11630  12073   2277    582  -1955  A    C  
ATOM    121  CG  LEU A  22      61.674 -14.699 -23.464  1.00 81.60      A    C  
ANISOU  121  CG  LEU A  22     7375  11794  11837   2087    730  -1840  A    C  
ATOM    122  CD1 LEU A  22      62.369 -14.080 -22.267  1.00 82.18      A    C  
ANISOU  122  CD1 LEU A  22     7300  11909  12017   1998    669  -1677  A    C  
ATOM    123  CD2 LEU A  22      62.567 -14.686 -24.679  1.00 83.29      A    C  
ANISOU  123  CD2 LEU A  22     7417  12285  11945   2194    918  -1986  A    C  
ATOM    124  N   ALA A  23      59.541 -18.730 -23.059  1.00 93.20      A    N  
ANISOU  124  N   ALA A  23     9467  12377  13569   2493    311  -2174  A    N  
ATOM    125  CA  ALA A  23      59.498 -20.074 -22.493  1.00 89.95      A    C  
ANISOU  125  CA  ALA A  23     9182  11684  13312   2663    157  -2252  A    C  
ATOM    126  C   ALA A  23      58.184 -20.371 -21.770  1.00 96.69      A    C  
ANISOU  126  C   ALA A  23    10281  12251  14205   2507      4  -2155  A    C  
ATOM    127  O   ALA A  23      57.735 -19.574 -20.946  1.00 99.47      A    O  
ANISOU  127  O   ALA A  23    10638  12595  14560   2312    -38  -1964  A    O  
ATOM    128  CB  ALA A  23      60.670 -20.255 -21.533  1.00 80.63      A    C  
ANISOU  128  CB  ALA A  23     7828  10520  12289   2806     94  -2196  A    C  
ATOM    129  N   LYS A  24      57.576 -21.519 -22.070  1.00 98.45      A    N  
ANISOU  129  N   LYS A  24    10709  12242  14455   2587    -75  -2290  A    N  
ATOM    130  CA  LYS A  24      56.436 -22.001 -21.293  1.00 95.64      A    C  
ANISOU  130  CA  LYS A  24    10580  11600  14160   2452   -230  -2207  A    C  
ATOM    131  C   LYS A  24      56.870 -22.193 -19.852  1.00 94.42      A    C  
ANISOU  131  C   LYS A  24    10407  11303  14166   2479   -360  -2059  A    C  
ATOM    132  O   LYS A  24      57.993 -22.609 -19.592  1.00 97.58      A    O  
ANISOU  132  O   LYS A  24    10694  11716  14665   2688   -378  -2100  A    O  
ATOM    133  CB  LYS A  24      55.917 -23.338 -21.825  1.00 99.58      A    C  
ANISOU  133  CB  LYS A  24    11299  11857  14679   2551   -301  -2393  A    C  
ATOM    134  CG  LYS A  24      55.051 -23.249 -23.070  1.00109.15      A    C  
ANISOU  134  CG  LYS A  24    12604  13143  15725   2458   -225  -2518  A    C  
ATOM    135  CD  LYS A  24      54.505 -24.626 -23.453  1.00116.78      A    C  
ANISOU  135  CD  LYS A  24    13813  13836  16723   2530   -320  -2697  A    C  
ATOM    136  CE  LYS A  24      54.158 -24.711 -24.941  1.00117.14      A    C  
ANISOU  136  CE  LYS A  24    13907  14001  16599   2542   -223  -2896  A    C  
ATOM    137  NZ  LYS A  24      53.607 -26.044 -25.335  1.00113.63      A    N1+
ANISOU  137  NZ  LYS A  24    13715  13283  16177   2595   -321  -3082  A    N1+
ATOM    138  N   ILE A  25      55.981 -21.883 -18.918  1.00 95.62      A    N  
ANISOU  138  N   ILE A  25    10665  11330  14335   2272   -450  -1887  A    N  
ATOM    139  CA  ILE A  25      56.249 -22.126 -17.508  1.00 99.21      A    C  
ANISOU  139  CA  ILE A  25    11144  11626  14924   2277   -586  -1740  A    C  
ATOM    140  C   ILE A  25      55.007 -22.699 -16.841  1.00109.45      A    C  
ANISOU  140  C   ILE A  25    12688  12646  16252   2121   -713  -1668  A    C  
ATOM    141  O   ILE A  25      54.803 -22.539 -15.635  1.00104.23      A    O  
ANISOU  141  O   ILE A  25    12069  11886  15649   2017   -806  -1497  A    O  
ATOM    142  CB  ILE A  25      56.725 -20.854 -16.778  1.00 87.85      A    C  
ANISOU  142  CB  ILE A  25     9521  10387  13470   2164   -549  -1559  A    C  
ATOM    143  CG1 ILE A  25      55.640 -19.778 -16.799  1.00 82.93      A    C  
ANISOU  143  CG1 ILE A  25     8938   9847  12726   1899   -492  -1443  A    C  
ATOM    144  CG2 ILE A  25      58.002 -20.331 -17.412  1.00 85.66      A    C  
ANISOU  144  CG2 ILE A  25     8989  10391  13167   2299   -423  -1628  A    C  
ATOM    145  CD1 ILE A  25      56.097 -18.435 -16.252  1.00 77.11      A    C  
ANISOU  145  CD1 ILE A  25     8038   9310  11952   1783   -436  -1286  A    C  
ATOM    146  N   GLY A  26      54.183 -23.368 -17.646  1.00118.30      A    N  
ANISOU  146  N   GLY A  26    13970  13653  17327   2096   -714  -1803  A    N  
ATOM    147  CA  GLY A  26      52.993 -24.040 -17.157  1.00120.13      A    C  
ANISOU  147  CA  GLY A  26    14435  13624  17584   1942   -829  -1761  A    C  
ATOM    148  C   GLY A  26      51.834 -24.070 -18.142  1.00121.06      A    C  
ANISOU  148  C   GLY A  26    14652  13761  17584   1800   -785  -1861  A    C  
ATOM    149  O   GLY A  26      51.979 -23.717 -19.317  1.00111.77      A    O  
ANISOU  149  O   GLY A  26    13392  12775  16302   1851   -672  -1987  A    O  
ATOM    150  N   GLN A  27      50.681 -24.520 -17.652  1.00129.16      A    N  
ANISOU  150  N   GLN A  27    15857  14594  18624   1616   -880  -1802  A    N  
ATOM    151  CA  GLN A  27      49.425 -24.470 -18.399  1.00128.92      A    C  
ANISOU  151  CA  GLN A  27    15905  14594  18483   1437   -860  -1864  A    C  
ATOM    152  C   GLN A  27      48.252 -24.223 -17.457  1.00125.74      A    C  
ANISOU  152  C   GLN A  27    15574  14120  18082   1182   -923  -1692  A    C  
ATOM    153  O   GLN A  27      47.798 -25.140 -16.765  1.00127.76      A    O  
ANISOU  153  O   GLN A  27    16003  14119  18419   1109  -1037  -1661  A    O  
ATOM    154  CB  GLN A  27      49.180 -25.757 -19.188  1.00126.18      A    C  
ANISOU  154  CB  GLN A  27    15745  14050  18148   1503   -916  -2073  A    C  
ATOM    155  CG  GLN A  27      47.735 -25.889 -19.646  1.00125.53      A    C  
ANISOU  155  CG  GLN A  27    15773  13945  17976   1272   -944  -2109  A    C  
ATOM    156  CD  GLN A  27      47.615 -26.422 -21.054  1.00133.20      A    C  
ANISOU  156  CD  GLN A  27    16813  14937  18859   1340   -914  -2347  A    C  
ATOM    157  NE2 GLN A  27      46.556 -26.019 -21.748  1.00127.11      A    N  
ANISOU  157  NE2 GLN A  27    16035  14303  17958   1166   -891  -2377  A    N  
ATOM    158  OE1 GLN A  27      48.465 -27.187 -21.518  1.00143.06      A    O  
ANISOU  158  OE1 GLN A  27    18120  16086  20150   1557   -914  -2507  A    O  
ATOM    159  N   GLY A  28      47.765 -22.985 -17.447  1.00116.33      A    N  
ANISOU  159  N   GLY A  28    14252  13155  16793   1051   -844  -1582  A    N  
ATOM    160  CA  GLY A  28      46.701 -22.570 -16.549  1.00116.04      A    C  
ANISOU  160  CA  GLY A  28    14246  13101  16745    828   -880  -1416  A    C  
ATOM    161  C   GLY A  28      45.326 -23.166 -16.815  1.00117.75      A    C  
ANISOU  161  C   GLY A  28    14592  13224  16924    643   -937  -1464  A    C  
ATOM    162  O   GLY A  28      45.189 -24.173 -17.518  1.00122.46      A    O  
ANISOU  162  O   GLY A  28    15310  13689  17532    674   -984  -1626  A    O  
ATOM    163  N   THR A  29      44.304 -22.528 -16.248  1.00112.67      A    N  
ANISOU  163  N   THR A  29    13917  12658  16235    446   -931  -1328  A    N  
ATOM    164  CA  THR A  29      42.931 -23.032 -16.300  1.00111.22      A    C  
ANISOU  164  CA  THR A  29    13827  12409  16022    239   -988  -1345  A    C  
ATOM    165  C   THR A  29      42.299 -22.936 -17.689  1.00108.03      A    C  
ANISOU  165  C   THR A  29    13390  12155  15500    212   -956  -1496  A    C  
ATOM    166  O   THR A  29      41.432 -23.737 -18.040  1.00105.12      A    O  
ANISOU  166  O   THR A  29    13126  11692  15121     84  -1024  -1584  A    O  
ATOM    167  CB  THR A  29      42.019 -22.298 -15.287  1.00103.98      A    C  
ANISOU  167  CB  THR A  29    12858  11569  15082     51   -978  -1156  A    C  
ATOM    168  CG2 THR A  29      40.619 -22.914 -15.268  1.00 98.19      A    C  
ANISOU  168  CG2 THR A  29    12205  10775  14328   -176  -1038  -1171  A    C  
ATOM    169  OG1 THR A  29      42.590 -22.384 -13.977  1.00107.58      A    O  
ANISOU  169  OG1 THR A  29    13357  11890  15630     67  -1012  -1014  A    O  
ATOM    170  N   PHE A  30      42.740 -21.962 -18.479  1.00104.42      A    N  
ANISOU  170  N   PHE A  30    12795  11930  14948    323   -857  -1524  A    N  
ATOM    171  CA  PHE A  30      42.092 -21.666 -19.750  1.00 98.79      A    C  
ANISOU  171  CA  PHE A  30    12039  11397  14098    293   -824  -1637  A    C  
ATOM    172  C   PHE A  30      43.038 -21.767 -20.932  1.00 97.86      A    C  
ANISOU  172  C   PHE A  30    11908  11350  13926    485   -765  -1803  A    C  
ATOM    173  O   PHE A  30      42.661 -21.404 -22.047  1.00101.93      A    O  
ANISOU  173  O   PHE A  30    12384  12040  14307    483   -725  -1892  A    O  
ATOM    174  CB  PHE A  30      41.490 -20.260 -19.705  1.00 99.05      A    C  
ANISOU  174  CB  PHE A  30    11928  11680  14027    223   -753  -1504  A    C  
ATOM    175  CG  PHE A  30      40.480 -20.072 -18.609  1.00100.12      A    C  
ANISOU  175  CG  PHE A  30    12059  11787  14196     42   -793  -1352  A    C  
ATOM    176  CD1 PHE A  30      39.208 -20.632 -18.719  1.00 92.42      A    C  
ANISOU  176  CD1 PHE A  30    11127  10789  13199   -137   -864  -1389  A    C  
ATOM    177  CD2 PHE A  30      40.801 -19.350 -17.464  1.00 96.37      A    C  
ANISOU  177  CD2 PHE A  30    11533  11317  13768     42   -758  -1178  A    C  
ATOM    178  CE1 PHE A  30      38.282 -20.471 -17.715  1.00 93.16      A    C  
ANISOU  178  CE1 PHE A  30    11200  10879  13318   -305   -887  -1252  A    C  
ATOM    179  CE2 PHE A  30      39.875 -19.185 -16.452  1.00 92.72      A    C  
ANISOU  179  CE2 PHE A  30    11068  10839  13324   -119   -783  -1045  A    C  
ATOM    180  CZ  PHE A  30      38.612 -19.745 -16.579  1.00 93.25      A    C  
ANISOU  180  CZ  PHE A  30    11165  10896  13369   -290   -842  -1081  A    C  
ATOM    181  N   GLY A  31      44.256 -22.255 -20.680  1.00 92.43      A    N  
ANISOU  181  N   GLY A  31    11247  10537  13336    654   -759  -1841  A    N  
ATOM    182  CA  GLY A  31      45.327 -22.262 -21.667  1.00 98.32      A    C  
ANISOU  182  CA  GLY A  31    11947  11373  14037    858   -680  -1983  A    C  
ATOM    183  C   GLY A  31      46.726 -22.256 -21.049  1.00110.46      A    C  
ANISOU  183  C   GLY A  31    13423  12863  15684   1036   -650  -1939  A    C  
ATOM    184  O   GLY A  31      46.879 -22.459 -19.844  1.00122.00      A    O  
ANISOU  184  O   GLY A  31    14914  14176  17266   1010   -714  -1814  A    O  
ATOM    185  N   GLU A  32      47.749 -22.010 -21.868  1.00 99.83      A    N  
ANISOU  185  N   GLU A  32    11982  11660  14287   1214   -551  -2040  A    N  
ATOM    186  CA  GLU A  32      49.137 -22.111 -21.423  1.00 91.49      A    C  
ANISOU  186  CA  GLU A  32    10846  10583  13333   1402   -524  -2029  A    C  
ATOM    187  C   GLU A  32      49.708 -20.844 -20.769  1.00 82.56      A    C  
ANISOU  187  C   GLU A  32     9540   9629  12200   1381   -453  -1846  A    C  
ATOM    188  O   GLU A  32      49.203 -19.742 -20.971  1.00 83.07      A    O  
ANISOU  188  O   GLU A  32     9534   9875  12155   1260   -387  -1755  A    O  
ATOM    189  CB  GLU A  32      50.027 -22.550 -22.584  1.00101.75      A    C  
ANISOU  189  CB  GLU A  32    12117  11956  14587   1610   -447  -2238  A    C  
ATOM    190  CG  GLU A  32      49.753 -23.971 -23.049  1.00110.67      A    C  
ANISOU  190  CG  GLU A  32    13443  12854  15753   1676   -532  -2433  A    C  
ATOM    191  CD  GLU A  32      50.916 -24.575 -23.818  1.00114.80      A    C  
ANISOU  191  CD  GLU A  32    13942  13394  16284   1941   -469  -2630  A    C  
ATOM    192  OE1 GLU A  32      51.218 -24.083 -24.927  1.00114.27      A    O  
ANISOU  192  OE1 GLU A  32    13780  13560  16076   2001   -343  -2732  A    O  
ATOM    193  OE2 GLU A  32      51.518 -25.551 -23.316  1.00114.49      A    O1-
ANISOU  193  OE2 GLU A  32    13983  13134  16384   2095   -545  -2683  A    O1-
ATOM    194  N   VAL A  33      50.764 -21.019 -19.979  1.00 74.59      A    N  
ANISOU  194  N   VAL A  33     8471   8559  11312   1502   -475  -1795  A    N  
ATOM    195  CA  VAL A  33      51.442 -19.904 -19.327  1.00 77.98      A    C  
ANISOU  195  CA  VAL A  33     8737   9144  11748   1484   -418  -1637  A    C  
ATOM    196  C   VAL A  33      52.863 -19.718 -19.871  1.00 82.68      A    C  
ANISOU  196  C   VAL A  33     9165   9908  12343   1673   -320  -1718  A    C  
ATOM    197  O   VAL A  33      53.664 -20.653 -19.848  1.00 87.21      A    O  
ANISOU  197  O   VAL A  33     9741  10382  13014   1861   -359  -1822  A    O  
ATOM    198  CB  VAL A  33      51.521 -20.114 -17.808  1.00 74.74      A    C  
ANISOU  198  CB  VAL A  33     8369   8560  11470   1442   -532  -1483  A    C  
ATOM    199  CG1 VAL A  33      51.943 -18.822 -17.115  1.00 69.05      A    C  
ANISOU  199  CG1 VAL A  33     7504   8003  10728   1367   -480  -1310  A    C  
ATOM    200  CG2 VAL A  33      50.188 -20.579 -17.283  1.00 75.87      A    C  
ANISOU  200  CG2 VAL A  33     8686   8515  11626   1273   -630  -1428  A    C  
ATOM    201  N   PHE A  34      53.170 -18.507 -20.343  1.00 75.25      A    N  
ANISOU  201  N   PHE A  34     8079   9222  11290   1624   -193  -1666  A    N  
ATOM    202  CA  PHE A  34      54.476 -18.194 -20.935  1.00 67.52      A    C  
ANISOU  202  CA  PHE A  34     6919   8449  10288   1766    -76  -1735  A    C  
ATOM    203  C   PHE A  34      55.237 -17.108 -20.189  1.00 67.86      A    C  
ANISOU  203  C   PHE A  34     6798   8636  10351   1706    -35  -1572  A    C  
ATOM    204  O   PHE A  34      54.647 -16.117 -19.745  1.00 66.15      A    O  
ANISOU  204  O   PHE A  34     6597   8458  10080   1526    -28  -1418  A    O  
ATOM    205  CB  PHE A  34      54.300 -17.693 -22.364  1.00 66.88      A    C  
ANISOU  205  CB  PHE A  34     6809   8575  10028   1752     63  -1834  A    C  
ATOM    206  CG  PHE A  34      53.734 -18.704 -23.296  1.00 78.75      A    C  
ANISOU  206  CG  PHE A  34     8453   9983  11486   1824     42  -2025  A    C  
ATOM    207  CD1 PHE A  34      54.559 -19.641 -23.903  1.00 86.35      A    C  
ANISOU  207  CD1 PHE A  34     9395  10933  12481   2040     70  -2217  A    C  
ATOM    208  CD2 PHE A  34      52.380 -18.718 -23.579  1.00 78.31      A    C  
ANISOU  208  CD2 PHE A  34     8546   9859  11350   1679     -8  -2021  A    C  
ATOM    209  CE1 PHE A  34      54.042 -20.578 -24.771  1.00 87.51      A    C  
ANISOU  209  CE1 PHE A  34     9692  10981  12578   2102     48  -2406  A    C  
ATOM    210  CE2 PHE A  34      51.854 -19.652 -24.447  1.00 88.89      A    C  
ANISOU  210  CE2 PHE A  34    10019  11114  12641   1727    -37  -2205  A    C  
ATOM    211  CZ  PHE A  34      52.689 -20.587 -25.044  1.00 90.51      A    C  
ANISOU  211  CZ  PHE A  34    10226  11288  12875   1936     -9  -2400  A    C  
ATOM    212  N   LYS A  35      56.552 -17.276 -20.077  1.00 68.92      A    N  
ANISOU  212  N   LYS A  35     6771   8859  10559   1857     -7  -1611  A    N  
ATOM    213  CA  LYS A  35      57.411 -16.158 -19.715  1.00 65.96      A    C  
ANISOU  213  CA  LYS A  35     6208   8687  10169   1792     65  -1491  A    C  
ATOM    214  C   LYS A  35      57.714 -15.400 -21.001  1.00 67.86      A    C  
ANISOU  214  C   LYS A  35     6344   9189  10249   1771    245  -1555  A    C  
ATOM    215  O   LYS A  35      57.975 -16.012 -22.036  1.00 72.85      A    O  
ANISOU  215  O   LYS A  35     6961   9882  10836   1912    314  -1728  A    O  
ATOM    216  CB  LYS A  35      58.708 -16.628 -19.069  1.00 67.73      A    C  
ANISOU  216  CB  LYS A  35     6275   8927  10533   1956     16  -1504  A    C  
ATOM    217  CG  LYS A  35      59.594 -15.471 -18.613  1.00 69.20      A    C  
ANISOU  217  CG  LYS A  35     6260   9325  10707   1859     75  -1376  A    C  
ATOM    218  CD  LYS A  35      60.952 -15.943 -18.138  1.00 72.59      A    C  
ANISOU  218  CD  LYS A  35     6494   9822  11264   2037     33  -1409  A    C  
ATOM    219  CE  LYS A  35      61.773 -14.777 -17.594  1.00 82.49      A    C  
ANISOU  219  CE  LYS A  35     7553  11283  12507   1904     74  -1274  A    C  
ATOM    220  NZ  LYS A  35      63.114 -15.192 -17.073  1.00 84.89      A    N1+
ANISOU  220  NZ  LYS A  35     7637  11681  12936   2069     19  -1298  A    N1+
ATOM    221  N   ALA A  36      57.658 -14.074 -20.956  1.00 57.10      A    N  
ANISOU  221  N   ALA A  36     4931   7974   8792   1594    322  -1418  A    N  
ATOM    222  CA  ALA A  36      57.924 -13.302 -22.162  1.00 59.33      A    C  
ANISOU  222  CA  ALA A  36     5136   8498   8908   1554    493  -1457  A    C  
ATOM    223  C   ALA A  36      58.585 -11.959 -21.908  1.00 62.36      A    C  
ANISOU  223  C   ALA A  36     5386   9068   9241   1406    581  -1313  A    C  
ATOM    224  O   ALA A  36      58.715 -11.497 -20.769  1.00 59.24      A    O  
ANISOU  224  O   ALA A  36     4970   8611   8926   1312    504  -1173  A    O  
ATOM    225  CB  ALA A  36      56.657 -13.126 -22.992  1.00 56.87      A    C  
ANISOU  225  CB  ALA A  36     5000   8157   8452   1473    516  -1480  A    C  
ATOM    226  N   ARG A  37      58.973 -11.330 -23.007  1.00 66.49      A    N  
ANISOU  226  N   ARG A  37     5832   9815   9615   1375    743  -1349  A    N  
ATOM    227  CA  ARG A  37      59.831 -10.163 -22.982  1.00 65.31      A    C  
ANISOU  227  CA  ARG A  37     5534   9873   9409   1244    853  -1243  A    C  
ATOM    228  C   ARG A  37      59.205  -9.082 -23.834  1.00 63.33      A    C  
ANISOU  228  C   ARG A  37     5388   9716   8958   1088    963  -1173  A    C  
ATOM    229  O   ARG A  37      58.906  -9.307 -25.007  1.00 60.50      A    O  
ANISOU  229  O   ARG A  37     5081   9435   8472   1144   1046  -1279  A    O  
ATOM    230  CB  ARG A  37      61.195 -10.548 -23.563  1.00 63.26      A    C  
ANISOU  230  CB  ARG A  37     5039   9833   9162   1380    965  -1370  A    C  
ATOM    231  CG  ARG A  37      62.213  -9.447 -23.575  1.00 60.01      A    C  
ANISOU  231  CG  ARG A  37     4440   9662   8698   1238   1086  -1276  A    C  
ATOM    232  CD  ARG A  37      63.483  -9.891 -24.297  1.00 56.73      A    C  
ANISOU  232  CD  ARG A  37     3778   9497   8280   1383   1216  -1420  A    C  
ATOM    233  NE  ARG A  37      64.456  -8.811 -24.288  1.00 67.41      A    N  
ANISOU  233  NE  ARG A  37     4938  11093   9580   1214   1334  -1322  A    N  
ATOM    234  CZ  ARG A  37      64.464  -7.808 -25.157  1.00 68.35      A    C  
ANISOU  234  CZ  ARG A  37     5076  11382   9514   1045   1495  -1267  A    C  
ATOM    235  NH1 ARG A  37      63.559  -7.763 -26.129  1.00 59.96      A    N1+
ANISOU  235  NH1 ARG A  37     4205  10282   8294   1042   1554  -1305  A    N1+
ATOM    236  NH2 ARG A  37      65.389  -6.862 -25.060  1.00 74.43      A    N  
ANISOU  236  NH2 ARG A  37     5672  12359  10248    873   1594  -1174  A    N  
ATOM    237  N   HIS A  38      58.993  -7.913 -23.247  1.00 58.50      A    N  
ANISOU  237  N   HIS A  38     4824   9090   8313    897    957   -997  A    N  
ATOM    238  CA  HIS A  38      58.520  -6.786 -24.021  1.00 57.48      A    C  
ANISOU  238  CA  HIS A  38     4796   9049   7993    753   1062   -913  A    C  
ATOM    239  C   HIS A  38      59.540  -6.475 -25.110  1.00 64.55      A    C  
ANISOU  239  C   HIS A  38     5545  10211   8768    747   1245   -972  A    C  
ATOM    240  O   HIS A  38      60.733  -6.377 -24.826  1.00 66.91      A    O  
ANISOU  240  O   HIS A  38     5643  10647   9132    735   1297   -972  A    O  
ATOM    241  CB  HIS A  38      58.313  -5.573 -23.127  1.00 61.91      A    C  
ANISOU  241  CB  HIS A  38     5427   9544   8552    560   1028   -719  A    C  
ATOM    242  CG  HIS A  38      57.665  -4.432 -23.835  1.00 68.71      A    C  
ANISOU  242  CG  HIS A  38     6436  10445   9224    429   1110   -620  A    C  
ATOM    243  CD2 HIS A  38      56.409  -3.930 -23.759  1.00 55.77      A    C  
ANISOU  243  CD2 HIS A  38     5000   8675   7517    378   1053   -535  A    C  
ATOM    244  ND1 HIS A  38      58.321  -3.688 -24.794  1.00 77.72      A    N  
ANISOU  244  ND1 HIS A  38     7525  11790  10214    346   1272   -602  A    N  
ATOM    245  CE1 HIS A  38      57.499  -2.767 -25.266  1.00 77.58      A    C  
ANISOU  245  CE1 HIS A  38     7690  11746  10041    250   1302   -502  A    C  
ATOM    246  NE2 HIS A  38      56.333  -2.893 -24.654  1.00 61.03      A    N  
ANISOU  246  NE2 HIS A  38     5742   9451   7995    278   1169   -464  A    N  
ATOM    247  N   ARG A  39      59.086  -6.319 -26.352  1.00 62.30      A    N  
ANISOU  247  N   ARG A  39     5352  10017   8303    753   1342  -1021  A    N  
ATOM    248  CA  ARG A  39      60.023  -6.226 -27.469  1.00 56.86      A    C  
ANISOU  248  CA  ARG A  39     4526   9589   7488    771   1524  -1104  A    C  
ATOM    249  C   ARG A  39      60.839  -4.936 -27.502  1.00 64.42      A    C  
ANISOU  249  C   ARG A  39     5397  10719   8361    568   1652   -963  A    C  
ATOM    250  O   ARG A  39      61.858  -4.864 -28.197  1.00 63.22      A    O  
ANISOU  250  O   ARG A  39     5075  10807   8137    565   1807  -1022  A    O  
ATOM    251  CB  ARG A  39      59.332  -6.463 -28.811  1.00 63.98      A    C  
ANISOU  251  CB  ARG A  39     5559  10546   8203    834   1590  -1202  A    C  
ATOM    252  CG  ARG A  39      58.978  -7.930 -29.060  1.00 82.79      A    C  
ANISOU  252  CG  ARG A  39     7965  12834  10657   1051   1513  -1403  A    C  
ATOM    253  CD  ARG A  39      58.545  -8.208 -30.513  1.00 87.87      A    C  
ANISOU  253  CD  ARG A  39     8706  13584  11096   1116   1600  -1531  A    C  
ATOM    254  NE  ARG A  39      57.662  -9.375 -30.604  1.00 86.40      A    N  
ANISOU  254  NE  ARG A  39     8643  13222  10962   1258   1471  -1674  A    N  
ATOM    255  CZ  ARG A  39      58.058 -10.612 -30.906  1.00 92.85      A    C  
ANISOU  255  CZ  ARG A  39     9404  14031  11843   1449   1469  -1880  A    C  
ATOM    256  NH1 ARG A  39      59.338 -10.867 -31.171  1.00 88.28      A    N1+
ANISOU  256  NH1 ARG A  39     8627  13630  11284   1548   1596  -1975  A    N1+
ATOM    257  NH2 ARG A  39      57.167 -11.600 -30.946  1.00 90.56      A    N  
ANISOU  257  NH2 ARG A  39     9257  13555  11597   1543   1341  -1995  A    N  
ATOM    258  N   LYS A  40      60.412  -3.927 -26.744  1.00 66.18      A    N  
ANISOU  258  N   LYS A  40     5735  10822   8590    395   1590   -783  A    N  
ATOM    259  CA  LYS A  40      61.090  -2.627 -26.774  1.00 57.70      A    C  
ANISOU  259  CA  LYS A  40     4622   9877   7424    174   1703   -639  A    C  
ATOM    260  C   LYS A  40      61.938  -2.345 -25.540  1.00 57.24      A    C  
ANISOU  260  C   LYS A  40     4415   9809   7526     78   1646   -564  A    C  
ATOM    261  O   LYS A  40      62.994  -1.728 -25.637  1.00 62.91      A    O  
ANISOU  261  O   LYS A  40     4979  10713   8211    -59   1757   -520  A    O  
ATOM    262  CB  LYS A  40      60.084  -1.500 -26.967  1.00 60.25      A    C  
ANISOU  262  CB  LYS A  40     5204  10090   7599     30   1697   -484  A    C  
ATOM    263  CG  LYS A  40      59.543  -1.369 -28.383  1.00 60.52      A    C  
ANISOU  263  CG  LYS A  40     5366  10217   7414     58   1797   -518  A    C  
ATOM    264  CD  LYS A  40      58.246  -0.557 -28.374  1.00 62.25      A    C  
ANISOU  264  CD  LYS A  40     5856  10264   7531     -6   1724   -384  A    C  
ATOM    265  CE  LYS A  40      57.819  -0.187 -29.779  1.00 70.53      A    C  
ANISOU  265  CE  LYS A  40     7037  11424   8335    -11   1826   -381  A    C  
ATOM    266  NZ  LYS A  40      58.930   0.462 -30.535  1.00 77.24      A    N1+
ANISOU  266  NZ  LYS A  40     7799  12503   9044   -147   2019   -344  A    N1+
ATOM    267  N   THR A  41      61.473  -2.806 -24.387  1.00 56.83      A    N  
ANISOU  267  N   THR A  41     4407   9548   7640    141   1472   -551  A    N  
ATOM    268  CA  THR A  41      62.071  -2.457 -23.103  1.00 59.34      A    C  
ANISOU  268  CA  THR A  41     4634   9819   8094     38   1388   -461  A    C  
ATOM    269  C   THR A  41      62.729  -3.653 -22.429  1.00 64.95      A    C  
ANISOU  269  C   THR A  41     5147  10533   8998    213   1292   -573  A    C  
ATOM    270  O   THR A  41      63.546  -3.485 -21.525  1.00 67.06      A    O  
ANISOU  270  O   THR A  41     5268  10838   9372    148   1240   -526  A    O  
ATOM    271  CB  THR A  41      60.988  -1.978 -22.134  1.00 58.16      A    C  
ANISOU  271  CB  THR A  41     4711   9410   7977    -34   1249   -339  A    C  
ATOM    272  CG2 THR A  41      60.062  -0.959 -22.822  1.00 42.40      A    C  
ANISOU  272  CG2 THR A  41     2950   7365   5795   -144   1314   -241  A    C  
ATOM    273  OG1 THR A  41      60.232  -3.116 -21.691  1.00 54.30      A    O  
ANISOU  273  OG1 THR A  41     4278   8750   7604    150   1112   -420  A    O  
ATOM    274  N   GLY A  42      62.345  -4.857 -22.847  1.00 63.28      A    N  
ANISOU  274  N   GLY A  42     4946  10270   8828    436   1258   -719  A    N  
ATOM    275  CA  GLY A  42      62.902  -6.077 -22.296  1.00 55.56      A    C  
ANISOU  275  CA  GLY A  42     3814   9268   8027    633   1163   -832  A    C  
ATOM    276  C   GLY A  42      62.192  -6.507 -21.028  1.00 58.04      A    C  
ANISOU  276  C   GLY A  42     4256   9314   8482    667    964   -777  A    C  
ATOM    277  O   GLY A  42      62.521  -7.542 -20.445  1.00 58.07      A    O  
ANISOU  277  O   GLY A  42     4178   9250   8637    830    858   -851  A    O  
ATOM    278  N   GLN A  43      61.209  -5.721 -20.597  1.00 59.41      A    N  
ANISOU  278  N   GLN A  43     4638   9335   8602    518    916   -646  A    N  
ATOM    279  CA  GLN A  43      60.478  -6.032 -19.366  1.00 63.14      A    C  
ANISOU  279  CA  GLN A  43     5238   9565   9187    527    742   -583  A    C  
ATOM    280  C   GLN A  43      59.894  -7.432 -19.426  1.00 64.88      A    C  
ANISOU  280  C   GLN A  43     5519   9641   9492    731    651   -706  A    C  
ATOM    281  O   GLN A  43      59.164  -7.754 -20.363  1.00 62.02      A    O  
ANISOU  281  O   GLN A  43     5258   9262   9045    792    696   -784  A    O  
ATOM    282  CB  GLN A  43      59.368  -5.013 -19.120  1.00 58.21      A    C  
ANISOU  282  CB  GLN A  43     4838   8814   8467    366    729   -448  A    C  
ATOM    283  CG  GLN A  43      58.425  -5.379 -17.985  1.00 67.60      A    C  
ANISOU  283  CG  GLN A  43     6173   9763   9747    381    570   -395  A    C  
ATOM    284  CD  GLN A  43      57.065  -4.707 -18.125  1.00 79.33      A    C  
ANISOU  284  CD  GLN A  43     7881  11137  11125    301    573   -319  A    C  
ATOM    285  NE2 GLN A  43      56.366  -4.546 -17.008  1.00 80.63      A    N  
ANISOU  285  NE2 GLN A  43     8165  11132  11340    249    466   -231  A    N  
ATOM    286  OE1 GLN A  43      56.647  -4.344 -19.230  1.00 82.30      A    O  
ANISOU  286  OE1 GLN A  43     8317  11587  11367    295    670   -339  A    O  
ATOM    287  N   LYS A  44      60.230  -8.266 -18.442  1.00 67.15      A    N  
ANISOU  287  N   LYS A  44     5751   9822   9940    831    517   -722  A    N  
ATOM    288  CA  LYS A  44      59.729  -9.639 -18.402  1.00 62.06      A    C  
ANISOU  288  CA  LYS A  44     5182   9011   9387   1016    418   -832  A    C  
ATOM    289  C   LYS A  44      58.324  -9.682 -17.814  1.00 67.84      A    C  
ANISOU  289  C   LYS A  44     6146   9513  10118    946    316   -758  A    C  
ATOM    290  O   LYS A  44      58.030  -9.004 -16.828  1.00 71.23      A    O  
ANISOU  290  O   LYS A  44     6640   9865  10558    812    255   -620  A    O  
ATOM    291  CB  LYS A  44      60.642 -10.538 -17.578  1.00 58.94      A    C  
ANISOU  291  CB  LYS A  44     4655   8581   9160   1160    308   -869  A    C  
ATOM    292  CG  LYS A  44      62.105 -10.572 -18.022  1.00 60.60      A    C  
ANISOU  292  CG  LYS A  44     4595   9038   9393   1250    397   -946  A    C  
ATOM    293  CD  LYS A  44      62.259 -11.006 -19.462  1.00 63.52      A    C  
ANISOU  293  CD  LYS A  44     4914   9539   9681   1378    537  -1109  A    C  
ATOM    294  CE  LYS A  44      63.729 -10.981 -19.873  1.00 67.03      A    C  
ANISOU  294  CE  LYS A  44     5068  10259  10142   1461    641  -1183  A    C  
ATOM    295  NZ  LYS A  44      64.408  -9.713 -19.484  1.00 63.66      A    N1+
ANISOU  295  NZ  LYS A  44     4502  10009   9675   1245    696  -1046  A    N1+
ATOM    296  N   VAL A  45      57.462 -10.486 -18.427  1.00 65.74      A    N  
ANISOU  296  N   VAL A  45     6001   9146   9833   1035    299   -857  A    N  
ATOM    297  CA  VAL A  45      56.073 -10.607 -18.003  1.00 62.79      A    C  
ANISOU  297  CA  VAL A  45     5827   8581   9451    969    212   -803  A    C  
ATOM    298  C   VAL A  45      55.630 -12.071 -18.088  1.00 66.60      A    C  
ANISOU  298  C   VAL A  45     6390   8898  10018   1111    120   -927  A    C  
ATOM    299  O   VAL A  45      56.318 -12.899 -18.682  1.00 62.33      A    O  
ANISOU  299  O   VAL A  45     5771   8396   9517   1271    141  -1067  A    O  
ATOM    300  CB  VAL A  45      55.143  -9.764 -18.903  1.00 63.21      A    C  
ANISOU  300  CB  VAL A  45     5978   8702   9337    869    304   -779  A    C  
ATOM    301  CG1 VAL A  45      55.593  -8.298 -18.931  1.00 60.37      A    C  
ANISOU  301  CG1 VAL A  45     5567   8489   8881    727    402   -659  A    C  
ATOM    302  CG2 VAL A  45      55.098 -10.344 -20.317  1.00 60.38      A    C  
ANISOU  302  CG2 VAL A  45     5612   8432   8897    978    381   -940  A    C  
ATOM    303  N   ALA A  46      54.483 -12.391 -17.494  1.00 66.68      A    N  
ANISOU  303  N   ALA A  46     6560   8722  10054   1051     21   -879  A    N  
ATOM    304  CA  ALA A  46      53.877 -13.709 -17.670  1.00 61.16      A    C  
ANISOU  304  CA  ALA A  46     5971   7854   9413   1143    -62   -991  A    C  
ATOM    305  C   ALA A  46      52.604 -13.567 -18.484  1.00 61.21      A    C  
ANISOU  305  C   ALA A  46     6093   7863   9300   1069    -32  -1025  A    C  
ATOM    306  O   ALA A  46      51.763 -12.714 -18.192  1.00 61.10      A    O  
ANISOU  306  O   ALA A  46     6137   7859   9218    931    -26   -910  A    O  
ATOM    307  CB  ALA A  46      53.576 -14.364 -16.328  1.00 56.04      A    C  
ANISOU  307  CB  ALA A  46     5413   6986   8892   1125   -210   -914  A    C  
ATOM    308  N   LEU A  47      52.475 -14.400 -19.511  1.00 63.90      A    N  
ANISOU  308  N   LEU A  47     6466   8200   9612   1169    -15  -1189  A    N  
ATOM    309  CA  LEU A  47      51.280 -14.421 -20.336  1.00 56.27      A    C  
ANISOU  309  CA  LEU A  47     5607   7240   8534   1107     -7  -1242  A    C  
ATOM    310  C   LEU A  47      50.469 -15.669 -20.012  1.00 61.29      A    C  
ANISOU  310  C   LEU A  47     6381   7654   9254   1112   -133  -1308  A    C  
ATOM    311  O   LEU A  47      50.947 -16.791 -20.174  1.00 71.65      A    O  
ANISOU  311  O   LEU A  47     7718   8859  10646   1240   -176  -1436  A    O  
ATOM    312  CB  LEU A  47      51.656 -14.407 -21.819  1.00 56.35      A    C  
ANISOU  312  CB  LEU A  47     5572   7420   8420   1193    106  -1385  A    C  
ATOM    313  CG  LEU A  47      52.596 -13.301 -22.294  1.00 58.76      A    C  
ANISOU  313  CG  LEU A  47     5739   7955   8633   1190    247  -1338  A    C  
ATOM    314  CD1 LEU A  47      52.877 -13.424 -23.788  1.00 52.71      A    C  
ANISOU  314  CD1 LEU A  47     4947   7351   7730   1273    359  -1490  A    C  
ATOM    315  CD2 LEU A  47      52.028 -11.926 -21.961  1.00 52.49      A    C  
ANISOU  315  CD2 LEU A  47     4965   7225   7753   1028    276  -1160  A    C  
ATOM    316  N   LYS A  48      49.248 -15.474 -19.536  1.00 58.96      A    N  
ANISOU  316  N   LYS A  48     6175   7286   8940    971   -193  -1220  A    N  
ATOM    317  CA  LYS A  48      48.357 -16.589 -19.252  1.00 59.05      A    C  
ANISOU  317  CA  LYS A  48     6320   7101   9017    931   -307  -1271  A    C  
ATOM    318  C   LYS A  48      47.215 -16.581 -20.247  1.00 56.51      A    C  
ANISOU  318  C   LYS A  48     6055   6845   8571    860   -299  -1347  A    C  
ATOM    319  O   LYS A  48      46.416 -15.648 -20.271  1.00 66.32      A    O  
ANISOU  319  O   LYS A  48     7281   8197   9722    754   -271  -1252  A    O  
ATOM    320  CB  LYS A  48      47.827 -16.502 -17.824  1.00 58.57      A    C  
ANISOU  320  CB  LYS A  48     6307   6908   9038    813   -388  -1112  A    C  
ATOM    321  CG  LYS A  48      48.928 -16.510 -16.785  1.00 76.38      A    C  
ANISOU  321  CG  LYS A  48     8514   9101  11407    876   -415  -1031  A    C  
ATOM    322  CD  LYS A  48      48.394 -16.891 -15.418  1.00 95.97      A    C  
ANISOU  322  CD  LYS A  48    11089  11398  13976    778   -521   -912  A    C  
ATOM    323  CE  LYS A  48      49.493 -16.852 -14.352  1.00101.67      A    C  
ANISOU  323  CE  LYS A  48    11764  12068  14797    840   -562   -822  A    C  
ATOM    324  NZ  LYS A  48      48.906 -16.967 -12.979  1.00103.23      A    N1+
ANISOU  324  NZ  LYS A  48    12057  12122  15045    719   -649   -680  A    N1+
ATOM    325  N   LYS A  49      47.147 -17.615 -21.079  1.00 55.76      A    N  
ANISOU  325  N   LYS A  49     6029   6687   8470    927   -327  -1524  A    N  
ATOM    326  CA  LYS A  49      46.148 -17.673 -22.136  1.00 65.46      A    C  
ANISOU  326  CA  LYS A  49     7309   7995   9569    866   -328  -1618  A    C  
ATOM    327  C   LYS A  49      44.783 -18.046 -21.560  1.00 67.66      A    C  
ANISOU  327  C   LYS A  49     7673   8157   9876    701   -434  -1567  A    C  
ATOM    328  O   LYS A  49      44.719 -18.785 -20.583  1.00 63.13      A    O  
ANISOU  328  O   LYS A  49     7170   7385   9434    663   -518  -1530  A    O  
ATOM    329  CB  LYS A  49      46.567 -18.690 -23.188  1.00 73.25      A    C  
ANISOU  329  CB  LYS A  49     8353   8944  10534    988   -327  -1837  A    C  
ATOM    330  CG  LYS A  49      45.911 -18.508 -24.547  1.00 83.16      A    C  
ANISOU  330  CG  LYS A  49     9629  10355  11613    963   -293  -1949  A    C  
ATOM    331  CD  LYS A  49      46.205 -19.704 -25.442  1.00 95.55      A    C  
ANISOU  331  CD  LYS A  49    11294  11841  13172   1070   -313  -2181  A    C  
ATOM    332  CE  LYS A  49      45.632 -19.518 -26.838  1.00107.41      A    C  
ANISOU  332  CE  LYS A  49    12819  13513  14478   1049   -280  -2301  A    C  
ATOM    333  NZ  LYS A  49      46.366 -18.482 -27.621  1.00111.80      A    N1+
ANISOU  333  NZ  LYS A  49    13264  14320  14894   1132   -134  -2282  A    N1+
ATOM    334  N   VAL A  50      43.712 -17.499 -22.142  1.00 68.78      A    N  
ANISOU  334  N   VAL A  50     7804   8437   9891    603   -430  -1556  A    N  
ATOM    335  CA  VAL A  50      42.330 -17.933 -21.864  1.00 72.15      A    C  
ANISOU  335  CA  VAL A  50     8291   8798  10324    443   -526  -1544  A    C  
ATOM    336  C   VAL A  50      41.815 -18.732 -23.071  1.00 65.18      A    C  
ANISOU  336  C   VAL A  50     7479   7926   9359    432   -571  -1736  A    C  
ATOM    337  O   VAL A  50      42.543 -18.900 -24.036  1.00 77.24      A    O  
ANISOU  337  O   VAL A  50     9016   9508  10826    558   -521  -1868  A    O  
ATOM    338  CB  VAL A  50      41.413 -16.741 -21.580  1.00 66.23      A    C  
ANISOU  338  CB  VAL A  50     7463   8208   9493    345   -502  -1392  A    C  
ATOM    339  CG1 VAL A  50      40.035 -17.220 -21.132  1.00 58.84      A    C  
ANISOU  339  CG1 VAL A  50     6560   7218   8580    176   -596  -1371  A    C  
ATOM    340  CG2 VAL A  50      42.042 -15.854 -20.533  1.00 58.13      A    C  
ANISOU  340  CG2 VAL A  50     6379   7183   8524    368   -445  -1223  A    C  
ATOM    341  N   GLU A  55      34.243 -21.482 -23.167  1.00114.74      A    N  
ANISOU  341  N   GLU A  55    13847  14217  15532   -647  -1114  -1890  A    N  
ATOM    342  CA  GLU A  55      33.913 -22.704 -23.898  1.00107.99      A    C  
ANISOU  342  CA  GLU A  55    13120  13247  14665   -751  -1215  -2084  A    C  
ATOM    343  C   GLU A  55      32.520 -22.752 -24.538  1.00 94.71      A    C  
ANISOU  343  C   GLU A  55    11357  11753  12874   -934  -1302  -2144  A    C  
ATOM    344  O   GLU A  55      32.324 -22.308 -25.673  1.00 91.60      A    O  
ANISOU  344  O   GLU A  55    10910  11564  12332   -869  -1309  -2229  A    O  
ATOM    345  CB  GLU A  55      34.071 -23.878 -22.930  1.00112.24      A    C  
ANISOU  345  CB  GLU A  55    13814  13467  15365   -864  -1270  -2079  A    C  
ATOM    346  CG  GLU A  55      35.163 -23.640 -21.861  1.00111.05      A    C  
ANISOU  346  CG  GLU A  55    13690  13169  15336   -725  -1197  -1943  A    C  
ATOM    347  CD  GLU A  55      34.820 -22.550 -20.827  1.00 97.45      A    C  
ANISOU  347  CD  GLU A  55    11815  11586  13627   -756  -1132  -1722  A    C  
ATOM    348  OE1 GLU A  55      33.649 -22.123 -20.728  1.00 96.90      A    O  
ANISOU  348  OE1 GLU A  55    11626  11691  13499   -903  -1148  -1661  A    O  
ATOM    349  OE2 GLU A  55      35.734 -22.124 -20.095  1.00 88.45      A    O1-
ANISOU  349  OE2 GLU A  55    10673  10381  12554   -629  -1067  -1614  A    O1-
ATOM    350  N   LYS A  56      31.558 -23.304 -23.805  1.00 86.51      A    N  
ANISOU  350  N   LYS A  56    10311  10654  11906  -1169  -1373  -2097  A    N  
ATOM    351  CA  LYS A  56      30.210 -23.509 -24.332  1.00 88.06      A    C  
ANISOU  351  CA  LYS A  56    10422  11021  12017  -1374  -1470  -2163  A    C  
ATOM    352  C   LYS A  56      29.295 -22.296 -24.128  1.00 71.63      A    C  
ANISOU  352  C   LYS A  56     8099   9256   9861  -1388  -1438  -2016  A    C  
ATOM    353  O   LYS A  56      28.183 -22.241 -24.641  1.00 73.81      A    O  
ANISOU  353  O   LYS A  56     8257   9740  10048  -1518  -1514  -2058  A    O  
ATOM    354  CB  LYS A  56      29.578 -24.753 -23.695  1.00 96.37      A    C  
ANISOU  354  CB  LYS A  56    11580  11862  13175  -1649  -1562  -2193  A    C  
ATOM    355  CG  LYS A  56      30.190 -26.085 -24.138  1.00100.23      A    C  
ANISOU  355  CG  LYS A  56    12326  12044  13712  -1667  -1630  -2379  A    C  
ATOM    356  CD  LYS A  56      29.293 -27.248 -23.731  1.00104.59      A    C  
ANISOU  356  CD  LYS A  56    12976  12432  14332  -1986  -1740  -2421  A    C  
ATOM    357  CE  LYS A  56      29.517 -28.461 -24.614  1.00108.68      A    C  
ANISOU  357  CE  LYS A  56    13728  12731  14834  -2035  -1838  -2657  A    C  
ATOM    358  NZ  LYS A  56      28.268 -29.262 -24.764  1.00108.31      A    N1+
ANISOU  358  NZ  LYS A  56    13699  12686  14768  -2378  -1964  -2735  A    N1+
ATOM    359  N   GLU A  57      29.767 -21.325 -23.371  1.00 59.49      A    N  
ANISOU  359  N   GLU A  57     6489   7756   8359  -1247  -1331  -1848  A    N  
ATOM    360  CA  GLU A  57      28.948 -20.180 -23.045  1.00 56.26      A    C  
ANISOU  360  CA  GLU A  57     5872   7611   7891  -1239  -1293  -1704  A    C  
ATOM    361  C   GLU A  57      29.724 -18.899 -23.313  1.00 53.32      A    C  
ANISOU  361  C   GLU A  57     5458   7353   7449   -981  -1191  -1624  A    C  
ATOM    362  O   GLU A  57      29.783 -18.016 -22.463  1.00 51.92      A    O  
ANISOU  362  O   GLU A  57     5204   7220   7301   -915  -1111  -1463  A    O  
ATOM    363  CB  GLU A  57      28.517 -20.264 -21.581  1.00 47.59      A    C  
ANISOU  363  CB  GLU A  57     4731   6439   6912  -1379  -1263  -1554  A    C  
ATOM    364  CG  GLU A  57      27.575 -21.421 -21.295  1.00 61.14      A    C  
ANISOU  364  CG  GLU A  57     6467   8083   8682  -1671  -1359  -1610  A    C  
ATOM    365  CD  GLU A  57      26.213 -21.249 -21.972  1.00 73.72      A    C  
ANISOU  365  CD  GLU A  57     7873   9969  10166  -1801  -1437  -1661  A    C  
ATOM    366  OE1 GLU A  57      25.706 -20.103 -22.027  1.00 68.01      A    O  
ANISOU  366  OE1 GLU A  57     6961   9517   9364  -1698  -1396  -1571  A    O  
ATOM    367  OE2 GLU A  57      25.651 -22.261 -22.450  1.00 81.92      A    O1-
ANISOU  367  OE2 GLU A  57     8959  10967  11198  -2006  -1545  -1794  A    O1-
ATOM    368  N   GLY A  58      30.331 -18.807 -24.492  1.00 52.24      A    N  
ANISOU  368  N   GLY A  58     5383   7255   7211   -843  -1191  -1738  A    N  
ATOM    369  CA  GLY A  58      31.170 -17.666 -24.814  1.00 50.78      A    C  
ANISOU  369  CA  GLY A  58     5181   7159   6954   -617  -1090  -1668  A    C  
ATOM    370  C   GLY A  58      32.355 -17.506 -23.871  1.00 52.06      A    C  
ANISOU  370  C   GLY A  58     5415   7128   7238   -520   -991  -1573  A    C  
ATOM    371  O   GLY A  58      32.876 -18.489 -23.328  1.00 54.13      A    O  
ANISOU  371  O   GLY A  58     5789   7152   7625   -574  -1008  -1616  A    O  
ATOM    372  N   PHE A  59      32.773 -16.259 -23.670  1.00 49.72      A    N  
ANISOU  372  N   PHE A  59     5058   6931   6901   -377   -897  -1442  A    N  
ATOM    373  CA  PHE A  59      33.896 -15.957 -22.797  1.00 45.22      A    C  
ANISOU  373  CA  PHE A  59     4537   6213   6431   -287   -807  -1345  A    C  
ATOM    374  C   PHE A  59      33.649 -16.439 -21.368  1.00 51.33      A    C  
ANISOU  374  C   PHE A  59     5323   6829   7353   -414   -822  -1254  A    C  
ATOM    375  O   PHE A  59      32.670 -16.062 -20.752  1.00 58.91      A    O  
ANISOU  375  O   PHE A  59     6190   7883   8312   -504   -830  -1159  A    O  
ATOM    376  CB  PHE A  59      34.213 -14.459 -22.806  1.00 45.03      A    C  
ANISOU  376  CB  PHE A  59     4449   6333   6326   -146   -712  -1213  A    C  
ATOM    377  CG  PHE A  59      35.557 -14.140 -22.226  1.00 54.50      A    C  
ANISOU  377  CG  PHE A  59     5702   7404   7600    -44   -622  -1147  A    C  
ATOM    378  CD1 PHE A  59      36.689 -14.113 -23.035  1.00 55.58      A    C  
ANISOU  378  CD1 PHE A  59     5890   7533   7694     78   -570  -1223  A    C  
ATOM    379  CD2 PHE A  59      35.705 -13.910 -20.871  1.00 52.36      A    C  
ANISOU  379  CD2 PHE A  59     5425   7030   7439    -79   -592  -1015  A    C  
ATOM    380  CE1 PHE A  59      37.947 -13.848 -22.507  1.00 49.41      A    C  
ANISOU  380  CE1 PHE A  59     5136   6654   6985    163   -492  -1167  A    C  
ATOM    381  CE2 PHE A  59      36.960 -13.642 -20.334  1.00 54.07      A    C  
ANISOU  381  CE2 PHE A  59     5684   7139   7723      6   -524   -959  A    C  
ATOM    382  CZ  PHE A  59      38.085 -13.615 -21.158  1.00 45.80      A    C  
ANISOU  382  CZ  PHE A  59     4669   6093   6639    125   -476  -1036  A    C  
ATOM    383  N   PRO A  60      34.549 -17.274 -20.837  1.00 60.98      A    N  
ANISOU  383  N   PRO A  60     6658   7814   8696   -412   -823  -1282  A    N  
ATOM    384  CA  PRO A  60      34.385 -17.913 -19.523  1.00 56.85      A    C  
ANISOU  384  CA  PRO A  60     6182   7110   8308   -540   -850  -1205  A    C  
ATOM    385  C   PRO A  60      34.084 -16.921 -18.396  1.00 55.85      A    C  
ANISOU  385  C   PRO A  60     5969   7057   8194   -552   -787  -1019  A    C  
ATOM    386  O   PRO A  60      34.867 -16.001 -18.091  1.00 51.46      A    O  
ANISOU  386  O   PRO A  60     5398   6522   7632   -420   -708   -930  A    O  
ATOM    387  CB  PRO A  60      35.747 -18.587 -19.285  1.00 52.29      A    C  
ANISOU  387  CB  PRO A  60     5735   6300   7833   -444   -842  -1247  A    C  
ATOM    388  CG  PRO A  60      36.301 -18.775 -20.646  1.00 54.87      A    C  
ANISOU  388  CG  PRO A  60     6093   6670   8084   -325   -840  -1407  A    C  
ATOM    389  CD  PRO A  60      35.856 -17.585 -21.437  1.00 56.89      A    C  
ANISOU  389  CD  PRO A  60     6230   7197   8190   -266   -792  -1380  A    C  
ATOM    390  N   ILE A  61      32.942 -17.144 -17.759  1.00 52.19      A    N  
ANISOU  390  N   ILE A  61     5452   6629   7747   -721   -820   -966  A    N  
ATOM    391  CA  ILE A  61      32.475 -16.301 -16.671  1.00 41.47      A    C  
ANISOU  391  CA  ILE A  61     4013   5352   6393   -746   -761   -806  A    C  
ATOM    392  C   ILE A  61      33.480 -16.300 -15.526  1.00 50.16      A    C  
ANISOU  392  C   ILE A  61     5206   6263   7590   -707   -719   -707  A    C  
ATOM    393  O   ILE A  61      33.616 -15.322 -14.788  1.00 59.40      A    O  
ANISOU  393  O   ILE A  61     6336   7488   8746   -649   -649   -583  A    O  
ATOM    394  CB  ILE A  61      31.048 -16.716 -16.223  1.00 57.85      A    C  
ANISOU  394  CB  ILE A  61     6004   7508   8468   -953   -802   -785  A    C  
ATOM    395  CG1 ILE A  61      30.510 -15.786 -15.138  1.00 52.46      A    C  
ANISOU  395  CG1 ILE A  61     5225   6935   7772   -962   -726   -629  A    C  
ATOM    396  CG2 ILE A  61      30.975 -18.225 -15.822  1.00 37.73      A    C  
ANISOU  396  CG2 ILE A  61     3579   4737   6022  -1144   -879   -838  A    C  
ATOM    397  CD1 ILE A  61      29.031 -15.976 -14.919  1.00 46.73      A    C  
ANISOU  397  CD1 ILE A  61     4365   6371   7019  -1136   -750   -618  A    C  
ATOM    398  N   THR A  62      34.216 -17.391 -15.409  1.00 56.85      A    N  
ANISOU  398  N   THR A  62     6185   6885   8529   -728   -770   -767  A    N  
ATOM    399  CA  THR A  62      35.244 -17.516 -14.385  1.00 54.91      A    C  
ANISOU  399  CA  THR A  62     6031   6455   8376   -680   -753   -682  A    C  
ATOM    400  C   THR A  62      36.419 -16.592 -14.667  1.00 55.21      A    C  
ANISOU  400  C   THR A  62     6049   6538   8391   -480   -686   -664  A    C  
ATOM    401  O   THR A  62      36.977 -15.979 -13.747  1.00 54.86      A    O  
ANISOU  401  O   THR A  62     6008   6465   8372   -437   -641   -547  A    O  
ATOM    402  CB  THR A  62      35.701 -18.984 -14.255  1.00 62.32      A    C  
ANISOU  402  CB  THR A  62     7125   7133   9420   -735   -838   -757  A    C  
ATOM    403  CG2 THR A  62      37.143 -19.076 -13.884  1.00 75.29      A    C  
ANISOU  403  CG2 THR A  62     8848   8621  11139   -584   -830   -737  A    C  
ATOM    404  OG1 THR A  62      34.939 -19.604 -13.217  1.00 66.43      A    O  
ANISOU  404  OG1 THR A  62     7695   7556   9990   -932   -874   -677  A    O  
ATOM    405  N   ALA A  63      36.788 -16.479 -15.940  1.00 48.05      A    N  
ANISOU  405  N   ALA A  63     5122   5711   7425   -372   -677   -780  A    N  
ATOM    406  CA  ALA A  63      37.846 -15.550 -16.328  1.00 50.48      A    C  
ANISOU  406  CA  ALA A  63     5398   6091   7692   -203   -603   -763  A    C  
ATOM    407  C   ALA A  63      37.399 -14.086 -16.174  1.00 56.20      A    C  
ANISOU  407  C   ALA A  63     6031   7001   8322   -177   -529   -649  A    C  
ATOM    408  O   ALA A  63      38.180 -13.240 -15.742  1.00 52.10      A    O  
ANISOU  408  O   ALA A  63     5506   6488   7802    -98   -467   -563  A    O  
ATOM    409  CB  ALA A  63      38.329 -15.835 -17.750  1.00 48.29      A    C  
ANISOU  409  CB  ALA A  63     5130   5860   7360   -103   -603   -918  A    C  
ATOM    410  N   LEU A  64      36.142 -13.790 -16.509  1.00 57.96      A    N  
ANISOU  410  N   LEU A  64     6184   7373   8466   -241   -540   -648  A    N  
ATOM    411  CA  LEU A  64      35.619 -12.440 -16.302  1.00 51.64      A    C  
ANISOU  411  CA  LEU A  64     5307   6734   7580   -201   -477   -539  A    C  
ATOM    412  C   LEU A  64      35.730 -12.063 -14.848  1.00 49.79      A    C  
ANISOU  412  C   LEU A  64     5091   6421   7404   -239   -441   -405  A    C  
ATOM    413  O   LEU A  64      36.119 -10.952 -14.520  1.00 55.28      A    O  
ANISOU  413  O   LEU A  64     5783   7159   8062   -160   -375   -317  A    O  
ATOM    414  CB  LEU A  64      34.156 -12.320 -16.724  1.00 47.26      A    C  
ANISOU  414  CB  LEU A  64     4659   6351   6947   -265   -508   -557  A    C  
ATOM    415  CG  LEU A  64      33.916 -12.415 -18.226  1.00 51.66      A    C  
ANISOU  415  CG  LEU A  64     5189   7034   7407   -216   -545   -677  A    C  
ATOM    416  CD1 LEU A  64      32.439 -12.539 -18.502  1.00 56.11      A    C  
ANISOU  416  CD1 LEU A  64     5649   7757   7914   -308   -602   -701  A    C  
ATOM    417  CD2 LEU A  64      34.531 -11.235 -18.976  1.00 39.16      A    C  
ANISOU  417  CD2 LEU A  64     3606   5556   5719    -55   -478   -648  A    C  
ATOM    418  N   ARG A  65      35.386 -12.992 -13.969  1.00 46.53      A    N  
ANISOU  418  N   ARG A  65     4713   5888   7077   -369   -487   -390  A    N  
ATOM    419  CA  ARG A  65      35.422 -12.707 -12.540  1.00 48.63      A    C  
ANISOU  419  CA  ARG A  65     5008   6086   7386   -419   -457   -262  A    C  
ATOM    420  C   ARG A  65      36.842 -12.373 -12.086  1.00 51.38      A    C  
ANISOU  420  C   ARG A  65     5424   6320   7778   -326   -431   -215  A    C  
ATOM    421  O   ARG A  65      37.057 -11.386 -11.376  1.00 53.32      A    O  
ANISOU  421  O   ARG A  65     5670   6594   7994   -291   -374   -115  A    O  
ATOM    422  CB  ARG A  65      34.855 -13.880 -11.755  1.00 46.57      A    C  
ANISOU  422  CB  ARG A  65     4789   5705   7199   -588   -514   -254  A    C  
ATOM    423  CG  ARG A  65      34.662 -13.639 -10.289  1.00 58.98      A    C  
ANISOU  423  CG  ARG A  65     6387   7232   8790   -663   -481   -123  A    C  
ATOM    424  CD  ARG A  65      34.256 -14.946  -9.655  1.00 66.42      A    C  
ANISOU  424  CD  ARG A  65     7400   8033   9806   -838   -544   -120  A    C  
ATOM    425  NE  ARG A  65      35.167 -15.999 -10.094  1.00 85.64      A    N  
ANISOU  425  NE  ARG A  65     9941  10277  12324   -811   -621   -204  A    N  
ATOM    426  CZ  ARG A  65      35.173 -17.242  -9.625  1.00 93.20      A    C  
ANISOU  426  CZ  ARG A  65    11010  11042  13359   -930   -693   -209  A    C  
ATOM    427  NH1 ARG A  65      34.299 -17.608  -8.692  1.00 92.09      A    N1+
ANISOU  427  NH1 ARG A  65    10887  10883  13220  -1110   -693   -128  A    N1+
ATOM    428  NH2 ARG A  65      36.059 -18.116 -10.092  1.00 93.92      A    N  
ANISOU  428  NH2 ARG A  65    11202  10958  13523   -866   -760   -294  A    N  
ATOM    429  N   GLU A  66      37.807 -13.181 -12.523  1.00 47.74      A    N  
ANISOU  429  N   GLU A  66     5018   5739   7383   -281   -474   -296  A    N  
ATOM    430  CA  GLU A  66      39.202 -12.981 -12.146  1.00 49.78      A    C  
ANISOU  430  CA  GLU A  66     5316   5906   7691   -192   -460   -263  A    C  
ATOM    431  C   GLU A  66      39.717 -11.631 -12.639  1.00 52.31      A    C  
ANISOU  431  C   GLU A  66     5586   6362   7929    -86   -379   -234  A    C  
ATOM    432  O   GLU A  66      40.315 -10.864 -11.880  1.00 50.64      A    O  
ANISOU  432  O   GLU A  66     5387   6136   7718    -66   -342   -141  A    O  
ATOM    433  CB  GLU A  66      40.072 -14.101 -12.704  1.00 53.94      A    C  
ANISOU  433  CB  GLU A  66     5891   6308   8297   -136   -517   -375  A    C  
ATOM    434  CG  GLU A  66      41.550 -13.960 -12.373  1.00 62.82      A    C  
ANISOU  434  CG  GLU A  66     7027   7362   9479    -32   -508   -352  A    C  
ATOM    435  CD  GLU A  66      42.386 -15.092 -12.951  1.00 74.95      A    C  
ANISOU  435  CD  GLU A  66     8601   8783  11093     51   -561   -474  A    C  
ATOM    436  OE1 GLU A  66      41.809 -15.970 -13.628  1.00 79.36      A    O  
ANISOU  436  OE1 GLU A  66     9197   9301  11656     21   -604   -581  A    O  
ATOM    437  OE2 GLU A  66      43.621 -15.106 -12.737  1.00 73.52      A    O1-
ANISOU  437  OE2 GLU A  66     8409   8556  10967    150   -562   -469  A    O1-
ATOM    438  N   ILE A  67      39.474 -11.349 -13.916  1.00 45.00      A    N  
ANISOU  438  N   ILE A  67     4613   5561   6922    -29   -354   -313  A    N  
ATOM    439  CA  ILE A  67      39.837 -10.073 -14.500  1.00 49.40      A    C  
ANISOU  439  CA  ILE A  67     5139   6246   7383     59   -277   -281  A    C  
ATOM    440  C   ILE A  67      39.231  -8.914 -13.703  1.00 51.53      A    C  
ANISOU  440  C   ILE A  67     5408   6572   7598     38   -231   -155  A    C  
ATOM    441  O   ILE A  67      39.920  -7.943 -13.375  1.00 44.36      A    O  
ANISOU  441  O   ILE A  67     4522   5667   6666     76   -177    -82  A    O  
ATOM    442  CB  ILE A  67      39.386  -9.994 -15.975  1.00 48.60      A    C  
ANISOU  442  CB  ILE A  67     5002   6282   7183    109   -269   -375  A    C  
ATOM    443  CG1 ILE A  67      40.171 -11.001 -16.811  1.00 48.48      A    C  
ANISOU  443  CG1 ILE A  67     5000   6215   7206    153   -297   -509  A    C  
ATOM    444  CG2 ILE A  67      39.561  -8.582 -16.526  1.00 38.49      A    C  
ANISOU  444  CG2 ILE A  67     3709   5132   5785    186   -191   -316  A    C  
ATOM    445  CD1 ILE A  67      39.667 -11.134 -18.238  1.00 51.87      A    C  
ANISOU  445  CD1 ILE A  67     5408   6769   7531    186   -303   -620  A    C  
ATOM    446  N   LYS A  68      37.946  -9.020 -13.374  1.00 45.10      A    N  
ANISOU  446  N   LYS A  68     4568   5804   6765    -27   -250   -135  A    N  
ATOM    447  CA  LYS A  68      37.278  -7.947 -12.636  1.00 47.95      A    C  
ANISOU  447  CA  LYS A  68     4924   6227   7068    -28   -201    -30  A    C  
ATOM    448  C   LYS A  68      38.002  -7.722 -11.309  1.00 47.11      A    C  
ANISOU  448  C   LYS A  68     4883   6000   7018    -61   -184     59  A    C  
ATOM    449  O   LYS A  68      38.285  -6.591 -10.934  1.00 46.91      A    O  
ANISOU  449  O   LYS A  68     4891   5991   6941    -19   -129    133  A    O  
ATOM    450  CB  LYS A  68      35.795  -8.264 -12.406  1.00 41.00      A    C  
ANISOU  450  CB  LYS A  68     3981   5427   6169    -99   -223    -30  A    C  
ATOM    451  CG  LYS A  68      35.105  -7.366 -11.388  1.00 49.59      A    C  
ANISOU  451  CG  LYS A  68     5064   6563   7216   -103   -169     72  A    C  
ATOM    452  CD  LYS A  68      33.791  -7.970 -10.875  1.00 58.74      A    C  
ANISOU  452  CD  LYS A  68     6149   7784   8385   -209   -189     73  A    C  
ATOM    453  CE  LYS A  68      34.050  -9.212 -10.016  1.00 62.07      A    C  
ANISOU  453  CE  LYS A  68     6621   8052   8909   -351   -235     75  A    C  
ATOM    454  NZ  LYS A  68      32.822  -9.761  -9.374  1.00 60.85      A    N1+
ANISOU  454  NZ  LYS A  68     6405   7955   8760   -484   -240     93  A    N1+
ATOM    455  N   ILE A  69      38.328  -8.815 -10.626  1.00 43.83      A    N  
ANISOU  455  N   ILE A  69     4499   5454   6701   -137   -240     51  A    N  
ATOM    456  CA  ILE A  69      39.046  -8.754  -9.354  1.00 41.50      A    C  
ANISOU  456  CA  ILE A  69     4269   5042   6456   -172   -245    133  A    C  
ATOM    457  C   ILE A  69      40.494  -8.231  -9.464  1.00 46.43      A    C  
ANISOU  457  C   ILE A  69     4916   5632   7095   -102   -230    143  A    C  
ATOM    458  O   ILE A  69      40.913  -7.381  -8.672  1.00 45.94      A    O  
ANISOU  458  O   ILE A  69     4893   5552   7009   -106   -199    225  A    O  
ATOM    459  CB  ILE A  69      38.964 -10.092  -8.615  1.00 46.05      A    C  
ANISOU  459  CB  ILE A  69     4887   5484   7126   -270   -319    131  A    C  
ATOM    460  CG1 ILE A  69      37.501 -10.327  -8.173  1.00 37.54      A    C  
ANISOU  460  CG1 ILE A  69     3785   4460   6017   -375   -312    156  A    C  
ATOM    461  CG2 ILE A  69      39.885 -10.079  -7.410  1.00 39.58      A    C  
ANISOU  461  CG2 ILE A  69     4141   4545   6354   -289   -342    212  A    C  
ATOM    462  CD1 ILE A  69      37.135 -11.760  -7.910  1.00 35.40      A    C  
ANISOU  462  CD1 ILE A  69     3549   4081   5822   -491   -385    127  A    C  
ATOM    463  N   LEU A  70      41.247  -8.719 -10.448  1.00 50.83      A    N  
ANISOU  463  N   LEU A  70     5442   6187   7684    -42   -247     57  A    N  
ATOM    464  CA  LEU A  70      42.592  -8.197 -10.720  1.00 43.34      A    C  
ANISOU  464  CA  LEU A  70     4482   5246   6740     22   -219     57  A    C  
ATOM    465  C   LEU A  70      42.561  -6.689 -11.032  1.00 48.27      A    C  
ANISOU  465  C   LEU A  70     5111   5975   7255     50   -136    112  A    C  
ATOM    466  O   LEU A  70      43.439  -5.945 -10.620  1.00 46.36      A    O  
ANISOU  466  O   LEU A  70     4888   5720   7005     47   -108    167  A    O  
ATOM    467  CB  LEU A  70      43.229  -8.951 -11.888  1.00 48.09      A    C  
ANISOU  467  CB  LEU A  70     5037   5862   7372     92   -233    -61  A    C  
ATOM    468  CG  LEU A  70      44.168 -10.150 -11.644  1.00 58.22      A    C  
ANISOU  468  CG  LEU A  70     6321   7024   8775    120   -303   -114  A    C  
ATOM    469  CD1 LEU A  70      44.191 -10.612 -10.206  1.00 52.26      A    C  
ANISOU  469  CD1 LEU A  70     5626   6134   8096     55   -371    -33  A    C  
ATOM    470  CD2 LEU A  70      43.814 -11.310 -12.580  1.00 41.61      A    C  
ANISOU  470  CD2 LEU A  70     4216   4896   6698    151   -342   -244  A    C  
ATOM    471  N   GLN A  71      41.545  -6.228 -11.753  1.00 48.62      A    N  
ANISOU  471  N   GLN A  71     5143   6119   7211     75   -101     99  A    N  
ATOM    472  CA  GLN A  71      41.459  -4.805 -12.056  1.00 48.55      A    C  
ANISOU  472  CA  GLN A  71     5165   6188   7095    114    -29    157  A    C  
ATOM    473  C   GLN A  71      41.147  -3.944 -10.832  1.00 49.83      A    C  
ANISOU  473  C   GLN A  71     5394   6306   7232     79     -6    259  A    C  
ATOM    474  O   GLN A  71      41.518  -2.776 -10.784  1.00 45.04      A    O  
ANISOU  474  O   GLN A  71     4844   5707   6561     96     46    316  A    O  
ATOM    475  CB  GLN A  71      40.419  -4.557 -13.132  1.00 37.08      A    C  
ANISOU  475  CB  GLN A  71     3684   4855   5549    169    -13    121  A    C  
ATOM    476  CG  GLN A  71      40.889  -4.938 -14.521  1.00 44.83      A    C  
ANISOU  476  CG  GLN A  71     4627   5903   6504    218    -10     29  A    C  
ATOM    477  CD  GLN A  71      39.723  -5.059 -15.475  1.00 55.74      A    C  
ANISOU  477  CD  GLN A  71     5974   7398   7807    255    -29    -22  A    C  
ATOM    478  NE2 GLN A  71      38.508  -5.139 -14.928  1.00 61.29      A    N  
ANISOU  478  NE2 GLN A  71     6655   8121   8510    229    -58      3  A    N  
ATOM    479  OE1 GLN A  71      39.906  -5.091 -16.684  1.00 59.41      A    O  
ANISOU  479  OE1 GLN A  71     6423   7944   8206    304    -18    -84  A    O  
ATOM    480  N   LEU A  72      40.454  -4.529  -9.858  1.00 43.14      A    N  
ANISOU  480  N   LEU A  72     4551   5411   6430     23    -42    278  A    N  
ATOM    481  CA  LEU A  72      40.106  -3.839  -8.629  1.00 39.36      A    C  
ANISOU  481  CA  LEU A  72     4138   4894   5923    -11    -17    363  A    C  
ATOM    482  C   LEU A  72      41.301  -3.734  -7.687  1.00 45.91      A    C  
ANISOU  482  C   LEU A  72     5025   5621   6799    -63    -37    410  A    C  
ATOM    483  O   LEU A  72      41.533  -2.674  -7.103  1.00 46.17      A    O  
ANISOU  483  O   LEU A  72     5133   5633   6776    -70      2    471  A    O  
ATOM    484  CB  LEU A  72      38.964  -4.573  -7.912  1.00 44.70      A    C  
ANISOU  484  CB  LEU A  72     4791   5571   6621    -68    -41    368  A    C  
ATOM    485  CG  LEU A  72      38.608  -4.006  -6.528  1.00 48.83      A    C  
ANISOU  485  CG  LEU A  72     5385   6059   7111   -110    -10    449  A    C  
ATOM    486  CD1 LEU A  72      37.984  -2.592  -6.637  1.00 35.55      A    C  
ANISOU  486  CD1 LEU A  72     3738   4452   5319    -26     67    483  A    C  
ATOM    487  CD2 LEU A  72      37.678  -4.944  -5.779  1.00 42.13      A    C  
ANISOU  487  CD2 LEU A  72     4508   5208   6293   -195    -34    456  A    C  
ATOM    488  N   LEU A  73      42.052  -4.833  -7.549  1.00 39.18      A    N  
ANISOU  488  N   LEU A  73     4142   4702   6045    -93   -103    377  A    N  
ATOM    489  CA  LEU A  73      43.111  -4.942  -6.550  1.00 45.22      A    C  
ANISOU  489  CA  LEU A  73     4944   5375   6862   -141   -147    422  A    C  
ATOM    490  C   LEU A  73      44.458  -4.347  -6.998  1.00 50.58      A    C  
ANISOU  490  C   LEU A  73     5601   6074   7543   -118   -132    417  A    C  
ATOM    491  O   LEU A  73      45.153  -4.930  -7.826  1.00 52.54      A    O  
ANISOU  491  O   LEU A  73     5774   6345   7843    -75   -148    352  A    O  
ATOM    492  CB  LEU A  73      43.288  -6.406  -6.149  1.00 46.94      A    C  
ANISOU  492  CB  LEU A  73     5146   5505   7184   -169   -234    398  A    C  
ATOM    493  CG  LEU A  73      42.020  -7.060  -5.601  1.00 47.59      A    C  
ANISOU  493  CG  LEU A  73     5254   5563   7265   -229   -249    414  A    C  
ATOM    494  CD1 LEU A  73      42.263  -8.525  -5.160  1.00 37.98      A    C  
ANISOU  494  CD1 LEU A  73     4055   4227   6150   -270   -343    402  A    C  
ATOM    495  CD2 LEU A  73      41.469  -6.214  -4.454  1.00 36.28      A    C  
ANISOU  495  CD2 LEU A  73     3893   4134   5757   -280   -208    500  A    C  
ATOM    496  N   LYS A  74      44.822  -3.192  -6.450  1.00 44.35      A    N  
ANISOU  496  N   LYS A  74     4878   5280   6695   -153    -98    480  A    N  
ATOM    497  CA  LYS A  74      46.129  -2.588  -6.746  1.00 47.45      A    C  
ANISOU  497  CA  LYS A  74     5247   5695   7086   -167    -84    485  A    C  
ATOM    498  C   LYS A  74      46.926  -2.325  -5.475  1.00 47.99      A    C  
ANISOU  498  C   LYS A  74     5362   5699   7173   -246   -135    545  A    C  
ATOM    499  O   LYS A  74      46.651  -1.379  -4.747  1.00 55.50      A    O  
ANISOU  499  O   LYS A  74     6418   6618   8051   -295   -109    601  A    O  
ATOM    500  CB  LYS A  74      45.974  -1.302  -7.549  1.00 39.49      A    C  
ANISOU  500  CB  LYS A  74     4282   4748   5974   -151      6    499  A    C  
ATOM    501  CG  LYS A  74      45.209  -1.509  -8.841  1.00 52.29      A    C  
ANISOU  501  CG  LYS A  74     5859   6447   7560    -70     46    444  A    C  
ATOM    502  CD  LYS A  74      45.806  -2.675  -9.616  1.00 59.82      A    C  
ANISOU  502  CD  LYS A  74     6698   7437   8595    -33     12    360  A    C  
ATOM    503  CE  LYS A  74      45.041  -2.955 -10.896  1.00 60.82      A    C  
ANISOU  503  CE  LYS A  74     6789   7644   8678     39     41    294  A    C  
ATOM    504  NZ  LYS A  74      45.897  -3.716 -11.839  1.00 54.71      A    N1+
ANISOU  504  NZ  LYS A  74     5921   6918   7948     80     38    208  A    N1+
ATOM    505  N   HIS A  75      47.927  -3.160  -5.220  1.00 43.97      A    N  
ANISOU  505  N   HIS A  75     4778   5172   6757   -250   -211    528  A    N  
ATOM    506  CA  HIS A  75      48.615  -3.121  -3.944  1.00 44.06      A    C  
ANISOU  506  CA  HIS A  75     4826   5126   6789   -320   -286    585  A    C  
ATOM    507  C   HIS A  75      49.993  -3.794  -4.043  1.00 55.62      A    C  
ANISOU  507  C   HIS A  75     6168   6614   8350   -298   -359    556  A    C  
ATOM    508  O   HIS A  75      50.161  -4.752  -4.806  1.00 58.25      A    O  
ANISOU  508  O   HIS A  75     6409   6965   8756   -213   -374    490  A    O  
ATOM    509  CB  HIS A  75      47.729  -3.792  -2.897  1.00 37.47      A    C  
ANISOU  509  CB  HIS A  75     4072   4204   5960   -339   -336    622  A    C  
ATOM    510  CG  HIS A  75      48.294  -3.758  -1.517  1.00 52.09      A    C  
ANISOU  510  CG  HIS A  75     5986   5995   7809   -412   -417    687  A    C  
ATOM    511  CD2 HIS A  75      48.119  -2.878  -0.503  1.00 50.92      A    C  
ANISOU  511  CD2 HIS A  75     5955   5818   7573   -490   -408    746  A    C  
ATOM    512  ND1 HIS A  75      49.162  -4.722  -1.048  1.00 54.19      A    N  
ANISOU  512  ND1 HIS A  75     6202   6224   8165   -400   -530    694  A    N  
ATOM    513  CE1 HIS A  75      49.498  -4.434   0.198  1.00 58.09      A    C  
ANISOU  513  CE1 HIS A  75     6774   6676   8621   -476   -592    760  A    C  
ATOM    514  NE2 HIS A  75      48.879  -3.321   0.553  1.00 60.83      A    N  
ANISOU  514  NE2 HIS A  75     7226   7027   8858   -537   -517    788  A    N  
ATOM    515  N   GLU A  76      50.978  -3.288  -3.293  1.00 46.98      A    N  
ANISOU  515  N   GLU A  76     5070   5527   7252   -369   -406    600  A    N  
ATOM    516  CA  GLU A  76      52.342  -3.808  -3.388  1.00 52.69      A    C  
ANISOU  516  CA  GLU A  76     5651   6305   8064   -342   -475    574  A    C  
ATOM    517  C   GLU A  76      52.433  -5.324  -3.172  1.00 49.95      A    C  
ANISOU  517  C   GLU A  76     5258   5896   7826   -245   -575    547  A    C  
ATOM    518  O   GLU A  76      53.301  -5.978  -3.736  1.00 52.62      A    O  
ANISOU  518  O   GLU A  76     5461   6285   8246   -160   -605    490  A    O  
ATOM    519  CB  GLU A  76      53.284  -3.082  -2.419  1.00 65.71      A    C  
ANISOU  519  CB  GLU A  76     7307   7971   9688   -450   -534    632  A    C  
ATOM    520  CG  GLU A  76      54.182  -2.051  -3.080  1.00 91.01      A    C  
ANISOU  520  CG  GLU A  76    10432  11290  12858   -519   -467    620  A    C  
ATOM    521  CD  GLU A  76      55.550  -2.606  -3.457  1.00108.04      A    C  
ANISOU  521  CD  GLU A  76    12382  13560  15108   -476   -515    577  A    C  
ATOM    522  OE1 GLU A  76      56.285  -3.048  -2.546  1.00114.20      A    O  
ANISOU  522  OE1 GLU A  76    13110  14337  15943   -483   -637    602  A    O  
ATOM    523  OE2 GLU A  76      55.901  -2.584  -4.660  1.00111.39      A    O1-
ANISOU  523  OE2 GLU A  76    12692  14087  15545   -432   -430    518  A    O1-
ATOM    524  N   ASN A  77      51.537  -5.871  -2.357  1.00 41.34      A    N  
ANISOU  524  N   ASN A  77     4285   4693   6730   -257   -623    588  A    N  
ATOM    525  CA  ASN A  77      51.554  -7.300  -2.045  1.00 46.58      A    C  
ANISOU  525  CA  ASN A  77     4945   5264   7488   -182   -726    578  A    C  
ATOM    526  C   ASN A  77      50.465  -8.107  -2.749  1.00 51.56      A    C  
ANISOU  526  C   ASN A  77     5610   5841   8139   -130   -687    525  A    C  
ATOM    527  O   ASN A  77      50.102  -9.196  -2.317  1.00 54.71      A    O  
ANISOU  527  O   ASN A  77     6067   6128   8591   -109   -762    535  A    O  
ATOM    528  CB  ASN A  77      51.519  -7.517  -0.528  1.00 47.47      A    C  
ANISOU  528  CB  ASN A  77     5169   5284   7585   -248   -830    672  A    C  
ATOM    529  CG  ASN A  77      52.622  -6.742   0.183  1.00 55.30      A    C  
ANISOU  529  CG  ASN A  77     6126   6334   8550   -309   -885    719  A    C  
ATOM    530  ND2 ASN A  77      53.867  -7.028  -0.175  1.00 53.37      A    N  
ANISOU  530  ND2 ASN A  77     5730   6161   8387   -241   -941    682  A    N  
ATOM    531  OD1 ASN A  77      52.355  -5.870   1.005  1.00 56.39      A    O  
ANISOU  531  OD1 ASN A  77     6367   6465   8594   -417   -873    778  A    O  
ATOM    532  N   VAL A  78      49.952  -7.564  -3.845  1.00 47.60      A    N  
ANISOU  532  N   VAL A  78     5077   5418   7591   -118   -576    470  A    N  
ATOM    533  CA  VAL A  78      49.025  -8.295  -4.684  1.00 40.84      A    C  
ANISOU  533  CA  VAL A  78     4228   4539   6751    -70   -545    403  A    C  
ATOM    534  C   VAL A  78      49.537  -8.267  -6.105  1.00 44.15      A    C  
ANISOU  534  C   VAL A  78     4533   5058   7184     15   -484    305  A    C  
ATOM    535  O   VAL A  78      50.018  -7.238  -6.583  1.00 47.28      A    O  
ANISOU  535  O   VAL A  78     4878   5563   7524      0   -411    306  A    O  
ATOM    536  CB  VAL A  78      47.615  -7.698  -4.618  1.00 43.01      A    C  
ANISOU  536  CB  VAL A  78     4587   4824   6931   -137   -471    434  A    C  
ATOM    537  CG1 VAL A  78      46.698  -8.408  -5.597  1.00 40.06      A    C  
ANISOU  537  CG1 VAL A  78     4197   4454   6570    -97   -445    356  A    C  
ATOM    538  CG2 VAL A  78      47.076  -7.817  -3.195  1.00 44.69      A    C  
ANISOU  538  CG2 VAL A  78     4910   4947   7122   -222   -520    525  A    C  
ATOM    539  N   VAL A  79      49.471  -9.413  -6.767  1.00 47.67      A    N  
ANISOU  539  N   VAL A  79     4951   5462   7698    100   -514    219  A    N  
ATOM    540  CA  VAL A  79      49.986  -9.535  -8.122  1.00 48.67      A    C  
ANISOU  540  CA  VAL A  79     4975   5685   7834    193   -457    111  A    C  
ATOM    541  C   VAL A  79      49.308  -8.491  -8.987  1.00 51.65      A    C  
ANISOU  541  C   VAL A  79     5354   6173   8096    155   -342    104  A    C  
ATOM    542  O   VAL A  79      48.145  -8.130  -8.764  1.00 52.53      A    O  
ANISOU  542  O   VAL A  79     5548   6264   8145     93   -320    147  A    O  
ATOM    543  CB  VAL A  79      49.775 -10.961  -8.687  1.00 55.66      A    C  
ANISOU  543  CB  VAL A  79     5868   6484   8796    285   -508      9  A    C  
ATOM    544  CG1 VAL A  79      48.340 -11.162  -9.132  1.00 48.79      A    C  
ANISOU  544  CG1 VAL A  79     5075   5588   7874    236   -480    -17  A    C  
ATOM    545  CG2 VAL A  79      50.730 -11.233  -9.817  1.00 62.55      A    C  
ANISOU  545  CG2 VAL A  79     6623   7447   9696    406   -470   -104  A    C  
ATOM    546  N   ASN A  80      50.059  -7.981  -9.949  1.00 47.38      A    N  
ANISOU  546  N   ASN A  80     4722   5757   7522    195   -269     57  A    N  
ATOM    547  CA  ASN A  80      49.593  -6.907 -10.798  1.00 43.64      A    C  
ANISOU  547  CA  ASN A  80     4261   5389   6930    164   -163     63  A    C  
ATOM    548  C   ASN A  80      49.331  -7.316 -12.239  1.00 48.73      A    C  
ANISOU  548  C   ASN A  80     4867   6109   7540    242   -111    -47  A    C  
ATOM    549  O   ASN A  80      50.247  -7.658 -12.986  1.00 55.83      A    O  
ANISOU  549  O   ASN A  80     5672   7079   8461    312    -83   -126  A    O  
ATOM    550  CB  ASN A  80      50.589  -5.757 -10.790  1.00 44.08      A    C  
ANISOU  550  CB  ASN A  80     4270   5538   6941    113   -104    115  A    C  
ATOM    551  CG  ASN A  80      50.152  -4.614 -11.686  1.00 49.67      A    C  
ANISOU  551  CG  ASN A  80     5016   6337   7519     81      4    133  A    C  
ATOM    552  ND2 ASN A  80      50.977  -4.285 -12.672  1.00 44.81      A    N  
ANISOU  552  ND2 ASN A  80     4318   5843   6865     97     80     93  A    N  
ATOM    553  OD1 ASN A  80      49.077  -4.042 -11.499  1.00 55.62      A    O  
ANISOU  553  OD1 ASN A  80     5874   7057   8204     49     19    184  A    O  
ATOM    554  N   LEU A  81      48.067  -7.257 -12.622  1.00 50.47      A    N  
ANISOU  554  N   LEU A  81     5154   6326   7696    229    -96    -54  A    N  
ATOM    555  CA  LEU A  81      47.667  -7.466 -13.998  1.00 52.67      A    C  
ANISOU  555  CA  LEU A  81     5413   6689   7909    287    -50   -148  A    C  
ATOM    556  C   LEU A  81      48.017  -6.203 -14.768  1.00 56.04      A    C  
ANISOU  556  C   LEU A  81     5826   7248   8218    275     54   -115  A    C  
ATOM    557  O   LEU A  81      47.529  -5.121 -14.451  1.00 55.45      A    O  
ANISOU  557  O   LEU A  81     5817   7181   8069    218     86    -20  A    O  
ATOM    558  CB  LEU A  81      46.164  -7.747 -14.069  1.00 42.11      A    C  
ANISOU  558  CB  LEU A  81     4142   5320   6538    264    -81   -156  A    C  
ATOM    559  CG  LEU A  81      45.555  -7.934 -15.455  1.00 46.28      A    C  
ANISOU  559  CG  LEU A  81     4660   5942   6982    311    -51   -250  A    C  
ATOM    560  CD1 LEU A  81      46.022  -9.260 -16.100  1.00 40.03      A    C  
ANISOU  560  CD1 LEU A  81     3833   5118   6257    381    -87   -391  A    C  
ATOM    561  CD2 LEU A  81      44.019  -7.876 -15.363  1.00 39.20      A    C  
ANISOU  561  CD2 LEU A  81     3810   5046   6037    268    -80   -227  A    C  
ATOM    562  N   ILE A  82      48.883  -6.328 -15.765  1.00 55.75      A    N  
ANISOU  562  N   ILE A  82     5712   7311   8159    328    111   -191  A    N  
ATOM    563  CA  ILE A  82      49.303  -5.162 -16.523  1.00 51.19      A    C  
ANISOU  563  CA  ILE A  82     5128   6860   7463    300    216   -152  A    C  
ATOM    564  C   ILE A  82      48.251  -4.776 -17.546  1.00 52.54      A    C  
ANISOU  564  C   ILE A  82     5366   7095   7501    320    254   -165  A    C  
ATOM    565  O   ILE A  82      47.875  -3.618 -17.651  1.00 54.10      A    O  
ANISOU  565  O   ILE A  82     5635   7323   7596    277    300    -75  A    O  
ATOM    566  CB  ILE A  82      50.641  -5.395 -17.231  1.00 50.86      A    C  
ANISOU  566  CB  ILE A  82     4967   6928   7431    342    278   -226  A    C  
ATOM    567  CG1 ILE A  82      51.758  -5.530 -16.197  1.00 49.09      A    C  
ANISOU  567  CG1 ILE A  82     4660   6669   7324    317    240   -193  A    C  
ATOM    568  CG2 ILE A  82      50.933  -4.250 -18.183  1.00 36.69      A    C  
ANISOU  568  CG2 ILE A  82     3181   5270   5490    298    396   -187  A    C  
ATOM    569  CD1 ILE A  82      52.940  -6.311 -16.701  1.00 53.32      A    C  
ANISOU  569  CD1 ILE A  82     5049   7288   7922    406    262   -300  A    C  
ATOM    570  N   GLU A  83      47.776  -5.758 -18.298  1.00 57.52      A    N  
ANISOU  570  N   GLU A  83     5981   7742   8131    389    225   -280  A    N  
ATOM    571  CA  GLU A  83      46.811  -5.510 -19.357  1.00 45.51      A    C  
ANISOU  571  CA  GLU A  83     4510   6302   6480    415    246   -307  A    C  
ATOM    572  C   GLU A  83      46.323  -6.841 -19.887  1.00 52.97      A    C  
ANISOU  572  C   GLU A  83     5438   7228   7459    471    184   -446  A    C  
ATOM    573  O   GLU A  83      46.829  -7.905 -19.503  1.00 55.53      A    O  
ANISOU  573  O   GLU A  83     5723   7469   7906    500    137   -521  A    O  
ATOM    574  CB  GLU A  83      47.459  -4.735 -20.507  1.00 44.59      A    C  
ANISOU  574  CB  GLU A  83     4385   6330   6228    426    355   -307  A    C  
ATOM    575  CG  GLU A  83      48.489  -5.564 -21.298  1.00 52.77      A    C  
ANISOU  575  CG  GLU A  83     5327   7441   7281    487    398   -438  A    C  
ATOM    576  CD  GLU A  83      49.126  -4.782 -22.448  1.00 62.71      A    C  
ANISOU  576  CD  GLU A  83     6577   8862   8389    483    521   -433  A    C  
ATOM    577  OE1 GLU A  83      48.451  -3.909 -23.029  1.00 71.99      A    O  
ANISOU  577  OE1 GLU A  83     7841  10092   9421    461    551   -366  A    O  
ATOM    578  OE2 GLU A  83      50.302  -5.045 -22.780  1.00 60.71      A    O1-
ANISOU  578  OE2 GLU A  83     6225   8687   8154    504    589   -495  A    O1-
ATOM    579  N   ILE A  84      45.344  -6.771 -20.782  1.00 57.51      A    N  
ANISOU  579  N   ILE A  84     6051   7876   7922    489    178   -482  A    N  
ATOM    580  CA  ILE A  84      44.856  -7.945 -21.495  1.00 53.09      A    C  
ANISOU  580  CA  ILE A  84     5489   7319   7365    529    122   -627  A    C  
ATOM    581  C   ILE A  84      45.155  -7.828 -22.987  1.00 52.46      A    C  
ANISOU  581  C   ILE A  84     5405   7387   7141    586    190   -713  A    C  
ATOM    582  O   ILE A  84      44.924  -6.785 -23.594  1.00 58.16      A    O  
ANISOU  582  O   ILE A  84     6159   8219   7720    581    245   -643  A    O  
ATOM    583  CB  ILE A  84      43.355  -8.156 -21.229  1.00 49.67      A    C  
ANISOU  583  CB  ILE A  84     5091   6854   6926    486     35   -612  A    C  
ATOM    584  CG1 ILE A  84      43.185  -8.659 -19.799  1.00 45.42      A    C  
ANISOU  584  CG1 ILE A  84     4555   6161   6541    428    -31   -562  A    C  
ATOM    585  CG2 ILE A  84      42.752  -9.130 -22.238  1.00 48.63      A    C  
ANISOU  585  CG2 ILE A  84     4967   6762   6749    508    -17   -761  A    C  
ATOM    586  CD1 ILE A  84      42.112  -7.961 -19.050  1.00 51.80      A    C  
ANISOU  586  CD1 ILE A  84     5386   6967   7331    372    -53   -447  A    C  
ATOM    587  N   CYS A  85      45.694  -8.893 -23.570  1.00 52.43      A    N  
ANISOU  587  N   CYS A  85     5375   7380   7167    645    188   -865  A    N  
ATOM    588  CA  CYS A  85      46.124  -8.837 -24.956  1.00 50.48      A    C  
ANISOU  588  CA  CYS A  85     5123   7280   6777    703    267   -959  A    C  
ATOM    589  C   CYS A  85      45.392  -9.852 -25.812  1.00 57.17      A    C  
ANISOU  589  C   CYS A  85     6010   8135   7575    736    201  -1118  A    C  
ATOM    590  O   CYS A  85      44.993 -10.919 -25.339  1.00 62.14      A    O  
ANISOU  590  O   CYS A  85     6657   8631   8323    728    106  -1193  A    O  
ATOM    591  CB  CYS A  85      47.645  -9.019 -25.056  1.00 64.22      A    C  
ANISOU  591  CB  CYS A  85     6783   9054   8563    759    357  -1010  A    C  
ATOM    592  SG  CYS A  85      48.612  -7.528 -24.578  1.00 61.02      A    S  
ANISOU  592  SG  CYS A  85     6330   8722   8133    695    468   -833  A    S  
ATOM    593  N   ARG A  86      45.204  -9.498 -27.076  1.00 58.33      A    N  
ANISOU  593  N   ARG A  86     6187   8438   7540    762    248  -1164  A    N  
ATOM    594  CA  ARG A  86      44.520 -10.355 -28.032  1.00 56.67      A    C  
ANISOU  594  CA  ARG A  86     6023   8261   7248    785    187  -1321  A    C  
ATOM    595  C   ARG A  86      45.518 -10.971 -29.003  1.00 66.52      A    C  
ANISOU  595  C   ARG A  86     7261   9576   8438    874    267  -1485  A    C  
ATOM    596  O   ARG A  86      46.730 -10.795 -28.880  1.00 57.89      A    O  
ANISOU  596  O   ARG A  86     6105   8508   7384    919    368  -1476  A    O  
ATOM    597  CB  ARG A  86      43.511  -9.538 -28.843  1.00 49.23      A    C  
ANISOU  597  CB  ARG A  86     5127   7464   6114    761    169  -1265  A    C  
ATOM    598  CG  ARG A  86      44.173  -8.436 -29.654  1.00 55.98      A    C  
ANISOU  598  CG  ARG A  86     5994   8478   6798    789    296  -1194  A    C  
ATOM    599  CD  ARG A  86      43.190  -7.581 -30.426  1.00 68.52      A    C  
ANISOU  599  CD  ARG A  86     7645  10199   8192    781    268  -1121  A    C  
ATOM    600  NE  ARG A  86      43.765  -6.266 -30.715  1.00 81.50      A    N  
ANISOU  600  NE  ARG A  86     9319  11935   9714    779    382   -978  A    N  
ATOM    601  CZ  ARG A  86      44.132  -5.839 -31.922  1.00 87.75      A    C  
ANISOU  601  CZ  ARG A  86    10158  12880  10303    805    464   -994  A    C  
ATOM    602  NH1 ARG A  86      43.979  -6.621 -32.981  1.00 89.14      A    N1+
ANISOU  602  NH1 ARG A  86    10355  13147  10367    845    446  -1157  A    N1+
ATOM    603  NH2 ARG A  86      44.643  -4.620 -32.071  1.00 87.75      A    N  
ANISOU  603  NH2 ARG A  86    10198  12940  10202    780    566   -845  A    N  
ATOM    604  N   THR A  87      44.966 -11.665 -29.990  1.00 79.84      A    N  
ANISOU  604  N   THR A  87     9006  11308  10022    896    221  -1637  A    N  
ATOM    605  CA  THR A  87      45.709 -12.315 -31.043  1.00 84.69      A    C  
ANISOU  605  CA  THR A  87     9633  11994  10551    987    290  -1819  A    C  
ATOM    606  C   THR A  87      44.640 -13.017 -31.838  1.00 96.49      A    C  
ANISOU  606  C   THR A  87    11215  13501  11946    966    185  -1956  A    C  
ATOM    607  O   THR A  87      44.471 -12.792 -33.035  1.00109.37      A    O  
ANISOU  607  O   THR A  87    12889  15293  13372    986    218  -2022  A    O  
ATOM    608  CB  THR A  87      46.581 -13.407 -30.482  1.00 89.76      A    C  
ANISOU  608  CB  THR A  87    10244  12483  11376   1062    288  -1933  A    C  
ATOM    609  CG2 THR A  87      45.743 -14.648 -30.222  1.00 73.33      A    C  
ANISOU  609  CG2 THR A  87     8244  10223   9393   1037    141  -2052  A    C  
ATOM    610  OG1 THR A  87      47.614 -13.716 -31.424  1.00109.33      A    O  
ANISOU  610  OG1 THR A  87    12701  15071  13769   1174    405  -2078  A    O  
ATOM    611  N   SER A  98      42.372 -15.667 -29.626  1.00 92.62      A    N  
ANISOU  611  N   SER A  98    10827  12477  11888    756   -211  -2058  A    N  
ATOM    612  CA  SER A  98      42.627 -15.890 -28.202  1.00 90.12      A    C  
ANISOU  612  CA  SER A  98    10485  11975  11783    728   -237  -1956  A    C  
ATOM    613  C   SER A  98      42.800 -14.615 -27.369  1.00 81.23      A    C  
ANISOU  613  C   SER A  98     9274  10907  10682    708   -176  -1735  A    C  
ATOM    614  O   SER A  98      42.746 -13.498 -27.884  1.00 88.42      A    O  
ANISOU  614  O   SER A  98    10151  11992  11452    719   -108  -1650  A    O  
ATOM    615  CB  SER A  98      43.851 -16.782 -28.015  1.00 93.03      A    C  
ANISOU  615  CB  SER A  98    10874  12201  12271    842   -202  -2067  A    C  
ATOM    616  OG  SER A  98      43.586 -18.089 -28.481  1.00106.12      A    O  
ANISOU  616  OG  SER A  98    12640  13734  13947    848   -282  -2264  A    O  
ATOM    617  N   ILE A  99      43.015 -14.813 -26.073  1.00 63.07      A    N  
ANISOU  617  N   ILE A  99     6959   8448   8558    678   -204  -1645  A    N  
ATOM    618  CA  ILE A  99      43.178 -13.729 -25.117  1.00 57.43      A    C  
ANISOU  618  CA  ILE A  99     6182   7754   7886    650   -160  -1447  A    C  
ATOM    619  C   ILE A  99      44.224 -14.109 -24.067  1.00 57.43      A    C  
ANISOU  619  C   ILE A  99     6162   7602   8059    690   -149  -1413  A    C  
ATOM    620  O   ILE A  99      44.338 -15.274 -23.680  1.00 62.21      A    O  
ANISOU  620  O   ILE A  99     6816   8036   8785    701   -220  -1498  A    O  
ATOM    621  CB  ILE A  99      41.830 -13.394 -24.438  1.00 59.27      A    C  
ANISOU  621  CB  ILE A  99     6415   7976   8130    529   -238  -1334  A    C  
ATOM    622  CG1 ILE A  99      40.953 -12.596 -25.398  1.00 63.90      A    C  
ANISOU  622  CG1 ILE A  99     6990   8757   8532    516   -233  -1317  A    C  
ATOM    623  CG2 ILE A  99      42.029 -12.629 -23.137  1.00 48.82      A    C  
ANISOU  623  CG2 ILE A  99     5055   6598   6897    497   -213  -1153  A    C  
ATOM    624  CD1 ILE A  99      41.624 -11.359 -25.945  1.00 59.60      A    C  
ANISOU  624  CD1 ILE A  99     6423   8360   7863    587   -119  -1237  A    C  
ATOM    625  N   TYR A 100      44.993 -13.126 -23.614  1.00 52.35      A    N  
ANISOU  625  N   TYR A 100     5453   7018   7421    711    -67  -1287  A    N  
ATOM    626  CA  TYR A 100      46.037 -13.375 -22.635  1.00 54.85      A    C  
ANISOU  626  CA  TYR A 100     5732   7222   7887    751    -62  -1246  A    C  
ATOM    627  C   TYR A 100      45.936 -12.369 -21.511  1.00 56.19      A    C  
ANISOU  627  C   TYR A 100     5874   7382   8093    673    -55  -1054  A    C  
ATOM    628  O   TYR A 100      45.764 -11.166 -21.752  1.00 55.90      A    O  
ANISOU  628  O   TYR A 100     5818   7474   7946    641     11   -958  A    O  
ATOM    629  CB  TYR A 100      47.433 -13.215 -23.259  1.00 59.98      A    C  
ANISOU  629  CB  TYR A 100     6306   7975   8509    866     45  -1308  A    C  
ATOM    630  CG  TYR A 100      47.822 -14.218 -24.316  1.00 60.35      A    C  
ANISOU  630  CG  TYR A 100     6372   8032   8525    976     59  -1512  A    C  
ATOM    631  CD1 TYR A 100      48.644 -15.293 -24.007  1.00 65.33      A    C  
ANISOU  631  CD1 TYR A 100     6997   8534   9291   1084     28  -1614  A    C  
ATOM    632  CD2 TYR A 100      47.395 -14.075 -25.627  1.00 64.40      A    C  
ANISOU  632  CD2 TYR A 100     6916   8686   8868    985    102  -1605  A    C  
ATOM    633  CE1 TYR A 100      49.019 -16.205 -24.967  1.00 64.26      A    C  
ANISOU  633  CE1 TYR A 100     6890   8399   9125   1203     47  -1813  A    C  
ATOM    634  CE2 TYR A 100      47.768 -14.988 -26.601  1.00 70.73      A    C  
ANISOU  634  CE2 TYR A 100     7747   9500   9628   1089    121  -1805  A    C  
ATOM    635  CZ  TYR A 100      48.582 -16.051 -26.266  1.00 69.65      A    C  
ANISOU  635  CZ  TYR A 100     7608   9225   9632   1201     97  -1913  A    C  
ATOM    636  OH  TYR A 100      48.955 -16.968 -27.231  1.00 78.56      A    O  
ANISOU  636  OH  TYR A 100     8777  10354  10717   1322    119  -2124  A    O  
ATOM    637  N   LEU A 101      46.070 -12.852 -20.282  1.00 50.06      A    N  
ANISOU  637  N   LEU A 101     5112   6446   7463    647   -123   -999  A    N  
ATOM    638  CA  LEU A 101      46.256 -11.954 -19.162  1.00 48.30      A    C  
ANISOU  638  CA  LEU A 101     4864   6210   7278    588   -110   -833  A    C  
ATOM    639  C   LEU A 101      47.750 -11.705 -19.041  1.00 56.25      A    C  
ANISOU  639  C   LEU A 101     5789   7256   8328    661    -50   -825  A    C  
ATOM    640  O   LEU A 101      48.534 -12.652 -19.013  1.00 47.71      A    O  
ANISOU  640  O   LEU A 101     4684   6102   7340    749    -78   -916  A    O  
ATOM    641  CB  LEU A 101      45.690 -12.561 -17.875  1.00 55.71      A    C  
ANISOU  641  CB  LEU A 101     5859   6973   8335    515   -211   -770  A    C  
ATOM    642  CG  LEU A 101      44.181 -12.363 -17.661  1.00 51.17      A    C  
ANISOU  642  CG  LEU A 101     5331   6402   7711    407   -249   -717  A    C  
ATOM    643  CD1 LEU A 101      43.410 -13.036 -18.756  1.00 42.49      A    C  
ANISOU  643  CD1 LEU A 101     4258   5337   6550    407   -278   -849  A    C  
ATOM    644  CD2 LEU A 101      43.757 -12.902 -16.315  1.00 49.45      A    C  
ANISOU  644  CD2 LEU A 101     5163   6024   7601    324   -329   -641  A    C  
ATOM    645  N   VAL A 102      48.149 -10.436 -19.000  1.00 54.64      A    N  
ANISOU  645  N   VAL A 102     5541   7167   8053    625     32   -720  A    N  
ATOM    646  CA  VAL A 102      49.560 -10.106 -18.849  1.00 52.92      A    C  
ANISOU  646  CA  VAL A 102     5227   7010   7872    665     90   -703  A    C  
ATOM    647  C   VAL A 102      49.911  -9.659 -17.427  1.00 54.16      A    C  
ANISOU  647  C   VAL A 102     5374   7088   8116    598     48   -567  A    C  
ATOM    648  O   VAL A 102      49.392  -8.652 -16.958  1.00 59.43      A    O  
ANISOU  648  O   VAL A 102     6087   7764   8727    505     63   -448  A    O  
ATOM    649  CB  VAL A 102      49.995  -9.016 -19.847  1.00 49.09      A    C  
ANISOU  649  CB  VAL A 102     4697   6715   7241    654    219   -687  A    C  
ATOM    650  CG1 VAL A 102      51.511  -8.879 -19.834  1.00 44.64      A    C  
ANISOU  650  CG1 VAL A 102     4006   6238   6719    693    284   -699  A    C  
ATOM    651  CG2 VAL A 102      49.505  -9.360 -21.237  1.00 45.02      A    C  
ANISOU  651  CG2 VAL A 102     4211   6286   6610    708    255   -808  A    C  
ATOM    652  N   PHE A 103      50.798 -10.398 -16.755  1.00 50.73      A    N  
ANISOU  652  N   PHE A 103     4887   6577   7811    656     -8   -590  A    N  
ATOM    653  CA  PHE A 103      51.282 -10.010 -15.423  1.00 53.71      A    C  
ANISOU  653  CA  PHE A 103     5248   6895   8264    598    -56   -468  A    C  
ATOM    654  C   PHE A 103      52.777  -9.672 -15.377  1.00 59.19      A    C  
ANISOU  654  C   PHE A 103     5801   7698   8990    633    -13   -465  A    C  
ATOM    655  O   PHE A 103      53.587 -10.283 -16.083  1.00 58.16      A    O  
ANISOU  655  O   PHE A 103     5573   7637   8888    748     18   -578  A    O  
ATOM    656  CB  PHE A 103      51.063 -11.134 -14.413  1.00 56.13      A    C  
ANISOU  656  CB  PHE A 103     5615   7012   8699    622   -186   -467  A    C  
ATOM    657  CG  PHE A 103      49.657 -11.662 -14.358  1.00 53.03      A    C  
ANISOU  657  CG  PHE A 103     5346   6508   8295    574   -238   -476  A    C  
ATOM    658  CD1 PHE A 103      48.778 -11.219 -13.384  1.00 48.09      A    C  
ANISOU  658  CD1 PHE A 103     4800   5817   7656    459   -273   -358  A    C  
ATOM    659  CD2 PHE A 103      49.231 -12.634 -15.249  1.00 54.23      A    C  
ANISOU  659  CD2 PHE A 103     5533   6625   8448    637   -254   -610  A    C  
ATOM    660  CE1 PHE A 103      47.488 -11.725 -13.308  1.00 54.71      A    C  
ANISOU  660  CE1 PHE A 103     5728   6574   8485    403   -317   -366  A    C  
ATOM    661  CE2 PHE A 103      47.936 -13.140 -15.181  1.00 63.76      A    C  
ANISOU  661  CE2 PHE A 103     6842   7739   9646    569   -308   -620  A    C  
ATOM    662  CZ  PHE A 103      47.067 -12.690 -14.207  1.00 58.20      A    C  
ANISOU  662  CZ  PHE A 103     6194   6987   8932    449   -337   -495  A    C  
ATOM    663  N   ASP A 104      53.144  -8.723 -14.517  1.00 63.65      A    N  
ANISOU  663  N   ASP A 104     6351   8283   9551    533    -13   -341  A    N  
ATOM    664  CA  ASP A 104      54.543  -8.540 -14.121  1.00 63.46      A    C  
ANISOU  664  CA  ASP A 104     6185   8340   9586    544    -12   -323  A    C  
ATOM    665  C   ASP A 104      55.111  -9.910 -13.732  1.00 63.50      A    C  
ANISOU  665  C   ASP A 104     6136   8258   9732    686   -114   -399  A    C  
ATOM    666  O   ASP A 104      54.496 -10.639 -12.957  1.00 70.33      A    O  
ANISOU  666  O   ASP A 104     7106   8949  10665    698   -223   -377  A    O  
ATOM    667  CB  ASP A 104      54.640  -7.573 -12.932  1.00 73.14      A    C  
ANISOU  667  CB  ASP A 104     7446   9537  10806    406    -47   -178  A    C  
ATOM    668  CG  ASP A 104      54.602  -6.088 -13.349  1.00 85.78      A    C  
ANISOU  668  CG  ASP A 104     9069  11248  12276    278     65   -106  A    C  
ATOM    669  OD1 ASP A 104      55.263  -5.719 -14.345  1.00 90.93      A    O  
ANISOU  669  OD1 ASP A 104     9625  12055  12870    283    169   -151  A    O  
ATOM    670  OD2 ASP A 104      53.931  -5.282 -12.659  1.00 81.50      A    O1-
ANISOU  670  OD2 ASP A 104     8648  10634  11686    171     51     -4  A    O1-
ATOM    671  N   PHE A 105      56.270 -10.274 -14.273  1.00 64.40      A    N  
ANISOU  671  N   PHE A 105     6091   8492   9887    799    -78   -488  A    N  
ATOM    672  CA  PHE A 105      56.856 -11.597 -14.013  1.00 64.85      A    C  
ANISOU  672  CA  PHE A 105     6098   8465  10077    970   -173   -574  A    C  
ATOM    673  C   PHE A 105      57.451 -11.739 -12.606  1.00 72.43      A    C  
ANISOU  673  C   PHE A 105     7027   9350  11142    964   -302   -478  A    C  
ATOM    674  O   PHE A 105      58.045 -10.797 -12.082  1.00 74.07      A    O  
ANISOU  674  O   PHE A 105     7151   9662  11328    859   -290   -386  A    O  
ATOM    675  CB  PHE A 105      57.919 -11.919 -15.065  1.00 57.19      A    C  
ANISOU  675  CB  PHE A 105     4951   7666   9111   1114    -83   -709  A    C  
ATOM    676  CG  PHE A 105      58.592 -13.249 -14.872  1.00 54.80      A    C  
ANISOU  676  CG  PHE A 105     4593   7284   8944   1324   -175   -808  A    C  
ATOM    677  CD1 PHE A 105      57.966 -14.418 -15.253  1.00 55.60      A    C  
ANISOU  677  CD1 PHE A 105     4824   7220   9083   1444   -224   -917  A    C  
ATOM    678  CD2 PHE A 105      59.878 -13.323 -14.336  1.00 60.60      A    C  
ANISOU  678  CD2 PHE A 105     5143   8114   9767   1406   -216   -796  A    C  
ATOM    679  CE1 PHE A 105      58.605 -15.652 -15.091  1.00 63.98      A    C  
ANISOU  679  CE1 PHE A 105     5856   8183  10268   1654   -311  -1012  A    C  
ATOM    680  CE2 PHE A 105      60.530 -14.553 -14.171  1.00 55.59      A    C  
ANISOU  680  CE2 PHE A 105     4456   7406   9260   1630   -307   -888  A    C  
ATOM    681  CZ  PHE A 105      59.894 -15.715 -14.546  1.00 57.43      A    C  
ANISOU  681  CZ  PHE A 105     4844   7448   9530   1760   -354   -995  A    C  
ATOM    682  N   CYS A 106      57.273 -12.914 -11.999  1.00 72.07      A    N  
ANISOU  682  N   CYS A 106     7064   9117  11202   1069   -432   -497  A    N  
ATOM    683  CA  CYS A 106      57.809 -13.196 -10.666  1.00 70.32      A    C  
ANISOU  683  CA  CYS A 106     6833   8810  11074   1083   -574   -406  A    C  
ATOM    684  C   CYS A 106      58.537 -14.531 -10.700  1.00 79.32      A    C  
ANISOU  684  C   CYS A 106     7922   9877  12340   1311   -663   -503  A    C  
ATOM    685  O   CYS A 106      57.962 -15.562 -11.070  1.00 72.26      A    O  
ANISOU  685  O   CYS A 106     7151   8823  11480   1408   -695   -588  A    O  
ATOM    686  CB  CYS A 106      56.711 -13.213  -9.587  1.00 70.90      A    C  
ANISOU  686  CB  CYS A 106     7111   8690  11138    956   -664   -287  A    C  
ATOM    687  SG  CYS A 106      55.596 -11.713  -9.486  1.00 97.97      A    S  
ANISOU  687  SG  CYS A 106    10640  12166  14418    714   -565   -179  A    S  
ATOM    688  N   GLU A 107      59.809 -14.499 -10.312  1.00 85.91      A    N  
ANISOU  688  N   GLU A 107     8574  10827  13239   1397   -708   -494  A    N  
ATOM    689  CA  GLU A 107      60.692 -15.648 -10.436  1.00 80.86      A    C  
ANISOU  689  CA  GLU A 107     7843  10162  12717   1647   -780   -595  A    C  
ATOM    690  C   GLU A 107      60.333 -16.773  -9.462  1.00 78.33      A    C  
ANISOU  690  C   GLU A 107     7705   9565  12493   1732   -961   -550  A    C  
ATOM    691  O   GLU A 107      60.244 -17.941  -9.849  1.00 74.27      A    O  
ANISOU  691  O   GLU A 107     7272   8902  12046   1909  -1004   -654  A    O  
ATOM    692  CB  GLU A 107      62.143 -15.198 -10.230  1.00 97.95      A    C  
ANISOU  692  CB  GLU A 107     9736  12560  14920   1703   -782   -585  A    C  
ATOM    693  CG  GLU A 107      63.173 -16.325 -10.281  1.00108.45      A    C  
ANISOU  693  CG  GLU A 107    10937  13893  16378   1990   -864   -685  A    C  
ATOM    694  CD  GLU A 107      63.325 -16.924 -11.667  1.00113.93      A    C  
ANISOU  694  CD  GLU A 107    11573  14646  17068   2169   -743   -875  A    C  
ATOM    695  OE1 GLU A 107      63.496 -16.150 -12.637  1.00118.86      A    O  
ANISOU  695  OE1 GLU A 107    12071  15491  17599   2094   -571   -930  A    O  
ATOM    696  OE2 GLU A 107      63.277 -18.169 -11.783  1.00109.64      A    O1-
ANISOU  696  OE2 GLU A 107    11126  13923  16609   2383   -820   -968  A    O1-
ATOM    697  N   HIS A 108      60.113 -16.420  -8.200  1.00 81.56      A    N  
ANISOU  697  N   HIS A 108     8195   9896  12898   1599  -1065   -393  A    N  
ATOM    698  CA  HIS A 108      59.935 -17.428  -7.156  1.00 80.59      A    C  
ANISOU  698  CA  HIS A 108     8234   9528  12857   1671  -1245   -326  A    C  
ATOM    699  C   HIS A 108      58.515 -17.555  -6.609  1.00 72.53      A    C  
ANISOU  699  C   HIS A 108     7478   8292  11786   1501  -1275   -239  A    C  
ATOM    700  O   HIS A 108      57.669 -16.688  -6.807  1.00 67.01      A    O  
ANISOU  700  O   HIS A 108     6826   7647  10986   1312  -1172   -204  A    O  
ATOM    701  CB  HIS A 108      60.895 -17.153  -5.997  1.00 83.11      A    C  
ANISOU  701  CB  HIS A 108     8446   9916  13216   1680  -1372   -213  A    C  
ATOM    702  CG  HIS A 108      62.277 -16.807  -6.442  1.00 93.15      A    C  
ANISOU  702  CG  HIS A 108     9420  11450  14524   1798  -1334   -280  A    C  
ATOM    703  CD2 HIS A 108      63.314 -17.591  -6.818  1.00 92.82      A    C  
ANISOU  703  CD2 HIS A 108     9217  11469  14582   2059  -1374   -384  A    C  
ATOM    704  ND1 HIS A 108      62.711 -15.503  -6.570  1.00 91.06      A    N  
ANISOU  704  ND1 HIS A 108     8982  11433  14184   1637  -1234   -246  A    N  
ATOM    705  CE1 HIS A 108      63.962 -15.502  -6.995  1.00 91.45      A    C  
ANISOU  705  CE1 HIS A 108     8765  11698  14285   1775  -1213   -321  A    C  
ATOM    706  NE2 HIS A 108      64.350 -16.755  -7.157  1.00 93.72      A    N  
ANISOU  706  NE2 HIS A 108     9043  11885  14679   2043  -1294   -409  A    N  
ATOM    707  N   ASP A 109      58.285 -18.654  -5.902  1.00 71.10      A    N  
ANISOU  707  N   ASP A 109     7469   7869  11676   1575  -1420   -201  A    N  
ATOM    708  CA  ASP A 109      57.056 -18.882  -5.174  1.00 74.56      A    C  
ANISOU  708  CA  ASP A 109     8151   8104  12075   1412  -1469   -100  A    C  
ATOM    709  C   ASP A 109      57.359 -19.621  -3.860  1.00 74.11      A    C  
ANISOU  709  C   ASP A 109     8213   7865  12079   1464  -1658     19  A    C  
ATOM    710  O   ASP A 109      58.192 -20.524  -3.817  1.00 79.47      A    O  
ANISOU  710  O   ASP A 109     8870   8467  12859   1681  -1765    -23  A    O  
ATOM    711  CB  ASP A 109      56.083 -19.680  -6.030  1.00 84.70      A    C  
ANISOU  711  CB  ASP A 109     9584   9236  13363   1420  -1422   -206  A    C  
ATOM    712  CG  ASP A 109      56.497 -21.113  -6.182  1.00 99.71      A    C  
ANISOU  712  CG  ASP A 109    11571  10937  15377   1638  -1531   -289  A    C  
ATOM    713  OD1 ASP A 109      57.436 -21.380  -6.964  1.00114.12      A    O  
ANISOU  713  OD1 ASP A 109    13248  12856  17257   1847  -1504   -418  A    O  
ATOM    714  OD2 ASP A 109      55.882 -21.970  -5.512  1.00103.73      A    O1-
ANISOU  714  OD2 ASP A 109    12303  11194  15915   1601  -1639   -224  A    O1-
ATOM    715  N   LEU A 110      56.679 -19.221  -2.793  1.00 67.96      A    N  
ANISOU  715  N   LEU A 110     7566   7023  11232   1271  -1697    167  A    N  
ATOM    716  CA  LEU A 110      56.919 -19.762  -1.464  1.00 65.65      A    C  
ANISOU  716  CA  LEU A 110     7398   6578  10966   1286  -1872    302  A    C  
ATOM    717  C   LEU A 110      56.999 -21.295  -1.417  1.00 70.41      A    C  
ANISOU  717  C   LEU A 110     8161   6920  11672   1462  -2002    275  A    C  
ATOM    718  O   LEU A 110      57.826 -21.847  -0.691  1.00 72.45      A    O  
ANISOU  718  O   LEU A 110     8429   7106  11991   1606  -2159    335  A    O  
ATOM    719  CB  LEU A 110      55.859 -19.238  -0.498  1.00 65.97      A    C  
ANISOU  719  CB  LEU A 110     7603   6564  10899   1035  -1862    444  A    C  
ATOM    720  CG  LEU A 110      56.274 -19.006   0.949  1.00 68.44      A    C  
ANISOU  720  CG  LEU A 110     7965   6865  11175    980  -1994    603  A    C  
ATOM    721  CD1 LEU A 110      57.655 -18.362   1.019  1.00 73.69      A    C  
ANISOU  721  CD1 LEU A 110     8392   7742  11865   1080  -2034    592  A    C  
ATOM    722  CD2 LEU A 110      55.229 -18.147   1.655  1.00 64.26      A    C  
ANISOU  722  CD2 LEU A 110     7546   6358  10514    724  -1923    707  A    C  
ATOM    723  N   ALA A 111      56.157 -21.987  -2.181  1.00 68.41      A    N  
ANISOU  723  N   ALA A 111     8039   6519  11434   1454  -1947    184  A    N  
ATOM    724  CA  ALA A 111      56.210 -23.452  -2.197  1.00 67.45      A    C  
ANISOU  724  CA  ALA A 111     8097   6122  11408   1615  -2067    146  A    C  
ATOM    725  C   ALA A 111      57.560 -23.966  -2.717  1.00 78.15      A    C  
ANISOU  725  C   ALA A 111     9298   7521  12873   1929  -2125     33  A    C  
ATOM    726  O   ALA A 111      58.140 -24.912  -2.158  1.00 80.00      A    O  
ANISOU  726  O   ALA A 111     9629   7578  13191   2109  -2287     70  A    O  
ATOM    727  CB  ALA A 111      55.068 -24.039  -3.008  1.00 58.25      A    C  
ANISOU  727  CB  ALA A 111     7092   4808  10234   1529  -1992     52  A    C  
ATOM    728  N   GLY A 112      58.048 -23.341  -3.788  1.00 73.86      A    N  
ANISOU  728  N   GLY A 112     8519   7220  12326   2000  -1990   -103  A    N  
ATOM    729  CA  GLY A 112      59.350 -23.665  -4.346  1.00 73.60      A    C  
ANISOU  729  CA  GLY A 112     8290   7293  12383   2288  -2011   -221  A    C  
ATOM    730  C   GLY A 112      60.516 -23.379  -3.411  1.00 79.50      A    C  
ANISOU  730  C   GLY A 112     8879   8161  13167   2389  -2134   -119  A    C  
ATOM    731  O   GLY A 112      61.373 -24.247  -3.190  1.00 84.24      A    O  
ANISOU  731  O   GLY A 112     9467   8673  13867   2648  -2270   -140  A    O  
ATOM    732  N   LEU A 113      60.554 -22.166  -2.862  1.00 72.97      A    N  
ANISOU  732  N   LEU A 113     7934   7534  12256   2192  -2095    -13  A    N  
ATOM    733  CA  LEU A 113      61.636 -21.772  -1.970  1.00 74.11      A    C  
ANISOU  733  CA  LEU A 113     7917   7823  12419   2250  -2213     83  A    C  
ATOM    734  C   LEU A 113      61.677 -22.667  -0.724  1.00 85.35      A    C  
ANISOU  734  C   LEU A 113     9548   9000  13881   2319  -2433    220  A    C  
ATOM    735  O   LEU A 113      62.749 -23.021  -0.228  1.00 92.65      A    O  
ANISOU  735  O   LEU A 113    10366   9961  14875   2518  -2581    249  A    O  
ATOM    736  CB  LEU A 113      61.505 -20.300  -1.581  1.00 70.41      A    C  
ANISOU  736  CB  LEU A 113     7339   7575  11837   1988  -2130    171  A    C  
ATOM    737  CG  LEU A 113      61.415 -19.287  -2.734  1.00 71.80      A    C  
ANISOU  737  CG  LEU A 113     7338   7988  11956   1888  -1915     64  A    C  
ATOM    738  CD1 LEU A 113      60.827 -17.940  -2.286  1.00 58.16      A    C  
ANISOU  738  CD1 LEU A 113     5626   6372  10102   1594  -1833    166  A    C  
ATOM    739  CD2 LEU A 113      62.771 -19.081  -3.391  1.00 71.54      A    C  
ANISOU  739  CD2 LEU A 113     6990   8211  11982   2065  -1880    -40  A    C  
ATOM    740  N   LEU A 114      60.505 -23.046  -0.234  1.00 79.57      A    N  
ANISOU  740  N   LEU A 114     9109   8025  13101   2156  -2455    307  A    N  
ATOM    741  CA  LEU A 114      60.416 -23.862   0.965  1.00 82.04      A    C  
ANISOU  741  CA  LEU A 114     9654   8091  13427   2183  -2651    455  A    C  
ATOM    742  C   LEU A 114      60.781 -25.333   0.709  1.00 91.54      A    C  
ANISOU  742  C   LEU A 114    10985   9042  14752   2469  -2774    390  A    C  
ATOM    743  O   LEU A 114      61.232 -26.038   1.620  1.00 81.21      A    O  
ANISOU  743  O   LEU A 114     9796   7578  13484   2597  -2969    497  A    O  
ATOM    744  CB  LEU A 114      59.016 -23.758   1.577  1.00 81.41      A    C  
ANISOU  744  CB  LEU A 114     9839   7851  13243   1892  -2617    572  A    C  
ATOM    745  CG  LEU A 114      58.681 -22.455   2.302  1.00 78.83      A    C  
ANISOU  745  CG  LEU A 114     9459   7707  12787   1631  -2558    686  A    C  
ATOM    746  CD1 LEU A 114      57.314 -22.545   2.959  1.00 72.85      A    C  
ANISOU  746  CD1 LEU A 114     8970   6775  11934   1382  -2535    799  A    C  
ATOM    747  CD2 LEU A 114      59.751 -22.118   3.327  1.00 81.05      A    C  
ANISOU  747  CD2 LEU A 114     9633   8103  13059   1693  -2711    794  A    C  
ATOM    748  N   SER A 115      60.579 -25.795  -0.523  1.00 94.63      A    N  
ANISOU  748  N   SER A 115    11370   9387  15197   2572  -2665    214  A    N  
ATOM    749  CA  SER A 115      60.927 -27.164  -0.879  1.00 92.96      A    C  
ANISOU  749  CA  SER A 115    11289   8931  15101   2856  -2767    125  A    C  
ATOM    750  C   SER A 115      62.373 -27.225  -1.363  1.00100.65      A    C  
ANISOU  750  C   SER A 115    11973  10100  16170   3182  -2795      9  A    C  
ATOM    751  O   SER A 115      62.788 -28.196  -2.000  1.00105.25      A    O  
ANISOU  751  O   SER A 115    12589  10552  16850   3459  -2828   -125  A    O  
ATOM    752  CB  SER A 115      59.989 -27.704  -1.957  1.00 88.94      A    C  
ANISOU  752  CB  SER A 115    10936   8262  14596   2809  -2646    -21  A    C  
ATOM    753  OG  SER A 115      60.375 -27.238  -3.241  1.00 91.66      A    O  
ANISOU  753  OG  SER A 115    11032   8846  14950   2899  -2481   -210  A    O  
ATOM    754  N   ASN A 116      63.135 -26.181  -1.059  1.00100.19      A    N  
ANISOU  754  N   ASN A 116    11629  10360  16080   3146  -2779     55  A    N  
ATOM    755  CA  ASN A 116      64.532 -26.107  -1.465  1.00106.34      A    C  
ANISOU  755  CA  ASN A 116    12085  11380  16939   3422  -2795    -45  A    C  
ATOM    756  C   ASN A 116      65.472 -26.000  -0.259  1.00114.28      A    C  
ANISOU  756  C   ASN A 116    12987  12470  17965   3510  -2996    103  A    C  
ATOM    757  O   ASN A 116      65.547 -24.953   0.394  1.00114.76      A    O  
ANISOU  757  O   ASN A 116    12935  12727  17943   3293  -2994    215  A    O  
ATOM    758  CB  ASN A 116      64.740 -24.931  -2.420  1.00102.18      A    C  
ANISOU  758  CB  ASN A 116    11256  11208  16358   3308  -2577   -155  A    C  
ATOM    759  CG  ASN A 116      66.093 -24.962  -3.101  1.00106.41      A    C  
ANISOU  759  CG  ASN A 116    11454  11999  16976   3594  -2551   -295  A    C  
ATOM    760  ND2 ASN A 116      66.117 -24.584  -4.371  1.00103.83      A    N  
ANISOU  760  ND2 ASN A 116    10968  11853  16630   3596  -2346   -460  A    N  
ATOM    761  OD1 ASN A 116      67.107 -25.314  -2.493  1.00110.78      A    O  
ANISOU  761  OD1 ASN A 116    11884  12601  17605   3812  -2713   -254  A    O  
ATOM    762  N   VAL A 117      66.188 -27.086   0.028  1.00110.73      A    N  
ANISOU  762  N   VAL A 117    12584  11867  17622   3834  -3177     98  A    N  
ATOM    763  CA  VAL A 117      67.047 -27.148   1.206  1.00111.92      A    C  
ANISOU  763  CA  VAL A 117    12668  12064  17792   3946  -3401    246  A    C  
ATOM    764  C   VAL A 117      68.141 -26.077   1.217  1.00111.61      A    C  
ANISOU  764  C   VAL A 117    12206  12457  17744   3944  -3374    230  A    C  
ATOM    765  O   VAL A 117      68.570 -25.637   2.284  1.00115.51      A    O  
ANISOU  765  O   VAL A 117    12637  13055  18196   3870  -3519    378  A    O  
ATOM    766  CB  VAL A 117      67.689 -28.546   1.375  1.00115.89      A    C  
ANISOU  766  CB  VAL A 117    13283  12330  18421   4345  -3600    226  A    C  
ATOM    767  CG1 VAL A 117      66.612 -29.601   1.588  1.00117.56      A    C  
ANISOU  767  CG1 VAL A 117    13953  12084  18631   4306  -3661    280  A    C  
ATOM    768  CG2 VAL A 117      68.557 -28.889   0.171  1.00111.16      A    C  
ANISOU  768  CG2 VAL A 117    12423  11882  17932   4674  -3511      0  A    C  
ATOM    769  N   LEU A 118      68.586 -25.658   0.036  1.00106.01      A    N  
ANISOU  769  N   LEU A 118    11213  12001  17064   4010  -3189     51  A    N  
ATOM    770  CA  LEU A 118      69.630 -24.640  -0.063  1.00106.01      A    C  
ANISOU  770  CA  LEU A 118    10801  12423  17056   3987  -3142     25  A    C  
ATOM    771  C   LEU A 118      69.113 -23.266   0.348  1.00105.62      A    C  
ANISOU  771  C   LEU A 118    10729  12532  16871   3577  -3050    131  A    C  
ATOM    772  O   LEU A 118      69.870 -22.439   0.852  1.00108.98      A    O  
ANISOU  772  O   LEU A 118    10912  13230  17267   3491  -3099    191  A    O  
ATOM    773  CB  LEU A 118      70.209 -24.583  -1.481  1.00112.09      A    C  
ANISOU  773  CB  LEU A 118    11288  13420  17881   4156  -2951   -194  A    C  
ATOM    774  CG  LEU A 118      70.922 -25.839  -2.004  1.00116.13      A    C  
ANISOU  774  CG  LEU A 118    11753  13841  18529   4602  -3020   -334  A    C  
ATOM    775  CD1 LEU A 118      71.402 -25.632  -3.438  1.00116.82      A    C  
ANISOU  775  CD1 LEU A 118    11561  14186  18640   4721  -2794   -554  A    C  
ATOM    776  CD2 LEU A 118      72.081 -26.252  -1.091  1.00108.83      A    C  
ANISOU  776  CD2 LEU A 118    10667  12996  17689   4868  -3266   -255  A    C  
ATOM    777  N   VAL A 119      67.821 -23.034   0.121  1.00103.14      A    N  
ANISOU  777  N   VAL A 119    10670  12046  16474   3329  -2920    146  A    N  
ATOM    778  CA  VAL A 119      67.162 -21.785   0.489  1.00 91.89      A    C  
ANISOU  778  CA  VAL A 119     9276  10723  14916   2954  -2825    241  A    C  
ATOM    779  C   VAL A 119      66.974 -21.724   1.997  1.00 95.61      A    C  
ANISOU  779  C   VAL A 119     9925  11076  15326   2827  -3018    442  A    C  
ATOM    780  O   VAL A 119      66.470 -22.676   2.592  1.00 98.73      A    O  
ANISOU  780  O   VAL A 119    10607  11169  15736   2896  -3149    522  A    O  
ATOM    781  CB  VAL A 119      65.764 -21.694  -0.157  1.00 84.12      A    C  
ANISOU  781  CB  VAL A 119     8528   9569  13865   2760  -2648    201  A    C  
ATOM    782  CG1 VAL A 119      65.082 -20.401   0.240  1.00 69.37      A    C  
ANISOU  782  CG1 VAL A 119     6694   7802  11861   2402  -2552    296  A    C  
ATOM    783  CG2 VAL A 119      65.854 -21.831  -1.672  1.00 83.03      A    C  
ANISOU  783  CG2 VAL A 119     8254   9523  13770   2884  -2462      1  A    C  
ATOM    784  N   LYS A 120      67.358 -20.611   2.617  1.00 97.12      A    N  
ANISOU  784  N   LYS A 120     9966  11497  15438   2629  -3034    523  A    N  
ATOM    785  CA  LYS A 120      67.288 -20.511   4.076  1.00102.53      A    C  
ANISOU  785  CA  LYS A 120    10806  12102  16051   2515  -3225    707  A    C  
ATOM    786  C   LYS A 120      66.784 -19.147   4.563  1.00104.84      A    C  
ANISOU  786  C   LYS A 120    11121  12517  16197   2153  -3137    785  A    C  
ATOM    787  O   LYS A 120      67.338 -18.103   4.208  1.00100.92      A    O  
ANISOU  787  O   LYS A 120    10369  12301  15673   2041  -3043    734  A    O  
ATOM    788  CB  LYS A 120      68.656 -20.836   4.693  1.00104.34      A    C  
ANISOU  788  CB  LYS A 120    10821  12474  16349   2742  -3446    744  A    C  
ATOM    789  CG  LYS A 120      68.598 -21.475   6.077  1.00108.58      A    C  
ANISOU  789  CG  LYS A 120    11596  12805  16853   2782  -3700    920  A    C  
ATOM    790  CD  LYS A 120      69.917 -22.167   6.415  1.00114.66      A    C  
ANISOU  790  CD  LYS A 120    12172  13666  17729   3113  -3927    927  A    C  
ATOM    791  CE  LYS A 120      69.802 -23.058   7.652  1.00116.55      A    C  
ANISOU  791  CE  LYS A 120    12698  13641  17945   3211  -4187   1100  A    C  
ATOM    792  NZ  LYS A 120      71.049 -23.843   7.914  1.00117.30      A    N1+
ANISOU  792  NZ  LYS A 120    12618  13799  18151   3580  -4417   1103  A    N1+
ATOM    793  N   PHE A 121      65.729 -19.165   5.375  1.00106.39      A    N  
ANISOU  793  N   PHE A 121    11631  12498  16294   1970  -3164    907  A    N  
ATOM    794  CA  PHE A 121      65.184 -17.939   5.955  1.00101.86      A    C  
ANISOU  794  CA  PHE A 121    11120  12009  15574   1647  -3093    985  A    C  
ATOM    795  C   PHE A 121      65.668 -17.766   7.395  1.00 99.74      A    C  
ANISOU  795  C   PHE A 121    10897  11769  15231   1588  -3308   1135  A    C  
ATOM    796  O   PHE A 121      65.728 -18.735   8.159  1.00 99.59      A    O  
ANISOU  796  O   PHE A 121    11041  11569  15230   1722  -3495   1230  A    O  
ATOM    797  CB  PHE A 121      63.648 -17.965   5.967  1.00100.44      A    C  
ANISOU  797  CB  PHE A 121    11245  11605  15311   1464  -2969   1021  A    C  
ATOM    798  CG  PHE A 121      63.010 -18.055   4.601  1.00105.13      A    C  
ANISOU  798  CG  PHE A 121    11823  12170  15953   1482  -2761    882  A    C  
ATOM    799  CD1 PHE A 121      62.736 -16.908   3.867  1.00 97.60      A    C  
ANISOU  799  CD1 PHE A 121    10750  11392  14941   1313  -2561    810  A    C  
ATOM    800  CD2 PHE A 121      62.645 -19.285   4.069  1.00105.63      A    C  
ANISOU  800  CD2 PHE A 121    12013  12016  16106   1661  -2771    827  A    C  
ATOM    801  CE1 PHE A 121      62.137 -16.990   2.624  1.00 84.33      A    C  
ANISOU  801  CE1 PHE A 121     9062   9690  13289   1331  -2382    689  A    C  
ATOM    802  CE2 PHE A 121      62.043 -19.368   2.825  1.00 96.83      A    C  
ANISOU  802  CE2 PHE A 121    10891  10879  15020   1668  -2589    695  A    C  
ATOM    803  CZ  PHE A 121      61.794 -18.219   2.103  1.00 83.85      A    C  
ANISOU  803  CZ  PHE A 121     9114   9430  13314   1506  -2397    628  A    C  
ATOM    804  N   THR A 122      66.007 -16.533   7.760  1.00 91.73      A    N  
ANISOU  804  N   THR A 122     9754  10974  14125   1382  -3285   1156  A    N  
ATOM    805  CA  THR A 122      66.232 -16.189   9.159  1.00 88.96      A    C  
ANISOU  805  CA  THR A 122     9495  10644  13663   1259  -3463   1296  A    C  
ATOM    806  C   THR A 122      64.889 -15.873   9.809  1.00 88.65      A    C  
ANISOU  806  C   THR A 122     9786  10419  13478   1020  -3389   1386  A    C  
ATOM    807  O   THR A 122      63.900 -15.630   9.112  1.00 92.98      A    O  
ANISOU  807  O   THR A 122    10426  10892  14010    920  -3185   1329  A    O  
ATOM    808  CB  THR A 122      67.156 -14.959   9.313  1.00 92.06      A    C  
ANISOU  808  CB  THR A 122     9625  11346  14009   1113  -3473   1273  A    C  
ATOM    809  CG2 THR A 122      68.502 -15.200   8.629  1.00 90.13      A    C  
ANISOU  809  CG2 THR A 122     9012  11329  13905   1333  -3526   1177  A    C  
ATOM    810  OG1 THR A 122      66.524 -13.796   8.754  1.00 85.28      A    O  
ANISOU  810  OG1 THR A 122     8771  10557  13073    869  -3244   1214  A    O  
ATOM    811  N   LEU A 123      64.845 -15.868  11.137  1.00 80.69      A    N  
ANISOU  811  N   LEU A 123     8949   9352  12356    932  -3552   1525  A    N  
ATOM    812  CA  LEU A 123      63.623 -15.496  11.839  1.00 84.20      A    C  
ANISOU  812  CA  LEU A 123     9691   9656  12646    699  -3477   1610  A    C  
ATOM    813  C   LEU A 123      63.129 -14.122  11.377  1.00 86.06      A    C  
ANISOU  813  C   LEU A 123     9874  10023  12803    465  -3258   1535  A    C  
ATOM    814  O   LEU A 123      61.928 -13.867  11.295  1.00 86.77      A    O  
ANISOU  814  O   LEU A 123    10151   9999  12818    325  -3101   1539  A    O  
ATOM    815  CB  LEU A 123      63.854 -15.476  13.349  1.00 85.31      A    C  
ANISOU  815  CB  LEU A 123     9983   9778  12654    622  -3684   1759  A    C  
ATOM    816  CG  LEU A 123      62.670 -14.996  14.194  1.00 87.58      A    C  
ANISOU  816  CG  LEU A 123    10566   9954  12757    373  -3606   1846  A    C  
ATOM    817  CD1 LEU A 123      61.487 -15.941  14.053  1.00 87.14      A    C  
ANISOU  817  CD1 LEU A 123    10760   9636  12712    396  -3525   1886  A    C  
ATOM    818  CD2 LEU A 123      63.063 -14.851  15.654  1.00 85.84      A    C  
ANISOU  818  CD2 LEU A 123    10467   9760  12389    293  -3813   1980  A    C  
ATOM    819  N   SER A 124      64.076 -13.244  11.071  1.00 84.90      A    N  
ANISOU  819  N   SER A 124     9468  10118  12673    427  -3253   1468  A    N  
ATOM    820  CA  SER A 124      63.782 -11.865  10.727  1.00 78.86      A    C  
ANISOU  820  CA  SER A 124     8659   9479  11826    202  -3074   1409  A    C  
ATOM    821  C   SER A 124      63.053 -11.754   9.383  1.00 83.68      A    C  
ANISOU  821  C   SER A 124     9240  10057  12499    214  -2835   1301  A    C  
ATOM    822  O   SER A 124      62.179 -10.901   9.191  1.00 71.99      A    O  
ANISOU  822  O   SER A 124     7866   8558  10928     39  -2666   1282  A    O  
ATOM    823  CB  SER A 124      65.089 -11.074  10.678  1.00 76.03      A    C  
ANISOU  823  CB  SER A 124     8017   9387  11484    160  -3142   1366  A    C  
ATOM    824  OG  SER A 124      64.840  -9.698  10.461  1.00 81.77      A    O  
ANISOU  824  OG  SER A 124     8737  10213  12117    -77  -2988   1322  A    O  
ATOM    825  N   GLU A 125      63.431 -12.616   8.449  1.00 88.58      A    N  
ANISOU  825  N   GLU A 125     9715  10672  13267    432  -2826   1226  A    N  
ATOM    826  CA  GLU A 125      62.860 -12.583   7.114  1.00 87.01      A    C  
ANISOU  826  CA  GLU A 125     9472  10461  13128    462  -2616   1115  A    C  
ATOM    827  C   GLU A 125      61.495 -13.273   7.106  1.00 80.98      A    C  
ANISOU  827  C   GLU A 125     8976   9451  12343    459  -2549   1143  A    C  
ATOM    828  O   GLU A 125      60.546 -12.794   6.477  1.00 73.32      A    O  
ANISOU  828  O   GLU A 125     8073   8454  11331    355  -2365   1097  A    O  
ATOM    829  CB  GLU A 125      63.831 -13.222   6.119  1.00 92.42      A    C  
ANISOU  829  CB  GLU A 125     9897  11250  13967    697  -2628   1011  A    C  
ATOM    830  CG  GLU A 125      65.136 -12.445   5.971  1.00 95.11      A    C  
ANISOU  830  CG  GLU A 125     9935  11875  14328    673  -2658    970  A    C  
ATOM    831  CD  GLU A 125      66.312 -13.322   5.569  1.00102.74      A    C  
ANISOU  831  CD  GLU A 125    10652  12946  15440    945  -2767    911  A    C  
ATOM    832  OE1 GLU A 125      66.433 -14.451   6.095  1.00102.03      A    O  
ANISOU  832  OE1 GLU A 125    10649  12711  15409   1137  -2934    961  A    O  
ATOM    833  OE2 GLU A 125      67.124 -12.872   4.731  1.00107.92      A    O1-
ANISOU  833  OE2 GLU A 125    11027  13832  16148    970  -2683    815  A    O1-
ATOM    834  N   ILE A 126      61.401 -14.388   7.821  1.00 81.36      A    N  
ANISOU  834  N   ILE A 126     9177   9323  12415    567  -2704   1226  A    N  
ATOM    835  CA  ILE A 126      60.125 -15.058   8.006  1.00 72.36      A    C  
ANISOU  835  CA  ILE A 126     8305   7949  11241    528  -2660   1274  A    C  
ATOM    836  C   ILE A 126      59.115 -14.048   8.547  1.00 75.64      A    C  
ANISOU  836  C   ILE A 126     8874   8368  11497    273  -2544   1325  A    C  
ATOM    837  O   ILE A 126      57.972 -14.001   8.090  1.00 75.66      A    O  
ANISOU  837  O   ILE A 126     8985   8289  11471    195  -2391   1297  A    O  
ATOM    838  CB  ILE A 126      60.244 -16.259   8.956  1.00 70.93      A    C  
ANISOU  838  CB  ILE A 126     8296   7579  11076    638  -2865   1388  A    C  
ATOM    839  CG1 ILE A 126      61.085 -17.366   8.322  1.00 78.18      A    C  
ANISOU  839  CG1 ILE A 126     9092   8452  12159    922  -2966   1325  A    C  
ATOM    840  CG2 ILE A 126      58.871 -16.806   9.315  1.00 64.28      A    C  
ANISOU  840  CG2 ILE A 126     7746   6509  10168    532  -2812   1458  A    C  
ATOM    841  CD1 ILE A 126      61.144 -18.648   9.158  1.00 74.91      A    C  
ANISOU  841  CD1 ILE A 126     8882   7811  11770   1054  -3169   1439  A    C  
ATOM    842  N   LYS A 127      59.541 -13.225   9.504  1.00 78.86      A    N  
ANISOU  842  N   LYS A 127     9286   8880  11799    149  -2618   1392  A    N  
ATOM    843  CA  LYS A 127      58.691 -12.148  10.012  1.00 77.23      A    C  
ANISOU  843  CA  LYS A 127     9216   8693  11436    -78  -2504   1423  A    C  
ATOM    844  C   LYS A 127      58.230 -11.232   8.887  1.00 77.27      A    C  
ANISOU  844  C   LYS A 127     9125   8789  11445   -146  -2286   1314  A    C  
ATOM    845  O   LYS A 127      57.060 -10.840   8.818  1.00 76.55      A    O  
ANISOU  845  O   LYS A 127     9171   8640  11275   -258  -2142   1313  A    O  
ATOM    846  CB  LYS A 127      59.428 -11.309  11.054  1.00 72.09      A    C  
ANISOU  846  CB  LYS A 127     8552   8163  10678   -193  -2619   1482  A    C  
ATOM    847  CG  LYS A 127      59.302 -11.830  12.457  1.00 72.26      A    C  
ANISOU  847  CG  LYS A 127     8781   8075  10598   -226  -2784   1617  A    C  
ATOM    848  CD  LYS A 127      60.091 -10.981  13.426  1.00 71.20      A    C  
ANISOU  848  CD  LYS A 127     8623   8076  10353   -340  -2907   1660  A    C  
ATOM    849  CE  LYS A 127      60.204 -11.688  14.765  1.00 77.82      A    C  
ANISOU  849  CE  LYS A 127     9644   8820  11105   -329  -3111   1799  A    C  
ATOM    850  NZ  LYS A 127      60.615 -10.751  15.842  1.00 85.90      A    N1+
ANISOU  850  NZ  LYS A 127    10718   9953  11967   -493  -3203   1844  A    N1+
ATOM    851  N   ARG A 128      59.162 -10.882   8.009  1.00 68.55      A    N  
ANISOU  851  N   ARG A 128     7781   7838  10426    -77  -2262   1224  A    N  
ATOM    852  CA  ARG A 128      58.864  -9.948   6.944  1.00 70.59      A    C  
ANISOU  852  CA  ARG A 128     7948   8195  10678   -145  -2067   1130  A    C  
ATOM    853  C   ARG A 128      57.868 -10.556   5.968  1.00 68.32      A    C  
ANISOU  853  C   ARG A 128     7713   7803  10445    -72  -1935   1072  A    C  
ATOM    854  O   ARG A 128      56.888  -9.908   5.584  1.00 60.39      A    O  
ANISOU  854  O   ARG A 128     6786   6788   9372   -173  -1779   1048  A    O  
ATOM    855  CB  ARG A 128      60.146  -9.537   6.227  1.00 73.67      A    C  
ANISOU  855  CB  ARG A 128     8065   8781  11144    -92  -2073   1055  A    C  
ATOM    856  CG  ARG A 128      59.949  -8.439   5.213  1.00 67.70      A    C  
ANISOU  856  CG  ARG A 128     7228   8135  10359   -189  -1880    976  A    C  
ATOM    857  CD  ARG A 128      59.510  -7.140   5.861  1.00 68.42      A    C  
ANISOU  857  CD  ARG A 128     7455   8240  10302   -406  -1824   1019  A    C  
ATOM    858  NE  ARG A 128      59.180  -6.157   4.831  1.00 67.48      A    N  
ANISOU  858  NE  ARG A 128     7298   8189  10154   -482  -1636    951  A    N  
ATOM    859  CZ  ARG A 128      57.959  -5.689   4.598  1.00 62.99      A    C  
ANISOU  859  CZ  ARG A 128     6888   7536   9508   -545  -1496    948  A    C  
ATOM    860  NH1 ARG A 128      56.931  -6.081   5.348  1.00 62.69      A    N1+
ANISOU  860  NH1 ARG A 128     7049   7356   9413   -558  -1511   1004  A    N1+
ATOM    861  NH2 ARG A 128      57.772  -4.812   3.622  1.00 56.31      A    N  
ANISOU  861  NH2 ARG A 128     6001   6757   8638   -595  -1342    892  A    N  
ATOM    862  N   VAL A 129      58.124 -11.804   5.577  1.00 67.03      A    N  
ANISOU  862  N   VAL A 129     7509   7559  10401    108  -2007   1045  A    N  
ATOM    863  CA  VAL A 129      57.230 -12.535   4.688  1.00 65.18      A    C  
ANISOU  863  CA  VAL A 129     7334   7209  10221    178  -1909    984  A    C  
ATOM    864  C   VAL A 129      55.791 -12.545   5.222  1.00 68.84      A    C  
ANISOU  864  C   VAL A 129     8031   7537  10588     42  -1846   1049  A    C  
ATOM    865  O   VAL A 129      54.851 -12.164   4.522  1.00 66.87      A    O  
ANISOU  865  O   VAL A 129     7806   7294  10307    -19  -1691    998  A    O  
ATOM    866  CB  VAL A 129      57.730 -13.982   4.451  1.00 67.45      A    C  
ANISOU  866  CB  VAL A 129     7598   7386  10643    391  -2029    960  A    C  
ATOM    867  CG1 VAL A 129      56.602 -14.870   3.901  1.00 70.79      A    C  
ANISOU  867  CG1 VAL A 129     8167   7631  11097    418  -1962    926  A    C  
ATOM    868  CG2 VAL A 129      58.922 -13.978   3.507  1.00 57.86      A    C  
ANISOU  868  CG2 VAL A 129     6123   6329   9532    548  -2025    853  A    C  
ATOM    869  N   MET A 130      55.625 -12.970   6.469  1.00 68.44      A    N  
ANISOU  869  N   MET A 130     8145   7377  10483     -6  -1966   1164  A    N  
ATOM    870  CA  MET A 130      54.305 -12.996   7.085  1.00 66.71      A    C  
ANISOU  870  CA  MET A 130     8137   7048  10160   -145  -1905   1233  A    C  
ATOM    871  C   MET A 130      53.665 -11.607   7.147  1.00 72.59      A    C  
ANISOU  871  C   MET A 130     8897   7902  10780   -303  -1756   1223  A    C  
ATOM    872  O   MET A 130      52.440 -11.464   7.060  1.00 72.41      A    O  
ANISOU  872  O   MET A 130     8975   7840  10696   -388  -1635   1223  A    O  
ATOM    873  CB  MET A 130      54.380 -13.616   8.478  1.00 64.76      A    C  
ANISOU  873  CB  MET A 130     8062   6685   9857   -176  -2064   1367  A    C  
ATOM    874  CG  MET A 130      54.656 -15.113   8.454  1.00 76.09      A    C  
ANISOU  874  CG  MET A 130     9554   7953  11404    -27  -2200   1393  A    C  
ATOM    875  SD  MET A 130      53.676 -15.957   7.191  1.00 77.23      A    S  
ANISOU  875  SD  MET A 130     9722   7978  11643     22  -2077   1296  A    S  
ATOM    876  CE  MET A 130      52.011 -15.556   7.718  1.00 52.82      A    C  
ANISOU  876  CE  MET A 130     6812   4850   8406   -211  -1936   1358  A    C  
ATOM    877  N   GLN A 131      54.499 -10.586   7.293  1.00 68.89      A    N  
ANISOU  877  N   GLN A 131     8328   7571  10274   -340  -1768   1211  A    N  
ATOM    878  CA  GLN A 131      54.020  -9.218   7.372  1.00 56.59      A    C  
ANISOU  878  CA  GLN A 131     6804   6100   8599   -479  -1640   1199  A    C  
ATOM    879  C   GLN A 131      53.445  -8.791   6.028  1.00 56.16      A    C  
ANISOU  879  C   GLN A 131     6665   6096   8576   -457  -1467   1101  A    C  
ATOM    880  O   GLN A 131      52.354  -8.220   5.956  1.00 51.90      A    O  
ANISOU  880  O   GLN A 131     6216   5550   7955   -535  -1339   1096  A    O  
ATOM    881  CB  GLN A 131      55.153  -8.282   7.784  1.00 64.36      A    C  
ANISOU  881  CB  GLN A 131     7704   7207   9545   -534  -1708   1204  A    C  
ATOM    882  CG  GLN A 131      54.700  -6.877   8.122  1.00 68.08      A    C  
ANISOU  882  CG  GLN A 131     8262   7730   9876   -688  -1602   1204  A    C  
ATOM    883  CD  GLN A 131      55.810  -6.046   8.725  1.00 67.29      A    C  
ANISOU  883  CD  GLN A 131     8112   7729   9725   -771  -1696   1218  A    C  
ATOM    884  NE2 GLN A 131      55.581  -5.544   9.929  1.00 59.10      A    N  
ANISOU  884  NE2 GLN A 131     7243   6664   8550   -891  -1739   1280  A    N  
ATOM    885  OE1 GLN A 131      56.864  -5.859   8.116  1.00 64.40      A    O  
ANISOU  885  OE1 GLN A 131     7558   7472   9438   -736  -1728   1171  A    O  
ATOM    886  N   MET A 132      54.175  -9.070   4.957  1.00 55.31      A    N  
ANISOU  886  N   MET A 132     6383   6049   8582   -343  -1464   1021  A    N  
ATOM    887  CA  MET A 132      53.696  -8.712   3.634  1.00 55.65      A    C  
ANISOU  887  CA  MET A 132     6349   6148   8647   -316  -1310    929  A    C  
ATOM    888  C   MET A 132      52.416  -9.499   3.308  1.00 60.15      A    C  
ANISOU  888  C   MET A 132     7018   6608   9228   -296  -1251    918  A    C  
ATOM    889  O   MET A 132      51.446  -8.936   2.813  1.00 55.32      A    O  
ANISOU  889  O   MET A 132     6439   6021   8559   -346  -1119    889  A    O  
ATOM    890  CB  MET A 132      54.781  -8.966   2.587  1.00 54.91      A    C  
ANISOU  890  CB  MET A 132     6051   6149   8664   -193  -1320    845  A    C  
ATOM    891  CG  MET A 132      55.999  -8.053   2.718  1.00 62.69      A    C  
ANISOU  891  CG  MET A 132     6904   7280   9635   -239  -1350    845  A    C  
ATOM    892  SD  MET A 132      57.362  -8.526   1.614  1.00 66.04      A    S  
ANISOU  892  SD  MET A 132     7060   7838  10193    -83  -1370    749  A    S  
ATOM    893  CE  MET A 132      57.133  -7.331   0.305  1.00 92.26      A    C  
ANISOU  893  CE  MET A 132    10309  11288  13459   -155  -1167    675  A    C  
ATOM    894  N   LEU A 133      52.423 -10.797   3.601  1.00 54.19      A    N  
ANISOU  894  N   LEU A 133     6314   5730   8545   -226  -1356    942  A    N  
ATOM    895  CA  LEU A 133      51.287 -11.656   3.312  1.00 55.40      A    C  
ANISOU  895  CA  LEU A 133     6562   5770   8717   -227  -1317    931  A    C  
ATOM    896  C   LEU A 133      50.039 -11.139   4.018  1.00 58.22      A    C  
ANISOU  896  C   LEU A 133     7058   6111   8949   -374  -1237    995  A    C  
ATOM    897  O   LEU A 133      49.008 -10.920   3.387  1.00 59.30      A    O  
ANISOU  897  O   LEU A 133     7199   6275   9059   -407  -1116    951  A    O  
ATOM    898  CB  LEU A 133      51.590 -13.101   3.715  1.00 57.89      A    C  
ANISOU  898  CB  LEU A 133     6947   5930   9120   -145  -1462    966  A    C  
ATOM    899  CG  LEU A 133      50.640 -14.207   3.247  1.00 68.96      A    C  
ANISOU  899  CG  LEU A 133     8437   7194  10570   -134  -1444    937  A    C  
ATOM    900  CD1 LEU A 133      51.376 -15.525   3.133  1.00 71.41      A    C  
ANISOU  900  CD1 LEU A 133     8761   7367  11003     13  -1581    921  A    C  
ATOM    901  CD2 LEU A 133      49.466 -14.346   4.193  1.00 73.75      A    C  
ANISOU  901  CD2 LEU A 133     9220   7719  11083   -290  -1424   1034  A    C  
ATOM    902  N   LEU A 134      50.146 -10.921   5.323  1.00 56.98      A    N  
ANISOU  902  N   LEU A 134     7011   5927   8712   -455  -1304   1094  A    N  
ATOM    903  CA  LEU A 134      49.032 -10.416   6.114  1.00 50.50      A    C  
ANISOU  903  CA  LEU A 134     6323   5104   7760   -588  -1225   1154  A    C  
ATOM    904  C   LEU A 134      48.584  -9.035   5.641  1.00 48.50      A    C  
ANISOU  904  C   LEU A 134     6024   4973   7429   -628  -1077   1102  A    C  
ATOM    905  O   LEU A 134      47.393  -8.703   5.684  1.00 51.05      A    O  
ANISOU  905  O   LEU A 134     6405   5314   7677   -689   -965   1104  A    O  
ATOM    906  CB  LEU A 134      49.396 -10.395   7.602  1.00 52.15      A    C  
ANISOU  906  CB  LEU A 134     6660   5271   7883   -661  -1332   1264  A    C  
ATOM    907  CG  LEU A 134      49.458 -11.783   8.257  1.00 57.75      A    C  
ANISOU  907  CG  LEU A 134     7477   5832   8634   -646  -1466   1345  A    C  
ATOM    908  CD1 LEU A 134      50.024 -11.702   9.655  1.00 57.26      A    C  
ANISOU  908  CD1 LEU A 134     7528   5746   8481   -701  -1591   1453  A    C  
ATOM    909  CD2 LEU A 134      48.072 -12.449   8.268  1.00 50.72      A    C  
ANISOU  909  CD2 LEU A 134     6690   4861   7718   -725  -1386   1368  A    C  
ATOM    910  N   ASN A 135      49.534  -8.242   5.166  1.00 45.12      A    N  
ANISOU  910  N   ASN A 135     5490   4632   7019   -590  -1075   1057  A    N  
ATOM    911  CA  ASN A 135      49.216  -6.920   4.640  1.00 43.90      A    C  
ANISOU  911  CA  ASN A 135     5310   4575   6796   -621   -943   1011  A    C  
ATOM    912  C   ASN A 135      48.458  -7.002   3.310  1.00 47.34      A    C  
ANISOU  912  C   ASN A 135     5669   5045   7272   -561   -831    932  A    C  
ATOM    913  O   ASN A 135      47.566  -6.204   3.043  1.00 50.23      A    O  
ANISOU  913  O   ASN A 135     6065   5458   7562   -587   -713    916  A    O  
ATOM    914  CB  ASN A 135      50.482  -6.080   4.476  1.00 43.74      A    C  
ANISOU  914  CB  ASN A 135     5202   4634   6781   -622   -975    990  A    C  
ATOM    915  CG  ASN A 135      50.177  -4.593   4.332  1.00 54.88      A    C  
ANISOU  915  CG  ASN A 135     6656   6108   8088   -688   -859    973  A    C  
ATOM    916  ND2 ASN A 135      50.944  -3.908   3.498  1.00 48.55      A    N  
ANISOU  916  ND2 ASN A 135     5750   5385   7312   -676   -826    925  A    N  
ATOM    917  OD1 ASN A 135      49.248  -4.076   4.954  1.00 55.87      A    O  
ANISOU  917  OD1 ASN A 135     6911   6208   8108   -746   -795   1001  A    O  
ATOM    918  N   GLY A 136      48.822  -7.968   2.476  1.00 47.79      A    N  
ANISOU  918  N   GLY A 136     5631   5081   7444   -470   -872    881  A    N  
ATOM    919  CA  GLY A 136      48.073  -8.244   1.268  1.00 47.77      A    C  
ANISOU  919  CA  GLY A 136     5571   5102   7476   -419   -786    804  A    C  
ATOM    920  C   GLY A 136      46.641  -8.661   1.593  1.00 54.16      A    C  
ANISOU  920  C   GLY A 136     6472   5865   8241   -480   -742    830  A    C  
ATOM    921  O   GLY A 136      45.679  -8.135   1.023  1.00 54.48      A    O  
ANISOU  921  O   GLY A 136     6498   5972   8231   -489   -633    797  A    O  
ATOM    922  N   LEU A 137      46.494  -9.602   2.519  1.00 43.00      A    N  
ANISOU  922  N   LEU A 137     5150   4345   6843   -524   -827    895  A    N  
ATOM    923  CA  LEU A 137      45.174 -10.049   2.939  1.00 48.35      A    C  
ANISOU  923  CA  LEU A 137     5912   4985   7474   -609   -784    930  A    C  
ATOM    924  C   LEU A 137      44.321  -8.898   3.470  1.00 53.18      A    C  
ANISOU  924  C   LEU A 137     6569   5685   7953   -680   -673    961  A    C  
ATOM    925  O   LEU A 137      43.147  -8.779   3.133  1.00 56.01      A    O  
ANISOU  925  O   LEU A 137     6910   6097   8272   -707   -578    939  A    O  
ATOM    926  CB  LEU A 137      45.288 -11.156   3.987  1.00 50.77      A    C  
ANISOU  926  CB  LEU A 137     6335   5155   7800   -662   -897   1015  A    C  
ATOM    927  CG  LEU A 137      45.739 -12.490   3.387  1.00 54.59      A    C  
ANISOU  927  CG  LEU A 137     6802   5525   8416   -587   -994    976  A    C  
ATOM    928  CD1 LEU A 137      45.910 -13.539   4.480  1.00 54.72      A    C  
ANISOU  928  CD1 LEU A 137     6961   5385   8445   -633  -1118   1076  A    C  
ATOM    929  CD2 LEU A 137      44.763 -12.966   2.291  1.00 47.96      A    C  
ANISOU  929  CD2 LEU A 137     5914   4693   7614   -590   -922    892  A    C  
ATOM    930  N   TYR A 138      44.913  -8.043   4.293  1.00 51.15      A    N  
ANISOU  930  N   TYR A 138     6366   5444   7624   -706   -687   1007  A    N  
ATOM    931  CA  TYR A 138      44.175  -6.924   4.849  1.00 41.91      A    C  
ANISOU  931  CA  TYR A 138     5260   4340   6322   -757   -584   1028  A    C  
ATOM    932  C   TYR A 138      43.604  -6.095   3.710  1.00 49.55      A    C  
ANISOU  932  C   TYR A 138     6144   5405   7278   -695   -466    953  A    C  
ATOM    933  O   TYR A 138      42.450  -5.661   3.750  1.00 47.14      A    O  
ANISOU  933  O   TYR A 138     5854   5159   6898   -708   -364    948  A    O  
ATOM    934  CB  TYR A 138      45.097  -6.055   5.704  1.00 47.18      A    C  
ANISOU  934  CB  TYR A 138     5997   5006   6922   -787   -627   1065  A    C  
ATOM    935  CG  TYR A 138      44.486  -4.726   6.070  1.00 53.29      A    C  
ANISOU  935  CG  TYR A 138     6843   5840   7565   -813   -515   1061  A    C  
ATOM    936  CD1 TYR A 138      43.750  -4.572   7.251  1.00 55.20      A    C  
ANISOU  936  CD1 TYR A 138     7209   6077   7688   -887   -478   1114  A    C  
ATOM    937  CD2 TYR A 138      44.639  -3.618   5.236  1.00 49.40      A    C  
ANISOU  937  CD2 TYR A 138     6306   5404   7059   -760   -442   1004  A    C  
ATOM    938  CE1 TYR A 138      43.183  -3.343   7.588  1.00 54.56      A    C  
ANISOU  938  CE1 TYR A 138     7202   6045   7482   -890   -370   1098  A    C  
ATOM    939  CE2 TYR A 138      44.071  -2.388   5.563  1.00 57.97      A    C  
ANISOU  939  CE2 TYR A 138     7480   6522   8024   -768   -343    997  A    C  
ATOM    940  CZ  TYR A 138      43.343  -2.259   6.741  1.00 64.80      A    C  
ANISOU  940  CZ  TYR A 138     8464   7380   8777   -824   -307   1038  A    C  
ATOM    941  OH  TYR A 138      42.779  -1.043   7.071  1.00 80.67      A    O  
ANISOU  941  OH  TYR A 138    10569   9417  10666   -810   -205   1019  A    O  
ATOM    942  N   TYR A 139      44.429  -5.872   2.692  1.00 42.21      A    N  
ANISOU  942  N   TYR A 139     5122   4499   6416   -622   -481    896  A    N  
ATOM    943  CA  TYR A 139      44.016  -5.091   1.537  1.00 39.91      A    C  
ANISOU  943  CA  TYR A 139     4763   4294   6107   -558   -382    832  A    C  
ATOM    944  C   TYR A 139      42.897  -5.755   0.730  1.00 49.35      A    C  
ANISOU  944  C   TYR A 139     5893   5526   7332   -531   -336    788  A    C  
ATOM    945  O   TYR A 139      41.905  -5.106   0.405  1.00 50.37      A    O  
ANISOU  945  O   TYR A 139     6013   5732   7394   -510   -243    771  A    O  
ATOM    946  CB  TYR A 139      45.205  -4.807   0.617  1.00 39.42      A    C  
ANISOU  946  CB  TYR A 139     4616   4257   6104   -501   -406    787  A    C  
ATOM    947  CG  TYR A 139      44.789  -4.119  -0.644  1.00 37.53      A    C  
ANISOU  947  CG  TYR A 139     4318   4101   5841   -437   -310    729  A    C  
ATOM    948  CD1 TYR A 139      44.553  -2.748  -0.654  1.00 36.20      A    C  
ANISOU  948  CD1 TYR A 139     4209   3970   5574   -437   -229    741  A    C  
ATOM    949  CD2 TYR A 139      44.596  -4.834  -1.826  1.00 27.90      A    C  
ANISOU  949  CD2 TYR A 139     3000   2914   4688   -373   -306    662  A    C  
ATOM    950  CE1 TYR A 139      44.153  -2.091  -1.817  1.00 33.49      A    C  
ANISOU  950  CE1 TYR A 139     3829   3696   5198   -370   -148    700  A    C  
ATOM    951  CE2 TYR A 139      44.189  -4.187  -2.999  1.00 35.76      A    C  
ANISOU  951  CE2 TYR A 139     3950   3993   5644   -314   -224    615  A    C  
ATOM    952  CZ  TYR A 139      43.964  -2.816  -2.982  1.00 44.88      A    C  
ANISOU  952  CZ  TYR A 139     5166   5186   6700   -310   -147    641  A    C  
ATOM    953  OH  TYR A 139      43.572  -2.154  -4.127  1.00 48.28      A    O  
ANISOU  953  OH  TYR A 139     5570   5691   7084   -244    -76    607  A    O  
ATOM    954  N   ILE A 140      43.052  -7.033   0.388  1.00 50.63      A    N  
ANISOU  954  N   ILE A 140     6012   5633   7591   -527   -408    765  A    N  
ATOM    955  CA  ILE A 140      42.044  -7.676  -0.453  1.00 57.05      A    C  
ANISOU  955  CA  ILE A 140     6763   6480   8431   -517   -375    711  A    C  
ATOM    956  C   ILE A 140      40.706  -7.782   0.288  1.00 55.60      A    C  
ANISOU  956  C   ILE A 140     6622   6323   8181   -602   -324    754  A    C  
ATOM    957  O   ILE A 140      39.649  -7.581  -0.298  1.00 50.03      A    O  
ANISOU  957  O   ILE A 140     5855   5713   7442   -591   -253    718  A    O  
ATOM    958  CB  ILE A 140      42.487  -9.051  -1.052  1.00 48.95      A    C  
ANISOU  958  CB  ILE A 140     5702   5373   7524   -494   -464    661  A    C  
ATOM    959  CG1 ILE A 140      42.450 -10.155  -0.018  1.00 46.36      A    C  
ANISOU  959  CG1 ILE A 140     5465   4918   7233   -575   -548    725  A    C  
ATOM    960  CG2 ILE A 140      43.883  -8.988  -1.678  1.00 52.19      A    C  
ANISOU  960  CG2 ILE A 140     6056   5773   7999   -402   -509    617  A    C  
ATOM    961  CD1 ILE A 140      42.404 -11.521  -0.652  1.00 56.40      A    C  
ANISOU  961  CD1 ILE A 140     6727   6100   8605   -565   -616    669  A    C  
ATOM    962  N   HIS A 141      40.756  -8.058   1.585  1.00 50.00      A    N  
ANISOU  962  N   HIS A 141     6011   5545   7442   -685   -358    834  A    N  
ATOM    963  CA  HIS A 141      39.536  -8.154   2.374  1.00 48.72      A    C  
ANISOU  963  CA  HIS A 141     5886   5421   7203   -777   -297    880  A    C  
ATOM    964  C   HIS A 141      38.832  -6.798   2.513  1.00 49.56      A    C  
ANISOU  964  C   HIS A 141     5985   5651   7196   -740   -177    876  A    C  
ATOM    965  O   HIS A 141      37.621  -6.695   2.392  1.00 54.15      A    O  
ANISOU  965  O   HIS A 141     6512   6332   7731   -754    -96    862  A    O  
ATOM    966  CB  HIS A 141      39.854  -8.728   3.745  1.00 42.59      A    C  
ANISOU  966  CB  HIS A 141     5234   4543   6405   -875   -361    973  A    C  
ATOM    967  CG  HIS A 141      40.301 -10.152   3.705  1.00 52.93      A    C  
ANISOU  967  CG  HIS A 141     6574   5719   7819   -910   -477    987  A    C  
ATOM    968  CD2 HIS A 141      40.130 -11.113   2.765  1.00 44.34      A    C  
ANISOU  968  CD2 HIS A 141     5430   4590   6828   -900   -514    928  A    C  
ATOM    969  ND1 HIS A 141      41.046 -10.725   4.714  1.00 52.63      A    N  
ANISOU  969  ND1 HIS A 141     6651   5559   7788   -954   -579   1068  A    N  
ATOM    970  CE1 HIS A 141      41.292 -11.989   4.407  1.00 51.61      A    C  
ANISOU  970  CE1 HIS A 141     6539   5308   7760   -960   -672   1063  A    C  
ATOM    971  NE2 HIS A 141      40.752 -12.247   3.229  1.00 46.55      A    N  
ANISOU  971  NE2 HIS A 141     5801   4711   7177   -931   -632    973  A    N  
ATOM    972  N   ARG A 142      39.617  -5.766   2.777  1.00 49.45      A    N  
ANISOU  972  N   ARG A 142     6027   5624   7137   -692   -172    886  A    N  
ATOM    973  CA  ARG A 142      39.133  -4.402   2.858  1.00 45.54      A    C  
ANISOU  973  CA  ARG A 142     5555   5211   6537   -637    -69    876  A    C  
ATOM    974  C   ARG A 142      38.382  -4.057   1.579  1.00 48.94      A    C  
ANISOU  974  C   ARG A 142     5874   5746   6977   -545     -4    811  A    C  
ATOM    975  O   ARG A 142      37.486  -3.216   1.585  1.00 50.97      A    O  
ANISOU  975  O   ARG A 142     6125   6092   7151   -491     89    801  A    O  
ATOM    976  CB  ARG A 142      40.334  -3.476   3.052  1.00 51.12      A    C  
ANISOU  976  CB  ARG A 142     6339   5864   7222   -610    -98    884  A    C  
ATOM    977  CG  ARG A 142      40.010  -2.053   3.350  1.00 60.84      A    C  
ANISOU  977  CG  ARG A 142     7648   7131   8338   -566     -8    881  A    C  
ATOM    978  CD  ARG A 142      41.291  -1.251   3.502  1.00 85.56      A    C  
ANISOU  978  CD  ARG A 142    10857  10196  11457   -574    -53    888  A    C  
ATOM    979  NE  ARG A 142      41.026   0.172   3.679  1.00109.75      A    N  
ANISOU  979  NE  ARG A 142    14022  13268  14412   -530     31    877  A    N  
ATOM    980  CZ  ARG A 142      41.859   1.020   4.274  1.00122.41      A    C  
ANISOU  980  CZ  ARG A 142    15746  14807  15959   -572      8    890  A    C  
ATOM    981  NH1 ARG A 142      43.017   0.583   4.753  1.00123.08      A    N1+
ANISOU  981  NH1 ARG A 142    15841  14837  16086   -657   -100    918  A    N1+
ATOM    982  NH2 ARG A 142      41.531   2.303   4.393  1.00124.56      A    N  
ANISOU  982  NH2 ARG A 142    16130  15067  16129   -526     87    874  A    N  
ATOM    983  N   ASN A 143      38.745  -4.730   0.489  1.00 47.27      A    N  
ANISOU  983  N   ASN A 143     5576   5524   6860   -518    -58    763  A    N  
ATOM    984  CA  ASN A 143      38.122  -4.515  -0.810  1.00 45.68      A    C  
ANISOU  984  CA  ASN A 143     5270   5421   6663   -435    -16    700  A    C  
ATOM    985  C   ASN A 143      37.084  -5.563  -1.135  1.00 48.19      A    C  
ANISOU  985  C   ASN A 143     5497   5794   7017   -486    -22    672  A    C  
ATOM    986  O   ASN A 143      36.719  -5.732  -2.298  1.00 45.22      A    O  
ANISOU  986  O   ASN A 143     5028   5488   6666   -436    -23    610  A    O  
ATOM    987  CB  ASN A 143      39.177  -4.509  -1.913  1.00 45.67      A    C  
ANISOU  987  CB  ASN A 143     5234   5394   6726   -374    -61    653  A    C  
ATOM    988  CG  ASN A 143      39.894  -3.192  -2.012  1.00 51.79      A    C  
ANISOU  988  CG  ASN A 143     6068   6165   7445   -316    -25    666  A    C  
ATOM    989  ND2 ASN A 143      41.066  -3.094  -1.373  1.00 45.59      A    N  
ANISOU  989  ND2 ASN A 143     5347   5294   6680   -360    -75    698  A    N  
ATOM    990  OD1 ASN A 143      39.405  -2.263  -2.655  1.00 58.58      A    O  
ANISOU  990  OD1 ASN A 143     6921   7096   8241   -237     41    649  A    O  
ATOM    991  N   LYS A 144      36.636  -6.284  -0.108  1.00 49.92      A    N  
ANISOU  991  N   LYS A 144     5752   5983   7234   -599    -31    720  A    N  
ATOM    992  CA  LYS A 144      35.505  -7.194  -0.231  1.00 49.94      A    C  
ANISOU  992  CA  LYS A 144     5675   6047   7254   -682    -23    706  A    C  
ATOM    993  C   LYS A 144      35.825  -8.359  -1.137  1.00 52.73      A    C  
ANISOU  993  C   LYS A 144     5988   6335   7714   -709   -112    651  A    C  
ATOM    994  O   LYS A 144      34.966  -8.861  -1.846  1.00 57.43      A    O  
ANISOU  994  O   LYS A 144     6489   7007   8324   -738   -109    600  A    O  
ATOM    995  CB  LYS A 144      34.272  -6.452  -0.751  1.00 52.24      A    C  
ANISOU  995  CB  LYS A 144     5856   6519   7474   -616     68    671  A    C  
ATOM    996  CG  LYS A 144      33.895  -5.275   0.109  1.00 55.71      A    C  
ANISOU  996  CG  LYS A 144     6343   7020   7804   -565    162    711  A    C  
ATOM    997  CD  LYS A 144      33.802  -5.723   1.546  1.00 73.95      A    C  
ANISOU  997  CD  LYS A 144     8738   9279  10081   -693    175    782  A    C  
ATOM    998  CE  LYS A 144      33.723  -4.548   2.501  1.00 88.42      A    C  
ANISOU  998  CE  LYS A 144    10659  11136  11799   -639    259    816  A    C  
ATOM    999  NZ  LYS A 144      33.730  -5.008   3.926  1.00 95.12      A    N1+
ANISOU  999  NZ  LYS A 144    11608  11933  12599   -770    266    887  A    N1+
ATOM   1000  N   ILE A 145      37.072  -8.798  -1.107  1.00 52.49      A    N  
ANISOU 1000  N   ILE A 145     6027   6164   7753   -696   -194    655  A    N  
ATOM   1001  CA  ILE A 145      37.452  -9.980  -1.855  1.00 43.61      A    C  
ANISOU 1001  CA  ILE A 145     4887   4953   6731   -709   -280    598  A    C  
ATOM   1002  C   ILE A 145      37.954 -11.068  -0.924  1.00 47.99      A    C  
ANISOU 1002  C   ILE A 145     5550   5341   7344   -801   -365    656  A    C  
ATOM   1003  O   ILE A 145      38.683 -10.790   0.024  1.00 52.10      A    O  
ANISOU 1003  O   ILE A 145     6154   5795   7847   -801   -388    727  A    O  
ATOM   1004  CB  ILE A 145      38.536  -9.674  -2.889  1.00 38.42      A    C  
ANISOU 1004  CB  ILE A 145     4199   4283   6117   -581   -307    533  A    C  
ATOM   1005  CG1 ILE A 145      38.095  -8.533  -3.820  1.00 40.04      A    C  
ANISOU 1005  CG1 ILE A 145     4321   4641   6251   -488   -226    490  A    C  
ATOM   1006  CG2 ILE A 145      38.877 -10.929  -3.657  1.00 44.13      A    C  
ANISOU 1006  CG2 ILE A 145     4912   4918   6939   -581   -389    459  A    C  
ATOM   1007  CD1 ILE A 145      36.886  -8.852  -4.645  1.00 44.58      A    C  
ANISOU 1007  CD1 ILE A 145     4804   5326   6810   -504   -206    430  A    C  
ATOM   1008  N   LEU A 146      37.524 -12.299  -1.187  1.00 51.59      A    N  
ANISOU 1008  N   LEU A 146     6014   5727   7861   -885   -418    629  A    N  
ATOM   1009  CA  LEU A 146      38.085 -13.488  -0.568  1.00 47.98      A    C  
ANISOU 1009  CA  LEU A 146     5677   5079   7476   -950   -519    672  A    C  
ATOM   1010  C   LEU A 146      38.967 -14.144  -1.610  1.00 55.17      A    C  
ANISOU 1010  C   LEU A 146     6577   5897   8489   -847   -599    579  A    C  
ATOM   1011  O   LEU A 146      38.574 -14.276  -2.774  1.00 57.84      A    O  
ANISOU 1011  O   LEU A 146     6834   6299   8845   -817   -583    478  A    O  
ATOM   1012  CB  LEU A 146      36.974 -14.457  -0.186  1.00 56.80      A    C  
ANISOU 1012  CB  LEU A 146     6830   6162   8590  -1126   -522    701  A    C  
ATOM   1013  CG  LEU A 146      35.867 -13.912   0.709  1.00 52.15      A    C  
ANISOU 1013  CG  LEU A 146     6220   5704   7892  -1240   -422    776  A    C  
ATOM   1014  CD1 LEU A 146      34.867 -15.012   1.003  1.00 49.41      A    C  
ANISOU 1014  CD1 LEU A 146     5903   5320   7552  -1436   -430    803  A    C  
ATOM   1015  CD2 LEU A 146      36.443 -13.347   2.001  1.00 50.89      A    C  
ANISOU 1015  CD2 LEU A 146     6160   5508   7669  -1234   -413    880  A    C  
ATOM   1016  N   HIS A 147      40.167 -14.537  -1.205  1.00 52.90      A    N  
ANISOU 1016  N   HIS A 147     6366   5470   8262   -784   -685    607  A    N  
ATOM   1017  CA  HIS A 147      41.102 -15.155  -2.129  1.00 53.73      A    C  
ANISOU 1017  CA  HIS A 147     6457   5493   8465   -663   -756    514  A    C  
ATOM   1018  C   HIS A 147      40.734 -16.614  -2.402  1.00 53.18      A    C  
ANISOU 1018  C   HIS A 147     6470   5267   8470   -727   -831    472  A    C  
ATOM   1019  O   HIS A 147      40.771 -17.067  -3.544  1.00 49.01      A    O  
ANISOU 1019  O   HIS A 147     5902   4730   7988   -667   -845    354  A    O  
ATOM   1020  CB  HIS A 147      42.530 -15.074  -1.598  1.00 56.04      A    C  
ANISOU 1020  CB  HIS A 147     6783   5708   8800   -560   -827    556  A    C  
ATOM   1021  CG  HIS A 147      43.532 -15.736  -2.490  1.00 47.81      A    C  
ANISOU 1021  CG  HIS A 147     5714   4594   7859   -418   -893    458  A    C  
ATOM   1022  CD2 HIS A 147      44.470 -15.218  -3.318  1.00 45.66      A    C  
ANISOU 1022  CD2 HIS A 147     5334   4407   7608   -278   -872    382  A    C  
ATOM   1023  ND1 HIS A 147      43.625 -17.106  -2.613  1.00 48.84      A    N  
ANISOU 1023  ND1 HIS A 147     5937   4545   8077   -410   -987    423  A    N  
ATOM   1024  CE1 HIS A 147      44.581 -17.404  -3.475  1.00 56.09      A    C  
ANISOU 1024  CE1 HIS A 147     6802   5443   9067   -252  -1019    322  A    C  
ATOM   1025  NE2 HIS A 147      45.115 -16.275  -3.910  1.00 55.98      A    N  
ANISOU 1025  NE2 HIS A 147     6657   5600   9014   -175   -947    298  A    N  
ATOM   1026  N   ARG A 148      40.407 -17.346  -1.342  1.00 57.46      A    N  
ANISOU 1026  N   ARG A 148     7141   5677   9014   -853   -882    569  A    N  
ATOM   1027  CA  ARG A 148      39.835 -18.690  -1.459  1.00 59.66      A    C  
ANISOU 1027  CA  ARG A 148     7525   5797   9346   -964   -945    548  A    C  
ATOM   1028  C   ARG A 148      40.783 -19.757  -2.005  1.00 64.31      A    C  
ANISOU 1028  C   ARG A 148     8196   6189  10050   -844  -1058    472  A    C  
ATOM   1029  O   ARG A 148      40.379 -20.889  -2.222  1.00 78.09      A    O  
ANISOU 1029  O   ARG A 148    10047   7778  11844   -924  -1117    437  A    O  
ATOM   1030  CB  ARG A 148      38.563 -18.666  -2.312  1.00 58.50      A    C  
ANISOU 1030  CB  ARG A 148     7286   5778   9164  -1067   -874    467  A    C  
ATOM   1031  CG  ARG A 148      37.462 -17.816  -1.741  1.00 56.56      A    C  
ANISOU 1031  CG  ARG A 148     6962   5717   8811  -1189   -767    538  A    C  
ATOM   1032  CD  ARG A 148      36.109 -18.326  -2.174  1.00 60.90      A    C  
ANISOU 1032  CD  ARG A 148     7468   6329   9342  -1356   -739    495  A    C  
ATOM   1033  NE  ARG A 148      35.891 -18.188  -3.605  1.00 62.74      A    N  
ANISOU 1033  NE  ARG A 148     7584   6666   9587  -1281   -728    353  A    N  
ATOM   1034  CZ  ARG A 148      34.766 -18.548  -4.209  1.00 63.33      A    C  
ANISOU 1034  CZ  ARG A 148     7592   6827   9644  -1407   -713    291  A    C  
ATOM   1035  NH1 ARG A 148      33.781 -19.062  -3.489  1.00 64.90      A    N1+
ANISOU 1035  NH1 ARG A 148     7820   7021   9818  -1621   -701    359  A    N1+
ATOM   1036  NH2 ARG A 148      34.626 -18.396  -5.520  1.00 60.77      A    N  
ANISOU 1036  NH2 ARG A 148     7169   6603   9319  -1329   -713    162  A    N  
ATOM   1037  N   ASP A 149      42.037 -19.408  -2.236  1.00 59.38      A    N  
ANISOU 1037  N   ASP A 149     7523   5572   9467   -655  -1087    441  A    N  
ATOM   1038  CA  ASP A 149      42.987 -20.403  -2.683  1.00 59.28      A    C  
ANISOU 1038  CA  ASP A 149     7579   5383   9563   -514  -1190    368  A    C  
ATOM   1039  C   ASP A 149      44.366 -20.175  -2.050  1.00 60.86      A    C  
ANISOU 1039  C   ASP A 149     7776   5549   9799   -362  -1256    428  A    C  
ATOM   1040  O   ASP A 149      45.401 -20.342  -2.695  1.00 59.41      A    O  
ANISOU 1040  O   ASP A 149     7536   5353   9686   -178  -1292    341  A    O  
ATOM   1041  CB  ASP A 149      43.058 -20.440  -4.211  1.00 63.71      A    C  
ANISOU 1041  CB  ASP A 149     8040   6016  10151   -410  -1152    195  A    C  
ATOM   1042  CG  ASP A 149      43.621 -21.757  -4.739  1.00 72.97      A    C  
ANISOU 1042  CG  ASP A 149     9323   6973  11429   -306  -1254     97  A    C  
ATOM   1043  OD1 ASP A 149      43.618 -22.762  -3.988  1.00 68.19      A    O  
ANISOU 1043  OD1 ASP A 149     8894   6142  10873   -358  -1353    163  A    O  
ATOM   1044  OD2 ASP A 149      44.071 -21.780  -5.905  1.00 76.11      A    O1-
ANISOU 1044  OD2 ASP A 149     9643   7424  11853   -168  -1232    -48  A    O1-
ATOM   1045  N   MET A 150      44.358 -19.809  -0.772  1.00 59.55      A    N  
ANISOU 1045  N   MET A 150     7667   5381   9580   -443  -1273    575  A    N  
ATOM   1046  CA  MET A 150      45.589 -19.617  -0.015  1.00 61.66      A    C  
ANISOU 1046  CA  MET A 150     7939   5619   9868   -327  -1354    647  A    C  
ATOM   1047  C   MET A 150      46.427 -20.885   0.019  1.00 75.15      A    C  
ANISOU 1047  C   MET A 150     9760   7105  11690   -196  -1498    632  A    C  
ATOM   1048  O   MET A 150      45.993 -21.919   0.538  1.00 82.24      A    O  
ANISOU 1048  O   MET A 150    10841   7798  12608   -279  -1575    691  A    O  
ATOM   1049  CB  MET A 150      45.273 -19.178   1.422  1.00 58.25      A    C  
ANISOU 1049  CB  MET A 150     7590   5198   9344   -464  -1358    809  A    C  
ATOM   1050  CG  MET A 150      44.853 -17.712   1.568  1.00 53.91      A    C  
ANISOU 1050  CG  MET A 150     6925   4874   8684   -530  -1230    829  A    C  
ATOM   1051  SD  MET A 150      46.206 -16.551   1.244  1.00 74.96      A    S  
ANISOU 1051  SD  MET A 150     9426   7698  11356   -367  -1219    787  A    S  
ATOM   1052  CE  MET A 150      45.978 -16.247  -0.494  1.00 66.75      A    C  
ANISOU 1052  CE  MET A 150     8233   6782  10347   -289  -1114    622  A    C  
ATOM   1053  N   LYS A 151      47.627 -20.803  -0.547  1.00 76.33      A    N  
ANISOU 1053  N   LYS A 151     9799   7294  11909     11  -1532    551  A    N  
ATOM   1054  CA  LYS A 151      48.620 -21.864  -0.408  1.00 76.17      A    C  
ANISOU 1054  CA  LYS A 151     9861   7086  11996    183  -1676    542  A    C  
ATOM   1055  C   LYS A 151      50.000 -21.347  -0.786  1.00 71.44      A    C  
ANISOU 1055  C   LYS A 151     9076   6624  11443    393  -1689    482  A    C  
ATOM   1056  O   LYS A 151      50.118 -20.361  -1.508  1.00 73.58      A    O  
ANISOU 1056  O   LYS A 151     9170   7110  11679    406  -1575    410  A    O  
ATOM   1057  CB  LYS A 151      48.246 -23.096  -1.238  1.00 80.21      A    C  
ANISOU 1057  CB  LYS A 151    10486   7406  12584    220  -1708    431  A    C  
ATOM   1058  CG  LYS A 151      48.120 -22.858  -2.734  1.00 75.54      A    C  
ANISOU 1058  CG  LYS A 151     9756   6941  12003    285  -1604    250  A    C  
ATOM   1059  CD  LYS A 151      47.406 -24.032  -3.409  1.00 75.28      A    C  
ANISOU 1059  CD  LYS A 151     9873   6714  12015    245  -1630    152  A    C  
ATOM   1060  CE  LYS A 151      47.721 -24.094  -4.902  1.00 77.19      A    C  
ANISOU 1060  CE  LYS A 151    10004   7035  12290    393  -1572    -48  A    C  
ATOM   1061  NZ  LYS A 151      46.682 -24.844  -5.669  1.00 73.01      A    N1+
ANISOU 1061  NZ  LYS A 151     9586   6397  11757    280  -1558   -152  A    N1+
ATOM   1062  N   ALA A 152      51.039 -22.009  -0.290  1.00 72.48      A    N  
ANISOU 1062  N   ALA A 152     9248   6639  11652    554  -1830    516  A    N  
ATOM   1063  CA  ALA A 152      52.413 -21.561  -0.507  1.00 74.92      A    C  
ANISOU 1063  CA  ALA A 152     9364   7094  12008    749  -1856    472  A    C  
ATOM   1064  C   ALA A 152      52.713 -21.285  -1.978  1.00 69.67      A    C  
ANISOU 1064  C   ALA A 152     8520   6577  11375    863  -1743    294  A    C  
ATOM   1065  O   ALA A 152      53.395 -20.317  -2.309  1.00 69.70      A    O  
ANISOU 1065  O   ALA A 152     8322   6804  11357    906  -1675    262  A    O  
ATOM   1066  CB  ALA A 152      53.400 -22.571   0.055  1.00 81.85      A    C  
ANISOU 1066  CB  ALA A 152    10317   7802  12982    941  -2034    510  A    C  
ATOM   1067  N   ALA A 153      52.193 -22.125  -2.860  1.00 66.61      A    N  
ANISOU 1067  N   ALA A 153     8215   6064  11028    897  -1721    178  A    N  
ATOM   1068  CA  ALA A 153      52.468 -21.967  -4.284  1.00 72.58      A    C  
ANISOU 1068  CA  ALA A 153     8823   6951  11802   1012  -1618      1  A    C  
ATOM   1069  C   ALA A 153      51.770 -20.748  -4.910  1.00 72.41      A    C  
ANISOU 1069  C   ALA A 153     8683   7154  11674    861  -1455    -24  A    C  
ATOM   1070  O   ALA A 153      52.149 -20.301  -5.993  1.00 76.78      A    O  
ANISOU 1070  O   ALA A 153     9084   7873  12216    944  -1358   -143  A    O  
ATOM   1071  CB  ALA A 153      52.121 -23.243  -5.037  1.00 65.33      A    C  
ANISOU 1071  CB  ALA A 153     8048   5825  10949   1092  -1652   -125  A    C  
ATOM   1072  N   ASN A 154      50.762 -20.211  -4.226  1.00 67.06      A    N  
ANISOU 1072  N   ASN A 154     8080   6486  10912    648  -1423     90  A    N  
ATOM   1073  CA  ASN A 154      50.078 -18.998  -4.691  1.00 63.07      A    C  
ANISOU 1073  CA  ASN A 154     7475   6186  10303    518  -1280     83  A    C  
ATOM   1074  C   ASN A 154      50.642 -17.718  -4.088  1.00 64.60      A    C  
ANISOU 1074  C   ASN A 154     7551   6555  10439    483  -1244    175  A    C  
ATOM   1075  O   ASN A 154      50.133 -16.630  -4.349  1.00 66.55      A    O  
ANISOU 1075  O   ASN A 154     7735   6957  10596    383  -1133    185  A    O  
ATOM   1076  CB  ASN A 154      48.585 -19.071  -4.399  1.00 57.66      A    C  
ANISOU 1076  CB  ASN A 154     6918   5439   9554    316  -1249    136  A    C  
ATOM   1077  CG  ASN A 154      47.873 -20.003  -5.328  1.00 68.55      A    C  
ANISOU 1077  CG  ASN A 154     8372   6714  10961    310  -1244     17  A    C  
ATOM   1078  ND2 ASN A 154      46.668 -20.432  -4.946  1.00 62.92      A    N  
ANISOU 1078  ND2 ASN A 154     7789   5901  10218    135  -1254     66  A    N  
ATOM   1079  OD1 ASN A 154      48.401 -20.346  -6.387  1.00 75.70      A    O  
ANISOU 1079  OD1 ASN A 154     9218   7636  11909    455  -1231   -123  A    O  
ATOM   1080  N   VAL A 155      51.671 -17.860  -3.255  1.00 53.57      A    N  
ANISOU 1080  N   VAL A 155     6138   5126   9091    564  -1348    243  A    N  
ATOM   1081  CA  VAL A 155      52.394 -16.716  -2.721  1.00 53.53      A    C  
ANISOU 1081  CA  VAL A 155     6014   5286   9038    538  -1332    314  A    C  
ATOM   1082  C   VAL A 155      53.672 -16.528  -3.532  1.00 64.99      A    C  
ANISOU 1082  C   VAL A 155     7267   6881  10545    704  -1312    215  A    C  
ATOM   1083  O   VAL A 155      54.549 -17.394  -3.539  1.00 72.29      A    O  
ANISOU 1083  O   VAL A 155     8161   7739  11567    874  -1408    176  A    O  
ATOM   1084  CB  VAL A 155      52.731 -16.926  -1.235  1.00 58.35      A    C  
ANISOU 1084  CB  VAL A 155     6720   5798   9652    505  -1467    457  A    C  
ATOM   1085  CG1 VAL A 155      53.499 -15.746  -0.680  1.00 52.30      A    C  
ANISOU 1085  CG1 VAL A 155     5835   5202   8832    464  -1461    520  A    C  
ATOM   1086  CG2 VAL A 155      51.463 -17.169  -0.437  1.00 57.36      A    C  
ANISOU 1086  CG2 VAL A 155     6791   5540   9464    334  -1474    554  A    C  
ATOM   1087  N   LEU A 156      53.771 -15.407  -4.235  1.00 59.81      A    N  
ANISOU 1087  N   LEU A 156     6478   6424   9824    659  -1183    176  A    N  
ATOM   1088  CA  LEU A 156      54.945 -15.138  -5.058  1.00 60.37      A    C  
ANISOU 1088  CA  LEU A 156     6347   6660   9930    788  -1140     84  A    C  
ATOM   1089  C   LEU A 156      55.931 -14.221  -4.354  1.00 73.94      A    C  
ANISOU 1089  C   LEU A 156     7943   8520  11630    748  -1166    164  A    C  
ATOM   1090  O   LEU A 156      55.552 -13.424  -3.493  1.00 77.17      A    O  
ANISOU 1090  O   LEU A 156     8419   8936  11964    593  -1170    273  A    O  
ATOM   1091  CB  LEU A 156      54.535 -14.511  -6.386  1.00 61.40      A    C  
ANISOU 1091  CB  LEU A 156     6408   6929   9993    761   -979    -12  A    C  
ATOM   1092  CG  LEU A 156      53.552 -15.356  -7.196  1.00 68.06      A    C  
ANISOU 1092  CG  LEU A 156     7359   7658  10842    788   -952   -106  A    C  
ATOM   1093  CD1 LEU A 156      53.362 -14.779  -8.584  1.00 64.04      A    C  
ANISOU 1093  CD1 LEU A 156     6763   7307  10262    792   -807   -210  A    C  
ATOM   1094  CD2 LEU A 156      54.040 -16.785  -7.270  1.00 68.34      A    C  
ANISOU 1094  CD2 LEU A 156     7433   7541  10994    963  -1056   -182  A    C  
ATOM   1095  N   ILE A 157      57.202 -14.343  -4.724  1.00 82.33      A    N  
ANISOU 1095  N   ILE A 157     8821   9702  12759    889  -1185    102  A    N  
ATOM   1096  CA  ILE A 157      58.232 -13.433  -4.243  1.00 76.48      A    C  
ANISOU 1096  CA  ILE A 157     7925   9134  12000    841  -1201    158  A    C  
ATOM   1097  C   ILE A 157      59.066 -12.956  -5.423  1.00 74.90      A    C  
ANISOU 1097  C   ILE A 157     7503   9154  11800    901  -1081     51  A    C  
ATOM   1098  O   ILE A 157      59.544 -13.767  -6.211  1.00 88.11      A    O  
ANISOU 1098  O   ILE A 157     9087  10846  13547   1084  -1071    -63  A    O  
ATOM   1099  CB  ILE A 157      59.110 -14.094  -3.181  1.00 68.32      A    C  
ANISOU 1099  CB  ILE A 157     6865   8044  11048    941  -1383    219  A    C  
ATOM   1100  CG1 ILE A 157      58.229 -14.612  -2.045  1.00 65.77      A    C  
ANISOU 1100  CG1 ILE A 157     6784   7496  10709    871  -1493    330  A    C  
ATOM   1101  CG2 ILE A 157      60.120 -13.102  -2.641  1.00 65.43      A    C  
ANISOU 1101  CG2 ILE A 157     6336   7869  10655    862  -1409    277  A    C  
ATOM   1102  CD1 ILE A 157      58.978 -14.962  -0.794  1.00 71.72      A    C  
ANISOU 1102  CD1 ILE A 157     7545   8205  11500    915  -1676    430  A    C  
ATOM   1103  N   THR A 158      59.203 -11.640  -5.566  1.00 65.78      A    N  
ANISOU 1103  N   THR A 158     6277   8160  10557    745   -982     87  A    N  
ATOM   1104  CA  THR A 158      59.940 -11.066  -6.695  1.00 73.76      A    C  
ANISOU 1104  CA  THR A 158     7090   9389  11545    763   -850      2  A    C  
ATOM   1105  C   THR A 158      61.441 -11.084  -6.451  1.00 82.39      A    C  
ANISOU 1105  C   THR A 158     7947  10649  12708    838   -911     -9  A    C  
ATOM   1106  O   THR A 158      61.893 -11.239  -5.310  1.00 73.57      A    O  
ANISOU 1106  O   THR A 158     6825   9494  11634    836  -1058     71  A    O  
ATOM   1107  CB  THR A 158      59.531  -9.606  -6.989  1.00 67.36      A    C  
ANISOU 1107  CB  THR A 158     6308   8679  10606    555   -718     51  A    C  
ATOM   1108  CG2 THR A 158      58.085  -9.530  -7.345  1.00 59.46      A    C  
ANISOU 1108  CG2 THR A 158     5505   7553   9535    499   -651     53  A    C  
ATOM   1109  OG1 THR A 158      59.788  -8.786  -5.838  1.00 65.98      A    O  
ANISOU 1109  OG1 THR A 158     6158   8514  10397    402   -786    167  A    O  
ATOM   1110  N   ARG A 159      62.206 -10.909  -7.527  1.00 92.02      A    N  
ANISOU 1110  N   ARG A 159     8965  12069  13929    901   -796   -107  A    N  
ATOM   1111  CA  ARG A 159      63.661 -10.866  -7.436  1.00 94.44      A    C  
ANISOU 1111  CA  ARG A 159     9003  12582  14297    969   -831   -130  A    C  
ATOM   1112  C   ARG A 159      64.088  -9.858  -6.383  1.00 83.13      A    C  
ANISOU 1112  C   ARG A 159     7538  11223  12827    770   -899     -6  A    C  
ATOM   1113  O   ARG A 159      65.182  -9.961  -5.836  1.00 90.46      A    O  
ANISOU 1113  O   ARG A 159     8280  12273  13818    815  -1000      8  A    O  
ATOM   1114  CB  ARG A 159      64.299 -10.510  -8.785  1.00113.97      A    C  
ANISOU 1114  CB  ARG A 159    11271  15294  16739    997   -655   -239  A    C  
ATOM   1115  CG  ARG A 159      64.410 -11.673  -9.775  1.00135.90      A    C  
ANISOU 1115  CG  ARG A 159    13994  18062  19578   1253   -613   -392  A    C  
ATOM   1116  CD  ARG A 159      65.107 -11.242 -11.068  1.00154.31      A    C  
ANISOU 1116  CD  ARG A 159    16112  20660  21858   1267   -427   -495  A    C  
ATOM   1117  NE  ARG A 159      64.595 -11.956 -12.239  1.00168.87      A    N  
ANISOU 1117  NE  ARG A 159    18025  22455  23683   1415   -329   -631  A    N  
ATOM   1118  CZ  ARG A 159      64.850 -11.613 -13.500  1.00177.96      A    C  
ANISOU 1118  CZ  ARG A 159    19066  23798  24754   1416   -149   -724  A    C  
ATOM   1119  NH1 ARG A 159      65.620 -10.563 -13.764  1.00181.48      A    N1+
ANISOU 1119  NH1 ARG A 159    19325  24496  25135   1267    -40   -688  A    N1+
ATOM   1120  NH2 ARG A 159      64.335 -12.320 -14.501  1.00177.42      A    N  
ANISOU 1120  NH2 ARG A 159    19083  23669  24661   1552    -77   -852  A    N  
ATOM   1121  N   ASP A 160      63.221  -8.893  -6.092  1.00 65.97      A    N  
ANISOU 1121  N   ASP A 160     5546   8974  10546    556   -851     78  A    N  
ATOM   1122  CA  ASP A 160      63.553  -7.842  -5.138  1.00 71.77      A    C  
ANISOU 1122  CA  ASP A 160     6282   9762  11225    348   -903    185  A    C  
ATOM   1123  C   ASP A 160      62.964  -8.066  -3.747  1.00 77.43      A    C  
ANISOU 1123  C   ASP A 160     7200  10280  11938    307  -1060    288  A    C  
ATOM   1124  O   ASP A 160      62.987  -7.169  -2.902  1.00 78.43      A    O  
ANISOU 1124  O   ASP A 160     7391  10412  11996    123  -1100    376  A    O  
ATOM   1125  CB  ASP A 160      63.136  -6.484  -5.686  1.00 84.63      A    C  
ANISOU 1125  CB  ASP A 160     7977  11451  12727    134   -745    211  A    C  
ATOM   1126  CG  ASP A 160      63.753  -6.200  -7.036  1.00107.16      A    C  
ANISOU 1126  CG  ASP A 160    10640  14512  15563    151   -585    124  A    C  
ATOM   1127  OD1 ASP A 160      64.430  -7.104  -7.580  1.00107.06      A    O  
ANISOU 1127  OD1 ASP A 160    10444  14596  15637    343   -587     29  A    O  
ATOM   1128  OD2 ASP A 160      63.566  -5.078  -7.555  1.00118.76      A    O1-
ANISOU 1128  OD2 ASP A 160    12151  16046  16927    -23   -455    149  A    O1-
ATOM   1129  N   GLY A 161      62.434  -9.264  -3.517  1.00 74.69      A    N  
ANISOU 1129  N   GLY A 161     6965   9756  11658    470  -1145    275  A    N  
ATOM   1130  CA  GLY A 161      61.986  -9.658  -2.196  1.00 67.78      A    C  
ANISOU 1130  CA  GLY A 161     6268   8701  10784    450  -1300    374  A    C  
ATOM   1131  C   GLY A 161      60.630  -9.106  -1.816  1.00 68.11      A    C  
ANISOU 1131  C   GLY A 161     6565   8593  10721    291  -1246    441  A    C  
ATOM   1132  O   GLY A 161      60.321  -8.978  -0.632  1.00 75.79      A    O  
ANISOU 1132  O   GLY A 161     7678   9466  11651    203  -1346    538  A    O  
ATOM   1133  N   VAL A 162      59.823  -8.764  -2.814  1.00 60.83      A    N  
ANISOU 1133  N   VAL A 162     5699   7664   9749    260  -1089    390  A    N  
ATOM   1134  CA  VAL A 162      58.449  -8.340  -2.559  1.00 59.73      A    C  
ANISOU 1134  CA  VAL A 162     5785   7391   9518    144  -1032    441  A    C  
ATOM   1135  C   VAL A 162      57.478  -9.515  -2.732  1.00 61.51      A    C  
ANISOU 1135  C   VAL A 162     6139   7445   9788    254  -1052    412  A    C  
ATOM   1136  O   VAL A 162      57.417 -10.128  -3.800  1.00 61.38      A    O  
ANISOU 1136  O   VAL A 162     6064   7439   9818    374   -993    314  A    O  
ATOM   1137  CB  VAL A 162      58.032  -7.180  -3.477  1.00 59.63      A    C  
ANISOU 1137  CB  VAL A 162     5777   7469   9410     34   -860    416  A    C  
ATOM   1138  CG1 VAL A 162      56.654  -6.687  -3.102  1.00 47.83      A    C  
ANISOU 1138  CG1 VAL A 162     4501   5851   7821    -69   -813    473  A    C  
ATOM   1139  CG2 VAL A 162      59.048  -6.040  -3.394  1.00 58.01      A    C  
ANISOU 1139  CG2 VAL A 162     5451   7428   9163    -93   -835    441  A    C  
ATOM   1140  N   LEU A 163      56.743  -9.831  -1.666  1.00 65.88      A    N  
ANISOU 1140  N   LEU A 163     6870   7842  10318    203  -1135    496  A    N  
ATOM   1141  CA  LEU A 163      55.729 -10.894  -1.672  1.00 59.42      A    C  
ANISOU 1141  CA  LEU A 163     6197   6850   9531    260  -1158    487  A    C  
ATOM   1142  C   LEU A 163      54.418 -10.426  -2.315  1.00 58.72      A    C  
ANISOU 1142  C   LEU A 163     6204   6746   9363    178  -1020    464  A    C  
ATOM   1143  O   LEU A 163      53.930  -9.333  -2.020  1.00 52.74      A    O  
ANISOU 1143  O   LEU A 163     5505   6030   8505     46   -952    516  A    O  
ATOM   1144  CB  LEU A 163      55.469 -11.377  -0.247  1.00 50.95      A    C  
ANISOU 1144  CB  LEU A 163     5276   5632   8450    217  -1294    597  A    C  
ATOM   1145  CG  LEU A 163      54.445 -12.500  -0.063  1.00 55.51      A    C  
ANISOU 1145  CG  LEU A 163     6021   6016   9052    241  -1331    610  A    C  
ATOM   1146  CD1 LEU A 163      54.782 -13.337   1.175  1.00 57.18      A    C  
ANISOU 1146  CD1 LEU A 163     6333   6095   9298    271  -1504    705  A    C  
ATOM   1147  CD2 LEU A 163      53.031 -11.949   0.016  1.00 46.64      A    C  
ANISOU 1147  CD2 LEU A 163     5030   4863   7827     95  -1224    641  A    C  
ATOM   1148  N   LYS A 164      53.867 -11.250  -3.203  1.00 60.13      A    N  
ANISOU 1148  N   LYS A 164     6397   6867   9583    264   -984    381  A    N  
ATOM   1149  CA  LYS A 164      52.616 -10.924  -3.893  1.00 55.60      A    C  
ANISOU 1149  CA  LYS A 164     5894   6293   8939    202   -869    351  A    C  
ATOM   1150  C   LYS A 164      51.663 -12.078  -3.749  1.00 56.19      A    C  
ANISOU 1150  C   LYS A 164     6096   6204   9051    216   -918    343  A    C  
ATOM   1151  O   LYS A 164      52.037 -13.231  -4.008  1.00 56.50      A    O  
ANISOU 1151  O   LYS A 164     6129   6155   9183    333   -990    285  A    O  
ATOM   1152  CB  LYS A 164      52.832 -10.706  -5.392  1.00 51.11      A    C  
ANISOU 1152  CB  LYS A 164     5207   5848   8366    273   -759    237  A    C  
ATOM   1153  CG  LYS A 164      54.036  -9.875  -5.765  1.00 54.71      A    C  
ANISOU 1153  CG  LYS A 164     5505   6471   8812    283   -713    221  A    C  
ATOM   1154  CD  LYS A 164      53.735  -8.410  -5.671  1.00 54.60      A    C  
ANISOU 1154  CD  LYS A 164     5521   6540   8683    141   -623    284  A    C  
ATOM   1155  CE  LYS A 164      54.755  -7.594  -6.440  1.00 54.63      A    C  
ANISOU 1155  CE  LYS A 164     5375   6719   8663    134   -543    250  A    C  
ATOM   1156  NZ  LYS A 164      54.482  -6.124  -6.258  1.00 59.38      A    N1+
ANISOU 1156  NZ  LYS A 164     6041   7369   9151    -15   -466    321  A    N1+
ATOM   1157  N   LEU A 165      50.430 -11.781  -3.351  1.00 51.06      A    N  
ANISOU 1157  N   LEU A 165     5562   5512   8325     97   -878    397  A    N  
ATOM   1158  CA  LEU A 165      49.369 -12.777  -3.429  1.00 51.85      A    C  
ANISOU 1158  CA  LEU A 165     5767   5487   8447     78   -897    379  A    C  
ATOM   1159  C   LEU A 165      49.031 -12.958  -4.906  1.00 52.21      A    C  
ANISOU 1159  C   LEU A 165     5748   5592   8499    141   -819    252  A    C  
ATOM   1160  O   LEU A 165      48.893 -11.985  -5.638  1.00 58.64      A    O  
ANISOU 1160  O   LEU A 165     6492   6546   9244    128   -715    222  A    O  
ATOM   1161  CB  LEU A 165      48.141 -12.328  -2.651  1.00 59.62      A    C  
ANISOU 1161  CB  LEU A 165     6860   6452   9341    -68   -859    465  A    C  
ATOM   1162  CG  LEU A 165      48.324 -12.025  -1.167  1.00 64.95      A    C  
ANISOU 1162  CG  LEU A 165     7619   7083   9977   -149   -920    590  A    C  
ATOM   1163  CD1 LEU A 165      47.025 -11.503  -0.553  1.00 66.07      A    C  
ANISOU 1163  CD1 LEU A 165     7852   7235  10015   -282   -851    655  A    C  
ATOM   1164  CD2 LEU A 165      48.801 -13.271  -0.461  1.00 70.53      A    C  
ANISOU 1164  CD2 LEU A 165     8401   7630  10765   -110  -1061    630  A    C  
ATOM   1165  N   ALA A 166      48.925 -14.202  -5.348  1.00 49.96      A    N  
ANISOU 1165  N   ALA A 166     5500   5193   8289    209   -873    177  A    N  
ATOM   1166  CA  ALA A 166      48.742 -14.488  -6.764  1.00 49.38      A    C  
ANISOU 1166  CA  ALA A 166     5372   5171   8220    280   -813     42  A    C  
ATOM   1167  C   ALA A 166      47.578 -15.440  -6.973  1.00 55.60      A    C  
ANISOU 1167  C   ALA A 166     6270   5837   9019    221   -838      2  A    C  
ATOM   1168  O   ALA A 166      47.045 -15.997  -6.004  1.00 53.51      A    O  
ANISOU 1168  O   ALA A 166     6122   5436   8772    133   -907     82  A    O  
ATOM   1169  CB  ALA A 166      50.018 -15.087  -7.341  1.00 49.19      A    C  
ANISOU 1169  CB  ALA A 166     5263   5146   8282    451   -849    -52  A    C  
ATOM   1170  N   ASP A 167      47.188 -15.636  -8.233  1.00 53.97      A    N  
ANISOU 1170  N   ASP A 167     6030   5684   8793    257   -786   -120  A    N  
ATOM   1171  CA  ASP A 167      46.167 -16.634  -8.559  1.00 65.04      A    C  
ANISOU 1171  CA  ASP A 167     7529   6972  10209    197   -821   -179  A    C  
ATOM   1172  C   ASP A 167      44.807 -16.342  -7.943  1.00 57.99      A    C  
ANISOU 1172  C   ASP A 167     6694   6088   9252     20   -801    -91  A    C  
ATOM   1173  O   ASP A 167      44.412 -16.980  -6.971  1.00 56.88      A    O  
ANISOU 1173  O   ASP A 167     6661   5806   9144    -71   -868    -14  A    O  
ATOM   1174  CB  ASP A 167      46.617 -18.025  -8.120  1.00 74.45      A    C  
ANISOU 1174  CB  ASP A 167     8834   7940  11513    253   -941   -198  A    C  
ATOM   1175  CG  ASP A 167      47.692 -18.588  -9.015  1.00102.76      A    C  
ANISOU 1175  CG  ASP A 167    12370  11510  15164    445   -956   -333  A    C  
ATOM   1176  OD1 ASP A 167      47.424 -18.729 -10.229  1.00108.32      A    O  
ANISOU 1176  OD1 ASP A 167    13044  12275  15837    482   -904   -465  A    O  
ATOM   1177  OD2 ASP A 167      48.802 -18.881  -8.509  1.00114.13      A    O1-
ANISOU 1177  OD2 ASP A 167    13796  12889  16680    565  -1020   -309  A    O1-
ATOM   1178  N   PHE A 168      44.089 -15.400  -8.540  1.00 48.64      A    N  
ANISOU 1178  N   PHE A 168     5435   5073   7972    -23   -708   -102  A    N  
ATOM   1179  CA  PHE A 168      42.768 -15.018  -8.064  1.00 58.69      A    C  
ANISOU 1179  CA  PHE A 168     6729   6394   9177   -168   -675    -31  A    C  
ATOM   1180  C   PHE A 168      41.645 -15.701  -8.840  1.00 54.73      A    C  
ANISOU 1180  C   PHE A 168     6239   5895   8660   -240   -683   -119  A    C  
ATOM   1181  O   PHE A 168      40.499 -15.266  -8.796  1.00 58.26      A    O  
ANISOU 1181  O   PHE A 168     6655   6443   9038   -339   -640    -88  A    O  
ATOM   1182  CB  PHE A 168      42.627 -13.485  -8.092  1.00 56.33      A    C  
ANISOU 1182  CB  PHE A 168     6349   6276   8778   -162   -577     25  A    C  
ATOM   1183  CG  PHE A 168      43.371 -12.807  -6.986  1.00 55.96      A    C  
ANISOU 1183  CG  PHE A 168     6319   6213   8730   -161   -578    136  A    C  
ATOM   1184  CD1 PHE A 168      42.711 -12.407  -5.832  1.00 39.50      A    C  
ANISOU 1184  CD1 PHE A 168     4287   4120   6600   -265   -566    246  A    C  
ATOM   1185  CD2 PHE A 168      44.756 -12.635  -7.065  1.00 54.08      A    C  
ANISOU 1185  CD2 PHE A 168     6042   5972   8534    -59   -594    124  A    C  
ATOM   1186  CE1 PHE A 168      43.415 -11.794  -4.786  1.00 45.33      A    C  
ANISOU 1186  CE1 PHE A 168     5056   4841   7327   -270   -575    341  A    C  
ATOM   1187  CE2 PHE A 168      45.463 -12.030  -6.027  1.00 45.26      A    C  
ANISOU 1187  CE2 PHE A 168     4938   4845   7413    -72   -610    222  A    C  
ATOM   1188  CZ  PHE A 168      44.792 -11.605  -4.887  1.00 45.42      A    C  
ANISOU 1188  CZ  PHE A 168     5029   4847   7381   -179   -604    329  A    C  
ATOM   1189  N   GLY A 169      41.979 -16.783  -9.533  1.00 50.22      A    N  
ANISOU 1189  N   GLY A 169     5712   5215   8154   -188   -742   -232  A    N  
ATOM   1190  CA  GLY A 169      41.027 -17.463 -10.394  1.00 42.70      A    C  
ANISOU 1190  CA  GLY A 169     4777   4263   7185   -257   -760   -338  A    C  
ATOM   1191  C   GLY A 169      39.893 -18.141  -9.655  1.00 48.28      A    C  
ANISOU 1191  C   GLY A 169     5561   4879   7903   -445   -804   -282  A    C  
ATOM   1192  O   GLY A 169      38.877 -18.486 -10.251  1.00 70.87      A    O  
ANISOU 1192  O   GLY A 169     8409   7787  10731   -545   -810   -348  A    O  
ATOM   1193  N   LEU A 170      40.071 -18.345  -8.357  1.00 53.38      A    N  
ANISOU 1193  N   LEU A 170     6287   5405   8590   -505   -837   -159  A    N  
ATOM   1194  CA  LEU A 170      39.016 -18.895  -7.519  1.00 56.16      A    C  
ANISOU 1194  CA  LEU A 170     6714   5687   8939   -703   -863    -82  A    C  
ATOM   1195  C   LEU A 170      38.524 -17.847  -6.531  1.00 57.72      A    C  
ANISOU 1195  C   LEU A 170     6854   6016   9062   -772   -789     55  A    C  
ATOM   1196  O   LEU A 170      37.652 -18.124  -5.706  1.00 54.38      A    O  
ANISOU 1196  O   LEU A 170     6473   5571   8618   -938   -787    136  A    O  
ATOM   1197  CB  LEU A 170      39.508 -20.112  -6.744  1.00 61.05      A    C  
ANISOU 1197  CB  LEU A 170     7507   6039   9651   -735   -966    -41  A    C  
ATOM   1198  CG  LEU A 170      39.940 -21.373  -7.497  1.00 73.41      A    C  
ANISOU 1198  CG  LEU A 170     9180   7411  11301   -676  -1054   -170  A    C  
ATOM   1199  CD1 LEU A 170      39.992 -22.561  -6.533  1.00 72.68      A    C  
ANISOU 1199  CD1 LEU A 170     9288   7047  11281   -768  -1156    -95  A    C  
ATOM   1200  CD2 LEU A 170      39.018 -21.671  -8.659  1.00 69.84      A    C  
ANISOU 1200  CD2 LEU A 170     8690   7033  10816   -753  -1042   -305  A    C  
ATOM   1201  N   ALA A 171      39.090 -16.643  -6.598  1.00 47.41      A    N  
ANISOU 1201  N   ALA A 171     5460   4843   7710   -651   -725     79  A    N  
ATOM   1202  CA  ALA A 171      38.652 -15.590  -5.695  1.00 45.67      A    C  
ANISOU 1202  CA  ALA A 171     5203   4739   7413   -700   -652    194  A    C  
ATOM   1203  C   ALA A 171      37.214 -15.141  -6.011  1.00 57.90      A    C  
ANISOU 1203  C   ALA A 171     6656   6464   8880   -793   -583    183  A    C  
ATOM   1204  O   ALA A 171      36.649 -15.464  -7.053  1.00 57.53      A    O  
ANISOU 1204  O   ALA A 171     6553   6479   8828   -805   -592     84  A    O  
ATOM   1205  CB  ALA A 171      39.595 -14.425  -5.741  1.00 41.86      A    C  
ANISOU 1205  CB  ALA A 171     4667   4338   6899   -562   -606    216  A    C  
ATOM   1206  N   ARG A 172      36.639 -14.374  -5.101  1.00 54.75      A    N  
ANISOU 1206  N   ARG A 172     6234   6155   8411   -849   -518    282  A    N  
ATOM   1207  CA  ARG A 172      35.248 -14.011  -5.191  1.00 51.46      A    C  
ANISOU 1207  CA  ARG A 172     5720   5910   7922   -935   -454    284  A    C  
ATOM   1208  C   ARG A 172      34.981 -12.781  -4.322  1.00 51.69      A    C  
ANISOU 1208  C   ARG A 172     5722   6055   7865   -910   -363    378  A    C  
ATOM   1209  O   ARG A 172      35.505 -12.672  -3.216  1.00 53.99      A    O  
ANISOU 1209  O   ARG A 172     6103   6256   8153   -930   -363    466  A    O  
ATOM   1210  CB  ARG A 172      34.398 -15.197  -4.712  1.00 57.68      A    C  
ANISOU 1210  CB  ARG A 172     6552   6623   8739  -1135   -493    302  A    C  
ATOM   1211  CG  ARG A 172      33.154 -14.799  -3.977  1.00 66.75      A    C  
ANISOU 1211  CG  ARG A 172     7629   7924   9810  -1257   -413    372  A    C  
ATOM   1212  CD  ARG A 172      32.305 -15.978  -3.596  1.00 77.45      A    C  
ANISOU 1212  CD  ARG A 172     9019   9221  11190  -1480   -446    389  A    C  
ATOM   1213  NE  ARG A 172      30.908 -15.569  -3.460  1.00 86.48      A    N  
ANISOU 1213  NE  ARG A 172    10013  10590  12255  -1581   -363    403  A    N  
ATOM   1214  CZ  ARG A 172      30.037 -15.532  -4.466  1.00 87.36      A    C  
ANISOU 1214  CZ  ARG A 172     9976  10869  12347  -1597   -361    313  A    C  
ATOM   1215  NH1 ARG A 172      30.406 -15.887  -5.688  1.00 88.79      A    N1+
ANISOU 1215  NH1 ARG A 172    10155  11008  12572  -1528   -434    201  A    N1+
ATOM   1216  NH2 ARG A 172      28.793 -15.142  -4.251  1.00 92.94      A    N  
ANISOU 1216  NH2 ARG A 172    10531  11797  12984  -1678   -286    333  A    N  
ATOM   1217  N   ALA A 173      34.169 -11.855  -4.822  1.00 54.16      A    N  
ANISOU 1217  N   ALA A 173     5916   6562   8100   -858   -290    355  A    N  
ATOM   1218  CA  ALA A 173      33.667 -10.751  -3.996  1.00 54.94      A    C  
ANISOU 1218  CA  ALA A 173     5990   6774   8109   -837   -197    432  A    C  
ATOM   1219  C   ALA A 173      32.702 -11.258  -2.921  1.00 51.33      A    C  
ANISOU 1219  C   ALA A 173     5535   6341   7629  -1005   -167    497  A    C  
ATOM   1220  O   ALA A 173      31.991 -12.239  -3.128  1.00 52.67      A    O  
ANISOU 1220  O   ALA A 173     5666   6516   7830  -1140   -199    469  A    O  
ATOM   1221  CB  ALA A 173      32.974  -9.717  -4.867  1.00 44.92      A    C  
ANISOU 1221  CB  ALA A 173     4599   5701   6767   -723   -137    388  A    C  
ATOM   1222  N   PHE A 174      32.672 -10.595  -1.772  1.00 53.04      A    N  
ANISOU 1222  N   PHE A 174     5800   6573   7782  -1009   -101    582  A    N  
ATOM   1223  CA  PHE A 174      31.728 -10.973  -0.724  1.00 54.58      A    C  
ANISOU 1223  CA  PHE A 174     5990   6816   7931  -1167    -51    648  A    C  
ATOM   1224  C   PHE A 174      30.991  -9.755  -0.186  1.00 66.06      A    C  
ANISOU 1224  C   PHE A 174     7378   8448   9274  -1100     70    678  A    C  
ATOM   1225  O   PHE A 174      31.292  -8.620  -0.568  1.00 67.68      A    O  
ANISOU 1225  O   PHE A 174     7571   8704   9442   -931    104    655  A    O  
ATOM   1226  CB  PHE A 174      32.426 -11.746   0.410  1.00 59.74      A    C  
ANISOU 1226  CB  PHE A 174     6811   7276   8612  -1280   -102    734  A    C  
ATOM   1227  CG  PHE A 174      33.305 -10.893   1.302  1.00 69.93      A    C  
ANISOU 1227  CG  PHE A 174     8210   8506   9853  -1196    -83    799  A    C  
ATOM   1228  CD1 PHE A 174      34.629 -10.627   0.959  1.00 67.25      A    C  
ANISOU 1228  CD1 PHE A 174     7935   8052   9564  -1074   -150    780  A    C  
ATOM   1229  CD2 PHE A 174      32.819 -10.384   2.497  1.00 68.35      A    C  
ANISOU 1229  CD2 PHE A 174     8046   8373   9551  -1248      3    873  A    C  
ATOM   1230  CE1 PHE A 174      35.447  -9.862   1.789  1.00 59.79      A    C  
ANISOU 1230  CE1 PHE A 174     7087   7058   8573  -1019   -144    837  A    C  
ATOM   1231  CE2 PHE A 174      33.635  -9.613   3.327  1.00 65.69      A    C  
ANISOU 1231  CE2 PHE A 174     7824   7977   9160  -1183     11    924  A    C  
ATOM   1232  CZ  PHE A 174      34.951  -9.357   2.969  1.00 63.52      A    C  
ANISOU 1232  CZ  PHE A 174     7611   7584   8941  -1075    -68    907  A    C  
ATOM   1233  N   SER A 175      30.027  -9.996   0.699  1.00 86.88      A    N  
ANISOU 1233  N   SER A 175     9980  11175  11854  -1232    139    728  A    N  
ATOM   1234  CA  SER A 175      29.191  -8.928   1.243  1.00 98.05      A    C  
ANISOU 1234  CA  SER A 175    11320  12777  13160  -1165    265    745  A    C  
ATOM   1235  C   SER A 175      28.544  -9.321   2.564  1.00107.29      A    C  
ANISOU 1235  C   SER A 175    12515  13988  14263  -1333    338    823  A    C  
ATOM   1236  O   SER A 175      29.045 -10.186   3.287  1.00102.97      A    O  
ANISOU 1236  O   SER A 175    12104  13281  13740  -1477    288    888  A    O  
ATOM   1237  CB  SER A 175      28.096  -8.570   0.245  1.00 95.46      A    C  
ANISOU 1237  CB  SER A 175    10784  12670  12815  -1094    301    672  A    C  
ATOM   1238  OG  SER A 175      27.347  -9.725  -0.085  1.00 93.82      A    O  
ANISOU 1238  OG  SER A 175    10477  12516  12655  -1274    264    649  A    O  
ATOM   1239  N   LEU A 176      27.426  -8.665   2.868  1.00124.29      A    N  
ANISOU 1239  N   LEU A 176    14538  16362  16325  -1303    460    817  A    N  
ATOM   1240  CA  LEU A 176      26.609  -8.986   4.036  1.00136.59      A    C  
ANISOU 1240  CA  LEU A 176    16078  18017  17801  -1465    557    881  A    C  
ATOM   1241  C   LEU A 176      25.129  -8.840   3.704  1.00139.06      A    C  
ANISOU 1241  C   LEU A 176    16145  18617  18074  -1480    650    837  A    C  
ATOM   1242  O   LEU A 176      24.677  -7.747   3.376  1.00141.58      A    O  
ANISOU 1242  O   LEU A 176    16356  19096  18343  -1284    717    788  A    O  
ATOM   1243  CB  LEU A 176      26.955  -8.068   5.211  1.00139.42      A    C  
ANISOU 1243  CB  LEU A 176    16569  18353  18049  -1386    641    931  A    C  
ATOM   1244  CG  LEU A 176      28.175  -8.416   6.064  1.00142.00      A    C  
ANISOU 1244  CG  LEU A 176    17135  18438  18380  -1452    569   1007  A    C  
ATOM   1245  CD1 LEU A 176      28.137  -7.637   7.367  1.00140.22      A    C  
ANISOU 1245  CD1 LEU A 176    17013  18249  18013  -1429    674   1055  A    C  
ATOM   1246  CD2 LEU A 176      28.218  -9.908   6.346  1.00146.55      A    C  
ANISOU 1246  CD2 LEU A 176    17770  18898  19013  -1689    495   1068  A    C  
ATOM   1247  N   PRO A 182      21.666 -13.852   4.052  1.00133.24      A    N  
ANISOU 1247  N   PRO A 182    15047  18151  17426  -2660    640    926  A    N  
ATOM   1248  CA  PRO A 182      22.243 -15.170   4.337  1.00132.58      A    C  
ANISOU 1248  CA  PRO A 182    15180  17788  17405  -2892    540    990  A    C  
ATOM   1249  C   PRO A 182      22.983 -15.703   3.110  1.00129.22      A    C  
ANISOU 1249  C   PRO A 182    14826  17161  17111  -2832    371    910  A    C  
ATOM   1250  O   PRO A 182      22.366 -16.354   2.265  1.00135.17      A    O  
ANISOU 1250  O   PRO A 182    15460  17980  17919  -2960    316    843  A    O  
ATOM   1251  CB  PRO A 182      21.011 -16.038   4.634  1.00134.85      A    C  
ANISOU 1251  CB  PRO A 182    15334  18239  17663  -3214    601   1021  A    C  
ATOM   1252  CG  PRO A 182      19.858 -15.069   4.804  1.00134.55      A    C  
ANISOU 1252  CG  PRO A 182    15011  18586  17526  -3135    761    990  A    C  
ATOM   1253  CD  PRO A 182      20.199 -13.904   3.943  1.00133.50      A    C  
ANISOU 1253  CD  PRO A 182    14795  18514  17413  -2787    735    896  A    C  
ATOM   1254  N   ASN A 183      24.282 -15.426   3.013  1.00115.42      A    N  
ANISOU 1254  N   ASN A 183    13264  15184  15407  -2645    292    911  A    N  
ATOM   1255  CA  ASN A 183      25.063 -15.781   1.827  1.00103.61      A    C  
ANISOU 1255  CA  ASN A 183    11826  13519  14024  -2544    150    825  A    C  
ATOM   1256  C   ASN A 183      25.213 -17.287   1.611  1.00 99.96      A    C  
ANISOU 1256  C   ASN A 183    11495  12835  13648  -2770     35    828  A    C  
ATOM   1257  O   ASN A 183      25.423 -18.042   2.560  1.00100.27      A    O  
ANISOU 1257  O   ASN A 183    11711  12707  13681  -2941     24    929  A    O  
ATOM   1258  CB  ASN A 183      26.452 -15.138   1.888  1.00100.72      A    C  
ANISOU 1258  CB  ASN A 183    11618  12973  13678  -2306    105    834  A    C  
ATOM   1259  CG  ASN A 183      26.404 -13.620   1.832  1.00 92.86      A    C  
ANISOU 1259  CG  ASN A 183    10514  12158  12610  -2065    196    809  A    C  
ATOM   1260  ND2 ASN A 183      27.355 -12.975   2.502  1.00 88.09      A    N  
ANISOU 1260  ND2 ASN A 183    10055  11439  11975  -1935    206    861  A    N  
ATOM   1261  OD1 ASN A 183      25.534 -13.037   1.187  1.00 87.06      A    O  
ANISOU 1261  OD1 ASN A 183     9575  11658  11845  -1995    248    744  A    O  
ATOM   1262  N   ARG A 184      25.111 -17.715   0.356  1.00 94.11      A    N  
ANISOU 1262  N   ARG A 184    10688  12088  12983  -2764    -55    715  A    N  
ATOM   1263  CA  ARG A 184      25.320 -19.116   0.009  1.00100.51      A    C  
ANISOU 1263  CA  ARG A 184    11645  12664  13882  -2950   -176    694  A    C  
ATOM   1264  C   ARG A 184      26.472 -19.240  -0.967  1.00102.74      A    C  
ANISOU 1264  C   ARG A 184    12036  12746  14254  -2752   -296    604  A    C  
ATOM   1265  O   ARG A 184      26.267 -19.569  -2.135  1.00107.62      A    O  
ANISOU 1265  O   ARG A 184    12584  13389  14917  -2749   -364    485  A    O  
ATOM   1266  CB  ARG A 184      24.072 -19.729  -0.630  1.00102.97      A    C  
ANISOU 1266  CB  ARG A 184    11787  13139  14196  -3175   -183    625  A    C  
ATOM   1267  CG  ARG A 184      23.017 -20.210   0.340  1.00109.27      A    C  
ANISOU 1267  CG  ARG A 184    12536  14048  14932  -3477    -96    720  A    C  
ATOM   1268  CD  ARG A 184      21.796 -20.692  -0.420  1.00120.43      A    C  
ANISOU 1268  CD  ARG A 184    13743  15665  16351  -3687   -109    636  A    C  
ATOM   1269  NE  ARG A 184      20.694 -21.046   0.468  1.00136.65      A    N  
ANISOU 1269  NE  ARG A 184    15700  17883  18336  -3984     -6    723  A    N  
ATOM   1270  CZ  ARG A 184      19.531 -21.539   0.050  1.00151.37      A    C  
ANISOU 1270  CZ  ARG A 184    17374  19946  20195  -4230     -3    673  A    C  
ATOM   1271  NH1 ARG A 184      19.319 -21.734  -1.246  1.00155.93      A    N1+
ANISOU 1271  NH1 ARG A 184    17847  20573  20826  -4207   -107    535  A    N1+
ATOM   1272  NH2 ARG A 184      18.577 -21.839   0.924  1.00154.32      A    N  
ANISOU 1272  NH2 ARG A 184    17656  20480  20500  -4508    105    761  A    N  
ATOM   1273  N   TYR A 185      27.684 -18.976  -0.493  1.00 97.39      A    N  
ANISOU 1273  N   TYR A 185    11523  11885  13595  -2589   -322    656  A    N  
ATOM   1274  CA  TYR A 185      28.860 -19.106  -1.341  1.00 89.38      A    C  
ANISOU 1274  CA  TYR A 185    10606  10690  12665  -2398   -425    575  A    C  
ATOM   1275  C   TYR A 185      29.190 -20.579  -1.508  1.00 88.05      A    C  
ANISOU 1275  C   TYR A 185    10627  10241  12586  -2540   -547    556  A    C  
ATOM   1276  O   TYR A 185      28.790 -21.405  -0.694  1.00 93.70      A    O  
ANISOU 1276  O   TYR A 185    11453  10851  13296  -2767   -553    644  A    O  
ATOM   1277  CB  TYR A 185      30.051 -18.347  -0.751  1.00 83.65      A    C  
ANISOU 1277  CB  TYR A 185     9976   9877  11930  -2190   -416    637  A    C  
ATOM   1278  CG  TYR A 185      29.782 -16.880  -0.493  1.00 82.44      A    C  
ANISOU 1278  CG  TYR A 185     9678   9961  11684  -2052   -298    660  A    C  
ATOM   1279  CD1 TYR A 185      28.965 -16.143  -1.347  1.00 79.42      A    C  
ANISOU 1279  CD1 TYR A 185     9087   9828  11262  -1984   -241    579  A    C  
ATOM   1280  CD2 TYR A 185      30.355 -16.225   0.597  1.00 80.52      A    C  
ANISOU 1280  CD2 TYR A 185     9520   9684  11388  -1982   -252    759  A    C  
ATOM   1281  CE1 TYR A 185      28.720 -14.796  -1.122  1.00 77.69      A    C  
ANISOU 1281  CE1 TYR A 185     8758   9803  10958  -1840   -138    598  A    C  
ATOM   1282  CE2 TYR A 185      30.117 -14.876   0.834  1.00 74.99      A    C  
ANISOU 1282  CE2 TYR A 185     8714   9179  10600  -1853   -146    770  A    C  
ATOM   1283  CZ  TYR A 185      29.300 -14.168  -0.032  1.00 76.66      A    C  
ANISOU 1283  CZ  TYR A 185     8728   9619  10779  -1776    -88    690  A    C  
ATOM   1284  OH  TYR A 185      29.050 -12.834   0.189  1.00 72.72      A    O  
ANISOU 1284  OH  TYR A 185     8144   9293  10194  -1632     13    699  A    O  
HETATM 1285  N   TPO A 186      29.918 -20.902  -2.568  1.00 84.95      A    N  
ANISOU 1285  N   TPO A 186    10281   9725  12270  -2405   -639    442  A    N  
HETATM 1286  CA  TPO A 186      30.295 -22.314  -2.873  1.00 86.63      A    C  
ANISOU 1286  CA  TPO A 186    10691   9651  12575  -2503   -763    397  A    C  
HETATM 1287  C   TPO A 186      31.300 -22.892  -1.898  1.00 91.82      A    C  
ANISOU 1287  C   TPO A 186    11587  10022  13277  -2479   -824    504  A    C  
HETATM 1288  O   TPO A 186      32.189 -22.191  -1.403  1.00 83.48      A    O  
ANISOU 1288  O   TPO A 186    10551   8958  12211  -2296   -808    563  A    O  
HETATM 1289  CB  TPO A 186      30.765 -22.285  -4.321  1.00 82.32      A    C  
ANISOU 1289  CB  TPO A 186    10097   9105  12076  -2327   -821    231  A    C  
HETATM 1290  CG2 TPO A 186      31.801 -23.357  -4.638  1.00 71.45      A    C  
ANISOU 1290  CG2 TPO A 186     8941   7406  10800  -2261   -943    174  A    C  
HETATM 1291  OG1 TPO A 186      31.309 -20.982  -4.506  1.00 91.79      A    O  
ANISOU 1291  OG1 TPO A 186    11174  10466  13237  -2084   -756    229  A    O  
HETATM 1292  P   TPO A 186      31.017 -20.067  -5.798  1.00 84.75      A    P  
ANISOU 1292  P   TPO A 186    10078   9823  12300  -1937   -719    107  A    P  
HETATM 1293  O1P TPO A 186      32.198 -20.328  -6.716  1.00 71.11      A    O  
ANISOU 1293  O1P TPO A 186     8436   7946  10636  -1746   -791      1  A    O  
HETATM 1294  O2P TPO A 186      29.701 -20.589  -6.322  1.00106.18      A    O1-
ANISOU 1294  O2P TPO A 186    12692  12660  14991  -2146   -731     42  A    O1-
HETATM 1295  O3P TPO A 186      30.929 -18.691  -5.183  1.00 77.23      A    O  
ANISOU 1295  O3P TPO A 186     9008   9066  11270  -1830   -609    197  A    O  
ATOM   1296  N   ASN A 187      31.087 -24.151  -1.533  1.00 95.68      A    N  
ANISOU 1296  N   ASN A 187    12268  10271  13813  -2671   -905    532  A    N  
ATOM   1297  CA  ASN A 187      31.914 -24.807  -0.530  1.00100.57      A    C  
ANISOU 1297  CA  ASN A 187    13135  10615  14462  -2691   -972    659  A    C  
ATOM   1298  C   ASN A 187      33.043 -25.534  -1.228  1.00105.79      A    C  
ANISOU 1298  C   ASN A 187    13976  10985  15233  -2503  -1105    590  A    C  
ATOM   1299  O   ASN A 187      33.932 -26.101  -0.591  1.00104.40      A    O  
ANISOU 1299  O   ASN A 187    13958  10626  15083  -2400  -1164    683  A    O  
ATOM   1300  CB  ASN A 187      31.081 -25.793   0.290  1.00110.35      A    C  
ANISOU 1300  CB  ASN A 187    14502  11748  15676  -3026   -977    754  A    C  
ATOM   1301  CG  ASN A 187      31.806 -26.277   1.531  1.00111.02      A    C  
ANISOU 1301  CG  ASN A 187    14808  11635  15738  -3079  -1006    933  A    C  
ATOM   1302  ND2 ASN A 187      31.082 -26.367   2.641  1.00108.62      A    N  
ANISOU 1302  ND2 ASN A 187    14766  11014  15490  -3210  -1115    975  A    N  
ATOM   1303  OD1 ASN A 187      33.002 -26.566   1.493  1.00114.50      A    O  
ANISOU 1303  OD1 ASN A 187    15198  12202  16105  -3006   -935   1034  A    O  
ATOM   1304  N   ARG A 188      33.015 -25.522  -2.555  1.00115.50      A    N  
ANISOU 1304  N   ARG A 188    15179  12185  16521  -2450  -1154    423  A    N  
ATOM   1305  CA  ARG A 188      34.092 -26.118  -3.336  1.00122.39      A    C  
ANISOU 1305  CA  ARG A 188    16206  12804  17495  -2255  -1268    329  A    C  
ATOM   1306  C   ARG A 188      35.252 -25.132  -3.393  1.00112.62      A    C  
ANISOU 1306  C   ARG A 188    14889  11628  16273  -1941  -1257    318  A    C  
ATOM   1307  O   ARG A 188      35.715 -24.764  -4.473  1.00115.58      A    O  
ANISOU 1307  O   ARG A 188    15264  11943  16709  -1738  -1304    188  A    O  
ATOM   1308  CB  ARG A 188      33.610 -26.445  -4.750  1.00133.83      A    C  
ANISOU 1308  CB  ARG A 188    17614  14259  18976  -2265  -1302    135  A    C  
ATOM   1309  CG  ARG A 188      34.731 -26.669  -5.752  1.00137.97      A    C  
ANISOU 1309  CG  ARG A 188    17865  15115  19443  -2149  -1213     31  A    C  
ATOM   1310  CD  ARG A 188      34.531 -25.828  -7.002  1.00143.43      A    C  
ANISOU 1310  CD  ARG A 188    18548  15771  20180  -1952  -1261   -158  A    C  
ATOM   1311  NE  ARG A 188      35.379 -26.274  -8.103  1.00146.52      A    N  
ANISOU 1311  NE  ARG A 188    18981  16068  20622  -1665  -1284   -162  A    N  
ATOM   1312  CZ  ARG A 188      36.484 -25.648  -8.495  1.00143.90      A    C  
ANISOU 1312  CZ  ARG A 188    18606  15756  20315  -1445  -1295   -308  A    C  
ATOM   1313  NH1 ARG A 188      36.879 -24.544  -7.876  1.00146.28      A    N1+
ANISOU 1313  NH1 ARG A 188    18835  16158  20586  -1473  -1291   -463  A    N1+
ATOM   1314  NH2 ARG A 188      37.195 -26.126  -9.508  1.00137.23      A    N  
ANISOU 1314  NH2 ARG A 188    17781  14842  19517  -1201  -1310   -300  A    N  
ATOM   1315  N   VAL A 189      35.711 -24.700  -2.222  1.00101.54      A    N  
ANISOU 1315  N   VAL A 189    13420  10351  14810  -1906  -1193    449  A    N  
ATOM   1316  CA  VAL A 189      36.738 -23.670  -2.144  1.00 88.42      A    C  
ANISOU 1316  CA  VAL A 189    11645   8804  13147  -1645  -1166    433  A    C  
ATOM   1317  C   VAL A 189      37.956 -24.039  -1.300  1.00 82.24      A    C  
ANISOU 1317  C   VAL A 189    11009   7830  12409  -1512  -1249    531  A    C  
ATOM   1318  O   VAL A 189      37.836 -24.592  -0.207  1.00 77.34      A    O  
ANISOU 1318  O   VAL A 189    10552   7058  11775  -1640  -1293    667  A    O  
ATOM   1319  CB  VAL A 189      36.161 -22.335  -1.637  1.00 88.06      A    C  
ANISOU 1319  CB  VAL A 189    11399   9062  12997  -1663  -1034    482  A    C  
ATOM   1320  CG1 VAL A 189      35.322 -21.675  -2.720  1.00 83.16      A    C  
ANISOU 1320  CG1 VAL A 189    10598   8655  12342  -1695   -968    357  A    C  
ATOM   1321  CG2 VAL A 189      35.339 -22.557  -0.377  1.00 90.40      A    C  
ANISOU 1321  CG2 VAL A 189    11751   9379  13219  -1875   -989    640  A    C  
ATOM   1322  N   VAL A 190      39.128 -23.712  -1.833  1.00 83.43      A    N  
ANISOU 1322  N   VAL A 190    11095   7999  12606  -1258  -1272    462  A    N  
ATOM   1323  CA  VAL A 190      40.412 -23.867  -1.139  1.00 82.29      A    C  
ANISOU 1323  CA  VAL A 190    11047   7711  12511  -1094  -1360    535  A    C  
ATOM   1324  C   VAL A 190      40.947 -25.290  -1.233  1.00 82.67      A    C  
ANISOU 1324  C   VAL A 190    11305   7444  12662  -1040  -1498    505  A    C  
ATOM   1325  O   VAL A 190      40.223 -26.246  -0.975  1.00 82.09      A    O  
ANISOU 1325  O   VAL A 190    11398   7197  12596  -1225  -1541    540  A    O  
ATOM   1326  CB  VAL A 190      40.322 -23.485   0.362  1.00 71.29      A    C  
ANISOU 1326  CB  VAL A 190     9716   6331  11042  -1197  -1352    724  A    C  
ATOM   1327  CG1 VAL A 190      41.714 -23.530   1.020  1.00 61.37      A    C  
ANISOU 1327  CG1 VAL A 190     8529   4960   9827  -1010  -1454    793  A    C  
ATOM   1328  CG2 VAL A 190      39.639 -22.117   0.551  1.00 55.17      A    C  
ANISOU 1328  CG2 VAL A 190     7493   4581   8888  -1266  -1209    755  A    C  
ATOM   1329  N   THR A 191      42.219 -25.427  -1.592  1.00 86.78      A    N  
ANISOU 1329  N   THR A 191    11820   7891  13261   -786  -1567    442  A    N  
ATOM   1330  CA  THR A 191      42.867 -26.732  -1.592  1.00 84.38      A    C  
ANISOU 1330  CA  THR A 191    11723   7278  13059   -685  -1706    418  A    C  
ATOM   1331  C   THR A 191      42.668 -27.413  -0.247  1.00 89.88      A    C  
ANISOU 1331  C   THR A 191    12646   7764  13740   -827  -1792    601  A    C  
ATOM   1332  O   THR A 191      42.708 -26.764   0.801  1.00 88.77      A    O  
ANISOU 1332  O   THR A 191    12481   7720  13528   -882  -1772    749  A    O  
ATOM   1333  CB  THR A 191      44.365 -26.615  -1.880  1.00 89.52      A    C  
ANISOU 1333  CB  THR A 191    12306   7923  13786   -373  -1764    358  A    C  
ATOM   1334  CG2 THR A 191      45.101 -27.877  -1.443  1.00 98.87      A    C  
ANISOU 1334  CG2 THR A 191    13721   8782  15064   -252  -1925    391  A    C  
ATOM   1335  OG1 THR A 191      44.555 -26.422  -3.284  1.00 90.14      A    O  
ANISOU 1335  OG1 THR A 191    12243   8116  13892   -244  -1704    165  A    O  
ATOM   1336  N   LEU A 192      42.455 -28.725  -0.286  1.00 90.83      A    N  
ANISOU 1336  N   LEU A 192    13003   7590  13919   -890  -1889    591  A    N  
ATOM   1337  CA  LEU A 192      42.132 -29.497   0.909  1.00 90.28      A    C  
ANISOU 1337  CA  LEU A 192    13184   7293  13827  -1061  -1970    768  A    C  
ATOM   1338  C   LEU A 192      43.053 -29.251   2.120  1.00 84.98      A    C  
ANISOU 1338  C   LEU A 192    12565   6587  13135   -942  -2047    933  A    C  
ATOM   1339  O   LEU A 192      42.573 -29.086   3.243  1.00 92.64      A    O  
ANISOU 1339  O   LEU A 192    13613   7572  14013  -1127  -2033   1104  A    O  
ATOM   1340  CB  LEU A 192      42.087 -30.994   0.579  1.00 87.60      A    C  
ANISOU 1340  CB  LEU A 192    13117   6593  13574  -1079  -2089    716  A    C  
ATOM   1341  CG  LEU A 192      41.634 -31.873   1.746  1.00 92.88      A    C  
ANISOU 1341  CG  LEU A 192    14078   7003  14210  -1294  -2170    904  A    C  
ATOM   1342  CD1 LEU A 192      40.134 -31.714   2.011  1.00 87.48      A    C  
ANISOU 1342  CD1 LEU A 192    13375   6440  13426  -1670  -2056    967  A    C  
ATOM   1343  CD2 LEU A 192      42.006 -33.335   1.508  1.00105.76      A    C  
ANISOU 1343  CD2 LEU A 192    16012   8227  15944  -1220  -2322    863  A    C  
ATOM   1344  N   TRP A 193      44.365 -29.235   1.902  1.00 65.37      A    N  
ANISOU 1344  N   TRP A 193    10035   4072  10731   -640  -2130    882  A    N  
ATOM   1345  CA  TRP A 193      45.302 -29.128   3.022  1.00 75.63      A    C  
ANISOU 1345  CA  TRP A 193    11393   5324  12019   -517  -2233   1033  A    C  
ATOM   1346  C   TRP A 193      45.240 -27.766   3.710  1.00 83.41      A    C  
ANISOU 1346  C   TRP A 193    12194   6608  12892   -586  -2138   1125  A    C  
ATOM   1347  O   TRP A 193      45.634 -27.609   4.875  1.00 76.99      A    O  
ANISOU 1347  O   TRP A 193    11456   5776  12022   -591  -2206   1284  A    O  
ATOM   1348  CB  TRP A 193      46.732 -29.401   2.562  1.00 83.16      A    C  
ANISOU 1348  CB  TRP A 193    12300   6208  13087   -168  -2341    942  A    C  
ATOM   1349  CG  TRP A 193      46.947 -30.782   2.032  1.00 87.64      A    C  
ANISOU 1349  CG  TRP A 193    13084   6450  13765    -55  -2454    859  A    C  
ATOM   1350  CD1 TRP A 193      46.093 -31.852   2.134  1.00 89.39      A    C  
ANISOU 1350  CD1 TRP A 193    13577   6396  13991   -247  -2496    891  A    C  
ATOM   1351  CD2 TRP A 193      48.104 -31.257   1.342  1.00 87.23      A    C  
ANISOU 1351  CD2 TRP A 193    13006   6306  13834    277  -2540    727  A    C  
ATOM   1352  CE2 TRP A 193      47.883 -32.620   1.041  1.00 92.48      A    C  
ANISOU 1352  CE2 TRP A 193    13948   6619  14571    285  -2634    678  A    C  
ATOM   1353  CE3 TRP A 193      49.304 -30.664   0.943  1.00 83.99      A    C  
ANISOU 1353  CE3 TRP A 193    12360   6078  13473    564  -2542    643  A    C  
ATOM   1354  NE1 TRP A 193      46.647 -32.956   1.532  1.00 90.26      A    N  
ANISOU 1354  NE1 TRP A 193    13850   6227  14217    -50  -2608    783  A    N  
ATOM   1355  CZ2 TRP A 193      48.821 -33.396   0.365  1.00 88.10      A    C  
ANISOU 1355  CZ2 TRP A 193    13448   5889  14136    595  -2729    541  A    C  
ATOM   1356  CZ3 TRP A 193      50.235 -31.438   0.269  1.00 90.54      A    C  
ANISOU 1356  CZ3 TRP A 193    13220   6758  14422    864  -2629    510  A    C  
ATOM   1357  CH2 TRP A 193      49.990 -32.789  -0.009  1.00 87.05      A    C  
ANISOU 1357  CH2 TRP A 193    13064   5963  14050    889  -2721    458  A    C  
ATOM   1358  N   TYR A 194      44.743 -26.777   2.979  1.00 79.45      A    N  
ANISOU 1358  N   TYR A 194    11463   6374  12351   -635  -1986   1023  A    N  
ATOM   1359  CA  TYR A 194      44.679 -25.435   3.509  1.00 76.54      A    C  
ANISOU 1359  CA  TYR A 194    10925   6278  11879   -685  -1889   1087  A    C  
ATOM   1360  C   TYR A 194      43.256 -25.063   3.905  1.00 75.88      A    C  
ANISOU 1360  C   TYR A 194    10847   6305  11681   -972  -1764   1152  A    C  
ATOM   1361  O   TYR A 194      43.022 -23.994   4.473  1.00 67.66      A    O  
ANISOU 1361  O   TYR A 194     9701   5471  10538  -1039  -1676   1216  A    O  
ATOM   1362  CB  TYR A 194      45.253 -24.451   2.494  1.00 76.62      A    C  
ANISOU 1362  CB  TYR A 194    10673   6521  11918   -511  -1810    941  A    C  
ATOM   1363  CG  TYR A 194      46.744 -24.606   2.289  1.00 82.35      A    C  
ANISOU 1363  CG  TYR A 194    11349   7203  12738   -231  -1917    895  A    C  
ATOM   1364  CD1 TYR A 194      47.642 -23.797   2.979  1.00 89.71      A    C  
ANISOU 1364  CD1 TYR A 194    12183   8265  13637   -139  -1948    970  A    C  
ATOM   1365  CD2 TYR A 194      47.256 -25.556   1.414  1.00 77.46      A    C  
ANISOU 1365  CD2 TYR A 194    10773   6422  12237    -59  -1988    771  A    C  
ATOM   1366  CE1 TYR A 194      49.009 -23.928   2.803  1.00 89.95      A    C  
ANISOU 1366  CE1 TYR A 194    12138   8285  13754    112  -2047    928  A    C  
ATOM   1367  CE2 TYR A 194      48.624 -25.696   1.230  1.00 80.79      A    C  
ANISOU 1367  CE2 TYR A 194    11126   6827  12745    213  -2079    723  A    C  
ATOM   1368  CZ  TYR A 194      49.497 -24.876   1.926  1.00 87.03      A    C  
ANISOU 1368  CZ  TYR A 194    11795   7768  13504    295  -2108    805  A    C  
ATOM   1369  OH  TYR A 194      50.864 -24.986   1.753  1.00 86.04      A    O  
ANISOU 1369  OH  TYR A 194    11569   7658  13464    559  -2198    758  A    O  
ATOM   1370  N   ARG A 195      42.309 -25.959   3.630  1.00 76.93      A    N  
ANISOU 1370  N   ARG A 195    11104   6298  11828  -1145  -1758   1135  A    N  
ATOM   1371  CA  ARG A 195      40.899 -25.650   3.857  1.00 81.02      A    C  
ANISOU 1371  CA  ARG A 195    11589   6949  12245  -1419  -1631   1176  A    C  
ATOM   1372  C   ARG A 195      40.537 -25.612   5.339  1.00 78.57      A    C  
ANISOU 1372  C   ARG A 195    11413   6619  11820  -1595  -1628   1374  A    C  
ATOM   1373  O   ARG A 195      40.850 -26.534   6.076  1.00 87.67      A    O  
ANISOU 1373  O   ARG A 195    12798   7528  12985  -1625  -1747   1488  A    O  
ATOM   1374  CB  ARG A 195      39.988 -26.621   3.107  1.00 82.01      A    C  
ANISOU 1374  CB  ARG A 195    11795   6949  12416  -1576  -1628   1094  A    C  
ATOM   1375  CG  ARG A 195      38.514 -26.259   3.228  1.00 84.54      A    C  
ANISOU 1375  CG  ARG A 195    12032   7453  12638  -1854  -1491   1119  A    C  
ATOM   1376  CD  ARG A 195      37.654 -27.269   2.516  1.00 81.26      A    C  
ANISOU 1376  CD  ARG A 195    11697   6910  12267  -2030  -1505   1039  A    C  
ATOM   1377  NE  ARG A 195      38.143 -27.463   1.162  1.00 82.70      A    N  
ANISOU 1377  NE  ARG A 195    11813   7060  12551  -1843  -1544    850  A    N  
ATOM   1378  CZ  ARG A 195      38.061 -28.604   0.493  1.00 84.72      A    C  
ANISOU 1378  CZ  ARG A 195    12218   7084  12887  -1876  -1627    758  A    C  
ATOM   1379  NH1 ARG A 195      37.506 -29.673   1.055  1.00 89.07      A    N1+
ANISOU 1379  NH1 ARG A 195    13003   7401  13437  -2101  -1686    846  A    N1+
ATOM   1380  NH2 ARG A 195      38.545 -28.675  -0.739  1.00 79.72      A    N  
ANISOU 1380  NH2 ARG A 195    11513   6450  12329  -1688  -1649    576  A    N  
ATOM   1381  N   PRO A 196      39.879 -24.527   5.775  1.00 80.37      A    N  
ANISOU 1381  N   PRO A 196    11502   7103  11930  -1704  -1491   1415  A    N  
ATOM   1382  CA  PRO A 196      39.482 -24.310   7.172  1.00 79.99      A    C  
ANISOU 1382  CA  PRO A 196    11556   7089  11748  -1869  -1459   1590  A    C  
ATOM   1383  C   PRO A 196      38.328 -25.228   7.594  1.00 81.72      A    C  
ANISOU 1383  C   PRO A 196    11930   7199  11919  -2160  -1432   1675  A    C  
ATOM   1384  O   PRO A 196      37.581 -25.690   6.735  1.00 74.75      A    O  
ANISOU 1384  O   PRO A 196    11006   6307  11089  -2263  -1396   1579  A    O  
ATOM   1385  CB  PRO A 196      38.999 -22.856   7.155  1.00 72.87      A    C  
ANISOU 1385  CB  PRO A 196    10428   6509  10750  -1876  -1299   1553  A    C  
ATOM   1386  CG  PRO A 196      38.498 -22.675   5.753  1.00 71.66      A    C  
ANISOU 1386  CG  PRO A 196    10093   6469  10667  -1844  -1227   1383  A    C  
ATOM   1387  CD  PRO A 196      39.558 -23.354   4.944  1.00 73.46      A    C  
ANISOU 1387  CD  PRO A 196    10365   6510  11035  -1645  -1359   1292  A    C  
ATOM   1388  N   PRO A 197      38.181 -25.468   8.910  1.00 88.43      A    N  
ANISOU 1388  N   PRO A 197    12957   7980  12662  -2305  -1449   1854  A    N  
ATOM   1389  CA  PRO A 197      37.126 -26.293   9.511  1.00 90.56      A    C  
ANISOU 1389  CA  PRO A 197    13391   8157  12861  -2610  -1415   1966  A    C  
ATOM   1390  C   PRO A 197      35.745 -25.945   8.969  1.00 94.38      A    C  
ANISOU 1390  C   PRO A 197    13685   8870  13307  -2808  -1245   1887  A    C  
ATOM   1391  O   PRO A 197      35.027 -26.853   8.544  1.00 89.71      A    O  
ANISOU 1391  O   PRO A 197    13161   8168  12758  -2992  -1251   1864  A    O  
ATOM   1392  CB  PRO A 197      37.185 -25.906  10.987  1.00 94.24      A    C  
ANISOU 1392  CB  PRO A 197    13964   8675  13169  -2690  -1395   2146  A    C  
ATOM   1393  CG  PRO A 197      38.574 -25.444  11.212  1.00 90.11      A    C  
ANISOU 1393  CG  PRO A 197    13444   8119  12674  -2412  -1510   2151  A    C  
ATOM   1394  CD  PRO A 197      39.067 -24.867   9.924  1.00 85.43      A    C  
ANISOU 1394  CD  PRO A 197    12622   7630  12206  -2185  -1500   1960  A    C  
ATOM   1395  N   GLU A 198      35.391 -24.656   8.992  1.00 92.79      A    N  
ANISOU 1395  N   GLU A 198    13254   8978  13025  -2767  -1104   1845  A    N  
ATOM   1396  CA  GLU A 198      34.087 -24.174   8.521  1.00 89.05      A    C  
ANISOU 1396  CA  GLU A 198    12568   8762  12505  -2919   -941   1770  A    C  
ATOM   1397  C   GLU A 198      33.677 -24.848   7.221  1.00 86.69      A    C  
ANISOU 1397  C   GLU A 198    12208   8403  12327  -2957   -971   1631  A    C  
ATOM   1398  O   GLU A 198      32.598 -25.429   7.119  1.00 92.25      A    O  
ANISOU 1398  O   GLU A 198    12910   9128  13012  -3208   -920   1636  A    O  
ATOM   1399  CB  GLU A 198      34.090 -22.653   8.283  1.00 95.04      A    C  
ANISOU 1399  CB  GLU A 198    13078   9819  13213  -2753   -825   1690  A    C  
ATOM   1400  CG  GLU A 198      34.757 -21.796   9.352  1.00 98.05      A    C  
ANISOU 1400  CG  GLU A 198    13504  10260  13491  -2648   -813   1783  A    C  
ATOM   1401  CD  GLU A 198      36.179 -21.399   8.991  1.00 96.41      A    C  
ANISOU 1401  CD  GLU A 198    13291   9973  13366  -2367   -926   1729  A    C  
ATOM   1402  OE1 GLU A 198      37.080 -22.240   9.159  1.00102.11      A    O  
ANISOU 1402  OE1 GLU A 198    14188  10450  14159  -2302  -1080   1777  A    O  
ATOM   1403  OE2 GLU A 198      36.400 -20.246   8.551  1.00 91.29      A    O1-
ANISOU 1403  OE2 GLU A 198    12467   9510  12711  -2211   -861   1640  A    O1-
ATOM   1404  N   LEU A 199      34.539 -24.752   6.218  1.00 85.89      A    N  
ANISOU 1404  N   LEU A 199    12052   8242  12342  -2713  -1051   1500  A    N  
ATOM   1405  CA  LEU A 199      34.224 -25.312   4.915  1.00 89.55      A    C  
ANISOU 1405  CA  LEU A 199    12457   8660  12909  -2722  -1081   1349  A    C  
ATOM   1406  C   LEU A 199      34.046 -26.830   4.991  1.00 91.33      A    C  
ANISOU 1406  C   LEU A 199    12932   8577  13191  -2905  -1188   1390  A    C  
ATOM   1407  O   LEU A 199      33.105 -27.374   4.420  1.00 91.57      A    O  
ANISOU 1407  O   LEU A 199    12936   8619  13238  -3103  -1163   1328  A    O  
ATOM   1408  CB  LEU A 199      35.282 -24.919   3.883  1.00 84.19      A    C  
ANISOU 1408  CB  LEU A 199    11686   7973  12330  -2415  -1142   1207  A    C  
ATOM   1409  CG  LEU A 199      35.448 -23.405   3.723  1.00 81.72      A    C  
ANISOU 1409  CG  LEU A 199    11141   7949  11961  -2250  -1037   1164  A    C  
ATOM   1410  CD1 LEU A 199      36.412 -23.084   2.598  1.00 86.17      A    C  
ANISOU 1410  CD1 LEU A 199    11610   8512  12617  -1982  -1086   1021  A    C  
ATOM   1411  CD2 LEU A 199      34.110 -22.737   3.483  1.00 72.05      A    C  
ANISOU 1411  CD2 LEU A 199     9714   7006  10654  -2394   -889   1129  A    C  
ATOM   1412  N   LEU A 200      34.940 -27.502   5.709  1.00 89.75      A    N  
ANISOU 1412  N   LEU A 200    12981   8102  13016  -2842  -1313   1498  A    N  
ATOM   1413  CA  LEU A 200      34.866 -28.950   5.865  1.00 92.94      A    C  
ANISOU 1413  CA  LEU A 200    13670   8173  13472  -2997  -1428   1554  A    C  
ATOM   1414  C   LEU A 200      33.573 -29.393   6.565  1.00 95.69      A    C  
ANISOU 1414  C   LEU A 200    14088   8551  13719  -3379  -1345   1672  A    C  
ATOM   1415  O   LEU A 200      33.103 -30.509   6.370  1.00 96.47      A    O  
ANISOU 1415  O   LEU A 200    14359   8438  13858  -3583  -1401   1676  A    O  
ATOM   1416  CB  LEU A 200      36.091 -29.456   6.623  1.00 90.13      A    C  
ANISOU 1416  CB  LEU A 200    13561   7540  13145  -2831  -1578   1668  A    C  
ATOM   1417  CG  LEU A 200      37.407 -29.259   5.877  1.00 84.15      A    C  
ANISOU 1417  CG  LEU A 200    12747   6721  12504  -2466  -1676   1546  A    C  
ATOM   1418  CD1 LEU A 200      38.580 -29.290   6.846  1.00 87.41      A    C  
ANISOU 1418  CD1 LEU A 200    13308   6997  12908  -2286  -1793   1678  A    C  
ATOM   1419  CD2 LEU A 200      37.565 -30.303   4.775  1.00 79.69      A    C  
ANISOU 1419  CD2 LEU A 200    12288   5918  12074  -2412  -1773   1403  A    C  
ATOM   1420  N   LEU A 201      33.000 -28.510   7.374  1.00 94.64      A    N  
ANISOU 1420  N   LEU A 201    13822   8685  13452  -3479  -1207   1763  A    N  
ATOM   1421  CA  LEU A 201      31.735 -28.794   8.034  1.00 92.54      A    C  
ANISOU 1421  CA  LEU A 201    13573   8512  13077  -3837  -1098   1868  A    C  
ATOM   1422  C   LEU A 201      30.543 -28.317   7.209  1.00102.52      A    C  
ANISOU 1422  C   LEU A 201    14542  10080  14329  -3967   -964   1739  A    C  
ATOM   1423  O   LEU A 201      29.407 -28.369   7.675  1.00107.62      A    O  
ANISOU 1423  O   LEU A 201    15126  10885  14881  -4254   -848   1806  A    O  
ATOM   1424  CB  LEU A 201      31.699 -28.149   9.417  1.00 85.73      A    C  
ANISOU 1424  CB  LEU A 201    12732   7783  12058  -3884  -1013   2037  A    C  
ATOM   1425  CG  LEU A 201      32.457 -28.911  10.500  1.00 85.99      A    C  
ANISOU 1425  CG  LEU A 201    13104   7512  12057  -3900  -1138   2220  A    C  
ATOM   1426  CD1 LEU A 201      32.370 -28.192  11.847  1.00 85.63      A    C  
ANISOU 1426  CD1 LEU A 201    13070   7633  11834  -3952  -1044   2375  A    C  
ATOM   1427  CD2 LEU A 201      31.929 -30.343  10.599  1.00 83.05      A    C  
ANISOU 1427  CD2 LEU A 201    12988   6860  11706  -4192  -1203   2298  A    C  
ATOM   1428  N   GLY A 202      30.810 -27.834   5.998  1.00106.18      A    N  
ANISOU 1428  N   GLY A 202    14819  10641  14882  -3752   -978   1559  A    N  
ATOM   1429  CA  GLY A 202      29.761 -27.452   5.064  1.00103.64      A    C  
ANISOU 1429  CA  GLY A 202    14229  10588  14561  -3844   -883   1424  A    C  
ATOM   1430  C   GLY A 202      29.240 -26.019   5.116  1.00 98.61      A    C  
ANISOU 1430  C   GLY A 202    13287  10347  13833  -3758   -724   1396  A    C  
ATOM   1431  O   GLY A 202      28.134 -25.754   4.645  1.00102.13      A    O  
ANISOU 1431  O   GLY A 202    13515  11043  14248  -3894   -630   1328  A    O  
ATOM   1432  N   GLU A 203      30.020 -25.093   5.671  1.00 88.02      A    N  
ANISOU 1432  N   GLU A 203    11931   9065  12448  -3532   -700   1443  A    N  
ATOM   1433  CA  GLU A 203      29.605 -23.686   5.735  1.00 87.78      A    C  
ANISOU 1433  CA  GLU A 203    11643   9379  12331  -3424   -555   1414  A    C  
ATOM   1434  C   GLU A 203      29.597 -23.002   4.360  1.00 85.60      A    C  
ANISOU 1434  C   GLU A 203    11139   9266  12120  -3228   -547   1235  A    C  
ATOM   1435  O   GLU A 203      30.503 -23.198   3.551  1.00 83.72      A    O  
ANISOU 1435  O   GLU A 203    10953   8873  11983  -3042   -655   1145  A    O  
ATOM   1436  CB  GLU A 203      30.497 -22.901   6.698  1.00 86.75      A    C  
ANISOU 1436  CB  GLU A 203    11587   9242  12134  -3247   -544   1507  A    C  
ATOM   1437  CG  GLU A 203      30.262 -21.400   6.663  1.00 85.43      A    C  
ANISOU 1437  CG  GLU A 203    11188   9383  11889  -3089   -412   1458  A    C  
ATOM   1438  CD  GLU A 203      28.992 -20.983   7.380  1.00 92.05      A    C  
ANISOU 1438  CD  GLU A 203    11902  10482  12593  -3279   -245   1517  A    C  
ATOM   1439  OE1 GLU A 203      28.944 -21.097   8.624  1.00 89.52      A    O  
ANISOU 1439  OE1 GLU A 203    11716  10132  12167  -3400   -204   1656  A    O  
ATOM   1440  OE2 GLU A 203      28.046 -20.526   6.704  1.00 95.29      A    O1-
ANISOU 1440  OE2 GLU A 203    12074  11137  12993  -3299   -153   1424  A    O1-
ATOM   1441  N   ARG A 204      28.569 -22.200   4.104  1.00 83.16      A    N  
ANISOU 1441  N   ARG A 204    10578   9275  11744  -3264   -418   1186  A    N  
ATOM   1442  CA  ARG A 204      28.434 -21.511   2.822  1.00 83.77      A    C  
ANISOU 1442  CA  ARG A 204    10439   9528  11863  -3090   -407   1030  A    C  
ATOM   1443  C   ARG A 204      28.290 -20.016   3.038  1.00 85.80      A    C  
ANISOU 1443  C   ARG A 204    10514  10054  12031  -2913   -284   1028  A    C  
ATOM   1444  O   ARG A 204      28.243 -19.237   2.092  1.00 92.92      A    O  
ANISOU 1444  O   ARG A 204    11247  11111  12948  -2739   -265    920  A    O  
ATOM   1445  CB  ARG A 204      27.231 -22.047   2.042  1.00 84.35      A    C  
ANISOU 1445  CB  ARG A 204    10367   9731  11951  -3296   -394    947  A    C  
ATOM   1446  CG  ARG A 204      27.373 -23.499   1.638  1.00 90.73      A    C  
ANISOU 1446  CG  ARG A 204    11364  10258  12852  -3463   -525    920  A    C  
ATOM   1447  CD  ARG A 204      26.135 -23.999   0.935  1.00101.25      A    C  
ANISOU 1447  CD  ARG A 204    12549  11734  14186  -3699   -514    839  A    C  
ATOM   1448  NE  ARG A 204      25.964 -23.396  -0.382  1.00105.13      A    N  
ANISOU 1448  NE  ARG A 204    12830  12412  14702  -3532   -524    679  A    N  
ATOM   1449  CZ  ARG A 204      26.527 -23.863  -1.491  1.00110.29      A    C  
ANISOU 1449  CZ  ARG A 204    13551  12911  15442  -3430   -640    551  A    C  
ATOM   1450  NH1 ARG A 204      27.310 -24.936  -1.438  1.00109.15      A    N1+
ANISOU 1450  NH1 ARG A 204    13676  12417  15378  -3461   -756    557  A    N1+
ATOM   1451  NH2 ARG A 204      26.316 -23.254  -2.652  1.00111.15      A    N  
ANISOU 1451  NH2 ARG A 204    13466  13214  15551  -3286   -641    416  A    N  
ATOM   1452  N   ASP A 205      28.205 -19.625   4.300  1.00 83.08      A    N  
ANISOU 1452  N   ASP A 205    10223   9758  11588  -2962   -200   1150  A    N  
ATOM   1453  CA  ASP A 205      28.143 -18.227   4.664  1.00 88.72      A    C  
ANISOU 1453  CA  ASP A 205    10813  10688  12210  -2793    -85   1155  A    C  
ATOM   1454  C   ASP A 205      29.437 -17.901   5.400  1.00 88.39      A    C  
ANISOU 1454  C   ASP A 205    10959  10468  12158  -2644   -138   1226  A    C  
ATOM   1455  O   ASP A 205      29.436 -17.618   6.597  1.00 92.21      A    O  
ANISOU 1455  O   ASP A 205    11525  10970  12539  -2694    -76   1333  A    O  
ATOM   1456  CB  ASP A 205      26.934 -17.975   5.560  1.00 96.56      A    C  
ANISOU 1456  CB  ASP A 205    11702  11910  13077  -2969     67   1225  A    C  
ATOM   1457  CG  ASP A 205      26.499 -16.528   5.556  1.00110.14      A    C  
ANISOU 1457  CG  ASP A 205    13228  13907  14711  -2789    197   1181  A    C  
ATOM   1458  OD1 ASP A 205      27.108 -15.722   4.824  1.00115.21      A    O  
ANISOU 1458  OD1 ASP A 205    13825  14558  15393  -2543    165   1101  A    O  
ATOM   1459  OD2 ASP A 205      25.543 -16.197   6.287  1.00119.12      A    O1-
ANISOU 1459  OD2 ASP A 205    14264  15255  15739  -2891    334   1225  A    O1-
ATOM   1460  N   TYR A 206      30.546 -17.978   4.673  1.00 82.43      A    N  
ANISOU 1460  N   TYR A 206    10267   9549  11504  -2466   -254   1164  A    N  
ATOM   1461  CA  TYR A 206      31.870 -17.768   5.249  1.00 78.23      A    C  
ANISOU 1461  CA  TYR A 206     9896   8848  10981  -2324   -328   1221  A    C  
ATOM   1462  C   TYR A 206      32.454 -16.455   4.747  1.00 77.09      A    C  
ANISOU 1462  C   TYR A 206     9642   8819  10830  -2075   -297   1148  A    C  
ATOM   1463  O   TYR A 206      31.948 -15.870   3.783  1.00 78.78      A    O  
ANISOU 1463  O   TYR A 206     9681   9200  11054  -1996   -243   1047  A    O  
ATOM   1464  CB  TYR A 206      32.795 -18.924   4.872  1.00 68.48      A    C  
ANISOU 1464  CB  TYR A 206     8824   7327   9869  -2308   -490   1213  A    C  
ATOM   1465  CG  TYR A 206      32.829 -19.172   3.389  1.00 70.89      A    C  
ANISOU 1465  CG  TYR A 206     9026   7628  10280  -2223   -538   1065  A    C  
ATOM   1466  CD1 TYR A 206      32.067 -20.188   2.809  1.00 70.30      A    C  
ANISOU 1466  CD1 TYR A 206     8950   7506  10254  -2394   -568   1018  A    C  
ATOM   1467  CD2 TYR A 206      33.602 -18.374   2.558  1.00 67.60      A    C  
ANISOU 1467  CD2 TYR A 206     8520   7263   9904  -1985   -552    972  A    C  
ATOM   1468  CE1 TYR A 206      32.093 -20.411   1.435  1.00 69.00      A    C  
ANISOU 1468  CE1 TYR A 206     8702   7343  10173  -2316   -615    874  A    C  
ATOM   1469  CE2 TYR A 206      33.633 -18.581   1.193  1.00 68.19      A    C  
ANISOU 1469  CE2 TYR A 206     8507   7346  10057  -1907   -589    837  A    C  
ATOM   1470  CZ  TYR A 206      32.884 -19.598   0.634  1.00 70.30      A    C  
ANISOU 1470  CZ  TYR A 206     8779   7565  10368  -2066   -624    784  A    C  
ATOM   1471  OH  TYR A 206      32.938 -19.780  -0.730  1.00 68.47      A    O  
ANISOU 1471  OH  TYR A 206     8469   7346  10199  -1983   -664    642  A    O  
ATOM   1472  N   GLY A 207      33.520 -15.999   5.401  1.00 71.12      A    N  
ANISOU 1472  N   GLY A 207     8997   7974  10054  -1961   -337   1202  A    N  
ATOM   1473  CA  GLY A 207      34.137 -14.725   5.075  1.00 65.16      A    C  
ANISOU 1473  CA  GLY A 207     8165   7311   9280  -1754   -307   1148  A    C  
ATOM   1474  C   GLY A 207      35.650 -14.777   5.097  1.00 66.80      A    C  
ANISOU 1474  C   GLY A 207     8479   7347   9554  -1619   -428   1157  A    C  
ATOM   1475  O   GLY A 207      36.240 -15.838   4.874  1.00 63.24      A    O  
ANISOU 1475  O   GLY A 207     8117   6711   9200  -1629   -546   1159  A    O  
ATOM   1476  N   PRO A 208      36.290 -13.622   5.354  1.00 65.47      A    N  
ANISOU 1476  N   PRO A 208     8299   7242   9335  -1490   -401   1157  A    N  
ATOM   1477  CA  PRO A 208      37.755 -13.468   5.355  1.00 59.50      A    C  
ANISOU 1477  CA  PRO A 208     7605   6370   8634  -1358   -506   1159  A    C  
ATOM   1478  C   PRO A 208      38.517 -14.440   6.255  1.00 61.57      A    C  
ANISOU 1478  C   PRO A 208     8037   6436   8921  -1411   -635   1256  A    C  
ATOM   1479  O   PRO A 208      39.658 -14.766   5.949  1.00 60.73      A    O  
ANISOU 1479  O   PRO A 208     7956   6215   8904  -1302   -748   1238  A    O  
ATOM   1480  CB  PRO A 208      37.952 -12.026   5.828  1.00 52.59      A    C  
ANISOU 1480  CB  PRO A 208     6711   5615   7655  -1285   -430   1167  A    C  
ATOM   1481  CG  PRO A 208      36.742 -11.321   5.313  1.00 59.46      A    C  
ANISOU 1481  CG  PRO A 208     7453   6671   8470  -1285   -292   1109  A    C  
ATOM   1482  CD  PRO A 208      35.603 -12.316   5.404  1.00 58.41      A    C  
ANISOU 1482  CD  PRO A 208     7304   6552   8338  -1444   -264   1131  A    C  
ATOM   1483  N   PRO A 209      37.907 -14.892   7.357  1.00 66.64      A    N  
ANISOU 1483  N   PRO A 209     8794   7048   9479  -1571   -617   1362  A    N  
ATOM   1484  CA  PRO A 209      38.608 -15.865   8.199  1.00 63.98      A    C  
ANISOU 1484  CA  PRO A 209     8639   6511   9159  -1619   -751   1468  A    C  
ATOM   1485  C   PRO A 209      39.107 -17.115   7.468  1.00 62.61      A    C  
ANISOU 1485  C   PRO A 209     8510   6145   9133  -1581   -879   1435  A    C  
ATOM   1486  O   PRO A 209      40.051 -17.735   7.954  1.00 63.83      A    O  
ANISOU 1486  O   PRO A 209     8795   6131   9328  -1535  -1015   1499  A    O  
ATOM   1487  CB  PRO A 209      37.555 -16.233   9.243  1.00 65.58      A    C  
ANISOU 1487  CB  PRO A 209     8939   6734   9243  -1829   -680   1574  A    C  
ATOM   1488  CG  PRO A 209      36.775 -14.974   9.403  1.00 63.67      A    C  
ANISOU 1488  CG  PRO A 209     8582   6725   8886  -1832   -516   1541  A    C  
ATOM   1489  CD  PRO A 209      36.696 -14.371   8.017  1.00 61.73      A    C  
ANISOU 1489  CD  PRO A 209     8147   6584   8723  -1695   -473   1401  A    C  
ATOM   1490  N   ILE A 210      38.521 -17.489   6.335  1.00 59.42      A    N  
ANISOU 1490  N   ILE A 210     8009   5762   8808  -1589   -846   1333  A    N  
ATOM   1491  CA  ILE A 210      39.026 -18.682   5.641  1.00 70.23      A    C  
ANISOU 1491  CA  ILE A 210     9441   6933  10312  -1543   -969   1288  A    C  
ATOM   1492  C   ILE A 210      40.422 -18.454   5.069  1.00 67.25      A    C  
ANISOU 1492  C   ILE A 210     9016   6510  10024  -1316  -1058   1221  A    C  
ATOM   1493  O   ILE A 210      41.246 -19.375   5.033  1.00 67.48      A    O  
ANISOU 1493  O   ILE A 210     9146   6347  10144  -1240  -1190   1229  A    O  
ATOM   1494  CB  ILE A 210      38.097 -19.192   4.511  1.00 68.12      A    C  
ANISOU 1494  CB  ILE A 210     9090   6692  10102  -1612   -924   1181  A    C  
ATOM   1495  CG1 ILE A 210      38.166 -18.256   3.298  1.00 59.34      A    C  
ANISOU 1495  CG1 ILE A 210     7777   5756   9014  -1464   -856   1043  A    C  
ATOM   1496  CG2 ILE A 210      36.665 -19.411   5.031  1.00 56.32      A    C  
ANISOU 1496  CG2 ILE A 210     7606   5274   8519  -1854   -829   1242  A    C  
ATOM   1497  CD1 ILE A 210      37.367 -18.749   2.092  1.00 57.53      A    C  
ANISOU 1497  CD1 ILE A 210     7462   5559   8836  -1512   -832    926  A    C  
ATOM   1498  N   ASP A 211      40.687 -17.229   4.626  1.00 56.85      A    N  
ANISOU 1498  N   ASP A 211     7548   5371   8681  -1207   -984   1156  A    N  
ATOM   1499  CA  ASP A 211      41.997 -16.901   4.081  1.00 61.03      A    C  
ANISOU 1499  CA  ASP A 211     8009   5894   9283  -1012  -1049   1094  A    C  
ATOM   1500  C   ASP A 211      43.048 -16.875   5.189  1.00 65.56      A    C  
ANISOU 1500  C   ASP A 211     8682   6389   9838   -969  -1154   1198  A    C  
ATOM   1501  O   ASP A 211      44.221 -17.208   4.970  1.00 59.29      A    O  
ANISOU 1501  O   ASP A 211     7881   5515   9131   -825  -1264   1175  A    O  
ATOM   1502  CB  ASP A 211      41.966 -15.568   3.323  1.00 57.45      A    C  
ANISOU 1502  CB  ASP A 211     7386   5647   8795   -933   -937   1008  A    C  
ATOM   1503  CG  ASP A 211      41.266 -15.677   1.979  1.00 58.67      A    C  
ANISOU 1503  CG  ASP A 211     7430   5871   8991   -918   -871    887  A    C  
ATOM   1504  OD1 ASP A 211      41.111 -16.810   1.474  1.00 58.77      A    O  
ANISOU 1504  OD1 ASP A 211     7486   5761   9082   -936   -930    843  A    O  
ATOM   1505  OD2 ASP A 211      40.872 -14.631   1.426  1.00 61.13      A    O1-
ANISOU 1505  OD2 ASP A 211     7623   6355   9250   -888   -767    836  A    O1-
ATOM   1506  N   LEU A 212      42.618 -16.495   6.386  1.00 61.00      A    N  
ANISOU 1506  N   LEU A 212     8192   5845   9140  -1090  -1123   1309  A    N  
ATOM   1507  CA  LEU A 212      43.550 -16.374   7.500  1.00 64.17      A    C  
ANISOU 1507  CA  LEU A 212     8691   6194   9498  -1064  -1225   1411  A    C  
ATOM   1508  C   LEU A 212      43.966 -17.728   8.064  1.00 68.15      A    C  
ANISOU 1508  C   LEU A 212     9366   6475  10054  -1071  -1379   1499  A    C  
ATOM   1509  O   LEU A 212      45.109 -17.912   8.479  1.00 69.20      A    O  
ANISOU 1509  O   LEU A 212     9539   6535  10220   -963  -1514   1541  A    O  
ATOM   1510  CB  LEU A 212      42.988 -15.443   8.573  1.00 60.70      A    C  
ANISOU 1510  CB  LEU A 212     8297   5872   8894  -1181  -1136   1489  A    C  
ATOM   1511  CG  LEU A 212      43.294 -13.997   8.166  1.00 64.22      A    C  
ANISOU 1511  CG  LEU A 212     8603   6493   9305  -1099  -1052   1411  A    C  
ATOM   1512  CD1 LEU A 212      42.279 -13.044   8.718  1.00 76.10      A    C  
ANISOU 1512  CD1 LEU A 212    10115   8136  10664  -1201   -906   1431  A    C  
ATOM   1513  CD2 LEU A 212      44.704 -13.604   8.601  1.00 62.22      A    C  
ANISOU 1513  CD2 LEU A 212     8354   6227   9060  -1003  -1168   1436  A    C  
ATOM   1514  N   TRP A 213      43.035 -18.675   8.058  1.00 72.45      A    N  
ANISOU 1514  N   TRP A 213    10011   6912  10606  -1200  -1364   1527  A    N  
ATOM   1515  CA  TRP A 213      43.346 -20.046   8.408  1.00 68.13      A    C  
ANISOU 1515  CA  TRP A 213     9646   6120  10119  -1207  -1508   1601  A    C  
ATOM   1516  C   TRP A 213      44.475 -20.507   7.509  1.00 67.59      A    C  
ANISOU 1516  C   TRP A 213     9518   5958  10204   -987  -1620   1505  A    C  
ATOM   1517  O   TRP A 213      45.428 -21.149   7.958  1.00 67.65      A    O  
ANISOU 1517  O   TRP A 213     9627   5814  10260   -880  -1776   1565  A    O  
ATOM   1518  CB  TRP A 213      42.131 -20.945   8.193  1.00 70.72      A    C  
ANISOU 1518  CB  TRP A 213    10061   6356  10453  -1387  -1457   1609  A    C  
ATOM   1519  CG  TRP A 213      42.473 -22.393   8.344  1.00 74.84      A    C  
ANISOU 1519  CG  TRP A 213    10785   6594  11056  -1381  -1608   1665  A    C  
ATOM   1520  CD1 TRP A 213      42.911 -23.239   7.367  1.00 76.60      A    C  
ANISOU 1520  CD1 TRP A 213    11019   6663  11425  -1255  -1691   1565  A    C  
ATOM   1521  CD2 TRP A 213      42.432 -23.158   9.551  1.00 74.04      A    C  
ANISOU 1521  CD2 TRP A 213    10925   6319  10888  -1497  -1699   1835  A    C  
ATOM   1522  CE2 TRP A 213      42.851 -24.463   9.231  1.00 81.22      A    C  
ANISOU 1522  CE2 TRP A 213    11989   6955  11915  -1429  -1840   1834  A    C  
ATOM   1523  CE3 TRP A 213      42.078 -22.868  10.871  1.00 78.60      A    C  
ANISOU 1523  CE3 TRP A 213    11614   6942  11308  -1649  -1672   1988  A    C  
ATOM   1524  NE1 TRP A 213      43.140 -24.485   7.891  1.00 83.34      A    N  
ANISOU 1524  NE1 TRP A 213    12110   7241  12313  -1277  -1830   1660  A    N  
ATOM   1525  CZ2 TRP A 213      42.925 -25.478  10.183  1.00 81.56      A    C  
ANISOU 1525  CZ2 TRP A 213    12303   6758  11927  -1510  -1962   1992  A    C  
ATOM   1526  CZ3 TRP A 213      42.152 -23.880  11.819  1.00 79.86      A    C  
ANISOU 1526  CZ3 TRP A 213    12035   6880  11428  -1739  -1788   2146  A    C  
ATOM   1527  CH2 TRP A 213      42.572 -25.165  11.469  1.00 79.29      A    C  
ANISOU 1527  CH2 TRP A 213    12120   6527  11479  -1670  -1935   2152  A    C  
ATOM   1528  N   GLY A 214      44.357 -20.171   6.229  1.00 65.43      A    N  
ANISOU 1528  N   GLY A 214     9075   5785  10000   -911  -1539   1355  A    N  
ATOM   1529  CA  GLY A 214      45.396 -20.476   5.267  1.00 71.50      A    C  
ANISOU 1529  CA  GLY A 214     9758   6508  10901   -697  -1614   1243  A    C  
ATOM   1530  C   GLY A 214      46.703 -19.757   5.564  1.00 66.66      A    C  
ANISOU 1530  C   GLY A 214     9048   5985  10293   -541  -1677   1255  A    C  
ATOM   1531  O   GLY A 214      47.779 -20.278   5.279  1.00 66.35      A    O  
ANISOU 1531  O   GLY A 214     8991   5864  10356   -362  -1792   1219  A    O  
ATOM   1532  N   ALA A 215      46.611 -18.553   6.119  1.00 58.26      A    N  
ANISOU 1532  N   ALA A 215     7920   5096   9119   -609  -1602   1297  A    N  
ATOM   1533  CA  ALA A 215      47.797 -17.797   6.485  1.00 58.44      A    C  
ANISOU 1533  CA  ALA A 215     7857   5215   9131   -502  -1663   1313  A    C  
ATOM   1534  C   ALA A 215      48.496 -18.571   7.590  1.00 63.90      A    C  
ANISOU 1534  C   ALA A 215     8701   5753   9824   -469  -1839   1439  A    C  
ATOM   1535  O   ALA A 215      49.713 -18.737   7.579  1.00 62.14      A    O  
ANISOU 1535  O   ALA A 215     8421   5517   9674   -307  -1962   1430  A    O  
ATOM   1536  CB  ALA A 215      47.420 -16.387   6.964  1.00 49.91      A    C  
ANISOU 1536  CB  ALA A 215     6724   4323   7917   -608  -1548   1339  A    C  
ATOM   1537  N   GLY A 216      47.704 -19.049   8.542  1.00 65.03      A    N  
ANISOU 1537  N   GLY A 216     9036   5790   9880   -625  -1851   1560  A    N  
ATOM   1538  CA  GLY A 216      48.206 -19.923   9.581  1.00 75.55      A    C  
ANISOU 1538  CA  GLY A 216    10555   6948  11202   -610  -2022   1695  A    C  
ATOM   1539  C   GLY A 216      48.996 -21.111   9.051  1.00 78.66      A    C  
ANISOU 1539  C   GLY A 216    10983   7153  11750   -423  -2168   1659  A    C  
ATOM   1540  O   GLY A 216      50.142 -21.321   9.454  1.00 81.96      A    O  
ANISOU 1540  O   GLY A 216    11400   7534  12207   -270  -2323   1700  A    O  
ATOM   1541  N   CYS A 217      48.390 -21.892   8.155  1.00 73.65      A    N  
ANISOU 1541  N   CYS A 217    10380   6402  11200   -428  -2124   1579  A    N  
ATOM   1542  CA  CYS A 217      49.038 -23.098   7.639  1.00 76.26      A    C  
ANISOU 1542  CA  CYS A 217    10778   6524  11673   -248  -2257   1534  A    C  
ATOM   1543  C   CYS A 217      50.343 -22.759   6.927  1.00 79.94      A    C  
ANISOU 1543  C   CYS A 217    11033   7099  12242      4  -2305   1421  A    C  
ATOM   1544  O   CYS A 217      51.315 -23.523   6.976  1.00 82.08      A    O  
ANISOU 1544  O   CYS A 217    11341   7242  12606    202  -2460   1427  A    O  
ATOM   1545  CB  CYS A 217      48.112 -23.865   6.690  1.00 77.03      A    C  
ANISOU 1545  CB  CYS A 217    10935   6499  11835   -315  -2185   1440  A    C  
ATOM   1546  SG  CYS A 217      46.545 -24.427   7.411  1.00 83.65      A    S  
ANISOU 1546  SG  CYS A 217    12007   7209  12567   -632  -2126   1563  A    S  
ATOM   1547  N   ILE A 218      50.359 -21.608   6.266  1.00 71.19      A    N  
ANISOU 1547  N   ILE A 218     9704   6231  11114     -1  -2170   1322  A    N  
ATOM   1548  CA  ILE A 218      51.546 -21.155   5.556  1.00 69.07      A    C  
ANISOU 1548  CA  ILE A 218     9213   6103  10926    203  -2187   1215  A    C  
ATOM   1549  C   ILE A 218      52.616 -20.682   6.534  1.00 74.32      A    C  
ANISOU 1549  C   ILE A 218     9831   6852  11556    266  -2308   1310  A    C  
ATOM   1550  O   ILE A 218      53.808 -20.960   6.357  1.00 71.93      A    O  
ANISOU 1550  O   ILE A 218     9425   6560  11344    472  -2420   1275  A    O  
ATOM   1551  CB  ILE A 218      51.209 -20.028   4.561  1.00 53.72      A    C  
ANISOU 1551  CB  ILE A 218     7068   4387   8957    157  -2003   1093  A    C  
ATOM   1552  CG1 ILE A 218      50.473 -20.602   3.363  1.00 50.32      A    C  
ANISOU 1552  CG1 ILE A 218     6643   3890   8588    162  -1916    968  A    C  
ATOM   1553  CG2 ILE A 218      52.479 -19.326   4.070  1.00 54.95      A    C  
ANISOU 1553  CG2 ILE A 218     6993   4726   9162    319  -2011   1016  A    C  
ATOM   1554  CD1 ILE A 218      49.644 -19.571   2.612  1.00 53.76      A    C  
ANISOU 1554  CD1 ILE A 218     6955   4514   8956     47  -1732    891  A    C  
ATOM   1555  N   MET A 219      52.194 -19.961   7.566  1.00 71.81      A    N  
ANISOU 1555  N   MET A 219     9581   6603  11099     90  -2285   1423  A    N  
ATOM   1556  CA  MET A 219      53.149 -19.482   8.549  1.00 72.07      A    C  
ANISOU 1556  CA  MET A 219     9585   6720  11080    123  -2407   1513  A    C  
ATOM   1557  C   MET A 219      53.900 -20.670   9.139  1.00 69.23      A    C  
ANISOU 1557  C   MET A 219     9350   6170  10784    275  -2622   1599  A    C  
ATOM   1558  O   MET A 219      55.124 -20.691   9.146  1.00 73.55      A    O  
ANISOU 1558  O   MET A 219     9768   6780  11399    456  -2746   1582  A    O  
ATOM   1559  CB  MET A 219      52.473 -18.660   9.650  1.00 65.97      A    C  
ANISOU 1559  CB  MET A 219     8917   6017  10133    -96  -2354   1624  A    C  
ATOM   1560  CG  MET A 219      53.475 -17.954  10.547  1.00 67.82      A    C  
ANISOU 1560  CG  MET A 219     9095   6375  10299    -78  -2466   1690  A    C  
ATOM   1561  SD  MET A 219      52.748 -16.803  11.715  1.00 80.61      A    S  
ANISOU 1561  SD  MET A 219    10823   8103  11702   -323  -2382   1783  A    S  
ATOM   1562  CE  MET A 219      54.138 -16.464  12.791  1.00 97.49      A    C  
ANISOU 1562  CE  MET A 219    12933  10322  13787   -264  -2591   1867  A    C  
ATOM   1563  N   ALA A 220      53.154 -21.661   9.617  1.00 72.82      A    N  
ANISOU 1563  N   ALA A 220    10055   6396  11218    201  -2667   1691  A    N  
ATOM   1564  CA  ALA A 220      53.741 -22.862  10.204  1.00 81.97      A    C  
ANISOU 1564  CA  ALA A 220    11383   7333  12429    339  -2876   1788  A    C  
ATOM   1565  C   ALA A 220      54.678 -23.538   9.212  1.00 83.64      A    C  
ANISOU 1565  C   ALA A 220    11471   7492  12817    620  -2950   1663  A    C  
ATOM   1566  O   ALA A 220      55.673 -24.144   9.595  1.00 83.69      A    O  
ANISOU 1566  O   ALA A 220    11496   7418  12883    819  -3138   1711  A    O  
ATOM   1567  CB  ALA A 220      52.644 -23.831  10.643  1.00 83.79      A    C  
ANISOU 1567  CB  ALA A 220    11911   7312  12615    187  -2877   1889  A    C  
ATOM   1568  N   GLU A 221      54.348 -23.414   7.932  1.00 86.20      A    N  
ANISOU 1568  N   GLU A 221    11665   7869  13216    644  -2802   1500  A    N  
ATOM   1569  CA  GLU A 221      55.107 -24.038   6.860  1.00 84.11      A    C  
ANISOU 1569  CA  GLU A 221    11284   7564  13108    901  -2837   1356  A    C  
ATOM   1570  C   GLU A 221      56.465 -23.367   6.667  1.00 81.43      A    C  
ANISOU 1570  C   GLU A 221    10664   7459  12817   1085  -2882   1297  A    C  
ATOM   1571  O   GLU A 221      57.373 -23.954   6.078  1.00 90.12      A    O  
ANISOU 1571  O   GLU A 221    11663   8536  14042   1341  -2958   1207  A    O  
ATOM   1572  CB  GLU A 221      54.292 -23.995   5.564  1.00 92.97      A    C  
ANISOU 1572  CB  GLU A 221    12352   8704  14268    844  -2654   1200  A    C  
ATOM   1573  CG  GLU A 221      54.781 -24.917   4.460  1.00101.27      A    C  
ANISOU 1573  CG  GLU A 221    13370   9642  15467   1083  -2682   1049  A    C  
ATOM   1574  CD  GLU A 221      53.678 -25.283   3.472  1.00102.77      A    C  
ANISOU 1574  CD  GLU A 221    13637   9741  15671    978  -2548    937  A    C  
ATOM   1575  OE1 GLU A 221      52.486 -25.116   3.816  1.00 96.30      A    O  
ANISOU 1575  OE1 GLU A 221    12944   8886  14758    723  -2470   1006  A    O  
ATOM   1576  OE2 GLU A 221      54.007 -25.748   2.358  1.00104.77      A    O1-
ANISOU 1576  OE2 GLU A 221    13820   9967  16022   1150  -2523    777  A    O1-
ATOM   1577  N   MET A 222      56.608 -22.145   7.175  1.00 73.98      A    N  
ANISOU 1577  N   MET A 222     9596   6742  11772    952  -2836   1343  A    N  
ATOM   1578  CA  MET A 222      57.871 -21.408   7.062  1.00 81.93      A    C  
ANISOU 1578  CA  MET A 222    10330   7991  12810   1077  -2877   1296  A    C  
ATOM   1579  C   MET A 222      58.996 -22.056   7.878  1.00 86.33      A    C  
ANISOU 1579  C   MET A 222    10898   8492  13413   1273  -3117   1385  A    C  
ATOM   1580  O   MET A 222      60.178 -21.837   7.606  1.00 79.98      A    O  
ANISOU 1580  O   MET A 222     9852   7856  12679   1449  -3179   1323  A    O  
ATOM   1581  CB  MET A 222      57.690 -19.939   7.469  1.00 77.10      A    C  
ANISOU 1581  CB  MET A 222     9620   7606  12067    861  -2776   1328  A    C  
ATOM   1582  CG  MET A 222      56.746 -19.144   6.562  1.00 76.81      A    C  
ANISOU 1582  CG  MET A 222     9526   7665  11991    708  -2543   1229  A    C  
ATOM   1583  SD  MET A 222      57.397 -18.856   4.895  1.00 73.68      A    S  
ANISOU 1583  SD  MET A 222     8841   7442  11711    868  -2420   1028  A    S  
ATOM   1584  CE  MET A 222      58.850 -17.862   5.243  1.00 70.63      A    C  
ANISOU 1584  CE  MET A 222     8194   7326  11317    913  -2489   1036  A    C  
ATOM   1585  N   TRP A 223      58.616 -22.849   8.878  1.00 87.74      A    N  
ANISOU 1585  N   TRP A 223    11352   8442  13544   1238  -3251   1534  A    N  
ATOM   1586  CA  TRP A 223      59.577 -23.572   9.704  1.00 85.80      A    C  
ANISOU 1586  CA  TRP A 223    11162   8108  13331   1431  -3497   1637  A    C  
ATOM   1587  C   TRP A 223      59.558 -25.064   9.387  1.00 94.14      A    C  
ANISOU 1587  C   TRP A 223    12402   8862  14503   1636  -3597   1627  A    C  
ATOM   1588  O   TRP A 223      60.610 -25.677   9.237  1.00 96.65      A    O  
ANISOU 1588  O   TRP A 223    12631   9159  14934   1923  -3744   1595  A    O  
ATOM   1589  CB  TRP A 223      59.299 -23.359  11.194  1.00 80.14      A    C  
ANISOU 1589  CB  TRP A 223    10643   7352  12454   1253  -3605   1834  A    C  
ATOM   1590  CG  TRP A 223      59.683 -22.001  11.705  1.00 80.48      A    C  
ANISOU 1590  CG  TRP A 223    10511   7680  12388   1114  -3580   1853  A    C  
ATOM   1591  CD1 TRP A 223      60.907 -21.617  12.167  1.00 79.25      A    C  
ANISOU 1591  CD1 TRP A 223    10172   7704  12235   1224  -3733   1876  A    C  
ATOM   1592  CD2 TRP A 223      58.831 -20.848  11.818  1.00 78.51      A    C  
ANISOU 1592  CD2 TRP A 223    10261   7561  12007    835  -3396   1847  A    C  
ATOM   1593  CE2 TRP A 223      59.609 -19.805  12.355  1.00 78.23      A    C  
ANISOU 1593  CE2 TRP A 223    10060   7764  11899    785  -3448   1865  A    C  
ATOM   1594  CE3 TRP A 223      57.486 -20.600  11.518  1.00 73.19      A    C  
ANISOU 1594  CE3 TRP A 223     9708   6831  11271    630  -3197   1826  A    C  
ATOM   1595  NE1 TRP A 223      60.872 -20.298  12.558  1.00 81.67      A    N  
ANISOU 1595  NE1 TRP A 223    10378   8233  12418   1015  -3657   1883  A    N  
ATOM   1596  CZ2 TRP A 223      59.091 -18.533  12.592  1.00 77.11      A    C  
ANISOU 1596  CZ2 TRP A 223     9895   7778  11624    545  -3306   1858  A    C  
ATOM   1597  CZ3 TRP A 223      56.971 -19.339  11.762  1.00 68.05      A    C  
ANISOU 1597  CZ3 TRP A 223     9016   6351  10490    410  -3056   1823  A    C  
ATOM   1598  CH2 TRP A 223      57.771 -18.322  12.290  1.00 72.95      A    C  
ANISOU 1598  CH2 TRP A 223     9496   7182  11041    373  -3109   1837  A    C  
ATOM   1599  N   THR A 224      58.368 -25.652   9.283  1.00 95.44      A    N  
ANISOU 1599  N   THR A 224    12825   8796  14644   1491  -3519   1650  A    N  
ATOM   1600  CA  THR A 224      58.278 -27.088   9.018  1.00 98.14      A    C  
ANISOU 1600  CA  THR A 224    13385   8815  15087   1656  -3616   1644  A    C  
ATOM   1601  C   THR A 224      58.660 -27.432   7.583  1.00100.41      A    C  
ANISOU 1601  C   THR A 224    13507   9117  15528   1875  -3539   1431  A    C  
ATOM   1602  O   THR A 224      58.872 -28.600   7.262  1.00104.45      A    O  
ANISOU 1602  O   THR A 224    14159   9381  16145   2082  -3636   1393  A    O  
ATOM   1603  CB  THR A 224      56.880 -27.676   9.312  1.00 90.11      A    C  
ANISOU 1603  CB  THR A 224    12700   7540  13999   1411  -3558   1730  A    C  
ATOM   1604  CG2 THR A 224      56.438 -27.341  10.725  1.00 88.66      A    C  
ANISOU 1604  CG2 THR A 224    12689   7353  13646   1183  -3613   1938  A    C  
ATOM   1605  OG1 THR A 224      55.930 -27.168   8.367  1.00 82.15      A    O  
ANISOU 1605  OG1 THR A 224    11610   6624  12981   1235  -3328   1601  A    O  
ATOM   1606  N   ARG A 225      58.734 -26.424   6.720  1.00 97.73      A    N  
ANISOU 1606  N   ARG A 225    12886   9055  15193   1831  -3364   1291  A    N  
ATOM   1607  CA  ARG A 225      59.152 -26.655   5.343  1.00 95.56      A    C  
ANISOU 1607  CA  ARG A 225    12433   8832  15042   2035  -3278   1084  A    C  
ATOM   1608  C   ARG A 225      58.231 -27.651   4.634  1.00 97.73      A    C  
ANISOU 1608  C   ARG A 225    12940   8828  15366   2017  -3220   1007  A    C  
ATOM   1609  O   ARG A 225      58.621 -28.289   3.657  1.00 97.64      A    O  
ANISOU 1609  O   ARG A 225    12882   8749  15467   2240  -3210    851  A    O  
ATOM   1610  CB  ARG A 225      60.585 -27.179   5.325  1.00 91.53      A    C  
ANISOU 1610  CB  ARG A 225    11781   8347  14648   2390  -3444   1048  A    C  
ATOM   1611  CG  ARG A 225      61.618 -26.131   5.637  1.00 88.57      A    C  
ANISOU 1611  CG  ARG A 225    11091   8312  14250   2425  -3470   1062  A    C  
ATOM   1612  CD  ARG A 225      61.912 -25.300   4.407  1.00 90.28      A    C  
ANISOU 1612  CD  ARG A 225    10992   8810  14499   2439  -3275    879  A    C  
ATOM   1613  NE  ARG A 225      62.783 -24.176   4.723  1.00 93.13      A    N  
ANISOU 1613  NE  ARG A 225    11063   9501  14821   2404  -3280    900  A    N  
ATOM   1614  CZ  ARG A 225      63.663 -23.650   3.879  1.00 93.29      A    C  
ANISOU 1614  CZ  ARG A 225    10754   9792  14899   2525  -3199    764  A    C  
ATOM   1615  NH1 ARG A 225      63.800 -24.158   2.658  1.00 86.85      A    N1+
ANISOU 1615  NH1 ARG A 225     9859   8962  14179   2708  -3101    591  A    N1+
ATOM   1616  NH2 ARG A 225      64.416 -22.621   4.264  1.00 94.15      A    N  
ANISOU 1616  NH2 ARG A 225    10619  10189  14963   2453  -3214    799  A    N  
ATOM   1617  N   SER A 226      57.004 -27.773   5.125  1.00 98.72      A    N  
ANISOU 1617  N   SER A 226    13311   8798  15400   1744  -3179   1109  A    N  
ATOM   1618  CA  SER A 226      56.077 -28.764   4.603  1.00102.85      A    C  
ANISOU 1618  CA  SER A 226    14078   9041  15958   1685  -3145   1058  A    C  
ATOM   1619  C   SER A 226      54.691 -28.550   5.201  1.00100.98      A    C  
ANISOU 1619  C   SER A 226    14033   8741  15595   1326  -3064   1178  A    C  
ATOM   1620  O   SER A 226      54.567 -28.226   6.384  1.00104.85      A    O  
ANISOU 1620  O   SER A 226    14606   9249  15982   1189  -3124   1354  A    O  
ATOM   1621  CB  SER A 226      56.588 -30.170   4.933  1.00105.52      A    C  
ANISOU 1621  CB  SER A 226    14657   9047  16389   1915  -3351   1103  A    C  
ATOM   1622  OG  SER A 226      55.779 -31.157   4.327  1.00112.23      A    O  
ANISOU 1622  OG  SER A 226    15746   9613  17284   1868  -3322   1030  A    O  
ATOM   1623  N   PRO A 227      53.642 -28.731   4.385  1.00 93.56      A    N  
ANISOU 1623  N   PRO A 227    13155   7740  14654   1174  -2927   1079  A    N  
ATOM   1624  CA  PRO A 227      52.261 -28.503   4.833  1.00 93.64      A    C  
ANISOU 1624  CA  PRO A 227    13306   7726  14546    830  -2828   1174  A    C  
ATOM   1625  C   PRO A 227      51.894 -29.333   6.064  1.00 89.90      A    C  
ANISOU 1625  C   PRO A 227    13154   6984  14020    714  -2964   1375  A    C  
ATOM   1626  O   PRO A 227      51.839 -30.555   5.997  1.00 88.57      A    O  
ANISOU 1626  O   PRO A 227    13226   6506  13920    779  -3068   1381  A    O  
ATOM   1627  CB  PRO A 227      51.422 -28.915   3.619  1.00 92.43      A    C  
ANISOU 1627  CB  PRO A 227    13180   7502  14439    762  -2711   1011  A    C  
ATOM   1628  CG  PRO A 227      52.338 -28.734   2.453  1.00 91.40      A    C  
ANISOU 1628  CG  PRO A 227    12818   7503  14407   1029  -2677    817  A    C  
ATOM   1629  CD  PRO A 227      53.712 -29.084   2.957  1.00 91.16      A    C  
ANISOU 1629  CD  PRO A 227    12764   7423  14449   1316  -2849    863  A    C  
ATOM   1630  N   ILE A 228      51.633 -28.649   7.173  1.00 90.41      A    N  
ANISOU 1630  N   ILE A 228    13235   7164  13954    535  -2957   1536  A    N  
ATOM   1631  CA  ILE A 228      51.387 -29.278   8.469  1.00 88.31      A    C  
ANISOU 1631  CA  ILE A 228    13258   6688  13607    420  -3084   1748  A    C  
ATOM   1632  C   ILE A 228      50.283 -30.344   8.496  1.00 90.43      A    C  
ANISOU 1632  C   ILE A 228    13829   6664  13867    221  -3076   1797  A    C  
ATOM   1633  O   ILE A 228      50.365 -31.294   9.276  1.00105.06      A    O  
ANISOU 1633  O   ILE A 228    15966   8242  15708    222  -3227   1942  A    O  
ATOM   1634  CB  ILE A 228      51.074 -28.212   9.536  1.00 87.01      A    C  
ANISOU 1634  CB  ILE A 228    13044   6740  13277    216  -3027   1886  A    C  
ATOM   1635  CG1 ILE A 228      49.880 -27.361   9.091  1.00 84.49      A    C  
ANISOU 1635  CG1 ILE A 228    12606   6615  12881    -39  -2798   1818  A    C  
ATOM   1636  CG2 ILE A 228      52.287 -27.329   9.760  1.00 89.65      A    C  
ANISOU 1636  CG2 ILE A 228    13143   7308  13613    403  -3088   1875  A    C  
ATOM   1637  CD1 ILE A 228      49.368 -26.402  10.141  1.00 79.58      A    C  
ANISOU 1637  CD1 ILE A 228    11977   6175  12086   -257  -2723   1947  A    C  
ATOM   1638  N   MET A 229      49.263 -30.192   7.655  1.00 84.55      A    N  
ANISOU 1638  N   MET A 229    13026   5976  13122     45  -2908   1682  A    N  
ATOM   1639  CA  MET A 229      48.113 -31.101   7.662  1.00 94.76      A    C  
ANISOU 1639  CA  MET A 229    14577   7031  14396   -195  -2883   1722  A    C  
ATOM   1640  C   MET A 229      47.722 -31.584   6.261  1.00100.20      A    C  
ANISOU 1640  C   MET A 229    15234   7646  15193   -169  -2814   1516  A    C  
ATOM   1641  O   MET A 229      46.960 -30.914   5.558  1.00 96.68      A    O  
ANISOU 1641  O   MET A 229    14608   7409  14717   -310  -2647   1409  A    O  
ATOM   1642  CB  MET A 229      46.912 -30.424   8.323  1.00 96.39      A    C  
ANISOU 1642  CB  MET A 229    14778   7401  14445   -542  -2738   1829  A    C  
ATOM   1643  CG  MET A 229      47.085 -30.178   9.808  1.00 97.09      A    C  
ANISOU 1643  CG  MET A 229    14984   7504  14402   -622  -2808   2047  A    C  
ATOM   1644  SD  MET A 229      45.715 -29.235  10.499  1.00125.97      A    S  
ANISOU 1644  SD  MET A 229    18589  11406  17868   -995  -2607   2139  A    S  
ATOM   1645  CE  MET A 229      45.980 -27.656   9.713  1.00101.82      A    C  
ANISOU 1645  CE  MET A 229    15128   8741  14816   -884  -2456   1969  A    C  
ATOM   1646  N   GLN A 230      48.219 -32.759   5.876  1.00109.24      A    N  
ANISOU 1646  N   GLN A 230    16568   8485  16454     13  -2949   1463  A    N  
ATOM   1647  CA  GLN A 230      48.071 -33.250   4.504  1.00112.31      A    C  
ANISOU 1647  CA  GLN A 230    16930   8794  16948     94  -2904   1245  A    C  
ATOM   1648  C   GLN A 230      47.052 -34.375   4.353  1.00113.40      A    C  
ANISOU 1648  C   GLN A 230    17370   8624  17094   -132  -2920   1251  A    C  
ATOM   1649  O   GLN A 230      47.415 -35.500   4.024  1.00112.68      A    O  
ANISOU 1649  O   GLN A 230    17500   8213  17101     14  -3042   1196  A    O  
ATOM   1650  CB  GLN A 230      49.424 -33.713   3.960  1.00112.34      A    C  
ANISOU 1650  CB  GLN A 230    16899   8699  17088    498  -3026   1130  A    C  
ATOM   1651  CG  GLN A 230      50.582 -32.829   4.380  1.00110.43      A    C  
ANISOU 1651  CG  GLN A 230    16414   8704  16842    721  -3063   1169  A    C  
ATOM   1652  CD  GLN A 230      51.847 -33.113   3.603  1.00108.27      A    C  
ANISOU 1652  CD  GLN A 230    16016   8422  16701   1113  -3136   1013  A    C  
ATOM   1653  NE2 GLN A 230      52.990 -32.759   4.181  1.00101.63      A    N  
ANISOU 1653  NE2 GLN A 230    15046   7694  15876   1334  -3238   1081  A    N  
ATOM   1654  OE1 GLN A 230      51.799 -33.638   2.493  1.00114.48      A    O  
ANISOU 1654  OE1 GLN A 230    16814   9114  17570   1214  -3101    828  A    O  
ATOM   1655  N   GLY A 231      45.778 -34.060   4.566  1.00117.64      A    N  
ANISOU 1655  N   GLY A 231    17908   9262  17528   -488  -2795   1308  A    N  
ATOM   1656  CA  GLY A 231      44.718 -35.049   4.470  1.00122.41      A    C  
ANISOU 1656  CA  GLY A 231    18775   9611  18126   -759  -2797   1323  A    C  
ATOM   1657  C   GLY A 231      44.547 -35.645   3.084  1.00126.24      A    C  
ANISOU 1657  C   GLY A 231    19271   9982  18712   -698  -2783   1092  A    C  
ATOM   1658  O   GLY A 231      45.105 -35.148   2.106  1.00126.06      A    O  
ANISOU 1658  O   GLY A 231    19014  10135  18748   -472  -2734    910  A    O  
ATOM   1659  N   ASN A 232      43.769 -36.721   3.001  1.00128.03      A    N  
ANISOU 1659  N   ASN A 232    19783   9912  18950   -915  -2824   1098  A    N  
ATOM   1660  CA  ASN A 232      43.505 -37.378   1.726  1.00125.08      A    C  
ANISOU 1660  CA  ASN A 232    19464   9403  18660   -897  -2820    878  A    C  
ATOM   1661  C   ASN A 232      42.047 -37.261   1.318  1.00121.82      A    C  
ANISOU 1661  C   ASN A 232    18999   9110  18176  -1284  -2691    833  A    C  
ATOM   1662  O   ASN A 232      41.720 -37.285   0.132  1.00120.82      A    O  
ANISOU 1662  O   ASN A 232    18773   9049  18085  -1287  -2635    627  A    O  
ATOM   1663  CB  ASN A 232      43.941 -38.839   1.776  1.00130.00      A    C  
ANISOU 1663  CB  ASN A 232    20480   9541  19375   -784  -2998    880  A    C  
ATOM   1664  CG  ASN A 232      45.447 -38.988   1.771  1.00134.43      A    C  
ANISOU 1664  CG  ASN A 232    21037  10009  20031   -327  -3122    845  A    C  
ATOM   1665  ND2 ASN A 232      46.097 -38.345   0.806  1.00135.10      A    N  
ANISOU 1665  ND2 ASN A 232    20826  10338  20167    -64  -3056    651  A    N  
ATOM   1666  OD1 ASN A 232      46.024 -39.656   2.631  1.00136.22      A    O  
ANISOU 1666  OD1 ASN A 232    21516   9962  20281   -212  -3276    995  A    O  
ATOM   1667  N   THR A 233      41.176 -37.140   2.315  1.00121.27      A    N  
ANISOU 1667  N   THR A 233    18993   9082  18002  -1610  -2645   1027  A    N  
ATOM   1668  CA  THR A 233      39.772 -36.820   2.084  1.00119.55      A    C  
ANISOU 1668  CA  THR A 233    18658   9065  17703  -1981  -2505   1009  A    C  
ATOM   1669  C   THR A 233      39.331 -35.789   3.118  1.00111.75      A    C  
ANISOU 1669  C   THR A 233    17495   8379  16585  -2141  -2394   1189  A    C  
ATOM   1670  O   THR A 233      40.041 -35.540   4.093  1.00111.72      A    O  
ANISOU 1670  O   THR A 233    17537   8361  16552  -2012  -2446   1343  A    O  
ATOM   1671  CB  THR A 233      38.860 -38.070   2.179  1.00115.44      A    C  
ANISOU 1671  CB  THR A 233    18463   8217  17181  -2312  -2561   1048  A    C  
ATOM   1672  CG2 THR A 233      39.403 -39.203   1.320  1.00116.23      A    C  
ANISOU 1672  CG2 THR A 233    18809   7947  17406  -2134  -2696    886  A    C  
ATOM   1673  OG1 THR A 233      38.768 -38.505   3.542  1.00118.01      A    O  
ANISOU 1673  OG1 THR A 233    19039   8357  17442  -2473  -2620   1301  A    O  
ATOM   1674  N   GLU A 234      38.163 -35.192   2.903  1.00104.37      A    N  
ANISOU 1674  N   GLU A 234    16361   7723  15571  -2412  -2244   1163  A    N  
ATOM   1675  CA  GLU A 234      37.609 -34.236   3.858  1.00106.20      A    C  
ANISOU 1675  CA  GLU A 234    16433   8245  15672  -2578  -2123   1319  A    C  
ATOM   1676  C   GLU A 234      37.566 -34.787   5.290  1.00111.91      A    C  
ANISOU 1676  C   GLU A 234    17434   8766  16323  -2741  -2184   1567  A    C  
ATOM   1677  O   GLU A 234      37.884 -34.080   6.252  1.00106.38      A    O  
ANISOU 1677  O   GLU A 234    16673   8209  15537  -2691  -2156   1708  A    O  
ATOM   1678  CB  GLU A 234      36.215 -33.783   3.420  1.00107.52      A    C  
ANISOU 1678  CB  GLU A 234    16393   8691  15771  -2875  -1968   1258  A    C  
ATOM   1679  CG  GLU A 234      36.182 -33.126   2.050  1.00114.65      A    C  
ANISOU 1679  CG  GLU A 234    17013   9828  16720  -2726  -1902   1030  A    C  
ATOM   1680  CD  GLU A 234      34.927 -32.305   1.835  1.00121.42      A    C  
ANISOU 1680  CD  GLU A 234    17599  11050  17486  -2956  -1740   1003  A    C  
ATOM   1681  OE1 GLU A 234      34.090 -32.258   2.761  1.00124.91      A    O  
ANISOU 1681  OE1 GLU A 234    18061  11568  17832  -3230  -1671   1155  A    O  
ATOM   1682  OE2 GLU A 234      34.779 -31.703   0.749  1.00119.43      A    O1-
ANISOU 1682  OE2 GLU A 234    17112  11014  17252  -2856  -1682    833  A    O1-
ATOM   1683  N   GLN A 235      37.173 -36.049   5.433  1.00118.83      A    N  
ANISOU 1683  N   GLN A 235    18627   9301  17221  -2944  -2271   1621  A    N  
ATOM   1684  CA  GLN A 235      37.136 -36.670   6.753  1.00121.97      A    C  
ANISOU 1684  CA  GLN A 235    19326   9474  17543  -3107  -2339   1864  A    C  
ATOM   1685  C   GLN A 235      38.532 -36.827   7.346  1.00114.64      A    C  
ANISOU 1685  C   GLN A 235    18553   8352  16655  -2768  -2495   1954  A    C  
ATOM   1686  O   GLN A 235      38.730 -36.626   8.545  1.00111.17      A    O  
ANISOU 1686  O   GLN A 235    18202   7924  16115  -2802  -2513   2156  A    O  
ATOM   1687  CB  GLN A 235      36.411 -38.014   6.714  1.00130.87      A    C  
ANISOU 1687  CB  GLN A 235    20781  10256  18688  -3412  -2401   1901  A    C  
ATOM   1688  CG  GLN A 235      34.904 -37.879   6.784  1.00142.04      A    C  
ANISOU 1688  CG  GLN A 235    22086  11879  20004  -3854  -2245   1928  A    C  
ATOM   1689  CD  GLN A 235      34.236 -39.108   7.367  1.00159.23      A    C  
ANISOU 1689  CD  GLN A 235    24630  13726  22143  -4219  -2300   2076  A    C  
ATOM   1690  NE2 GLN A 235      33.080 -38.909   7.994  1.00163.07      A    N  
ANISOU 1690  NE2 GLN A 235    25048  14412  22499  -4608  -2161   2196  A    N  
ATOM   1691  OE1 GLN A 235      34.750 -40.224   7.256  1.00166.85      A    O  
ANISOU 1691  OE1 GLN A 235    25942  14262  23192  -4152  -2463   2082  A    O  
ATOM   1692  N   HIS A 236      39.497 -37.186   6.506  1.00108.62      A    N  
ANISOU 1692  N   HIS A 236    17815   7424  16031  -2438  -2608   1801  A    N  
ATOM   1693  CA  HIS A 236      40.880 -37.286   6.952  1.00106.12      A    C  
ANISOU 1693  CA  HIS A 236    17593   6962  15765  -2079  -2759   1862  A    C  
ATOM   1694  C   HIS A 236      41.391 -35.904   7.352  1.00108.96      A    C  
ANISOU 1694  C   HIS A 236    17638   7702  16061  -1919  -2682   1891  A    C  
ATOM   1695  O   HIS A 236      42.101 -35.752   8.352  1.00109.71      A    O  
ANISOU 1695  O   HIS A 236    17808   7769  16106  -1800  -2767   2050  A    O  
ATOM   1696  CB  HIS A 236      41.759 -37.900   5.859  1.00106.89      A    C  
ANISOU 1696  CB  HIS A 236    17738   6848  16025  -1750  -2871   1664  A    C  
ATOM   1697  CG  HIS A 236      43.156 -38.204   6.306  1.00114.93      A    C  
ANISOU 1697  CG  HIS A 236    18879   7682  17109  -1379  -3045   1726  A    C  
ATOM   1698  CD2 HIS A 236      43.669 -38.430   7.540  1.00118.92      A    C  
ANISOU 1698  CD2 HIS A 236    19578   8048  17558  -1331  -3165   1949  A    C  
ATOM   1699  ND1 HIS A 236      44.219 -38.284   5.431  1.00114.88      A    N  
ANISOU 1699  ND1 HIS A 236    18779   7638  17233   -990  -3116   1546  A    N  
ATOM   1700  CE1 HIS A 236      45.322 -38.557   6.104  1.00115.12      A    C  
ANISOU 1700  CE1 HIS A 236    18927   7518  17294   -715  -3274   1653  A    C  
ATOM   1701  NE2 HIS A 236      45.017 -38.648   7.386  1.00119.24      A    N  
ANISOU 1701  NE2 HIS A 236    19629   7972  17703   -913  -3314   1899  A    N  
ATOM   1702  N   GLN A 237      41.011 -34.896   6.571  1.00103.66      A    N  
ANISOU 1702  N   GLN A 237    16624   7378  15383  -1925  -2527   1739  A    N  
ATOM   1703  CA  GLN A 237      41.386 -33.518   6.854  1.00100.82      A    C  
ANISOU 1703  CA  GLN A 237    15966   7381  14959  -1802  -2439   1750  A    C  
ATOM   1704  C   GLN A 237      40.798 -33.078   8.191  1.00101.19      A    C  
ANISOU 1704  C   GLN A 237    16056   7549  14843  -2047  -2374   1964  A    C  
ATOM   1705  O   GLN A 237      41.496 -32.500   9.026  1.00 91.05      A    O  
ANISOU 1705  O   GLN A 237    14740   6356  13498  -1919  -2411   2072  A    O  
ATOM   1706  CB  GLN A 237      40.911 -32.587   5.732  1.00 97.37      A    C  
ANISOU 1706  CB  GLN A 237    15193   7269  14536  -1802  -2280   1555  A    C  
ATOM   1707  CG  GLN A 237      41.600 -31.231   5.714  1.00 99.80      A    C  
ANISOU 1707  CG  GLN A 237    15204   7897  14818  -1589  -2215   1518  A    C  
ATOM   1708  CD  GLN A 237      43.093 -31.328   5.422  1.00102.19      A    C  
ANISOU 1708  CD  GLN A 237    15489   8109  15228  -1213  -2345   1454  A    C  
ATOM   1709  NE2 GLN A 237      43.450 -32.110   4.407  1.00103.21      A    N  
ANISOU 1709  NE2 GLN A 237    15679   8054  15482  -1060  -2412   1300  A    N  
ATOM   1710  OE1 GLN A 237      43.915 -30.710   6.107  1.00100.08      A    O  
ANISOU 1710  OE1 GLN A 237    15152   7946  14928  -1065  -2385   1538  A    O  
ATOM   1711  N   LEU A 238      39.512 -33.361   8.391  1.00106.82      A    N  
ANISOU 1711  N   LEU A 238    16839   8271  15478  -2404  -2276   2020  A    N  
ATOM   1712  CA  LEU A 238      38.839 -32.987   9.632  1.00109.91      A    C  
ANISOU 1712  CA  LEU A 238    17270   8790  15701  -2660  -2191   2215  A    C  
ATOM   1713  C   LEU A 238      39.440 -33.716  10.826  1.00113.80      A    C  
ANISOU 1713  C   LEU A 238    18092   9002  16143  -2646  -2346   2430  A    C  
ATOM   1714  O   LEU A 238      39.502 -33.178  11.934  1.00113.61      A    O  
ANISOU 1714  O   LEU A 238    18081   9103  15984  -2697  -2321   2587  A    O  
ATOM   1715  CB  LEU A 238      37.336 -33.249   9.545  1.00110.87      A    C  
ANISOU 1715  CB  LEU A 238    17391   8978  15757  -3053  -2056   2224  A    C  
ATOM   1716  CG  LEU A 238      36.481 -32.034   9.179  1.00112.42      A    C  
ANISOU 1716  CG  LEU A 238    17228   9600  15887  -3149  -1851   2129  A    C  
ATOM   1717  CD1 LEU A 238      35.043 -32.454   8.907  1.00117.27      A    C  
ANISOU 1717  CD1 LEU A 238    17827  10266  16464  -3516  -1741   2112  A    C  
ATOM   1718  CD2 LEU A 238      36.541 -30.978  10.279  1.00104.06      A    C  
ANISOU 1718  CD2 LEU A 238    16069   8791  14679  -3146  -1765   2258  A    C  
ATOM   1719  N   ALA A 239      39.884 -34.946  10.594  1.00112.88      A    N  
ANISOU 1719  N   ALA A 239    18257   8501  16131  -2569  -2510   2435  A    N  
ATOM   1720  CA  ALA A 239      40.543 -35.709  11.636  1.00110.80      A    C  
ANISOU 1720  CA  ALA A 239    18328   7939  15833  -2512  -2683   2636  A    C  
ATOM   1721  C   ALA A 239      41.891 -35.072  11.926  1.00108.41      A    C  
ANISOU 1721  C   ALA A 239    17909   7729  15552  -2142  -2786   2642  A    C  
ATOM   1722  O   ALA A 239      42.228 -34.822  13.084  1.00114.11      A    O  
ANISOU 1722  O   ALA A 239    18719   8482  16156  -2143  -2836   2823  A    O  
ATOM   1723  CB  ALA A 239      40.713 -37.159  11.214  1.00107.68      A    C  
ANISOU 1723  CB  ALA A 239    18262   7095  15555  -2487  -2838   2621  A    C  
ATOM   1724  N   LEU A 240      42.659 -34.808  10.872  1.00 98.96      A    N  
ANISOU 1724  N   LEU A 240    16511   6591  14500  -1835  -2815   2442  A    N  
ATOM   1725  CA  LEU A 240      43.982 -34.214  11.034  1.00103.15      A    C  
ANISOU 1725  CA  LEU A 240    16900   7226  15065  -1484  -2911   2428  A    C  
ATOM   1726  C   LEU A 240      43.910 -32.905  11.812  1.00101.82      A    C  
ANISOU 1726  C   LEU A 240    16523   7414  14752  -1551  -2805   2506  A    C  
ATOM   1727  O   LEU A 240      44.693 -32.691  12.742  1.00 99.48      A    O  
ANISOU 1727  O   LEU A 240    16281   7125  14392  -1428  -2914   2638  A    O  
ATOM   1728  CB  LEU A 240      44.665 -34.008   9.681  1.00104.63      A    C  
ANISOU 1728  CB  LEU A 240    16857   7484  15415  -1189  -2912   2184  A    C  
ATOM   1729  CG  LEU A 240      45.271 -35.277   9.079  1.00113.57      A    C  
ANISOU 1729  CG  LEU A 240    18210   8242  16698   -979  -3075   2111  A    C  
ATOM   1730  CD1 LEU A 240      46.017 -34.976   7.791  1.00115.42      A    C  
ANISOU 1730  CD1 LEU A 240    18192   8588  17073   -672  -3060   1868  A    C  
ATOM   1731  CD2 LEU A 240      46.195 -35.934  10.083  1.00117.03      A    C  
ANISOU 1731  CD2 LEU A 240    18906   8429  17133   -804  -3287   2290  A    C  
ATOM   1732  N   ILE A 241      42.963 -32.047  11.432  1.00 98.50      A    N  
ANISOU 1732  N   ILE A 241    15870   7282  14274  -1742  -2600   2422  A    N  
ATOM   1733  CA  ILE A 241      42.721 -30.777  12.122  1.00101.72      A    C  
ANISOU 1733  CA  ILE A 241    16090   8023  14534  -1829  -2475   2479  A    C  
ATOM   1734  C   ILE A 241      42.458 -30.968  13.618  1.00103.92      A    C  
ANISOU 1734  C   ILE A 241    16604   8239  14641  -2022  -2507   2721  A    C  
ATOM   1735  O   ILE A 241      42.939 -30.194  14.449  1.00 99.49      A    O  
ANISOU 1735  O   ILE A 241    15989   7839  13975  -1959  -2521   2804  A    O  
ATOM   1736  CB  ILE A 241      41.535 -29.988  11.488  1.00 87.84      A    C  
ANISOU 1736  CB  ILE A 241    14088   6549  12737  -2029  -2247   2361  A    C  
ATOM   1737  CG1 ILE A 241      41.970 -29.310  10.182  1.00 83.95      A    C  
ANISOU 1737  CG1 ILE A 241    13302   6229  12368  -1803  -2198   2137  A    C  
ATOM   1738  CG2 ILE A 241      40.989 -28.943  12.463  1.00 80.98      A    C  
ANISOU 1738  CG2 ILE A 241    13127   5957  11686  -2194  -2112   2464  A    C  
ATOM   1739  CD1 ILE A 241      40.861 -28.534   9.491  1.00 77.09      A    C  
ANISOU 1739  CD1 ILE A 241    12193   5632  11464  -1963  -1995   2019  A    C  
ATOM   1740  N   SER A 242      41.691 -31.999  13.957  1.00107.88      A    N  
ANISOU 1740  N   SER A 242    17377   8508  15106  -2269  -2520   2833  A    N  
ATOM   1741  CA  SER A 242      41.391 -32.297  15.353  1.00111.37      A    C  
ANISOU 1741  CA  SER A 242    18073   8869  15373  -2476  -2547   3073  A    C  
ATOM   1742  C   SER A 242      42.633 -32.763  16.107  1.00109.91      A    C  
ANISOU 1742  C   SER A 242    18105   8469  15188  -2243  -2781   3209  A    C  
ATOM   1743  O   SER A 242      42.811 -32.447  17.285  1.00105.13      A    O  
ANISOU 1743  O   SER A 242    17595   7929  14422  -2294  -2813   3378  A    O  
ATOM   1744  CB  SER A 242      40.280 -33.345  15.458  1.00118.76      A    C  
ANISOU 1744  CB  SER A 242    19254   9594  16275  -2813  -2504   3160  A    C  
ATOM   1745  OG  SER A 242      39.005 -32.759  15.255  1.00120.47      A    O  
ANISOU 1745  OG  SER A 242    19276  10082  16415  -3092  -2275   3103  A    O  
ATOM   1746  N   GLN A 243      43.490 -33.510  15.418  1.00113.49      A    N  
ANISOU 1746  N   GLN A 243    18631   8675  15816  -1979  -2946   3131  A    N  
ATOM   1747  CA  GLN A 243      44.713 -34.024  16.022  1.00117.52      A    C  
ANISOU 1747  CA  GLN A 243    19329   8974  16348  -1717  -3186   3246  A    C  
ATOM   1748  C   GLN A 243      45.744 -32.916  16.222  1.00116.60      A    C  
ANISOU 1748  C   GLN A 243    18951   9132  16218  -1460  -3224   3202  A    C  
ATOM   1749  O   GLN A 243      46.811 -33.145  16.801  1.00117.96      A    O  
ANISOU 1749  O   GLN A 243    19223   9204  16393  -1235  -3423   3297  A    O  
ATOM   1750  CB  GLN A 243      45.295 -35.157  15.175  1.00121.21      A    C  
ANISOU 1750  CB  GLN A 243    19943   9100  17012  -1492  -3342   3157  A    C  
ATOM   1751  CG  GLN A 243      44.436 -36.415  15.151  1.00127.92      A    C  
ANISOU 1751  CG  GLN A 243    21135   9601  17867  -1741  -3356   3233  A    C  
ATOM   1752  CD  GLN A 243      44.869 -37.384  14.072  1.00131.15      A    C  
ANISOU 1752  CD  GLN A 243    21643   9709  18479  -1528  -3467   3083  A    C  
ATOM   1753  NE2 GLN A 243      44.169 -38.510  13.962  1.00122.98      A    N  
ANISOU 1753  NE2 GLN A 243    20920   8343  17462  -1738  -3491   3130  A    N  
ATOM   1754  OE1 GLN A 243      45.822 -37.120  13.338  1.00138.23      A    O  
ANISOU 1754  OE1 GLN A 243    22340  10672  19509  -1183  -3526   2923  A    O  
ATOM   1755  N   LEU A 244      45.419 -31.715  15.749  1.00108.24      A    N  
ANISOU 1755  N   LEU A 244    17561   8421  15143  -1499  -3040   3062  A    N  
ATOM   1756  CA  LEU A 244      46.301 -30.567  15.922  1.00 99.10      A    C  
ANISOU 1756  CA  LEU A 244    16152   7539  13963  -1302  -3055   3014  A    C  
ATOM   1757  C   LEU A 244      45.681 -29.464  16.769  1.00 99.42      A    C  
ANISOU 1757  C   LEU A 244    16105   7867  13802  -1520  -2904   3086  A    C  
ATOM   1758  O   LEU A 244      46.335 -28.910  17.655  1.00100.72      A    O  
ANISOU 1758  O   LEU A 244    16267   8141  13861  -1450  -2983   3177  A    O  
ATOM   1759  CB  LEU A 244      46.726 -29.987  14.575  1.00 94.37      A    C  
ANISOU 1759  CB  LEU A 244    15229   7102  13526  -1094  -2989   2772  A    C  
ATOM   1760  CG  LEU A 244      47.802 -28.903  14.710  1.00 93.45      A    C  
ANISOU 1760  CG  LEU A 244    14867   7237  13404   -878  -3031   2725  A    C  
ATOM   1761  CD1 LEU A 244      49.091 -29.524  15.205  1.00 93.80      A    C  
ANISOU 1761  CD1 LEU A 244    15033   7109  13498   -616  -3285   2814  A    C  
ATOM   1762  CD2 LEU A 244      48.030 -28.177  13.396  1.00 92.97      A    C  
ANISOU 1762  CD2 LEU A 244    14478   7376  13469   -736  -2920   2495  A    C  
ATOM   1763  N   CYS A 245      44.423 -29.139  16.497  1.00 99.54      A    N  
ANISOU 1763  N   CYS A 245    16046   8013  13762  -1777  -2690   3038  A    N  
ATOM   1764  CA  CYS A 245      43.810 -27.964  17.110  1.00108.47      A    C  
ANISOU 1764  CA  CYS A 245    17045   9450  14720  -1946  -2518   3060  A    C  
ATOM   1765  C   CYS A 245      42.840 -28.312  18.235  1.00107.71      A    C  
ANISOU 1765  C   CYS A 245    17185   9313  14428  -2260  -2451   3250  A    C  
ATOM   1766  O   CYS A 245      42.064 -27.465  18.679  1.00100.87      A    O  
ANISOU 1766  O   CYS A 245    16222   8692  13413  -2438  -2273   3259  A    O  
ATOM   1767  CB  CYS A 245      43.096 -27.122  16.043  1.00115.57      A    C  
ANISOU 1767  CB  CYS A 245    17643  10592  15675  -1987  -2309   2864  A    C  
ATOM   1768  SG  CYS A 245      44.075 -26.793  14.543  1.00104.70      A    S  
ANISOU 1768  SG  CYS A 245    15994   9264  14525  -1657  -2355   2630  A    S  
ATOM   1769  N   GLY A 246      42.898 -29.553  18.704  1.00113.29      A    N  
ANISOU 1769  N   GLY A 246    18207   9708  15128  -2321  -2591   3404  A    N  
ATOM   1770  CA  GLY A 246      41.903 -30.051  19.635  1.00115.75      A    C  
ANISOU 1770  CA  GLY A 246    18761   9952  15266  -2649  -2518   3585  A    C  
ATOM   1771  C   GLY A 246      40.709 -30.508  18.827  1.00120.43      A    C  
ANISOU 1771  C   GLY A 246    19316  10514  15926  -2875  -2364   3503  A    C  
ATOM   1772  O   GLY A 246      40.772 -30.539  17.601  1.00116.27      A    O  
ANISOU 1772  O   GLY A 246    18617   9981  15579  -2752  -2348   3319  A    O  
ATOM   1773  N   SER A 247      39.617 -30.859  19.493  1.00130.20      A    N  
ANISOU 1773  N   SER A 247    20706  11748  17014  -3214  -2248   3635  A    N  
ATOM   1774  CA  SER A 247      38.454 -31.364  18.772  1.00130.95      A    C  
ANISOU 1774  CA  SER A 247    20770  11817  17168  -3460  -2112   3567  A    C  
ATOM   1775  C   SER A 247      37.310 -30.360  18.716  1.00128.71      A    C  
ANISOU 1775  C   SER A 247    20211  11910  16781  -3658  -1848   3489  A    C  
ATOM   1776  O   SER A 247      37.160 -29.509  19.595  1.00125.93      A    O  
ANISOU 1776  O   SER A 247    19804  11790  16253  -3707  -1751   3556  A    O  
ATOM   1777  CB  SER A 247      37.984 -32.698  19.356  1.00135.97      A    C  
ANISOU 1777  CB  SER A 247    21780  12138  17745  -3722  -2178   3759  A    C  
ATOM   1778  OG  SER A 247      37.876 -32.631  20.764  1.00139.74      A    O  
ANISOU 1778  OG  SER A 247    22453  12647  17996  -3877  -2169   3978  A    O  
ATOM   1779  N   ILE A 248      36.512 -30.472  17.660  1.00127.94      A    N  
ANISOU 1779  N   ILE A 248    19945  11872  16794  -3758  -1738   3342  A    N  
ATOM   1780  CA  ILE A 248      35.397 -29.568  17.420  1.00121.02      A    C  
ANISOU 1780  CA  ILE A 248    18781  11354  15849  -3916  -1497   3246  A    C  
ATOM   1781  C   ILE A 248      34.359 -29.705  18.531  1.00120.76      A    C  
ANISOU 1781  C   ILE A 248    18864  11417  15601  -4268  -1355   3417  A    C  
ATOM   1782  O   ILE A 248      33.639 -30.701  18.604  1.00113.99      A    O  
ANISOU 1782  O   ILE A 248    18176  10404  14733  -4547  -1342   3503  A    O  
ATOM   1783  CB  ILE A 248      34.733 -29.866  16.059  1.00115.32      A    C  
ANISOU 1783  CB  ILE A 248    17888  10642  15286  -3974  -1438   3068  A    C  
ATOM   1784  CG1 ILE A 248      35.721 -30.557  15.109  1.00110.58      A    C  
ANISOU 1784  CG1 ILE A 248    17368   9753  14895  -3723  -1635   2968  A    C  
ATOM   1785  CG2 ILE A 248      34.169 -28.599  15.441  1.00100.53      A    C  
ANISOU 1785  CG2 ILE A 248    15635   9154  13409  -3920  -1254   2899  A    C  
ATOM   1786  CD1 ILE A 248      36.718 -29.633  14.464  1.00 87.77      A    C  
ANISOU 1786  CD1 ILE A 248    14254   6992  12104  -3359  -1678   2815  A    C  
ATOM   1787  N   THR A 249      34.290 -28.699  19.396  1.00126.88      A    N  
ANISOU 1787  N   THR A 249    19554  12451  16202  -4260  -1247   3465  A    N  
ATOM   1788  CA  THR A 249      33.409 -28.744  20.554  1.00134.00      A    C  
ANISOU 1788  CA  THR A 249    20570  13469  16875  -4567  -1105   3630  A    C  
ATOM   1789  C   THR A 249      32.563 -27.489  20.633  1.00128.62      A    C  
ANISOU 1789  C   THR A 249    19582  13207  16082  -4613   -861   3534  A    C  
ATOM   1790  O   THR A 249      33.086 -26.386  20.545  1.00124.23      A    O  
ANISOU 1790  O   THR A 249    18854  12824  15525  -4369   -845   3432  A    O  
ATOM   1791  CB  THR A 249      34.218 -28.850  21.855  1.00139.96      A    C  
ANISOU 1791  CB  THR A 249    21609  14099  17471  -4521  -1229   3826  A    C  
ATOM   1792  CG2 THR A 249      33.293 -28.860  23.059  1.00143.91      A    C  
ANISOU 1792  CG2 THR A 249    22226  14738  17712  -4843  -1066   3995  A    C  
ATOM   1793  OG1 THR A 249      34.991 -30.055  21.839  1.00143.30      A    O  
ANISOU 1793  OG1 THR A 249    22336  14120  17991  -4465  -1466   3930  A    O  
ATOM   1794  N   PRO A 250      31.245 -27.652  20.805  1.00127.77      A    N  
ANISOU 1794  N   PRO A 250    19404  13264  15878  -4928   -668   3565  A    N  
ATOM   1795  CA  PRO A 250      30.368 -26.489  20.967  1.00124.22      A    C  
ANISOU 1795  CA  PRO A 250    18668  13222  15307  -4969   -425   3481  A    C  
ATOM   1796  C   PRO A 250      30.851 -25.595  22.105  1.00120.90      A    C  
ANISOU 1796  C   PRO A 250    18312  12933  14690  -4858   -394   3552  A    C  
ATOM   1797  O   PRO A 250      30.461 -24.430  22.185  1.00119.02      A    O  
ANISOU 1797  O   PRO A 250    17847  13005  14371  -4781   -230   3452  A    O  
ATOM   1798  CB  PRO A 250      29.017 -27.119  21.313  1.00123.66      A    C  
ANISOU 1798  CB  PRO A 250    18609  13247  15129  -5369   -258   3572  A    C  
ATOM   1799  CG  PRO A 250      29.071 -28.473  20.686  1.00119.95      A    C  
ANISOU 1799  CG  PRO A 250    18316  12444  14816  -5501   -406   3607  A    C  
ATOM   1800  CD  PRO A 250      30.497 -28.921  20.823  1.00121.97      A    C  
ANISOU 1800  CD  PRO A 250    18846  12350  15149  -5262   -664   3673  A    C  
ATOM   1801  N   GLU A 251      31.694 -26.141  22.975  1.00120.08      A    N  
ANISOU 1801  N   GLU A 251    18527  12589  14508  -4845   -559   3720  A    N  
ATOM   1802  CA  GLU A 251      32.288 -25.357  24.045  1.00121.70      A    C  
ANISOU 1802  CA  GLU A 251    18822  12891  14529  -4731   -568   3787  A    C  
ATOM   1803  C   GLU A 251      33.401 -24.498  23.480  1.00115.72      A    C  
ANISOU 1803  C   GLU A 251    17928  12141  13898  -4366   -689   3640  A    C  
ATOM   1804  O   GLU A 251      33.524 -23.318  23.806  1.00113.56      A    O  
ANISOU 1804  O   GLU A 251    17529  12094  13525  -4241   -604   3568  A    O  
ATOM   1805  CB  GLU A 251      32.859 -26.262  25.128  1.00132.56      A    C  
ANISOU 1805  CB  GLU A 251    20586  14003  15776  -4832   -727   4021  A    C  
ATOM   1806  CG  GLU A 251      33.895 -25.563  25.982  1.00141.64      A    C  
ANISOU 1806  CG  GLU A 251    21842  15175  16799  -4627   -836   4067  A    C  
ATOM   1807  CD  GLU A 251      34.614 -26.506  26.914  1.00154.41      A    C  
ANISOU 1807  CD  GLU A 251    23843  16505  18319  -4675  -1042   4293  A    C  
ATOM   1808  OE1 GLU A 251      34.019 -27.538  27.290  1.00158.67      A    O  
ANISOU 1808  OE1 GLU A 251    24597  16898  18791  -4947  -1024   4452  A    O  
ATOM   1809  OE2 GLU A 251      35.775 -26.213  27.271  1.00158.02      A    O1-
ANISOU 1809  OE2 GLU A 251    24391  16885  18765  -4444  -1227   4315  A    O1-
ATOM   1810  N   VAL A 252      34.217 -25.112  22.634  1.00112.24      A    N  
ANISOU 1810  N   VAL A 252    17523  11448  13675  -4201   -887   3596  A    N  
ATOM   1811  CA  VAL A 252      35.326 -24.434  21.981  1.00105.47      A    C  
ANISOU 1811  CA  VAL A 252    16531  10582  12960  -3864  -1012   3459  A    C  
ATOM   1812  C   VAL A 252      34.812 -23.524  20.860  1.00110.29      A    C  
ANISOU 1812  C   VAL A 252    16792  11430  13683  -3768   -861   3241  A    C  
ATOM   1813  O   VAL A 252      35.262 -22.386  20.694  1.00108.74      A    O  
ANISOU 1813  O   VAL A 252    16432  11396  13488  -3566   -836   3129  A    O  
ATOM   1814  CB  VAL A 252      36.332 -25.478  21.432  1.00 97.75      A    C  
ANISOU 1814  CB  VAL A 252    15707   9259  12175  -3719  -1264   3482  A    C  
ATOM   1815  CG1 VAL A 252      37.199 -24.896  20.353  1.00 95.82      A    C  
ANISOU 1815  CG1 VAL A 252    15247   9036  12124  -3409  -1345   3298  A    C  
ATOM   1816  CG2 VAL A 252      37.198 -26.016  22.557  1.00 99.69      A    C  
ANISOU 1816  CG2 VAL A 252    16267   9300  12308  -3696  -1452   3678  A    C  
ATOM   1817  N   TRP A 253      33.833 -24.033  20.125  1.00112.44      A    N  
ANISOU 1817  N   TRP A 253    16961  11722  14039  -3929   -762   3188  A    N  
ATOM   1818  CA  TRP A 253      33.312 -23.393  18.927  1.00103.56      A    C  
ANISOU 1818  CA  TRP A 253    15521  10787  13039  -3845   -648   2990  A    C  
ATOM   1819  C   TRP A 253      31.792 -23.307  19.043  1.00104.05      A    C  
ANISOU 1819  C   TRP A 253    15449  11086  12999  -4109   -418   2987  A    C  
ATOM   1820  O   TRP A 253      31.072 -24.171  18.531  1.00 98.54      A    O  
ANISOU 1820  O   TRP A 253    14741  10324  12375  -4301   -397   2988  A    O  
ATOM   1821  CB  TRP A 253      33.695 -24.248  17.720  1.00102.05      A    C  
ANISOU 1821  CB  TRP A 253    15325  10369  13080  -3764   -790   2908  A    C  
ATOM   1822  CG  TRP A 253      33.267 -23.732  16.392  1.00 97.74      A    C  
ANISOU 1822  CG  TRP A 253    14483   9983  12671  -3669   -708   2708  A    C  
ATOM   1823  CD1 TRP A 253      32.397 -22.713  16.141  1.00 93.31      A    C  
ANISOU 1823  CD1 TRP A 253    13660   9740  12053  -3681   -514   2606  A    C  
ATOM   1824  CD2 TRP A 253      33.663 -24.248  15.116  1.00 90.32      A    C  
ANISOU 1824  CD2 TRP A 253    13487   8888  11940  -3544   -820   2587  A    C  
ATOM   1825  CE2 TRP A 253      33.006 -23.484  14.134  1.00 84.56      A    C  
ANISOU 1825  CE2 TRP A 253    12461   8403  11264  -3495   -689   2420  A    C  
ATOM   1826  CE3 TRP A 253      34.517 -25.276  14.710  1.00 89.55      A    C  
ANISOU 1826  CE3 TRP A 253    13569   8472  11985  -3456  -1018   2599  A    C  
ATOM   1827  NE1 TRP A 253      32.241 -22.551  14.783  1.00 89.67      A    N  
ANISOU 1827  NE1 TRP A 253    12987   9334  11751  -3573   -508   2438  A    N  
ATOM   1828  CZ2 TRP A 253      33.177 -23.715  12.774  1.00 81.65      A    C  
ANISOU 1828  CZ2 TRP A 253    11975   7975  11073  -3377   -750   2269  A    C  
ATOM   1829  CZ3 TRP A 253      34.684 -25.505  13.364  1.00 89.92      A    C  
ANISOU 1829  CZ3 TRP A 253    13494   8458  12212  -3332  -1069   2440  A    C  
ATOM   1830  CH2 TRP A 253      34.018 -24.727  12.410  1.00 86.22      A    C  
ANISOU 1830  CH2 TRP A 253    12734   8244  11782  -3301   -935   2278  A    C  
ATOM   1831  N   PRO A 254      31.301 -22.267  19.733  1.00106.57      A    N  
ANISOU 1831  N   PRO A 254    15663  11685  13143  -4122   -245   2981  A    N  
ATOM   1832  CA  PRO A 254      29.882 -22.006  20.006  1.00107.97      A    C  
ANISOU 1832  CA  PRO A 254    15689  12143  13193  -4344     -5   2978  A    C  
ATOM   1833  C   PRO A 254      28.974 -22.232  18.800  1.00109.95      A    C  
ANISOU 1833  C   PRO A 254    15693  12494  13589  -4417     70   2851  A    C  
ATOM   1834  O   PRO A 254      29.089 -21.518  17.808  1.00108.90      A    O  
ANISOU 1834  O   PRO A 254    15338  12463  13576  -4205     75   2686  A    O  
ATOM   1835  CB  PRO A 254      29.875 -20.524  20.386  1.00107.13      A    C  
ANISOU 1835  CB  PRO A 254    15436  12305  12964  -4169    125   2895  A    C  
ATOM   1836  CG  PRO A 254      31.197 -20.310  21.023  1.00108.34      A    C  
ANISOU 1836  CG  PRO A 254    15799  12288  13076  -4000    -40   2958  A    C  
ATOM   1837  CD  PRO A 254      32.170 -21.229  20.314  1.00107.99      A    C  
ANISOU 1837  CD  PRO A 254    15869  11928  13235  -3905   -278   2968  A    C  
ATOM   1838  N   ASN A 255      28.080 -23.212  18.897  1.00118.66      A    N  
ANISOU 1838  N   ASN A 255    16841  13573  14671  -4726    124   2932  A    N  
ATOM   1839  CA  ASN A 255      27.104 -23.493  17.841  1.00122.55      A    C  
ANISOU 1839  CA  ASN A 255    17101  14182  15280  -4845    197   2820  A    C  
ATOM   1840  C   ASN A 255      27.604 -24.421  16.736  1.00118.08      A    C  
ANISOU 1840  C   ASN A 255    16602  13331  14934  -4807      7   2762  A    C  
ATOM   1841  O   ASN A 255      26.857 -24.734  15.805  1.00115.46      A    O  
ANISOU 1841  O   ASN A 255    16097  13071  14701  -4912     42   2664  A    O  
ATOM   1842  CB  ASN A 255      26.559 -22.200  17.219  1.00123.47      A    C  
ANISOU 1842  CB  ASN A 255    16865  14643  15406  -4666    346   2646  A    C  
ATOM   1843  CG  ASN A 255      25.249 -21.761  17.836  1.00127.96      A    C  
ANISOU 1843  CG  ASN A 255    17257  15558  15802  -4856    592   2665  A    C  
ATOM   1844  ND2 ASN A 255      24.494 -20.952  17.100  1.00126.08      A    N  
ANISOU 1844  ND2 ASN A 255    16693  15613  15600  -4760    717   2513  A    N  
ATOM   1845  OD1 ASN A 255      24.914 -22.146  18.957  1.00132.74      A    O  
ANISOU 1845  OD1 ASN A 255    18017  16178  16240  -5082    669   2815  A    O  
ATOM   1846  N   VAL A 256      28.855 -24.863  16.834  1.00113.58      A    N  
ANISOU 1846  N   VAL A 256    16277  12446  14433  -4653   -195   2816  A    N  
ATOM   1847  CA  VAL A 256      29.417 -25.732  15.803  1.00110.74      A    C  
ANISOU 1847  CA  VAL A 256    15995  11804  14277  -4581   -376   2750  A    C  
ATOM   1848  C   VAL A 256      28.490 -26.905  15.493  1.00118.09      A    C  
ANISOU 1848  C   VAL A 256    16984  12638  15248  -4909   -363   2783  A    C  
ATOM   1849  O   VAL A 256      28.376 -27.334  14.345  1.00115.51      A    O  
ANISOU 1849  O   VAL A 256    16574  12235  15078  -4895   -426   2658  A    O  
ATOM   1850  CB  VAL A 256      30.809 -26.275  16.173  1.00101.42      A    C  
ANISOU 1850  CB  VAL A 256    15112  10279  13144  -4415   -596   2841  A    C  
ATOM   1851  CG1 VAL A 256      30.751 -27.085  17.462  1.00103.02      A    C  
ANISOU 1851  CG1 VAL A 256    15630  10313  13199  -4649   -625   3067  A    C  
ATOM   1852  CG2 VAL A 256      31.345 -27.122  15.035  1.00 92.22      A    C  
ANISOU 1852  CG2 VAL A 256    14005   8844  12192  -4315   -765   2748  A    C  
ATOM   1853  N   ASP A 257      27.824 -27.422  16.516  1.00129.69      A    N  
ANISOU 1853  N   ASP A 257    18598  14113  16563  -5218   -281   2950  A    N  
ATOM   1854  CA  ASP A 257      26.905 -28.530  16.306  1.00142.55      A    C  
ANISOU 1854  CA  ASP A 257    20291  15656  18214  -5574   -259   2995  A    C  
ATOM   1855  C   ASP A 257      25.634 -28.068  15.605  1.00146.29      A    C  
ANISOU 1855  C   ASP A 257    20400  16486  18698  -5705    -82   2859  A    C  
ATOM   1856  O   ASP A 257      24.597 -27.871  16.240  1.00151.52      A    O  
ANISOU 1856  O   ASP A 257    20947  17412  19212  -5949    105   2922  A    O  
ATOM   1857  CB  ASP A 257      26.595 -29.241  17.621  1.00146.24      A    C  
ANISOU 1857  CB  ASP A 257    21037  16021  18506  -5883   -222   3227  A    C  
ATOM   1858  CG  ASP A 257      27.666 -30.242  17.997  1.00152.76      A    C  
ANISOU 1858  CG  ASP A 257    22273  16396  19373  -5837   -448   3363  A    C  
ATOM   1859  OD1 ASP A 257      28.479 -30.609  17.118  1.00148.79      A    O  
ANISOU 1859  OD1 ASP A 257    21830  15645  19056  -5621   -628   3267  A    O  
ATOM   1860  OD2 ASP A 257      27.694 -30.666  19.169  1.00162.67      A    O1-
ANISOU 1860  OD2 ASP A 257    23790  17548  20469  -6010   -446   3568  A    O1-
ATOM   1861  N   ASN A 258      25.742 -27.895  14.289  1.00139.60      A    N  
ANISOU 1861  N   ASN A 258    19367  15654  18021  -5532   -144   2671  A    N  
ATOM   1862  CA  ASN A 258      24.621 -27.509  13.443  1.00130.81      A    C  
ANISOU 1862  CA  ASN A 258    17904  14857  16939  -5622    -17   2526  A    C  
ATOM   1863  C   ASN A 258      24.827 -27.928  11.986  1.00127.61      A    C  
ANISOU 1863  C   ASN A 258    17438  14316  16731  -5525   -152   2358  A    C  
ATOM   1864  O   ASN A 258      24.646 -27.116  11.084  1.00123.60      A    O  
ANISOU 1864  O   ASN A 258    16646  14034  16283  -5337   -112   2194  A    O  
ATOM   1865  CB  ASN A 258      24.383 -25.995  13.512  1.00121.43      A    C  
ANISOU 1865  CB  ASN A 258    16412  14053  15674  -5398    139   2441  A    C  
ATOM   1866  CG  ASN A 258      23.565 -25.578  14.726  1.00124.39      A    C  
ANISOU 1866  CG  ASN A 258    16729  14696  15840  -5585    343   2558  A    C  
ATOM   1867  ND2 ASN A 258      23.645 -24.302  15.081  1.00118.90      A    N  
ANISOU 1867  ND2 ASN A 258    15877  14245  15053  -5356    455   2516  A    N  
ATOM   1868  OD1 ASN A 258      22.863 -26.387  15.328  1.00136.87      A    O  
ANISOU 1868  OD1 ASN A 258    18408  16262  17336  -5936    404   2682  A    O  
ATOM   1869  N   TYR A 259      25.209 -29.184  11.747  1.00128.88      A    N  
ANISOU 1869  N   TYR A 259    17878  14105  16987  -5645   -312   2395  A    N  
ATOM   1870  CA  TYR A 259      25.343 -29.657  10.368  1.00131.69      A    C  
ANISOU 1870  CA  TYR A 259    18193  14328  17517  -5577   -435   2227  A    C  
ATOM   1871  C   TYR A 259      25.232 -31.158  10.148  1.00125.05      A    C  
ANISOU 1871  C   TYR A 259    17630  13134  16749  -5845   -561   2266  A    C  
ATOM   1872  O   TYR A 259      24.273 -31.612   9.539  1.00128.61      A    O  
ANISOU 1872  O   TYR A 259    17967  13670  17228  -6103   -529   2194  A    O  
ATOM   1873  CB  TYR A 259      26.629 -29.161   9.720  1.00145.99      A    C  
ANISOU 1873  CB  TYR A 259    20015  16015  19441  -5149   -560   2117  A    C  
ATOM   1874  CG  TYR A 259      26.687 -29.498   8.248  1.00151.91      A    C  
ANISOU 1874  CG  TYR A 259    20682  16691  20347  -5064   -657   1924  A    C  
ATOM   1875  CD1 TYR A 259      26.329 -28.555   7.291  1.00148.37      A    C  
ANISOU 1875  CD1 TYR A 259    19897  16549  19928  -4908   -587   1756  A    C  
ATOM   1876  CD2 TYR A 259      27.074 -30.766   7.815  1.00153.57      A    C  
ANISOU 1876  CD2 TYR A 259    21163  16522  20666  -5141   -820   1910  A    C  
ATOM   1877  CE1 TYR A 259      26.371 -28.851   5.947  1.00148.48      A    C  
ANISOU 1877  CE1 TYR A 259    19842  16509  20066  -4835   -675   1580  A    C  
ATOM   1878  CE2 TYR A 259      27.119 -31.072   6.469  1.00153.87      A    C  
ANISOU 1878  CE2 TYR A 259    21135  16496  20833  -5064   -904   1723  A    C  
ATOM   1879  CZ  TYR A 259      26.766 -30.108   5.539  1.00152.25      A    C  
ANISOU 1879  CZ  TYR A 259    20587  16616  20645  -4915   -830   1559  A    C  
ATOM   1880  OH  TYR A 259      26.804 -30.393   4.194  1.00151.87      A    O  
ANISOU 1880  OH  TYR A 259    20477  16521  20708  -4840   -913   1372  A    O  
ATOM   1881  N   LEU A 267      33.175 -37.282  13.695  1.00130.94      A    N  
ANISOU 1881  N   LEU A 267    21227  10754  17771  -4925  -1958   3140  A    N  
ATOM   1882  CA  LEU A 267      34.387 -36.660  14.230  1.00132.12      A    C  
ANISOU 1882  CA  LEU A 267    21367  10929  17903  -4558  -2048   3190  A    C  
ATOM   1883  C   LEU A 267      34.929 -37.304  15.498  1.00144.48      A    C  
ANISOU 1883  C   LEU A 267    23316  12216  19365  -4580  -2180   3447  A    C  
ATOM   1884  O   LEU A 267      34.287 -38.172  16.096  1.00144.50      A    O  
ANISOU 1884  O   LEU A 267    23601  12021  19281  -4913  -2179   3612  A    O  
ATOM   1885  CB  LEU A 267      34.141 -35.177  14.504  1.00120.95      A    C  
ANISOU 1885  CB  LEU A 267    19583   9991  16381  -4505  -1869   3152  A    C  
ATOM   1886  CG  LEU A 267      33.795 -34.303  13.300  1.00116.05      A    C  
ANISOU 1886  CG  LEU A 267    18559   9681  15852  -4400  -1749   2906  A    C  
ATOM   1887  CD1 LEU A 267      33.357 -32.921  13.760  1.00110.90      A    C  
ANISOU 1887  CD1 LEU A 267    17600   9472  15065  -4411  -1560   2906  A    C  
ATOM   1888  CD2 LEU A 267      34.982 -34.213  12.358  1.00117.10      A    C  
ANISOU 1888  CD2 LEU A 267    18631   9702  16160  -3990  -1889   2740  A    C  
ATOM   1889  N   VAL A 268      36.119 -36.856  15.897  1.00151.42      A    N  
ANISOU 1889  N   VAL A 268    24198  13089  20247  -4229  -2297   3480  A    N  
ATOM   1890  CA  VAL A 268      36.764 -37.310  17.126  1.00157.94      A    C  
ANISOU 1890  CA  VAL A 268    25356  13692  20963  -4194  -2440   3721  A    C  
ATOM   1891  C   VAL A 268      36.074 -36.671  18.323  1.00159.65      A    C  
ANISOU 1891  C   VAL A 268    25538  14182  20940  -4456  -2282   3891  A    C  
ATOM   1892  O   VAL A 268      35.191 -35.828  18.158  1.00159.59      A    O  
ANISOU 1892  O   VAL A 268    25229  14540  20869  -4618  -2066   3806  A    O  
ATOM   1893  CB  VAL A 268      38.253 -36.919  17.165  1.00151.83      A    C  
ANISOU 1893  CB  VAL A 268    24543  12885  20261  -3732  -2613   3689  A    C  
ATOM   1894  CG1 VAL A 268      38.978 -37.433  15.931  1.00149.20      A    C  
ANISOU 1894  CG1 VAL A 268    24196  12333  20162  -3436  -2748   3497  A    C  
ATOM   1895  CG2 VAL A 268      38.389 -35.416  17.275  1.00143.81      A    C  
ANISOU 1895  CG2 VAL A 268    23150  12315  19178  -3604  -2481   3607  A    C  
ATOM   1896  N   LYS A 269      36.483 -37.060  19.527  1.00156.09      A    N  
ANISOU 1896  N   LYS A 269    25397  13562  20349  -4486  -2389   4128  A    N  
ATOM   1897  CA  LYS A 269      35.830 -36.554  20.728  1.00151.03      A    C  
ANISOU 1897  CA  LYS A 269    24767  13158  19458  -4750  -2240   4301  A    C  
ATOM   1898  C   LYS A 269      36.793 -36.261  21.879  1.00145.89      A    C  
ANISOU 1898  C   LYS A 269    24273  12489  18669  -4559  -2371   4471  A    C  
ATOM   1899  O   LYS A 269      36.492 -35.444  22.748  1.00141.71      A    O  
ANISOU 1899  O   LYS A 269    23652  12249  17942  -4662  -2242   4549  A    O  
ATOM   1900  CB  LYS A 269      34.727 -37.518  21.177  1.00155.56      A    C  
ANISOU 1900  CB  LYS A 269    25608  13573  19925  -5210  -2163   4466  A    C  
ATOM   1901  CG  LYS A 269      33.686 -37.802  20.095  1.00151.75      A    C  
ANISOU 1901  CG  LYS A 269    24961  13136  19561  -5444  -2032   4302  A    C  
ATOM   1902  CD  LYS A 269      32.697 -38.880  20.510  1.00146.87      A    C  
ANISOU 1902  CD  LYS A 269    24637  12315  18852  -5909  -1985   4469  A    C  
ATOM   1903  CE  LYS A 269      31.710 -39.157  19.389  1.00142.51      A    C  
ANISOU 1903  CE  LYS A 269    23906  11817  18425  -6137  -1874   4292  A    C  
ATOM   1904  NZ  LYS A 269      30.646 -40.103  19.813  1.00149.80      A    N1+
ANISOU 1904  NZ  LYS A 269    25073  12599  19246  -6640  -1801   4450  A    N1+
ATOM   1905  N   GLY A 270      37.953 -36.913  21.879  1.00146.83      A    N  
ANISOU 1905  N   GLY A 270    24622  12280  18888  -4273  -2628   4521  A    N  
ATOM   1906  CA  GLY A 270      38.892 -36.771  22.980  1.00151.48      A    C  
ANISOU 1906  CA  GLY A 270    25386  12823  19346  -4096  -2786   4696  A    C  
ATOM   1907  C   GLY A 270      40.095 -35.872  22.735  1.00151.24      A    C  
ANISOU 1907  C   GLY A 270    25105  12958  19400  -3671  -2890   4566  A    C  
ATOM   1908  O   GLY A 270      40.797 -35.492  23.674  1.00148.43      A    O  
ANISOU 1908  O   GLY A 270    24819  12664  18913  -3544  -2991   4689  A    O  
ATOM   1909  N   GLN A 271      40.333 -35.526  21.474  1.00152.21      A    N  
ANISOU 1909  N   GLN A 271    24937  13162  19735  -3463  -2865   4318  A    N  
ATOM   1910  CA  GLN A 271      41.531 -34.783  21.092  1.00152.74      A    C  
ANISOU 1910  CA  GLN A 271    24768  13358  19910  -3060  -2971   4183  A    C  
ATOM   1911  C   GLN A 271      41.722 -33.490  21.889  1.00150.80      A    C  
ANISOU 1911  C   GLN A 271    24331  13474  19492  -3032  -2892   4209  A    C  
ATOM   1912  O   GLN A 271      40.756 -32.832  22.267  1.00152.30      A    O  
ANISOU 1912  O   GLN A 271    24413  13924  19530  -3291  -2677   4222  A    O  
ATOM   1913  CB  GLN A 271      41.508 -34.486  19.591  1.00153.41      A    C  
ANISOU 1913  CB  GLN A 271    24542  13534  20214  -2913  -2895   3908  A    C  
ATOM   1914  CG  GLN A 271      41.378 -35.725  18.713  1.00156.04      A    C  
ANISOU 1914  CG  GLN A 271    25056  13511  20722  -2917  -2978   3849  A    C  
ATOM   1915  CD  GLN A 271      42.658 -36.540  18.642  1.00159.64      A    C  
ANISOU 1915  CD  GLN A 271    25720  13631  21304  -2573  -3251   3880  A    C  
ATOM   1916  NE2 GLN A 271      42.515 -37.854  18.515  1.00165.42      A    N  
ANISOU 1916  NE2 GLN A 271    26793  13959  22102  -2642  -3364   3950  A    N  
ATOM   1917  OE1 GLN A 271      43.760 -35.995  18.695  1.00157.90      A    O  
ANISOU 1917  OE1 GLN A 271    25355  13517  21124  -2249  -3360   3839  A    O  
ATOM   1918  N   LYS A 272      42.978 -33.133  22.137  1.00147.18      A    N  
ANISOU 1918  N   LYS A 272    23829  13034  19057  -2714  -3068   4211  A    N  
ATOM   1919  CA  LYS A 272      43.304 -31.930  22.895  1.00143.21      A    C  
ANISOU 1919  CA  LYS A 272    23169  12848  18397  -2669  -3027   4229  A    C  
ATOM   1920  C   LYS A 272      44.351 -31.103  22.153  1.00140.87      A    C  
ANISOU 1920  C   LYS A 272    22554  12717  18253  -2324  -3089   4036  A    C  
ATOM   1921  O   LYS A 272      45.209 -31.659  21.469  1.00144.52      A    O  
ANISOU 1921  O   LYS A 272    23013  12993  18906  -2058  -3255   3966  A    O  
ATOM   1922  CB  LYS A 272      43.808 -32.306  24.287  1.00145.33      A    C  
ANISOU 1922  CB  LYS A 272    23753  12991  18474  -2682  -3201   4481  A    C  
ATOM   1923  CG  LYS A 272      42.904 -33.290  25.017  1.00149.00      A    C  
ANISOU 1923  CG  LYS A 272    24581  13239  18792  -3012  -3169   4696  A    C  
ATOM   1924  CD  LYS A 272      43.529 -33.751  26.317  1.00149.90      A    C  
ANISOU 1924  CD  LYS A 272    25034  13194  18728  -2986  -3375   4951  A    C  
ATOM   1925  CE  LYS A 272      42.602 -34.684  27.068  1.00155.54      A    C  
ANISOU 1925  CE  LYS A 272    26120  13704  19276  -3342  -3328   5177  A    C  
ATOM   1926  NZ  LYS A 272      43.246 -35.219  28.302  1.00159.07      A    N1+
ANISOU 1926  NZ  LYS A 272    26930  13964  19545  -3303  -3550   5440  A    N1+
ATOM   1927  N   ARG A 273      44.278 -29.781  22.299  1.00133.63      A    N  
ANISOU 1927  N   ARG A 273    21379  12148  17247  -2332  -2953   3949  A    N  
ATOM   1928  CA  ARG A 273      45.105 -28.853  21.519  1.00131.34      A    C  
ANISOU 1928  CA  ARG A 273    20759  12052  17091  -2061  -2965   3753  A    C  
ATOM   1929  C   ARG A 273      46.606 -29.111  21.620  1.00118.26      A    C  
ANISOU 1929  C   ARG A 273    19128  10280  15524  -1735  -3234   3777  A    C  
ATOM   1930  O   ARG A 273      47.192 -29.033  22.699  1.00112.78      A    O  
ANISOU 1930  O   ARG A 273    18572   9589  14688  -1700  -3375   3926  A    O  
ATOM   1931  CB  ARG A 273      44.813 -27.400  21.908  1.00143.31      A    C  
ANISOU 1931  CB  ARG A 273    22063  13931  18458  -2143  -2796   3695  A    C  
ATOM   1932  CG  ARG A 273      43.390 -26.951  21.639  1.00156.05      A    C  
ANISOU 1932  CG  ARG A 273    23567  15717  20006  -2408  -2516   3627  A    C  
ATOM   1933  CD  ARG A 273      43.177 -25.503  22.064  1.00166.29      A    C  
ANISOU 1933  CD  ARG A 273    24677  17352  21154  -2451  -2363   3567  A    C  
ATOM   1934  NE  ARG A 273      41.760 -25.188  22.233  1.00174.93      A    N  
ANISOU 1934  NE  ARG A 273    25740  18603  22122  -2728  -2111   3566  A    N  
ATOM   1935  CZ  ARG A 273      41.295 -24.013  22.647  1.00178.09      A    C  
ANISOU 1935  CZ  ARG A 273    26009  19285  22372  -2803  -1941   3519  A    C  
ATOM   1936  NH1 ARG A 273      42.135 -23.028  22.937  1.00176.98      A    N1+
ANISOU 1936  NH1 ARG A 273    25772  19286  22185  -2641  -1997   3470  A    N1+
ATOM   1937  NH2 ARG A 273      39.988 -23.822  22.772  1.00179.73      A    N  
ANISOU 1937  NH2 ARG A 273    26180  19636  22474  -3041  -1714   3517  A    N  
ATOM   1938  N   LYS A 274      47.224 -29.388  20.478  1.00112.11      A    N  
ANISOU 1938  N   LYS A 274    18200   9421  14974  -1492  -3301   3622  A    N  
ATOM   1939  CA  LYS A 274      48.653 -29.662  20.426  1.00109.48      A    C  
ANISOU 1939  CA  LYS A 274    17848   8997  14753  -1156  -3545   3620  A    C  
ATOM   1940  C   LYS A 274      49.376 -28.737  19.443  1.00102.88      A    C  
ANISOU 1940  C   LYS A 274    16632   8396  14062   -932  -3506   3399  A    C  
ATOM   1941  O   LYS A 274      50.493 -29.034  19.012  1.00 99.73      A    O  
ANISOU 1941  O   LYS A 274    16152   7931  13809   -636  -3673   3342  A    O  
ATOM   1942  CB  LYS A 274      48.899 -31.133  20.056  1.00112.85      A    C  
ANISOU 1942  CB  LYS A 274    18515   9042  15323  -1031  -3708   3665  A    C  
ATOM   1943  CG  LYS A 274      48.084 -32.123  20.885  1.00117.95      A    C  
ANISOU 1943  CG  LYS A 274    19555   9422  15838  -1286  -3729   3879  A    C  
ATOM   1944  CD  LYS A 274      48.659 -33.524  20.844  1.00125.08      A    C  
ANISOU 1944  CD  LYS A 274    20749   9924  16852  -1107  -3962   3969  A    C  
ATOM   1945  CE  LYS A 274      48.016 -34.393  21.923  1.00137.27      A    C  
ANISOU 1945  CE  LYS A 274    22715  11219  18223  -1362  -4013   4226  A    C  
ATOM   1946  NZ  LYS A 274      48.798 -35.627  22.252  1.00139.90      A    N1+
ANISOU 1946  NZ  LYS A 274    23375  11169  18612  -1152  -4292   4370  A    N1+
ATOM   1947  N   VAL A 275      48.742 -27.616  19.093  1.00 96.82      A    N  
ANISOU 1947  N   VAL A 275    15634   7905  13249  -1069  -3283   3279  A    N  
ATOM   1948  CA  VAL A 275      49.308 -26.706  18.097  1.00 90.27      A    C  
ANISOU 1948  CA  VAL A 275    14457   7296  12546   -892  -3221   3073  A    C  
ATOM   1949  C   VAL A 275      50.686 -26.231  18.509  1.00 88.56      A    C  
ANISOU 1949  C   VAL A 275    14129   7189  12332   -666  -3400   3086  A    C  
ATOM   1950  O   VAL A 275      51.619 -26.234  17.703  1.00 86.63      A    O  
ANISOU 1950  O   VAL A 275    13693   6968  12252   -414  -3478   2963  A    O  
ATOM   1951  CB  VAL A 275      48.426 -25.461  17.848  1.00 85.49      A    C  
ANISOU 1951  CB  VAL A 275    13650   6975  11857  -1077  -2967   2970  A    C  
ATOM   1952  CG1 VAL A 275      49.181 -24.442  16.982  1.00 65.35      A    C  
ANISOU 1952  CG1 VAL A 275    10768   4649   9411   -891  -2929   2786  A    C  
ATOM   1953  CG2 VAL A 275      47.101 -25.852  17.201  1.00 85.18      A    C  
ANISOU 1953  CG2 VAL A 275    13643   6874  11846  -1274  -2783   2918  A    C  
ATOM   1954  N   LYS A 276      50.810 -25.818  19.764  1.00 92.79      A    N  
ANISOU 1954  N   LYS A 276    14775   7805  12674   -763  -3463   3231  A    N  
ATOM   1955  CA  LYS A 276      52.082 -25.310  20.261  1.00104.43      A    C  
ANISOU 1955  CA  LYS A 276    16144   9409  14128   -582  -3642   3251  A    C  
ATOM   1956  C   LYS A 276      53.075 -26.427  20.586  1.00110.46      A    C  
ANISOU 1956  C   LYS A 276    17062   9945  14964   -351  -3923   3362  A    C  
ATOM   1957  O   LYS A 276      54.283 -26.228  20.488  1.00113.05      A    O  
ANISOU 1957  O   LYS A 276    17222  10361  15371   -113  -4082   3319  A    O  
ATOM   1958  CB  LYS A 276      51.881 -24.383  21.466  1.00106.19      A    C  
ANISOU 1958  CB  LYS A 276    16425   9817  14106   -767  -3610   3348  A    C  
ATOM   1959  CG  LYS A 276      51.551 -22.943  21.093  1.00 98.29      A    C  
ANISOU 1959  CG  LYS A 276    15173   9107  13064   -864  -3400   3197  A    C  
ATOM   1960  CD  LYS A 276      51.525 -22.026  22.307  1.00 99.76      A    C  
ANISOU 1960  CD  LYS A 276    15427   9466  13011  -1012  -3396   3279  A    C  
ATOM   1961  CE  LYS A 276      51.319 -20.569  21.881  1.00109.50      A    C  
ANISOU 1961  CE  LYS A 276    16418  10967  14220  -1075  -3205   3117  A    C  
ATOM   1962  NZ  LYS A 276      51.799 -19.552  22.875  1.00111.75      A    N1+
ANISOU 1962  NZ  LYS A 276    16706  11435  14320  -1133  -3260   3149  A    N1+
ATOM   1963  N   ASP A 277      52.566 -27.597  20.959  1.00113.38      A    N  
ANISOU 1963  N   ASP A 277    17747  10024  15307   -419  -3986   3505  A    N  
ATOM   1964  CA  ASP A 277      53.424 -28.747  21.247  1.00118.88      A    C  
ANISOU 1964  CA  ASP A 277    18631  10463  16075   -189  -4256   3619  A    C  
ATOM   1965  C   ASP A 277      54.029 -29.371  19.987  1.00111.36      A    C  
ANISOU 1965  C   ASP A 277    17541   9388  15383     96  -4310   3463  A    C  
ATOM   1966  O   ASP A 277      55.218 -29.692  19.947  1.00106.12      A    O  
ANISOU 1966  O   ASP A 277    16809   8694  14820    394  -4520   3459  A    O  
ATOM   1967  CB  ASP A 277      52.654 -29.818  22.027  1.00130.77      A    C  
ANISOU 1967  CB  ASP A 277    20550  11671  17465   -367  -4302   3828  A    C  
ATOM   1968  CG  ASP A 277      52.643 -29.560  23.519  1.00141.44      A    C  
ANISOU 1968  CG  ASP A 277    22100  13081  18560   -516  -4388   4037  A    C  
ATOM   1969  OD1 ASP A 277      52.873 -28.399  23.925  1.00144.36      A    O  
ANISOU 1969  OD1 ASP A 277    22287  13746  18817   -565  -4341   3999  A    O  
ATOM   1970  OD2 ASP A 277      52.408 -30.521  24.284  1.00146.14      A    O1-
ANISOU 1970  OD2 ASP A 277    23047  13420  19058   -588  -4505   4239  A    O1-
ATOM   1971  N   ARG A 278      53.205 -29.544  18.960  1.00107.83      A    N  
ANISOU 1971  N   ARG A 278    17048   8882  15040      6  -4121   3329  A    N  
ATOM   1972  CA  ARG A 278      53.640 -30.235  17.757  1.00108.95      A    C  
ANISOU 1972  CA  ARG A 278    17105   8880  15411    253  -4156   3178  A    C  
ATOM   1973  C   ARG A 278      54.552 -29.356  16.910  1.00103.03      A    C  
ANISOU 1973  C   ARG A 278    15957   8408  14783    469  -4126   2982  A    C  
ATOM   1974  O   ARG A 278      55.377 -29.860  16.151  1.00104.83      A    O  
ANISOU 1974  O   ARG A 278    16082   8563  15186    759  -4222   2876  A    O  
ATOM   1975  CB  ARG A 278      52.432 -30.712  16.944  1.00119.21      A    C  
ANISOU 1975  CB  ARG A 278    18497  10032  16766     66  -3969   3097  A    C  
ATOM   1976  CG  ARG A 278      52.717 -31.907  16.036  1.00129.32      A    C  
ANISOU 1976  CG  ARG A 278    19877  11017  18242    282  -4059   3011  A    C  
ATOM   1977  CD  ARG A 278      51.453 -32.385  15.334  1.00135.10      A    C  
ANISOU 1977  CD  ARG A 278    20724  11602  19005     52  -3885   2943  A    C  
ATOM   1978  NE  ARG A 278      51.747 -33.192  14.153  1.00141.32      A    N  
ANISOU 1978  NE  ARG A 278    21506  12197  19992    267  -3919   2781  A    N  
ATOM   1979  CZ  ARG A 278      52.000 -32.694  12.944  1.00144.47      A    C  
ANISOU 1979  CZ  ARG A 278    21603  12773  20516    403  -3809   2553  A    C  
ATOM   1980  NH1 ARG A 278      52.003 -31.381  12.744  1.00137.25      A    N1+
ANISOU 1980  NH1 ARG A 278    20371  12223  19555    346  -3664   2469  A    N1+
ATOM   1981  NH2 ARG A 278      52.256 -33.511  11.932  1.00150.66      A    N  
ANISOU 1981  NH2 ARG A 278    22417  13363  21465    599  -3846   2410  A    N  
ATOM   1982  N   LEU A 279      54.407 -28.041  17.053  1.00 97.48      A    N  
ANISOU 1982  N   LEU A 279    15036   8020  13981    326  -3989   2934  A    N  
ATOM   1983  CA  LEU A 279      55.216 -27.086  16.301  1.00 90.64      A    C  
ANISOU 1983  CA  LEU A 279    13797   7434  13207    482  -3943   2760  A    C  
ATOM   1984  C   LEU A 279      56.345 -26.516  17.155  1.00 84.24      A    C  
ANISOU 1984  C   LEU A 279    12879   6801  12326    594  -4119   2834  A    C  
ATOM   1985  O   LEU A 279      57.282 -25.891  16.642  1.00 80.18      A    O  
ANISOU 1985  O   LEU A 279    12065   6499  11899    760  -4139   2713  A    O  
ATOM   1986  CB  LEU A 279      54.340 -25.952  15.767  1.00 87.81      A    C  
ANISOU 1986  CB  LEU A 279    13262   7303  12797    259  -3674   2641  A    C  
ATOM   1987  CG  LEU A 279      53.438 -26.337  14.601  1.00 91.74      A    C  
ANISOU 1987  CG  LEU A 279    13754   7704  13400    200  -3499   2509  A    C  
ATOM   1988  CD1 LEU A 279      52.697 -25.115  14.071  1.00 93.52      A    C  
ANISOU 1988  CD1 LEU A 279    13775   8185  13573     19  -3253   2392  A    C  
ATOM   1989  CD2 LEU A 279      54.266 -26.982  13.504  1.00 90.56      A    C  
ANISOU 1989  CD2 LEU A 279    13482   7468  13458    498  -3573   2368  A    C  
ATOM   1990  N   LYS A 280      56.218 -26.716  18.463  1.00 84.75      A    N  
ANISOU 1990  N   LYS A 280    13190   6787  12222    481  -4240   3035  A    N  
ATOM   1991  CA  LYS A 280      57.244 -26.368  19.446  1.00103.46      A    C  
ANISOU 1991  CA  LYS A 280    15524   9285  14501    576  -4449   3138  A    C  
ATOM   1992  C   LYS A 280      58.654 -26.690  18.940  1.00112.93      A    C  
ANISOU 1992  C   LYS A 280    16509  10521  15879    935  -4638   3061  A    C  
ATOM   1993  O   LYS A 280      59.594 -25.916  19.148  1.00106.46      A    O  
ANISOU 1993  O   LYS A 280    15452   9953  15046   1018  -4723   3028  A    O  
ATOM   1994  CB  LYS A 280      56.973 -27.151  20.738  1.00109.59      A    C  
ANISOU 1994  CB  LYS A 280    16678   9843  15117    491  -4609   3379  A    C  
ATOM   1995  CG  LYS A 280      57.729 -26.693  21.973  1.00107.97      A    C  
ANISOU 1995  CG  LYS A 280    16496   9782  14748    499  -4802   3514  A    C  
ATOM   1996  CD  LYS A 280      57.389 -27.604  23.153  1.00107.18      A    C  
ANISOU 1996  CD  LYS A 280    16802   9432  14488    419  -4953   3760  A    C  
ATOM   1997  CE  LYS A 280      58.214 -27.257  24.378  1.00108.22      A    C  
ANISOU 1997  CE  LYS A 280    16972   9694  14453    454  -5179   3900  A    C  
ATOM   1998  NZ  LYS A 280      57.939 -28.172  25.517  1.00109.32      A    N1+
ANISOU 1998  NZ  LYS A 280    17520   9588  14427    389  -5339   4150  A    N1+
ATOM   1999  N   ALA A 281      58.787 -27.845  18.286  1.00119.45      A    N  
ANISOU 1999  N   ALA A 281    17422  11097  16868   1144  -4704   3030  A    N  
ATOM   2000  CA  ALA A 281      60.059 -28.291  17.723  1.00112.02      A    C  
ANISOU 2000  CA  ALA A 281    16286  10169  16108   1515  -4869   2945  A    C  
ATOM   2001  C   ALA A 281      60.614 -27.281  16.719  1.00104.25      A    C  
ANISOU 2001  C   ALA A 281    14878   9504  15228   1583  -4735   2731  A    C  
ATOM   2002  O   ALA A 281      61.633 -26.628  16.963  1.00 99.34      A    O  
ANISOU 2002  O   ALA A 281    14010   9132  14601   1686  -4838   2713  A    O  
ATOM   2003  CB  ALA A 281      59.892 -29.665  17.061  1.00103.46      A    C  
ANISOU 2003  CB  ALA A 281    15394   8739  15177   1699  -4911   2918  A    C  
ATOM   2004  N   TYR A 282      59.912 -27.148  15.599  1.00100.24      A    N  
ANISOU 2004  N   TYR A 282    14293   8990  14803   1508  -4504   2574  A    N  
ATOM   2005  CA  TYR A 282      60.361 -26.340  14.472  1.00 91.14      A    C  
ANISOU 2005  CA  TYR A 282    12770   8099  13760   1583  -4360   2366  A    C  
ATOM   2006  C   TYR A 282      60.527 -24.853  14.770  1.00 92.98      A    C  
ANISOU 2006  C   TYR A 282    12777   8669  13880   1400  -4272   2344  A    C  
ATOM   2007  O   TYR A 282      61.512 -24.240  14.353  1.00 94.17      A    O  
ANISOU 2007  O   TYR A 282    12615   9066  14100   1529  -4291   2242  A    O  
ATOM   2008  CB  TYR A 282      59.398 -26.525  13.301  1.00 86.27      A    C  
ANISOU 2008  CB  TYR A 282    12173   7386  13221   1502  -4132   2225  A    C  
ATOM   2009  CG  TYR A 282      59.188 -27.969  12.934  1.00 93.53      A    C  
ANISOU 2009  CG  TYR A 282    13328   7959  14251   1660  -4207   2227  A    C  
ATOM   2010  CD1 TYR A 282      58.173 -28.713  13.521  1.00 98.07      A    C  
ANISOU 2010  CD1 TYR A 282    14269   8249  14745   1482  -4218   2365  A    C  
ATOM   2011  CD2 TYR A 282      60.018 -28.598  12.012  1.00100.52      A    C  
ANISOU 2011  CD2 TYR A 282    14077   8799  15317   1984  -4266   2090  A    C  
ATOM   2012  CE1 TYR A 282      57.984 -30.046  13.195  1.00104.30      A    C  
ANISOU 2012  CE1 TYR A 282    15301   8697  15633   1610  -4293   2369  A    C  
ATOM   2013  CE2 TYR A 282      59.838 -29.929  11.676  1.00105.89      A    C  
ANISOU 2013  CE2 TYR A 282    14998   9138  16096   2138  -4339   2082  A    C  
ATOM   2014  CZ  TYR A 282      58.818 -30.649  12.270  1.00109.11      A    C  
ANISOU 2014  CZ  TYR A 282    15787   9246  16423   1943  -4357   2224  A    C  
ATOM   2015  OH  TYR A 282      58.631 -31.975  11.941  1.00115.12      A    O  
ANISOU 2015  OH  TYR A 282    16813   9647  17282   2077  -4434   2217  A    O  
ATOM   2016  N   VAL A 283      59.566 -24.274  15.486  1.00 97.75      A    N  
ANISOU 2016  N   VAL A 283    13544   9286  14309   1099  -4172   2435  A    N  
ATOM   2017  CA  VAL A 283      59.474 -22.817  15.588  1.00102.70      A    C  
ANISOU 2017  CA  VAL A 283    13990  10201  14831    900  -4037   2384  A    C  
ATOM   2018  C   VAL A 283      60.377 -22.217  16.665  1.00105.98      A    C  
ANISOU 2018  C   VAL A 283    14341  10791  15135    895  -4216   2479  A    C  
ATOM   2019  O   VAL A 283      61.171 -21.312  16.387  1.00108.27      A    O  
ANISOU 2019  O   VAL A 283    14347  11339  15450    924  -4209   2386  A    O  
ATOM   2020  CB  VAL A 283      58.011 -22.356  15.803  1.00100.71      A    C  
ANISOU 2020  CB  VAL A 283    13916   9911  14439    589  -3827   2414  A    C  
ATOM   2021  CG1 VAL A 283      57.906 -20.834  15.742  1.00 92.71      A    C  
ANISOU 2021  CG1 VAL A 283    12715   9177  13335    414  -3672   2336  A    C  
ATOM   2022  CG2 VAL A 283      57.104 -22.993  14.766  1.00 96.73      A    C  
ANISOU 2022  CG2 VAL A 283    13474   9240  14039    581  -3669   2325  A    C  
ATOM   2023  N   ARG A 284      60.234 -22.709  17.892  1.00101.02      A    N  
ANISOU 2023  N   ARG A 284    13984  10026  14374    841  -4375   2664  A    N  
ATOM   2024  CA  ARG A 284      61.082 -22.277  19.004  1.00104.65      A    C  
ANISOU 2024  CA  ARG A 284    14420  10631  14713    842  -4578   2768  A    C  
ATOM   2025  C   ARG A 284      60.739 -20.884  19.550  1.00 98.50      A    C  
ANISOU 2025  C   ARG A 284    13601  10071  13752    565  -4461   2760  A    C  
ATOM   2026  O   ARG A 284      60.518 -20.732  20.752  1.00 94.93      A    O  
ANISOU 2026  O   ARG A 284    13354   9607  13107    421  -4545   2900  A    O  
ATOM   2027  CB  ARG A 284      62.563 -22.368  18.622  1.00109.74      A    C  
ANISOU 2027  CB  ARG A 284    14766  11424  15505   1128  -4756   2699  A    C  
ATOM   2028  CG  ARG A 284      63.011 -23.779  18.272  1.00115.77      A    C  
ANISOU 2028  CG  ARG A 284    15595  11963  16430   1438  -4911   2722  A    C  
ATOM   2029  CD  ARG A 284      64.448 -23.801  17.787  1.00123.47      A    C  
ANISOU 2029  CD  ARG A 284    16231  13123  17560   1733  -5055   2628  A    C  
ATOM   2030  NE  ARG A 284      64.952 -25.165  17.644  1.00134.50      A    N  
ANISOU 2030  NE  ARG A 284    17714  14297  19091   2060  -5239   2666  A    N  
ATOM   2031  CZ  ARG A 284      66.241 -25.475  17.536  1.00140.22      A    C  
ANISOU 2031  CZ  ARG A 284    18209  15137  19932   2367  -5435   2636  A    C  
ATOM   2032  NH1 ARG A 284      67.159 -24.515  17.556  1.00138.59      A    N1+
ANISOU 2032  NH1 ARG A 284    17659  15277  19721   2364  -5471   2571  A    N1+
ATOM   2033  NH2 ARG A 284      66.614 -26.744  17.412  1.00141.84      A    N  
ANISOU 2033  NH2 ARG A 284    18527  15111  20257   2678  -5596   2671  A    N  
ATOM   2034  N   ASP A 285      60.691 -19.877  18.678  1.00 94.78      A    N  
ANISOU 2034  N   ASP A 285    12886   9791  13335    494  -4268   2596  A    N  
ATOM   2035  CA  ASP A 285      60.314 -18.528  19.105  1.00 87.24      A    C  
ANISOU 2035  CA  ASP A 285    11911   9020  12216    240  -4140   2572  A    C  
ATOM   2036  C   ASP A 285      58.898 -18.471  19.672  1.00 85.07      A    C  
ANISOU 2036  C   ASP A 285    11926   8619  11776      4  -3989   2650  A    C  
ATOM   2037  O   ASP A 285      57.936 -18.838  18.999  1.00 81.97      A    O  
ANISOU 2037  O   ASP A 285    11601   8101  11442    -33  -3815   2609  A    O  
ATOM   2038  CB  ASP A 285      60.443 -17.529  17.960  1.00 89.17      A    C  
ANISOU 2038  CB  ASP A 285    11868   9457  12557    214  -3950   2387  A    C  
ATOM   2039  CG  ASP A 285      60.090 -16.109  18.385  1.00 95.92      A    C  
ANISOU 2039  CG  ASP A 285    12719  10480  13246    -35  -3826   2358  A    C  
ATOM   2040  OD1 ASP A 285      58.889 -15.762  18.421  1.00 83.88      A    O  
ANISOU 2040  OD1 ASP A 285    11349   8895  11626   -209  -3633   2355  A    O  
ATOM   2041  OD2 ASP A 285      61.023 -15.334  18.684  1.00108.39      A    O1-
ANISOU 2041  OD2 ASP A 285    14140  12254  14790    -55  -3923   2333  A    O1-
ATOM   2042  N   PRO A 286      58.768 -17.998  20.917  1.00 89.67      A    N  
ANISOU 2042  N   PRO A 286    12675   9252  12145   -159  -4053   2759  A    N  
ATOM   2043  CA  PRO A 286      57.474 -17.901  21.599  1.00 90.73      A    C  
ANISOU 2043  CA  PRO A 286    13081   9297  12095   -387  -3911   2840  A    C  
ATOM   2044  C   PRO A 286      56.438 -17.132  20.775  1.00 90.04      A    C  
ANISOU 2044  C   PRO A 286    12920   9269  12024   -524  -3612   2708  A    C  
ATOM   2045  O   PRO A 286      55.319 -17.625  20.609  1.00 96.15      A    O  
ANISOU 2045  O   PRO A 286    13840   9906  12786   -607  -3471   2733  A    O  
ATOM   2046  CB  PRO A 286      57.806 -17.118  22.874  1.00 84.55      A    C  
ANISOU 2046  CB  PRO A 286    12387   8649  11088   -522  -4016   2917  A    C  
ATOM   2047  CG  PRO A 286      59.249 -17.325  23.086  1.00 90.02      A    C  
ANISOU 2047  CG  PRO A 286    12936   9420  11846   -340  -4287   2942  A    C  
ATOM   2048  CD  PRO A 286      59.865 -17.452  21.731  1.00 91.00      A    C  
ANISOU 2048  CD  PRO A 286    12762   9590  12224   -146  -4257   2798  A    C  
ATOM   2049  N   TYR A 287      56.803 -15.950  20.276  1.00 81.69      A    N  
ANISOU 2049  N   TYR A 287    11641   8411  10988   -553  -3523   2574  A    N  
ATOM   2050  CA  TYR A 287      55.850 -15.071  19.583  1.00 90.57      A    C  
ANISOU 2050  CA  TYR A 287    12706   9604  12102   -681  -3251   2455  A    C  
ATOM   2051  C   TYR A 287      55.291 -15.688  18.307  1.00 86.61      A    C  
ANISOU 2051  C   TYR A 287    12124   9005  11781   -594  -3115   2373  A    C  
ATOM   2052  O   TYR A 287      54.084 -15.639  18.060  1.00 79.10      A    O  
ANISOU 2052  O   TYR A 287    11258   8004  10792   -708  -2925   2354  A    O  
ATOM   2053  CB  TYR A 287      56.469 -13.703  19.278  1.00 91.59      A    C  
ANISOU 2053  CB  TYR A 287    12629   9948  12223   -720  -3204   2336  A    C  
ATOM   2054  CG  TYR A 287      56.828 -12.924  20.516  1.00 98.49      A    C  
ANISOU 2054  CG  TYR A 287    13603  10925  12896   -851  -3303   2395  A    C  
ATOM   2055  CD1 TYR A 287      55.901 -12.745  21.536  1.00100.17      A    C  
ANISOU 2055  CD1 TYR A 287    14072  11093  12897  -1019  -3237   2477  A    C  
ATOM   2056  CD2 TYR A 287      58.092 -12.368  20.671  1.00 99.40      A    C  
ANISOU 2056  CD2 TYR A 287    13554  11191  13023   -815  -3461   2363  A    C  
ATOM   2057  CE1 TYR A 287      56.222 -12.039  22.675  1.00100.03      A    C  
ANISOU 2057  CE1 TYR A 287    14162  11166  12678  -1138  -3328   2522  A    C  
ATOM   2058  CE2 TYR A 287      58.422 -11.656  21.807  1.00 98.69      A    C  
ANISOU 2058  CE2 TYR A 287    13565  11193  12739   -947  -3562   2409  A    C  
ATOM   2059  CZ  TYR A 287      57.483 -11.494  22.806  1.00 98.61      A    C  
ANISOU 2059  CZ  TYR A 287    13828  11124  12514  -1105  -3496   2486  A    C  
ATOM   2060  OH  TYR A 287      57.803 -10.786  23.940  1.00 97.91      A    O  
ANISOU 2060  OH  TYR A 287    13857  11127  12219  -1236  -3595   2522  A    O  
ATOM   2061  N   ALA A 288      56.180 -16.260  17.503  1.00 86.36      A    N  
ANISOU 2061  N   ALA A 288    11919   8956  11937   -389  -3216   2317  A    N  
ATOM   2062  CA  ALA A 288      55.777 -16.996  16.318  1.00 86.17      A    C  
ANISOU 2062  CA  ALA A 288    11836   8821  12082   -284  -3121   2238  A    C  
ATOM   2063  C   ALA A 288      54.751 -18.077  16.665  1.00 88.23      A    C  
ANISOU 2063  C   ALA A 288    12359   8856  12310   -345  -3104   2341  A    C  
ATOM   2064  O   ALA A 288      53.722 -18.215  15.998  1.00 87.77      A    O  
ANISOU 2064  O   ALA A 288    12324   8740  12283   -417  -2929   2286  A    O  
ATOM   2065  CB  ALA A 288      56.983 -17.609  15.651  1.00 81.67      A    C  
ANISOU 2065  CB  ALA A 288    11083   8252  11698    -34  -3268   2185  A    C  
ATOM   2066  N   LEU A 289      55.031 -18.845  17.708  1.00 90.35      A    N  
ANISOU 2066  N   LEU A 289    12824   8998  12507   -326  -3292   2496  A    N  
ATOM   2067  CA  LEU A 289      54.119 -19.907  18.109  1.00 91.54      A    C  
ANISOU 2067  CA  LEU A 289    13244   8922  12615   -403  -3289   2612  A    C  
ATOM   2068  C   LEU A 289      52.784 -19.335  18.578  1.00 88.00      A    C  
ANISOU 2068  C   LEU A 289    12926   8515  11994   -665  -3088   2643  A    C  
ATOM   2069  O   LEU A 289      51.728 -19.907  18.306  1.00 85.67      A    O  
ANISOU 2069  O   LEU A 289    12744   8099  11709   -761  -2968   2655  A    O  
ATOM   2070  CB  LEU A 289      54.742 -20.795  19.190  1.00 88.47      A    C  
ANISOU 2070  CB  LEU A 289    13057   8389  12167   -329  -3543   2787  A    C  
ATOM   2071  CG  LEU A 289      55.809 -21.789  18.723  1.00 89.81      A    C  
ANISOU 2071  CG  LEU A 289    13165   8436  12522    -45  -3745   2780  A    C  
ATOM   2072  CD1 LEU A 289      56.609 -22.301  19.911  1.00 85.84      A    C  
ANISOU 2072  CD1 LEU A 289    12818   7867  11932     37  -4015   2950  A    C  
ATOM   2073  CD2 LEU A 289      55.191 -22.951  17.952  1.00 88.63      A    C  
ANISOU 2073  CD2 LEU A 289    13128   8040  12506      9  -3696   2760  A    C  
ATOM   2074  N   ASP A 290      52.824 -18.200  19.270  1.00 82.37      A    N  
ANISOU 2074  N   ASP A 290    12194   7981  11123   -780  -3048   2646  A    N  
ATOM   2075  CA  ASP A 290      51.588 -17.607  19.759  1.00 83.08      A    C  
ANISOU 2075  CA  ASP A 290    12400   8127  11040  -1006  -2853   2667  A    C  
ATOM   2076  C   ASP A 290      50.713 -17.121  18.607  1.00 81.40      A    C  
ANISOU 2076  C   ASP A 290    12035   7982  10911  -1046  -2613   2520  A    C  
ATOM   2077  O   ASP A 290      49.501 -17.344  18.607  1.00 84.57      A    O  
ANISOU 2077  O   ASP A 290    12534   8340  11258  -1184  -2460   2539  A    O  
ATOM   2078  CB  ASP A 290      51.857 -16.462  20.726  1.00 88.91      A    C  
ANISOU 2078  CB  ASP A 290    13160   9034  11587  -1105  -2863   2685  A    C  
ATOM   2079  CG  ASP A 290      50.579 -15.919  21.342  1.00 93.86      A    C  
ANISOU 2079  CG  ASP A 290    13928   9715  12019  -1321  -2664   2711  A    C  
ATOM   2080  OD1 ASP A 290      49.809 -16.717  21.921  1.00 91.94      A    O  
ANISOU 2080  OD1 ASP A 290    13891   9352  11688  -1426  -2644   2831  A    O  
ATOM   2081  OD2 ASP A 290      50.344 -14.696  21.245  1.00 94.29      A    O1-
ANISOU 2081  OD2 ASP A 290    13891   9931  12005  -1383  -2524   2611  A    O1-
ATOM   2082  N   LEU A 291      51.326 -16.464  17.625  1.00 70.45      A    N  
ANISOU 2082  N   LEU A 291    10406   6712   9651   -929  -2583   2377  A    N  
ATOM   2083  CA  LEU A 291      50.578 -15.993  16.465  1.00 73.11      A    C  
ANISOU 2083  CA  LEU A 291    10596   7116  10068   -947  -2373   2238  A    C  
ATOM   2084  C   LEU A 291      49.983 -17.142  15.646  1.00 77.68      A    C  
ANISOU 2084  C   LEU A 291    11199   7534  10780   -908  -2338   2221  A    C  
ATOM   2085  O   LEU A 291      48.818 -17.069  15.228  1.00 74.56      A    O  
ANISOU 2085  O   LEU A 291    10810   7151  10369  -1017  -2161   2181  A    O  
ATOM   2086  CB  LEU A 291      51.433 -15.084  15.577  1.00 64.64      A    C  
ANISOU 2086  CB  LEU A 291     9272   6194   9093   -834  -2356   2100  A    C  
ATOM   2087  CG  LEU A 291      50.754 -14.548  14.305  1.00 60.90      A    C  
ANISOU 2087  CG  LEU A 291     8645   5797   8699   -835  -2151   1958  A    C  
ATOM   2088  CD1 LEU A 291      49.369 -13.987  14.595  1.00 58.24      A    C  
ANISOU 2088  CD1 LEU A 291     8399   5506   8225  -1005  -1959   1964  A    C  
ATOM   2089  CD2 LEU A 291      51.624 -13.494  13.627  1.00 61.21      A    C  
ANISOU 2089  CD2 LEU A 291     8469   5996   8793   -760  -2132   1845  A    C  
ATOM   2090  N   ILE A 292      50.772 -18.194  15.415  1.00 72.74      A    N  
ANISOU 2090  N   ILE A 292    10588   6764  10285   -752  -2509   2246  A    N  
ATOM   2091  CA  ILE A 292      50.276 -19.337  14.653  1.00 75.03      A    C  
ANISOU 2091  CA  ILE A 292    10930   6876  10704   -712  -2493   2223  A    C  
ATOM   2092  C   ILE A 292      49.103 -19.971  15.374  1.00 82.12      A    C  
ANISOU 2092  C   ILE A 292    12068   7646  11488   -909  -2441   2344  A    C  
ATOM   2093  O   ILE A 292      48.129 -20.398  14.753  1.00 87.11      A    O  
ANISOU 2093  O   ILE A 292    12718   8217  12164   -991  -2320   2302  A    O  
ATOM   2094  CB  ILE A 292      51.325 -20.422  14.468  1.00 73.88      A    C  
ANISOU 2094  CB  ILE A 292    10806   6567  10698   -501  -2701   2245  A    C  
ATOM   2095  CG1 ILE A 292      52.498 -19.910  13.639  1.00 69.57      A    C  
ANISOU 2095  CG1 ILE A 292     9995   6160  10280   -299  -2743   2115  A    C  
ATOM   2096  CG2 ILE A 292      50.686 -21.645  13.809  1.00 75.46      A    C  
ANISOU 2096  CG2 ILE A 292    11117   6548  11006   -491  -2684   2229  A    C  
ATOM   2097  CD1 ILE A 292      53.734 -20.810  13.717  1.00 72.55      A    C  
ANISOU 2097  CD1 ILE A 292    10371   6425  10770    -65  -2973   2148  A    C  
ATOM   2098  N   ASP A 293      49.210 -20.037  16.694  1.00 82.03      A    N  
ANISOU 2098  N   ASP A 293    12238   7604  11323   -993  -2534   2497  A    N  
ATOM   2099  CA  ASP A 293      48.131 -20.552  17.522  1.00 92.45      A    C  
ANISOU 2099  CA  ASP A 293    13793   8829  12504  -1203  -2476   2629  A    C  
ATOM   2100  C   ASP A 293      46.841 -19.736  17.340  1.00 90.91      A    C  
ANISOU 2100  C   ASP A 293    13530   8794  12217  -1388  -2223   2564  A    C  
ATOM   2101  O   ASP A 293      45.734 -20.283  17.351  1.00 89.79      A    O  
ANISOU 2101  O   ASP A 293    13488   8585  12042  -1546  -2118   2603  A    O  
ATOM   2102  CB  ASP A 293      48.570 -20.549  18.989  1.00102.42      A    C  
ANISOU 2102  CB  ASP A 293    15247  10077  13592  -1254  -2615   2795  A    C  
ATOM   2103  CG  ASP A 293      47.602 -21.275  19.892  1.00107.33      A    C  
ANISOU 2103  CG  ASP A 293    16141  10573  14068  -1463  -2583   2955  A    C  
ATOM   2104  OD1 ASP A 293      46.924 -22.214  19.418  1.00115.95      A    O  
ANISOU 2104  OD1 ASP A 293    17313  11504  15238  -1522  -2541   2967  A    O  
ATOM   2105  OD2 ASP A 293      47.525 -20.903  21.081  1.00103.83      A    O1-
ANISOU 2105  OD2 ASP A 293    15834  10195  13422  -1577  -2598   3067  A    O1-
ATOM   2106  N   LYS A 294      46.993 -18.426  17.164  1.00 87.10      A    N  
ANISOU 2106  N   LYS A 294    12874   8524  11695  -1365  -2128   2465  A    N  
ATOM   2107  CA  LYS A 294      45.847 -17.536  17.005  1.00 84.33      A    C  
ANISOU 2107  CA  LYS A 294    12451   8337  11255  -1502  -1896   2397  A    C  
ATOM   2108  C   LYS A 294      45.293 -17.529  15.580  1.00 80.15      A    C  
ANISOU 2108  C   LYS A 294    11741   7838  10875  -1460  -1768   2253  A    C  
ATOM   2109  O   LYS A 294      44.149 -17.134  15.361  1.00 77.48      A    O  
ANISOU 2109  O   LYS A 294    11357   7600  10482  -1577  -1585   2210  A    O  
ATOM   2110  CB  LYS A 294      46.206 -16.127  17.468  1.00 85.14      A    C  
ANISOU 2110  CB  LYS A 294    12482   8629  11238  -1498  -1853   2356  A    C  
ATOM   2111  CG  LYS A 294      46.547 -16.094  18.940  1.00 91.24      A    C  
ANISOU 2111  CG  LYS A 294    13449   9390  11827  -1574  -1959   2496  A    C  
ATOM   2112  CD  LYS A 294      46.831 -14.696  19.442  1.00 91.54      A    C  
ANISOU 2112  CD  LYS A 294    13443   9605  11732  -1591  -1912   2447  A    C  
ATOM   2113  CE  LYS A 294      47.149 -14.738  20.928  1.00 92.57      A    C  
ANISOU 2113  CE  LYS A 294    13786   9722  11664  -1675  -2028   2586  A    C  
ATOM   2114  NZ  LYS A 294      47.393 -13.385  21.491  1.00 96.25      A    N1+
ANISOU 2114  NZ  LYS A 294    14239  10349  11981  -1710  -1986   2533  A    N1+
ATOM   2115  N   LEU A 295      46.109 -17.968  14.622  1.00 77.06      A    N  
ANISOU 2115  N   LEU A 295    11245   7371  10664  -1287  -1867   2175  A    N  
ATOM   2116  CA  LEU A 295      45.659 -18.181  13.249  1.00 69.16      A    C  
ANISOU 2116  CA  LEU A 295    10102   6370   9805  -1240  -1775   2044  A    C  
ATOM   2117  C   LEU A 295      44.911 -19.515  13.096  1.00 79.17      A    C  
ANISOU 2117  C   LEU A 295    11509   7449  11124  -1330  -1787   2091  A    C  
ATOM   2118  O   LEU A 295      43.835 -19.565  12.503  1.00 80.64      A    O  
ANISOU 2118  O   LEU A 295    11645   7676  11320  -1435  -1647   2033  A    O  
ATOM   2119  CB  LEU A 295      46.841 -18.146  12.282  1.00 59.91      A    C  
ANISOU 2119  CB  LEU A 295     8770   5199   8795  -1020  -1867   1936  A    C  
ATOM   2120  CG  LEU A 295      47.531 -16.804  12.054  1.00 62.63      A    C  
ANISOU 2120  CG  LEU A 295     8935   5739   9122   -940  -1829   1855  A    C  
ATOM   2121  CD1 LEU A 295      48.794 -17.007  11.250  1.00 65.61      A    C  
ANISOU 2121  CD1 LEU A 295     9171   6103   9654   -734  -1942   1774  A    C  
ATOM   2122  CD2 LEU A 295      46.603 -15.851  11.341  1.00 60.33      A    C  
ANISOU 2122  CD2 LEU A 295     8519   5605   8800  -1005  -1624   1752  A    C  
ATOM   2123  N   LEU A 296      45.475 -20.596  13.630  1.00 78.41      A    N  
ANISOU 2123  N   LEU A 296    11592   7143  11057  -1294  -1961   2199  A    N  
ATOM   2124  CA  LEU A 296      44.836 -21.904  13.497  1.00 83.90      A    C  
ANISOU 2124  CA  LEU A 296    12451   7625  11803  -1386  -1987   2248  A    C  
ATOM   2125  C   LEU A 296      43.792 -22.135  14.586  1.00 88.93      A    C  
ANISOU 2125  C   LEU A 296    13276   8242  12270  -1642  -1917   2395  A    C  
ATOM   2126  O   LEU A 296      43.783 -23.169  15.239  1.00 94.98      A    O  
ANISOU 2126  O   LEU A 296    14275   8803  13011  -1713  -2025   2530  A    O  
ATOM   2127  CB  LEU A 296      45.871 -23.032  13.476  1.00 81.97      A    C  
ANISOU 2127  CB  LEU A 296    12333   7135  11676  -1217  -2205   2292  A    C  
ATOM   2128  CG  LEU A 296      46.892 -22.971  12.335  1.00 77.53      A    C  
ANISOU 2128  CG  LEU A 296    11582   6588  11290   -958  -2268   2140  A    C  
ATOM   2129  CD1 LEU A 296      47.841 -24.158  12.387  1.00 79.52      A    C  
ANISOU 2129  CD1 LEU A 296    11972   6591  11652   -778  -2482   2186  A    C  
ATOM   2130  CD2 LEU A 296      46.194 -22.904  10.990  1.00 74.24      A    C  
ANISOU 2130  CD2 LEU A 296    11015   6226  10965   -973  -2124   1976  A    C  
ATOM   2131  N   VAL A 297      42.916 -21.152  14.766  1.00 88.64      A    N  
ANISOU 2131  N   VAL A 297    13140   8425  12114  -1774  -1732   2367  A    N  
ATOM   2132  CA  VAL A 297      41.810 -21.244  15.713  1.00 79.44      A    C  
ANISOU 2132  CA  VAL A 297    12109   7296  10779  -2022  -1623   2484  A    C  
ATOM   2133  C   VAL A 297      40.581 -21.827  15.018  1.00 81.24      A    C  
ANISOU 2133  C   VAL A 297    12306   7505  11055  -2182  -1500   2438  A    C  
ATOM   2134  O   VAL A 297      40.272 -21.463  13.882  1.00 81.29      A    O  
ANISOU 2134  O   VAL A 297    12113   7613  11163  -2122  -1413   2287  A    O  
ATOM   2135  CB  VAL A 297      41.495 -19.855  16.322  1.00 78.91      A    C  
ANISOU 2135  CB  VAL A 297    11950   7484  10547  -2068  -1483   2470  A    C  
ATOM   2136  CG1 VAL A 297      40.066 -19.777  16.819  1.00 79.56      A    C  
ANISOU 2136  CG1 VAL A 297    12066   7679  10486  -2307  -1296   2518  A    C  
ATOM   2137  CG2 VAL A 297      42.469 -19.538  17.437  1.00 78.52      A    C  
ANISOU 2137  CG2 VAL A 297    12024   7423  10388  -2009  -1614   2571  A    C  
ATOM   2138  N   LEU A 298      39.888 -22.737  15.700  1.00 84.28      A    N  
ANISOU 2138  N   LEU A 298    12893   7766  11365  -2394  -1497   2572  A    N  
ATOM   2139  CA  LEU A 298      38.770 -23.473  15.110  1.00 79.41      A    C  
ANISOU 2139  CA  LEU A 298    12273   7103  10796  -2577  -1407   2545  A    C  
ATOM   2140  C   LEU A 298      37.562 -22.605  14.750  1.00 78.46      A    C  
ANISOU 2140  C   LEU A 298    11933   7265  10615  -2695  -1180   2452  A    C  
ATOM   2141  O   LEU A 298      37.087 -22.628  13.619  1.00 76.21      A    O  
ANISOU 2141  O   LEU A 298    11484   7031  10439  -2682  -1120   2319  A    O  
ATOM   2142  CB  LEU A 298      38.332 -24.591  16.048  1.00 78.51      A    C  
ANISOU 2142  CB  LEU A 298    12441   6796  10592  -2803  -1454   2729  A    C  
ATOM   2143  CG  LEU A 298      39.260 -25.797  16.120  1.00 86.33      A    C  
ANISOU 2143  CG  LEU A 298    13672   7447  11681  -2708  -1682   2812  A    C  
ATOM   2144  CD1 LEU A 298      38.908 -26.651  17.334  1.00 90.14      A    C  
ANISOU 2144  CD1 LEU A 298    14462   7766  12022  -2932  -1724   3029  A    C  
ATOM   2145  CD2 LEU A 298      39.188 -26.607  14.829  1.00 82.97      A    C  
ANISOU 2145  CD2 LEU A 298    13212   6860  11452  -2659  -1726   2687  A    C  
ATOM   2146  N   ASP A 299      37.046 -21.859  15.717  1.00 81.04      A    N  
ANISOU 2146  N   ASP A 299    12258   7777  10758  -2804  -1057   2520  A    N  
ATOM   2147  CA  ASP A 299      35.914 -20.987  15.451  1.00 86.95      A    C  
ANISOU 2147  CA  ASP A 299    12794   8804  11440  -2887   -842   2433  A    C  
ATOM   2148  C   ASP A 299      36.377 -19.793  14.612  1.00 94.07      A    C  
ANISOU 2148  C   ASP A 299    13468   9862  12411  -2652   -809   2273  A    C  
ATOM   2149  O   ASP A 299      37.167 -18.963  15.074  1.00 93.30      A    O  
ANISOU 2149  O   ASP A 299    13377   9815  12257  -2516   -843   2276  A    O  
ATOM   2150  CB  ASP A 299      35.282 -20.519  16.762  1.00 94.03      A    C  
ANISOU 2150  CB  ASP A 299    13765   9851  12112  -3049   -714   2545  A    C  
ATOM   2151  CG  ASP A 299      34.036 -19.686  16.545  1.00103.34      A    C  
ANISOU 2151  CG  ASP A 299    14724  11323  13217  -3130   -486   2460  A    C  
ATOM   2152  OD1 ASP A 299      33.489 -19.718  15.421  1.00106.65      A    O  
ANISOU 2152  OD1 ASP A 299    14957  11809  13756  -3117   -434   2340  A    O  
ATOM   2153  OD2 ASP A 299      33.602 -18.999  17.497  1.00105.71      A    O1-
ANISOU 2153  OD2 ASP A 299    15038  11793  13335  -3198   -361   2508  A    O1-
ATOM   2154  N   PRO A 300      35.888 -19.710  13.366  1.00 94.16      A    N  
ANISOU 2154  N   PRO A 300    13287   9949  12541  -2613   -748   2134  A    N  
ATOM   2155  CA  PRO A 300      36.239 -18.634  12.431  1.00 81.40      A    C  
ANISOU 2155  CA  PRO A 300    11460   8475  10993  -2404   -712   1983  A    C  
ATOM   2156  C   PRO A 300      36.083 -17.266  13.069  1.00 81.54      A    C  
ANISOU 2156  C   PRO A 300    11409   8708  10866  -2361   -590   1977  A    C  
ATOM   2157  O   PRO A 300      36.777 -16.326  12.691  1.00 85.27      A    O  
ANISOU 2157  O   PRO A 300    11791   9242  11365  -2178   -603   1897  A    O  
ATOM   2158  CB  PRO A 300      35.196 -18.795  11.315  1.00 77.38      A    C  
ANISOU 2158  CB  PRO A 300    10776   8068  10559  -2467   -615   1873  A    C  
ATOM   2159  CG  PRO A 300      34.107 -19.648  11.928  1.00 85.15      A    C  
ANISOU 2159  CG  PRO A 300    11848   9038  11468  -2742   -552   1972  A    C  
ATOM   2160  CD  PRO A 300      34.873 -20.602  12.785  1.00 91.15      A    C  
ANISOU 2160  CD  PRO A 300    12877   9538  12217  -2792   -702   2114  A    C  
ATOM   2161  N   ALA A 301      35.175 -17.160  14.031  1.00 83.74      A    N  
ANISOU 2161  N   ALA A 301    11737   9095  10985  -2534   -469   2059  A    N  
ATOM   2162  CA  ALA A 301      34.857 -15.873  14.635  1.00 83.47      A    C  
ANISOU 2162  CA  ALA A 301    11642   9271  10800  -2498   -331   2039  A    C  
ATOM   2163  C   ALA A 301      35.823 -15.524  15.750  1.00 81.43      A    C  
ANISOU 2163  C   ALA A 301    11561   8946  10434  -2452   -416   2125  A    C  
ATOM   2164  O   ALA A 301      35.905 -14.365  16.159  1.00 81.84      A    O  
ANISOU 2164  O   ALA A 301    11584   9132  10379  -2376   -342   2089  A    O  
ATOM   2165  CB  ALA A 301      33.430 -15.863  15.149  1.00 84.55      A    C  
ANISOU 2165  CB  ALA A 301    11733   9587  10805  -2690   -147   2073  A    C  
ATOM   2166  N   GLN A 302      36.545 -16.526  16.243  1.00 81.38      A    N  
ANISOU 2166  N   GLN A 302    11746   8727  10450  -2497   -579   2239  A    N  
ATOM   2167  CA  GLN A 302      37.545 -16.304  17.282  1.00 84.99      A    C  
ANISOU 2167  CA  GLN A 302    12372   9112  10808  -2451   -694   2328  A    C  
ATOM   2168  C   GLN A 302      38.951 -16.304  16.686  1.00 84.55      A    C  
ANISOU 2168  C   GLN A 302    12295   8928  10902  -2246   -879   2279  A    C  
ATOM   2169  O   GLN A 302      39.934 -16.021  17.376  1.00 80.92      A    O  
ANISOU 2169  O   GLN A 302    11934   8426  10386  -2176   -995   2330  A    O  
ATOM   2170  CB  GLN A 302      37.438 -17.360  18.378  1.00 86.23      A    C  
ANISOU 2170  CB  GLN A 302    12771   9132  10861  -2629   -760   2505  A    C  
ATOM   2171  CG  GLN A 302      36.174 -17.293  19.220  1.00 93.33      A    C  
ANISOU 2171  CG  GLN A 302    13713  10178  11572  -2847   -574   2574  A    C  
ATOM   2172  CD  GLN A 302      36.167 -18.347  20.325  1.00102.85      A    C  
ANISOU 2172  CD  GLN A 302    15184  11234  12662  -3032   -649   2765  A    C  
ATOM   2173  NE2 GLN A 302      35.159 -19.215  20.313  1.00 95.84      A    N  
ANISOU 2173  NE2 GLN A 302    14325  10327  11763  -3246   -566   2827  A    N  
ATOM   2174  OE1 GLN A 302      37.066 -18.383  21.171  1.00108.16      A    O  
ANISOU 2174  OE1 GLN A 302    16036  11809  13252  -2989   -786   2860  A    O  
ATOM   2175  N   ARG A 303      39.033 -16.626  15.399  1.00 80.38      A    N  
ANISOU 2175  N   ARG A 303    11628   8353  10557  -2155   -903   2178  A    N  
ATOM   2176  CA  ARG A 303      40.291 -16.600  14.663  1.00 73.81      A    C  
ANISOU 2176  CA  ARG A 303    10736   7433   9876  -1954  -1049   2110  A    C  
ATOM   2177  C   ARG A 303      40.744 -15.164  14.425  1.00 73.55      A    C  
ANISOU 2177  C   ARG A 303    10566   7562   9818  -1823   -995   2011  A    C  
ATOM   2178  O   ARG A 303      39.969 -14.326  13.954  1.00 83.38      A    O  
ANISOU 2178  O   ARG A 303    11677   8969  11034  -1823   -836   1922  A    O  
ATOM   2179  CB  ARG A 303      40.119 -17.318  13.326  1.00 71.02      A    C  
ANISOU 2179  CB  ARG A 303    10276   7004   9705  -1905  -1064   2017  A    C  
ATOM   2180  CG  ARG A 303      41.397 -17.523  12.531  1.00 67.52      A    C  
ANISOU 2180  CG  ARG A 303     9777   6455   9422  -1701  -1213   1949  A    C  
ATOM   2181  CD  ARG A 303      41.094 -18.423  11.353  1.00 68.90      A    C  
ANISOU 2181  CD  ARG A 303     9896   6531   9750  -1683  -1225   1868  A    C  
ATOM   2182  NE  ARG A 303      40.268 -19.548  11.782  1.00 73.92      A    N  
ANISOU 2182  NE  ARG A 303    10689   7037  10360  -1872  -1228   1962  A    N  
ATOM   2183  CZ  ARG A 303      39.318 -20.124  11.052  1.00 69.51      A    C  
ANISOU 2183  CZ  ARG A 303    10088   6465   9857  -1977  -1159   1908  A    C  
ATOM   2184  NH1 ARG A 303      39.039 -19.691   9.828  1.00 62.57      A    N1+
ANISOU 2184  NH1 ARG A 303     9012   5701   9059  -1900  -1084   1758  A    N1+
ATOM   2185  NH2 ARG A 303      38.635 -21.135  11.563  1.00 71.73      A    N  
ANISOU 2185  NH2 ARG A 303    10531   6619  10103  -2174  -1169   2008  A    N  
ATOM   2186  N   ILE A 304      42.002 -14.888  14.747  1.00 64.10      A    N  
ANISOU 2186  N   ILE A 304     9406   6319   8630  -1711  -1134   2028  A    N  
ATOM   2187  CA  ILE A 304      42.562 -13.547  14.588  1.00 64.83      A    C  
ANISOU 2187  CA  ILE A 304     9394   6543   8695  -1608  -1102   1943  A    C  
ATOM   2188  C   ILE A 304      42.443 -13.041  13.138  1.00 63.43      A    C  
ANISOU 2188  C   ILE A 304     9009   6445   8646  -1499  -1019   1796  A    C  
ATOM   2189  O   ILE A 304      42.475 -13.826  12.186  1.00 62.12      A    O  
ANISOU 2189  O   ILE A 304     8774   6202   8626  -1448  -1057   1752  A    O  
ATOM   2190  CB  ILE A 304      44.037 -13.511  15.062  1.00 65.91      A    C  
ANISOU 2190  CB  ILE A 304     9583   6613   8847  -1515  -1292   1985  A    C  
ATOM   2191  CG1 ILE A 304      44.474 -12.082  15.372  1.00 61.14      A    C  
ANISOU 2191  CG1 ILE A 304     8939   6144   8147  -1484  -1253   1933  A    C  
ATOM   2192  CG2 ILE A 304      44.958 -14.174  14.039  1.00 66.18      A    C  
ANISOU 2192  CG2 ILE A 304     9514   6549   9081  -1365  -1418   1931  A    C  
ATOM   2193  CD1 ILE A 304      45.859 -12.001  15.961  1.00 60.83      A    C  
ANISOU 2193  CD1 ILE A 304     8945   6066   8099  -1425  -1441   1979  A    C  
ATOM   2194  N   ASP A 305      42.272 -11.733  12.971  1.00 63.49      A    N  
ANISOU 2194  N   ASP A 305     8934   6599   8591  -1463   -906   1721  A    N  
ATOM   2195  CA  ASP A 305      42.171 -11.159  11.628  1.00 62.34      A    C  
ANISOU 2195  CA  ASP A 305     8608   6532   8545  -1359   -829   1593  A    C  
ATOM   2196  C   ASP A 305      43.492 -10.518  11.213  1.00 61.91      A    C  
ANISOU 2196  C   ASP A 305     8485   6482   8554  -1235   -916   1540  A    C  
ATOM   2197  O   ASP A 305      44.406 -10.373  12.027  1.00 59.46      A    O  
ANISOU 2197  O   ASP A 305     8255   6139   8199  -1235  -1026   1596  A    O  
ATOM   2198  CB  ASP A 305      41.015 -10.161  11.526  1.00 65.06      A    C  
ANISOU 2198  CB  ASP A 305     8897   7032   8791  -1388   -639   1539  A    C  
ATOM   2199  CG  ASP A 305      41.187  -8.957  12.448  1.00 82.31      A    C  
ANISOU 2199  CG  ASP A 305    11163   9290  10822  -1397   -594   1550  A    C  
ATOM   2200  OD1 ASP A 305      42.328  -8.655  12.874  1.00 85.97      A    O  
ANISOU 2200  OD1 ASP A 305    11683   9707  11274  -1366   -708   1571  A    O  
ATOM   2201  OD2 ASP A 305      40.170  -8.295  12.739  1.00 87.22      A    O1-
ANISOU 2201  OD2 ASP A 305    11789  10020  11330  -1433   -444   1531  A    O1-
ATOM   2202  N   SER A 306      43.601 -10.143   9.947  1.00 59.02      A    N  
ANISOU 2202  N   SER A 306     7968   6168   8288  -1137   -870   1435  A    N  
ATOM   2203  CA  SER A 306      44.869  -9.647   9.449  1.00 62.61      A    C  
ANISOU 2203  CA  SER A 306     8340   6635   8813  -1033   -946   1386  A    C  
ATOM   2204  C   SER A 306      45.313  -8.404  10.219  1.00 68.23      A    C  
ANISOU 2204  C   SER A 306     9109   7414   9404  -1061   -935   1398  A    C  
ATOM   2205  O   SER A 306      46.499  -8.220  10.500  1.00 73.08      A    O  
ANISOU 2205  O   SER A 306     9720   8014  10034  -1034  -1051   1412  A    O  
ATOM   2206  CB  SER A 306      44.789  -9.381   7.948  1.00 65.02      A    C  
ANISOU 2206  CB  SER A 306     8486   7000   9219   -939   -874   1274  A    C  
ATOM   2207  OG  SER A 306      43.663  -8.590   7.641  1.00 77.89      A    O  
ANISOU 2207  OG  SER A 306    10090   8729  10776   -962   -717   1232  A    O  
ATOM   2208  N   ASP A 307      44.358  -7.565  10.595  1.00 67.05      A    N  
ANISOU 2208  N   ASP A 307     9011   7337   9126  -1116   -799   1390  A    N  
ATOM   2209  CA  ASP A 307      44.707  -6.322  11.266  1.00 62.11      A    C  
ANISOU 2209  CA  ASP A 307     8459   6761   8379  -1141   -777   1385  A    C  
ATOM   2210  C   ASP A 307      45.349  -6.582  12.619  1.00 66.71      A    C  
ANISOU 2210  C   ASP A 307     9182   7291   8873  -1216   -903   1476  A    C  
ATOM   2211  O   ASP A 307      46.390  -6.009  12.941  1.00 71.15      A    O  
ANISOU 2211  O   ASP A 307     9761   7859   9414  -1216   -993   1473  A    O  
ATOM   2212  CB  ASP A 307      43.491  -5.407  11.416  1.00 66.98      A    C  
ANISOU 2212  CB  ASP A 307     9116   7459   8873  -1163   -601   1351  A    C  
ATOM   2213  CG  ASP A 307      43.883  -3.973  11.729  1.00 79.69      A    C  
ANISOU 2213  CG  ASP A 307    10791   9106  10382  -1158   -566   1311  A    C  
ATOM   2214  OD1 ASP A 307      44.606  -3.344  10.912  1.00 84.96      A    O  
ANISOU 2214  OD1 ASP A 307    11380   9782  11117  -1101   -582   1254  A    O  
ATOM   2215  OD2 ASP A 307      43.471  -3.478  12.799  1.00 82.90      A    O1-
ANISOU 2215  OD2 ASP A 307    11335   9527  10634  -1219   -519   1336  A    O1-
ATOM   2216  N   ASP A 308      44.730  -7.448  13.412  1.00 65.29      A    N  
ANISOU 2216  N   ASP A 308     9106   7066   8635  -1291   -914   1560  A    N  
ATOM   2217  CA  ASP A 308      45.258  -7.759  14.734  1.00 72.17      A    C  
ANISOU 2217  CA  ASP A 308    10131   7887   9404  -1365  -1037   1659  A    C  
ATOM   2218  C   ASP A 308      46.534  -8.579  14.630  1.00 68.62      A    C  
ANISOU 2218  C   ASP A 308     9644   7354   9074  -1305  -1239   1699  A    C  
ATOM   2219  O   ASP A 308      47.441  -8.465  15.462  1.00 65.61      A    O  
ANISOU 2219  O   ASP A 308     9335   6961   8633  -1325  -1375   1751  A    O  
ATOM   2220  CB  ASP A 308      44.217  -8.500  15.572  1.00 80.26      A    C  
ANISOU 2220  CB  ASP A 308    11283   8886  10326  -1470   -984   1748  A    C  
ATOM   2221  CG  ASP A 308      43.003  -7.649  15.866  1.00 86.22      A    C  
ANISOU 2221  CG  ASP A 308    12072   9747  10939  -1523   -786   1711  A    C  
ATOM   2222  OD1 ASP A 308      43.165  -6.421  16.031  1.00 91.34      A    O  
ANISOU 2222  OD1 ASP A 308    12740  10460  11503  -1501   -732   1650  A    O  
ATOM   2223  OD2 ASP A 308      41.888  -8.206  15.927  1.00 83.68      A    O1-
ANISOU 2223  OD2 ASP A 308    11757   9447  10591  -1586   -684   1740  A    O1-
ATOM   2224  N   ALA A 309      46.596  -9.406  13.597  1.00 65.51      A    N  
ANISOU 2224  N   ALA A 309     9134   6910   8847  -1225  -1260   1669  A    N  
ATOM   2225  CA  ALA A 309      47.750 -10.251  13.391  1.00 62.00      A    C  
ANISOU 2225  CA  ALA A 309     8640   6386   8529  -1137  -1441   1694  A    C  
ATOM   2226  C   ALA A 309      48.935  -9.355  13.115  1.00 61.48      A    C  
ANISOU 2226  C   ALA A 309     8464   6401   8495  -1077  -1501   1634  A    C  
ATOM   2227  O   ALA A 309      50.023  -9.582  13.642  1.00 63.59      A    O  
ANISOU 2227  O   ALA A 309     8737   6652   8773  -1050  -1668   1681  A    O  
ATOM   2228  CB  ALA A 309      47.514 -11.218  12.235  1.00 60.44      A    C  
ANISOU 2228  CB  ALA A 309     8345   6123   8498  -1055  -1429   1647  A    C  
ATOM   2229  N   LEU A 310      48.721  -8.330  12.292  1.00 57.91      A    N  
ANISOU 2229  N   LEU A 310     7910   6040   8052  -1062  -1368   1535  A    N  
ATOM   2230  CA  LEU A 310      49.789  -7.386  11.975  1.00 62.53      A    C  
ANISOU 2230  CA  LEU A 310     8394   6706   8659  -1034  -1405   1478  A    C  
ATOM   2231  C   LEU A 310      50.282  -6.679  13.236  1.00 65.94      A    C  
ANISOU 2231  C   LEU A 310     8947   7164   8942  -1129  -1482   1528  A    C  
ATOM   2232  O   LEU A 310      51.450  -6.298  13.335  1.00 57.44      A    O  
ANISOU 2232  O   LEU A 310     7805   6135   7886  -1125  -1594   1517  A    O  
ATOM   2233  CB  LEU A 310      49.327  -6.374  10.933  1.00 57.66      A    C  
ANISOU 2233  CB  LEU A 310     7690   6165   8053  -1017  -1239   1378  A    C  
ATOM   2234  CG  LEU A 310      49.293  -6.955   9.524  1.00 56.77      A    C  
ANISOU 2234  CG  LEU A 310     7420   6052   8097   -909  -1200   1311  A    C  
ATOM   2235  CD1 LEU A 310      48.814  -5.912   8.522  1.00 49.90      A    C  
ANISOU 2235  CD1 LEU A 310     6481   5260   7219   -894  -1041   1224  A    C  
ATOM   2236  CD2 LEU A 310      50.665  -7.472   9.153  1.00 50.94      A    C  
ANISOU 2236  CD2 LEU A 310     6552   5318   7483   -825  -1342   1300  A    C  
ATOM   2237  N   ASN A 311      49.386  -6.535  14.207  1.00 63.32      A    N  
ANISOU 2237  N   ASN A 311     8789   6812   8457  -1221  -1422   1579  A    N  
ATOM   2238  CA  ASN A 311      49.695  -5.826  15.438  1.00 69.30      A    C  
ANISOU 2238  CA  ASN A 311     9691   7595   9047  -1319  -1477   1616  A    C  
ATOM   2239  C   ASN A 311      50.409  -6.711  16.465  1.00 74.30      A    C  
ANISOU 2239  C   ASN A 311    10407   8178   9648  -1338  -1679   1726  A    C  
ATOM   2240  O   ASN A 311      51.032  -6.214  17.404  1.00 77.48      A    O  
ANISOU 2240  O   ASN A 311    10896   8610   9932  -1407  -1780   1755  A    O  
ATOM   2241  CB  ASN A 311      48.409  -5.242  16.022  1.00 73.53      A    C  
ANISOU 2241  CB  ASN A 311    10376   8145   9417  -1397  -1311   1614  A    C  
ATOM   2242  CG  ASN A 311      48.660  -4.381  17.242  1.00 83.40      A    C  
ANISOU 2242  CG  ASN A 311    11791   9421  10475  -1496  -1345   1629  A    C  
ATOM   2243  ND2 ASN A 311      47.879  -4.609  18.295  1.00 86.79      A    N  
ANISOU 2243  ND2 ASN A 311    12391   9838  10746  -1570  -1304   1693  A    N  
ATOM   2244  OD1 ASN A 311      49.541  -3.517  17.240  1.00 78.47      A    O  
ANISOU 2244  OD1 ASN A 311    11146   8833   9837  -1517  -1405   1582  A    O  
ATOM   2245  N   HIS A 312      50.319  -8.022  16.263  1.00 74.43      A    N  
ANISOU 2245  N   HIS A 312    10405   8110   9766  -1275  -1744   1785  A    N  
ATOM   2246  CA  HIS A 312      50.918  -9.015  17.153  1.00 71.11      A    C  
ANISOU 2246  CA  HIS A 312    10077   7617   9327  -1269  -1940   1902  A    C  
ATOM   2247  C   HIS A 312      52.411  -8.782  17.407  1.00 71.99      A    C  
ANISOU 2247  C   HIS A 312    10105   7781   9466  -1228  -2136   1905  A    C  
ATOM   2248  O   HIS A 312      53.152  -8.361  16.513  1.00 65.39      A    O  
ANISOU 2248  O   HIS A 312     9079   7014   8750  -1160  -2143   1819  A    O  
ATOM   2249  CB  HIS A 312      50.696 -10.421  16.591  1.00 67.83      A    C  
ANISOU 2249  CB  HIS A 312     9632   7083   9056  -1181  -1977   1940  A    C  
ATOM   2250  CG  HIS A 312      51.067 -11.516  17.540  1.00 77.81      A    C  
ANISOU 2250  CG  HIS A 312    11039   8240  10287  -1176  -2162   2077  A    C  
ATOM   2251  CD2 HIS A 312      50.302 -12.307  18.332  1.00 79.19      A    C  
ANISOU 2251  CD2 HIS A 312    11410   8312  10365  -1256  -2164   2191  A    C  
ATOM   2252  ND1 HIS A 312      52.371 -11.909  17.751  1.00 79.10      A    N  
ANISOU 2252  ND1 HIS A 312    11147   8392  10513  -1077  -2380   2114  A    N  
ATOM   2253  CE1 HIS A 312      52.395 -12.892  18.632  1.00 86.52      A    C  
ANISOU 2253  CE1 HIS A 312    12258   9218  11399  -1084  -2517   2248  A    C  
ATOM   2254  NE2 HIS A 312      51.152 -13.154  18.998  1.00 86.82      A    N  
ANISOU 2254  NE2 HIS A 312    12458   9193  11336  -1201  -2386   2300  A    N  
ATOM   2255  N   ASP A 313      52.845  -9.076  18.631  1.00 78.63      A    N  
ANISOU 2255  N   ASP A 313    11087   8602  10189  -1275  -2298   2009  A    N  
ATOM   2256  CA  ASP A 313      54.212  -8.784  19.064  1.00 85.29      A    C  
ANISOU 2256  CA  ASP A 313    11862   9519  11025  -1259  -2497   2020  A    C  
ATOM   2257  C   ASP A 313      55.282  -9.440  18.188  1.00 86.28      A    C  
ANISOU 2257  C   ASP A 313    11764   9655  11364  -1095  -2625   1993  A    C  
ATOM   2258  O   ASP A 313      56.433  -9.005  18.168  1.00 87.40      A    O  
ANISOU 2258  O   ASP A 313    11765   9902  11539  -1074  -2747   1962  A    O  
ATOM   2259  CB  ASP A 313      54.409  -9.182  20.529  1.00 96.89      A    C  
ANISOU 2259  CB  ASP A 313    13533  10954  12325  -1325  -2664   2151  A    C  
ATOM   2260  CG  ASP A 313      53.780  -8.191  21.494  1.00102.18      A    C  
ANISOU 2260  CG  ASP A 313    14394  11670  12759  -1492  -2570   2149  A    C  
ATOM   2261  OD1 ASP A 313      53.650  -6.997  21.133  1.00 97.84      A    O  
ANISOU 2261  OD1 ASP A 313    13794  11198  12180  -1549  -2440   2039  A    O  
ATOM   2262  OD2 ASP A 313      53.424  -8.611  22.618  1.00106.72      A    O1-
ANISOU 2262  OD2 ASP A 313    15179  12198  13170  -1562  -2626   2258  A    O1-
ATOM   2263  N   PHE A 314      54.897 -10.489  17.473  1.00 84.22      A    N  
ANISOU 2263  N   PHE A 314    11469   9289  11240   -984  -2593   2001  A    N  
ATOM   2264  CA  PHE A 314      55.788 -11.157  16.532  1.00 78.85      A    C  
ANISOU 2264  CA  PHE A 314    10583   8610  10765   -807  -2683   1958  A    C  
ATOM   2265  C   PHE A 314      56.405 -10.169  15.517  1.00 73.52      A    C  
ANISOU 2265  C   PHE A 314     9670   8087  10179   -789  -2603   1824  A    C  
ATOM   2266  O   PHE A 314      57.534 -10.353  15.078  1.00 75.26      A    O  
ANISOU 2266  O   PHE A 314     9696   8381  10518   -676  -2717   1791  A    O  
ATOM   2267  CB  PHE A 314      55.011 -12.281  15.833  1.00 73.85      A    C  
ANISOU 2267  CB  PHE A 314     9984   7828  10246   -720  -2611   1961  A    C  
ATOM   2268  CG  PHE A 314      55.767 -12.977  14.728  1.00 73.95      A    C  
ANISOU 2268  CG  PHE A 314     9798   7830  10468   -526  -2668   1893  A    C  
ATOM   2269  CD1 PHE A 314      56.790 -13.867  15.017  1.00 78.51      A    C  
ANISOU 2269  CD1 PHE A 314    10341   8365  11125   -375  -2886   1950  A    C  
ATOM   2270  CD2 PHE A 314      55.414 -12.774  13.398  1.00 73.09      A    C  
ANISOU 2270  CD2 PHE A 314     9548   7753  10471   -482  -2501   1770  A    C  
ATOM   2271  CE1 PHE A 314      57.463 -14.521  14.004  1.00 81.31      A    C  
ANISOU 2271  CE1 PHE A 314    10515   8712  11668   -179  -2927   1876  A    C  
ATOM   2272  CE2 PHE A 314      56.081 -13.423  12.380  1.00 75.64      A    C  
ANISOU 2272  CE2 PHE A 314     9698   8070  10972   -301  -2540   1698  A    C  
ATOM   2273  CZ  PHE A 314      57.109 -14.299  12.683  1.00 82.51      A    C  
ANISOU 2273  CZ  PHE A 314    10529   8899  11922   -146  -2749   1746  A    C  
ATOM   2274  N   PHE A 315      55.670  -9.123  15.150  1.00 61.58      A    N  
ANISOU 2274  N   PHE A 315     8173   6623   8602   -898  -2408   1752  A    N  
ATOM   2275  CA  PHE A 315      56.182  -8.144  14.191  1.00 71.62      A    C  
ANISOU 2275  CA  PHE A 315     9251   8022   9939   -901  -2321   1637  A    C  
ATOM   2276  C   PHE A 315      56.807  -6.935  14.888  1.00 78.79      A    C  
ANISOU 2276  C   PHE A 315    10173   9041  10723  -1038  -2371   1629  A    C  
ATOM   2277  O   PHE A 315      57.312  -6.018  14.233  1.00 78.93      A    O  
ANISOU 2277  O   PHE A 315    10053   9164  10774  -1076  -2312   1545  A    O  
ATOM   2278  CB  PHE A 315      55.070  -7.682  13.231  1.00 68.67      A    C  
ANISOU 2278  CB  PHE A 315     8879   7632   9580   -921  -2085   1558  A    C  
ATOM   2279  CG  PHE A 315      54.392  -8.807  12.520  1.00 65.38      A    C  
ANISOU 2279  CG  PHE A 315     8454   7112   9275   -812  -2032   1555  A    C  
ATOM   2280  CD1 PHE A 315      53.149  -9.256  12.935  1.00 65.59      A    C  
ANISOU 2280  CD1 PHE A 315     8657   7035   9230   -864  -1956   1608  A    C  
ATOM   2281  CD2 PHE A 315      55.011  -9.445  11.458  1.00 66.77      A    C  
ANISOU 2281  CD2 PHE A 315     8446   7299   9623   -664  -2061   1497  A    C  
ATOM   2282  CE1 PHE A 315      52.522 -10.314  12.288  1.00 63.64      A    C  
ANISOU 2282  CE1 PHE A 315     8409   6688   9084   -787  -1916   1603  A    C  
ATOM   2283  CE2 PHE A 315      54.401 -10.512  10.819  1.00 65.72      A    C  
ANISOU 2283  CE2 PHE A 315     8326   7058   9589   -570  -2023   1486  A    C  
ATOM   2284  CZ  PHE A 315      53.148 -10.942  11.229  1.00 56.26      A    C  
ANISOU 2284  CZ  PHE A 315     7310   5747   8320   -640  -1954   1539  A    C  
ATOM   2285  N   TRP A 316      56.782  -6.938  16.216  1.00 79.17      A    N  
ANISOU 2285  N   TRP A 316    10399   9062  10619  -1124  -2481   1715  A    N  
ATOM   2286  CA  TRP A 316      57.205  -5.762  16.965  1.00 79.52      A    C  
ANISOU 2286  CA  TRP A 316    10505   9194  10517  -1277  -2519   1700  A    C  
ATOM   2287  C   TRP A 316      58.208  -6.069  18.083  1.00 79.84      A    C  
ANISOU 2287  C   TRP A 316    10567   9278  10489  -1297  -2771   1781  A    C  
ATOM   2288  O   TRP A 316      58.393  -5.284  19.014  1.00 76.36      A    O  
ANISOU 2288  O   TRP A 316    10246   8883   9884  -1439  -2828   1791  A    O  
ATOM   2289  CB  TRP A 316      55.974  -5.011  17.472  1.00 71.79      A    C  
ANISOU 2289  CB  TRP A 316     9754   8160   9365  -1400  -2351   1691  A    C  
ATOM   2290  CG  TRP A 316      55.072  -4.586  16.333  1.00 74.45      A    C  
ANISOU 2290  CG  TRP A 316    10044   8477   9768  -1373  -2119   1606  A    C  
ATOM   2291  CD1 TRP A 316      53.875  -5.146  15.980  1.00 69.34      A    C  
ANISOU 2291  CD1 TRP A 316     9457   7747   9141  -1321  -1980   1616  A    C  
ATOM   2292  CD2 TRP A 316      55.314  -3.530  15.387  1.00 73.36      A    C  
ANISOU 2292  CD2 TRP A 316     9787   8408   9679  -1399  -2008   1504  A    C  
ATOM   2293  CE2 TRP A 316      54.217  -3.507  14.500  1.00 70.85      A    C  
ANISOU 2293  CE2 TRP A 316     9470   8045   9406  -1344  -1811   1459  A    C  
ATOM   2294  CE3 TRP A 316      56.346  -2.600  15.209  1.00 71.70      A    C  
ANISOU 2294  CE3 TRP A 316     9476   8295   9473  -1475  -2059   1451  A    C  
ATOM   2295  NE1 TRP A 316      53.355  -4.499  14.888  1.00 63.67      A    N  
ANISOU 2295  NE1 TRP A 316     8660   7051   8480  -1301  -1799   1525  A    N  
ATOM   2296  CZ2 TRP A 316      54.122  -2.584  13.448  1.00 68.60      A    C  
ANISOU 2296  CZ2 TRP A 316     9100   7800   9163  -1348  -1668   1369  A    C  
ATOM   2297  CZ3 TRP A 316      56.248  -1.681  14.163  1.00 66.89      A    C  
ANISOU 2297  CZ3 TRP A 316     8789   7718   8908  -1496  -1907   1363  A    C  
ATOM   2298  CH2 TRP A 316      55.146  -1.682  13.299  1.00 68.33      A    C  
ANISOU 2298  CH2 TRP A 316     8988   7846   9129  -1425  -1716   1326  A    C  
ATOM   2299  N   SER A 317      58.863  -7.216  17.965  1.00 82.45      A    N  
ANISOU 2299  N   SER A 317    10785   9596  10945  -1145  -2929   1835  A    N  
ATOM   2300  CA  SER A 317      59.944  -7.577  18.866  1.00 86.12      A    C  
ANISOU 2300  CA  SER A 317    11225  10121  11374  -1125  -3189   1911  A    C  
ATOM   2301  C   SER A 317      61.165  -7.991  18.050  1.00 89.66      A    C  
ANISOU 2301  C   SER A 317    11370  10677  12020   -972  -3302   1869  A    C  
ATOM   2302  O   SER A 317      61.059  -8.245  16.844  1.00 82.98      A    O  
ANISOU 2302  O   SER A 317    10372   9824  11334   -864  -3179   1797  A    O  
ATOM   2303  CB  SER A 317      59.511  -8.695  19.816  1.00 88.36      A    C  
ANISOU 2303  CB  SER A 317    11720  10269  11583  -1073  -3305   2048  A    C  
ATOM   2304  OG  SER A 317      59.121  -9.854  19.105  1.00 95.48      A    O  
ANISOU 2304  OG  SER A 317    12594  11048  12637   -910  -3266   2068  A    O  
ATOM   2305  N   ASP A 318      62.324  -8.032  18.704  1.00 98.73      A    N  
ANISOU 2305  N   ASP A 318    12423  11941  13150   -963  -3533   1909  A    N  
ATOM   2306  CA  ASP A 318      63.575  -8.394  18.039  1.00 99.74      A    C  
ANISOU 2306  CA  ASP A 318    12237  12205  13453   -814  -3655   1870  A    C  
ATOM   2307  C   ASP A 318      63.652  -9.898  17.825  1.00 93.36      A    C  
ANISOU 2307  C   ASP A 318    11406  11285  12780   -564  -3753   1931  A    C  
ATOM   2308  O   ASP A 318      63.145 -10.667  18.640  1.00 91.48      A    O  
ANISOU 2308  O   ASP A 318    11398  10895  12464   -531  -3839   2043  A    O  
ATOM   2309  CB  ASP A 318      64.774  -7.928  18.864  1.00103.63      A    C  
ANISOU 2309  CB  ASP A 318    12625  12876  13874   -893  -3883   1893  A    C  
ATOM   2310  CG  ASP A 318      64.727  -6.444  19.167  1.00115.08      A    C  
ANISOU 2310  CG  ASP A 318    14133  14416  15178  -1157  -3804   1832  A    C  
ATOM   2311  OD1 ASP A 318      64.244  -5.666  18.311  1.00117.77      A    O  
ANISOU 2311  OD1 ASP A 318    14449  14752  15547  -1239  -3578   1738  A    O  
ATOM   2312  OD2 ASP A 318      65.176  -6.053  20.264  1.00121.85      A    O1-
ANISOU 2312  OD2 ASP A 318    15072  15340  15884  -1280  -3973   1877  A    O1-
ATOM   2313  N   PRO A 319      64.279 -10.321  16.716  1.00 87.67      A    N  
ANISOU 2313  N   PRO A 319    10422  10633  12258   -389  -3736   1855  A    N  
ATOM   2314  CA  PRO A 319      64.821  -9.421  15.694  1.00 83.99      A    C  
ANISOU 2314  CA  PRO A 319     9691  10346  11874   -442  -3611   1726  A    C  
ATOM   2315  C   PRO A 319      63.681  -8.851  14.870  1.00 86.75      A    C  
ANISOU 2315  C   PRO A 319    10136  10612  12214   -537  -3330   1653  A    C  
ATOM   2316  O   PRO A 319      62.846  -9.620  14.394  1.00 84.94      A    O  
ANISOU 2316  O   PRO A 319    10005  10225  12045   -430  -3232   1656  A    O  
ATOM   2317  CB  PRO A 319      65.642 -10.368  14.815  1.00 85.74      A    C  
ANISOU 2317  CB  PRO A 319     9650  10626  12303   -180  -3673   1683  A    C  
ATOM   2318  CG  PRO A 319      64.945 -11.691  14.962  1.00 86.00      A    C  
ANISOU 2318  CG  PRO A 319     9880  10423  12375     -8  -3710   1757  A    C  
ATOM   2319  CD  PRO A 319      64.591 -11.731  16.417  1.00 87.40      A    C  
ANISOU 2319  CD  PRO A 319    10329  10506  12372   -120  -3849   1891  A    C  
ATOM   2320  N   MET A 320      63.641  -7.535  14.706  1.00 83.51      A    N  
ANISOU 2320  N   MET A 320     9705  10299  11725   -735  -3210   1590  A    N  
ATOM   2321  CA  MET A 320      62.591  -6.913  13.913  1.00 79.57      A    C  
ANISOU 2321  CA  MET A 320     9292   9730  11210   -815  -2952   1522  A    C  
ATOM   2322  C   MET A 320      62.640  -7.415  12.474  1.00 84.71      A    C  
ANISOU 2322  C   MET A 320     9749  10396  12039   -652  -2831   1440  A    C  
ATOM   2323  O   MET A 320      63.695  -7.858  12.013  1.00 82.49      A    O  
ANISOU 2323  O   MET A 320     9221  10236  11885   -521  -2923   1409  A    O  
ATOM   2324  CB  MET A 320      62.723  -5.393  13.958  1.00 72.31      A    C  
ANISOU 2324  CB  MET A 320     8377   8913  10185  -1041  -2867   1468  A    C  
ATOM   2325  CG  MET A 320      62.379  -4.814  15.304  1.00 76.69      A    C  
ANISOU 2325  CG  MET A 320     9179   9419  10540  -1211  -2936   1528  A    C  
ATOM   2326  SD  MET A 320      60.613  -4.815  15.623  1.00 88.69      A    S  
ANISOU 2326  SD  MET A 320    11029  10732  11937  -1249  -2756   1559  A    S  
ATOM   2327  CE  MET A 320      60.061  -3.611  14.413  1.00 54.04      A    C  
ANISOU 2327  CE  MET A 320     6603   6362   7568  -1333  -2489   1443  A    C  
ATOM   2328  N   PRO A 321      61.493  -7.354  11.762  1.00 86.85      A    N  
ANISOU 2328  N   PRO A 321    10128  10556  12314   -655  -2626   1401  A    N  
ATOM   2329  CA  PRO A 321      61.384  -7.838  10.375  1.00 82.71      A    C  
ANISOU 2329  CA  PRO A 321     9456  10033  11938   -510  -2500   1319  A    C  
ATOM   2330  C   PRO A 321      62.444  -7.215   9.465  1.00 79.71      A    C  
ANISOU 2330  C   PRO A 321     8793   9856  11637   -514  -2461   1230  A    C  
ATOM   2331  O   PRO A 321      62.695  -6.013   9.556  1.00 76.43      A    O  
ANISOU 2331  O   PRO A 321     8359   9541  11140   -694  -2413   1210  A    O  
ATOM   2332  CB  PRO A 321      59.991  -7.370   9.944  1.00 67.57      A    C  
ANISOU 2332  CB  PRO A 321     7710   8008   9954   -593  -2286   1293  A    C  
ATOM   2333  CG  PRO A 321      59.237  -7.168  11.212  1.00 68.49      A    C  
ANISOU 2333  CG  PRO A 321     8087   8021   9914   -715  -2322   1380  A    C  
ATOM   2334  CD  PRO A 321      60.227  -6.774  12.253  1.00 76.30      A    C  
ANISOU 2334  CD  PRO A 321     9056   9103  10830   -799  -2502   1428  A    C  
ATOM   2335  N   SER A 322      63.047  -8.016   8.594  1.00 78.51      A    N  
ANISOU 2335  N   SER A 322     8434   9760  11636   -322  -2473   1175  A    N  
ATOM   2336  CA  SER A 322      64.084  -7.507   7.705  1.00 84.36      A    C  
ANISOU 2336  CA  SER A 322     8886  10715  12450   -321  -2427   1091  A    C  
ATOM   2337  C   SER A 322      63.822  -7.880   6.250  1.00 86.93      A    C  
ANISOU 2337  C   SER A 322     9106  11044  12880   -189  -2258    995  A    C  
ATOM   2338  O   SER A 322      63.109  -8.841   5.971  1.00 89.53      A    O  
ANISOU 2338  O   SER A 322     9540  11218  13261    -46  -2235    990  A    O  
ATOM   2339  CB  SER A 322      65.475  -7.996   8.147  1.00 83.40      A    C  
ANISOU 2339  CB  SER A 322     8539  10745  12403   -215  -2637   1108  A    C  
ATOM   2340  OG  SER A 322      65.627  -9.399   7.979  1.00 78.69      A    O  
ANISOU 2340  OG  SER A 322     7900  10070  11929     51  -2729   1109  A    O  
ATOM   2341  N   ASP A 323      64.419  -7.121   5.335  1.00 87.02      A    N  
ANISOU 2341  N   ASP A 323     8915  11235  12914   -249  -2144    919  A    N  
ATOM   2342  CA  ASP A 323      64.235  -7.325   3.903  1.00 93.05      A    C  
ANISOU 2342  CA  ASP A 323     9572  12031  13751   -146  -1972    822  A    C  
ATOM   2343  C   ASP A 323      64.788  -8.644   3.366  1.00 96.75      A    C  
ANISOU 2343  C   ASP A 323     9877  12518  14367    127  -2034    767  A    C  
ATOM   2344  O   ASP A 323      65.625  -9.287   3.996  1.00101.45      A    O  
ANISOU 2344  O   ASP A 323    10366  13157  15023    244  -2215    796  A    O  
ATOM   2345  CB  ASP A 323      64.818  -6.150   3.121  1.00 99.27      A    C  
ANISOU 2345  CB  ASP A 323    10190  13017  14510   -296  -1840    767  A    C  
ATOM   2346  CG  ASP A 323      63.936  -4.923   3.188  1.00118.78      A    C  
ANISOU 2346  CG  ASP A 323    12870  15415  16846   -520  -1711    794  A    C  
ATOM   2347  OD1 ASP A 323      62.690  -5.087   3.209  1.00123.52      A    O  
ANISOU 2347  OD1 ASP A 323    13697  15833  17402   -504  -1643    811  A    O  
ATOM   2348  OD2 ASP A 323      64.485  -3.800   3.220  1.00125.60      A    O1-
ANISOU 2348  OD2 ASP A 323    13673  16403  17648   -711  -1681    796  A    O1-
ATOM   2349  N   LEU A 324      64.308  -9.029   2.186  1.00 97.12      A    N  
ANISOU 2349  N   LEU A 324     9910  12528  14463    234  -1886    682  A    N  
ATOM   2350  CA  LEU A 324      64.664 -10.298   1.568  1.00 97.32      A    C  
ANISOU 2350  CA  LEU A 324     9822  12534  14619    502  -1920    611  A    C  
ATOM   2351  C   LEU A 324      65.728 -10.124   0.480  1.00108.78      A    C  
ANISOU 2351  C   LEU A 324    10961  14234  16138    580  -1832    504  A    C  
ATOM   2352  O   LEU A 324      65.711  -9.144  -0.272  1.00101.38      A    O  
ANISOU 2352  O   LEU A 324     9954  13422  15142    434  -1668    464  A    O  
ATOM   2353  CB  LEU A 324      63.415 -10.962   0.985  1.00 87.74      A    C  
ANISOU 2353  CB  LEU A 324     8812  11112  13412    574  -1823    577  A    C  
ATOM   2354  CG  LEU A 324      62.541 -11.815   1.912  1.00 82.83      A    C  
ANISOU 2354  CG  LEU A 324     8456  10234  12782    608  -1938    661  A    C  
ATOM   2355  CD1 LEU A 324      62.327 -11.153   3.253  1.00 79.66      A    C  
ANISOU 2355  CD1 LEU A 324     8197   9797  12272    421  -2030    785  A    C  
ATOM   2356  CD2 LEU A 324      61.203 -12.133   1.249  1.00 79.22      A    C  
ANISOU 2356  CD2 LEU A 324     8183   9612  12306    601  -1807    624  A    C  
ATOM   2357  N   LYS A 325      66.650 -11.086   0.411  1.00121.66      A    N  
ANISOU 2357  N   LYS A 325    12406  15932  17886    815  -1942    459  A    N  
ATOM   2358  CA  LYS A 325      67.731 -11.078  -0.578  1.00128.29      A    C  
ANISOU 2358  CA  LYS A 325    12922  17024  18797    926  -1865    350  A    C  
ATOM   2359  C   LYS A 325      68.316 -12.473  -0.840  1.00126.93      A    C  
ANISOU 2359  C   LYS A 325    12630  16833  18763   1263  -1958    277  A    C  
ATOM   2360  O   LYS A 325      68.359 -13.331   0.045  1.00120.23      A    O  
ANISOU 2360  O   LYS A 325    11879  15837  17965   1402  -2149    338  A    O  
ATOM   2361  CB  LYS A 325      68.841 -10.108  -0.161  1.00132.55      A    C  
ANISOU 2361  CB  LYS A 325    13224  17831  19309    765  -1911    383  A    C  
ATOM   2362  CG  LYS A 325      68.525  -8.654  -0.472  1.00135.97      A    C  
ANISOU 2362  CG  LYS A 325    13697  18345  19620    458  -1749    400  A    C  
ATOM   2363  CD  LYS A 325      69.614  -7.712   0.011  1.00138.05      A    C  
ANISOU 2363  CD  LYS A 325    13746  18853  19852    271  -1809    435  A    C  
ATOM   2364  CE  LYS A 325      69.196  -6.257  -0.176  1.00135.54      A    C  
ANISOU 2364  CE  LYS A 325    13538  18558  19405    -47  -1664    465  A    C  
ATOM   2365  NZ  LYS A 325      70.263  -5.302   0.243  1.00136.46      A    N1+
ANISOU 2365  NZ  LYS A 325    13455  18907  19485   -262  -1717    493  A    N1+
TER   
CONECT 1275 1285
CONECT 1285 1275 1286
CONECT 1286 1285 1287 1289
CONECT 1287 1286 1288 1296
CONECT 1288 1287
CONECT 1289 1286 1290 1291
CONECT 1290 1289
CONECT 1291 1289 1292
CONECT 1292 1291 1293 1294 1295
CONECT 1293 1292
CONECT 1294 1292
CONECT 1295 1292
CONECT 1296 1287
END


A second structure was input as follows:


CRYST1  172.800  172.800   98.880  90.00  90.00 120.00 H 3           9
ATOM      1  N   SER A   7      38.394  -6.576 -41.180  1.00125.82      A    N  
ANISOU    1  N   SER A   7    17143  19120  11540   1440  -2133  -1310  A    N  
ATOM      2  CA  SER A   7      39.010  -6.387 -39.812  1.00135.15      A    C  
ANISOU    2  CA  SER A   7    18172  20127  13051   1425  -1913  -1243  A    C  
ATOM      3  C   SER A   7      38.676  -4.996 -39.225  1.00128.71      A    C  
ANISOU    3  C   SER A   7    17172  19324  12407   1468  -1873   -978  A    C  
ATOM      4  O   SER A   7      38.372  -4.056 -39.983  1.00117.81      A    O  
ANISOU    4  O   SER A   7    15822  18079  10860   1553  -1935   -817  A    O  
ATOM      5  CB  SER A   7      40.528  -6.593 -39.841  1.00138.24      A    C  
ANISOU    5  CB  SER A   7    18692  20458  13373   1506  -1628  -1277  A    C  
ATOM      6  OG  SER A   7      41.147  -5.449 -40.416  1.00142.21      A    O  
ANISOU    6  OG  SER A   7    19245  21070  13716   1621  -1484  -1073  A    O  
ATOM      7  N   VAL A   8      38.750  -4.871 -37.891  1.00115.00      A    N  
ANISOU    7  N   VAL A   8    15266  17439  10989   1415  -1768   -935  A    N  
ATOM      8  CA  VAL A   8      38.016  -3.804 -37.186  1.00109.96      A    C  
ANISOU    8  CA  VAL A   8    14436  16789  10553   1427  -1797   -743  A    C  
ATOM      9  C   VAL A   8      38.792  -2.965 -36.141  1.00108.07      A    C  
ANISOU    9  C   VAL A   8    14126  16418  10518   1452  -1556   -596  A    C  
ATOM     10  O   VAL A   8      39.659  -3.462 -35.432  1.00 95.73      A    O  
ANISOU   10  O   VAL A   8    12568  14734   9069   1405  -1396   -670  A    O  
ATOM     11  CB  VAL A   8      36.696  -4.358 -36.569  1.00106.89      A    C  
ANISOU   11  CB  VAL A   8    13862  16388  10361   1314  -2005   -822  A    C  
ATOM     12  CG1 VAL A   8      36.989  -5.416 -35.497  1.00 96.17      A    C  
ANISOU   12  CG1 VAL A   8    12457  14862   9220   1189  -1930   -981  A    C  
ATOM     13  CG2 VAL A   8      35.819  -3.220 -36.041  1.00101.76      A    C  
ANISOU   13  CG2 VAL A   8    13020  15764   9879   1366  -2047   -622  A    C  
ATOM     14  N   GLU A   9      38.441  -1.679 -36.077  1.00113.76      A    N  
ANISOU   14  N   GLU A   9    14787  17159  11275   1529  -1545   -385  A    N  
ATOM     15  CA  GLU A   9      38.931  -0.708 -35.085  1.00107.24      A    C  
ANISOU   15  CA  GLU A   9    13899  16201  10644   1544  -1357   -232  A    C  
ATOM     16  C   GLU A   9      39.120  -1.313 -33.721  1.00 94.03      A    C  
ANISOU   16  C   GLU A   9    12114  14377   9236   1437  -1272   -332  A    C  
ATOM     17  O   GLU A   9      38.218  -1.939 -33.201  1.00 99.20      A    O  
ANISOU   17  O   GLU A   9    12645  15015  10029   1369  -1398   -427  A    O  
ATOM     18  CB  GLU A   9      37.906   0.434 -34.943  1.00128.06      A    C  
ANISOU   18  CB  GLU A   9    16437  18854  13363   1623  -1445    -52  A    C  
ATOM     19  CG  GLU A   9      37.750   1.349 -36.152  1.00138.17      A    C  
ANISOU   19  CG  GLU A   9    17831  20259  14406   1750  -1509    112  A    C  
ATOM     20  CD  GLU A   9      39.037   2.089 -36.453  1.00140.76      A    C  
ANISOU   20  CD  GLU A   9    18320  20543  14619   1783  -1293    239  A    C  
ATOM     21  OE1 GLU A   9      39.997   2.000 -35.633  1.00130.14      A    O  
ANISOU   21  OE1 GLU A   9    16970  19072  13405   1710  -1100    211  A    O  
ATOM     22  OE2 GLU A   9      39.078   2.760 -37.512  1.00145.69      A    O1-
ANISOU   22  OE2 GLU A   9    19070  21268  15017   1875  -1322    376  A    O1-
ATOM     23  N   CYS A  10      40.271  -1.113 -33.118  1.00 91.01      A    N  
ANISOU   23  N   CYS A  10    11765  13889   8924   1414  -1064   -299  A    N  
ATOM     24  CA  CYS A  10      40.490  -1.732 -31.819  1.00 86.76      A    C  
ANISOU   24  CA  CYS A  10    11132  13213   8619   1314   -994   -390  A    C  
ATOM     25  C   CYS A  10      41.536  -1.039 -30.944  1.00 83.67      A    C  
ANISOU   25  C   CYS A  10    10739  12704   8345   1291   -785   -285  A    C  
ATOM     26  O   CYS A  10      42.496  -1.666 -30.505  1.00 91.69      A    O  
ANISOU   26  O   CYS A  10    11767  13664   9404   1239   -676   -358  A    O  
ATOM     27  CB  CYS A  10      40.839  -3.205 -31.981  1.00 92.50      A    C  
ANISOU   27  CB  CYS A  10    11905  13936   9302   1257  -1024   -597  A    C  
ATOM     28  SG  CYS A  10      40.605  -4.068 -30.429  1.00107.68      A    S  
ANISOU   28  SG  CYS A  10    13699  15699  11514   1128  -1015   -703  A    S  
ATOM     29  N   PRO A  11      41.318   0.249 -30.661  1.00 75.82      A    N  
ANISOU   29  N   PRO A  11     9732  11668   7408   1329   -741   -114  A    N  
ATOM     30  CA  PRO A  11      42.223   1.167 -29.979  1.00 64.02      A    C  
ANISOU   30  CA  PRO A  11     8264  10064   5995   1299   -564     11  A    C  
ATOM     31  C   PRO A  11      42.768   0.657 -28.661  1.00 77.75      A    C  
ANISOU   31  C   PRO A  11     9933  11682   7926   1190   -474    -64  A    C  
ATOM     32  O   PRO A  11      43.877   1.035 -28.294  1.00 88.42      A    O  
ANISOU   32  O   PRO A  11    11316  12979   9297   1142   -331      0  A    O  
ATOM     33  CB  PRO A  11      41.319   2.380 -29.675  1.00 65.56      A    C  
ANISOU   33  CB  PRO A  11     8436  10200   6272   1359   -598    152  A    C  
ATOM     34  CG  PRO A  11      40.256   2.326 -30.701  1.00 79.26      A    C  
ANISOU   34  CG  PRO A  11    10164  12070   7880   1458   -774    157  A    C  
ATOM     35  CD  PRO A  11      40.016   0.872 -30.964  1.00 88.83      A    C  
ANISOU   35  CD  PRO A  11    11330  13367   9055   1405   -885    -37  A    C  
ATOM     36  N   PHE A  12      41.980  -0.150 -27.941  1.00 83.31      A    N  
ANISOU   36  N   PHE A  12    10538  12348   8768   1143   -562   -183  A    N  
ATOM     37  CA  PHE A  12      42.318  -0.422 -26.542  1.00 72.29      A    C  
ANISOU   37  CA  PHE A  12     9080  10824   7563   1044   -483   -221  A    C  
ATOM     38  C   PHE A  12      42.659  -1.874 -26.304  1.00 73.19      A    C  
ANISOU   38  C   PHE A  12     9170  10930   7707    981   -505   -381  A    C  
ATOM     39  O   PHE A  12      42.648  -2.344 -25.158  1.00 77.53      A    O  
ANISOU   39  O   PHE A  12     9659  11384   8414    898   -483   -431  A    O  
ATOM     40  CB  PHE A  12      41.188   0.013 -25.612  1.00 65.36      A    C  
ANISOU   40  CB  PHE A  12     8111   9875   6846   1033   -523   -196  A    C  
ATOM     41  CG  PHE A  12      40.797   1.448 -25.778  1.00 66.86      A    C  
ANISOU   41  CG  PHE A  12     8338  10044   7022   1119   -498    -41  A    C  
ATOM     42  CD1 PHE A  12      41.748   2.438 -25.744  1.00 57.80      A    C  
ANISOU   42  CD1 PHE A  12     7293   8827   5839   1114   -372     77  A    C  
ATOM     43  CD2 PHE A  12      39.471   1.801 -25.996  1.00 76.76      A    C  
ANISOU   43  CD2 PHE A  12     9520  11344   8299   1206   -606     -9  A    C  
ATOM     44  CE1 PHE A  12      41.394   3.768 -25.909  1.00 63.51      A    C  
ANISOU   44  CE1 PHE A  12     8080   9500   6549   1194   -348    223  A    C  
ATOM     45  CE2 PHE A  12      39.113   3.125 -26.142  1.00 63.24      A    C  
ANISOU   45  CE2 PHE A  12     7854   9595   6579   1312   -579    139  A    C  
ATOM     46  CZ  PHE A  12      40.072   4.107 -26.111  1.00 61.83      A    C  
ANISOU   46  CZ  PHE A  12     7810   9319   6361   1307   -450    254  A    C  
ATOM     47  N   CYS A  13      42.879  -2.611 -27.377  1.00 66.59      A    N  
ANISOU   47  N   CYS A  13     8396  10188   6715   1026   -555   -465  A    N  
ATOM     48  CA  CYS A  13      43.242  -4.010 -27.222  1.00 64.82      A    C  
ANISOU   48  CA  CYS A  13     8182   9934   6513    985   -572   -622  A    C  
ATOM     49  C   CYS A  13      44.344  -4.315 -28.212  1.00 70.36      A    C  
ANISOU   49  C   CYS A  13     8984  10714   7035   1058   -495   -649  A    C  
ATOM     50  O   CYS A  13      44.089  -4.533 -29.417  1.00 80.10      A    O  
ANISOU   50  O   CYS A  13    10300  12052   8083   1126   -566   -699  A    O  
ATOM     51  CB  CYS A  13      42.047  -4.925 -27.446  1.00 74.71      A    C  
ANISOU   51  CB  CYS A  13     9408  11201   7776    952   -747   -753  A    C  
ATOM     52  SG  CYS A  13      42.330  -6.609 -26.876  1.00 70.35      A    S  
ANISOU   52  SG  CYS A  13     8874  10539   7313    872   -770   -935  A    S  
ATOM     53  N   ASP A  14      45.575  -4.349 -27.708  1.00 66.67      A    N  
ANISOU   53  N   ASP A  14     8507  10209   6616   1046   -350   -615  A    N  
ATOM     54  CA  ASP A  14      46.758  -4.549 -28.544  1.00 62.83      A    C  
ANISOU   54  CA  ASP A  14     8086   9811   5975   1125   -237   -616  A    C  
ATOM     55  C   ASP A  14      46.949  -6.023 -28.874  1.00 65.57      A    C  
ANISOU   55  C   ASP A  14     8490  10145   6275   1170   -270   -802  A    C  
ATOM     56  O   ASP A  14      46.563  -6.913 -28.099  1.00 74.97      A    O  
ANISOU   56  O   ASP A  14     9656  11223   7607   1113   -341   -905  A    O  
ATOM     57  CB  ASP A  14      48.021  -4.033 -27.851  1.00 72.51      A    C  
ANISOU   57  CB  ASP A  14     9248  11018   7282   1091    -74   -500  A    C  
ATOM     58  CG  ASP A  14      48.103  -2.521 -27.774  1.00 85.61      A    C  
ANISOU   58  CG  ASP A  14    10896  12690   8941   1051    -15   -313  A    C  
ATOM     59  OD1 ASP A  14      47.096  -1.820 -28.042  1.00 82.73      A    O  
ANISOU   59  OD1 ASP A  14    10563  12322   8549   1059    -99   -264  A    O  
ATOM     60  OD2 ASP A  14      49.196  -2.051 -27.390  1.00 89.93      A    O1-
ANISOU   60  OD2 ASP A  14    11401  13241   9525   1007    111   -213  A    O1-
ATOM     61  N   GLU A  15      47.550  -6.285 -30.032  1.00 75.68      A    N  
ANISOU   61  N   GLU A  15     9867  11534   7351   1276   -211   -844  A    N  
ATOM     62  CA  GLU A  15      47.935  -7.653 -30.391  1.00 74.40      A    C  
ANISOU   62  CA  GLU A  15     9789  11348   7130   1346   -208  -1023  A    C  
ATOM     63  C   GLU A  15      49.129  -8.101 -29.548  1.00 68.84      A    C  
ANISOU   63  C   GLU A  15     9010  10583   6560   1364    -70  -1009  A    C  
ATOM     64  O   GLU A  15      50.077  -7.342 -29.361  1.00 63.97      A    O  
ANISOU   64  O   GLU A  15     8311  10033   5959   1371     70   -865  A    O  
ATOM     65  CB  GLU A  15      48.262  -7.719 -31.882  1.00 69.86      A    C  
ANISOU   65  CB  GLU A  15     9349  10917   6275   1469   -164  -1069  A    C  
ATOM     66  CG  GLU A  15      47.384  -6.794 -32.715  1.00 81.56      A    C  
ANISOU   66  CG  GLU A  15    10877  12505   7607   1459   -262   -990  A    C  
ATOM     67  CD  GLU A  15      47.478  -7.047 -34.203  1.00114.05      A    C  
ANISOU   67  CD  GLU A  15    15157  16756  11420   1568   -262  -1067  A    C  
ATOM     68  OE1 GLU A  15      47.995  -8.099 -34.636  1.00123.49      A    O  
ANISOU   68  OE1 GLU A  15    16455  17945  12518   1649   -215  -1227  A    O  
ATOM     69  OE2 GLU A  15      46.982  -6.184 -34.968  1.00134.24      A    O1-
ANISOU   69  OE2 GLU A  15    17758  19424  13824   1579   -316   -968  A    O1-
ATOM     70  N   VAL A  16      49.059  -9.328 -29.038  1.00 65.40      A    N  
ANISOU   70  N   VAL A  16     8603  10020   6225   1364   -122  -1151  A    N  
ATOM     71  CA  VAL A  16      50.074  -9.841 -28.102  1.00 63.80      A    C  
ANISOU   71  CA  VAL A  16     8322   9744   6174   1384    -22  -1133  A    C  
ATOM     72  C   VAL A  16      51.457  -9.969 -28.778  1.00 63.96      A    C  
ANISOU   72  C   VAL A  16     8344   9883   6074   1539    157  -1115  A    C  
ATOM     73  O   VAL A  16      52.493 -10.080 -28.123  1.00 67.20      A    O  
ANISOU   73  O   VAL A  16     8646  10293   6591   1569    264  -1046  A    O  
ATOM     74  CB  VAL A  16      49.624 -11.189 -27.481  1.00 63.66      A    C  
ANISOU   74  CB  VAL A  16     8364   9546   6278   1358   -127  -1286  A    C  
ATOM     75  CG1 VAL A  16      49.792 -12.318 -28.470  1.00 60.80      A    C  
ANISOU   75  CG1 VAL A  16     8169   9163   5766   1489   -129  -1470  A    C  
ATOM     76  CG2 VAL A  16      50.354 -11.471 -26.190  1.00 59.33      A    C  
ANISOU   76  CG2 VAL A  16     7710   8905   5927   1332    -70  -1220  A    C  
ATOM     77  N   SER A  17      51.466  -9.911 -30.107  1.00 62.51      A    N  
ANISOU   77  N   SER A  17     8272   9819   5659   1638    192  -1166  A    N  
ATOM     78  CA  SER A  17      52.719  -9.929 -30.870  1.00 63.46      A    C  
ANISOU   78  CA  SER A  17     8390  10084   5637   1791    386  -1139  A    C  
ATOM     79  C   SER A  17      53.632  -8.751 -30.527  1.00 63.45      A    C  
ANISOU   79  C   SER A  17     8215  10205   5688   1743    528   -914  A    C  
ATOM     80  O   SER A  17      54.795  -8.741 -30.899  1.00 61.09      A    O  
ANISOU   80  O   SER A  17     7853  10034   5323   1847    704   -859  A    O  
ATOM     81  CB  SER A  17      52.411  -9.927 -32.360  1.00 68.67      A    C  
ANISOU   81  CB  SER A  17     9218  10859   6012   1882    388  -1222  A    C  
ATOM     82  OG  SER A  17      51.749  -8.722 -32.707  1.00 72.87      A    O  
ANISOU   82  OG  SER A  17     9742  11474   6469   1786    329  -1094  A    O  
ATOM     83  N   LYS A  18      53.125  -7.743 -29.824  1.00 64.90      A    N  
ANISOU   83  N   LYS A  18     8321  10352   5986   1583    459   -782  A    N  
ATOM     84  CA  LYS A  18      53.972  -6.651 -29.346  1.00 63.84      A    C  
ANISOU   84  CA  LYS A  18     8036  10294   5922   1503    573   -576  A    C  
ATOM     85  C   LYS A  18      55.014  -7.188 -28.369  1.00 67.79      A    C  
ANISOU   85  C   LYS A  18     8393  10768   6593   1513    644   -553  A    C  
ATOM     86  O   LYS A  18      56.070  -6.560 -28.152  1.00 73.09      A    O  
ANISOU   86  O   LYS A  18     8924  11547   7299   1480    769   -401  A    O  
ATOM     87  CB  LYS A  18      53.138  -5.559 -28.649  1.00 59.58      A    C  
ANISOU   87  CB  LYS A  18     7474   9675   5488   1335    472   -467  A    C  
ATOM     88  CG  LYS A  18      52.543  -6.025 -27.325  1.00 67.36      A    C  
ANISOU   88  CG  LYS A  18     8420  10486   6687   1244    350   -525  A    C  
ATOM     89  CD  LYS A  18      51.527  -5.026 -26.791  1.00 72.37      A    C  
ANISOU   89  CD  LYS A  18     9059  11043   7395   1114    254   -449  A    C  
ATOM     90  CE  LYS A  18      52.185  -3.767 -26.246  1.00 70.40      A    C  
ANISOU   90  CE  LYS A  18     8728  10813   7205   1007    340   -263  A    C  
ATOM     91  NZ  LYS A  18      51.165  -3.005 -25.444  1.00 71.81      A    N1+
ANISOU   91  NZ  LYS A  18     8922  10869   7491    897    245   -221  A    N1+
ATOM     92  N   TYR A  19      54.685  -8.330 -27.762  1.00 63.43      A    N  
ANISOU   92  N   TYR A  19     7875  10072   6151   1546    553   -693  A    N  
ATOM     93  CA  TYR A  19      55.574  -9.022 -26.857  1.00 64.58      A    C  
ANISOU   93  CA  TYR A  19     7908  10177   6451   1583    595   -683  A    C  
ATOM     94  C   TYR A  19      56.236 -10.155 -27.605  1.00 69.91      A    C  
ANISOU   94  C   TYR A  19     8637  10892   7033   1801    690   -807  A    C  
ATOM     95  O   TYR A  19      55.648 -10.753 -28.487  1.00 81.52      A    O  
ANISOU   95  O   TYR A  19    10279  12330   8362   1890    655   -962  A    O  
ATOM     96  CB  TYR A  19      54.824  -9.531 -25.617  1.00 62.04      A    C  
ANISOU   96  CB  TYR A  19     7598   9656   6316   1479    442   -736  A    C  
ATOM     97  CG  TYR A  19      54.187  -8.416 -24.826  1.00 60.42      A    C  
ANISOU   97  CG  TYR A  19     7346   9409   6199   1283    369   -623  A    C  
ATOM     98  CD1 TYR A  19      54.952  -7.627 -23.983  1.00 61.86      A    C  
ANISOU   98  CD1 TYR A  19     7389   9634   6482   1181    419   -464  A    C  
ATOM     99  CD2 TYR A  19      52.833  -8.113 -24.957  1.00 65.47      A    C  
ANISOU   99  CD2 TYR A  19     8084   9976   6816   1206    250   -674  A    C  
ATOM    100  CE1 TYR A  19      54.390  -6.575 -23.277  1.00 62.34      A    C  
ANISOU  100  CE1 TYR A  19     7436   9639   6609   1011    363   -373  A    C  
ATOM    101  CE2 TYR A  19      52.255  -7.062 -24.245  1.00 66.41      A    C  
ANISOU  101  CE2 TYR A  19     8165  10054   7013   1056    202   -572  A    C  
ATOM    102  CZ  TYR A  19      53.037  -6.328 -23.375  1.00 60.80      A    C  
ANISOU  102  CZ  TYR A  19     7344   9359   6397    962    261   -431  A    C  
ATOM    103  OH  TYR A  19      52.481  -5.287 -22.677  1.00 66.18      A    O  
ANISOU  103  OH  TYR A  19     8019   9980   7143    823    222   -345  A    O  
ATOM    104  N   GLU A  20      57.481 -10.428 -27.257  1.00 77.71      A    N  
ANISOU  104  N   GLU A  20     9476  11955   8092   1889    810   -737  A    N  
ATOM    105  CA  GLU A  20      58.200 -11.512 -27.869  1.00 85.30      A    C  
ANISOU  105  CA  GLU A  20    10475  12949   8983   2126    920   -847  A    C  
ATOM    106  C   GLU A  20      58.358 -12.639 -26.874  1.00 79.74      A    C  
ANISOU  106  C   GLU A  20     9761  12074   8460   2186    850   -912  A    C  
ATOM    107  O   GLU A  20      58.961 -12.459 -25.816  1.00 76.52      A    O  
ANISOU  107  O   GLU A  20     9179  11674   8220   2122    844   -782  A    O  
ATOM    108  CB  GLU A  20      59.552 -10.990 -28.339  1.00 98.00      A    C  
ANISOU  108  CB  GLU A  20    11903  14802  10528   2215   1130   -704  A    C  
ATOM    109  CG  GLU A  20      60.321 -11.969 -29.195  1.00123.16      A    C  
ANISOU  109  CG  GLU A  20    15130  18064  13600   2493   1288   -813  A    C  
ATOM    110  CD  GLU A  20      61.519 -11.296 -29.836  1.00145.84      A    C  
ANISOU  110  CD  GLU A  20    17819  21216  16376   2563   1513   -661  A    C  
ATOM    111  OE1 GLU A  20      61.883 -10.180 -29.377  1.00142.67      A    O  
ANISOU  111  OE1 GLU A  20    17234  20923  16048   2379   1528   -459  A    O  
ATOM    112  OE2 GLU A  20      62.068 -11.866 -30.807  1.00153.21      A    O1-
ANISOU  112  OE2 GLU A  20    18803  22255  17153   2792   1678   -744  A    O1-
ATOM    113  N   LYS A  21      57.795 -13.798 -27.179  1.00 77.37      A    N  
ANISOU  113  N   LYS A  21     9661  11609   8124   2294    785  -1109  A    N  
ATOM    114  CA  LYS A  21      57.936 -14.945 -26.270  1.00 74.13      A    C  
ANISOU  114  CA  LYS A  21     9273  11010   7882   2360    720  -1169  A    C  
ATOM    115  C   LYS A  21      59.372 -15.412 -26.063  1.00 75.39      A    C  
ANISOU  115  C   LYS A  21     9276  11260   8108   2566    867  -1097  A    C  
ATOM    116  O   LYS A  21      60.175 -15.538 -26.983  1.00 74.11      A    O  
ANISOU  116  O   LYS A  21     9089  11247   7820   2765   1038  -1117  A    O  
ATOM    117  CB  LYS A  21      57.007 -16.084 -26.644  1.00 72.29      A    C  
ANISOU  117  CB  LYS A  21     9307  10558   7600   2410    613  -1394  A    C  
ATOM    118  CG  LYS A  21      55.562 -15.847 -26.250  1.00 73.85      A    C  
ANISOU  118  CG  LYS A  21     9598  10622   7840   2172    419  -1433  A    C  
ATOM    119  CD  LYS A  21      54.649 -16.821 -26.939  1.00 82.01      A    C  
ANISOU  119  CD  LYS A  21    10891  11491   8776   2201    320  -1656  A    C  
ATOM    120  CE  LYS A  21      53.186 -16.462 -26.688  1.00 84.24      A    C  
ANISOU  120  CE  LYS A  21    11225  11694   9085   1960    135  -1679  A    C  
ATOM    121  NZ  LYS A  21      52.258 -17.375 -27.410  1.00 92.99      A    N1+
ANISOU  121  NZ  LYS A  21    12577  12661  10093   1954     18  -1895  A    N1+
ATOM    122  N   LEU A  22      59.756 -15.554 -24.804  1.00 80.29      A    N  
ANISOU  122  N   LEU A  22     9758  11820   8926   2512    807   -987  A    N  
ATOM    123  CA  LEU A  22      61.087 -16.058 -24.452  1.00 83.43      A    C  
ANISOU  123  CA  LEU A  22     9982  12299   9416   2708    914   -902  A    C  
ATOM    124  C   LEU A  22      61.052 -17.519 -24.014  1.00 94.89      A    C  
ANISOU  124  C   LEU A  22    11575  13512  10965   2874    853  -1020  A    C  
ATOM    125  O   LEU A  22      61.830 -18.323 -24.513  1.00 98.36      A    O  
ANISOU  125  O   LEU A  22    12028  13968  11375   3151    977  -1080  A    O  
ATOM    126  CB  LEU A  22      61.724 -15.222 -23.348  1.00 76.77      A    C  
ANISOU  126  CB  LEU A  22     8872  11577   8719   2550    886   -678  A    C  
ATOM    127  CG  LEU A  22      61.955 -13.756 -23.669  1.00 70.51      A    C  
ANISOU  127  CG  LEU A  22     7925  11010   7853   2381    955   -534  A    C  
ATOM    128  CD1 LEU A  22      62.295 -12.981 -22.417  1.00 74.18      A    C  
ANISOU  128  CD1 LEU A  22     8196  11522   8467   2168    871   -347  A    C  
ATOM    129  CD2 LEU A  22      63.017 -13.631 -24.721  1.00 65.27      A    C  
ANISOU  129  CD2 LEU A  22     7138  10588   7073   2570   1170   -496  A    C  
ATOM    130  N   ALA A  23      60.142 -17.864 -23.096  1.00 94.03      A    N  
ANISOU  130  N   ALA A  23    11581  13177  10969   2711    673  -1050  A    N  
ATOM    131  CA  ALA A  23      60.132 -19.206 -22.525  1.00 82.68      A    C  
ANISOU  131  CA  ALA A  23    10275  11494   9643   2839    604  -1127  A    C  
ATOM    132  C   ALA A  23      58.846 -19.524 -21.765  1.00 84.32      A    C  
ANISOU  132  C   ALA A  23    10655  11453   9930   2617    411  -1185  A    C  
ATOM    133  O   ALA A  23      58.353 -18.679 -21.031  1.00105.75      A    O  
ANISOU  133  O   ALA A  23    13277  14205  12699   2374    325  -1079  A    O  
ATOM    134  CB  ALA A  23      61.325 -19.375 -21.610  1.00 79.90      A    C  
ANISOU  134  CB  ALA A  23     9698  11218   9441   2950    636   -954  A    C  
ATOM    135  N   LYS A  24      58.330 -20.741 -21.939  1.00 79.13      A    N  
ANISOU  135  N   LYS A  24    10248  10540   9277   2702    353  -1352  A    N  
ATOM    136  CA  LYS A  24      57.263 -21.242 -21.069  1.00 78.08      A    C  
ANISOU  136  CA  LYS A  24    10259  10158   9249   2506    179  -1384  A    C  
ATOM    137  C   LYS A  24      57.764 -21.310 -19.646  1.00 85.83      A    C  
ANISOU  137  C   LYS A  24    11099  11107  10404   2464    125  -1203  A    C  
ATOM    138  O   LYS A  24      58.921 -21.656 -19.423  1.00103.34      A    O  
ANISOU  138  O   LYS A  24    13204  13380  12679   2674    200  -1119  A    O  
ATOM    139  CB  LYS A  24      56.793 -22.634 -21.493  1.00 77.35      A    C  
ANISOU  139  CB  LYS A  24    10467   9780   9140   2614    132  -1585  A    C  
ATOM    140  CG  LYS A  24      55.587 -22.648 -22.397  1.00102.03      A    C  
ANISOU  140  CG  LYS A  24    13793  12839  12135   2480     61  -1769  A    C  
ATOM    141  CD  LYS A  24      54.997 -24.053 -22.547  1.00127.16      A    C  
ANISOU  141  CD  LYS A  24    17285  15695  15334   2511    -27  -1955  A    C  
ATOM    142  CE  LYS A  24      53.600 -23.998 -23.151  1.00134.74      A    C  
ANISOU  142  CE  LYS A  24    18406  16589  16197   2288   -153  -2106  A    C  
ATOM    143  NZ  LYS A  24      53.113 -25.316 -23.647  1.00149.03      A    N1+
ANISOU  143  NZ  LYS A  24    20543  18108  17972   2328   -226  -2323  A    N1+
ATOM    144  N   ILE A  25      56.922 -20.974 -18.680  1.00 90.97      A    N  
ANISOU  144  N   ILE A  25    11745  11685  11132   2203      0  -1137  A    N  
ATOM    145  CA  ILE A  25      57.286 -21.099 -17.282  1.00 99.13      A    C  
ANISOU  145  CA  ILE A  25    12685  12671  12309   2144    -67   -974  A    C  
ATOM    146  C   ILE A  25      56.131 -21.678 -16.458  1.00117.39      A    C  
ANISOU  146  C   ILE A  25    15169  14735  14697   1946   -208  -1005  A    C  
ATOM    147  O   ILE A  25      56.195 -21.616 -15.238  1.00123.87      A    O  
ANISOU  147  O   ILE A  25    15926  15526  15613   1838   -274   -866  A    O  
ATOM    148  CB  ILE A  25      57.742 -19.756 -16.671  1.00 92.71      A    C  
ANISOU  148  CB  ILE A  25    11614  12102  11507   2005    -52   -792  A    C  
ATOM    149  CG1 ILE A  25      56.591 -18.760 -16.620  1.00 88.50      A    C  
ANISOU  149  CG1 ILE A  25    11093  11604  10926   1734   -104   -807  A    C  
ATOM    150  CG2 ILE A  25      58.895 -19.175 -17.478  1.00103.89      A    C  
ANISOU  150  CG2 ILE A  25    12844  13773  12854   2173     91   -744  A    C  
ATOM    151  CD1 ILE A  25      56.988 -17.350 -16.231  1.00 81.72      A    C  
ANISOU  151  CD1 ILE A  25    10024  10968  10055   1600    -75   -657  A    C  
ATOM    152  N   GLY A  26      55.036 -22.117 -17.091  1.00125.10      A    N  
ANISOU  152  N   GLY A  26    16346  15561  15622   1867   -256  -1174  A    N  
ATOM    153  CA  GLY A  26      53.916 -22.722 -16.358  1.00134.95      A    C  
ANISOU  153  CA  GLY A  26    17746  16579  16946   1665   -382  -1201  A    C  
ATOM    154  C   GLY A  26      53.329 -23.923 -17.060  1.00151.08      A    C  
ANISOU  154  C   GLY A  26    20059  18375  18969   1713   -426  -1392  A    C  
ATOM    155  O   GLY A  26      52.218 -23.865 -17.529  1.00155.71      A    O  
ANISOU  155  O   GLY A  26    20738  18919  19506   1547   -489  -1505  A    O  
ATOM    156  N   GLN A  27      54.065 -25.021 -17.156  1.00165.23      A    N  
ANISOU  156  N   GLN A  27    21983  19997  20797   1943   -399  -1432  A    N  
ATOM    157  CA  GLN A  27      53.571 -26.180 -17.949  1.00160.27      A    C  
ANISOU  157  CA  GLN A  27    21650  19111  20131   2003   -435  -1641  A    C  
ATOM    158  C   GLN A  27      52.355 -26.837 -17.300  1.00148.11      A    C  
ANISOU  158  C   GLN A  27    20281  17318  18675   1740   -577  -1668  A    C  
ATOM    159  O   GLN A  27      51.359 -27.119 -17.963  1.00136.07      A    O  
ANISOU  159  O   GLN A  27    18912  15695  17093   1601   -647  -1827  A    O  
ATOM    160  CB  GLN A  27      54.661 -27.232 -18.209  1.00162.79      A    C  
ANISOU  160  CB  GLN A  27    22096  19281  20472   2338   -360  -1684  A    C  
ATOM    161  CG  GLN A  27      55.721 -26.835 -19.226  1.00164.75      A    C  
ANISOU  161  CG  GLN A  27    22237  19752  20608   2621   -201  -1724  A    C  
ATOM    162  CD  GLN A  27      56.828 -25.970 -18.625  1.00171.38      A    C  
ANISOU  162  CD  GLN A  27    22751  20867  21498   2710   -119  -1505  A    C  
ATOM    163  NE2 GLN A  27      57.039 -24.796 -19.219  1.00165.05      A    N  
ANISOU  163  NE2 GLN A  27    21752  20366  20592   2682    -36  -1477  A    N  
ATOM    164  OE1 GLN A  27      57.486 -26.347 -17.640  1.00167.13      A    O  
ANISOU  164  OE1 GLN A  27    22143  20272  21086   2794   -138  -1356  A    O  
ATOM    165  N   GLY A  28      52.436 -27.047 -15.992  1.00149.70      A    N  
ANISOU  165  N   GLY A  28    20442  17432  19005   1660   -623  -1501  A    N  
ATOM    166  CA  GLY A  28      51.406 -27.776 -15.269  1.00161.47      A    C  
ANISOU  166  CA  GLY A  28    22096  18672  20584   1423   -739  -1499  A    C  
ATOM    167  C   GLY A  28      50.621 -26.971 -14.261  1.00174.15      A    C  
ANISOU  167  C   GLY A  28    23540  20395  22234   1134   -786  -1357  A    C  
ATOM    168  O   GLY A  28      49.679 -27.503 -13.675  1.00157.54      A    O  
ANISOU  168  O   GLY A  28    21548  18113  20196    913   -870  -1348  A    O  
ATOM    169  N   THR A  29      50.975 -25.694 -14.074  1.00195.92      A    N  
ANISOU  169  N   THR A  29    26044  23444  24951   1127   -727  -1252  A    N  
ATOM    170  CA  THR A  29      50.219 -24.818 -13.159  1.00188.85      A    C  
ANISOU  170  CA  THR A  29    25002  22670  24080    869   -755  -1134  A    C  
ATOM    171  C   THR A  29      49.159 -24.009 -13.900  1.00187.16      A    C  
ANISOU  171  C   THR A  29    24721  22597  23792    708   -766  -1233  A    C  
ATOM    172  O   THR A  29      49.446 -22.992 -14.560  1.00165.39      A    O  
ANISOU  172  O   THR A  29    21823  20067  20949    775   -705  -1245  A    O  
ATOM    173  CB  THR A  29      51.128 -23.874 -12.361  1.00162.34      A    C  
ANISOU  173  CB  THR A  29    21430  19521  20727    920   -700   -954  A    C  
ATOM    174  CG2 THR A  29      52.199 -24.686 -11.567  1.00130.27      A    C  
ANISOU  174  CG2 THR A  29    17414  15339  16742   1086   -709   -833  A    C  
ATOM    175  OG1 THR A  29      51.713 -22.914 -13.262  1.00138.82      A    O  
ANISOU  175  OG1 THR A  29    18303  16782  17659   1043   -620   -986  A    O  
ATOM    176  N   PHE A  30      47.928 -24.509 -13.810  1.00198.71      A    N  
ANISOU  176  N   PHE A  30    26289  23920  25291    493   -848  -1296  A    N  
ATOM    177  CA  PHE A  30      46.790 -23.926 -14.490  1.00205.91      A    C  
ANISOU  177  CA  PHE A  30    27145  24944  26147    332   -884  -1388  A    C  
ATOM    178  C   PHE A  30      47.104 -23.801 -15.977  1.00199.19      A    C  
ANISOU  178  C   PHE A  30    26334  24173  25173    498   -866  -1544  A    C  
ATOM    179  O   PHE A  30      47.629 -24.745 -16.589  1.00205.23      A    O  
ANISOU  179  O   PHE A  30    27281  24781  25914    656   -869  -1656  A    O  
ATOM    180  CB  PHE A  30      46.443 -22.581 -13.848  1.00212.08      A    C  
ANISOU  180  CB  PHE A  30    27701  25954  26926    213   -842  -1261  A    C  
ATOM    181  CG  PHE A  30      46.038 -22.686 -12.400  1.00210.06      A    C  
ANISOU  181  CG  PHE A  30    27419  25630  26763     40   -851  -1119  A    C  
ATOM    182  CD1 PHE A  30      46.833 -23.400 -11.483  1.00192.20      A    C  
ANISOU  182  CD1 PHE A  30    25240  23223  24563    106   -847  -1017  A    C  
ATOM    183  CD2 PHE A  30      44.868 -22.067 -11.944  1.00195.16      A    C  
ANISOU  183  CD2 PHE A  30    25423  23832  24894   -176   -859  -1080  A    C  
ATOM    184  CE1 PHE A  30      46.457 -23.510 -10.167  1.00155.65      A    C  
ANISOU  184  CE1 PHE A  30    20606  18536  19997    -55   -855   -882  A    C  
ATOM    185  CE2 PHE A  30      44.491 -22.167 -10.615  1.00179.59      A    C  
ANISOU  185  CE2 PHE A  30    23436  21808  22989   -332   -849   -951  A    C  
ATOM    186  CZ  PHE A  30      45.292 -22.890  -9.729  1.00171.34      A    C  
ANISOU  186  CZ  PHE A  30    22494  20617  21990   -278   -848   -852  A    C  
ATOM    187  N   GLY A  31      46.803 -22.640 -16.552  1.00183.80      A    N  
ANISOU  187  N   GLY A  31    24233  22463  23140    475   -841  -1550  A    N  
ATOM    188  CA  GLY A  31      47.038 -22.403 -17.973  1.00165.10      A    C  
ANISOU  188  CA  GLY A  31    21898  20200  20630    617   -820  -1682  A    C  
ATOM    189  C   GLY A  31      48.513 -22.234 -18.289  1.00139.73      A    C  
ANISOU  189  C   GLY A  31    18656  17069  17365    886   -701  -1650  A    C  
ATOM    190  O   GLY A  31      49.319 -22.001 -17.395  1.00141.69      A    O  
ANISOU  190  O   GLY A  31    18801  17350  17685    944   -641  -1505  A    O  
ATOM    191  N   GLU A  32      48.867 -22.337 -19.562  1.00128.32      A    N  
ANISOU  191  N   GLU A  32    17293  15673  15787   1047   -665  -1782  A    N  
ATOM    192  CA  GLU A  32      50.228 -22.060 -19.990  1.00123.48      A    C  
ANISOU  192  CA  GLU A  32    16618  15186  15110   1303   -531  -1748  A    C  
ATOM    193  C   GLU A  32      50.606 -20.617 -19.688  1.00102.13      A    C  
ANISOU  193  C   GLU A  32    13667  12742  12394   1275   -457  -1585  A    C  
ATOM    194  O   GLU A  32      49.868 -19.680 -19.995  1.00 88.12      A    O  
ANISOU  194  O   GLU A  32    11812  11105  10561   1147   -482  -1574  A    O  
ATOM    195  CB  GLU A  32      50.381 -22.266 -21.491  1.00140.34      A    C  
ANISOU  195  CB  GLU A  32    18884  17365  17074   1456   -495  -1922  A    C  
ATOM    196  CG  GLU A  32      49.350 -23.134 -22.185  1.00133.73      A    C  
ANISOU  196  CG  GLU A  32    18281  16352  16177   1360   -619  -2122  A    C  
ATOM    197  CD  GLU A  32      48.985 -22.537 -23.525  1.00146.81      A    C  
ANISOU  197  CD  GLU A  32    19959  18184  17638   1375   -623  -2230  A    C  
ATOM    198  OE1 GLU A  32      48.421 -21.420 -23.526  1.00172.54      A    O  
ANISOU  198  OE1 GLU A  32    23050  21634  20872   1243   -647  -2142  A    O  
ATOM    199  OE2 GLU A  32      49.293 -23.145 -24.576  1.00149.93      A    O1-
ANISOU  199  OE2 GLU A  32    20543  18530  17893   1531   -596  -2397  A    O1-
ATOM    200  N   VAL A  33      51.785 -20.462 -19.107  1.00 93.20      A    N  
ANISOU  200  N   VAL A  33    12420  11672  11317   1402   -370  -1457  A    N  
ATOM    201  CA  VAL A  33      52.328 -19.147 -18.759  1.00 75.52      A    C  
ANISOU  201  CA  VAL A  33     9958   9663   9073   1373   -299  -1296  A    C  
ATOM    202  C   VAL A  33      53.664 -18.942 -19.477  1.00 77.51      A    C  
ANISOU  202  C   VAL A  33    10127  10072   9249   1606   -164  -1272  A    C  
ATOM    203  O   VAL A  33      54.522 -19.818 -19.420  1.00 89.96      A    O  
ANISOU  203  O   VAL A  33    11743  11573  10864   1794   -121  -1283  A    O  
ATOM    204  CB  VAL A  33      52.557 -19.072 -17.244  1.00 66.83      A    C  
ANISOU  204  CB  VAL A  33     8763   8516   8110   1273   -331  -1137  A    C  
ATOM    205  CG1 VAL A  33      52.952 -17.688 -16.808  1.00 68.01      A    C  
ANISOU  205  CG1 VAL A  33     8712   8874   8252   1195   -282   -987  A    C  
ATOM    206  CG2 VAL A  33      51.283 -19.497 -16.531  1.00 64.71      A    C  
ANISOU  206  CG2 VAL A  33     8593   8076   7917   1063   -444  -1165  A    C  
ATOM    207  N   PHE A  34      53.827 -17.804 -20.147  1.00 71.01      A    N  
ANISOU  207  N   PHE A  34     9192   9467   8322   1598    -93  -1232  A    N  
ATOM    208  CA  PHE A  34      55.078 -17.483 -20.860  1.00 65.66      A    C  
ANISOU  208  CA  PHE A  34     8409   8974   7563   1795     52  -1190  A    C  
ATOM    209  C   PHE A  34      55.808 -16.282 -20.285  1.00 66.87      A    C  
ANISOU  209  C   PHE A  34     8330   9322   7753   1722    110   -995  A    C  
ATOM    210  O   PHE A  34      55.176 -15.304 -19.877  1.00 77.25      A    O  
ANISOU  210  O   PHE A  34     9592  10680   9078   1525     61   -926  A    O  
ATOM    211  CB  PHE A  34      54.770 -17.164 -22.305  1.00 73.11      A    C  
ANISOU  211  CB  PHE A  34     9433  10021   8323   1853    103  -1303  A    C  
ATOM    212  CG  PHE A  34      54.276 -18.333 -23.089  1.00 95.77      A    C  
ANISOU  212  CG  PHE A  34    12541  12726  11119   1952     63  -1511  A    C  
ATOM    213  CD1 PHE A  34      55.178 -19.165 -23.728  1.00 94.96      A    C  
ANISOU  213  CD1 PHE A  34    12516  12605  10957   2208    169  -1596  A    C  
ATOM    214  CD2 PHE A  34      52.917 -18.554 -23.263  1.00104.31      A    C  
ANISOU  214  CD2 PHE A  34    13770  13685  12177   1790    -76  -1626  A    C  
ATOM    215  CE1 PHE A  34      54.744 -20.228 -24.492  1.00 99.50      A    C  
ANISOU  215  CE1 PHE A  34    13345  13012  11447   2300    134  -1805  A    C  
ATOM    216  CE2 PHE A  34      52.472 -19.622 -24.014  1.00104.59      A    C  
ANISOU  216  CE2 PHE A  34    14039  13565  12135   1857   -128  -1827  A    C  
ATOM    217  CZ  PHE A  34      53.386 -20.471 -24.621  1.00107.23      A    C  
ANISOU  217  CZ  PHE A  34    14484  13852  12405   2110    -24  -1924  A    C  
ATOM    218  N   LYS A  35      57.134 -16.353 -20.251  1.00 69.25      A    N  
ANISOU  218  N   LYS A  35     8494   9741   8077   1880    212   -906  A    N  
ATOM    219  CA  LYS A  35      57.923 -15.143 -20.021  1.00 71.63      A    C  
ANISOU  219  CA  LYS A  35     8574  10263   8379   1810    281   -733  A    C  
ATOM    220  C   LYS A  35      58.092 -14.482 -21.379  1.00 74.30      A    C  
ANISOU  220  C   LYS A  35     8899  10776   8552   1876    401   -762  A    C  
ATOM    221  O   LYS A  35      58.352 -15.170 -22.372  1.00 79.45      A    O  
ANISOU  221  O   LYS A  35     9639  11438   9109   2077    483   -876  A    O  
ATOM    222  CB  LYS A  35      59.287 -15.450 -19.416  1.00 72.00      A    C  
ANISOU  222  CB  LYS A  35     8441  10393   8520   1935    332   -607  A    C  
ATOM    223  CG  LYS A  35      60.134 -14.209 -19.158  1.00 66.31      A    C  
ANISOU  223  CG  LYS A  35     7483   9905   7806   1830    389   -424  A    C  
ATOM    224  CD  LYS A  35      61.551 -14.555 -18.782  1.00 67.39      A    C  
ANISOU  224  CD  LYS A  35     7413  10169   8023   1978    446   -302  A    C  
ATOM    225  CE  LYS A  35      62.358 -13.328 -18.392  1.00 68.82      A    C  
ANISOU  225  CE  LYS A  35     7352  10571   8223   1823    473   -112  A    C  
ATOM    226  NZ  LYS A  35      63.828 -13.642 -18.188  1.00 70.71      A    N1+
ANISOU  226  NZ  LYS A  35     7343  10987   8533   1979    538     16  A    N1+
ATOM    227  N   ALA A  36      57.937 -13.166 -21.442  1.00 73.28      A    N  
ANISOU  227  N   ALA A  36     8686  10776   8380   1714    416   -662  A    N  
ATOM    228  CA  ALA A  36      58.127 -12.477 -22.707  1.00 75.73      A    C  
ANISOU  228  CA  ALA A  36     8989  11258   8528   1766    533   -662  A    C  
ATOM    229  C   ALA A  36      58.727 -11.082 -22.573  1.00 80.46      A    C  
ANISOU  229  C   ALA A  36     9410  12038   9120   1632    598   -477  A    C  
ATOM    230  O   ALA A  36      58.889 -10.544 -21.476  1.00 79.22      A    O  
ANISOU  230  O   ALA A  36     9149  11868   9079   1473    538   -359  A    O  
ATOM    231  CB  ALA A  36      56.847 -12.439 -23.515  1.00 71.67      A    C  
ANISOU  231  CB  ALA A  36     8670  10667   7894   1726    469   -799  A    C  
ATOM    232  N   ARG A  37      59.045 -10.511 -23.725  1.00 73.94      A    N  
ANISOU  232  N   ARG A  37     8571  11377   8144   1689    722   -455  A    N  
ATOM    233  CA  ARG A  37      59.830  -9.303 -23.804  1.00 64.62      A    C  
ANISOU  233  CA  ARG A  37     7223  10384   6943   1588    817   -275  A    C  
ATOM    234  C   ARG A  37      59.129  -8.310 -24.700  1.00 68.14      A    C  
ANISOU  234  C   ARG A  37     7773  10874   7240   1505    836   -265  A    C  
ATOM    235  O   ARG A  37      58.794  -8.622 -25.836  1.00 85.39      A    O  
ANISOU  235  O   ARG A  37    10085  13090   9268   1632    884   -369  A    O  
ATOM    236  CB  ARG A  37      61.196  -9.651 -24.406  1.00 67.61      A    C  
ANISOU  236  CB  ARG A  37     7446  10962   7279   1774    992   -223  A    C  
ATOM    237  CG  ARG A  37      62.080  -8.444 -24.613  1.00 65.25      A    C  
ANISOU  237  CG  ARG A  37     6959  10880   6950   1661   1107    -28  A    C  
ATOM    238  CD  ARG A  37      63.408  -8.842 -25.203  1.00 60.51      A    C  
ANISOU  238  CD  ARG A  37     6179  10498   6313   1853   1293     26  A    C  
ATOM    239  NE  ARG A  37      64.257  -7.658 -25.289  1.00 63.90      A    N  
ANISOU  239  NE  ARG A  37     6407  11137   6733   1700   1393    233  A    N  
ATOM    240  CZ  ARG A  37      64.188  -6.790 -26.284  1.00 70.77      A    C  
ANISOU  240  CZ  ARG A  37     7323  12120   7446   1646   1500    289  A    C  
ATOM    241  NH1 ARG A  37      63.340  -7.003 -27.291  1.00 74.20      A    N1+
ANISOU  241  NH1 ARG A  37     7987  12497   7709   1750   1517    152  A    N1+
ATOM    242  NH2 ARG A  37      65.000  -5.750 -26.304  1.00 81.29      A    N  
ANISOU  242  NH2 ARG A  37     8473  13629   8784   1488   1588    487  A    N  
ATOM    243  N   HIS A  38      58.884  -7.116 -24.184  1.00 65.04      A    N  
ANISOU  243  N   HIS A  38     7347  10475   6890   1296    792   -142  A    N  
ATOM    244  CA  HIS A  38      58.295  -6.078 -25.017  1.00 70.10      A    C  
ANISOU  244  CA  HIS A  38     8083  11157   7396   1226    814   -102  A    C  
ATOM    245  C   HIS A  38      59.269  -5.769 -26.153  1.00 70.25      A    C  
ANISOU  245  C   HIS A  38     8030  11393   7268   1318    996    -22  A    C  
ATOM    246  O   HIS A  38      60.460  -5.550 -25.906  1.00 68.94      A    O  
ANISOU  246  O   HIS A  38     7675  11364   7155   1297   1097    104  A    O  
ATOM    247  CB  HIS A  38      58.024  -4.833 -24.196  1.00 71.73      A    C  
ANISOU  247  CB  HIS A  38     8266  11303   7685    998    752     25  A    C  
ATOM    248  CG  HIS A  38      57.297  -3.777 -24.955  1.00 69.35      A    C  
ANISOU  248  CG  HIS A  38     8083  11004   7262    939    756     70  A    C  
ATOM    249  CD2 HIS A  38      56.024  -3.333 -24.852  1.00 65.15      A    C  
ANISOU  249  CD2 HIS A  38     7685  10341   6726    878    646     30  A    C  
ATOM    250  ND1 HIS A  38      57.886  -3.056 -25.983  1.00 78.94      A    N  
ANISOU  250  ND1 HIS A  38     9280  12378   8336    951    888    180  A    N  
ATOM    251  CE1 HIS A  38      56.993  -2.223 -26.486  1.00 84.96      A    C  
ANISOU  251  CE1 HIS A  38    10179  13092   9010    904    848    206  A    C  
ATOM    252  NE2 HIS A  38      55.862  -2.354 -25.800  1.00 77.28      A    N  
ANISOU  252  NE2 HIS A  38     9290  11948   8125    864    701    117  A    N  
ATOM    253  N   ARG A  39      58.768  -5.743 -27.389  1.00 69.96      A    N  
ANISOU  253  N   ARG A  39     8136  11403   7040   1414   1036    -88  A    N  
ATOM    254  CA  ARG A  39      59.667  -5.692 -28.542  1.00 69.78      A    C  
ANISOU  254  CA  ARG A  39     8068  11592   6851   1539   1226    -40  A    C  
ATOM    255  C   ARG A  39      60.393  -4.361 -28.704  1.00 63.82      A    C  
ANISOU  255  C   ARG A  39     7194  10985   6068   1391   1338    182  A    C  
ATOM    256  O   ARG A  39      61.381  -4.295 -29.432  1.00 65.16      A    O  
ANISOU  256  O   ARG A  39     7261  11356   6137   1469   1519    261  A    O  
ATOM    257  CB  ARG A  39      58.933  -6.048 -29.839  1.00 84.64      A    C  
ANISOU  257  CB  ARG A  39    10160  13489   8508   1678   1232   -176  A    C  
ATOM    258  CG  ARG A  39      58.689  -7.540 -30.002  1.00100.28      A    C  
ANISOU  258  CG  ARG A  39    12244  15382  10472   1868   1193   -398  A    C  
ATOM    259  CD  ARG A  39      58.164  -7.923 -31.407  1.00 97.51      A    C  
ANISOU  259  CD  ARG A  39    12105  15079   9864   2011   1217   -538  A    C  
ATOM    260  NE  ARG A  39      57.369  -9.154 -31.343  1.00 96.50      A    N  
ANISOU  260  NE  ARG A  39    12140  14775   9750   2096   1082   -765  A    N  
ATOM    261  CZ  ARG A  39      57.839 -10.385 -31.546  1.00111.39      A    C  
ANISOU  261  CZ  ARG A  39    14075  16630  11615   2289   1144   -914  A    C  
ATOM    262  NH1 ARG A  39      59.112 -10.581 -31.880  1.00129.75      A    N1+
ANISOU  262  NH1 ARG A  39    16285  19115  13898   2447   1352   -864  A    N1+
ATOM    263  NH2 ARG A  39      57.021 -11.424 -31.383  1.00 98.60      A    N  
ANISOU  263  NH2 ARG A  39    12619  14815  10028   2321    997  -1110  A    N  
ATOM    264  N   LYS A  40      59.918  -3.320 -28.019  1.00 68.01      A    N  
ANISOU  264  N   LYS A  40     7741  11411   6686   1178   1240    283  A    N  
ATOM    265  CA  LYS A  40      60.511  -2.000 -28.166  1.00 77.28      A    C  
ANISOU  265  CA  LYS A  40     8842  12685   7835   1011   1330    493  A    C  
ATOM    266  C   LYS A  40      61.390  -1.563 -26.999  1.00 78.78      A    C  
ANISOU  266  C   LYS A  40     8836  12885   8212    831   1323    625  A    C  
ATOM    267  O   LYS A  40      62.417  -0.922 -27.199  1.00 70.96      A    O  
ANISOU  267  O   LYS A  40     7698  12055   7209    737   1448    792  A    O  
ATOM    268  CB  LYS A  40      59.419  -0.964 -28.423  1.00 69.83      A    C  
ANISOU  268  CB  LYS A  40     8085  11622   6824    904   1246    533  A    C  
ATOM    269  CG  LYS A  40      58.963  -0.927 -29.892  1.00 68.80      A    C  
ANISOU  269  CG  LYS A  40     8110  11578   6450   1037   1305    503  A    C  
ATOM    270  CD  LYS A  40      57.655  -0.167 -29.991  1.00 79.92      A    C  
ANISOU  270  CD  LYS A  40     9704  12838   7822    974   1170    506  A    C  
ATOM    271  CE  LYS A  40      57.037  -0.284 -31.366  1.00 87.62      A    C  
ANISOU  271  CE  LYS A  40    10845  13889   8557   1116   1179    453  A    C  
ATOM    272  NZ  LYS A  40      57.722   0.595 -32.334  1.00 97.55      A    N1+
ANISOU  272  NZ  LYS A  40    12113  15306   9642   1088   1340    633  A    N1+
ATOM    273  N   THR A  41      60.983  -1.939 -25.794  1.00 74.75      A    N  
ANISOU  273  N   THR A  41     8322  12212   7865    775   1174    552  A    N  
ATOM    274  CA  THR A  41      61.561  -1.425 -24.564  1.00 72.00      A    C  
ANISOU  274  CA  THR A  41     7840  11834   7681    574   1118    663  A    C  
ATOM    275  C   THR A  41      62.312  -2.498 -23.784  1.00 73.90      A    C  
ANISOU  275  C   THR A  41     7906  12121   8050    654   1096    624  A    C  
ATOM    276  O   THR A  41      63.085  -2.183 -22.860  1.00 71.65      A    O  
ANISOU  276  O   THR A  41     7461  11875   7885    503   1064    733  A    O  
ATOM    277  CB  THR A  41      60.441  -0.947 -23.633  1.00 70.99      A    C  
ANISOU  277  CB  THR A  41     7866  11469   7635    437    955    616  A    C  
ATOM    278  CG2 THR A  41      59.511  -0.023 -24.361  1.00 70.53      A    C  
ANISOU  278  CG2 THR A  41     7997  11337   7463    405    953    636  A    C  
ATOM    279  OG1 THR A  41      59.756  -2.093 -23.088  1.00 76.87      A    O  
ANISOU  279  OG1 THR A  41     8664  12094   8449    555    846    448  A    O  
ATOM    280  N   GLY A  42      62.028  -3.758 -24.108  1.00 68.74      A    N  
ANISOU  280  N   GLY A  42     7301  11445   7371    883   1094    466  A    N  
ATOM    281  CA  GLY A  42      62.698  -4.878 -23.481  1.00 66.64      A    C  
ANISOU  281  CA  GLY A  42     6895  11206   7218   1004   1079    425  A    C  
ATOM    282  C   GLY A  42      62.036  -5.271 -22.175  1.00 63.18      A    C  
ANISOU  282  C   GLY A  42     6522  10561   6920    927    897    356  A    C  
ATOM    283  O   GLY A  42      62.428  -6.235 -21.531  1.00 67.03      A    O  
ANISOU  283  O   GLY A  42     6930  11029   7507   1022    854    320  A    O  
ATOM    284  N   GLN A  43      61.001  -4.525 -21.789  1.00 54.96      A    N  
ANISOU  284  N   GLN A  43     5634   9363   5882    766    797    341  A    N  
ATOM    285  CA  GLN A  43      60.290  -4.799 -20.559  1.00 59.84      A    C  
ANISOU  285  CA  GLN A  43     6326   9794   6617    680    642    280  A    C  
ATOM    286  C   GLN A  43      59.863  -6.250 -20.449  1.00 68.20      A    C  
ANISOU  286  C   GLN A  43     7448  10753   7709    861    588    126  A    C  
ATOM    287  O   GLN A  43      59.219  -6.761 -21.354  1.00 80.60      A    O  
ANISOU  287  O   GLN A  43     9144  12290   9188    998    610      4  A    O  
ATOM    288  CB  GLN A  43      59.074  -3.889 -20.430  1.00 63.15      A    C  
ANISOU  288  CB  GLN A  43     6920  10065   7008    543    573    259  A    C  
ATOM    289  CG  GLN A  43      58.278  -4.146 -19.147  1.00 77.45      A    C  
ANISOU  289  CG  GLN A  43     8808  11692   8927    455    433    196  A    C  
ATOM    290  CD  GLN A  43      56.966  -3.396 -19.192  1.00 88.45      A    C  
ANISOU  290  CD  GLN A  43    10368  12951  10285    380    385    155  A    C  
ATOM    291  NE2 GLN A  43      56.225  -3.435 -18.084  1.00 72.21      A    N  
ANISOU  291  NE2 GLN A  43     8379  10746   8311    291    288    113  A    N  
ATOM    292  OE1 GLN A  43      56.621  -2.787 -20.242  1.00 87.25      A    O  
ANISOU  292  OE1 GLN A  43    10283  12839  10026    414    441    168  A    O  
ATOM    293  N   LYS A  44      60.265  -6.932 -19.381  1.00 64.13      A    N  
ANISOU  293  N   LYS A  44     6856  10193   7317    860    515    136  A    N  
ATOM    294  CA  LYS A  44      59.902  -8.349 -19.215  1.00 64.42      A    C  
ANISOU  294  CA  LYS A  44     6970  10110   7397   1025    462      2  A    C  
ATOM    295  C   LYS A  44      58.509  -8.493 -18.630  1.00 64.08      A    C  
ANISOU  295  C   LYS A  44     7106   9855   7384    934    337    -97  A    C  
ATOM    296  O   LYS A  44      58.166  -7.766 -17.684  1.00 71.59      A    O  
ANISOU  296  O   LYS A  44     8067  10745   8388    746    265    -37  A    O  
ATOM    297  CB  LYS A  44      60.922  -9.070 -18.340  1.00 61.90      A    C  
ANISOU  297  CB  LYS A  44     6497   9827   7192   1083    434     70  A    C  
ATOM    298  CG  LYS A  44      62.367  -8.989 -18.820  1.00 70.34      A    C  
ANISOU  298  CG  LYS A  44     7340  11131   8254   1182    559    184  A    C  
ATOM    299  CD  LYS A  44      62.566  -9.434 -20.254  1.00 66.87      A    C  
ANISOU  299  CD  LYS A  44     6924  10785   7697   1407    709    105  A    C  
ATOM    300  CE  LYS A  44      64.041  -9.419 -20.625  1.00 71.39      A    C  
ANISOU  300  CE  LYS A  44     7242  11608   8275   1519    849    230  A    C  
ATOM    301  NZ  LYS A  44      64.657  -8.077 -20.621  1.00 67.37      A    N1+
ANISOU  301  NZ  LYS A  44     6569  11274   7751   1309    898    404  A    N1+
ATOM    302  N   VAL A  45      57.699  -9.403 -19.164  1.00 61.89      A    N  
ANISOU  302  N   VAL A  45     6972   9470   7071   1055    312   -248  A    N  
ATOM    303  CA  VAL A  45      56.325  -9.581 -18.690  1.00 65.15      A    C  
ANISOU  303  CA  VAL A  45     7533   9703   7515    963    200   -340  A    C  
ATOM    304  C   VAL A  45      55.955 -11.067 -18.638  1.00 62.51      A    C  
ANISOU  304  C   VAL A  45     7300   9228   7221   1085    144   -472  A    C  
ATOM    305  O   VAL A  45      56.681 -11.897 -19.170  1.00 67.83      A    O  
ANISOU  305  O   VAL A  45     7959   9934   7875   1266    202   -513  A    O  
ATOM    306  CB  VAL A  45      55.313  -8.866 -19.630  1.00 61.25      A    C  
ANISOU  306  CB  VAL A  45     7142   9217   6911    931    206   -393  A    C  
ATOM    307  CG1 VAL A  45      55.673  -7.401 -19.806  1.00 61.98      A    C  
ANISOU  307  CG1 VAL A  45     7167   9426   6956    824    269   -259  A    C  
ATOM    308  CG2 VAL A  45      55.246  -9.571 -20.966  1.00 59.75      A    C  
ANISOU  308  CG2 VAL A  45     7030   9065   6604   1108    253   -511  A    C  
ATOM    309  N   ALA A  46      54.829 -11.396 -18.013  1.00 56.57      A    N  
ANISOU  309  N   ALA A  46     6655   8315   6523    987     40   -537  A    N  
ATOM    310  CA  ALA A  46      54.302 -12.752 -18.040  1.00 55.50      A    C  
ANISOU  310  CA  ALA A  46     6645   8022   6421   1066    -21   -666  A    C  
ATOM    311  C   ALA A  46      53.005 -12.779 -18.825  1.00 62.53      A    C  
ANISOU  311  C   ALA A  46     7662   8858   7239   1032    -69   -792  A    C  
ATOM    312  O   ALA A  46      52.101 -11.979 -18.581  1.00 69.92      A    O  
ANISOU  312  O   ALA A  46     8598   9791   8175    891   -110   -769  A    O  
ATOM    313  CB  ALA A  46      54.068 -13.290 -16.625  1.00 48.19      A    C  
ANISOU  313  CB  ALA A  46     5735   6952   5623    967   -109   -629  A    C  
ATOM    314  N   LEU A  47      52.891 -13.722 -19.751  1.00 54.67      A    N  
ANISOU  314  N   LEU A  47     6777   7813   6178   1165    -70   -929  A    N  
ATOM    315  CA  LEU A  47      51.678 -13.908 -20.510  1.00 55.68      A    C  
ANISOU  315  CA  LEU A  47     7030   7890   6234   1127   -142  -1058  A    C  
ATOM    316  C   LEU A  47      50.916 -15.146 -20.043  1.00 66.01      A    C  
ANISOU  316  C   LEU A  47     8462   8991   7625   1080   -249  -1166  A    C  
ATOM    317  O   LEU A  47      51.465 -16.243 -19.948  1.00 76.13      A    O  
ANISOU  317  O   LEU A  47     9818  10162   8945   1190   -243  -1219  A    O  
ATOM    318  CB  LEU A  47      51.974 -14.020 -22.009  1.00 59.24      A    C  
ANISOU  318  CB  LEU A  47     7551   8438   6518   1283    -80  -1152  A    C  
ATOM    319  CG  LEU A  47      52.823 -12.917 -22.637  1.00 59.14      A    C  
ANISOU  319  CG  LEU A  47     7430   8636   6404   1343     45  -1044  A    C  
ATOM    320  CD1 LEU A  47      53.079 -13.183 -24.116  1.00 61.71      A    C  
ANISOU  320  CD1 LEU A  47     7850   9052   6545   1506    114  -1147  A    C  
ATOM    321  CD2 LEU A  47      52.208 -11.553 -22.424  1.00 54.65      A    C  
ANISOU  321  CD2 LEU A  47     6792   8139   5831   1187     22   -937  A    C  
ATOM    322  N   LYS A  48      49.610 -14.978 -19.846  1.00 66.41      A    N  
ANISOU  322  N   LYS A  48     8542   8990   7701    922   -345  -1198  A    N  
ATOM    323  CA  LYS A  48      48.733 -16.106 -19.582  1.00 65.79      A    C  
ANISOU  323  CA  LYS A  48     8582   8726   7686    845   -452  -1304  A    C  
ATOM    324  C   LYS A  48      47.626 -16.148 -20.607  1.00 69.75      A    C  
ANISOU  324  C   LYS A  48     9160   9247   8094    796   -537  -1428  A    C  
ATOM    325  O   LYS A  48      46.790 -15.253 -20.631  1.00 82.19      A    O  
ANISOU  325  O   LYS A  48    10654  10915   9656    692   -571  -1384  A    O  
ATOM    326  CB  LYS A  48      48.116 -15.939 -18.187  1.00 69.12      A    C  
ANISOU  326  CB  LYS A  48     8940   9077   8245    666   -496  -1210  A    C  
ATOM    327  CG  LYS A  48      48.250 -17.163 -17.327  1.00 81.56      A    C  
ANISOU  327  CG  LYS A  48    10602  10457   9930    645   -536  -1221  A    C  
ATOM    328  CD  LYS A  48      47.130 -17.191 -16.268  1.00 97.50      A    C  
ANISOU  328  CD  LYS A  48    12601  12395  12049    434   -601  -1178  A    C  
ATOM    329  CE  LYS A  48      46.908 -18.592 -15.703  1.00108.19      A    C  
ANISOU  329  CE  LYS A  48    14087  13525  13493    383   -666  -1220  A    C  
ATOM    330  NZ  LYS A  48      46.415 -18.526 -14.277  1.00132.95      A    N1+
ANISOU  330  NZ  LYS A  48    17178  16606  16731    213   -678  -1106  A    N1+
ATOM    331  N   LYS A  49      47.550 -17.211 -21.396  1.00 73.52      A    N  
ANISOU  331  N   LYS A  49     9798   9625   8509    864   -584  -1584  A    N  
ATOM    332  CA  LYS A  49      46.433 -17.379 -22.338  1.00 79.20      A    C  
ANISOU  332  CA  LYS A  49    10603  10354   9135    791   -699  -1714  A    C  
ATOM    333  C   LYS A  49      45.163 -17.777 -21.589  1.00 69.49      A    C  
ANISOU  333  C   LYS A  49     9363   9010   8030    573   -824  -1724  A    C  
ATOM    334  O   LYS A  49      45.258 -18.497 -20.593  1.00 82.11      A    O  
ANISOU  334  O   LYS A  49    10989  10448   9760    514   -829  -1697  A    O  
ATOM    335  CB  LYS A  49      46.808 -18.444 -23.357  1.00 87.54      A    C  
ANISOU  335  CB  LYS A  49    11863  11320  10078    924   -710  -1890  A    C  
ATOM    336  CG  LYS A  49      45.846 -18.655 -24.510  1.00 84.59      A    C  
ANISOU  336  CG  LYS A  49    11606  10970   9563    867   -834  -2043  A    C  
ATOM    337  CD  LYS A  49      46.124 -19.998 -25.193  1.00 96.86      A    C  
ANISOU  337  CD  LYS A  49    13410  12350  11040    961   -862  -2240  A    C  
ATOM    338  CE  LYS A  49      45.696 -20.026 -26.655  1.00108.03      A    C  
ANISOU  338  CE  LYS A  49    14963  13849  12233    992   -934  -2396  A    C  
ATOM    339  NZ  LYS A  49      46.459 -19.031 -27.470  1.00140.07      A    N1+
ANISOU  339  NZ  LYS A  49    18955  18140  16123   1164   -803  -2334  A    N1+
ATOM    340  N   VAL A  50      44.011 -17.286 -22.034  1.00 66.13      A    N  
ANISOU  340  N   VAL A  50     8883   8679   7563    457   -919  -1745  A    N  
ATOM    341  CA  VAL A  50      42.707 -17.655 -21.452  1.00 68.49      A    C  
ANISOU  341  CA  VAL A  50     9144   8904   7974    242  -1038  -1756  A    C  
ATOM    342  C   VAL A  50      42.191 -18.901 -22.162  1.00 81.36      A    C  
ANISOU  342  C   VAL A  50    10955  10397   9561    179  -1171  -1937  A    C  
ATOM    343  O   VAL A  50      41.913 -18.839 -23.372  1.00 77.18      A    O  
ANISOU  343  O   VAL A  50    10491   9952   8879    216  -1242  -2043  A    O  
ATOM    344  CB  VAL A  50      41.726 -16.476 -21.544  1.00 60.94      A    C  
ANISOU  344  CB  VAL A  50     8014   8132   7007    163  -1074  -1675  A    C  
ATOM    345  CG1 VAL A  50      40.296 -16.873 -21.189  1.00 63.88      A    C  
ANISOU  345  CG1 VAL A  50     8324   8472   7476    -48  -1203  -1698  A    C  
ATOM    346  CG2 VAL A  50      42.202 -15.375 -20.631  1.00 52.48      A    C  
ANISOU  346  CG2 VAL A  50     6801   7136   6000    198   -945  -1507  A    C  
ATOM    347  N   LEU A  51      42.099 -20.016 -21.420  1.00 84.39      A    N  
ANISOU  347  N   LEU A  51    11435  10561  10065     82  -1205  -1969  A    N  
ATOM    348  CA  LEU A  51      41.743 -21.319 -21.980  1.00 92.27      A    C  
ANISOU  348  CA  LEU A  51    12648  11373  11037     14  -1325  -2145  A    C  
ATOM    349  C   LEU A  51      40.294 -21.404 -22.415  1.00 96.28      A    C  
ANISOU  349  C   LEU A  51    13116  11929  11535   -205  -1497  -2213  A    C  
ATOM    350  O   LEU A  51      39.356 -20.923 -21.704  1.00107.72      A    O  
ANISOU  350  O   LEU A  51    14370  13461  13095   -375  -1529  -2103  A    O  
ATOM    351  CB  LEU A  51      42.009 -22.417 -20.955  1.00 98.69      A    C  
ANISOU  351  CB  LEU A  51    13572  11926  11999    -43  -1312  -2129  A    C  
ATOM    352  CG  LEU A  51      43.431 -22.692 -20.477  1.00102.78      A    C  
ANISOU  352  CG  LEU A  51    14159  12347  12545    167  -1176  -2075  A    C  
ATOM    353  CD1 LEU A  51      44.291 -23.303 -21.590  1.00 86.92      A    C  
ANISOU  353  CD1 LEU A  51    12357  10269  10399    387  -1147  -2233  A    C  
ATOM    354  CD2 LEU A  51      44.034 -21.417 -19.862  1.00122.97      A    C  
ANISOU  354  CD2 LEU A  51    16494  15105  15121    252  -1047  -1894  A    C  
ATOM    355  N   MET A  52      40.090 -22.048 -23.562  1.00 93.52      A    N  
ANISOU  355  N   MET A  52    12949  11532  11053   -205  -1610  -2395  A    N  
ATOM    356  CA  MET A  52      38.755 -22.086 -24.137  1.00 94.15      A    C  
ANISOU  356  CA  MET A  52    12983  11691  11097   -411  -1797  -2465  A    C  
ATOM    357  C   MET A  52      38.299 -23.502 -24.467  1.00101.85      A    C  
ANISOU  357  C   MET A  52    14195  12429  12072   -572  -1949  -2646  A    C  
ATOM    358  O   MET A  52      37.912 -23.787 -25.606  1.00105.37      A    O  
ANISOU  358  O   MET A  52    14770  12902  12364   -605  -2086  -2805  A    O  
ATOM    359  CB  MET A  52      38.707 -21.172 -25.355  1.00 91.81      A    C  
ANISOU  359  CB  MET A  52    12644  11638  10601   -292  -1827  -2495  A    C  
ATOM    360  CG  MET A  52      39.139 -19.745 -25.098  1.00 91.38      A    C  
ANISOU  360  CG  MET A  52    12380  11797  10541   -145  -1684  -2317  A    C  
ATOM    361  SD  MET A  52      37.885 -18.782 -24.239  1.00108.09      A    S  
ANISOU  361  SD  MET A  52    14179  14076  12812   -319  -1723  -2140  A    S  
ATOM    362  CE  MET A  52      36.419 -18.920 -25.279  1.00 95.02      A    C  
ANISOU  362  CE  MET A  52    12481  12550  11069   -493  -1974  -2240  A    C  
ATOM    363  N   GLU A  53      38.317 -24.362 -23.444  1.00111.59      A    N  
ANISOU  363  N   GLU A  53    15493  13429  13475   -684  -1930  -2614  A    N  
ATOM    364  CA  GLU A  53      37.911 -25.750 -23.584  1.00124.03      A    C  
ANISOU  364  CA  GLU A  53    17313  14732  15081   -858  -2064  -2767  A    C  
ATOM    365  C   GLU A  53      36.449 -25.991 -23.338  1.00127.33      A    C  
ANISOU  365  C   GLU A  53    17609  15171  15599  -1201  -2235  -2754  A    C  
ATOM    366  O   GLU A  53      36.106 -26.843 -22.529  1.00123.73      A    O  
ANISOU  366  O   GLU A  53    17214  14503  15294  -1392  -2264  -2728  A    O  
ATOM    367  CB  GLU A  53      38.771 -26.663 -22.695  1.00136.70      A    C  
ANISOU  367  CB  GLU A  53    19093  16041  16804   -786  -1958  -2741  A    C  
ATOM    368  CG  GLU A  53      39.866 -27.428 -23.450  1.00138.89      A    C  
ANISOU  368  CG  GLU A  53    19686  16127  16958   -544  -1911  -2910  A    C  
ATOM    369  CD  GLU A  53      40.532 -26.575 -24.524  1.00140.48      A    C  
ANISOU  369  CD  GLU A  53    19859  16561  16953   -288  -1836  -2961  A    C  
ATOM    370  OE1 GLU A  53      40.615 -25.309 -24.357  1.00138.59      A    O  
ANISOU  370  OE1 GLU A  53    19352  16598  16706   -220  -1753  -2809  A    O  
ATOM    371  OE2 GLU A  53      40.944 -27.183 -25.543  1.00142.14      A    O1-
ANISOU  371  OE2 GLU A  53    20330  16668  17005   -163  -1859  -3155  A    O1-
ATOM    372  N   ASN A  54      35.599 -25.257 -24.069  1.00135.49      A    N  
ANISOU  372  N   ASN A  54    18471  16463  16544  -1276  -2351  -2764  A    N  
ATOM    373  CA  ASN A  54      34.134 -25.285 -23.932  1.00140.22      A    C  
ANISOU  373  CA  ASN A  54    18879  17163  17233  -1589  -2520  -2732  A    C  
ATOM    374  C   ASN A  54      33.587 -24.877 -22.539  1.00129.99      A    C  
ANISOU  374  C   ASN A  54    17303  15932  16152  -1722  -2428  -2516  A    C  
ATOM    375  O   ASN A  54      33.157 -25.755 -21.771  1.00134.16      A    O  
ANISOU  375  O   ASN A  54    17874  16273  16827  -1947  -2458  -2495  A    O  
ATOM    376  CB  ASN A  54      33.557 -26.644 -24.421  1.00172.40      A    C  
ANISOU  376  CB  ASN A  54    23199  21007  21295  -1841  -2723  -2920  A    C  
ATOM    377  CG  ASN A  54      34.372 -27.865 -23.948  1.00169.96      A    C  
ANISOU  377  CG  ASN A  54    23215  20313  21049  -1813  -2654  -2995  A    C  
ATOM    378  ND2 ASN A  54      33.973 -28.445 -22.819  1.00162.84      A    N  
ANISOU  378  ND2 ASN A  54    22275  19248  20347  -2023  -2638  -2891  A    N  
ATOM    379  OD1 ASN A  54      35.340 -28.279 -24.600  1.00172.56      A    O  
ANISOU  379  OD1 ASN A  54    23825  20497  21244  -1597  -2610  -3138  A    O  
ATOM    380  N   GLU A  55      33.530 -23.583 -22.196  1.00123.48      A    N  
ANISOU  380  N   GLU A  55    16207  15365  15345  -1601  -2318  -2357  A    N  
ATOM    381  CA  GLU A  55      33.488 -22.435 -23.096  1.00118.72      A    C  
ANISOU  381  CA  GLU A  55    15474  15036  14597  -1435  -2335  -2348  A    C  
ATOM    382  C   GLU A  55      32.585 -22.653 -24.304  1.00113.77      A    C  
ANISOU  382  C   GLU A  55    14858  14516  13850  -1570  -2573  -2481  A    C  
ATOM    383  O   GLU A  55      32.924 -22.394 -25.441  1.00119.58      A    O  
ANISOU  383  O   GLU A  55    15707  15336  14390  -1426  -2629  -2582  A    O  
ATOM    384  CB  GLU A  55      34.852 -21.912 -23.429  1.00119.95      A    C  
ANISOU  384  CB  GLU A  55    15753  15195  14628  -1122  -2181  -2353  A    C  
ATOM    385  CG  GLU A  55      35.467 -21.218 -22.194  1.00126.12      A    C  
ANISOU  385  CG  GLU A  55    16401  15989  15530  -1009  -1969  -2168  A    C  
ATOM    386  CD  GLU A  55      35.887 -22.205 -21.102  1.00115.36      A    C  
ANISOU  386  CD  GLU A  55    15162  14361  14308  -1087  -1898  -2147  A    C  
ATOM    387  OE1 GLU A  55      35.948 -23.422 -21.394  1.00127.30      A    O  
ANISOU  387  OE1 GLU A  55    16905  15649  15812  -1173  -1988  -2283  A    O  
ATOM    388  OE2 GLU A  55      36.131 -21.767 -19.957  1.00100.89      A    O1-
ANISOU  388  OE2 GLU A  55    13211  12537  12586  -1065  -1759  -1993  A    O1-
ATOM    389  N   LYS A  56      31.402 -23.166 -23.982  1.00112.15      A    N  
ANISOU  389  N   LYS A  56    14529  14312  13769  -1870  -2713  -2470  A    N  
ATOM    390  CA  LYS A  56      30.270 -23.191 -24.905  1.00114.92      A    C  
ANISOU  390  CA  LYS A  56    14779  14834  14050  -2049  -2957  -2542  A    C  
ATOM    391  C   LYS A  56      29.372 -21.998 -24.554  1.00 94.14      A    C  
ANISOU  391  C   LYS A  56    11745  12519  11503  -2049  -2940  -2353  A    C  
ATOM    392  O   LYS A  56      28.258 -21.832 -25.031  1.00 97.79      A    O  
ANISOU  392  O   LYS A  56    12010  13181  11963  -2203  -3124  -2345  A    O  
ATOM    393  CB  LYS A  56      29.526 -24.528 -24.733  1.00126.74      A    C  
ANISOU  393  CB  LYS A  56    16374  16134  15645  -2400  -3124  -2638  A    C  
ATOM    394  CG  LYS A  56      30.452 -25.740 -24.925  1.00124.75      A    C  
ANISOU  394  CG  LYS A  56    16545  15519  15332  -2379  -3114  -2817  A    C  
ATOM    395  CD  LYS A  56      29.676 -27.038 -24.960  1.00142.17      A    C  
ANISOU  395  CD  LYS A  56    18890  17520  17609  -2739  -3311  -2933  A    C  
ATOM    396  CE  LYS A  56      30.336 -28.087 -25.843  1.00145.68      A    C  
ANISOU  396  CE  LYS A  56    19779  17678  17893  -2706  -3400  -3183  A    C  
ATOM    397  NZ  LYS A  56      31.235 -28.978 -25.055  1.00133.18      A    N1+
ANISOU  397  NZ  LYS A  56    18464  15729  16407  -2646  -3249  -3196  A    N1+
ATOM    398  N   GLU A  57      29.911 -21.114 -23.743  1.00 87.60      A    N  
ANISOU  398  N   GLU A  57    10800  11742  10742  -1854  -2715  -2199  A    N  
ATOM    399  CA  GLU A  57      29.180 -19.990 -23.234  1.00 78.68      A    C  
ANISOU  399  CA  GLU A  57     9323  10864   9707  -1822  -2653  -2018  A    C  
ATOM    400  C   GLU A  57      29.987 -18.718 -23.464  1.00 80.81      A    C  
ANISOU  400  C   GLU A  57     9579  11254   9871  -1498  -2505  -1941  A    C  
ATOM    401  O   GLU A  57      30.065 -17.872 -22.600  1.00 81.32      A    O  
ANISOU  401  O   GLU A  57     9483  11385  10028  -1397  -2334  -1791  A    O  
ATOM    402  CB  GLU A  57      28.926 -20.213 -21.743  1.00 67.03      A    C  
ANISOU  402  CB  GLU A  57     7721   9302   8445  -1953  -2506  -1891  A    C  
ATOM    403  CG  GLU A  57      27.828 -21.292 -21.573  1.00 73.71      A    C  
ANISOU  403  CG  GLU A  57     8500  10097   9408  -2312  -2670  -1929  A    C  
ATOM    404  CD  GLU A  57      26.458 -20.723 -21.905  1.00 84.10      A    C  
ANISOU  404  CD  GLU A  57     9467  11721  10767  -2424  -2808  -1856  A    C  
ATOM    405  OE1 GLU A  57      26.164 -19.593 -21.411  1.00 96.28      A    O  
ANISOU  405  OE1 GLU A  57    10747  13467  12368  -2280  -2677  -1698  A    O  
ATOM    406  OE2 GLU A  57      25.665 -21.373 -22.624  1.00 81.05      A    O1-
ANISOU  406  OE2 GLU A  57     9059  11376  10358  -2651  -3045  -1949  A    O1-
ATOM    407  N   GLY A  58      30.584 -18.633 -24.653  1.00 80.38      A    N  
ANISOU  407  N   GLY A  58     9712  11216   9610  -1352  -2575  -2052  A    N  
ATOM    408  CA  GLY A  58      31.422 -17.507 -24.991  1.00 75.78      A    C  
ANISOU  408  CA  GLY A  58     9149  10733   8911  -1065  -2442  -1986  A    C  
ATOM    409  C   GLY A  58      32.598 -17.318 -24.056  1.00 70.83      A    C  
ANISOU  409  C   GLY A  58     8609   9956   8346   -922  -2198  -1919  A    C  
ATOM    410  O   GLY A  58      33.130 -18.290 -23.468  1.00 74.72      A    O  
ANISOU  410  O   GLY A  58     9260  10221   8907   -993  -2145  -1977  A    O  
ATOM    411  N   PHE A  59      32.996 -16.061 -23.901  1.00 64.10      A    N  
ANISOU  411  N   PHE A  59     7656   9226   7471   -727  -2060  -1789  A    N  
ATOM    412  CA  PHE A  59      34.127 -15.712 -23.046  1.00 59.10      A    C  
ANISOU  412  CA  PHE A  59     7084   8484   6884   -593  -1841  -1713  A    C  
ATOM    413  C   PHE A  59      33.892 -16.141 -21.605  1.00 60.95      A    C  
ANISOU  413  C   PHE A  59     7242   8599   7317   -735  -1754  -1645  A    C  
ATOM    414  O   PHE A  59      32.912 -15.757 -20.997  1.00 61.03      A    O  
ANISOU  414  O   PHE A  59     7038   8709   7442   -832  -1754  -1551  A    O  
ATOM    415  CB  PHE A  59      34.440 -14.228 -23.142  1.00 53.62      A    C  
ANISOU  415  CB  PHE A  59     6289   7945   6136   -395  -1728  -1582  A    C  
ATOM    416  CG  PHE A  59      35.737 -13.841 -22.502  1.00 59.32      A    C  
ANISOU  416  CG  PHE A  59     7099   8571   6867   -259  -1528  -1520  A    C  
ATOM    417  CD1 PHE A  59      36.945 -13.929 -23.184  1.00 58.59      A    C  
ANISOU  417  CD1 PHE A  59     7190   8435   6636   -114  -1475  -1579  A    C  
ATOM    418  CD2 PHE A  59      35.754 -13.451 -21.166  1.00 64.42      A    C  
ANISOU  418  CD2 PHE A  59     7640   9174   7660   -289  -1394  -1405  A    C  
ATOM    419  CE1 PHE A  59      38.134 -13.563 -22.590  1.00 56.00      A    C  
ANISOU  419  CE1 PHE A  59     6910   8042   6325     -3  -1302  -1509  A    C  
ATOM    420  CE2 PHE A  59      36.936 -13.041 -20.572  1.00 60.30      A    C  
ANISOU  420  CE2 PHE A  59     7189   8580   7140   -179  -1231  -1342  A    C  
ATOM    421  CZ  PHE A  59      38.133 -13.099 -21.283  1.00 59.68      A    C  
ANISOU  421  CZ  PHE A  59     7267   8473   6935    -42  -1191  -1390  A    C  
ATOM    422  N   PRO A  60      34.811 -16.945 -21.049  1.00 64.43      A    N  
ANISOU  422  N   PRO A  60     7859   8828   7791   -738  -1673  -1684  A    N  
ATOM    423  CA  PRO A  60      34.634 -17.590 -19.741  1.00 60.80      A    C  
ANISOU  423  CA  PRO A  60     7377   8224   7497   -891  -1611  -1631  A    C  
ATOM    424  C   PRO A  60      34.285 -16.605 -18.643  1.00 63.88      A    C  
ANISOU  424  C   PRO A  60     7561   8718   7991   -884  -1476  -1466  A    C  
ATOM    425  O   PRO A  60      35.026 -15.627 -18.385  1.00 67.89      A    O  
ANISOU  425  O   PRO A  60     8057   9275   8463   -713  -1342  -1386  A    O  
ATOM    426  CB  PRO A  60      35.991 -18.233 -19.478  1.00 60.85      A    C  
ANISOU  426  CB  PRO A  60     7610   8025   7482   -791  -1522  -1672  A    C  
ATOM    427  CG  PRO A  60      36.549 -18.463 -20.848  1.00 68.58      A    C  
ANISOU  427  CG  PRO A  60     8758   9006   8293   -664  -1596  -1811  A    C  
ATOM    428  CD  PRO A  60      36.110 -17.274 -21.652  1.00 67.54      A    C  
ANISOU  428  CD  PRO A  60     8483   9117   8060   -576  -1628  -1773  A    C  
ATOM    429  N   ILE A  61      33.153 -16.852 -17.997  1.00 67.26      A    N  
ANISOU  429  N   ILE A  61     7829   9180   8543  -1075  -1506  -1417  A    N  
ATOM    430  CA  ILE A  61      32.716 -16.046 -16.865  1.00 63.04      A    C  
ANISOU  430  CA  ILE A  61     7109   8734   8108  -1081  -1365  -1272  A    C  
ATOM    431  C   ILE A  61      33.769 -16.035 -15.759  1.00 60.69      A    C  
ANISOU  431  C   ILE A  61     6930   8293   7836  -1022  -1199  -1208  A    C  
ATOM    432  O   ILE A  61      33.911 -15.080 -15.000  1.00 59.89      A    O  
ANISOU  432  O   ILE A  61     6748   8254   7752   -939  -1059  -1104  A    O  
ATOM    433  CB  ILE A  61      31.342 -16.553 -16.333  1.00 60.74      A    C  
ANISOU  433  CB  ILE A  61     6633   8494   7949  -1321  -1417  -1235  A    C  
ATOM    434  CG1 ILE A  61      30.778 -15.602 -15.291  1.00 59.58      A    C  
ANISOU  434  CG1 ILE A  61     6275   8476   7885  -1296  -1259  -1091  A    C  
ATOM    435  CG2 ILE A  61      31.498 -17.865 -15.634  1.00 66.89      A    C  
ANISOU  435  CG2 ILE A  61     7551   9056   8805  -1511  -1421  -1259  A    C  
ATOM    436  CD1 ILE A  61      29.258 -15.634 -15.299  1.00 63.32      A    C  
ANISOU  436  CD1 ILE A  61     6479   9123   8456  -1452  -1330  -1050  A    C  
ATOM    437  N   THR A  62      34.553 -17.099 -15.719  1.00 68.24      A    N  
ANISOU  437  N   THR A  62     8093   9050   8785  -1053  -1225  -1276  A    N  
ATOM    438  CA  THR A  62      35.637 -17.239 -14.774  1.00 68.55      A    C  
ANISOU  438  CA  THR A  62     8255   8950   8839   -993  -1101  -1219  A    C  
ATOM    439  C   THR A  62      36.747 -16.238 -15.042  1.00 66.61      A    C  
ANISOU  439  C   THR A  62     8045   8765   8496   -766  -1013  -1193  A    C  
ATOM    440  O   THR A  62      37.317 -15.647 -14.119  1.00 59.43      A    O  
ANISOU  440  O   THR A  62     7125   7853   7601   -712   -888  -1096  A    O  
ATOM    441  CB  THR A  62      36.225 -18.668 -14.908  1.00 71.98      A    C  
ANISOU  441  CB  THR A  62     8913   9154   9281  -1046  -1172  -1309  A    C  
ATOM    442  CG2 THR A  62      37.610 -18.715 -14.364  1.00 82.10      A    C  
ANISOU  442  CG2 THR A  62    10329  10323  10540   -903  -1072  -1267  A    C  
ATOM    443  OG1 THR A  62      35.404 -19.518 -14.147  1.00 83.45      A    O  
ANISOU  443  OG1 THR A  62    10348  10511  10846  -1274  -1200  -1278  A    O  
ATOM    444  N   ALA A  63      37.060 -16.066 -16.326  1.00 65.26      A    N  
ANISOU  444  N   ALA A  63     7925   8653   8218   -647  -1084  -1279  A    N  
ATOM    445  CA  ALA A  63      38.050 -15.086 -16.736  1.00 61.51      A    C  
ANISOU  445  CA  ALA A  63     7471   8254   7643   -448  -1004  -1249  A    C  
ATOM    446  C   ALA A  63      37.565 -13.651 -16.491  1.00 63.76      A    C  
ANISOU  446  C   ALA A  63     7592   8702   7929   -399   -931  -1144  A    C  
ATOM    447  O   ALA A  63      38.345 -12.798 -16.059  1.00 61.13      A    O  
ANISOU  447  O   ALA A  63     7266   8386   7573   -299   -818  -1067  A    O  
ATOM    448  CB  ALA A  63      38.460 -15.294 -18.193  1.00 59.52      A    C  
ANISOU  448  CB  ALA A  63     7324   8031   7260   -337  -1086  -1363  A    C  
ATOM    449  N   LEU A  64      36.283 -13.385 -16.736  1.00 61.70      A    N  
ANISOU  449  N   LEU A  64     7184   8556   7700   -470   -997  -1139  A    N  
ATOM    450  CA  LEU A  64      35.727 -12.069 -16.435  1.00 57.30      A    C  
ANISOU  450  CA  LEU A  64     6473   8137   7159   -407   -921  -1038  A    C  
ATOM    451  C   LEU A  64      35.918 -11.744 -14.978  1.00 61.68      A    C  
ANISOU  451  C   LEU A  64     7010   8633   7792   -442   -774   -946  A    C  
ATOM    452  O   LEU A  64      36.301 -10.630 -14.629  1.00 64.55      A    O  
ANISOU  452  O   LEU A  64     7364   9033   8128   -339   -667   -873  A    O  
ATOM    453  CB  LEU A  64      34.243 -12.000 -16.770  1.00 51.02      A    C  
ANISOU  453  CB  LEU A  64     5494   7477   6413   -485  -1016  -1037  A    C  
ATOM    454  CG  LEU A  64      33.953 -12.083 -18.270  1.00 62.79      A    C  
ANISOU  454  CG  LEU A  64     6990   9065   7802   -441  -1178  -1116  A    C  
ATOM    455  CD1 LEU A  64      32.450 -12.110 -18.486  1.00 73.65      A    C  
ANISOU  455  CD1 LEU A  64     8155  10584   9242   -543  -1290  -1104  A    C  
ATOM    456  CD2 LEU A  64      34.636 -10.967 -19.043  1.00 57.46      A    C  
ANISOU  456  CD2 LEU A  64     6366   8465   7000   -236  -1139  -1083  A    C  
ATOM    457  N   ARG A  65      35.649 -12.715 -14.126  1.00 59.03      A    N  
ANISOU  457  N   ARG A  65     6686   8199   7541   -597   -771   -948  A    N  
ATOM    458  CA  ARG A  65      35.760 -12.511 -12.686  1.00 59.93      A    C  
ANISOU  458  CA  ARG A  65     6796   8262   7713   -648   -636   -860  A    C  
ATOM    459  C   ARG A  65      37.197 -12.121 -12.299  1.00 61.77      A    C  
ANISOU  459  C   ARG A  65     7168   8417   7884   -545   -555   -828  A    C  
ATOM    460  O   ARG A  65      37.430 -11.154 -11.566  1.00 55.15      A    O  
ANISOU  460  O   ARG A  65     6318   7605   7032   -497   -443   -756  A    O  
ATOM    461  CB  ARG A  65      35.372 -13.810 -11.972  1.00 61.61      A    C  
ANISOU  461  CB  ARG A  65     7035   8362   8011   -840   -663   -867  A    C  
ATOM    462  CG  ARG A  65      35.132 -13.673 -10.495  1.00 69.21      A    C  
ANISOU  462  CG  ARG A  65     7967   9302   9026   -925   -531   -770  A    C  
ATOM    463  CD  ARG A  65      34.781 -15.049  -9.961  1.00 80.02      A    C  
ANISOU  463  CD  ARG A  65     9383  10549  10471  -1121   -574   -771  A    C  
ATOM    464  NE  ARG A  65      35.772 -16.008 -10.443  1.00108.91      A    N  
ANISOU  464  NE  ARG A  65    13230  14047  14103  -1100   -666   -840  A    N  
ATOM    465  CZ  ARG A  65      35.898 -17.256 -10.008  1.00103.31      A    C  
ANISOU  465  CZ  ARG A  65    12640  13168  13442  -1228   -706   -842  A    C  
ATOM    466  NH1 ARG A  65      35.086 -17.712  -9.056  1.00 88.17      A    N1+
ANISOU  466  NH1 ARG A  65    10671  11228  11601  -1413   -662   -771  A    N1+
ATOM    467  NH2 ARG A  65      36.820 -18.055 -10.545  1.00 95.21      A    N  
ANISOU  467  NH2 ARG A  65    11790  11995  12389  -1167   -784   -912  A    N  
ATOM    468  N   GLU A  66      38.157 -12.893 -12.815  1.00 58.55      A    N  
ANISOU  468  N   GLU A  66     6892   7915   7437   -510   -616   -887  A    N  
ATOM    469  CA  GLU A  66      39.560 -12.673 -12.493  1.00 54.09      A    C  
ANISOU  469  CA  GLU A  66     6433   7292   6825   -419   -555   -852  A    C  
ATOM    470  C   GLU A  66      40.025 -11.297 -12.971  1.00 61.53      A    C  
ANISOU  470  C   GLU A  66     7346   8342   7690   -284   -499   -816  A    C  
ATOM    471  O   GLU A  66      40.651 -10.535 -12.233  1.00 59.14      A    O  
ANISOU  471  O   GLU A  66     7062   8037   7371   -260   -410   -743  A    O  
ATOM    472  CB  GLU A  66      40.429 -13.756 -13.120  1.00 55.17      A    C  
ANISOU  472  CB  GLU A  66     6696   7327   6936   -375   -626   -927  A    C  
ATOM    473  CG  GLU A  66      41.914 -13.587 -12.836  1.00 61.00      A    C  
ANISOU  473  CG  GLU A  66     7510   8031   7635   -271   -568   -881  A    C  
ATOM    474  CD  GLU A  66      42.753 -14.750 -13.328  1.00 81.82      A    C  
ANISOU  474  CD  GLU A  66    10266  10558  10261   -206   -621   -948  A    C  
ATOM    475  OE1 GLU A  66      42.178 -15.704 -13.900  1.00 92.27      A    O  
ANISOU  475  OE1 GLU A  66    11645  11810  11602   -250   -706  -1044  A    O  
ATOM    476  OE2 GLU A  66      43.991 -14.737 -13.109  1.00 91.73      A    O1-
ANISOU  476  OE2 GLU A  66    11561  11794  11495   -111   -578   -906  A    O1-
ATOM    477  N   ILE A  67      39.710 -10.992 -14.225  1.00 62.78      A    N  
ANISOU  477  N   ILE A  67     7470   8589   7791   -207   -559   -866  A    N  
ATOM    478  CA  ILE A  67      40.011  -9.697 -14.800  1.00 55.27      A    C  
ANISOU  478  CA  ILE A  67     6499   7736   6765    -86   -514   -823  A    C  
ATOM    479  C   ILE A  67      39.430  -8.569 -13.946  1.00 52.11      A    C  
ANISOU  479  C   ILE A  67     6027   7371   6401    -96   -422   -739  A    C  
ATOM    480  O   ILE A  67      40.126  -7.587 -13.641  1.00 60.30      A    O  
ANISOU  480  O   ILE A  67     7103   8406   7399    -41   -339   -677  A    O  
ATOM    481  CB  ILE A  67      39.477  -9.612 -16.248  1.00 53.88      A    C  
ANISOU  481  CB  ILE A  67     6293   7659   6519    -17   -609   -881  A    C  
ATOM    482  CG1 ILE A  67      40.273 -10.574 -17.135  1.00 58.51      A    C  
ANISOU  482  CG1 ILE A  67     6989   8203   7035     24   -674   -973  A    C  
ATOM    483  CG2 ILE A  67      39.593  -8.193 -16.785  1.00 45.69      A    C  
ANISOU  483  CG2 ILE A  67     5232   6718   5408    101   -561   -813  A    C  
ATOM    484  CD1 ILE A  67      39.772 -10.679 -18.554  1.00 65.29      A    C  
ANISOU  484  CD1 ILE A  67     7853   9153   7801     75   -782  -1049  A    C  
ATOM    485  N   LYS A  68      38.169  -8.708 -13.542  1.00 49.00      A    N  
ANISOU  485  N   LYS A  68     5529   7008   6079   -168   -430   -738  A    N  
ATOM    486  CA  LYS A  68      37.536  -7.680 -12.727  1.00 56.99      A    C  
ANISOU  486  CA  LYS A  68     6473   8055   7124   -156   -325   -668  A    C  
ATOM    487  C   LYS A  68      38.344  -7.479 -11.446  1.00 67.20      A    C  
ANISOU  487  C   LYS A  68     7862   9254   8416   -202   -220   -620  A    C  
ATOM    488  O   LYS A  68      38.629  -6.348 -11.046  1.00 69.93      A    O  
ANISOU  488  O   LYS A  68     8246   9596   8728   -146   -131   -571  A    O  
ATOM    489  CB  LYS A  68      36.075  -8.038 -12.386  1.00 56.37      A    C  
ANISOU  489  CB  LYS A  68     6245   8037   7133   -237   -337   -669  A    C  
ATOM    490  CG  LYS A  68      35.448  -7.071 -11.385  1.00 68.39      A    C  
ANISOU  490  CG  LYS A  68     7706   9588   8690   -213   -198   -601  A    C  
ATOM    491  CD  LYS A  68      34.128  -7.576 -10.795  1.00 78.76      A    C  
ANISOU  491  CD  LYS A  68     8861  10963  10098   -315   -176   -589  A    C  
ATOM    492  CE  LYS A  68      34.372  -8.772  -9.873  1.00 85.89      A    C  
ANISOU  492  CE  LYS A  68     9827  11768  11038   -488   -167   -597  A    C  
ATOM    493  NZ  LYS A  68      33.129  -9.417  -9.361  1.00 80.09      A    N1+
ANISOU  493  NZ  LYS A  68     8940  11093  10397   -622   -150   -578  A    N1+
ATOM    494  N   ILE A  69      38.736  -8.589 -10.826  1.00 65.96      A    N  
ANISOU  494  N   ILE A  69     7759   9013   8289   -306   -241   -635  A    N  
ATOM    495  CA  ILE A  69      39.479  -8.547  -9.560  1.00 63.80      A    C  
ANISOU  495  CA  ILE A  69     7576   8659   8005   -364   -164   -585  A    C  
ATOM    496  C   ILE A  69      40.906  -7.986  -9.717  1.00 64.02      A    C  
ANISOU  496  C   ILE A  69     7697   8664   7962   -296   -154   -560  A    C  
ATOM    497  O   ILE A  69      41.340  -7.161  -8.905  1.00 60.93      A    O  
ANISOU  497  O   ILE A  69     7359   8253   7537   -308    -79   -509  A    O  
ATOM    498  CB  ILE A  69      39.473  -9.933  -8.879  1.00 57.03      A    C  
ANISOU  498  CB  ILE A  69     6754   7714   7199   -489   -200   -591  A    C  
ATOM    499  CG1 ILE A  69      38.067 -10.213  -8.332  1.00 56.64      A    C  
ANISOU  499  CG1 ILE A  69     6605   7696   7218   -591   -165   -582  A    C  
ATOM    500  CG2 ILE A  69      40.505 -10.005  -7.777  1.00 51.79      A    C  
ANISOU  500  CG2 ILE A  69     6201   6973   6504   -529   -158   -534  A    C  
ATOM    501  CD1 ILE A  69      37.697 -11.643  -8.122  1.00 51.58      A    C  
ANISOU  501  CD1 ILE A  69     5972   6983   6642   -726   -228   -598  A    C  
ATOM    502  N   LEU A  70      41.605  -8.403 -10.779  1.00 57.01      A    N  
ANISOU  502  N   LEU A  70     6827   7787   7046   -229   -227   -597  A    N  
ATOM    503  CA  LEU A  70      42.951  -7.890 -11.052  1.00 42.46      A    C  
ANISOU  503  CA  LEU A  70     5039   5951   5141   -165   -212   -564  A    C  
ATOM    504  C   LEU A  70      42.908  -6.372 -11.292  1.00 52.72      A    C  
ANISOU  504  C   LEU A  70     6335   7303   6392   -109   -149   -521  A    C  
ATOM    505  O   LEU A  70      43.807  -5.637 -10.888  1.00 57.10      A    O  
ANISOU  505  O   LEU A  70     6942   7843   6908   -119   -104   -467  A    O  
ATOM    506  CB  LEU A  70      43.548  -8.589 -12.263  1.00 41.25      A    C  
ANISOU  506  CB  LEU A  70     4895   5819   4958    -84   -281   -617  A    C  
ATOM    507  CG  LEU A  70      44.511  -9.745 -12.062  1.00 50.91      A    C  
ANISOU  507  CG  LEU A  70     6169   6974   6198    -84   -317   -630  A    C  
ATOM    508  CD1 LEU A  70      44.657 -10.124 -10.597  1.00 45.83      A    C  
ANISOU  508  CD1 LEU A  70     5559   6250   5604   -187   -299   -576  A    C  
ATOM    509  CD2 LEU A  70      44.171 -10.939 -12.949  1.00 57.76      A    C  
ANISOU  509  CD2 LEU A  70     7059   7810   7078    -52   -397   -727  A    C  
ATOM    510  N   GLN A  71      41.855  -5.904 -11.959  1.00 55.45      A    N  
ANISOU  510  N   GLN A  71     6622   7705   6741    -54   -154   -539  A    N  
ATOM    511  CA  GLN A  71      41.727  -4.481 -12.206  1.00 51.93      A    C  
ANISOU  511  CA  GLN A  71     6189   7287   6254     15    -96   -491  A    C  
ATOM    512  C   GLN A  71      41.485  -3.680 -10.937  1.00 53.09      A    C  
ANISOU  512  C   GLN A  71     6379   7374   6416    -33      0   -452  A    C  
ATOM    513  O   GLN A  71      41.991  -2.575 -10.817  1.00 59.06      A    O  
ANISOU  513  O   GLN A  71     7211   8100   7128    -12     55   -407  A    O  
ATOM    514  CB  GLN A  71      40.611  -4.220 -13.212  1.00 41.46      A    C  
ANISOU  514  CB  GLN A  71     4782   6042   4929    103   -137   -510  A    C  
ATOM    515  CG  GLN A  71      41.064  -4.498 -14.622  1.00 48.52      A    C  
ANISOU  515  CG  GLN A  71     5680   6999   5756    175   -215   -536  A    C  
ATOM    516  CD  GLN A  71      39.965  -4.826 -15.549  1.00 53.45      A    C  
ANISOU  516  CD  GLN A  71     6220   7707   6380    220   -304   -580  A    C  
ATOM    517  NE2 GLN A  71      40.340  -5.117 -16.776  1.00 50.32      A    N  
ANISOU  517  NE2 GLN A  71     5850   7367   5902    280   -374   -614  A    N  
ATOM    518  OE1 GLN A  71      38.792  -4.893 -15.170  1.00 67.42      A    O  
ANISOU  518  OE1 GLN A  71     7897   9500   8217    195   -314   -586  A    O  
ATOM    519  N   LEU A  72      40.814  -4.298  -9.966  1.00 53.28      A    N  
ANISOU  519  N   LEU A  72     6375   7373   6492   -110     22   -469  A    N  
ATOM    520  CA  LEU A  72      40.504  -3.649  -8.710  1.00 53.44      A    C  
ANISOU  520  CA  LEU A  72     6448   7344   6510   -154    125   -444  A    C  
ATOM    521  C   LEU A  72      41.729  -3.556  -7.802  1.00 53.47      A    C  
ANISOU  521  C   LEU A  72     6574   7277   6464   -243    142   -415  A    C  
ATOM    522  O   LEU A  72      41.999  -2.491  -7.251  1.00 52.69      A    O  
ANISOU  522  O   LEU A  72     6570   7132   6317   -250    209   -391  A    O  
ATOM    523  CB  LEU A  72      39.399  -4.404  -7.957  1.00 48.66      A    C  
ANISOU  523  CB  LEU A  72     5767   6752   5966   -219    155   -461  A    C  
ATOM    524  CG  LEU A  72      39.069  -3.771  -6.584  1.00 45.43      A    C  
ANISOU  524  CG  LEU A  72     5428   6299   5534   -259    284   -440  A    C  
ATOM    525  CD1 LEU A  72      38.319  -2.460  -6.767  1.00 50.95      A    C  
ANISOU  525  CD1 LEU A  72     6114   7015   6227   -135    373   -434  A    C  
ATOM    526  CD2 LEU A  72      38.286  -4.738  -5.706  1.00 53.09      A    C  
ANISOU  526  CD2 LEU A  72     6340   7282   6549   -360    317   -442  A    C  
ATOM    527  N   LEU A  73      42.474  -4.652  -7.703  1.00 54.72      A    N  
ANISOU  527  N   LEU A  73     6733   7426   6632   -304     71   -417  A    N  
ATOM    528  CA  LEU A  73      43.601  -4.757  -6.780  1.00 53.65      A    C  
ANISOU  528  CA  LEU A  73     6685   7243   6455   -391     63   -378  A    C  
ATOM    529  C   LEU A  73      44.867  -4.054  -7.274  1.00 52.51      A    C  
ANISOU  529  C   LEU A  73     6575   7112   6262   -372     39   -342  A    C  
ATOM    530  O   LEU A  73      45.451  -4.477  -8.263  1.00 62.35      A    O  
ANISOU  530  O   LEU A  73     7769   8404   7517   -314    -14   -345  A    O  
ATOM    531  CB  LEU A  73      43.878  -6.247  -6.520  1.00 52.67      A    C  
ANISOU  531  CB  LEU A  73     6540   7099   6370   -441     -7   -381  A    C  
ATOM    532  CG  LEU A  73      42.658  -6.967  -5.914  1.00 56.64      A    C  
ANISOU  532  CG  LEU A  73     7014   7582   6921   -499     19   -399  A    C  
ATOM    533  CD1 LEU A  73      42.936  -8.425  -5.572  1.00 67.82      A    C  
ANISOU  533  CD1 LEU A  73     8445   8947   8376   -562    -48   -390  A    C  
ATOM    534  CD2 LEU A  73      42.201  -6.232  -4.654  1.00 54.20      A    C  
ANISOU  534  CD2 LEU A  73     6771   7252   6568   -563    123   -375  A    C  
ATOM    535  N   LYS A  74      45.264  -2.976  -6.613  1.00 51.98      A    N  
ANISOU  535  N   LYS A  74     6601   7007   6139   -426     86   -311  A    N  
ATOM    536  CA  LYS A  74      46.529  -2.293  -6.954  1.00 56.82      A    C  
ANISOU  536  CA  LYS A  74     7244   7635   6710   -450     62   -263  A    C  
ATOM    537  C   LYS A  74      47.377  -2.073  -5.706  1.00 61.48      A    C  
ANISOU  537  C   LYS A  74     7922   8187   7248   -586     46   -226  A    C  
ATOM    538  O   LYS A  74      47.096  -1.168  -4.911  1.00 58.13      A    O  
ANISOU  538  O   LYS A  74     7616   7697   6774   -647    101   -234  A    O  
ATOM    539  CB  LYS A  74      46.265  -0.959  -7.653  1.00 56.84      A    C  
ANISOU  539  CB  LYS A  74     7289   7621   6687   -392    117   -255  A    C  
ATOM    540  CG  LYS A  74      45.577  -1.135  -9.001  1.00 72.92      A    C  
ANISOU  540  CG  LYS A  74     9236   9716   8754   -256    110   -277  A    C  
ATOM    541  CD  LYS A  74      46.298  -2.176  -9.834  1.00 71.68      A    C  
ANISOU  541  CD  LYS A  74     8988   9637   8609   -223     38   -279  A    C  
ATOM    542  CE  LYS A  74      45.523  -2.548 -11.084  1.00 59.41      A    C  
ANISOU  542  CE  LYS A  74     7361   8141   7068   -103     14   -320  A    C  
ATOM    543  NZ  LYS A  74      46.308  -3.521 -11.887  1.00 62.95      A    N1+
ANISOU  543  NZ  LYS A  74     7755   8652   7510    -63    -42   -335  A    N1+
ATOM    544  N   HIS A  75      48.419  -2.878  -5.527  1.00 56.39      A    N  
ANISOU  544  N   HIS A  75     7229   7586   6610   -628    -32   -186  A    N  
ATOM    545  CA  HIS A  75      49.157  -2.853  -4.279  1.00 53.36      A    C  
ANISOU  545  CA  HIS A  75     6915   7183   6173   -760    -74   -144  A    C  
ATOM    546  C   HIS A  75      50.565  -3.452  -4.456  1.00 61.14      A    C  
ANISOU  546  C   HIS A  75     7807   8248   7174   -775   -169    -76  A    C  
ATOM    547  O   HIS A  75      50.746  -4.371  -5.259  1.00 66.85      A    O  
ANISOU  547  O   HIS A  75     8425   9018   7955   -669   -195    -78  A    O  
ATOM    548  CB  HIS A  75      48.350  -3.607  -3.224  1.00 55.41      A    C  
ANISOU  548  CB  HIS A  75     7227   7396   6428   -794    -60   -167  A    C  
ATOM    549  CG  HIS A  75      48.968  -3.597  -1.866  1.00 56.17      A    C  
ANISOU  549  CG  HIS A  75     7419   7474   6447   -930   -105   -124  A    C  
ATOM    550  CD2 HIS A  75      48.778  -2.782  -0.805  1.00 56.77      A    C  
ANISOU  550  CD2 HIS A  75     7644   7497   6427  -1034    -65   -138  A    C  
ATOM    551  ND1 HIS A  75      49.912  -4.523  -1.476  1.00 57.71      A    N  
ANISOU  551  ND1 HIS A  75     7569   7710   6647   -963   -209    -59  A    N  
ATOM    552  CE1 HIS A  75      50.286  -4.270  -0.237  1.00 70.64      A    C  
ANISOU  552  CE1 HIS A  75     9314   9333   8192  -1093   -245    -26  A    C  
ATOM    553  NE2 HIS A  75      49.596  -3.231   0.207  1.00 66.02      A    N  
ANISOU  553  NE2 HIS A  75     8858   8688   7537  -1144   -156    -81  A    N  
ATOM    554  N   GLU A  76      51.551  -2.921  -3.723  1.00 57.76      A    N  
ANISOU  554  N   GLU A  76     7416   7838   6690   -902   -220    -18  A    N  
ATOM    555  CA  GLU A  76      52.931  -3.370  -3.852  1.00 53.55      A    C  
ANISOU  555  CA  GLU A  76     6766   7406   6175   -917   -310     62  A    C  
ATOM    556  C   GLU A  76      53.109  -4.882  -3.727  1.00 60.37      A    C  
ANISOU  556  C   GLU A  76     7551   8292   7093   -830   -369     81  A    C  
ATOM    557  O   GLU A  76      54.016  -5.450  -4.313  1.00 61.49      A    O  
ANISOU  557  O   GLU A  76     7564   8519   7281   -752   -411    128  A    O  
ATOM    558  CB  GLU A  76      53.860  -2.658  -2.860  1.00 63.25      A    C  
ANISOU  558  CB  GLU A  76     8046   8654   7331  -1097   -382    124  A    C  
ATOM    559  CG  GLU A  76      54.687  -1.535  -3.494  1.00 93.22      A    C  
ANISOU  559  CG  GLU A  76    11802  12502  11114  -1170   -377    167  A    C  
ATOM    560  CD  GLU A  76      56.071  -1.999  -3.919  1.00124.46      A    C  
ANISOU  560  CD  GLU A  76    15563  16610  15114  -1160   -452    264  A    C  
ATOM    561  OE1 GLU A  76      56.853  -2.395  -3.028  1.00119.65      A    O  
ANISOU  561  OE1 GLU A  76    14914  16059  14487  -1244   -560    329  A    O  
ATOM    562  OE2 GLU A  76      56.390  -1.956  -5.135  1.00130.83      A    O1-
ANISOU  562  OE2 GLU A  76    16252  17490  15966  -1063   -402    282  A    O1-
ATOM    563  N   ASN A  77      52.255  -5.528  -2.929  1.00 56.41      A    N  
ANISOU  563  N   ASN A  77     7135   7712   6585   -842   -365     51  A    N  
ATOM    564  CA  ASN A  77      52.363  -6.959  -2.706  1.00 54.51      A    C  
ANISOU  564  CA  ASN A  77     6857   7458   6393   -775   -423     77  A    C  
ATOM    565  C   ASN A  77      51.347  -7.815  -3.458  1.00 62.00      A    C  
ANISOU  565  C   ASN A  77     7794   8349   7414   -659   -376      3  A    C  
ATOM    566  O   ASN A  77      51.092  -8.960  -3.099  1.00 65.99      A    O  
ANISOU  566  O   ASN A  77     8321   8796   7955   -634   -409     11  A    O  
ATOM    567  CB  ASN A  77      52.366  -7.259  -1.201  1.00 56.76      A    C  
ANISOU  567  CB  ASN A  77     7245   7703   6614   -892   -478    127  A    C  
ATOM    568  CG  ASN A  77      53.457  -6.498  -0.480  1.00 69.57      A    C  
ANISOU  568  CG  ASN A  77     8878   9395   8159  -1019   -556    199  A    C  
ATOM    569  ND2 ASN A  77      54.706  -6.703  -0.898  1.00 80.92      A    N  
ANISOU  569  ND2 ASN A  77    10174  10936   9636   -979   -635    273  A    N  
ATOM    570  OD1 ASN A  77      53.183  -5.684   0.398  1.00 85.72      A    O  
ANISOU  570  OD1 ASN A  77    11053  11408  10108  -1154   -541    184  A    O  
ATOM    571  N   VAL A  78      50.765  -7.233  -4.496  1.00 66.31      A    N  
ANISOU  571  N   VAL A  78     8314   8906   7975   -600   -307    -62  A    N  
ATOM    572  CA  VAL A  78      49.857  -7.983  -5.350  1.00 60.29      A    C  
ANISOU  572  CA  VAL A  78     7528   8106   7272   -500   -282   -136  A    C  
ATOM    573  C   VAL A  78      50.327  -7.843  -6.783  1.00 65.05      A    C  
ANISOU  573  C   VAL A  78     8044   8780   7890   -380   -272   -161  A    C  
ATOM    574  O   VAL A  78      50.699  -6.767  -7.237  1.00 70.32      A    O  
ANISOU  574  O   VAL A  78     8689   9509   8521   -388   -238   -143  A    O  
ATOM    575  CB  VAL A  78      48.419  -7.507  -5.218  1.00 54.01      A    C  
ANISOU  575  CB  VAL A  78     6783   7266   6470   -536   -209   -196  A    C  
ATOM    576  CG1 VAL A  78      47.534  -8.251  -6.190  1.00 53.19      A    C  
ANISOU  576  CG1 VAL A  78     6635   7146   6428   -450   -207   -269  A    C  
ATOM    577  CG2 VAL A  78      47.930  -7.689  -3.789  1.00 51.92      A    C  
ANISOU  577  CG2 VAL A  78     6608   6942   6177   -650   -196   -171  A    C  
ATOM    578  N   VAL A  79      50.362  -8.974  -7.464  1.00 66.60      A    N  
ANISOU  578  N   VAL A  79     8209   8961   8135   -273   -301   -198  A    N  
ATOM    579  CA  VAL A  79      50.827  -9.022  -8.839  1.00 58.05      A    C  
ANISOU  579  CA  VAL A  79     7058   7947   7048   -144   -285   -230  A    C  
ATOM    580  C   VAL A  79      50.026  -8.012  -9.652  1.00 50.04      A    C  
ANISOU  580  C   VAL A  79     6048   6965   5997   -138   -229   -276  A    C  
ATOM    581  O   VAL A  79      48.887  -7.729  -9.334  1.00 51.67      A    O  
ANISOU  581  O   VAL A  79     6299   7123   6209   -193   -211   -310  A    O  
ATOM    582  CB  VAL A  79      50.684 -10.455  -9.405  1.00 58.84      A    C  
ANISOU  582  CB  VAL A  79     7172   7988   7196    -33   -321   -296  A    C  
ATOM    583  CG1 VAL A  79      49.228 -10.736  -9.777  1.00 47.84      A    C  
ANISOU  583  CG1 VAL A  79     5829   6527   5818    -52   -320   -390  A    C  
ATOM    584  CG2 VAL A  79      51.620 -10.638 -10.569  1.00 72.83      A    C  
ANISOU  584  CG2 VAL A  79     8879   9843   8950    114   -302   -308  A    C  
ATOM    585  N   ASN A  80      50.649  -7.435 -10.658  1.00 59.04      A    N  
ANISOU  585  N   ASN A  80     7138   8197   7098    -70   -197   -262  A    N  
ATOM    586  CA  ASN A  80      50.049  -6.329 -11.418  1.00 53.24      A    C  
ANISOU  586  CA  ASN A  80     6415   7495   6317    -62   -148   -276  A    C  
ATOM    587  C   ASN A  80      49.669  -6.670 -12.852  1.00 56.08      A    C  
ANISOU  587  C   ASN A  80     6759   7900   6647     63   -144   -345  A    C  
ATOM    588  O   ASN A  80      50.539  -6.934 -13.686  1.00 59.87      A    O  
ANISOU  588  O   ASN A  80     7198   8455   7095    153   -128   -339  A    O  
ATOM    589  CB  ASN A  80      51.028  -5.154 -11.452  1.00 53.19      A    C  
ANISOU  589  CB  ASN A  80     6386   7557   6267   -113   -109   -187  A    C  
ATOM    590  CG  ASN A  80      50.530  -4.016 -12.308  1.00 55.71      A    C  
ANISOU  590  CG  ASN A  80     6734   7898   6534    -92    -57   -183  A    C  
ATOM    591  ND2 ASN A  80      51.205  -3.765 -13.429  1.00 54.80      A    N  
ANISOU  591  ND2 ASN A  80     6572   7877   6370    -22    -24   -153  A    N  
ATOM    592  OD1 ASN A  80      49.494  -3.427 -12.012  1.00 68.96      A    O  
ANISOU  592  OD1 ASN A  80     8475   9511   8215   -121    -42   -206  A    O  
ATOM    593  N   LEU A  81      48.376  -6.616 -13.138  1.00 56.71      A    N  
ANISOU  593  N   LEU A  81     6868   7946   6730     70   -155   -407  A    N  
ATOM    594  CA  LEU A  81      47.913  -6.877 -14.494  1.00 56.53      A    C  
ANISOU  594  CA  LEU A  81     6842   7973   6662    174   -172   -475  A    C  
ATOM    595  C   LEU A  81      48.124  -5.604 -15.295  1.00 59.52      A    C  
ANISOU  595  C   LEU A  81     7218   8432   6964    209   -120   -419  A    C  
ATOM    596  O   LEU A  81      47.559  -4.573 -14.959  1.00 60.16      A    O  
ANISOU  596  O   LEU A  81     7320   8492   7047    162    -95   -378  A    O  
ATOM    597  CB  LEU A  81      46.439  -7.291 -14.497  1.00 54.13      A    C  
ANISOU  597  CB  LEU A  81     6548   7623   6395    153   -222   -550  A    C  
ATOM    598  CG  LEU A  81      45.799  -7.552 -15.863  1.00 47.06      A    C  
ANISOU  598  CG  LEU A  81     5653   6783   5443    239   -268   -626  A    C  
ATOM    599  CD1 LEU A  81      46.327  -8.823 -16.520  1.00 61.77      A    C  
ANISOU  599  CD1 LEU A  81     7550   8634   7285    307   -309   -708  A    C  
ATOM    600  CD2 LEU A  81      44.286  -7.600 -15.740  1.00 42.23      A    C  
ANISOU  600  CD2 LEU A  81     5015   6154   4874    192   -318   -668  A    C  
ATOM    601  N   ILE A  82      48.951  -5.681 -16.333  1.00 66.27      A    N  
ANISOU  601  N   ILE A  82     8056   9374   7749    296    -95   -411  A    N  
ATOM    602  CA  ILE A  82      49.265  -4.527 -17.136  1.00 54.22      A    C  
ANISOU  602  CA  ILE A  82     6533   7926   6139    322    -39   -340  A    C  
ATOM    603  C   ILE A  82      48.128  -4.230 -18.116  1.00 56.00      A    C  
ANISOU  603  C   ILE A  82     6794   8176   6304    390    -70   -382  A    C  
ATOM    604  O   ILE A  82      47.675  -3.109 -18.225  1.00 56.79      A    O  
ANISOU  604  O   ILE A  82     6921   8273   6382    378    -49   -322  A    O  
ATOM    605  CB  ILE A  82      50.559  -4.706 -17.942  1.00 48.05      A    C  
ANISOU  605  CB  ILE A  82     5711   7252   5292    393     15   -306  A    C  
ATOM    606  CG1 ILE A  82      51.746  -4.844 -17.026  1.00 57.70      A    C  
ANISOU  606  CG1 ILE A  82     6868   8480   6574    329     38   -239  A    C  
ATOM    607  CG2 ILE A  82      50.744  -3.528 -18.874  1.00 44.47      A    C  
ANISOU  607  CG2 ILE A  82     5275   6879   4741    411     75   -226  A    C  
ATOM    608  CD1 ILE A  82      52.928  -5.540 -17.656  1.00 55.68      A    C  
ANISOU  608  CD1 ILE A  82     6540   8328   6286    431     83   -233  A    C  
ATOM    609  N   GLU A  83      47.687  -5.250 -18.830  1.00 59.79      A    N  
ANISOU  609  N   GLU A  83     7283   8677   6756    463   -128   -484  A    N  
ATOM    610  CA  GLU A  83      46.746  -5.077 -19.923  1.00 65.30      A    C  
ANISOU  610  CA  GLU A  83     8008   9429   7373    531   -178   -525  A    C  
ATOM    611  C   GLU A  83      46.314  -6.452 -20.402  1.00 74.54      A    C  
ANISOU  611  C   GLU A  83     9199  10589   8532    570   -261   -661  A    C  
ATOM    612  O   GLU A  83      46.874  -7.479 -19.985  1.00 75.13      A    O  
ANISOU  612  O   GLU A  83     9280  10608   8655    565   -262   -714  A    O  
ATOM    613  CB  GLU A  83      47.378  -4.330 -21.101  1.00 53.93      A    C  
ANISOU  613  CB  GLU A  83     6595   8098   5796    610   -121   -461  A    C  
ATOM    614  CG  GLU A  83      48.430  -5.157 -21.847  1.00 61.90      A    C  
ANISOU  614  CG  GLU A  83     7613   9178   6725    692    -81   -506  A    C  
ATOM    615  CD  GLU A  83      48.937  -4.507 -23.134  1.00 74.13      A    C  
ANISOU  615  CD  GLU A  83     9196  10855   8115    774    -17   -448  A    C  
ATOM    616  OE1 GLU A  83      48.172  -3.758 -23.784  1.00 77.78      A    O  
ANISOU  616  OE1 GLU A  83     9699  11351   8501    796    -50   -413  A    O  
ATOM    617  OE2 GLU A  83      50.110  -4.758 -23.504  1.00 66.21      A    O1-
ANISOU  617  OE2 GLU A  83     8172   9925   7058    825     70   -428  A    O1-
ATOM    618  N   ILE A  84      45.303  -6.456 -21.258  1.00 66.57      A    N  
ANISOU  618  N   ILE A  84     8207   9627   7459    605   -340   -713  A    N  
ATOM    619  CA  ILE A  84      44.820  -7.679 -21.897  1.00 53.74      A    C  
ANISOU  619  CA  ILE A  84     6624   7994   5798    626   -438   -852  A    C  
ATOM    620  C   ILE A  84      45.016  -7.586 -23.401  1.00 58.52      A    C  
ANISOU  620  C   ILE A  84     7297   8713   6223    735   -450   -885  A    C  
ATOM    621  O   ILE A  84      44.689  -6.570 -24.018  1.00 81.50      A    O  
ANISOU  621  O   ILE A  84    10202  11711   9050    772   -450   -810  A    O  
ATOM    622  CB  ILE A  84      43.344  -7.941 -21.532  1.00 54.24      A    C  
ANISOU  622  CB  ILE A  84     6641   8023   5944    542   -548   -898  A    C  
ATOM    623  CG1 ILE A  84      43.296  -8.433 -20.082  1.00 52.41      A    C  
ANISOU  623  CG1 ILE A  84     6371   7670   5869    435   -527   -891  A    C  
ATOM    624  CG2 ILE A  84      42.723  -8.962 -22.468  1.00 54.31      A    C  
ANISOU  624  CG2 ILE A  84     6703   8049   5884    549   -673  -1034  A    C  
ATOM    625  CD1 ILE A  84      42.224  -7.762 -19.291  1.00 54.08      A    C  
ANISOU  625  CD1 ILE A  84     6497   7877   6173    362   -533   -832  A    C  
ATOM    626  N   CYS A  85      45.536  -8.640 -24.003  1.00 61.68      A    N  
ANISOU  626  N   CYS A  85     7775   9107   6553    796   -458   -996  A    N  
ATOM    627  CA  CYS A  85      45.896  -8.590 -25.416  1.00 61.86      A    C  
ANISOU  627  CA  CYS A  85     7881   9244   6379    910   -443  -1032  A    C  
ATOM    628  C   CYS A  85      45.140  -9.641 -26.206  1.00 64.91      A    C  
ANISOU  628  C   CYS A  85     8364   9615   6681    917   -577  -1200  A    C  
ATOM    629  O   CYS A  85      44.813 -10.719 -25.694  1.00 71.37      A    O  
ANISOU  629  O   CYS A  85     9209  10311   7597    855   -645  -1305  A    O  
ATOM    630  CB  CYS A  85      47.406  -8.780 -25.587  1.00 70.16      A    C  
ANISOU  630  CB  CYS A  85     8951  10325   7380   1005   -299  -1011  A    C  
ATOM    631  SG  CYS A  85      48.435  -7.368 -25.130  1.00 76.11      A    S  
ANISOU  631  SG  CYS A  85     9605  11151   8162    990   -147   -805  A    S  
ATOM    632  N   ARG A  86      44.834  -9.288 -27.446  1.00 70.32      A    N  
ANISOU  632  N   ARG A  86     9113  10422   7182    981   -622  -1217  A    N  
ATOM    633  CA  ARG A  86      44.213 -10.239 -28.370  1.00 72.99      A    C  
ANISOU  633  CA  ARG A  86     9570  10764   7397    988   -757  -1386  A    C  
ATOM    634  C   ARG A  86      45.263 -10.803 -29.297  1.00 75.25      A    C  
ANISOU  634  C   ARG A  86     9997  11085   7507   1124   -666  -1476  A    C  
ATOM    635  O   ARG A  86      46.460 -10.642 -29.074  1.00 73.70      A    O  
ANISOU  635  O   ARG A  86     9779  10899   7324   1205   -500  -1411  A    O  
ATOM    636  CB  ARG A  86      43.139  -9.551 -29.181  1.00 79.43      A    C  
ANISOU  636  CB  ARG A  86    10375  11705   8099    974   -887  -1356  A    C  
ATOM    637  CG  ARG A  86      43.667  -8.443 -30.066  1.00 79.89      A    C  
ANISOU  637  CG  ARG A  86    10461  11913   7980   1085   -798  -1235  A    C  
ATOM    638  CD  ARG A  86      42.525  -7.683 -30.762  1.00 84.01      A    C  
ANISOU  638  CD  ARG A  86    10960  12552   8405   1080   -942  -1176  A    C  
ATOM    639  NE  ARG A  86      43.054  -6.389 -31.225  1.00111.86      A    N  
ANISOU  639  NE  ARG A  86    14491  16183  11827   1167   -831  -1003  A    N  
ATOM    640  CZ  ARG A  86      43.606  -6.196 -32.421  1.00117.13      A    C  
ANISOU  640  CZ  ARG A  86    15281  16969  12252   1267   -784   -994  A    C  
ATOM    641  NH1 ARG A  86      43.622  -7.188 -33.316  1.00107.08      A    N1+
ANISOU  641  NH1 ARG A  86    14144  15734  10805   1303   -850  -1163  A    N1+
ATOM    642  NH2 ARG A  86      44.099  -4.999 -32.726  1.00115.14      A    N  
ANISOU  642  NH2 ARG A  86    15028  16792  11926   1323   -674   -816  A    N  
ATOM    643  N   THR A  87      44.830 -11.462 -30.358  1.00 83.60      A    N  
ANISOU  643  N   THR A  87    11200  12170   8392   1152   -771  -1625  A    N  
ATOM    644  CA  THR A  87      45.789 -12.230 -31.088  1.00 86.39      A    C  
ANISOU  644  CA  THR A  87    11707  12520   8596   1287   -677  -1745  A    C  
ATOM    645  C   THR A  87      45.655 -11.930 -32.557  1.00 98.75      A    C  
ANISOU  645  C   THR A  87    13400  14244   9875   1368   -707  -1786  A    C  
ATOM    646  O   THR A  87      46.650 -11.621 -33.215  1.00107.28      A    O  
ANISOU  646  O   THR A  87    14530  15431  10801   1505   -546  -1748  A    O  
ATOM    647  CB  THR A  87      45.607 -13.703 -30.770  1.00 86.29      A    C  
ANISOU  647  CB  THR A  87    11806  12317   8661   1249   -755  -1933  A    C  
ATOM    648  CG2 THR A  87      44.624 -14.316 -31.690  1.00 85.94      A    C  
ANISOU  648  CG2 THR A  87    11914  12272   8467   1192   -944  -2101  A    C  
ATOM    649  OG1 THR A  87      46.872 -14.360 -30.822  1.00103.22      A    O  
ANISOU  649  OG1 THR A  87    14031  14407  10779   1400   -594  -1989  A    O  
ATOM    650  N   LYS A  88      44.429 -11.949 -33.069  1.00106.42      A    N  
ANISOU  650  N   LYS A  88    14411  15253  10771   1280   -911  -1846  A    N  
ATOM    651  CA  LYS A  88      44.193 -11.770 -34.509  1.00117.72      A    C  
ANISOU  651  CA  LYS A  88    15988  16837  11903   1347   -977  -1900  A    C  
ATOM    652  C   LYS A  88      44.334 -13.089 -35.252  1.00114.65      A    C  
ANISOU  652  C   LYS A  88    15833  16375  11352   1391  -1024  -2147  A    C  
ATOM    653  O   LYS A  88      43.783 -13.244 -36.329  1.00133.21      A    O  
ANISOU  653  O   LYS A  88    18329  18813  13471   1389  -1157  -2248  A    O  
ATOM    654  CB  LYS A  88      45.167 -10.744 -35.114  1.00117.39      A    C  
ANISOU  654  CB  LYS A  88    15943  16956  11703   1485   -785  -1747  A    C  
ATOM    655  CG  LYS A  88      44.579  -9.886 -36.223  1.00121.27      A    C  
ANISOU  655  CG  LYS A  88    16487  17632  11958   1507   -877  -1672  A    C  
ATOM    656  CD  LYS A  88      43.887  -8.632 -35.672  1.00124.66      A    C  
ANISOU  656  CD  LYS A  88    16733  18104  12529   1435   -934  -1459  A    C  
ATOM    657  CE  LYS A  88      44.061  -7.401 -36.573  1.00117.12      A    C  
ANISOU  657  CE  LYS A  88    15808  17324  11367   1518   -880  -1283  A    C  
ATOM    658  NZ  LYS A  88      42.990  -7.207 -37.601  1.00110.25      A    N1+
ANISOU  658  NZ  LYS A  88    15018  16581  10290   1515  -1094  -1300  A    N1+
ATOM    659  N   GLY A  97      41.079 -17.276 -32.740  1.00 89.60      A    N  
ANISOU  659  N   GLY A  97    12743  12458   8842    705  -1678  -2659  A    N  
ATOM    660  CA  GLY A  97      41.606 -16.074 -32.074  1.00 94.97      A    C  
ANISOU  660  CA  GLY A  97    13206  13245   9631    791  -1506  -2428  A    C  
ATOM    661  C   GLY A  97      41.635 -16.196 -30.548  1.00 98.68      A    C  
ANISOU  661  C   GLY A  97    13520  13573  10401    702  -1444  -2330  A    C  
ATOM    662  O   GLY A  97      40.717 -16.750 -29.981  1.00104.53      A    O  
ANISOU  662  O   GLY A  97    14217  14213  11283    522  -1581  -2370  A    O  
ATOM    663  N   SER A  98      42.684 -15.694 -29.879  1.00 96.68      A    N  
ANISOU  663  N   SER A  98    13180  13316  10235    816  -1241  -2200  A    N  
ATOM    664  CA  SER A  98      42.891 -15.884 -28.439  1.00 85.11      A    C  
ANISOU  664  CA  SER A  98    11602  11712   9024    751  -1172  -2115  A    C  
ATOM    665  C   SER A  98      43.004 -14.599 -27.621  1.00 80.87      A    C  
ANISOU  665  C   SER A  98    10847  11275   8603    746  -1073  -1899  A    C  
ATOM    666  O   SER A  98      42.976 -13.492 -28.158  1.00 87.08      A    O  
ANISOU  666  O   SER A  98    11567  12231   9287    803  -1045  -1800  A    O  
ATOM    667  CB  SER A  98      44.124 -16.752 -28.180  1.00 85.49      A    C  
ANISOU  667  CB  SER A  98    11771  11611   9098    879  -1036  -2179  A    C  
ATOM    668  OG  SER A  98      43.812 -18.120 -28.366  1.00112.39      A    O  
ANISOU  668  OG  SER A  98    15371  14829  12501    825  -1142  -2369  A    O  
ATOM    669  N   ILE A  99      43.141 -14.768 -26.306  1.00 74.29      A    N  
ANISOU  669  N   ILE A  99     9923  10324   7978    676  -1021  -1827  A    N  
ATOM    670  CA  ILE A  99      43.193 -13.636 -25.383  1.00 64.92      A    C  
ANISOU  670  CA  ILE A  99     8555   9201   6910    650   -936  -1641  A    C  
ATOM    671  C   ILE A  99      44.214 -13.906 -24.276  1.00 62.57      A    C  
ANISOU  671  C   ILE A  99     8234   8791   6747    677   -808  -1578  A    C  
ATOM    672  O   ILE A  99      44.321 -15.034 -23.759  1.00 68.91      A    O  
ANISOU  672  O   ILE A  99     9113   9429   7638    639   -833  -1655  A    O  
ATOM    673  CB  ILE A  99      41.829 -13.356 -24.758  1.00 70.30      A    C  
ANISOU  673  CB  ILE A  99     9106   9888   7715    485  -1047  -1595  A    C  
ATOM    674  CG1 ILE A  99      40.858 -12.771 -25.776  1.00 63.05      A    C  
ANISOU  674  CG1 ILE A  99     8156   9126   6673    478  -1169  -1603  A    C  
ATOM    675  CG2 ILE A  99      41.975 -12.398 -23.562  1.00 76.40      A    C  
ANISOU  675  CG2 ILE A  99     9728  10670   8627    459   -939  -1426  A    C  
ATOM    676  CD1 ILE A  99      41.364 -11.499 -26.407  1.00 63.24      A    C  
ANISOU  676  CD1 ILE A  99     8155   9303   6569    613  -1081  -1490  A    C  
ATOM    677  N   TYR A 100      44.977 -12.879 -23.915  1.00 58.55      A    N  
ANISOU  677  N   TYR A 100     7628   8366   6250    736   -681  -1433  A    N  
ATOM    678  CA  TYR A 100      46.101 -13.069 -23.009  1.00 59.40      A    C  
ANISOU  678  CA  TYR A 100     7708   8405   6456    775   -567  -1367  A    C  
ATOM    679  C   TYR A 100      46.066 -12.033 -21.903  1.00 63.77      A    C  
ANISOU  679  C   TYR A 100     8123   8983   7122    691   -516  -1209  A    C  
ATOM    680  O   TYR A 100      45.817 -10.865 -22.153  1.00 70.67      A    O  
ANISOU  680  O   TYR A 100     8934   9968   7949    687   -493  -1123  A    O  
ATOM    681  CB  TYR A 100      47.413 -12.912 -23.756  1.00 57.31      A    C  
ANISOU  681  CB  TYR A 100     7474   8231   6070    945   -442  -1354  A    C  
ATOM    682  CG  TYR A 100      47.792 -14.060 -24.658  1.00 69.06      A    C  
ANISOU  682  CG  TYR A 100     9118   9668   7451   1068   -447  -1514  A    C  
ATOM    683  CD1 TYR A 100      47.368 -14.103 -25.971  1.00 79.10      A    C  
ANISOU  683  CD1 TYR A 100    10497  11017   8540   1118   -497  -1620  A    C  
ATOM    684  CD2 TYR A 100      48.657 -15.050 -24.212  1.00 85.30      A    C  
ANISOU  684  CD2 TYR A 100    11224  11606   9580   1152   -392  -1554  A    C  
ATOM    685  CE1 TYR A 100      47.773 -15.131 -26.819  1.00 79.86      A    C  
ANISOU  685  CE1 TYR A 100    10765  11062   8517   1242   -487  -1780  A    C  
ATOM    686  CE2 TYR A 100      49.054 -16.079 -25.041  1.00 86.80      A    C  
ANISOU  686  CE2 TYR A 100    11576  11735   9669   1291   -378  -1706  A    C  
ATOM    687  CZ  TYR A 100      48.611 -16.119 -26.339  1.00 81.53      A    C  
ANISOU  687  CZ  TYR A 100    11030  11135   8810   1333   -421  -1827  A    C  
ATOM    688  OH  TYR A 100      49.033 -17.138 -27.167  1.00 96.13      A    O  
ANISOU  688  OH  TYR A 100    13067  12916  10542   1480   -397  -1994  A    O  
ATOM    689  N   LEU A 101      46.294 -12.483 -20.675  1.00 55.89      A    N  
ANISOU  689  N   LEU A 101     7098   7870   6265    625   -501  -1172  A    N  
ATOM    690  CA  LEU A 101      46.490 -11.557 -19.584  1.00 54.33      A    C  
ANISOU  690  CA  LEU A 101     6798   7690   6153    556   -440  -1032  A    C  
ATOM    691  C   LEU A 101      47.969 -11.236 -19.543  1.00 61.73      A    C  
ANISOU  691  C   LEU A 101     7705   8684   7063    649   -330   -953  A    C  
ATOM    692  O   LEU A 101      48.805 -12.140 -19.535  1.00 72.95      A    O  
ANISOU  692  O   LEU A 101     9162  10056   8496    731   -308   -990  A    O  
ATOM    693  CB  LEU A 101      46.023 -12.171 -18.265  1.00 56.08      A    C  
ANISOU  693  CB  LEU A 101     7011   7778   6519    432   -479  -1021  A    C  
ATOM    694  CG  LEU A 101      44.556 -12.102 -17.914  1.00 60.40      A    C  
ANISOU  694  CG  LEU A 101     7522   8301   7124    301   -554  -1038  A    C  
ATOM    695  CD1 LEU A 101      43.666 -12.378 -19.091  1.00 57.81      A    C  
ANISOU  695  CD1 LEU A 101     7225   8017   6721    311   -649  -1144  A    C  
ATOM    696  CD2 LEU A 101      44.253 -13.114 -16.810  1.00 63.32      A    C  
ANISOU  696  CD2 LEU A 101     7919   8523   7615    190   -588  -1050  A    C  
ATOM    697  N   VAL A 102      48.312  -9.953 -19.540  1.00 61.75      A    N  
ANISOU  697  N   VAL A 102     7639   8789   7032    640   -262   -840  A    N  
ATOM    698  CA  VAL A 102      49.723  -9.563 -19.466  1.00 56.52      A    C  
ANISOU  698  CA  VAL A 102     6920   8200   6352    696   -162   -747  A    C  
ATOM    699  C   VAL A 102      50.097  -9.033 -18.089  1.00 56.58      A    C  
ANISOU  699  C   VAL A 102     6861   8172   6464    585   -142   -634  A    C  
ATOM    700  O   VAL A 102      49.564  -8.026 -17.648  1.00 63.09      A    O  
ANISOU  700  O   VAL A 102     7669   8997   7303    490   -140   -573  A    O  
ATOM    701  CB  VAL A 102      50.069  -8.511 -20.532  1.00 64.12      A    C  
ANISOU  701  CB  VAL A 102     7868   9307   7186    753    -91   -690  A    C  
ATOM    702  CG1 VAL A 102      51.574  -8.330 -20.602  1.00 71.21      A    C  
ANISOU  702  CG1 VAL A 102     8693  10297   8063    813     16   -604  A    C  
ATOM    703  CG2 VAL A 102      49.534  -8.944 -21.888  1.00 64.15      A    C  
ANISOU  703  CG2 VAL A 102     7958   9355   7061    849   -127   -802  A    C  
ATOM    704  N   PHE A 103      51.044  -9.705 -17.418  1.00 60.06      A    N  
ANISOU  704  N   PHE A 103     7270   8582   6967    606   -128   -607  A    N  
ATOM    705  CA  PHE A 103      51.508  -9.261 -16.087  1.00 66.17      A    C  
ANISOU  705  CA  PHE A 103     7985   9332   7821    494   -125   -499  A    C  
ATOM    706  C   PHE A 103      52.957  -8.776 -16.055  1.00 65.50      A    C  
ANISOU  706  C   PHE A 103     7800   9363   7722    519    -57   -390  A    C  
ATOM    707  O   PHE A 103      53.761  -9.170 -16.911  1.00 73.63      A    O  
ANISOU  707  O   PHE A 103     8792  10478   8705    652     -4   -401  A    O  
ATOM    708  CB  PHE A 103      51.388 -10.393 -15.078  1.00 64.98      A    C  
ANISOU  708  CB  PHE A 103     7868   9054   7765    467   -188   -525  A    C  
ATOM    709  CG  PHE A 103      50.008 -10.977 -14.959  1.00 59.24      A    C  
ANISOU  709  CG  PHE A 103     7223   8212   7071    412   -255   -619  A    C  
ATOM    710  CD1 PHE A 103      49.103 -10.490 -14.023  1.00 51.07      A    C  
ANISOU  710  CD1 PHE A 103     6194   7127   6081    272   -276   -589  A    C  
ATOM    711  CD2 PHE A 103      49.660 -12.092 -15.700  1.00 54.28      A    C  
ANISOU  711  CD2 PHE A 103     6670   7521   6433    493   -296   -736  A    C  
ATOM    712  CE1 PHE A 103      47.851 -11.061 -13.881  1.00 53.21      A    C  
ANISOU  712  CE1 PHE A 103     6512   7313   6392    211   -330   -661  A    C  
ATOM    713  CE2 PHE A 103      48.414 -12.700 -15.549  1.00 54.42      A    C  
ANISOU  713  CE2 PHE A 103     6751   7433   6491    413   -369   -815  A    C  
ATOM    714  CZ  PHE A 103      47.503 -12.167 -14.642  1.00 59.47      A    C  
ANISOU  714  CZ  PHE A 103     7364   8049   7182    269   -384   -770  A    C  
ATOM    715  N   ASP A 104      53.264  -7.862 -15.137  1.00 61.57      A    N  
ANISOU  715  N   ASP A 104     7260   8879   7255    386    -55   -286  A    N  
ATOM    716  CA  ASP A 104      54.664  -7.538 -14.827  1.00 63.97      A    C  
ANISOU  716  CA  ASP A 104     7448   9286   7569    368    -20   -172  A    C  
ATOM    717  C   ASP A 104      55.377  -8.845 -14.470  1.00 71.17      A    C  
ANISOU  717  C   ASP A 104     8314  10183   8542    472    -50   -181  A    C  
ATOM    718  O   ASP A 104      54.843  -9.662 -13.713  1.00 67.88      A    O  
ANISOU  718  O   ASP A 104     7966   9640   8185    457   -120   -225  A    O  
ATOM    719  CB  ASP A 104      54.741  -6.578 -13.646  1.00 71.32      A    C  
ANISOU  719  CB  ASP A 104     8377  10192   8529    183    -49    -83  A    C  
ATOM    720  CG  ASP A 104      54.519  -5.106 -14.036  1.00 83.92      A    C  
ANISOU  720  CG  ASP A 104    10001  11819  10065     92      0    -35  A    C  
ATOM    721  OD1 ASP A 104      54.861  -4.698 -15.165  1.00 98.84      A    O  
ANISOU  721  OD1 ASP A 104    11858  13806  11891    157     68    -13  A    O  
ATOM    722  OD2 ASP A 104      54.048  -4.356 -13.175  1.00 87.81      A    O1-
ANISOU  722  OD2 ASP A 104    10560  12234  10570    -41    -22    -14  A    O1-
ATOM    723  N   PHE A 105      56.584  -9.051 -14.994  1.00 77.40      A    N  
ANISOU  723  N   PHE A 105     8987  11102   9319    584      7   -130  A    N  
ATOM    724  CA  PHE A 105      57.312 -10.303 -14.685  1.00 69.74      A    C  
ANISOU  724  CA  PHE A 105     7969  10116   8413    720    -15   -130  A    C  
ATOM    725  C   PHE A 105      57.956 -10.296 -13.294  1.00 70.62      A    C  
ANISOU  725  C   PHE A 105     8001  10228   8602    618    -91    -15  A    C  
ATOM    726  O   PHE A 105      58.513  -9.279 -12.866  1.00 72.04      A    O  
ANISOU  726  O   PHE A 105     8088  10508   8775    479    -92     92  A    O  
ATOM    727  CB  PHE A 105      58.357 -10.579 -15.747  1.00 66.51      A    C  
ANISOU  727  CB  PHE A 105     7451   9855   7964    905     87   -119  A    C  
ATOM    728  CG  PHE A 105      59.133 -11.842 -15.523  1.00 77.26      A    C  
ANISOU  728  CG  PHE A 105     8763  11200   9392   1085     78   -119  A    C  
ATOM    729  CD1 PHE A 105      58.572 -13.087 -15.790  1.00 80.81      A    C  
ANISOU  729  CD1 PHE A 105     9359  11489   9854   1226     54   -251  A    C  
ATOM    730  CD2 PHE A 105      60.442 -11.790 -15.069  1.00 85.22      A    C  
ANISOU  730  CD2 PHE A 105     9575  12351  10453   1118     91     17  A    C  
ATOM    731  CE1 PHE A 105      59.310 -14.249 -15.597  1.00 76.18      A    C  
ANISOU  731  CE1 PHE A 105     8746  10863   9332   1414     51   -248  A    C  
ATOM    732  CE2 PHE A 105      61.216 -12.954 -14.938  1.00 81.02      A    C  
ANISOU  732  CE2 PHE A 105     8982  11813   9985   1325     91     28  A    C  
ATOM    733  CZ  PHE A 105      60.628 -14.182 -15.161  1.00 78.20      A    C  
ANISOU  733  CZ  PHE A 105     8798  11270   9643   1477     72   -104  A    C  
ATOM    734  N   CYS A 106      57.919 -11.432 -12.612  1.00 70.49      A    N  
ANISOU  734  N   CYS A 106     8030  10100   8653    682   -160    -33  A    N  
ATOM    735  CA  CYS A 106      58.591 -11.586 -11.308  1.00 71.18      A    C  
ANISOU  735  CA  CYS A 106     8048  10195   8802    611   -247     84  A    C  
ATOM    736  C   CYS A 106      59.627 -12.682 -11.430  1.00 73.38      A    C  
ANISOU  736  C   CYS A 106     8229  10513   9136    824   -245    122  A    C  
ATOM    737  O   CYS A 106      59.313 -13.799 -11.899  1.00 82.03      A    O  
ANISOU  737  O   CYS A 106     9425  11489  10252    993   -232     25  A    O  
ATOM    738  CB  CYS A 106      57.577 -11.953 -10.221  1.00 76.13      A    C  
ANISOU  738  CB  CYS A 106     8829  10641   9455    492   -336     54  A    C  
ATOM    739  SG  CYS A 106      56.367 -10.690  -9.949  1.00 74.44      A    S  
ANISOU  739  SG  CYS A 106     8715  10382   9183    271   -326     16  A    S  
ATOM    740  N   GLU A 107      60.852 -12.390 -11.007  1.00 62.32      A    N  
ANISOU  740  N   GLU A 107     6639   9275   7764    819   -263    262  A    N  
ATOM    741  CA  GLU A 107      61.977 -13.286 -11.187  1.00 68.41      A    C  
ANISOU  741  CA  GLU A 107     7269  10130   8593   1045   -247    321  A    C  
ATOM    742  C   GLU A 107      61.822 -14.642 -10.489  1.00 72.99      A    C  
ANISOU  742  C   GLU A 107     7956  10532   9244   1167   -333    310  A    C  
ATOM    743  O   GLU A 107      62.066 -15.694 -11.094  1.00 75.20      A    O  
ANISOU  743  O   GLU A 107     8263  10753   9555   1413   -285    253  A    O  
ATOM    744  CB  GLU A 107      63.270 -12.597 -10.759  1.00 74.66      A    C  
ANISOU  744  CB  GLU A 107     7807  11151   9406    976   -270    493  A    C  
ATOM    745  CG  GLU A 107      64.528 -13.430 -10.941  1.00 95.29      A    C  
ANISOU  745  CG  GLU A 107    10221  13895  12089   1223   -246    578  A    C  
ATOM    746  CD  GLU A 107      64.732 -13.884 -12.380  1.00110.62      A    C  
ANISOU  746  CD  GLU A 107    12143  15883  14004   1477    -80    485  A    C  
ATOM    747  OE1 GLU A 107      64.035 -13.355 -13.280  1.00102.27      A    O  
ANISOU  747  OE1 GLU A 107    11191  14803  12862   1427      8    378  A    O  
ATOM    748  OE2 GLU A 107      65.554 -14.796 -12.592  1.00119.31      A    O1-
ANISOU  748  OE2 GLU A 107    13135  17034  15160   1735    -42    517  A    O1-
ATOM    749  N   HIS A 108      61.425 -14.612  -9.224  1.00 74.04      A    N  
ANISOU  749  N   HIS A 108     8167  10570   9393    999   -455    365  A    N  
ATOM    750  CA  HIS A 108      61.355 -15.836  -8.422  1.00 77.42      A    C  
ANISOU  750  CA  HIS A 108     8696  10835   9884   1090   -547    392  A    C  
ATOM    751  C   HIS A 108      59.954 -16.290  -8.064  1.00 77.28      A    C  
ANISOU  751  C   HIS A 108     8930  10576   9857    989   -582    289  A    C  
ATOM    752  O   HIS A 108      59.016 -15.502  -8.107  1.00 82.34      A    O  
ANISOU  752  O   HIS A 108     9648  11193  10443    807   -560    222  A    O  
ATOM    753  CB  HIS A 108      62.184 -15.690  -7.129  1.00 76.01      A    C  
ANISOU  753  CB  HIS A 108     8398  10752   9730   1004   -675    570  A    C  
ATOM    754  CG  HIS A 108      63.519 -15.062  -7.368  1.00 75.17      A    C  
ANISOU  754  CG  HIS A 108     8011  10913   9634   1039   -658    689  A    C  
ATOM    755  CD2 HIS A 108      64.030 -13.875  -6.966  1.00 79.78      A    C  
ANISOU  755  CD2 HIS A 108     8450  11681  10181    831   -697    785  A    C  
ATOM    756  ND1 HIS A 108      64.480 -15.648  -8.165  1.00 71.55      A    N  
ANISOU  756  ND1 HIS A 108     7390  10565   9230   1308   -582    714  A    N  
ATOM    757  CE1 HIS A 108      65.525 -14.847  -8.242  1.00 85.39      A    C  
ANISOU  757  CE1 HIS A 108     8884  12576  10983   1258   -572    832  A    C  
ATOM    758  NE2 HIS A 108      65.282 -13.768  -7.518  1.00 90.52      A    N  
ANISOU  758  NE2 HIS A 108     9545  13269  11580    959   -650    877  A    N  
ATOM    759  N   ASP A 109      59.846 -17.554  -7.646  1.00 78.86      A    N  
ANISOU  759  N   ASP A 109     9249  10598  10115   1105   -639    293  A    N  
ATOM    760  CA  ASP A 109      58.623 -18.062  -7.049  1.00 81.58      A    C  
ANISOU  760  CA  ASP A 109     9814  10719  10461    980   -688    237  A    C  
ATOM    761  C   ASP A 109      58.915 -18.807  -5.739  1.00 87.28      A    C  
ANISOU  761  C   ASP A 109    10589  11348  11222    971   -807    373  A    C  
ATOM    762  O   ASP A 109      59.730 -19.720  -5.720  1.00 82.09      A    O  
ANISOU  762  O   ASP A 109     9903  10657  10627   1182   -837    436  A    O  
ATOM    763  CB  ASP A 109      57.911 -18.985  -8.032  1.00 77.72      A    C  
ANISOU  763  CB  ASP A 109     9484  10049   9994   1106   -634     77  A    C  
ATOM    764  CG  ASP A 109      56.960 -19.890  -7.323  1.00 91.61      A    C  
ANISOU  764  CG  ASP A 109    11454  11564  11788   1020   -701     59  A    C  
ATOM    765  OD1 ASP A 109      56.376 -19.391  -6.345  1.00107.74      A    O  
ANISOU  765  OD1 ASP A 109    13527  13604  13802    803   -746    117  A    O  
ATOM    766  OD2 ASP A 109      56.865 -21.085  -7.633  1.00108.53      A    O1-
ANISOU  766  OD2 ASP A 109    13733  13518  13982   1164   -710      3  A    O1-
ATOM    767  N   LEU A 110      58.285 -18.385  -4.645  1.00 93.61      A    N  
ANISOU  767  N   LEU A 110    11469  12118  11981    741   -868    424  A    N  
ATOM    768  CA  LEU A 110      58.566 -18.935  -3.325  1.00 81.67      A    C  
ANISOU  768  CA  LEU A 110    10011  10545  10475    703   -984    570  A    C  
ATOM    769  C   LEU A 110      58.581 -20.470  -3.284  1.00 87.53      A    C  
ANISOU  769  C   LEU A 110    10891  11069  11296    887  -1021    585  A    C  
ATOM    770  O   LEU A 110      59.411 -21.059  -2.589  1.00100.11      A    O  
ANISOU  770  O   LEU A 110    12455  12661  12920    993  -1113    730  A    O  
ATOM    771  CB  LEU A 110      57.557 -18.385  -2.318  1.00 66.58      A    C  
ANISOU  771  CB  LEU A 110     8223   8586   8487    431  -1008    578  A    C  
ATOM    772  CG  LEU A 110      57.847 -18.669  -0.850  1.00 68.01      A    C  
ANISOU  772  CG  LEU A 110     8462   8749   8630    344  -1129    739  A    C  
ATOM    773  CD1 LEU A 110      59.177 -18.044  -0.444  1.00 63.03      A    C  
ANISOU  773  CD1 LEU A 110     7635   8341   7970    359  -1213    870  A    C  
ATOM    774  CD2 LEU A 110      56.702 -18.179   0.008  1.00 76.56      A    C  
ANISOU  774  CD2 LEU A 110     9690   9773   9625     91  -1114    718  A    C  
ATOM    775  N   ALA A 111      57.679 -21.127  -4.004  1.00 77.29      A    N  
ANISOU  775  N   ALA A 111     9752   9582  10032    921   -960    443  A    N  
ATOM    776  CA  ALA A 111      57.741 -22.601  -4.081  1.00 82.07      A    C  
ANISOU  776  CA  ALA A 111    10513   9952  10718   1103   -990    444  A    C  
ATOM    777  C   ALA A 111      59.132 -23.030  -4.617  1.00 93.61      A    C  
ANISOU  777  C   ALA A 111    11834  11496  12236   1415   -984    494  A    C  
ATOM    778  O   ALA A 111      59.757 -23.962  -4.095  1.00 81.75      A    O  
ANISOU  778  O   ALA A 111    10374   9894  10793   1578  -1055    608  A    O  
ATOM    779  CB  ALA A 111      56.623 -23.138  -4.964  1.00 73.11      A    C  
ANISOU  779  CB  ALA A 111     9555   8620   9602   1083   -927    260  A    C  
ATOM    780  N   GLY A 112      59.590 -22.325  -5.657  1.00101.66      A    N  
ANISOU  780  N   GLY A 112    12685  12704  13235   1499   -891    416  A    N  
ATOM    781  CA  GLY A 112      60.888 -22.583  -6.242  1.00 89.63      A    C  
ANISOU  781  CA  GLY A 112    10991  11306  11757   1786   -853    460  A    C  
ATOM    782  C   GLY A 112      62.060 -22.329  -5.312  1.00 87.17      A    C  
ANISOU  782  C   GLY A 112    10472  11183  11464   1822   -947    672  A    C  
ATOM    783  O   GLY A 112      62.934 -23.190  -5.167  1.00 92.10      A    O  
ANISOU  783  O   GLY A 112    11053  11779  12162   2073   -984    768  A    O  
ATOM    784  N   LEU A 113      62.094 -21.148  -4.695  1.00 84.02      A    N  
ANISOU  784  N   LEU A 113     9947  10976  10999   1578   -992    746  A    N  
ATOM    785  CA  LEU A 113      63.187 -20.788  -3.798  1.00 90.33      A    C  
ANISOU  785  CA  LEU A 113    10543  11978  11800   1565  -1103    944  A    C  
ATOM    786  C   LEU A 113      63.266 -21.775  -2.612  1.00 96.66      A    C  
ANISOU  786  C   LEU A 113    11471  12623  12630   1607  -1245   1085  A    C  
ATOM    787  O   LEU A 113      64.341 -22.161  -2.164  1.00 94.51      A    O  
ANISOU  787  O   LEU A 113    11054  12449  12405   1769  -1334   1246  A    O  
ATOM    788  CB  LEU A 113      62.952 -19.383  -3.238  1.00 82.80      A    C  
ANISOU  788  CB  LEU A 113     9518  11189  10750   1246  -1137    969  A    C  
ATOM    789  CG  LEU A 113      62.933 -18.198  -4.176  1.00 76.19      A    C  
ANISOU  789  CG  LEU A 113     8553  10522   9871   1154  -1023    875  A    C  
ATOM    790  CD1 LEU A 113      62.132 -17.030  -3.577  1.00 78.90      A    C  
ANISOU  790  CD1 LEU A 113     8973  10885  10116    826  -1044    847  A    C  
ATOM    791  CD2 LEU A 113      64.357 -17.745  -4.496  1.00 67.76      A    C  
ANISOU  791  CD2 LEU A 113     7177   9735   8834   1258  -1020    987  A    C  
ATOM    792  N   LEU A 114      62.099 -22.160  -2.111  1.00 92.68      A    N  
ANISOU  792  N   LEU A 114    11232  11886  12097   1455  -1265   1033  A    N  
ATOM    793  CA  LEU A 114      62.036 -23.045  -0.959  1.00 85.32      A    C  
ANISOU  793  CA  LEU A 114    10453  10791  11174   1456  -1391   1171  A    C  
ATOM    794  C   LEU A 114      62.478 -24.477  -1.306  1.00 93.27      A    C  
ANISOU  794  C   LEU A 114    11544  11601  12291   1784  -1395   1197  A    C  
ATOM    795  O   LEU A 114      62.997 -25.184  -0.450  1.00 97.06      A    O  
ANISOU  795  O   LEU A 114    12057  12022  12799   1885  -1514   1368  A    O  
ATOM    796  CB  LEU A 114      60.617 -23.055  -0.384  1.00 81.18      A    C  
ANISOU  796  CB  LEU A 114    10182  10075  10585   1192  -1386   1109  A    C  
ATOM    797  CG  LEU A 114      60.209 -21.891   0.511  1.00 81.87      A    C  
ANISOU  797  CG  LEU A 114    10249  10305  10550    880  -1423   1146  A    C  
ATOM    798  CD1 LEU A 114      58.879 -22.189   1.198  1.00 70.95      A    C  
ANISOU  798  CD1 LEU A 114     9121   8718   9117    672  -1414   1117  A    C  
ATOM    799  CD2 LEU A 114      61.279 -21.614   1.560  1.00 93.84      A    C  
ANISOU  799  CD2 LEU A 114    11632  12003  12019    864  -1573   1347  A    C  
ATOM    800  N   SER A 115      62.252 -24.884  -2.555  1.00 96.43      A    N  
ANISOU  800  N   SER A 115    11998  11895  12745   1948  -1267   1026  A    N  
ATOM    801  CA  SER A 115      62.586 -26.234  -2.973  1.00 97.15      A    C  
ANISOU  801  CA  SER A 115    12213  11765  12934   2263  -1252   1016  A    C  
ATOM    802  C   SER A 115      64.028 -26.286  -3.476  1.00103.20      A    C  
ANISOU  802  C   SER A 115    12712  12735  13761   2585  -1224   1090  A    C  
ATOM    803  O   SER A 115      64.469 -27.303  -3.988  1.00123.40      A    O  
ANISOU  803  O   SER A 115    15335  15147  16403   2901  -1183   1069  A    O  
ATOM    804  CB  SER A 115      61.647 -26.736  -4.061  1.00103.80      A    C  
ANISOU  804  CB  SER A 115    13271  12375  13791   2289  -1135    786  A    C  
ATOM    805  OG  SER A 115      62.012 -26.195  -5.325  1.00116.42      A    O  
ANISOU  805  OG  SER A 115    14711  14145  15376   2410  -1004    651  A    O  
ATOM    806  N   ASN A 116      64.755 -25.203  -3.265  1.00 97.46      A    N  
ANISOU  806  N   ASN A 116    11692  12341  12996   2497  -1250   1185  A    N  
ATOM    807  CA  ASN A 116      66.124 -25.103  -3.734  1.00107.78      A    C  
ANISOU  807  CA  ASN A 116    12693  13898  14361   2762  -1217   1269  A    C  
ATOM    808  C   ASN A 116      67.109 -25.161  -2.561  1.00113.63      A    C  
ANISOU  808  C   ASN A 116    13254  14793  15125   2801  -1392   1528  A    C  
ATOM    809  O   ASN A 116      67.232 -24.207  -1.788  1.00112.75      A    O  
ANISOU  809  O   ASN A 116    13012  14884  14941   2537  -1494   1628  A    O  
ATOM    810  CB  ASN A 116      66.335 -23.844  -4.561  1.00107.37      A    C  
ANISOU  810  CB  ASN A 116    12410  14130  14255   2649  -1104   1187  A    C  
ATOM    811  CG  ASN A 116      67.673 -23.841  -5.292  1.00108.22      A    C  
ANISOU  811  CG  ASN A 116    12207  14484  14427   2947  -1021   1248  A    C  
ATOM    812  ND2 ASN A 116      67.701 -23.188  -6.428  1.00115.10      A    N  
ANISOU  812  ND2 ASN A 116    12973  15496  15262   2950   -862   1120  A    N  
ATOM    813  OD1 ASN A 116      68.663 -24.451  -4.855  1.00107.86      A    O  
ANISOU  813  OD1 ASN A 116    12016  14504  14461   3184  -1095   1414  A    O  
ATOM    814  N   VAL A 117      67.805 -26.289  -2.447  1.00117.21      A    N  
ANISOU  814  N   VAL A 117    13711  15145  15676   3138  -1431   1634  A    N  
ATOM    815  CA  VAL A 117      68.735 -26.520  -1.353  1.00118.37      A    C  
ANISOU  815  CA  VAL A 117    13702  15419  15854   3220  -1614   1893  A    C  
ATOM    816  C   VAL A 117      69.845 -25.467  -1.258  1.00119.80      A    C  
ANISOU  816  C   VAL A 117    13461  16031  16023   3166  -1661   2021  A    C  
ATOM    817  O   VAL A 117      70.328 -25.178  -0.168  1.00108.17      A    O  
ANISOU  817  O   VAL A 117    11867  14715  14517   3043  -1848   2217  A    O  
ATOM    818  CB  VAL A 117      69.352 -27.934  -1.438  1.00114.19      A    C  
ANISOU  818  CB  VAL A 117    13234  14704  15448   3654  -1624   1977  A    C  
ATOM    819  CG1 VAL A 117      68.248 -28.995  -1.357  1.00106.31      A    C  
ANISOU  819  CG1 VAL A 117    12680  13253  14459   3659  -1610   1875  A    C  
ATOM    820  CG2 VAL A 117      70.141 -28.094  -2.733  1.00114.10      A    C  
ANISOU  820  CG2 VAL A 117    13019  14813  15519   4003  -1444   1889  A    C  
ATOM    821  N   LEU A 118      70.233 -24.888  -2.393  1.00135.64      A    N  
ANISOU  821  N   LEU A 118    15256  18232  18048   3238  -1496   1915  A    N  
ATOM    822  CA  LEU A 118      71.229 -23.827  -2.416  1.00139.79      A    C  
ANISOU  822  CA  LEU A 118    15382  19165  18565   3149  -1520   2026  A    C  
ATOM    823  C   LEU A 118      70.764 -22.542  -1.716  1.00131.02      A    C  
ANISOU  823  C   LEU A 118    14269  18181  17331   2686  -1619   2034  A    C  
ATOM    824  O   LEU A 118      71.535 -21.868  -1.051  1.00124.03      A    O  
ANISOU  824  O   LEU A 118    13133  17568  16424   2546  -1757   2197  A    O  
ATOM    825  CB  LEU A 118      71.614 -23.501  -3.874  1.00140.03      A    C  
ANISOU  825  CB  LEU A 118    15229  19348  18628   3313  -1291   1896  A    C  
ATOM    826  CG  LEU A 118      72.463 -24.556  -4.603  1.00125.30      A    C  
ANISOU  826  CG  LEU A 118    13249  17476  16881   3802  -1178   1918  A    C  
ATOM    827  CD1 LEU A 118      72.536 -24.269  -6.098  1.00123.52      A    C  
ANISOU  827  CD1 LEU A 118    12944  17340  16647   3932   -924   1742  A    C  
ATOM    828  CD2 LEU A 118      73.841 -24.561  -3.962  1.00118.35      A    C  
ANISOU  828  CD2 LEU A 118    11982  16903  16081   3947  -1311   2184  A    C  
ATOM    829  N   VAL A 119      69.477 -22.245  -1.872  1.00134.39      A    N  
ANISOU  829  N   VAL A 119    14987  18396  17676   2458  -1549   1853  A    N  
ATOM    830  CA  VAL A 119      68.888 -20.996  -1.390  1.00114.71      A    C  
ANISOU  830  CA  VAL A 119    12532  15987  15064   2046  -1596   1817  A    C  
ATOM    831  C   VAL A 119      68.809 -21.006   0.129  1.00107.94      A    C  
ANISOU  831  C   VAL A 119    11767  15107  14136   1853  -1813   1970  A    C  
ATOM    832  O   VAL A 119      68.400 -22.004   0.708  1.00104.89      A    O  
ANISOU  832  O   VAL A 119    11605  14485  13761   1945  -1879   2010  A    O  
ATOM    833  CB  VAL A 119      67.453 -20.832  -1.930  1.00106.68      A    C  
ANISOU  833  CB  VAL A 119    11814  14730  13990   1897  -1463   1590  A    C  
ATOM    834  CG1 VAL A 119      66.837 -19.543  -1.404  1.00 97.96      A    C  
ANISOU  834  CG1 VAL A 119    10754  13699  12764   1502  -1500   1555  A    C  
ATOM    835  CG2 VAL A 119      67.455 -20.850  -3.458  1.00109.08      A    C  
ANISOU  835  CG2 VAL A 119    12062  15044  14336   2082  -1255   1429  A    C  
ATOM    836  N   LYS A 120      69.185 -19.901   0.765  1.00103.83      A    N  
ANISOU  836  N   LYS A 120    11095  14821  13534   1576  -1924   2052  A    N  
ATOM    837  CA  LYS A 120      69.105 -19.823   2.227  1.00104.60      A    C  
ANISOU  837  CA  LYS A 120    11299  14914  13531   1369  -2134   2188  A    C  
ATOM    838  C   LYS A 120      68.484 -18.562   2.806  1.00110.24      A    C  
ANISOU  838  C   LYS A 120    12115  15675  14095    961  -2169   2123  A    C  
ATOM    839  O   LYS A 120      68.702 -17.447   2.293  1.00118.68      A    O  
ANISOU  839  O   LYS A 120    13029  16920  15143    804  -2107   2062  A    O  
ATOM    840  CB  LYS A 120      70.480 -20.095   2.840  1.00108.59      A    C  
ANISOU  840  CB  LYS A 120    11519  15658  14080   1503  -2323   2429  A    C  
ATOM    841  CG  LYS A 120      70.578 -21.434   3.564  1.00118.93      A    C  
ANISOU  841  CG  LYS A 120    12964  16795  15428   1734  -2445   2572  A    C  
ATOM    842  CD  LYS A 120      71.980 -22.040   3.358  1.00129.80      A    C  
ANISOU  842  CD  LYS A 120    14004  18373  16939   2079  -2513   2755  A    C  
ATOM    843  CE  LYS A 120      72.083 -23.464   3.888  1.00136.53      A    C  
ANISOU  843  CE  LYS A 120    15004  19016  17853   2376  -2607   2890  A    C  
ATOM    844  NZ  LYS A 120      73.504 -23.899   4.119  1.00127.07      A    N1+
ANISOU  844  NZ  LYS A 120    13463  18064  16754   2656  -2749   3129  A    N1+
ATOM    845  N   PHE A 121      67.660 -18.715   3.849  1.00102.31      A    N  
ANISOU  845  N   PHE A 121    11393  14501  12980    788  -2252   2131  A    N  
ATOM    846  CA  PHE A 121      67.006 -17.560   4.482  1.00 96.80      A    C  
ANISOU  846  CA  PHE A 121    10829  13825  12126    419  -2274   2061  A    C  
ATOM    847  C   PHE A 121      67.518 -17.340   5.904  1.00100.18      A    C  
ANISOU  847  C   PHE A 121    11258  14378  12426    242  -2511   2234  A    C  
ATOM    848  O   PHE A 121      67.657 -18.302   6.670  1.00122.12      A    O  
ANISOU  848  O   PHE A 121    14124  17079  15195    357  -2635   2373  A    O  
ATOM    849  CB  PHE A 121      65.486 -17.773   4.573  1.00 96.83      A    C  
ANISOU  849  CB  PHE A 121    11175  13542  12072    324  -2155   1911  A    C  
ATOM    850  CG  PHE A 121      64.780 -17.842   3.243  1.00112.80      A    C  
ANISOU  850  CG  PHE A 121    13235  15437  14185    432  -1938   1720  A    C  
ATOM    851  CD1 PHE A 121      64.308 -16.674   2.635  1.00120.79      A    C  
ANISOU  851  CD1 PHE A 121    14232  16504  15157    257  -1818   1573  A    C  
ATOM    852  CD2 PHE A 121      64.542 -19.059   2.621  1.00100.48      A    C  
ANISOU  852  CD2 PHE A 121    11752  13686  12738    699  -1862   1685  A    C  
ATOM    853  CE1 PHE A 121      63.622 -16.725   1.441  1.00103.44      A    C  
ANISOU  853  CE1 PHE A 121    12079  14198  13024    349  -1636   1406  A    C  
ATOM    854  CE2 PHE A 121      63.865 -19.115   1.417  1.00107.39      A    C  
ANISOU  854  CE2 PHE A 121    12679  14448  13674    778  -1680   1503  A    C  
ATOM    855  CZ  PHE A 121      63.408 -17.945   0.825  1.00117.78      A    C  
ANISOU  855  CZ  PHE A 121    13963  15844  14942    604  -1571   1368  A    C  
ATOM    856  N   THR A 122      67.768 -16.088   6.271  1.00 93.08      A    N  
ANISOU  856  N   THR A 122    10289  13656  11419    -42  -2578   2225  A    N  
ATOM    857  CA  THR A 122      67.971 -15.745   7.674  1.00 95.66      A    C  
ANISOU  857  CA  THR A 122    10705  14065  11576   -274  -2791   2340  A    C  
ATOM    858  C   THR A 122      66.608 -15.514   8.314  1.00 99.57      A    C  
ANISOU  858  C   THR A 122    11570  14341  11920   -477  -2719   2217  A    C  
ATOM    859  O   THR A 122      65.606 -15.284   7.624  1.00 96.48      A    O  
ANISOU  859  O   THR A 122    11309  13790  11556   -493  -2514   2038  A    O  
ATOM    860  CB  THR A 122      68.837 -14.483   7.870  1.00 95.72      A    C  
ANISOU  860  CB  THR A 122    10505  14347  11518   -522  -2912   2377  A    C  
ATOM    861  CG2 THR A 122      70.199 -14.632   7.215  1.00 92.09      A    C  
ANISOU  861  CG2 THR A 122     9636  14140  11211   -341  -2970   2508  A    C  
ATOM    862  OG1 THR A 122      68.153 -13.342   7.332  1.00104.34      A    O  
ANISOU  862  OG1 THR A 122    11688  15388  12567   -727  -2751   2186  A    O  
ATOM    863  N   LEU A 123      66.567 -15.583   9.640  1.00113.11      A    N  
ANISOU  863  N   LEU A 123    13449  16059  13468   -628  -2885   2320  A    N  
ATOM    864  CA  LEU A 123      65.339 -15.284  10.358  1.00110.56      A    C  
ANISOU  864  CA  LEU A 123    13466  15565  12978   -835  -2813   2216  A    C  
ATOM    865  C   LEU A 123      64.810 -13.901   9.964  1.00111.39      A    C  
ANISOU  865  C   LEU A 123    13614  15684  13025  -1061  -2681   2024  A    C  
ATOM    866  O   LEU A 123      63.607 -13.681   9.915  1.00103.48      A    O  
ANISOU  866  O   LEU A 123    12834  14508  11973  -1137  -2513   1878  A    O  
ATOM    867  CB  LEU A 123      65.584 -15.316  11.877  1.00100.14      A    C  
ANISOU  867  CB  LEU A 123    12290  14308  11447  -1001  -3031   2361  A    C  
ATOM    868  CG  LEU A 123      64.371 -14.883  12.716  1.00 92.69      A    C  
ANISOU  868  CG  LEU A 123    11697  13220  10298  -1233  -2948   2255  A    C  
ATOM    869  CD1 LEU A 123      63.239 -15.889  12.571  1.00 87.20      A    C  
ANISOU  869  CD1 LEU A 123    11204  12267   9659  -1098  -2780   2217  A    C  
ATOM    870  CD2 LEU A 123      64.732 -14.576  14.138  1.00 90.00      A    C  
ANISOU  870  CD2 LEU A 123    11489  12992   9713  -1444  -3163   2368  A    C  
ATOM    871  N   SER A 124      65.725 -12.978   9.692  1.00109.17      A    N  
ANISOU  871  N   SER A 124    13115  15611  12754  -1168  -2758   2036  A    N  
ATOM    872  CA  SER A 124      65.375 -11.596   9.415  1.00100.64      A    C  
ANISOU  872  CA  SER A 124    12084  14545  11607  -1400  -2664   1880  A    C  
ATOM    873  C   SER A 124      64.612 -11.442   8.097  1.00 97.73      A    C  
ANISOU  873  C   SER A 124    11706  14050  11375  -1284  -2410   1713  A    C  
ATOM    874  O   SER A 124      63.669 -10.639   7.982  1.00 89.45      A    O  
ANISOU  874  O   SER A 124    10836  12889  10259  -1422  -2271   1556  A    O  
ATOM    875  CB  SER A 124      66.637 -10.742   9.383  1.00 99.20      A    C  
ANISOU  875  CB  SER A 124    11651  14617  11423  -1543  -2820   1956  A    C  
ATOM    876  OG  SER A 124      66.281  -9.370   9.307  1.00115.32      A    O  
ANISOU  876  OG  SER A 124    13800  16642  13374  -1801  -2751   1813  A    O  
ATOM    877  N   GLU A 125      65.005 -12.241   7.113  1.00 95.82      A    N  
ANISOU  877  N   GLU A 125    11265  13824  11317  -1016  -2352   1749  A    N  
ATOM    878  CA  GLU A 125      64.388 -12.203   5.801  1.00 80.87      A    C  
ANISOU  878  CA  GLU A 125     9348  11830   9547   -886  -2132   1603  A    C  
ATOM    879  C   GLU A 125      63.020 -12.916   5.837  1.00 84.58      A    C  
ANISOU  879  C   GLU A 125    10076  12048  10012   -814  -2000   1504  A    C  
ATOM    880  O   GLU A 125      62.026 -12.440   5.261  1.00 97.01      A    O  
ANISOU  880  O   GLU A 125    11760  13508  11589   -857  -1832   1346  A    O  
ATOM    881  CB  GLU A 125      65.321 -12.901   4.803  1.00 87.58      A    C  
ANISOU  881  CB  GLU A 125     9914  12787  10574   -613  -2119   1676  A    C  
ATOM    882  CG  GLU A 125      66.625 -12.156   4.560  1.00113.37      A    C  
ANISOU  882  CG  GLU A 125    12879  16324  13870   -682  -2210   1769  A    C  
ATOM    883  CD  GLU A 125      67.713 -13.030   3.958  1.00120.96      A    C  
ANISOU  883  CD  GLU A 125    13546  17427  14986   -395  -2240   1897  A    C  
ATOM    884  OE1 GLU A 125      68.181 -13.971   4.643  1.00107.15      A    O  
ANISOU  884  OE1 GLU A 125    11766  15695  13250   -261  -2382   2041  A    O  
ATOM    885  OE2 GLU A 125      68.110 -12.798   2.793  1.00144.77      A    O1-
ANISOU  885  OE2 GLU A 125    16361  20537  18105   -285  -2113   1859  A    O1-
ATOM    886  N   ILE A 126      62.999 -14.063   6.506  1.00 81.07      A    N  
ANISOU  886  N   ILE A 126     9716  11520   9564   -705  -2084   1610  A    N  
ATOM    887  CA  ILE A 126      61.763 -14.794   6.681  1.00 85.80      A    C  
ANISOU  887  CA  ILE A 126    10557  11887  10153   -670  -1981   1545  A    C  
ATOM    888  C   ILE A 126      60.712 -13.872   7.294  1.00 83.78      A    C  
ANISOU  888  C   ILE A 126    10520  11569   9744   -921  -1904   1435  A    C  
ATOM    889  O   ILE A 126      59.558 -13.856   6.872  1.00 75.47      A    O  
ANISOU  889  O   ILE A 126     9590  10372   8713   -926  -1739   1303  A    O  
ATOM    890  CB  ILE A 126      61.958 -16.049   7.546  1.00 83.71      A    C  
ANISOU  890  CB  ILE A 126    10382  11546   9875   -566  -2107   1706  A    C  
ATOM    891  CG1 ILE A 126      62.901 -17.035   6.846  1.00 89.40      A    C  
ANISOU  891  CG1 ILE A 126    10904  12295  10767   -269  -2154   1801  A    C  
ATOM    892  CG2 ILE A 126      60.622 -16.730   7.799  1.00 71.78      A    C  
ANISOU  892  CG2 ILE A 126     9134   9795   8344   -581  -1994   1646  A    C  
ATOM    893  CD1 ILE A 126      63.151 -18.312   7.594  1.00100.61      A    C  
ANISOU  893  CD1 ILE A 126    12411  13619  12194   -128  -2279   1970  A    C  
ATOM    894  N   LYS A 127      61.127 -13.079   8.280  1.00 84.05      A    N  
ANISOU  894  N   LYS A 127    10597  11718   9618  -1128  -2026   1486  A    N  
ATOM    895  CA  LYS A 127      60.241 -12.071   8.872  1.00 85.15      A    C  
ANISOU  895  CA  LYS A 127    10947  11808   9597  -1359  -1949   1372  A    C  
ATOM    896  C   LYS A 127      59.701 -11.128   7.807  1.00 86.47      A    C  
ANISOU  896  C   LYS A 127    11075  11949   9832  -1378  -1774   1201  A    C  
ATOM    897  O   LYS A 127      58.508 -10.796   7.801  1.00 84.64      A    O  
ANISOU  897  O   LYS A 127    11007  11592   9557  -1435  -1620   1077  A    O  
ATOM    898  CB  LYS A 127      60.989 -11.237   9.919  1.00 90.79      A    C  
ANISOU  898  CB  LYS A 127    11693  12668  10133  -1578  -2122   1438  A    C  
ATOM    899  CG  LYS A 127      60.952 -11.847  11.301  1.00 96.62      A    C  
ANISOU  899  CG  LYS A 127    12612  13391  10707  -1647  -2253   1559  A    C  
ATOM    900  CD  LYS A 127      61.682 -10.984  12.297  1.00 87.95      A    C  
ANISOU  900  CD  LYS A 127    11559  12442   9415  -1878  -2437   1609  A    C  
ATOM    901  CE  LYS A 127      61.851 -11.719  13.605  1.00 81.51      A    C  
ANISOU  901  CE  LYS A 127    10890  11643   8437  -1916  -2601   1764  A    C  
ATOM    902  NZ  LYS A 127      62.221 -10.775  14.703  1.00 80.80      A    N1+
ANISOU  902  NZ  LYS A 127    10938  11663   8099  -2186  -2752   1767  A    N1+
ATOM    903  N   ARG A 128      60.586 -10.684   6.920  1.00 88.37      A    N  
ANISOU  903  N   ARG A 128    11089  12315  10172  -1329  -1796   1206  A    N  
ATOM    904  CA  ARG A 128      60.203  -9.713   5.915  1.00 82.23      A    C  
ANISOU  904  CA  ARG A 128    10273  11525   9444  -1357  -1648   1068  A    C  
ATOM    905  C   ARG A 128      59.199 -10.314   4.940  1.00 78.11      A    C  
ANISOU  905  C   ARG A 128     9774  10861   9040  -1182  -1473    966  A    C  
ATOM    906  O   ARG A 128      58.165  -9.695   4.625  1.00 76.60      A    O  
ANISOU  906  O   ARG A 128     9696  10577   8829  -1234  -1330    835  A    O  
ATOM    907  CB  ARG A 128      61.429  -9.196   5.187  1.00 74.82      A    C  
ANISOU  907  CB  ARG A 128     9079  10764   8583  -1346  -1709   1120  A    C  
ATOM    908  CG  ARG A 128      61.136  -8.052   4.241  1.00 77.42      A    C  
ANISOU  908  CG  ARG A 128     9388  11088   8940  -1409  -1573    999  A    C  
ATOM    909  CD  ARG A 128      60.658  -6.817   4.990  1.00 85.53      A    C  
ANISOU  909  CD  ARG A 128    10622  12062   9810  -1659  -1567    922  A    C  
ATOM    910  NE  ARG A 128      60.172  -5.822   4.044  1.00 93.08      A    N  
ANISOU  910  NE  ARG A 128    11595  12968  10802  -1683  -1416    804  A    N  
ATOM    911  CZ  ARG A 128      58.905  -5.440   3.927  1.00 93.46      A    C  
ANISOU  911  CZ  ARG A 128    11827  12863  10819  -1682  -1265    675  A    C  
ATOM    912  NH1 ARG A 128      57.968  -5.961   4.715  1.00 94.96      A    N1+
ANISOU  912  NH1 ARG A 128    12195  12942  10940  -1674  -1230    641  A    N1+
ATOM    913  NH2 ARG A 128      58.575  -4.536   3.011  1.00 92.80      A    N  
ANISOU  913  NH2 ARG A 128    11739  12745  10773  -1685  -1145    590  A    N  
ATOM    914  N   VAL A 129      59.500 -11.522   4.476  1.00 73.19      A    N  
ANISOU  914  N   VAL A 129     9051  10219   8538   -973  -1493   1026  A    N  
ATOM    915  CA  VAL A 129      58.603 -12.249   3.578  1.00 61.62      A    C  
ANISOU  915  CA  VAL A 129     7620   8610   7180   -813  -1354    932  A    C  
ATOM    916  C   VAL A 129      57.193 -12.353   4.161  1.00 61.70      A    C  
ANISOU  916  C   VAL A 129     7858   8463   7121   -908  -1266    858  A    C  
ATOM    917  O   VAL A 129      56.204 -11.984   3.510  1.00 70.30      A    O  
ANISOU  917  O   VAL A 129     8992   9480   8237   -912  -1125    730  A    O  
ATOM    918  CB  VAL A 129      59.146 -13.676   3.289  1.00 67.86      A    C  
ANISOU  918  CB  VAL A 129     8330   9367   8086   -585  -1411   1020  A    C  
ATOM    919  CG1 VAL A 129      58.047 -14.611   2.816  1.00 59.68      A    C  
ANISOU  919  CG1 VAL A 129     7419   8134   7123   -480  -1305    934  A    C  
ATOM    920  CG2 VAL A 129      60.320 -13.615   2.330  1.00 84.23      A    C  
ANISOU  920  CG2 VAL A 129    10153  11590  10259   -435  -1429   1055  A    C  
ATOM    921  N   MET A 130      57.099 -12.862   5.384  1.00 70.41      A    N  
ANISOU  921  N   MET A 130     9096   9524   8132   -982  -1347    950  A    N  
ATOM    922  CA  MET A 130      55.812 -12.997   6.051  1.00 71.17      A    C  
ANISOU  922  CA  MET A 130     9398   9491   8149  -1083  -1255    901  A    C  
ATOM    923  C   MET A 130      55.097 -11.658   6.208  1.00 68.72      A    C  
ANISOU  923  C   MET A 130     9172   9198   7738  -1241  -1148    784  A    C  
ATOM    924  O   MET A 130      53.853 -11.593   6.161  1.00 62.32      A    O  
ANISOU  924  O   MET A 130     8463   8293   6923  -1270  -1007    694  A    O  
ATOM    925  CB  MET A 130      55.998 -13.657   7.417  1.00 66.47      A    C  
ANISOU  925  CB  MET A 130     8937   8876   7441  -1151  -1370   1041  A    C  
ATOM    926  CG  MET A 130      56.302 -15.155   7.272  1.00 73.37      A    C  
ANISOU  926  CG  MET A 130     9787   9661   8427   -976  -1437   1147  A    C  
ATOM    927  SD  MET A 130      55.140 -15.938   6.140  1.00 78.17      A    S  
ANISOU  927  SD  MET A 130    10416  10087   9195   -857  -1274   1025  A    S  
ATOM    928  CE  MET A 130      53.568 -15.567   6.926  1.00 68.62      A    C  
ANISOU  928  CE  MET A 130     9407   8797   7868  -1059  -1134    957  A    C  
ATOM    929  N   GLN A 131      55.884 -10.604   6.397  1.00 64.15      A    N  
ANISOU  929  N   GLN A 131     8551   8737   7084  -1342  -1216    790  A    N  
ATOM    930  CA  GLN A 131      55.333  -9.283   6.560  1.00 66.08      A    C  
ANISOU  930  CA  GLN A 131     8898   8979   7231  -1484  -1124    681  A    C  
ATOM    931  C   GLN A 131      54.673  -8.804   5.274  1.00 71.57      A    C  
ANISOU  931  C   GLN A 131     9519   9633   8038  -1397   -974    556  A    C  
ATOM    932  O   GLN A 131      53.548  -8.292   5.292  1.00 72.59      A    O  
ANISOU  932  O   GLN A 131     9757   9689   8134  -1434   -836    455  A    O  
ATOM    933  CB  GLN A 131      56.425  -8.300   6.987  1.00 65.33      A    C  
ANISOU  933  CB  GLN A 131     8778   9005   7039  -1626  -1251    719  A    C  
ATOM    934  CG  GLN A 131      55.846  -6.924   7.291  1.00 74.50      A    C  
ANISOU  934  CG  GLN A 131    10098  10127   8079  -1780  -1159    602  A    C  
ATOM    935  CD  GLN A 131      56.776  -6.074   8.098  1.00 73.55      A    C  
ANISOU  935  CD  GLN A 131    10036  10094   7816  -1973  -1303    640  A    C  
ATOM    936  NE2 GLN A 131      56.304  -5.675   9.296  1.00 75.86      A    N  
ANISOU  936  NE2 GLN A 131    10569  10339   7915  -2119  -1297    605  A    N  
ATOM    937  OE1 GLN A 131      57.900  -5.787   7.674  1.00 69.75      A    O  
ANISOU  937  OE1 GLN A 131     9387   9726   7387  -1999  -1418    699  A    O  
ATOM    938  N   MET A 132      55.365  -8.973   4.157  1.00 70.54      A    N  
ANISOU  938  N   MET A 132     9202   9562   8037  -1273   -998    568  A    N  
ATOM    939  CA  MET A 132      54.805  -8.562   2.885  1.00 65.19      A    C  
ANISOU  939  CA  MET A 132     8457   8858   7452  -1185   -870    461  A    C  
ATOM    940  C   MET A 132      53.553  -9.391   2.565  1.00 70.06      A    C  
ANISOU  940  C   MET A 132     9127   9358   8135  -1094   -766    397  A    C  
ATOM    941  O   MET A 132      52.528  -8.850   2.143  1.00 67.04      A    O  
ANISOU  941  O   MET A 132     8785   8926   7758  -1098   -644    297  A    O  
ATOM    942  CB  MET A 132      55.840  -8.692   1.762  1.00 59.51      A    C  
ANISOU  942  CB  MET A 132     7532   8238   6841  -1063   -909    495  A    C  
ATOM    943  CG  MET A 132      57.090  -7.870   2.002  1.00 68.16      A    C  
ANISOU  943  CG  MET A 132     8538   9468   7888  -1171  -1011    569  A    C  
ATOM    944  SD  MET A 132      58.393  -8.159   0.805  1.00 70.48      A    S  
ANISOU  944  SD  MET A 132     8559   9912   8307  -1020  -1047    638  A    S  
ATOM    945  CE  MET A 132      58.149  -6.726  -0.252  1.00 92.99      A    C  
ANISOU  945  CE  MET A 132    11393  12781  11158  -1079   -924    546  A    C  
ATOM    946  N   LEU A 133      53.650 -10.703   2.765  1.00 70.46      A    N  
ANISOU  946  N   LEU A 133     9174   9361   8237  -1015   -823    463  A    N  
ATOM    947  CA  LEU A 133      52.544 -11.603   2.458  1.00 66.02      A    C  
ANISOU  947  CA  LEU A 133     8659   8680   7745   -952   -745    413  A    C  
ATOM    948  C   LEU A 133      51.301 -11.208   3.260  1.00 66.99      A    C  
ANISOU  948  C   LEU A 133     8926   8746   7781  -1081   -645    368  A    C  
ATOM    949  O   LEU A 133      50.229 -11.015   2.693  1.00 60.33      A    O  
ANISOU  949  O   LEU A 133     8077   7862   6981  -1065   -531    274  A    O  
ATOM    950  CB  LEU A 133      52.960 -13.038   2.739  1.00 57.22      A    C  
ANISOU  950  CB  LEU A 133     7555   7501   6683   -869   -836    508  A    C  
ATOM    951  CG  LEU A 133      52.019 -14.174   2.380  1.00 57.24      A    C  
ANISOU  951  CG  LEU A 133     7611   7361   6775   -809   -786    472  A    C  
ATOM    952  CD1 LEU A 133      52.764 -15.479   2.313  1.00 67.92      A    C  
ANISOU  952  CD1 LEU A 133     8955   8647   8204   -677   -886    559  A    C  
ATOM    953  CD2 LEU A 133      50.917 -14.243   3.429  1.00 62.49      A    C  
ANISOU  953  CD2 LEU A 133     8423   7958   7360   -959   -724    484  A    C  
ATOM    954  N   LEU A 134      51.461 -11.067   4.576  1.00 65.01      A    N  
ANISOU  954  N   LEU A 134     8795   8506   7399  -1205   -686    437  A    N  
ATOM    955  CA  LEU A 134      50.366 -10.663   5.440  1.00 64.32      A    C  
ANISOU  955  CA  LEU A 134     8852   8380   7206  -1322   -576    400  A    C  
ATOM    956  C   LEU A 134      49.814  -9.286   5.074  1.00 63.06      A    C  
ANISOU  956  C   LEU A 134     8698   8246   7014  -1350   -460    284  A    C  
ATOM    957  O   LEU A 134      48.613  -9.020   5.179  1.00 67.35      A    O  
ANISOU  957  O   LEU A 134     9292   8751   7544  -1369   -321    216  A    O  
ATOM    958  CB  LEU A 134      50.811 -10.696   6.916  1.00 62.18      A    C  
ANISOU  958  CB  LEU A 134     8726   8131   6768  -1448   -654    497  A    C  
ATOM    959  CG  LEU A 134      50.927 -12.144   7.465  1.00 59.08      A    C  
ANISOU  959  CG  LEU A 134     8376   7678   6392  -1428   -733    622  A    C  
ATOM    960  CD1 LEU A 134      51.554 -12.170   8.830  1.00 53.24      A    C  
ANISOU  960  CD1 LEU A 134     7768   6981   5480  -1538   -842    736  A    C  
ATOM    961  CD2 LEU A 134      49.520 -12.783   7.526  1.00 61.55      A    C  
ANISOU  961  CD2 LEU A 134     8750   7892   6744  -1446   -593    593  A    C  
ATOM    962  N   ASN A 135      50.697  -8.414   4.617  1.00 60.16      A    N  
ANISOU  962  N   ASN A 135     8272   7943   6643  -1346   -514    268  A    N  
ATOM    963  CA  ASN A 135      50.287  -7.083   4.187  1.00 55.51      A    C  
ANISOU  963  CA  ASN A 135     7701   7356   6032  -1362   -414    169  A    C  
ATOM    964  C   ASN A 135      49.441  -7.155   2.904  1.00 59.00      A    C  
ANISOU  964  C   ASN A 135     8034   7774   6608  -1234   -316     92  A    C  
ATOM    965  O   ASN A 135      48.448  -6.462   2.791  1.00 64.05      A    O  
ANISOU  965  O   ASN A 135     8714   8384   7235  -1228   -193     15  A    O  
ATOM    966  CB  ASN A 135      51.515  -6.200   3.955  1.00 55.97      A    C  
ANISOU  966  CB  ASN A 135     7719   7483   6061  -1409   -507    189  A    C  
ATOM    967  CG  ASN A 135      51.169  -4.728   3.848  1.00 62.27      A    C  
ANISOU  967  CG  ASN A 135     8605   8253   6799  -1465   -417    101  A    C  
ATOM    968  ND2 ASN A 135      51.866  -4.016   2.976  1.00 70.30      A    N  
ANISOU  968  ND2 ASN A 135     9535   9309   7864  -1453   -445     97  A    N  
ATOM    969  OD1 ASN A 135      50.283  -4.239   4.539  1.00 68.93      A    O  
ANISOU  969  OD1 ASN A 135     9598   9037   7553  -1514   -315     42  A    O  
ATOM    970  N   GLY A 136      49.836  -8.023   1.977  1.00 59.03      A    N  
ANISOU  970  N   GLY A 136     7907   7791   6730  -1125   -375    114  A    N  
ATOM    971  CA  GLY A 136      49.060  -8.261   0.784  1.00 57.74      A    C  
ANISOU  971  CA  GLY A 136     7652   7607   6677  -1013   -307     42  A    C  
ATOM    972  C   GLY A 136      47.672  -8.800   1.109  1.00 63.56      A    C  
ANISOU  972  C   GLY A 136     8431   8283   7433  -1032   -218      9  A    C  
ATOM    973  O   GLY A 136      46.649  -8.299   0.607  1.00 64.57      A    O  
ANISOU  973  O   GLY A 136     8531   8411   7591  -1000   -119    -64  A    O  
ATOM    974  N   LEU A 137      47.615  -9.784   1.997  1.00 65.26      A    N  
ANISOU  974  N   LEU A 137     8711   8454   7628  -1089   -253     75  A    N  
ATOM    975  CA  LEU A 137      46.333 -10.325   2.430  1.00 66.39      A    C  
ANISOU  975  CA  LEU A 137     8892   8548   7784  -1138   -163     64  A    C  
ATOM    976  C   LEU A 137      45.439  -9.256   3.058  1.00 64.95      A    C  
ANISOU  976  C   LEU A 137     8775   8391   7512  -1199    -26     17  A    C  
ATOM    977  O   LEU A 137      44.246  -9.169   2.769  1.00 65.88      A    O  
ANISOU  977  O   LEU A 137     8843   8511   7678  -1183     81    -34  A    O  
ATOM    978  CB  LEU A 137      46.536 -11.498   3.371  1.00 64.87      A    C  
ANISOU  978  CB  LEU A 137     8782   8297   7565  -1203   -224    164  A    C  
ATOM    979  CG  LEU A 137      47.034 -12.759   2.654  1.00 60.43      A    C  
ANISOU  979  CG  LEU A 137     8165   7672   7121  -1116   -328    194  A    C  
ATOM    980  CD1 LEU A 137      47.244 -13.894   3.656  1.00 58.84      A    C  
ANISOU  980  CD1 LEU A 137     8071   7393   6892  -1175   -390    311  A    C  
ATOM    981  CD2 LEU A 137      46.097 -13.182   1.519  1.00 56.76      A    C  
ANISOU  981  CD2 LEU A 137     7613   7171   6781  -1060   -282    107  A    C  
ATOM    982  N   TYR A 138      46.020  -8.435   3.915  1.00 68.00      A    N  
ANISOU  982  N   TYR A 138     9273   8798   7766  -1267    -31     34  A    N  
ATOM    983  CA  TYR A 138      45.263  -7.383   4.569  1.00 70.96      A    C  
ANISOU  983  CA  TYR A 138     9744   9178   8038  -1311    105    -19  A    C  
ATOM    984  C   TYR A 138      44.617  -6.508   3.505  1.00 66.81      A    C  
ANISOU  984  C   TYR A 138     9127   8664   7590  -1208    191   -109  A    C  
ATOM    985  O   TYR A 138      43.460  -6.119   3.627  1.00 71.69      A    O  
ANISOU  985  O   TYR A 138     9742   9286   8208  -1185    331   -157  A    O  
ATOM    986  CB  TYR A 138      46.179  -6.537   5.452  1.00 68.54      A    C  
ANISOU  986  CB  TYR A 138     9586   8880   7575  -1399     56     -5  A    C  
ATOM    987  CG  TYR A 138      45.544  -5.247   5.908  1.00 63.42      A    C  
ANISOU  987  CG  TYR A 138     9058   8216   6823  -1417    196    -88  A    C  
ATOM    988  CD1 TYR A 138      45.627  -4.093   5.127  1.00 65.46      A    C  
ANISOU  988  CD1 TYR A 138     9298   8460   7112  -1355    225   -160  A    C  
ATOM    989  CD2 TYR A 138      44.863  -5.173   7.119  1.00 64.44      A    C  
ANISOU  989  CD2 TYR A 138     9333   8335   6815  -1488    308    -93  A    C  
ATOM    990  CE1 TYR A 138      45.015  -2.914   5.527  1.00 63.23      A    C  
ANISOU  990  CE1 TYR A 138     9146   8136   6741  -1349    360   -239  A    C  
ATOM    991  CE2 TYR A 138      44.274  -3.977   7.548  1.00 59.10      A    C  
ANISOU  991  CE2 TYR A 138     8785   7633   6037  -1480    453   -181  A    C  
ATOM    992  CZ  TYR A 138      44.330  -2.868   6.734  1.00 60.07      A    C  
ANISOU  992  CZ  TYR A 138     8891   7724   6208  -1403    478   -256  A    C  
ATOM    993  OH  TYR A 138      43.704  -1.699   7.119  1.00 79.38      A    O  
ANISOU  993  OH  TYR A 138    11476  10119   8563  -1371    628   -344  A    O  
ATOM    994  N   TYR A 139      45.380  -6.189   2.469  1.00 62.44      A    N  
ANISOU  994  N   TYR A 139     8496   8127   7101  -1140    109   -123  A    N  
ATOM    995  CA  TYR A 139      44.893  -5.350   1.385  1.00 58.80      A    C  
ANISOU  995  CA  TYR A 139     7958   7677   6704  -1038    170   -192  A    C  
ATOM    996  C   TYR A 139      43.753  -5.997   0.597  1.00 58.46      A    C  
ANISOU  996  C   TYR A 139     7781   7651   6779   -960    217   -222  A    C  
ATOM    997  O   TYR A 139      42.722  -5.365   0.369  1.00 52.14      A    O  
ANISOU  997  O   TYR A 139     6949   6864   5997   -904    325   -270  A    O  
ATOM    998  CB  TYR A 139      46.030  -4.978   0.426  1.00 57.70      A    C  
ANISOU  998  CB  TYR A 139     7762   7561   6598   -994     72   -182  A    C  
ATOM    999  CG  TYR A 139      45.535  -4.256  -0.798  1.00 52.13      A    C  
ANISOU  999  CG  TYR A 139     6980   6870   5957   -883    124   -236  A    C  
ATOM   1000  CD1 TYR A 139      45.238  -2.898  -0.746  1.00 47.81      A    C  
ANISOU 1000  CD1 TYR A 139     6515   6291   5358   -869    208   -273  A    C  
ATOM   1001  CD2 TYR A 139      45.344  -4.927  -1.995  1.00 59.45      A    C  
ANISOU 1001  CD2 TYR A 139     7771   7830   6986   -786     86   -249  A    C  
ATOM   1002  CE1 TYR A 139      44.773  -2.219  -1.858  1.00 46.22      A    C  
ANISOU 1002  CE1 TYR A 139     6253   6097   5211   -757    250   -305  A    C  
ATOM   1003  CE2 TYR A 139      44.899  -4.248  -3.149  1.00 56.38      A    C  
ANISOU 1003  CE2 TYR A 139     7318   7465   6639   -682    121   -288  A    C  
ATOM   1004  CZ  TYR A 139      44.616  -2.895  -3.065  1.00 52.83      A    C  
ANISOU 1004  CZ  TYR A 139     6943   6988   6142   -665    201   -307  A    C  
ATOM   1005  OH  TYR A 139      44.137  -2.200  -4.135  1.00 65.64      A    O  
ANISOU 1005  OH  TYR A 139     8514   8625   7798   -555    234   -330  A    O  
ATOM   1006  N   ILE A 140      43.928  -7.248   0.171  1.00 64.20      A    N  
ANISOU 1006  N   ILE A 140     8432   8375   7586   -953    131   -194  A    N  
ATOM   1007  CA  ILE A 140      42.895  -7.873  -0.659  1.00 54.49      A    C  
ANISOU 1007  CA  ILE A 140     7081   7158   6466   -901    150   -231  A    C  
ATOM   1008  C   ILE A 140      41.605  -8.056   0.142  1.00 54.05      A    C  
ANISOU 1008  C   ILE A 140     7023   7107   6404   -965    267   -228  A    C  
ATOM   1009  O   ILE A 140      40.517  -7.859  -0.379  1.00 49.44      A    O  
ANISOU 1009  O   ILE A 140     6334   6567   5883   -920    333   -268  A    O  
ATOM   1010  CB  ILE A 140      43.353  -9.193  -1.349  1.00 46.70      A    C  
ANISOU 1010  CB  ILE A 140     6040   6141   5563   -881     32   -219  A    C  
ATOM   1011  CG1 ILE A 140      43.415 -10.341  -0.379  1.00 48.78      A    C  
ANISOU 1011  CG1 ILE A 140     6372   6342   5820   -978      2   -153  A    C  
ATOM   1012  CG2 ILE A 140      44.715  -9.055  -2.028  1.00 55.65      A    C  
ANISOU 1012  CG2 ILE A 140     7166   7286   6691   -809    -62   -210  A    C  
ATOM   1013  CD1 ILE A 140      43.678 -11.650  -1.087  1.00 57.33      A    C  
ANISOU 1013  CD1 ILE A 140     7423   7365   6995   -945    -99   -153  A    C  
ATOM   1014  N   HIS A 141      41.732  -8.419   1.417  1.00 59.49      A    N  
ANISOU 1014  N   HIS A 141     7821   7767   7013  -1070    293   -172  A    N  
ATOM   1015  CA  HIS A 141      40.573  -8.610   2.266  1.00 51.73      A    C  
ANISOU 1015  CA  HIS A 141     6842   6802   6009  -1141    422   -156  A    C  
ATOM   1016  C   HIS A 141      39.825  -7.299   2.522  1.00 57.93      A    C  
ANISOU 1016  C   HIS A 141     7636   7634   6739  -1085    576   -208  A    C  
ATOM   1017  O   HIS A 141      38.598  -7.235   2.475  1.00 68.15      A    O  
ANISOU 1017  O   HIS A 141     8827   8983   8083  -1064    691   -224  A    O  
ATOM   1018  CB  HIS A 141      40.993  -9.223   3.584  1.00 50.67      A    C  
ANISOU 1018  CB  HIS A 141     6849   6628   5772  -1262    414    -76  A    C  
ATOM   1019  CG  HIS A 141      41.473 -10.627   3.467  1.00 61.08      A    C  
ANISOU 1019  CG  HIS A 141     8167   7884   7155  -1309    287    -11  A    C  
ATOM   1020  CD2 HIS A 141      41.322 -11.545   2.481  1.00 63.59      A    C  
ANISOU 1020  CD2 HIS A 141     8385   8167   7609  -1279    208    -24  A    C  
ATOM   1021  ND1 HIS A 141      42.217 -11.235   4.455  1.00 73.46      A    N  
ANISOU 1021  ND1 HIS A 141     9868   9405   8638  -1389    225     78  A    N  
ATOM   1022  CE1 HIS A 141      42.519 -12.464   4.070  1.00 83.81      A    C  
ANISOU 1022  CE1 HIS A 141    11158  10644  10040  -1392    117    123  A    C  
ATOM   1023  NE2 HIS A 141      41.977 -12.682   2.881  1.00 68.03      A    N  
ANISOU 1023  NE2 HIS A 141     9027   8645   8173  -1331    108     54  A    N  
ATOM   1024  N   ARG A 142      40.590  -6.260   2.812  1.00 59.84      A    N  
ANISOU 1024  N   ARG A 142     8002   7853   6880  -1063    577   -230  A    N  
ATOM   1025  CA  ARG A 142      40.059  -4.923   3.011  1.00 64.15      A    C  
ANISOU 1025  CA  ARG A 142     8599   8406   7367   -993    713   -288  A    C  
ATOM   1026  C   ARG A 142      39.236  -4.523   1.795  1.00 58.36      A    C  
ANISOU 1026  C   ARG A 142     7699   7717   6757   -857    745   -331  A    C  
ATOM   1027  O   ARG A 142      38.322  -3.722   1.893  1.00 68.83      A    O  
ANISOU 1027  O   ARG A 142     9004   9067   8078   -774    884   -366  A    O  
ATOM   1028  CB  ARG A 142      41.226  -3.971   3.224  1.00 64.38      A    C  
ANISOU 1028  CB  ARG A 142     8789   8380   7292  -1008    656   -306  A    C  
ATOM   1029  CG  ARG A 142      40.868  -2.547   3.513  1.00 63.23      A    C  
ANISOU 1029  CG  ARG A 142     8757   8198   7067   -946    785   -371  A    C  
ATOM   1030  CD  ARG A 142      42.129  -1.690   3.351  1.00 93.15      A    C  
ANISOU 1030  CD  ARG A 142    12673  11926  10793   -977    685   -384  A    C  
ATOM   1031  NE  ARG A 142      41.882  -0.297   3.701  1.00128.82      A    N  
ANISOU 1031  NE  ARG A 142    17351  16372  15223   -935    799   -451  A    N  
ATOM   1032  CZ  ARG A 142      42.814   0.520   4.184  1.00156.52      A    C  
ANISOU 1032  CZ  ARG A 142    21051  19804  18613  -1022    751   -472  A    C  
ATOM   1033  NH1 ARG A 142      44.052   0.073   4.366  1.00166.72      A    N1+
ANISOU 1033  NH1 ARG A 142    22364  21113  19869  -1153    588   -419  A    N1+
ATOM   1034  NH2 ARG A 142      42.505   1.777   4.482  1.00165.72      A    N  
ANISOU 1034  NH2 ARG A 142    22387  20877  19701   -978    863   -544  A    N  
ATOM   1035  N   ASN A 143      39.563  -5.108   0.648  1.00 56.67      A    N  
ANISOU 1035  N   ASN A 143     7368   7516   6647   -826    615   -327  A    N  
ATOM   1036  CA  ASN A 143      38.866  -4.834  -0.600  1.00 59.15      A    C  
ANISOU 1036  CA  ASN A 143     7526   7881   7065   -706    610   -361  A    C  
ATOM   1037  C   ASN A 143      37.856  -5.907  -0.943  1.00 63.74      A    C  
ANISOU 1037  C   ASN A 143     7940   8524   7754   -735    600   -351  A    C  
ATOM   1038  O   ASN A 143      37.433  -6.016  -2.091  1.00 71.25      A    O  
ANISOU 1038  O   ASN A 143     8755   9523   8793   -664    541   -374  A    O  
ATOM   1039  CB  ASN A 143      39.851  -4.704  -1.750  1.00 64.53      A    C  
ANISOU 1039  CB  ASN A 143     8197   8548   7774   -650    478   -370  A    C  
ATOM   1040  CG  ASN A 143      40.514  -3.356  -1.787  1.00 67.87      A    C  
ANISOU 1040  CG  ASN A 143     8735   8928   8122   -599    502   -383  A    C  
ATOM   1041  ND2 ASN A 143      41.722  -3.251  -1.203  1.00 65.03      A    N  
ANISOU 1041  ND2 ASN A 143     8507   8520   7682   -686    447   -360  A    N  
ATOM   1042  OD1 ASN A 143      39.960  -2.425  -2.347  1.00 80.85      A    O  
ANISOU 1042  OD1 ASN A 143    10352  10582   9784   -488    560   -407  A    O  
ATOM   1043  N   LYS A 144      37.477  -6.696   0.057  1.00 65.24      A    N  
ANISOU 1043  N   LYS A 144     8148   8711   7926   -853    653   -312  A    N  
ATOM   1044  CA  LYS A 144      36.395  -7.657  -0.083  1.00 72.95      A    C  
ANISOU 1044  CA  LYS A 144     8970   9744   9001   -916    666   -293  A    C  
ATOM   1045  C   LYS A 144      36.741  -8.760  -1.052  1.00 68.69      A    C  
ANISOU 1045  C   LYS A 144     8373   9173   8552   -952    498   -299  A    C  
ATOM   1046  O   LYS A 144      35.860  -9.263  -1.739  1.00 80.39      A    O  
ANISOU 1046  O   LYS A 144     9702  10709  10132   -966    468   -314  A    O  
ATOM   1047  CB  LYS A 144      35.107  -6.950  -0.525  1.00 79.59      A    C  
ANISOU 1047  CB  LYS A 144     9640  10693   9906   -815    768   -318  A    C  
ATOM   1048  CG  LYS A 144      34.625  -5.913   0.474  1.00 84.80      A    C  
ANISOU 1048  CG  LYS A 144    10361  11379  10481   -759    963   -318  A    C  
ATOM   1049  CD  LYS A 144      34.567  -6.557   1.846  1.00112.91      A    C  
ANISOU 1049  CD  LYS A 144    14015  14921  13962   -906   1052   -268  A    C  
ATOM   1050  CE  LYS A 144      34.649  -5.525   2.965  1.00113.15      A    C  
ANISOU 1050  CE  LYS A 144    14215  14929  13845   -865   1215   -285  A    C  
ATOM   1051  NZ  LYS A 144      34.998  -6.195   4.264  1.00111.83      A    N1+
ANISOU 1051  NZ  LYS A 144    14201  14726  13562  -1022   1253   -231  A    N1+
ATOM   1052  N   ILE A 145      38.007  -9.138  -1.138  1.00 57.08      A    N  
ANISOU 1052  N   ILE A 145     7021   7620   7047   -963    387   -292  A    N  
ATOM   1053  CA  ILE A 145      38.375 -10.243  -2.012  1.00 66.12      A    C  
ANISOU 1053  CA  ILE A 145     8136   8717   8267   -979    241   -306  A    C  
ATOM   1054  C   ILE A 145      38.984 -11.387  -1.224  1.00 69.55      A    C  
ANISOU 1054  C   ILE A 145     8686   9053   8687  -1089    190   -246  A    C  
ATOM   1055  O   ILE A 145      39.796 -11.147  -0.318  1.00 59.47      A    O  
ANISOU 1055  O   ILE A 145     7534   7742   7318  -1109    205   -198  A    O  
ATOM   1056  CB  ILE A 145      39.377  -9.794  -3.087  1.00 61.04      A    C  
ANISOU 1056  CB  ILE A 145     7509   8069   7613   -856    147   -349  A    C  
ATOM   1057  CG1 ILE A 145      38.820  -8.623  -3.893  1.00 53.58      A    C  
ANISOU 1057  CG1 ILE A 145     6472   7210   6673   -740    191   -393  A    C  
ATOM   1058  CG2 ILE A 145      39.719 -10.953  -3.996  1.00 56.60      A    C  
ANISOU 1058  CG2 ILE A 145     6932   7457   7117   -855     15   -378  A    C  
ATOM   1059  CD1 ILE A 145      37.574  -8.949  -4.657  1.00 54.89      A    C  
ANISOU 1059  CD1 ILE A 145     6479   7448   6928   -734    176   -426  A    C  
ATOM   1060  N   LEU A 146      38.572 -12.610  -1.559  1.00 60.68      A    N  
ANISOU 1060  N   LEU A 146     7528   7877   7650  -1165    122   -245  A    N  
ATOM   1061  CA  LEU A 146      39.162 -13.812  -0.991  1.00 55.05      A    C  
ANISOU 1061  CA  LEU A 146     6935   7041   6939  -1250     54   -184  A    C  
ATOM   1062  C   LEU A 146      40.021 -14.407  -2.084  1.00 63.81      A    C  
ANISOU 1062  C   LEU A 146     8068   8080   8096  -1160    -85   -235  A    C  
ATOM   1063  O   LEU A 146      39.572 -14.529  -3.235  1.00 69.20      A    O  
ANISOU 1063  O   LEU A 146     8663   8785   8842  -1119   -135   -314  A    O  
ATOM   1064  CB  LEU A 146      38.086 -14.822  -0.610  1.00 54.85      A    C  
ANISOU 1064  CB  LEU A 146     6879   6979   6982  -1409     81   -146  A    C  
ATOM   1065  CG  LEU A 146      37.078 -14.376   0.444  1.00 58.17      A    C  
ANISOU 1065  CG  LEU A 146     7252   7487   7363  -1504    243    -91  A    C  
ATOM   1066  CD1 LEU A 146      36.117 -15.526   0.730  1.00 60.11      A    C  
ANISOU 1066  CD1 LEU A 146     7459   7691   7687  -1684    256    -38  A    C  
ATOM   1067  CD2 LEU A 146      37.746 -13.979   1.743  1.00 56.99      A    C  
ANISOU 1067  CD2 LEU A 146     7251   7323   7078  -1519    313    -18  A    C  
ATOM   1068  N   HIS A 147      41.253 -14.764  -1.736  1.00 61.69      A    N  
ANISOU 1068  N   HIS A 147     7915   7736   7788  -1120   -148   -189  A    N  
ATOM   1069  CA  HIS A 147      42.165 -15.294  -2.735  1.00 57.98      A    C  
ANISOU 1069  CA  HIS A 147     7465   7208   7354  -1006   -259   -234  A    C  
ATOM   1070  C   HIS A 147      41.864 -16.756  -3.054  1.00 57.69      A    C  
ANISOU 1070  C   HIS A 147     7485   7030   7404  -1059   -335   -249  A    C  
ATOM   1071  O   HIS A 147      41.873 -17.163  -4.214  1.00 71.78      A    O  
ANISOU 1071  O   HIS A 147     9251   8784   9236   -992   -403   -339  A    O  
ATOM   1072  CB  HIS A 147      43.612 -15.139  -2.274  1.00 60.55      A    C  
ANISOU 1072  CB  HIS A 147     7866   7522   7618   -930   -299   -171  A    C  
ATOM   1073  CG  HIS A 147      44.606 -15.710  -3.237  1.00 56.89      A    C  
ANISOU 1073  CG  HIS A 147     7412   7012   7192   -792   -392   -207  A    C  
ATOM   1074  CD2 HIS A 147      45.472 -15.115  -4.094  1.00 55.04      A    C  
ANISOU 1074  CD2 HIS A 147     7123   6853   6937   -657   -412   -246  A    C  
ATOM   1075  ND1 HIS A 147      44.771 -17.065  -3.405  1.00 62.53      A    N  
ANISOU 1075  ND1 HIS A 147     8206   7581   7969   -779   -465   -205  A    N  
ATOM   1076  CE1 HIS A 147      45.698 -17.286  -4.314  1.00 72.06      A    C  
ANISOU 1076  CE1 HIS A 147     9407   8780   9190   -624   -520   -250  A    C  
ATOM   1077  NE2 HIS A 147      46.149 -16.117  -4.745  1.00 67.47      A    N  
ANISOU 1077  NE2 HIS A 147     8735   8343   8557   -552   -485   -270  A    N  
ATOM   1078  N   ARG A 148      41.627 -17.543  -2.013  1.00 57.76      A    N  
ANISOU 1078  N   ARG A 148     7582   6944   7420  -1185   -325   -161  A    N  
ATOM   1079  CA  ARG A 148      41.135 -18.921  -2.156  1.00 67.84      A    C  
ANISOU 1079  CA  ARG A 148     8929   8063   8782  -1281   -385   -162  A    C  
ATOM   1080  C   ARG A 148      42.133 -19.894  -2.767  1.00 73.35      A    C  
ANISOU 1080  C   ARG A 148     9741   8608   9517  -1164   -498   -189  A    C  
ATOM   1081  O   ARG A 148      41.793 -21.029  -3.098  1.00 79.68      A    O  
ANISOU 1081  O   ARG A 148    10626   9253  10393  -1223   -559   -216  A    O  
ATOM   1082  CB  ARG A 148      39.827 -18.943  -2.940  1.00 73.03      A    C  
ANISOU 1082  CB  ARG A 148     9470   8769   9508  -1369   -376   -249  A    C  
ATOM   1083  CG  ARG A 148      38.722 -18.136  -2.269  1.00 80.83      A    C  
ANISOU 1083  CG  ARG A 148    10333   9902  10475  -1479   -250   -209  A    C  
ATOM   1084  CD  ARG A 148      37.361 -18.616  -2.621  1.00 80.89      A    C  
ANISOU 1084  CD  ARG A 148    10238   9925  10571  -1631   -250   -240  A    C  
ATOM   1085  NE  ARG A 148      37.029 -18.533  -4.033  1.00 84.02      A    N  
ANISOU 1085  NE  ARG A 148    10540  10367  11014  -1572   -335   -363  A    N  
ATOM   1086  CZ  ARG A 148      35.831 -18.856  -4.511  1.00 86.17      A    C  
ANISOU 1086  CZ  ARG A 148    10695  10683  11363  -1702   -362   -401  A    C  
ATOM   1087  NH1 ARG A 148      34.867 -19.206  -3.669  1.00 93.89      A    N1+
ANISOU 1087  NH1 ARG A 148    11613  11676  12383  -1893   -288   -319  A    N1+
ATOM   1088  NH2 ARG A 148      35.568 -18.775  -5.807  1.00 81.05      A    N  
ANISOU 1088  NH2 ARG A 148     9973  10083  10737  -1648   -458   -514  A    N  
ATOM   1089  N   ASP A 149      43.380 -19.473  -2.911  1.00 81.28      A    N  
ANISOU 1089  N   ASP A 149    10753   9653  10474   -998   -522   -179  A    N  
ATOM   1090  CA  ASP A 149      44.385 -20.397  -3.409  1.00 77.56      A    C  
ANISOU 1090  CA  ASP A 149    10381   9049  10039   -858   -611   -193  A    C  
ATOM   1091  C   ASP A 149      45.769 -20.075  -2.849  1.00 73.78      A    C  
ANISOU 1091  C   ASP A 149     9912   8615   9504   -731   -628   -100  A    C  
ATOM   1092  O   ASP A 149      46.782 -20.123  -3.558  1.00 73.37      A    O  
ANISOU 1092  O   ASP A 149     9843   8576   9457   -553   -667   -133  A    O  
ATOM   1093  CB  ASP A 149      44.373 -20.427  -4.936  1.00 82.60      A    C  
ANISOU 1093  CB  ASP A 149    10979   9700  10706   -745   -646   -343  A    C  
ATOM   1094  CG  ASP A 149      45.004 -21.685  -5.503  1.00 85.21      A    C  
ANISOU 1094  CG  ASP A 149    11447   9840  11087   -631   -725   -386  A    C  
ATOM   1095  OD1 ASP A 149      45.140 -22.685  -4.745  1.00 80.46      A    O  
ANISOU 1095  OD1 ASP A 149    10981   9064  10525   -676   -761   -303  A    O  
ATOM   1096  OD2 ASP A 149      45.364 -21.642  -6.699  1.00 78.81      A    O1-
ANISOU 1096  OD2 ASP A 149    10619   9055  10268   -490   -745   -500  A    O1-
ATOM   1097  N   MET A 150      45.803 -19.806  -1.549  1.00 77.83      A    N  
ANISOU 1097  N   MET A 150    10454   9158   9960   -829   -601     22  A    N  
ATOM   1098  CA  MET A 150      47.081 -19.537  -0.869  1.00 71.37      A    C  
ANISOU 1098  CA  MET A 150     9645   8390   9079   -742   -641    127  A    C  
ATOM   1099  C   MET A 150      47.994 -20.745  -0.928  1.00 77.05      A    C  
ANISOU 1099  C   MET A 150    10461   8959   9855   -611   -734    181  A    C  
ATOM   1100  O   MET A 150      47.656 -21.818  -0.415  1.00 93.94      A    O  
ANISOU 1100  O   MET A 150    12736  10925  12032   -676   -765    243  A    O  
ATOM   1101  CB  MET A 150      46.825 -19.138   0.579  1.00 74.96      A    C  
ANISOU 1101  CB  MET A 150    10147   8889   9443   -892   -603    242  A    C  
ATOM   1102  CG  MET A 150      46.358 -17.693   0.762  1.00 80.23      A    C  
ANISOU 1102  CG  MET A 150    10725   9728  10031   -963   -510    200  A    C  
ATOM   1103  SD  MET A 150      47.768 -16.688   0.217  1.00 83.49      A    S  
ANISOU 1103  SD  MET A 150    11035  10282  10404   -810   -554    183  A    S  
ATOM   1104  CE  MET A 150      47.177 -16.150  -1.377  1.00102.43      A    C  
ANISOU 1104  CE  MET A 150    13316  12736  12864   -735   -502     23  A    C  
ATOM   1105  N   LYS A 151      49.153 -20.583  -1.554  1.00 78.11      A    N  
ANISOU 1105  N   LYS A 151    10526   9155   9995   -422   -772    166  A    N  
ATOM   1106  CA  LYS A 151      50.194 -21.615  -1.515  1.00 81.55      A    C  
ANISOU 1106  CA  LYS A 151    11031   9474  10479   -255   -854    237  A    C  
ATOM   1107  C   LYS A 151      51.524 -21.040  -1.963  1.00 82.14      A    C  
ANISOU 1107  C   LYS A 151    10966   9705  10536    -72   -873    250  A    C  
ATOM   1108  O   LYS A 151      51.567 -20.022  -2.681  1.00 85.71      A    O  
ANISOU 1108  O   LYS A 151    11291  10316  10959    -58   -820    168  A    O  
ATOM   1109  CB  LYS A 151      49.811 -22.839  -2.367  1.00 82.45      A    C  
ANISOU 1109  CB  LYS A 151    11265   9374  10688   -186   -873    143  A    C  
ATOM   1110  CG  LYS A 151      49.590 -22.535  -3.848  1.00 83.90      A    C  
ANISOU 1110  CG  LYS A 151    11376   9609  10890   -102   -833    -33  A    C  
ATOM   1111  CD  LYS A 151      49.007 -23.716  -4.577  1.00 74.40      A    C  
ANISOU 1111  CD  LYS A 151    10324   8184   9760    -89   -860   -140  A    C  
ATOM   1112  CE  LYS A 151      49.206 -23.631  -6.070  1.00 81.66      A    C  
ANISOU 1112  CE  LYS A 151    11205   9141  10680     64   -842   -304  A    C  
ATOM   1113  NZ  LYS A 151      48.244 -24.459  -6.848  1.00 96.09      A    N1+
ANISOU 1113  NZ  LYS A 151    13166  10793  12550     -5   -867   -445  A    N1+
ATOM   1114  N   ALA A 152      52.613 -21.702  -1.583  1.00 75.95      A    N  
ANISOU 1114  N   ALA A 152    10200   8880   9777     73   -948    362  A    N  
ATOM   1115  CA  ALA A 152      53.952 -21.244  -1.926  1.00 81.06      A    C  
ANISOU 1115  CA  ALA A 152    10687   9692  10417    247   -970    400  A    C  
ATOM   1116  C   ALA A 152      54.082 -20.885  -3.401  1.00 74.83      A    C  
ANISOU 1116  C   ALA A 152     9800   8980   9653    374   -898    252  A    C  
ATOM   1117  O   ALA A 152      54.729 -19.884  -3.738  1.00 77.97      A    O  
ANISOU 1117  O   ALA A 152    10032   9580  10010    404   -871    255  A    O  
ATOM   1118  CB  ALA A 152      54.989 -22.324  -1.580  1.00109.89      A    C  
ANISOU 1118  CB  ALA A 152    14378  13250  14125    441  -1057    522  A    C  
ATOM   1119  N   ALA A 153      53.505 -21.727  -4.262  1.00 72.46      A    N  
ANISOU 1119  N   ALA A 153     9609   8512   9407    441   -874    129  A    N  
ATOM   1120  CA  ALA A 153      53.681 -21.560  -5.701  1.00 66.08      A    C  
ANISOU 1120  CA  ALA A 153     8739   7762   8604    585   -812    -12  A    C  
ATOM   1121  C   ALA A 153      52.995 -20.302  -6.268  1.00 69.24      A    C  
ANISOU 1121  C   ALA A 153     9043   8321   8941    455   -744   -103  A    C  
ATOM   1122  O   ALA A 153      53.431 -19.760  -7.295  1.00 70.32      A    O  
ANISOU 1122  O   ALA A 153     9077   8588   9051    565   -691   -172  A    O  
ATOM   1123  CB  ALA A 153      53.267 -22.811  -6.444  1.00 56.51      A    C  
ANISOU 1123  CB  ALA A 153     7699   6320   7452    684   -817   -128  A    C  
ATOM   1124  N   ASN A 154      52.012 -19.797  -5.534  1.00 65.62      A    N  
ANISOU 1124  N   ASN A 154     8612   7864   8454    235   -741    -84  A    N  
ATOM   1125  CA  ASN A 154      51.287 -18.594  -5.888  1.00 62.42      A    C  
ANISOU 1125  CA  ASN A 154     8128   7593   7995    115   -680   -150  A    C  
ATOM   1126  C   ASN A 154      51.865 -17.319  -5.268  1.00 74.40      A    C  
ANISOU 1126  C   ASN A 154     9526   9292   9447     51   -664    -59  A    C  
ATOM   1127  O   ASN A 154      51.287 -16.230  -5.399  1.00 79.71      A    O  
ANISOU 1127  O   ASN A 154    10151  10061  10072    -50   -612    -97  A    O  
ATOM   1128  CB  ASN A 154      49.825 -18.732  -5.460  1.00 65.49      A    C  
ANISOU 1128  CB  ASN A 154     8603   7886   8393    -77   -671   -185  A    C  
ATOM   1129  CG  ASN A 154      49.051 -19.650  -6.366  1.00 74.58      A    C  
ANISOU 1129  CG  ASN A 154     9845   8896   9596    -59   -684   -310  A    C  
ATOM   1130  ND2 ASN A 154      47.908 -20.118  -5.895  1.00 74.66      A    N  
ANISOU 1130  ND2 ASN A 154     9935   8794   9637   -227   -693   -317  A    N  
ATOM   1131  OD1 ASN A 154      49.480 -19.943  -7.487  1.00 85.34      A    O  
ANISOU 1131  OD1 ASN A 154    11208  10253  10964     96   -684   -402  A    O  
ATOM   1132  N   VAL A 155      52.969 -17.447  -4.545  1.00 73.04      A    N  
ANISOU 1132  N   VAL A 155     9317   9161   9272    102   -718     64  A    N  
ATOM   1133  CA  VAL A 155      53.690 -16.299  -4.012  1.00 63.55      A    C  
ANISOU 1133  CA  VAL A 155     8004   8133   8007     37   -724    149  A    C  
ATOM   1134  C   VAL A 155      54.934 -16.047  -4.852  1.00 67.01      A    C  
ANISOU 1134  C   VAL A 155     8290   8710   8457    201   -715    164  A    C  
ATOM   1135  O   VAL A 155      55.807 -16.918  -4.967  1.00 72.62      A    O  
ANISOU 1135  O   VAL A 155     8971   9400   9219    368   -754    213  A    O  
ATOM   1136  CB  VAL A 155      54.077 -16.539  -2.537  1.00 59.24      A    C  
ANISOU 1136  CB  VAL A 155     7507   7569   7432    -48   -807    293  A    C  
ATOM   1137  CG1 VAL A 155      54.887 -15.377  -1.979  1.00 57.32      A    C  
ANISOU 1137  CG1 VAL A 155     7160   7503   7115   -132   -835    374  A    C  
ATOM   1138  CG2 VAL A 155      52.828 -16.772  -1.710  1.00 58.05      A    C  
ANISOU 1138  CG2 VAL A 155     7504   7294   7256   -214   -792    285  A    C  
ATOM   1139  N   LEU A 156      55.051 -14.849  -5.418  1.00 61.37      A    N  
ANISOU 1139  N   LEU A 156     7478   8141   7698    159   -657    133  A    N  
ATOM   1140  CA  LEU A 156      56.234 -14.515  -6.214  1.00 65.30      A    C  
ANISOU 1140  CA  LEU A 156     7815   8794   8200    290   -632    161  A    C  
ATOM   1141  C   LEU A 156      57.107 -13.495  -5.499  1.00 78.94      A    C  
ANISOU 1141  C   LEU A 156     9427  10681   9885    175   -671    279  A    C  
ATOM   1142  O   LEU A 156      56.629 -12.787  -4.599  1.00 80.36      A    O  
ANISOU 1142  O   LEU A 156     9673  10850  10010    -14   -696    302  A    O  
ATOM   1143  CB  LEU A 156      55.823 -13.957  -7.577  1.00 62.17      A    C  
ANISOU 1143  CB  LEU A 156     7393   8447   7778    336   -535     45  A    C  
ATOM   1144  CG  LEU A 156      54.861 -14.849  -8.355  1.00 60.54      A    C  
ANISOU 1144  CG  LEU A 156     7310   8096   7597    418   -510    -88  A    C  
ATOM   1145  CD1 LEU A 156      54.423 -14.212  -9.638  1.00 62.35      A    C  
ANISOU 1145  CD1 LEU A 156     7519   8391   7778    448   -432   -191  A    C  
ATOM   1146  CD2 LEU A 156      55.456 -16.209  -8.576  1.00 61.06      A    C  
ANISOU 1146  CD2 LEU A 156     7405   8071   7722    611   -535    -92  A    C  
ATOM   1147  N   ILE A 157      58.382 -13.402  -5.886  1.00 73.53      A    N  
ANISOU 1147  N   ILE A 157     8569  10147   9219    281   -675    353  A    N  
ATOM   1148  CA  ILE A 157      59.258 -12.366  -5.394  1.00 69.11      A    C  
ANISOU 1148  CA  ILE A 157     7877   9757   8622    153   -716    461  A    C  
ATOM   1149  C   ILE A 157      60.068 -11.762  -6.537  1.00 75.50      A    C  
ANISOU 1149  C   ILE A 157     8511  10739   9436    231   -634    467  A    C  
ATOM   1150  O   ILE A 157      60.687 -12.494  -7.288  1.00 78.97      A    O  
ANISOU 1150  O   ILE A 157     8854  11225   9924    441   -593    468  A    O  
ATOM   1151  CB  ILE A 157      60.207 -12.854  -4.291  1.00 70.51      A    C  
ANISOU 1151  CB  ILE A 157     7983   9987   8818    154   -845    607  A    C  
ATOM   1152  CG1 ILE A 157      59.442 -13.613  -3.221  1.00 68.84      A    C  
ANISOU 1152  CG1 ILE A 157     7959   9599   8596    101   -917    614  A    C  
ATOM   1153  CG2 ILE A 157      60.894 -11.649  -3.662  1.00 64.59      A    C  
ANISOU 1153  CG2 ILE A 157     7132   9397   8009    -47   -907    701  A    C  
ATOM   1154  CD1 ILE A 157      60.327 -14.007  -2.065  1.00 59.79      A    C  
ANISOU 1154  CD1 ILE A 157     6762   8509   7446     86  -1060    771  A    C  
ATOM   1155  N   THR A 158      60.106 -10.428  -6.613  1.00 77.71      A    N  
ANISOU 1155  N   THR A 158     8756  11110   9660     59   -606    481  A    N  
ATOM   1156  CA  THR A 158      60.799  -9.705  -7.671  1.00 74.37      A    C  
ANISOU 1156  CA  THR A 158     8180  10849   9228     90   -519    501  A    C  
ATOM   1157  C   THR A 158      62.295  -9.670  -7.464  1.00 77.58      A    C  
ANISOU 1157  C   THR A 158     8352  11455   9669    108   -567    647  A    C  
ATOM   1158  O   THR A 158      62.773  -9.922  -6.352  1.00 96.51      A    O  
ANISOU 1158  O   THR A 158    10714  13873  12082     43   -692    741  A    O  
ATOM   1159  CB  THR A 158      60.325  -8.236  -7.802  1.00 77.07      A    C  
ANISOU 1159  CB  THR A 158     8583  11197   9500   -112   -476    478  A    C  
ATOM   1160  CG2 THR A 158      58.857  -8.192  -8.116  1.00 74.59      A    C  
ANISOU 1160  CG2 THR A 158     8463  10718   9157   -110   -421    344  A    C  
ATOM   1161  OG1 THR A 158      60.581  -7.515  -6.584  1.00 74.58      A    O  
ANISOU 1161  OG1 THR A 158     8288  10895   9152   -334   -575    554  A    O  
ATOM   1162  N   ARG A 159      63.029  -9.350  -8.534  1.00 84.37      A    N  
ANISOU 1162  N   ARG A 159     9044  12475  10535    192   -468    674  A    N  
ATOM   1163  CA  ARG A 159      64.492  -9.322  -8.438  1.00 95.19      A    C  
ANISOU 1163  CA  ARG A 159    10146  14070  11950    218   -498    824  A    C  
ATOM   1164  C   ARG A 159      64.903  -8.372  -7.320  1.00 80.59      A    C  
ANISOU 1164  C   ARG A 159     8256  12289  10075    -65   -627    931  A    C  
ATOM   1165  O   ARG A 159      66.004  -8.497  -6.794  1.00 80.30      A    O  
ANISOU 1165  O   ARG A 159     8017  12413  10077    -82   -719   1066  A    O  
ATOM   1166  CB  ARG A 159      65.154  -8.953  -9.758  1.00109.53      A    C  
ANISOU 1166  CB  ARG A 159    11789  16063  13761    316   -350    844  A    C  
ATOM   1167  CG  ARG A 159      66.548  -9.578  -9.978  1.00126.04      A    C  
ANISOU 1167  CG  ARG A 159    13592  18372  15925    501   -333    965  A    C  
ATOM   1168  CD  ARG A 159      67.149  -9.203 -11.338  1.00117.96      A    C  
ANISOU 1168  CD  ARG A 159    12404  17534  14880    600   -155    982  A    C  
ATOM   1169  NE  ARG A 159      67.432  -7.773 -11.455  1.00125.58      A    N  
ANISOU 1169  NE  ARG A 159    13293  18619  15800    329   -135   1061  A    N  
ATOM   1170  CZ  ARG A 159      66.555  -6.862 -11.887  1.00141.16      A    C  
ANISOU 1170  CZ  ARG A 159    15454  20484  17694    181    -81    983  A    C  
ATOM   1171  NH1 ARG A 159      65.338  -7.233 -12.271  1.00141.32      A    N1+
ANISOU 1171  NH1 ARG A 159    15721  20301  17672    279    -43    826  A    N1+
ATOM   1172  NH2 ARG A 159      66.886  -5.576 -11.931  1.00136.26      A    N  
ANISOU 1172  NH2 ARG A 159    14777  19954  17040    -66    -70   1068  A    N  
ATOM   1173  N   ASP A 160      64.012  -7.468  -6.923  1.00 72.08      A    N  
ANISOU 1173  N   ASP A 160     7376  11084   8928   -280   -641    867  A    N  
ATOM   1174  CA  ASP A 160      64.344  -6.503  -5.885  1.00 76.53      A    C  
ANISOU 1174  CA  ASP A 160     7945  11685   9445   -561   -758    943  A    C  
ATOM   1175  C   ASP A 160      63.785  -6.866  -4.505  1.00 83.92      A    C  
ANISOU 1175  C   ASP A 160     9058  12482  10345   -649   -890    927  A    C  
ATOM   1176  O   ASP A 160      63.812  -6.039  -3.584  1.00 77.02      A    O  
ANISOU 1176  O   ASP A 160     8263  11597   9404   -892   -982    955  A    O  
ATOM   1177  CB  ASP A 160      63.891  -5.103  -6.281  1.00 89.34      A    C  
ANISOU 1177  CB  ASP A 160     9675  13266  11005   -756   -686    899  A    C  
ATOM   1178  CG  ASP A 160      64.459  -4.663  -7.595  1.00113.46      A    C  
ANISOU 1178  CG  ASP A 160    12569  16463  14077   -698   -556    934  A    C  
ATOM   1179  OD1 ASP A 160      64.993  -5.517  -8.332  1.00136.14      A    O  
ANISOU 1179  OD1 ASP A 160    15276  19447  17003   -470   -492    957  A    O  
ATOM   1180  OD2 ASP A 160      64.381  -3.446  -7.897  1.00129.66      A    O1-
ANISOU 1180  OD2 ASP A 160    14671  18509  16082   -878   -511    941  A    O1-
ATOM   1181  N   GLY A 161      63.287  -8.090  -4.374  1.00 82.84      A    N  
ANISOU 1181  N   GLY A 161     8996  12234  10243   -460   -894    883  A    N  
ATOM   1182  CA  GLY A 161      62.872  -8.593  -3.074  1.00 76.40      A    C  
ANISOU 1182  CA  GLY A 161     8329  11306   9394   -523  -1014    895  A    C  
ATOM   1183  C   GLY A 161      61.509  -8.124  -2.635  1.00 70.85      A    C  
ANISOU 1183  C   GLY A 161     7891  10413   8614   -655   -977    779  A    C  
ATOM   1184  O   GLY A 161      61.212  -8.067  -1.447  1.00 82.85      A    O  
ANISOU 1184  O   GLY A 161     9544  11867  10066   -792  -1066    796  A    O  
ATOM   1185  N   VAL A 162      60.664  -7.764  -3.590  1.00 62.31      A    N  
ANISOU 1185  N   VAL A 162     6885   9254   7536   -611   -840    665  A    N  
ATOM   1186  CA  VAL A 162      59.263  -7.465  -3.268  1.00 56.21      A    C  
ANISOU 1186  CA  VAL A 162     6341   8306   6710   -688   -789    553  A    C  
ATOM   1187  C   VAL A 162      58.381  -8.684  -3.539  1.00 60.69      A    C  
ANISOU 1187  C   VAL A 162     6988   8743   7326   -516   -748    479  A    C  
ATOM   1188  O   VAL A 162      58.335  -9.181  -4.649  1.00 69.66      A    O  
ANISOU 1188  O   VAL A 162     8063   9885   8519   -346   -677    431  A    O  
ATOM   1189  CB  VAL A 162      58.751  -6.252  -4.058  1.00 52.62      A    C  
ANISOU 1189  CB  VAL A 162     5933   7834   6223   -757   -680    481  A    C  
ATOM   1190  CG1 VAL A 162      57.335  -5.915  -3.638  1.00 48.43      A    C  
ANISOU 1190  CG1 VAL A 162     5616   7141   5644   -822   -629    379  A    C  
ATOM   1191  CG2 VAL A 162      59.669  -5.057  -3.859  1.00 54.24      A    C  
ANISOU 1191  CG2 VAL A 162     6071   8150   6387   -943   -721    559  A    C  
ATOM   1192  N   LEU A 163      57.684  -9.166  -2.525  1.00 65.40      A    N  
ANISOU 1192  N   LEU A 163     7731   9222   7894   -571   -792    469  A    N  
ATOM   1193  CA  LEU A 163      56.752 -10.306  -2.629  1.00 68.34      A    C  
ANISOU 1193  CA  LEU A 163     8201   9452   8312   -457   -761    405  A    C  
ATOM   1194  C   LEU A 163      55.406  -9.895  -3.244  1.00 71.18      A    C  
ANISOU 1194  C   LEU A 163     8659   9720   8664   -472   -649    276  A    C  
ATOM   1195  O   LEU A 163      54.849  -8.841  -2.909  1.00 69.00      A    O  
ANISOU 1195  O   LEU A 163     8460   9432   8324   -607   -609    244  A    O  
ATOM   1196  CB  LEU A 163      56.528 -10.902  -1.240  1.00 70.00      A    C  
ANISOU 1196  CB  LEU A 163     8530   9584   8483   -539   -846    466  A    C  
ATOM   1197  CG  LEU A 163      55.554 -12.068  -1.104  1.00 69.23      A    C  
ANISOU 1197  CG  LEU A 163     8553   9325   8425   -473   -825    424  A    C  
ATOM   1198  CD1 LEU A 163      55.943 -12.973   0.059  1.00 84.72      A    C  
ANISOU 1198  CD1 LEU A 163    10573  11244  10370   -485   -936    540  A    C  
ATOM   1199  CD2 LEU A 163      54.135 -11.543  -0.936  1.00 63.39      A    C  
ANISOU 1199  CD2 LEU A 163     7944   8499   7642   -588   -732    327  A    C  
ATOM   1200  N   LYS A 164      54.904 -10.717  -4.168  1.00 64.06      A    N  
ANISOU 1200  N   LYS A 164     7756   8755   7826   -326   -602    202  A    N  
ATOM   1201  CA  LYS A 164      53.636 -10.460  -4.837  1.00 61.63      A    C  
ANISOU 1201  CA  LYS A 164     7517   8379   7519   -326   -516     87  A    C  
ATOM   1202  C   LYS A 164      52.745 -11.668  -4.751  1.00 69.54      A    C  
ANISOU 1202  C   LYS A 164     8605   9245   8569   -282   -524     37  A    C  
ATOM   1203  O   LYS A 164      53.160 -12.786  -5.121  1.00 68.65      A    O  
ANISOU 1203  O   LYS A 164     8479   9091   8514   -153   -559     39  A    O  
ATOM   1204  CB  LYS A 164      53.838 -10.151  -6.323  1.00 58.27      A    C  
ANISOU 1204  CB  LYS A 164     7004   8027   7108   -207   -455     31  A    C  
ATOM   1205  CG  LYS A 164      54.941  -9.184  -6.648  1.00 56.38      A    C  
ANISOU 1205  CG  LYS A 164     6651   7931   6839   -225   -444     98  A    C  
ATOM   1206  CD  LYS A 164      54.500  -7.751  -6.439  1.00 62.94      A    C  
ANISOU 1206  CD  LYS A 164     7535   8771   7608   -373   -403     91  A    C  
ATOM   1207  CE  LYS A 164      55.520  -6.802  -7.038  1.00 75.16      A    C  
ANISOU 1207  CE  LYS A 164     8975  10449   9132   -395   -380    151  A    C  
ATOM   1208  NZ  LYS A 164      55.146  -5.390  -6.710  1.00 87.30      A    N1+
ANISOU 1208  NZ  LYS A 164    10598  11960  10610   -552   -350    150  A    N1+
ATOM   1209  N   LEU A 165      51.500 -11.450  -4.312  1.00 64.78      A    N  
ANISOU 1209  N   LEU A 165     8094   8571   7948   -386   -484     -9  A    N  
ATOM   1210  CA  LEU A 165      50.484 -12.479  -4.380  1.00 69.09      A    C  
ANISOU 1210  CA  LEU A 165     8709   8997   8545   -376   -480    -65  A    C  
ATOM   1211  C   LEU A 165      50.003 -12.614  -5.824  1.00 69.70      A    C  
ANISOU 1211  C   LEU A 165     8747   9077   8659   -272   -446   -173  A    C  
ATOM   1212  O   LEU A 165      49.740 -11.627  -6.502  1.00 68.65      A    O  
ANISOU 1212  O   LEU A 165     8568   9020   8495   -267   -394   -216  A    O  
ATOM   1213  CB  LEU A 165      49.297 -12.134  -3.469  1.00 67.39      A    C  
ANISOU 1213  CB  LEU A 165     8571   8735   8296   -523   -433    -72  A    C  
ATOM   1214  CG  LEU A 165      49.607 -12.031  -1.983  1.00 71.28      A    C  
ANISOU 1214  CG  LEU A 165     9139   9220   8724   -639   -460     23  A    C  
ATOM   1215  CD1 LEU A 165      48.402 -11.531  -1.180  1.00 71.84      A    C  
ANISOU 1215  CD1 LEU A 165     9284   9265   8744   -768   -379      3  A    C  
ATOM   1216  CD2 LEU A 165      50.005 -13.428  -1.524  1.00 74.04      A    C  
ANISOU 1216  CD2 LEU A 165     9536   9479   9115   -606   -539     91  A    C  
ATOM   1217  N   ALA A 166      49.897 -13.851  -6.288  1.00 59.71      A    N  
ANISOU 1217  N   ALA A 166     7517   7717   7451   -190   -481   -216  A    N  
ATOM   1218  CA  ALA A 166      49.646 -14.114  -7.694  1.00 56.91      A    C  
ANISOU 1218  CA  ALA A 166     7144   7366   7113    -80   -468   -323  A    C  
ATOM   1219  C   ALA A 166      48.529 -15.137  -7.853  1.00 66.05      A    C  
ANISOU 1219  C   ALA A 166     8385   8387   8320   -121   -495   -400  A    C  
ATOM   1220  O   ALA A 166      48.038 -15.704  -6.866  1.00 72.79      A    O  
ANISOU 1220  O   ALA A 166     9308   9143   9206   -228   -515   -356  A    O  
ATOM   1221  CB  ALA A 166      50.926 -14.630  -8.347  1.00 59.38      A    C  
ANISOU 1221  CB  ALA A 166     7420   7707   7435     91   -484   -314  A    C  
ATOM   1222  N   ASP A 167      48.116 -15.374  -9.098  1.00 65.21      A    N  
ANISOU 1222  N   ASP A 167     8281   8279   8214    -50   -498   -511  A    N  
ATOM   1223  CA  ASP A 167      47.072 -16.325  -9.405  1.00 67.42      A    C  
ANISOU 1223  CA  ASP A 167     8637   8438   8540   -104   -540   -597  A    C  
ATOM   1224  C   ASP A 167      45.740 -16.054  -8.735  1.00 73.74      A    C  
ANISOU 1224  C   ASP A 167     9423   9231   9363   -282   -526   -585  A    C  
ATOM   1225  O   ASP A 167      45.376 -16.717  -7.760  1.00 79.99      A    O  
ANISOU 1225  O   ASP A 167    10275   9918  10198   -391   -540   -533  A    O  
ATOM   1226  CB  ASP A 167      47.542 -17.697  -9.040  1.00 78.84      A    C  
ANISOU 1226  CB  ASP A 167    10196   9717  10041    -64   -592   -582  A    C  
ATOM   1227  CG  ASP A 167      46.952 -18.769  -9.931  1.00 96.32      A    C  
ANISOU 1227  CG  ASP A 167    12512  11799  12287    -47   -644   -709  A    C  
ATOM   1228  OD1 ASP A 167      45.791 -18.612 -10.382  1.00 78.45      A    O  
ANISOU 1228  OD1 ASP A 167    10230   9553  10021   -152   -659   -783  A    O  
ATOM   1229  OD2 ASP A 167      47.667 -19.765 -10.159  1.00110.30      A    O1-
ANISOU 1229  OD2 ASP A 167    14381  13446  14081     74   -674   -731  A    O1-
ATOM   1230  N   PHE A 168      44.989 -15.096  -9.282  1.00 68.76      A    N  
ANISOU 1230  N   PHE A 168     8709   8714   8701   -305   -493   -626  A    N  
ATOM   1231  CA  PHE A 168      43.661 -14.795  -8.736  1.00 70.36      A    C  
ANISOU 1231  CA  PHE A 168     8868   8933   8930   -449   -467   -617  A    C  
ATOM   1232  C   PHE A 168      42.541 -15.560  -9.439  1.00 68.95      A    C  
ANISOU 1232  C   PHE A 168     8688   8709   8798   -514   -527   -708  A    C  
ATOM   1233  O   PHE A 168      41.387 -15.196  -9.371  1.00 78.87      A    O  
ANISOU 1233  O   PHE A 168     9862  10026  10076   -606   -511   -714  A    O  
ATOM   1234  CB  PHE A 168      43.449 -13.299  -8.686  1.00 61.31      A    C  
ANISOU 1234  CB  PHE A 168     7635   7925   7735   -438   -394   -588  A    C  
ATOM   1235  CG  PHE A 168      44.199 -12.637  -7.552  1.00 71.45      A    C  
ANISOU 1235  CG  PHE A 168     8941   9224   8982   -461   -339   -490  A    C  
ATOM   1236  CD1 PHE A 168      45.571 -12.431  -7.619  1.00 68.85      A    C  
ANISOU 1236  CD1 PHE A 168     8627   8916   8614   -376   -350   -451  A    C  
ATOM   1237  CD2 PHE A 168      43.520 -12.243  -6.399  1.00 65.62      A    C  
ANISOU 1237  CD2 PHE A 168     8206   8487   8240   -574   -276   -438  A    C  
ATOM   1238  CE1 PHE A 168      46.261 -11.846  -6.559  1.00 67.58      A    C  
ANISOU 1238  CE1 PHE A 168     8488   8775   8414   -422   -323   -363  A    C  
ATOM   1239  CE2 PHE A 168      44.200 -11.656  -5.339  1.00 51.69      A    C  
ANISOU 1239  CE2 PHE A 168     6488   6731   6421   -608   -238   -361  A    C  
ATOM   1240  CZ  PHE A 168      45.568 -11.413  -5.428  1.00 51.75      A    C  
ANISOU 1240  CZ  PHE A 168     6511   6759   6389   -541   -271   -324  A    C  
ATOM   1241  N   GLY A 169      42.914 -16.683 -10.033  1.00 64.43      A    N  
ANISOU 1241  N   GLY A 169     8212   8022   8245   -469   -600   -774  A    N  
ATOM   1242  CA  GLY A 169      42.004 -17.451 -10.869  1.00 63.22      A    C  
ANISOU 1242  CA  GLY A 169     8084   7816   8121   -531   -681   -881  A    C  
ATOM   1243  C   GLY A 169      40.883 -18.115 -10.114  1.00 72.70      A    C  
ANISOU 1243  C   GLY A 169     9283   8936   9402   -733   -700   -855  A    C  
ATOM   1244  O   GLY A 169      39.807 -18.377 -10.664  1.00 99.74      A    O  
ANISOU 1244  O   GLY A 169    12662  12377  12855   -835   -759   -922  A    O  
ATOM   1245  N   LEU A 170      41.092 -18.343  -8.827  1.00 74.67      A    N  
ANISOU 1245  N   LEU A 170     9573   9115   9683   -805   -651   -747  A    N  
ATOM   1246  CA  LEU A 170      40.018 -18.900  -8.001  1.00 86.27      A    C  
ANISOU 1246  CA  LEU A 170    11032  10524  11221  -1011   -644   -698  A    C  
ATOM   1247  C   LEU A 170      39.472 -17.830  -7.071  1.00 82.39      A    C  
ANISOU 1247  C   LEU A 170    10416  10175  10711  -1072   -533   -608  A    C  
ATOM   1248  O   LEU A 170      38.597 -18.113  -6.246  1.00 82.91      A    O  
ANISOU 1248  O   LEU A 170    10452  10229  10821  -1235   -491   -548  A    O  
ATOM   1249  CB  LEU A 170      40.505 -20.086  -7.191  1.00 99.02      A    C  
ANISOU 1249  CB  LEU A 170    12810  11936  12876  -1066   -669   -636  A    C  
ATOM   1250  CG  LEU A 170      40.703 -21.460  -7.823  1.00 93.78      A    C  
ANISOU 1250  CG  LEU A 170    12309  11063  12259  -1064   -773   -715  A    C  
ATOM   1251  CD1 LEU A 170      40.587 -22.549  -6.752  1.00 87.79      A    C  
ANISOU 1251  CD1 LEU A 170    11685  10108  11561  -1205   -782   -618  A    C  
ATOM   1252  CD2 LEU A 170      39.680 -21.694  -8.932  1.00109.66      A    C  
ANISOU 1252  CD2 LEU A 170    14277  13095  14293  -1150   -850   -845  A    C  
ATOM   1253  N   ALA A 171      40.037 -16.624  -7.151  1.00 73.28      A    N  
ANISOU 1253  N   ALA A 171     9206   9147   9489   -942   -475   -594  A    N  
ATOM   1254  CA  ALA A 171      39.592 -15.576  -6.255  1.00 65.84      A    C  
ANISOU 1254  CA  ALA A 171     8181   8316   8519   -981   -363   -522  A    C  
ATOM   1255  C   ALA A 171      38.145 -15.147  -6.534  1.00 64.90      A    C  
ANISOU 1255  C   ALA A 171     7906   8312   8438  -1053   -331   -548  A    C  
ATOM   1256  O   ALA A 171      37.574 -15.439  -7.580  1.00 71.64      A    O  
ANISOU 1256  O   ALA A 171     8699   9193   9328  -1057   -412   -626  A    O  
ATOM   1257  CB  ALA A 171      40.513 -14.394  -6.306  1.00 68.98      A    C  
ANISOU 1257  CB  ALA A 171     8575   8796   8838   -842   -318   -506  A    C  
ATOM   1258  N   ARG A 172      37.559 -14.474  -5.569  1.00 73.95      A    N  
ANISOU 1258  N   ARG A 172     8990   9533   9573  -1106   -214   -480  A    N  
ATOM   1259  CA  ARG A 172      36.147 -14.147  -5.616  1.00 68.00      A    C  
ANISOU 1259  CA  ARG A 172     8069   8898   8869  -1175   -163   -481  A    C  
ATOM   1260  C   ARG A 172      35.896 -13.004  -4.615  1.00 80.39      A    C  
ANISOU 1260  C   ARG A 172     9601  10557  10387  -1144     -4   -418  A    C  
ATOM   1261  O   ARG A 172      36.501 -12.949  -3.528  1.00 63.91      A    O  
ANISOU 1261  O   ARG A 172     7630   8411   8239  -1171     63   -358  A    O  
ATOM   1262  CB  ARG A 172      35.351 -15.389  -5.205  1.00 66.25      A    C  
ANISOU 1262  CB  ARG A 172     7835   8608   8728  -1375   -187   -454  A    C  
ATOM   1263  CG  ARG A 172      34.169 -15.084  -4.314  1.00 74.69      A    C  
ANISOU 1263  CG  ARG A 172     8767   9783   9825  -1484    -55   -383  A    C  
ATOM   1264  CD  ARG A 172      33.378 -16.310  -3.964  1.00 87.27      A    C  
ANISOU 1264  CD  ARG A 172    10338  11316  11502  -1706    -78   -344  A    C  
ATOM   1265  NE  ARG A 172      31.980 -15.987  -3.720  1.00102.56      A    N  
ANISOU 1265  NE  ARG A 172    12053  13418  13495  -1796     15   -305  A    N  
ATOM   1266  CZ  ARG A 172      31.067 -15.792  -4.673  1.00 98.74      A    C  
ANISOU 1266  CZ  ARG A 172    11371  13066  13080  -1796    -48   -356  A    C  
ATOM   1267  NH1 ARG A 172      31.414 -15.844  -5.948  1.00106.77      A    N1+
ANISOU 1267  NH1 ARG A 172    12407  14063  14096  -1711   -204   -454  A    N1+
ATOM   1268  NH2 ARG A 172      29.817 -15.520  -4.362  1.00107.13      A    N  
ANISOU 1268  NH2 ARG A 172    12209  14293  14202  -1873     45   -304  A    N  
ATOM   1269  N   ALA A 173      35.013 -12.083  -4.987  1.00 80.22      A    N  
ANISOU 1269  N   ALA A 173     9425  10673  10380  -1078     51   -434  A    N  
ATOM   1270  CA  ALA A 173      34.558 -11.049  -4.042  1.00 62.10      A    C  
ANISOU 1270  CA  ALA A 173     7094   8455   8044  -1044    219   -385  A    C  
ATOM   1271  C   ALA A 173      33.671 -11.659  -2.957  1.00 66.85      A    C  
ANISOU 1271  C   ALA A 173     7645   9075   8679  -1205    321   -320  A    C  
ATOM   1272  O   ALA A 173      32.981 -12.645  -3.196  1.00 71.62      A    O  
ANISOU 1272  O   ALA A 173     8160   9681   9368  -1339    262   -314  A    O  
ATOM   1273  CB  ALA A 173      33.826  -9.955  -4.772  1.00 55.09      A    C  
ANISOU 1273  CB  ALA A 173     6055   7700   7174   -907    251   -413  A    C  
ATOM   1274  N   PHE A 174      33.702 -11.102  -1.756  1.00 73.54      A    N  
ANISOU 1274  N   PHE A 174     8560   9930   9450  -1207    473   -269  A    N  
ATOM   1275  CA  PHE A 174      32.838 -11.571  -0.687  1.00 74.04      A    C  
ANISOU 1275  CA  PHE A 174     8575  10031   9523  -1350    600   -198  A    C  
ATOM   1276  C   PHE A 174      32.124 -10.399  -0.019  1.00 82.62      A    C  
ANISOU 1276  C   PHE A 174     9593  11238  10562  -1260    799   -184  A    C  
ATOM   1277  O   PHE A 174      32.471  -9.239  -0.252  1.00 84.96      A    O  
ANISOU 1277  O   PHE A 174     9930  11547  10804  -1093    831   -228  A    O  
ATOM   1278  CB  PHE A 174      33.613 -12.407   0.341  1.00 67.81      A    C  
ANISOU 1278  CB  PHE A 174     7987   9111   8667  -1477    595   -134  A    C  
ATOM   1279  CG  PHE A 174      34.485 -11.585   1.264  1.00 71.89      A    C  
ANISOU 1279  CG  PHE A 174     8682   9592   9037  -1408    674   -119  A    C  
ATOM   1280  CD1 PHE A 174      33.954 -11.034   2.432  1.00 70.85      A    C  
ANISOU 1280  CD1 PHE A 174     8575   9525   8818  -1430    863    -78  A    C  
ATOM   1281  CD2 PHE A 174      35.797 -11.288   0.929  1.00 69.84      A    C  
ANISOU 1281  CD2 PHE A 174     8558   9252   8724  -1318    565   -152  A    C  
ATOM   1282  CE1 PHE A 174      34.739 -10.242   3.263  1.00 70.58      A    C  
ANISOU 1282  CE1 PHE A 174     8725   9455   8634  -1378    923    -79  A    C  
ATOM   1283  CE2 PHE A 174      36.604 -10.529   1.777  1.00 71.51      A    C  
ANISOU 1283  CE2 PHE A 174     8930   9438   8801  -1282    617   -138  A    C  
ATOM   1284  CZ  PHE A 174      36.084 -10.056   2.975  1.00 72.16      A    C  
ANISOU 1284  CZ  PHE A 174     9064   9565   8786  -1323    787   -104  A    C  
ATOM   1285  N   SER A 175      31.170 -10.714   0.850  1.00 95.38      A    N  
ANISOU 1285  N   SER A 175    11121  12928  12189  -1370    943   -120  A    N  
ATOM   1286  CA  SER A 175      30.361  -9.684   1.498  1.00103.67      A    C  
ANISOU 1286  CA  SER A 175    12089  14103  13197  -1272   1158   -108  A    C  
ATOM   1287  C   SER A 175      29.846 -10.107   2.862  1.00108.24      A    C  
ANISOU 1287  C   SER A 175    12693  14716  13715  -1411   1337    -26  A    C  
ATOM   1288  O   SER A 175      30.048 -11.245   3.317  1.00100.98      A    O  
ANISOU 1288  O   SER A 175    11848  13723  12794  -1600   1289     36  A    O  
ATOM   1289  CB  SER A 175      29.219  -9.269   0.601  1.00 96.57      A    C  
ANISOU 1289  CB  SER A 175    10907  13362  12420  -1178   1167   -126  A    C  
ATOM   1290  OG  SER A 175      28.476 -10.411   0.231  1.00112.12      A    O  
ANISOU 1290  OG  SER A 175    12698  15388  14512  -1355   1087    -87  A    O  
ATOM   1291  N   LEU A 176      29.283  -9.156   3.584  1.00125.90      A    N  
ANISOU 1291  N   LEU A 176    14907  17047  15881  -1306   1552    -25  A    N  
ATOM   1292  CA  LEU A 176      29.200  -9.353   5.042  1.00148.74      A    C  
ANISOU 1292  CA  LEU A 176    17931  19941  18643  -1410   1732     39  A    C  
ATOM   1293  C   LEU A 176      27.808  -9.662   5.482  1.00157.36      A    C  
ANISOU 1293  C   LEU A 176    18789  21204  19797  -1488   1917    112  A    C  
ATOM   1294  O   LEU A 176      26.858  -8.921   5.199  1.00144.27      A    O  
ANISOU 1294  O   LEU A 176    16916  19697  18203  -1348   2040     93  A    O  
ATOM   1295  CB  LEU A 176      29.828  -8.190   5.788  1.00157.24      A    C  
ANISOU 1295  CB  LEU A 176    19238  20963  19541  -1271   1846    -14  A    C  
ATOM   1296  CG  LEU A 176      31.372  -8.154   5.873  1.00160.51      A    C  
ANISOU 1296  CG  LEU A 176    19934  21205  19847  -1285   1683    -46  A    C  
ATOM   1297  CD1 LEU A 176      32.094  -8.253   4.523  1.00160.53      A    C  
ANISOU 1297  CD1 LEU A 176    19901  21135  19957  -1230   1446    -95  A    C  
ATOM   1298  CD2 LEU A 176      31.811  -6.889   6.591  1.00137.01      A    C  
ANISOU 1298  CD2 LEU A 176    17166  18192  16700  -1162   1803   -107  A    C  
ATOM   1299  N   ALA A 177      27.682 -10.811   6.151  1.00170.42      A    N  
ANISOU 1299  N   ALA A 177    20474  22836  21440  -1718   1932    208  A    N  
ATOM   1300  CA  ALA A 177      26.391 -11.454   6.418  1.00173.32      A    C  
ANISOU 1300  CA  ALA A 177    20590  23359  21901  -1867   2062    302  A    C  
ATOM   1301  C   ALA A 177      25.616 -11.656   5.084  1.00169.81      A    C  
ANISOU 1301  C   ALA A 177    19831  23018  21670  -1863   1928    280  A    C  
ATOM   1302  O   ALA A 177      26.190 -12.237   4.142  1.00163.15      A    O  
ANISOU 1302  O   ALA A 177    19027  22056  20904  -1914   1682    240  A    O  
ATOM   1303  CB  ALA A 177      25.609 -10.682   7.476  1.00155.84      A    C  
ANISOU 1303  CB  ALA A 177    18328  21301  19582  -1783   2376    332  A    C  
ATOM   1304  N   LYS A 178      24.375 -11.168   4.967  1.00174.14      A    N  
ANISOU 1304  N   LYS A 178    20076  23784  22304  -1790   2079    301  A    N  
ATOM   1305  CA  LYS A 178      23.691 -10.390   6.018  1.00186.27      A    C  
ANISOU 1305  CA  LYS A 178    21561  25466  23746  -1684   2391    335  A    C  
ATOM   1306  C   LYS A 178      22.231 -10.809   6.193  1.00192.33      A    C  
ANISOU 1306  C   LYS A 178    21967  26474  24636  -1800   2546    439  A    C  
ATOM   1307  O   LYS A 178      21.667 -11.473   5.340  1.00195.54      A    O  
ANISOU 1307  O   LYS A 178    22127  26952  25215  -1929   2396    468  A    O  
ATOM   1308  CB  LYS A 178      23.779  -8.868   5.765  1.00174.63      A    C  
ANISOU 1308  CB  LYS A 178    20110  24019  22223  -1356   2471    235  A    C  
ATOM   1309  CG  LYS A 178      23.309  -8.062   6.977  1.00169.56      A    C  
ANISOU 1309  CG  LYS A 178    19515  23470  21439  -1231   2800    246  A    C  
ATOM   1310  CD  LYS A 178      23.248  -6.551   6.866  1.00155.10      A    C  
ANISOU 1310  CD  LYS A 178    17719  21654  19557   -904   2921    152  A    C  
ATOM   1311  CE  LYS A 178      22.752  -6.042   8.219  1.00157.05      A    C  
ANISOU 1311  CE  LYS A 178    18039  21985  19646   -833   3262    169  A    C  
ATOM   1312  NZ  LYS A 178      22.619  -4.571   8.358  1.00155.96      A    N1+
ANISOU 1312  NZ  LYS A 178    17980  21845  19433   -511   3436     75  A    N1+
ATOM   1313  N   ASN A 179      21.627 -10.402   7.308  1.00194.70      A    N  
ANISOU 1313  N   ASN A 179    22236  26904  24837  -1757   2852    492  A    N  
ATOM   1314  CA  ASN A 179      20.222 -10.671   7.604  1.00208.55      A    C  
ANISOU 1314  CA  ASN A 179    23627  28918  26692  -1845   3051    602  A    C  
ATOM   1315  C   ASN A 179      20.040 -12.067   8.184  1.00214.35      A    C  
ANISOU 1315  C   ASN A 179    24367  29636  27439  -2208   3052    733  A    C  
ATOM   1316  O   ASN A 179      18.904 -12.527   8.321  1.00219.28      A    O  
ANISOU 1316  O   ASN A 179    24672  30469  28174  -2355   3174    843  A    O  
ATOM   1317  CB  ASN A 179      19.320 -10.481   6.366  1.00205.87      A    C  
ANISOU 1317  CB  ASN A 179    22884  28759  26577  -1767   2936    594  A    C  
ATOM   1318  CG  ASN A 179      19.253  -9.036   5.887  1.00212.26      A    C  
ANISOU 1318  CG  ASN A 179    23645  29620  27381  -1390   2988    496  A    C  
ATOM   1319  ND2 ASN A 179      18.949  -8.872   4.612  1.00208.21      A    N  
ANISOU 1319  ND2 ASN A 179    22907  29174  27029  -1308   2785    465  A    N  
ATOM   1320  OD1 ASN A 179      19.467  -8.083   6.644  1.00224.36      A    O  
ANISOU 1320  OD1 ASN A 179    25357  31126  28762  -1177   3202    449  A    O  
ATOM   1321  N   SER A 180      21.155 -12.726   8.529  1.00204.85      A    N  
ANISOU 1321  N   SER A 180    23521  28187  26124  -2348   2916    733  A    N  
ATOM   1322  CA  SER A 180      21.159 -14.106   9.032  1.00193.46      A    C  
ANISOU 1322  CA  SER A 180    22151  26668  24687  -2689   2879    860  A    C  
ATOM   1323  C   SER A 180      20.857 -15.126   7.910  1.00195.11      A    C  
ANISOU 1323  C   SER A 180    22169  26843  25118  -2901   2615    880  A    C  
ATOM   1324  O   SER A 180      20.553 -16.302   8.154  1.00202.55      A    O  
ANISOU 1324  O   SER A 180    23090  27750  26120  -3206   2584    994  A    O  
ATOM   1325  CB  SER A 180      20.202 -14.247  10.205  1.00172.35      A    C  
ANISOU 1325  CB  SER A 180    19350  24188  21945  -2804   3207    997  A    C  
ATOM   1326  OG  SER A 180      18.888 -13.993   9.780  1.00188.37      A    O  
ANISOU 1326  OG  SER A 180    20937  26493  24141  -2777   3322   1032  A    O  
ATOM   1327  N   GLN A 181      20.991 -14.656   6.671  1.00185.35      A    N  
ANISOU 1327  N   GLN A 181    20828  25604  23993  -2738   2416    763  A    N  
ATOM   1328  CA  GLN A 181      21.064 -15.533   5.504  1.00171.19      A    C  
ANISOU 1328  CA  GLN A 181    18967  23716  22362  -2898   2114    734  A    C  
ATOM   1329  C   GLN A 181      22.528 -15.701   5.128  1.00168.50      A    C  
ANISOU 1329  C   GLN A 181    18992  23088  21941  -2831   1890    638  A    C  
ATOM   1330  O   GLN A 181      23.219 -14.713   4.763  1.00174.22      A    O  
ANISOU 1330  O   GLN A 181    19828  23771  22597  -2562   1850    527  A    O  
ATOM   1331  CB  GLN A 181      20.311 -14.983   4.312  1.00166.66      A    C  
ANISOU 1331  CB  GLN A 181    18053  23326  21945  -2770   2015    671  A    C  
ATOM   1332  CG  GLN A 181      18.905 -14.472   4.567  1.00177.48      A    C  
ANISOU 1332  CG  GLN A 181    19017  25020  23396  -2730   2243    749  A    C  
ATOM   1333  CD  GLN A 181      18.396 -13.663   3.380  1.00175.91      A    C  
ANISOU 1333  CD  GLN A 181    18535  24983  23318  -2511   2130    674  A    C  
ATOM   1334  NE2 GLN A 181      17.076 -13.589   3.254  1.00163.99      A    N  
ANISOU 1334  NE2 GLN A 181    16598  23763  21944  -2550   2226    756  A    N  
ATOM   1335  OE1 GLN A 181      19.181 -13.118   2.576  1.00161.96      A    O  
ANISOU 1335  OE1 GLN A 181    16926  23090  21521  -2312   1956    555  A    O  
ATOM   1336  N   PRO A 182      23.013 -16.941   5.279  1.00169.07      A    N  
ANISOU 1336  N   PRO A 182    19258  22960  22021  -3074   1759    690  A    N  
ATOM   1337  CA  PRO A 182      24.408 -17.258   5.044  1.00157.04      A    C  
ANISOU 1337  CA  PRO A 182    18076  21166  20425  -3024   1563    623  A    C  
ATOM   1338  C   PRO A 182      24.760 -17.137   3.568  1.00132.04      A    C  
ANISOU 1338  C   PRO A 182    14865  17945  17359  -2910   1309    489  A    C  
ATOM   1339  O   PRO A 182      23.962 -17.477   2.693  1.00132.53      A    O  
ANISOU 1339  O   PRO A 182    14686  18097  17569  -3009   1203    472  A    O  
ATOM   1340  CB  PRO A 182      24.533 -18.715   5.515  1.00155.95      A    C  
ANISOU 1340  CB  PRO A 182    18094  20852  20306  -3327   1500    734  A    C  
ATOM   1341  CG  PRO A 182      23.389 -18.903   6.443  1.00166.91      A    C  
ANISOU 1341  CG  PRO A 182    19295  22421  21699  -3508   1743    877  A    C  
ATOM   1342  CD  PRO A 182      22.279 -18.056   5.902  1.00167.62      A    C  
ANISOU 1342  CD  PRO A 182    18998  22796  21892  -3400   1835    838  A    C  
ATOM   1343  N   ASN A 183      25.933 -16.577   3.291  1.00119.26      A    N  
ANISOU 1343  N   ASN A 183    13465  16198  15647  -2700   1218    394  A    N  
ATOM   1344  CA  ASN A 183      26.555 -16.713   1.965  1.00125.57      A    C  
ANISOU 1344  CA  ASN A 183    14309  16889  16510  -2619    965    277  A    C  
ATOM   1345  C   ASN A 183      26.695 -18.181   1.562  1.00122.91      A    C  
ANISOU 1345  C   ASN A 183    14067  16372  16262  -2855    777    292  A    C  
ATOM   1346  O   ASN A 183      26.996 -19.041   2.404  1.00127.09      A    O  
ANISOU 1346  O   ASN A 183    14778  16756  16753  -3018    806    384  A    O  
ATOM   1347  CB  ASN A 183      27.950 -16.061   1.978  1.00124.10      A    C  
ANISOU 1347  CB  ASN A 183    14384  16572  16195  -2400    918    206  A    C  
ATOM   1348  CG  ASN A 183      27.891 -14.554   2.167  1.00113.66      A    C  
ANISOU 1348  CG  ASN A 183    13001  15391  14792  -2158   1067    165  A    C  
ATOM   1349  ND2 ASN A 183      28.873 -13.995   2.877  1.00105.98      A    N  
ANISOU 1349  ND2 ASN A 183    12263  14333  13671  -2047   1127    158  A    N  
ATOM   1350  OD1 ASN A 183      26.947 -13.901   1.713  1.00121.39      A    O  
ANISOU 1350  OD1 ASN A 183    13727  16553  15842  -2076   1128    146  A    O  
ATOM   1351  N   ARG A 184      26.467 -18.461   0.280  1.00108.13      A    N  
ANISOU 1351  N   ARG A 184    12086  14499  14498  -2871    583    203  A    N  
ATOM   1352  CA  ARG A 184      26.640 -19.816  -0.235  1.00 99.45      A    C  
ANISOU 1352  CA  ARG A 184    11107  13201  13477  -3076    389    187  A    C  
ATOM   1353  C   ARG A 184      27.749 -19.862  -1.262  1.00 95.45      A    C  
ANISOU 1353  C   ARG A 184    10788  12535  12944  -2913    189     54  A    C  
ATOM   1354  O   ARG A 184      27.510 -20.065  -2.437  1.00 93.62      A    O  
ANISOU 1354  O   ARG A 184    10476  12312  12780  -2923     22    -41  A    O  
ATOM   1355  CB  ARG A 184      25.351 -20.315  -0.882  1.00104.07      A    C  
ANISOU 1355  CB  ARG A 184    11418  13913  14210  -3290    314    191  A    C  
ATOM   1356  CG  ARG A 184      24.198 -20.481   0.062  1.00111.49      A    C  
ANISOU 1356  CG  ARG A 184    12147  15014  15199  -3497    504    335  A    C  
ATOM   1357  CD  ARG A 184      22.860 -20.569  -0.668  1.00104.64      A    C  
ANISOU 1357  CD  ARG A 184    10918  14362  14478  -3646    441    334  A    C  
ATOM   1358  NE  ARG A 184      21.764 -20.781   0.269  1.00114.65      A    N  
ANISOU 1358  NE  ARG A 184    11964  15797  15799  -3858    639    487  A    N  
ATOM   1359  CZ  ARG A 184      20.543 -21.185  -0.077  1.00139.36      A    C  
ANISOU 1359  CZ  ARG A 184    14779  19098  19070  -4090    601    536  A    C  
ATOM   1360  NH1 ARG A 184      20.269 -21.423  -1.351  1.00160.52      A    N1+
ANISOU 1360  NH1 ARG A 184    17349  21796  21842  -4140    355    434  A    N1+
ATOM   1361  NH2 ARG A 184      19.603 -21.360   0.846  1.00130.04      A    N  
ANISOU 1361  NH2 ARG A 184    13394  18082  17932  -4279    808    689  A    N  
ATOM   1362  N   TYR A 185      28.979 -19.629  -0.808  1.00 99.37      A    N  
ANISOU 1362  N   TYR A 185    11528  12899  13328  -2758    211     52  A    N  
ATOM   1363  CA  TYR A 185      30.127 -19.695  -1.694  1.00104.04      A    C  
ANISOU 1363  CA  TYR A 185    12296  13346  13888  -2596     46    -57  A    C  
ATOM   1364  C   TYR A 185      30.476 -21.158  -1.930  1.00107.76      A    C  
ANISOU 1364  C   TYR A 185    12961  13566  14414  -2755   -103    -64  A    C  
ATOM   1365  O   TYR A 185      30.060 -22.026  -1.162  1.00113.32      A    O  
ANISOU 1365  O   TYR A 185    13715  14183  15155  -2976    -62     38  A    O  
ATOM   1366  CB  TYR A 185      31.327 -18.945  -1.109  1.00107.99      A    C  
ANISOU 1366  CB  TYR A 185    12964  13807  14257  -2388    116    -46  A    C  
ATOM   1367  CG  TYR A 185      31.046 -17.498  -0.766  1.00 94.64      A    C  
ANISOU 1367  CG  TYR A 185    11137  12321  12501  -2233    274    -41  A    C  
ATOM   1368  CD1 TYR A 185      30.187 -16.731  -1.554  1.00 85.07      A    C  
ANISOU 1368  CD1 TYR A 185     9683  11295  11343  -2159    281    -98  A    C  
ATOM   1369  CD2 TYR A 185      31.628 -16.893   0.355  1.00 82.05      A    C  
ANISOU 1369  CD2 TYR A 185     9665  10725  10784  -2159    411     19  A    C  
ATOM   1370  CE1 TYR A 185      29.900 -15.415  -1.226  1.00 78.55      A    C  
ANISOU 1370  CE1 TYR A 185     8749  10633  10462  -2002    433    -92  A    C  
ATOM   1371  CE2 TYR A 185      31.357 -15.571   0.675  1.00 84.00      A    C  
ANISOU 1371  CE2 TYR A 185     9818  11132  10966  -2018    559     10  A    C  
ATOM   1372  CZ  TYR A 185      30.507 -14.830  -0.138  1.00 87.97      A    C  
ANISOU 1372  CZ  TYR A 185    10089  11800  11535  -1929    573    -46  A    C  
ATOM   1373  OH  TYR A 185      30.222 -13.514   0.155  1.00 89.58      A    O  
ANISOU 1373  OH  TYR A 185    10215  12140  11681  -1769    723    -55  A    O  
HETATM 1374  N   TPO A 186      31.278 -21.409  -2.960  1.00101.09      A    N  
ANISOU 1374  N   TPO A 186    12244  12600  13566  -2634   -266   -182  A    N  
HETATM 1375  CA  TPO A 186      31.731 -22.745  -3.388  1.00 94.49      A    C  
ANISOU 1375  CA  TPO A 186    11623  11502  12776  -2729   -421   -223  A    C  
HETATM 1376  C   TPO A 186      32.638 -23.415  -2.398  1.00101.15      A    C  
ANISOU 1376  C   TPO A 186    12719  12135  13578  -2734   -389   -124  A    C  
HETATM 1377  O   TPO A 186      33.596 -22.795  -1.909  1.00101.25      A    O  
ANISOU 1377  O   TPO A 186    12810  12162  13496  -2547   -329    -93  A    O  
HETATM 1378  CB  TPO A 186      32.692 -22.480  -4.530  1.00 87.76      A    C  
ANISOU 1378  CB  TPO A 186    10861  10605  11879  -2496   -542   -364  A    C  
HETATM 1379  CG2 TPO A 186      32.780 -23.635  -5.526  1.00 78.95      A    C  
ANISOU 1379  CG2 TPO A 186     9890   9288  10817  -2572   -724   -475  A    C  
HETATM 1380  OG1 TPO A 186      32.438 -21.095  -4.935  1.00 91.67      A    O  
ANISOU 1380  OG1 TPO A 186    11147  11352  12331  -2337   -482   -402  A    O  
HETATM 1381  P   TPO A 186      32.215 -20.330  -6.308  1.00 82.42      A    P  
ANISOU 1381  P   TPO A 186     9832  10337  11147  -2198   -570   -529  A    P  
HETATM 1382  O1P TPO A 186      33.540 -20.515  -7.090  1.00 77.25      A    O  
ANISOU 1382  O1P TPO A 186     9382   9541  10427  -2007   -668   -626  A    O  
HETATM 1383  O2P TPO A 186      30.963 -20.963  -6.860  1.00 93.70      A    O1-
ANISOU 1383  O2P TPO A 186    11119  11809  12671  -2419   -668   -561  A    O1-
HETATM 1384  O3P TPO A 186      31.955 -18.966  -5.746  1.00 75.75      A    O  
ANISOU 1384  O3P TPO A 186     8819   9702  10258  -2082   -411   -464  A    O  
ATOM   1385  N   ASN A 187      32.394 -24.700  -2.120  1.00118.08      A    N  
ANISOU 1385  N   ASN A 187    15003  14072  15790  -2948   -445    -71  A    N  
ATOM   1386  CA  ASN A 187      33.223 -25.391  -1.162  1.00112.43      A    C  
ANISOU 1386  CA  ASN A 187    14536  13147  15035  -2949   -424     42  A    C  
ATOM   1387  C   ASN A 187      34.502 -25.931  -1.780  1.00116.11      A    C  
ANISOU 1387  C   ASN A 187    15236  13393  15487  -2758   -558    -38  A    C  
ATOM   1388  O   ASN A 187      35.491 -26.146  -1.080  1.00101.68      A    O  
ANISOU 1388  O   ASN A 187    13584  11447  13603  -2651   -544     45  A    O  
ATOM   1389  CB  ASN A 187      32.472 -26.485  -0.426  1.00102.73      A    C  
ANISOU 1389  CB  ASN A 187    13379  11779  13875  -3252   -401    169  A    C  
ATOM   1390  CG  ASN A 187      33.252 -26.988   0.786  1.00110.32      A    C  
ANISOU 1390  CG  ASN A 187    14574  12573  14768  -3244   -348    326  A    C  
ATOM   1391  ND2 ASN A 187      32.566 -27.571   1.730  1.00120.67      A    N  
ANISOU 1391  ND2 ASN A 187    15912  13840  16096  -3491   -263    479  A    N  
ATOM   1392  OD1 ASN A 187      34.456 -26.823   0.856  1.00114.11      A    O  
ANISOU 1392  OD1 ASN A 187    15198  12980  15177  -3016   -384    317  A    O  
ATOM   1393  N   ARG A 188      34.472 -26.178  -3.080  1.00132.76      A    N  
ANISOU 1393  N   ARG A 188    17346  15454  17642  -2715   -689   -198  A    N  
ATOM   1394  CA  ARG A 188      35.611 -26.761  -3.769  1.00136.52      A    C  
ANISOU 1394  CA  ARG A 188    18043  15722  18107  -2528   -805   -290  A    C  
ATOM   1395  C   ARG A 188      36.664 -25.696  -4.051  1.00129.54      A    C  
ANISOU 1395  C   ARG A 188    17107  14981  17128  -2225   -773   -335  A    C  
ATOM   1396  O   ARG A 188      36.988 -25.416  -5.209  1.00126.66      A    O  
ANISOU 1396  O   ARG A 188    16720  14658  16746  -2074   -843   -478  A    O  
ATOM   1397  CB  ARG A 188      35.134 -27.402  -5.079  1.00132.91      A    C  
ANISOU 1397  CB  ARG A 188    17620  15168  17712  -2604   -950   -457  A    C  
ATOM   1398  CG  ARG A 188      36.126 -28.287  -5.791  1.00139.69      A    C  
ANISOU 1398  CG  ARG A 188    18745  15759  18569  -2451  -1065   -562  A    C  
ATOM   1399  CD  ARG A 188      36.877 -27.551  -6.903  1.00167.83      A    C  
ANISOU 1399  CD  ARG A 188    22265  19445  22057  -2170  -1097   -709  A    C  
ATOM   1400  NE  ARG A 188      36.058 -27.271  -8.078  1.00166.31      A    N  
ANISOU 1400  NE  ARG A 188    21944  19381  21864  -2237  -1177   -858  A    N  
ATOM   1401  CZ  ARG A 188      36.167 -26.170  -8.819  1.00158.34      A    C  
ANISOU 1401  CZ  ARG A 188    20768  18610  20784  -2073  -1163   -934  A    C  
ATOM   1402  NH1 ARG A 188      37.068 -25.231  -8.512  1.00152.68      A    N1+
ANISOU 1402  NH1 ARG A 188    19992  18021  19996  -1845  -1066   -880  A    N1+
ATOM   1403  NH2 ARG A 188      35.375 -26.008  -9.870  1.00146.45      A    N  
ANISOU 1403  NH2 ARG A 188    19159  17211  19272  -2147  -1255  -1058  A    N  
ATOM   1404  N   VAL A 189      37.250 -25.143  -2.995  1.00114.63      A    N  
ANISOU 1404  N   VAL A 189    15219  13161  15172  -2145   -674   -209  A    N  
ATOM   1405  CA  VAL A 189      38.269 -24.095  -3.150  1.00106.45      A    C  
ANISOU 1405  CA  VAL A 189    14132  12265  14049  -1890   -643   -235  A    C  
ATOM   1406  C   VAL A 189      39.555 -24.402  -2.381  1.00108.32      A    C  
ANISOU 1406  C   VAL A 189    14536  12383  14238  -1757   -649   -132  A    C  
ATOM   1407  O   VAL A 189      39.492 -25.035  -1.328  1.00107.98      A    O  
ANISOU 1407  O   VAL A 189    14606  12224  14197  -1875   -626      2  A    O  
ATOM   1408  CB  VAL A 189      37.720 -22.726  -2.696  1.00 92.49      A    C  
ANISOU 1408  CB  VAL A 189    12152  10764  12222  -1901   -517   -199  A    C  
ATOM   1409  CG1 VAL A 189      36.779 -22.156  -3.735  1.00 81.41      A    C  
ANISOU 1409  CG1 VAL A 189    10558   9518  10853  -1924   -531   -316  A    C  
ATOM   1410  CG2 VAL A 189      37.039 -22.829  -1.340  1.00103.76      A    C  
ANISOU 1410  CG2 VAL A 189    13572  12212  13639  -2093   -407    -51  A    C  
ATOM   1411  N   VAL A 190      40.696 -23.967  -2.922  1.00 98.92      A    N  
ANISOU 1411  N   VAL A 190    13351  11230  13003  -1517   -681   -187  A    N  
ATOM   1412  CA  VAL A 190      41.997 -24.089  -2.260  1.00 96.18      A    C  
ANISOU 1412  CA  VAL A 190    13111  10822  12608  -1366   -695    -88  A    C  
ATOM   1413  C   VAL A 190      42.616 -25.477  -2.445  1.00 93.37      A    C  
ANISOU 1413  C   VAL A 190    12968  10193  12314  -1297   -791    -80  A    C  
ATOM   1414  O   VAL A 190      41.955 -26.487  -2.237  1.00 86.85      A    O  
ANISOU 1414  O   VAL A 190    12267   9178  11554  -1460   -821    -54  A    O  
ATOM   1415  CB  VAL A 190      41.919 -23.816  -0.728  1.00 93.20      A    C  
ANISOU 1415  CB  VAL A 190    12749  10496  12166  -1478   -620     83  A    C  
ATOM   1416  CG1 VAL A 190      43.327 -23.813  -0.114  1.00 94.88      A    C  
ANISOU 1416  CG1 VAL A 190    13046  10686  12318  -1312   -659    184  A    C  
ATOM   1417  CG2 VAL A 190      41.161 -22.519  -0.430  1.00 89.16      A    C  
ANISOU 1417  CG2 VAL A 190    12056  10225  11593  -1557   -506     75  A    C  
ATOM   1418  N   THR A 191      43.888 -25.513  -2.822  1.00 87.60      A    N  
ANISOU 1418  N   THR A 191    12277   9438  11565  -1054   -834    -97  A    N  
ATOM   1419  CA  THR A 191      44.613 -26.766  -2.921  1.00 88.87      A    C  
ANISOU 1419  CA  THR A 191    12642   9342  11782   -936   -913    -78  A    C  
ATOM   1420  C   THR A 191      44.472 -27.558  -1.630  1.00100.32      A    C  
ANISOU 1420  C   THR A 191    14243  10627  13247  -1071   -923    100  A    C  
ATOM   1421  O   THR A 191      44.513 -26.978  -0.533  1.00 90.89      A    O  
ANISOU 1421  O   THR A 191    12991   9561  11982  -1141   -875    237  A    O  
ATOM   1422  CB  THR A 191      46.119 -26.511  -3.139  1.00 96.43      A    C  
ANISOU 1422  CB  THR A 191    13573  10359  12705   -645   -933    -62  A    C  
ATOM   1423  CG2 THR A 191      46.880 -27.823  -2.983  1.00105.55      A    C  
ANISOU 1423  CG2 THR A 191    14940  11244  13920   -507  -1004     -3  A    C  
ATOM   1424  OG1 THR A 191      46.314 -25.960  -4.422  1.00 99.14      A    O  
ANISOU 1424  OG1 THR A 191    13812  10822  13034   -511   -921   -224  A    O  
ATOM   1425  N   LEU A 192      44.337 -28.873  -1.752  1.00107.47      A    N  
ANISOU 1425  N   LEU A 192    15360  11240  14231  -1104   -987    100  A    N  
ATOM   1426  CA  LEU A 192      44.103 -29.730  -0.586  1.00 99.45      A    C  
ANISOU 1426  CA  LEU A 192    14516  10036  13234  -1254   -999    278  A    C  
ATOM   1427  C   LEU A 192      45.091 -29.512   0.579  1.00 99.84      A    C  
ANISOU 1427  C   LEU A 192    14580  10145  13207  -1141  -1001    472  A    C  
ATOM   1428  O   LEU A 192      44.685 -29.415   1.744  1.00102.49      A    O  
ANISOU 1428  O   LEU A 192    14935  10518  13486  -1313   -960    626  A    O  
ATOM   1429  CB  LEU A 192      44.099 -31.213  -0.984  1.00 92.69      A    C  
ANISOU 1429  CB  LEU A 192    13924   8816  12477  -1248  -1082    249  A    C  
ATOM   1430  CG  LEU A 192      43.824 -32.071   0.281  1.00 99.33      A    C  
ANISOU 1430  CG  LEU A 192    14952   9457  13332  -1421  -1090    460  A    C  
ATOM   1431  CD1 LEU A 192      42.324 -32.136   0.529  1.00100.97      A    C  
ANISOU 1431  CD1 LEU A 192    15124   9674  13564  -1782  -1038    467  A    C  
ATOM   1432  CD2 LEU A 192      44.478 -33.444   0.322  1.00 96.76      A    C  
ANISOU 1432  CD2 LEU A 192    14920   8765  13077  -1293  -1179    521  A    C  
ATOM   1433  N   TRP A 193      46.386 -29.434   0.280  1.00102.45      A    N  
ANISOU 1433  N   TRP A 193    14898  10499  13528   -855  -1049    469  A    N  
ATOM   1434  CA  TRP A 193      47.389 -29.322   1.333  1.00 99.64      A    C  
ANISOU 1434  CA  TRP A 193    14555  10197  13107   -743  -1081    656  A    C  
ATOM   1435  C   TRP A 193      47.267 -28.040   2.147  1.00 99.50      A    C  
ANISOU 1435  C   TRP A 193    14365  10473  12966   -853  -1018    724  A    C  
ATOM   1436  O   TRP A 193      47.690 -27.958   3.301  1.00 98.83      A    O  
ANISOU 1436  O   TRP A 193    14319  10432  12800   -874  -1039    897  A    O  
ATOM   1437  CB  TRP A 193      48.797 -29.472   0.776  1.00 95.43      A    C  
ANISOU 1437  CB  TRP A 193    14001   9659  12599   -411  -1144    638  A    C  
ATOM   1438  CG  TRP A 193      49.070 -30.832   0.207  1.00100.33      A    C  
ANISOU 1438  CG  TRP A 193    14838   9956  13326   -265  -1204    602  A    C  
ATOM   1439  CD1 TRP A 193      48.288 -31.945   0.324  1.00112.15      A    C  
ANISOU 1439  CD1 TRP A 193    16568  11151  14891   -416  -1226    615  A    C  
ATOM   1440  CD2 TRP A 193      50.247 -31.240  -0.496  1.00107.99      A    C  
ANISOU 1440  CD2 TRP A 193    15824  10861  14344     67  -1244    558  A    C  
ATOM   1441  CE2 TRP A 193      50.090 -32.603  -0.817  1.00110.44      A    C  
ANISOU 1441  CE2 TRP A 193    16403  10810  14749    116  -1287    528  A    C  
ATOM   1442  CE3 TRP A 193      51.413 -30.587  -0.893  1.00113.64      A    C  
ANISOU 1442  CE3 TRP A 193    16353  11790  15033    325  -1241    543  A    C  
ATOM   1443  NE1 TRP A 193      48.878 -33.005  -0.326  1.00118.51      A    N  
ANISOU 1443  NE1 TRP A 193    17556  11687  15783   -197  -1282    561  A    N  
ATOM   1444  CZ2 TRP A 193      51.071 -33.331  -1.486  1.00113.80      A    C  
ANISOU 1444  CZ2 TRP A 193    16924  11076  15237    442  -1319    480  A    C  
ATOM   1445  CZ3 TRP A 193      52.390 -31.313  -1.560  1.00107.56      A    C  
ANISOU 1445  CZ3 TRP A 193    15649  10887  14329    641  -1269    507  A    C  
ATOM   1446  CH2 TRP A 193      52.208 -32.664  -1.857  1.00110.13      A    C  
ANISOU 1446  CH2 TRP A 193    16251  10849  14743    710  -1303    470  A    C  
ATOM   1447  N   TYR A 194      46.695 -27.026   1.508  1.00 86.58      A    N  
ANISOU 1447  N   TYR A 194    12550   9034  11311   -915   -945    580  A    N  
ATOM   1448  CA  TYR A 194      46.614 -25.719   2.112  1.00 81.01      A    C  
ANISOU 1448  CA  TYR A 194    11690   8594  10493   -989   -878    611  A    C  
ATOM   1449  C   TYR A 194      45.186 -25.415   2.564  1.00 89.67      A    C  
ANISOU 1449  C   TYR A 194    12763   9743  11565  -1256   -777    608  A    C  
ATOM   1450  O   TYR A 194      44.911 -24.373   3.165  1.00 92.19      A    O  
ANISOU 1450  O   TYR A 194    12982  10260  11785  -1339   -699    630  A    O  
ATOM   1451  CB  TYR A 194      47.127 -24.677   1.132  1.00 77.69      A    C  
ANISOU 1451  CB  TYR A 194    11085   8371  10063   -837   -862    474  A    C  
ATOM   1452  CG  TYR A 194      48.600 -24.829   0.804  1.00 89.04      A    C  
ANISOU 1452  CG  TYR A 194    12504   9813  11513   -576   -942    500  A    C  
ATOM   1453  CD1 TYR A 194      49.030 -25.738  -0.167  1.00 95.88      A    C  
ANISOU 1453  CD1 TYR A 194    13439  10514  12474   -397   -989    422  A    C  
ATOM   1454  CD2 TYR A 194      49.558 -24.083   1.467  1.00 87.63      A    C  
ANISOU 1454  CD2 TYR A 194    12238   9807  11248   -510   -968    600  A    C  
ATOM   1455  CE1 TYR A 194      50.373 -25.875  -0.468  1.00 92.15      A    C  
ANISOU 1455  CE1 TYR A 194    12929  10066  12017   -139  -1042    451  A    C  
ATOM   1456  CE2 TYR A 194      50.908 -24.228   1.193  1.00 86.19      A    C  
ANISOU 1456  CE2 TYR A 194    12004   9655  11086   -277  -1041    640  A    C  
ATOM   1457  CZ  TYR A 194      51.313 -25.115   0.213  1.00 95.77      A    C  
ANISOU 1457  CZ  TYR A 194    13265  10719  12401    -81  -1068    567  A    C  
ATOM   1458  OH  TYR A 194      52.659 -25.247  -0.071  1.00112.98      A    O  
ANISOU 1458  OH  TYR A 194    15370  12950  14605    170  -1122    611  A    O  
ATOM   1459  N   ARG A 195      44.270 -26.342   2.290  1.00 95.84      A    N  
ANISOU 1459  N   ARG A 195    13636  10342  12434  -1394   -774    580  A    N  
ATOM   1460  CA  ARG A 195      42.867 -26.126   2.609  1.00 95.71      A    C  
ANISOU 1460  CA  ARG A 195    13563  10388  12415  -1649   -674    577  A    C  
ATOM   1461  C   ARG A 195      42.578 -26.179   4.103  1.00 89.42      A    C  
ANISOU 1461  C   ARG A 195    12845   9606  11521  -1811   -611    764  A    C  
ATOM   1462  O   ARG A 195      42.980 -27.114   4.775  1.00 90.08      A    O  
ANISOU 1462  O   ARG A 195    13114   9510  11601  -1822   -668    906  A    O  
ATOM   1463  CB  ARG A 195      41.948 -27.088   1.860  1.00105.59      A    C  
ANISOU 1463  CB  ARG A 195    14873  11455  13791  -1781   -701    496  A    C  
ATOM   1464  CG  ARG A 195      40.468 -26.729   2.064  1.00104.07      A    C  
ANISOU 1464  CG  ARG A 195    14553  11381  13605  -2039   -594    486  A    C  
ATOM   1465  CD  ARG A 195      39.585 -27.727   1.351  1.00109.61      A    C  
ANISOU 1465  CD  ARG A 195    15310  11902  14432  -2201   -643    414  A    C  
ATOM   1466  NE  ARG A 195      39.940 -27.794  -0.060  1.00 99.16      A    N  
ANISOU 1466  NE  ARG A 195    13971  10536  13168  -2041   -735    229  A    N  
ATOM   1467  CZ  ARG A 195      39.914 -28.916  -0.774  1.00101.21      A    C  
ANISOU 1467  CZ  ARG A 195    14392  10543  13519  -2059   -836    155  A    C  
ATOM   1468  NH1 ARG A 195      39.582 -30.069  -0.207  1.00108.30      A    N1+
ANISOU 1468  NH1 ARG A 195    15483  11193  14473  -2232   -863    260  A    N1+
ATOM   1469  NH2 ARG A 195      40.282 -28.881  -2.041  1.00107.23      A    N  
ANISOU 1469  NH2 ARG A 195    15145  11291  14305  -1897   -906    -19  A    N  
ATOM   1470  N   PRO A 196      41.880 -25.157   4.622  1.00 85.68      A    N  
ANISOU 1470  N   PRO A 196    12241   9349  10961  -1926   -487    765  A    N  
ATOM   1471  CA  PRO A 196      41.522 -25.041   6.032  1.00 91.08      A    C  
ANISOU 1471  CA  PRO A 196    12992  10089  11523  -2082   -397    924  A    C  
ATOM   1472  C   PRO A 196      40.435 -26.043   6.444  1.00109.09      A    C  
ANISOU 1472  C   PRO A 196    15361  12227  13859  -2325   -344   1015  A    C  
ATOM   1473  O   PRO A 196      39.663 -26.482   5.587  1.00111.83      A    O  
ANISOU 1473  O   PRO A 196    15649  12502  14336  -2411   -350    920  A    O  
ATOM   1474  CB  PRO A 196      40.964 -23.613   6.112  1.00 83.90      A    C  
ANISOU 1474  CB  PRO A 196    11897   9446  10534  -2105   -265    843  A    C  
ATOM   1475  CG  PRO A 196      40.408 -23.373   4.765  1.00 83.09      A    C  
ANISOU 1475  CG  PRO A 196    11633   9380  10555  -2071   -268    668  A    C  
ATOM   1476  CD  PRO A 196      41.391 -24.011   3.834  1.00 84.58      A    C  
ANISOU 1476  CD  PRO A 196    11889   9416  10829  -1896   -420    608  A    C  
ATOM   1477  N   PRO A 197      40.343 -26.347   7.751  1.00109.67      A    N  
ANISOU 1477  N   PRO A 197    15568  12277  13823  -2451   -291   1199  A    N  
ATOM   1478  CA  PRO A 197      39.340 -27.243   8.341  1.00108.29      A    C  
ANISOU 1478  CA  PRO A 197    15484  11984  13674  -2707   -219   1324  A    C  
ATOM   1479  C   PRO A 197      37.929 -26.903   7.880  1.00106.14      A    C  
ANISOU 1479  C   PRO A 197    15010  11839  13478  -2884    -92   1228  A    C  
ATOM   1480  O   PRO A 197      37.214 -27.792   7.423  1.00116.48      A    O  
ANISOU 1480  O   PRO A 197    16336  13001  14920  -3043   -115   1223  A    O  
ATOM   1481  CB  PRO A 197      39.451 -26.965   9.835  1.00106.11      A    C  
ANISOU 1481  CB  PRO A 197    15310  11803  13203  -2780   -132   1502  A    C  
ATOM   1482  CG  PRO A 197      40.833 -26.452  10.028  1.00114.83      A    C  
ANISOU 1482  CG  PRO A 197    16464  12958  14207  -2548   -241   1507  A    C  
ATOM   1483  CD  PRO A 197      41.246 -25.770   8.760  1.00108.89      A    C  
ANISOU 1483  CD  PRO A 197    15540  12284  13549  -2358   -300   1303  A    C  
ATOM   1484  N   GLU A 198      37.538 -25.628   7.987  1.00 90.64      A    N  
ANISOU 1484  N   GLU A 198    12859  10143  11436  -2856     32   1155  A    N  
ATOM   1485  CA  GLU A 198      36.165 -25.194   7.655  1.00 84.64      A    C  
ANISOU 1485  CA  GLU A 198    11876   9543  10738  -3002    167   1083  A    C  
ATOM   1486  C   GLU A 198      35.695 -25.835   6.363  1.00 89.13      A    C  
ANISOU 1486  C   GLU A 198    12367   9999  11499  -3050     65    965  A    C  
ATOM   1487  O   GLU A 198      34.633 -26.448   6.300  1.00 90.85      A    O  
ANISOU 1487  O   GLU A 198    12529  10182  11808  -3277    108    998  A    O  
ATOM   1488  CB  GLU A 198      36.075 -23.667   7.477  1.00 85.07      A    C  
ANISOU 1488  CB  GLU A 198    11738   9862  10720  -2863    263    963  A    C  
ATOM   1489  CG  GLU A 198      36.794 -22.818   8.504  1.00 97.03      A    C  
ANISOU 1489  CG  GLU A 198    13341  11487  12038  -2762    324   1020  A    C  
ATOM   1490  CD  GLU A 198      38.143 -22.329   8.055  1.00 97.96      A    C  
ANISOU 1490  CD  GLU A 198    13505  11590  12124  -2529    184    944  A    C  
ATOM   1491  OE1 GLU A 198      39.108 -23.142   8.078  1.00107.43      A    O  
ANISOU 1491  OE1 GLU A 198    14865  12615  13338  -2466     37   1010  A    O  
ATOM   1492  OE2 GLU A 198      38.291 -21.151   7.676  1.00 93.80      A    O1-
ANISOU 1492  OE2 GLU A 198    12858  11219  11562  -2401    218    827  A    O1-
ATOM   1493  N   LEU A 199      36.481 -25.647   5.307  1.00 92.08      A    N  
ANISOU 1493  N   LEU A 199    12731  10331  11925  -2841    -67    822  A    N  
ATOM   1494  CA  LEU A 199      36.107 -26.145   4.005  1.00 93.94      A    C  
ANISOU 1494  CA  LEU A 199    12906  10474  12312  -2862   -171    685  A    C  
ATOM   1495  C   LEU A 199      35.981 -27.668   4.005  1.00 89.28      A    C  
ANISOU 1495  C   LEU A 199    12516   9586  11817  -3024   -263    756  A    C  
ATOM   1496  O   LEU A 199      35.016 -28.213   3.473  1.00 95.39      A    O  
ANISOU 1496  O   LEU A 199    13229  10309  12704  -3219   -282    712  A    O  
ATOM   1497  CB  LEU A 199      37.125 -25.659   2.963  1.00 99.24      A    C  
ANISOU 1497  CB  LEU A 199    13562  11155  12989  -2588   -283    533  A    C  
ATOM   1498  CG  LEU A 199      37.157 -24.132   2.832  1.00 92.64      A    C  
ANISOU 1498  CG  LEU A 199    12530  10595  12073  -2449   -198    455  A    C  
ATOM   1499  CD1 LEU A 199      38.087 -23.716   1.706  1.00 99.00      A    C  
ANISOU 1499  CD1 LEU A 199    13314  11408  12893  -2207   -304    314  A    C  
ATOM   1500  CD2 LEU A 199      35.756 -23.588   2.597  1.00 80.71      A    C  
ANISOU 1500  CD2 LEU A 199    10789   9269  10606  -2589    -91    408  A    C  
ATOM   1501  N   LEU A 200      36.956 -28.340   4.612  1.00 78.91      A    N  
ANISOU 1501  N   LEU A 200    11444   8077  10460  -2947   -327    870  A    N  
ATOM   1502  CA  LEU A 200      36.952 -29.790   4.686  1.00 81.22      A    C  
ANISOU 1502  CA  LEU A 200    11971   8050  10836  -3074   -415    952  A    C  
ATOM   1503  C   LEU A 200      35.732 -30.327   5.455  1.00 88.09      A    C  
ANISOU 1503  C   LEU A 200    12840   8900  11728  -3414   -310   1094  A    C  
ATOM   1504  O   LEU A 200      35.283 -31.441   5.223  1.00 91.06      A    O  
ANISOU 1504  O   LEU A 200    13344   9040  12213  -3600   -373   1121  A    O  
ATOM   1505  CB  LEU A 200      38.246 -30.285   5.323  1.00 91.02      A    C  
ANISOU 1505  CB  LEU A 200    13455   9116  12011  -2898   -492   1076  A    C  
ATOM   1506  CG  LEU A 200      39.512 -29.976   4.545  1.00 98.38      A    C  
ANISOU 1506  CG  LEU A 200    14395  10039  12943  -2571   -603    956  A    C  
ATOM   1507  CD1 LEU A 200      40.748 -30.202   5.423  1.00115.74      A    C  
ANISOU 1507  CD1 LEU A 200    16766  12158  15051  -2400   -657   1113  A    C  
ATOM   1508  CD2 LEU A 200      39.625 -30.736   3.245  1.00 93.63      A    C  
ANISOU 1508  CD2 LEU A 200    13869   9226  12477  -2501   -724    798  A    C  
ATOM   1509  N   LEU A 201      35.191 -29.523   6.361  1.00 93.63      A    N  
ANISOU 1509  N   LEU A 201    13401   9850  12322  -3499   -142   1183  A    N  
ATOM   1510  CA  LEU A 201      33.993 -29.895   7.098  1.00 97.49      A    C  
ANISOU 1510  CA  LEU A 201    13844  10375  12819  -3815     -8   1321  A    C  
ATOM   1511  C   LEU A 201      32.724 -29.389   6.416  1.00108.41      A    C  
ANISOU 1511  C   LEU A 201    14921  11971  14296  -3957     64   1207  A    C  
ATOM   1512  O   LEU A 201      31.650 -29.355   7.051  1.00113.16      A    O  
ANISOU 1512  O   LEU A 201    15394  12709  14892  -4193    219   1313  A    O  
ATOM   1513  CB  LEU A 201      34.060 -29.349   8.520  1.00 98.75      A    C  
ANISOU 1513  CB  LEU A 201    14031  10694  12795  -3829    153   1489  A    C  
ATOM   1514  CG  LEU A 201      34.830 -30.218   9.516  1.00 96.29      A    C  
ANISOU 1514  CG  LEU A 201    14033  10156  12394  -3840    106   1691  A    C  
ATOM   1515  CD1 LEU A 201      34.789 -29.609  10.922  1.00 96.67      A    C  
ANISOU 1515  CD1 LEU A 201    14103  10395  12232  -3875    272   1848  A    C  
ATOM   1516  CD2 LEU A 201      34.293 -31.629   9.497  1.00 98.26      A    C  
ANISOU 1516  CD2 LEU A 201    14444  10122  12767  -4096     57   1798  A    C  
ATOM   1517  N   GLY A 202      32.870 -28.889   5.191  1.00105.42      A    N  
ANISOU 1517  N   GLY A 202    14409  11658  13986  -3797    -31   1004  A    N  
ATOM   1518  CA  GLY A 202      31.720 -28.549   4.365  1.00 94.45      A    C  
ANISOU 1518  CA  GLY A 202    12742  10442  12702  -3921    -12    891  A    C  
ATOM   1519  C   GLY A 202      31.201 -27.115   4.445  1.00 94.91      A    C  
ANISOU 1519  C   GLY A 202    12507  10857  12697  -3823    138    842  A    C  
ATOM   1520  O   GLY A 202      30.038 -26.863   4.144  1.00 95.89      A    O  
ANISOU 1520  O   GLY A 202    12377  11160  12896  -3970    203    816  A    O  
ATOM   1521  N   GLU A 203      32.039 -26.171   4.866  1.00 97.48      A    N  
ANISOU 1521  N   GLU A 203    12863  11286  12886  -3580    194    833  A    N  
ATOM   1522  CA  GLU A 203      31.545 -24.791   5.025  1.00 98.56      A    C  
ANISOU 1522  CA  GLU A 203    12757  11733  12956  -3483    350    789  A    C  
ATOM   1523  C   GLU A 203      31.349 -24.071   3.685  1.00 97.51      A    C  
ANISOU 1523  C   GLU A 203    12419  11727  12902  -3340    271    603  A    C  
ATOM   1524  O   GLU A 203      32.177 -24.211   2.780  1.00 94.62      A    O  
ANISOU 1524  O   GLU A 203    12147  11239  12565  -3188    108    490  A    O  
ATOM   1525  CB  GLU A 203      32.448 -23.990   5.948  1.00 91.55      A    C  
ANISOU 1525  CB  GLU A 203    11987  10908  11889  -3301    433    838  A    C  
ATOM   1526  CG  GLU A 203      32.003 -22.559   6.129  1.00102.90      A    C  
ANISOU 1526  CG  GLU A 203    13221  12626  13249  -3186    595    783  A    C  
ATOM   1527  CD  GLU A 203      30.701 -22.402   6.897  1.00 98.44      A    C  
ANISOU 1527  CD  GLU A 203    12490  12241  12670  -3369    812    879  A    C  
ATOM   1528  OE1 GLU A 203      30.636 -22.793   8.076  1.00100.23      A    O  
ANISOU 1528  OE1 GLU A 203    12846  12440  12796  -3498    924   1032  A    O  
ATOM   1529  OE2 GLU A 203      29.729 -21.901   6.291  1.00 97.86      A    O1-
ANISOU 1529  OE2 GLU A 203    12147  12346  12688  -3381    869    809  A    O1-
ATOM   1530  N   ARG A 204      30.265 -23.311   3.552  1.00 87.91      A    N  
ANISOU 1530  N   ARG A 204    10923  10760  11716  -3379    389    577  A    N  
ATOM   1531  CA  ARG A 204      30.023 -22.527   2.344  1.00 98.23      A    C  
ANISOU 1531  CA  ARG A 204    12028  12210  13083  -3233    321    420  A    C  
ATOM   1532  C   ARG A 204      29.857 -21.056   2.687  1.00 99.78      A    C  
ANISOU 1532  C   ARG A 204    12070  12653  13189  -3051    486    402  A    C  
ATOM   1533  O   ARG A 204      29.721 -20.205   1.807  1.00106.74      A    O  
ANISOU 1533  O   ARG A 204    12795  13665  14096  -2893    452    289  A    O  
ATOM   1534  CB  ARG A 204      28.785 -23.036   1.608  1.00104.63      A    C  
ANISOU 1534  CB  ARG A 204    12622  13086  14045  -3443    265    393  A    C  
ATOM   1535  CG  ARG A 204      28.956 -24.416   1.018  1.00112.58      A    C  
ANISOU 1535  CG  ARG A 204    13798  13830  15147  -3609     73    368  A    C  
ATOM   1536  CD  ARG A 204      27.654 -24.935   0.443  1.00122.08      A    C  
ANISOU 1536  CD  ARG A 204    14786  15108  16491  -3871     20    357  A    C  
ATOM   1537  NE  ARG A 204      27.121 -24.053  -0.592  1.00122.02      A    N  
ANISOU 1537  NE  ARG A 204    14509  15328  16522  -3753    -27    234  A    N  
ATOM   1538  CZ  ARG A 204      27.455 -24.126  -1.872  1.00120.98      A    C  
ANISOU 1538  CZ  ARG A 204    14413  15135  16419  -3657   -222     78  A    C  
ATOM   1539  NH1 ARG A 204      28.362 -25.013  -2.273  1.00133.06      A    N1+
ANISOU 1539  NH1 ARG A 204    16234  16378  17944  -3643   -373     14  A    N1+
ATOM   1540  NH2 ARG A 204      26.917 -23.285  -2.747  1.00110.37      A    N  
ANISOU 1540  NH2 ARG A 204    12821  14016  15098  -3553   -260    -11  A    N  
ATOM   1541  N   ASP A 205      29.799 -20.775   3.981  1.00 92.78      A    N  
ANISOU 1541  N   ASP A 205    11237  11824  12190  -3082    669    517  A    N  
ATOM   1542  CA  ASP A 205      29.734 -19.424   4.469  1.00 99.95      A    C  
ANISOU 1542  CA  ASP A 205    12062  12924  12988  -2909    837    500  A    C  
ATOM   1543  C   ASP A 205      31.032 -19.132   5.206  1.00 97.53      A    C  
ANISOU 1543  C   ASP A 205    12024  12512  12520  -2779    834    521  A    C  
ATOM   1544  O   ASP A 205      31.059 -18.967   6.429  1.00 96.33      A    O  
ANISOU 1544  O   ASP A 205    11972  12391  12235  -2820    982    619  A    O  
ATOM   1545  CB  ASP A 205      28.540 -19.266   5.412  1.00111.03      A    C  
ANISOU 1545  CB  ASP A 205    13306  14508  14372  -3049   1073    608  A    C  
ATOM   1546  CG  ASP A 205      28.230 -17.822   5.701  1.00115.91      A    C  
ANISOU 1546  CG  ASP A 205    13798  15338  14905  -2853   1255    562  A    C  
ATOM   1547  OD1 ASP A 205      28.667 -16.959   4.903  1.00125.96      A    O  
ANISOU 1547  OD1 ASP A 205    15040  16636  16181  -2637   1177    440  A    O  
ATOM   1548  OD2 ASP A 205      27.538 -17.546   6.708  1.00116.40      A    O1-
ANISOU 1548  OD2 ASP A 205    13798  15534  14892  -2910   1482    649  A    O1-
ATOM   1549  N   TYR A 206      32.116 -19.041   4.449  1.00 90.15      A    N  
ANISOU 1549  N   TYR A 206    11198  11466  11589  -2622    663    430  A    N  
ATOM   1550  CA  TYR A 206      33.445 -18.783   5.010  1.00 86.21      A    C  
ANISOU 1550  CA  TYR A 206    10926  10875  10953  -2497    623    448  A    C  
ATOM   1551  C   TYR A 206      33.901 -17.398   4.559  1.00 84.91      A    C  
ANISOU 1551  C   TYR A 206    10705  10822  10732  -2272    636    335  A    C  
ATOM   1552  O   TYR A 206      33.209 -16.752   3.764  1.00 74.94      A    O  
ANISOU 1552  O   TYR A 206     9246   9685   9543  -2205    663    250  A    O  
ATOM   1553  CB  TYR A 206      34.428 -19.851   4.528  1.00 75.36      A    C  
ANISOU 1553  CB  TYR A 206     9723   9277   9632  -2492    420    449  A    C  
ATOM   1554  CG  TYR A 206      34.422 -19.998   3.033  1.00 81.14      A    C  
ANISOU 1554  CG  TYR A 206    10355   9978  10496  -2419    275    316  A    C  
ATOM   1555  CD1 TYR A 206      35.138 -19.112   2.236  1.00 73.21      A    C  
ANISOU 1555  CD1 TYR A 206     9319   9027   9469  -2204    214    204  A    C  
ATOM   1556  CD2 TYR A 206      33.665 -20.996   2.405  1.00 89.53      A    C  
ANISOU 1556  CD2 TYR A 206    11359  10963  11695  -2578    202    303  A    C  
ATOM   1557  CE1 TYR A 206      35.097 -19.204   0.857  1.00 72.22      A    C  
ANISOU 1557  CE1 TYR A 206     9108   8890   9440  -2134     92     84  A    C  
ATOM   1558  CE2 TYR A 206      33.625 -21.101   1.026  1.00 90.28      A    C  
ANISOU 1558  CE2 TYR A 206    11376  11039  11885  -2515     66    170  A    C  
ATOM   1559  CZ  TYR A 206      34.368 -20.210   0.254  1.00 78.72      A    C  
ANISOU 1559  CZ  TYR A 206     9889   9637  10383  -2283     13     62  A    C  
ATOM   1560  OH  TYR A 206      34.354 -20.304  -1.118  1.00 74.81      A    O  
ANISOU 1560  OH  TYR A 206     9332   9131   9958  -2215   -115    -65  A    O  
ATOM   1561  N   GLY A 207      35.022 -16.931   5.101  1.00 87.80      A    N  
ANISOU 1561  N   GLY A 207    11242  11148  10967  -2168    615    346  A    N  
ATOM   1562  CA  GLY A 207      35.559 -15.624   4.761  1.00 77.18      A    C  
ANISOU 1562  CA  GLY A 207     9878   9886   9560  -1980    623    251  A    C  
ATOM   1563  C   GLY A 207      37.070 -15.585   4.774  1.00 78.70      A    C  
ANISOU 1563  C   GLY A 207    10240   9980   9682  -1883    486    250  A    C  
ATOM   1564  O   GLY A 207      37.742 -16.607   4.568  1.00 72.49      A    O  
ANISOU 1564  O   GLY A 207     9544   9056   8942  -1905    346    288  A    O  
ATOM   1565  N   PRO A 208      37.641 -14.400   5.080  1.00 75.19      A    N  
ANISOU 1565  N   PRO A 208     9845   9601   9121  -1776    527    212  A    N  
ATOM   1566  CA  PRO A 208      39.097 -14.158   5.053  1.00 67.94      A    C  
ANISOU 1566  CA  PRO A 208     9051   8628   8136  -1685    398    209  A    C  
ATOM   1567  C   PRO A 208      39.931 -15.174   5.818  1.00 69.17      A    C  
ANISOU 1567  C   PRO A 208     9370   8671   8238  -1755    299    324  A    C  
ATOM   1568  O   PRO A 208      41.067 -15.427   5.432  1.00 77.42      A    O  
ANISOU 1568  O   PRO A 208    10461   9653   9299  -1673    153    328  A    O  
ATOM   1569  CB  PRO A 208      39.240 -12.761   5.626  1.00 62.84      A    C  
ANISOU 1569  CB  PRO A 208     8451   8071   7351  -1630    499    171  A    C  
ATOM   1570  CG  PRO A 208      37.945 -12.090   5.222  1.00 65.97      A    C  
ANISOU 1570  CG  PRO A 208     8689   8569   7805  -1598    648    101  A    C  
ATOM   1571  CD  PRO A 208      36.886 -13.150   5.214  1.00 70.92      A    C  
ANISOU 1571  CD  PRO A 208     9217   9195   8533  -1717    689    153  A    C  
ATOM   1572  N   PRO A 209      39.385 -15.745   6.899  1.00 71.00      A    N  
ANISOU 1572  N   PRO A 209     9686   8886   8404  -1896    383    428  A    N  
ATOM   1573  CA  PRO A 209      40.204 -16.700   7.658  1.00 78.41      A    C  
ANISOU 1573  CA  PRO A 209    10797   9711   9282  -1953    279    556  A    C  
ATOM   1574  C   PRO A 209      40.743 -17.871   6.836  1.00 77.65      A    C  
ANISOU 1574  C   PRO A 209    10707   9465   9330  -1912    114    572  A    C  
ATOM   1575  O   PRO A 209      41.745 -18.463   7.233  1.00 82.56      A    O  
ANISOU 1575  O   PRO A 209    11457   9998   9914  -1884     -5    661  A    O  
ATOM   1576  CB  PRO A 209      39.265 -17.161   8.755  1.00 74.61      A    C  
ANISOU 1576  CB  PRO A 209    10381   9239   8727  -2123    419    661  A    C  
ATOM   1577  CG  PRO A 209      38.422 -15.963   9.022  1.00 73.26      A    C  
ANISOU 1577  CG  PRO A 209    10127   9226   8482  -2116    608    588  A    C  
ATOM   1578  CD  PRO A 209      38.197 -15.321   7.659  1.00 70.73      A    C  
ANISOU 1578  CD  PRO A 209     9618   8953   8302  -1989    586    444  A    C  
ATOM   1579  N   ILE A 210      40.125 -18.211   5.710  1.00 73.13      A    N  
ANISOU 1579  N   ILE A 210    10006   8863   8914  -1899    100    487  A    N  
ATOM   1580  CA  ILE A 210      40.662 -19.338   4.928  1.00 80.78      A    C  
ANISOU 1580  CA  ILE A 210    11016   9670  10005  -1852    -51    485  A    C  
ATOM   1581  C   ILE A 210      42.009 -18.994   4.301  1.00 80.24      A    C  
ANISOU 1581  C   ILE A 210    10949   9601   9934  -1661   -174    435  A    C  
ATOM   1582  O   ILE A 210      42.883 -19.866   4.168  1.00 85.29      A    O  
ANISOU 1582  O   ILE A 210    11681  10113  10613  -1592   -297    484  A    O  
ATOM   1583  CB  ILE A 210      39.702 -19.846   3.822  1.00 67.56      A    C  
ANISOU 1583  CB  ILE A 210     9225   7955   8487  -1897    -57    394  A    C  
ATOM   1584  CG1 ILE A 210      39.653 -18.846   2.661  1.00 71.84      A    C  
ANISOU 1584  CG1 ILE A 210     9606   8622   9068  -1764    -59    245  A    C  
ATOM   1585  CG2 ILE A 210      38.315 -20.155   4.379  1.00 68.31      A    C  
ANISOU 1585  CG2 ILE A 210     9273   8079   8602  -2102     68    448  A    C  
ATOM   1586  CD1 ILE A 210      38.881 -19.354   1.459  1.00 72.62      A    C  
ANISOU 1586  CD1 ILE A 210     9601   8687   9304  -1791   -105    147  A    C  
ATOM   1587  N   ASP A 211      42.181 -17.728   3.921  1.00 68.28      A    N  
ANISOU 1587  N   ASP A 211     9334   8229   8377  -1573   -135    347  A    N  
ATOM   1588  CA  ASP A 211      43.451 -17.294   3.342  1.00 68.25      A    C  
ANISOU 1588  CA  ASP A 211     9312   8252   8365  -1412   -236    310  A    C  
ATOM   1589  C   ASP A 211      44.557 -17.293   4.392  1.00 71.47      A    C  
ANISOU 1589  C   ASP A 211     9837   8658   8659  -1404   -302    427  A    C  
ATOM   1590  O   ASP A 211      45.738 -17.558   4.098  1.00 68.71      A    O  
ANISOU 1590  O   ASP A 211     9496   8282   8328  -1287   -421    453  A    O  
ATOM   1591  CB  ASP A 211      43.319 -15.930   2.668  1.00 60.05      A    C  
ANISOU 1591  CB  ASP A 211     8150   7354   7312  -1339   -176    199  A    C  
ATOM   1592  CG  ASP A 211      42.582 -16.003   1.337  1.00 71.08      A    C  
ANISOU 1592  CG  ASP A 211     9423   8756   8828  -1294   -169     85  A    C  
ATOM   1593  OD1 ASP A 211      42.534 -17.132   0.764  1.00 82.47      A    O  
ANISOU 1593  OD1 ASP A 211    10885  10083  10366  -1290   -245     74  A    O  
ATOM   1594  OD2 ASP A 211      42.068 -14.955   0.864  1.00 63.93      A    O1-
ANISOU 1594  OD2 ASP A 211     8414   7960   7915  -1260    -97      8  A    O1-
ATOM   1595  N   LEU A 212      44.170 -17.020   5.634  1.00 69.06      A    N  
ANISOU 1595  N   LEU A 212     9619   8392   8229  -1529   -224    502  A    N  
ATOM   1596  CA  LEU A 212      45.157 -16.922   6.704  1.00 67.68      A    C  
ANISOU 1596  CA  LEU A 212     9563   8236   7915  -1541   -296    613  A    C  
ATOM   1597  C   LEU A 212      45.656 -18.294   7.149  1.00 71.18      A    C  
ANISOU 1597  C   LEU A 212    10122   8540   8383  -1544   -407    750  A    C  
ATOM   1598  O   LEU A 212      46.832 -18.451   7.508  1.00 69.40      A    O  
ANISOU 1598  O   LEU A 212     9944   8315   8108  -1475   -534    835  A    O  
ATOM   1599  CB  LEU A 212      44.599 -16.092   7.852  1.00 69.30      A    C  
ANISOU 1599  CB  LEU A 212     9844   8534   7951  -1664   -173    632  A    C  
ATOM   1600  CG  LEU A 212      44.814 -14.616   7.540  1.00 79.08      A    C  
ANISOU 1600  CG  LEU A 212    11015   9893   9135  -1611   -131    520  A    C  
ATOM   1601  CD1 LEU A 212      43.745 -13.724   8.132  1.00106.99      A    C  
ANISOU 1601  CD1 LEU A 212    14577  13504  12571  -1692     52    468  A    C  
ATOM   1602  CD2 LEU A 212      46.185 -14.208   8.060  1.00 85.04      A    C  
ANISOU 1602  CD2 LEU A 212    11839  10693   9778  -1589   -262    575  A    C  
ATOM   1603  N   TRP A 213      44.768 -19.288   7.107  1.00 71.07      A    N  
ANISOU 1603  N   TRP A 213    10148   8404   8450  -1625   -364    779  A    N  
ATOM   1604  CA  TRP A 213      45.178 -20.658   7.344  1.00 79.20      A    C  
ANISOU 1604  CA  TRP A 213    11300   9259   9530  -1615   -469    901  A    C  
ATOM   1605  C   TRP A 213      46.292 -20.996   6.384  1.00 73.68      A    C  
ANISOU 1605  C   TRP A 213    10552   8507   8936  -1415   -606    864  A    C  
ATOM   1606  O   TRP A 213      47.311 -21.592   6.765  1.00 70.77      A    O  
ANISOU 1606  O   TRP A 213    10262   8074   8551  -1327   -728    978  A    O  
ATOM   1607  CB  TRP A 213      44.020 -21.618   7.137  1.00 80.34      A    C  
ANISOU 1607  CB  TRP A 213    11478   9267   9779  -1737   -406    905  A    C  
ATOM   1608  CG  TRP A 213      44.457 -23.049   7.196  1.00 79.08      A    C  
ANISOU 1608  CG  TRP A 213    11463   8886   9694  -1710   -519   1013  A    C  
ATOM   1609  CD1 TRP A 213      44.897 -23.815   6.160  1.00 79.12      A    C  
ANISOU 1609  CD1 TRP A 213    11470   8745   9844  -1576   -618    954  A    C  
ATOM   1610  CD2 TRP A 213      44.505 -23.876   8.361  1.00 88.46      A    C  
ANISOU 1610  CD2 TRP A 213    12838   9965  10808  -1809   -542   1202  A    C  
ATOM   1611  CE2 TRP A 213      44.971 -25.142   7.954  1.00 90.69      A    C  
ANISOU 1611  CE2 TRP A 213    13230  10017  11210  -1723   -660   1253  A    C  
ATOM   1612  CE3 TRP A 213      44.189 -23.674   9.708  1.00 87.66      A    C  
ANISOU 1612  CE3 TRP A 213    12836   9931  10537  -1957   -469   1333  A    C  
ATOM   1613  NE1 TRP A 213      45.215 -25.077   6.607  1.00 88.06      A    N  
ANISOU 1613  NE1 TRP A 213    12783   9666  11008  -1577   -701   1091  A    N  
ATOM   1614  CZ2 TRP A 213      45.135 -26.203   8.848  1.00 85.21      A    C  
ANISOU 1614  CZ2 TRP A 213    12740   9151  10484  -1780   -714   1444  A    C  
ATOM   1615  CZ3 TRP A 213      44.349 -24.724  10.597  1.00 96.52      A    C  
ANISOU 1615  CZ3 TRP A 213    14155  10901  11614  -2024   -522   1525  A    C  
ATOM   1616  CH2 TRP A 213      44.821 -25.978  10.157  1.00 91.61      A    C  
ANISOU 1616  CH2 TRP A 213    13639  10041  11127  -1934   -648   1584  A    C  
ATOM   1617  N   GLY A 214      46.102 -20.604   5.123  1.00 75.94      A    N  
ANISOU 1617  N   GLY A 214    10701   8829   9323  -1333   -582    709  A    N  
ATOM   1618  CA  GLY A 214      47.122 -20.861   4.103  1.00 73.90      A    C  
ANISOU 1618  CA  GLY A 214    10384   8539   9155  -1133   -685    657  A    C  
ATOM   1619  C   GLY A 214      48.437 -20.140   4.428  1.00 83.04      A    C  
ANISOU 1619  C   GLY A 214    11491   9831  10228  -1029   -760    711  A    C  
ATOM   1620  O   GLY A 214      49.526 -20.665   4.175  1.00 82.96      A    O  
ANISOU 1620  O   GLY A 214    11475   9782  10263   -873   -867    761  A    O  
ATOM   1621  N   ALA A 215      48.322 -18.946   4.992  1.00 83.43      A    N  
ANISOU 1621  N   ALA A 215    11505  10037  10158  -1118   -702    700  A    N  
ATOM   1622  CA  ALA A 215      49.461 -18.149   5.370  1.00 78.35      A    C  
ANISOU 1622  CA  ALA A 215    10817   9530   9422  -1072   -776    745  A    C  
ATOM   1623  C   ALA A 215      50.252 -18.909   6.419  1.00 80.77      A    C  
ANISOU 1623  C   ALA A 215    11234   9789   9665  -1068   -897    921  A    C  
ATOM   1624  O   ALA A 215      51.482 -19.002   6.354  1.00 79.05      A    O  
ANISOU 1624  O   ALA A 215    10958   9619   9456   -945  -1019    987  A    O  
ATOM   1625  CB  ALA A 215      49.012 -16.791   5.939  1.00 77.57      A    C  
ANISOU 1625  CB  ALA A 215    10716   9566   9189  -1202   -684    698  A    C  
ATOM   1626  N   GLY A 216      49.526 -19.470   7.384  1.00 83.39      A    N  
ANISOU 1626  N   GLY A 216    11718  10035   9931  -1200   -861   1008  A    N  
ATOM   1627  CA  GLY A 216      50.127 -20.367   8.353  1.00 88.44      A    C  
ANISOU 1627  CA  GLY A 216    12489  10598  10513  -1196   -976   1191  A    C  
ATOM   1628  C   GLY A 216      50.943 -21.485   7.713  1.00 89.37      A    C  
ANISOU 1628  C   GLY A 216    12593  10586  10775  -1000  -1092   1243  A    C  
ATOM   1629  O   GLY A 216      52.124 -21.669   8.043  1.00 82.39      A    O  
ANISOU 1629  O   GLY A 216    11691   9745   9867   -887  -1230   1357  A    O  
ATOM   1630  N   CYS A 217      50.330 -22.240   6.804  1.00 86.22      A    N  
ANISOU 1630  N   CYS A 217    12205  10030  10524   -954  -1042   1161  A    N  
ATOM   1631  CA  CYS A 217      50.994 -23.368   6.163  1.00 86.33      A    C  
ANISOU 1631  CA  CYS A 217    12244   9884  10674   -759  -1133   1190  A    C  
ATOM   1632  C   CYS A 217      52.265 -22.941   5.450  1.00 88.94      A    C  
ANISOU 1632  C   CYS A 217    12405  10342  11045   -548  -1206   1157  A    C  
ATOM   1633  O   CYS A 217      53.273 -23.666   5.430  1.00105.01      A    O  
ANISOU 1633  O   CYS A 217    14444  12320  13133   -363  -1314   1254  A    O  
ATOM   1634  CB  CYS A 217      50.065 -24.051   5.149  1.00 83.62      A    C  
ANISOU 1634  CB  CYS A 217    11936   9366  10469   -764  -1060   1060  A    C  
ATOM   1635  SG  CYS A 217      48.579 -24.743   5.896  1.00 99.66      A    S  
ANISOU 1635  SG  CYS A 217    14146  11235  12485  -1022   -977   1116  A    S  
ATOM   1636  N   ILE A 218      52.207 -21.758   4.852  1.00 77.16      A    N  
ANISOU 1636  N   ILE A 218    10759   9024   9532   -571  -1140   1027  A    N  
ATOM   1637  CA  ILE A 218      53.350 -21.224   4.130  1.00 77.42      A    C  
ANISOU 1637  CA  ILE A 218    10613   9202   9598   -402  -1188    994  A    C  
ATOM   1638  C   ILE A 218      54.432 -20.766   5.100  1.00 84.79      A    C  
ANISOU 1638  C   ILE A 218    11498  10291  10427   -407  -1304   1142  A    C  
ATOM   1639  O   ILE A 218      55.624 -20.993   4.868  1.00 90.15      A    O  
ANISOU 1639  O   ILE A 218    12067  11032  11153   -231  -1399   1212  A    O  
ATOM   1640  CB  ILE A 218      52.940 -20.044   3.226  1.00 78.55      A    C  
ANISOU 1640  CB  ILE A 218    10624   9480   9741   -444  -1083    826  A    C  
ATOM   1641  CG1 ILE A 218      52.031 -20.524   2.122  1.00 85.99      A    C  
ANISOU 1641  CG1 ILE A 218    11589  10294  10789   -411   -999    681  A    C  
ATOM   1642  CG2 ILE A 218      54.185 -19.368   2.655  1.00 68.02      A    C  
ANISOU 1642  CG2 ILE A 218     9104   8322   8418   -308  -1128    823  A    C  
ATOM   1643  CD1 ILE A 218      51.257 -19.417   1.438  1.00 86.68      A    C  
ANISOU 1643  CD1 ILE A 218    11585  10489  10857   -495   -890    534  A    C  
ATOM   1644  N   MET A 219      54.019 -20.110   6.185  1.00 80.88      A    N  
ANISOU 1644  N   MET A 219    11078   9867   9782   -609  -1295   1189  A    N  
ATOM   1645  CA  MET A 219      54.987 -19.641   7.153  1.00 82.58      A    C  
ANISOU 1645  CA  MET A 219    11267  10234   9876   -647  -1421   1321  A    C  
ATOM   1646  C   MET A 219      55.817 -20.824   7.645  1.00 86.71      A    C  
ANISOU 1646  C   MET A 219    11839  10676  10430   -506  -1567   1503  A    C  
ATOM   1647  O   MET A 219      57.044 -20.793   7.604  1.00 89.06      A    O  
ANISOU 1647  O   MET A 219    11999  11091  10748   -374  -1690   1589  A    O  
ATOM   1648  CB  MET A 219      54.322 -18.916   8.322  1.00 82.77      A    C  
ANISOU 1648  CB  MET A 219    11421  10312   9713   -885  -1384   1339  A    C  
ATOM   1649  CG  MET A 219      55.339 -18.257   9.255  1.00 89.52      A    C  
ANISOU 1649  CG  MET A 219    12252  11342  10419   -949  -1526   1447  A    C  
ATOM   1650  SD  MET A 219      54.618 -17.254  10.549  1.00 97.04      A    S  
ANISOU 1650  SD  MET A 219    13377  12366  11125  -1220  -1470   1433  A    S  
ATOM   1651  CE  MET A 219      56.087 -16.736  11.441  1.00 91.22      A    C  
ANISOU 1651  CE  MET A 219    12594  11822  10240  -1263  -1697   1569  A    C  
ATOM   1652  N   ALA A 220      55.140 -21.876   8.099  1.00 85.53      A    N  
ANISOU 1652  N   ALA A 220    11879  10324  10291   -531  -1553   1571  A    N  
ATOM   1653  CA  ALA A 220      55.825 -23.069   8.602  1.00 89.41      A    C  
ANISOU 1653  CA  ALA A 220    12455  10700  10814   -391  -1688   1757  A    C  
ATOM   1654  C   ALA A 220      56.778 -23.621   7.544  1.00 91.46      A    C  
ANISOU 1654  C   ALA A 220    12571  10934  11244   -104  -1737   1742  A    C  
ATOM   1655  O   ALA A 220      57.866 -24.114   7.838  1.00 93.19      A    O  
ANISOU 1655  O   ALA A 220    12738  11184  11484     65  -1876   1894  A    O  
ATOM   1656  CB  ALA A 220      54.806 -24.132   8.993  1.00 87.67      A    C  
ANISOU 1656  CB  ALA A 220    12471  10227  10609   -468  -1634   1806  A    C  
ATOM   1657  N   GLU A 221      56.353 -23.486   6.289  1.00 86.44      A    N  
ANISOU 1657  N   GLU A 221    11863  10257  10720    -45  -1616   1555  A    N  
ATOM   1658  CA  GLU A 221      57.088 -24.035   5.154  1.00 82.54      A    C  
ANISOU 1658  CA  GLU A 221    11259   9722  10380    229  -1621   1505  A    C  
ATOM   1659  C   GLU A 221      58.400 -23.276   4.922  1.00 86.89      A    C  
ANISOU 1659  C   GLU A 221    11553  10535  10926    349  -1690   1543  A    C  
ATOM   1660  O   GLU A 221      59.303 -23.784   4.269  1.00 88.29      A    O  
ANISOU 1660  O   GLU A 221    11616  10718  11209    605  -1721   1566  A    O  
ATOM   1661  CB  GLU A 221      56.204 -23.962   3.915  1.00 84.13      A    C  
ANISOU 1661  CB  GLU A 221    11464   9836  10664    222  -1474   1288  A    C  
ATOM   1662  CG  GLU A 221      56.649 -24.763   2.719  1.00 88.89      A    C  
ANISOU 1662  CG  GLU A 221    12039  10324  11411    489  -1452   1208  A    C  
ATOM   1663  CD  GLU A 221      55.485 -25.091   1.781  1.00104.28      A    C  
ANISOU 1663  CD  GLU A 221    14099  12098  13423    434  -1338   1020  A    C  
ATOM   1664  OE1 GLU A 221      54.322 -25.059   2.244  1.00 99.62      A    O  
ANISOU 1664  OE1 GLU A 221    13636  11425  12790    203  -1295    998  A    O  
ATOM   1665  OE2 GLU A 221      55.731 -25.403   0.593  1.00121.17      A    O1-
ANISOU 1665  OE2 GLU A 221    16198  14191  15648    619  -1293    897  A    O1-
ATOM   1666  N   MET A 222      58.506 -22.078   5.495  1.00 87.51      A    N  
ANISOU 1666  N   MET A 222    11546  10825  10876    159  -1713   1555  A    N  
ATOM   1667  CA  MET A 222      59.716 -21.263   5.349  1.00 84.49      A    C  
ANISOU 1667  CA  MET A 222    10916  10703  10481    216  -1787   1599  A    C  
ATOM   1668  C   MET A 222      60.913 -21.885   6.079  1.00 95.77      A    C  
ANISOU 1668  C   MET A 222    12279  12197  11912    362  -1970   1817  A    C  
ATOM   1669  O   MET A 222      62.060 -21.573   5.760  1.00116.49      A    O  
ANISOU 1669  O   MET A 222    14663  15016  14579    487  -2036   1872  A    O  
ATOM   1670  CB  MET A 222      59.474 -19.834   5.877  1.00 79.51      A    C  
ANISOU 1670  CB  MET A 222    10256  10249   9703    -52  -1778   1556  A    C  
ATOM   1671  CG  MET A 222      58.464 -19.033   5.052  1.00 82.96      A    C  
ANISOU 1671  CG  MET A 222    10705  10667  10147   -162  -1605   1350  A    C  
ATOM   1672  SD  MET A 222      59.086 -18.539   3.426  1.00 86.73      A    S  
ANISOU 1672  SD  MET A 222    10938  11267  10747      7  -1521   1228  A    S  
ATOM   1673  CE  MET A 222      60.514 -17.537   3.881  1.00 78.28      A    C  
ANISOU 1673  CE  MET A 222     9642  10489   9612    -48  -1654   1349  A    C  
ATOM   1674  N   TRP A 223      60.634 -22.759   7.049  1.00 86.34      A    N  
ANISOU 1674  N   TRP A 223    11288  10845  10671    344  -2049   1951  A    N  
ATOM   1675  CA  TRP A 223      61.691 -23.483   7.745  1.00 88.21      A    C  
ANISOU 1675  CA  TRP A 223    11486  11115  10914    507  -2231   2175  A    C  
ATOM   1676  C   TRP A 223      61.736 -24.945   7.308  1.00 93.83      A    C  
ANISOU 1676  C   TRP A 223    12304  11569  11775    782  -2220   2218  A    C  
ATOM   1677  O   TRP A 223      62.799 -25.461   7.006  1.00 96.90      A    O  
ANISOU 1677  O   TRP A 223    12546  12005  12265   1054  -2295   2314  A    O  
ATOM   1678  CB  TRP A 223      61.503 -23.412   9.265  1.00 97.61      A    C  
ANISOU 1678  CB  TRP A 223    12842  12325  11919    300  -2357   2331  A    C  
ATOM   1679  CG  TRP A 223      61.863 -22.088   9.863  1.00 98.61      A    C  
ANISOU 1679  CG  TRP A 223    12856  12722  11888     78  -2430   2336  A    C  
ATOM   1680  CD1 TRP A 223      63.100 -21.676  10.270  1.00 93.93      A    C  
ANISOU 1680  CD1 TRP A 223    12061  12375  11252    105  -2610   2470  A    C  
ATOM   1681  CD2 TRP A 223      60.971 -20.990  10.119  1.00 94.83      A    C  
ANISOU 1681  CD2 TRP A 223    12468  12290  11272   -209  -2328   2196  A    C  
ATOM   1682  CE2 TRP A 223      61.746 -19.937  10.644  1.00 92.36      A    C  
ANISOU 1682  CE2 TRP A 223    12023  12232  10836   -346  -2452   2240  A    C  
ATOM   1683  CE3 TRP A 223      59.596 -20.793   9.933  1.00 83.29      A    C  
ANISOU 1683  CE3 TRP A 223    11178  10681   9786   -356  -2144   2038  A    C  
ATOM   1684  NE1 TRP A 223      63.040 -20.385  10.728  1.00 94.42      A    N  
ANISOU 1684  NE1 TRP A 223    12097  12618  11158   -163  -2630   2411  A    N  
ATOM   1685  CZ2 TRP A 223      61.194 -18.704  10.983  1.00 85.60      A    C  
ANISOU 1685  CZ2 TRP A 223    11232  11461   9831   -614  -2390   2122  A    C  
ATOM   1686  CZ3 TRP A 223      59.047 -19.573  10.269  1.00 77.08      A    C  
ANISOU 1686  CZ3 TRP A 223    10430   9999   8859   -601  -2077   1931  A    C  
ATOM   1687  CH2 TRP A 223      59.844 -18.545  10.798  1.00 81.88      A    C  
ANISOU 1687  CH2 TRP A 223    10936  10833   9341   -723  -2196   1969  A    C  
ATOM   1688  N   THR A 224      60.574 -25.590   7.258  1.00 93.66      A    N  
ANISOU 1688  N   THR A 224    12537  11276  11770    707  -2121   2145  A    N  
ATOM   1689  CA  THR A 224      60.514 -27.005   6.919  1.00 92.27      A    C  
ANISOU 1689  CA  THR A 224    12520  10810  11726    932  -2114   2181  A    C  
ATOM   1690  C   THR A 224      60.830 -27.256   5.447  1.00 93.36      A    C  
ANISOU 1690  C   THR A 224    12539  10907  12026   1183  -2011   2022  A    C  
ATOM   1691  O   THR A 224      61.073 -28.387   5.045  1.00 99.84      A    O  
ANISOU 1691  O   THR A 224    13457  11511  12965   1432  -2014   2046  A    O  
ATOM   1692  CB  THR A 224      59.137 -27.638   7.233  1.00 96.57      A    C  
ANISOU 1692  CB  THR A 224    13373  11069  12250    748  -2036   2143  A    C  
ATOM   1693  CG2 THR A 224      58.744 -27.369   8.686  1.00 93.86      A    C  
ANISOU 1693  CG2 THR A 224    13162  10773  11724    491  -2108   2294  A    C  
ATOM   1694  OG1 THR A 224      58.134 -27.110   6.352  1.00105.37      A    O  
ANISOU 1694  OG1 THR A 224    14484  12161  13390    608  -1869   1908  A    O  
ATOM   1695  N   ARG A 225      60.830 -26.194   4.644  1.00 88.34      A    N  
ANISOU 1695  N   ARG A 225    11709  10470  11384   1121  -1916   1860  A    N  
ATOM   1696  CA  ARG A 225      61.179 -26.324   3.242  1.00 91.90      A    C  
ANISOU 1696  CA  ARG A 225    12038  10921  11959   1351  -1811   1712  A    C  
ATOM   1697  C   ARG A 225      60.280 -27.328   2.511  1.00 99.08      A    C  
ANISOU 1697  C   ARG A 225    13187  11501  12956   1418  -1711   1572  A    C  
ATOM   1698  O   ARG A 225      60.641 -27.855   1.470  1.00 92.66      A    O  
ANISOU 1698  O   ARG A 225    12350  10608  12247   1669  -1647   1477  A    O  
ATOM   1699  CB  ARG A 225      62.631 -26.748   3.123  1.00 82.52      A    C  
ANISOU 1699  CB  ARG A 225    10657   9844  10852   1674  -1897   1850  A    C  
ATOM   1700  CG  ARG A 225      63.601 -25.652   3.495  1.00 80.06      A    C  
ANISOU 1700  CG  ARG A 225    10047   9896  10475   1613  -1981   1949  A    C  
ATOM   1701  CD  ARG A 225      63.741 -24.654   2.366  1.00 79.34      A    C  
ANISOU 1701  CD  ARG A 225     9740  10003  10399   1596  -1851   1781  A    C  
ATOM   1702  NE  ARG A 225      64.755 -23.656   2.700  1.00 79.92      A    N  
ANISOU 1702  NE  ARG A 225     9524  10417  10425   1534  -1939   1889  A    N  
ATOM   1703  CZ  ARG A 225      65.590 -23.121   1.813  1.00 93.79      A    C  
ANISOU 1703  CZ  ARG A 225    11001  12397  12238   1657  -1877   1854  A    C  
ATOM   1704  NH1 ARG A 225      65.555 -23.513   0.542  1.00 91.85      A    N1+
ANISOU 1704  NH1 ARG A 225    10739  12072  12085   1874  -1722   1711  A    N1+
ATOM   1705  NH2 ARG A 225      66.479 -22.214   2.207  1.00108.44      A    N  
ANISOU 1705  NH2 ARG A 225    12597  14555  14047   1557  -1973   1965  A    N  
ATOM   1706  N   SER A 226      59.089 -27.553   3.057  1.00101.09      A    N  
ANISOU 1706  N   SER A 226    13674  11574  13161   1176  -1694   1554  A    N  
ATOM   1707  CA  SER A 226      58.191 -28.554   2.517  1.00 99.74      A    C  
ANISOU 1707  CA  SER A 226    13746  11079  13069   1189  -1625   1443  A    C  
ATOM   1708  C   SER A 226      56.821 -28.435   3.179  1.00108.65      A    C  
ANISOU 1708  C   SER A 226    15053  12106  14122    850  -1592   1428  A    C  
ATOM   1709  O   SER A 226      56.729 -28.209   4.385  1.00124.75      A    O  
ANISOU 1709  O   SER A 226    17133  14206  16059    687  -1658   1583  A    O  
ATOM   1710  CB  SER A 226      58.775 -29.944   2.723  1.00101.43      A    C  
ANISOU 1710  CB  SER A 226    14118  11042  13376   1448  -1705   1573  A    C  
ATOM   1711  OG  SER A 226      57.955 -30.934   2.106  1.00115.77      A    O  
ANISOU 1711  OG  SER A 226    16188  12521  15275   1460  -1642   1449  A    O  
ATOM   1712  N   PRO A 227      55.752 -28.598   2.378  1.00 98.83      A    N  
ANISOU 1712  N   PRO A 227    13911  10717  12922    746  -1488   1242  A    N  
ATOM   1713  CA  PRO A 227      54.378 -28.481   2.874  1.00105.63      A    C  
ANISOU 1713  CA  PRO A 227    14905  11499  13728    427  -1436   1215  A    C  
ATOM   1714  C   PRO A 227      54.092 -29.402   4.061  1.00112.76      A    C  
ANISOU 1714  C   PRO A 227    16038  12195  14608    330  -1505   1407  A    C  
ATOM   1715  O   PRO A 227      54.145 -30.618   3.930  1.00117.00      A    O  
ANISOU 1715  O   PRO A 227    16767  12449  15237    449  -1542   1446  A    O  
ATOM   1716  CB  PRO A 227      53.533 -28.878   1.659  1.00103.32      A    C  
ANISOU 1716  CB  PRO A 227    14690  11040  13524    413  -1350   1000  A    C  
ATOM   1717  CG  PRO A 227      54.398 -28.535   0.494  1.00102.26      A    C  
ANISOU 1717  CG  PRO A 227    14385  11033  13433    666  -1324    878  A    C  
ATOM   1718  CD  PRO A 227      55.801 -28.819   0.925  1.00 89.33      A    C  
ANISOU 1718  CD  PRO A 227    12678   9451  11812    921  -1413   1043  A    C  
ATOM   1719  N   ILE A 228      53.799 -28.794   5.204  1.00102.43      A    N  
ANISOU 1719  N   ILE A 228    14724  11025  13169    116  -1517   1525  A    N  
ATOM   1720  CA  ILE A 228      53.649 -29.500   6.475  1.00 91.14      A    C  
ANISOU 1720  CA  ILE A 228    13496   9457  11676     17  -1586   1740  A    C  
ATOM   1721  C   ILE A 228      52.590 -30.603   6.501  1.00 96.46      A    C  
ANISOU 1721  C   ILE A 228    14425   9807  12416   -116  -1543   1743  A    C  
ATOM   1722  O   ILE A 228      52.720 -31.563   7.275  1.00106.39      A    O  
ANISOU 1722  O   ILE A 228    15887  10864  13672   -102  -1617   1929  A    O  
ATOM   1723  CB  ILE A 228      53.360 -28.500   7.605  1.00 99.93      A    C  
ANISOU 1723  CB  ILE A 228    14561  10799  12607   -218  -1575   1824  A    C  
ATOM   1724  CG1 ILE A 228      52.090 -27.695   7.302  1.00112.44      A    C  
ANISOU 1724  CG1 ILE A 228    16095  12467  14159   -465  -1423   1654  A    C  
ATOM   1725  CG2 ILE A 228      54.531 -27.551   7.790  1.00102.51      A    C  
ANISOU 1725  CG2 ILE A 228    14674  11414  12859   -105  -1657   1865  A    C  
ATOM   1726  CD1 ILE A 228      51.599 -26.897   8.520  1.00 95.95      A    C  
ANISOU 1726  CD1 ILE A 228    14026  10543  11884   -708  -1385   1738  A    C  
ATOM   1727  N   MET A 229      51.524 -30.452   5.713  1.00104.44      A    N  
ANISOU 1727  N   MET A 229    15427  10773  13480   -265  -1432   1552  A    N  
ATOM   1728  CA  MET A 229      50.430 -31.430   5.699  1.00103.57      A    C  
ANISOU 1728  CA  MET A 229    15538  10375  13437   -441  -1393   1545  A    C  
ATOM   1729  C   MET A 229      50.031 -31.891   4.294  1.00103.19      A    C  
ANISOU 1729  C   MET A 229    15515  10161  13528   -380  -1356   1326  A    C  
ATOM   1730  O   MET A 229      49.211 -31.245   3.636  1.00109.12      A    O  
ANISOU 1730  O   MET A 229    16148  11029  14284   -521  -1272   1153  A    O  
ATOM   1731  CB  MET A 229      49.215 -30.861   6.426  1.00 99.30      A    C  
ANISOU 1731  CB  MET A 229    14987   9944  12796   -780  -1293   1566  A    C  
ATOM   1732  CG  MET A 229      49.510 -30.634   7.913  1.00 98.73      A    C  
ANISOU 1732  CG  MET A 229    14968   9979  12565   -862  -1329   1794  A    C  
ATOM   1733  SD  MET A 229      48.225 -29.784   8.811  1.00109.89      A    S  
ANISOU 1733  SD  MET A 229    16348  11575  13829  -1216  -1186   1812  A    S  
ATOM   1734  CE  MET A 229      48.206 -28.207   7.962  1.00106.25      A    C  
ANISOU 1734  CE  MET A 229    15588  11432  13348  -1180  -1109   1580  A    C  
ATOM   1735  N   GLN A 230      50.613 -33.000   3.851  1.00110.63      A    N  
ANISOU 1735  N   GLN A 230    16623  10833  14576   -163  -1424   1334  A    N  
ATOM   1736  CA  GLN A 230      50.413 -33.475   2.477  1.00113.52      A    C  
ANISOU 1736  CA  GLN A 230    17040  11034  15057    -64  -1402   1114  A    C  
ATOM   1737  C   GLN A 230      49.393 -34.591   2.370  1.00125.35      A    C  
ANISOU 1737  C   GLN A 230    18806  12184  16637   -257  -1402   1088  A    C  
ATOM   1738  O   GLN A 230      49.742 -35.710   2.005  1.00130.67      A    O  
ANISOU 1738  O   GLN A 230    19702  12543  17403    -97  -1456   1081  A    O  
ATOM   1739  CB  GLN A 230      51.753 -33.948   1.907  1.00115.52      A    C  
ANISOU 1739  CB  GLN A 230    17304  11213  15375    331  -1461   1106  A    C  
ATOM   1740  CG  GLN A 230      52.878 -32.969   2.133  1.00119.09      A    C  
ANISOU 1740  CG  GLN A 230    17491  11998  15757    515  -1479   1174  A    C  
ATOM   1741  CD  GLN A 230      54.107 -33.279   1.300  1.00112.39      A    C  
ANISOU 1741  CD  GLN A 230    16585  11136  14981    905  -1502   1122  A    C  
ATOM   1742  NE2 GLN A 230      55.218 -32.641   1.638  1.00112.82      A    N  
ANISOU 1742  NE2 GLN A 230    16422  11452  14991   1077  -1542   1231  A    N  
ATOM   1743  OE1 GLN A 230      54.058 -34.070   0.362  1.00115.99      A    O  
ANISOU 1743  OE1 GLN A 230    17186  11356  15526   1045  -1482    982  A    O  
ATOM   1744  N   GLY A 231      48.126 -34.281   2.651  1.00130.67      A    N  
ANISOU 1744  N   GLY A 231    19455  12912  17279   -600  -1338   1069  A    N  
ATOM   1745  CA  GLY A 231      47.059 -35.277   2.530  1.00131.02      A    C  
ANISOU 1745  CA  GLY A 231    19724  12651  17403   -837  -1337   1043  A    C  
ATOM   1746  C   GLY A 231      46.890 -35.826   1.119  1.00132.98      A    C  
ANISOU 1746  C   GLY A 231    20062  12708  17756   -757  -1358    805  A    C  
ATOM   1747  O   GLY A 231      47.387 -35.251   0.154  1.00118.03      A    O  
ANISOU 1747  O   GLY A 231    18016  10972  15857   -555  -1345    636  A    O  
ATOM   1748  N   ASN A 232      46.219 -36.966   0.995  1.00143.82      A    N  
ANISOU 1748  N   ASN A 232    21699  13729  19215   -917  -1392    793  A    N  
ATOM   1749  CA  ASN A 232      45.915 -37.550  -0.313  1.00131.73      A    C  
ANISOU 1749  CA  ASN A 232    20293  11989  17767   -893  -1422    554  A    C  
ATOM   1750  C   ASN A 232      44.441 -37.367  -0.685  1.00138.26      A    C  
ANISOU 1750  C   ASN A 232    21055  12865  18612  -1274  -1393    436  A    C  
ATOM   1751  O   ASN A 232      44.076 -37.275  -1.843  1.00132.21      A    O  
ANISOU 1751  O   ASN A 232    20254  12110  17868  -1285  -1407    208  A    O  
ATOM   1752  CB  ASN A 232      46.228 -39.035  -0.324  1.00126.90      A    C  
ANISOU 1752  CB  ASN A 232    20059  10906  17249   -798  -1498    597  A    C  
ATOM   1753  CG  ASN A 232      47.707 -39.324  -0.295  1.00142.74      A    C  
ANISOU 1753  CG  ASN A 232    22131  12840  19263   -361  -1532    663  A    C  
ATOM   1754  ND2 ASN A 232      48.473 -38.571  -1.078  1.00150.81      A    N  
ANISOU 1754  ND2 ASN A 232    22939  14110  20249    -87  -1503    525  A    N  
ATOM   1755  OD1 ASN A 232      48.158 -40.220   0.414  1.00159.25      A    O  
ANISOU 1755  OD1 ASN A 232    24454  14658  21392   -268  -1584    846  A    O  
ATOM   1756  N   THR A 233      43.613 -37.362   0.350  1.00149.73      A    N  
ANISOU 1756  N   THR A 233    22495  14346  20048  -1583  -1356    608  A    N  
ATOM   1757  CA  THR A 233      42.193 -37.080   0.214  1.00128.63      A    C  
ANISOU 1757  CA  THR A 233    19700  11783  17390  -1956  -1314    544  A    C  
ATOM   1758  C   THR A 233      41.778 -36.184   1.380  1.00125.02      A    C  
ANISOU 1758  C   THR A 233    19029  11630  16840  -2122  -1213    723  A    C  
ATOM   1759  O   THR A 233      42.529 -35.999   2.340  1.00127.69      A    O  
ANISOU 1759  O   THR A 233    19382  12027  17105  -1990  -1196    903  A    O  
ATOM   1760  CB  THR A 233      41.340 -38.373   0.239  1.00120.03      A    C  
ANISOU 1760  CB  THR A 233    18889  10313  16402  -2246  -1367    567  A    C  
ATOM   1761  CG2 THR A 233      41.867 -39.378  -0.770  1.00118.20      A    C  
ANISOU 1761  CG2 THR A 233    18941   9720  16249  -2058  -1469    404  A    C  
ATOM   1762  OG1 THR A 233      41.365 -38.944   1.564  1.00128.91      A    O  
ANISOU 1762  OG1 THR A 233    20176  11286  17516  -2359  -1349    841  A    O  
ATOM   1763  N   GLU A 234      40.572 -35.639   1.285  1.00114.73      A    N  
ANISOU 1763  N   GLU A 234    17532  10522  15537  -2406  -1147    669  A    N  
ATOM   1764  CA  GLU A 234      40.039 -34.795   2.346  1.00112.87      A    C  
ANISOU 1764  CA  GLU A 234    17102  10571  15211  -2572  -1029    819  A    C  
ATOM   1765  C   GLU A 234      40.098 -35.451   3.724  1.00126.39      A    C  
ANISOU 1765  C   GLU A 234    19005  12129  16885  -2691  -1004   1086  A    C  
ATOM   1766  O   GLU A 234      40.448 -34.799   4.717  1.00131.69      A    O  
ANISOU 1766  O   GLU A 234    19599  12999  17438  -2642   -938   1233  A    O  
ATOM   1767  CB  GLU A 234      38.617 -34.366   1.972  1.00110.96      A    C  
ANISOU 1767  CB  GLU A 234    16649  10506  15005  -2871   -967    726  A    C  
ATOM   1768  CG  GLU A 234      38.486 -34.194   0.434  1.00118.09      A    C  
ANISOU 1768  CG  GLU A 234    17466  11433  15968  -2788  -1042    459  A    C  
ATOM   1769  CD  GLU A 234      37.450 -33.164   0.065  1.00131.97      A    C  
ANISOU 1769  CD  GLU A 234    18904  13523  17713  -2938   -972    367  A    C  
ATOM   1770  OE1 GLU A 234      36.604 -32.864   0.932  1.00132.78      A    O  
ANISOU 1770  OE1 GLU A 234    18880  13775  17796  -3167   -866    499  A    O  
ATOM   1771  OE2 GLU A 234      37.505 -32.639  -1.071  1.00142.91      A    O1-
ANISOU 1771  OE2 GLU A 234    20166  15029  19102  -2810  -1015    171  A    O1-
ATOM   1772  N   GLN A 235      39.773 -36.739   3.784  1.00131.02      A    N  
ANISOU 1772  N   GLN A 235    19860  12355  17563  -2851  -1063   1151  A    N  
ATOM   1773  CA  GLN A 235      39.830 -37.453   5.063  1.00135.37      A    C  
ANISOU 1773  CA  GLN A 235    20626  12728  18077  -2968  -1045   1422  A    C  
ATOM   1774  C   GLN A 235      41.264 -37.583   5.567  1.00129.15      A    C  
ANISOU 1774  C   GLN A 235    19979  11866  17226  -2626  -1111   1543  A    C  
ATOM   1775  O   GLN A 235      41.529 -37.456   6.769  1.00132.87      A    O  
ANISOU 1775  O   GLN A 235    20488  12410  17585  -2640  -1074   1766  A    O  
ATOM   1776  CB  GLN A 235      39.183 -38.832   4.962  1.00133.69      A    C  
ANISOU 1776  CB  GLN A 235    20694  12115  17987  -3221  -1101   1467  A    C  
ATOM   1777  CG  GLN A 235      37.679 -38.803   4.975  1.00139.62      A    C  
ANISOU 1777  CG  GLN A 235    21310  12957  18783  -3643  -1021   1459  A    C  
ATOM   1778  CD  GLN A 235      37.069 -40.063   5.552  1.00159.02      A    C  
ANISOU 1778  CD  GLN A 235    24044  15067  21308  -3957  -1034   1638  A    C  
ATOM   1779  NE2 GLN A 235      35.852 -39.940   6.062  1.00180.15      A    N  
ANISOU 1779  NE2 GLN A 235    26577  17888  23983  -4335   -922   1733  A    N  
ATOM   1780  OE1 GLN A 235      37.680 -41.135   5.536  1.00162.68      A    O  
ANISOU 1780  OE1 GLN A 235    24847  15135  21829  -3860  -1137   1694  A    O  
ATOM   1781  N   HIS A 236      42.190 -37.836   4.642  1.00118.14      A    N  
ANISOU 1781  N   HIS A 236    18655  10337  15893  -2315  -1209   1400  A    N  
ATOM   1782  CA  HIS A 236      43.589 -37.920   5.002  1.00121.33      A    C  
ANISOU 1782  CA  HIS A 236    19144  10703  16252  -1963  -1276   1504  A    C  
ATOM   1783  C   HIS A 236      44.087 -36.557   5.477  1.00125.41      A    C  
ANISOU 1783  C   HIS A 236    19378  11640  16629  -1843  -1221   1534  A    C  
ATOM   1784  O   HIS A 236      44.852 -36.453   6.448  1.00156.17      A    O  
ANISOU 1784  O   HIS A 236    23311  15595  20429  -1723  -1246   1727  A    O  
ATOM   1785  CB  HIS A 236      44.423 -38.428   3.821  1.00123.73      A    C  
ANISOU 1785  CB  HIS A 236    19553  10803  16653  -1647  -1368   1325  A    C  
ATOM   1786  CG  HIS A 236      45.846 -38.735   4.188  1.00145.62      A    C  
ANISOU 1786  CG  HIS A 236    22430  13490  19408  -1279  -1442   1454  A    C  
ATOM   1787  CD2 HIS A 236      46.403 -39.071   5.379  1.00142.83      A    C  
ANISOU 1787  CD2 HIS A 236    22200  13074  18994  -1220  -1479   1722  A    C  
ATOM   1788  ND1 HIS A 236      46.889 -38.637   3.291  1.00148.91      A    N  
ANISOU 1788  ND1 HIS A 236    22796  13920  19860   -910  -1486   1312  A    N  
ATOM   1789  CE1 HIS A 236      48.019 -38.947   3.898  1.00141.05      A    C  
ANISOU 1789  CE1 HIS A 236    21880  12865  18845   -636  -1550   1489  A    C  
ATOM   1790  NE2 HIS A 236      47.753 -39.214   5.167  1.00132.61      A    N  
ANISOU 1790  NE2 HIS A 236    20922  11746  17715   -817  -1557   1740  A    N  
ATOM   1791  N   GLN A 237      43.629 -35.510   4.798  1.00102.09      A    N  
ANISOU 1791  N   GLN A 237    16154   8974  13660  -1886  -1155   1345  A    N  
ATOM   1792  CA  GLN A 237      43.992 -34.143   5.163  1.00 99.74      A    C  
ANISOU 1792  CA  GLN A 237    15596   9063  13236  -1801  -1096   1349  A    C  
ATOM   1793  C   GLN A 237      43.460 -33.824   6.551  1.00108.17      A    C  
ANISOU 1793  C   GLN A 237    16656  10265  14179  -2029  -1011   1551  A    C  
ATOM   1794  O   GLN A 237      44.186 -33.281   7.400  1.00129.46      A    O  
ANISOU 1794  O   GLN A 237    19317  13123  16746  -1921  -1017   1679  A    O  
ATOM   1795  CB  GLN A 237      43.430 -33.142   4.144  1.00110.51      A    C  
ANISOU 1795  CB  GLN A 237    16697  10673  14615  -1832  -1034   1114  A    C  
ATOM   1796  CG  GLN A 237      44.165 -31.814   4.109  1.00 99.75      A    C  
ANISOU 1796  CG  GLN A 237    15102   9643  13155  -1640  -1008   1066  A    C  
ATOM   1797  CD  GLN A 237      45.583 -31.937   3.564  1.00108.69      A    C  
ANISOU 1797  CD  GLN A 237    16255  10731  14309  -1288  -1102   1028  A    C  
ATOM   1798  NE2 GLN A 237      46.490 -31.155   4.144  1.00 92.79      A    N  
ANISOU 1798  NE2 GLN A 237    14129   8930  12193  -1142  -1112   1116  A    N  
ATOM   1799  OE1 GLN A 237      45.873 -32.693   2.609  1.00136.05      A    O  
ANISOU 1799  OE1 GLN A 237    19829  13984  17879  -1145  -1163    916  A    O  
ATOM   1800  N   LEU A 238      42.190 -34.157   6.791  1.00109.20      A    N  
ANISOU 1800  N   LEU A 238    16817  10336  14337  -2353   -931   1583  A    N  
ATOM   1801  CA  LEU A 238      41.583 -33.898   8.092  1.00113.28      A    C  
ANISOU 1801  CA  LEU A 238    17331  10983  14727  -2583   -823   1774  A    C  
ATOM   1802  C   LEU A 238      42.268 -34.684   9.197  1.00113.68      A    C  
ANISOU 1802  C   LEU A 238    17642  10846  14705  -2539   -886   2031  A    C  
ATOM   1803  O   LEU A 238      42.450 -34.194  10.310  1.00114.93      A    O  
ANISOU 1803  O   LEU A 238    17792  11176  14697  -2568   -839   2188  A    O  
ATOM   1804  CB  LEU A 238      40.086 -34.176   8.082  1.00116.86      A    C  
ANISOU 1804  CB  LEU A 238    17747  11412  15239  -2941   -718   1767  A    C  
ATOM   1805  CG  LEU A 238      39.199 -32.923   7.937  1.00111.34      A    C  
ANISOU 1805  CG  LEU A 238    16734  11074  14493  -3058   -576   1648  A    C  
ATOM   1806  CD1 LEU A 238      37.738 -33.298   7.771  1.00124.63      A    C  
ANISOU 1806  CD1 LEU A 238    18352  12734  16267  -3397   -491   1635  A    C  
ATOM   1807  CD2 LEU A 238      39.370 -31.993   9.138  1.00100.57      A    C  
ANISOU 1807  CD2 LEU A 238    15300   9977  12932  -3050   -469   1777  A    C  
ATOM   1808  N   ALA A 239      42.739 -35.879   8.861  1.00115.11      A    N  
ANISOU 1808  N   ALA A 239    18063  10672  14998  -2437  -1004   2069  A    N  
ATOM   1809  CA  ALA A 239      43.485 -36.672   9.821  1.00132.63      A    C  
ANISOU 1809  CA  ALA A 239    20539  12691  17161  -2348  -1086   2319  A    C  
ATOM   1810  C   ALA A 239      44.787 -35.954  10.156  1.00128.40      A    C  
ANISOU 1810  C   ALA A 239    19908  12365  16513  -2040  -1158   2362  A    C  
ATOM   1811  O   ALA A 239      45.094 -35.725  11.325  1.00123.73      A    O  
ANISOU 1811  O   ALA A 239    19361  11889  15761  -2062  -1159   2562  A    O  
ATOM   1812  CB  ALA A 239      43.737 -38.065   9.294  1.00141.70      A    C  
ANISOU 1812  CB  ALA A 239    21971  13400  18468  -2269  -1196   2332  A    C  
ATOM   1813  N   LEU A 240      45.523 -35.579   9.116  1.00127.54      A    N  
ANISOU 1813  N   LEU A 240    19660  12318  16479  -1771  -1218   2172  A    N  
ATOM   1814  CA  LEU A 240      46.816 -34.925   9.294  1.00120.18      A    C  
ANISOU 1814  CA  LEU A 240    18610  11585  15465  -1478  -1297   2202  A    C  
ATOM   1815  C   LEU A 240      46.680 -33.673  10.153  1.00115.88      A    C  
ANISOU 1815  C   LEU A 240    17886  11408  14732  -1594  -1222   2249  A    C  
ATOM   1816  O   LEU A 240      47.451 -33.472  11.106  1.00112.49      A    O  
ANISOU 1816  O   LEU A 240    17491  11081  14167  -1509  -1289   2423  A    O  
ATOM   1817  CB  LEU A 240      47.448 -34.569   7.942  1.00111.27      A    C  
ANISOU 1817  CB  LEU A 240    17317  10514  14444  -1215  -1333   1967  A    C  
ATOM   1818  CG  LEU A 240      47.997 -35.762   7.164  1.00107.05      A    C  
ANISOU 1818  CG  LEU A 240    16976   9631  14067   -993  -1426   1930  A    C  
ATOM   1819  CD1 LEU A 240      48.544 -35.355   5.811  1.00 98.25      A    C  
ANISOU 1819  CD1 LEU A 240    15694   8601  13033   -748  -1434   1688  A    C  
ATOM   1820  CD2 LEU A 240      49.078 -36.371   8.027  1.00110.87      A    C  
ANISOU 1820  CD2 LEU A 240    17612  10000  14511   -783  -1542   2173  A    C  
ATOM   1821  N   ILE A 241      45.696 -32.841   9.814  1.00112.91      A    N  
ANISOU 1821  N   ILE A 241    17331  11224  14344  -1784  -1089   2093  A    N  
ATOM   1822  CA  ILE A 241      45.421 -31.598  10.550  1.00103.10      A    C  
ANISOU 1822  CA  ILE A 241    15931  10315  12927  -1900   -991   2104  A    C  
ATOM   1823  C   ILE A 241      45.148 -31.880  12.037  1.00106.53      A    C  
ANISOU 1823  C   ILE A 241    16538  10741  13196  -2083   -956   2353  A    C  
ATOM   1824  O   ILE A 241      45.589 -31.125  12.915  1.00102.10      A    O  
ANISOU 1824  O   ILE A 241    15944  10397  12451  -2066   -958   2437  A    O  
ATOM   1825  CB  ILE A 241      44.204 -30.835   9.953  1.00101.59      A    C  
ANISOU 1825  CB  ILE A 241    15543  10284  12770  -2086   -838   1914  A    C  
ATOM   1826  CG1 ILE A 241      44.570 -30.115   8.656  1.00102.45      A    C  
ANISOU 1826  CG1 ILE A 241    15443  10514  12969  -1899   -861   1676  A    C  
ATOM   1827  CG2 ILE A 241      43.627 -29.845  10.961  1.00106.90      A    C  
ANISOU 1827  CG2 ILE A 241    16133  11225  13258  -2261   -702   1970  A    C  
ATOM   1828  CD1 ILE A 241      43.380 -29.457   7.960  1.00105.41      A    C  
ANISOU 1828  CD1 ILE A 241    15631  11025  13394  -2058   -735   1495  A    C  
ATOM   1829  N   SER A 242      44.412 -32.961  12.312  1.00113.42      A    N  
ANISOU 1829  N   SER A 242    17606  11362  14125  -2270   -925   2470  A    N  
ATOM   1830  CA  SER A 242      44.110 -33.334  13.688  1.00114.68      A    C  
ANISOU 1830  CA  SER A 242    17952  11493  14126  -2454   -883   2722  A    C  
ATOM   1831  C   SER A 242      45.361 -33.787  14.435  1.00116.55      A    C  
ANISOU 1831  C   SER A 242    18365  11647  14270  -2254  -1048   2932  A    C  
ATOM   1832  O   SER A 242      45.512 -33.527  15.626  1.00119.22      A    O  
ANISOU 1832  O   SER A 242    18783  12113  14400  -2323  -1041   3110  A    O  
ATOM   1833  CB  SER A 242      43.044 -34.434  13.732  1.00121.39      A    C  
ANISOU 1833  CB  SER A 242    18971  12075  15076  -2715   -814   2807  A    C  
ATOM   1834  OG  SER A 242      41.744 -33.888  13.590  1.00129.04      A    O  
ANISOU 1834  OG  SER A 242    19770  13208  16050  -2974   -632   2700  A    O  
ATOM   1835  N   GLN A 243      46.259 -34.464  13.724  1.00119.56      A    N  
ANISOU 1835  N   GLN A 243    18805  11821  14799  -1995  -1199   2910  A    N  
ATOM   1836  CA  GLN A 243      47.498 -34.945  14.333  1.00127.48      A    C  
ANISOU 1836  CA  GLN A 243    19949  12744  15742  -1764  -1371   3112  A    C  
ATOM   1837  C   GLN A 243      48.416 -33.787  14.722  1.00140.68      A    C  
ANISOU 1837  C   GLN A 243    21434  14760  17256  -1619  -1434   3102  A    C  
ATOM   1838  O   GLN A 243      49.333 -33.951  15.534  1.00136.94      A    O  
ANISOU 1838  O   GLN A 243    21049  14314  16667  -1492  -1570   3301  A    O  
ATOM   1839  CB  GLN A 243      48.215 -35.895  13.390  1.00130.55      A    C  
ANISOU 1839  CB  GLN A 243    20422  12841  16340  -1494  -1496   3068  A    C  
ATOM   1840  CG  GLN A 243      47.516 -37.226  13.175  1.00130.77      A    C  
ANISOU 1840  CG  GLN A 243    20713  12462  16509  -1621  -1479   3124  A    C  
ATOM   1841  CD  GLN A 243      48.093 -37.979  11.990  1.00136.27      A    C  
ANISOU 1841  CD  GLN A 243    21468  12888  17419  -1353  -1569   2993  A    C  
ATOM   1842  NE2 GLN A 243      47.587 -39.182  11.736  1.00144.14      A    N  
ANISOU 1842  NE2 GLN A 243    22726  13492  18547  -1442  -1575   3026  A    N  
ATOM   1843  OE1 GLN A 243      48.989 -37.479  11.315  1.00134.78      A    O  
ANISOU 1843  OE1 GLN A 243    21098  12841  17271  -1072  -1628   2863  A    O  
ATOM   1844  N   LEU A 244      48.112 -32.608  14.182  1.00153.32      A    N  
ANISOU 1844  N   LEU A 244    22785  16622  18845  -1660  -1337   2881  A    N  
ATOM   1845  CA  LEU A 244      48.946 -31.432  14.425  1.00141.19      A    C  
ANISOU 1845  CA  LEU A 244    21066  15403  17174  -1545  -1392   2841  A    C  
ATOM   1846  C   LEU A 244      48.275 -30.383  15.304  1.00127.43      A    C  
ANISOU 1846  C   LEU A 244    19281  13923  15213  -1779  -1263   2838  A    C  
ATOM   1847  O   LEU A 244      48.903 -29.818  16.206  1.00121.99      A    O  
ANISOU 1847  O   LEU A 244    18604  13419  14326  -1765  -1334   2942  A    O  
ATOM   1848  CB  LEU A 244      49.357 -30.797  13.105  1.00127.77      A    C  
ANISOU 1848  CB  LEU A 244    19122  13804  15620  -1363  -1398   2595  A    C  
ATOM   1849  CG  LEU A 244      50.365 -29.656  13.267  1.00121.92      A    C  
ANISOU 1849  CG  LEU A 244    18193  13365  14766  -1235  -1477   2564  A    C  
ATOM   1850  CD1 LEU A 244      51.687 -30.225  13.758  1.00128.87      A    C  
ANISOU 1850  CD1 LEU A 244    19141  14203  15620  -1014  -1679   2765  A    C  
ATOM   1851  CD2 LEU A 244      50.564 -28.902  11.962  1.00115.30      A    C  
ANISOU 1851  CD2 LEU A 244    17109  12645  14054  -1109  -1441   2316  A    C  
ATOM   1852  N   CYS A 245      47.001 -30.114  15.039  1.00120.86      A    N  
ANISOU 1852  N   CYS A 245    18397  13112  14412  -1991  -1075   2715  A    N  
ATOM   1853  CA  CYS A 245      46.328 -29.007  15.719  1.00121.79      A    C  
ANISOU 1853  CA  CYS A 245    18445  13491  14339  -2177   -924   2671  A    C  
ATOM   1854  C   CYS A 245      45.380 -29.464  16.820  1.00138.03      A    C  
ANISOU 1854  C   CYS A 245    20689  15500  16256  -2435   -797   2846  A    C  
ATOM   1855  O   CYS A 245      44.585 -28.680  17.329  1.00144.96      A    O  
ANISOU 1855  O   CYS A 245    21518  16566  16992  -2605   -627   2802  A    O  
ATOM   1856  CB  CYS A 245      45.578 -28.141  14.707  1.00114.47      A    C  
ANISOU 1856  CB  CYS A 245    17284  12689  13519  -2214   -784   2410  A    C  
ATOM   1857  SG  CYS A 245      46.545 -27.659  13.266  1.00115.44      A    S  
ANISOU 1857  SG  CYS A 245    17190  12855  13815  -1933   -902   2200  A    S  
ATOM   1858  N   GLY A 246      45.485 -30.729  17.200  1.00150.34      A    N  
ANISOU 1858  N   GLY A 246    22469  16804  17849  -2455   -874   3050  A    N  
ATOM   1859  CA  GLY A 246      44.522 -31.321  18.119  1.00143.41      A    C  
ANISOU 1859  CA  GLY A 246    21775  15844  16869  -2718   -744   3228  A    C  
ATOM   1860  C   GLY A 246      43.365 -31.815  17.273  1.00130.19      A    C  
ANISOU 1860  C   GLY A 246    20037  14019  15406  -2874   -614   3119  A    C  
ATOM   1861  O   GLY A 246      43.403 -31.709  16.032  1.00127.48      A    O  
ANISOU 1861  O   GLY A 246    19533  13634  15266  -2761   -646   2913  A    O  
ATOM   1862  N   SER A 247      42.367 -32.429  17.902  1.00126.50      A    N  
ANISOU 1862  N   SER A 247    19702  13461  14898  -3138   -481   3266  A    N  
ATOM   1863  CA  SER A 247      41.211 -32.880  17.138  1.00129.10      A    C  
ANISOU 1863  CA  SER A 247    19954  13670  15427  -3326   -364   3170  A    C  
ATOM   1864  C   SER A 247      39.994 -31.974  17.305  1.00111.45      A    C  
ANISOU 1864  C   SER A 247    17518  11706  13121  -3535   -122   3071  A    C  
ATOM   1865  O   SER A 247      39.831 -31.282  18.294  1.00100.72      A    O  
ANISOU 1865  O   SER A 247    16167  10568  11532  -3603     -5   3140  A    O  
ATOM   1866  CB  SER A 247      40.870 -34.352  17.387  1.00148.19      A    C  
ANISOU 1866  CB  SER A 247    22629  15745  17931  -3484   -393   3374  A    C  
ATOM   1867  OG  SER A 247      40.929 -34.675  18.752  1.00163.36      A    O  
ANISOU 1867  OG  SER A 247    24772  17663  19634  -3595   -363   3648  A    O  
ATOM   1868  N   ILE A 248      39.197 -31.933  16.240  1.00113.57      A    N  
ANISOU 1868  N   ILE A 248    17595  11961  13593  -3606    -60   2887  A    N  
ATOM   1869  CA  ILE A 248      38.089 -31.000  16.112  1.00112.38      A    C  
ANISOU 1869  CA  ILE A 248    17195  12077  13427  -3745    149   2754  A    C  
ATOM   1870  C   ILE A 248      37.039 -31.283  17.175  1.00120.61      A    C  
ANISOU 1870  C   ILE A 248    18303  13175  14346  -4041    353   2942  A    C  
ATOM   1871  O   ILE A 248      36.307 -32.273  17.102  1.00121.96      A    O  
ANISOU 1871  O   ILE A 248    18538  13162  14636  -4263    388   3043  A    O  
ATOM   1872  CB  ILE A 248      37.470 -31.136  14.710  1.00105.73      A    C  
ANISOU 1872  CB  ILE A 248    16157  11171  12845  -3771    134   2551  A    C  
ATOM   1873  CG1 ILE A 248      38.582 -31.493  13.699  1.00 94.42      A    C  
ANISOU 1873  CG1 ILE A 248    14776   9544  11554  -3509    -95   2439  A    C  
ATOM   1874  CG2 ILE A 248      36.693 -29.922  14.305  1.00106.61      A    C  
ANISOU 1874  CG2 ILE A 248    15966  11583  12956  -3786    289   2364  A    C  
ATOM   1875  CD1 ILE A 248      38.629 -30.612  12.513  1.00 90.58      A    C  
ANISOU 1875  CD1 ILE A 248    14039   9206  11171  -3353   -115   2176  A    C  
ATOM   1876  N   THR A 249      36.959 -30.406  18.168  1.00119.88      A    N  
ANISOU 1876  N   THR A 249    18202  13338  14008  -4053    494   2988  A    N  
ATOM   1877  CA  THR A 249      36.062 -30.603  19.304  1.00120.27      A    C  
ANISOU 1877  CA  THR A 249    18331  13472  13892  -4311    708   3180  A    C  
ATOM   1878  C   THR A 249      35.209 -29.371  19.526  1.00127.76      A    C  
ANISOU 1878  C   THR A 249    19048  14759  14733  -4353    955   3056  A    C  
ATOM   1879  O   THR A 249      35.718 -28.261  19.486  1.00142.01      A    O  
ANISOU 1879  O   THR A 249    20775  16745  16436  -4159    944   2908  A    O  
ATOM   1880  CB  THR A 249      36.880 -30.847  20.580  1.00115.09      A    C  
ANISOU 1880  CB  THR A 249    17974  12783  12971  -4279    648   3405  A    C  
ATOM   1881  CG2 THR A 249      35.982 -30.946  21.805  1.00115.19      A    C  
ANISOU 1881  CG2 THR A 249    18080  12915  12771  -4535    890   3602  A    C  
ATOM   1882  OG1 THR A 249      37.619 -32.063  20.425  1.00111.56      A    O  
ANISOU 1882  OG1 THR A 249    17750  12005  12629  -4232    428   3547  A    O  
ATOM   1883  N   PRO A 250      33.898 -29.556  19.727  1.00126.97      A    N  
ANISOU 1883  N   PRO A 250    18829  14744  14667  -4604   1180   3114  A    N  
ATOM   1884  CA  PRO A 250      33.024 -28.426  20.031  1.00122.75      A    C  
ANISOU 1884  CA  PRO A 250    18078  14537  14023  -4632   1443   3018  A    C  
ATOM   1885  C   PRO A 250      33.546 -27.619  21.205  1.00124.58      A    C  
ANISOU 1885  C   PRO A 250    18470  14942  13920  -4535   1524   3064  A    C  
ATOM   1886  O   PRO A 250      33.139 -26.474  21.395  1.00126.84      A    O  
ANISOU 1886  O   PRO A 250    18614  15485  14094  -4468   1703   2936  A    O  
ATOM   1887  CB  PRO A 250      31.693 -29.090  20.373  1.00132.10      A    C  
ANISOU 1887  CB  PRO A 250    19186  15747  15259  -4950   1659   3169  A    C  
ATOM   1888  CG  PRO A 250      31.715 -30.367  19.606  1.00144.66      A    C  
ANISOU 1888  CG  PRO A 250    20835  17023  17105  -5069   1474   3225  A    C  
ATOM   1889  CD  PRO A 250      33.149 -30.812  19.616  1.00139.47      A    C  
ANISOU 1889  CD  PRO A 250    20458  16123  16409  -4873   1202   3266  A    C  
ATOM   1890  N   GLU A 251      34.443 -28.208  21.989  1.00130.46      A    N  
ANISOU 1890  N   GLU A 251    19522  15544  14503  -4522   1385   3247  A    N  
ATOM   1891  CA  GLU A 251      35.097 -27.485  23.065  1.00139.36      A    C  
ANISOU 1891  CA  GLU A 251    20829  16820  15300  -4425   1405   3286  A    C  
ATOM   1892  C   GLU A 251      36.144 -26.543  22.494  1.00142.02      A    C  
ANISOU 1892  C   GLU A 251    21107  17210  15644  -4149   1222   3076  A    C  
ATOM   1893  O   GLU A 251      36.245 -25.386  22.887  1.00143.43      A    O  
ANISOU 1893  O   GLU A 251    21262  17599  15633  -4059   1313   2958  A    O  
ATOM   1894  CB  GLU A 251      35.776 -28.444  24.037  1.00146.07      A    C  
ANISOU 1894  CB  GLU A 251    22020  17503  15977  -4492   1281   3561  A    C  
ATOM   1895  CG  GLU A 251      36.851 -27.759  24.863  1.00160.62      A    C  
ANISOU 1895  CG  GLU A 251    24053  19453  17521  -4335   1172   3572  A    C  
ATOM   1896  CD  GLU A 251      37.105 -28.433  26.191  1.00193.90      A    C  
ANISOU 1896  CD  GLU A 251    28595  23620  21456  -4456   1165   3862  A    C  
ATOM   1897  OE1 GLU A 251      36.802 -29.637  26.312  1.00222.87      A    O  
ANISOU 1897  OE1 GLU A 251    32381  27085  25214  -4613   1155   4073  A    O  
ATOM   1898  OE2 GLU A 251      37.595 -27.744  27.107  1.00194.96      A    O1-
ANISOU 1898  OE2 GLU A 251    28879  23918  21276  -4401   1168   3877  A    O1-
ATOM   1899  N   VAL A 252      36.929 -27.069  21.560  1.00139.93      A    N  
ANISOU 1899  N   VAL A 252    20828  16740  15597  -4021    967   3031  A    N  
ATOM   1900  CA  VAL A 252      37.971 -26.301  20.899  1.00119.33      A    C  
ANISOU 1900  CA  VAL A 252    18145  14164  13028  -3768    781   2848  A    C  
ATOM   1901  C   VAL A 252      37.361 -25.360  19.860  1.00118.79      A    C  
ANISOU 1901  C   VAL A 252    17774  14235  13124  -3698    884   2589  A    C  
ATOM   1902  O   VAL A 252      37.754 -24.195  19.733  1.00131.29      A    O  
ANISOU 1902  O   VAL A 252    19281  15975  14628  -3548    883   2427  A    O  
ATOM   1903  CB  VAL A 252      39.014 -27.239  20.255  1.00118.41      A    C  
ANISOU 1903  CB  VAL A 252    18114  13788  13086  -3641    492   2900  A    C  
ATOM   1904  CG1 VAL A 252      39.848 -26.489  19.245  1.00114.37      A    C  
ANISOU 1904  CG1 VAL A 252    17442  13319  12693  -3399    339   2683  A    C  
ATOM   1905  CG2 VAL A 252      39.941 -27.807  21.324  1.00131.27      A    C  
ANISOU 1905  CG2 VAL A 252    20035  15332  14509  -3623    347   3133  A    C  
ATOM   1906  N   TRP A 253      36.361 -25.868  19.150  1.00119.04      A    N  
ANISOU 1906  N   TRP A 253    17640  14209  13378  -3820    974   2562  A    N  
ATOM   1907  CA  TRP A 253      35.751 -25.184  18.020  1.00118.76      A    C  
ANISOU 1907  CA  TRP A 253    17311  14276  13536  -3756   1036   2338  A    C  
ATOM   1908  C   TRP A 253      34.239 -25.161  18.213  1.00116.85      A    C  
ANISOU 1908  C   TRP A 253    16904  14169  13323  -3961   1306   2363  A    C  
ATOM   1909  O   TRP A 253      33.519 -26.012  17.670  1.00119.51      A    O  
ANISOU 1909  O   TRP A 253    17147  14399  13861  -4117   1312   2403  A    O  
ATOM   1910  CB  TRP A 253      36.100 -25.956  16.744  1.00115.20      A    C  
ANISOU 1910  CB  TRP A 253    16799  13606  13364  -3694    826   2271  A    C  
ATOM   1911  CG  TRP A 253      35.598 -25.363  15.472  1.00107.50      A    C  
ANISOU 1911  CG  TRP A 253    15543  12714  12589  -3619    843   2049  A    C  
ATOM   1912  CD1 TRP A 253      34.675 -24.362  15.331  1.00111.50      A    C  
ANISOU 1912  CD1 TRP A 253    15823  13454  13088  -3628   1038   1929  A    C  
ATOM   1913  CD2 TRP A 253      35.964 -25.763  14.150  1.00 95.64      A    C  
ANISOU 1913  CD2 TRP A 253    13962  11059  11316  -3517    658   1927  A    C  
ATOM   1914  CE2 TRP A 253      35.235 -24.955  13.250  1.00 94.41      A    C  
ANISOU 1914  CE2 TRP A 253    13532  11064  11276  -3479    739   1740  A    C  
ATOM   1915  CE3 TRP A 253      36.847 -26.715  13.638  1.00 92.92      A    C  
ANISOU 1915  CE3 TRP A 253    13761  10460  11084  -3438    435   1957  A    C  
ATOM   1916  NE1 TRP A 253      34.460 -24.107  13.993  1.00101.43      A    N  
ANISOU 1916  NE1 TRP A 253    14329  12184  12025  -3541    969   1749  A    N  
ATOM   1917  CZ2 TRP A 253      35.351 -25.083  11.872  1.00 92.67      A    C  
ANISOU 1917  CZ2 TRP A 253    13185  10762  11260  -3385    601   1586  A    C  
ATOM   1918  CZ3 TRP A 253      36.968 -26.832  12.258  1.00 97.28      A    C  
ANISOU 1918  CZ3 TRP A 253    14189  10929  11844  -3334    313   1789  A    C  
ATOM   1919  CH2 TRP A 253      36.225 -26.035  11.401  1.00 96.79      A    C  
ANISOU 1919  CH2 TRP A 253    13865  11034  11875  -3318    393   1609  A    C  
ATOM   1920  N   PRO A 254      33.749 -24.191  18.996  1.00114.71      A    N  
ANISOU 1920  N   PRO A 254    16598  14136  12848  -3964   1532   2340  A    N  
ATOM   1921  CA  PRO A 254      32.338 -24.041  19.386  1.00107.19      A    C  
ANISOU 1921  CA  PRO A 254    15485  13362  11877  -4135   1830   2379  A    C  
ATOM   1922  C   PRO A 254      31.364 -24.206  18.232  1.00105.23      A    C  
ANISOU 1922  C   PRO A 254    14923  13134  11923  -4199   1863   2281  A    C  
ATOM   1923  O   PRO A 254      31.364 -23.399  17.308  1.00 96.33      A    O  
ANISOU 1923  O   PRO A 254    13601  12087  10913  -4032   1824   2081  A    O  
ATOM   1924  CB  PRO A 254      32.285 -22.623  19.933  1.00106.77      A    C  
ANISOU 1924  CB  PRO A 254    15409  13550  11607  -3993   2004   2258  A    C  
ATOM   1925  CG  PRO A 254      33.633 -22.463  20.575  1.00112.22      A    C  
ANISOU 1925  CG  PRO A 254    16392  14164  12080  -3881   1829   2292  A    C  
ATOM   1926  CD  PRO A 254      34.599 -23.162  19.620  1.00120.72      A    C  
ANISOU 1926  CD  PRO A 254    17493  15009  13364  -3797   1513   2275  A    C  
ATOM   1927  N   ASN A 255      30.556 -25.266  18.278  1.00117.88      A    N  
ANISOU 1927  N   ASN A 255    16487  14659  13641  -4452   1921   2430  A    N  
ATOM   1928  CA  ASN A 255      29.518 -25.498  17.273  1.00128.96      A    C  
ANISOU 1928  CA  ASN A 255    17586  16099  15311  -4563   1953   2358  A    C  
ATOM   1929  C   ASN A 255      29.974 -26.241  16.025  1.00125.26      A    C  
ANISOU 1929  C   ASN A 255    17112  15387  15093  -4542   1672   2278  A    C  
ATOM   1930  O   ASN A 255      29.154 -26.551  15.162  1.00116.34      A    O  
ANISOU 1930  O   ASN A 255    15758  14264  14182  -4659   1662   2222  A    O  
ATOM   1931  CB  ASN A 255      28.817 -24.189  16.873  1.00124.07      A    C  
ANISOU 1931  CB  ASN A 255    16661  15764  14714  -4423   2122   2178  A    C  
ATOM   1932  CG  ASN A 255      27.536 -23.963  17.656  1.00145.15      A    C  
ANISOU 1932  CG  ASN A 255    19166  18679  17304  -4581   2452   2277  A    C  
ATOM   1933  ND2 ASN A 255      26.588 -23.260  17.051  1.00151.88      A    N  
ANISOU 1933  ND2 ASN A 255    19677  19746  18285  -4533   2583   2158  A    N  
ATOM   1934  OD1 ASN A 255      27.378 -24.463  18.777  1.00150.45      A    O  
ANISOU 1934  OD1 ASN A 255    20007  19349  17805  -4747   2590   2470  A    O  
ATOM   1935  N   VAL A 256      31.275 -26.524  15.921  1.00130.21      A    N  
ANISOU 1935  N   VAL A 256    17981  15807  15684  -4390   1443   2270  A    N  
ATOM   1936  CA  VAL A 256      31.776 -27.398  14.858  1.00126.04      A    C  
ANISOU 1936  CA  VAL A 256    17504  15013  15370  -4369   1188   2217  A    C  
ATOM   1937  C   VAL A 256      30.843 -28.599  14.657  1.00139.76      A    C  
ANISOU 1937  C   VAL A 256    19215  16608  17278  -4673   1202   2330  A    C  
ATOM   1938  O   VAL A 256      30.649 -29.078  13.543  1.00138.95      A    O  
ANISOU 1938  O   VAL A 256    19021  16379  17393  -4709   1064   2227  A    O  
ATOM   1939  CB  VAL A 256      33.189 -27.944  15.181  1.00118.91      A    C  
ANISOU 1939  CB  VAL A 256    16921  13877  14382  -4235    981   2299  A    C  
ATOM   1940  CG1 VAL A 256      33.238 -28.368  16.638  1.00114.93      A    C  
ANISOU 1940  CG1 VAL A 256    16654  13354  13659  -4371   1083   2543  A    C  
ATOM   1941  CG2 VAL A 256      33.537 -29.113  14.277  1.00128.11      A    C  
ANISOU 1941  CG2 VAL A 256    18184  14731  15761  -4258    761   2290  A    C  
ATOM   1942  N   ASP A 257      30.211 -29.036  15.740  1.00156.43      A    N  
ANISOU 1942  N   ASP A 257    21400  18755  19280  -4906   1380   2539  A    N  
ATOM   1943  CA  ASP A 257      29.362 -30.195  15.689  1.00152.70      A    C  
ANISOU 1943  CA  ASP A 257    20928  18139  18952  -5227   1401   2677  A    C  
ATOM   1944  C   ASP A 257      28.175 -30.095  14.733  1.00134.19      A    C  
ANISOU 1944  C   ASP A 257    18232  15925  16827  -5373   1452   2559  A    C  
ATOM   1945  O   ASP A 257      27.421 -31.053  14.602  1.00135.31      A    O  
ANISOU 1945  O   ASP A 257    18350  15952  17107  -5669   1454   2662  A    O  
ATOM   1946  CB  ASP A 257      28.951 -30.671  17.098  1.00145.81      A    C  
ANISOU 1946  CB  ASP A 257    20213  17288  17898  -5457   1597   2948  A    C  
ATOM   1947  CG  ASP A 257      28.401 -29.558  17.991  1.00137.68      A    C  
ANISOU 1947  CG  ASP A 257    19036  16619  16656  -5423   1887   2961  A    C  
ATOM   1948  OD1 ASP A 257      27.235 -29.128  17.819  1.00124.37      A    O  
ANISOU 1948  OD1 ASP A 257    17036  15174  15043  -5536   2084   2921  A    O  
ATOM   1949  OD2 ASP A 257      29.122 -29.125  18.906  1.00140.75      A    O1-
ANISOU 1949  OD2 ASP A 257    19630  17053  16794  -5284   1923   3019  A    O1-
ATOM   1950  N   ASN A 258      28.039 -29.017  13.958  1.00122.63      A    N  
ANISOU 1950  N   ASN A 258    16505  14672  15415  -5174   1458   2344  A    N  
ATOM   1951  CA  ASN A 258      26.782 -28.840  13.243  1.00113.41      A    C  
ANISOU 1951  CA  ASN A 258    14976  13689  14425  -5322   1537   2268  A    C  
ATOM   1952  C   ASN A 258      26.911 -28.906  11.751  1.00110.14      A    C  
ANISOU 1952  C   ASN A 258    14449  13180  14218  -5237   1307   2063  A    C  
ATOM   1953  O   ASN A 258      25.997 -28.525  11.017  1.00106.54      A    O  
ANISOU 1953  O   ASN A 258    13670  12912  13896  -5290   1339   1963  A    O  
ATOM   1954  CB  ASN A 258      26.047 -27.595  13.714  1.00109.89      A    C  
ANISOU 1954  CB  ASN A 258    14258  13622  13872  -5239   1807   2238  A    C  
ATOM   1955  CG  ASN A 258      26.186 -27.407  15.214  1.00126.18      A    C  
ANISOU 1955  CG  ASN A 258    16502  15767  15673  -5257   2022   2411  A    C  
ATOM   1956  ND2 ASN A 258      25.095 -27.607  15.930  1.00131.73      A    N  
ANISOU 1956  ND2 ASN A 258    17067  16635  16346  -5500   2269   2568  A    N  
ATOM   1957  OD1 ASN A 258      27.272 -27.116  15.728  1.00144.83      A    O  
ANISOU 1957  OD1 ASN A 258    19126  18048  17855  -5065   1963   2409  A    O  
ATOM   1958  N   TYR A 259      28.042 -29.425  11.271  1.00117.97      A    N  
ANISOU 1958  N   TYR A 259    15702  13883  15235  -5101   1069   2004  A    N  
ATOM   1959  CA  TYR A 259      28.115 -29.777   9.854  1.00142.10      A    C  
ANISOU 1959  CA  TYR A 259    18702  16801  18488  -5073    846   1829  A    C  
ATOM   1960  C   TYR A 259      27.565 -31.152   9.777  1.00147.24      A    C  
ANISOU 1960  C   TYR A 259    19456  17213  19275  -5409    777   1941  A    C  
ATOM   1961  O   TYR A 259      27.877 -31.993  10.629  1.00144.90      A    O  
ANISOU 1961  O   TYR A 259    19435  16706  18914  -5533    789   2128  A    O  
ATOM   1962  CB  TYR A 259      29.534 -29.846   9.354  1.00157.22      A    C  
ANISOU 1962  CB  TYR A 259    20859  18498  20379  -4791    636   1722  A    C  
ATOM   1963  CG  TYR A 259      30.175 -28.496   9.420  1.00148.01      A    C  
ANISOU 1963  CG  TYR A 259    19612  17546  19078  -4473    687   1615  A    C  
ATOM   1964  CD1 TYR A 259      29.709 -27.459   8.619  1.00138.00      A    C  
ANISOU 1964  CD1 TYR A 259    18049  16522  17863  -4354    719   1442  A    C  
ATOM   1965  CD2 TYR A 259      31.237 -28.242  10.282  1.00133.00      A    C  
ANISOU 1965  CD2 TYR A 259    17931  15604  16996  -4301    694   1691  A    C  
ATOM   1966  CE1 TYR A 259      30.273 -26.206   8.677  1.00130.77      A    C  
ANISOU 1966  CE1 TYR A 259    17076  15782  16827  -4078    768   1347  A    C  
ATOM   1967  CE2 TYR A 259      31.812 -26.985  10.352  1.00117.86      A    C  
ANISOU 1967  CE2 TYR A 259    15947  13878  14955  -4040    734   1589  A    C  
ATOM   1968  CZ  TYR A 259      31.320 -25.972   9.546  1.00123.49      A    C  
ANISOU 1968  CZ  TYR A 259    16381  14809  15728  -3933    777   1417  A    C  
ATOM   1969  OH  TYR A 259      31.887 -24.719   9.590  1.00122.52      A    O  
ANISOU 1969  OH  TYR A 259    16212  14849  15488  -3684    815   1317  A    O  
ATOM   1970  N   GLU A 260      26.789 -31.387   8.726  1.00149.90      A    N  
ANISOU 1970  N   GLU A 260    19590  17567  19797  -5555    686   1826  A    N  
ATOM   1971  CA  GLU A 260      26.296 -32.717   8.397  1.00151.96      A    C  
ANISOU 1971  CA  GLU A 260    19959  17565  20214  -5886    570   1888  A    C  
ATOM   1972  C   GLU A 260      27.459 -33.664   8.042  1.00149.96      A    C  
ANISOU 1972  C   GLU A 260    20107  16887  19983  -5779    343   1854  A    C  
ATOM   1973  O   GLU A 260      27.255 -34.840   7.681  1.00174.54      A    O  
ANISOU 1973  O   GLU A 260    23391  19703  23223  -6014    211   1880  A    O  
ATOM   1974  CB  GLU A 260      25.298 -32.619   7.249  1.00150.29      A    C  
ANISOU 1974  CB  GLU A 260    19430  17493  20178  -6031    492   1739  A    C  
ATOM   1975  CG  GLU A 260      24.454 -33.868   7.044  1.00164.63      A    C  
ANISOU 1975  CG  GLU A 260    21278  19118  22155  -6459    415   1823  A    C  
ATOM   1976  CD  GLU A 260      23.598 -33.792   5.799  1.00172.55      A    C  
ANISOU 1976  CD  GLU A 260    21991  20245  23325  -6589    285   1654  A    C  
ATOM   1977  OE1 GLU A 260      23.713 -32.792   5.055  1.00173.37      A    O  
ANISOU 1977  OE1 GLU A 260    21889  20567  23417  -6322    248   1474  A    O  
ATOM   1978  OE2 GLU A 260      22.807 -34.732   5.566  1.00177.70      A    O1-
ANISOU 1978  OE2 GLU A 260    22627  20776  24115  -6968    213   1708  A    O1-
ATOM   1979  N   LEU A 261      28.678 -33.148   8.171  1.00129.64      A    N  
ANISOU 1979  N   LEU A 261    17686  14284  17285  -5426    301   1802  A    N  
ATOM   1980  CA  LEU A 261      29.881 -33.908   7.880  1.00122.98      A    C  
ANISOU 1980  CA  LEU A 261    17193  13080  16451  -5257    106   1773  A    C  
ATOM   1981  C   LEU A 261      30.747 -34.143   9.103  1.00120.84      A    C  
ANISOU 1981  C   LEU A 261    17200  12691  16022  -5160    156   1973  A    C  
ATOM   1982  O   LEU A 261      31.841 -34.726   8.984  1.00116.49      A    O  
ANISOU 1982  O   LEU A 261    16935  11858  15467  -4979      3   1975  A    O  
ATOM   1983  CB  LEU A 261      30.693 -33.233   6.763  1.00116.78      A    C  
ANISOU 1983  CB  LEU A 261    16353  12337  15681  -4912    -32   1528  A    C  
ATOM   1984  CG  LEU A 261      30.266 -33.561   5.335  1.00114.55      A    C  
ANISOU 1984  CG  LEU A 261    15984  11975  15563  -4979   -191   1324  A    C  
ATOM   1985  CD1 LEU A 261      31.355 -33.156   4.372  1.00103.29      A    C  
ANISOU 1985  CD1 LEU A 261    14617  10503  14123  -4618   -333   1123  A    C  
ATOM   1986  CD2 LEU A 261      29.951 -35.056   5.219  1.00123.69      A    C  
ANISOU 1986  CD2 LEU A 261    17389  12762  16844  -5270   -302   1392  A    C  
ATOM   1987  N   TYR A 262      30.259 -33.687  10.261  1.00119.94      A    N  
ANISOU 1987  N   TYR A 262    16998  12800  15772  -5270    369   2141  A    N  
ATOM   1988  CA  TYR A 262      30.956 -33.869  11.515  1.00124.82      A    C  
ANISOU 1988  CA  TYR A 262    17869  13343  16212  -5212    426   2348  A    C  
ATOM   1989  C   TYR A 262      30.914 -35.367  11.800  1.00137.44      A    C  
ANISOU 1989  C   TYR A 262    19773  14561  17885  -5450    345   2527  A    C  
ATOM   1990  O   TYR A 262      31.940 -35.996  12.112  1.00145.33      A    O  
ANISOU 1990  O   TYR A 262    21091  15288  18837  -5309    222   2619  A    O  
ATOM   1991  CB  TYR A 262      30.300 -33.061  12.653  1.00123.55      A    C  
ANISOU 1991  CB  TYR A 262    17549  13516  15877  -5305    690   2476  A    C  
ATOM   1992  CG  TYR A 262      31.049 -33.213  13.959  1.00128.81      A    C  
ANISOU 1992  CG  TYR A 262    18493  14120  16327  -5243    737   2686  A    C  
ATOM   1993  CD1 TYR A 262      31.462 -34.475  14.397  1.00135.54      A    C  
ANISOU 1993  CD1 TYR A 262    19683  14626  17187  -5354    635   2877  A    C  
ATOM   1994  CD2 TYR A 262      31.377 -32.112  14.747  1.00129.29      A    C  
ANISOU 1994  CD2 TYR A 262    18502  14451  16168  -5070    867   2694  A    C  
ATOM   1995  CE1 TYR A 262      32.177 -34.640  15.565  1.00134.57      A    C  
ANISOU 1995  CE1 TYR A 262    19821  14446  16860  -5288    653   3080  A    C  
ATOM   1996  CE2 TYR A 262      32.089 -32.270  15.938  1.00130.13      A    C  
ANISOU 1996  CE2 TYR A 262    18878  14505  16059  -5022    885   2886  A    C  
ATOM   1997  CZ  TYR A 262      32.495 -33.540  16.331  1.00134.13      A    C  
ANISOU 1997  CZ  TYR A 262    19701  14681  16578  -5126    772   3084  A    C  
ATOM   1998  OH  TYR A 262      33.198 -33.734  17.481  1.00137.37      A    O  
ANISOU 1998  OH  TYR A 262    20380  15040  16773  -5076    770   3287  A    O  
ATOM   1999  N   GLU A 263      29.714 -35.929  11.651  1.00144.69      A    N  
ANISOU 1999  N   GLU A 263    20583  15460  18929  -5811    407   2577  A    N  
ATOM   2000  CA  GLU A 263      29.428 -37.337  11.910  1.00150.47      A    C  
ANISOU 2000  CA  GLU A 263    21581  15839  19749  -6113    353   2754  A    C  
ATOM   2001  C   GLU A 263      30.090 -38.275  10.903  1.00142.17      A    C  
ANISOU 2001  C   GLU A 263    20786  14378  18854  -6027     94   2631  A    C  
ATOM   2002  O   GLU A 263      30.733 -39.270  11.273  1.00135.25      A    O  
ANISOU 2002  O   GLU A 263    20277  13138  17974  -6020     -2   2770  A    O  
ATOM   2003  CB  GLU A 263      27.908 -37.536  11.888  1.00162.25      A    C  
ANISOU 2003  CB  GLU A 263    22822  17473  21349  -6533    488   2811  A    C  
ATOM   2004  CG  GLU A 263      27.138 -36.595  12.809  1.00171.66      A    C  
ANISOU 2004  CG  GLU A 263    23729  19093  22399  -6611    771   2918  A    C  
ATOM   2005  CD  GLU A 263      27.590 -36.713  14.266  1.00184.60      A    C  
ANISOU 2005  CD  GLU A 263    25612  20711  23814  -6597    906   3176  A    C  
ATOM   2006  OE1 GLU A 263      28.664 -37.297  14.542  1.00182.58      A    O  
ANISOU 2006  OE1 GLU A 263    25716  20156  23497  -6445    765   3253  A    O  
ATOM   2007  OE2 GLU A 263      26.865 -36.228  15.160  1.00196.98      A    O1-
ANISOU 2007  OE2 GLU A 263    27015  22570  25256  -6734   1158   3309  A    O1-
ATOM   2008  N   LYS A 264      29.904 -37.936   9.629  1.00136.52      A    N  
ANISOU 2008  N   LYS A 264    19876  13726  18266  -5954     -9   2369  A    N  
ATOM   2009  CA  LYS A 264      30.386 -38.728   8.513  1.00143.33      A    C  
ANISOU 2009  CA  LYS A 264    20943  14240  19274  -5880   -240   2205  A    C  
ATOM   2010  C   LYS A 264      31.899 -38.805   8.522  1.00151.31      A    C  
ANISOU 2010  C   LYS A 264    22223  15057  20211  -5476   -359   2182  A    C  
ATOM   2011  O   LYS A 264      32.469 -39.852   8.225  1.00159.01      A    O  
ANISOU 2011  O   LYS A 264    23525  15628  21262  -5433   -510   2187  A    O  
ATOM   2012  CB  LYS A 264      29.869 -38.154   7.187  1.00141.86      A    C  
ANISOU 2012  CB  LYS A 264    20463  14239  19199  -5863   -310   1928  A    C  
ATOM   2013  CG  LYS A 264      28.351 -38.201   7.095  1.00149.44      A    C  
ANISOU 2013  CG  LYS A 264    21146  15376  20258  -6277   -223   1957  A    C  
ATOM   2014  CD  LYS A 264      27.772 -37.601   5.828  1.00149.74      A    C  
ANISOU 2014  CD  LYS A 264    20871  15628  20394  -6269   -302   1704  A    C  
ATOM   2015  CE  LYS A 264      26.261 -37.760   5.866  1.00148.95      A    C  
ANISOU 2015  CE  LYS A 264    20493  15701  20398  -6706   -220   1774  A    C  
ATOM   2016  NZ  LYS A 264      25.587 -37.111   4.712  1.00146.26      A    N1+
ANISOU 2016  NZ  LYS A 264    19806  15620  20145  -6711   -293   1555  A    N1+
ATOM   2017  N   LEU A 265      32.543 -37.698   8.884  1.00166.04      A    N  
ANISOU 2017  N   LEU A 265    23949  17208  21928  -5181   -289   2161  A    N  
ATOM   2018  CA  LEU A 265      34.002 -37.644   8.937  1.00173.37      A    C  
ANISOU 2018  CA  LEU A 265    25074  18016  22780  -4794   -397   2149  A    C  
ATOM   2019  C   LEU A 265      34.561 -38.670   9.916  1.00170.78      A    C  
ANISOU 2019  C   LEU A 265    25116  17371  22400  -4819   -432   2406  A    C  
ATOM   2020  O   LEU A 265      35.593 -39.291   9.649  1.00163.88      A    O  
ANISOU 2020  O   LEU A 265    24498  16207  21559  -4582   -584   2397  A    O  
ATOM   2021  CB  LEU A 265      34.504 -36.249   9.314  1.00185.10      A    C  
ANISOU 2021  CB  LEU A 265    26344  19882  24104  -4536   -306   2111  A    C  
ATOM   2022  CG  LEU A 265      36.036 -36.098   9.445  1.00192.89      A    C  
ANISOU 2022  CG  LEU A 265    27491  20795  25002  -4149   -417   2117  A    C  
ATOM   2023  CD1 LEU A 265      36.753 -36.312   8.117  1.00184.90      A    C  
ANISOU 2023  CD1 LEU A 265    26520  19618  24115  -3900   -587   1894  A    C  
ATOM   2024  CD2 LEU A 265      36.427 -34.750  10.036  1.00191.35      A    C  
ANISOU 2024  CD2 LEU A 265    27105  20970  24629  -3972   -317   2117  A    C  
ATOM   2025  N   GLU A 266      33.880 -38.838  11.047  1.00168.68      A    N  
ANISOU 2025  N   GLU A 266    24873  17167  22049  -5094   -284   2642  A    N  
ATOM   2026  CA  GLU A 266      34.366 -39.736  12.076  1.00177.67      A    C  
ANISOU 2026  CA  GLU A 266    26359  18034  23110  -5126   -306   2916  A    C  
ATOM   2027  C   GLU A 266      35.839 -39.420  12.353  1.00176.61      A    C  
ANISOU 2027  C   GLU A 266    26350  17894  22857  -4707   -407   2935  A    C  
ATOM   2028  O   GLU A 266      36.712 -40.307  12.339  1.00173.50      A    O  
ANISOU 2028  O   GLU A 266    26262  17156  22503  -4544   -556   3012  A    O  
ATOM   2029  CB  GLU A 266      34.215 -41.197  11.650  1.00183.22      A    C  
ANISOU 2029  CB  GLU A 266    27371  18256  23986  -5301   -434   2959  A    C  
ATOM   2030  CG  GLU A 266      34.213 -42.133  12.848  1.00193.56      A    C  
ANISOU 2030  CG  GLU A 266    29001  19319  25222  -5483   -398   3291  A    C  
ATOM   2031  CD  GLU A 266      35.107 -43.347  12.674  1.00196.18      A    C  
ANISOU 2031  CD  GLU A 266    29753  19146  25638  -5328   -588   3361  A    C  
ATOM   2032  OE1 GLU A 266      34.718 -44.254  11.919  1.00200.22      A    O  
ANISOU 2032  OE1 GLU A 266    30419  19324  26331  -5494   -679   3280  A    O  
ATOM   2033  OE2 GLU A 266      36.180 -43.419  13.317  1.00193.13      A    O1-
ANISOU 2033  OE2 GLU A 266    29554  18689  25135  -5046   -648   3504  A    O1-
ATOM   2034  N   LEU A 267      36.105 -38.142  12.578  1.00171.88      A    N  
ANISOU 2034  N   LEU A 267    25507  17680  22120  -4532   -329   2862  A    N  
ATOM   2035  CA  LEU A 267      37.476 -37.670  12.849  1.00175.42      A    C  
ANISOU 2035  CA  LEU A 267    26016  18190  22446  -4156   -423   2872  A    C  
ATOM   2036  C   LEU A 267      38.056 -38.266  14.127  1.00177.04      A    C  
ANISOU 2036  C   LEU A 267    26511  18251  22502  -4144   -446   3173  A    C  
ATOM   2037  O   LEU A 267      37.326 -38.526  15.082  1.00169.01      A    O  
ANISOU 2037  O   LEU A 267    25568  17255  21390  -4423   -316   3378  A    O  
ATOM   2038  CB  LEU A 267      37.478 -36.150  12.924  1.00180.11      A    C  
ANISOU 2038  CB  LEU A 267    26296  19224  22910  -4040   -317   2745  A    C  
ATOM   2039  CG  LEU A 267      38.768 -35.406  13.235  1.00199.26      A    C  
ANISOU 2039  CG  LEU A 267    28717  21799  25193  -3701   -394   2739  A    C  
ATOM   2040  CD1 LEU A 267      39.885 -35.855  12.305  1.00208.27      A    C  
ANISOU 2040  CD1 LEU A 267    29953  22718  26462  -3395   -595   2629  A    C  
ATOM   2041  CD2 LEU A 267      38.546 -33.908  13.151  1.00196.19      A    C  
ANISOU 2041  CD2 LEU A 267    28020  21815  24707  -3644   -278   2581  A    C  
ATOM   2042  N   VAL A 268      39.369 -38.472  14.126  1.00181.23      A    N  
ANISOU 2042  N   VAL A 268    27196  18651  23009  -3816   -610   3206  A    N  
ATOM   2043  CA  VAL A 268      40.119 -38.970  15.278  1.00171.23      A    C  
ANISOU 2043  CA  VAL A 268    26197  17267  21594  -3735   -672   3489  A    C  
ATOM   2044  C   VAL A 268      39.788 -38.158  16.524  1.00167.44      A    C  
ANISOU 2044  C   VAL A 268    25638  17121  20861  -3872   -520   3635  A    C  
ATOM   2045  O   VAL A 268      39.446 -36.969  16.405  1.00177.70      A    O  
ANISOU 2045  O   VAL A 268    26654  18772  22089  -3877   -405   3476  A    O  
ATOM   2046  CB  VAL A 268      41.642 -38.825  15.018  1.00162.80      A    C  
ANISOU 2046  CB  VAL A 268    25164  16174  20517  -3307   -858   3450  A    C  
ATOM   2047  CG1 VAL A 268      41.954 -39.152  13.551  1.00142.04      A    C  
ANISOU 2047  CG1 VAL A 268    22497  13353  18118  -3120   -965   3203  A    C  
ATOM   2048  CG2 VAL A 268      42.071 -37.388  15.329  1.00165.40      A    C  
ANISOU 2048  CG2 VAL A 268    25235  16937  20670  -3168   -815   3368  A    C  
ATOM   2049  N   LYS A 269      39.948 -38.751  17.716  1.00148.98      A    N  
ANISOU 2049  N   LYS A 269    23561  14673  18370  -3957   -520   3934  A    N  
ATOM   2050  CA  LYS A 269      39.585 -38.033  18.918  1.00154.60      A    C  
ANISOU 2050  CA  LYS A 269    24229  15693  18818  -4100   -363   4072  A    C  
ATOM   2051  C   LYS A 269      40.493 -38.169  20.113  1.00159.59      A    C  
ANISOU 2051  C   LYS A 269    25091  16328  19214  -3977   -453   4330  A    C  
ATOM   2052  O   LYS A 269      40.155 -37.659  21.181  1.00167.05      A    O  
ANISOU 2052  O   LYS A 269    26046  17511  19914  -4118   -318   4458  A    O  
ATOM   2053  CB  LYS A 269      38.104 -38.271  19.301  1.00157.98      A    C  
ANISOU 2053  CB  LYS A 269    24628  16154  19240  -4514   -137   4158  A    C  
ATOM   2054  CG  LYS A 269      37.149 -37.512  18.373  1.00163.62      A    C  
ANISOU 2054  CG  LYS A 269    24991  17086  20090  -4622     -4   3883  A    C  
ATOM   2055  CD  LYS A 269      35.768 -37.303  18.976  1.00166.95      A    C  
ANISOU 2055  CD  LYS A 269    25291  17704  20436  -4982    257   3967  A    C  
ATOM   2056  CE  LYS A 269      34.784 -36.838  17.911  1.00166.50      A    C  
ANISOU 2056  CE  LYS A 269    24902  17788  20570  -5097    349   3717  A    C  
ATOM   2057  NZ  LYS A 269      33.456 -37.513  18.078  1.00192.38      A    N1+
ANISOU 2057  NZ  LYS A 269    28156  21004  23933  -5505    505   3838  A    N1+
ATOM   2058  N   GLY A 270      41.635 -38.833  19.966  1.00158.28      A    N  
ANISOU 2058  N   GLY A 270    25111  15918  19109  -3710   -677   4410  A    N  
ATOM   2059  CA  GLY A 270      42.668 -38.777  21.026  1.00158.00      A    C  
ANISOU 2059  CA  GLY A 270    25241  15949  18843  -3535   -801   4632  A    C  
ATOM   2060  C   GLY A 270      43.694 -37.644  20.868  1.00157.48      A    C  
ANISOU 2060  C   GLY A 270    24962  16183  18687  -3239   -906   4478  A    C  
ATOM   2061  O   GLY A 270      44.364 -37.251  21.816  1.00148.35      A    O  
ANISOU 2061  O   GLY A 270    23871  15201  17294  -3155   -975   4622  A    O  
ATOM   2062  N   GLN A 271      43.779 -37.107  19.659  1.00161.97      A    N  
ANISOU 2062  N   GLN A 271    25279  16821  19440  -3104   -916   4184  A    N  
ATOM   2063  CA  GLN A 271      44.828 -36.160  19.302  1.00143.57      A    C  
ANISOU 2063  CA  GLN A 271    22749  14722  17078  -2813  -1032   4031  A    C  
ATOM   2064  C   GLN A 271      44.843 -34.918  20.185  1.00143.53      A    C  
ANISOU 2064  C   GLN A 271    22632  15105  16794  -2874   -954   4029  A    C  
ATOM   2065  O   GLN A 271      43.805 -34.395  20.561  1.00152.04      A    O  
ANISOU 2065  O   GLN A 271    23648  16351  17769  -3121   -747   3992  A    O  
ATOM   2066  CB  GLN A 271      44.692 -35.767  17.829  1.00131.10      A    C  
ANISOU 2066  CB  GLN A 271    20921  13158  15733  -2712  -1014   3714  A    C  
ATOM   2067  CG  GLN A 271      44.741 -36.964  16.869  1.00131.39      A    C  
ANISOU 2067  CG  GLN A 271    21084  12803  16036  -2631  -1101   3680  A    C  
ATOM   2068  CD  GLN A 271      46.121 -37.606  16.821  1.00153.98      A    C  
ANISOU 2068  CD  GLN A 271    24084  15478  18943  -2291  -1322   3792  A    C  
ATOM   2069  NE2 GLN A 271      46.157 -38.927  16.685  1.00169.05      A    N  
ANISOU 2069  NE2 GLN A 271    26257  16985  20987  -2267  -1396   3916  A    N  
ATOM   2070  OE1 GLN A 271      47.139 -36.925  16.935  1.00167.21      A    O  
ANISOU 2070  OE1 GLN A 271    25630  17367  20532  -2057  -1426   3776  A    O  
ATOM   2071  N   LYS A 272      46.044 -34.415  20.467  1.00137.75      A    N  
ANISOU 2071  N   LYS A 272    21865  14524  15948  -2641  -1121   4055  A    N  
ATOM   2072  CA  LYS A 272      46.209 -33.184  21.248  1.00130.73      A    C  
ANISOU 2072  CA  LYS A 272    20886  13994  14790  -2680  -1080   4028  A    C  
ATOM   2073  C   LYS A 272      47.202 -32.267  20.536  1.00132.87      A    C  
ANISOU 2073  C   LYS A 272    20917  14450  15117  -2428  -1206   3830  A    C  
ATOM   2074  O   LYS A 272      48.120 -32.758  19.880  1.00136.88      A    O  
ANISOU 2074  O   LYS A 272    21398  14819  15792  -2182  -1381   3828  A    O  
ATOM   2075  CB  LYS A 272      46.705 -33.518  22.660  1.00129.15      A    C  
ANISOU 2075  CB  LYS A 272    20939  13813  14316  -2709  -1178   4330  A    C  
ATOM   2076  CG  LYS A 272      46.058 -34.758  23.268  1.00134.93      A    C  
ANISOU 2076  CG  LYS A 272    21957  14273  15035  -2891  -1121   4587  A    C  
ATOM   2077  CD  LYS A 272      45.972 -34.679  24.791  1.00134.69      A    C  
ANISOU 2077  CD  LYS A 272    22146  14377  14654  -3049  -1089   4836  A    C  
ATOM   2078  CE  LYS A 272      45.020 -35.754  25.303  1.00143.31      A    C  
ANISOU 2078  CE  LYS A 272    23482  15230  15738  -3301   -955   5058  A    C  
ATOM   2079  NZ  LYS A 272      44.758 -35.642  26.751  1.00160.15      A    N1+
ANISOU 2079  NZ  LYS A 272    25825  17510  17513  -3486   -875   5289  A    N1+
ATOM   2080  N   ARG A 273      47.045 -30.956  20.692  1.00137.58      A    N  
ANISOU 2080  N   ARG A 273    21352  15353  15570  -2487  -1114   3674  A    N  
ATOM   2081  CA  ARG A 273      47.788 -29.977  19.874  1.00149.88      A    C  
ANISOU 2081  CA  ARG A 273    22658  17087  17203  -2295  -1193   3454  A    C  
ATOM   2082  C   ARG A 273      49.303 -30.133  19.925  1.00144.12      A    C  
ANISOU 2082  C   ARG A 273    21922  16369  16469  -2037  -1457   3554  A    C  
ATOM   2083  O   ARG A 273      49.908 -30.002  20.979  1.00153.70      A    O  
ANISOU 2083  O   ARG A 273    23249  17694  17455  -2040  -1573   3726  A    O  
ATOM   2084  CB  ARG A 273      47.402 -28.538  20.223  1.00156.04      A    C  
ANISOU 2084  CB  ARG A 273    23318  18175  17793  -2413  -1057   3301  A    C  
ATOM   2085  CG  ARG A 273      45.911 -28.297  20.284  1.00163.35      A    C  
ANISOU 2085  CG  ARG A 273    24228  19134  18702  -2652   -784   3217  A    C  
ATOM   2086  CD  ARG A 273      45.517 -26.831  20.350  1.00190.96      A    C  
ANISOU 2086  CD  ARG A 273    27577  22908  22069  -2712   -638   3019  A    C  
ATOM   2087  NE  ARG A 273      44.293 -26.645  21.147  1.00222.50      A    N  
ANISOU 2087  NE  ARG A 273    31655  26984  25901  -2950   -392   3057  A    N  
ATOM   2088  CZ  ARG A 273      43.525 -25.561  21.117  1.00219.12      A    C  
ANISOU 2088  CZ  ARG A 273    31102  26749  25404  -3027   -191   2882  A    C  
ATOM   2089  NH1 ARG A 273      43.828 -24.554  20.306  1.00226.22      A    N1+
ANISOU 2089  NH1 ARG A 273    31801  27765  26387  -2900   -212   2658  A    N1+
ATOM   2090  NH2 ARG A 273      42.449 -25.503  21.890  1.00186.52      A    N  
ANISOU 2090  NH2 ARG A 273    27050  22692  21125  -3226     39   2940  A    N  
ATOM   2091  N   LYS A 274      49.909 -30.342  18.763  1.00137.76      A    N  
ANISOU 2091  N   LYS A 274    20964  15473  15906  -1813  -1548   3436  A    N  
ATOM   2092  CA  LYS A 274      51.348 -30.579  18.676  1.00131.26      A    C  
ANISOU 2092  CA  LYS A 274    20096  14655  15120  -1539  -1788   3531  A    C  
ATOM   2093  C   LYS A 274      52.054 -29.533  17.784  1.00124.94      A    C  
ANISOU 2093  C   LYS A 274    19001  14070  14400  -1385  -1830   3314  A    C  
ATOM   2094  O   LYS A 274      53.176 -29.757  17.340  1.00124.99      A    O  
ANISOU 2094  O   LYS A 274    18904  14072  14512  -1133  -1996   3344  A    O  
ATOM   2095  CB  LYS A 274      51.618 -31.983  18.132  1.00140.84      A    C  
ANISOU 2095  CB  LYS A 274    21425  15532  16555  -1361  -1872   3631  A    C  
ATOM   2096  CG  LYS A 274      50.776 -33.094  18.710  1.00142.01      A    C  
ANISOU 2096  CG  LYS A 274    21861  15406  16690  -1529  -1804   3812  A    C  
ATOM   2097  CD  LYS A 274      51.250 -34.474  18.269  1.00135.56      A    C  
ANISOU 2097  CD  LYS A 274    21194  14236  16074  -1320  -1923   3932  A    C  
ATOM   2098  CE  LYS A 274      50.380 -35.538  18.944  1.00148.15      A    C  
ANISOU 2098  CE  LYS A 274    23099  15552  17636  -1529  -1853   4132  A    C  
ATOM   2099  NZ  LYS A 274      50.858 -36.933  18.785  1.00152.95      A    N1+
ANISOU 2099  NZ  LYS A 274    23927  15786  18399  -1340  -1982   4301  A    N1+
ATOM   2100  N   VAL A 275      51.358 -28.430  17.500  1.00115.44      A    N  
ANISOU 2100  N   VAL A 275    17663  13043  13155  -1532  -1669   3103  A    N  
ATOM   2101  CA  VAL A 275      51.821 -27.490  16.485  1.00110.93      A    C  
ANISOU 2101  CA  VAL A 275    16827  12632  12690  -1410  -1673   2882  A    C  
ATOM   2102  C   VAL A 275      53.202 -26.956  16.828  1.00116.60      A    C  
ANISOU 2102  C   VAL A 275    17440  13550  13311  -1270  -1876   2954  A    C  
ATOM   2103  O   VAL A 275      54.099 -26.919  15.979  1.00118.37      A    O  
ANISOU 2103  O   VAL A 275    17481  13804  13688  -1053  -1974   2895  A    O  
ATOM   2104  CB  VAL A 275      50.877 -26.278  16.309  1.00106.62      A    C  
ANISOU 2104  CB  VAL A 275    16176  12257  12075  -1594  -1476   2670  A    C  
ATOM   2105  CG1 VAL A 275      51.519 -25.248  15.388  1.00 99.73      A    C  
ANISOU 2105  CG1 VAL A 275    15050  11558  11281  -1468  -1507   2479  A    C  
ATOM   2106  CG2 VAL A 275      49.506 -26.709  15.804  1.00115.74      A    C  
ANISOU 2106  CG2 VAL A 275    17367  13254  13354  -1727  -1279   2578  A    C  
ATOM   2107  N   LYS A 276      53.366 -26.543  18.077  1.00115.00      A    N  
ANISOU 2107  N   LYS A 276    17351  13495  12847  -1402  -1937   3083  A    N  
ATOM   2108  CA  LYS A 276      54.622 -25.967  18.525  1.00110.31      A    C  
ANISOU 2108  CA  LYS A 276    16662  13117  12132  -1319  -2145   3158  A    C  
ATOM   2109  C   LYS A 276      55.694 -27.026  18.784  1.00121.81      A    C  
ANISOU 2109  C   LYS A 276    18159  14481  13641  -1104  -2374   3399  A    C  
ATOM   2110  O   LYS A 276      56.881 -26.754  18.617  1.00139.92      A    O  
ANISOU 2110  O   LYS A 276    20276  16923  15962   -942  -2554   3434  A    O  
ATOM   2111  CB  LYS A 276      54.413 -25.114  19.785  1.00106.32      A    C  
ANISOU 2111  CB  LYS A 276    16285  12805  11303  -1547  -2140   3197  A    C  
ATOM   2112  CG  LYS A 276      53.837 -23.745  19.527  1.00 99.71      A    C  
ANISOU 2112  CG  LYS A 276    15350  12132  10400  -1695  -1977   2952  A    C  
ATOM   2113  CD  LYS A 276      53.672 -22.929  20.812  1.00102.35      A    C  
ANISOU 2113  CD  LYS A 276    15849  12641  10398  -1906  -1972   2984  A    C  
ATOM   2114  CE  LYS A 276      53.465 -21.450  20.470  1.00115.32      A    C  
ANISOU 2114  CE  LYS A 276    17370  14454  11990  -1997  -1865   2736  A    C  
ATOM   2115  NZ  LYS A 276      53.840 -20.481  21.535  1.00124.64      A    N1+
ANISOU 2115  NZ  LYS A 276    18662  15834  12861  -2147  -1947   2741  A    N1+
ATOM   2116  N   ASP A 277      55.271 -28.228  19.185  1.00124.01      A    N  
ANISOU 2116  N   ASP A 277    18665  14514  13937  -1102  -2365   3572  A    N  
ATOM   2117  CA  ASP A 277      56.209 -29.327  19.409  1.00132.88      A    C  
ANISOU 2117  CA  ASP A 277    19854  15507  15125   -873  -2572   3812  A    C  
ATOM   2118  C   ASP A 277      56.781 -29.896  18.106  1.00135.63      A    C  
ANISOU 2118  C   ASP A 277    20036  15716  15780   -578  -2601   3731  A    C  
ATOM   2119  O   ASP A 277      57.984 -30.152  18.003  1.00141.38      A    O  
ANISOU 2119  O   ASP A 277    20642  16501  16572   -330  -2790   3842  A    O  
ATOM   2120  CB  ASP A 277      55.550 -30.459  20.207  1.00123.33      A    C  
ANISOU 2120  CB  ASP A 277    18967  14046  13846   -965  -2545   4027  A    C  
ATOM   2121  CG  ASP A 277      55.728 -30.305  21.701  1.00126.28      A    C  
ANISOU 2121  CG  ASP A 277    19521  14559  13899  -1110  -2656   4248  A    C  
ATOM   2122  OD1 ASP A 277      56.042 -29.183  22.151  1.00139.13      A    O  
ANISOU 2122  OD1 ASP A 277    21051  16476  15334  -1212  -2703   4183  A    O  
ATOM   2123  OD2 ASP A 277      55.565 -31.316  22.419  1.00123.69      A    O1-
ANISOU 2123  OD2 ASP A 277    19448  14042  13506  -1123  -2702   4488  A    O1-
ATOM   2124  N   ARG A 278      55.909 -30.097  17.123  1.00121.80      A    N  
ANISOU 2124  N   ARG A 278    18279  13791  14208   -605  -2412   3540  A    N  
ATOM   2125  CA  ARG A 278      56.315 -30.760  15.893  1.00115.66      A    C  
ANISOU 2125  CA  ARG A 278    17403  12840  13703   -336  -2417   3455  A    C  
ATOM   2126  C   ARG A 278      57.178 -29.839  15.033  1.00111.90      A    C  
ANISOU 2126  C   ARG A 278    16602  12608  13306   -181  -2453   3294  A    C  
ATOM   2127  O   ARG A 278      58.070 -30.313  14.343  1.00117.89      A    O  
ANISOU 2127  O   ARG A 278    17242  13320  14230    107  -2537   3309  A    O  
ATOM   2128  CB  ARG A 278      55.094 -31.249  15.125  1.00131.32      A    C  
ANISOU 2128  CB  ARG A 278    19493  14569  15832   -440  -2220   3297  A    C  
ATOM   2129  CG  ARG A 278      55.256 -32.541  14.325  1.00143.74      A    C  
ANISOU 2129  CG  ARG A 278    21168  15808  17637   -211  -2241   3311  A    C  
ATOM   2130  CD  ARG A 278      53.889 -33.209  14.071  1.00136.82      A    C  
ANISOU 2130  CD  ARG A 278    20498  14649  16836   -414  -2080   3241  A    C  
ATOM   2131  NE  ARG A 278      53.853 -33.916  12.788  1.00130.18      A    N  
ANISOU 2131  NE  ARG A 278    19662  13564  16234   -239  -2042   3089  A    N  
ATOM   2132  CZ  ARG A 278      53.592 -33.329  11.620  1.00129.36      A    C  
ANISOU 2132  CZ  ARG A 278    19370  13543  16236   -222  -1939   2822  A    C  
ATOM   2133  NH1 ARG A 278      53.318 -32.036  11.556  1.00111.43      A    N1+
ANISOU 2133  NH1 ARG A 278    16892  11574  13869   -366  -1861   2684  A    N1+
ATOM   2134  NH2 ARG A 278      53.600 -34.036  10.499  1.00148.10      A    N  
ANISOU 2134  NH2 ARG A 278    21782  15687  18803    -56  -1916   2691  A    N  
ATOM   2135  N   LEU A 279      56.974 -28.531  15.178  1.00109.39      A    N  
ANISOU 2135  N   LEU A 279    16153  12555  12855   -370  -2396   3164  A    N  
ATOM   2136  CA  LEU A 279      57.702 -27.534  14.424  1.00109.77      A    C  
ANISOU 2136  CA  LEU A 279    15906  12844  12958   -279  -2417   3014  A    C  
ATOM   2137  C   LEU A 279      58.855 -26.921  15.214  1.00119.51      A    C  
ANISOU 2137  C   LEU A 279    17016  14351  14039   -260  -2621   3156  A    C  
ATOM   2138  O   LEU A 279      59.756 -26.274  14.644  1.00116.56      A    O  
ANISOU 2138  O   LEU A 279    16378  14178  13728   -145  -2686   3092  A    O  
ATOM   2139  CB  LEU A 279      56.745 -26.427  13.979  1.00106.32      A    C  
ANISOU 2139  CB  LEU A 279    15403  12507  12485   -496  -2224   2770  A    C  
ATOM   2140  CG  LEU A 279      55.824 -26.818  12.823  1.00105.37      A    C  
ANISOU 2140  CG  LEU A 279    15295  12186  12555   -474  -2045   2583  A    C  
ATOM   2141  CD1 LEU A 279      55.013 -25.600  12.376  1.00 94.08      A    C  
ANISOU 2141  CD1 LEU A 279    13760  10899  11087   -658  -1878   2357  A    C  
ATOM   2142  CD2 LEU A 279      56.678 -27.337  11.671  1.00111.41      A    C  
ANISOU 2142  CD2 LEU A 279    15910  12885  13535   -168  -2095   2537  A    C  
ATOM   2143  N   LYS A 280      58.785 -27.122  16.526  1.00136.04      A    N  
ANISOU 2143  N   LYS A 280    19306  16457  15925   -392  -2718   3350  A    N  
ATOM   2144  CA  LYS A 280      59.813 -26.708  17.480  1.00135.31      A    C  
ANISOU 2144  CA  LYS A 280    19153  16604  15652   -401  -2946   3522  A    C  
ATOM   2145  C   LYS A 280      61.227 -26.889  16.930  1.00124.00      A    C  
ANISOU 2145  C   LYS A 280    17451  15288  14374   -108  -3123   3598  A    C  
ATOM   2146  O   LYS A 280      62.077 -26.001  17.062  1.00119.84      A    O  
ANISOU 2146  O   LYS A 280    16712  15044  13776   -134  -3250   3597  A    O  
ATOM   2147  CB  LYS A 280      59.625 -27.519  18.758  1.00135.60      A    C  
ANISOU 2147  CB  LYS A 280    19478  16529  15512   -469  -3044   3776  A    C  
ATOM   2148  CG  LYS A 280      60.598 -27.337  19.893  1.00127.15      A    C  
ANISOU 2148  CG  LYS A 280    18408  15671  14229   -481  -3304   3999  A    C  
ATOM   2149  CD  LYS A 280      60.188 -28.253  21.058  1.00116.96      A    C  
ANISOU 2149  CD  LYS A 280    17450  14220  12768   -553  -3358   4244  A    C  
ATOM   2150  CE  LYS A 280      61.306 -29.216  21.420  1.00115.12      A    C  
ANISOU 2150  CE  LYS A 280    17207  13955  12578   -286  -3617   4532  A    C  
ATOM   2151  NZ  LYS A 280      60.778 -30.566  21.772  1.00119.02      A    N1+
ANISOU 2151  NZ  LYS A 280    18000  14118  13104   -223  -3586   4720  A    N1+
ATOM   2152  N   ALA A 281      61.454 -28.036  16.288  1.00118.70      A    N  
ANISOU 2152  N   ALA A 281    16788  14393  13917    168  -3121   3657  A    N  
ATOM   2153  CA  ALA A 281      62.750 -28.398  15.723  1.00114.57      A    C  
ANISOU 2153  CA  ALA A 281    16018  13948  13562    498  -3261   3742  A    C  
ATOM   2154  C   ALA A 281      63.252 -27.349  14.734  1.00128.04      A    C  
ANISOU 2154  C   ALA A 281    17392  15894  15361    527  -3207   3544  A    C  
ATOM   2155  O   ALA A 281      64.237 -26.645  14.992  1.00131.01      A    O  
ANISOU 2155  O   ALA A 281    17537  16564  15675    526  -3363   3610  A    O  
ATOM   2156  CB  ALA A 281      62.648 -29.765  15.028  1.00106.62      A    C  
ANISOU 2156  CB  ALA A 281    15124  12606  12780    780  -3200   3772  A    C  
ATOM   2157  N   TYR A 282      62.541 -27.224  13.618  1.00128.13      A    N  
ANISOU 2157  N   TYR A 282    17387  15782  15512    528  -2989   3306  A    N  
ATOM   2158  CA  TYR A 282      62.941 -26.357  12.517  1.00102.01      A    C  
ANISOU 2158  CA  TYR A 282    13788  12657  12311    580  -2909   3117  A    C  
ATOM   2159  C   TYR A 282      62.995 -24.868  12.871  1.00103.16      A    C  
ANISOU 2159  C   TYR A 282    13809  13094  12292    306  -2928   3034  A    C  
ATOM   2160  O   TYR A 282      63.928 -24.169  12.482  1.00108.53      A    O  
ANISOU 2160  O   TYR A 282    14208  14019  13008    359  -2995   3018  A    O  
ATOM   2161  CB  TYR A 282      62.028 -26.552  11.328  1.00 94.09      A    C  
ANISOU 2161  CB  TYR A 282    12841  11449  11458    610  -2679   2885  A    C  
ATOM   2162  CG  TYR A 282      61.762 -27.981  10.965  1.00111.37      A    C  
ANISOU 2162  CG  TYR A 282    15214  13306  13796    826  -2640   2927  A    C  
ATOM   2163  CD1 TYR A 282      60.698 -28.670  11.544  1.00117.33      A    C  
ANISOU 2163  CD1 TYR A 282    16286  13798  14496    678  -2589   2968  A    C  
ATOM   2164  CD2 TYR A 282      62.550 -28.644  10.032  1.00115.30      A    C  
ANISOU 2164  CD2 TYR A 282    15580  13741  14486   1171  -2643   2921  A    C  
ATOM   2165  CE1 TYR A 282      60.420 -29.977  11.191  1.00116.75      A    C  
ANISOU 2165  CE1 TYR A 282    16406  13390  14562    849  -2554   3000  A    C  
ATOM   2166  CE2 TYR A 282      62.292 -29.962   9.686  1.00120.06      A    C  
ANISOU 2166  CE2 TYR A 282    16387  14005  15222   1370  -2606   2944  A    C  
ATOM   2167  CZ  TYR A 282      61.222 -30.621  10.265  1.00121.48      A    C  
ANISOU 2167  CZ  TYR A 282    16895  13909  15349   1198  -2568   2982  A    C  
ATOM   2168  OH  TYR A 282      60.944 -31.925   9.919  1.00124.48      A    O  
ANISOU 2168  OH  TYR A 282    17502  13929  15863   1368  -2535   3002  A    O  
ATOM   2169  N   VAL A 283      61.995 -24.389  13.600  1.00109.23      A    N  
ANISOU 2169  N   VAL A 283    14791  13828  12880     13  -2860   2981  A    N  
ATOM   2170  CA  VAL A 283      61.776 -22.949  13.745  1.00115.81      A    C  
ANISOU 2170  CA  VAL A 283    15558  14869  13573   -247  -2816   2840  A    C  
ATOM   2171  C   VAL A 283      62.643 -22.296  14.818  1.00131.22      A    C  
ANISOU 2171  C   VAL A 283    17452  17076  15327   -377  -3037   2982  A    C  
ATOM   2172  O   VAL A 283      63.331 -21.301  14.540  1.00143.73      A    O  
ANISOU 2172  O   VAL A 283    18814  18891  16904   -434  -3093   2921  A    O  
ATOM   2173  CB  VAL A 283      60.280 -22.650  14.016  1.00110.03      A    C  
ANISOU 2173  CB  VAL A 283    15073  13998  12733   -491  -2622   2703  A    C  
ATOM   2174  CG1 VAL A 283      60.014 -21.145  14.067  1.00 99.17      A    C  
ANISOU 2174  CG1 VAL A 283    13642  12807  11228   -728  -2554   2538  A    C  
ATOM   2175  CG2 VAL A 283      59.439 -23.287  12.909  1.00105.74      A    C  
ANISOU 2175  CG2 VAL A 283    14565  13219  12389   -381  -2426   2561  A    C  
ATOM   2176  N   ARG A 284      62.627 -22.854  16.026  1.00120.34      A    N  
ANISOU 2176  N   ARG A 284    16278  15658  13785   -433  -3170   3176  A    N  
ATOM   2177  CA  ARG A 284      63.534 -22.369  17.090  1.00138.25      A    C  
ANISOU 2177  CA  ARG A 284    18501  18173  15853   -541  -3420   3336  A    C  
ATOM   2178  C   ARG A 284      63.034 -21.067  17.743  1.00144.45      A    C  
ANISOU 2178  C   ARG A 284    19400  19090  16393   -882  -3384   3206  A    C  
ATOM   2179  O   ARG A 284      62.837 -21.014  18.951  1.00161.93      A    O  
ANISOU 2179  O   ARG A 284    21833  21334  18358  -1052  -3475   3307  A    O  
ATOM   2180  CB  ARG A 284      64.942 -22.128  16.537  1.00134.59      A    C  
ANISOU 2180  CB  ARG A 284    17673  17939  15524   -371  -3583   3396  A    C  
ATOM   2181  CG  ARG A 284      65.589 -23.338  15.886  1.00144.50      A    C  
ANISOU 2181  CG  ARG A 284    18790  19093  17018      0  -3623   3523  A    C  
ATOM   2182  CD  ARG A 284      66.805 -22.914  15.059  1.00145.11      A    C  
ANISOU 2182  CD  ARG A 284    18466  19412  17255    160  -3697   3519  A    C  
ATOM   2183  NE  ARG A 284      67.812 -23.970  14.999  1.00166.80      A    N  
ANISOU 2183  NE  ARG A 284    21061  22171  20144    500  -3849   3738  A    N  
ATOM   2184  CZ  ARG A 284      69.110 -23.749  14.786  1.00174.38      A    C  
ANISOU 2184  CZ  ARG A 284    21667  23403  21185    639  -4007   3846  A    C  
ATOM   2185  NH1 ARG A 284      69.550 -22.510  14.609  1.00177.18      A    N1+
ANISOU 2185  NH1 ARG A 284    21796  24030  21491    438  -4038   3756  A    N1+
ATOM   2186  NH2 ARG A 284      69.966 -24.763  14.758  1.00170.84      A    N  
ANISOU 2186  NH2 ARG A 284    21088  22954  20869    977  -4133   4052  A    N  
ATOM   2187  N   ASP A 285      62.875 -20.022  16.934  1.00129.14      A    N  
ANISOU 2187  N   ASP A 285    17320  17228  14519   -967  -3253   2987  A    N  
ATOM   2188  CA  ASP A 285      62.435 -18.723  17.451  1.00113.86      A    C  
ANISOU 2188  CA  ASP A 285    15493  15398  12369  -1267  -3207   2845  A    C  
ATOM   2189  C   ASP A 285      61.053 -18.789  18.107  1.00110.51      A    C  
ANISOU 2189  C   ASP A 285    15400  14805  11781  -1429  -3028   2780  A    C  
ATOM   2190  O   ASP A 285      60.080 -19.204  17.491  1.00107.75      A    O  
ANISOU 2190  O   ASP A 285    15114  14264  11560  -1369  -2812   2680  A    O  
ATOM   2191  CB  ASP A 285      62.397 -17.680  16.338  1.00110.40      A    C  
ANISOU 2191  CB  ASP A 285    14863  15023  12058  -1301  -3068   2624  A    C  
ATOM   2192  CG  ASP A 285      61.981 -16.305  16.835  1.00115.13      A    C  
ANISOU 2192  CG  ASP A 285    15588  15707  12447  -1593  -3020   2472  A    C  
ATOM   2193  OD1 ASP A 285      60.789 -16.046  17.076  1.00112.97      A    O  
ANISOU 2193  OD1 ASP A 285    15541  15305  12075  -1713  -2829   2348  A    O  
ATOM   2194  OD2 ASP A 285      62.866 -15.436  16.900  1.00117.67      A    O1-
ANISOU 2194  OD2 ASP A 285    15765  16226  12717  -1699  -3166   2468  A    O1-
ATOM   2195  N   PRO A 286      60.977 -18.384  19.378  1.00114.70      A    N  
ANISOU 2195  N   PRO A 286    16140  15420  12019  -1639  -3121   2841  A    N  
ATOM   2196  CA  PRO A 286      59.729 -18.464  20.157  1.00113.63      A    C  
ANISOU 2196  CA  PRO A 286    16323  15155  11694  -1795  -2953   2807  A    C  
ATOM   2197  C   PRO A 286      58.583 -17.717  19.477  1.00109.77      A    C  
ANISOU 2197  C   PRO A 286    15861  14580  11265  -1878  -2662   2550  A    C  
ATOM   2198  O   PRO A 286      57.487 -18.266  19.325  1.00114.00      A    O  
ANISOU 2198  O   PRO A 286    16517  14941  11857  -1862  -2459   2514  A    O  
ATOM   2199  CB  PRO A 286      60.089 -17.785  21.471  1.00115.71      A    C  
ANISOU 2199  CB  PRO A 286    16754  15587  11620  -2015  -3118   2867  A    C  
ATOM   2200  CG  PRO A 286      61.568 -17.920  21.571  1.00121.33      A    C  
ANISOU 2200  CG  PRO A 286    17259  16481  12360  -1930  -3432   3034  A    C  
ATOM   2201  CD  PRO A 286      62.089 -17.828  20.160  1.00116.77      A    C  
ANISOU 2201  CD  PRO A 286    16344  15918  12101  -1748  -3396   2948  A    C  
ATOM   2202  N   TYR A 287      58.839 -16.478  19.058  1.00106.87      A    N  
ANISOU 2202  N   TYR A 287    15376  14335  10893  -1968  -2646   2382  A    N  
ATOM   2203  CA  TYR A 287      57.806 -15.615  18.467  1.00101.46      A    C  
ANISOU 2203  CA  TYR A 287    14719  13584  10244  -2046  -2387   2143  A    C  
ATOM   2204  C   TYR A 287      57.251 -16.195  17.160  1.00 93.42      A    C  
ANISOU 2204  C   TYR A 287    13555  12418   9522  -1862  -2214   2064  A    C  
ATOM   2205  O   TYR A 287      56.043 -16.201  16.943  1.00 95.05      A    O  
ANISOU 2205  O   TYR A 287    13858  12502   9754  -1893  -1989   1954  A    O  
ATOM   2206  CB  TYR A 287      58.356 -14.209  18.206  1.00100.15      A    C  
ANISOU 2206  CB  TYR A 287    14451  13564  10035  -2161  -2434   2001  A    C  
ATOM   2207  CG  TYR A 287      58.779 -13.475  19.440  1.00109.83      A    C  
ANISOU 2207  CG  TYR A 287    15851  14923  10954  -2378  -2587   2030  A    C  
ATOM   2208  CD1 TYR A 287      57.905 -13.324  20.504  1.00111.52      A    C  
ANISOU 2208  CD1 TYR A 287    16374  15089  10907  -2526  -2484   2005  A    C  
ATOM   2209  CD2 TYR A 287      60.049 -12.907  19.542  1.00123.18      A    C  
ANISOU 2209  CD2 TYR A 287    17401  16795  12606  -2446  -2833   2078  A    C  
ATOM   2210  CE1 TYR A 287      58.273 -12.622  21.639  1.00119.82      A    C  
ANISOU 2210  CE1 TYR A 287    17617  16257  11649  -2731  -2622   2012  A    C  
ATOM   2211  CE2 TYR A 287      60.438 -12.243  20.689  1.00131.51      A    C  
ANISOU 2211  CE2 TYR A 287    18633  17969  13364  -2666  -2995   2097  A    C  
ATOM   2212  CZ  TYR A 287      59.541 -12.084  21.723  1.00129.34      A    C  
ANISOU 2212  CZ  TYR A 287    18693  17632  12818  -2805  -2887   2054  A    C  
ATOM   2213  OH  TYR A 287      59.919 -11.395  22.851  1.00133.60      A    O  
ANISOU 2213  OH  TYR A 287    19436  18286  13040  -3027  -3045   2055  A    O  
ATOM   2214  N   ALA A 288      58.153 -16.655  16.291  1.00 82.66      A    N  
ANISOU 2214  N   ALA A 288    11952  11079   8373  -1673  -2324   2120  A    N  
ATOM   2215  CA  ALA A 288      57.769 -17.335  15.079  1.00 82.11      A    C  
ANISOU 2215  CA  ALA A 288    11761  10868   8567  -1484  -2193   2060  A    C  
ATOM   2216  C   ALA A 288      56.811 -18.494  15.366  1.00 93.44      A    C  
ANISOU 2216  C   ALA A 288    13381  12098  10021  -1453  -2091   2129  A    C  
ATOM   2217  O   ALA A 288      55.778 -18.646  14.708  1.00 99.99      A    O  
ANISOU 2217  O   ALA A 288    14231  12796  10962  -1442  -1893   2006  A    O  
ATOM   2218  CB  ALA A 288      58.997 -17.840  14.350  1.00 79.93      A    C  
ANISOU 2218  CB  ALA A 288    11238  10653   8477  -1268  -2346   2151  A    C  
ATOM   2219  N   LEU A 289      57.149 -19.309  16.352  1.00 90.24      A    N  
ANISOU 2219  N   LEU A 289    13110  11669   9505  -1449  -2232   2334  A    N  
ATOM   2220  CA  LEU A 289      56.311 -20.443  16.701  1.00 88.52      A    C  
ANISOU 2220  CA  LEU A 289    13084  11250   9296  -1438  -2148   2429  A    C  
ATOM   2221  C   LEU A 289      54.953 -19.983  17.222  1.00 87.64      A    C  
ANISOU 2221  C   LEU A 289    13163  11098   9036  -1649  -1935   2328  A    C  
ATOM   2222  O   LEU A 289      53.926 -20.589  16.930  1.00 90.57      A    O  
ANISOU 2222  O   LEU A 289    13606  11305   9500  -1656  -1768   2296  A    O  
ATOM   2223  CB  LEU A 289      57.008 -21.361  17.719  1.00 90.83      A    C  
ANISOU 2223  CB  LEU A 289    13498  11531   9480  -1392  -2356   2693  A    C  
ATOM   2224  CG  LEU A 289      58.134 -22.235  17.153  1.00106.46      A    C  
ANISOU 2224  CG  LEU A 289    15311  13481  11657  -1124  -2532   2824  A    C  
ATOM   2225  CD1 LEU A 289      59.063 -22.719  18.243  1.00120.17      A    C  
ANISOU 2225  CD1 LEU A 289    17118  15296  13244  -1091  -2784   3082  A    C  
ATOM   2226  CD2 LEU A 289      57.602 -23.380  16.322  1.00117.08      A    C  
ANISOU 2226  CD2 LEU A 289    16684  14567  13233   -961  -2418   2814  A    C  
ATOM   2227  N   ASP A 290      54.944 -18.900  17.987  1.00 89.53      A    N  
ANISOU 2227  N   ASP A 290    13481  11490   9044  -1822  -1936   2274  A    N  
ATOM   2228  CA  ASP A 290      53.700 -18.388  18.522  1.00 96.95      A    C  
ANISOU 2228  CA  ASP A 290    14596  12411   9827  -2001  -1719   2175  A    C  
ATOM   2229  C   ASP A 290      52.767 -17.890  17.426  1.00103.61      A    C  
ANISOU 2229  C   ASP A 290    15320  13199  10845  -1982  -1493   1958  A    C  
ATOM   2230  O   ASP A 290      51.563 -18.184  17.437  1.00103.58      A    O  
ANISOU 2230  O   ASP A 290    15398  13097  10861  -2040  -1294   1919  A    O  
ATOM   2231  CB  ASP A 290      53.943 -17.282  19.542  1.00 96.75      A    C  
ANISOU 2231  CB  ASP A 290    14701  12552   9507  -2174  -1769   2143  A    C  
ATOM   2232  CG  ASP A 290      52.657 -16.859  20.235  1.00102.22      A    C  
ANISOU 2232  CG  ASP A 290    15602  13224  10013  -2337  -1531   2060  A    C  
ATOM   2233  OD1 ASP A 290      52.016 -17.746  20.835  1.00113.44      A    O  
ANISOU 2233  OD1 ASP A 290    17177  14555  11370  -2375  -1457   2188  A    O  
ATOM   2234  OD2 ASP A 290      52.331 -15.658  20.207  1.00100.83      A    O1-
ANISOU 2234  OD2 ASP A 290    15440  13121   9749  -2422  -1421   1881  A    O1-
ATOM   2235  N   LEU A 291      53.322 -17.149  16.472  1.00102.52      A    N  
ANISOU 2235  N   LEU A 291    14981  13135  10837  -1904  -1527   1829  A    N  
ATOM   2236  CA  LEU A 291      52.536 -16.641  15.356  1.00 89.73      A    C  
ANISOU 2236  CA  LEU A 291    13236  11473   9381  -1869  -1338   1633  A    C  
ATOM   2237  C   LEU A 291      51.975 -17.772  14.484  1.00 85.87      A    C  
ANISOU 2237  C   LEU A 291    12682  10818   9125  -1748  -1263   1643  A    C  
ATOM   2238  O   LEU A 291      50.790 -17.735  14.104  1.00 85.33      A    O  
ANISOU 2238  O   LEU A 291    12621  10680   9119  -1791  -1069   1538  A    O  
ATOM   2239  CB  LEU A 291      53.352 -15.668  14.492  1.00 77.94      A    C  
ANISOU 2239  CB  LEU A 291    11548  10091   7975  -1808  -1404   1519  A    C  
ATOM   2240  CG  LEU A 291      52.637 -15.113  13.247  1.00 75.58      A    C  
ANISOU 2240  CG  LEU A 291    11114   9757   7844  -1753  -1229   1327  A    C  
ATOM   2241  CD1 LEU A 291      51.251 -14.588  13.603  1.00 79.54      A    C  
ANISOU 2241  CD1 LEU A 291    11743  10226   8252  -1872  -1006   1220  A    C  
ATOM   2242  CD2 LEU A 291      53.467 -14.033  12.575  1.00 72.40      A    C  
ANISOU 2242  CD2 LEU A 291    10556   9471   7480  -1729  -1292   1234  A    C  
ATOM   2243  N   ILE A 292      52.816 -18.759  14.169  1.00 83.10      A    N  
ANISOU 2243  N   ILE A 292    12269  10404   8899  -1598  -1418   1765  A    N  
ATOM   2244  CA  ILE A 292      52.372 -19.879  13.348  1.00 83.38      A    C  
ANISOU 2244  CA  ILE A 292    12275  10257   9148  -1482  -1365   1768  A    C  
ATOM   2245  C   ILE A 292      51.239 -20.615  14.047  1.00 95.51      A    C  
ANISOU 2245  C   ILE A 292    14006  11659  10622  -1610  -1248   1841  A    C  
ATOM   2246  O   ILE A 292      50.271 -21.046  13.415  1.00 97.80      A    O  
ANISOU 2246  O   ILE A 292    14284  11826  11047  -1623  -1112   1765  A    O  
ATOM   2247  CB  ILE A 292      53.481 -20.910  13.125  1.00 73.78      A    C  
ANISOU 2247  CB  ILE A 292    11013   8973   8045  -1289  -1551   1912  A    C  
ATOM   2248  CG1 ILE A 292      54.633 -20.292  12.348  1.00 77.51      A    C  
ANISOU 2248  CG1 ILE A 292    11259   9588   8601  -1149  -1655   1854  A    C  
ATOM   2249  CG2 ILE A 292      52.916 -22.130  12.420  1.00 75.37      A    C  
ANISOU 2249  CG2 ILE A 292    11252   8945   8438  -1193  -1490   1913  A    C  
ATOM   2250  CD1 ILE A 292      55.885 -21.141  12.324  1.00 86.28      A    C  
ANISOU 2250  CD1 ILE A 292    12302  10691   9790   -950  -1850   2017  A    C  
ATOM   2251  N   ASP A 293      51.383 -20.762  15.362  1.00 91.13      A    N  
ANISOU 2251  N   ASP A 293    13630  11138   9857  -1716  -1310   1997  A    N  
ATOM   2252  CA  ASP A 293      50.368 -21.398  16.164  1.00 93.04      A    C  
ANISOU 2252  CA  ASP A 293    14066  11278  10006  -1859  -1193   2091  A    C  
ATOM   2253  C   ASP A 293      49.027 -20.662  16.067  1.00 93.98      A    C  
ANISOU 2253  C   ASP A 293    14176  11438  10093  -2001   -945   1931  A    C  
ATOM   2254  O   ASP A 293      47.952 -21.285  16.059  1.00115.56      A    O  
ANISOU 2254  O   ASP A 293    16964  14059  12882  -2084   -800   1948  A    O  
ATOM   2255  CB  ASP A 293      50.829 -21.478  17.623  1.00 96.44      A    C  
ANISOU 2255  CB  ASP A 293    14692  11778  10171  -1952  -1303   2278  A    C  
ATOM   2256  CG  ASP A 293      49.922 -22.361  18.466  1.00103.74      A    C  
ANISOU 2256  CG  ASP A 293    15833  12579  11003  -2084  -1200   2424  A    C  
ATOM   2257  OD1 ASP A 293      49.413 -23.365  17.918  1.00112.22      A    O  
ANISOU 2257  OD1 ASP A 293    16909  13463  12264  -2051  -1148   2457  A    O  
ATOM   2258  OD2 ASP A 293      49.697 -22.035  19.647  1.00105.21      A    O1-
ANISOU 2258  OD2 ASP A 293    16190  12857  10925  -2232  -1164   2500  A    O1-
ATOM   2259  N   LYS A 294      49.089 -19.330  15.994  1.00 75.02      A    N  
ANISOU 2259  N   LYS A 294    11701   9196   7607  -2029   -896   1783  A    N  
ATOM   2260  CA  LYS A 294      47.853 -18.534  15.970  1.00 74.67      A    C  
ANISOU 2260  CA  LYS A 294    11649   9203   7520  -2137   -659   1636  A    C  
ATOM   2261  C   LYS A 294      47.258 -18.436  14.565  1.00 85.36      A    C  
ANISOU 2261  C   LYS A 294    12804  10508   9121  -2054   -560   1475  A    C  
ATOM   2262  O   LYS A 294      46.079 -18.121  14.404  1.00 87.69      A    O  
ANISOU 2262  O   LYS A 294    13065  10813   9437  -2125   -364   1382  A    O  
ATOM   2263  CB  LYS A 294      48.038 -17.180  16.609  1.00 72.26      A    C  
ANISOU 2263  CB  LYS A 294    11400   9058   6995  -2209   -629   1550  A    C  
ATOM   2264  CG  LYS A 294      48.517 -17.276  18.028  1.00 84.54      A    C  
ANISOU 2264  CG  LYS A 294    13173  10669   8278  -2311   -724   1700  A    C  
ATOM   2265  CD  LYS A 294      48.695 -15.954  18.734  1.00 92.95      A    C  
ANISOU 2265  CD  LYS A 294    14337  11878   9100  -2402   -702   1605  A    C  
ATOM   2266  CE  LYS A 294      49.027 -16.233  20.202  1.00105.25      A    C  
ANISOU 2266  CE  LYS A 294    16142  13484  10364  -2518   -790   1769  A    C  
ATOM   2267  NZ  LYS A 294      49.318 -15.017  20.982  1.00127.00      A    N1+
ANISOU 2267  NZ  LYS A 294    19035  16369  12850  -2620   -803   1681  A    N1+
ATOM   2268  N   LEU A 295      48.081 -18.744  13.554  1.00 82.31      A    N  
ANISOU 2268  N   LEU A 295    12282  10075   8914  -1898   -698   1451  A    N  
ATOM   2269  CA  LEU A 295      47.599 -18.895  12.186  1.00 78.60      A    C  
ANISOU 2269  CA  LEU A 295    11650   9540   8674  -1811   -634   1320  A    C  
ATOM   2270  C   LEU A 295      46.926 -20.256  11.959  1.00 85.70      A    C  
ANISOU 2270  C   LEU A 295    12598  10255   9708  -1831   -606   1390  A    C  
ATOM   2271  O   LEU A 295      45.843 -20.330  11.370  1.00 83.51      A    O  
ANISOU 2271  O   LEU A 295    12252   9939   9535  -1882   -472   1297  A    O  
ATOM   2272  CB  LEU A 295      48.734 -18.701  11.182  1.00 80.94      A    C  
ANISOU 2272  CB  LEU A 295    11796   9863   9094  -1635   -775   1264  A    C  
ATOM   2273  CG  LEU A 295      49.283 -17.262  11.051  1.00 77.79      A    C  
ANISOU 2273  CG  LEU A 295    11309   9633   8615  -1625   -785   1160  A    C  
ATOM   2274  CD1 LEU A 295      50.526 -17.268  10.187  1.00 83.88      A    C  
ANISOU 2274  CD1 LEU A 295    11933  10437   9501  -1462   -934   1153  A    C  
ATOM   2275  CD2 LEU A 295      48.242 -16.375  10.422  1.00 70.37      A    C  
ANISOU 2275  CD2 LEU A 295    10289   8732   7715  -1659   -606    988  A    C  
ATOM   2276  N   LEU A 296      47.544 -21.324  12.453  1.00 88.12      A    N  
ANISOU 2276  N   LEU A 296    13027  10446  10007  -1800   -737   1560  A    N  
ATOM   2277  CA  LEU A 296      46.968 -22.653  12.292  1.00 83.58      A    C  
ANISOU 2277  CA  LEU A 296    12536   9665   9556  -1832   -723   1638  A    C  
ATOM   2278  C   LEU A 296      45.971 -22.998  13.382  1.00 85.73      A    C  
ANISOU 2278  C   LEU A 296    12964   9908   9701  -2040   -597   1752  A    C  
ATOM   2279  O   LEU A 296      46.059 -24.055  14.002  1.00 99.15      A    O  
ANISOU 2279  O   LEU A 296    14829  11465  11379  -2081   -655   1929  A    O  
ATOM   2280  CB  LEU A 296      48.074 -23.722  12.189  1.00 76.77      A    C  
ANISOU 2280  CB  LEU A 296    11741   8655   8773  -1673   -915   1768  A    C  
ATOM   2281  CG  LEU A 296      48.987 -23.564  10.970  1.00 80.18      A    C  
ANISOU 2281  CG  LEU A 296    12005   9101   9357  -1452  -1014   1656  A    C  
ATOM   2282  CD1 LEU A 296      50.033 -24.649  10.922  1.00 83.20      A    C  
ANISOU 2282  CD1 LEU A 296    12453   9339   9818  -1272  -1183   1791  A    C  
ATOM   2283  CD2 LEU A 296      48.164 -23.501   9.680  1.00 70.85      A    C  
ANISOU 2283  CD2 LEU A 296    10704   7871   8345  -1442   -906   1464  A    C  
ATOM   2284  N   VAL A 297      45.020 -22.109  13.610  1.00 86.82      A    N  
ANISOU 2284  N   VAL A 297    13050  10181   9755  -2163   -416   1659  A    N  
ATOM   2285  CA  VAL A 297      43.963 -22.335  14.601  1.00 87.39      A    C  
ANISOU 2285  CA  VAL A 297    13241  10260   9703  -2363   -255   1754  A    C  
ATOM   2286  C   VAL A 297      42.758 -22.974  13.926  1.00 88.83      A    C  
ANISOU 2286  C   VAL A 297    13345  10339  10068  -2457   -134   1711  A    C  
ATOM   2287  O   VAL A 297      42.373 -22.570  12.827  1.00 91.76      A    O  
ANISOU 2287  O   VAL A 297    13534  10740  10591  -2401    -95   1542  A    O  
ATOM   2288  CB  VAL A 297      43.583 -21.015  15.311  1.00 80.33      A    C  
ANISOU 2288  CB  VAL A 297    12344   9576   8601  -2433   -109   1681  A    C  
ATOM   2289  CG1 VAL A 297      42.174 -21.061  15.866  1.00 74.23      A    C  
ANISOU 2289  CG1 VAL A 297    11593   8841   7767  -2612    127   1705  A    C  
ATOM   2290  CG2 VAL A 297      44.589 -20.695  16.396  1.00 74.90      A    C  
ANISOU 2290  CG2 VAL A 297    11818   8963   7676  -2426   -226   1786  A    C  
ATOM   2291  N   LEU A 298      42.158 -23.966  14.588  1.00 91.29      A    N  
ANISOU 2291  N   LEU A 298    13794  10533  10358  -2614    -81   1870  A    N  
ATOM   2292  CA  LEU A 298      41.053 -24.738  14.007  1.00 81.26      A    C  
ANISOU 2292  CA  LEU A 298    12464   9144   9266  -2740      8   1856  A    C  
ATOM   2293  C   LEU A 298      39.784 -23.921  13.768  1.00 87.14      A    C  
ANISOU 2293  C   LEU A 298    13020  10059  10028  -2843    221   1727  A    C  
ATOM   2294  O   LEU A 298      39.254 -23.888  12.656  1.00 88.55      A    O  
ANISOU 2294  O   LEU A 298    13024  10227  10392  -2825    235   1588  A    O  
ATOM   2295  CB  LEU A 298      40.734 -25.936  14.881  1.00 79.89      A    C  
ANISOU 2295  CB  LEU A 298    12496   8808   9048  -2908     21   2078  A    C  
ATOM   2296  CG  LEU A 298      41.742 -27.078  14.832  1.00 93.60      A    C  
ANISOU 2296  CG  LEU A 298    14410  10301  10850  -2806   -190   2209  A    C  
ATOM   2297  CD1 LEU A 298      41.531 -28.027  15.998  1.00122.14      A    C  
ANISOU 2297  CD1 LEU A 298    18267  13791  14349  -2970   -169   2462  A    C  
ATOM   2298  CD2 LEU A 298      41.679 -27.816  13.504  1.00 88.27      A    C  
ANISOU 2298  CD2 LEU A 298    13668   9428  10439  -2740   -275   2103  A    C  
ATOM   2299  N   ASP A 299      39.282 -23.271  14.807  1.00 89.90      A    N  
ANISOU 2299  N   ASP A 299    13406  10572  10180  -2942    390   1773  A    N  
ATOM   2300  CA  ASP A 299      38.098 -22.440  14.652  1.00 90.17      A    C  
ANISOU 2300  CA  ASP A 299    13255  10783  10222  -3007    607   1659  A    C  
ATOM   2301  C   ASP A 299      38.465 -21.163  13.891  1.00 89.38      A    C  
ANISOU 2301  C   ASP A 299    13002  10813  10145  -2823    586   1455  A    C  
ATOM   2302  O   ASP A 299      39.221 -20.317  14.392  1.00 88.81      A    O  
ANISOU 2302  O   ASP A 299    13008  10829   9904  -2732    557   1429  A    O  
ATOM   2303  CB  ASP A 299      37.506 -22.114  16.018  1.00 97.99      A    C  
ANISOU 2303  CB  ASP A 299    14348  11907  10976  -3143    810   1765  A    C  
ATOM   2304  CG  ASP A 299      36.215 -21.332  15.927  1.00109.00      A    C  
ANISOU 2304  CG  ASP A 299    15543  13487  12384  -3199   1060   1666  A    C  
ATOM   2305  OD1 ASP A 299      35.626 -21.275  14.820  1.00104.21      A    O  
ANISOU 2305  OD1 ASP A 299    14714  12889  11992  -3175   1067   1548  A    O  
ATOM   2306  OD2 ASP A 299      35.782 -20.812  16.983  1.00118.34      A    O1-
ANISOU 2306  OD2 ASP A 299    16797  14810  13355  -3263   1249   1713  A    O1-
ATOM   2307  N   PRO A 300      37.926 -21.015  12.675  1.00 89.03      A    N  
ANISOU 2307  N   PRO A 300    12746  10777  10301  -2778    594   1315  A    N  
ATOM   2308  CA  PRO A 300      38.187 -19.852  11.816  1.00 85.39      A    C  
ANISOU 2308  CA  PRO A 300    12135  10426   9883  -2607    576   1130  A    C  
ATOM   2309  C   PRO A 300      37.946 -18.546  12.558  1.00 82.33      A    C  
ANISOU 2309  C   PRO A 300    11751  10222   9307  -2583    740   1078  A    C  
ATOM   2310  O   PRO A 300      38.554 -17.535  12.228  1.00 88.39      A    O  
ANISOU 2310  O   PRO A 300    12492  11054  10037  -2444    696    965  A    O  
ATOM   2311  CB  PRO A 300      37.133 -20.002  10.709  1.00 77.27      A    C  
ANISOU 2311  CB  PRO A 300    10884   9411   9063  -2638    627   1032  A    C  
ATOM   2312  CG  PRO A 300      36.126 -20.952  11.264  1.00 80.50      A    C  
ANISOU 2312  CG  PRO A 300    11309   9779   9498  -2856    734   1163  A    C  
ATOM   2313  CD  PRO A 300      36.938 -21.914  12.064  1.00 81.57      A    C  
ANISOU 2313  CD  PRO A 300    11694   9749   9546  -2910    626   1328  A    C  
ATOM   2314  N   ALA A 301      37.069 -18.580  13.550  1.00 81.40      A    N  
ANISOU 2314  N   ALA A 301    11677  10182   9070  -2721    933   1163  A    N  
ATOM   2315  CA  ALA A 301      36.676 -17.386  14.275  1.00 79.31      A    C  
ANISOU 2315  CA  ALA A 301    11426  10084   8621  -2697   1124   1105  A    C  
ATOM   2316  C   ALA A 301      37.659 -17.056  15.384  1.00 82.61      A    C  
ANISOU 2316  C   ALA A 301    12095  10507   8783  -2689   1069   1164  A    C  
ATOM   2317  O   ALA A 301      37.655 -15.949  15.918  1.00 87.40      A    O  
ANISOU 2317  O   ALA A 301    12764  11226   9219  -2641   1178   1086  A    O  
ATOM   2318  CB  ALA A 301      35.276 -17.539  14.849  1.00 75.76      A    C  
ANISOU 2318  CB  ALA A 301    10900   9738   8146  -2837   1379   1166  A    C  
ATOM   2319  N   GLN A 302      38.485 -18.026  15.761  1.00 79.59      A    N  
ANISOU 2319  N   GLN A 302    11872  10000   8367  -2737    898   1305  A    N  
ATOM   2320  CA  GLN A 302      39.530 -17.781  16.750  1.00 85.59      A    C  
ANISOU 2320  CA  GLN A 302    12859  10770   8890  -2729    797   1374  A    C  
ATOM   2321  C   GLN A 302      40.895 -17.617  16.081  1.00 92.26      A    C  
ANISOU 2321  C   GLN A 302    13694  11555   9804  -2586    542   1323  A    C  
ATOM   2322  O   GLN A 302      41.881 -17.283  16.737  1.00 99.73      A    O  
ANISOU 2322  O   GLN A 302    14788  12529  10576  -2565    422   1360  A    O  
ATOM   2323  CB  GLN A 302      39.570 -18.885  17.790  1.00101.01      A    C  
ANISOU 2323  CB  GLN A 302    15009  12650  10720  -2871    780   1592  A    C  
ATOM   2324  CG  GLN A 302      38.320 -18.990  18.673  1.00113.16      A    C  
ANISOU 2324  CG  GLN A 302    16585  14274  12134  -3031   1049   1668  A    C  
ATOM   2325  CD  GLN A 302      38.453 -20.094  19.711  1.00121.15      A    C  
ANISOU 2325  CD  GLN A 302    17817  15204  13008  -3177   1020   1904  A    C  
ATOM   2326  NE2 GLN A 302      37.583 -21.116  19.640  1.00108.09      A    N  
ANISOU 2326  NE2 GLN A 302    16116  13473  11479  -3319   1110   2020  A    N  
ATOM   2327  OE1 GLN A 302      39.347 -20.034  20.562  1.00122.48      A    O  
ANISOU 2327  OE1 GLN A 302    18200  15377  12959  -3169    904   1988  A    O  
ATOM   2328  N   ARG A 303      40.935 -17.839  14.779  1.00 97.08      A    N  
ANISOU 2328  N   ARG A 303    14124  12100  10661  -2493    462   1239  A    N  
ATOM   2329  CA  ARG A 303      42.161 -17.715  13.989  1.00 76.40      A    C  
ANISOU 2329  CA  ARG A 303    11459   9436   8133  -2346    246   1186  A    C  
ATOM   2330  C   ARG A 303      42.546 -16.259  13.802  1.00 74.20      A    C  
ANISOU 2330  C   ARG A 303    11136   9279   7778  -2260    261   1038  A    C  
ATOM   2331  O   ARG A 303      41.714 -15.442  13.418  1.00 80.52      A    O  
ANISOU 2331  O   ARG A 303    11827  10153   8610  -2242    419    912  A    O  
ATOM   2332  CB  ARG A 303      41.973 -18.389  12.628  1.00 74.89      A    C  
ANISOU 2332  CB  ARG A 303    11102   9141   8211  -2277    184   1130  A    C  
ATOM   2333  CG  ARG A 303      43.249 -18.533  11.817  1.00 76.19      A    C  
ANISOU 2333  CG  ARG A 303    11227   9246   8476  -2120    -28   1103  A    C  
ATOM   2334  CD  ARG A 303      42.947 -19.293  10.536  1.00 71.19      A    C  
ANISOU 2334  CD  ARG A 303    10467   8498   8082  -2063    -68   1043  A    C  
ATOM   2335  NE  ARG A 303      42.239 -20.522  10.846  1.00 83.96      A    N  
ANISOU 2335  NE  ARG A 303    12163   9982   9755  -2191    -36   1155  A    N  
ATOM   2336  CZ  ARG A 303      41.297 -21.085  10.099  1.00 83.50      A    C  
ANISOU 2336  CZ  ARG A 303    12011   9854   9860  -2250     17   1106  A    C  
ATOM   2337  NH1 ARG A 303      40.944 -20.550   8.940  1.00 73.42      A    N1+
ANISOU 2337  NH1 ARG A 303    10554   8633   8706  -2176     37    945  A    N1+
ATOM   2338  NH2 ARG A 303      40.704 -22.195  10.516  1.00 96.56      A    N  
ANISOU 2338  NH2 ARG A 303    13760  11379  11548  -2398     43   1227  A    N  
ATOM   2339  N   ILE A 304      43.810 -15.939  14.046  1.00 72.73      A    N  
ANISOU 2339  N   ILE A 304    11025   9109   7498  -2208     90   1060  A    N  
ATOM   2340  CA  ILE A 304      44.316 -14.573  13.912  1.00 74.02      A    C  
ANISOU 2340  CA  ILE A 304    11171   9369   7582  -2152     78    931  A    C  
ATOM   2341  C   ILE A 304      44.058 -13.976  12.524  1.00 72.58      A    C  
ANISOU 2341  C   ILE A 304    10784   9195   7595  -2038    114    776  A    C  
ATOM   2342  O   ILE A 304      44.102 -14.695  11.532  1.00 74.72      A    O  
ANISOU 2342  O   ILE A 304    10927   9396   8066  -1967     46    775  A    O  
ATOM   2343  CB  ILE A 304      45.840 -14.522  14.226  1.00 78.14      A    C  
ANISOU 2343  CB  ILE A 304    11766   9906   8017  -2124   -154   1000  A    C  
ATOM   2344  CG1 ILE A 304      46.272 -13.097  14.572  1.00 77.84      A    C  
ANISOU 2344  CG1 ILE A 304    11790   9969   7817  -2144   -152    896  A    C  
ATOM   2345  CG2 ILE A 304      46.654 -15.105  13.082  1.00 73.32      A    C  
ANISOU 2345  CG2 ILE A 304    10998   9234   7623  -1992   -320   1009  A    C  
ATOM   2346  CD1 ILE A 304      47.703 -12.983  14.992  1.00 74.08      A    C  
ANISOU 2346  CD1 ILE A 304    11375   9534   7236  -2154   -382    969  A    C  
ATOM   2347  N   ASP A 305      43.829 -12.664  12.456  1.00 67.58      A    N  
ANISOU 2347  N   ASP A 305    10141   8639   6895  -2014    214    646  A    N  
ATOM   2348  CA  ASP A 305      43.683 -12.003  11.159  1.00 66.68      A    C  
ANISOU 2348  CA  ASP A 305     9851   8536   6947  -1899    233    513  A    C  
ATOM   2349  C   ASP A 305      44.966 -11.279  10.747  1.00 76.65      A    C  
ANISOU 2349  C   ASP A 305    11102   9820   8198  -1838     76    472  A    C  
ATOM   2350  O   ASP A 305      45.900 -11.145  11.546  1.00 72.93      A    O  
ANISOU 2350  O   ASP A 305    10758   9372   7580  -1895    -38    533  A    O  
ATOM   2351  CB  ASP A 305      42.487 -11.060  11.152  1.00 63.84      A    C  
ANISOU 2351  CB  ASP A 305     9460   8232   6563  -1889    455    402  A    C  
ATOM   2352  CG  ASP A 305      42.638  -9.888  12.105  1.00 74.02      A    C  
ANISOU 2352  CG  ASP A 305    10924   9570   7628  -1927    530    348  A    C  
ATOM   2353  OD1 ASP A 305      43.765  -9.607  12.569  1.00 94.34      A    O  
ANISOU 2353  OD1 ASP A 305    13621  12144  10080  -1964    384    374  A    O  
ATOM   2354  OD2 ASP A 305      41.652  -9.160  12.292  1.00 74.42      A    O1-
ANISOU 2354  OD2 ASP A 305    10981   9659   7634  -1907    730    268  A    O1-
ATOM   2355  N   SER A 306      45.007 -10.812   9.503  1.00 76.79      A    N  
ANISOU 2355  N   SER A 306    10967   9843   8368  -1731     68    375  A    N  
ATOM   2356  CA  SER A 306      46.217 -10.194   9.010  1.00 78.65      A    C  
ANISOU 2356  CA  SER A 306    11167  10105   8611  -1682    -70    350  A    C  
ATOM   2357  C   SER A 306      46.606  -8.963   9.828  1.00 69.63      A    C  
ANISOU 2357  C   SER A 306    10172   9006   7276  -1758    -58    308  A    C  
ATOM   2358  O   SER A 306      47.788  -8.694  10.066  1.00 67.86      A    O  
ANISOU 2358  O   SER A 306     9986   8813   6984  -1795   -212    346  A    O  
ATOM   2359  CB  SER A 306      46.102  -9.879   7.523  1.00 69.72      A    C  
ANISOU 2359  CB  SER A 306     9858   8974   7658  -1559    -59    259  A    C  
ATOM   2360  OG  SER A 306      44.813  -9.474   7.174  1.00 79.99      A    O  
ANISOU 2360  OG  SER A 306    11109  10276   9006  -1532    110    174  A    O  
ATOM   2361  N   ASP A 307      45.621  -8.227  10.294  1.00 70.33      A    N  
ANISOU 2361  N   ASP A 307    10349   9098   7272  -1786    121    231  A    N  
ATOM   2362  CA  ASP A 307      45.906  -7.005  11.047  1.00 72.56      A    C  
ANISOU 2362  CA  ASP A 307    10808   9397   7365  -1855    147    167  A    C  
ATOM   2363  C   ASP A 307      46.623  -7.317  12.355  1.00 69.54      A    C  
ANISOU 2363  C   ASP A 307    10607   9037   6775  -1986     37    259  A    C  
ATOM   2364  O   ASP A 307      47.641  -6.701  12.675  1.00 78.47      A    O  
ANISOU 2364  O   ASP A 307    11823  10190   7799  -2055    -98    256  A    O  
ATOM   2365  CB  ASP A 307      44.637  -6.203  11.311  1.00 78.50      A    C  
ANISOU 2365  CB  ASP A 307    11629  10140   8056  -1829    386     62  A    C  
ATOM   2366  CG  ASP A 307      44.919  -4.747  11.616  1.00 80.74      A    C  
ANISOU 2366  CG  ASP A 307    12073  10402   8201  -1851    419    -45  A    C  
ATOM   2367  OD1 ASP A 307      45.466  -4.031  10.740  1.00 86.99      A    O  
ANISOU 2367  OD1 ASP A 307    12799  11172   9082  -1805    349    -98  A    O  
ATOM   2368  OD2 ASP A 307      44.530  -4.289  12.704  1.00 79.50      A    O1-
ANISOU 2368  OD2 ASP A 307    12120  10242   7844  -1914    530    -82  A    O1-
ATOM   2369  N   ASP A 308      46.109  -8.275  13.103  1.00 69.45      A    N  
ANISOU 2369  N   ASP A 308    10656   9024   6704  -2032     84    351  A    N  
ATOM   2370  CA  ASP A 308      46.720  -8.657  14.371  1.00 73.98      A    C  
ANISOU 2370  CA  ASP A 308    11414   9625   7068  -2153    -22    458  A    C  
ATOM   2371  C   ASP A 308      48.051  -9.364  14.143  1.00 66.28      A    C  
ANISOU 2371  C   ASP A 308    10358   8664   6159  -2145   -281    577  A    C  
ATOM   2372  O   ASP A 308      48.979  -9.244  14.941  1.00 71.94      A    O  
ANISOU 2372  O   ASP A 308    11192   9427   6713  -2234   -438    641  A    O  
ATOM   2373  CB  ASP A 308      45.778  -9.581  15.164  1.00 83.92      A    C  
ANISOU 2373  CB  ASP A 308    12752  10875   8257  -2202    107    546  A    C  
ATOM   2374  CG  ASP A 308      44.565  -8.847  15.687  1.00 92.79      A    C  
ANISOU 2374  CG  ASP A 308    13979  12017   9260  -2220    368    446  A    C  
ATOM   2375  OD1 ASP A 308      44.736  -7.728  16.201  1.00 91.41      A    O  
ANISOU 2375  OD1 ASP A 308    13963  11859   8910  -2255    405    349  A    O  
ATOM   2376  OD2 ASP A 308      43.443  -9.402  15.640  1.00103.44      A    O1-
ANISOU 2376  OD2 ASP A 308    15257  13363  10680  -2205    540    469  A    O1-
ATOM   2377  N   ALA A 309      48.117 -10.104  13.047  1.00 67.15      A    N  
ANISOU 2377  N   ALA A 309    10268   8740   6506  -2033   -323    604  A    N  
ATOM   2378  CA  ALA A 309      49.299 -10.866  12.734  1.00 71.53      A    C  
ANISOU 2378  CA  ALA A 309    10725   9303   7148  -1985   -540    716  A    C  
ATOM   2379  C   ALA A 309      50.428  -9.888  12.489  1.00 76.97      A    C  
ANISOU 2379  C   ALA A 309    11372  10064   7807  -2001   -674    675  A    C  
ATOM   2380  O   ALA A 309      51.545 -10.096  12.951  1.00 72.98      A    O  
ANISOU 2380  O   ALA A 309    10876   9617   7234  -2040   -868    777  A    O  
ATOM   2381  CB  ALA A 309      49.069 -11.738  11.499  1.00 66.78      A    C  
ANISOU 2381  CB  ALA A 309     9934   8638   6801  -1847   -530    718  A    C  
ATOM   2382  N   LEU A 310      50.124  -8.806  11.766  1.00 77.67      A    N  
ANISOU 2382  N   LEU A 310    11410  10152   7948  -1975   -573    533  A    N  
ATOM   2383  CA  LEU A 310      51.165  -7.825  11.460  1.00 71.57      A    C  
ANISOU 2383  CA  LEU A 310    10596   9437   7159  -2011   -690    496  A    C  
ATOM   2384  C   LEU A 310      51.667  -7.166  12.734  1.00 78.79      A    C  
ANISOU 2384  C   LEU A 310    11718  10396   7823  -2180   -775    508  A    C  
ATOM   2385  O   LEU A 310      52.821  -6.739  12.811  1.00 97.30      A    O  
ANISOU 2385  O   LEU A 310    14033  12810  10125  -2252   -951    542  A    O  
ATOM   2386  CB  LEU A 310      50.648  -6.795  10.470  1.00 67.55      A    C  
ANISOU 2386  CB  LEU A 310    10023   8895   6744  -1954   -554    352  A    C  
ATOM   2387  CG  LEU A 310      50.604  -7.348   9.038  1.00 59.97      A    C  
ANISOU 2387  CG  LEU A 310     8834   7925   6025  -1796   -543    349  A    C  
ATOM   2388  CD1 LEU A 310      50.044  -6.290   8.105  1.00 59.80      A    C  
ANISOU 2388  CD1 LEU A 310     8767   7876   6077  -1740   -413    219  A    C  
ATOM   2389  CD2 LEU A 310      52.008  -7.767   8.631  1.00 59.09      A    C  
ANISOU 2389  CD2 LEU A 310     8577   7884   5988  -1765   -740    445  A    C  
ATOM   2390  N   ASN A 311      50.799  -7.121  13.738  1.00 75.79      A    N  
ANISOU 2390  N   ASN A 311    11544   9984   7269  -2249   -651    484  A    N  
ATOM   2391  CA  ASN A 311      51.134  -6.487  15.002  1.00 73.73      A    C  
ANISOU 2391  CA  ASN A 311    11523   9756   6735  -2412   -711    475  A    C  
ATOM   2392  C   ASN A 311      51.913  -7.399  15.942  1.00 74.26      A    C  
ANISOU 2392  C   ASN A 311    11647   9890   6678  -2484   -909    645  A    C  
ATOM   2393  O   ASN A 311      52.554  -6.942  16.891  1.00 80.13      A    O  
ANISOU 2393  O   ASN A 311    12554  10690   7201  -2629  -1041    663  A    O  
ATOM   2394  CB  ASN A 311      49.860  -6.004  15.706  1.00 80.10      A    C  
ANISOU 2394  CB  ASN A 311    12539  10509   7383  -2442   -471    372  A    C  
ATOM   2395  CG  ASN A 311      50.178  -5.085  16.866  1.00 89.49      A    C  
ANISOU 2395  CG  ASN A 311    14007  11715   8279  -2603   -510    313  A    C  
ATOM   2396  ND2 ASN A 311      49.587  -5.342  18.034  1.00103.92      A    N  
ANISOU 2396  ND2 ASN A 311    16050  13550   9883  -2669   -417    334  A    N  
ATOM   2397  OD1 ASN A 311      50.916  -4.117  16.697  1.00111.24      A    O  
ANISOU 2397  OD1 ASN A 311    16793  14471  11001  -2677   -614    242  A    O  
ATOM   2398  N   HIS A 312      51.861  -8.699  15.660  1.00 74.33      A    N  
ANISOU 2398  N   HIS A 312    11529   9884   6827  -2382   -940    771  A    N  
ATOM   2399  CA  HIS A 312      52.516  -9.726  16.463  1.00 78.10      A    C  
ANISOU 2399  CA  HIS A 312    12051  10405   7218  -2412  -1120    956  A    C  
ATOM   2400  C   HIS A 312      53.990  -9.435  16.727  1.00 84.76      A    C  
ANISOU 2400  C   HIS A 312    12851  11360   7991  -2482  -1392   1032  A    C  
ATOM   2401  O   HIS A 312      54.694  -8.908  15.860  1.00 89.71      A    O  
ANISOU 2401  O   HIS A 312    13299  12030   8756  -2449  -1467    987  A    O  
ATOM   2402  CB  HIS A 312      52.374 -11.090  15.780  1.00 84.51      A    C  
ANISOU 2402  CB  HIS A 312    12700  11154   8254  -2259  -1122   1063  A    C  
ATOM   2403  CG  HIS A 312      52.779 -12.240  16.648  1.00100.07      A    C  
ANISOU 2403  CG  HIS A 312    14754  13129  10138  -2270  -1264   1261  A    C  
ATOM   2404  CD2 HIS A 312      52.035 -13.151  17.326  1.00 90.28      A    C  
ANISOU 2404  CD2 HIS A 312    13652  11820   8828  -2291  -1183   1359  A    C  
ATOM   2405  ND1 HIS A 312      54.096 -12.571  16.878  1.00 93.30      A    N  
ANISOU 2405  ND1 HIS A 312    13830  12354   9264  -2257  -1522   1399  A    N  
ATOM   2406  CE1 HIS A 312      54.152 -13.610  17.681  1.00 93.78      A    C  
ANISOU 2406  CE1 HIS A 312    14000  12390   9240  -2257  -1602   1572  A    C  
ATOM   2407  NE2 HIS A 312      52.911 -13.994  17.957  1.00 89.56      A    N  
ANISOU 2407  NE2 HIS A 312    13598  11756   8672  -2284  -1396   1552  A    N  
ATOM   2408  N   ASP A 313      54.459  -9.795  17.922  1.00 87.43      A    N  
ANISOU 2408  N   ASP A 313    13343  11760   8114  -2584  -1545   1158  A    N  
ATOM   2409  CA  ASP A 313      55.817  -9.441  18.348  1.00 85.89      A    C  
ANISOU 2409  CA  ASP A 313    13121  11696   7815  -2685  -1820   1234  A    C  
ATOM   2410  C   ASP A 313      56.900  -9.993  17.418  1.00 83.96      A    C  
ANISOU 2410  C   ASP A 313    12568  11517   7815  -2550  -1992   1342  A    C  
ATOM   2411  O   ASP A 313      58.027  -9.480  17.379  1.00 88.05      A    O  
ANISOU 2411  O   ASP A 313    12975  12159   8321  -2620  -2191   1373  A    O  
ATOM   2412  CB  ASP A 313      56.056  -9.851  19.789  1.00 93.79      A    C  
ANISOU 2412  CB  ASP A 313    14343  12756   8534  -2804  -1960   1367  A    C  
ATOM   2413  CG  ASP A 313      55.390  -8.903  20.787  1.00103.94      A    C  
ANISOU 2413  CG  ASP A 313    15947  14028   9517  -2982  -1843   1236  A    C  
ATOM   2414  OD1 ASP A 313      55.156  -7.723  20.450  1.00116.39      A    O  
ANISOU 2414  OD1 ASP A 313    17563  15574  11083  -3042  -1739   1050  A    O  
ATOM   2415  OD2 ASP A 313      55.128  -9.331  21.927  1.00115.15      A    O1-
ANISOU 2415  OD2 ASP A 313    17591  15463  10697  -3057  -1857   1321  A    O1-
ATOM   2416  N   PHE A 314      56.550 -11.027  16.665  1.00 83.88      A    N  
ANISOU 2416  N   PHE A 314    12420  11425   8025  -2361  -1911   1394  A    N  
ATOM   2417  CA  PHE A 314      57.426 -11.585  15.648  1.00 87.74      A    C  
ANISOU 2417  CA  PHE A 314    12623  11953   8758  -2193  -2020   1470  A    C  
ATOM   2418  C   PHE A 314      57.985 -10.520  14.696  1.00 87.78      A    C  
ANISOU 2418  C   PHE A 314    12444  12031   8874  -2208  -2025   1356  A    C  
ATOM   2419  O   PHE A 314      59.124 -10.623  14.251  1.00 97.63      A    O  
ANISOU 2419  O   PHE A 314    13472  13394  10228  -2151  -2187   1441  A    O  
ATOM   2420  CB  PHE A 314      56.672 -12.687  14.873  1.00 83.80      A    C  
ANISOU 2420  CB  PHE A 314    12059  11311   8469  -2001  -1872   1481  A    C  
ATOM   2421  CG  PHE A 314      57.448 -13.274  13.715  1.00 92.19      A    C  
ANISOU 2421  CG  PHE A 314    12851  12391   9785  -1801  -1942   1528  A    C  
ATOM   2422  CD1 PHE A 314      58.552 -14.094  13.934  1.00101.83      A    C  
ANISOU 2422  CD1 PHE A 314    13962  13682  11044  -1700  -2153   1713  A    C  
ATOM   2423  CD2 PHE A 314      57.068 -13.011  12.408  1.00 94.84      A    C  
ANISOU 2423  CD2 PHE A 314    13044  12677  10313  -1699  -1792   1392  A    C  
ATOM   2424  CE1 PHE A 314      59.267 -14.621  12.884  1.00 99.50      A    C  
ANISOU 2424  CE1 PHE A 314    13422  13408  10973  -1495  -2196   1751  A    C  
ATOM   2425  CE2 PHE A 314      57.784 -13.531  11.342  1.00 94.12      A    C  
ANISOU 2425  CE2 PHE A 314    12720  12608  10431  -1509  -1840   1426  A    C  
ATOM   2426  CZ  PHE A 314      58.877 -14.341  11.580  1.00102.17      A    C  
ANISOU 2426  CZ  PHE A 314    13634  13696  11488  -1402  -2032   1601  A    C  
ATOM   2427  N   PHE A 315      57.184  -9.501  14.382  1.00 82.57      A    N  
ANISOU 2427  N   PHE A 315    11871  11308   8190  -2281  -1841   1175  A    N  
ATOM   2428  CA  PHE A 315      57.621  -8.464  13.456  1.00 86.63      A    C  
ANISOU 2428  CA  PHE A 315    12239  11868   8805  -2302  -1827   1071  A    C  
ATOM   2429  C   PHE A 315      58.227  -7.261  14.175  1.00 92.50      A    C  
ANISOU 2429  C   PHE A 315    13098  12695   9353  -2533  -1949   1031  A    C  
ATOM   2430  O   PHE A 315      58.688  -6.315  13.531  1.00 95.87      A    O  
ANISOU 2430  O   PHE A 315    13426  13158   9840  -2592  -1959    959  A    O  
ATOM   2431  CB  PHE A 315      56.467  -8.019  12.557  1.00 81.85      A    C  
ANISOU 2431  CB  PHE A 315    11647  11140   8310  -2228  -1572    905  A    C  
ATOM   2432  CG  PHE A 315      55.846  -9.133  11.789  1.00 73.58      A    C  
ANISOU 2432  CG  PHE A 315    10494  10010   7453  -2030  -1463    927  A    C  
ATOM   2433  CD1 PHE A 315      56.464  -9.635  10.659  1.00 70.90      A    C  
ANISOU 2433  CD1 PHE A 315     9910   9704   7326  -1869  -1505    966  A    C  
ATOM   2434  CD2 PHE A 315      54.625  -9.652  12.178  1.00 79.51      A    C  
ANISOU 2434  CD2 PHE A 315    11393  10651   8165  -2012  -1309    900  A    C  
ATOM   2435  CE1 PHE A 315      55.886 -10.679   9.937  1.00 74.76      A    C  
ANISOU 2435  CE1 PHE A 315    10328  10098   7979  -1694  -1412    970  A    C  
ATOM   2436  CE2 PHE A 315      54.017 -10.678  11.451  1.00 67.30      A    C  
ANISOU 2436  CE2 PHE A 315     9757   9017   6796  -1856  -1218    913  A    C  
ATOM   2437  CZ  PHE A 315      54.664 -11.195  10.342  1.00 68.55      A    C  
ANISOU 2437  CZ  PHE A 315     9698   9192   7156  -1700  -1278    943  A    C  
ATOM   2438  N   TRP A 316      58.254  -7.325  15.504  1.00 98.19      A    N  
ANISOU 2438  N   TRP A 316    14035  13441   9830  -2671  -2048   1083  A    N  
ATOM   2439  CA  TRP A 316      58.666  -6.163  16.283  1.00 94.41      A    C  
ANISOU 2439  CA  TRP A 316    13729  13014   9128  -2911  -2152   1016  A    C  
ATOM   2440  C   TRP A 316      59.733  -6.462  17.334  1.00 90.12      A    C  
ANISOU 2440  C   TRP A 316    13209  12621   8411  -3041  -2445   1173  A    C  
ATOM   2441  O   TRP A 316      59.922  -5.712  18.280  1.00105.85      A    O  
ANISOU 2441  O   TRP A 316    15417  14645  10154  -3256  -2542   1127  A    O  
ATOM   2442  CB  TRP A 316      57.422  -5.503  16.884  1.00 90.76      A    C  
ANISOU 2442  CB  TRP A 316    13584  12418   8482  -2988  -1938    854  A    C  
ATOM   2443  CG  TRP A 316      56.464  -5.054  15.797  1.00 87.68      A    C  
ANISOU 2443  CG  TRP A 316    13141  11902   8268  -2865  -1676    704  A    C  
ATOM   2444  CD1 TRP A 316      55.287  -5.649  15.438  1.00 83.27      A    C  
ANISOU 2444  CD1 TRP A 316    12583  11244   7809  -2707  -1455    671  A    C  
ATOM   2445  CD2 TRP A 316      56.627  -3.933  14.916  1.00 85.64      A    C  
ANISOU 2445  CD2 TRP A 316    12815  11614   8111  -2895  -1625    585  A    C  
ATOM   2446  CE2 TRP A 316      55.517  -3.913  14.060  1.00 80.99      A    C  
ANISOU 2446  CE2 TRP A 316    12189  10911   7672  -2735  -1376    486  A    C  
ATOM   2447  CE3 TRP A 316      57.600  -2.931  14.782  1.00 95.92      A    C  
ANISOU 2447  CE3 TRP A 316    14087  12972   9386  -3056  -1770    559  A    C  
ATOM   2448  NE1 TRP A 316      54.716  -4.972  14.404  1.00 79.05      A    N  
ANISOU 2448  NE1 TRP A 316    11978  10633   7425  -2629  -1282    538  A    N  
ATOM   2449  CZ2 TRP A 316      55.347  -2.929  13.070  1.00 84.33      A    C  
ANISOU 2449  CZ2 TRP A 316    12556  11271   8212  -2710  -1269    368  A    C  
ATOM   2450  CZ3 TRP A 316      57.422  -1.955  13.794  1.00 86.42      A    C  
ANISOU 2450  CZ3 TRP A 316    12836  11693   8305  -3044  -1650    441  A    C  
ATOM   2451  CH2 TRP A 316      56.304  -1.955  12.971  1.00 75.26      A    C  
ANISOU 2451  CH2 TRP A 316    11401  10163   7029  -2865  -1403    349  A    C  
ATOM   2452  N   SER A 317      60.462  -7.544  17.115  1.00 87.85      A    N  
ANISOU 2452  N   SER A 317    12694  12426   8259  -2901  -2592   1356  A    N  
ATOM   2453  CA  SER A 317      61.570  -7.922  17.969  1.00 95.34      A    C  
ANISOU 2453  CA  SER A 317    13600  13540   9083  -2985  -2892   1535  A    C  
ATOM   2454  C   SER A 317      62.793  -8.227  17.109  1.00 99.81      A    C  
ANISOU 2454  C   SER A 317    13784  14255   9882  -2876  -3051   1659  A    C  
ATOM   2455  O   SER A 317      62.677  -8.321  15.877  1.00 90.79      A    O  
ANISOU 2455  O   SER A 317    12439  13068   8986  -2713  -2907   1611  A    O  
ATOM   2456  CB  SER A 317      61.193  -9.117  18.845  1.00 97.05      A    C  
ANISOU 2456  CB  SER A 317    13961  13722   9190  -2901  -2920   1677  A    C  
ATOM   2457  OG  SER A 317      60.778 -10.222  18.067  1.00104.02      A    O  
ANISOU 2457  OG  SER A 317    14703  14508  10308  -2646  -2791   1735  A    O  
ATOM   2458  N   ASP A 318      63.957  -8.384  17.741  1.00106.63      A    N  
ANISOU 2458  N   ASP A 318    14543  15308  10663  -2960  -3345   1823  A    N  
ATOM   2459  CA  ASP A 318      65.195  -8.652  17.026  1.00105.73      A    C  
ANISOU 2459  CA  ASP A 318    14044  15372  10757  -2861  -3506   1959  A    C  
ATOM   2460  C   ASP A 318      65.272 -10.103  16.576  1.00102.05      A    C  
ANISOU 2460  C   ASP A 318    13404  14882  10487  -2542  -3485   2109  A    C  
ATOM   2461  O   ASP A 318      64.760 -10.985  17.253  1.00101.58      A    O  
ANISOU 2461  O   ASP A 318    13524  14731  10340  -2462  -3480   2186  A    O  
ATOM   2462  CB  ASP A 318      66.400  -8.328  17.906  1.00111.42      A    C  
ANISOU 2462  CB  ASP A 318    14695  16320  11317  -3064  -3842   2093  A    C  
ATOM   2463  CG  ASP A 318      66.588  -6.837  18.105  1.00126.54      A    C  
ANISOU 2463  CG  ASP A 318    16717  18271  13089  -3386  -3890   1946  A    C  
ATOM   2464  OD1 ASP A 318      66.002  -6.038  17.332  1.00125.27      A    O  
ANISOU 2464  OD1 ASP A 318    16603  17982  13011  -3415  -3669   1763  A    O  
ATOM   2465  OD2 ASP A 318      67.321  -6.480  19.035  1.00153.51      A    O1-
ANISOU 2465  OD2 ASP A 318    20181  21838  16307  -3609  -4157   2018  A    O1-
ATOM   2466  N   PRO A 319      65.910 -10.344  15.420  1.00104.52      A    N  
ANISOU 2466  N   PRO A 319    13381  15268  11063  -2361  -3462   2149  A    N  
ATOM   2467  CA  PRO A 319      66.374  -9.290  14.515  1.00104.83      A    C  
ANISOU 2467  CA  PRO A 319    13223  15394  11211  -2456  -3419   2051  A    C  
ATOM   2468  C   PRO A 319      65.193  -8.730  13.758  1.00 96.24      A    C  
ANISOU 2468  C   PRO A 319    12286  14104  10176  -2448  -3121   1831  A    C  
ATOM   2469  O   PRO A 319      64.371  -9.511  13.274  1.00102.51      A    O  
ANISOU 2469  O   PRO A 319    13127  14742  11078  -2238  -2939   1795  A    O  
ATOM   2470  CB  PRO A 319      67.268 -10.066  13.526  1.00107.06      A    C  
ANISOU 2470  CB  PRO A 319    13118  15799  11758  -2188  -3448   2183  A    C  
ATOM   2471  CG  PRO A 319      66.720 -11.439  13.534  1.00111.36      A    C  
ANISOU 2471  CG  PRO A 319    13738  16198  12375  -1916  -3372   2249  A    C  
ATOM   2472  CD  PRO A 319      66.349 -11.680  14.973  1.00107.95      A    C  
ANISOU 2472  CD  PRO A 319    13602  15720  11692  -2050  -3497   2312  A    C  
ATOM   2473  N   MET A 320      65.084  -7.412  13.648  1.00 94.28      A    N  
ANISOU 2473  N   MET A 320    12120  13848   9855  -2672  -3075   1690  A    N  
ATOM   2474  CA  MET A 320      63.981  -6.815  12.901  1.00 90.87      A    C  
ANISOU 2474  CA  MET A 320    11820  13229   9476  -2651  -2799   1491  A    C  
ATOM   2475  C   MET A 320      64.006  -7.266  11.444  1.00 87.88      A    C  
ANISOU 2475  C   MET A 320    11182  12839   9367  -2402  -2649   1486  A    C  
ATOM   2476  O   MET A 320      65.061  -7.649  10.933  1.00 94.05      A    O  
ANISOU 2476  O   MET A 320    11662  13783  10288  -2302  -2756   1612  A    O  
ATOM   2477  CB  MET A 320      64.032  -5.296  12.994  1.00 83.17      A    C  
ANISOU 2477  CB  MET A 320    10964  12247   8388  -2924  -2797   1360  A    C  
ATOM   2478  CG  MET A 320      63.714  -4.768  14.366  1.00 84.31      A    C  
ANISOU 2478  CG  MET A 320    11443  12347   8241  -3159  -2883   1307  A    C  
ATOM   2479  SD  MET A 320      61.955  -4.896  14.740  1.00 92.74      A    S  
ANISOU 2479  SD  MET A 320    12870  13165   9199  -3082  -2606   1149  A    S  
ATOM   2480  CE  MET A 320      61.285  -3.688  13.611  1.00 81.35      A    C  
ANISOU 2480  CE  MET A 320    11453  11582   7870  -3091  -2361    946  A    C  
ATOM   2481  N   PRO A 321      62.833  -7.231  10.772  1.00 82.67      A    N  
ANISOU 2481  N   PRO A 321    10638  11998   8775  -2297  -2400   1340  A    N  
ATOM   2482  CA  PRO A 321      62.705  -7.725   9.383  1.00 80.11      A    C  
ANISOU 2482  CA  PRO A 321    10111  11643   8681  -2055  -2248   1318  A    C  
ATOM   2483  C   PRO A 321      63.657  -6.980   8.453  1.00 80.74      A    C  
ANISOU 2483  C   PRO A 321     9935  11868   8872  -2092  -2272   1330  A    C  
ATOM   2484  O   PRO A 321      63.813  -5.777   8.604  1.00 90.68      A    O  
ANISOU 2484  O   PRO A 321    11260  13150  10045  -2318  -2294   1268  A    O  
ATOM   2485  CB  PRO A 321      61.257  -7.410   9.029  1.00 81.18      A    C  
ANISOU 2485  CB  PRO A 321    10455  11579   8811  -2032  -2009   1143  A    C  
ATOM   2486  CG  PRO A 321      60.544  -7.306  10.359  1.00 85.40      A    C  
ANISOU 2486  CG  PRO A 321    11289  12026   9129  -2178  -2023   1113  A    C  
ATOM   2487  CD  PRO A 321      61.549  -6.760  11.326  1.00 84.49      A    C  
ANISOU 2487  CD  PRO A 321    11193  12051   8854  -2394  -2251   1194  A    C  
ATOM   2488  N   SER A 322      64.285  -7.678   7.511  1.00 86.82      A    N  
ANISOU 2488  N   SER A 322    10429  12729   9827  -1877  -2259   1409  A    N  
ATOM   2489  CA  SER A 322      65.255  -7.034   6.627  1.00 91.42      A    C  
ANISOU 2489  CA  SER A 322    10743  13477  10513  -1907  -2271   1443  A    C  
ATOM   2490  C   SER A 322      64.965  -7.321   5.153  1.00 99.18      A    C  
ANISOU 2490  C   SER A 322    11595  14416  11670  -1676  -2068   1378  A    C  
ATOM   2491  O   SER A 322      64.289  -8.287   4.826  1.00 91.58      A    O  
ANISOU 2491  O   SER A 322    10689  13332  10775  -1459  -1967   1343  A    O  
ATOM   2492  CB  SER A 322      66.686  -7.449   6.980  1.00 89.17      A    C  
ANISOU 2492  CB  SER A 322    10182  13433  10263  -1899  -2493   1638  A    C  
ATOM   2493  OG  SER A 322      66.932  -8.836   6.687  1.00102.81      A    O  
ANISOU 2493  OG  SER A 322    11764  15180  12119  -1591  -2495   1737  A    O  
ATOM   2494  N   ASP A 323      65.578  -6.530   4.281  1.00100.96      A    N  
ANISOU 2494  N   ASP A 323    11636  14758  11965  -1731  -2024   1378  A    N  
ATOM   2495  CA  ASP A 323      65.515  -6.708   2.841  1.00106.41      A    C  
ANISOU 2495  CA  ASP A 323    12176  15453  12800  -1528  -1847   1335  A    C  
ATOM   2496  C   ASP A 323      66.055  -8.042   2.326  1.00101.02      A    C  
ANISOU 2496  C   ASP A 323    11280  14847  12253  -1222  -1845   1425  A    C  
ATOM   2497  O   ASP A 323      66.812  -8.737   3.014  1.00 97.16      A    O  
ANISOU 2497  O   ASP A 323    10677  14466  11772  -1169  -2006   1564  A    O  
ATOM   2498  CB  ASP A 323      66.265  -5.559   2.148  1.00122.34      A    C  
ANISOU 2498  CB  ASP A 323    14022  17613  14845  -1682  -1825   1356  A    C  
ATOM   2499  CG  ASP A 323      65.474  -4.274   2.145  1.00144.14      A    C  
ANISOU 2499  CG  ASP A 323    17024  20229  17513  -1898  -1740   1224  A    C  
ATOM   2500  OD1 ASP A 323      64.228  -4.344   2.010  1.00137.50      A    O  
ANISOU 2500  OD1 ASP A 323    16408  19187  16645  -1822  -1606   1092  A    O  
ATOM   2501  OD2 ASP A 323      66.096  -3.198   2.276  1.00146.90      A    O1-
ANISOU 2501  OD2 ASP A 323    17334  20662  17818  -2145  -1809   1256  A    O1-
ATOM   2502  N   LEU A 324      65.647  -8.395   1.105  1.00 92.89      A    N  
ANISOU 2502  N   LEU A 324    10213  13757  11324  -1012  -1663   1345  A    N  
ATOM   2503  CA  LEU A 324      66.014  -9.690   0.528  1.00 84.55      A    C  
ANISOU 2503  CA  LEU A 324     9007  12727  10389   -696  -1631   1396  A    C  
ATOM   2504  C   LEU A 324      67.275  -9.599  -0.322  1.00108.07      A    C  
ANISOU 2504  C   LEU A 324    11645  15946  13467   -595  -1613   1495  A    C  
ATOM   2505  O   LEU A 324      67.256  -9.626  -1.549  1.00104.06      A    O  
ANISOU 2505  O   LEU A 324    11050  15457  13028   -445  -1449   1436  A    O  
ATOM   2506  CB  LEU A 324      64.853 -10.304  -0.195  1.00 80.48      A    C  
ANISOU 2506  CB  LEU A 324     8666  12002   9911   -520  -1466   1251  A    C  
ATOM   2507  CG  LEU A 324      63.613 -10.411   0.697  1.00 87.46      A    C  
ANISOU 2507  CG  LEU A 324     9856  12672  10702   -630  -1478   1171  A    C  
ATOM   2508  CD1 LEU A 324      62.620 -11.423   0.140  1.00 88.33      A    C  
ANISOU 2508  CD1 LEU A 324    10100  12588  10872   -428  -1361   1070  A    C  
ATOM   2509  CD2 LEU A 324      63.959 -10.764   2.129  1.00 83.58      A    C  
ANISOU 2509  CD2 LEU A 324     9421  12200  10135   -724  -1665   1290  A    C  
ATOM   2510  N   LYS A 325      68.409  -9.466   0.355  1.00142.63      A    N  
ANISOU 2510  N   LYS A 325    15818  20530  17843   -688  -1786   1655  A    N  
ATOM   2511  CA  LYS A 325      69.611  -9.112  -0.393  1.00154.13      A    C  
ANISOU 2511  CA  LYS A 325    16927  22248  19384   -660  -1764   1758  A    C  
ATOM   2512  C   LYS A 325      70.364 -10.353  -0.831  1.00150.36      A    C  
ANISOU 2512  C   LYS A 325    16216  21879  19034   -309  -1748   1855  A    C  
ATOM   2513  O   LYS A 325      70.531 -11.311  -0.053  1.00139.97      A    O  
ANISOU 2513  O   LYS A 325    14915  20533  17732   -178  -1878   1938  A    O  
ATOM   2514  CB  LYS A 325      70.494  -8.146   0.404  1.00164.02      A    C  
ANISOU 2514  CB  LYS A 325    18042  23699  20578   -975  -1950   1879  A    C  
ATOM   2515  CG  LYS A 325      69.880  -6.786   0.627  1.00174.32      A    C  
ANISOU 2515  CG  LYS A 325    19567  24900  21766  -1312  -1936   1775  A    C  
ATOM   2516  CD  LYS A 325      70.844  -5.634   0.355  1.00179.36      A    C  
ANISOU 2516  CD  LYS A 325    19984  25753  22412  -1563  -1975   1858  A    C  
ATOM   2517  CE  LYS A 325      70.089  -4.321   0.113  1.00166.98      A    C  
ANISOU 2517  CE  LYS A 325    18659  24027  20758  -1817  -1878   1725  A    C  
ATOM   2518  NZ  LYS A 325      70.854  -3.362  -0.750  1.00164.94      A    N1+
ANISOU 2518  NZ  LYS A 325    18184  23935  20548  -1963  -1809   1786  A    N1+
ATOM   2519  N   GLY A 326      70.756 -10.353  -2.107  1.00156.61      A    N  
ANISOU 2519  N   GLY A 326    16817  22777  19910   -141  -1574   1839  A    N  
ATOM   2520  CA  GLY A 326      71.384 -11.499  -2.745  1.00155.00      A    C  
ANISOU 2520  CA  GLY A 326    16414  22655  19824    232  -1502   1897  A    C  
ATOM   2521  C   GLY A 326      70.323 -12.511  -3.084  1.00162.41      A    C  
ANISOU 2521  C   GLY A 326    17629  23307  20772    468  -1397   1750  A    C  
ATOM   2522  O   GLY A 326      69.108 -12.201  -3.032  1.00166.90      A    O  
ANISOU 2522  O   GLY A 326    18498  23651  21263    335  -1349   1602  A    O  
ATOM   2523  N   MET A 327      70.774 -13.724  -3.407  1.00163.67      A    N  
ANISOU 2523  N   MET A 327    17689  23470  21028    817  -1364   1793  A    N  
ATOM   2524  CA  MET A 327      69.867 -14.815  -3.747  1.00158.41      A    C  
ANISOU 2524  CA  MET A 327    17283  22523  20381   1052  -1275   1661  A    C  
ATOM   2525  C   MET A 327      69.030 -14.379  -4.930  1.00148.92      A    C  
ANISOU 2525  C   MET A 327    16218  21220  19142   1039  -1072   1473  A    C  
ATOM   2526  O   MET A 327      68.889 -15.124  -5.888  1.00139.45      A    O  
ANISOU 2526  O   MET A 327    15054  19942  17985   1307   -931   1381  A    O  
ATOM   2527  CB  MET A 327      68.922 -15.130  -2.581  1.00150.72      A    C  
ANISOU 2527  CB  MET A 327    16614  21310  19342    913  -1410   1636  A    C  
ATOM   2528  CG  MET A 327      69.396 -14.591  -1.238  1.00123.20      A    C  
ANISOU 2528  CG  MET A 327    13066  17949  15794    662  -1629   1786  A    C  
ATOM   2529  SD  MET A 327      67.997 -14.227  -0.141  1.00134.51      A    S  
ANISOU 2529  SD  MET A 327    14891  19131  17085    364  -1705   1692  A    S  
ATOM   2530  CE  MET A 327      66.756 -15.449  -0.608  1.00 97.42      A    C  
ANISOU 2530  CE  MET A 327    10489  14099  12427    588  -1575   1542  A    C  
TER   
CONECT 1364 1374 1374
CONECT 1374 1364 1364 1375
CONECT 1375 1374 1376 1378
CONECT 1376 1375 1377 1385
CONECT 1377 1376
CONECT 1378 1375 1379 1380
CONECT 1379 1378
CONECT 1380 1378 1381
CONECT 1381 1380 1382 1383 1384
CONECT 1382 1381
CONECT 1383 1381
CONECT 1384 1381
CONECT 1385 1376
END



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