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***  3BLH_A_VS_3MY1_A  ***

elNémo ID: 22051216131673072

Job options:

ID        	=	 22051216131673072
JOBID     	=	 3BLH_A_VS_3MY1_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_3MY1_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  173.789  173.789   99.221  90.00  90.00 120.00 H 3           9
ATOM      1  N   ASP A   6      37.101  -7.026 -44.024  1.00160.02      A    N  
ANISOU    1  N   ASP A   6    20300  24161  16340   -292   -219  -1279  A    N  
ATOM      2  CA  ASP A   6      37.871  -5.861 -43.587  1.00162.47      A    C  
ANISOU    2  CA  ASP A   6    20616  24452  16663   -277   -103  -1089  A    C  
ATOM      3  C   ASP A   6      38.163  -5.852 -42.080  1.00157.43      A    C  
ANISOU    3  C   ASP A   6    19893  23595  16328   -214    -61  -1036  A    C  
ATOM      4  O   ASP A   6      38.091  -6.892 -41.418  1.00156.50      A    O  
ANISOU    4  O   ASP A   6    19715  23344  16403   -175    -82  -1178  A    O  
ATOM      5  CB  ASP A   6      37.223  -4.538 -44.046  1.00167.11      A    C  
ANISOU    5  CB  ASP A   6    21266  25139  17089   -304   -173   -832  A    C  
ATOM      6  CG  ASP A   6      35.724  -4.467 -43.759  1.00170.32      A    C  
ANISOU    6  CG  ASP A   6    21649  25485  17579   -291   -372   -724  A    C  
ATOM      7  OD1 ASP A   6      35.174  -5.401 -43.136  1.00173.13      A    O  
ANISOU    7  OD1 ASP A   6    21943  25713  18126   -266   -450   -843  A    O  
ATOM      8  OD2 ASP A   6      35.093  -3.464 -44.165  1.00168.42      A    O1-
ANISOU    8  OD2 ASP A   6    21452  25322  17219   -305   -446   -515  A    O1-
ATOM      9  N   SER A   7      38.484  -4.672 -41.551  1.00150.45      A    N  
ANISOU    9  N   SER A   7    19007  22678  15480   -207      3   -830  A    N  
ATOM     10  CA  SER A   7      39.068  -4.550 -40.213  1.00143.16      A    C  
ANISOU   10  CA  SER A   7    18010  21585  14799   -162     79   -789  A    C  
ATOM     11  C   SER A   7      38.234  -3.663 -39.277  1.00138.59      A    C  
ANISOU   11  C   SER A   7    17412  20882  14363   -152      7   -563  A    C  
ATOM     12  O   SER A   7      37.574  -2.722 -39.725  1.00142.94      A    O  
ANISOU   12  O   SER A   7    18010  21499  14803   -180    -45   -388  A    O  
ATOM     13  CB  SER A   7      40.497  -3.996 -40.335  1.00137.60      A    C  
ANISOU   13  CB  SER A   7    17305  20946  14030   -173    266   -790  A    C  
ATOM     14  OG  SER A   7      41.337  -4.451 -39.288  1.00131.91      A    O  
ANISOU   14  OG  SER A   7    16499  20099  13520   -126    344   -870  A    O  
ATOM     15  N   VAL A   8      38.271  -3.964 -37.980  1.00126.82      A    N  
ANISOU   15  N   VAL A   8    15855  19212  13120   -112      8   -565  A    N  
ATOM     16  CA  VAL A   8      37.551  -3.163 -36.985  1.00117.60      A    C  
ANISOU   16  CA  VAL A   8    14666  17912  12106   -110    -38   -369  A    C  
ATOM     17  C   VAL A   8      38.509  -2.332 -36.126  1.00109.44      A    C  
ANISOU   17  C   VAL A   8    13600  16823  11160   -111     99   -271  A    C  
ATOM     18  O   VAL A   8      39.556  -2.827 -35.694  1.00101.05      A    O  
ANISOU   18  O   VAL A   8    12493  15737  10165    -86    188   -388  A    O  
ATOM     19  CB  VAL A   8      36.701  -4.044 -36.038  1.00107.56      A    C  
ANISOU   19  CB  VAL A   8    13350  16463  11056    -77   -146   -426  A    C  
ATOM     20  CG1 VAL A   8      35.866  -3.170 -35.122  1.00 99.18      A    C  
ANISOU   20  CG1 VAL A   8    12274  15273  10138    -87   -189   -226  A    C  
ATOM     21  CG2 VAL A   8      35.820  -4.988 -36.829  1.00104.02      A    C  
ANISOU   21  CG2 VAL A   8    12920  16061  10542    -80   -271   -557  A    C  
ATOM     22  N   GLU A   9      38.143  -1.075 -35.875  1.00106.21      A    N  
ANISOU   22  N   GLU A   9    13205  16393  10757   -141    116    -62  A    N  
ATOM     23  CA  GLU A   9      38.954  -0.188 -35.039  1.00104.90      A    C  
ANISOU   23  CA  GLU A   9    13006  16173  10677   -156    249     35  A    C  
ATOM     24  C   GLU A   9      39.141  -0.804 -33.657  1.00 92.66      A    C  
ANISOU   24  C   GLU A   9    11388  14463   9357   -125    243    -28  A    C  
ATOM     25  O   GLU A   9      38.208  -1.410 -33.108  1.00 82.93      A    O  
ANISOU   25  O   GLU A   9    10144  13110   8254   -104    130    -42  A    O  
ATOM     26  CB  GLU A   9      38.297   1.196 -34.890  1.00114.47      A    C  
ANISOU   26  CB  GLU A   9    14242  17353  11898   -194    259    272  A    C  
ATOM     27  CG  GLU A   9      38.128   1.995 -36.183  1.00127.03      A    C  
ANISOU   27  CG  GLU A   9    15906  19096  13263   -222    273    380  A    C  
ATOM     28  CD  GLU A   9      39.399   2.708 -36.612  1.00137.19      A    C  
ANISOU   28  CD  GLU A   9    17213  20488  14424   -253    453    393  A    C  
ATOM     29  OE1 GLU A   9      40.154   3.156 -35.723  1.00139.01      A    O  
ANISOU   29  OE1 GLU A   9    17395  20647  14775   -268    572    410  A    O  
ATOM     30  OE2 GLU A   9      39.639   2.826 -37.838  1.00139.77      A    O1-
ANISOU   30  OE2 GLU A   9    17606  20971  14528   -269    479    381  A    O1-
ATOM     31  N   CYS A  10      40.333  -0.650 -33.084  1.00 86.91      A    N  
ANISOU   31  N   CYS A  10    10613  13731   8677   -124    364    -64  A    N  
ATOM     32  CA  CYS A  10      40.561  -1.205 -31.758  1.00 83.38      A    C  
ANISOU   32  CA  CYS A  10    10105  13144   8432    -93    353   -112  A    C  
ATOM     33  C   CYS A  10      41.618  -0.478 -30.948  1.00 91.36      A    C  
ANISOU   33  C   CYS A  10    11064  14146   9504   -116    479    -67  A    C  
ATOM     34  O   CYS A  10      42.689  -1.009 -30.676  1.00113.15      A    O  
ANISOU   34  O   CYS A  10    13767  16928  12296    -85    534   -185  A    O  
ATOM     35  CB  CYS A  10      40.852  -2.707 -31.830  1.00 73.95      A    C  
ANISOU   35  CB  CYS A  10     8886  11934   7278    -30    304   -312  A    C  
ATOM     36  SG  CYS A  10      40.482  -3.521 -30.288  1.00107.34      A    S  
ANISOU   36  SG  CYS A  10    13073  15959  11753     14    229   -332  A    S  
ATOM     37  N   PRO A  11      41.290   0.733 -30.524  1.00 83.67      A    N  
ANISOU   37  N   PRO A  11    10099  13133   8558   -172    525    102  A    N  
ATOM     38  CA  PRO A  11      42.146   1.678 -29.820  1.00 82.52      A    C  
ANISOU   38  CA  PRO A  11     9910  12986   8458   -218    655    165  A    C  
ATOM     39  C   PRO A  11      42.680   1.125 -28.511  1.00 82.51      A    C  
ANISOU   39  C   PRO A  11     9839  12895   8617   -195    648     97  A    C  
ATOM     40  O   PRO A  11      43.789   1.475 -28.122  1.00 78.04      A    O  
ANISOU   40  O   PRO A  11     9215  12375   8062   -213    751     67  A    O  
ATOM     41  CB  PRO A  11      41.190   2.831 -29.502  1.00 89.12      A    C  
ANISOU   41  CB  PRO A  11    10779  13743   9340   -276    662    359  A    C  
ATOM     42  CG  PRO A  11      40.076   2.679 -30.442  1.00 93.05      A    C  
ANISOU   42  CG  PRO A  11    11340  14261   9754   -259    556    404  A    C  
ATOM     43  CD  PRO A  11      39.908   1.216 -30.606  1.00 88.15      A    C  
ANISOU   43  CD  PRO A  11    10715  13635   9145   -195    441    242  A    C  
ATOM     44  N   PHE A  12      41.906   0.295 -27.821  1.00 78.91      A    N  
ANISOU   44  N   PHE A  12     9387  12313   8281   -159    530     76  A    N  
ATOM     45  CA  PHE A  12      42.274  -0.056 -26.453  1.00 65.67      A    C  
ANISOU   45  CA  PHE A  12     7659  10538   6754   -147    522     53  A    C  
ATOM     46  C   PHE A  12      42.595  -1.515 -26.230  1.00 63.75      A    C  
ANISOU   46  C   PHE A  12     7389  10262   6572    -61    446    -94  A    C  
ATOM     47  O   PHE A  12      42.594  -1.993 -25.102  1.00 65.57      A    O  
ANISOU   47  O   PHE A  12     7596  10387   6930    -40    404    -99  A    O  
ATOM     48  CB  PHE A  12      41.201   0.386 -25.481  1.00 70.25      A    C  
ANISOU   48  CB  PHE A  12     8265  10969   7455   -193    479    178  A    C  
ATOM     49  CG  PHE A  12      40.746   1.786 -25.699  1.00 82.32      A    C  
ANISOU   49  CG  PHE A  12     9821  12506   8950   -272    552    330  A    C  
ATOM     50  CD1 PHE A  12      41.658   2.786 -25.938  1.00 81.30      A    C  
ANISOU   50  CD1 PHE A  12     9667  12477   8747   -321    688    365  A    C  
ATOM     51  CD2 PHE A  12      39.401   2.109 -25.654  1.00 86.99      A    C  
ANISOU   51  CD2 PHE A  12    10458  12998   9598   -296    492    438  A    C  
ATOM     52  CE1 PHE A  12      41.237   4.084 -26.136  1.00 80.71      A    C  
ANISOU   52  CE1 PHE A  12     9619  12395   8653   -391    768    512  A    C  
ATOM     53  CE2 PHE A  12      38.978   3.407 -25.848  1.00 85.06      A    C  
ANISOU   53  CE2 PHE A  12    10232  12748   9339   -361    564    588  A    C  
ATOM     54  CZ  PHE A  12      39.896   4.392 -26.091  1.00 82.83      A    C  
ANISOU   54  CZ  PHE A  12     9932  12559   8981   -407    705    628  A    C  
ATOM     55  N   CYS A  13      42.887  -2.234 -27.299  1.00 70.62      A    N  
ANISOU   55  N   CYS A  13     8263  11219   7350    -13    437   -213  A    N  
ATOM     56  CA  CYS A  13      43.354  -3.604 -27.137  1.00 66.38      A    C  
ANISOU   56  CA  CYS A  13     7690  10650   6879     73    391   -363  A    C  
ATOM     57  C   CYS A  13      44.431  -3.847 -28.164  1.00 67.50      A    C  
ANISOU   57  C   CYS A  13     7798  10939   6911     99    470   -489  A    C  
ATOM     58  O   CYS A  13      44.134  -4.015 -29.349  1.00 72.02      A    O  
ANISOU   58  O   CYS A  13     8416  11587   7360     94    467   -542  A    O  
ATOM     59  CB  CYS A  13      42.205  -4.569 -27.337  1.00 64.40      A    C  
ANISOU   59  CB  CYS A  13     7492  10304   6673    108    276   -406  A    C  
ATOM     60  SG  CYS A  13      42.557  -6.237 -26.917  1.00 73.13      A    S  
ANISOU   60  SG  CYS A  13     8564  11320   7903    211    223   -562  A    S  
ATOM     61  N   ASP A  14      45.685  -3.824 -27.716  1.00 62.48      A    N  
ANISOU   61  N   ASP A  14     7079  10346   6313    120    542   -538  A    N  
ATOM     62  CA  ASP A  14      46.818  -3.989 -28.626  1.00 59.50      A    C  
ANISOU   62  CA  ASP A  14     6656  10104   5849    139    638   -664  A    C  
ATOM     63  C   ASP A  14      47.017  -5.465 -28.972  1.00 65.46      A    C  
ANISOU   63  C   ASP A  14     7390  10831   6652    229    595   -831  A    C  
ATOM     64  O   ASP A  14      46.669  -6.347 -28.162  1.00 65.72      A    O  
ANISOU   64  O   ASP A  14     7412  10735   6823    291    506   -847  A    O  
ATOM     65  CB  ASP A  14      48.075  -3.396 -28.012  1.00 66.60      A    C  
ANISOU   65  CB  ASP A  14     7459  11061   6786    125    733   -662  A    C  
ATOM     66  CG  ASP A  14      48.043  -1.881 -27.970  1.00 86.64      A    C  
ANISOU   66  CG  ASP A  14    10016  13650   9252     24    819   -526  A    C  
ATOM     67  OD1 ASP A  14      47.148  -1.287 -28.626  1.00 92.91      A    O  
ANISOU   67  OD1 ASP A  14    10900  14454   9949    -27    816   -437  A    O  
ATOM     68  OD2 ASP A  14      48.917  -1.289 -27.283  1.00 87.51      A    O1-
ANISOU   68  OD2 ASP A  14    10049  13792   9409     -5    891   -510  A    O1-
ATOM     69  N   GLU A  15      47.534  -5.733 -30.177  1.00 67.79      A    N  
ANISOU   69  N   GLU A  15     7684  11238   6834    233    665   -955  A    N  
ATOM     70  CA  GLU A  15      47.854  -7.110 -30.580  1.00 79.58      A    C  
ANISOU   70  CA  GLU A  15     9148  12709   8378    313    653  -1133  A    C  
ATOM     71  C   GLU A  15      49.091  -7.596 -29.813  1.00 75.13      A    C  
ANISOU   71  C   GLU A  15     8464  12124   7958    388    691  -1203  A    C  
ATOM     72  O   GLU A  15      50.077  -6.864 -29.699  1.00 71.42      A    O  
ANISOU   72  O   GLU A  15     7925  11742   7468    363    782  -1190  A    O  
ATOM     73  CB  GLU A  15      48.087  -7.229 -32.096  1.00 84.64      A    C  
ANISOU   73  CB  GLU A  15     9825  13482   8850    284    731  -1256  A    C  
ATOM     74  CG  GLU A  15      47.372  -6.179 -32.951  1.00 95.31      A    C  
ANISOU   74  CG  GLU A  15    11276  14930  10007    190    742  -1151  A    C  
ATOM     75  CD  GLU A  15      47.439  -6.479 -34.454  1.00108.97      A    C  
ANISOU   75  CD  GLU A  15    13061  16787  11557    162    797  -1278  A    C  
ATOM     76  OE1 GLU A  15      48.516  -6.309 -35.062  1.00110.03      A    O  
ANISOU   76  OE1 GLU A  15    13161  17029  11617    147    928  -1366  A    O  
ATOM     77  OE2 GLU A  15      46.404  -6.874 -35.037  1.00118.12      A    O1-
ANISOU   77  OE2 GLU A  15    14296  17941  12643    147    710  -1294  A    O1-
ATOM     78  N   VAL A  16      49.016  -8.815 -29.277  1.00 66.69      A    N  
ANISOU   78  N   VAL A  16     7366  10935   7039    480    621  -1273  A    N  
ATOM     79  CA  VAL A  16      50.072  -9.374 -28.438  1.00 67.54      A    C  
ANISOU   79  CA  VAL A  16     7357  11003   7301    568    629  -1319  A    C  
ATOM     80  C   VAL A  16      51.401  -9.527 -29.197  1.00 72.18      A    C  
ANISOU   80  C   VAL A  16     7851  11708   7865    593    753  -1467  A    C  
ATOM     81  O   VAL A  16      52.468  -9.678 -28.597  1.00 68.84      A    O  
ANISOU   81  O   VAL A  16     7310  11294   7551    651    779  -1496  A    O  
ATOM     82  CB  VAL A  16      49.687 -10.754 -27.888  1.00 62.26      A    C  
ANISOU   82  CB  VAL A  16     6688  10174   6792    670    540  -1370  A    C  
ATOM     83  CG1 VAL A  16      49.829 -11.799 -28.980  1.00 58.96      A    C  
ANISOU   83  CG1 VAL A  16     6270   9764   6369    713    589  -1557  A    C  
ATOM     84  CG2 VAL A  16      50.580 -11.131 -26.725  1.00 60.65      A    C  
ANISOU   84  CG2 VAL A  16     6377   9916   6751    758    515  -1349  A    C  
ATOM     85  N   SER A  17      51.340  -9.494 -30.518  1.00 70.82      A    N  
ANISOU   85  N   SER A  17     7729  11629   7552    546    830  -1563  A    N  
ATOM     86  CA  SER A  17      52.559  -9.528 -31.308  1.00 73.27      A    C  
ANISOU   86  CA  SER A  17     7961  12054   7826    551    968  -1705  A    C  
ATOM     87  C   SER A  17      53.528  -8.381 -30.947  1.00 70.86      A    C  
ANISOU   87  C   SER A  17     7576  11848   7500    505   1051  -1640  A    C  
ATOM     88  O   SER A  17      54.667  -8.372 -31.392  1.00 74.35      A    O  
ANISOU   88  O   SER A  17     7928  12377   7945    513   1169  -1754  A    O  
ATOM     89  CB  SER A  17      52.208  -9.466 -32.792  1.00 86.24      A    C  
ANISOU   89  CB  SER A  17     9696  13793   9277    481   1038  -1794  A    C  
ATOM     90  OG  SER A  17      51.589  -8.226 -33.123  1.00 94.38      A    O  
ANISOU   90  OG  SER A  17    10822  14903  10136    376   1042  -1654  A    O  
ATOM     91  N   LYS A  18      53.098  -7.411 -30.148  1.00 62.94      A    N  
ANISOU   91  N   LYS A  18     6600  10833   6483    451   1002  -1469  A    N  
ATOM     92  CA  LYS A  18      54.010  -6.334 -29.778  1.00 70.51      A    C  
ANISOU   92  CA  LYS A  18     7479  11882   7430    400   1089  -1420  A    C  
ATOM     93  C   LYS A  18      55.055  -6.843 -28.800  1.00 72.65      A    C  
ANISOU   93  C   LYS A  18     7596  12127   7880    488   1069  -1469  A    C  
ATOM     94  O   LYS A  18      56.079  -6.191 -28.579  1.00 64.95      A    O  
ANISOU   94  O   LYS A  18     6517  11240   6920    461   1152  -1483  A    O  
ATOM     95  CB  LYS A  18      53.269  -5.143 -29.176  1.00 65.16      A    C  
ANISOU   95  CB  LYS A  18     6869  11191   6698    311   1055  -1231  A    C  
ATOM     96  CG  LYS A  18      52.740  -5.389 -27.793  1.00 70.45      A    C  
ANISOU   96  CG  LYS A  18     7531  11735   7501    349    921  -1127  A    C  
ATOM     97  CD  LYS A  18      51.731  -4.324 -27.440  1.00 69.87      A    C  
ANISOU   97  CD  LYS A  18     7553  11632   7364    255    893   -955  A    C  
ATOM     98  CE  LYS A  18      52.171  -3.477 -26.284  1.00 63.86      A    C  
ANISOU   98  CE  LYS A  18     6726  10875   6663    210    906   -862  A    C  
ATOM     99  NZ  LYS A  18      51.012  -2.677 -25.862  1.00 74.28      A    N1+
ANISOU   99  NZ  LYS A  18     8144  12125   7953    132    866   -703  A    N1+
ATOM    100  N   TYR A  19      54.758  -8.000 -28.209  1.00 72.58      A    N  
ANISOU  100  N   TYR A  19     7575  11995   8009    591    956  -1488  A    N  
ATOM    101  CA  TYR A  19      55.668  -8.720 -27.335  1.00 71.62      A    C  
ANISOU  101  CA  TYR A  19     7313  11834   8065    699    915  -1533  A    C  
ATOM    102  C   TYR A  19      56.235  -9.909 -28.097  1.00 85.17      A    C  
ANISOU  102  C   TYR A  19     8972  13535   9856    792    966  -1714  A    C  
ATOM    103  O   TYR A  19      55.559 -10.472 -28.951  1.00 92.62      A    O  
ANISOU  103  O   TYR A  19    10007  14441  10742    789    976  -1782  A    O  
ATOM    104  CB  TYR A  19      54.927  -9.212 -26.099  1.00 71.23      A    C  
ANISOU  104  CB  TYR A  19     7298  11642   8125    755    760  -1415  A    C  
ATOM    105  CG  TYR A  19      54.354  -8.092 -25.261  1.00 76.54      A    C  
ANISOU  105  CG  TYR A  19     8025  12316   8741    661    715  -1244  A    C  
ATOM    106  CD1 TYR A  19      55.170  -7.372 -24.394  1.00 72.13      A    C  
ANISOU  106  CD1 TYR A  19     7365  11826   8216    636    725  -1193  A    C  
ATOM    107  CD2 TYR A  19      53.001  -7.744 -25.335  1.00 74.10      A    C  
ANISOU  107  CD2 TYR A  19     7861  11941   8352    592    668  -1143  A    C  
ATOM    108  CE1 TYR A  19      54.667  -6.345 -23.625  1.00 69.60      A    C  
ANISOU  108  CE1 TYR A  19     7092  11504   7849    540    699  -1050  A    C  
ATOM    109  CE2 TYR A  19      52.488  -6.704 -24.564  1.00 71.52      A    C  
ANISOU  109  CE2 TYR A  19     7579  11606   7990    503    642   -992  A    C  
ATOM    110  CZ  TYR A  19      53.334  -6.014 -23.714  1.00 75.18      A    C  
ANISOU  110  CZ  TYR A  19     7945  12134   8486    475    664   -950  A    C  
ATOM    111  OH  TYR A  19      52.877  -4.982 -22.944  1.00 78.33      A    O  
ANISOU  111  OH  TYR A  19     8382  12524   8855    378    654   -815  A    O  
ATOM    112  N   GLU A  20      57.476 -10.278 -27.791  1.00 88.67      A    N  
ANISOU  112  N   GLU A  20     9254  14007  10429    872   1001  -1797  A    N  
ATOM    113  CA  GLU A  20      58.157 -11.400 -28.433  1.00 87.27      A    C  
ANISOU  113  CA  GLU A  20     8996  13807  10355    967   1065  -1975  A    C  
ATOM    114  C   GLU A  20      58.233 -12.543 -27.433  1.00 78.98      A    C  
ANISOU  114  C   GLU A  20     7879  12616   9513   1113    945  -1954  A    C  
ATOM    115  O   GLU A  20      58.889 -12.416 -26.399  1.00 80.47      A    O  
ANISOU  115  O   GLU A  20     7955  12813   9806   1167    884  -1887  A    O  
ATOM    116  CB  GLU A  20      59.568 -10.961 -28.831  1.00100.32      A    C  
ANISOU  116  CB  GLU A  20    10500  15593  12024    955   1202  -2086  A    C  
ATOM    117  CG  GLU A  20      60.331 -11.891 -29.766  1.00112.73      A    C  
ANISOU  117  CG  GLU A  20    11991  17166  13673   1021   1317  -2293  A    C  
ATOM    118  CD  GLU A  20      61.647 -11.278 -30.258  1.00128.46      A    C  
ANISOU  118  CD  GLU A  20    13849  19300  15658    981   1475  -2404  A    C  
ATOM    119  OE1 GLU A  20      61.929 -10.087 -29.952  1.00129.80      A    O  
ANISOU  119  OE1 GLU A  20    13998  19571  15748    893   1501  -2321  A    O  
ATOM    120  OE2 GLU A  20      62.398 -11.992 -30.960  1.00133.25      A    O1-
ANISOU  120  OE2 GLU A  20    14370  19911  16348   1033   1583  -2581  A    O1-
ATOM    121  N   LYS A  21      57.548 -13.649 -27.708  1.00 75.37      A    N  
ANISOU  121  N   LYS A  21     7493  12030   9113   1176    910  -2007  A    N  
ATOM    122  CA  LYS A  21      57.566 -14.768 -26.757  1.00 82.40      A    C  
ANISOU  122  CA  LYS A  21     8334  12768  10205   1319    805  -1975  A    C  
ATOM    123  C   LYS A  21      59.002 -15.268 -26.510  1.00 92.01      A    C  
ANISOU  123  C   LYS A  21     9353  14008  11597   1437    842  -2060  A    C  
ATOM    124  O   LYS A  21      59.877 -15.150 -27.376  1.00 87.25      A    O  
ANISOU  124  O   LYS A  21     8663  13505  10985   1422    976  -2205  A    O  
ATOM    125  CB  LYS A  21      56.651 -15.913 -27.219  1.00 84.65      A    C  
ANISOU  125  CB  LYS A  21     8723  12907  10535   1362    791  -2045  A    C  
ATOM    126  CG  LYS A  21      55.150 -15.571 -27.273  1.00 87.53      A    C  
ANISOU  126  CG  LYS A  21     9269  13225  10765   1266    723  -1950  A    C  
ATOM    127  CD  LYS A  21      54.289 -16.815 -27.558  1.00 94.11      A    C  
ANISOU  127  CD  LYS A  21    10183  13898  11675   1319    700  -2025  A    C  
ATOM    128  CE  LYS A  21      52.772 -16.516 -27.529  1.00 93.80      A    C  
ANISOU  128  CE  LYS A  21    10309  13806  11524   1229    621  -1931  A    C  
ATOM    129  NZ  LYS A  21      52.233 -15.808 -28.745  1.00 88.31      A    N1+
ANISOU  129  NZ  LYS A  21     9703  13235  10617   1097    682  -1985  A    N1+
ATOM    130  N   LEU A  22      59.258 -15.814 -25.326  1.00101.56      A    N  
ANISOU  130  N   LEU A  22    10490  15130  12968   1555    726  -1968  A    N  
ATOM    131  CA  LEU A  22      60.602 -16.315 -25.020  1.00104.50      A    C  
ANISOU  131  CA  LEU A  22    10662  15522  13522   1681    741  -2034  A    C  
ATOM    132  C   LEU A  22      60.639 -17.757 -24.538  1.00117.58      A    C  
ANISOU  132  C   LEU A  22    12278  17000  15396   1854    676  -2039  A    C  
ATOM    133  O   LEU A  22      61.379 -18.574 -25.090  1.00126.39      A    O  
ANISOU  133  O   LEU A  22    13284  18082  16655   1948    763  -2184  A    O  
ATOM    134  CB  LEU A  22      61.306 -15.420 -24.013  1.00 92.34      A    C  
ANISOU  134  CB  LEU A  22     9014  14096  11977   1665    670  -1921  A    C  
ATOM    135  CG  LEU A  22      61.640 -14.077 -24.637  1.00 86.22      A    C  
ANISOU  135  CG  LEU A  22     8228  13500  11031   1512    781  -1960  A    C  
ATOM    136  CD1 LEU A  22      62.572 -13.271 -23.746  1.00 82.65      A    C  
ANISOU  136  CD1 LEU A  22     7629  13172  10602   1499    739  -1896  A    C  
ATOM    137  CD2 LEU A  22      62.249 -14.319 -26.006  1.00 75.71      A    C  
ANISOU  137  CD2 LEU A  22     6844  12221   9701   1502    956  -2165  A    C  
ATOM    138  N   ALA A  23      59.851 -18.070 -23.514  1.00112.93      A    N  
ANISOU  138  N   ALA A  23    11779  16291  14838   1894    536  -1881  A    N  
ATOM    139  CA  ALA A  23      59.884 -19.403 -22.928  1.00110.76      A    C  
ANISOU  139  CA  ALA A  23    11474  15838  14774   2063    470  -1857  A    C  
ATOM    140  C   ALA A  23      58.672 -19.675 -22.057  1.00109.90      A    C  
ANISOU  140  C   ALA A  23    11526  15584  14649   2064    346  -1698  A    C  
ATOM    141  O   ALA A  23      58.294 -18.837 -21.250  1.00107.88      A    O  
ANISOU  141  O   ALA A  23    11327  15380  14284   1988    255  -1548  A    O  
ATOM    142  CB  ALA A  23      61.147 -19.573 -22.113  1.00104.16      A    C  
ANISOU  142  CB  ALA A  23    10441  15044  14093   2192    409  -1815  A    C  
ATOM    143  N   LYS A  24      58.073 -20.851 -22.214  1.00110.50      A    N  
ANISOU  143  N   LYS A  24    11673  15473  14840   2143    356  -1737  A    N  
ATOM    144  CA  LYS A  24      57.031 -21.287 -21.300  1.00109.93      A    C  
ANISOU  144  CA  LYS A  24    11737  15238  14793   2167    246  -1590  A    C  
ATOM    145  C   LYS A  24      57.569 -21.262 -19.868  1.00106.16      A    C  
ANISOU  145  C   LYS A  24    11189  14754  14391   2261    109  -1412  A    C  
ATOM    146  O   LYS A  24      58.647 -21.781 -19.603  1.00108.02      A    O  
ANISOU  146  O   LYS A  24    11268  14993  14780   2398     97  -1426  A    O  
ATOM    147  CB  LYS A  24      56.548 -22.696 -21.655  1.00120.42      A    C  
ANISOU  147  CB  LYS A  24    13118  16357  16280   2263    294  -1677  A    C  
ATOM    148  CG  LYS A  24      55.827 -22.810 -22.999  1.00134.31      A    C  
ANISOU  148  CG  LYS A  24    14969  18110  17952   2161    413  -1851  A    C  
ATOM    149  CD  LYS A  24      54.667 -23.821 -22.923  1.00145.17      A    C  
ANISOU  149  CD  LYS A  24    16482  19269  19408   2186    404  -1856  A    C  
ATOM    150  CE  LYS A  24      53.908 -23.950 -24.250  1.00146.33      A    C  
ANISOU  150  CE  LYS A  24    16717  19423  19460   2077    510  -2036  A    C  
ATOM    151  NZ  LYS A  24      52.598 -24.654 -24.082  1.00142.33      A    N1+
ANISOU  151  NZ  LYS A  24    16357  18730  18992   2061    484  -2023  A    N1+
ATOM    152  N   ILE A  25      56.821 -20.648 -18.954  1.00104.26      A    N  
ANISOU  152  N   ILE A  25    11061  14511  14042   2183      6  -1246  A    N  
ATOM    153  CA  ILE A  25      57.199 -20.582 -17.542  1.00105.15      A    C  
ANISOU  153  CA  ILE A  25    11134  14624  14194   2251   -132  -1068  A    C  
ATOM    154  C   ILE A  25      56.029 -20.964 -16.640  1.00113.45      A    C  
ANISOU  154  C   ILE A  25    12359  15503  15243   2246   -218   -920  A    C  
ATOM    155  O   ILE A  25      56.170 -21.009 -15.415  1.00112.70      A    O  
ANISOU  155  O   ILE A  25    12266  15385  15169   2298   -336   -760  A    O  
ATOM    156  CB  ILE A  25      57.628 -19.164 -17.137  1.00 97.70      A    C  
ANISOU  156  CB  ILE A  25    10138  13891  13093   2131   -170  -1004  A    C  
ATOM    157  CG1 ILE A  25      56.444 -18.205 -17.270  1.00 99.09      A    C  
ANISOU  157  CG1 ILE A  25    10481  14088  13082   1947   -154   -961  A    C  
ATOM    158  CG2 ILE A  25      58.781 -18.693 -17.986  1.00 95.83      A    C  
ANISOU  158  CG2 ILE A  25     9730  13827  12852   2120    -76  -1149  A    C  
ATOM    159  CD1 ILE A  25      56.622 -16.892 -16.545  1.00101.03      A    C  
ANISOU  159  CD1 ILE A  25    10711  14489  13188   1828   -205   -858  A    C  
ATOM    160  N   GLY A  26      54.878 -21.232 -17.257  1.00127.11      A    N  
ANISOU  160  N   GLY A  26    14235  17118  16943   2180   -158   -979  A    N  
ATOM    161  CA  GLY A  26      53.623 -21.418 -16.540  1.00143.23      A    C  
ANISOU  161  CA  GLY A  26    16454  19006  18962   2138   -217   -859  A    C  
ATOM    162  C   GLY A  26      53.405 -22.827 -16.031  1.00160.46      A    C  
ANISOU  162  C   GLY A  26    18677  20959  21330   2289   -242   -818  A    C  
ATOM    163  O   GLY A  26      52.307 -23.387 -16.147  1.00154.10      A    O  
ANISOU  163  O   GLY A  26    18009  19985  20555   2265   -214   -831  A    O  
ATOM    164  N   GLN A  27      54.462 -23.373 -15.431  1.00180.79      A    N  
ANISOU  164  N   GLN A  27    21130  23529  24034   2444   -296   -761  A    N  
ATOM    165  CA  GLN A  27      54.557 -24.795 -15.106  1.00189.52      A    C  
ANISOU  165  CA  GLN A  27    22235  24424  25350   2620   -300   -737  A    C  
ATOM    166  C   GLN A  27      53.424 -25.351 -14.228  1.00195.43      A    C  
ANISOU  166  C   GLN A  27    23166  24962  26125   2624   -349   -602  A    C  
ATOM    167  O   GLN A  27      52.512 -24.624 -13.811  1.00190.13      A    O  
ANISOU  167  O   GLN A  27    22625  24306  25310   2485   -385   -524  A    O  
ATOM    168  CB  GLN A  27      55.954 -25.128 -14.558  1.00185.53      A    C  
ANISOU  168  CB  GLN A  27    21549  23976  24967   2786   -367   -678  A    C  
ATOM    169  CG  GLN A  27      57.055 -24.911 -15.601  1.00184.09      A    C  
ANISOU  169  CG  GLN A  27    21179  23947  24819   2807   -280   -853  A    C  
ATOM    170  CD  GLN A  27      58.447 -25.239 -15.092  1.00186.78      A    C  
ANISOU  170  CD  GLN A  27    21322  24347  25300   2973   -347   -804  A    C  
ATOM    171  NE2 GLN A  27      59.318 -25.673 -15.995  1.00186.38      A    N  
ANISOU  171  NE2 GLN A  27    21116  24318  25383   3055   -246   -968  A    N  
ATOM    172  OE1 GLN A  27      58.738 -25.096 -13.905  1.00187.80      A    O  
ANISOU  172  OE1 GLN A  27    21434  24506  25414   3025   -487   -625  A    O  
ATOM    173  N   GLY A  28      53.493 -26.653 -13.969  1.00202.76      A    N  
ANISOU  173  N   GLY A  28    24102  25687  27252   2784   -337   -580  A    N  
ATOM    174  CA  GLY A  28      52.333 -27.407 -13.535  1.00208.56      A    C  
ANISOU  174  CA  GLY A  28    25013  26183  28047   2787   -325   -519  A    C  
ATOM    175  C   GLY A  28      51.574 -27.786 -14.796  1.00214.36      A    C  
ANISOU  175  C   GLY A  28    25799  26837  28812   2718   -187   -725  A    C  
ATOM    176  O   GLY A  28      50.567 -28.499 -14.754  1.00212.71      A    O  
ANISOU  176  O   GLY A  28    25722  26424  28674   2709   -142   -737  A    O  
ATOM    177  N   THR A  29      52.092 -27.296 -15.923  1.00218.34      A    N  
ANISOU  177  N   THR A  29    26194  27508  29258   2665   -119   -892  A    N  
ATOM    178  CA  THR A  29      51.492 -27.472 -17.247  1.00216.91      A    C  
ANISOU  178  CA  THR A  29    26045  27308  29061   2579      6  -1103  A    C  
ATOM    179  C   THR A  29      50.157 -26.732 -17.368  1.00210.60      A    C  
ANISOU  179  C   THR A  29    25399  26527  28092   2395     -5  -1095  A    C  
ATOM    180  O   THR A  29      49.347 -27.041 -18.240  1.00211.44      A    O  
ANISOU  180  O   THR A  29    25571  26571  28195   2325     77  -1239  A    O  
ATOM    181  CB  THR A  29      51.346 -28.974 -17.628  1.00193.52      A    C  
ANISOU  181  CB  THR A  29    23093  24111  26324   2699    107  -1213  A    C  
ATOM    182  CG2 THR A  29      50.856 -29.139 -19.065  1.00192.05      A    C  
ANISOU  182  CG2 THR A  29    22922  23938  26110   2603    238  -1454  A    C  
ATOM    183  OG1 THR A  29      52.616 -29.622 -17.499  1.00194.87      A    O  
ANISOU  183  OG1 THR A  29    23110  24264  26667   2877    118  -1212  A    O  
ATOM    184  N   PHE A  30      49.932 -25.742 -16.505  1.00202.21      A    N  
ANISOU  184  N   PHE A  30    24386  25554  26890   2314   -104   -932  A    N  
ATOM    185  CA  PHE A  30      48.660 -25.018 -16.529  1.00192.89      A    C  
ANISOU  185  CA  PHE A  30    23343  24378  25568   2145   -116   -910  A    C  
ATOM    186  C   PHE A  30      48.747 -23.503 -16.681  1.00184.07      A    C  
ANISOU  186  C   PHE A  30    22202  23491  24243   2003   -149   -878  A    C  
ATOM    187  O   PHE A  30      49.669 -22.859 -16.182  1.00183.40      A    O  
ANISOU  187  O   PHE A  30    22028  23548  24107   2021   -203   -794  A    O  
ATOM    188  CB  PHE A  30      47.764 -25.410 -15.350  1.00191.46      A    C  
ANISOU  188  CB  PHE A  30    23305  24004  25438   2151   -172   -756  A    C  
ATOM    189  CG  PHE A  30      46.831 -26.544 -15.668  1.00192.46      A    C  
ANISOU  189  CG  PHE A  30    23526  23900  25701   2175    -98   -845  A    C  
ATOM    190  CD1 PHE A  30      45.557 -26.294 -16.155  1.00188.97      A    C  
ANISOU  190  CD1 PHE A  30    23189  23419  25192   2035    -64   -918  A    C  
ATOM    191  CD2 PHE A  30      47.242 -27.863 -15.515  1.00195.08      A    C  
ANISOU  191  CD2 PHE A  30    23833  24053  26235   2337    -57   -865  A    C  
ATOM    192  CE1 PHE A  30      44.701 -27.336 -16.465  1.00189.02      A    C  
ANISOU  192  CE1 PHE A  30    23273  23218  25327   2048      8  -1017  A    C  
ATOM    193  CE2 PHE A  30      46.392 -28.911 -15.821  1.00193.79      A    C  
ANISOU  193  CE2 PHE A  30    23755  23670  26206   2352     27   -960  A    C  
ATOM    194  CZ  PHE A  30      45.118 -28.647 -16.297  1.00191.51      A    C  
ANISOU  194  CZ  PHE A  30    23569  23352  25844   2203     59  -1043  A    C  
ATOM    195  N   GLY A  31      47.753 -22.960 -17.381  1.00175.25      A    N  
ANISOU  195  N   GLY A  31    21166  22405  23017   1861   -114   -946  A    N  
ATOM    196  CA  GLY A  31      47.709 -21.559 -17.747  1.00163.58      A    C  
ANISOU  196  CA  GLY A  31    19675  21127  21349   1721   -121   -934  A    C  
ATOM    197  C   GLY A  31      48.171 -21.326 -19.177  1.00154.79      A    C  
ANISOU  197  C   GLY A  31    18481  20162  20169   1690    -37  -1109  A    C  
ATOM    198  O   GLY A  31      47.500 -20.633 -19.950  1.00148.33      A    O  
ANISOU  198  O   GLY A  31    17711  19427  19221   1565    -10  -1161  A    O  
ATOM    199  N   GLU A  32      49.303 -21.938 -19.532  1.00148.39      A    N  
ANISOU  199  N   GLU A  32    17549  19380  19453   1807      7  -1197  A    N  
ATOM    200  CA  GLU A  32      50.068 -21.576 -20.729  1.00131.88      A    C  
ANISOU  200  CA  GLU A  32    15358  17459  17291   1782     90  -1347  A    C  
ATOM    201  C   GLU A  32      50.613 -20.152 -20.609  1.00114.54      A    C  
ANISOU  201  C   GLU A  32    13109  15475  14937   1693     68  -1272  A    C  
ATOM    202  O   GLU A  32      50.111 -19.223 -21.243  1.00105.91      A    O  
ANISOU  202  O   GLU A  32    12064  14491  13685   1560     94  -1291  A    O  
ATOM    203  CB  GLU A  32      49.253 -21.742 -22.011  1.00130.82      A    C  
ANISOU  203  CB  GLU A  32    15290  17324  17090   1696    167  -1507  A    C  
ATOM    204  CG  GLU A  32      49.650 -22.963 -22.812  1.00137.69      A    C  
ANISOU  204  CG  GLU A  32    16108  18114  18096   1789    261  -1691  A    C  
ATOM    205  CD  GLU A  32      49.655 -22.706 -24.309  1.00143.53      A    C  
ANISOU  205  CD  GLU A  32    16836  18988  18710   1700    358  -1876  A    C  
ATOM    206  OE1 GLU A  32      49.188 -21.622 -24.737  1.00143.10      A    O  
ANISOU  206  OE1 GLU A  32    16832  19075  18465   1567    342  -1849  A    O  
ATOM    207  OE2 GLU A  32      50.131 -23.592 -25.054  1.00145.11      A    O1-
ANISOU  207  OE2 GLU A  32    16978  19151  19006   1762    453  -2046  A    O1-
ATOM    208  N   VAL A  33      51.646 -20.008 -19.782  1.00107.35      A    N  
ANISOU  208  N   VAL A  33    12095  14617  14078   1769     21  -1186  A    N  
ATOM    209  CA  VAL A  33      52.257 -18.720 -19.465  1.00 99.47      A    C  
ANISOU  209  CA  VAL A  33    11032  13806  12955   1692     -2  -1111  A    C  
ATOM    210  C   VAL A  33      53.634 -18.575 -20.123  1.00100.76      A    C  
ANISOU  210  C   VAL A  33    11029  14121  13132   1737     69  -1225  A    C  
ATOM    211  O   VAL A  33      54.481 -19.450 -19.992  1.00106.60      A    O  
ANISOU  211  O   VAL A  33    11663  14815  14026   1878     72  -1268  A    O  
ATOM    212  CB  VAL A  33      52.429 -18.581 -17.948  1.00 91.38      A    C  
ANISOU  212  CB  VAL A  33    10006  12748  11965   1730   -116   -929  A    C  
ATOM    213  CG1 VAL A  33      53.017 -17.247 -17.599  1.00 87.12      A    C  
ANISOU  213  CG1 VAL A  33     9401  12401  11299   1637   -133   -864  A    C  
ATOM    214  CG2 VAL A  33      51.096 -18.788 -17.247  1.00 94.53      A    C  
ANISOU  214  CG2 VAL A  33    10570  12982  12363   1687   -173   -821  A    C  
ATOM    215  N   PHE A  34      53.854 -17.475 -20.836  1.00 97.55      A    N  
ANISOU  215  N   PHE A  34    10599  13889  12575   1620    133  -1272  A    N  
ATOM    216  CA  PHE A  34      55.134 -17.228 -21.498  1.00 90.60      A    C  
ANISOU  216  CA  PHE A  34     9566  13158  11698   1643    217  -1387  A    C  
ATOM    217  C   PHE A  34      55.863 -16.058 -20.842  1.00 84.11      A    C  
ANISOU  217  C   PHE A  34     8661  12497  10802   1585    187  -1297  A    C  
ATOM    218  O   PHE A  34      55.234 -15.113 -20.368  1.00 90.30      A    O  
ANISOU  218  O   PHE A  34     9527  13315  11466   1471    148  -1183  A    O  
ATOM    219  CB  PHE A  34      54.926 -16.897 -22.982  1.00 96.75      A    C  
ANISOU  219  CB  PHE A  34    10381  14023  12356   1548    341  -1535  A    C  
ATOM    220  CG  PHE A  34      54.281 -17.997 -23.791  1.00107.05      A    C  
ANISOU  220  CG  PHE A  34    11757  15200  13718   1585    387  -1660  A    C  
ATOM    221  CD1 PHE A  34      55.055 -18.956 -24.426  1.00112.58      A    C  
ANISOU  221  CD1 PHE A  34    12361  15870  14545   1686    471  -1819  A    C  
ATOM    222  CD2 PHE A  34      52.903 -18.045 -23.957  1.00110.67      A    C  
ANISOU  222  CD2 PHE A  34    12371  15572  14105   1512    356  -1630  A    C  
ATOM    223  CE1 PHE A  34      54.464 -19.962 -25.190  1.00114.67      A    C  
ANISOU  223  CE1 PHE A  34    12690  16019  14861   1708    526  -1950  A    C  
ATOM    224  CE2 PHE A  34      52.308 -19.048 -24.723  1.00114.40      A    C  
ANISOU  224  CE2 PHE A  34    12904  15937  14628   1535    401  -1761  A    C  
ATOM    225  CZ  PHE A  34      53.092 -20.009 -25.337  1.00111.43      A    C  
ANISOU  225  CZ  PHE A  34    12435  15530  14372   1630    489  -1923  A    C  
ATOM    226  N   LYS A  35      57.187 -16.115 -20.800  1.00 81.48      A    N  
ANISOU  226  N   LYS A  35     8156  12257  10547   1659    211  -1353  A    N  
ATOM    227  CA  LYS A  35      57.963 -14.909 -20.537  1.00 80.62      A    C  
ANISOU  227  CA  LYS A  35     7951  12330  10351   1578    224  -1323  A    C  
ATOM    228  C   LYS A  35      58.062 -14.234 -21.888  1.00 80.49      A    C  
ANISOU  228  C   LYS A  35     7942  12430  10212   1471    371  -1452  A    C  
ATOM    229  O   LYS A  35      58.092 -14.897 -22.920  1.00 80.58      A    O  
ANISOU  229  O   LYS A  35     7956  12408  10254   1506    457  -1591  A    O  
ATOM    230  CB  LYS A  35      59.352 -15.232 -19.973  1.00 78.49      A    C  
ANISOU  230  CB  LYS A  35     7481  12122  10220   1698    188  -1341  A    C  
ATOM    231  CG  LYS A  35      60.337 -14.045 -19.902  1.00 80.36      A    C  
ANISOU  231  CG  LYS A  35     7586  12564  10385   1615    230  -1359  A    C  
ATOM    232  CD  LYS A  35      61.709 -14.453 -19.311  1.00 84.61      A    C  
ANISOU  232  CD  LYS A  35     7908  13163  11077   1745    178  -1380  A    C  
ATOM    233  CE  LYS A  35      62.652 -13.258 -19.090  1.00 86.68      A    C  
ANISOU  233  CE  LYS A  35     8033  13628  11273   1653    208  -1396  A    C  
ATOM    234  NZ  LYS A  35      63.990 -13.626 -18.484  1.00 82.39      A    N1+
ANISOU  234  NZ  LYS A  35     7263  13158  10883   1778    144  -1418  A    N1+
ATOM    235  N   ALA A  36      58.064 -12.916 -21.907  1.00 80.72      A    N  
ANISOU  235  N   ALA A  36     7986  12590  10096   1334    408  -1406  A    N  
ATOM    236  CA  ALA A  36      58.186 -12.245 -23.182  1.00 81.54      A    C  
ANISOU  236  CA  ALA A  36     8103  12804  10074   1233    552  -1515  A    C  
ATOM    237  C   ALA A  36      58.789 -10.872 -23.027  1.00 79.78      A    C  
ANISOU  237  C   ALA A  36     7816  12743   9753   1121    607  -1482  A    C  
ATOM    238  O   ALA A  36      58.917 -10.347 -21.917  1.00 76.51      A    O  
ANISOU  238  O   ALA A  36     7369  12355   9348   1098    527  -1369  A    O  
ATOM    239  CB  ALA A  36      56.850 -12.173 -23.892  1.00 76.47      A    C  
ANISOU  239  CB  ALA A  36     7645  12098   9312   1153    568  -1501  A    C  
ATOM    240  N   ARG A  37      59.152 -10.310 -24.170  1.00 77.95      A    N  
ANISOU  240  N   ARG A  37     7574  12619   9426   1045    752  -1588  A    N  
ATOM    241  CA  ARG A  37      59.919  -9.091 -24.245  1.00 76.54      A    C  
ANISOU  241  CA  ARG A  37     7316  12596   9172    944    845  -1597  A    C  
ATOM    242  C   ARG A  37      59.230  -8.130 -25.198  1.00 78.93      A    C  
ANISOU  242  C   ARG A  37     7755  12950   9285    802    950  -1583  A    C  
ATOM    243  O   ARG A  37      58.900  -8.486 -26.327  1.00 81.95      A    O  
ANISOU  243  O   ARG A  37     8212  13322   9603    796   1020  -1669  A    O  
ATOM    244  CB  ARG A  37      61.305  -9.434 -24.779  1.00 77.30      A    C  
ANISOU  244  CB  ARG A  37     7235  12776   9361   1008    945  -1762  A    C  
ATOM    245  CG  ARG A  37      62.060  -8.260 -25.352  1.00 76.05      A    C  
ANISOU  245  CG  ARG A  37     7014  12776   9107    890   1099  -1824  A    C  
ATOM    246  CD  ARG A  37      63.453  -8.649 -25.784  1.00 63.19      A    C  
ANISOU  246  CD  ARG A  37     5195  11221   7595    957   1197  -1993  A    C  
ATOM    247  NE  ARG A  37      64.347  -7.500 -25.751  1.00 76.35      A    N  
ANISOU  247  NE  ARG A  37     6752  13035   9221    858   1301  -2022  A    N  
ATOM    248  CZ  ARG A  37      64.428  -6.581 -26.707  1.00 73.17      A    C  
ANISOU  248  CZ  ARG A  37     6403  12720   8676    731   1469  -2072  A    C  
ATOM    249  NH1 ARG A  37      63.669  -6.660 -27.794  1.00 73.45      A    N1+
ANISOU  249  NH1 ARG A  37     6601  12724   8582    686   1542  -2094  A    N1+
ATOM    250  NH2 ARG A  37      65.270  -5.578 -26.570  1.00 76.24      A    N  
ANISOU  250  NH2 ARG A  37     6685  13231   9052    645   1566  -2100  A    N  
ATOM    251  N   HIS A  38      59.003  -6.912 -24.740  1.00 73.06      A    N  
ANISOU  251  N   HIS A  38     7046  12263   8452    686    960  -1472  A    N  
ATOM    252  CA  HIS A  38      58.430  -5.888 -25.595  1.00 73.59      A    C  
ANISOU  252  CA  HIS A  38     7231  12383   8347    554   1065  -1439  A    C  
ATOM    253  C   HIS A  38      59.396  -5.585 -26.741  1.00 76.49      A    C  
ANISOU  253  C   HIS A  38     7531  12873   8659    520   1239  -1583  A    C  
ATOM    254  O   HIS A  38      60.563  -5.278 -26.514  1.00 84.11      A    O  
ANISOU  254  O   HIS A  38     8344  13927   9686    520   1305  -1650  A    O  
ATOM    255  CB  HIS A  38      58.174  -4.623 -24.776  1.00 76.57      A    C  
ANISOU  255  CB  HIS A  38     7631  12792   8672    442   1059  -1300  A    C  
ATOM    256  CG  HIS A  38      57.506  -3.534 -25.551  1.00 78.13      A    C  
ANISOU  256  CG  HIS A  38     7954  13024   8707    313   1160  -1238  A    C  
ATOM    257  CD2 HIS A  38      56.255  -3.021 -25.467  1.00 68.81      A    C  
ANISOU  257  CD2 HIS A  38     6919  11775   7448    246   1119  -1102  A    C  
ATOM    258  ND1 HIS A  38      58.141  -2.848 -26.567  1.00 78.33      A    N  
ANISOU  258  ND1 HIS A  38     7959  13163   8638    244   1327  -1313  A    N  
ATOM    259  CE1 HIS A  38      57.307  -1.955 -27.073  1.00 81.55      A    C  
ANISOU  259  CE1 HIS A  38     8503  13573   8911    144   1380  -1215  A    C  
ATOM    260  NE2 HIS A  38      56.156  -2.041 -26.426  1.00 75.52      A    N  
ANISOU  260  NE2 HIS A  38     7835  12700   8160    145   1253  -1088  A    N  
ATOM    261  N   ARG A  39      58.914  -5.650 -27.973  1.00 70.16      A    N  
ANISOU  261  N   ARG A  39     6840  12080   7737    485   1316  -1634  A    N  
ATOM    262  CA  ARG A  39      59.806  -5.547 -29.130  1.00 65.24      A    C  
ANISOU  262  CA  ARG A  39     6167  11562   7060    459   1486  -1786  A    C  
ATOM    263  C   ARG A  39      60.465  -4.184 -29.317  1.00 68.41      A    C  
ANISOU  263  C   ARG A  39     6530  12087   7377    340   1633  -1771  A    C  
ATOM    264  O   ARG A  39      61.194  -3.973 -30.278  1.00 77.18      A    O  
ANISOU  264  O   ARG A  39     7609  13286   8430    302   1792  -1890  A    O  
ATOM    265  CB  ARG A  39      59.080  -5.952 -30.420  1.00 67.66      A    C  
ANISOU  265  CB  ARG A  39     6616  11857   7234    441   1529  -1842  A    C  
ATOM    266  CG  ARG A  39      58.608  -7.401 -30.447  1.00 80.48      A    C  
ANISOU  266  CG  ARG A  39     8261  13366   8952    554   1426  -1909  A    C  
ATOM    267  CD  ARG A  39      58.063  -7.795 -31.817  1.00 96.72      A    C  
ANISOU  267  CD  ARG A  39    10439  15439  10871    523   1489  -2001  A    C  
ATOM    268  NE  ARG A  39      57.268  -9.022 -31.741  1.00109.45      A    N  
ANISOU  268  NE  ARG A  39    12104  16925  12557    607   1374  -2031  A    N  
ATOM    269  CZ  ARG A  39      57.720 -10.240 -32.039  1.00115.47      A    C  
ANISOU  269  CZ  ARG A  39    12799  17636  13437    700   1396  -2190  A    C  
ATOM    270  NH1 ARG A  39      58.973 -10.415 -32.453  1.00116.29      A    N1+
ANISOU  270  NH1 ARG A  39    12776  17807  13603    726   1527  -2338  A    N1+
ATOM    271  NH2 ARG A  39      56.911 -11.289 -31.925  1.00112.28      A    N  
ANISOU  271  NH2 ARG A  39    12454  17107  13102    766   1297  -2207  A    N  
ATOM    272  N   LYS A  40      60.221  -3.248 -28.416  1.00 73.60      A    N  
ANISOU  272  N   LYS A  40     7192  12746   8027    274   1595  -1634  A    N  
ATOM    273  CA  LYS A  40      60.749  -1.908 -28.628  1.00 79.99      A    C  
ANISOU  273  CA  LYS A  40     7979  13658   8754    150   1749  -1617  A    C  
ATOM    274  C   LYS A  40      61.608  -1.419 -27.469  1.00 84.65      A    C  
ANISOU  274  C   LYS A  40     8409  14294   9461    135   1738  -1609  A    C  
ATOM    275  O   LYS A  40      62.547  -0.647 -27.669  1.00 87.26      A    O  
ANISOU  275  O   LYS A  40     8646  14726   9783     63   1885  -1675  A    O  
ATOM    276  CB  LYS A  40      59.606  -0.928 -28.909  1.00 79.09      A    C  
ANISOU  276  CB  LYS A  40     8043  13523   8487     43   1767  -1460  A    C  
ATOM    277  CG  LYS A  40      59.222  -0.808 -30.374  1.00 78.83      A    C  
ANISOU  277  CG  LYS A  40     8142  13526   8284      0   1871  -1487  A    C  
ATOM    278  CD  LYS A  40      57.872  -0.155 -30.552  1.00 84.93      A    C  
ANISOU  278  CD  LYS A  40     9090  14249   8930    -65   1827  -1315  A    C  
ATOM    279  CE  LYS A  40      57.666   0.284 -31.987  1.00 96.03      A    C  
ANISOU  279  CE  LYS A  40    10618  15725  10145   -130   1954  -1324  A    C  
ATOM    280  NZ  LYS A  40      58.610   1.381 -32.339  1.00105.70      A    N1+
ANISOU  280  NZ  LYS A  40    11797  17049  11317   -225   2156  -1346  A    N1+
ATOM    281  N   THR A  41      61.292  -1.889 -26.267  1.00 84.22      A    N  
ANISOU  281  N   THR A  41     8323  14168   9510    199   1566  -1534  A    N  
ATOM    282  CA  THR A  41      61.904  -1.375 -25.054  1.00 81.74      A    C  
ANISOU  282  CA  THR A  41     7878  13897   9281    172   1528  -1502  A    C  
ATOM    283  C   THR A  41      62.619  -2.461 -24.272  1.00 85.57      A    C  
ANISOU  283  C   THR A  41     8209  14373   9932    309   1400  -1567  A    C  
ATOM    284  O   THR A  41      63.357  -2.177 -23.317  1.00 92.97      A    O  
ANISOU  284  O   THR A  41     9004  15372  10948    302   1362  -1570  A    O  
ATOM    285  CB  THR A  41      60.840  -0.790 -24.143  1.00 81.21      A    C  
ANISOU  285  CB  THR A  41     7921  13758   9176    106   1435  -1328  A    C  
ATOM    286  CG2 THR A  41      59.992   0.191 -24.924  1.00 77.14      A    C  
ANISOU  286  CG2 THR A  41     7568  13232   8512    -10   1544  -1243  A    C  
ATOM    287  OG1 THR A  41      60.029  -1.852 -23.625  1.00 83.68      A    O  
ANISOU  287  OG1 THR A  41     8300  13949   9545    210   1257  -1267  A    O  
ATOM    288  N   GLY A  42      62.388  -3.705 -24.673  1.00 81.78      A    N  
ANISOU  288  N   GLY A  42     7754  13813   9504    432   1332  -1618  A    N  
ATOM    289  CA  GLY A  42      63.057  -4.839 -24.066  1.00 80.97      A    C  
ANISOU  289  CA  GLY A  42     7509  13684   9570    580   1220  -1678  A    C  
ATOM    290  C   GLY A  42      62.426  -5.197 -22.736  1.00 76.97      A    C  
ANISOU  290  C   GLY A  42     7037  13090   9120    629   1027  -1537  A    C  
ATOM    291  O   GLY A  42      62.826  -6.170 -22.090  1.00 79.21      A    O  
ANISOU  291  O   GLY A  42     7223  13333   9539    761    909  -1549  A    O  
ATOM    292  N   GLN A  43      61.435  -4.410 -22.328  1.00 66.15      A    N  
ANISOU  292  N   GLN A  43     5804  11684   7647    525   1001  -1399  A    N  
ATOM    293  CA  GLN A  43      60.728  -4.668 -21.077  1.00 74.09      A    C  
ANISOU  293  CA  GLN A  43     6864  12598   8688    550    834  -1262  A    C  
ATOM    294  C   GLN A  43      60.155  -6.077 -21.026  1.00 81.54      A    C  
ANISOU  294  C   GLN A  43     7868  13401   9712    692    713  -1251  A    C  
ATOM    295  O   GLN A  43      59.478  -6.520 -21.952  1.00 80.20      A    O  
ANISOU  295  O   GLN A  43     7808  13161   9502    709    748  -1282  A    O  
ATOM    296  CB  GLN A  43      59.612  -3.661 -20.903  1.00 65.74      A    C  
ANISOU  296  CB  GLN A  43     5965  11503   7511    414    854  -1132  A    C  
ATOM    297  CG  GLN A  43      58.683  -3.956 -19.766  1.00 74.85      A    C  
ANISOU  297  CG  GLN A  43     7209  12542   8690    428    702   -995  A    C  
ATOM    298  CD  GLN A  43      57.398  -3.147 -19.898  1.00 81.36      A    C  
ANISOU  298  CD  GLN A  43     8207  13298   9409    310    735   -882  A    C  
ATOM    299  NE2 GLN A  43      56.541  -3.203 -18.873  1.00 58.83      A    N  
ANISOU  299  NE2 GLN A  43     5437  10345   6571    293    626   -761  A    N  
ATOM    300  OE1 GLN A  43      57.184  -2.474 -20.921  1.00 89.20      A    O  
ANISOU  300  OE1 GLN A  43     9257  14326  10309    235    860   -901  A    O  
ATOM    301  N   LYS A  44      60.442  -6.793 -19.950  1.00 83.65      A    N  
ANISOU  301  N   LYS A  44     8061  13629  10093    794    573  -1209  A    N  
ATOM    302  CA  LYS A  44      60.019  -8.180 -19.881  1.00 81.08      A    C  
ANISOU  302  CA  LYS A  44     7779  13162   9865    938    472  -1204  A    C  
ATOM    303  C   LYS A  44      58.649  -8.237 -19.221  1.00 75.08      A    C  
ANISOU  303  C   LYS A  44     7196  12269   9063    905    373  -1057  A    C  
ATOM    304  O   LYS A  44      58.322  -7.391 -18.381  1.00 71.18      A    O  
ANISOU  304  O   LYS A  44     6740  11797   8507    806    340   -951  A    O  
ATOM    305  CB  LYS A  44      61.038  -9.036 -19.123  1.00 75.79      A    C  
ANISOU  305  CB  LYS A  44     6941  12503   9351   1083    373  -1228  A    C  
ATOM    306  CG  LYS A  44      62.491  -8.676 -19.390  1.00 81.46      A    C  
ANISOU  306  CG  LYS A  44     7452  13380  10119   1089    454  -1350  A    C  
ATOM    307  CD  LYS A  44      62.980  -9.051 -20.799  1.00 84.82      A    C  
ANISOU  307  CD  LYS A  44     7831  13825  10573   1124    600  -1519  A    C  
ATOM    308  CE  LYS A  44      64.469  -8.699 -21.002  1.00 91.22      A    C  
ANISOU  308  CE  LYS A  44     8421  14788  11450   1129    687  -1647  A    C  
ATOM    309  NZ  LYS A  44      65.015  -7.637 -20.055  1.00 98.34      A    N1+
ANISOU  309  NZ  LYS A  44     9225  15823  12318   1037    656  -1592  A    N1+
ATOM    310  N   VAL A  45      57.855  -9.227 -19.624  1.00 67.76      A    N  
ANISOU  310  N   VAL A  45     6373  11202   8172    981    339  -1065  A    N  
ATOM    311  CA  VAL A  45      56.502  -9.406 -19.123  1.00 69.64      A    C  
ANISOU  311  CA  VAL A  45     6779  11297   8385    956    257   -945  A    C  
ATOM    312  C   VAL A  45      56.141 -10.882 -19.062  1.00 75.13      A    C  
ANISOU  312  C   VAL A  45     7511  11835   9200   1100    180   -961  A    C  
ATOM    313  O   VAL A  45      56.870 -11.742 -19.561  1.00 80.51      A    O  
ANISOU  313  O   VAL A  45     8098  12514   9978   1214    204  -1071  A    O  
ATOM    314  CB  VAL A  45      55.446  -8.727 -20.032  1.00 70.01      A    C  
ANISOU  314  CB  VAL A  45     6969  11330   8302    837    338   -936  A    C  
ATOM    315  CG1 VAL A  45      55.622  -7.219 -20.055  1.00 53.23      A    C  
ANISOU  315  CG1 VAL A  45     4833   9331   6062    688    423   -897  A    C  
ATOM    316  CG2 VAL A  45      55.489  -9.313 -21.436  1.00 75.19      A    C  
ANISOU  316  CG2 VAL A  45     7635  11988   8947    879    421  -1074  A    C  
ATOM    317  N   ALA A  46      55.001 -11.167 -18.448  1.00 71.34      A    N  
ANISOU  317  N   ALA A  46     7168  11215   8722   1090     99   -854  A    N  
ATOM    318  CA  ALA A  46      54.435 -12.509 -18.483  1.00 72.81      A    C  
ANISOU  318  CA  ALA A  46     7420  11231   9015   1205     46   -870  A    C  
ATOM    319  C   ALA A  46      53.128 -12.468 -19.271  1.00 69.98      A    C  
ANISOU  319  C   ALA A  46     7215  10792   8584   1130     84   -884  A    C  
ATOM    320  O   ALA A  46      52.316 -11.575 -19.082  1.00 67.53      A    O  
ANISOU  320  O   ALA A  46     6997  10485   8176   1010     83   -798  A    O  
ATOM    321  CB  ALA A  46      54.193 -13.016 -17.084  1.00 66.77      A    C  
ANISOU  321  CB  ALA A  46     6686  10356   8326   1265    -81   -739  A    C  
ATOM    322  N   LEU A  47      52.953 -13.411 -20.184  1.00 63.73      A    N  
ANISOU  322  N   LEU A  47     6440   9932   7843   1199    121  -1000  A    N  
ATOM    323  CA  LEU A  47      51.735 -13.492 -20.953  1.00 64.29      A    C  
ANISOU  323  CA  LEU A  47     6645   9933   7851   1137    145  -1027  A    C  
ATOM    324  C   LEU A  47      50.995 -14.729 -20.491  1.00 75.09      A    C  
ANISOU  324  C   LEU A  47     8086  11102   9344   1225     76  -1011  A    C  
ATOM    325  O   LEU A  47      51.487 -15.847 -20.635  1.00 80.97      A    O  
ANISOU  325  O   LEU A  47     8775  11778  10213   1348     82  -1096  A    O  
ATOM    326  CB  LEU A  47      52.032 -13.633 -22.442  1.00 58.88      A    C  
ANISOU  326  CB  LEU A  47     5933   9329   7111   1130    251  -1190  A    C  
ATOM    327  CG  LEU A  47      52.878 -12.575 -23.114  1.00 60.38      A    C  
ANISOU  327  CG  LEU A  47     6047   9710   7186   1055    348  -1235  A    C  
ATOM    328  CD1 LEU A  47      52.998 -12.933 -24.569  1.00 63.49      A    C  
ANISOU  328  CD1 LEU A  47     6444  10153   7527   1052    449  -1399  A    C  
ATOM    329  CD2 LEU A  47      52.257 -11.224 -22.957  1.00 61.54      A    C  
ANISOU  329  CD2 LEU A  47     6268   9920   7195    914    351  -1117  A    C  
ATOM    330  N   LYS A  48      49.815 -14.528 -19.931  1.00 65.79      A    N  
ANISOU  330  N   LYS A  48     7031   9822   8143   1161     20   -906  A    N  
ATOM    331  CA  LYS A  48      48.969 -15.636 -19.563  1.00 67.71      A    C  
ANISOU  331  CA  LYS A  48     7360   9868   8497   1224    -30   -897  A    C  
ATOM    332  C   LYS A  48      47.797 -15.697 -20.562  1.00 72.55      A    C  
ANISOU  332  C   LYS A  48     8075  10440   9053   1151      3   -970  A    C  
ATOM    333  O   LYS A  48      46.889 -14.872 -20.536  1.00 69.47      A    O  
ANISOU  333  O   LYS A  48     7765  10059   8573   1038    -11   -897  A    O  
ATOM    334  CB  LYS A  48      48.529 -15.468 -18.105  1.00 74.33      A    C  
ANISOU  334  CB  LYS A  48     8260  10613   9369   1210   -116   -730  A    C  
ATOM    335  CG  LYS A  48      47.571 -16.534 -17.572  1.00 98.25      A    C  
ANISOU  335  CG  LYS A  48    11395  13423  12512   1262   -162   -699  A    C  
ATOM    336  CD  LYS A  48      47.376 -16.376 -16.061  1.00109.92      A    C  
ANISOU  336  CD  LYS A  48    12924  14825  14016   1254   -240   -533  A    C  
ATOM    337  CE  LYS A  48      46.123 -17.077 -15.568  1.00116.59      A    C  
ANISOU  337  CE  LYS A  48    13905  15455  14937   1251   -266   -488  A    C  
ATOM    338  NZ  LYS A  48      46.108 -17.121 -14.078  1.00120.84      A    N1+
ANISOU  338  NZ  LYS A  48    14492  15915  15507   1265   -336   -333  A    N1+
ATOM    339  N   LYS A  49      47.845 -16.653 -21.482  1.00 82.09      A    N  
ANISOU  339  N   LYS A  49     9270  11610  10312   1212     49  -1120  A    N  
ATOM    340  CA  LYS A  49      46.781 -16.812 -22.477  1.00 83.03      A    C  
ANISOU  340  CA  LYS A  49     9474  11702  10373   1146     74  -1208  A    C  
ATOM    341  C   LYS A  49      45.518 -17.323 -21.788  1.00 82.09      A    C  
ANISOU  341  C   LYS A  49     9464  11391  10334   1137     11  -1142  A    C  
ATOM    342  O   LYS A  49      45.596 -18.140 -20.871  1.00 86.61      A    O  
ANISOU  342  O   LYS A  49    10044  11818  11047   1226    -23  -1098  A    O  
ATOM    343  CB  LYS A  49      47.252 -17.774 -23.572  1.00 87.96      A    C  
ANISOU  343  CB  LYS A  49    10049  12333  11038   1212    148  -1400  A    C  
ATOM    344  CG  LYS A  49      46.228 -18.249 -24.606  1.00 91.36      A    C  
ANISOU  344  CG  LYS A  49    10559  12726  11430   1160    171  -1525  A    C  
ATOM    345  CD  LYS A  49      46.957 -19.103 -25.668  1.00104.89      A    C  
ANISOU  345  CD  LYS A  49    12206  14472  13175   1219    265  -1726  A    C  
ATOM    346  CE  LYS A  49      46.015 -19.846 -26.614  1.00111.06      A    C  
ANISOU  346  CE  LYS A  49    13057  15197  13946   1180    290  -1877  A    C  
ATOM    347  NZ  LYS A  49      46.746 -20.791 -27.520  1.00110.17      A    N1+
ANISOU  347  NZ  LYS A  49    12879  15091  13888   1240    393  -2081  A    N1+
ATOM    348  N   VAL A  50      44.361 -16.813 -22.196  1.00 78.04      A    N  
ANISOU  348  N   VAL A  50     9036  10879   9737   1030     -4  -1129  A    N  
ATOM    349  CA  VAL A  50      43.098 -17.256 -21.613  1.00 80.88      A    C  
ANISOU  349  CA  VAL A  50     9494  11059  10177   1009    -54  -1081  A    C  
ATOM    350  C   VAL A  50      42.671 -18.592 -22.208  1.00 91.08      A    C  
ANISOU  350  C   VAL A  50    10809  12228  11570   1065    -29  -1235  A    C  
ATOM    351  O   VAL A  50      42.361 -18.687 -23.404  1.00 79.56      A    O  
ANISOU  351  O   VAL A  50     9352  10839  10037   1023      3  -1367  A    O  
ATOM    352  CB  VAL A  50      41.952 -16.256 -21.825  1.00 71.02      A    C  
ANISOU  352  CB  VAL A  50     8316   9845   8824    877    -81  -1015  A    C  
ATOM    353  CG1 VAL A  50      40.633 -16.932 -21.513  1.00 59.49      A    C  
ANISOU  353  CG1 VAL A  50     6944   8196   7463    860   -117  -1021  A    C  
ATOM    354  CG2 VAL A  50      42.141 -15.027 -20.955  1.00 66.44      A    C  
ANISOU  354  CG2 VAL A  50     7733   9326   8186    815   -101   -848  A    C  
ATOM    355  N   LEU A  51      42.624 -19.602 -21.342  1.00102.45      A    N  
ANISOU  355  N   LEU A  51    12270  13482  13173   1154    -42  -1213  A    N  
ATOM    356  CA  LEU A  51      42.523 -20.988 -21.754  1.00116.09      A    C  
ANISOU  356  CA  LEU A  51    14001  15076  15031   1234      1  -1359  A    C  
ATOM    357  C   LEU A  51      41.578 -21.221 -22.938  1.00124.39      A    C  
ANISOU  357  C   LEU A  51    15091  16140  16031   1156     27  -1513  A    C  
ATOM    358  O   LEU A  51      42.052 -21.436 -24.063  1.00133.80      A    O  
ANISOU  358  O   LEU A  51    16233  17439  17168   1160     83  -1664  A    O  
ATOM    359  CB  LEU A  51      42.203 -21.874 -20.549  1.00124.06      A    C  
ANISOU  359  CB  LEU A  51    15066  15856  16214   1310    -22  -1278  A    C  
ATOM    360  CG  LEU A  51      43.348 -21.842 -19.527  1.00124.69      A    C  
ANISOU  360  CG  LEU A  51    15089  15944  16343   1410    -49  -1151  A    C  
ATOM    361  CD1 LEU A  51      43.106 -22.755 -18.318  1.00123.52      A    C  
ANISOU  361  CD1 LEU A  51    15004  15571  16356   1496    -74  -1055  A    C  
ATOM    362  CD2 LEU A  51      44.657 -22.190 -20.224  1.00122.81      A    C  
ANISOU  362  CD2 LEU A  51    14729  15810  16123   1502      4  -1261  A    C  
ATOM    363  N   MET A  52      40.266 -21.177 -22.702  1.00113.85      A    N  
ANISOU  363  N   MET A  52    13842  14704  14713   1082    -13  -1481  A    N  
ATOM    364  CA  MET A  52      39.298 -21.389 -23.787  1.00111.67      A    C  
ANISOU  364  CA  MET A  52    13596  14447  14387   1003     -6  -1626  A    C  
ATOM    365  C   MET A  52      39.073 -22.856 -24.212  1.00121.76      A    C  
ANISOU  365  C   MET A  52    14879  15579  15804   1058     53  -1809  A    C  
ATOM    366  O   MET A  52      38.544 -23.099 -25.297  1.00114.65      A    O  
ANISOU  366  O   MET A  52    13983  14733  14847    997     71  -1967  A    O  
ATOM    367  CB  MET A  52      39.710 -20.589 -25.033  1.00 97.20      A    C  
ANISOU  367  CB  MET A  52    11716  12855  12359    942      9  -1694  A    C  
ATOM    368  CG  MET A  52      39.512 -19.095 -24.930  1.00 95.56      A    C  
ANISOU  368  CG  MET A  52    11520  12787  12000    852    -42  -1543  A    C  
ATOM    369  SD  MET A  52      37.780 -18.597 -24.975  1.00132.51      A    S  
ANISOU  369  SD  MET A  52    16278  17420  16649    734   -116  -1493  A    S  
ATOM    370  CE  MET A  52      37.269 -19.298 -26.542  1.00189.75      A    C  
ANISOU  370  CE  MET A  52    23525  24740  23831    696   -100  -1724  A    C  
ATOM    371  N   GLU A  53      39.460 -23.822 -23.378  1.00141.20      A    N  
ANISOU  371  N   GLU A  53    17344  17859  18446   1168     85  -1790  A    N  
ATOM    372  CA  GLU A  53      39.491 -25.228 -23.816  1.00158.84      A    C  
ANISOU  372  CA  GLU A  53    19569  19955  20826   1234    166  -1969  A    C  
ATOM    373  C   GLU A  53      38.261 -25.587 -24.652  1.00162.13      A    C  
ANISOU  373  C   GLU A  53    20030  20344  21229   1135    174  -2128  A    C  
ATOM    374  O   GLU A  53      38.349 -25.715 -25.874  1.00165.80      A    O  
ANISOU  374  O   GLU A  53    20460  20931  21606   1093    213  -2301  A    O  
ATOM    375  CB  GLU A  53      39.711 -26.212 -22.645  1.00167.27      A    C  
ANISOU  375  CB  GLU A  53    20662  20786  22109   1355    189  -1894  A    C  
ATOM    376  CG  GLU A  53      38.497 -26.499 -21.758  1.00172.89      A    C  
ANISOU  376  CG  GLU A  53    21476  21293  22921   1320    162  -1817  A    C  
ATOM    377  CD  GLU A  53      38.171 -25.367 -20.793  1.00174.90      A    C  
ANISOU  377  CD  GLU A  53    21776  21586  23091   1261     75  -1603  A    C  
ATOM    378  OE1 GLU A  53      39.112 -24.768 -20.228  1.00175.63      A    O  
ANISOU  378  OE1 GLU A  53    21831  21770  23130   1308     42  -1468  A    O  
ATOM    379  OE2 GLU A  53      36.970 -25.087 -20.585  1.00173.52      A    O1-
ANISOU  379  OE2 GLU A  53    21671  21347  22912   1165     44  -1577  A    O1-
ATOM    380  N   ASN A  54      37.117 -25.734 -23.998  1.00159.78      A    N  
ANISOU  380  N   ASN A  54    19807  19891  21012   1092    140  -2073  A    N  
ATOM    381  CA  ASN A  54      35.859 -25.858 -24.713  1.00159.98      A    C  
ANISOU  381  CA  ASN A  54    19864  19910  21009    982    126  -2202  A    C  
ATOM    382  C   ASN A  54      35.140 -24.512 -24.710  1.00149.66      A    C  
ANISOU  382  C   ASN A  54    18579  18738  19549    872     28  -2078  A    C  
ATOM    383  O   ASN A  54      35.044 -23.849 -25.749  1.00148.95      A    O  
ANISOU  383  O   ASN A  54    18460  18848  19286    798     -4  -2136  A    O  
ATOM    384  CB  ASN A  54      34.990 -26.971 -24.116  1.00165.41      A    C  
ANISOU  384  CB  ASN A  54    20612  20330  21906    998    167  -2255  A    C  
ATOM    385  CG  ASN A  54      35.122 -27.075 -22.608  1.00165.69      A    C  
ANISOU  385  CG  ASN A  54    20700  20183  22070   1072    161  -2059  A    C  
ATOM    386  ND2 ASN A  54      35.781 -28.135 -22.147  1.00165.98      A    N  
ANISOU  386  ND2 ASN A  54    20736  20058  22269   1194    235  -2075  A    N  
ATOM    387  OD1 ASN A  54      34.632 -26.219 -21.865  1.00162.55      A    O  
ANISOU  387  OD1 ASN A  54    20345  19789  21628   1019     93  -1895  A    O  
ATOM    388  N   GLU A  55      34.658 -24.109 -23.535  1.00134.97      A    N  
ANISOU  388  N   GLU A  55    16770  16763  17751    862    -14  -1903  A    N  
ATOM    389  CA  GLU A  55      34.041 -22.802 -23.356  1.00118.11      A    C  
ANISOU  389  CA  GLU A  55    14651  14727  15497    767    -93  -1763  A    C  
ATOM    390  C   GLU A  55      32.933 -22.567 -24.387  1.00113.71      A    C  
ANISOU  390  C   GLU A  55    14090  14255  14861    658   -137  -1876  A    C  
ATOM    391  O   GLU A  55      33.128 -21.922 -25.420  1.00114.74      A    O  
ANISOU  391  O   GLU A  55    14180  14597  14817    614   -165  -1918  A    O  
ATOM    392  CB  GLU A  55      35.105 -21.696 -23.413  1.00109.80      A    C  
ANISOU  392  CB  GLU A  55    13554  13876  14290    779   -114  -1644  A    C  
ATOM    393  CG  GLU A  55      36.198 -21.813 -22.352  1.00102.40      A    C  
ANISOU  393  CG  GLU A  55    12608  12879  13420    879    -90  -1523  A    C  
ATOM    394  CD  GLU A  55      35.661 -21.789 -20.918  1.00105.93      A    C  
ANISOU  394  CD  GLU A  55    13126  13143  13981    878   -111  -1367  A    C  
ATOM    395  OE1 GLU A  55      34.511 -21.333 -20.698  1.00101.19      A    O  
ANISOU  395  OE1 GLU A  55    12574  12492  13383    785   -146  -1322  A    O  
ATOM    396  OE2 GLU A  55      36.402 -22.221 -20.004  1.00109.69      A    O1-
ANISOU  396  OE2 GLU A  55    13608  13528  14540    970    -94  -1287  A    O1-
ATOM    397  N   LYS A  56      31.757 -23.096 -24.092  1.00108.47      A    N  
ANISOU  397  N   LYS A  56    13466  13425  14323    615   -142  -1925  A    N  
ATOM    398  CA  LYS A  56      30.659 -23.054 -25.038  1.00107.23      A    C  
ANISOU  398  CA  LYS A  56    13294  13331  14116    518   -188  -2052  A    C  
ATOM    399  C   LYS A  56      29.678 -21.954 -24.653  1.00 95.36      A    C  
ANISOU  399  C   LYS A  56    11807  11846  12581    431   -269  -1907  A    C  
ATOM    400  O   LYS A  56      28.572 -21.876 -25.171  1.00 97.03      A    O  
ANISOU  400  O   LYS A  56    12006  12073  12788    350   -320  -1980  A    O  
ATOM    401  CB  LYS A  56      29.994 -24.431 -25.099  1.00117.71      A    C  
ANISOU  401  CB  LYS A  56    14640  14468  15617    520   -131  -2236  A    C  
ATOM    402  CG  LYS A  56      30.963 -25.533 -25.568  1.00124.76      A    C  
ANISOU  402  CG  LYS A  56    15511  15339  16553    605    -38  -2393  A    C  
ATOM    403  CD  LYS A  56      30.689 -26.890 -24.921  1.00128.47      A    C  
ANISOU  403  CD  LYS A  56    16020  15532  17260    657     53  -2477  A    C  
ATOM    404  CE  LYS A  56      31.769 -27.905 -25.293  1.00132.83      A    C  
ANISOU  404  CE  LYS A  56    16545  16052  17872    756    154  -2605  A    C  
ATOM    405  NZ  LYS A  56      31.536 -29.252 -24.690  1.00134.59      A    N1+
ANISOU  405  NZ  LYS A  56    16808  15994  18336    814    255  -2683  A    N1+
ATOM    406  N   GLU A  57      30.120 -21.086 -23.753  1.00 81.02      A    N  
ANISOU  406  N   GLU A  57    10009  10032  10743    447   -278  -1705  A    N  
ATOM    407  CA  GLU A  57      29.301 -20.000 -23.257  1.00 61.81      A    C  
ANISOU  407  CA  GLU A  57     7589   7598   8296    370   -334  -1554  A    C  
ATOM    408  C   GLU A  57      29.971 -18.650 -23.474  1.00 62.20      A    C  
ANISOU  408  C   GLU A  57     7610   7852   8170    355   -367  -1413  A    C  
ATOM    409  O   GLU A  57      29.805 -17.727 -22.661  1.00 58.71      A    O  
ANISOU  409  O   GLU A  57     7188   7386   7735    321   -379  -1243  A    O  
ATOM    410  CB  GLU A  57      29.024 -20.192 -21.765  1.00 59.19      A    C  
ANISOU  410  CB  GLU A  57     7322   7039   8130    382   -297  -1437  A    C  
ATOM    411  CG  GLU A  57      27.879 -21.108 -21.457  1.00 76.69      A    C  
ANISOU  411  CG  GLU A  57     9574   9042  10524    351   -275  -1535  A    C  
ATOM    412  CD  GLU A  57      26.594 -20.658 -22.137  1.00 88.93      A    C  
ANISOU  412  CD  GLU A  57    11088  10642  12059    250   -342  -1592  A    C  
ATOM    413  OE1 GLU A  57      26.340 -19.433 -22.180  1.00 91.97      A    O  
ANISOU  413  OE1 GLU A  57    11451  11139  12353    196   -398  -1466  A    O  
ATOM    414  OE2 GLU A  57      25.843 -21.525 -22.628  1.00 87.07      A    O1-
ANISOU  414  OE2 GLU A  57    10841  10333  11908    225   -337  -1763  A    O1-
ATOM    415  N   GLY A  58      30.734 -18.525 -24.558  1.00 65.86      A    N  
ANISOU  415  N   GLY A  58     8032   8513   8480    373   -369  -1486  A    N  
ATOM    416  CA  GLY A  58      31.378 -17.253 -24.865  1.00 63.26      A    C  
ANISOU  416  CA  GLY A  58     7676   8379   7979    355   -386  -1363  A    C  
ATOM    417  C   GLY A  58      32.660 -17.024 -24.072  1.00 72.58      A    C  
ANISOU  417  C   GLY A  58     8855   9564   9157    421   -333  -1259  A    C  
ATOM    418  O   GLY A  58      33.325 -17.990 -23.658  1.00 70.85      A    O  
ANISOU  418  O   GLY A  58     8639   9248   9031    502   -285  -1318  A    O  
ATOM    419  N   PHE A  59      33.023 -15.757 -23.871  1.00 69.95      A    N  
ANISOU  419  N   PHE A  59     8510   9343   8724    388   -341  -1107  A    N  
ATOM    420  CA  PHE A  59      34.226 -15.450 -23.107  1.00 67.34      A    C  
ANISOU  420  CA  PHE A  59     8168   9034   8386    438   -297  -1011  A    C  
ATOM    421  C   PHE A  59      34.051 -15.966 -21.691  1.00 66.59      A    C  
ANISOU  421  C   PHE A  59     8117   8729   8456    468   -285   -942  A    C  
ATOM    422  O   PHE A  59      33.028 -15.723 -21.064  1.00 76.18      A    O  
ANISOU  422  O   PHE A  59     9374   9822   9748    409   -305   -873  A    O  
ATOM    423  CB  PHE A  59      34.518 -13.948 -23.084  1.00 66.80      A    C  
ANISOU  423  CB  PHE A  59     8081   9108   8193    380   -298   -863  A    C  
ATOM    424  CG  PHE A  59      35.886 -13.615 -22.562  1.00 70.48      A    C  
ANISOU  424  CG  PHE A  59     8514   9642   8623    426   -251   -798  A    C  
ATOM    425  CD1 PHE A  59      37.003 -13.745 -23.373  1.00 63.86      A    C  
ANISOU  425  CD1 PHE A  59     7623   8953   7687    475   -214   -883  A    C  
ATOM    426  CD2 PHE A  59      36.062 -13.203 -21.254  1.00 78.19      A    C  
ANISOU  426  CD2 PHE A  59     9508  10535   9666    418   -241   -664  A    C  
ATOM    427  CE1 PHE A  59      38.257 -13.455 -22.896  1.00 64.81      A    C  
ANISOU  427  CE1 PHE A  59     7700   9139   7788    517   -173   -833  A    C  
ATOM    428  CE2 PHE A  59      37.325 -12.914 -20.773  1.00 77.10      A    C  
ANISOU  428  CE2 PHE A  59     9329  10472   9493    457   -207   -614  A    C  
ATOM    429  CZ  PHE A  59      38.425 -13.047 -21.601  1.00 68.42      A    C  
ANISOU  429  CZ  PHE A  59     8167   9521   8308    510   -175   -700  A    C  
ATOM    430  N   PRO A  60      35.046 -16.700 -21.188  1.00 59.79      A    N  
ANISOU  430  N   PRO A  60     7246   7820   7651    561   -249   -960  A    N  
ATOM    431  CA  PRO A  60      34.878 -17.446 -19.939  1.00 58.56      A    C  
ANISOU  431  CA  PRO A  60     7143   7453   7652    603   -239   -912  A    C  
ATOM    432  C   PRO A  60      34.595 -16.553 -18.760  1.00 65.12      A    C  
ANISOU  432  C   PRO A  60     8015   8232   8494    543   -250   -736  A    C  
ATOM    433  O   PRO A  60      35.338 -15.615 -18.489  1.00 66.27      A    O  
ANISOU  433  O   PRO A  60     8131   8501   8549    527   -247   -636  A    O  
ATOM    434  CB  PRO A  60      36.211 -18.160 -19.766  1.00 56.54      A    C  
ANISOU  434  CB  PRO A  60     6850   7212   7422    721   -207   -943  A    C  
ATOM    435  CG  PRO A  60      36.749 -18.260 -21.152  1.00 66.80      A    C  
ANISOU  435  CG  PRO A  60     8084   8674   8622    739   -188  -1084  A    C  
ATOM    436  CD  PRO A  60      36.312 -17.022 -21.860  1.00 67.41      A    C  
ANISOU  436  CD  PRO A  60     8150   8914   8550    636   -215  -1046  A    C  
ATOM    437  N   ILE A  61      33.512 -16.855 -18.057  1.00 68.22      A    N  
ANISOU  437  N   ILE A  61     8476   8440   9005    502   -252   -708  A    N  
ATOM    438  CA  ILE A  61      33.099 -16.032 -16.933  1.00 69.45      A    C  
ANISOU  438  CA  ILE A  61     8679   8529   9180    428   -251   -555  A    C  
ATOM    439  C   ILE A  61      34.194 -15.951 -15.846  1.00 73.57      A    C  
ANISOU  439  C   ILE A  61     9209   9055   9688    477   -239   -445  A    C  
ATOM    440  O   ILE A  61      34.455 -14.883 -15.308  1.00 82.72      A    O  
ANISOU  440  O   ILE A  61    10363  10290  10779    417   -236   -329  A    O  
ATOM    441  CB  ILE A  61      31.735 -16.506 -16.392  1.00 61.22      A    C  
ANISOU  441  CB  ILE A  61     7709   7270   8280    376   -242   -565  A    C  
ATOM    442  CG1 ILE A  61      31.056 -15.437 -15.550  1.00 66.61      A    C  
ANISOU  442  CG1 ILE A  61     8429   7907   8972    268   -234   -429  A    C  
ATOM    443  CG2 ILE A  61      31.866 -17.796 -15.636  1.00 60.03      A    C  
ANISOU  443  CG2 ILE A  61     7619   6932   8257    455   -214   -590  A    C  
ATOM    444  CD1 ILE A  61      29.698 -15.874 -15.086  1.00 69.87      A    C  
ANISOU  444  CD1 ILE A  61     8906   8109   9533    211   -216   -451  A    C  
ATOM    445  N   THR A  62      34.864 -17.059 -15.559  1.00 67.13      A    N  
ANISOU  445  N   THR A  62     8400   8168   8938    587   -232   -484  A    N  
ATOM    446  CA  THR A  62      35.895 -17.038 -14.537  1.00 72.33      A    C  
ANISOU  446  CA  THR A  62     9059   8838   9583    642   -236   -378  A    C  
ATOM    447  C   THR A  62      37.093 -16.184 -14.947  1.00 74.91      A    C  
ANISOU  447  C   THR A  62     9292   9394   9775    653   -245   -356  A    C  
ATOM    448  O   THR A  62      37.823 -15.710 -14.091  1.00 74.83      A    O  
ANISOU  448  O   THR A  62     9270   9436   9724    654   -255   -252  A    O  
ATOM    449  CB  THR A  62      36.372 -18.446 -14.168  1.00 77.32      A    C  
ANISOU  449  CB  THR A  62     9712   9338  10326    771   -230   -414  A    C  
ATOM    450  CG2 THR A  62      35.181 -19.313 -13.805  1.00 79.29      A    C  
ANISOU  450  CG2 THR A  62    10059   9352  10716    756   -205   -445  A    C  
ATOM    451  OG1 THR A  62      37.084 -19.025 -15.271  1.00 71.55      A    O  
ANISOU  451  OG1 THR A  62     8901   8699   9587    859   -221   -547  A    O  
ATOM    452  N   ALA A  63      37.295 -15.991 -16.249  1.00 69.72      A    N  
ANISOU  452  N   ALA A  63     8567   8877   9046    655   -238   -460  A    N  
ATOM    453  CA  ALA A  63      38.343 -15.079 -16.724  1.00 62.74      A    C  
ANISOU  453  CA  ALA A  63     7598   8210   8031    648   -230   -445  A    C  
ATOM    454  C   ALA A  63      37.950 -13.633 -16.528  1.00 70.95      A    C  
ANISOU  454  C   ALA A  63     8645   9329   8984    524   -224   -341  A    C  
ATOM    455  O   ALA A  63      38.798 -12.811 -16.214  1.00 72.11      A    O  
ANISOU  455  O   ALA A  63     8745   9600   9053    504   -212   -273  A    O  
ATOM    456  CB  ALA A  63      38.663 -15.316 -18.190  1.00 56.29      A    C  
ANISOU  456  CB  ALA A  63     6718   7515   7153    681   -213   -588  A    C  
ATOM    457  N   LEU A  64      36.672 -13.321 -16.755  1.00 69.82      A    N  
ANISOU  457  N   LEU A  64     8552   9115   8862    441   -227   -335  A    N  
ATOM    458  CA  LEU A  64      36.153 -11.987 -16.490  1.00 71.56      A    C  
ANISOU  458  CA  LEU A  64     8784   9374   9032    323   -213   -228  A    C  
ATOM    459  C   LEU A  64      36.322 -11.633 -15.021  1.00 69.67      A    C  
ANISOU  459  C   LEU A  64     8583   9061   8825    285   -201   -106  A    C  
ATOM    460  O   LEU A  64      36.622 -10.495 -14.662  1.00 66.69      A    O  
ANISOU  460  O   LEU A  64     8186   8772   8381    211   -173    -19  A    O  
ATOM    461  CB  LEU A  64      34.672 -11.917 -16.828  1.00 64.28      A    C  
ANISOU  461  CB  LEU A  64     7907   8350   8167    255   -225   -244  A    C  
ATOM    462  CG  LEU A  64      34.336 -11.972 -18.305  1.00 63.34      A    C  
ANISOU  462  CG  LEU A  64     7750   8330   7986    260   -246   -347  A    C  
ATOM    463  CD1 LEU A  64      32.860 -11.919 -18.398  1.00 54.70      A    C  
ANISOU  463  CD1 LEU A  64     6693   7122   6968    193   -269   -348  A    C  
ATOM    464  CD2 LEU A  64      34.978 -10.830 -19.096  1.00 59.37      A    C  
ANISOU  464  CD2 LEU A  64     7189   8038   7332    228   -227   -313  A    C  
ATOM    465  N   ARG A  65      36.093 -12.628 -14.181  1.00 59.73      A    N  
ANISOU  465  N   ARG A  65     7387   7638   7670    332   -215   -102  A    N  
ATOM    466  CA  ARG A  65      36.222 -12.493 -12.748  1.00 63.22      A    C  
ANISOU  466  CA  ARG A  65     7883   7998   8138    302   -210      8  A    C  
ATOM    467  C   ARG A  65      37.672 -12.127 -12.424  1.00 67.96      A    C  
ANISOU  467  C   ARG A  65     8415   8759   8649    341   -218     49  A    C  
ATOM    468  O   ARG A  65      37.933 -11.141 -11.740  1.00 74.77      A    O  
ANISOU  468  O   ARG A  65     9272   9685   9452    259   -199    137  A    O  
ATOM    469  CB  ARG A  65      35.830 -13.840 -12.110  1.00 67.48      A    C  
ANISOU  469  CB  ARG A  65     8501   8336   8800    371   -224     -9  A    C  
ATOM    470  CG  ARG A  65      35.673 -13.871 -10.598  1.00 67.33      A    C  
ANISOU  470  CG  ARG A  65     8571   8194   8817    332   -217    106  A    C  
ATOM    471  CD  ARG A  65      35.289 -15.275 -10.121  1.00 81.35      A    C  
ANISOU  471  CD  ARG A  65    10430   9765  10716    412   -221     84  A    C  
ATOM    472  NE  ARG A  65      36.310 -16.250 -10.486  1.00107.86      A    N  
ANISOU  472  NE  ARG A  65    13736  13162  14086    561   -252     30  A    N  
ATOM    473  CZ  ARG A  65      36.295 -17.529 -10.123  1.00117.85      A    C  
ANISOU  473  CZ  ARG A  65    15054  14268  15455    659   -254     15  A    C  
ATOM    474  NH1 ARG A  65      35.298 -17.995  -9.374  1.00117.94      A    N1+
ANISOU  474  NH1 ARG A  65    15182  14071  15559    619   -224     50  A    N1+
ATOM    475  NH2 ARG A  65      37.282 -18.336 -10.510  1.00117.15      A    N  
ANISOU  475  NH2 ARG A  65    14904  14223  15387    797   -275    -34  A    N  
ATOM    476  N   GLU A  66      38.612 -12.923 -12.939  1.00 66.26      A    N  
ANISOU  476  N   GLU A  66     8139   8607   8431    463   -242    -26  A    N  
ATOM    477  CA  GLU A  66      40.032 -12.716 -12.696  1.00 65.27      A    C  
ANISOU  477  CA  GLU A  66     7930   8630   8239    517   -255     -5  A    C  
ATOM    478  C   GLU A  66      40.471 -11.339 -13.187  1.00 68.81      A    C  
ANISOU  478  C   GLU A  66     8306   9268   8569    430   -218      9  A    C  
ATOM    479  O   GLU A  66      41.091 -10.579 -12.457  1.00 73.71      A    O  
ANISOU  479  O   GLU A  66     8898   9973   9133    381   -211     82  A    O  
ATOM    480  CB  GLU A  66      40.847 -13.807 -13.373  1.00 71.63      A    C  
ANISOU  480  CB  GLU A  66     8672   9462   9082    662   -273   -107  A    C  
ATOM    481  CG  GLU A  66      42.320 -13.829 -13.009  1.00 79.67      A    C  
ANISOU  481  CG  GLU A  66     9597  10607  10068    740   -296    -88  A    C  
ATOM    482  CD  GLU A  66      43.140 -14.718 -13.938  1.00 89.31      A    C  
ANISOU  482  CD  GLU A  66    10733  11875  11326    871   -292   -209  A    C  
ATOM    483  OE1 GLU A  66      42.557 -15.488 -14.737  1.00 94.37      A    O  
ANISOU  483  OE1 GLU A  66    11402  12429  12026    908   -273   -307  A    O  
ATOM    484  OE2 GLU A  66      44.382 -14.646 -13.874  1.00 95.32      A    O1-
ANISOU  484  OE2 GLU A  66    11393  12762  12062    933   -302   -214  A    O1-
ATOM    485  N   ILE A  67      40.126 -11.008 -14.422  1.00 63.94      A    N  
ANISOU  485  N   ILE A  67     7664   8717   7913    407   -190    -61  A    N  
ATOM    486  CA  ILE A  67      40.414  -9.686 -14.950  1.00 57.07      A    C  
ANISOU  486  CA  ILE A  67     6741   8007   6935    321   -143    -39  A    C  
ATOM    487  C   ILE A  67      39.791  -8.561 -14.133  1.00 62.42      A    C  
ANISOU  487  C   ILE A  67     7464   8650   7602    188   -111     75  A    C  
ATOM    488  O   ILE A  67      40.350  -7.484 -14.044  1.00 65.78      A    O  
ANISOU  488  O   ILE A  67     7841   9198   7953    120    -66    117  A    O  
ATOM    489  CB  ILE A  67      39.936  -9.547 -16.380  1.00 58.62      A    C  
ANISOU  489  CB  ILE A  67     6926   8260   7087    312   -125   -116  A    C  
ATOM    490  CG1 ILE A  67      40.774 -10.437 -17.291  1.00 60.09      A    C  
ANISOU  490  CG1 ILE A  67     7051   8522   7258    425   -131   -241  A    C  
ATOM    491  CG2 ILE A  67      40.024  -8.085 -16.833  1.00 53.77      A    C  
ANISOU  491  CG2 ILE A  67     6279   7782   6369    212    -69    -63  A    C  
ATOM    492  CD1 ILE A  67      40.250 -10.456 -18.697  1.00 62.60      A    C  
ANISOU  492  CD1 ILE A  67     7371   8891   7522    415   -121   -329  A    C  
ATOM    493  N   LYS A  68      38.627  -8.788 -13.547  1.00 68.72      A    N  
ANISOU  493  N   LYS A  68     8351   9276   8482    144   -122    117  A    N  
ATOM    494  CA  LYS A  68      38.029  -7.744 -12.725  1.00 69.26      A    C  
ANISOU  494  CA  LYS A  68     8462   9299   8555     13    -78    217  A    C  
ATOM    495  C   LYS A  68      38.905  -7.541 -11.502  1.00 76.03      A    C  
ANISOU  495  C   LYS A  68     9311  10194   9383     -5    -77    279  A    C  
ATOM    496  O   LYS A  68      39.279  -6.418 -11.157  1.00 77.50      A    O  
ANISOU  496  O   LYS A  68     9465  10472   9508    -98    -27    330  A    O  
ATOM    497  CB  LYS A  68      36.627  -8.132 -12.287  1.00 67.55      A    C  
ANISOU  497  CB  LYS A  68     8340   8878   8447    -28    -84    239  A    C  
ATOM    498  CG  LYS A  68      35.916  -7.086 -11.472  1.00 67.58      A    C  
ANISOU  498  CG  LYS A  68     8388   8816   8474   -168    -26    332  A    C  
ATOM    499  CD  LYS A  68      34.640  -7.636 -10.892  1.00 72.51      A    C  
ANISOU  499  CD  LYS A  68     9105   9225   9219   -200    -28    344  A    C  
ATOM    500  CE  LYS A  68      34.926  -8.846 -10.013  1.00 73.09      A    C  
ANISOU  500  CE  LYS A  68     9240   9196   9335   -126    -68    339  A    C  
ATOM    501  NZ  LYS A  68      33.651  -9.501  -9.617  1.00 77.41      A    N1+
ANISOU  501  NZ  LYS A  68     9880   9526  10008   -150    -60    332  A    N1+
ATOM    502  N   ILE A  69      39.251  -8.646 -10.860  1.00 68.58      A    N  
ANISOU  502  N   ILE A  69     8395   9181   8482     85   -133    273  A    N  
ATOM    503  CA  ILE A  69      40.023  -8.587  -9.633  1.00 65.08      A    C  
ANISOU  503  CA  ILE A  69     7952   8769   8007     76   -153    338  A    C  
ATOM    504  C   ILE A  69      41.436  -7.999  -9.811  1.00 64.51      A    C  
ANISOU  504  C   ILE A  69     7760   8911   7840     91   -150    322  A    C  
ATOM    505  O   ILE A  69      41.871  -7.154  -9.021  1.00 63.69      A    O  
ANISOU  505  O   ILE A  69     7638   8884   7678      2   -127    377  A    O  
ATOM    506  CB  ILE A  69      40.037  -9.956  -8.966  1.00 63.21      A    C  
ANISOU  506  CB  ILE A  69     7776   8402   7841    182   -218    347  A    C  
ATOM    507  CG1 ILE A  69      38.593 -10.296  -8.527  1.00 65.29      A    C  
ANISOU  507  CG1 ILE A  69     8166   8447   8196    126   -198    376  A    C  
ATOM    508  CG2 ILE A  69      41.015  -9.963  -7.810  1.00 60.86      A    C  
ANISOU  508  CG2 ILE A  69     7461   8170   7491    195   -260    416  A    C  
ATOM    509  CD1 ILE A  69      38.330 -11.775  -8.186  1.00 61.09      A    C  
ANISOU  509  CD1 ILE A  69     7706   7747   7759    236   -242    365  A    C  
ATOM    510  N   LEU A  70      42.142  -8.420 -10.856  1.00 58.47      A    N  
ANISOU  510  N   LEU A  70     6912   8242   7062    194   -165    236  A    N  
ATOM    511  CA  LEU A  70      43.449  -7.853 -11.143  1.00 55.73      A    C  
ANISOU  511  CA  LEU A  70     6444   8095   6636    206   -149    206  A    C  
ATOM    512  C   LEU A  70      43.369  -6.338 -11.366  1.00 58.93      A    C  
ANISOU  512  C   LEU A  70     6823   8599   6967     63    -61    232  A    C  
ATOM    513  O   LEU A  70      44.258  -5.613 -10.976  1.00 62.74      A    O  
ANISOU  513  O   LEU A  70     7234   9214   7391     15    -36    244  A    O  
ATOM    514  CB  LEU A  70      44.091  -8.534 -12.341  1.00 53.99      A    C  
ANISOU  514  CB  LEU A  70     6146   7947   6421    328   -158     98  A    C  
ATOM    515  CG  LEU A  70      44.346 -10.024 -12.147  1.00 59.66      A    C  
ANISOU  515  CG  LEU A  70     6871   8572   7226    478   -230     65  A    C  
ATOM    516  CD1 LEU A  70      44.539 -10.717 -13.504  1.00 56.13      A    C  
ANISOU  516  CD1 LEU A  70     6377   8148   6800    574   -215    -58  A    C  
ATOM    517  CD2 LEU A  70      45.523 -10.269 -11.181  1.00 51.79      A    C  
ANISOU  517  CD2 LEU A  70     5806   7647   6225    540   -286    104  A    C  
ATOM    518  N   GLN A  71      42.299  -5.868 -11.987  1.00 54.90      A    N  
ANISOU  518  N   GLN A  71     6367   8023   6469     -3    -14    241  A    N  
ATOM    519  CA  GLN A  71      42.142  -4.447 -12.262  1.00 54.15      A    C  
ANISOU  519  CA  GLN A  71     6252   8002   6320   -129     77    276  A    C  
ATOM    520  C   GLN A  71      41.873  -3.632 -11.006  1.00 59.64      A    C  
ANISOU  520  C   GLN A  71     6987   8654   7019   -259    117    361  A    C  
ATOM    521  O   GLN A  71      42.153  -2.433 -10.949  1.00 65.34      A    O  
ANISOU  521  O   GLN A  71     7670   9463   7694   -364    200    386  A    O  
ATOM    522  CB  GLN A  71      41.026  -4.225 -13.283  1.00 47.75      A    C  
ANISOU  522  CB  GLN A  71     5486   7128   5527   -151    103    272  A    C  
ATOM    523  CG  GLN A  71      41.438  -4.686 -14.655  1.00 54.61      A    C  
ANISOU  523  CG  GLN A  71     6306   8090   6354    -57     89    182  A    C  
ATOM    524  CD  GLN A  71      40.338  -4.586 -15.665  1.00 63.87      A    C  
ANISOU  524  CD  GLN A  71     7523   9213   7532    -71     93    176  A    C  
ATOM    525  NE2 GLN A  71      40.719  -4.367 -16.915  1.00 69.30      A    N  
ANISOU  525  NE2 GLN A  71     8166  10026   8139    -45    119    123  A    N  
ATOM    526  OE1 GLN A  71      39.155  -4.706 -15.337  1.00 67.26      A    O  
ANISOU  526  OE1 GLN A  71     8024   9496   8036   -108     73    216  A    O  
ATOM    527  N   LEU A  72      41.332  -4.296 -10.002  1.00 61.43      A    N  
ANISOU  527  N   LEU A  72     7296   8742   7304   -256     67    400  A    N  
ATOM    528  CA  LEU A  72      40.940  -3.627  -8.786  1.00 65.51      A    C  
ANISOU  528  CA  LEU A  72     7867   9198   7825   -387    109    474  A    C  
ATOM    529  C   LEU A  72      42.099  -3.620  -7.816  1.00 69.14      A    C  
ANISOU  529  C   LEU A  72     8280   9770   8221   -391     77    484  A    C  
ATOM    530  O   LEU A  72      42.234  -2.689  -7.028  1.00 78.76      A    O  
ANISOU  530  O   LEU A  72     9497  11029   9400   -520    135    520  A    O  
ATOM    531  CB  LEU A  72      39.743  -4.329  -8.148  1.00 66.95      A    C  
ANISOU  531  CB  LEU A  72     8171   9170   8096   -395     82    512  A    C  
ATOM    532  CG  LEU A  72      39.524  -3.986  -6.676  1.00 56.91      A    C  
ANISOU  532  CG  LEU A  72     6970   7833   6821   -509    108    581  A    C  
ATOM    533  CD1 LEU A  72      38.807  -2.670  -6.594  1.00 44.86      A    C  
ANISOU  533  CD1 LEU A  72     5458   6274   5312   -669    223    616  A    C  
ATOM    534  CD2 LEU A  72      38.749  -5.091  -5.964  1.00 45.05      A    C  
ANISOU  534  CD2 LEU A  72     5584   6143   5392   -470     56    607  A    C  
ATOM    535  N   LEU A  73      42.921  -4.662  -7.870  1.00 67.06      A    N  
ANISOU  535  N   LEU A  73     7974   9555   7951   -250    -15    448  A    N  
ATOM    536  CA  LEU A  73      44.065  -4.797  -6.965  1.00 66.14      A    C  
ANISOU  536  CA  LEU A  73     7800   9552   7779   -230    -71    460  A    C  
ATOM    537  C   LEU A  73      45.328  -4.111  -7.491  1.00 69.38      A    C  
ANISOU  537  C   LEU A  73     8064  10175   8121   -231    -40    401  A    C  
ATOM    538  O   LEU A  73      46.024  -4.621  -8.370  1.00 73.99      A    O  
ANISOU  538  O   LEU A  73     8565  10835   8711   -112    -68    334  A    O  
ATOM    539  CB  LEU A  73      44.335  -6.269  -6.675  1.00 55.23      A    C  
ANISOU  539  CB  LEU A  73     6439   8105   6440    -71   -185    464  A    C  
ATOM    540  CG  LEU A  73      43.103  -6.885  -6.019  1.00 57.08      A    C  
ANISOU  540  CG  LEU A  73     6824   8123   6739    -89   -199    525  A    C  
ATOM    541  CD1 LEU A  73      43.379  -8.245  -5.354  1.00 56.25      A    C  
ANISOU  541  CD1 LEU A  73     6762   7940   6670     45   -303    559  A    C  
ATOM    542  CD2 LEU A  73      42.592  -5.902  -5.009  1.00 52.97      A    C  
ANISOU  542  CD2 LEU A  73     6371   7577   6180   -265   -138    589  A    C  
ATOM    543  N   LYS A  74      45.626  -2.944  -6.947  1.00 63.88      A    N  
ANISOU  543  N   LYS A  74     7335   9571   7366   -373     29    418  A    N  
ATOM    544  CA  LYS A  74      46.829  -2.221  -7.346  1.00 55.74      A    C  
ANISOU  544  CA  LYS A  74     6163   8739   6275   -392     72    357  A    C  
ATOM    545  C   LYS A  74      47.647  -1.926  -6.115  1.00 58.97      A    C  
ANISOU  545  C   LYS A  74     6524   9258   6624   -456     37    373  A    C  
ATOM    546  O   LYS A  74      47.278  -1.100  -5.290  1.00 65.21      A    O  
ANISOU  546  O   LYS A  74     7360  10032   7383   -609     96    411  A    O  
ATOM    547  CB  LYS A  74      46.458  -0.953  -8.103  1.00 48.36      A    C  
ANISOU  547  CB  LYS A  74     5219   7828   5328   -510    213    345  A    C  
ATOM    548  CG  LYS A  74      45.768  -1.248  -9.459  1.00 54.10      A    C  
ANISOU  548  CG  LYS A  74     5979   8481   6095   -437    234    325  A    C  
ATOM    549  CD  LYS A  74      46.679  -2.109 -10.320  1.00 64.80      A    C  
ANISOU  549  CD  LYS A  74     7248   9929   7445   -282    175    245  A    C  
ATOM    550  CE  LYS A  74      46.020  -2.559 -11.601  1.00 67.63      A    C  
ANISOU  550  CE  LYS A  74     7645  10221   7829   -207    181    214  A    C  
ATOM    551  NZ  LYS A  74      46.994  -3.339 -12.406  1.00 68.88      A    N1+
ANISOU  551  NZ  LYS A  74     7713  10476   7981    -71    144    122  A    N1+
ATOM    552  N   HIS A  75      48.757  -2.634  -5.974  1.00 63.58      A    N  
ANISOU  552  N   HIS A  75     7010   9952   7194   -339    -63    341  A    N  
ATOM    553  CA  HIS A  75      49.476  -2.605  -4.713  1.00 62.87      A    C  
ANISOU  553  CA  HIS A  75     6882   9960   7045   -375   -136    367  A    C  
ATOM    554  C   HIS A  75      50.847  -3.253  -4.859  1.00 64.60      A    C  
ANISOU  554  C   HIS A  75     6951  10330   7264   -233   -235    316  A    C  
ATOM    555  O   HIS A  75      51.019  -4.166  -5.663  1.00 68.49      A    O  
ANISOU  555  O   HIS A  75     7416  10787   7821    -75   -277    285  A    O  
ATOM    556  CB  HIS A  75      48.652  -3.320  -3.652  1.00 56.17      A    C  
ANISOU  556  CB  HIS A  75     6180   8957   6204   -372   -213    463  A    C  
ATOM    557  CG  HIS A  75      49.303  -3.344  -2.311  1.00 58.05      A    C  
ANISOU  557  CG  HIS A  75     6400   9293   6362   -412   -299    504  A    C  
ATOM    558  CD2 HIS A  75      49.002  -2.690  -1.165  1.00 52.38      A    C  
ANISOU  558  CD2 HIS A  75     5750   8581   5572   -574   -274    548  A    C  
ATOM    559  ND1 HIS A  75      50.412  -4.111  -2.043  1.00 62.25      A    N  
ANISOU  559  ND1 HIS A  75     6831   9941   6882   -276   -432    501  A    N  
ATOM    560  CE1 HIS A  75      50.771  -3.927  -0.781  1.00 67.82      A    C  
ANISOU  560  CE1 HIS A  75     7543  10729   7499   -351   -497    549  A    C  
ATOM    561  NE2 HIS A  75      49.929  -3.072  -0.225  1.00 57.86      A    N  
ANISOU  561  NE2 HIS A  75     6388   9404   6194   -538   -399    573  A    N  
ATOM    562  N   GLU A  76      51.823  -2.775  -4.088  1.00 65.53      A    N  
ANISOU  562  N   GLU A  76     6967  10618   7315   -292   -267    300  A    N  
ATOM    563  CA  GLU A  76      53.211  -3.202  -4.265  1.00 63.45      A    C  
ANISOU  563  CA  GLU A  76     6529  10519   7059   -172   -348    239  A    C  
ATOM    564  C   GLU A  76      53.419  -4.710  -4.067  1.00 69.00      A    C  
ANISOU  564  C   GLU A  76     7240  11156   7822     32   -502    286  A    C  
ATOM    565  O   GLU A  76      54.346  -5.303  -4.599  1.00 70.99      A    O  
ANISOU  565  O   GLU A  76     7361  11485   8127    175   -553    230  A    O  
ATOM    566  CB  GLU A  76      54.137  -2.430  -3.341  1.00 62.27      A    C  
ANISOU  566  CB  GLU A  76     6270  10563   6826   -283   -368    216  A    C  
ATOM    567  CG  GLU A  76      55.543  -2.369  -3.891  1.00 89.92      A    C  
ANISOU  567  CG  GLU A  76     9562  14257  10347   -211   -381    113  A    C  
ATOM    568  CD  GLU A  76      56.493  -1.600  -3.002  1.00115.24      A    C  
ANISOU  568  CD  GLU A  76    12643  17669  13474   -326   -404     75  A    C  
ATOM    569  OE1 GLU A  76      56.018  -0.976  -2.023  1.00126.52      A    O  
ANISOU  569  OE1 GLU A  76    14156  19093  14822   -483   -387    121  A    O  
ATOM    570  OE2 GLU A  76      57.714  -1.622  -3.283  1.00118.36      A    O1-
ANISOU  570  OE2 GLU A  76    12851  18230  13891   -263   -434    -10  A    O1-
ATOM    571  N   ASN A  77      52.546  -5.344  -3.310  1.00 68.08      A    N  
ANISOU  571  N   ASN A  77     7277  10883   7708     47   -565    388  A    N  
ATOM    572  CA  ASN A  77      52.696  -6.764  -3.097  1.00 67.14      A    C  
ANISOU  572  CA  ASN A  77     7176  10681   7652    238   -698    442  A    C  
ATOM    573  C   ASN A  77      51.701  -7.633  -3.870  1.00 67.84      A    C  
ANISOU  573  C   ASN A  77     7381  10556   7839    334   -669    450  A    C  
ATOM    574  O   ASN A  77      51.513  -8.800  -3.581  1.00 76.93      A    O  
ANISOU  574  O   ASN A  77     8594  11587   9050    468   -756    510  A    O  
ATOM    575  CB  ASN A  77      52.664  -7.014  -1.615  1.00 66.93      A    C  
ANISOU  575  CB  ASN A  77     7221  10653   7554    209   -808    554  A    C  
ATOM    576  CG  ASN A  77      53.707  -6.202  -0.907  1.00 73.55      A    C  
ANISOU  576  CG  ASN A  77     7928  11722   8293    117   -846    530  A    C  
ATOM    577  ND2 ASN A  77      54.905  -6.215  -1.457  1.00 67.58      A    N  
ANISOU  577  ND2 ASN A  77     6980  11128   7571    204   -874    447  A    N  
ATOM    578  OD1 ASN A  77      53.445  -5.546   0.102  1.00 81.83      A    O  
ANISOU  578  OD1 ASN A  77     9044  12808   9240    -39   -842    574  A    O  
ATOM    579  N   VAL A  78      51.083  -7.061  -4.883  1.00 59.73      A    N  
ANISOU  579  N   VAL A  78     6381   9486   6830    266   -545    387  A    N  
ATOM    580  CA  VAL A  78      50.215  -7.841  -5.719  1.00 61.15      A    C  
ANISOU  580  CA  VAL A  78     6649   9490   7096    351   -519    374  A    C  
ATOM    581  C   VAL A  78      50.709  -7.744  -7.140  1.00 66.84      A    C  
ANISOU  581  C   VAL A  78     7259  10286   7849    408   -452    258  A    C  
ATOM    582  O   VAL A  78      51.167  -6.696  -7.577  1.00 76.89      A    O  
ANISOU  582  O   VAL A  78     8447  11698   9068    314   -371    200  A    O  
ATOM    583  CB  VAL A  78      48.751  -7.381  -5.603  1.00 59.41      A    C  
ANISOU  583  CB  VAL A  78     6592   9112   6868    220   -442    419  A    C  
ATOM    584  CG1 VAL A  78      47.866  -8.140  -6.592  1.00 57.46      A    C  
ANISOU  584  CG1 VAL A  78     6419   8703   6711    302   -415    385  A    C  
ATOM    585  CG2 VAL A  78      48.256  -7.594  -4.180  1.00 49.18      A    C  
ANISOU  585  CG2 VAL A  78     5417   7727   5543    167   -501    529  A    C  
ATOM    586  N   VAL A  79      50.638  -8.853  -7.856  1.00 67.68      A    N  
ANISOU  586  N   VAL A  79     7370  10301   8046    559   -478    219  A    N  
ATOM    587  CA  VAL A  79      51.112  -8.888  -9.217  1.00 69.84      A    C  
ANISOU  587  CA  VAL A  79     7548  10642   8348    617   -414    101  A    C  
ATOM    588  C   VAL A  79      50.384  -7.777  -9.979  1.00 68.17      A    C  
ANISOU  588  C   VAL A  79     7385  10441   8075    471   -292     73  A    C  
ATOM    589  O   VAL A  79      49.367  -7.273  -9.524  1.00 65.16      A    O  
ANISOU  589  O   VAL A  79     7121   9971   7667    358   -266    142  A    O  
ATOM    590  CB  VAL A  79      50.872 -10.274  -9.819  1.00 74.64      A    C  
ANISOU  590  CB  VAL A  79     8185  11112   9062    779   -446     64  A    C  
ATOM    591  CG1 VAL A  79      49.402 -10.462 -10.134  1.00 71.42      A    C  
ANISOU  591  CG1 VAL A  79     7937  10524   8674    732   -408     84  A    C  
ATOM    592  CG2 VAL A  79      51.719 -10.471 -11.045  1.00 77.72      A    C  
ANISOU  592  CG2 VAL A  79     8446  11599   9484    862   -396    -65  A    C  
ATOM    593  N   ASN A  80      50.921  -7.367 -11.117  1.00 68.35      A    N  
ANISOU  593  N   ASN A  80     7318  10574   8078    472   -212    -25  A    N  
ATOM    594  CA  ASN A  80      50.416  -6.186 -11.804  1.00 58.88      A    C  
ANISOU  594  CA  ASN A  80     6149   9412   6810    334    -96    -38  A    C  
ATOM    595  C   ASN A  80      50.038  -6.428 -13.245  1.00 65.59      A    C  
ANISOU  595  C   ASN A  80     7019  10235   7666    375    -36   -115  A    C  
ATOM    596  O   ASN A  80      50.901  -6.588 -14.104  1.00 73.88      A    O  
ANISOU  596  O   ASN A  80     7970  11387   8715    438      0   -212  A    O  
ATOM    597  CB  ASN A  80      51.443  -5.062 -11.781  1.00 58.57      A    C  
ANISOU  597  CB  ASN A  80     5987   9562   6705    246    -27    -74  A    C  
ATOM    598  CG  ASN A  80      50.942  -3.805 -12.476  1.00 72.52      A    C  
ANISOU  598  CG  ASN A  80     7789  11358   8407    106    105    -75  A    C  
ATOM    599  ND2 ASN A  80      51.513  -3.510 -13.646  1.00 72.71      A    N  
ANISOU  599  ND2 ASN A  80     7740  11483   8403    120    189   -163  A    N  
ATOM    600  OD1 ASN A  80      50.047  -3.106 -11.968  1.00 75.02      A    O  
ANISOU  600  OD1 ASN A  80     8200  11603   8702    -13    137      4  A    O  
ATOM    601  N   LEU A  81      48.740  -6.416 -13.502  1.00 67.99      A    N  
ANISOU  601  N   LEU A  81     7451  10407   7974    330    -22    -76  A    N  
ATOM    602  CA  LEU A  81      48.211  -6.536 -14.844  1.00 65.71      A    C  
ANISOU  602  CA  LEU A  81     7196  10098   7672    346     29   -139  A    C  
ATOM    603  C   LEU A  81      48.462  -5.218 -15.536  1.00 65.74      A    C  
ANISOU  603  C   LEU A  81     7161  10232   7584    237    139   -151  A    C  
ATOM    604  O   LEU A  81      48.053  -4.177 -15.042  1.00 75.27      A    O  
ANISOU  604  O   LEU A  81     8404  11440   8757    113    183    -74  A    O  
ATOM    605  CB  LEU A  81      46.714  -6.821 -14.790  1.00 55.91      A    C  
ANISOU  605  CB  LEU A  81     6095   8683   6466    318      3    -85  A    C  
ATOM    606  CG  LEU A  81      46.030  -7.126 -16.112  1.00 63.78      A    C  
ANISOU  606  CG  LEU A  81     7134   9648   7452    342     28   -151  A    C  
ATOM    607  CD1 LEU A  81      46.474  -8.473 -16.666  1.00 67.76      A    C  
ANISOU  607  CD1 LEU A  81     7603  10129   8013    486    -11   -256  A    C  
ATOM    608  CD2 LEU A  81      44.547  -7.126 -15.870  1.00 71.00      A    C  
ANISOU  608  CD2 LEU A  81     8171  10405   8402    285      6    -85  A    C  
ATOM    609  N   ILE A  82      49.170  -5.272 -16.659  1.00 65.18      A    N  
ANISOU  609  N   ILE A  82     7019  10269   7477    281    194   -249  A    N  
ATOM    610  CA  ILE A  82      49.542  -4.091 -17.424  1.00 65.36      A    C  
ANISOU  610  CA  ILE A  82     7003  10421   7410    190    311   -267  A    C  
ATOM    611  C   ILE A  82      48.470  -3.792 -18.444  1.00 65.16      A    C  
ANISOU  611  C   ILE A  82     7077  10350   7332    147    351   -250  A    C  
ATOM    612  O   ILE A  82      48.092  -2.641 -18.648  1.00 61.75      A    O  
ANISOU  612  O   ILE A  82     6676   9946   6841     38    429   -187  A    O  
ATOM    613  CB  ILE A  82      50.832  -4.340 -18.221  1.00 62.17      A    C  
ANISOU  613  CB  ILE A  82     6478  10155   6989    258    361   -390  A    C  
ATOM    614  CG1 ILE A  82      51.995  -4.572 -17.290  1.00 63.04      A    C  
ANISOU  614  CG1 ILE A  82     6465  10334   7154    304    319   -413  A    C  
ATOM    615  CG2 ILE A  82      51.155  -3.171 -19.142  1.00 55.35      A    C  
ANISOU  615  CG2 ILE A  82     5591   9414   6026    164    497   -412  A    C  
ATOM    616  CD1 ILE A  82      53.192  -5.015 -18.045  1.00 70.28      A    C  
ANISOU  616  CD1 ILE A  82     7257  11359   8085    390    358   -541  A    C  
ATOM    617  N   GLU A  83      48.023  -4.846 -19.116  1.00 65.12      A    N  
ANISOU  617  N   GLU A  83     7113  10279   7351    237    301   -310  A    N  
ATOM    618  CA  GLU A  83      47.059  -4.726 -20.189  1.00 70.73      A    C  
ANISOU  618  CA  GLU A  83     7907  10962   8005    210    320   -311  A    C  
ATOM    619  C   GLU A  83      46.560  -6.103 -20.573  1.00 74.05      A    C  
ANISOU  619  C   GLU A  83     8368  11286   8481    312    244   -386  A    C  
ATOM    620  O   GLU A  83      47.057  -7.108 -20.069  1.00 71.94      A    O  
ANISOU  620  O   GLU A  83     8061  10974   8300    407    191   -435  A    O  
ATOM    621  CB  GLU A  83      47.676  -4.034 -21.404  1.00 67.14      A    C  
ANISOU  621  CB  GLU A  83     7413  10659   7437    177    427   -366  A    C  
ATOM    622  CG  GLU A  83      48.768  -4.807 -22.086  1.00 72.18      A    C  
ANISOU  622  CG  GLU A  83     7968  11385   8071    268    450   -507  A    C  
ATOM    623  CD  GLU A  83      49.297  -4.065 -23.289  1.00 81.13      A    C  
ANISOU  623  CD  GLU A  83     9080  12662   9082    220    569   -556  A    C  
ATOM    624  OE1 GLU A  83      48.561  -3.213 -23.830  1.00 88.09      A    O  
ANISOU  624  OE1 GLU A  83    10038  13556   9877    138    609   -482  A    O  
ATOM    625  OE2 GLU A  83      50.445  -4.323 -23.695  1.00 80.57      A    O1-
ANISOU  625  OE2 GLU A  83     8918  12689   9006    264    625   -664  A    O1-
ATOM    626  N   ILE A  84      45.555  -6.135 -21.442  1.00 72.18      A    N  
ANISOU  626  N   ILE A  84     8209  11015   8201    289    237   -391  A    N  
ATOM    627  CA  ILE A  84      45.066  -7.376 -22.014  1.00 62.04      A    C  
ANISOU  627  CA  ILE A  84     6961   9657   6956    370    182   -485  A    C  
ATOM    628  C   ILE A  84      45.205  -7.249 -23.518  1.00 62.19      A    C  
ANISOU  628  C   ILE A  84     6979   9796   6855    361    238   -573  A    C  
ATOM    629  O   ILE A  84      44.981  -6.179 -24.069  1.00 69.35      A    O  
ANISOU  629  O   ILE A  84     7909  10785   7656    278    289   -514  A    O  
ATOM    630  CB  ILE A  84      43.619  -7.631 -21.600  1.00 63.33      A    C  
ANISOU  630  CB  ILE A  84     7220   9661   7181    344    110   -421  A    C  
ATOM    631  CG1 ILE A  84      43.595  -8.350 -20.251  1.00 65.17      A    C  
ANISOU  631  CG1 ILE A  84     7460   9755   7545    393     49   -385  A    C  
ATOM    632  CG2 ILE A  84      42.897  -8.458 -22.636  1.00 64.68      A    C  
ANISOU  632  CG2 ILE A  84     7435   9799   7340    379     78   -518  A    C  
ATOM    633  CD1 ILE A  84      42.549  -7.814 -19.325  1.00 64.34      A    C  
ANISOU  633  CD1 ILE A  84     7428   9533   7485    312     23   -260  A    C  
ATOM    634  N   CYS A  85      45.621  -8.321 -24.182  1.00 59.96      A    N  
ANISOU  634  N   CYS A  85     6669   9524   6587    444    238   -713  A    N  
ATOM    635  CA  CYS A  85      45.976  -8.224 -25.589  1.00 59.61      A    C  
ANISOU  635  CA  CYS A  85     6617   9613   6418    433    306   -814  A    C  
ATOM    636  C   CYS A  85      45.250  -9.270 -26.389  1.00 70.77      A    C  
ANISOU  636  C   CYS A  85     8083  10974   7832    470    264   -923  A    C  
ATOM    637  O   CYS A  85      44.877 -10.323 -25.858  1.00 76.82      A    O  
ANISOU  637  O   CYS A  85     8860  11602   8726    535    202   -960  A    O  
ATOM    638  CB  CYS A  85      47.477  -8.432 -25.763  1.00 74.13      A    C  
ANISOU  638  CB  CYS A  85     8350  11552   8265    487    383   -913  A    C  
ATOM    639  SG  CYS A  85      48.464  -7.042 -25.268  1.00 71.36      A    S  
ANISOU  639  SG  CYS A  85     7925  11321   7867    419    465   -826  A    S  
ATOM    640  N   ARG A  86      45.070  -8.985 -27.674  1.00 70.77      A    N  
ANISOU  640  N   ARG A  86     8116  11086   7686    424    303   -978  A    N  
ATOM    641  CA  ARG A  86      44.414  -9.916 -28.576  1.00 72.19      A    C  
ANISOU  641  CA  ARG A  86     8344  11246   7841    443    270  -1100  A    C  
ATOM    642  C   ARG A  86      45.369 -10.446 -29.664  1.00 79.50      A    C  
ANISOU  642  C   ARG A  86     9228  12285   8694    473    357  -1274  A    C  
ATOM    643  O   ARG A  86      46.576 -10.203 -29.618  1.00 76.63      A    O  
ANISOU  643  O   ARG A  86     8788  11997   8329    494    440  -1302  A    O  
ATOM    644  CB  ARG A  86      43.202  -9.242 -29.207  1.00 68.96      A    C  
ANISOU  644  CB  ARG A  86     8019  10871   7313    359    223  -1025  A    C  
ATOM    645  CG  ARG A  86      43.518  -7.903 -29.815  1.00 71.70      A    C  
ANISOU  645  CG  ARG A  86     8375  11370   7496    284    291   -938  A    C  
ATOM    646  CD  ARG A  86      42.413  -7.429 -30.744  1.00 83.64      A    C  
ANISOU  646  CD  ARG A  86     9968  12940   8872    219    243   -890  A    C  
ATOM    647  NE  ARG A  86      42.817  -6.160 -31.323  1.00100.11      A    N  
ANISOU  647  NE  ARG A  86    12067  15166  10804    155    322   -798  A    N  
ATOM    648  CZ  ARG A  86      43.297  -6.021 -32.550  1.00109.62      A    C  
ANISOU  648  CZ  ARG A  86    13290  16523  11836    131    390   -872  A    C  
ATOM    649  NH1 ARG A  86      43.385  -7.080 -33.342  1.00120.80      A    N1+
ANISOU  649  NH1 ARG A  86    14713  17975  13211    161    383  -1047  A    N1+
ATOM    650  NH2 ARG A  86      43.672  -4.822 -32.988  1.00104.47      A    N  
ANISOU  650  NH2 ARG A  86    12656  15984  11054     73    473   -773  A    N  
ATOM    651  N   THR A  87      44.817 -11.151 -30.648  1.00 81.59      A    N  
ANISOU  651  N   THR A  87     9538  12563   8899    467    343  -1397  A    N  
ATOM    652  CA  THR A  87      45.628 -11.802 -31.660  1.00 89.76      A    C  
ANISOU  652  CA  THR A  87    10540  13685   9879    492    430  -1582  A    C  
ATOM    653  C   THR A  87      45.356 -11.358 -33.092  1.00106.94      A    C  
ANISOU  653  C   THR A  87    12779  16021  11831    409    466  -1634  A    C  
ATOM    654  O   THR A  87      46.294 -11.060 -33.831  1.00113.09      A    O  
ANISOU  654  O   THR A  87    13533  16932  12503    389    574  -1703  A    O  
ATOM    655  CB  THR A  87      45.425 -13.305 -31.616  1.00 95.02      A    C  
ANISOU  655  CB  THR A  87    11194  14223  10684    566    407  -1733  A    C  
ATOM    656  CG2 THR A  87      46.416 -13.976 -32.519  1.00 97.41      A    C  
ANISOU  656  CG2 THR A  87    11447  14601  10962    596    517  -1928  A    C  
ATOM    657  OG1 THR A  87      45.616 -13.773 -30.279  1.00101.59      A    O  
ANISOU  657  OG1 THR A  87    11980  14899  11720    648    366  -1672  A    O  
ATOM    658  N   LYS A  88      44.079 -11.351 -33.474  1.00120.36      A    N  
ANISOU  658  N   LYS A  88    14559  17710  13463    360    375  -1605  A    N  
ATOM    659  CA  LYS A  88      43.633 -11.115 -34.858  1.00131.87      A    C  
ANISOU  659  CA  LYS A  88    16085  19316  14702    286    379  -1661  A    C  
ATOM    660  C   LYS A  88      43.534 -12.429 -35.650  1.00129.45      A    C  
ANISOU  660  C   LYS A  88    15785  19005  14394    301    391  -1888  A    C  
ATOM    661  O   LYS A  88      42.590 -12.647 -36.420  1.00123.91      A    O  
ANISOU  661  O   LYS A  88    15145  18349  13584    250    326  -1940  A    O  
ATOM    662  CB  LYS A  88      44.544 -10.121 -35.593  1.00139.88      A    C  
ANISOU  662  CB  LYS A  88    17103  20507  15539    236    491  -1632  A    C  
ATOM    663  CG  LYS A  88      45.618 -10.790 -36.448  1.00147.22      A    C  
ANISOU  663  CG  LYS A  88    17998  21521  16416    249    616  -1837  A    C  
ATOM    664  CD  LYS A  88      46.884  -9.949 -36.522  1.00150.32      A    C  
ANISOU  664  CD  LYS A  88    18346  22016  16755    236    749  -1805  A    C  
ATOM    665  CE  LYS A  88      47.982 -10.678 -37.281  1.00154.02      A    C  
ANISOU  665  CE  LYS A  88    18766  22548  17205    254    883  -2020  A    C  
ATOM    666  NZ  LYS A  88      49.248  -9.892 -37.345  1.00156.61      A    N1+
ANISOU  666  NZ  LYS A  88    19038  22970  17496    239   1022  -2004  A    N1+
ATOM    667  N   LYS A  96      40.752 -18.336 -34.981  1.00146.54      A    N  
ANISOU  667  N   LYS A  96    17946  20512  17219    456    234  -2520  A    N  
ATOM    668  CA  LYS A  96      39.873 -18.405 -33.814  1.00148.07      A    C  
ANISOU  668  CA  LYS A  96    18155  20527  17579    484    141  -2391  A    C  
ATOM    669  C   LYS A  96      39.926 -17.135 -32.964  1.00144.67      A    C  
ANISOU  669  C   LYS A  96    17727  20113  17130    481     91  -2143  A    C  
ATOM    670  O   LYS A  96      38.889 -16.633 -32.515  1.00144.67      A    O  
ANISOU  670  O   LYS A  96    17763  20064  17140    442     -4  -2016  A    O  
ATOM    671  CB  LYS A  96      40.211 -19.620 -32.942  1.00148.49      A    C  
ANISOU  671  CB  LYS A  96    18169  20363  17887    587    187  -2462  A    C  
ATOM    672  CG  LYS A  96      39.907 -20.952 -33.601  1.00150.74      A    C  
ANISOU  672  CG  LYS A  96    18456  20580  18238    586    235  -2703  A    C  
ATOM    673  CD  LYS A  96      39.909 -22.099 -32.599  1.00147.64      A    C  
ANISOU  673  CD  LYS A  96    18044  19936  18118    684    262  -2734  A    C  
ATOM    674  CE  LYS A  96      39.490 -23.400 -33.280  1.00145.84      A    C  
ANISOU  674  CE  LYS A  96    17820  19630  17961    669    319  -2980  A    C  
ATOM    675  NZ  LYS A  96      39.243 -24.514 -32.322  1.00143.80      A    N1+
ANISOU  675  NZ  LYS A  96    17559  19107  17971    753    342  -3002  A    N1+
ATOM    676  N   GLY A  97      41.137 -16.628 -32.746  1.00135.66      A    N  
ANISOU  676  N   GLY A  97    16540  19036  15969    519    164  -2085  A    N  
ATOM    677  CA  GLY A  97      41.341 -15.469 -31.897  1.00129.16      A    C  
ANISOU  677  CA  GLY A  97    15710  18225  15141    515    138  -1869  A    C  
ATOM    678  C   GLY A  97      41.715 -15.894 -30.490  1.00128.38      A    C  
ANISOU  678  C   GLY A  97    15572  17950  15257    604    135  -1798  A    C  
ATOM    679  O   GLY A  97      41.195 -16.888 -29.987  1.00137.52      A    O  
ANISOU  679  O   GLY A  97    16740  18939  16571    648    105  -1850  A    O  
ATOM    680  N   SER A  98      42.623 -15.151 -29.858  1.00115.81      A    N  
ANISOU  680  N   SER A  98    13935  16399  13669    627    166  -1681  A    N  
ATOM    681  CA  SER A  98      43.100 -15.478 -28.512  1.00 98.68      A    C  
ANISOU  681  CA  SER A  98    11723  14090  11680    710    156  -1603  A    C  
ATOM    682  C   SER A  98      43.183 -14.223 -27.651  1.00 88.93      A    C  
ANISOU  682  C   SER A  98    10487  12887  10414    670    129  -1403  A    C  
ATOM    683  O   SER A  98      43.320 -13.114 -28.166  1.00 86.63      A    O  
ANISOU  683  O   SER A  98    10201  12744   9972    598    154  -1343  A    O  
ATOM    684  CB  SER A  98      44.487 -16.125 -28.563  1.00 94.97      A    C  
ANISOU  684  CB  SER A  98    11165  13637  11283    802    241  -1709  A    C  
ATOM    685  OG  SER A  98      44.478 -17.375 -29.220  1.00 98.88      A    O  
ANISOU  685  OG  SER A  98    11654  14074  11843    846    282  -1899  A    O  
ATOM    686  N   ILE A  99      43.120 -14.407 -26.338  1.00 77.94      A    N  
ANISOU  686  N   ILE A  99     9092  11356   9166    714     87  -1302  A    N  
ATOM    687  CA  ILE A  99      43.255 -13.300 -25.412  1.00 73.50      A    C  
ANISOU  687  CA  ILE A  99     8525  10814   8588    674     69  -1127  A    C  
ATOM    688  C   ILE A  99      44.377 -13.554 -24.419  1.00 83.34      A    C  
ANISOU  688  C   ILE A  99     9697  12029   9939    756     83  -1094  A    C  
ATOM    689  O   ILE A  99      44.424 -14.605 -23.781  1.00 89.62      A    O  
ANISOU  689  O   ILE A  99    10487  12684  10879    843     56  -1121  A    O  
ATOM    690  CB  ILE A  99      41.965 -13.075 -24.632  1.00 71.93      A    C  
ANISOU  690  CB  ILE A  99     8402  10482   8445    624     -5  -1009  A    C  
ATOM    691  CG1 ILE A  99      40.929 -12.412 -25.529  1.00 67.48      A    C  
ANISOU  691  CG1 ILE A  99     7894   9985   7761    530    -27   -996  A    C  
ATOM    692  CG2 ILE A  99      42.227 -12.235 -23.382  1.00 79.51      A    C  
ANISOU  692  CG2 ILE A  99     9352  11420   9437    600    -16   -845  A    C  
ATOM    693  CD1 ILE A  99      41.480 -11.304 -26.359  1.00 72.27      A    C  
ANISOU  693  CD1 ILE A  99     8477  10785   8195    473     26   -969  A    C  
ATOM    694  N   TYR A 100      45.276 -12.585 -24.282  1.00 76.84      A    N  
ANISOU  694  N   TYR A 100     8815  11336   9045    729    124  -1034  A    N  
ATOM    695  CA  TYR A 100      46.384 -12.705 -23.350  1.00 67.46      A    C  
ANISOU  695  CA  TYR A 100     7542  10146   7942    798    128  -1000  A    C  
ATOM    696  C   TYR A 100      46.290 -11.631 -22.239  1.00 71.27      A    C  
ANISOU  696  C   TYR A 100     8035  10636   8410    731     98   -831  A    C  
ATOM    697  O   TYR A 100      46.037 -10.449 -22.513  1.00 65.42      A    O  
ANISOU  697  O   TYR A 100     7315   9985   7556    629    129   -765  A    O  
ATOM    698  CB  TYR A 100      47.706 -12.577 -24.102  1.00 62.82      A    C  
ANISOU  698  CB  TYR A 100     6853   9713   7303    827    214  -1103  A    C  
ATOM    699  CG  TYR A 100      48.012 -13.679 -25.110  1.00 78.73      A    C  
ANISOU  699  CG  TYR A 100     8842  11724   9349    897    261  -1284  A    C  
ATOM    700  CD1 TYR A 100      48.700 -14.834 -24.735  1.00 82.09      A    C  
ANISOU  700  CD1 TYR A 100     9197  12061   9931   1023    260  -1357  A    C  
ATOM    701  CD2 TYR A 100      47.660 -13.545 -26.444  1.00 82.03      A    C  
ANISOU  701  CD2 TYR A 100     9302  12228   9638    836    313  -1383  A    C  
ATOM    702  CE1 TYR A 100      48.996 -15.830 -25.654  1.00 80.33      A    C  
ANISOU  702  CE1 TYR A 100     8947  11824   9749   1082    321  -1532  A    C  
ATOM    703  CE2 TYR A 100      47.957 -14.537 -27.372  1.00 87.49      A    C  
ANISOU  703  CE2 TYR A 100     9972  12921  10351    887    368  -1562  A    C  
ATOM    704  CZ  TYR A 100      48.624 -15.675 -26.972  1.00 91.64      A    C  
ANISOU  704  CZ  TYR A 100    10426  13347  11047   1008    379  -1642  A    C  
ATOM    705  OH  TYR A 100      48.913 -16.657 -27.900  1.00101.78      A    O  
ANISOU  705  OH  TYR A 100    11685  14621  12365   1052    450  -1829  A    O  
ATOM    706  N   LEU A 101      46.456 -12.070 -20.991  1.00 66.09      A    N  
ANISOU  706  N   LEU A 101     7369   9876   7867    786     42   -762  A    N  
ATOM    707  CA  LEU A 101      46.660 -11.197 -19.837  1.00 64.97      A    C  
ANISOU  707  CA  LEU A 101     7216   9753   7718    733     20   -625  A    C  
ATOM    708  C   LEU A 101      48.149 -10.905 -19.694  1.00 66.34      A    C  
ANISOU  708  C   LEU A 101     7260  10065   7879    770     55   -651  A    C  
ATOM    709  O   LEU A 101      48.929 -11.836 -19.529  1.00 66.03      A    O  
ANISOU  709  O   LEU A 101     7151  10006   7931    885     37   -711  A    O  
ATOM    710  CB  LEU A 101      46.209 -11.897 -18.552  1.00 64.93      A    C  
ANISOU  710  CB  LEU A 101     7261   9579   7829    779    -59   -544  A    C  
ATOM    711  CG  LEU A 101      44.733 -11.825 -18.175  1.00 63.64      A    C  
ANISOU  711  CG  LEU A 101     7223   9273   7686    709    -94   -470  A    C  
ATOM    712  CD1 LEU A 101      43.941 -12.417 -19.272  1.00 67.52      A    C  
ANISOU  712  CD1 LEU A 101     7760   9715   8179    719    -84   -571  A    C  
ATOM    713  CD2 LEU A 101      44.482 -12.574 -16.895  1.00 57.64      A    C  
ANISOU  713  CD2 LEU A 101     6510   8352   7038    761   -157   -396  A    C  
ATOM    714  N   VAL A 102      48.536  -9.628 -19.723  1.00 61.51      A    N  
ANISOU  714  N   VAL A 102     6614   9587   7170    674    109   -605  A    N  
ATOM    715  CA  VAL A 102      49.942  -9.230 -19.699  1.00 56.21      A    C  
ANISOU  715  CA  VAL A 102     5812   9064   6482    690    156   -644  A    C  
ATOM    716  C   VAL A 102      50.377  -8.693 -18.329  1.00 66.12      A    C  
ANISOU  716  C   VAL A 102     7024  10339   7760    660    114   -540  A    C  
ATOM    717  O   VAL A 102      49.856  -7.689 -17.870  1.00 75.79      A    O  
ANISOU  717  O   VAL A 102     8301  11570   8928    545    128   -445  A    O  
ATOM    718  CB  VAL A 102      50.206  -8.178 -20.778  1.00 58.59      A    C  
ANISOU  718  CB  VAL A 102     6094   9513   6655    600    266   -685  A    C  
ATOM    719  CG1 VAL A 102      51.686  -8.001 -21.009  1.00 67.57      A    C  
ANISOU  719  CG1 VAL A 102     7089  10794   7789    631    332   -769  A    C  
ATOM    720  CG2 VAL A 102      49.550  -8.596 -22.062  1.00 58.52      A    C  
ANISOU  720  CG2 VAL A 102     6155   9487   6595    606    294   -767  A    C  
ATOM    721  N   PHE A 103      51.334  -9.358 -17.680  1.00 72.47      A    N  
ANISOU  721  N   PHE A 103     7732  11155   8648    761     63   -559  A    N  
ATOM    722  CA  PHE A 103      51.845  -8.921 -16.365  1.00 77.77      A    C  
ANISOU  722  CA  PHE A 103     8353  11866   9331    737      9   -468  A    C  
ATOM    723  C   PHE A 103      53.266  -8.333 -16.400  1.00 76.28      A    C  
ANISOU  723  C   PHE A 103     8003  11860   9120    731     55   -524  A    C  
ATOM    724  O   PHE A 103      54.042  -8.672 -17.288  1.00 78.75      A    O  
ANISOU  724  O   PHE A 103     8225  12242   9454    796    109   -641  A    O  
ATOM    725  CB  PHE A 103      51.864 -10.098 -15.396  1.00 76.72      A    C  
ANISOU  725  CB  PHE A 103     8229  11614   9309    858   -105   -422  A    C  
ATOM    726  CG  PHE A 103      50.522 -10.683 -15.120  1.00 79.98      A    C  
ANISOU  726  CG  PHE A 103     8794  11837   9758    859   -150   -360  A    C  
ATOM    727  CD1 PHE A 103      49.755 -10.221 -14.070  1.00 86.83      A    C  
ANISOU  727  CD1 PHE A 103     9756  12634  10601    771   -190   -237  A    C  
ATOM    728  CD2 PHE A 103      50.031 -11.701 -15.895  1.00 74.20      A    C  
ANISOU  728  CD2 PHE A 103     8109  10995   9088    940   -145   -435  A    C  
ATOM    729  CE1 PHE A 103      48.516 -10.764 -13.807  1.00 84.50      A    C  
ANISOU  729  CE1 PHE A 103     9598  12158  10349    768   -223   -187  A    C  
ATOM    730  CE2 PHE A 103      48.790 -12.241 -15.635  1.00 78.59      A    C  
ANISOU  730  CE2 PHE A 103     8799  11376   9687    935   -181   -388  A    C  
ATOM    731  CZ  PHE A 103      48.037 -11.775 -14.584  1.00 76.68      A    C  
ANISOU  731  CZ  PHE A 103     8648  11061   9427    851   -219   -263  A    C  
ATOM    732  N   ASP A 104      53.611  -7.476 -15.430  1.00 73.46      A    N  
ANISOU  732  N   ASP A 104     7607  11579   8727    648     41   -453  A    N  
ATOM    733  CA  ASP A 104      55.016  -7.079 -15.220  1.00 69.39      A    C  
ANISOU  733  CA  ASP A 104     6922  11231   8215    655     59   -507  A    C  
ATOM    734  C   ASP A 104      55.761  -8.338 -14.816  1.00 78.35      A    C  
ANISOU  734  C   ASP A 104     7963  12340   9466    825    -43   -533  A    C  
ATOM    735  O   ASP A 104      55.370  -9.007 -13.867  1.00 85.27      A    O  
ANISOU  735  O   ASP A 104     8897  13111  10391    883   -155   -444  A    O  
ATOM    736  CB  ASP A 104      55.165  -6.044 -14.099  1.00 73.43      A    C  
ANISOU  736  CB  ASP A 104     7414  11817   8670    532     45   -425  A    C  
ATOM    737  CG  ASP A 104      54.999  -4.592 -14.582  1.00 90.77      A    C  
ANISOU  737  CG  ASP A 104     9627  14095  10767    366    183   -431  A    C  
ATOM    738  OD1 ASP A 104      55.378  -4.294 -15.739  1.00 88.49      A    O  
ANISOU  738  OD1 ASP A 104     9295  13877  10449    358    291   -521  A    O  
ATOM    739  OD2 ASP A 104      54.509  -3.740 -13.786  1.00 95.10      A    O1-
ANISOU  739  OD2 ASP A 104    10233  14634  11267    240    191   -346  A    O1-
ATOM    740  N   PHE A 105      56.833  -8.668 -15.526  1.00 82.16      A    N  
ANISOU  740  N   PHE A 105     8305  12911   9999    907      1   -653  A    N  
ATOM    741  CA  PHE A 105      57.588  -9.875 -15.222  1.00 85.39      A    C  
ANISOU  741  CA  PHE A 105     8611  13291  10541   1081    -87   -681  A    C  
ATOM    742  C   PHE A 105      58.310  -9.818 -13.868  1.00 85.44      A    C  
ANISOU  742  C   PHE A 105     8519  13368  10575   1108   -205   -602  A    C  
ATOM    743  O   PHE A 105      58.667  -8.739 -13.367  1.00 77.16      A    O  
ANISOU  743  O   PHE A 105     7420  12450   9447    989   -190   -580  A    O  
ATOM    744  CB  PHE A 105      58.583 -10.160 -16.334  1.00 90.93      A    C  
ANISOU  744  CB  PHE A 105     9176  14075  11299   1150      5   -839  A    C  
ATOM    745  CG  PHE A 105      59.228 -11.503 -16.232  1.00 92.35      A    C  
ANISOU  745  CG  PHE A 105     9258  14193  11638   1340    -63   -879  A    C  
ATOM    746  CD1 PHE A 105      58.499 -12.655 -16.458  1.00 93.16      A    C  
ANISOU  746  CD1 PHE A 105     9461  14117  11817   1439    -93   -874  A    C  
ATOM    747  CD2 PHE A 105      60.573 -11.620 -15.930  1.00 88.59      A    C  
ANISOU  747  CD2 PHE A 105     8582  13832  11247   1419    -92   -927  A    C  
ATOM    748  CE1 PHE A 105      59.112 -13.910 -16.375  1.00 93.12      A    C  
ANISOU  748  CE1 PHE A 105     9365  14040  11978   1620   -142   -910  A    C  
ATOM    749  CE2 PHE A 105      61.177 -12.870 -15.844  1.00 83.03      A    C  
ANISOU  749  CE2 PHE A 105     7779  13061  10709   1605   -152   -958  A    C  
ATOM    750  CZ  PHE A 105      60.452 -14.009 -16.061  1.00 77.89      A    C  
ANISOU  750  CZ  PHE A 105     7234  12222  10137   1706   -174   -946  A    C  
ATOM    751  N   CYS A 106      58.512 -11.003 -13.296  1.00 84.78      A    N  
ANISOU  751  N   CYS A 106     8411  13198  10605   1266   -320   -560  A    N  
ATOM    752  CA  CYS A 106      59.123 -11.175 -11.986  1.00 91.94      A    C  
ANISOU  752  CA  CYS A 106     9238  14155  11540   1319   -459   -467  A    C  
ATOM    753  C   CYS A 106      60.027 -12.391 -12.103  1.00107.80      A    C  
ANISOU  753  C   CYS A 106    11110  16139  13709   1523   -518   -512  A    C  
ATOM    754  O   CYS A 106      59.564 -13.469 -12.481  1.00109.05      A    O  
ANISOU  754  O   CYS A 106    11339  16135  13962   1637   -520   -518  A    O  
ATOM    755  CB  CYS A 106      58.050 -11.433 -10.920  1.00 93.05      A    C  
ANISOU  755  CB  CYS A 106     9553  14157  11644   1297   -557   -310  A    C  
ATOM    756  SG  CYS A 106      56.800 -10.093 -10.676  1.00 99.82      A    S  
ANISOU  756  SG  CYS A 106    10587  15001  12339   1060   -487   -244  A    S  
ATOM    757  N   GLU A 107      61.313 -12.230 -11.795  1.00112.43      A    N  
ANISOU  757  N   GLU A 107    11495  16884  14340   1571   -560   -550  A    N  
ATOM    758  CA  GLU A 107      62.284 -13.290 -12.070  1.00112.56      A    C  
ANISOU  758  CA  GLU A 107    11351  16889  14528   1764   -593   -614  A    C  
ATOM    759  C   GLU A 107      62.090 -14.584 -11.261  1.00108.56      A    C  
ANISOU  759  C   GLU A 107    10886  16228  14133   1939   -736   -490  A    C  
ATOM    760  O   GLU A 107      62.292 -15.682 -11.786  1.00107.22      A    O  
ANISOU  760  O   GLU A 107    10678  15945  14117   2095   -720   -540  A    O  
ATOM    761  CB  GLU A 107      63.716 -12.765 -11.930  1.00124.15      A    C  
ANISOU  761  CB  GLU A 107    12576  18569  16025   1770   -606   -688  A    C  
ATOM    762  CG  GLU A 107      64.813 -13.843 -11.973  1.00137.95      A    C  
ANISOU  762  CG  GLU A 107    14131  20315  17969   1981   -667   -733  A    C  
ATOM    763  CD  GLU A 107      64.976 -14.505 -13.340  1.00144.28      A    C  
ANISOU  763  CD  GLU A 107    14897  21033  18890   2063   -526   -886  A    C  
ATOM    764  OE1 GLU A 107      64.297 -14.081 -14.301  1.00147.47      A    O  
ANISOU  764  OE1 GLU A 107    15421  21403  19208   1950   -383   -964  A    O  
ATOM    765  OE2 GLU A 107      65.790 -15.452 -13.451  1.00141.96      A    O1-
ANISOU  765  OE2 GLU A 107    14453  20708  18777   2240   -556   -930  A    O1-
ATOM    766  N   HIS A 108      61.688 -14.467  -9.999  1.00102.92      A    N  
ANISOU  766  N   HIS A 108    10258  15502  13346   1909   -865   -331  A    N  
ATOM    767  CA  HIS A 108      61.679 -15.632  -9.124  1.00108.07      A    C  
ANISOU  767  CA  HIS A 108    10933  16031  14098   2078  -1009   -199  A    C  
ATOM    768  C   HIS A 108      60.321 -15.915  -8.537  1.00108.30      A    C  
ANISOU  768  C   HIS A 108    11206  15880  14064   2035  -1041    -67  A    C  
ATOM    769  O   HIS A 108      59.513 -15.010  -8.368  1.00113.52      A    O  
ANISOU  769  O   HIS A 108    11996  16557  14580   1857  -1000    -41  A    O  
ATOM    770  CB  HIS A 108      62.646 -15.442  -7.948  1.00116.96      A    C  
ANISOU  770  CB  HIS A 108    11916  17316  15207   2118  -1169   -109  A    C  
ATOM    771  CG  HIS A 108      64.008 -14.958  -8.344  1.00122.61      A    C  
ANISOU  771  CG  HIS A 108    12377  18240  15969   2130  -1147   -236  A    C  
ATOM    772  CD2 HIS A 108      65.004 -15.565  -9.030  1.00121.39      A    C  
ANISOU  772  CD2 HIS A 108    12031  18108  15985   2278  -1117   -345  A    C  
ATOM    773  ND1 HIS A 108      64.470 -13.702  -8.021  1.00127.73      A    N  
ANISOU  773  ND1 HIS A 108    12941  19100  16490   1971  -1143   -270  A    N  
ATOM    774  CE1 HIS A 108      65.697 -13.551  -8.494  1.00127.99      A    C  
ANISOU  774  CE1 HIS A 108    12739  19280  16610   2019  -1114   -397  A    C  
ATOM    775  NE2 HIS A 108      66.040 -14.663  -9.112  1.00127.43      A    N  
ANISOU  775  NE2 HIS A 108    12599  19099  16721   2205  -1098   -444  A    N  
ATOM    776  N   ASP A 109      60.082 -17.175  -8.196  1.00 96.87      A    N  
ANISOU  776  N   ASP A 109    11916  11406  13485   1971  -3317    530  A    N  
ATOM    777  CA  ASP A 109      58.998 -17.495  -7.282  1.00104.28      A    C  
ANISOU  777  CA  ASP A 109    13081  12142  14399   1685  -3277    569  A    C  
ATOM    778  C   ASP A 109      59.508 -18.280  -6.075  1.00108.87      A    C  
ANISOU  778  C   ASP A 109    13903  12489  14974   1618  -3436    721  A    C  
ATOM    779  O   ASP A 109      60.619 -18.807  -6.081  1.00116.72      A    O  
ANISOU  779  O   ASP A 109    14900  13450  15999   1820  -3595    767  A    O  
ATOM    780  CB  ASP A 109      57.845 -18.215  -7.978  1.00109.98      A    C  
ANISOU  780  CB  ASP A 109    13838  12757  15192   1654  -3226    396  A    C  
ATOM    781  CG  ASP A 109      58.222 -19.573  -8.456  1.00117.75      A    C  
ANISOU  781  CG  ASP A 109    14899  13550  16288   1844  -3386    307  A    C  
ATOM    782  OD1 ASP A 109      58.938 -19.651  -9.476  1.00120.44      A    O  
ANISOU  782  OD1 ASP A 109    15071  14022  16668   2125  -3437    213  A    O  
ATOM    783  OD2 ASP A 109      57.801 -20.557  -7.813  1.00121.45      A    O1-
ANISOU  783  OD2 ASP A 109    15603  13736  16808   1716  -3452    334  A    O1-
ATOM    784  N   LEU A 110      58.683 -18.339  -5.039  1.00108.50      A    N  
ANISOU  784  N   LEU A 110    14056  12294  14877   1344  -3386    807  A    N  
ATOM    785  CA  LEU A 110      59.103 -18.809  -3.731  1.00108.48      A    C  
ANISOU  785  CA  LEU A 110    14279  12113  14824   1251  -3504    986  A    C  
ATOM    786  C   LEU A 110      59.238 -20.325  -3.709  1.00111.85      A    C  
ANISOU  786  C   LEU A 110    14897  12252  15351   1353  -3650    982  A    C  
ATOM    787  O   LEU A 110      59.877 -20.887  -2.823  1.00109.10      A    O  
ANISOU  787  O   LEU A 110    14718  11759  14974   1377  -3783   1130  A    O  
ATOM    788  CB  LEU A 110      58.101 -18.349  -2.669  1.00104.66      A    C  
ANISOU  788  CB  LEU A 110    13945  11577  14246    928  -3382   1077  A    C  
ATOM    789  CG  LEU A 110      58.568 -18.327  -1.217  1.00103.10      A    C  
ANISOU  789  CG  LEU A 110    13933  11303  13938    813  -3464   1280  A    C  
ATOM    790  CD1 LEU A 110      59.656 -17.279  -1.039  1.00105.09      A    C  
ANISOU  790  CD1 LEU A 110    14020  11801  14110    894  -3500   1338  A    C  
ATOM    791  CD2 LEU A 110      57.394 -18.059  -0.291  1.00 94.36      A    C  
ANISOU  791  CD2 LEU A 110    12988  10119  12747    503  -3330   1348  A    C  
ATOM    792  N   ALA A 111      58.626 -20.990  -4.680  1.00114.70      A    N  
ANISOU  792  N   ALA A 111    15232  12524  15825   1417  -3624    809  A    N  
ATOM    793  CA  ALA A 111      58.769 -22.436  -4.781  1.00114.44      A    C  
ANISOU  793  CA  ALA A 111    15373  12202  15907   1529  -3755    780  A    C  
ATOM    794  C   ALA A 111      60.139 -22.756  -5.358  1.00113.57      A    C  
ANISOU  794  C   ALA A 111    15158  12160  15835   1869  -3912    766  A    C  
ATOM    795  O   ALA A 111      60.837 -23.648  -4.863  1.00110.79      A    O  
ANISOU  795  O   ALA A 111    14970  11616  15509   1984  -4063    866  A    O  
ATOM    796  CB  ALA A 111      57.674 -23.020  -5.646  1.00112.73      A    C  
ANISOU  796  CB  ALA A 111    15151  11877  15803   1479  -3679    575  A    C  
ATOM    797  N   GLY A 112      60.510 -22.016  -6.404  1.00113.56      A    N  
ANISOU  797  N   GLY A 112    14882  12438  15830   2038  -3868    651  A    N  
ATOM    798  CA  GLY A 112      61.812 -22.149  -7.033  1.00118.45      A    C  
ANISOU  798  CA  GLY A 112    15355  13177  16474   2364  -3993    635  A    C  
ATOM    799  C   GLY A 112      62.956 -21.914  -6.058  1.00122.70      A    C  
ANISOU  799  C   GLY A 112    15928  13761  16932   2408  -4109    836  A    C  
ATOM    800  O   GLY A 112      63.952 -22.645  -6.052  1.00126.43      A    O  
ANISOU  800  O   GLY A 112    16437  14164  17437   2639  -4271    880  A    O  
ATOM    801  N   LEU A 113      62.807 -20.897  -5.217  1.00116.95      A    N  
ANISOU  801  N   LEU A 113    15188  13155  16093   2191  -4030    954  A    N  
ATOM    802  CA  LEU A 113      63.850 -20.553  -4.260  1.00116.82      A    C  
ANISOU  802  CA  LEU A 113    15183  13217  15986   2209  -4137   1128  A    C  
ATOM    803  C   LEU A 113      63.912 -21.495  -3.051  1.00116.40      A    C  
ANISOU  803  C   LEU A 113    15430  12897  15901   2141  -4262   1285  A    C  
ATOM    804  O   LEU A 113      64.988 -21.776  -2.528  1.00115.68      A    O  
ANISOU  804  O   LEU A 113    15366  12816  15770   2288  -4418   1401  A    O  
ATOM    805  CB  LEU A 113      63.704 -19.094  -3.820  1.00113.80      A    C  
ANISOU  805  CB  LEU A 113    14676  13066  15498   2007  -4007   1180  A    C  
ATOM    806  CG  LEU A 113      63.878 -18.123  -4.987  1.00112.61      A    C  
ANISOU  806  CG  LEU A 113    14220  13191  15374   2115  -3889   1059  A    C  
ATOM    807  CD1 LEU A 113      64.069 -16.709  -4.491  1.00109.97      A    C  
ANISOU  807  CD1 LEU A 113    13761  13075  14947   1958  -3790   1129  A    C  
ATOM    808  CD2 LEU A 113      65.055 -18.551  -5.863  1.00113.10      A    C  
ANISOU  808  CD2 LEU A 113    14120  13347  15508   2456  -4012   1010  A    C  
ATOM    809  N   LEU A 114      62.759 -21.987  -2.616  1.00117.02      A    N  
ANISOU  809  N   LEU A 114    15726  12743  15995   1925  -4188   1292  A    N  
ATOM    810  CA  LEU A 114      62.702 -22.875  -1.465  1.00121.62      A    C  
ANISOU  810  CA  LEU A 114    16607  13056  16546   1847  -4278   1455  A    C  
ATOM    811  C   LEU A 114      63.223 -24.274  -1.780  1.00125.30      A    C  
ANISOU  811  C   LEU A 114    17204  13282  17122   2093  -4428   1446  A    C  
ATOM    812  O   LEU A 114      63.631 -25.007  -0.873  1.00124.83      A    O  
ANISOU  812  O   LEU A 114    17362  13042  17028   2131  -4543   1609  A    O  
ATOM    813  CB  LEU A 114      61.276 -22.968  -0.915  1.00123.53      A    C  
ANISOU  813  CB  LEU A 114    17036  13121  16778   1530  -4135   1471  A    C  
ATOM    814  CG  LEU A 114      60.762 -21.780  -0.100  1.00119.73      A    C  
ANISOU  814  CG  LEU A 114    16534  12804  16155   1261  -4008   1550  A    C  
ATOM    815  CD1 LEU A 114      59.394 -22.101   0.485  1.00116.73      A    C  
ANISOU  815  CD1 LEU A 114    16363  12217  15772    975  -3882   1581  A    C  
ATOM    816  CD2 LEU A 114      61.748 -21.407   0.997  1.00118.12      A    C  
ANISOU  816  CD2 LEU A 114    16372  12701  15809   1285  -4124   1732  A    C  
ATOM    817  N   SER A 115      63.198 -24.650  -3.056  1.00124.81      A    N  
ANISOU  817  N   SER A 115    17018  13219  17187   2270  -4423   1257  A    N  
ATOM    818  CA  SER A 115      63.650 -25.979  -3.458  1.00129.26      A    C  
ANISOU  818  CA  SER A 115    17702  13544  17865   2514  -4556   1220  A    C  
ATOM    819  C   SER A 115      65.140 -25.963  -3.793  1.00134.75      A    C  
ANISOU  819  C   SER A 115    18240  14417  18542   2850  -4709   1247  A    C  
ATOM    820  O   SER A 115      65.882 -26.885  -3.427  1.00137.38      A    O  
ANISOU  820  O   SER A 115    18721  14586  18892   3041  -4860   1345  A    O  
ATOM    821  CB  SER A 115      62.840 -26.489  -4.648  1.00127.29      A    C  
ANISOU  821  CB  SER A 115    17414  13189  17761   2539  -4482    984  A    C  
ATOM    822  OG  SER A 115      62.972 -25.610  -5.750  1.00125.00      A    O  
ANISOU  822  OG  SER A 115    16816  13213  17467   2642  -4414    827  A    O  
ATOM    823  N   ASN A 116      65.567 -24.904  -4.480  1.00134.57      A    N  
ANISOU  823  N   ASN A 116    17914  14731  18484   2923  -4661   1168  A    N  
ATOM    824  CA  ASN A 116      66.977 -24.701  -4.822  1.00137.05      A    C  
ANISOU  824  CA  ASN A 116    18030  15268  18776   3217  -4783   1193  A    C  
ATOM    825  C   ASN A 116      67.882 -24.539  -3.588  1.00138.54      A    C  
ANISOU  825  C   ASN A 116    18282  15511  18844   3219  -4908   1409  A    C  
ATOM    826  O   ASN A 116      67.782 -23.540  -2.866  1.00137.20      A    O  
ANISOU  826  O   ASN A 116    18063  15502  18566   3006  -4849   1494  A    O  
ATOM    827  CB  ASN A 116      67.120 -23.491  -5.755  1.00127.44      A    C  
ANISOU  827  CB  ASN A 116    16478  14397  17545   3246  -4669   1078  A    C  
ATOM    828  CG  ASN A 116      68.562 -23.228  -6.166  1.00121.82      A    C  
ANISOU  828  CG  ASN A 116    15533  13932  16820   3538  -4776   1099  A    C  
ATOM    829  ND2 ASN A 116      68.768 -22.169  -6.948  1.00105.39      A    N  
ANISOU  829  ND2 ASN A 116    13162  12150  14731   3570  -4670   1021  A    N  
ATOM    830  OD1 ASN A 116      69.480 -23.970  -5.789  1.00123.04      A    O  
ANISOU  830  OD1 ASN A 116    15766  14014  16972   3737  -4946   1190  A    O  
ATOM    831  N   VAL A 117      68.768 -25.514  -3.365  1.00136.69      A    N  
ANISOU  831  N   VAL A 117    18155  15155  18625   3470  -5083   1490  A    N  
ATOM    832  CA  VAL A 117      69.615 -25.542  -2.165  1.00137.97      A    C  
ANISOU  832  CA  VAL A 117    18402  15354  18667   3502  -5223   1697  A    C  
ATOM    833  C   VAL A 117      70.790 -24.545  -2.208  1.00141.87      A    C  
ANISOU  833  C   VAL A 117    18593  16229  19081   3613  -5282   1722  A    C  
ATOM    834  O   VAL A 117      71.454 -24.314  -1.197  1.00131.86      A    O  
ANISOU  834  O   VAL A 117    17348  15059  17695   3598  -5386   1874  A    O  
ATOM    835  CB  VAL A 117      70.134 -26.963  -1.847  1.00136.94      A    C  
ANISOU  835  CB  VAL A 117    18508  14952  18572   3744  -5387   1791  A    C  
ATOM    836  CG1 VAL A 117      70.713 -27.002  -0.444  1.00139.82      A    C  
ANISOU  836  CG1 VAL A 117    19011  15328  18787   3722  -5508   2021  A    C  
ATOM    837  CG2 VAL A 117      69.015 -27.990  -1.973  1.00136.75      A    C  
ANISOU  837  CG2 VAL A 117    18763  14535  18662   3646  -5318   1740  A    C  
ATOM    838  N   LEU A 118      71.026 -23.949  -3.376  1.00152.90      A    N  
ANISOU  838  N   LEU A 118    19705  17845  20543   3719  -5211   1572  A    N  
ATOM    839  CA  LEU A 118      71.996 -22.858  -3.526  1.00154.93      A    C  
ANISOU  839  CA  LEU A 118    19650  18469  20748   3776  -5222   1580  A    C  
ATOM    840  C   LEU A 118      71.492 -21.545  -2.918  1.00152.59      A    C  
ANISOU  840  C   LEU A 118    19287  18326  20364   3442  -5090   1611  A    C  
ATOM    841  O   LEU A 118      72.162 -20.512  -2.995  1.00148.79      A    O  
ANISOU  841  O   LEU A 118    18552  18133  19848   3430  -5068   1610  A    O  
ATOM    842  CB  LEU A 118      72.292 -22.611  -5.011  1.00154.41      A    C  
ANISOU  842  CB  LEU A 118    19309  18578  20781   3983  -5155   1416  A    C  
ATOM    843  CG  LEU A 118      73.178 -23.573  -5.804  1.00150.15      A    C  
ANISOU  843  CG  LEU A 118    18711  18021  20316   4374  -5286   1365  A    C  
ATOM    844  CD1 LEU A 118      73.249 -23.119  -7.268  1.00144.72      A    C  
ANISOU  844  CD1 LEU A 118    17747  17535  19706   4524  -5174   1197  A    C  
ATOM    845  CD2 LEU A 118      74.570 -23.663  -5.177  1.00143.90      A    C  
ANISOU  845  CD2 LEU A 118    17839  17381  19456   4562  -5469   1501  A    C  
ATOM    846  N   VAL A 119      70.301 -21.583  -2.332  1.00151.43      A    N  
ANISOU  846  N   VAL A 119    19366  17984  20189   3169  -4993   1634  A    N  
ATOM    847  CA  VAL A 119      69.642 -20.370  -1.873  1.00142.21      A    C  
ANISOU  847  CA  VAL A 119    18150  16936  18946   2855  -4842   1641  A    C  
ATOM    848  C   VAL A 119      69.377 -20.453  -0.387  1.00128.15      A    C  
ANISOU  848  C   VAL A 119    16613  15041  17038   2649  -4893   1798  A    C  
ATOM    849  O   VAL A 119      68.877 -21.464   0.103  1.00123.85      A    O  
ANISOU  849  O   VAL A 119    16344  14221  16493   2630  -4938   1866  A    O  
ATOM    850  CB  VAL A 119      68.302 -20.187  -2.586  1.00148.32      A    C  
ANISOU  850  CB  VAL A 119    18948  17620  19789   2698  -4645   1511  A    C  
ATOM    851  CG1 VAL A 119      67.658 -18.878  -2.169  1.00149.21      A    C  
ANISOU  851  CG1 VAL A 119    18997  17872  19824   2399  -4480   1516  A    C  
ATOM    852  CG2 VAL A 119      68.496 -20.248  -4.096  1.00149.68      A    C  
ANISOU  852  CG2 VAL A 119    18903  17892  20077   2929  -4599   1350  A    C  
ATOM    853  N   LYS A 120      69.703 -19.391   0.336  1.00118.56      A    N  
ANISOU  853  N   LYS A 120    15300  14034  15713   2493  -4881   1854  A    N  
ATOM    854  CA  LYS A 120      69.549 -19.422   1.785  1.00121.23      A    C  
ANISOU  854  CA  LYS A 120    15856  14301  15905   2317  -4942   2003  A    C  
ATOM    855  C   LYS A 120      69.038 -18.104   2.323  1.00117.25      A    C  
ANISOU  855  C   LYS A 120    15293  13945  15311   2017  -4803   1992  A    C  
ATOM    856  O   LYS A 120      69.433 -17.027   1.862  1.00108.35      A    O  
ANISOU  856  O   LYS A 120    13908  13058  14204   1992  -4734   1913  A    O  
ATOM    857  CB  LYS A 120      70.875 -19.767   2.468  1.00128.26      A    C  
ANISOU  857  CB  LYS A 120    16727  15295  16712   2511  -5167   2119  A    C  
ATOM    858  CG  LYS A 120      71.086 -21.238   2.791  1.00130.72      A    C  
ANISOU  858  CG  LYS A 120    17283  15358  17028   2715  -5320   2227  A    C  
ATOM    859  CD  LYS A 120      72.411 -21.405   3.523  1.00133.76      A    C  
ANISOU  859  CD  LYS A 120    17620  15900  17303   2903  -5538   2344  A    C  
ATOM    860  CE  LYS A 120      72.572 -22.787   4.143  1.00136.36      A    C  
ANISOU  860  CE  LYS A 120    18238  15979  17594   3079  -5685   2495  A    C  
ATOM    861  NZ  LYS A 120      73.807 -22.866   4.985  1.00135.60      A    N1+
ANISOU  861  NZ  LYS A 120    18097  16067  17358   3250  -5897   2620  A    N1+
ATOM    862  N   PHE A 121      68.170 -18.193   3.321  1.00122.74      A    N  
ANISOU  862  N   PHE A 121    16237  14492  15906   1792  -4757   2078  A    N  
ATOM    863  CA  PHE A 121      67.569 -17.000   3.894  1.00127.33      A    C  
ANISOU  863  CA  PHE A 121    16798  15187  16393   1502  -4616   2067  A    C  
ATOM    864  C   PHE A 121      68.063 -16.754   5.307  1.00124.49      A    C  
ANISOU  864  C   PHE A 121    16539  14909  15853   1413  -4736   2195  A    C  
ATOM    865  O   PHE A 121      67.965 -17.634   6.168  1.00126.36      A    O  
ANISOU  865  O   PHE A 121    17026  14981  16006   1431  -4836   2329  A    O  
ATOM    866  CB  PHE A 121      66.042 -17.121   3.908  1.00133.64      A    C  
ANISOU  866  CB  PHE A 121    17782  15789  17206   1285  -4435   2047  A    C  
ATOM    867  CG  PHE A 121      65.410 -17.109   2.539  1.00137.98      A    C  
ANISOU  867  CG  PHE A 121    18207  16309  17911   1328  -4291   1896  A    C  
ATOM    868  CD1 PHE A 121      65.277 -15.920   1.830  1.00133.46      A    C  
ANISOU  868  CD1 PHE A 121    17397  15941  17373   1265  -4140   1782  A    C  
ATOM    869  CD2 PHE A 121      64.931 -18.284   1.971  1.00139.28      A    C  
ANISOU  869  CD2 PHE A 121    18496  16240  18184   1432  -4304   1865  A    C  
ATOM    870  CE1 PHE A 121      64.693 -15.903   0.580  1.00128.03      A    C  
ANISOU  870  CE1 PHE A 121    16591  15247  16805   1322  -4010   1647  A    C  
ATOM    871  CE2 PHE A 121      64.347 -18.273   0.722  1.00137.78      A    C  
ANISOU  871  CE2 PHE A 121    18184  16044  18121   1477  -4182   1711  A    C  
ATOM    872  CZ  PHE A 121      64.228 -17.077   0.025  1.00133.32      A    C  
ANISOU  872  CZ  PHE A 121    17377  15708  17572   1429  -4037   1605  A    C  
ATOM    873  N   THR A 122      68.596 -15.559   5.544  1.00115.91      A    N  
ANISOU  873  N   THR A 122    15259  14075  14708   1321  -4722   2152  A    N  
ATOM    874  CA  THR A 122      68.854 -15.114   6.906  1.00115.48      A    C  
ANISOU  874  CA  THR A 122    15294  14117  14468   1180  -4802   2240  A    C  
ATOM    875  C   THR A 122      67.506 -14.956   7.608  1.00112.57      A    C  
ANISOU  875  C   THR A 122    15164  13599  14007    912  -4650   2281  A    C  
ATOM    876  O   THR A 122      66.491 -14.717   6.954  1.00118.80      A    O  
ANISOU  876  O   THR A 122    15954  14301  14884    799  -4458   2204  A    O  
ATOM    877  CB  THR A 122      69.613 -13.773   6.926  1.00119.55      A    C  
ANISOU  877  CB  THR A 122    15538  14924  14962   1105  -4793   2152  A    C  
ATOM    878  CG2 THR A 122      70.562 -13.676   5.734  1.00118.57      A    C  
ANISOU  878  CG2 THR A 122    15117  14941  14993   1324  -4828   2064  A    C  
ATOM    879  OG1 THR A 122      68.681 -12.685   6.883  1.00122.41      A    O  
ANISOU  879  OG1 THR A 122    15881  15309  15319    846  -4573   2074  A    O  
ATOM    880  N   LEU A 123      67.478 -15.103   8.927  1.00107.61      A    N  
ANISOU  880  N   LEU A 123    14736  12954  13198    822  -4733   2403  A    N  
ATOM    881  CA  LEU A 123      66.238 -14.905   9.669  1.00108.96      A    C  
ANISOU  881  CA  LEU A 123    15127  13006  13265    567  -4586   2450  A    C  
ATOM    882  C   LEU A 123      65.520 -13.610   9.262  1.00113.73      A    C  
ANISOU  882  C   LEU A 123    15595  13712  13904    350  -4366   2316  A    C  
ATOM    883  O   LEU A 123      64.307 -13.605   9.075  1.00120.60      A    O  
ANISOU  883  O   LEU A 123    16572  14447  14803    203  -4187   2299  A    O  
ATOM    884  CB  LEU A 123      66.498 -14.880  11.173  1.00109.58      A    C  
ANISOU  884  CB  LEU A 123    15376  13145  13114    496  -4704   2578  A    C  
ATOM    885  CG  LEU A 123      65.235 -14.710  12.023  1.00112.25      A    C  
ANISOU  885  CG  LEU A 123    15954  13371  13326    243  -4552   2642  A    C  
ATOM    886  CD1 LEU A 123      64.324 -15.929  11.891  1.00112.58      A    C  
ANISOU  886  CD1 LEU A 123    16234  13108  13433    259  -4491   2742  A    C  
ATOM    887  CD2 LEU A 123      65.569 -14.451  13.480  1.00112.97      A    C  
ANISOU  887  CD2 LEU A 123    16171  13581  13170    172  -4661   2743  A    C  
ATOM    888  N   SER A 124      66.272 -12.521   9.127  1.00108.09      A    N  
ANISOU  888  N   SER A 124    14645  13235  13191    331  -4375   2222  A    N  
ATOM    889  CA  SER A 124      65.696 -11.210   8.839  1.00109.50      A    C  
ANISOU  889  CA  SER A 124    14700  13513  13391    132  -4167   2105  A    C  
ATOM    890  C   SER A 124      65.076 -11.121   7.439  1.00115.52      A    C  
ANISOU  890  C   SER A 124    15337  14217  14339    172  -3991   2005  A    C  
ATOM    891  O   SER A 124      64.091 -10.402   7.225  1.00113.78      A    O  
ANISOU  891  O   SER A 124    15118  13986  14127      3  -3782   1944  A    O  
ATOM    892  CB  SER A 124      66.748 -10.102   9.020  1.00105.78      A    C  
ANISOU  892  CB  SER A 124    14003  13295  12895    108  -4225   2029  A    C  
ATOM    893  OG  SER A 124      67.627 -10.013   7.906  1.00 97.73      A    O  
ANISOU  893  OG  SER A 124    12716  12380  12039    292  -4259   1954  A    O  
ATOM    894  N   GLU A 125      65.668 -11.833   6.485  1.00116.01      A    N  
ANISOU  894  N   GLU A 125    15284  14257  14538    409  -4076   1984  A    N  
ATOM    895  CA  GLU A 125      65.145 -11.846   5.130  1.00113.85      A    C  
ANISOU  895  CA  GLU A 125    14889  13943  14428    480  -3930   1884  A    C  
ATOM    896  C   GLU A 125      63.785 -12.538   5.163  1.00108.55      A    C  
ANISOU  896  C   GLU A 125    14441  13046  13756    380  -3823   1910  A    C  
ATOM    897  O   GLU A 125      62.768 -11.973   4.731  1.00 97.92      A    O  
ANISOU  897  O   GLU A 125    13072  11693  12439    247  -3621   1838  A    O  
ATOM    898  CB  GLU A 125      66.128 -12.531   4.168  1.00120.76      A    C  
ANISOU  898  CB  GLU A 125    15604  14847  15433    772  -4061   1857  A    C  
ATOM    899  CG  GLU A 125      67.408 -11.712   3.907  1.00133.03      A    C  
ANISOU  899  CG  GLU A 125    16880  16649  17016    862  -4124   1811  A    C  
ATOM    900  CD  GLU A 125      68.429 -12.431   3.026  1.00140.70      A    C  
ANISOU  900  CD  GLU A 125    17693  17664  18101   1165  -4261   1795  A    C  
ATOM    901  OE1 GLU A 125      68.655 -13.643   3.233  1.00147.21      A    O  
ANISOU  901  OE1 GLU A 125    18664  18353  18917   1319  -4418   1868  A    O  
ATOM    902  OE2 GLU A 125      69.017 -11.777   2.135  1.00138.48      A    O1-
ANISOU  902  OE2 GLU A 125    17145  17553  17918   1256  -4204   1716  A    O1-
ATOM    903  N   ILE A 126      63.769 -13.751   5.706  1.00104.60      A    N  
ANISOU  903  N   ILE A 126    14156  12364  13221    443  -3956   2016  A    N  
ATOM    904  CA  ILE A 126      62.521 -14.452   5.950  1.00100.74      A    C  
ANISOU  904  CA  ILE A 126    13902  11650  12725    319  -3864   2060  A    C  
ATOM    905  C   ILE A 126      61.478 -13.490   6.522  1.00101.89      A    C  
ANISOU  905  C   ILE A 126    14107  11838  12768     41  -3674   2050  A    C  
ATOM    906  O   ILE A 126      60.390 -13.342   5.962  1.00106.56      A    O  
ANISOU  906  O   ILE A 126    14693  12374  13420    -59  -3496   1978  A    O  
ATOM    907  CB  ILE A 126      62.726 -15.642   6.899  1.00106.50      A    C  
ANISOU  907  CB  ILE A 126    14889  12196  13378    371  -4026   2219  A    C  
ATOM    908  CG1 ILE A 126      63.465 -16.775   6.174  1.00108.81      A    C  
ANISOU  908  CG1 ILE A 126    15158  12384  13800    651  -4178   2219  A    C  
ATOM    909  CG2 ILE A 126      61.389 -16.140   7.429  1.00107.85      A    C  
ANISOU  909  CG2 ILE A 126    15313  12154  13512    176  -3904   2286  A    C  
ATOM    910  CD1 ILE A 126      63.882 -17.928   7.063  1.00105.33      A    C  
ANISOU  910  CD1 ILE A 126    14955  11775  13288    752  -4352   2386  A    C  
ATOM    911  N   LYS A 127      61.816 -12.835   7.629  1.00 99.30      A    N  
ANISOU  911  N   LYS A 127    13829  11619  12280    -74  -3714   2114  A    N  
ATOM    912  CA  LYS A 127      60.957 -11.812   8.222  1.00 98.17      A    C  
ANISOU  912  CA  LYS A 127    13733  11541  12027   -322  -3541   2096  A    C  
ATOM    913  C   LYS A 127      60.387 -10.844   7.181  1.00 91.84      A    C  
ANISOU  913  C   LYS A 127    12735  10833  11326   -374  -3332   1953  A    C  
ATOM    914  O   LYS A 127      59.203 -10.514   7.210  1.00 88.39      A    O  
ANISOU  914  O   LYS A 127    12365  10353  10864   -537  -3147   1930  A    O  
ATOM    915  CB  LYS A 127      61.718 -11.017   9.288  1.00102.49      A    C  
ANISOU  915  CB  LYS A 127    14274  12255  12414   -394  -3629   2130  A    C  
ATOM    916  CG  LYS A 127      61.912 -11.756  10.598  1.00109.29      A    C  
ANISOU  916  CG  LYS A 127    15377  13041  13107   -407  -3782   2286  A    C  
ATOM    917  CD  LYS A 127      62.348 -10.811  11.714  1.00111.64      A    C  
ANISOU  917  CD  LYS A 127    15682  13517  13218   -529  -3827   2293  A    C  
ATOM    918  CE  LYS A 127      62.517 -11.557  13.034  1.00113.99      A    C  
ANISOU  918  CE  LYS A 127    16226  13761  13325   -524  -3978   2457  A    C  
ATOM    919  NZ  LYS A 127      62.926 -10.658  14.150  1.00114.04      A    N1+
ANISOU  919  NZ  LYS A 127    16242  13956  13131   -639  -4032   2449  A    N1+
ATOM    920  N   ARG A 128      61.227 -10.382   6.265  1.00 87.03      A    N  
ANISOU  920  N   ARG A 128    11879  10361  10827   -227  -3354   1864  A    N  
ATOM    921  CA  ARG A 128      60.758  -9.446   5.262  1.00 85.15      A    C  
ANISOU  921  CA  ARG A 128    11453  10222  10678   -250  -3153   1744  A    C  
ATOM    922  C   ARG A 128      59.771 -10.145   4.338  1.00 87.93      A    C  
ANISOU  922  C   ARG A 128    11827  10449  11135   -204  -3054   1696  A    C  
ATOM    923  O   ARG A 128      58.701  -9.630   4.042  1.00 93.94      A    O  
ANISOU  923  O   ARG A 128    12579  11217  11895   -321  -2857   1641  A    O  
ATOM    924  CB  ARG A 128      61.928  -8.876   4.466  1.00 84.78      A    C  
ANISOU  924  CB  ARG A 128    11137  10345  10730    -89  -3198   1676  A    C  
ATOM    925  CG  ARG A 128      61.543  -7.781   3.471  1.00 82.91      A    C  
ANISOU  925  CG  ARG A 128    10701  10225  10575   -103  -2978   1569  A    C  
ATOM    926  CD  ARG A 128      61.276  -6.436   4.138  1.00 88.60      A    C  
ANISOU  926  CD  ARG A 128    11422  11039  11203   -315  -2837   1553  A    C  
ATOM    927  NE  ARG A 128      61.046  -5.412   3.122  1.00 98.05      A    N  
ANISOU  927  NE  ARG A 128    12421  12343  12490   -293  -2630   1465  A    N  
ATOM    928  CZ  ARG A 128      59.859  -4.874   2.864  1.00 96.86      A    C  
ANISOU  928  CZ  ARG A 128    12302  12179  12322   -394  -2411   1429  A    C  
ATOM    929  NH1 ARG A 128      58.803  -5.247   3.575  1.00 97.70      A    N1+
ANISOU  929  NH1 ARG A 128    12621  12173  12328   -541  -2372   1467  A    N1+
ATOM    930  NH2 ARG A 128      59.732  -3.959   1.908  1.00 90.44      A    N  
ANISOU  930  NH2 ARG A 128    11305  11469  11588   -343  -2227   1362  A    N  
ATOM    931  N   VAL A 129      60.141 -11.324   3.876  1.00 91.40      A    N  
ANISOU  931  N   VAL A 129    12288  10777  11664    -25  -3192   1708  A    N  
ATOM    932  CA  VAL A 129      59.258 -12.093   3.025  1.00 89.17      A    C  
ANISOU  932  CA  VAL A 129    12031  10365  11486     20  -3122   1646  A    C  
ATOM    933  C   VAL A 129      57.872 -12.193   3.657  1.00 85.21      A    C  
ANISOU  933  C   VAL A 129    11723   9743  10911   -213  -2987   1680  A    C  
ATOM    934  O   VAL A 129      56.882 -11.827   3.027  1.00 77.89      A    O  
ANISOU  934  O   VAL A 129    10730   8844  10020   -281  -2810   1591  A    O  
ATOM    935  CB  VAL A 129      59.855 -13.481   2.730  1.00 91.00      A    C  
ANISOU  935  CB  VAL A 129    12324  10447  11805    222  -3311   1672  A    C  
ATOM    936  CG1 VAL A 129      58.769 -14.512   2.452  1.00 88.23      A    C  
ANISOU  936  CG1 VAL A 129    12121   9881  11522    179  -3263   1648  A    C  
ATOM    937  CG2 VAL A 129      60.831 -13.378   1.569  1.00 93.21      A    C  
ANISOU  937  CG2 VAL A 129    12356  10860  12200    474  -3370   1584  A    C  
ATOM    938  N   MET A 130      57.801 -12.658   4.902  1.00 82.95      A    N  
ANISOU  938  N   MET A 130    11666   9339  10511   -328  -3065   1811  A    N  
ATOM    939  CA  MET A 130      56.513 -12.766   5.585  1.00 82.18      A    C  
ANISOU  939  CA  MET A 130    11756   9133  10336   -554  -2933   1859  A    C  
ATOM    940  C   MET A 130      55.796 -11.425   5.680  1.00 87.89      A    C  
ANISOU  940  C   MET A 130    12401  10012  10981   -721  -2728   1804  A    C  
ATOM    941  O   MET A 130      54.586 -11.328   5.451  1.00 93.99      A    O  
ANISOU  941  O   MET A 130    13194  10756  11762   -844  -2558   1760  A    O  
ATOM    942  CB  MET A 130      56.670 -13.365   6.979  1.00 75.20      A    C  
ANISOU  942  CB  MET A 130    11127   8127   9320   -637  -3046   2028  A    C  
ATOM    943  CG  MET A 130      56.994 -14.844   6.958  1.00 85.18      A    C  
ANISOU  943  CG  MET A 130    12529   9173  10661   -504  -3203   2102  A    C  
ATOM    944  SD  MET A 130      56.140 -15.729   5.640  1.00108.38      A    S  
ANISOU  944  SD  MET A 130    15422  11951  13807   -450  -3124   1975  A    S  
ATOM    945  CE  MET A 130      54.435 -15.457   6.104  1.00 68.21      A    C  
ANISOU  945  CE  MET A 130    10450   6809   8656   -751  -2891   1982  A    C  
ATOM    946  N   GLN A 131      56.548 -10.393   6.029  1.00 78.62      A    N  
ANISOU  946  N   GLN A 131    11137   9003   9733   -726  -2743   1803  A    N  
ATOM    947  CA  GLN A 131      55.983  -9.065   6.116  1.00 78.84      A    C  
ANISOU  947  CA  GLN A 131    11092   9170   9693   -868  -2549   1748  A    C  
ATOM    948  C   GLN A 131      55.310  -8.660   4.801  1.00 76.06      A    C  
ANISOU  948  C   GLN A 131    10557   8884   9457   -813  -2375   1622  A    C  
ATOM    949  O   GLN A 131      54.201  -8.146   4.803  1.00 78.43      A    O  
ANISOU  949  O   GLN A 131    10876   9209   9715   -946  -2186   1591  A    O  
ATOM    950  CB  GLN A 131      57.072  -8.070   6.464  1.00 81.92      A    C  
ANISOU  950  CB  GLN A 131    11376   9719  10031   -850  -2607   1740  A    C  
ATOM    951  CG  GLN A 131      56.598  -6.931   7.308  1.00 88.36      A    C  
ANISOU  951  CG  GLN A 131    12250  10616  10706  -1050  -2470   1740  A    C  
ATOM    952  CD  GLN A 131      57.677  -5.910   7.482  1.00 87.84      A    C  
ANISOU  952  CD  GLN A 131    12049  10702  10623  -1034  -2515   1700  A    C  
ATOM    953  NE2 GLN A 131      57.681  -5.248   8.625  1.00 87.61      A    N  
ANISOU  953  NE2 GLN A 131    12128  10720  10440  -1193  -2507   1726  A    N  
ATOM    954  OE1 GLN A 131      58.509  -5.718   6.591  1.00 87.81      A    O  
ANISOU  954  OE1 GLN A 131    11842  10778  10744   -882  -2555   1642  A    O  
ATOM    955  N   MET A 132      55.984  -8.881   3.681  1.00 70.18      A    N  
ANISOU  955  N   MET A 132     9633   8184   8849   -605  -2436   1551  A    N  
ATOM    956  CA  MET A 132      55.428  -8.476   2.402  1.00 75.72      A    C  
ANISOU  956  CA  MET A 132    10150   8974   9645   -524  -2278   1433  A    C  
ATOM    957  C   MET A 132      54.198  -9.318   2.107  1.00 81.67      A    C  
ANISOU  957  C   MET A 132    10991   9607  10432   -579  -2212   1400  A    C  
ATOM    958  O   MET A 132      53.137  -8.783   1.809  1.00 86.51      A    O  
ANISOU  958  O   MET A 132    11564  10282  11025   -666  -2024   1343  A    O  
ATOM    959  CB  MET A 132      56.469  -8.559   1.280  1.00 79.03      A    C  
ANISOU  959  CB  MET A 132    10358   9480  10192   -274  -2362   1370  A    C  
ATOM    960  CG  MET A 132      57.650  -7.594   1.473  1.00 82.31      A    C  
ANISOU  960  CG  MET A 132    10648  10037  10590   -235  -2398   1389  A    C  
ATOM    961  SD  MET A 132      58.756  -7.474   0.048  1.00 82.18      A    S  
ANISOU  961  SD  MET A 132    10345  10158  10722     50  -2438   1316  A    S  
ATOM    962  CE  MET A 132      59.725  -8.966   0.267  1.00 66.51      A    C  
ANISOU  962  CE  MET A 132     8444   8047   8779    206  -2727   1369  A    C  
ATOM    963  N   LEU A 133      54.334 -10.633   2.224  1.00 76.92      A    N  
ANISOU  963  N   LEU A 133    10512   8831   9884   -531  -2366   1435  A    N  
ATOM    964  CA  LEU A 133      53.212 -11.540   2.054  1.00 74.09      A    C  
ANISOU  964  CA  LEU A 133    10254   8327   9570   -609  -2318   1404  A    C  
ATOM    965  C   LEU A 133      51.997 -11.148   2.911  1.00 80.39      A    C  
ANISOU  965  C   LEU A 133    11184   9107  10252   -864  -2156   1453  A    C  
ATOM    966  O   LEU A 133      50.882 -11.015   2.403  1.00 82.49      A    O  
ANISOU  966  O   LEU A 133    11394   9409  10541   -932  -2000   1370  A    O  
ATOM    967  CB  LEU A 133      53.649 -12.966   2.365  1.00 76.21      A    C  
ANISOU  967  CB  LEU A 133    10685   8376   9897   -549  -2510   1471  A    C  
ATOM    968  CG  LEU A 133      52.706 -14.105   1.994  1.00 81.85      A    C  
ANISOU  968  CG  LEU A 133    11486   8905  10709   -593  -2492   1418  A    C  
ATOM    969  CD1 LEU A 133      53.508 -15.341   1.627  1.00 87.16      A    C  
ANISOU  969  CD1 LEU A 133    12205   9413  11500   -406  -2688   1417  A    C  
ATOM    970  CD2 LEU A 133      51.786 -14.405   3.148  1.00 82.96      A    C  
ANISOU  970  CD2 LEU A 133    11854   8907  10762   -842  -2425   1530  A    C  
ATOM    971  N   LEU A 134      52.192 -10.956   4.207  1.00 77.11      A    N  
ANISOU  971  N   LEU A 134    10938   8654   9706   -998  -2192   1582  A    N  
ATOM    972  CA  LEU A 134      51.060 -10.579   5.042  1.00 71.38      A    C  
ANISOU  972  CA  LEU A 134    10339   7922   8860  -1229  -2035   1632  A    C  
ATOM    973  C   LEU A 134      50.507  -9.208   4.639  1.00 72.25      A    C  
ANISOU  973  C   LEU A 134    10294   8232   8925  -1270  -1829   1546  A    C  
ATOM    974  O   LEU A 134      49.303  -8.973   4.655  1.00 74.02      A    O  
ANISOU  974  O   LEU A 134    10532   8481   9112  -1400  -1657   1518  A    O  
ATOM    975  CB  LEU A 134      51.431 -10.650   6.525  1.00 68.76      A    C  
ANISOU  975  CB  LEU A 134    10223   7524   8379  -1344  -2120   1788  A    C  
ATOM    976  CG  LEU A 134      51.582 -12.112   6.987  1.00 71.78      A    C  
ANISOU  976  CG  LEU A 134    10800   7678   8796  -1334  -2272   1893  A    C  
ATOM    977  CD1 LEU A 134      52.324 -12.273   8.305  1.00 68.45      A    C  
ANISOU  977  CD1 LEU A 134    10564   7211   8231  -1362  -2410   2052  A    C  
ATOM    978  CD2 LEU A 134      50.224 -12.774   7.073  1.00 67.59      A    C  
ANISOU  978  CD2 LEU A 134    10379   7011   8290  -1495  -2147   1904  A    C  
ATOM    979  N   ASN A 135      51.382  -8.303   4.238  1.00 72.76      A    N  
ANISOU  979  N   ASN A 135    10205   8441   9000  -1153  -1837   1505  A    N  
ATOM    980  CA  ASN A 135      50.924  -6.972   3.875  1.00 67.77      A    C  
ANISOU  980  CA  ASN A 135     9440   7981   8330  -1180  -1634   1437  A    C  
ATOM    981  C   ASN A 135      49.983  -7.029   2.689  1.00 72.50      A    C  
ANISOU  981  C   ASN A 135     9895   8639   9013  -1115  -1495   1325  A    C  
ATOM    982  O   ASN A 135      48.952  -6.356   2.660  1.00 80.97      A    O  
ANISOU  982  O   ASN A 135    10944   9796  10025  -1208  -1301   1293  A    O  
ATOM    983  CB  ASN A 135      52.101  -6.066   3.553  1.00 60.30      A    C  
ANISOU  983  CB  ASN A 135     8343   7159   7409  -1056  -1667   1413  A    C  
ATOM    984  CG  ASN A 135      51.724  -4.612   3.584  1.00 67.48      A    C  
ANISOU  984  CG  ASN A 135     9181   8208   8251  -1126  -1461   1380  A    C  
ATOM    985  ND2 ASN A 135      52.339  -3.812   2.714  1.00 69.83      A    N  
ANISOU  985  ND2 ASN A 135     9281   8627   8623   -987  -1405   1320  A    N  
ATOM    986  OD1 ASN A 135      50.877  -4.207   4.378  1.00 73.54      A    O  
ANISOU  986  OD1 ASN A 135    10072   8969   8900  -1299  -1342   1411  A    O  
ATOM    987  N   GLY A 136      50.357  -7.827   1.700  1.00 71.01      A    N  
ANISOU  987  N   GLY A 136     9605   8419   8957   -942  -1599   1258  A    N  
ATOM    988  CA  GLY A 136      49.516  -8.056   0.539  1.00 70.46      A    C  
ANISOU  988  CA  GLY A 136     9397   8407   8967   -864  -1501   1136  A    C  
ATOM    989  C   GLY A 136      48.196  -8.744   0.857  1.00 72.95      A    C  
ANISOU  989  C   GLY A 136     9826   8627   9266  -1035  -1433   1126  A    C  
ATOM    990  O   GLY A 136      47.169  -8.438   0.243  1.00 71.00      A    O  
ANISOU  990  O   GLY A 136     9473   8487   9018  -1050  -1276   1036  A    O  
ATOM    991  N   LEU A 137      48.203  -9.678   1.805  1.00 68.20      A    N  
ANISOU  991  N   LEU A 137     9434   7830   8649  -1161  -1546   1222  A    N  
ATOM    992  CA  LEU A 137      46.935 -10.252   2.234  1.00 69.14      A    C  
ANISOU  992  CA  LEU A 137     9668   7854   8748  -1355  -1460   1232  A    C  
ATOM    993  C   LEU A 137      46.058  -9.178   2.878  1.00 74.92      A    C  
ANISOU  993  C   LEU A 137    10423   8710   9335  -1519  -1258   1267  A    C  
ATOM    994  O   LEU A 137      44.849  -9.166   2.662  1.00 75.66      A    O  
ANISOU  994  O   LEU A 137    10476   8851   9420  -1616  -1112   1210  A    O  
ATOM    995  CB  LEU A 137      47.122 -11.462   3.154  1.00 68.33      A    C  
ANISOU  995  CB  LEU A 137     9799   7505   8658  -1455  -1603   1349  A    C  
ATOM    996  CG  LEU A 137      47.712 -12.695   2.454  1.00 71.70      A    C  
ANISOU  996  CG  LEU A 137    10219   7779   9246  -1303  -1780   1296  A    C  
ATOM    997  CD1 LEU A 137      47.991 -13.818   3.425  1.00 68.55      A    C  
ANISOU  997  CD1 LEU A 137    10068   7128   8852  -1384  -1914   1436  A    C  
ATOM    998  CD2 LEU A 137      46.825 -13.184   1.326  1.00 73.07      A    C  
ANISOU  998  CD2 LEU A 137    10258   7964   9540  -1277  -1714   1129  A    C  
ATOM    999  N   TYR A 138      46.664  -8.263   3.641  1.00 74.76      A    N  
ANISOU  999  N   TYR A 138    10455   8748   9201  -1545  -1249   1351  A    N  
ATOM   1000  CA  TYR A 138      45.904  -7.175   4.266  1.00 68.92      A    C  
ANISOU 1000  CA  TYR A 138     9746   8124   8319  -1686  -1056   1378  A    C  
ATOM   1001  C   TYR A 138      45.201  -6.393   3.185  1.00 66.49      A    C  
ANISOU 1001  C   TYR A 138     9228   8000   8037  -1602   -875   1255  A    C  
ATOM   1002  O   TYR A 138      44.028  -6.035   3.303  1.00 70.32      A    O  
ANISOU 1002  O   TYR A 138     9705   8558   8453  -1711   -700   1235  A    O  
ATOM   1003  CB  TYR A 138      46.808  -6.224   5.049  1.00 67.60      A    C  
ANISOU 1003  CB  TYR A 138     9633   8006   8046  -1694  -1083   1448  A    C  
ATOM   1004  CG  TYR A 138      46.084  -5.029   5.664  1.00 68.69      A    C  
ANISOU 1004  CG  TYR A 138     9803   8257   8038  -1822   -881   1461  A    C  
ATOM   1005  CD1 TYR A 138      45.427  -5.138   6.894  1.00 71.53      A    C  
ANISOU 1005  CD1 TYR A 138    10360   8560   8259  -2019   -833   1555  A    C  
ATOM   1006  CD2 TYR A 138      46.079  -3.788   5.028  1.00 70.84      A    C  
ANISOU 1006  CD2 TYR A 138     9917   8690   8308  -1735   -732   1386  A    C  
ATOM   1007  CE1 TYR A 138      44.776  -4.052   7.467  1.00 73.99      A    C  
ANISOU 1007  CE1 TYR A 138    10707   8976   8430  -2124   -648   1561  A    C  
ATOM   1008  CE2 TYR A 138      45.420  -2.694   5.586  1.00 72.39      A    C  
ANISOU 1008  CE2 TYR A 138    10154   8978   8375  -1840   -543   1395  A    C  
ATOM   1009  CZ  TYR A 138      44.774  -2.834   6.803  1.00 83.18      A    C  
ANISOU 1009  CZ  TYR A 138    11715  10289   9602  -2033   -505   1476  A    C  
ATOM   1010  OH  TYR A 138      44.121  -1.755   7.354  1.00 93.10      A    O  
ANISOU 1010  OH  TYR A 138    13014  11638  10724  -2125   -316   1478  A    O  
ATOM   1011  N   TYR A 139      45.930  -6.142   2.112  1.00 62.12      A    N  
ANISOU 1011  N   TYR A 139     8496   7529   7577  -1394   -916   1176  A    N  
ATOM   1012  CA  TYR A 139      45.420  -5.280   1.065  1.00 63.62      A    C  
ANISOU 1012  CA  TYR A 139     8482   7912   7778  -1277   -743   1075  A    C  
ATOM   1013  C   TYR A 139      44.255  -5.928   0.348  1.00 69.39      A    C  
ANISOU 1013  C   TYR A 139     9131   8676   8557  -1283   -678    975  A    C  
ATOM   1014  O   TYR A 139      43.216  -5.292   0.166  1.00 69.35      A    O  
ANISOU 1014  O   TYR A 139     9055   8808   8486  -1322   -489    934  A    O  
ATOM   1015  CB  TYR A 139      46.531  -4.874   0.088  1.00 59.48      A    C  
ANISOU 1015  CB  TYR A 139     7788   7472   7341  -1043   -799   1029  A    C  
ATOM   1016  CG  TYR A 139      46.011  -4.182  -1.140  1.00 54.93      A    C  
ANISOU 1016  CG  TYR A 139     6997   7091   6784   -886   -632    928  A    C  
ATOM   1017  CD1 TYR A 139      45.614  -2.856  -1.097  1.00 49.40      A    C  
ANISOU 1017  CD1 TYR A 139     6247   6526   5997   -894   -424    941  A    C  
ATOM   1018  CD2 TYR A 139      45.922  -4.851  -2.347  1.00 63.14      A    C  
ANISOU 1018  CD2 TYR A 139     7886   8180   7924   -717   -681    819  A    C  
ATOM   1019  CE1 TYR A 139      45.106  -2.229  -2.215  1.00 48.67      A    C  
ANISOU 1019  CE1 TYR A 139     5964   6617   5911   -732   -263    863  A    C  
ATOM   1020  CE2 TYR A 139      45.440  -4.219  -3.478  1.00 69.41      A    C  
ANISOU 1020  CE2 TYR A 139     8480   9174   8717   -554   -530    730  A    C  
ATOM   1021  CZ  TYR A 139      45.033  -2.912  -3.399  1.00 62.85      A    C  
ANISOU 1021  CZ  TYR A 139     7608   8478   7795   -559   -319    761  A    C  
ATOM   1022  OH  TYR A 139      44.550  -2.285  -4.509  1.00 68.52      A    O  
ANISOU 1022  OH  TYR A 139     8134   9398   8501   -380   -163    689  A    O  
ATOM   1023  N   ILE A 140      44.411  -7.194  -0.044  1.00 73.55      A    N  
ANISOU 1023  N   ILE A 140     9666   9079   9199  -1246   -833    930  A    N  
ATOM   1024  CA  ILE A 140      43.367  -7.826  -0.847  1.00 71.71      A    C  
ANISOU 1024  CA  ILE A 140     9329   8887   9029  -1243   -784    803  A    C  
ATOM   1025  C   ILE A 140      42.116  -8.043  -0.022  1.00 71.31      A    C  
ANISOU 1025  C   ILE A 140     9392   8792   8909  -1489   -675    839  A    C  
ATOM   1026  O   ILE A 140      41.025  -7.718  -0.464  1.00 76.22      A    O  
ANISOU 1026  O   ILE A 140     9897   9564   9500  -1513   -521    756  A    O  
ATOM   1027  CB  ILE A 140      43.802  -9.130  -1.538  1.00 66.70      A    C  
ANISOU 1027  CB  ILE A 140     8673   8124   8546  -1141   -970    721  A    C  
ATOM   1028  CG1 ILE A 140      43.967 -10.247  -0.536  1.00 77.80      A    C  
ANISOU 1028  CG1 ILE A 140    10310   9264   9985  -1304  -1107    819  A    C  
ATOM   1029  CG2 ILE A 140      45.084  -8.937  -2.326  1.00 61.95      A    C  
ANISOU 1029  CG2 ILE A 140     7957   7573   8007   -888  -1078    694  A    C  
ATOM   1030  CD1 ILE A 140      44.451 -11.491  -1.183  1.00 86.38      A    C  
ANISOU 1030  CD1 ILE A 140    11392  10205  11225  -1193  -1285    741  A    C  
ATOM   1031  N   HIS A 141      42.276  -8.558   1.189  1.00 69.77      A    N  
ANISOU 1031  N   HIS A 141     9421   8409   8679  -1664   -748    969  A    N  
ATOM   1032  CA  HIS A 141      41.136  -8.743   2.077  1.00 70.83      A    C  
ANISOU 1032  CA  HIS A 141     9676   8500   8737  -1905   -634   1028  A    C  
ATOM   1033  C   HIS A 141      40.385  -7.442   2.370  1.00 74.98      A    C  
ANISOU 1033  C   HIS A 141    10153   9223   9114  -1959   -415   1042  A    C  
ATOM   1034  O   HIS A 141      39.153  -7.438   2.465  1.00 77.26      A    O  
ANISOU 1034  O   HIS A 141    10413   9582   9361  -2086   -271   1012  A    O  
ATOM   1035  CB  HIS A 141      41.575  -9.404   3.377  1.00 72.71      A    C  
ANISOU 1035  CB  HIS A 141    10172   8515   8939  -2054   -746   1190  A    C  
ATOM   1036  CG  HIS A 141      42.123 -10.780   3.186  1.00 69.95      A    C  
ANISOU 1036  CG  HIS A 141     9897   7947   8733  -2019   -939   1188  A    C  
ATOM   1037  CD2 HIS A 141      42.010 -11.642   2.148  1.00 67.56      A    C  
ANISOU 1037  CD2 HIS A 141     9487   7595   8589  -1932  -1010   1054  A    C  
ATOM   1038  ND1 HIS A 141      42.918 -11.405   4.125  1.00 67.14      A    N  
ANISOU 1038  ND1 HIS A 141     9753   7392   8363  -2061  -1087   1334  A    N  
ATOM   1039  CE1 HIS A 141      43.265 -12.596   3.672  1.00 75.07      A    C  
ANISOU 1039  CE1 HIS A 141    10785   8222   9518  -1998  -1233   1297  A    C  
ATOM   1040  NE2 HIS A 141      42.724 -12.767   2.476  1.00 75.01      A    N  
ANISOU 1040  NE2 HIS A 141    10587   8295   9620  -1926  -1191   1122  A    N  
ATOM   1041  N   ARG A 142      41.128  -6.346   2.506  1.00 72.80      A    N  
ANISOU 1041  N   ARG A 142     9864   9033   8763  -1863   -387   1083  A    N  
ATOM   1042  CA  ARG A 142      40.525  -5.039   2.731  1.00 66.68      A    C  
ANISOU 1042  CA  ARG A 142     9049   8431   7855  -1888   -177   1092  A    C  
ATOM   1043  C   ARG A 142      39.642  -4.741   1.537  1.00 66.16      A    C  
ANISOU 1043  C   ARG A 142     8757   8560   7821  -1775    -39    956  A    C  
ATOM   1044  O   ARG A 142      38.581  -4.145   1.675  1.00 73.81      A    O  
ANISOU 1044  O   ARG A 142     9688   9661   8694  -1842    148    944  A    O  
ATOM   1045  CB  ARG A 142      41.599  -3.952   2.903  1.00 72.72      A    C  
ANISOU 1045  CB  ARG A 142     9820   9238   8572  -1786   -182   1136  A    C  
ATOM   1046  CG  ARG A 142      41.110  -2.671   3.574  1.00 82.59      A    C  
ANISOU 1046  CG  ARG A 142    11117  10595   9668  -1862     14   1178  A    C  
ATOM   1047  CD  ARG A 142      42.246  -1.679   3.935  1.00122.91      A    C  
ANISOU 1047  CD  ARG A 142    16263  15701  14737  -1804     -8   1221  A    C  
ATOM   1048  NE  ARG A 142      43.082  -1.332   2.783  1.00127.56      A    N  
ANISOU 1048  NE  ARG A 142    16671  16356  15438  -1586    -42   1156  A    N  
ATOM   1049  CZ  ARG A 142      42.782  -0.398   1.880  1.00130.75      A    C  
ANISOU 1049  CZ  ARG A 142    16910  16920  15849  -1443    128   1093  A    C  
ATOM   1050  NH1 ARG A 142      41.656   0.298   1.990  1.00138.87      A    N1+
ANISOU 1050  NH1 ARG A 142    17927  18060  16777  -1489    341   1082  A    N1+
ATOM   1051  NH2 ARG A 142      43.602  -0.160   0.860  1.00120.39      A    N  
ANISOU 1051  NH2 ARG A 142    15442  15662  14639  -1242     93   1050  A    N  
ATOM   1052  N   ASN A 143      40.069  -5.183   0.359  1.00 61.60      A    N  
ANISOU 1052  N   ASN A 143     8026   8012   7369  -1593   -134    852  A    N  
ATOM   1053  CA  ASN A 143      39.309  -4.938  -0.860  1.00 60.32      A    C  
ANISOU 1053  CA  ASN A 143     7635   8054   7228  -1454    -22    714  A    C  
ATOM   1054  C   ASN A 143      38.323  -6.043  -1.169  1.00 71.38      A    C  
ANISOU 1054  C   ASN A 143     8990   9434   8698  -1551    -47    615  A    C  
ATOM   1055  O   ASN A 143      37.859  -6.173  -2.310  1.00 67.87      A    O  
ANISOU 1055  O   ASN A 143     8346   9141   8302  -1418    -20    471  A    O  
ATOM   1056  CB  ASN A 143      40.239  -4.713  -2.042  1.00 66.20      A    C  
ANISOU 1056  CB  ASN A 143     8219   8880   8054  -1185    -89    644  A    C  
ATOM   1057  CG  ASN A 143      40.851  -3.330  -2.030  1.00 74.69      A    C  
ANISOU 1057  CG  ASN A 143     9265  10054   9058  -1072     21    709  A    C  
ATOM   1058  ND2 ASN A 143      41.958  -3.179  -1.316  1.00 72.08      A    N  
ANISOU 1058  ND2 ASN A 143     9067   9589   8733  -1106    -81    808  A    N  
ATOM   1059  OD1 ASN A 143      40.325  -2.405  -2.645  1.00 77.97      A    O  
ANISOU 1059  OD1 ASN A 143     9543  10666   9416   -956    199    669  A    O  
ATOM   1060  N   LYS A 144      38.025  -6.845  -0.143  1.00 75.93      A    N  
ANISOU 1060  N   LYS A 144     9750   9823   9278  -1784    -98    693  A    N  
ATOM   1061  CA  LYS A 144      36.911  -7.772  -0.192  1.00 73.02      A    C  
ANISOU 1061  CA  LYS A 144     9357   9425   8961  -1940    -77    619  A    C  
ATOM   1062  C   LYS A 144      37.192  -8.911  -1.170  1.00 75.26      A    C  
ANISOU 1062  C   LYS A 144     9553   9627   9415  -1847   -241    481  A    C  
ATOM   1063  O   LYS A 144      36.277  -9.458  -1.790  1.00 75.97      A    O  
ANISOU 1063  O   LYS A 144     9513   9784   9566  -1885   -211    341  A    O  
ATOM   1064  CB  LYS A 144      35.621  -7.017  -0.567  1.00 70.27      A    C  
ANISOU 1064  CB  LYS A 144     8839   9339   8521  -1945    138    540  A    C  
ATOM   1065  CG  LYS A 144      35.182  -5.972   0.463  1.00 72.64      A    C  
ANISOU 1065  CG  LYS A 144     9241   9710   8651  -2055    315    668  A    C  
ATOM   1066  CD  LYS A 144      35.209  -6.600   1.849  1.00 95.06      A    C  
ANISOU 1066  CD  LYS A 144    12332  12321  11466  -2302    264    814  A    C  
ATOM   1067  CE  LYS A 144      34.990  -5.603   2.978  1.00103.14      A    C  
ANISOU 1067  CE  LYS A 144    13489  13389  12311  -2401    409    947  A    C  
ATOM   1068  NZ  LYS A 144      35.004  -6.306   4.308  1.00105.19      A    N1+
ANISOU 1068  NZ  LYS A 144    13993  13438  12538  -2630    355   1092  A    N1+
ATOM   1069  N   ILE A 145      38.463  -9.275  -1.298  1.00 67.20      A    N  
ANISOU 1069  N   ILE A 145     8599   8465   8471  -1724   -416    513  A    N  
ATOM   1070  CA  ILE A 145      38.849 -10.356  -2.195  1.00 64.42      A    C  
ANISOU 1070  CA  ILE A 145     8181   8018   8278  -1616   -581    386  A    C  
ATOM   1071  C   ILE A 145      39.456 -11.511  -1.412  1.00 65.70      A    C  
ANISOU 1071  C   ILE A 145     8571   7864   8529  -1734   -750    482  A    C  
ATOM   1072  O   ILE A 145      40.198 -11.281  -0.463  1.00 71.54      A    O  
ANISOU 1072  O   ILE A 145     9482   8494   9206  -1774   -796    647  A    O  
ATOM   1073  CB  ILE A 145      39.874  -9.861  -3.218  1.00 63.19      A    C  
ANISOU 1073  CB  ILE A 145     7881   7983   8145  -1318   -646    326  A    C  
ATOM   1074  CG1 ILE A 145      39.296  -8.705  -4.033  1.00 63.35      A    C  
ANISOU 1074  CG1 ILE A 145     7681   8314   8073  -1175   -468    246  A    C  
ATOM   1075  CG2 ILE A 145      40.314 -10.985  -4.138  1.00 59.82      A    C  
ANISOU 1075  CG2 ILE A 145     7393   7462   7873  -1189   -820    189  A    C  
ATOM   1076  CD1 ILE A 145      38.227  -9.120  -4.974  1.00 70.46      A    C  
ANISOU 1076  CD1 ILE A 145     8397   9362   9013  -1151   -421     57  A    C  
ATOM   1077  N   LEU A 146      39.130 -12.747  -1.797  1.00 66.25      A    N  
ANISOU 1077  N   LEU A 146     8644   7788   8741  -1789   -840    376  A    N  
ATOM   1078  CA  LEU A 146      39.842 -13.926  -1.297  1.00 69.60      A    C  
ANISOU 1078  CA  LEU A 146     9271   7900   9274  -1839  -1016    451  A    C  
ATOM   1079  C   LEU A 146      40.734 -14.498  -2.392  1.00 77.81      A    C  
ANISOU 1079  C   LEU A 146    10218   8903  10442  -1596  -1185    322  A    C  
ATOM   1080  O   LEU A 146      40.305 -14.631  -3.542  1.00 80.50      A    O  
ANISOU 1080  O   LEU A 146    10362   9379  10846  -1489  -1174    123  A    O  
ATOM   1081  CB  LEU A 146      38.877 -15.004  -0.837  1.00 72.02      A    C  
ANISOU 1081  CB  LEU A 146     9684   8014   9667  -2094   -994    441  A    C  
ATOM   1082  CG  LEU A 146      37.851 -14.524   0.181  1.00 80.12      A    C  
ANISOU 1082  CG  LEU A 146    10781   9090  10569  -2341   -812    555  A    C  
ATOM   1083  CD1 LEU A 146      36.932 -15.660   0.542  1.00 80.90      A    C  
ANISOU 1083  CD1 LEU A 146    10969   8991  10777  -2590   -788    540  A    C  
ATOM   1084  CD2 LEU A 146      38.546 -13.985   1.408  1.00 78.07      A    C  
ANISOU 1084  CD2 LEU A 146    10724   8765  10174  -2378   -817    785  A    C  
ATOM   1085  N   HIS A 147      41.970 -14.843  -2.035  1.00 73.89      A    N  
ANISOU 1085  N   HIS A 147     9861   8239   9975  -1499  -1342    431  A    N  
ATOM   1086  CA  HIS A 147      42.913 -15.359  -3.016  1.00 73.65      A    C  
ANISOU 1086  CA  HIS A 147     9751   8176  10056  -1251  -1503    324  A    C  
ATOM   1087  C   HIS A 147      42.574 -16.788  -3.388  1.00 74.85      A    C  
ANISOU 1087  C   HIS A 147     9954   8107  10377  -1303  -1600    201  A    C  
ATOM   1088  O   HIS A 147      42.509 -17.140  -4.574  1.00 71.00      A    O  
ANISOU 1088  O   HIS A 147     9304   7693   9981  -1152  -1647     -2  A    O  
ATOM   1089  CB  HIS A 147      44.344 -15.293  -2.494  1.00 79.82      A    C  
ANISOU 1089  CB  HIS A 147    10655   8857  10815  -1129  -1642    479  A    C  
ATOM   1090  CG  HIS A 147      45.359 -15.666  -3.521  1.00 83.21      A    C  
ANISOU 1090  CG  HIS A 147    10980   9296  11341   -851  -1791    377  A    C  
ATOM   1091  CD2 HIS A 147      46.079 -14.909  -4.383  1.00 80.64      A    C  
ANISOU 1091  CD2 HIS A 147    10466   9184  10989   -606  -1798    321  A    C  
ATOM   1092  ND1 HIS A 147      45.697 -16.975  -3.789  1.00 85.17      A    N  
ANISOU 1092  ND1 HIS A 147    11314   9313  11733   -797  -1947    316  A    N  
ATOM   1093  CE1 HIS A 147      46.593 -17.006  -4.756  1.00 84.48      A    C  
ANISOU 1093  CE1 HIS A 147    11096   9307  11697   -524  -2050    224  A    C  
ATOM   1094  NE2 HIS A 147      46.845 -15.765  -5.134  1.00 78.84      A    N  
ANISOU 1094  NE2 HIS A 147    10210   8866  10880   -405  -1960    230  A    N  
ATOM   1095  N   ARG A 148      42.372 -17.599  -2.353  1.00 75.89      A    N  
ANISOU 1095  N   ARG A 148    10320   7965  10548  -1515  -1627    327  A    N  
ATOM   1096  CA  ARG A 148      41.886 -18.970  -2.490  1.00 81.28      A    C  
ANISOU 1096  CA  ARG A 148    11091   8393  11401  -1630  -1686    235  A    C  
ATOM   1097  C   ARG A 148      42.833 -19.912  -3.214  1.00 85.13      A    C  
ANISOU 1097  C   ARG A 148    11597   8716  12032  -1418  -1878    141  A    C  
ATOM   1098  O   ARG A 148      42.388 -20.893  -3.790  1.00 88.95      A    O  
ANISOU 1098  O   ARG A 148    12067   9060  12668  -1452  -1921    -23  A    O  
ATOM   1099  CB  ARG A 148      40.549 -18.983  -3.208  1.00 81.67      A    C  
ANISOU 1099  CB  ARG A 148    10954   8586  11492  -1742  -1564     28  A    C  
ATOM   1100  CG  ARG A 148      39.489 -18.180  -2.519  1.00 91.25      A    C  
ANISOU 1100  CG  ARG A 148    12145   9952  12575  -1959  -1367    107  A    C  
ATOM   1101  CD  ARG A 148      38.122 -18.768  -2.822  1.00 96.66      A    C  
ANISOU 1101  CD  ARG A 148    12745  10628  13353  -2166  -1276    -54  A    C  
ATOM   1102  NE  ARG A 148      37.791 -18.681  -4.239  1.00 92.24      A    N  
ANISOU 1102  NE  ARG A 148    11915  10290  12842  -2005  -1286   -324  A    N  
ATOM   1103  CZ  ARG A 148      36.623 -19.052  -4.745  1.00 94.79      A    C  
ANISOU 1103  CZ  ARG A 148    12096  10686  13235  -2140  -1216   -516  A    C  
ATOM   1104  NH1 ARG A 148      35.686 -19.541  -3.946  1.00102.52      A    N1+
ANISOU 1104  NH1 ARG A 148    13177  11519  14258  -2449  -1123   -460  A    N1+
ATOM   1105  NH2 ARG A 148      36.392 -18.937  -6.045  1.00 93.84      A    N  
ANISOU 1105  NH2 ARG A 148    11725  10792  13137  -1965  -1238   -765  A    N  
ATOM   1106  N   ASP A 149      44.128 -19.623  -3.193  1.00 84.59      A    N  
ANISOU 1106  N   ASP A 149    11553   8666  11920  -1199  -1994    235  A    N  
ATOM   1107  CA  ASP A 149      45.084 -20.482  -3.874  1.00 93.36      A    C  
ANISOU 1107  CA  ASP A 149    12678   9637  13158   -973  -2175    153  A    C  
ATOM   1108  C   ASP A 149      46.486 -20.126  -3.423  1.00 90.47      A    C  
ANISOU 1108  C   ASP A 149    12384   9272  12717   -795  -2287    327  A    C  
ATOM   1109  O   ASP A 149      47.429 -20.047  -4.221  1.00 86.90      A    O  
ANISOU 1109  O   ASP A 149    11817   8913  12290   -527  -2391    256  A    O  
ATOM   1110  CB  ASP A 149      44.945 -20.368  -5.396  1.00101.62      A    C  
ANISOU 1110  CB  ASP A 149    13461  10893  14258   -772  -2183   -111  A    C  
ATOM   1111  CG  ASP A 149      45.723 -21.447  -6.141  1.00101.70      A    C  
ANISOU 1111  CG  ASP A 149    13495  10730  14417   -563  -2362   -232  A    C  
ATOM   1112  OD1 ASP A 149      46.122 -22.438  -5.489  1.00 98.94      A    O  
ANISOU 1112  OD1 ASP A 149    13377  10060  14156   -615  -2465   -131  A    O  
ATOM   1113  OD2 ASP A 149      45.937 -21.295  -7.368  1.00 98.67      A    O1-
ANISOU 1113  OD2 ASP A 149    12903  10534  14054   -334  -2396   -422  A    O1-
ATOM   1114  N   MET A 150      46.608 -19.906  -2.123  1.00 86.16      A    N  
ANISOU 1114  N   MET A 150    12025   8638  12074   -948  -2264    553  A    N  
ATOM   1115  CA  MET A 150      47.894 -19.618  -1.526  1.00 84.01      A    C  
ANISOU 1115  CA  MET A 150    11837   8360  11724   -813  -2377    725  A    C  
ATOM   1116  C   MET A 150      48.793 -20.831  -1.631  1.00 95.42      A    C  
ANISOU 1116  C   MET A 150    13413   9550  13292   -656  -2568    740  A    C  
ATOM   1117  O   MET A 150      48.412 -21.928  -1.246  1.00106.08      A    O  
ANISOU 1117  O   MET A 150    14952  10615  14740   -774  -2597    768  A    O  
ATOM   1118  CB  MET A 150      47.709 -19.244  -0.062  1.00 83.05      A    C  
ANISOU 1118  CB  MET A 150    11903   8186  11465  -1025  -2313    951  A    C  
ATOM   1119  CG  MET A 150      47.111 -17.878   0.126  1.00 78.67      A    C  
ANISOU 1119  CG  MET A 150    11225   7902  10764  -1131  -2140    959  A    C  
ATOM   1120  SD  MET A 150      48.206 -16.643  -0.566  1.00 89.36      A    S  
ANISOU 1120  SD  MET A 150    12353   9551  12047   -871  -2170    920  A    S  
ATOM   1121  CE  MET A 150      49.588 -16.827   0.540  1.00 98.72      A    C  
ANISOU 1121  CE  MET A 150    13730  10613  13168   -808  -2342   1135  A    C  
ATOM   1122  N   LYS A 151      49.986 -20.630  -2.168  1.00 98.77      A    N  
ANISOU 1122  N   LYS A 151    13736  10076  13716   -386  -2690    722  A    N  
ATOM   1123  CA  LYS A 151      50.996 -21.680  -2.220  1.00100.88      A    C  
ANISOU 1123  CA  LYS A 151    14122  10128  14079   -199  -2878    755  A    C  
ATOM   1124  C   LYS A 151      52.276 -21.044  -2.736  1.00 97.15      A    C  
ANISOU 1124  C   LYS A 151    13484   9869  13561     80  -2973    753  A    C  
ATOM   1125  O   LYS A 151      52.235 -20.196  -3.621  1.00 98.50      A    O  
ANISOU 1125  O   LYS A 151    13417  10304  13706    179  -2902    629  A    O  
ATOM   1126  CB  LYS A 151      50.541 -22.867  -3.089  1.00 98.96      A    C  
ANISOU 1126  CB  LYS A 151    13893   9689  14020   -159  -2920    564  A    C  
ATOM   1127  CG  LYS A 151      50.467 -22.606  -4.592  1.00103.69      A    C  
ANISOU 1127  CG  LYS A 151    14222  10502  14676     29  -2909    310  A    C  
ATOM   1128  CD  LYS A 151      49.756 -23.747  -5.341  1.00110.94      A    C  
ANISOU 1128  CD  LYS A 151    15160  11226  15767      3  -2929     98  A    C  
ATOM   1129  CE  LYS A 151      49.858 -23.585  -6.867  1.00118.03      A    C  
ANISOU 1129  CE  LYS A 151    15797  12342  16708    243  -2949   -158  A    C  
ATOM   1130  NZ  LYS A 151      48.618 -24.027  -7.609  1.00124.08      A    N1+
ANISOU 1130  NZ  LYS A 151    16480  13096  17571    121  -2875   -402  A    N1+
ATOM   1131  N   ALA A 152      53.406 -21.421  -2.160  1.00 96.16      A    N  
ANISOU 1131  N   ALA A 152    13479   9640  13418    207  -3125    899  A    N  
ATOM   1132  CA  ALA A 152      54.669 -20.778  -2.489  1.00 99.80      A    C  
ANISOU 1132  CA  ALA A 152    13782  10309  13827    448  -3214    921  A    C  
ATOM   1133  C   ALA A 152      54.829 -20.516  -3.985  1.00103.73      A    C  
ANISOU 1133  C   ALA A 152    14017  11001  14395    666  -3199    712  A    C  
ATOM   1134  O   ALA A 152      55.474 -19.547  -4.385  1.00109.22      A    O  
ANISOU 1134  O   ALA A 152    14516  11954  15029    797  -3180    707  A    O  
ATOM   1135  CB  ALA A 152      55.821 -21.605  -1.980  1.00107.21      A    C  
ANISOU 1135  CB  ALA A 152    14872  11076  14786    610  -3406   1050  A    C  
ATOM   1136  N   ALA A 153      54.244 -21.378  -4.812  1.00 98.51      A    N  
ANISOU 1136  N   ALA A 153    13351  10218  13861    704  -3204    537  A    N  
ATOM   1137  CA  ALA A 153      54.387 -21.248  -6.261  1.00 97.56      A    C  
ANISOU 1137  CA  ALA A 153    12992  10279  13798    933  -3202    328  A    C  
ATOM   1138  C   ALA A 153      53.788 -19.938  -6.773  1.00101.80      A    C  
ANISOU 1138  C   ALA A 153    13301  11132  14245    883  -3026    258  A    C  
ATOM   1139  O   ALA A 153      54.287 -19.322  -7.722  1.00103.93      A    O  
ANISOU 1139  O   ALA A 153    13347  11643  14498   1098  -3009    176  A    O  
ATOM   1140  CB  ALA A 153      53.759 -22.441  -6.953  1.00 98.98      A    C  
ANISOU 1140  CB  ALA A 153    13226  10257  14125    950  -3239    140  A    C  
ATOM   1141  N   ASN A 154      52.716 -19.517  -6.118  1.00102.32      A    N  
ANISOU 1141  N   ASN A 154    13432  11193  14251    605  -2887    303  A    N  
ATOM   1142  CA  ASN A 154      52.018 -18.297  -6.469  1.00 98.94      A    C  
ANISOU 1142  CA  ASN A 154    12821  11040  13732    537  -2706    253  A    C  
ATOM   1143  C   ASN A 154      52.585 -17.041  -5.791  1.00 98.94      A    C  
ANISOU 1143  C   ASN A 154    12782  11210  13600    504  -2646    421  A    C  
ATOM   1144  O   ASN A 154      52.036 -15.945  -5.933  1.00 95.77      A    O  
ANISOU 1144  O   ASN A 154    12255  11018  13116    436  -2483    408  A    O  
ATOM   1145  CB  ASN A 154      50.541 -18.465  -6.152  1.00 94.39      A    C  
ANISOU 1145  CB  ASN A 154    12319  10389  13157    263  -2579    204  A    C  
ATOM   1146  CG  ASN A 154      49.850 -19.373  -7.129  1.00100.71      A    C  
ANISOU 1146  CG  ASN A 154    13064  11121  14081    304  -2598    -22  A    C  
ATOM   1147  ND2 ASN A 154      48.919 -20.177  -6.630  1.00 98.78      A    N  
ANISOU 1147  ND2 ASN A 154    12978  10653  13903     71  -2577    -40  A    N  
ATOM   1148  OD1 ASN A 154      50.140 -19.347  -8.328  1.00105.48      A    O  
ANISOU 1148  OD1 ASN A 154    13481  11879  14719    541  -2627   -184  A    O  
ATOM   1149  N   VAL A 155      53.686 -17.199  -5.063  1.00 92.82      A    N  
ANISOU 1149  N   VAL A 155    12113  10346  12807    558  -2778    572  A    N  
ATOM   1150  CA  VAL A 155      54.341 -16.057  -4.442  1.00 86.86      A    C  
ANISOU 1150  CA  VAL A 155    11314   9750  11940    534  -2743    710  A    C  
ATOM   1151  C   VAL A 155      55.596 -15.728  -5.236  1.00 81.38      A    C  
ANISOU 1151  C   VAL A 155    10427   9221  11273    817  -2820    684  A    C  
ATOM   1152  O   VAL A 155      56.552 -16.469  -5.202  1.00 92.40      A    O  
ANISOU 1152  O   VAL A 155    11872  10515  12721    971  -2989    718  A    O  
ATOM   1153  CB  VAL A 155      54.718 -16.355  -2.973  1.00 87.14      A    C  
ANISOU 1153  CB  VAL A 155    11587   9609  11912    387  -2835    904  A    C  
ATOM   1154  CG1 VAL A 155      55.214 -15.105  -2.279  1.00 81.30      A    C  
ANISOU 1154  CG1 VAL A 155    10800   9041  11047    320  -2783   1020  A    C  
ATOM   1155  CG2 VAL A 155      53.527 -16.902  -2.230  1.00 90.98      A    C  
ANISOU 1155  CG2 VAL A 155    12277   9902  12389    128  -2769    938  A    C  
ATOM   1156  N   LEU A 156      55.593 -14.621  -5.958  1.00 73.29      A    N  
ANISOU 1156  N   LEU A 156     9183   8451  10213    893  -2688    629  A    N  
ATOM   1157  CA  LEU A 156      56.742 -14.268  -6.768  1.00 76.29      A    C  
ANISOU 1157  CA  LEU A 156     9365   9000  10623   1158  -2737    607  A    C  
ATOM   1158  C   LEU A 156      57.611 -13.272  -6.035  1.00 89.94      A    C  
ANISOU 1158  C   LEU A 156    11060  10834  12279   1112  -2731    750  A    C  
ATOM   1159  O   LEU A 156      57.207 -12.707  -5.022  1.00 97.42      A    O  
ANISOU 1159  O   LEU A 156    12118  11756  13142    882  -2663    844  A    O  
ATOM   1160  CB  LEU A 156      56.292 -13.637  -8.077  1.00 75.23      A    C  
ANISOU 1160  CB  LEU A 156     8997   9090  10496   1294  -2588    468  A    C  
ATOM   1161  CG  LEU A 156      55.119 -14.311  -8.786  1.00 76.12      A    C  
ANISOU 1161  CG  LEU A 156     9114   9158  10652   1284  -2543    301  A    C  
ATOM   1162  CD1 LEU A 156      54.917 -13.650 -10.130  1.00 77.36      A    C  
ANISOU 1162  CD1 LEU A 156     9017   9578  10797   1478  -2416    175  A    C  
ATOM   1163  CD2 LEU A 156      55.348 -15.802  -8.947  1.00 73.55      A    C  
ANISOU 1163  CD2 LEU A 156     8906   8610  10431   1376  -2727    229  A    C  
ATOM   1164  N   ILE A 157      58.812 -13.064  -6.562  1.00 88.89      A    N  
ANISOU 1164  N   ILE A 157    10768  10827  12181   1333  -2802    758  A    N  
ATOM   1165  CA  ILE A 157      59.685 -11.996  -6.111  1.00 82.85      A    C  
ANISOU 1165  CA  ILE A 157     9908  10204  11366   1310  -2777    861  A    C  
ATOM   1166  C   ILE A 157      60.420 -11.413  -7.309  1.00 91.23      A    C  
ANISOU 1166  C   ILE A 157    10699  11488  12477   1555  -2723    805  A    C  
ATOM   1167  O   ILE A 157      60.855 -12.151  -8.191  1.00101.76      A    O  
ANISOU 1167  O   ILE A 157    11951  12831  13881   1793  -2812    730  A    O  
ATOM   1168  CB  ILE A 157      60.737 -12.502  -5.134  1.00 77.39      A    C  
ANISOU 1168  CB  ILE A 157     9332   9410  10663   1311  -2979    978  A    C  
ATOM   1169  CG1 ILE A 157      60.102 -13.346  -4.033  1.00 62.54      A    C  
ANISOU 1169  CG1 ILE A 157     7735   7286   8741   1120  -3057   1044  A    C  
ATOM   1170  CG2 ILE A 157      61.511 -11.324  -4.546  1.00 79.33      A    C  
ANISOU 1170  CG2 ILE A 157     9485   9805  10850   1234  -2946   1069  A    C  
ATOM   1171  CD1 ILE A 157      61.085 -13.650  -2.914  1.00 56.11      A    C  
ANISOU 1171  CD1 ILE A 157     7040   6400   7878   1104  -3236   1181  A    C  
ATOM   1172  N   THR A 158      60.571 -10.093  -7.332  1.00 93.12      A    N  
ANISOU 1172  N   THR A 158    10804  11899  12679   1500  -2570    846  A    N  
ATOM   1173  CA  THR A 158      61.251  -9.414  -8.431  1.00104.03      A    C  
ANISOU 1173  CA  THR A 158    11926  13496  14106   1716  -2485    815  A    C  
ATOM   1174  C   THR A 158      62.756  -9.366  -8.210  1.00110.17      A    C  
ANISOU 1174  C   THR A 158    12609  14330  14921   1823  -2621    891  A    C  
ATOM   1175  O   THR A 158      63.237  -9.693  -7.128  1.00104.04      A    O  
ANISOU 1175  O   THR A 158    11966  13445  14119   1712  -2769    970  A    O  
ATOM   1176  CB  THR A 158      60.758  -7.967  -8.589  1.00107.15      A    C  
ANISOU 1176  CB  THR A 158    12215  14040  14457   1613  -2239    833  A    C  
ATOM   1177  CG2 THR A 158      59.273  -7.944  -8.874  1.00105.53      A    C  
ANISOU 1177  CG2 THR A 158    12073  13816  14206   1528  -2095    756  A    C  
ATOM   1178  OG1 THR A 158      61.021  -7.234  -7.384  1.00108.30      A    O  
ANISOU 1178  OG1 THR A 158    12446  14150  14552   1384  -2229    936  A    O  
ATOM   1179  N   ARG A 159      63.490  -8.951  -9.240  1.00116.24      A    N  
ANISOU 1179  N   ARG A 159    13140  15284  15743   2045  -2567    868  A    N  
ATOM   1180  CA  ARG A 159      64.926  -8.770  -9.116  1.00113.84      A    C  
ANISOU 1180  CA  ARG A 159    12703  15071  15480   2146  -2670    937  A    C  
ATOM   1181  C   ARG A 159      65.200  -7.932  -7.880  1.00105.08      A    C  
ANISOU 1181  C   ARG A 159    11655  13946  14324   1889  -2660   1034  A    C  
ATOM   1182  O   ARG A 159      66.010  -8.310  -7.042  1.00107.62      A    O  
ANISOU 1182  O   ARG A 159    12036  14219  14637   1855  -2841   1094  A    O  
ATOM   1183  CB  ARG A 159      65.515  -8.075 -10.348  1.00123.82      A    C  
ANISOU 1183  CB  ARG A 159    13687  16562  16800   2365  -2538    917  A    C  
ATOM   1184  CG  ARG A 159      65.471  -8.899 -11.632  1.00133.45      A    C  
ANISOU 1184  CG  ARG A 159    14814  17833  18057   2665  -2566    815  A    C  
ATOM   1185  CD  ARG A 159      66.427  -8.365 -12.716  1.00137.25      A    C  
ANISOU 1185  CD  ARG A 159    15011  18546  18591   2917  -2485    825  A    C  
ATOM   1186  NE  ARG A 159      67.842  -8.625 -12.419  1.00139.73      A    N  
ANISOU 1186  NE  ARG A 159    15236  18900  18954   3012  -2650    889  A    N  
ATOM   1187  CZ  ARG A 159      68.468  -9.787 -12.633  1.00141.34      A    C  
ANISOU 1187  CZ  ARG A 159    15452  19062  19188   3221  -2851    854  A    C  
ATOM   1188  NH1 ARG A 159      67.811 -10.826 -13.141  1.00143.11      A    N1+
ANISOU 1188  NH1 ARG A 159    15786  19183  19408   3347  -2917    747  A    N1+
ATOM   1189  NH2 ARG A 159      69.756  -9.918 -12.329  1.00137.21      A    N  
ANISOU 1189  NH2 ARG A 159    14832  18600  18702   3305  -2989    920  A    N  
ATOM   1190  N   ASP A 160      64.506  -6.805  -7.752  1.00 88.95      A    N  
ANISOU 1190  N   ASP A 160     9603  11950  12244   1714  -2451   1043  A    N  
ATOM   1191  CA  ASP A 160      64.803  -5.872  -6.672  1.00 90.38      A    C  
ANISOU 1191  CA  ASP A 160     9820  12134  12385   1478  -2421   1115  A    C  
ATOM   1192  C   ASP A 160      64.243  -6.296  -5.317  1.00 92.65      A    C  
ANISOU 1192  C   ASP A 160    10377  12246  12581   1244  -2525   1151  A    C  
ATOM   1193  O   ASP A 160      64.134  -5.465  -4.405  1.00 97.73      A    O  
ANISOU 1193  O   ASP A 160    11084  12883  13165   1020  -2464   1192  A    O  
ATOM   1194  CB  ASP A 160      64.320  -4.465  -7.017  1.00104.03      A    C  
ANISOU 1194  CB  ASP A 160    11447  13966  14113   1385  -2150   1115  A    C  
ATOM   1195  CG  ASP A 160      64.934  -3.938  -8.303  1.00122.02      A    C  
ANISOU 1195  CG  ASP A 160    13458  16426  16478   1612  -2027   1105  A    C  
ATOM   1196  OD1 ASP A 160      65.602  -4.734  -9.003  1.00127.57      A    O  
ANISOU 1196  OD1 ASP A 160    14058  17181  17233   1850  -2149   1082  A    O  
ATOM   1197  OD2 ASP A 160      64.748  -2.735  -8.615  1.00123.91      A    O1-
ANISOU 1197  OD2 ASP A 160    13595  16753  16730   1560  -1801   1124  A    O1-
ATOM   1198  N   GLY A 161      63.881  -7.572  -5.187  1.00 85.43      A    N  
ANISOU 1198  N   GLY A 161     9620  11185  11653   1296  -2671   1136  A    N  
ATOM   1199  CA  GLY A 161      63.436  -8.119  -3.913  1.00 89.45      A    C  
ANISOU 1199  CA  GLY A 161    10390  11521  12077   1100  -2780   1189  A    C  
ATOM   1200  C   GLY A 161      62.037  -7.763  -3.418  1.00 90.03      A    C  
ANISOU 1200  C   GLY A 161    10627  11510  12072    868  -2626   1182  A    C  
ATOM   1201  O   GLY A 161      61.781  -7.762  -2.211  1.00 92.96      A    O  
ANISOU 1201  O   GLY A 161    11183  11786  12353    666  -2671   1245  A    O  
ATOM   1202  N   VAL A 162      61.126  -7.471  -4.340  1.00 78.36      A    N  
ANISOU 1202  N   VAL A 162     9077  10079  10616    908  -2445   1107  A    N  
ATOM   1203  CA  VAL A 162      59.763  -7.164  -3.969  1.00 78.39      A    C  
ANISOU 1203  CA  VAL A 162     9214  10023  10548    710  -2294   1094  A    C  
ATOM   1204  C   VAL A 162      58.892  -8.393  -4.166  1.00 86.09      A    C  
ANISOU 1204  C   VAL A 162    10322  10853  11536    729  -2354   1043  A    C  
ATOM   1205  O   VAL A 162      58.816  -8.924  -5.269  1.00 84.21      A    O  
ANISOU 1205  O   VAL A 162     9980  10646  11370    923  -2360    956  A    O  
ATOM   1206  CB  VAL A 162      59.203  -6.070  -4.852  1.00 86.61      A    C  
ANISOU 1206  CB  VAL A 162    10093  11217  11597    742  -2048   1042  A    C  
ATOM   1207  CG1 VAL A 162      58.080  -5.338  -4.122  1.00 90.58      A    C  
ANISOU 1207  CG1 VAL A 162    10724  11689  12003    498  -1882   1060  A    C  
ATOM   1208  CG2 VAL A 162      60.311  -5.105  -5.288  1.00 78.06      A    C  
ANISOU 1208  CG2 VAL A 162     8798  10292  10567    846  -1995   1066  A    C  
ATOM   1209  N   LEU A 163      58.240  -8.845  -3.097  1.00 88.41      A    N  
ANISOU 1209  N   LEU A 163    10845  10988  11759    526  -2395   1094  A    N  
ATOM   1210  CA  LEU A 163      57.349 -10.002  -3.169  1.00 79.44      A    C  
ANISOU 1210  CA  LEU A 163     9850   9688  10644    502  -2438   1052  A    C  
ATOM   1211  C   LEU A 163      55.951  -9.637  -3.672  1.00 77.42      A    C  
ANISOU 1211  C   LEU A 163     9567   9480  10370    417  -2234    968  A    C  
ATOM   1212  O   LEU A 163      55.377  -8.621  -3.288  1.00 80.98      A    O  
ANISOU 1212  O   LEU A 163    10019  10007  10742    266  -2071    992  A    O  
ATOM   1213  CB  LEU A 163      57.235 -10.657  -1.799  1.00 76.61      A    C  
ANISOU 1213  CB  LEU A 163     9750   9140  10219    321  -2554   1158  A    C  
ATOM   1214  CG  LEU A 163      56.138 -11.712  -1.634  1.00 73.46      A    C  
ANISOU 1214  CG  LEU A 163     9529   8549   9834    220  -2557   1137  A    C  
ATOM   1215  CD1 LEU A 163      56.545 -12.669  -0.542  1.00 75.37      A    C  
ANISOU 1215  CD1 LEU A 163     9998   8591  10048    162  -2735   1256  A    C  
ATOM   1216  CD2 LEU A 163      54.784 -11.083  -1.327  1.00 63.05      A    C  
ANISOU 1216  CD2 LEU A 163     8260   7256   8440      0  -2355   1122  A    C  
ATOM   1217  N   LYS A 164      55.388 -10.480  -4.519  1.00 78.96      A    N  
ANISOU 1217  N   LYS A 164     9736   9630  10634    517  -2247    861  A    N  
ATOM   1218  CA  LYS A 164      54.075 -10.188  -5.076  1.00 76.06      A    C  
ANISOU 1218  CA  LYS A 164     9317   9335  10249    457  -2068    765  A    C  
ATOM   1219  C   LYS A 164      53.237 -11.440  -5.114  1.00 74.80      A    C  
ANISOU 1219  C   LYS A 164     9281   9001  10137    397  -2131    694  A    C  
ATOM   1220  O   LYS A 164      53.702 -12.471  -5.575  1.00 83.03      A    O  
ANISOU 1220  O   LYS A 164    10331   9945  11270    543  -2281    640  A    O  
ATOM   1221  CB  LYS A 164      54.221  -9.603  -6.473  1.00 65.68      A    C  
ANISOU 1221  CB  LYS A 164     7748   8237   8970    687  -1966    665  A    C  
ATOM   1222  CG  LYS A 164      55.084  -8.339  -6.516  1.00 69.30      A    C  
ANISOU 1222  CG  LYS A 164     8072   8858   9402    748  -1885    738  A    C  
ATOM   1223  CD  LYS A 164      55.162  -7.794  -7.937  1.00 78.31      A    C  
ANISOU 1223  CD  LYS A 164     8969  10212  10575    987  -1765    654  A    C  
ATOM   1224  CE  LYS A 164      55.918  -6.477  -8.020  1.00 77.10      A    C  
ANISOU 1224  CE  LYS A 164     8678  10208  10408   1032  -1648    731  A    C  
ATOM   1225  NZ  LYS A 164      55.451  -5.457  -7.057  1.00 69.50      A    N1+
ANISOU 1225  NZ  LYS A 164     7808   9236   9362    795  -1509    809  A    N1+
ATOM   1226  N   LEU A 165      52.016 -11.365  -4.598  1.00 71.37      A    N  
ANISOU 1226  N   LEU A 165     8948   8522   9648    178  -2015    694  A    N  
ATOM   1227  CA  LEU A 165      51.107 -12.496  -4.684  1.00 71.39      A    C  
ANISOU 1227  CA  LEU A 165     9048   8367   9709     96  -2049    614  A    C  
ATOM   1228  C   LEU A 165      50.547 -12.526  -6.095  1.00 69.44      A    C  
ANISOU 1228  C   LEU A 165     8600   8270   9515    253  -1976    429  A    C  
ATOM   1229  O   LEU A 165      50.259 -11.479  -6.678  1.00 71.32      A    O  
ANISOU 1229  O   LEU A 165     8668   8734   9696    317  -1822    391  A    O  
ATOM   1230  CB  LEU A 165      49.971 -12.378  -3.676  1.00 75.01      A    C  
ANISOU 1230  CB  LEU A 165     9663   8749  10090   -194  -1938    677  A    C  
ATOM   1231  CG  LEU A 165      50.305 -12.049  -2.227  1.00 84.52      A    C  
ANISOU 1231  CG  LEU A 165    11055   9864  11196   -369  -1959    858  A    C  
ATOM   1232  CD1 LEU A 165      49.014 -11.739  -1.483  1.00 90.97      A    C  
ANISOU 1232  CD1 LEU A 165    11972  10670  11924   -627  -1800    892  A    C  
ATOM   1233  CD2 LEU A 165      51.046 -13.192  -1.565  1.00 96.71      A    C  
ANISOU 1233  CD2 LEU A 165    12786  11173  12787   -364  -2163    948  A    C  
ATOM   1234  N   ALA A 166      50.400 -13.722  -6.653  1.00 70.20      A    N  
ANISOU 1234  N   ALA A 166     8715   8242   9716    326  -2087    311  A    N  
ATOM   1235  CA  ALA A 166      49.954 -13.835  -8.036  1.00 76.28      A    C  
ANISOU 1235  CA  ALA A 166     9288   9165  10531    499  -2044    115  A    C  
ATOM   1236  C   ALA A 166      48.941 -14.947  -8.278  1.00 78.98      A    C  
ANISOU 1236  C   ALA A 166     9689   9367  10953    400  -2074    -31  A    C  
ATOM   1237  O   ALA A 166      48.528 -15.662  -7.357  1.00 73.71      A    O  
ANISOU 1237  O   ALA A 166     9225   8464  10317    181  -2114     30  A    O  
ATOM   1238  CB  ALA A 166      51.152 -13.984  -8.975  1.00 77.98      A    C  
ANISOU 1238  CB  ALA A 166     9368   9459  10802    810  -2156     66  A    C  
ATOM   1239  N   ASP A 167      48.551 -15.071  -9.541  1.00 82.25      A    N  
ANISOU 1239  N   ASP A 167     9917   9936  11400    564  -2048   -227  A    N  
ATOM   1240  CA  ASP A 167      47.586 -16.066  -9.962  1.00 89.57      A    C  
ANISOU 1240  CA  ASP A 167    10854  10768  12409    489  -2074   -410  A    C  
ATOM   1241  C   ASP A 167      46.304 -15.912  -9.159  1.00 84.77      A    C  
ANISOU 1241  C   ASP A 167    10332  10118  11758    176  -1944   -376  A    C  
ATOM   1242  O   ASP A 167      46.079 -16.596  -8.165  1.00 83.40      A    O  
ANISOU 1242  O   ASP A 167    10371   9688  11630    -45  -1988   -288  A    O  
ATOM   1243  CB  ASP A 167      48.155 -17.480  -9.844  1.00102.69      A    C  
ANISOU 1243  CB  ASP A 167    12677  12131  14211    518  -2272   -442  A    C  
ATOM   1244  CG  ASP A 167      47.359 -18.494 -10.651  1.00121.52      A    C  
ANISOU 1244  CG  ASP A 167    15018  14450  16702    517  -2313   -686  A    C  
ATOM   1245  OD1 ASP A 167      46.505 -18.078 -11.473  1.00116.78      A    O  
ANISOU 1245  OD1 ASP A 167    14226  14084  16060    548  -2207   -848  A    O  
ATOM   1246  OD2 ASP A 167      47.588 -19.709 -10.459  1.00132.92      A    O1-
ANISOU 1246  OD2 ASP A 167    16623  15608  18273    489  -2450   -720  A    O1-
ATOM   1247  N   PHE A 168      45.477 -14.977  -9.601  1.00 76.97      A    N  
ANISOU 1247  N   PHE A 168     9174   9397  10676    174  -1775   -435  A    N  
ATOM   1248  CA  PHE A 168      44.161 -14.782  -9.038  1.00 75.73      A    C  
ANISOU 1248  CA  PHE A 168     9049   9256  10470    -91  -1635   -434  A    C  
ATOM   1249  C   PHE A 168      43.075 -15.503  -9.861  1.00 79.03      A    C  
ANISOU 1249  C   PHE A 168     9352   9720  10957   -121  -1629   -677  A    C  
ATOM   1250  O   PHE A 168      41.901 -15.120  -9.854  1.00 78.30      A    O  
ANISOU 1250  O   PHE A 168     9177   9770  10805   -258  -1488   -734  A    O  
ATOM   1251  CB  PHE A 168      43.885 -13.289  -8.931  1.00 65.41      A    C  
ANISOU 1251  CB  PHE A 168     7634   8208   9010    -80  -1446   -343  A    C  
ATOM   1252  CG  PHE A 168      44.641 -12.617  -7.825  1.00 67.00      A    C  
ANISOU 1252  CG  PHE A 168     7983   8329   9144   -157  -1432   -112  A    C  
ATOM   1253  CD1 PHE A 168      43.984 -12.172  -6.691  1.00 68.61      A    C  
ANISOU 1253  CD1 PHE A 168     8315   8489   9265   -410  -1320     16  A    C  
ATOM   1254  CD2 PHE A 168      46.006 -12.421  -7.917  1.00 70.88      A    C  
ANISOU 1254  CD2 PHE A 168     8476   8804   9650     26  -1532    -30  A    C  
ATOM   1255  CE1 PHE A 168      44.674 -11.542  -5.668  1.00 68.61      A    C  
ANISOU 1255  CE1 PHE A 168     8448   8427   9193   -479  -1313    210  A    C  
ATOM   1256  CE2 PHE A 168      46.709 -11.788  -6.893  1.00 67.78      A    C  
ANISOU 1256  CE2 PHE A 168     8206   8353   9194    -51  -1528    165  A    C  
ATOM   1257  CZ  PHE A 168      46.041 -11.357  -5.768  1.00 70.46      A    C  
ANISOU 1257  CZ  PHE A 168     8679   8645   9447   -304  -1422    279  A    C  
ATOM   1258  N   GLY A 169      43.473 -16.564 -10.556  1.00 79.12      A    N  
ANISOU 1258  N   GLY A 169     9357   9612  11093      6  -1785   -828  A    N  
ATOM   1259  CA  GLY A 169      42.551 -17.300 -11.407  1.00 78.30      A    C  
ANISOU 1259  CA  GLY A 169     9135   9549  11064     -8  -1802  -1088  A    C  
ATOM   1260  C   GLY A 169      41.432 -17.989 -10.645  1.00 72.19      A    C  
ANISOU 1260  C   GLY A 169     8486   8583  10360   -350  -1762  -1108  A    C  
ATOM   1261  O   GLY A 169      40.374 -18.285 -11.198  1.00 82.81      A    O  
ANISOU 1261  O   GLY A 169     9702  10027  11735   -427  -1718  -1310  A    O  
ATOM   1262  N   LEU A 170      41.680 -18.243  -9.365  1.00 65.90      A    N  
ANISOU 1262  N   LEU A 170     7935   7518   9585   -554  -1777   -895  A    N  
ATOM   1263  CA  LEU A 170      40.696 -18.818  -8.459  1.00 73.65      A    C  
ANISOU 1263  CA  LEU A 170     9062   8301  10620   -893  -1718   -857  A    C  
ATOM   1264  C   LEU A 170      40.100 -17.782  -7.499  1.00 82.52      A    C  
ANISOU 1264  C   LEU A 170    10215   9544  11594  -1079  -1541   -673  A    C  
ATOM   1265  O   LEU A 170      39.179 -18.089  -6.737  1.00 90.03      A    O  
ANISOU 1265  O   LEU A 170    11261  10383  12563  -1362  -1459   -630  A    O  
ATOM   1266  CB  LEU A 170      41.337 -19.934  -7.634  1.00 77.65      A    C  
ANISOU 1266  CB  LEU A 170     9848   8403  11253   -994  -1852   -735  A    C  
ATOM   1267  CG  LEU A 170      41.258 -21.347  -8.190  1.00 81.93      A    C  
ANISOU 1267  CG  LEU A 170    10435   8704  11991   -998  -1982   -929  A    C  
ATOM   1268  CD1 LEU A 170      41.469 -22.359  -7.061  1.00 83.79      A    C  
ANISOU 1268  CD1 LEU A 170    10978   8523  12334  -1198  -2044   -762  A    C  
ATOM   1269  CD2 LEU A 170      39.900 -21.511  -8.817  1.00 89.35      A    C  
ANISOU 1269  CD2 LEU A 170    11198   9780  12972  -1136  -1893  -1168  A    C  
ATOM   1270  N   ALA A 171      40.631 -16.565  -7.518  1.00 72.93      A    N  
ANISOU 1270  N   ALA A 171     8925   8548  10237   -923  -1476   -563  A    N  
ATOM   1271  CA  ALA A 171      40.198 -15.564  -6.563  1.00 70.54      A    C  
ANISOU 1271  CA  ALA A 171     8674   8337   9792  -1081  -1316   -385  A    C  
ATOM   1272  C   ALA A 171      38.728 -15.221  -6.765  1.00 77.05      A    C  
ANISOU 1272  C   ALA A 171     9350   9361  10563  -1223  -1149   -497  A    C  
ATOM   1273  O   ALA A 171      38.198 -15.349  -7.869  1.00 79.60      A    O  
ANISOU 1273  O   ALA A 171     9466   9863  10917  -1116  -1142   -715  A    O  
ATOM   1274  CB  ALA A 171      41.044 -14.324  -6.698  1.00 65.17      A    C  
ANISOU 1274  CB  ALA A 171     7920   7852   8988   -873  -1275   -280  A    C  
ATOM   1275  N   ARG A 172      38.073 -14.784  -5.693  1.00 77.10      A    N  
ANISOU 1275  N   ARG A 172     9458   9352  10482  -1456  -1016   -349  A    N  
ATOM   1276  CA  ARG A 172      36.712 -14.263  -5.787  1.00 74.63      A    C  
ANISOU 1276  CA  ARG A 172     8999   9266  10091  -1578   -836   -425  A    C  
ATOM   1277  C   ARG A 172      36.455 -13.202  -4.722  1.00 77.55      A    C  
ANISOU 1277  C   ARG A 172     9457   9709  10300  -1698   -677   -221  A    C  
ATOM   1278  O   ARG A 172      37.176 -13.133  -3.723  1.00 78.32      A    O  
ANISOU 1278  O   ARG A 172     9766   9626  10366  -1763   -716    -25  A    O  
ATOM   1279  CB  ARG A 172      35.686 -15.380  -5.634  1.00 70.79      A    C  
ANISOU 1279  CB  ARG A 172     8537   8633   9727  -1832   -839   -535  A    C  
ATOM   1280  CG  ARG A 172      35.447 -15.792  -4.199  1.00 76.01      A    C  
ANISOU 1280  CG  ARG A 172     9450   9033  10396  -2128   -801   -336  A    C  
ATOM   1281  CD  ARG A 172      34.184 -16.612  -4.074  1.00 84.02      A    C  
ANISOU 1281  CD  ARG A 172    10439   9978  11507  -2399   -739   -442  A    C  
ATOM   1282  NE  ARG A 172      33.033 -15.845  -4.525  1.00 98.82      A    N  
ANISOU 1282  NE  ARG A 172    12073  12191  13282  -2417   -575   -559  A    N  
ATOM   1283  CZ  ARG A 172      31.815 -16.346  -4.702  1.00109.39      A    C  
ANISOU 1283  CZ  ARG A 172    13294  13582  14687  -2612   -504   -706  A    C  
ATOM   1284  NH1 ARG A 172      31.573 -17.634  -4.465  1.00116.69      A    N1+
ANISOU 1284  NH1 ARG A 172    14327  14217  15793  -2824   -575   -756  A    N1+
ATOM   1285  NH2 ARG A 172      30.841 -15.550  -5.121  1.00106.62      A    N  
ANISOU 1285  NH2 ARG A 172    12713  13574  14223  -2592   -358   -803  A    N  
ATOM   1286  N   ALA A 173      35.428 -12.378  -4.938  1.00 72.87      A    N  
ANISOU 1286  N   ALA A 173     8700   9389   9597  -1718   -499   -274  A    N  
ATOM   1287  CA  ALA A 173      35.027 -11.370  -3.946  1.00 67.42      A    C  
ANISOU 1287  CA  ALA A 173     8088   8779   8750  -1838   -329   -101  A    C  
ATOM   1288  C   ALA A 173      34.150 -11.985  -2.872  1.00 72.93      A    C  
ANISOU 1288  C   ALA A 173     8931   9317   9463  -2164   -270    -26  A    C  
ATOM   1289  O   ALA A 173      33.507 -13.014  -3.095  1.00 79.05      A    O  
ANISOU 1289  O   ALA A 173     9674  10000  10362  -2302   -309   -146  A    O  
ATOM   1290  CB  ALA A 173      34.310 -10.210  -4.597  1.00 48.18      A    C  
ANISOU 1290  CB  ALA A 173     5426   6697   6182  -1704   -154   -175  A    C  
ATOM   1291  N   PHE A 174      34.126 -11.360  -1.703  1.00 72.91      A    N  
ANISOU 1291  N   PHE A 174     9087   9279   9336  -2289   -172    171  A    N  
ATOM   1292  CA  PHE A 174      33.344 -11.900  -0.604  1.00 78.96      A    C  
ANISOU 1292  CA  PHE A 174    10005   9896  10099  -2591   -103    271  A    C  
ATOM   1293  C   PHE A 174      32.573 -10.802   0.080  1.00 93.47      A    C  
ANISOU 1293  C   PHE A 174    11833  11926  11754  -2675    106    367  A    C  
ATOM   1294  O   PHE A 174      32.926  -9.628  -0.020  1.00 90.14      A    O  
ANISOU 1294  O   PHE A 174    11367  11674  11208  -2512    176    407  A    O  
ATOM   1295  CB  PHE A 174      34.207 -12.684   0.387  1.00 71.87      A    C  
ANISOU 1295  CB  PHE A 174     9390   8660   9256  -2698   -237    443  A    C  
ATOM   1296  CG  PHE A 174      35.077 -11.832   1.254  1.00 79.46      A    C  
ANISOU 1296  CG  PHE A 174    10511   9604  10077  -2642   -235    635  A    C  
ATOM   1297  CD1 PHE A 174      36.344 -11.459   0.837  1.00 80.25      A    C  
ANISOU 1297  CD1 PHE A 174    10604   9705  10180  -2409   -358    642  A    C  
ATOM   1298  CD2 PHE A 174      34.646 -11.426   2.503  1.00 81.99      A    C  
ANISOU 1298  CD2 PHE A 174    10985   9907  10260  -2826   -114    803  A    C  
ATOM   1299  CE1 PHE A 174      37.164 -10.684   1.651  1.00 80.29      A    C  
ANISOU 1299  CE1 PHE A 174    10747   9696  10065  -2373   -364    804  A    C  
ATOM   1300  CE2 PHE A 174      35.460 -10.649   3.321  1.00 83.78      A    C  
ANISOU 1300  CE2 PHE A 174    11358  10120  10353  -2779   -123    961  A    C  
ATOM   1301  CZ  PHE A 174      36.723 -10.283   2.895  1.00 79.85      A    C  
ANISOU 1301  CZ  PHE A 174    10847   9622   9871  -2559   -251    956  A    C  
ATOM   1302  N   SER A 175      31.501 -11.194   0.758  1.00111.90      A    N  
ANISOU 1302  N   SER A 175    14208  14229  14079  -2931    215    401  A    N  
ATOM   1303  CA  SER A 175      30.536 -10.239   1.275  1.00119.16      A    C  
ANISOU 1303  CA  SER A 175    15078  15365  14831  -3012    430    457  A    C  
ATOM   1304  C   SER A 175      30.321 -10.402   2.771  1.00124.71      A    C  
ANISOU 1304  C   SER A 175    16026  15902  15458  -3257    497    665  A    C  
ATOM   1305  O   SER A 175      30.512 -11.483   3.338  1.00120.33      A    O  
ANISOU 1305  O   SER A 175    15640  15075  15003  -3421    405    740  A    O  
ATOM   1306  CB  SER A 175      29.204 -10.384   0.532  1.00123.65      A    C  
ANISOU 1306  CB  SER A 175    15393  16156  15431  -3068    539    274  A    C  
ATOM   1307  OG  SER A 175      28.283  -9.383   0.928  1.00123.43      A    O  
ANISOU 1307  OG  SER A 175    15295  16370  15233  -3106    752    319  A    O  
ATOM   1308  N   LEU A 176      29.937  -9.299   3.398  1.00137.11      A    N  
ANISOU 1308  N   LEU A 176    17617  17638  16841  -3265    663    759  A    N  
ATOM   1309  CA  LEU A 176      29.547  -9.291   4.794  1.00148.36      A    C  
ANISOU 1309  CA  LEU A 176    19243  18972  18155  -3484    764    944  A    C  
ATOM   1310  C   LEU A 176      28.221 -10.046   4.879  1.00158.82      A    C  
ANISOU 1310  C   LEU A 176    20483  20317  19543  -3720    869    894  A    C  
ATOM   1311  O   LEU A 176      27.187  -9.580   4.394  1.00155.06      A    O  
ANISOU 1311  O   LEU A 176    19792  20102  19024  -3716   1015    782  A    O  
ATOM   1312  CB  LEU A 176      29.429  -7.845   5.294  1.00147.73      A    C  
ANISOU 1312  CB  LEU A 176    19180  19092  17860  -3406    922   1021  A    C  
ATOM   1313  CG  LEU A 176      30.658  -6.934   5.071  1.00142.39      A    C  
ANISOU 1313  CG  LEU A 176    18541  18432  17129  -3169    844   1040  A    C  
ATOM   1314  CD1 LEU A 176      30.961  -6.675   3.585  1.00132.15      A    C  
ANISOU 1314  CD1 LEU A 176    17011  17278  15923  -2922    790    865  A    C  
ATOM   1315  CD2 LEU A 176      30.516  -5.606   5.817  1.00141.70      A    C  
ANISOU 1315  CD2 LEU A 176    18523  18483  16834  -3145   1007   1134  A    C  
ATOM   1316  N   ALA A 177      28.270 -11.234   5.471  1.00172.31      A    N  
ANISOU 1316  N   ALA A 177    22356  21751  21364  -3920    796    978  A    N  
ATOM   1317  CA  ALA A 177      27.148 -12.163   5.419  1.00187.06      A    C  
ANISOU 1317  CA  ALA A 177    24139  23585  23350  -4155    867    912  A    C  
ATOM   1318  C   ALA A 177      26.125 -11.953   6.533  1.00200.69      A    C  
ANISOU 1318  C   ALA A 177    25933  25374  24945  -4383   1073   1054  A    C  
ATOM   1319  O   ALA A 177      26.071 -12.731   7.488  1.00206.88      A    O  
ANISOU 1319  O   ALA A 177    26920  25926  25759  -4591   1080   1213  A    O  
ATOM   1320  CB  ALA A 177      27.657 -13.603   5.435  1.00188.55      A    C  
ANISOU 1320  CB  ALA A 177    24468  23427  23747  -4261    701    925  A    C  
ATOM   1321  N   LYS A 178      25.314 -10.906   6.410  1.00204.03      A    N  
ANISOU 1321  N   LYS A 178    26187  26113  25220  -4334   1247   1004  A    N  
ATOM   1322  CA  LYS A 178      24.186 -10.720   7.320  1.00207.95      A    C  
ANISOU 1322  CA  LYS A 178    26698  26714  25599  -4544   1459   1108  A    C  
ATOM   1323  C   LYS A 178      22.855 -10.841   6.571  1.00214.90      A    C  
ANISOU 1323  C   LYS A 178    27275  27836  26541  -4627   1580    924  A    C  
ATOM   1324  O   LYS A 178      22.830 -11.280   5.419  1.00216.89      A    O  
ANISOU 1324  O   LYS A 178    27333  28127  26947  -4555   1481    720  A    O  
ATOM   1325  CB  LYS A 178      24.293  -9.400   8.095  1.00199.85      A    C  
ANISOU 1325  CB  LYS A 178    25771  25843  24319  -4444   1583   1239  A    C  
ATOM   1326  CG  LYS A 178      24.549  -8.172   7.243  1.00191.90      A    C  
ANISOU 1326  CG  LYS A 178    24602  25088  23224  -4159   1600   1119  A    C  
ATOM   1327  CD  LYS A 178      24.654  -6.932   8.115  1.00185.66      A    C  
ANISOU 1327  CD  LYS A 178    23940  24406  22198  -4089   1729   1251  A    C  
ATOM   1328  CE  LYS A 178      24.864  -5.677   7.283  1.00178.19      A    C  
ANISOU 1328  CE  LYS A 178    22840  23693  21171  -3810   1771   1143  A    C  
ATOM   1329  NZ  LYS A 178      24.964  -4.457   8.136  1.00173.94      A    N1+
ANISOU 1329  NZ  LYS A 178    22436  23239  20413  -3748   1902   1259  A    N1+
ATOM   1330  N   ASN A 179      21.763 -10.457   7.229  1.00216.25      A    N  
ANISOU 1330  N   ASN A 179    27399  28180  26585  -4772   1792    990  A    N  
ATOM   1331  CA  ASN A 179      20.414 -10.664   6.699  1.00215.84      A    C  
ANISOU 1331  CA  ASN A 179    27063  28357  26588  -4895   1919    836  A    C  
ATOM   1332  C   ASN A 179      19.971 -12.110   6.890  1.00218.72      A    C  
ANISOU 1332  C   ASN A 179    27451  28488  27165  -5197   1891    830  A    C  
ATOM   1333  O   ASN A 179      19.086 -12.594   6.185  1.00221.04      A    O  
ANISOU 1333  O   ASN A 179    27495  28905  27584  -5303   1923    646  A    O  
ATOM   1334  CB  ASN A 179      20.323 -10.280   5.218  1.00213.53      A    C  
ANISOU 1334  CB  ASN A 179    26474  28315  26344  -4663   1860    581  A    C  
ATOM   1335  CG  ASN A 179      20.654  -8.821   4.969  1.00210.65      A    C  
ANISOU 1335  CG  ASN A 179    26069  28189  25779  -4365   1917    588  A    C  
ATOM   1336  ND2 ASN A 179      21.870  -8.559   4.496  1.00206.97      A    N  
ANISOU 1336  ND2 ASN A 179    25684  27620  25334  -4140   1760    576  A    N  
ATOM   1337  OD1 ASN A 179      19.825  -7.939   5.193  1.00210.38      A    O  
ANISOU 1337  OD1 ASN A 179    25930  28426  25579  -4335   2108    605  A    O  
ATOM   1338  N   SER A 180      20.605 -12.789   7.844  1.00218.41      A    N  
ANISOU 1338  N   SER A 180    27713  28110  27163  -5331   1833   1030  A    N  
ATOM   1339  CA  SER A 180      20.302 -14.185   8.174  1.00218.09      A    C  
ANISOU 1339  CA  SER A 180    27754  27785  27324  -5621   1816   1071  A    C  
ATOM   1340  C   SER A 180      20.323 -15.125   6.966  1.00217.59      A    C  
ANISOU 1340  C   SER A 180    27519  27630  27524  -5635   1667    825  A    C  
ATOM   1341  O   SER A 180      19.398 -15.917   6.773  1.00219.58      A    O  
ANISOU 1341  O   SER A 180    27631  27868  27934  -5872   1732    725  A    O  
ATOM   1342  CB  SER A 180      18.961 -14.297   8.909  1.00216.10      A    C  
ANISOU 1342  CB  SER A 180    27433  27649  27025  -5897   2052   1149  A    C  
ATOM   1343  OG  SER A 180      18.699 -15.638   9.289  1.00214.69      A    O  
ANISOU 1343  OG  SER A 180    27353  27170  27050  -6189   2052   1210  A    O  
ATOM   1344  N   GLN A 181      21.382 -15.036   6.165  1.00211.67      A    N  
ANISOU 1344  N   GLN A 181    26778  26822  26823  -5384   1471    724  A    N  
ATOM   1345  CA  GLN A 181      21.560 -15.925   5.018  1.00206.10      A    C  
ANISOU 1345  CA  GLN A 181    25939  26015  26356  -5362   1308    490  A    C  
ATOM   1346  C   GLN A 181      23.036 -16.181   4.723  1.00198.55      A    C  
ANISOU 1346  C   GLN A 181    25163  24814  25462  -5151   1082    511  A    C  
ATOM   1347  O   GLN A 181      23.644 -15.462   3.926  1.00198.81      A    O  
ANISOU 1347  O   GLN A 181    25095  25014  25431  -4866    993    406  A    O  
ATOM   1348  CB  GLN A 181      20.876 -15.356   3.771  1.00203.94      A    C  
ANISOU 1348  CB  GLN A 181    25297  26124  26067  -5220   1333    213  A    C  
ATOM   1349  CG  GLN A 181      19.359 -15.430   3.794  1.00205.18      A    C  
ANISOU 1349  CG  GLN A 181    25216  26510  26232  -5448   1519    121  A    C  
ATOM   1350  CD  GLN A 181      18.746 -15.167   2.435  1.00203.60      A    C  
ANISOU 1350  CD  GLN A 181    24646  26652  26061  -5314   1498   -186  A    C  
ATOM   1351  NE2 GLN A 181      17.424 -15.266   2.351  1.00203.80      A    N  
ANISOU 1351  NE2 GLN A 181    24428  26903  26103  -5503   1644   -296  A    N  
ATOM   1352  OE1 GLN A 181      19.453 -14.881   1.469  1.00201.42      A    O  
ANISOU 1352  OE1 GLN A 181    24295  26448  25788  -5037   1354   -323  A    O  
ATOM   1353  N   PRO A 182      23.619 -17.206   5.367  1.00187.95      A    N  
ANISOU 1353  N   PRO A 182    24089  23081  24245  -5284    996    657  A    N  
ATOM   1354  CA  PRO A 182      25.023 -17.562   5.135  1.00177.10      A    C  
ANISOU 1354  CA  PRO A 182    22891  21461  22940  -5092    778    685  A    C  
ATOM   1355  C   PRO A 182      25.334 -17.743   3.653  1.00165.10      A    C  
ANISOU 1355  C   PRO A 182    21156  20020  21555  -4897    624    400  A    C  
ATOM   1356  O   PRO A 182      24.471 -18.157   2.877  1.00163.74      A    O  
ANISOU 1356  O   PRO A 182    20751  19952  21509  -4994    651    176  A    O  
ATOM   1357  CB  PRO A 182      25.170 -18.887   5.884  1.00179.55      A    C  
ANISOU 1357  CB  PRO A 182    23454  21352  23413  -5324    745    831  A    C  
ATOM   1358  CG  PRO A 182      24.192 -18.782   6.991  1.00182.57      A    C  
ANISOU 1358  CG  PRO A 182    23898  21774  23697  -5583    964   1010  A    C  
ATOM   1359  CD  PRO A 182      23.011 -18.042   6.416  1.00186.32      A    C  
ANISOU 1359  CD  PRO A 182    24044  22645  24104  -5610   1113    828  A    C  
ATOM   1360  N   ASN A 183      26.566 -17.425   3.274  1.00156.02      A    N  
ANISOU 1360  N   ASN A 183    20078  18832  20373  -4622    463    405  A    N  
ATOM   1361  CA  ASN A 183      26.990 -17.479   1.879  1.00149.50      A    C  
ANISOU 1361  CA  ASN A 183    19057  18102  19642  -4392    316    154  A    C  
ATOM   1362  C   ASN A 183      27.097 -18.898   1.342  1.00144.74      A    C  
ANISOU 1362  C   ASN A 183    18477  17215  19304  -4485    179      9  A    C  
ATOM   1363  O   ASN A 183      27.216 -19.856   2.104  1.00151.45      A    O  
ANISOU 1363  O   ASN A 183    19555  17721  20269  -4680    162    146  A    O  
ATOM   1364  CB  ASN A 183      28.346 -16.788   1.712  1.00145.15      A    C  
ANISOU 1364  CB  ASN A 183    18595  17566  18989  -4083    189    226  A    C  
ATOM   1365  CG  ASN A 183      28.287 -15.307   1.995  1.00141.93      A    C  
ANISOU 1365  CG  ASN A 183    18131  17457  18338  -3954    315    317  A    C  
ATOM   1366  ND2 ASN A 183      29.230 -14.821   2.802  1.00143.75      A    N  
ANISOU 1366  ND2 ASN A 183    18578  17590  18449  -3871    280    526  A    N  
ATOM   1367  OD1 ASN A 183      27.416 -14.600   1.485  1.00137.86      A    O  
ANISOU 1367  OD1 ASN A 183    17379  17259  17743  -3921    441    194  A    O  
ATOM   1368  N   ARG A 184      27.065 -19.029   0.022  1.00132.30      A    N  
ANISOU 1368  N   ARG A 184    16668  15778  17821  -4335     85   -269  A    N  
ATOM   1369  CA  ARG A 184      27.351 -20.307  -0.605  1.00132.07      A    C  
ANISOU 1369  CA  ARG A 184    16663  15479  18037  -4368    -71   -433  A    C  
ATOM   1370  C   ARG A 184      28.514 -20.141  -1.560  1.00122.21      A    C  
ANISOU 1370  C   ARG A 184    15379  14261  16793  -4023   -258   -541  A    C  
ATOM   1371  O   ARG A 184      28.316 -19.885  -2.743  1.00122.15      A    O  
ANISOU 1371  O   ARG A 184    15113  14507  16790  -3856   -299   -789  A    O  
ATOM   1372  CB  ARG A 184      26.124 -20.844  -1.346  1.00142.29      A    C  
ANISOU 1372  CB  ARG A 184    17698  16893  19471  -4544    -19   -711  A    C  
ATOM   1373  CG  ARG A 184      25.213 -21.707  -0.488  1.00148.20      A    C  
ANISOU 1373  CG  ARG A 184    18545  17415  20349  -4936    102   -632  A    C  
ATOM   1374  CD  ARG A 184      24.908 -23.025  -1.180  1.00154.05      A    C  
ANISOU 1374  CD  ARG A 184    19225  17935  21372  -5085      9   -879  A    C  
ATOM   1375  NE  ARG A 184      24.639 -24.096  -0.225  1.00161.28      A    N  
ANISOU 1375  NE  ARG A 184    20374  18449  22455  -5413     70   -726  A    N  
ATOM   1376  CZ  ARG A 184      24.387 -25.355  -0.569  1.00170.15      A    C  
ANISOU 1376  CZ  ARG A 184    21513  19287  23849  -5599     13   -890  A    C  
ATOM   1377  NH1 ARG A 184      24.365 -25.703  -1.850  1.00171.74      A    N1+
ANISOU 1377  NH1 ARG A 184    21504  19574  24175  -5488   -118  -1230  A    N1+
ATOM   1378  NH2 ARG A 184      24.153 -26.265   0.367  1.00174.82      A    N  
ANISOU 1378  NH2 ARG A 184    22333  19504  24585  -5894     92   -716  A    N  
ATOM   1379  N   TYR A 185      29.731 -20.258  -1.041  1.00116.16      A    N  
ANISOU 1379  N   TYR A 185    14866  13259  16013  -3906   -368   -350  A    N  
ATOM   1380  CA  TYR A 185      30.906 -20.166  -1.897  1.00115.32      A    C  
ANISOU 1380  CA  TYR A 185    14735  13162  15921  -3583   -546   -436  A    C  
ATOM   1381  C   TYR A 185      31.370 -21.571  -2.238  1.00115.48      A    C  
ANISOU 1381  C   TYR A 185    14871  12827  16178  -3608   -709   -535  A    C  
ATOM   1382  O   TYR A 185      31.079 -22.516  -1.512  1.00122.03      A    O  
ANISOU 1382  O   TYR A 185    15885  13344  17136  -3859   -687   -445  A    O  
ATOM   1383  CB  TYR A 185      32.055 -19.382  -1.234  1.00116.49      A    C  
ANISOU 1383  CB  TYR A 185    15058  13297  15907  -3404   -583   -189  A    C  
ATOM   1384  CG  TYR A 185      31.753 -17.938  -0.879  1.00105.86      A    C  
ANISOU 1384  CG  TYR A 185    13625  12272  14326  -3354   -430    -86  A    C  
ATOM   1385  CD1 TYR A 185      30.934 -17.164  -1.684  1.00106.32      A    C  
ANISOU 1385  CD1 TYR A 185    13397  12694  14307  -3283   -325   -259  A    C  
ATOM   1386  CD2 TYR A 185      32.301 -17.349   0.253  1.00 97.72      A    C  
ANISOU 1386  CD2 TYR A 185    12799  11182  13147  -3365   -393    180  A    C  
ATOM   1387  CE1 TYR A 185      30.649 -15.844  -1.372  1.00100.58      A    C  
ANISOU 1387  CE1 TYR A 185    12600  12244  13370  -3225   -175   -164  A    C  
ATOM   1388  CE2 TYR A 185      32.020 -16.024   0.579  1.00 98.75      A    C  
ANISOU 1388  CE2 TYR A 185    12860  11591  13070  -3320   -248    261  A    C  
ATOM   1389  CZ  TYR A 185      31.190 -15.275  -0.245  1.00 98.34      A    C  
ANISOU 1389  CZ  TYR A 185    12531  11880  12955  -3248   -135     91  A    C  
ATOM   1390  OH  TYR A 185      30.892 -13.953   0.039  1.00 94.45      A    O  
ANISOU 1390  OH  TYR A 185    11973  11655  12261  -3189     18    167  A    O  
HETATM 1391  N   TPO A 186      32.088 -21.693  -3.348  1.00111.46      A    N  
ANISOU 1391  N   TPO A 186    14256  12368  15724  -3340   -863   -719  A    N  
HETATM 1392  CA  TPO A 186      32.678 -22.985  -3.812  1.00106.12      A    C  
ANISOU 1392  CA  TPO A 186    13686  11366  15270  -3302  -1037   -838  A    C  
HETATM 1393  C   TPO A 186      33.597 -23.566  -2.781  1.00107.39      A    C  
ANISOU 1393  C   TPO A 186    14185  11147  15470  -3334  -1108   -572  A    C  
HETATM 1394  O   TPO A 186      34.441 -22.867  -2.220  1.00107.09      A    O  
ANISOU 1394  O   TPO A 186    14259  11152  15280  -3191  -1127   -358  A    O  
HETATM 1395  CB  TPO A 186      33.417 -22.562  -5.066  1.00101.57      A    C  
ANISOU 1395  CB  TPO A 186    12926  11011  14654  -2943  -1163  -1021  A    C  
HETATM 1396  CG2 TPO A 186      33.479 -23.653  -6.118  1.00 92.67      A    C  
ANISOU 1396  CG2 TPO A 186    11729   9749  13733  -2882  -1305  -1307  A    C  
HETATM 1397  OG1 TPO A 186      32.593 -21.511  -5.548  1.00106.41      A    O  
ANISOU 1397  OG1 TPO A 186    13268  12045  15120  -2907  -1034  -1125  A    O  
HETATM 1398  P   TPO A 186      32.998 -20.463  -6.689  1.00105.90      A    P  
ANISOU 1398  P   TPO A 186    12953  12373  14911  -2550  -1061  -1254  A    P  
HETATM 1399  O1P TPO A 186      32.904 -19.182  -5.913  1.00 98.98      A    O  
ANISOU 1399  O1P TPO A 186    12093  11692  13822  -2556   -909  -1024  A    O  
HETATM 1400  O2P TPO A 186      34.375 -20.879  -7.194  1.00 85.80      A    O1-
ANISOU 1400  O2P TPO A 186    10498   9670  12433  -2282  -1253  -1269  A    O1-
HETATM 1401  O3P TPO A 186      31.865 -20.620  -7.681  1.00113.52      A    O  
ANISOU 1401  O3P TPO A 186    13632  13580  15920  -2592  -1022  -1561  A    O  
ATOM   1402  N   ASN A 187      33.448 -24.853  -2.499  1.00114.92      A    N  
ANISOU 1402  N   ASN A 187    15310  11726  16629  -3522  -1146   -579  A    N  
ATOM   1403  CA  ASN A 187      34.217 -25.450  -1.415  1.00119.69      A    C  
ANISOU 1403  CA  ASN A 187    16251  11961  17262  -3567  -1194   -300  A    C  
ATOM   1404  C   ASN A 187      35.579 -25.990  -1.829  1.00123.04      A    C  
ANISOU 1404  C   ASN A 187    16798  12188  17762  -3290  -1401   -308  A    C  
ATOM   1405  O   ASN A 187      36.578 -25.774  -1.144  1.00118.10      A    O  
ANISOU 1405  O   ASN A 187    16358  11476  17037  -3159  -1464    -72  A    O  
ATOM   1406  CB  ASN A 187      33.433 -26.559  -0.736  1.00123.92      A    C  
ANISOU 1406  CB  ASN A 187    16954  12155  17975  -3908  -1110   -244  A    C  
ATOM   1407  CG  ASN A 187      34.274 -27.304   0.268  1.00129.12      A    C  
ANISOU 1407  CG  ASN A 187    17969  12414  18678  -3919  -1172     33  A    C  
ATOM   1408  ND2 ASN A 187      34.161 -26.917   1.535  1.00132.61      A    N  
ANISOU 1408  ND2 ASN A 187    18578  12834  18973  -4052  -1057    331  A    N  
ATOM   1409  OD1 ASN A 187      35.047 -28.199  -0.092  1.00125.73      A    O  
ANISOU 1409  OD1 ASN A 187    17663  11708  18400  -3789  -1323    -18  A    O  
ATOM   1410  N   ARG A 188      35.607 -26.707  -2.943  1.00127.41      A    N  
ANISOU 1410  N   ARG A 188    17243  12678  18489  -3199  -1509   -587  A    N  
ATOM   1411  CA  ARG A 188      36.834 -27.318  -3.429  1.00130.65      A    C  
ANISOU 1411  CA  ARG A 188    17757  12896  18988  -2932  -1704   -624  A    C  
ATOM   1412  C   ARG A 188      37.826 -26.281  -3.994  1.00124.36      A    C  
ANISOU 1412  C   ARG A 188    16823  12411  18017  -2578  -1791   -624  A    C  
ATOM   1413  O   ARG A 188      38.232 -26.347  -5.156  1.00126.04      A    O  
ANISOU 1413  O   ARG A 188    16876  12739  18274  -2340  -1901   -850  A    O  
ATOM   1414  CB  ARG A 188      36.480 -28.411  -4.447  1.00138.60      A    C  
ANISOU 1414  CB  ARG A 188    18688  13740  20234  -2956  -1783   -942  A    C  
ATOM   1415  CG  ARG A 188      35.421 -29.389  -3.897  1.00153.81      A    C  
ANISOU 1415  CG  ARG A 188    20732  15362  22348  -3339  -1676   -951  A    C  
ATOM   1416  CD  ARG A 188      34.578 -30.063  -4.991  1.00158.68      A    C  
ANISOU 1416  CD  ARG A 188    21150  15983  23159  -3438  -1692  -1334  A    C  
ATOM   1417  NE  ARG A 188      33.293 -30.562  -4.489  1.00154.39      A    N  
ANISOU 1417  NE  ARG A 188    20614  15305  22741  -3842  -1537  -1355  A    N  
ATOM   1418  CZ  ARG A 188      32.320 -31.047  -5.261  1.00149.80      A    C  
ANISOU 1418  CZ  ARG A 188    19836  14763  22317  -4008  -1514  -1676  A    C  
ATOM   1419  NH1 ARG A 188      32.476 -31.106  -6.578  1.00142.57      A    N1+
ANISOU 1419  NH1 ARG A 188    18708  14020  21441  -3794  -1642  -2009  A    N1+
ATOM   1420  NH2 ARG A 188      31.186 -31.473  -4.718  1.00152.18      A    N  
ANISOU 1420  NH2 ARG A 188    20148  14942  22734  -4388  -1363  -1670  A    N  
ATOM   1421  N   VAL A 189      38.214 -25.320  -3.159  1.00117.16      A    N  
ANISOU 1421  N   VAL A 189    15973  11635  16906  -2546  -1735   -370  A    N  
ATOM   1422  CA  VAL A 189      39.230 -24.336  -3.538  1.00112.09      A    C  
ANISOU 1422  CA  VAL A 189    15229  11250  16109  -2236  -1807   -333  A    C  
ATOM   1423  C   VAL A 189      40.552 -24.562  -2.806  1.00109.70      A    C  
ANISOU 1423  C   VAL A 189    15168  10737  15777  -2095  -1931    -93  A    C  
ATOM   1424  O   VAL A 189      40.609 -25.270  -1.796  1.00106.76      A    O  
ANISOU 1424  O   VAL A 189    15056  10057  15453  -2251  -1933     97  A    O  
ATOM   1425  CB  VAL A 189      38.765 -22.884  -3.292  1.00106.30      A    C  
ANISOU 1425  CB  VAL A 189    14341  10887  15159  -2263  -1654   -259  A    C  
ATOM   1426  CG1 VAL A 189      38.025 -22.349  -4.497  1.00103.58      A    C  
ANISOU 1426  CG1 VAL A 189    13679  10878  14798  -2190  -1594   -530  A    C  
ATOM   1427  CG2 VAL A 189      37.908 -22.787  -2.033  1.00106.48      A    C  
ANISOU 1427  CG2 VAL A 189    14506  10831  15122  -2582  -1497    -65  A    C  
ATOM   1428  N   VAL A 190      41.611 -23.956  -3.328  1.00107.66      A    N  
ANISOU 1428  N   VAL A 190    14815  10656  15435  -1795  -2031   -101  A    N  
ATOM   1429  CA  VAL A 190      42.938 -24.051  -2.718  1.00108.87      A    C  
ANISOU 1429  CA  VAL A 190    15152  10670  15543  -1631  -2159    110  A    C  
ATOM   1430  C   VAL A 190      43.546 -25.439  -2.863  1.00115.47      A    C  
ANISOU 1430  C   VAL A 190    16166  11144  16564  -1547  -2314     82  A    C  
ATOM   1431  O   VAL A 190      42.893 -26.435  -2.554  1.00114.15      A    O  
ANISOU 1431  O   VAL A 190    16145  10689  16539  -1754  -2285     70  A    O  
ATOM   1432  CB  VAL A 190      42.915 -23.720  -1.209  1.00 99.48      A    C  
ANISOU 1432  CB  VAL A 190    14174   9402  14223  -1814  -2084    411  A    C  
ATOM   1433  CG1 VAL A 190      44.337 -23.556  -0.695  1.00 94.72      A    C  
ANISOU 1433  CG1 VAL A 190    13697   8758  13535  -1607  -2222    603  A    C  
ATOM   1434  CG2 VAL A 190      42.088 -22.474  -0.941  1.00 97.70      A    C  
ANISOU 1434  CG2 VAL A 190    13807   9483  13831  -1951  -1906    436  A    C  
ATOM   1435  N   THR A 191      44.802 -25.488  -3.315  1.00120.56      A    N  
ANISOU 1435  N   THR A 191    16798  11802  17207  -1244  -2471     80  A    N  
ATOM   1436  CA  THR A 191      45.581 -26.725  -3.362  1.00122.06      A    C  
ANISOU 1436  CA  THR A 191    17175  11656  17547  -1115  -2628     89  A    C  
ATOM   1437  C   THR A 191      45.356 -27.529  -2.096  1.00125.15      A    C  
ANISOU 1437  C   THR A 191    17877  11690  17984  -1338  -2601    315  A    C  
ATOM   1438  O   THR A 191      45.072 -26.967  -1.034  1.00129.05      A    O  
ANISOU 1438  O   THR A 191    18458  12233  18341  -1509  -2502    528  A    O  
ATOM   1439  CB  THR A 191      47.092 -26.443  -3.467  1.00125.68      A    C  
ANISOU 1439  CB  THR A 191    17630  12194  17930   -789  -2781    184  A    C  
ATOM   1440  CG2 THR A 191      47.889 -27.744  -3.410  1.00131.18      A    C  
ANISOU 1440  CG2 THR A 191    18541  12532  18772   -650  -2938    218  A    C  
ATOM   1441  OG1 THR A 191      47.377 -25.768  -4.697  1.00124.11      A    O  
ANISOU 1441  OG1 THR A 191    17147  12309  17698   -560  -2805    -17  A    O  
ATOM   1442  N   LEU A 192      45.494 -28.843  -2.197  1.00123.43      A    N  
ANISOU 1442  N   LEU A 192    17835  11109  17955  -1327  -2683    274  A    N  
ATOM   1443  CA  LEU A 192      45.244 -29.690  -1.047  1.00121.15      A    C  
ANISOU 1443  CA  LEU A 192    17851  10453  17726  -1534  -2643    492  A    C  
ATOM   1444  C   LEU A 192      46.182 -29.374   0.125  1.00123.35      A    C  
ANISOU 1444  C   LEU A 192    18316  10715  17836  -1449  -2695    819  A    C  
ATOM   1445  O   LEU A 192      45.726 -29.158   1.250  1.00125.35      A    O  
ANISOU 1445  O   LEU A 192    18708  10928  17990  -1663  -2587   1035  A    O  
ATOM   1446  CB  LEU A 192      45.338 -31.161  -1.430  1.00119.33      A    C  
ANISOU 1446  CB  LEU A 192    17783   9819  17739  -1504  -2727    386  A    C  
ATOM   1447  CG  LEU A 192      44.869 -32.087  -0.310  1.00124.43      A    C  
ANISOU 1447  CG  LEU A 192    18741  10063  18474  -1756  -2649    598  A    C  
ATOM   1448  CD1 LEU A 192      43.367 -31.925  -0.083  1.00123.91      A    C  
ANISOU 1448  CD1 LEU A 192    18609  10031  18441  -2130  -2450    542  A    C  
ATOM   1449  CD2 LEU A 192      45.231 -33.531  -0.612  1.00130.43      A    C  
ANISOU 1449  CD2 LEU A 192    19699  10390  19468  -1670  -2748    533  A    C  
ATOM   1450  N   TRP A 193      47.485 -29.333  -0.133  1.00122.96      A    N  
ANISOU 1450  N   TRP A 193    18260  10713  17747  -1133  -2860    851  A    N  
ATOM   1451  CA  TRP A 193      48.456 -29.187   0.955  1.00127.49      A    C  
ANISOU 1451  CA  TRP A 193    19015  11251  18174  -1032  -2936   1147  A    C  
ATOM   1452  C   TRP A 193      48.303 -27.864   1.720  1.00118.16      A    C  
ANISOU 1452  C   TRP A 193    17756  10380  16758  -1141  -2841   1294  A    C  
ATOM   1453  O   TRP A 193      48.479 -27.806   2.946  1.00105.50      A    O  
ANISOU 1453  O   TRP A 193    16348   8706  15031  -1223  -2826   1554  A    O  
ATOM   1454  CB  TRP A 193      49.890 -29.352   0.435  1.00136.05      A    C  
ANISOU 1454  CB  TRP A 193    20065  12366  19263   -661  -3133   1128  A    C  
ATOM   1455  CG  TRP A 193      50.176 -30.702  -0.190  1.00144.71      A    C  
ANISOU 1455  CG  TRP A 193    21277  13129  20576   -522  -3238   1011  A    C  
ATOM   1456  CD1 TRP A 193      49.506 -31.870   0.033  1.00147.62      A    C  
ANISOU 1456  CD1 TRP A 193    21861  13107  21122   -694  -3190   1011  A    C  
ATOM   1457  CD2 TRP A 193      51.219 -31.012  -1.131  1.00147.91      A    C  
ANISOU 1457  CD2 TRP A 193    21594  13559  21047   -181  -3402    877  A    C  
ATOM   1458  CE2 TRP A 193      51.114 -32.382  -1.435  1.00147.47      A    C  
ANISOU 1458  CE2 TRP A 193    21714  13113  21205   -157  -3450    792  A    C  
ATOM   1459  CE3 TRP A 193      52.229 -30.263  -1.747  1.00146.19      A    C  
ANISOU 1459  CE3 TRP A 193    21162  13653  20731    105  -3506    822  A    C  
ATOM   1460  NE1 TRP A 193      50.061 -32.883  -0.715  1.00150.05      A    N  
ANISOU 1460  NE1 TRP A 193    22226  13183  21603   -480  -3316    876  A    N  
ATOM   1461  CZ2 TRP A 193      51.978 -33.016  -2.326  1.00143.72      A    C  
ANISOU 1461  CZ2 TRP A 193    21212  12557  20837    155  -3601    649  A    C  
ATOM   1462  CZ3 TRP A 193      53.085 -30.899  -2.633  1.00140.33      A    C  
ANISOU 1462  CZ3 TRP A 193    20385  12842  20094    411  -3652    688  A    C  
ATOM   1463  CH2 TRP A 193      52.952 -32.257  -2.914  1.00137.89      A    C  
ANISOU 1463  CH2 TRP A 193    20256  12148  19986    440  -3701    600  A    C  
ATOM   1464  N   TYR A 194      47.972 -26.804   0.990  1.00119.80      A    N  
ANISOU 1464  N   TYR A 194    17685  10931  16902  -1134  -2775   1125  A    N  
ATOM   1465  CA  TYR A 194      47.818 -25.493   1.598  1.00112.82      A    C  
ANISOU 1465  CA  TYR A 194    16715  10345  15809  -1225  -2678   1233  A    C  
ATOM   1466  C   TYR A 194      46.358 -25.179   1.886  1.00113.44      A    C  
ANISOU 1466  C   TYR A 194    16764  10470  15867  -1542  -2475   1206  A    C  
ATOM   1467  O   TYR A 194      46.020 -24.037   2.199  1.00114.14      A    O  
ANISOU 1467  O   TYR A 194    16745  10826  15795  -1626  -2368   1244  A    O  
ATOM   1468  CB  TYR A 194      48.388 -24.421   0.691  1.00105.20      A    C  
ANISOU 1468  CB  TYR A 194    15467   9733  14771  -1013  -2713   1094  A    C  
ATOM   1469  CG  TYR A 194      49.820 -24.631   0.284  1.00107.86      A    C  
ANISOU 1469  CG  TYR A 194    15783  10074  15127   -692  -2903   1099  A    C  
ATOM   1470  CD1 TYR A 194      50.842 -23.905   0.878  1.00114.89      A    C  
ANISOU 1470  CD1 TYR A 194    16671  11120  15861   -569  -2976   1260  A    C  
ATOM   1471  CD2 TYR A 194      50.151 -25.531  -0.711  1.00112.31      A    C  
ANISOU 1471  CD2 TYR A 194    16314  10500  15861   -509  -3009    931  A    C  
ATOM   1472  CE1 TYR A 194      52.164 -24.073   0.497  1.00121.05      A    C  
ANISOU 1472  CE1 TYR A 194    17408  11927  16657   -274  -3148   1263  A    C  
ATOM   1473  CE2 TYR A 194      51.469 -25.712  -1.099  1.00123.56      A    C  
ANISOU 1473  CE2 TYR A 194    17708  11944  17297   -201  -3179    936  A    C  
ATOM   1474  CZ  TYR A 194      52.475 -24.978  -0.494  1.00125.87      A    C  
ANISOU 1474  CZ  TYR A 194    17988  12403  17435    -85  -3246   1106  A    C  
ATOM   1475  OH  TYR A 194      53.790 -25.154  -0.880  1.00126.00      A    O  
ANISOU 1475  OH  TYR A 194    17955  12456  17462    220  -3413   1111  A    O  
ATOM   1476  N   ARG A 195      45.496 -26.187   1.771  1.00110.13      A    N  
ANISOU 1476  N   ARG A 195    16436   9791  15616  -1716  -2419   1135  A    N  
ATOM   1477  CA  ARG A 195      44.089 -26.018   2.107  1.00107.53      A    C  
ANISOU 1477  CA  ARG A 195    16088   9485  15282  -2033  -2225   1119  A    C  
ATOM   1478  C   ARG A 195      43.889 -26.141   3.617  1.00111.18      A    C  
ANISOU 1478  C   ARG A 195    16811   9795  15636  -2227  -2148   1417  A    C  
ATOM   1479  O   ARG A 195      44.566 -26.934   4.272  1.00114.97      A    O  
ANISOU 1479  O   ARG A 195    17536  10008  16141  -2164  -2242   1599  A    O  
ATOM   1480  CB  ARG A 195      43.223 -27.041   1.365  1.00108.10      A    C  
ANISOU 1480  CB  ARG A 195    16136   9350  15588  -2161  -2190    908  A    C  
ATOM   1481  CG  ARG A 195      41.727 -26.854   1.584  1.00111.85      A    C  
ANISOU 1481  CG  ARG A 195    16544   9884  16071  -2487  -1988    860  A    C  
ATOM   1482  CD  ARG A 195      40.909 -27.860   0.821  1.00121.92      A    C  
ANISOU 1482  CD  ARG A 195    17775  10965  17585  -2620  -1964    628  A    C  
ATOM   1483  NE  ARG A 195      41.266 -27.919  -0.593  1.00128.91      A    N  
ANISOU 1483  NE  ARG A 195    18449  11968  18564  -2389  -2080    338  A    N  
ATOM   1484  CZ  ARG A 195      40.772 -28.816  -1.444  1.00128.29      A    C  
ANISOU 1484  CZ  ARG A 195    18313  11734  18697  -2439  -2104     90  A    C  
ATOM   1485  NH1 ARG A 195      39.903 -29.725  -1.016  1.00127.15      A    N1+
ANISOU 1485  NH1 ARG A 195    18307  11296  18710  -2727  -2014     99  A    N1+
ATOM   1486  NH2 ARG A 195      41.145 -28.803  -2.719  1.00123.04      A    N  
ANISOU 1486  NH2 ARG A 195    17453  11208  18089  -2204  -2213   -171  A    N  
ATOM   1487  N   PRO A 196      42.967 -25.336   4.174  1.00109.90      A    N  
ANISOU 1487  N   PRO A 196    16597   9817  15343  -2445  -1975   1473  A    N  
ATOM   1488  CA  PRO A 196      42.640 -25.291   5.605  1.00110.03      A    C  
ANISOU 1488  CA  PRO A 196    16833   9748  15225  -2640  -1875   1746  A    C  
ATOM   1489  C   PRO A 196      41.499 -26.224   5.982  1.00113.65      A    C  
ANISOU 1489  C   PRO A 196    17423   9940  15818  -2932  -1737   1781  A    C  
ATOM   1490  O   PRO A 196      40.717 -26.603   5.111  1.00119.15      A    O  
ANISOU 1490  O   PRO A 196    17979  10606  16687  -3031  -1684   1557  A    O  
ATOM   1491  CB  PRO A 196      42.172 -23.844   5.810  1.00100.51      A    C  
ANISOU 1491  CB  PRO A 196    15457   8916  13816  -2709  -1748   1739  A    C  
ATOM   1492  CG  PRO A 196      41.966 -23.267   4.439  1.00 98.08      A    C  
ANISOU 1492  CG  PRO A 196    14840   8856  13571  -2601  -1745   1453  A    C  
ATOM   1493  CD  PRO A 196      42.216 -24.322   3.418  1.00101.50      A    C  
ANISOU 1493  CD  PRO A 196    15243   9091  14232  -2487  -1864   1273  A    C  
ATOM   1494  N   PRO A 197      41.374 -26.552   7.277  1.00115.05      A    N  
ANISOU 1494  N   PRO A 197    17858   9944  15911  -3074  -1671   2057  A    N  
ATOM   1495  CA  PRO A 197      40.352 -27.500   7.744  1.00118.75      A    C  
ANISOU 1495  CA  PRO A 197    18479  10127  16512  -3359  -1529   2130  A    C  
ATOM   1496  C   PRO A 197      38.935 -27.096   7.343  1.00120.98      A    C  
ANISOU 1496  C   PRO A 197    18549  10581  16837  -3612  -1340   1957  A    C  
ATOM   1497  O   PRO A 197      38.180 -27.968   6.930  1.00131.15      A    O  
ANISOU 1497  O   PRO A 197    19829  11662  18339  -3783  -1278   1838  A    O  
ATOM   1498  CB  PRO A 197      40.489 -27.452   9.271  1.00115.69      A    C  
ANISOU 1498  CB  PRO A 197    18356   9667  15935  -3437  -1470   2473  A    C  
ATOM   1499  CG  PRO A 197      41.864 -26.908   9.520  1.00114.32      A    C  
ANISOU 1499  CG  PRO A 197    18221   9626  15589  -3145  -1648   2572  A    C  
ATOM   1500  CD  PRO A 197      42.136 -25.964   8.391  1.00109.07      A    C  
ANISOU 1500  CD  PRO A 197    17248   9281  14913  -2985  -1713   2312  A    C  
ATOM   1501  N   GLU A 198      38.584 -25.816   7.455  1.00113.73      A    N  
ANISOU 1501  N   GLU A 198    17460  10029  15722  -3633  -1251   1936  A    N  
ATOM   1502  CA  GLU A 198      37.211 -25.378   7.211  1.00116.54      A    C  
ANISOU 1502  CA  GLU A 198    17623  10572  16087  -3868  -1059   1803  A    C  
ATOM   1503  C   GLU A 198      36.678 -25.972   5.932  1.00117.18      A    C  
ANISOU 1503  C   GLU A 198    17511  10601  16409  -3902  -1076   1500  A    C  
ATOM   1504  O   GLU A 198      35.512 -26.375   5.846  1.00119.23      A    O  
ANISOU 1504  O   GLU A 198    17709  10808  16785  -4159   -935   1416  A    O  
ATOM   1505  CB  GLU A 198      37.121 -23.860   7.070  1.00122.90      A    C  
ANISOU 1505  CB  GLU A 198    18214  11805  16677  -3788  -1004   1743  A    C  
ATOM   1506  CG  GLU A 198      37.817 -23.061   8.132  1.00126.09      A    C  
ANISOU 1506  CG  GLU A 198    18757  12321  16829  -3702  -1020   1979  A    C  
ATOM   1507  CD  GLU A 198      39.136 -22.534   7.655  1.00129.31      A    C  
ANISOU 1507  CD  GLU A 198    19105  12850  17178  -3391  -1207   1932  A    C  
ATOM   1508  OE1 GLU A 198      39.865 -23.308   7.008  1.00130.14      A    O  
ANISOU 1508  OE1 GLU A 198    19231  12776  17439  -3233  -1365   1854  A    O  
ATOM   1509  OE2 GLU A 198      39.444 -21.354   7.919  1.00133.28      A    O1-
ANISOU 1509  OE2 GLU A 198    19536  13620  17482  -3307  -1190   1968  A    O1-
ATOM   1510  N   LEU A 199      37.539 -25.999   4.924  1.00112.98      A    N  
ANISOU 1510  N   LEU A 199    16875  10107  15946  -3637  -1250   1328  A    N  
ATOM   1511  CA  LEU A 199      37.111 -26.385   3.589  1.00115.21      A    C  
ANISOU 1511  CA  LEU A 199    16939  10414  16422  -3619  -1282   1006  A    C  
ATOM   1512  C   LEU A 199      36.969 -27.908   3.457  1.00112.88      A    C  
ANISOU 1512  C   LEU A 199    16802   9693  16393  -3733  -1322    961  A    C  
ATOM   1513  O   LEU A 199      36.048 -28.406   2.806  1.00111.65      A    O  
ANISOU 1513  O   LEU A 199    16517   9494  16412  -3901  -1260    742  A    O  
ATOM   1514  CB  LEU A 199      38.067 -25.799   2.541  1.00105.73      A    C  
ANISOU 1514  CB  LEU A 199    15557   9433  15181  -3283  -1440    839  A    C  
ATOM   1515  CG  LEU A 199      38.234 -24.279   2.616  1.00 97.65      A    C  
ANISOU 1515  CG  LEU A 199    14376   8810  13915  -3169  -1392    877  A    C  
ATOM   1516  CD1 LEU A 199      39.127 -23.782   1.488  1.00103.05      A    C  
ANISOU 1516  CD1 LEU A 199    14871   9694  14588  -2847  -1533    705  A    C  
ATOM   1517  CD2 LEU A 199      36.888 -23.554   2.599  1.00 84.90      A    C  
ANISOU 1517  CD2 LEU A 199    12575   7456  12227  -3378  -1191    797  A    C  
ATOM   1518  N   LEU A 200      37.881 -28.639   4.086  1.00110.28      A    N  
ANISOU 1518  N   LEU A 200    16755   9051  16094  -3640  -1424   1166  A    N  
ATOM   1519  CA  LEU A 200      37.801 -30.086   4.115  1.00121.20      A    C  
ANISOU 1519  CA  LEU A 200    18337   9990  17723  -3744  -1448   1168  A    C  
ATOM   1520  C   LEU A 200      36.510 -30.546   4.797  1.00127.24      A    C  
ANISOU 1520  C   LEU A 200    19177  10598  18569  -4128  -1239   1249  A    C  
ATOM   1521  O   LEU A 200      35.837 -31.459   4.315  1.00126.18      A    O  
ANISOU 1521  O   LEU A 200    19025  10239  18678  -4304  -1199   1081  A    O  
ATOM   1522  CB  LEU A 200      39.036 -30.654   4.801  1.00122.58      A    C  
ANISOU 1522  CB  LEU A 200    18811   9892  17872  -3552  -1581   1419  A    C  
ATOM   1523  CG  LEU A 200      40.281 -30.085   4.116  1.00119.24      A    C  
ANISOU 1523  CG  LEU A 200    18274   9675  17357  -3181  -1777   1333  A    C  
ATOM   1524  CD1 LEU A 200      41.586 -30.512   4.797  1.00119.60      A    C  
ANISOU 1524  CD1 LEU A 200    18584   9516  17344  -2958  -1922   1581  A    C  
ATOM   1525  CD2 LEU A 200      40.276 -30.463   2.639  1.00117.64      A    C  
ANISOU 1525  CD2 LEU A 200    17869   9482  17345  -3063  -1871    982  A    C  
ATOM   1526  N   LEU A 201      36.155 -29.894   5.901  1.00129.75      A    N  
ANISOU 1526  N   LEU A 201    19569  11044  18686  -4260  -1102   1495  A    N  
ATOM   1527  CA  LEU A 201      34.895 -30.182   6.575  1.00139.34      A    C  
ANISOU 1527  CA  LEU A 201    20827  12167  19947  -4621   -884   1583  A    C  
ATOM   1528  C   LEU A 201      33.705 -29.652   5.789  1.00144.71      A    C  
ANISOU 1528  C   LEU A 201    21175  13142  20665  -4788   -769   1305  A    C  
ATOM   1529  O   LEU A 201      32.587 -29.626   6.300  1.00152.84      A    O  
ANISOU 1529  O   LEU A 201    22175  14202  21695  -5080   -575   1358  A    O  
ATOM   1530  CB  LEU A 201      34.868 -29.578   7.976  1.00140.40      A    C  
ANISOU 1530  CB  LEU A 201    21128  12389  19830  -4692   -770   1921  A    C  
ATOM   1531  CG  LEU A 201      35.927 -30.066   8.955  1.00144.30      A    C  
ANISOU 1531  CG  LEU A 201    21961  12619  20246  -4552   -860   2236  A    C  
ATOM   1532  CD1 LEU A 201      35.405 -29.947  10.385  1.00147.09      A    C  
ANISOU 1532  CD1 LEU A 201    22508  12942  20438  -4756   -680   2557  A    C  
ATOM   1533  CD2 LEU A 201      36.314 -31.494   8.634  1.00145.85      A    C  
ANISOU 1533  CD2 LEU A 201    22340  12362  20713  -4526   -950   2213  A    C  
ATOM   1534  N   GLY A 202      33.949 -29.219   4.556  1.00139.65      A    N  
ANISOU 1534  N   GLY A 202    20279  12735  20046  -4590   -885   1015  A    N  
ATOM   1535  CA  GLY A 202      32.890 -28.725   3.693  1.00134.41      A    C  
ANISOU 1535  CA  GLY A 202    19284  12375  19410  -4701   -798    730  A    C  
ATOM   1536  C   GLY A 202      32.240 -27.419   4.130  1.00129.61      A    C  
ANISOU 1536  C   GLY A 202    18522  12169  18556  -4766   -645    803  A    C  
ATOM   1537  O   GLY A 202      31.017 -27.306   4.145  1.00125.82      A    O  
ANISOU 1537  O   GLY A 202    17892  11813  18100  -5015   -480    724  A    O  
ATOM   1538  N   GLU A 203      33.042 -26.418   4.477  1.00128.99      A    N  
ANISOU 1538  N   GLU A 203    18471  12298  18241  -4545   -696    946  A    N  
ATOM   1539  CA  GLU A 203      32.472 -25.112   4.792  1.00125.22      A    C  
ANISOU 1539  CA  GLU A 203    17840  12207  17531  -4576   -556    988  A    C  
ATOM   1540  C   GLU A 203      32.201 -24.317   3.518  1.00121.75      A    C  
ANISOU 1540  C   GLU A 203    17057  12136  17068  -4429   -577    691  A    C  
ATOM   1541  O   GLU A 203      32.937 -24.423   2.541  1.00117.32      A    O  
ANISOU 1541  O   GLU A 203    16409  11589  16578  -4191   -739    520  A    O  
ATOM   1542  CB  GLU A 203      33.378 -24.317   5.727  1.00120.42      A    C  
ANISOU 1542  CB  GLU A 203    17400  11674  16679  -4421   -588   1254  A    C  
ATOM   1543  CG  GLU A 203      32.914 -22.888   5.930  1.00120.68      A    C  
ANISOU 1543  CG  GLU A 203    17269  12110  16473  -4410   -459   1267  A    C  
ATOM   1544  CD  GLU A 203      31.871 -22.758   7.018  1.00124.83      A    C  
ANISOU 1544  CD  GLU A 203    17872  12656  16904  -4693   -245   1442  A    C  
ATOM   1545  OE1 GLU A 203      32.011 -23.429   8.060  1.00122.27      A    O  
ANISOU 1545  OE1 GLU A 203    17819  12058  16582  -4817   -220   1683  A    O  
ATOM   1546  OE2 GLU A 203      30.922 -21.969   6.842  1.00126.99      A    O1-
ANISOU 1546  OE2 GLU A 203    17935  13227  17087  -4779    -97   1348  A    O1-
ATOM   1547  N   ARG A 204      31.130 -23.535   3.531  1.00126.70      A    N  
ANISOU 1547  N   ARG A 204    17486  13064  17589  -4560   -407    634  A    N  
ATOM   1548  CA  ARG A 204      30.775 -22.701   2.387  1.00126.60      A    C  
ANISOU 1548  CA  ARG A 204    17145  13431  17526  -4415   -402    373  A    C  
ATOM   1549  C   ARG A 204      30.569 -21.242   2.799  1.00115.09      A    C  
ANISOU 1549  C   ARG A 204    15599  12329  15802  -4349   -278    477  A    C  
ATOM   1550  O   ARG A 204      30.298 -20.387   1.957  1.00105.19      A    O  
ANISOU 1550  O   ARG A 204    14087  11410  14469  -4208   -252    303  A    O  
ATOM   1551  CB  ARG A 204      29.520 -23.238   1.690  1.00131.56      A    C  
ANISOU 1551  CB  ARG A 204    17553  14114  18320  -4623   -321    121  A    C  
ATOM   1552  CG  ARG A 204      29.733 -24.533   0.946  1.00134.11      A    C  
ANISOU 1552  CG  ARG A 204    17897  14144  18912  -4639   -460    -70  A    C  
ATOM   1553  CD  ARG A 204      28.429 -25.027   0.359  1.00145.24      A    C  
ANISOU 1553  CD  ARG A 204    19085  15621  20480  -4878   -371   -323  A    C  
ATOM   1554  NE  ARG A 204      27.962 -24.181  -0.732  1.00146.28      A    N  
ANISOU 1554  NE  ARG A 204    18869  16188  20524  -4729   -363   -583  A    N  
ATOM   1555  CZ  ARG A 204      28.337 -24.329  -1.998  1.00146.25      A    C  
ANISOU 1555  CZ  ARG A 204    18698  16274  20595  -4510   -512   -854  A    C  
ATOM   1556  NH1 ARG A 204      29.200 -25.287  -2.331  1.00144.36      A    N1+
ANISOU 1556  NH1 ARG A 204    18610  15714  20527  -4416   -683   -908  A    N1+
ATOM   1557  NH2 ARG A 204      27.855 -23.515  -2.929  1.00144.48      A    N  
ANISOU 1557  NH2 ARG A 204    18161  16468  20268  -4370   -487  -1066  A    N  
ATOM   1558  N   ASP A 205      30.671 -20.980   4.101  1.00116.68      A    N  
ANISOU 1558  N   ASP A 205    16019  12453  15862  -4450   -195    759  A    N  
ATOM   1559  CA  ASP A 205      30.663 -19.622   4.627  1.00123.29      A    C  
ANISOU 1559  CA  ASP A 205    16827  13577  16441  -4373    -93    880  A    C  
ATOM   1560  C   ASP A 205      32.037 -19.350   5.241  1.00121.31      A    C  
ANISOU 1560  C   ASP A 205    16800  13213  16079  -4186   -222   1078  A    C  
ATOM   1561  O   ASP A 205      32.195 -19.244   6.461  1.00124.15      A    O  
ANISOU 1561  O   ASP A 205    17379  13480  16312  -4275   -171   1324  A    O  
ATOM   1562  CB  ASP A 205      29.539 -19.420   5.653  1.00126.95      A    C  
ANISOU 1562  CB  ASP A 205    17333  14098  16802  -4647    126   1025  A    C  
ATOM   1563  CG  ASP A 205      29.419 -17.971   6.118  1.00135.11      A    C  
ANISOU 1563  CG  ASP A 205    18317  15448  17571  -4564    245   1115  A    C  
ATOM   1564  OD1 ASP A 205      29.815 -17.050   5.360  1.00134.40      A    O  
ANISOU 1564  OD1 ASP A 205    18064  15600  17402  -4327    201    994  A    O  
ATOM   1565  OD2 ASP A 205      28.922 -17.755   7.246  1.00137.73      A    O1-
ANISOU 1565  OD2 ASP A 205    18778  15781  17772  -4734    390   1309  A    O1-
ATOM   1566  N   TYR A 206      33.035 -19.264   4.373  1.00108.52      A    N  
ANISOU 1566  N   TYR A 206    15115  11612  14507  -3922   -393    963  A    N  
ATOM   1567  CA  TYR A 206      34.394 -19.037   4.811  1.00106.51      A    C  
ANISOU 1567  CA  TYR A 206    15035  11269  14166  -3729   -533   1118  A    C  
ATOM   1568  C   TYR A 206      34.815 -17.640   4.413  1.00 97.67      A    C  
ANISOU 1568  C   TYR A 206    13757  10473  12881  -3513   -524   1069  A    C  
ATOM   1569  O   TYR A 206      34.106 -16.967   3.672  1.00 90.84      A    O  
ANISOU 1569  O   TYR A 206    12652   9877  11988  -3484   -424    905  A    O  
ATOM   1570  CB  TYR A 206      35.334 -20.067   4.192  1.00111.34      A    C  
ANISOU 1570  CB  TYR A 206    15713  11628  14964  -3585   -740   1048  A    C  
ATOM   1571  CG  TYR A 206      35.241 -20.160   2.689  1.00105.36      A    C  
ANISOU 1571  CG  TYR A 206    14698  10995  14340  -3441   -805    753  A    C  
ATOM   1572  CD1 TYR A 206      34.459 -21.130   2.080  1.00104.47      A    C  
ANISOU 1572  CD1 TYR A 206    14505  10761  14426  -3580   -794    574  A    C  
ATOM   1573  CD2 TYR A 206      35.941 -19.288   1.880  1.00 96.17      A    C  
ANISOU 1573  CD2 TYR A 206    13368  10069  13102  -3166   -875    652  A    C  
ATOM   1574  CE1 TYR A 206      34.376 -21.223   0.708  1.00 98.93      A    C  
ANISOU 1574  CE1 TYR A 206    13567  10191  13831  -3438   -861    292  A    C  
ATOM   1575  CE2 TYR A 206      35.859 -19.371   0.506  1.00 93.92      A    C  
ANISOU 1575  CE2 TYR A 206    12849   9914  12921  -3016   -931    390  A    C  
ATOM   1576  CZ  TYR A 206      35.076 -20.340  -0.073  1.00 95.08      A    C  
ANISOU 1576  CZ  TYR A 206    12922   9955  13251  -3148   -930    206  A    C  
ATOM   1577  OH  TYR A 206      35.000 -20.421  -1.442  1.00 94.48      A    O  
ANISOU 1577  OH  TYR A 206    12609  10026  13261  -2988   -993    -67  A    O  
ATOM   1578  N   GLY A 207      35.968 -17.207   4.909  1.00 99.21      A    N  
ANISOU 1578  N   GLY A 207    14086  10642  12968  -3360   -625   1212  A    N  
ATOM   1579  CA  GLY A 207      36.442 -15.866   4.622  1.00 99.29      A    C  
ANISOU 1579  CA  GLY A 207    13967  10928  12829  -3170   -609   1182  A    C  
ATOM   1580  C   GLY A 207      37.950 -15.718   4.580  1.00 96.12      A    C  
ANISOU 1580  C   GLY A 207    13640  10470  12411  -2940   -792   1241  A    C  
ATOM   1581  O   GLY A 207      38.681 -16.694   4.407  1.00 91.75      A    O  
ANISOU 1581  O   GLY A 207    13182   9691  11987  -2868   -955   1248  A    O  
ATOM   1582  N   PRO A 208      38.426 -14.478   4.743  1.00 98.06      A    N  
ANISOU 1582  N   PRO A 208    13839  10921  12500  -2824   -760   1281  A    N  
ATOM   1583  CA  PRO A 208      39.858 -14.178   4.777  1.00 91.01      A    C  
ANISOU 1583  CA  PRO A 208    12996  10010  11575  -2621   -919   1339  A    C  
ATOM   1584  C   PRO A 208      40.698 -15.234   5.481  1.00 89.89      A    C  
ANISOU 1584  C   PRO A 208    13091   9581  11482  -2626  -1088   1487  A    C  
ATOM   1585  O   PRO A 208      41.815 -15.476   5.033  1.00 95.26      A    O  
ANISOU 1585  O   PRO A 208    13761  10206  12229  -2430  -1257   1464  A    O  
ATOM   1586  CB  PRO A 208      39.895 -12.856   5.524  1.00 86.00      A    C  
ANISOU 1586  CB  PRO A 208    12382   9562  10734  -2640   -810   1434  A    C  
ATOM   1587  CG  PRO A 208      38.661 -12.156   4.999  1.00 85.83      A    C  
ANISOU 1587  CG  PRO A 208    12170   9764  10678  -2701   -608   1312  A    C  
ATOM   1588  CD  PRO A 208      37.617 -13.248   4.828  1.00 95.15      A    C  
ANISOU 1588  CD  PRO A 208    13347  10823  11982  -2872   -565   1256  A    C  
ATOM   1589  N   PRO A 209      40.176 -15.865   6.546  1.00 83.78      A    N  
ANISOU 1589  N   PRO A 209    12526   8633  10675  -2836  -1039   1641  A    N  
ATOM   1590  CA  PRO A 209      41.039 -16.829   7.238  1.00 79.62      A    C  
ANISOU 1590  CA  PRO A 209    12236   7838  10179  -2812  -1198   1801  A    C  
ATOM   1591  C   PRO A 209      41.595 -17.980   6.386  1.00 85.62      A    C  
ANISOU 1591  C   PRO A 209    12989   8391  11153  -2682  -1361   1708  A    C  
ATOM   1592  O   PRO A 209      42.659 -18.495   6.721  1.00 93.73      A    O  
ANISOU 1592  O   PRO A 209    14159   9263  12191  -2560  -1525   1815  A    O  
ATOM   1593  CB  PRO A 209      40.141 -17.342   8.363  1.00 73.67      A    C  
ANISOU 1593  CB  PRO A 209    11681   6941   9371  -3070  -1077   1966  A    C  
ATOM   1594  CG  PRO A 209      39.274 -16.161   8.698  1.00 68.17      A    C  
ANISOU 1594  CG  PRO A 209    10890   6502   8507  -3184   -881   1957  A    C  
ATOM   1595  CD  PRO A 209      38.984 -15.524   7.350  1.00 79.17      A    C  
ANISOU 1595  CD  PRO A 209    11991   8114   9975  -3072   -838   1718  A    C  
ATOM   1596  N   ILE A 210      40.930 -18.367   5.305  1.00 79.40      A    N  
ANISOU 1596  N   ILE A 210    12034   7610  10524  -2693  -1324   1508  A    N  
ATOM   1597  CA  ILE A 210      41.436 -19.494   4.528  1.00 84.25      A    C  
ANISOU 1597  CA  ILE A 210    12656   8015  11340  -2573  -1478   1409  A    C  
ATOM   1598  C   ILE A 210      42.784 -19.194   3.861  1.00 92.96      A    C  
ANISOU 1598  C   ILE A 210    13671   9200  12450  -2272  -1649   1354  A    C  
ATOM   1599  O   ILE A 210      43.541 -20.125   3.512  1.00 88.69      A    O  
ANISOU 1599  O   ILE A 210    13199   8462  12039  -2135  -1809   1336  A    O  
ATOM   1600  CB  ILE A 210      40.457 -19.960   3.432  1.00 83.98      A    C  
ANISOU 1600  CB  ILE A 210    12442   7992  11473  -2638  -1414   1172  A    C  
ATOM   1601  CG1 ILE A 210      40.520 -19.026   2.229  1.00 78.11      A    C  
ANISOU 1601  CG1 ILE A 210    11407   7561  10710  -2451  -1401    966  A    C  
ATOM   1602  CG2 ILE A 210      39.029 -20.106   3.969  1.00 90.80      A    C  
ANISOU 1602  CG2 ILE A 210    13334   8836  12332  -2942  -1223   1198  A    C  
ATOM   1603  CD1 ILE A 210      39.912 -19.634   0.988  1.00 78.08      A    C  
ANISOU 1603  CD1 ILE A 210    11225   7561  10880  -2432  -1407    709  A    C  
ATOM   1604  N   ASP A 211      43.072 -17.905   3.662  1.00 90.15      A    N  
ANISOU 1604  N   ASP A 211    13160   9130  11962  -2168  -1607   1325  A    N  
ATOM   1605  CA  ASP A 211      44.341 -17.494   3.056  1.00 85.58      A    C  
ANISOU 1605  CA  ASP A 211    12478   8655  11383  -1896  -1748   1282  A    C  
ATOM   1606  C   ASP A 211      45.412 -17.427   4.128  1.00 88.82      A    C  
ANISOU 1606  C   ASP A 211    13075   8988  11683  -1849  -1862   1490  A    C  
ATOM   1607  O   ASP A 211      46.569 -17.748   3.885  1.00 89.82      A    O  
ANISOU 1607  O   ASP A 211    13213   9059  11857  -1649  -2033   1502  A    O  
ATOM   1608  CB  ASP A 211      44.226 -16.148   2.334  1.00 82.14      A    C  
ANISOU 1608  CB  ASP A 211    11794   8546  10869  -1800  -1646   1163  A    C  
ATOM   1609  CG  ASP A 211      43.351 -16.218   1.095  1.00 86.81      A    C  
ANISOU 1609  CG  ASP A 211    12169   9251  11564  -1777  -1564    939  A    C  
ATOM   1610  OD1 ASP A 211      43.224 -17.339   0.545  1.00 89.44      A    O  
ANISOU 1610  OD1 ASP A 211    12515   9413  12056  -1762  -1645    839  A    O  
ATOM   1611  OD2 ASP A 211      42.798 -15.157   0.673  1.00 77.85      A    O1-
ANISOU 1611  OD2 ASP A 211    10855   8377  10349  -1767  -1421    861  A    O1-
ATOM   1612  N   LEU A 212      45.017 -17.018   5.324  1.00 97.36      A    N  
ANISOU 1612  N   LEU A 212    14301  10081  12612  -2029  -1770   1649  A    N  
ATOM   1613  CA  LEU A 212      45.958 -16.908   6.425  1.00103.14      A    C  
ANISOU 1613  CA  LEU A 212    15210  10767  13213  -1995  -1875   1843  A    C  
ATOM   1614  C   LEU A 212      46.580 -18.250   6.727  1.00 99.61      A    C  
ANISOU 1614  C   LEU A 212    14958  10031  12858  -1933  -2037   1947  A    C  
ATOM   1615  O   LEU A 212      47.768 -18.333   7.022  1.00 98.65      A    O  
ANISOU 1615  O   LEU A 212    14898   9888  12696  -1771  -2200   2033  A    O  
ATOM   1616  CB  LEU A 212      45.255 -16.378   7.659  1.00108.21      A    C  
ANISOU 1616  CB  LEU A 212    15986  11454  13673  -2212  -1735   1987  A    C  
ATOM   1617  CG  LEU A 212      44.966 -14.898   7.509  1.00107.02      A    C  
ANISOU 1617  CG  LEU A 212    15666  11595  13401  -2226  -1601   1910  A    C  
ATOM   1618  CD1 LEU A 212      43.947 -14.495   8.558  1.00120.46      A    C  
ANISOU 1618  CD1 LEU A 212    17483  13335  14949  -2459  -1426   2015  A    C  
ATOM   1619  CD2 LEU A 212      46.267 -14.140   7.644  1.00 94.20      A    C  
ANISOU 1619  CD2 LEU A 212    14002  10096  11693  -2055  -1723   1937  A    C  
ATOM   1620  N   TRP A 213      45.763 -19.297   6.653  1.00 99.75      A    N  
ANISOU 1620  N   TRP A 213    15069   9827  13003  -2063  -1989   1938  A    N  
ATOM   1621  CA  TRP A 213      46.237 -20.664   6.825  1.00100.22      A    C  
ANISOU 1621  CA  TRP A 213    15321   9576  13182  -2006  -2123   2023  A    C  
ATOM   1622  C   TRP A 213      47.295 -20.978   5.777  1.00 93.22      A    C  
ANISOU 1622  C   TRP A 213    14316   8682  12421  -1728  -2299   1896  A    C  
ATOM   1623  O   TRP A 213      48.375 -21.459   6.106  1.00 91.82      A    O  
ANISOU 1623  O   TRP A 213    14258   8393  12236  -1566  -2463   2006  A    O  
ATOM   1624  CB  TRP A 213      45.076 -21.645   6.708  1.00108.14      A    C  
ANISOU 1624  CB  TRP A 213    16400  10352  14334  -2207  -2016   1986  A    C  
ATOM   1625  CG  TRP A 213      45.448 -23.084   6.874  1.00115.05      A    C  
ANISOU 1625  CG  TRP A 213    17489  10871  15352  -2167  -2127   2072  A    C  
ATOM   1626  CD1 TRP A 213      45.897 -23.937   5.904  1.00118.27      A    C  
ANISOU 1626  CD1 TRP A 213    17858  11122  15956  -2005  -2250   1934  A    C  
ATOM   1627  CD2 TRP A 213      45.384 -23.848   8.084  1.00123.89      A    C  
ANISOU 1627  CD2 TRP A 213    18904  11738  16429  -2282  -2117   2320  A    C  
ATOM   1628  CE2 TRP A 213      45.815 -25.159   7.776  1.00126.24      A    C  
ANISOU 1628  CE2 TRP A 213    19336  11716  16912  -2182  -2232   2324  A    C  
ATOM   1629  CE3 TRP A 213      45.008 -23.553   9.401  1.00125.70      A    C  
ANISOU 1629  CE3 TRP A 213    19302  11982  16475  -2450  -2016   2542  A    C  
ATOM   1630  NE1 TRP A 213      46.121 -25.188   6.439  1.00125.67      A    N  
ANISOU 1630  NE1 TRP A 213    19055  11710  16985  -2015  -2315   2078  A    N  
ATOM   1631  CZ2 TRP A 213      45.879 -26.170   8.736  1.00126.43      A    C  
ANISOU 1631  CZ2 TRP A 213    19660  11428  16949  -2243  -2243   2555  A    C  
ATOM   1632  CZ3 TRP A 213      45.074 -24.559  10.354  1.00128.44      A    C  
ANISOU 1632  CZ3 TRP A 213    19941  12036  16823  -2509  -2029   2771  A    C  
ATOM   1633  CH2 TRP A 213      45.505 -25.851  10.015  1.00128.51      A    C  
ANISOU 1633  CH2 TRP A 213    20082  11721  17025  -2405  -2139   2782  A    C  
ATOM   1634  N   GLY A 214      46.990 -20.698   4.514  1.00 86.77      A    N  
ANISOU 1634  N   GLY A 214    13260   7999  11709  -1660  -2263   1666  A    N  
ATOM   1635  CA  GLY A 214      48.000 -20.815   3.481  1.00 92.74      A    C  
ANISOU 1635  CA  GLY A 214    13875   8803  12557  -1382  -2413   1540  A    C  
ATOM   1636  C   GLY A 214      49.297 -20.148   3.925  1.00 99.81      A    C  
ANISOU 1636  C   GLY A 214    14766   9836  13321  -1210  -2532   1655  A    C  
ATOM   1637  O   GLY A 214      50.380 -20.736   3.854  1.00105.10      A    O  
ANISOU 1637  O   GLY A 214    15492  10404  14037  -1011  -2706   1699  A    O  
ATOM   1638  N   ALA A 215      49.179 -18.913   4.408  1.00 91.88      A    N  
ANISOU 1638  N   ALA A 215    13694   9065  12152  -1290  -2437   1701  A    N  
ATOM   1639  CA  ALA A 215      50.339 -18.131   4.804  1.00 87.78      A    C  
ANISOU 1639  CA  ALA A 215    13138   8705  11508  -1155  -2534   1783  A    C  
ATOM   1640  C   ALA A 215      51.130 -18.819   5.906  1.00 93.25      A    C  
ANISOU 1640  C   ALA A 215    14070   9227  12134  -1122  -2682   1988  A    C  
ATOM   1641  O   ALA A 215      52.344 -18.617   6.032  1.00 91.63      A    O  
ANISOU 1641  O   ALA A 215    13836   9098  11881   -944  -2830   2037  A    O  
ATOM   1642  CB  ALA A 215      49.913 -16.742   5.243  1.00 85.70      A    C  
ANISOU 1642  CB  ALA A 215    12795   8683  11084  -1287  -2385   1795  A    C  
ATOM   1643  N   GLY A 216      50.439 -19.614   6.717  1.00 96.49      A    N  
ANISOU 1643  N   GLY A 216    14711   9415  12536  -1291  -2636   2115  A    N  
ATOM   1644  CA  GLY A 216      51.108 -20.403   7.731  1.00100.25      A    C  
ANISOU 1644  CA  GLY A 216    15433   9704  12952  -1246  -2768   2323  A    C  
ATOM   1645  C   GLY A 216      51.964 -21.460   7.061  1.00100.64      A    C  
ANISOU 1645  C   GLY A 216    15499   9578  13160  -1011  -2942   2288  A    C  
ATOM   1646  O   GLY A 216      53.193 -21.457   7.156  1.00106.95      A    O  
ANISOU 1646  O   GLY A 216    16286  10432  13919   -800  -3110   2341  A    O  
ATOM   1647  N   CYS A 217      51.306 -22.361   6.354  1.00 93.82      A    N  
ANISOU 1647  N   CYS A 217    14654   8510  12482  -1045  -2901   2185  A    N  
ATOM   1648  CA  CYS A 217      52.005 -23.405   5.639  1.00100.01      A    C  
ANISOU 1648  CA  CYS A 217    15459   9108  13432   -826  -3050   2127  A    C  
ATOM   1649  C   CYS A 217      53.223 -22.847   4.915  1.00106.01      A    C  
ANISOU 1649  C   CYS A 217    16008  10088  14183   -553  -3188   2035  A    C  
ATOM   1650  O   CYS A 217      54.234 -23.525   4.779  1.00120.21      A    O  
ANISOU 1650  O   CYS A 217    17857  11785  16033   -326  -3356   2073  A    O  
ATOM   1651  CB  CYS A 217      51.050 -24.083   4.665  1.00101.18      A    C  
ANISOU 1651  CB  CYS A 217    15558   9103  13784   -905  -2966   1939  A    C  
ATOM   1652  SG  CYS A 217      49.552 -24.684   5.486  1.00116.90      A    S  
ANISOU 1652  SG  CYS A 217    17764  10851  15801  -1258  -2782   2037  A    S  
ATOM   1653  N   ILE A 218      53.135 -21.604   4.463  1.00102.80      A    N  
ANISOU 1653  N   ILE A 218    15367   9983  13711   -568  -3109   1923  A    N  
ATOM   1654  CA  ILE A 218      54.270 -20.985   3.788  1.00103.17      A    C  
ANISOU 1654  CA  ILE A 218    15200  10250  13749   -326  -3216   1845  A    C  
ATOM   1655  C   ILE A 218      55.337 -20.491   4.767  1.00106.25      A    C  
ANISOU 1655  C   ILE A 218    15639  10756  13975   -258  -3330   2012  A    C  
ATOM   1656  O   ILE A 218      56.522 -20.561   4.465  1.00109.62      A    O  
ANISOU 1656  O   ILE A 218    15982  11251  14418    -23  -3484   2009  A    O  
ATOM   1657  CB  ILE A 218      53.843 -19.829   2.855  1.00 93.77      A    C  
ANISOU 1657  CB  ILE A 218    13733   9336  12561   -346  -3083   1664  A    C  
ATOM   1658  CG1 ILE A 218      52.636 -20.239   2.015  1.00 92.04      A    C  
ANISOU 1658  CG1 ILE A 218    13463   9035  12472   -446  -2959   1499  A    C  
ATOM   1659  CG2 ILE A 218      55.002 -19.406   1.951  1.00 84.58      A    C  
ANISOU 1659  CG2 ILE A 218    12344   8361  11432    -74  -3188   1571  A    C  
ATOM   1660  CD1 ILE A 218      52.399 -19.351   0.810  1.00 90.51      A    C  
ANISOU 1660  CD1 ILE A 218    12981   9100  12307   -370  -2865   1302  A    C  
ATOM   1661  N   MET A 219      54.931 -19.983   5.927  1.00106.98      A    N  
ANISOU 1661  N   MET A 219    15855  10886  13905   -456  -3257   2149  A    N  
ATOM   1662  CA  MET A 219      55.915 -19.549   6.912  1.00108.21      A    C  
ANISOU 1662  CA  MET A 219    16063  11157  13894   -399  -3374   2296  A    C  
ATOM   1663  C   MET A 219      56.867 -20.696   7.180  1.00115.04      A    C  
ANISOU 1663  C   MET A 219    17077  11841  14792   -194  -3572   2413  A    C  
ATOM   1664  O   MET A 219      58.090 -20.529   7.116  1.00118.04      A    O  
ANISOU 1664  O   MET A 219    17360  12348  15140     12  -3729   2426  A    O  
ATOM   1665  CB  MET A 219      55.265 -19.107   8.227  1.00107.61      A    C  
ANISOU 1665  CB  MET A 219    16155  11097  13633   -637  -3275   2440  A    C  
ATOM   1666  CG  MET A 219      55.297 -17.608   8.457  1.00110.49      A    C  
ANISOU 1666  CG  MET A 219    16367  11753  13861   -728  -3194   2392  A    C  
ATOM   1667  SD  MET A 219      55.424 -17.078  10.178  1.00105.79      A    S  
ANISOU 1667  SD  MET A 219    15958  11239  13000   -869  -3209   2582  A    S  
ATOM   1668  CE  MET A 219      57.193 -16.871  10.321  1.00127.06      A    C  
ANISOU 1668  CE  MET A 219    18551  14089  15636   -622  -3454   2608  A    C  
ATOM   1669  N   ALA A 220      56.300 -21.866   7.471  1.00109.48      A    N  
ANISOU 1669  N   ALA A 220    16603  10837  14156   -250  -3560   2499  A    N  
ATOM   1670  CA  ALA A 220      57.106 -23.029   7.827  1.00107.31      A    C  
ANISOU 1670  CA  ALA A 220    16513  10353  13909    -60  -3731   2636  A    C  
ATOM   1671  C   ALA A 220      57.936 -23.518   6.637  1.00111.89      A    C  
ANISOU 1671  C   ALA A 220    16945  10914  14653    218  -3858   2499  A    C  
ATOM   1672  O   ALA A 220      59.091 -23.914   6.788  1.00111.00      A    O  
ANISOU 1672  O   ALA A 220    16855  10803  14517    454  -4037   2577  A    O  
ATOM   1673  CB  ALA A 220      56.227 -24.132   8.369  1.00 99.06      A    C  
ANISOU 1673  CB  ALA A 220    15751   8971  12916   -201  -3658   2757  A    C  
ATOM   1674  N   GLU A 221      57.346 -23.468   5.450  1.00114.95      A    N  
ANISOU 1674  N   GLU A 221    17175  11305  15196    200  -3766   2292  A    N  
ATOM   1675  CA  GLU A 221      58.040 -23.862   4.230  1.00120.87      A    C  
ANISOU 1675  CA  GLU A 221    17768  12062  16096    462  -3868   2139  A    C  
ATOM   1676  C   GLU A 221      59.282 -22.991   4.005  1.00121.61      A    C  
ANISOU 1676  C   GLU A 221    17635  12460  16110    659  -3978   2118  A    C  
ATOM   1677  O   GLU A 221      60.090 -23.257   3.117  1.00123.46      A    O  
ANISOU 1677  O   GLU A 221    17732  12739  16438    910  -4083   2023  A    O  
ATOM   1678  CB  GLU A 221      57.075 -23.765   3.041  1.00122.83      A    C  
ANISOU 1678  CB  GLU A 221    17865  12317  16490    383  -3730   1910  A    C  
ATOM   1679  CG  GLU A 221      57.511 -24.474   1.769  1.00126.98      A    C  
ANISOU 1679  CG  GLU A 221    18285  12772  17190    630  -3817   1739  A    C  
ATOM   1680  CD  GLU A 221      56.323 -24.873   0.910  1.00128.58      A    C  
ANISOU 1680  CD  GLU A 221    18459  12854  17543    508  -3691   1549  A    C  
ATOM   1681  OE1 GLU A 221      55.289 -25.268   1.496  1.00125.54      A    O  
ANISOU 1681  OE1 GLU A 221    18252  12275  17173    262  -3587   1604  A    O  
ATOM   1682  OE2 GLU A 221      56.423 -24.797  -0.338  1.00127.90      A    O1-
ANISOU 1682  OE2 GLU A 221    18168  12875  17553    659  -3697   1344  A    O1-
ATOM   1683  N   MET A 222      59.430 -21.946   4.812  1.00118.50      A    N  
ANISOU 1683  N   MET A 222    17201  12279  15545    540  -3950   2202  A    N  
ATOM   1684  CA  MET A 222      60.560 -21.038   4.679  1.00115.02      A    C  
ANISOU 1684  CA  MET A 222    16541  12131  15032    685  -4040   2180  A    C  
ATOM   1685  C   MET A 222      61.765 -21.599   5.414  1.00126.13      A    C  
ANISOU 1685  C   MET A 222    18050  13511  16362    878  -4249   2338  A    C  
ATOM   1686  O   MET A 222      62.908 -21.242   5.130  1.00130.03      A    O  
ANISOU 1686  O   MET A 222    18363  14200  16841   1073  -4371   2313  A    O  
ATOM   1687  CB  MET A 222      60.204 -19.661   5.229  1.00102.60      A    C  
ANISOU 1687  CB  MET A 222    14880  10788  13315    469  -3919   2185  A    C  
ATOM   1688  CG  MET A 222      59.180 -18.907   4.401  1.00 91.78      A    C  
ANISOU 1688  CG  MET A 222    13356   9510  12009    325  -3716   2021  A    C  
ATOM   1689  SD  MET A 222      59.858 -18.285   2.851  1.00107.72      A    S  
ANISOU 1689  SD  MET A 222    15026  11757  14147    545  -3716   1827  A    S  
ATOM   1690  CE  MET A 222      61.352 -17.499   3.444  1.00118.75      A    C  
ANISOU 1690  CE  MET A 222    16302  13391  15425    656  -3859   1911  A    C  
ATOM   1691  N   TRP A 223      61.498 -22.485   6.364  1.00129.88      A    N  
ANISOU 1691  N   TRP A 223    18814  13750  16784    827  -4286   2507  A    N  
ATOM   1692  CA  TRP A 223      62.561 -23.157   7.097  1.00131.10      A    C  
ANISOU 1692  CA  TRP A 223    19098  13855  16858   1027  -4483   2675  A    C  
ATOM   1693  C   TRP A 223      62.694 -24.620   6.662  1.00128.06      A    C  
ANISOU 1693  C   TRP A 223    18872  13161  16626   1221  -4562   2698  A    C  
ATOM   1694  O   TRP A 223      63.798 -25.108   6.438  1.00126.00      A    O  
ANISOU 1694  O   TRP A 223    18571  12916  16388   1503  -4732   2722  A    O  
ATOM   1695  CB  TRP A 223      62.328 -23.044   8.607  1.00133.96      A    C  
ANISOU 1695  CB  TRP A 223    19680  14201  17017    866  -4480   2879  A    C  
ATOM   1696  CG  TRP A 223      62.697 -21.700   9.166  1.00139.46      A    C  
ANISOU 1696  CG  TRP A 223    20223  15226  17541    768  -4481   2871  A    C  
ATOM   1697  CD1 TRP A 223      63.945 -21.278   9.513  1.00141.93      A    C  
ANISOU 1697  CD1 TRP A 223    20412  15770  17745    926  -4649   2905  A    C  
ATOM   1698  CD2 TRP A 223      61.813 -20.601   9.441  1.00140.46      A    C  
ANISOU 1698  CD2 TRP A 223    20298  15484  17588    489  -4306   2816  A    C  
ATOM   1699  CE2 TRP A 223      62.600 -19.551   9.954  1.00136.64      A    C  
ANISOU 1699  CE2 TRP A 223    19671  15292  16954    489  -4377   2815  A    C  
ATOM   1700  CE3 TRP A 223      60.436 -20.405   9.301  1.00137.20      A    C  
ANISOU 1700  CE3 TRP A 223    19940  14972  17216    243  -4095   2763  A    C  
ATOM   1701  NE1 TRP A 223      63.896 -19.989   9.987  1.00140.82      A    N  
ANISOU 1701  NE1 TRP A 223    20152  15883  17471    751  -4590   2867  A    N  
ATOM   1702  CZ2 TRP A 223      62.057 -18.325  10.330  1.00129.46      A    C  
ANISOU 1702  CZ2 TRP A 223    18691  14558  15939    257  -4242   2763  A    C  
ATOM   1703  CZ3 TRP A 223      59.900 -19.187   9.678  1.00131.03      A    C  
ANISOU 1703  CZ3 TRP A 223    19083  14381  16320     25  -3961   2721  A    C  
ATOM   1704  CH2 TRP A 223      60.709 -18.163  10.186  1.00127.65      A    C  
ANISOU 1704  CH2 TRP A 223    18529  14223  15747     36  -4033   2721  A    C  
ATOM   1705  N   THR A 224      61.567 -25.309   6.519  1.00124.04      A    N  
ANISOU 1705  N   THR A 224    18533  12371  16226   1070  -4436   2682  A    N  
ATOM   1706  CA  THR A 224      61.584 -26.716   6.142  1.00119.67      A    C  
ANISOU 1706  CA  THR A 224    18154  11484  15830   1222  -4493   2695  A    C  
ATOM   1707  C   THR A 224      61.835 -26.912   4.649  1.00119.53      A    C  
ANISOU 1707  C   THR A 224    17932  11484  16000   1406  -4517   2465  A    C  
ATOM   1708  O   THR A 224      61.948 -28.041   4.171  1.00125.18      A    O  
ANISOU 1708  O   THR A 224    18761  11941  16862   1564  -4575   2436  A    O  
ATOM   1709  CB  THR A 224      60.276 -27.428   6.541  1.00112.42      A    C  
ANISOU 1709  CB  THR A 224    17494  10241  14978    976  -4344   2754  A    C  
ATOM   1710  CG2 THR A 224      59.901 -27.080   7.973  1.00102.19      A    C  
ANISOU 1710  CG2 THR A 224    16376   8969  13481    772  -4288   2969  A    C  
ATOM   1711  OG1 THR A 224      59.218 -27.043   5.652  1.00111.39      A    O  
ANISOU 1711  OG1 THR A 224    17223  10133  14968    790  -4180   2544  A    O  
ATOM   1712  N   ARG A 225      61.918 -25.809   3.918  1.00114.30      A    N  
ANISOU 1712  N   ARG A 225    16974  11125  15329   1391  -4467   2304  A    N  
ATOM   1713  CA  ARG A 225      62.170 -25.861   2.482  1.00116.45      A    C  
ANISOU 1713  CA  ARG A 225    17027  11466  15754   1575  -4480   2087  A    C  
ATOM   1714  C   ARG A 225      61.217 -26.811   1.746  1.00120.11      A    C  
ANISOU 1714  C   ARG A 225    17595  11637  16403   1525  -4400   1953  A    C  
ATOM   1715  O   ARG A 225      61.403 -27.089   0.558  1.00117.01      A    O  
ANISOU 1715  O   ARG A 225    17062  11254  16143   1701  -4425   1769  A    O  
ATOM   1716  CB  ARG A 225      63.618 -26.266   2.221  1.00116.08      A    C  
ANISOU 1716  CB  ARG A 225    16907  11483  15714   1928  -4679   2116  A    C  
ATOM   1717  CG  ARG A 225      64.623 -25.475   3.029  1.00113.40      A    C  
ANISOU 1717  CG  ARG A 225    16477  11414  15196   1982  -4781   2251  A    C  
ATOM   1718  CD  ARG A 225      64.577 -24.016   2.656  1.00108.73      A    C  
ANISOU 1718  CD  ARG A 225    15599  11163  14551   1864  -4683   2140  A    C  
ATOM   1719  NE  ARG A 225      65.145 -23.771   1.334  1.00114.16      A    N  
ANISOU 1719  NE  ARG A 225    16012  12019  15345   2076  -4701   1965  A    N  
ATOM   1720  CZ  ARG A 225      66.182 -22.963   1.100  1.00120.39      A    C  
ANISOU 1720  CZ  ARG A 225    16548  13109  16084   2210  -4766   1946  A    C  
ATOM   1721  NH1 ARG A 225      66.777 -22.316   2.104  1.00116.75      A    N1+
ANISOU 1721  NH1 ARG A 225    16071  12817  15472   2149  -4831   2075  A    N1+
ATOM   1722  NH2 ARG A 225      66.624 -22.798  -0.144  1.00120.79      A    N  
ANISOU 1722  NH2 ARG A 225    16357  13299  16237   2405  -4763   1793  A    N  
ATOM   1723  N   SER A 226      60.186 -27.282   2.445  1.00123.99      A    N  
ANISOU 1723  N   SER A 226    18326  11881  16904   1280  -4300   2038  A    N  
ATOM   1724  CA  SER A 226      59.289 -28.304   1.908  1.00126.65      A    C  
ANISOU 1724  CA  SER A 226    18794  11900  17426   1208  -4231   1928  A    C  
ATOM   1725  C   SER A 226      57.876 -28.205   2.489  1.00121.84      A    C  
ANISOU 1725  C   SER A 226    18315  11172  16808    844  -4048   1963  A    C  
ATOM   1726  O   SER A 226      57.703 -28.163   3.712  1.00117.32      A    O  
ANISOU 1726  O   SER A 226    17929  10536  16111    697  -4021   2178  A    O  
ATOM   1727  CB  SER A 226      59.867 -29.702   2.183  1.00129.20      A    C  
ANISOU 1727  CB  SER A 226    19372  11885  17834   1404  -4363   2041  A    C  
ATOM   1728  OG  SER A 226      58.998 -30.724   1.727  1.00129.42      A    O  
ANISOU 1728  OG  SER A 226    19546  11574  18054   1315  -4293   1934  A    O  
ATOM   1729  N   PRO A 227      56.860 -28.180   1.611  1.00120.49      A    N  
ANISOU 1729  N   PRO A 227    18038  10980  16762    706  -3923   1750  A    N  
ATOM   1730  CA  PRO A 227      55.458 -28.171   2.038  1.00120.54      A    C  
ANISOU 1730  CA  PRO A 227    18146  10870  16784    364  -3744   1757  A    C  
ATOM   1731  C   PRO A 227      55.248 -29.135   3.197  1.00124.52      A    C  
ANISOU 1731  C   PRO A 227    18993  11031  17289    255  -3743   1989  A    C  
ATOM   1732  O   PRO A 227      55.440 -30.342   3.061  1.00132.16      A    O  
ANISOU 1732  O   PRO A 227    20137  11679  18399    362  -3811   2001  A    O  
ATOM   1733  CB  PRO A 227      54.718 -28.642   0.790  1.00118.11      A    C  
ANISOU 1733  CB  PRO A 227    17734  10471  16673    344  -3686   1485  A    C  
ATOM   1734  CG  PRO A 227      55.558 -28.127  -0.333  1.00116.34      A    C  
ANISOU 1734  CG  PRO A 227    17236  10513  16453    621  -3775   1315  A    C  
ATOM   1735  CD  PRO A 227      56.987 -28.203   0.143  1.00119.18      A    C  
ANISOU 1735  CD  PRO A 227    17646  10910  16727    881  -3947   1485  A    C  
ATOM   1736  N   ILE A 228      54.849 -28.588   4.335  1.00121.14      A    N  
ANISOU 1736  N   ILE A 228    18661  10669  16696     47  -3657   2175  A    N  
ATOM   1737  CA  ILE A 228      54.918 -29.305   5.600  1.00120.65      A    C  
ANISOU 1737  CA  ILE A 228    18915  10356  16570     -7  -3673   2448  A    C  
ATOM   1738  C   ILE A 228      53.867 -30.387   5.807  1.00123.50      A    C  
ANISOU 1738  C   ILE A 228    19508  10329  17086   -214  -3556   2481  A    C  
ATOM   1739  O   ILE A 228      54.012 -31.225   6.688  1.00134.46      A    O  
ANISOU 1739  O   ILE A 228    21180  11446  18464   -209  -3578   2703  A    O  
ATOM   1740  CB  ILE A 228      54.850 -28.322   6.773  1.00121.03      A    C  
ANISOU 1740  CB  ILE A 228    18986  10627  16373   -153  -3620   2633  A    C  
ATOM   1741  CG1 ILE A 228      53.594 -27.452   6.651  1.00125.86      A    C  
ANISOU 1741  CG1 ILE A 228    19465  11395  16959   -452  -3419   2521  A    C  
ATOM   1742  CG2 ILE A 228      56.115 -27.465   6.808  1.00111.70      A    C  
ANISOU 1742  CG2 ILE A 228    17635   9766  15039     74  -3768   2651  A    C  
ATOM   1743  CD1 ILE A 228      52.858 -27.245   7.969  1.00127.25      A    C  
ANISOU 1743  CD1 ILE A 228    19828  11537  16982   -711  -3291   2732  A    C  
ATOM   1744  N   MET A 229      52.809 -30.371   5.009  1.00124.97      A    N  
ANISOU 1744  N   MET A 229    19575  10492  17415   -398  -3427   2263  A    N  
ATOM   1745  CA  MET A 229      51.744 -31.359   5.149  1.00132.38      A    C  
ANISOU 1745  CA  MET A 229    20706  11073  18521   -627  -3304   2267  A    C  
ATOM   1746  C   MET A 229      51.282 -31.875   3.789  1.00141.10      A    C  
ANISOU 1746  C   MET A 229    21674  12073  19863   -617  -3293   1958  A    C  
ATOM   1747  O   MET A 229      50.321 -31.354   3.203  1.00138.85      A    O  
ANISOU 1747  O   MET A 229    21199  11942  19618   -804  -3171   1763  A    O  
ATOM   1748  CB  MET A 229      50.553 -30.770   5.910  1.00126.91      A    C  
ANISOU 1748  CB  MET A 229    20033  10458  17728   -976  -3105   2351  A    C  
ATOM   1749  CG  MET A 229      50.848 -30.369   7.341  1.00122.74      A    C  
ANISOU 1749  CG  MET A 229    19673   9998  16964  -1017  -3097   2657  A    C  
ATOM   1750  SD  MET A 229      49.347 -29.856   8.201  1.00137.04      A    S  
ANISOU 1750  SD  MET A 229    21531  11856  18681  -1429  -2847   2749  A    S  
ATOM   1751  CE  MET A 229      48.817 -28.489   7.173  1.00176.39      A    C  
ANISOU 1751  CE  MET A 229    26126  17259  23637  -1496  -2771   2455  A    C  
ATOM   1752  N   GLN A 230      51.968 -32.899   3.290  1.00144.52      A    N  
ANISOU 1752  N   GLN A 230    22207  12256  20448   -388  -3423   1908  A    N  
ATOM   1753  CA  GLN A 230      51.627 -33.482   1.997  1.00143.67      A    C  
ANISOU 1753  CA  GLN A 230    21989  12034  20566   -349  -3433   1603  A    C  
ATOM   1754  C   GLN A 230      50.651 -34.646   2.164  1.00145.11      A    C  
ANISOU 1754  C   GLN A 230    22394  11785  20959   -587  -3326   1591  A    C  
ATOM   1755  O   GLN A 230      50.927 -35.606   2.882  1.00150.09      A    O  
ANISOU 1755  O   GLN A 230    23321  12060  21645   -560  -3349   1794  A    O  
ATOM   1756  CB  GLN A 230      52.891 -33.919   1.254  1.00143.93      A    C  
ANISOU 1756  CB  GLN A 230    21986  12047  20654     40  -3628   1521  A    C  
ATOM   1757  CG  GLN A 230      53.975 -32.845   1.209  1.00143.59      A    C  
ANISOU 1757  CG  GLN A 230    21742  12405  20409    278  -3737   1570  A    C  
ATOM   1758  CD  GLN A 230      55.194 -33.269   0.410  1.00147.66      A    C  
ANISOU 1758  CD  GLN A 230    22196  12923  20984    664  -3921   1477  A    C  
ATOM   1759  NE2 GLN A 230      56.268 -32.490   0.506  1.00144.94      A    N  
ANISOU 1759  NE2 GLN A 230    21712  12882  20475    882  -4027   1558  A    N  
ATOM   1760  OE1 GLN A 230      55.171 -34.285  -0.288  1.00151.45      A    O  
ANISOU 1760  OE1 GLN A 230    22750  13136  21658    763  -3964   1327  A    O  
ATOM   1761  N   GLY A 231      49.501 -34.544   1.510  1.00142.72      A    N  
ANISOU 1761  N   GLY A 231    21941  11517  20770   -821  -3202   1355  A    N  
ATOM   1762  CA  GLY A 231      48.468 -35.553   1.625  1.00145.74      A    C  
ANISOU 1762  CA  GLY A 231    22494  11519  21362  -1091  -3083   1315  A    C  
ATOM   1763  C   GLY A 231      48.036 -36.084   0.274  1.00152.92      A    C  
ANISOU 1763  C   GLY A 231    23255  12349  22497  -1082  -3103    945  A    C  
ATOM   1764  O   GLY A 231      48.057 -35.355  -0.717  1.00150.91      A    O  
ANISOU 1764  O   GLY A 231    22705  12433  22201   -977  -3140    705  A    O  
ATOM   1765  N   ASN A 232      47.650 -37.359   0.238  1.00162.87      A    N  
ANISOU 1765  N   ASN A 232    24728  13160  23997  -1187  -3076    900  A    N  
ATOM   1766  CA  ASN A 232      47.150 -37.994  -0.980  1.00163.10      A    C  
ANISOU 1766  CA  ASN A 232    24645  13067  24261  -1212  -3090    534  A    C  
ATOM   1767  C   ASN A 232      45.754 -37.486  -1.341  1.00160.73      A    C  
ANISOU 1767  C   ASN A 232    24119  12958  23991  -1545  -2934    328  A    C  
ATOM   1768  O   ASN A 232      45.503 -37.091  -2.484  1.00155.24      A    O  
ANISOU 1768  O   ASN A 232    23143  12522  23318  -1485  -2966     12  A    O  
ATOM   1769  CB  ASN A 232      47.143 -39.523  -0.838  1.00166.79      A    C  
ANISOU 1769  CB  ASN A 232    25423  12963  24985  -1245  -3097    552  A    C  
ATOM   1770  CG  ASN A 232      48.548 -40.117  -0.707  1.00168.32      A    C  
ANISOU 1770  CG  ASN A 232    25818  12968  25170   -865  -3267    702  A    C  
ATOM   1771  ND2 ASN A 232      48.621 -41.443  -0.585  1.00170.57      A    N  
ANISOU 1771  ND2 ASN A 232    26390  12744  25675   -858  -3274    730  A    N  
ATOM   1772  OD1 ASN A 232      49.550 -39.396  -0.713  1.00163.41      A    O  
ANISOU 1772  OD1 ASN A 232    25090  12650  24349   -582  -3386    791  A    O  
ATOM   1773  N   THR A 233      44.852 -37.488  -0.360  1.00162.47      A    N  
ANISOU 1773  N   THR A 233    24460  13068  24202  -1884  -2764    513  A    N  
ATOM   1774  CA  THR A 233      43.486 -37.006  -0.569  1.00160.23      A    C  
ANISOU 1774  CA  THR A 233    23971  12970  23938  -2215  -2603    350  A    C  
ATOM   1775  C   THR A 233      42.980 -36.156   0.600  1.00158.89      A    C  
ANISOU 1775  C   THR A 233    23825  12983  23562  -2433  -2453    631  A    C  
ATOM   1776  O   THR A 233      43.684 -35.969   1.594  1.00161.11      A    O  
ANISOU 1776  O   THR A 233    24291  13237  23687  -2335  -2477    950  A    O  
ATOM   1777  CB  THR A 233      42.519 -38.173  -0.754  1.00157.03      A    C  
ANISOU 1777  CB  THR A 233    23673  12165  23826  -2498  -2511    195  A    C  
ATOM   1778  CG2 THR A 233      42.913 -39.002  -1.972  1.00155.94      A    C  
ANISOU 1778  CG2 THR A 233    23498  11855  23897  -2299  -2654   -128  A    C  
ATOM   1779  OG1 THR A 233      42.553 -38.992   0.421  1.00156.14      A    O  
ANISOU 1779  OG1 THR A 233    23919  11627  23780  -2630  -2437    513  A    O  
ATOM   1780  N   GLU A 234      41.752 -35.656   0.477  1.00150.89      A    N  
ANISOU 1780  N   GLU A 234    22621  12163  22546  -2722  -2300    505  A    N  
ATOM   1781  CA  GLU A 234      41.140 -34.823   1.512  1.00142.04      A    C  
ANISOU 1781  CA  GLU A 234    21500  11236  21234  -2942  -2141    737  A    C  
ATOM   1782  C   GLU A 234      41.082 -35.510   2.879  1.00147.93      A    C  
ANISOU 1782  C   GLU A 234    22596  11617  21993  -3107  -2050   1089  A    C  
ATOM   1783  O   GLU A 234      41.084 -34.843   3.912  1.00145.58      A    O  
ANISOU 1783  O   GLU A 234    22370  11462  21483  -3166  -1974   1360  A    O  
ATOM   1784  CB  GLU A 234      39.739 -34.385   1.084  1.00137.76      A    C  
ANISOU 1784  CB  GLU A 234    20704  10911  20729  -3234  -1986    519  A    C  
ATOM   1785  CG  GLU A 234      39.724 -33.509  -0.155  1.00138.14      A    C  
ANISOU 1785  CG  GLU A 234    20393  11386  20707  -3067  -2052    211  A    C  
ATOM   1786  CD  GLU A 234      38.392 -33.536  -0.888  1.00144.97      A    C  
ANISOU 1786  CD  GLU A 234    21020  12367  21697  -3317  -1942    -91  A    C  
ATOM   1787  OE1 GLU A 234      37.653 -34.539  -0.760  1.00150.96      A    O  
ANISOU 1787  OE1 GLU A 234    21887  12795  22675  -3579  -1865   -148  A    O  
ATOM   1788  OE2 GLU A 234      38.092 -32.556  -1.607  1.00142.59      A    O1-
ANISOU 1788  OE2 GLU A 234    20416  12489  21274  -3247  -1932   -274  A    O1-
ATOM   1789  N   GLN A 235      41.031 -36.839   2.884  1.00157.44      A    N  
ANISOU 1789  N   GLN A 235    24025  12351  23446  -3175  -2052   1086  A    N  
ATOM   1790  CA  GLN A 235      40.986 -37.594   4.137  1.00160.30      A    C  
ANISOU 1790  CA  GLN A 235    24738  12330  23838  -3318  -1956   1429  A    C  
ATOM   1791  C   GLN A 235      42.371 -37.817   4.741  1.00152.59      A    C  
ANISOU 1791  C   GLN A 235    24006  11226  22743  -2993  -2102   1702  A    C  
ATOM   1792  O   GLN A 235      42.541 -37.721   5.959  1.00144.06      A    O  
ANISOU 1792  O   GLN A 235    23136  10094  21507  -3028  -2041   2048  A    O  
ATOM   1793  CB  GLN A 235      40.273 -38.932   3.943  1.00169.87      A    C  
ANISOU 1793  CB  GLN A 235    26099  13065  25379  -3555  -1869   1325  A    C  
ATOM   1794  CG  GLN A 235      38.773 -38.812   3.779  1.00175.95      A    C  
ANISOU 1794  CG  GLN A 235    26687  13910  26254  -3955  -1679   1156  A    C  
ATOM   1795  CD  GLN A 235      38.127 -40.134   3.417  1.00186.77      A    C  
ANISOU 1795  CD  GLN A 235    28170  14816  27977  -4182  -1613    993  A    C  
ATOM   1796  NE2 GLN A 235      36.798 -40.163   3.401  1.00188.99      A    N  
ANISOU 1796  NE2 GLN A 235    28319  15116  28371  -4563  -1434    874  A    N  
ATOM   1797  OE1 GLN A 235      38.816 -41.120   3.150  1.00191.31      A    O  
ANISOU 1797  OE1 GLN A 235    28944  15019  28726  -4018  -1720    970  A    O  
ATOM   1798  N   HIS A 236      43.353 -38.125   3.894  1.00154.04      A    N  
ANISOU 1798  N   HIS A 236    24161  11372  22994  -2671  -2295   1546  A    N  
ATOM   1799  CA  HIS A 236      44.731 -38.240   4.357  1.00159.30      A    C  
ANISOU 1799  CA  HIS A 236    25010  11983  23533  -2328  -2453   1777  A    C  
ATOM   1800  C   HIS A 236      45.186 -36.882   4.876  1.00168.63      A    C  
ANISOU 1800  C   HIS A 236    26056  13626  24390  -2221  -2483   1928  A    C  
ATOM   1801  O   HIS A 236      45.872 -36.792   5.898  1.00176.94      A    O  
ANISOU 1801  O   HIS A 236    27301  14661  25269  -2107  -2519   2240  A    O  
ATOM   1802  CB  HIS A 236      45.664 -38.726   3.239  1.00156.37      A    C  
ANISOU 1802  CB  HIS A 236    24585  11541  23289  -1995  -2651   1547  A    C  
ATOM   1803  CG  HIS A 236      47.088 -38.914   3.676  1.00162.42      A    C  
ANISOU 1803  CG  HIS A 236    25528  12246  23937  -1632  -2816   1775  A    C  
ATOM   1804  CD2 HIS A 236      47.628 -39.650   4.678  1.00169.90      A    C  
ANISOU 1804  CD2 HIS A 236    26813  12873  24868  -1552  -2828   2099  A    C  
ATOM   1805  ND1 HIS A 236      48.153 -38.295   3.050  1.00161.03      A    N  
ANISOU 1805  ND1 HIS A 236    25168  12379  23637  -1290  -2995   1678  A    N  
ATOM   1806  CE1 HIS A 236      49.279 -38.643   3.644  1.00162.48      A    C  
ANISOU 1806  CE1 HIS A 236    25556  12443  23735  -1021  -3115   1921  A    C  
ATOM   1807  NE2 HIS A 236      48.989 -39.464   4.638  1.00167.68      A    N  
ANISOU 1807  NE2 HIS A 236    26537  12724  24450  -1164  -3021   2181  A    N  
ATOM   1808  N   GLN A 237      44.796 -35.824   4.171  1.00162.24      A    N  
ANISOU 1808  N   GLN A 237    24917  13230  23498  -2256  -2467   1701  A    N  
ATOM   1809  CA  GLN A 237      45.174 -34.479   4.569  1.00155.11      A    C  
ANISOU 1809  CA  GLN A 237    23866  12762  22305  -2169  -2484   1809  A    C  
ATOM   1810  C   GLN A 237      44.632 -34.191   5.955  1.00153.37      A    C  
ANISOU 1810  C   GLN A 237    23810  12536  21927  -2404  -2331   2114  A    C  
ATOM   1811  O   GLN A 237      45.395 -33.986   6.894  1.00157.74      A    O  
ANISOU 1811  O   GLN A 237    24523  13118  22295  -2274  -2387   2389  A    O  
ATOM   1812  CB  GLN A 237      44.635 -33.441   3.585  1.00152.87      A    C  
ANISOU 1812  CB  GLN A 237    23215  12889  21982  -2208  -2451   1517  A    C  
ATOM   1813  CG  GLN A 237      45.173 -32.031   3.811  1.00147.07      A    C  
ANISOU 1813  CG  GLN A 237    22313  12596  20971  -2072  -2485   1593  A    C  
ATOM   1814  CD  GLN A 237      46.613 -31.891   3.364  1.00147.56      A    C  
ANISOU 1814  CD  GLN A 237    22331  12758  20976  -1690  -2693   1579  A    C  
ATOM   1815  NE2 GLN A 237      47.233 -30.770   3.704  1.00143.39      A    N  
ANISOU 1815  NE2 GLN A 237    21699  12563  20219  -1568  -2733   1681  A    N  
ATOM   1816  OE1 GLN A 237      47.161 -32.781   2.717  1.00153.80      A    O  
ANISOU 1816  OE1 GLN A 237    23177  13326  21932  -1508  -2812   1472  A    O  
ATOM   1817  N   LEU A 238      43.311 -34.195   6.082  1.00147.58      A    N  
ANISOU 1817  N   LEU A 238    23032  11776  21264  -2747  -2138   2062  A    N  
ATOM   1818  CA  LEU A 238      42.671 -33.760   7.317  1.00147.53      A    C  
ANISOU 1818  CA  LEU A 238    23133  11833  21090  -2982  -1972   2323  A    C  
ATOM   1819  C   LEU A 238      43.219 -34.479   8.556  1.00153.90      A    C  
ANISOU 1819  C   LEU A 238    24305  12334  21836  -2936  -1979   2692  A    C  
ATOM   1820  O   LEU A 238      43.246 -33.917   9.649  1.00157.23      A    O  
ANISOU 1820  O   LEU A 238    24822  12892  22024  -2980  -1919   2948  A    O  
ATOM   1821  CB  LEU A 238      41.151 -33.900   7.213  1.00145.22      A    C  
ANISOU 1821  CB  LEU A 238    22754  11496  20929  -3360  -1761   2206  A    C  
ATOM   1822  CG  LEU A 238      40.294 -33.433   8.393  1.00144.53      A    C  
ANISOU 1822  CG  LEU A 238    22741  11496  20680  -3635  -1558   2443  A    C  
ATOM   1823  CD1 LEU A 238      40.460 -31.960   8.696  1.00131.24      A    C  
ANISOU 1823  CD1 LEU A 238    20887  10281  18697  -3561  -1557   2485  A    C  
ATOM   1824  CD2 LEU A 238      38.841 -33.737   8.114  1.00153.65      A    C  
ANISOU 1824  CD2 LEU A 238    23789  12578  22013  -3992  -1365   2290  A    C  
ATOM   1825  N   ALA A 239      43.664 -35.717   8.387  1.00155.05      A    N  
ANISOU 1825  N   ALA A 239    24660  12070  22182  -2833  -2053   2718  A    N  
ATOM   1826  CA  ALA A 239      44.307 -36.423   9.486  1.00153.10      A    C  
ANISOU 1826  CA  ALA A 239    24763  11536  21873  -2731  -2078   3070  A    C  
ATOM   1827  C   ALA A 239      45.671 -35.796   9.756  1.00150.20      A    C  
ANISOU 1827  C   ALA A 239    24388  11418  21264  -2378  -2273   3191  A    C  
ATOM   1828  O   ALA A 239      45.992 -35.436  10.886  1.00146.90      A    O  
ANISOU 1828  O   ALA A 239    24111  11094  20611  -2346  -2262   3478  A    O  
ATOM   1829  CB  ALA A 239      44.451 -37.902   9.160  1.00149.79      A    C  
ANISOU 1829  CB  ALA A 239    24566  10605  21743  -2691  -2105   3053  A    C  
ATOM   1830  N   LEU A 240      46.458 -35.660   8.693  1.00150.97      A    N  
ANISOU 1830  N   LEU A 240    24308  11635  21419  -2116  -2450   2958  A    N  
ATOM   1831  CA  LEU A 240      47.812 -35.122   8.760  1.00150.43      A    C  
ANISOU 1831  CA  LEU A 240    24195  11801  21160  -1769  -2648   3028  A    C  
ATOM   1832  C   LEU A 240      47.842 -33.750   9.440  1.00146.50      A    C  
ANISOU 1832  C   LEU A 240    23568  11734  20362  -1810  -2620   3132  A    C  
ATOM   1833  O   LEU A 240      48.801 -33.406  10.135  1.00145.47      A    O  
ANISOU 1833  O   LEU A 240    23512  11736  20023  -1610  -2734   3327  A    O  
ATOM   1834  CB  LEU A 240      48.396 -35.045   7.346  1.00150.22      A    C  
ANISOU 1834  CB  LEU A 240    23931  11888  21257  -1537  -2801   2710  A    C  
ATOM   1835  CG  LEU A 240      49.890 -34.792   7.161  1.00152.00      A    C  
ANISOU 1835  CG  LEU A 240    24109  12278  21365  -1145  -3023   2740  A    C  
ATOM   1836  CD1 LEU A 240      50.704 -35.657   8.099  1.00155.21      A    C  
ANISOU 1836  CD1 LEU A 240    24842  12402  21728   -970  -3105   3047  A    C  
ATOM   1837  CD2 LEU A 240      50.263 -35.071   5.723  1.00152.44      A    C  
ANISOU 1837  CD2 LEU A 240    23982  12331  21606   -952  -3137   2425  A    C  
ATOM   1838  N   ILE A 241      46.785 -32.972   9.230  1.00144.30      A    N  
ANISOU 1838  N   ILE A 241    23091  11674  20061  -2067  -2469   2993  A    N  
ATOM   1839  CA  ILE A 241      46.622 -31.690   9.903  1.00139.45      A    C  
ANISOU 1839  CA  ILE A 241    22370  11437  19177  -2149  -2407   3083  A    C  
ATOM   1840  C   ILE A 241      46.430 -31.919  11.397  1.00138.97      A    C  
ANISOU 1840  C   ILE A 241    22594  11249  18958  -2270  -2313   3431  A    C  
ATOM   1841  O   ILE A 241      47.115 -31.316  12.219  1.00141.10      A    O  
ANISOU 1841  O   ILE A 241    22918  11714  18980  -2147  -2383   3614  A    O  
ATOM   1842  CB  ILE A 241      45.414 -30.896   9.337  1.00118.88      A    C  
ANISOU 1842  CB  ILE A 241    19505   9066  16599  -2402  -2244   2859  A    C  
ATOM   1843  CG1 ILE A 241      45.755 -30.285   7.977  1.00110.88      A    C  
ANISOU 1843  CG1 ILE A 241    18176   8308  15644  -2234  -2345   2544  A    C  
ATOM   1844  CG2 ILE A 241      44.984 -29.791  10.293  1.00119.31      A    C  
ANISOU 1844  CG2 ILE A 241    19532   9410  16390  -2551  -2125   3005  A    C  
ATOM   1845  CD1 ILE A 241      44.602 -29.530   7.350  1.00103.32      A    C  
ANISOU 1845  CD1 ILE A 241    16956   7591  14709  -2447  -2194   2320  A    C  
ATOM   1846  N   SER A 242      45.499 -32.803  11.740  1.00140.56      A    N  
ANISOU 1846  N   SER A 242    22975  11127  19305  -2511  -2153   3520  A    N  
ATOM   1847  CA  SER A 242      45.216 -33.121  13.135  1.00144.60      A    C  
ANISOU 1847  CA  SER A 242    23770  11490  19681  -2638  -2038   3862  A    C  
ATOM   1848  C   SER A 242      46.434 -33.755  13.809  1.00149.64      A    C  
ANISOU 1848  C   SER A 242    24669  11955  20230  -2352  -2196   4120  A    C  
ATOM   1849  O   SER A 242      46.566 -33.715  15.035  1.00150.03      A    O  
ANISOU 1849  O   SER A 242    24923  12010  20070  -2356  -2158   4419  A    O  
ATOM   1850  CB  SER A 242      44.001 -34.050  13.239  1.00143.40      A    C  
ANISOU 1850  CB  SER A 242    23750  10989  19747  -2952  -1830   3893  A    C  
ATOM   1851  OG  SER A 242      43.368 -33.921  14.500  1.00141.20      A    O  
ANISOU 1851  OG  SER A 242    23640  10710  19300  -3154  -1656   4172  A    O  
ATOM   1852  N   GLN A 243      47.323 -34.333  13.003  1.00151.91      A    N  
ANISOU 1852  N   GLN A 243    24946  12106  20667  -2092  -2373   4001  A    N  
ATOM   1853  CA  GLN A 243      48.566 -34.900  13.517  1.00157.60      A    C  
ANISOU 1853  CA  GLN A 243    25882  12696  21305  -1778  -2544   4218  A    C  
ATOM   1854  C   GLN A 243      49.622 -33.807  13.657  1.00157.26      A    C  
ANISOU 1854  C   GLN A 243    25675  13077  21001  -1538  -2719   4215  A    C  
ATOM   1855  O   GLN A 243      50.825 -34.074  13.667  1.00160.61      A    O  
ANISOU 1855  O   GLN A 243    26155  13493  21375  -1223  -2912   4283  A    O  
ATOM   1856  CB  GLN A 243      49.079 -36.024  12.612  1.00162.39      A    C  
ANISOU 1856  CB  GLN A 243    26554  12964  22184  -1590  -2656   4096  A    C  
ATOM   1857  CG  GLN A 243      49.953 -37.041  13.342  1.00165.89      A    C  
ANISOU 1857  CG  GLN A 243    27328  13101  22602  -1350  -2748   4390  A    C  
ATOM   1858  CD  GLN A 243      50.748 -37.923  12.402  1.00165.50      A    C  
ANISOU 1858  CD  GLN A 243    27303  12809  22770  -1078  -2905   4250  A    C  
ATOM   1859  NE2 GLN A 243      51.594 -38.777  12.968  1.00165.34      A    N  
ANISOU 1859  NE2 GLN A 243    27557  12541  22722   -827  -2999   4496  A    N  
ATOM   1860  OE1 GLN A 243      50.608 -37.836  11.181  1.00164.53      A    O  
ANISOU 1860  OE1 GLN A 243    26956  12729  22827  -1078  -2941   3926  A    O  
ATOM   1861  N   LEU A 244      49.155 -32.567  13.759  1.00151.10      A    N  
ANISOU 1861  N   LEU A 244    24686  12666  20061  -1690  -2647   4129  A    N  
ATOM   1862  CA  LEU A 244      50.034 -31.434  13.985  1.00134.15      A    C  
ANISOU 1862  CA  LEU A 244    22382  10923  17664  -1515  -2783   4125  A    C  
ATOM   1863  C   LEU A 244      49.373 -30.378  14.879  1.00132.68      A    C  
ANISOU 1863  C   LEU A 244    22162  11015  17236  -1731  -2646   4216  A    C  
ATOM   1864  O   LEU A 244      50.044 -29.745  15.695  1.00138.50      A    O  
ANISOU 1864  O   LEU A 244    22926  11982  17714  -1619  -2730   4356  A    O  
ATOM   1865  CB  LEU A 244      50.455 -30.816  12.661  1.00127.59      A    C  
ANISOU 1865  CB  LEU A 244    21229  10318  16931  -1384  -2890   3805  A    C  
ATOM   1866  CG  LEU A 244      51.304 -29.556  12.863  1.00133.36      A    C  
ANISOU 1866  CG  LEU A 244    21776  11472  17421  -1237  -3009   3786  A    C  
ATOM   1867  CD1 LEU A 244      52.731 -29.942  13.230  1.00138.56      A    C  
ANISOU 1867  CD1 LEU A 244    22544  12116  17989   -909  -3229   3935  A    C  
ATOM   1868  CD2 LEU A 244      51.276 -28.633  11.642  1.00123.87      A    C  
ANISOU 1868  CD2 LEU A 244    20226  10547  16291  -1221  -3021   3473  A    C  
ATOM   1869  N   CYS A 245      48.059 -30.207  14.746  1.00130.58      A    N  
ANISOU 1869  N   CYS A 245    21837  10730  17048  -2038  -2435   4132  A    N  
ATOM   1870  CA  CYS A 245      47.348 -29.130  15.450  1.00134.35      A    C  
ANISOU 1870  CA  CYS A 245    22248  11491  17309  -2244  -2291   4178  A    C  
ATOM   1871  C   CYS A 245      46.499 -29.564  16.653  1.00137.82      A    C  
ANISOU 1871  C   CYS A 245    22945  11764  17656  -2466  -2106   4450  A    C  
ATOM   1872  O   CYS A 245      46.066 -28.725  17.453  1.00135.55      A    O  
ANISOU 1872  O   CYS A 245    22651  11711  17143  -2596  -2004   4538  A    O  
ATOM   1873  CB  CYS A 245      46.466 -28.355  14.467  1.00132.22      A    C  
ANISOU 1873  CB  CYS A 245    21679  11416  17141  -2419  -2178   3882  A    C  
ATOM   1874  SG  CYS A 245      47.361 -27.677  13.063  1.00138.10      A    S  
ANISOU 1874  SG  CYS A 245    22101  12406  17966  -2171  -2361   3570  A    S  
ATOM   1875  N   GLY A 246      46.261 -30.865  16.776  1.00139.94      A    N  
ANISOU 1875  N   GLY A 246    23443  11626  18101  -2508  -2055   4583  A    N  
ATOM   1876  CA  GLY A 246      45.393 -31.383  17.816  1.00139.34      A    C  
ANISOU 1876  CA  GLY A 246    23610  11354  17978  -2731  -1856   4842  A    C  
ATOM   1877  C   GLY A 246      44.135 -31.934  17.187  1.00140.46      A    C  
ANISOU 1877  C   GLY A 246    23701  11270  18397  -3023  -1663   4704  A    C  
ATOM   1878  O   GLY A 246      43.920 -31.795  15.985  1.00133.42      A    O  
ANISOU 1878  O   GLY A 246    22573  10420  17700  -3047  -1690   4400  A    O  
ATOM   1879  N   SER A 247      43.298 -32.573  17.990  1.00149.45      A    N  
ANISOU 1879  N   SER A 247    25056  12174  19556  -3244  -1467   4926  A    N  
ATOM   1880  CA  SER A 247      42.071 -33.136  17.452  1.00156.01      A    C  
ANISOU 1880  CA  SER A 247    25835  12782  20658  -3546  -1276   4800  A    C  
ATOM   1881  C   SER A 247      41.000 -32.064  17.362  1.00149.12      A    C  
ANISOU 1881  C   SER A 247    24716  12243  19701  -3796  -1114   4651  A    C  
ATOM   1882  O   SER A 247      40.893 -31.195  18.231  1.00147.30      A    O  
ANISOU 1882  O   SER A 247    24492  12289  19187  -3823  -1057   4787  A    O  
ATOM   1883  CB  SER A 247      41.589 -34.334  18.281  1.00166.18      A    C  
ANISOU 1883  CB  SER A 247    27451  13650  22040  -3696  -1115   5095  A    C  
ATOM   1884  OG  SER A 247      41.348 -33.973  19.627  1.00170.37      A    O  
ANISOU 1884  OG  SER A 247    28144  14303  22288  -3766   -995   5399  A    O  
ATOM   1885  N   ILE A 248      40.224 -32.123  16.289  1.00144.23      A    N  
ANISOU 1885  N   ILE A 248    23876  11604  19321  -3962  -1047   4362  A    N  
ATOM   1886  CA  ILE A 248      39.137 -31.186  16.095  1.00143.51      A    C  
ANISOU 1886  CA  ILE A 248    23536  11815  19175  -4195   -887   4203  A    C  
ATOM   1887  C   ILE A 248      37.993 -31.530  17.046  1.00153.97      A    C  
ANISOU 1887  C   ILE A 248    25007  13013  20480  -4507   -627   4420  A    C  
ATOM   1888  O   ILE A 248      37.422 -32.619  16.971  1.00159.83      A    O  
ANISOU 1888  O   ILE A 248    25867  13396  21464  -4687   -518   4459  A    O  
ATOM   1889  CB  ILE A 248      38.662 -31.210  14.638  1.00139.54      A    C  
ANISOU 1889  CB  ILE A 248    22748  11337  18932  -4261   -902   3827  A    C  
ATOM   1890  CG1 ILE A 248      39.860 -31.017  13.697  1.00130.59      A    C  
ANISOU 1890  CG1 ILE A 248    21496  10289  17831  -3933  -1156   3637  A    C  
ATOM   1891  CG2 ILE A 248      37.600 -30.150  14.415  1.00138.62      A    C  
ANISOU 1891  CG2 ILE A 248    22360  11577  18734  -4462   -748   3663  A    C  
ATOM   1892  CD1 ILE A 248      39.524 -31.085  12.212  1.00121.48      A    C  
ANISOU 1892  CD1 ILE A 248    20072   9165  16920  -3949  -1194   3263  A    C  
ATOM   1893  N   THR A 249      37.681 -30.606  17.954  1.00153.11      A    N  
ANISOU 1893  N   THR A 249    24897  13195  20084  -4570   -525   4563  A    N  
ATOM   1894  CA  THR A 249      36.646 -30.821  18.967  1.00153.00      A    C  
ANISOU 1894  CA  THR A 249    25022  13109  20001  -4844   -273   4796  A    C  
ATOM   1895  C   THR A 249      35.936 -29.514  19.304  1.00154.71      A    C  
ANISOU 1895  C   THR A 249    25052  13751  19980  -4962   -145   4747  A    C  
ATOM   1896  O   THR A 249      36.536 -28.445  19.214  1.00146.03      A    O  
ANISOU 1896  O   THR A 249    23825  12978  18680  -4778   -268   4654  A    O  
ATOM   1897  CB  THR A 249      37.239 -31.383  20.274  1.00143.56      A    C  
ANISOU 1897  CB  THR A 249    24190  11725  18632  -4740   -276   5192  A    C  
ATOM   1898  CG2 THR A 249      37.885 -32.741  20.030  1.00136.95      A    C  
ANISOU 1898  CG2 THR A 249    23570  10435  18030  -4623   -378   5274  A    C  
ATOM   1899  OG1 THR A 249      38.217 -30.466  20.790  1.00139.01      A    O  
ANISOU 1899  OG1 THR A 249    23626  11451  17738  -4480   -437   5262  A    O  
ATOM   1900  N   PRO A 250      34.654 -29.594  19.702  1.00163.35      A    N  
ANISOU 1900  N   PRO A 250    26128  14839  21099  -5270    111   4810  A    N  
ATOM   1901  CA  PRO A 250      33.957 -28.376  20.128  1.00161.36      A    C  
ANISOU 1901  CA  PRO A 250    25722  14984  20602  -5372    248   4790  A    C  
ATOM   1902  C   PRO A 250      34.732 -27.667  21.244  1.00161.37      A    C  
ANISOU 1902  C   PRO A 250    25888  15186  20238  -5179    178   5015  A    C  
ATOM   1903  O   PRO A 250      34.635 -26.446  21.390  1.00155.09      A    O  
ANISOU 1903  O   PRO A 250    24946  14760  19219  -5143    192   4933  A    O  
ATOM   1904  CB  PRO A 250      32.612 -28.904  20.643  1.00162.76      A    C  
ANISOU 1904  CB  PRO A 250    25948  15031  20864  -5715    535   4921  A    C  
ATOM   1905  CG  PRO A 250      32.402 -30.186  19.905  1.00162.78      A    C  
ANISOU 1905  CG  PRO A 250    25977  14631  21242  -5834    537   4835  A    C  
ATOM   1906  CD  PRO A 250      33.777 -30.780  19.744  1.00164.87      A    C  
ANISOU 1906  CD  PRO A 250    26426  14665  21553  -5540    291   4891  A    C  
ATOM   1907  N   GLU A 251      35.501 -28.431  22.015  1.00168.61      A    N  
ANISOU 1907  N   GLU A 251    27109  15862  21095  -5048    101   5290  A    N  
ATOM   1908  CA  GLU A 251      36.313 -27.864  23.088  1.00169.07      A    C  
ANISOU 1908  CA  GLU A 251    27333  16102  20804  -4848     12   5503  A    C  
ATOM   1909  C   GLU A 251      37.332 -26.879  22.529  1.00160.66      A    C  
ANISOU 1909  C   GLU A 251    26095  15319  19630  -4588   -225   5290  A    C  
ATOM   1910  O   GLU A 251      37.406 -25.735  22.968  1.00153.08      A    O  
ANISOU 1910  O   GLU A 251    25059  14700  18406  -4541   -226   5268  A    O  
ATOM   1911  CB  GLU A 251      37.024 -28.967  23.880  1.00175.61      A    C  
ANISOU 1911  CB  GLU A 251    28509  16605  21611  -4722    -49   5823  A    C  
ATOM   1912  CG  GLU A 251      37.899 -28.440  25.011  1.00177.60      A    C  
ANISOU 1912  CG  GLU A 251    28935  17056  21490  -4500   -157   6043  A    C  
ATOM   1913  CD  GLU A 251      38.565 -29.545  25.812  1.00185.13      A    C  
ANISOU 1913  CD  GLU A 251    30232  17702  22406  -4359   -209   6376  A    C  
ATOM   1914  OE1 GLU A 251      38.331 -30.736  25.508  1.00186.76      A    O  
ANISOU 1914  OE1 GLU A 251    30560  17513  22889  -4442   -147   6447  A    O  
ATOM   1915  OE2 GLU A 251      39.323 -29.217  26.749  1.00187.90      A    O1-
ANISOU 1915  OE2 GLU A 251    30735  18208  22449  -4160   -311   6563  A    O1-
ATOM   1916  N   VAL A 252      38.114 -27.334  21.557  1.00161.03      A    N  
ANISOU 1916  N   VAL A 252    26080  15216  19888  -4423   -419   5132  A    N  
ATOM   1917  CA  VAL A 252      39.124 -26.496  20.920  1.00156.04      A    C  
ANISOU 1917  CA  VAL A 252    25273  14825  19191  -4176   -643   4927  A    C  
ATOM   1918  C   VAL A 252      38.486 -25.583  19.870  1.00150.17      A    C  
ANISOU 1918  C   VAL A 252    24188  14333  18535  -4270   -587   4599  A    C  
ATOM   1919  O   VAL A 252      38.936 -24.456  19.663  1.00149.93      A    O  
ANISOU 1919  O   VAL A 252    23997  14614  18356  -4143   -675   4462  A    O  
ATOM   1920  CB  VAL A 252      40.247 -27.359  20.276  1.00111.19      A    C  
ANISOU 1920  CB  VAL A 252    19658   8896  13695  -3940   -871   4892  A    C  
ATOM   1921  CG1 VAL A 252      41.384 -26.491  19.771  1.00 98.31      A    C  
ANISOU 1921  CG1 VAL A 252    17862   7525  11966  -3674  -1100   4723  A    C  
ATOM   1922  CG2 VAL A 252      40.778 -28.367  21.283  1.00118.24      A    C  
ANISOU 1922  CG2 VAL A 252    20897   9510  14520  -3848   -905   5229  A    C  
ATOM   1923  N   TRP A 253      37.420 -26.064  19.233  1.00146.09      A    N  
ANISOU 1923  N   TRP A 253    23565  13686  18257  -4495   -435   4479  A    N  
ATOM   1924  CA  TRP A 253      36.796 -25.369  18.104  1.00138.11      A    C  
ANISOU 1924  CA  TRP A 253    22226  12888  17362  -4568   -390   4158  A    C  
ATOM   1925  C   TRP A 253      35.264 -25.358  18.218  1.00140.44      A    C  
ANISOU 1925  C   TRP A 253    22434  13219  17710  -4887   -121   4140  A    C  
ATOM   1926  O   TRP A 253      34.591 -26.194  17.618  1.00142.95      A    O  
ANISOU 1926  O   TRP A 253    22700  13321  18291  -5053    -46   4047  A    O  
ATOM   1927  CB  TRP A 253      37.243 -26.033  16.790  1.00129.54      A    C  
ANISOU 1927  CB  TRP A 253    21026  11621  16571  -4460   -542   3932  A    C  
ATOM   1928  CG  TRP A 253      36.629 -25.478  15.524  1.00127.15      A    C  
ANISOU 1928  CG  TRP A 253    20389  11515  16408  -4514   -508   3596  A    C  
ATOM   1929  CD1 TRP A 253      35.641 -24.534  15.421  1.00127.45      A    C  
ANISOU 1929  CD1 TRP A 253    20221  11848  16358  -4663   -343   3482  A    C  
ATOM   1930  CD2 TRP A 253      36.971 -25.843  14.180  1.00121.25      A    C  
ANISOU 1930  CD2 TRP A 253    19476  10693  15900  -4399   -644   3335  A    C  
ATOM   1931  CE2 TRP A 253      36.148 -25.084  13.315  1.00118.12      A    C  
ANISOU 1931  CE2 TRP A 253    18774  10564  15543  -4485   -552   3073  A    C  
ATOM   1932  CE3 TRP A 253      37.895 -26.731  13.623  1.00116.63      A    C  
ANISOU 1932  CE3 TRP A 253    18974   9851  15491  -4217   -832   3295  A    C  
ATOM   1933  NE1 TRP A 253      35.347 -24.292  14.094  1.00119.48      A    N  
ANISOU 1933  NE1 TRP A 253    18927  10956  15515  -4644   -369   3171  A    N  
ATOM   1934  CZ2 TRP A 253      36.221 -25.197  11.929  1.00113.59      A    C  
ANISOU 1934  CZ2 TRP A 253    17977  10014  15170  -4397   -645   2779  A    C  
ATOM   1935  CZ3 TRP A 253      37.968 -26.838  12.243  1.00112.26      A    C  
ANISOU 1935  CZ3 TRP A 253    18198   9314  15141  -4134   -922   2996  A    C  
ATOM   1936  CH2 TRP A 253      37.136 -26.081  11.414  1.00112.33      A    C  
ANISOU 1936  CH2 TRP A 253    17906   9598  15177  -4224   -830   2742  A    C  
ATOM   1937  N   PRO A 254      34.709 -24.395  18.976  1.00139.20      A    N  
ANISOU 1937  N   PRO A 254    22250  13341  17300  -4974     22   4217  A    N  
ATOM   1938  CA  PRO A 254      33.266 -24.309  19.253  1.00140.10      A    C  
ANISOU 1938  CA  PRO A 254    22288  13525  17418  -5266    289   4234  A    C  
ATOM   1939  C   PRO A 254      32.381 -24.551  18.026  1.00147.80      A    C  
ANISOU 1939  C   PRO A 254    22998  14486  18674  -5422    360   3954  A    C  
ATOM   1940  O   PRO A 254      32.696 -24.085  16.940  1.00151.05      A    O  
ANISOU 1940  O   PRO A 254    23187  15038  19167  -5287    239   3690  A    O  
ATOM   1941  CB  PRO A 254      33.098 -22.868  19.746  1.00130.98      A    C  
ANISOU 1941  CB  PRO A 254    21038  12769  15959  -5227    355   4221  A    C  
ATOM   1942  CG  PRO A 254      34.395 -22.551  20.389  1.00127.69      A    C  
ANISOU 1942  CG  PRO A 254    20797  12389  15330  -4978    167   4356  A    C  
ATOM   1943  CD  PRO A 254      35.448 -23.267  19.574  1.00131.58      A    C  
ANISOU 1943  CD  PRO A 254    21305  12662  16028  -4789    -66   4269  A    C  
ATOM   1944  N   ASN A 255      31.283 -25.277  18.210  1.00158.99      A    N  
ANISOU 1944  N   ASN A 255    24432  15743  20233  -5702    558   4013  A    N  
ATOM   1945  CA  ASN A 255      30.327 -25.533  17.130  1.00164.98      A    C  
ANISOU 1945  CA  ASN A 255    24930  16505  21251  -5882    640   3746  A    C  
ATOM   1946  C   ASN A 255      30.902 -26.216  15.887  1.00159.04      A    C  
ANISOU 1946  C   ASN A 255    24092  15556  20778  -5766    450   3514  A    C  
ATOM   1947  O   ASN A 255      30.305 -26.146  14.811  1.00155.65      A    O  
ANISOU 1947  O   ASN A 255    23396  15225  20519  -5837    466   3230  A    O  
ATOM   1948  CB  ASN A 255      29.606 -24.241  16.720  1.00167.49      A    C  
ANISOU 1948  CB  ASN A 255    24947  17254  21437  -5904    736   3547  A    C  
ATOM   1949  CG  ASN A 255      28.216 -24.121  17.331  1.00174.20      A    C  
ANISOU 1949  CG  ASN A 255    25743  18214  22232  -6195   1015   3631  A    C  
ATOM   1950  ND2 ASN A 255      27.551 -22.999  17.063  1.00167.12      A    N  
ANISOU 1950  ND2 ASN A 255    24600  17694  21204  -6206   1113   3481  A    N  
ATOM   1951  OD1 ASN A 255      27.742 -25.026  18.031  1.00182.26      A    O  
ANISOU 1951  OD1 ASN A 255    26938  18984  23328  -6402   1148   3835  A    O  
ATOM   1952  N   VAL A 256      32.050 -26.874  16.029  1.00156.12      A    N  
ANISOU 1952  N   VAL A 256    23946  14925  20448  -5579    270   3631  A    N  
ATOM   1953  CA  VAL A 256      32.632 -27.613  14.915  1.00155.38      A    C  
ANISOU 1953  CA  VAL A 256    23801  14618  20618  -5459     91   3429  A    C  
ATOM   1954  C   VAL A 256      31.812 -28.862  14.643  1.00167.72      A    C  
ANISOU 1954  C   VAL A 256    25398  15842  22488  -5721    204   3391  A    C  
ATOM   1955  O   VAL A 256      31.908 -29.466  13.577  1.00166.06      A    O  
ANISOU 1955  O   VAL A 256    25083  15480  22532  -5696    105   3156  A    O  
ATOM   1956  CB  VAL A 256      34.086 -28.032  15.185  1.00149.80      A    C  
ANISOU 1956  CB  VAL A 256    23333  13715  19870  -5179   -127   3578  A    C  
ATOM   1957  CG1 VAL A 256      34.162 -28.926  16.409  1.00152.55      A    C  
ANISOU 1957  CG1 VAL A 256    24030  13747  20185  -5263    -49   3933  A    C  
ATOM   1958  CG2 VAL A 256      34.660 -28.744  13.970  1.00146.38      A    C  
ANISOU 1958  CG2 VAL A 256    22828  13085  19705  -5042   -306   3348  A    C  
ATOM   1959  N   ASP A 257      31.001 -29.245  15.621  1.00182.51      A    N  
ANISOU 1959  N   ASP A 257    27415  17594  24335  -5974    417   3622  A    N  
ATOM   1960  CA  ASP A 257      30.165 -30.426  15.492  1.00192.46      A    C  
ANISOU 1960  CA  ASP A 257    28720  18518  25889  -6260    555   3613  A    C  
ATOM   1961  C   ASP A 257      29.226 -30.319  14.289  1.00190.46      A    C  
ANISOU 1961  C   ASP A 257    28117  18408  25840  -6421    601   3243  A    C  
ATOM   1962  O   ASP A 257      29.082 -31.273  13.523  1.00192.31      A    O  
ANISOU 1962  O   ASP A 257    28321  18370  26378  -6509    562   3071  A    O  
ATOM   1963  CB  ASP A 257      29.360 -30.644  16.771  1.00203.60      A    C  
ANISOU 1963  CB  ASP A 257    30304  19852  27201  -6513    806   3926  A    C  
ATOM   1964  CG  ASP A 257      28.428 -31.834  16.671  1.00220.78      A    C  
ANISOU 1964  CG  ASP A 257    32515  21680  29692  -6840    974   3923  A    C  
ATOM   1965  OD1 ASP A 257      28.621 -32.658  15.752  1.00226.65      A    O  
ANISOU 1965  OD1 ASP A 257    33227  22161  30728  -6840    868   3722  A    O  
ATOM   1966  OD2 ASP A 257      27.504 -31.951  17.506  1.00227.25      A    O1-
ANISOU 1966  OD2 ASP A 257    33390  22486  30469  -7101   1216   4115  A    O1-
ATOM   1967  N   ASN A 258      28.609 -29.149  14.122  1.00185.53      A    N  
ANISOU 1967  N   ASN A 258    27231  18216  25044  -6445    679   3117  A    N  
ATOM   1968  CA  ASN A 258      27.544 -28.940  13.129  1.00180.44      A    C  
ANISOU 1968  CA  ASN A 258    26240  17772  24547  -6615    759   2794  A    C  
ATOM   1969  C   ASN A 258      27.887 -29.282  11.670  1.00171.65      A    C  
ANISOU 1969  C   ASN A 258    24941  16612  23666  -6491    572   2443  A    C  
ATOM   1970  O   ASN A 258      26.994 -29.369  10.824  1.00166.89      A    O  
ANISOU 1970  O   ASN A 258    24071  16113  23226  -6650    630   2169  A    O  
ATOM   1971  CB  ASN A 258      27.000 -27.505  13.210  1.00179.13      A    C  
ANISOU 1971  CB  ASN A 258    25843  18103  24116  -6588    854   2736  A    C  
ATOM   1972  CG  ASN A 258      26.407 -27.171  14.573  1.00181.00      A    C  
ANISOU 1972  CG  ASN A 258    26217  18417  24137  -6752   1072   3040  A    C  
ATOM   1973  ND2 ASN A 258      25.518 -26.184  14.600  1.00178.36      A    N  
ANISOU 1973  ND2 ASN A 258    25654  18464  23648  -6833   1220   2964  A    N  
ATOM   1974  OD1 ASN A 258      26.751 -27.783  15.587  1.00183.35      A    O  
ANISOU 1974  OD1 ASN A 258    26823  18444  24397  -6789   1108   3342  A    O  
ATOM   1975  N   TYR A 259      29.171 -29.460  11.374  1.00168.36      A    N  
ANISOU 1975  N   TYR A 259    24655  16061  23253  -6200    348   2444  A    N  
ATOM   1976  CA  TYR A 259      29.588 -29.847  10.030  1.00165.96      A    C  
ANISOU 1976  CA  TYR A 259    24203  15694  23160  -6058    165   2128  A    C  
ATOM   1977  C   TYR A 259      29.195 -31.296   9.794  1.00166.29      A    C  
ANISOU 1977  C   TYR A 259    24345  15300  23538  -6277    199   2069  A    C  
ATOM   1978  O   TYR A 259      29.562 -32.179  10.567  1.00166.62      A    O  
ANISOU 1978  O   TYR A 259    24700  14958  23649  -6323    218   2322  A    O  
ATOM   1979  CB  TYR A 259      31.105 -29.695   9.854  1.00167.69      A    C  
ANISOU 1979  CB  TYR A 259    24550  15875  23291  -5686    -75   2171  A    C  
ATOM   1980  CG  TYR A 259      31.634 -28.268   9.831  1.00163.32      A    C  
ANISOU 1980  CG  TYR A 259    23866  15743  22447  -5443   -143   2163  A    C  
ATOM   1981  CD1 TYR A 259      32.250 -27.753   8.698  1.00158.04      A    C  
ANISOU 1981  CD1 TYR A 259    22992  15275  21782  -5185   -313   1911  A    C  
ATOM   1982  CD2 TYR A 259      31.531 -27.447  10.947  1.00162.65      A    C  
ANISOU 1982  CD2 TYR A 259    23869  15844  22086  -5470    -32   2410  A    C  
ATOM   1983  CE1 TYR A 259      32.738 -26.464   8.674  1.00156.38      A    C  
ANISOU 1983  CE1 TYR A 259    22668  15423  21325  -4974   -361   1910  A    C  
ATOM   1984  CE2 TYR A 259      32.014 -26.156  10.933  1.00157.69      A    C  
ANISOU 1984  CE2 TYR A 259    23131  15575  21210  -5260    -89   2393  A    C  
ATOM   1985  CZ  TYR A 259      32.618 -25.667   9.795  1.00157.78      A    C  
ANISOU 1985  CZ  TYR A 259    22940  15764  21246  -5018   -249   2147  A    C  
ATOM   1986  OH  TYR A 259      33.108 -24.377   9.783  1.00154.33      A    O  
ANISOU 1986  OH  TYR A 259    22397  15665  20575  -4819   -293   2137  A    O  
ATOM   1987  N   GLU A 260      28.448 -31.544   8.726  1.00170.13      A    N  
ANISOU 1987  N   GLU A 260    24567  15840  24233  -6408    210   1733  A    N  
ATOM   1988  CA  GLU A 260      28.021 -32.903   8.425  1.00180.34      A    C  
ANISOU 1988  CA  GLU A 260    25932  16722  25868  -6636    243   1633  A    C  
ATOM   1989  C   GLU A 260      29.181 -33.894   8.500  1.00181.55      A    C  
ANISOU 1989  C   GLU A 260    26399  16431  26152  -6456     84   1748  A    C  
ATOM   1990  O   GLU A 260      29.022 -35.006   8.999  1.00190.02      A    O  
ANISOU 1990  O   GLU A 260    27709  17070  27421  -6642    166   1894  A    O  
ATOM   1991  CB  GLU A 260      27.363 -32.986   7.042  1.00186.21      A    C  
ANISOU 1991  CB  GLU A 260    26331  17615  26806  -6706    199   1193  A    C  
ATOM   1992  CG  GLU A 260      25.929 -32.471   6.974  1.00189.89      A    C  
ANISOU 1992  CG  GLU A 260    26502  18398  27250  -6990    397   1065  A    C  
ATOM   1993  CD  GLU A 260      25.172 -33.009   5.766  1.00192.36      A    C  
ANISOU 1993  CD  GLU A 260    26537  18718  27833  -7145    374    655  A    C  
ATOM   1994  OE1 GLU A 260      25.204 -34.241   5.540  1.00193.23      A    O  
ANISOU 1994  OE1 GLU A 260    26777  18404  28238  -7279    344    577  A    O  
ATOM   1995  OE2 GLU A 260      24.542 -32.201   5.049  1.00191.17      A    O1-
ANISOU 1995  OE2 GLU A 260    26041  18997  27596  -7130    387    407  A    O1-
ATOM   1996  N   LEU A 261      30.347 -33.484   8.012  1.00172.37      A    N  
ANISOU 1996  N   LEU A 261    25236  15376  24881  -6091   -135   1689  A    N  
ATOM   1997  CA  LEU A 261      31.455 -34.413   7.809  1.00169.23      A    C  
ANISOU 1997  CA  LEU A 261    25076  14597  24626  -5884   -313   1721  A    C  
ATOM   1998  C   LEU A 261      32.340 -34.615   9.036  1.00170.86      A    C  
ANISOU 1998  C   LEU A 261    25647  14589  24683  -5754   -328   2133  A    C  
ATOM   1999  O   LEU A 261      33.333 -35.338   8.974  1.00166.18      A    O  
ANISOU 1999  O   LEU A 261    25268  13695  24177  -5552   -476   2198  A    O  
ATOM   2000  CB  LEU A 261      32.307 -33.967   6.616  1.00163.90      A    C  
ANISOU 2000  CB  LEU A 261    24215  14134  23927  -5544   -545   1445  A    C  
ATOM   2001  CG  LEU A 261      31.620 -33.982   5.251  1.00160.81      A    C  
ANISOU 2001  CG  LEU A 261    23489  13902  23709  -5612   -573   1012  A    C  
ATOM   2002  CD1 LEU A 261      32.574 -33.521   4.162  1.00153.95      A    C  
ANISOU 2002  CD1 LEU A 261    22466  13244  22785  -5241   -798    787  A    C  
ATOM   2003  CD2 LEU A 261      31.084 -35.375   4.944  1.00163.63      A    C  
ANISOU 2003  CD2 LEU A 261    23930  13822  24419  -5855   -531    876  A    C  
ATOM   2004  N   TYR A 262      31.982 -33.984  10.149  1.00179.21      A    N  
ANISOU 2004  N   TYR A 262    26774  15811  25508  -5860   -178   2406  A    N  
ATOM   2005  CA  TYR A 262      32.816 -34.032  11.350  1.00189.30      A    C  
ANISOU 2005  CA  TYR A 262    28375  16957  26592  -5717   -198   2795  A    C  
ATOM   2006  C   TYR A 262      33.023 -35.465  11.853  1.00193.22      A    C  
ANISOU 2006  C   TYR A 262    29212  16901  27300  -5794   -165   2999  A    C  
ATOM   2007  O   TYR A 262      34.052 -36.087  11.579  1.00195.05      A    O  
ANISOU 2007  O   TYR A 262    29606  16886  27618  -5554   -342   3009  A    O  
ATOM   2008  CB  TYR A 262      32.238 -33.117  12.442  1.00196.08      A    C  
ANISOU 2008  CB  TYR A 262    29233  18101  27167  -5846    -21   3028  A    C  
ATOM   2009  CG  TYR A 262      32.800 -33.341  13.830  1.00204.58      A    C  
ANISOU 2009  CG  TYR A 262    30661  19009  28062  -5782     14   3448  A    C  
ATOM   2010  CD1 TYR A 262      34.170 -33.321  14.067  1.00206.39      A    C  
ANISOU 2010  CD1 TYR A 262    31069  19189  28160  -5446   -189   3585  A    C  
ATOM   2011  CD2 TYR A 262      31.954 -33.553  14.910  1.00209.42      A    C  
ANISOU 2011  CD2 TYR A 262    31415  19534  28621  -6051    251   3710  A    C  
ATOM   2012  CE1 TYR A 262      34.679 -33.525  15.340  1.00209.93      A    C  
ANISOU 2012  CE1 TYR A 262    31832  19508  28425  -5374   -165   3965  A    C  
ATOM   2013  CE2 TYR A 262      32.453 -33.756  16.182  1.00213.04      A    C  
ANISOU 2013  CE2 TYR A 262    32195  19856  28895  -5979    286   4099  A    C  
ATOM   2014  CZ  TYR A 262      33.813 -33.742  16.394  1.00213.15      A    C  
ANISOU 2014  CZ  TYR A 262    32385  19829  28776  -5637     73   4223  A    C  
ATOM   2015  OH  TYR A 262      34.304 -33.946  17.665  1.00215.46      A    O  
ANISOU 2015  OH  TYR A 262    32989  20007  28868  -5552    101   4606  A    O  
ATOM   2016  N   GLU A 263      32.039 -35.979  12.583  1.00193.80      A    N  
ANISOU 2016  N   GLU A 263    29393  16784  27457  -6126     69   3167  A    N  
ATOM   2017  CA  GLU A 263      32.060 -37.354  13.068  1.00197.07      A    C  
ANISOU 2017  CA  GLU A 263    30128  16654  28096  -6246    145   3367  A    C  
ATOM   2018  C   GLU A 263      31.772 -38.294  11.909  1.00196.02      A    C  
ANISOU 2018  C   GLU A 263    29900  16234  28343  -6354     99   3035  A    C  
ATOM   2019  O   GLU A 263      32.002 -39.499  11.987  1.00194.26      A    O  
ANISOU 2019  O   GLU A 263    29928  15524  28357  -6389    105   3118  A    O  
ATOM   2020  CB  GLU A 263      30.995 -37.533  14.150  1.00199.87      A    C  
ANISOU 2020  CB  GLU A 263    30588  16928  28425  -6591    433   3632  A    C  
ATOM   2021  CG  GLU A 263      30.866 -38.943  14.688  1.00205.61      A    C  
ANISOU 2021  CG  GLU A 263    31642  17084  29398  -6759    557   3856  A    C  
ATOM   2022  CD  GLU A 263      31.865 -39.245  15.785  1.00206.76      A    C  
ANISOU 2022  CD  GLU A 263    32171  17030  29360  -6523    515   4274  A    C  
ATOM   2023  OE1 GLU A 263      32.750 -38.394  16.036  1.00199.95      A    O  
ANISOU 2023  OE1 GLU A 263    31308  16470  28195  -6216    357   4352  A    O  
ATOM   2024  OE2 GLU A 263      31.756 -40.336  16.397  1.00210.27      A    O1-
ANISOU 2024  OE2 GLU A 263    32913  17016  29962  -6647    643   4522  A    O1-
ATOM   2025  N   LYS A 264      31.267 -37.715  10.827  1.00195.96      A    N  
ANISOU 2025  N   LYS A 264    29528  16540  28386  -6398     54   2655  A    N  
ATOM   2026  CA  LYS A 264      30.849 -38.462   9.653  1.00199.09      A    C  
ANISOU 2026  CA  LYS A 264    29774  16751  29121  -6520     14   2285  A    C  
ATOM   2027  C   LYS A 264      32.008 -38.645   8.671  1.00196.62      A    C  
ANISOU 2027  C   LYS A 264    29454  16386  28868  -6158   -260   2075  A    C  
ATOM   2028  O   LYS A 264      31.796 -38.750   7.462  1.00192.19      A    O  
ANISOU 2028  O   LYS A 264    28656  15892  28477  -6155   -350   1690  A    O  
ATOM   2029  CB  LYS A 264      29.698 -37.716   8.977  1.00199.98      A    C  
ANISOU 2029  CB  LYS A 264    29481  17268  29233  -6732    102   1977  A    C  
ATOM   2030  CG  LYS A 264      28.782 -38.568   8.126  1.00208.48      A    C  
ANISOU 2030  CG  LYS A 264    30405  18141  30666  -7021    162   1652  A    C  
ATOM   2031  CD  LYS A 264      27.596 -37.752   7.627  1.00209.43      A    C  
ANISOU 2031  CD  LYS A 264    30124  18710  30741  -7229    266   1395  A    C  
ATOM   2032  CE  LYS A 264      26.559 -38.641   6.952  1.00213.98      A    C  
ANISOU 2032  CE  LYS A 264    30550  19081  31671  -7574    355   1096  A    C  
ATOM   2033  NZ  LYS A 264      25.401 -37.852   6.449  1.00212.81      A    N1+
ANISOU 2033  NZ  LYS A 264    29994  19396  31469  -7762    450    839  A    N1+
ATOM   2034  N   LEU A 265      33.232 -38.677   9.196  1.00198.59      A    N  
ANISOU 2034  N   LEU A 265    29955  16534  28966  -5847   -391   2327  A    N  
ATOM   2035  CA  LEU A 265      34.429 -38.797   8.363  1.00199.30      A    C  
ANISOU 2035  CA  LEU A 265    30047  16597  29081  -5474   -650   2168  A    C  
ATOM   2036  C   LEU A 265      35.556 -39.487   9.124  1.00199.91      A    C  
ANISOU 2036  C   LEU A 265    30509  16323  29125  -5243   -733   2496  A    C  
ATOM   2037  O   LEU A 265      36.726 -39.398   8.746  1.00196.05      A    O  
ANISOU 2037  O   LEU A 265    30052  15872  28564  -4885   -947   2466  A    O  
ATOM   2038  CB  LEU A 265      34.887 -37.416   7.866  1.00196.85      A    C  
ANISOU 2038  CB  LEU A 265    29457  16837  28500  -5222   -785   2030  A    C  
ATOM   2039  CG  LEU A 265      36.134 -37.293   6.980  1.00191.74      A    C  
ANISOU 2039  CG  LEU A 265    28755  16267  27830  -4819  -1047   1863  A    C  
ATOM   2040  CD1 LEU A 265      36.169 -38.394   5.929  1.00197.81      A    C  
ANISOU 2040  CD1 LEU A 265    29523  16705  28930  -4810  -1134   1573  A    C  
ATOM   2041  CD2 LEU A 265      36.209 -35.917   6.329  1.00178.04      A    C  
ANISOU 2041  CD2 LEU A 265    26679  15086  25881  -4667  -1122   1667  A    C  
ATOM   2042  N   GLU A 266      35.194 -40.180  10.198  1.00204.54      A    N  
ANISOU 2042  N   GLU A 266    31382  16574  29760  -5443   -558   2816  A    N  
ATOM   2043  CA  GLU A 266      36.170 -40.923  10.986  1.00207.65      A    C  
ANISOU 2043  CA  GLU A 266    32161  16609  30128  -5235   -614   3152  A    C  
ATOM   2044  C   GLU A 266      37.413 -40.063  11.200  1.00204.50      A    C  
ANISOU 2044  C   GLU A 266    31762  16530  29409  -4835   -816   3270  A    C  
ATOM   2045  O   GLU A 266      38.492 -40.362  10.689  1.00204.60      A    O  
ANISOU 2045  O   GLU A 266    31834  16450  29456  -4516  -1022   3201  A    O  
ATOM   2046  CB  GLU A 266      36.530 -42.247  10.294  1.00207.35      A    C  
ANISOU 2046  CB  GLU A 266    32283  16069  30432  -5174   -695   3010  A    C  
ATOM   2047  CG  GLU A 266      36.442 -43.485  11.188  1.00208.93      A    C  
ANISOU 2047  CG  GLU A 266    32883  15704  30798  -5303   -547   3332  A    C  
ATOM   2048  CD  GLU A 266      36.628 -44.784  10.413  1.00213.14      A    C  
ANISOU 2048  CD  GLU A 266    33551  15727  31706  -5288   -603   3142  A    C  
ATOM   2049  OE1 GLU A 266      36.897 -44.712   9.196  1.00213.73      A    O  
ANISOU 2049  OE1 GLU A 266    33411  15907  31889  -5152   -774   2761  A    O  
ATOM   2050  OE2 GLU A 266      36.505 -45.875  11.015  1.00214.16      A    O1-
ANISOU 2050  OE2 GLU A 266    34005  15346  32020  -5407   -472   3371  A    O1-
ATOM   2051  N   LEU A 267      37.243 -38.975  11.938  1.00200.67      A    N  
ANISOU 2051  N   LEU A 267    31197  16434  28616  -4860   -752   3432  A    N  
ATOM   2052  CA  LEU A 267      38.357 -38.116  12.302  1.00198.93      A    C  
ANISOU 2052  CA  LEU A 267    30985  16521  28080  -4521   -921   3567  A    C  
ATOM   2053  C   LEU A 267      39.050 -38.700  13.532  1.00203.63      A    C  
ANISOU 2053  C   LEU A 267    31965  16849  28556  -4390   -917   3993  A    C  
ATOM   2054  O   LEU A 267      38.385 -39.101  14.487  1.00210.04      A    O  
ANISOU 2054  O   LEU A 267    32971  17471  29362  -4619   -715   4256  A    O  
ATOM   2055  CB  LEU A 267      37.847 -36.702  12.581  1.00196.30      A    C  
ANISOU 2055  CB  LEU A 267    30409  16702  27474  -4611   -847   3548  A    C  
ATOM   2056  CG  LEU A 267      38.853 -35.587  12.857  1.00195.20      A    C  
ANISOU 2056  CG  LEU A 267    30207  16954  27007  -4307  -1007   3624  A    C  
ATOM   2057  CD1 LEU A 267      38.177 -34.251  12.679  1.00192.26      A    C  
ANISOU 2057  CD1 LEU A 267    29527  17061  26463  -4423   -931   3472  A    C  
ATOM   2058  CD2 LEU A 267      39.450 -35.692  14.252  1.00199.28      A    C  
ANISOU 2058  CD2 LEU A 267    31034  17388  27293  -4201   -999   4039  A    C  
ATOM   2059  N   VAL A 268      40.379 -38.755  13.509  1.00199.93      A    N  
ANISOU 2059  N   VAL A 268    31601  16376  27987  -4015  -1135   4065  A    N  
ATOM   2060  CA  VAL A 268      41.135 -39.370  14.602  1.00198.20      A    C  
ANISOU 2060  CA  VAL A 268    31747  15907  27654  -3842  -1157   4458  A    C  
ATOM   2061  C   VAL A 268      40.882 -38.674  15.944  1.00189.33      A    C  
ANISOU 2061  C   VAL A 268    30715  15015  26207  -3926  -1033   4780  A    C  
ATOM   2062  O   VAL A 268      41.180 -37.488  16.107  1.00182.35      A    O  
ANISOU 2062  O   VAL A 268    29657  14579  25049  -3822  -1109   4753  A    O  
ATOM   2063  CB  VAL A 268      42.647 -39.404  14.304  1.00197.27      A    C  
ANISOU 2063  CB  VAL A 268    31675  15825  27453  -3402  -1431   4456  A    C  
ATOM   2064  CG1 VAL A 268      43.384 -40.156  15.403  1.00200.14      A    C  
ANISOU 2064  CG1 VAL A 268    32423  15907  27716  -3217  -1449   4861  A    C  
ATOM   2065  CG2 VAL A 268      42.904 -40.053  12.953  1.00195.78      A    C  
ANISOU 2065  CG2 VAL A 268    31387  15431  27569  -3302  -1553   4126  A    C  
ATOM   2066  N   LYS A 269      40.349 -39.433  16.900  1.00183.55      A    N  
ANISOU 2066  N   LYS A 269    30263  13966  25510  -4108   -839   5085  A    N  
ATOM   2067  CA  LYS A 269      39.882 -38.890  18.178  1.00175.44      A    C  
ANISOU 2067  CA  LYS A 269    29332  13124  24202  -4241   -676   5387  A    C  
ATOM   2068  C   LYS A 269      40.988 -38.402  19.121  1.00173.80      A    C  
ANISOU 2068  C   LYS A 269    29273  13130  23634  -3920   -819   5662  A    C  
ATOM   2069  O   LYS A 269      40.836 -37.363  19.770  1.00169.49      A    O  
ANISOU 2069  O   LYS A 269    28638  12969  22791  -3948   -784   5740  A    O  
ATOM   2070  CB  LYS A 269      39.043 -39.935  18.922  1.00175.47      A    C  
ANISOU 2070  CB  LYS A 269    29611  12701  24359  -4512   -420   5655  A    C  
ATOM   2071  CG  LYS A 269      37.920 -40.572  18.123  1.00166.50      A    C  
ANISOU 2071  CG  LYS A 269    28363  11299  23599  -4859   -259   5415  A    C  
ATOM   2072  CD  LYS A 269      37.246 -41.643  18.953  1.00159.83      A    C  
ANISOU 2072  CD  LYS A 269    27824  10005  22900  -5101     -9   5723  A    C  
ATOM   2073  CE  LYS A 269      36.145 -42.354  18.187  1.00157.75      A    C  
ANISOU 2073  CE  LYS A 269    27457   9446  23034  -5465    153   5482  A    C  
ATOM   2074  NZ  LYS A 269      35.672 -43.571  18.930  1.00162.83      A    N1+
ANISOU 2074  NZ  LYS A 269    28438   9565  23867  -5667    382   5791  A    N1+
ATOM   2075  N   GLY A 270      42.082 -39.161  19.212  1.00175.47      A    N  
ANISOU 2075  N   GLY A 270    29709  13091  23868  -3616   -979   5803  A    N  
ATOM   2076  CA  GLY A 270      43.120 -38.904  20.202  1.00178.05      A    C  
ANISOU 2076  CA  GLY A 270    30215  13569  23866  -3313  -1106   6098  A    C  
ATOM   2077  C   GLY A 270      44.379 -38.232  19.681  1.00180.22      A    C  
ANISOU 2077  C   GLY A 270    30322  14152  24003  -2958  -1399   5933  A    C  
ATOM   2078  O   GLY A 270      45.272 -38.899  19.154  1.00177.63      A    O  
ANISOU 2078  O   GLY A 270    30067  13618  23808  -2699  -1569   5888  A    O  
ATOM   2079  N   GLN A 271      44.453 -36.910  19.853  1.00181.58      A    N  
ANISOU 2079  N   GLN A 271    30271  14812  23907  -2946  -1451   5849  A    N  
ATOM   2080  CA  GLN A 271      45.544 -36.090  19.317  1.00180.41      A    C  
ANISOU 2080  CA  GLN A 271    29912  15007  23630  -2656  -1706   5663  A    C  
ATOM   2081  C   GLN A 271      45.682 -34.749  20.058  1.00176.61      A    C  
ANISOU 2081  C   GLN A 271    29313  15011  22782  -2639  -1729   5718  A    C  
ATOM   2082  O   GLN A 271      44.728 -33.971  20.126  1.00173.38      A    O  
ANISOU 2082  O   GLN A 271    28747  14817  22311  -2896  -1574   5628  A    O  
ATOM   2083  CB  GLN A 271      45.317 -35.822  17.825  1.00178.51      A    C  
ANISOU 2083  CB  GLN A 271    29356  14835  23634  -2711  -1759   5245  A    C  
ATOM   2084  CG  GLN A 271      45.611 -36.999  16.907  1.00180.81      A    C  
ANISOU 2084  CG  GLN A 271    29720  14723  24258  -2610  -1832   5122  A    C  
ATOM   2085  CD  GLN A 271      47.098 -37.229  16.713  1.00181.60      A    C  
ANISOU 2085  CD  GLN A 271    29874  14822  24302  -2196  -2093   5151  A    C  
ATOM   2086  NE2 GLN A 271      47.440 -38.238  15.920  1.00183.73      A    N  
ANISOU 2086  NE2 GLN A 271    30215  14751  24846  -2072  -2169   5042  A    N  
ATOM   2087  OE1 GLN A 271      47.930 -36.507  17.266  1.00178.84      A    O  
ANISOU 2087  OE1 GLN A 271    29498  14784  23669  -1989  -2227   5259  A    O  
ATOM   2088  N   LYS A 272      46.870 -34.477  20.598  1.00173.07      A    N  
ANISOU 2088  N   LYS A 272    28932  14736  22090  -2332  -1925   5855  A    N  
ATOM   2089  CA  LYS A 272      47.121 -33.226  21.322  1.00165.44      A    C  
ANISOU 2089  CA  LYS A 272    27865  14222  20775  -2295  -1970   5897  A    C  
ATOM   2090  C   LYS A 272      48.119 -32.329  20.579  1.00164.75      A    C  
ANISOU 2090  C   LYS A 272    27501  14469  20628  -2070  -2204   5643  A    C  
ATOM   2091  O   LYS A 272      49.058 -32.825  19.956  1.00166.94      A    O  
ANISOU 2091  O   LYS A 272    27768  14635  21026  -1818  -2388   5574  A    O  
ATOM   2092  CB  LYS A 272      47.579 -33.514  22.759  1.00161.23      A    C  
ANISOU 2092  CB  LYS A 272    27631  13672  19956  -2160  -1982   6282  A    C  
ATOM   2093  CG  LYS A 272      46.435 -33.914  23.695  1.00157.17      A    C  
ANISOU 2093  CG  LYS A 272    27335  12984  19398  -2431  -1709   6537  A    C  
ATOM   2094  CD  LYS A 272      46.852 -34.939  24.745  1.00148.31      A    C  
ANISOU 2094  CD  LYS A 272    26589  11590  18172  -2273  -1699   6935  A    C  
ATOM   2095  CE  LYS A 272      45.669 -35.308  25.629  1.00151.01      A    C  
ANISOU 2095  CE  LYS A 272    27133  11765  18481  -2558  -1406   7187  A    C  
ATOM   2096  NZ  LYS A 272      45.888 -36.578  26.405  1.00161.68      A    N1+
ANISOU 2096  NZ  LYS A 272    28866  12723  19840  -2443  -1347   7565  A    N1+
ATOM   2097  N   ARG A 273      47.906 -31.014  20.658  1.00162.24      A    N  
ANISOU 2097  N   ARG A 273    26965  14552  20127  -2161  -2186   5511  A    N  
ATOM   2098  CA  ARG A 273      48.601 -30.029  19.812  1.00164.23      A    C  
ANISOU 2098  CA  ARG A 273    26911  15126  20362  -2020  -2353   5230  A    C  
ATOM   2099  C   ARG A 273      50.132 -30.084  19.812  1.00167.05      A    C  
ANISOU 2099  C   ARG A 273    27272  15572  20625  -1659  -2625   5263  A    C  
ATOM   2100  O   ARG A 273      50.777 -29.636  20.762  1.00167.45      A    O  
ANISOU 2100  O   ARG A 273    27395  15835  20393  -1532  -2719   5422  A    O  
ATOM   2101  CB  ARG A 273      48.152 -28.605  20.158  1.00161.15      A    C  
ANISOU 2101  CB  ARG A 273    26341  15138  19750  -2170  -2274   5141  A    C  
ATOM   2102  CG  ARG A 273      48.840 -27.541  19.323  1.00156.08      A    C  
ANISOU 2102  CG  ARG A 273    25391  14821  19093  -2039  -2424   4867  A    C  
ATOM   2103  CD  ARG A 273      48.249 -26.173  19.569  1.00155.46      A    C  
ANISOU 2103  CD  ARG A 273    25140  15091  18836  -2212  -2313   4763  A    C  
ATOM   2104  NE  ARG A 273      48.601 -25.246  18.499  1.00154.38      A    N  
ANISOU 2104  NE  ARG A 273    24689  15198  18770  -2145  -2393   4467  A    N  
ATOM   2105  CZ  ARG A 273      47.867 -25.044  17.408  1.00155.29      A    C  
ANISOU 2105  CZ  ARG A 273    24600  15313  19092  -2273  -2291   4230  A    C  
ATOM   2106  NH1 ARG A 273      46.727 -25.696  17.233  1.00155.48      A    N1+
ANISOU 2106  NH1 ARG A 273    24685  15112  19277  -2490  -2111   4235  A    N1+
ATOM   2107  NH2 ARG A 273      48.271 -24.182  16.487  1.00156.86      A    N  
ANISOU 2107  NH2 ARG A 273    24523  15744  19331  -2183  -2367   3987  A    N  
ATOM   2108  N   LYS A 274      50.702 -30.586  18.718  1.00166.02      A    N  
ANISOU 2108  N   LYS A 274    27046  15306  20729  -1493  -2753   5094  A    N  
ATOM   2109  CA  LYS A 274      52.146 -30.795  18.609  1.00162.70      A    C  
ANISOU 2109  CA  LYS A 274    26626  14935  20259  -1138  -3007   5121  A    C  
ATOM   2110  C   LYS A 274      52.783 -29.956  17.499  1.00156.15      A    C  
ANISOU 2110  C   LYS A 274    25457  14381  19490  -1015  -3147   4815  A    C  
ATOM   2111  O   LYS A 274      53.499 -30.485  16.648  1.00156.46      A    O  
ANISOU 2111  O   LYS A 274    25438  14310  19701   -803  -3285   4707  A    O  
ATOM   2112  CB  LYS A 274      52.445 -32.285  18.389  1.00163.21      A    C  
ANISOU 2112  CB  LYS A 274    26918  14564  20531   -987  -3050   5238  A    C  
ATOM   2113  CG  LYS A 274      51.999 -33.179  19.548  1.00164.34      A    C  
ANISOU 2113  CG  LYS A 274    27423  14418  20602  -1060  -2923   5584  A    C  
ATOM   2114  CD  LYS A 274      52.510 -34.608  19.425  1.00163.63      A    C  
ANISOU 2114  CD  LYS A 274    27578  13908  20688   -854  -2989   5727  A    C  
ATOM   2115  CE  LYS A 274      52.425 -35.338  20.763  1.00161.54      A    C  
ANISOU 2115  CE  LYS A 274    27677  13437  20265   -832  -2909   6123  A    C  
ATOM   2116  NZ  LYS A 274      52.803 -36.773  20.649  1.00161.22      A    N1+
ANISOU 2116  NZ  LYS A 274    27900  12941  20417   -649  -2939   6275  A    N1+
ATOM   2117  N   VAL A 275      52.538 -28.649  17.527  1.00149.55      A    N  
ANISOU 2117  N   VAL A 275    24408  13902  18513  -1139  -3105   4684  A    N  
ATOM   2118  CA  VAL A 275      52.945 -27.761  16.437  1.00147.08      A    C  
ANISOU 2118  CA  VAL A 275    23764  13848  18271  -1069  -3188   4391  A    C  
ATOM   2119  C   VAL A 275      54.275 -27.044  16.673  1.00141.78      A    C  
ANISOU 2119  C   VAL A 275    22975  13486  17410   -826  -3401   4388  A    C  
ATOM   2120  O   VAL A 275      55.189 -27.136  15.850  1.00134.62      A    O  
ANISOU 2120  O   VAL A 275    21922  12619  16609   -601  -3561   4260  A    O  
ATOM   2121  CB  VAL A 275      51.858 -26.719  16.154  1.00147.71      A    C  
ANISOU 2121  CB  VAL A 275    23654  14126  18342  -1347  -3002   4218  A    C  
ATOM   2122  CG1 VAL A 275      51.263 -26.235  17.463  1.00153.54      A    C  
ANISOU 2122  CG1 VAL A 275    24537  14973  18829  -1530  -2876   4409  A    C  
ATOM   2123  CG2 VAL A 275      52.424 -25.564  15.338  1.00137.41      A    C  
ANISOU 2123  CG2 VAL A 275    22028  13157  17025  -1254  -3090   3973  A    C  
ATOM   2124  N   LYS A 276      54.376 -26.311  17.780  1.00144.12      A    N  
ANISOU 2124  N   LYS A 276    23322  14011  17427   -875  -3401   4517  A    N  
ATOM   2125  CA  LYS A 276      55.646 -25.701  18.153  1.00147.01      A    C  
ANISOU 2125  CA  LYS A 276    23596  14663  17600   -656  -3609   4530  A    C  
ATOM   2126  C   LYS A 276      56.732 -26.779  18.179  1.00154.88      A    C  
ANISOU 2126  C   LYS A 276    24722  15489  18635   -348  -3805   4663  A    C  
ATOM   2127  O   LYS A 276      57.792 -26.618  17.570  1.00155.48      A    O  
ANISOU 2127  O   LYS A 276    24622  15699  18754   -122  -3985   4548  A    O  
ATOM   2128  CB  LYS A 276      55.556 -24.999  19.516  1.00143.66      A    C  
ANISOU 2128  CB  LYS A 276    23273  14456  16855   -748  -3583   4685  A    C  
ATOM   2129  CG  LYS A 276      54.788 -23.683  19.506  1.00138.60      A    C  
ANISOU 2129  CG  LYS A 276    22460  14067  16134   -994  -3433   4527  A    C  
ATOM   2130  CD  LYS A 276      55.285 -22.723  20.591  1.00140.87      A    C  
ANISOU 2130  CD  LYS A 276    22745  14674  16104   -981  -3507   4588  A    C  
ATOM   2131  CE  LYS A 276      54.765 -21.288  20.354  1.00140.29      A    C  
ANISOU 2131  CE  LYS A 276    22451  14871  15983  -1176  -3389   4377  A    C  
ATOM   2132  NZ  LYS A 276      55.622 -20.180  20.928  1.00131.70      A    N1+
ANISOU 2132  NZ  LYS A 276    21247  14129  14665  -1110  -3521   4321  A    N1+
ATOM   2133  N   ASP A 277      56.443 -27.884  18.865  1.00155.67      A    N  
ANISOU 2133  N   ASP A 277    25130  15290  18727   -337  -3759   4911  A    N  
ATOM   2134  CA  ASP A 277      57.395 -28.982  19.044  1.00157.91      A    C  
ANISOU 2134  CA  ASP A 277    25588  15384  19028    -38  -3926   5081  A    C  
ATOM   2135  C   ASP A 277      57.933 -29.606  17.753  1.00153.50      A    C  
ANISOU 2135  C   ASP A 277    24914  14665  18746    152  -4026   4914  A    C  
ATOM   2136  O   ASP A 277      59.144 -29.694  17.561  1.00152.81      A    O  
ANISOU 2136  O   ASP A 277    24746  14687  18626    443  -4235   4903  A    O  
ATOM   2137  CB  ASP A 277      56.788 -30.072  19.925  1.00166.84      A    C  
ANISOU 2137  CB  ASP A 277    27082  16174  20135    -96  -3808   5375  A    C  
ATOM   2138  CG  ASP A 277      57.168 -29.919  21.384  1.00174.31      A    C  
ANISOU 2138  CG  ASP A 277    28209  17279  20741    -19  -3864   5644  A    C  
ATOM   2139  OD1 ASP A 277      58.228 -29.316  21.665  1.00175.05      A    O  
ANISOU 2139  OD1 ASP A 277    28179  17688  20645    176  -4061   5623  A    O  
ATOM   2140  OD2 ASP A 277      56.409 -30.410  22.248  1.00176.99      A    O1-
ANISOU 2140  OD2 ASP A 277    28811  17434  21002   -153  -3710   5875  A    O1-
ATOM   2141  N   ARG A 278      57.040 -30.048  16.877  1.00151.29      A    N  
ANISOU 2141  N   ARG A 278    24621  14133  18730     -5  -3881   4778  A    N  
ATOM   2142  CA  ARG A 278      57.459 -30.689  15.632  1.00153.12      A    C  
ANISOU 2142  CA  ARG A 278    24757  14197  19227    168  -3964   4606  A    C  
ATOM   2143  C   ARG A 278      58.199 -29.718  14.698  1.00145.30      A    C  
ANISOU 2143  C   ARG A 278    23410  13546  18252    289  -4088   4347  A    C  
ATOM   2144  O   ARG A 278      58.719 -30.122  13.654  1.00144.36      A    O  
ANISOU 2144  O   ARG A 278    23177  13355  18319    474  -4180   4195  A    O  
ATOM   2145  CB  ARG A 278      56.248 -31.305  14.922  1.00159.53      A    C  
ANISOU 2145  CB  ARG A 278    25618  14688  20307    -58  -3774   4495  A    C  
ATOM   2146  CG  ARG A 278      56.581 -32.314  13.821  1.00164.82      A    C  
ANISOU 2146  CG  ARG A 278    26290  15078  21256    122  -3846   4366  A    C  
ATOM   2147  CD  ARG A 278      55.311 -32.805  13.125  1.00166.97      A    C  
ANISOU 2147  CD  ARG A 278    26583  15072  21787   -137  -3655   4220  A    C  
ATOM   2148  NE  ARG A 278      55.580 -33.722  12.017  1.00168.43      A    N  
ANISOU 2148  NE  ARG A 278    26757  14999  22241     23  -3722   4059  A    N  
ATOM   2149  CZ  ARG A 278      55.737 -33.350  10.746  1.00167.08      A    C  
ANISOU 2149  CZ  ARG A 278    26308  14969  22204     91  -3773   3761  A    C  
ATOM   2150  NH1 ARG A 278      55.668 -32.065  10.397  1.00156.56      A    N1+
ANISOU 2150  NH1 ARG A 278    24684  14029  20772     16  -3760   3598  A    N1+
ATOM   2151  NH2 ARG A 278      55.974 -34.270   9.820  1.00169.25      A    N  
ANISOU 2151  NH2 ARG A 278    26604  14990  22713    247  -3833   3627  A    N  
ATOM   2152  N   LEU A 279      58.254 -28.445  15.082  1.00136.19      A    N  
ANISOU 2152  N   LEU A 279    22086  12756  16903    188  -4083   4298  A    N  
ATOM   2153  CA  LEU A 279      58.870 -27.427  14.240  1.00132.13      A    C  
ANISOU 2153  CA  LEU A 279    21233  12564  16404    267  -4168   4061  A    C  
ATOM   2154  C   LEU A 279      60.115 -26.764  14.839  1.00140.36      A    C  
ANISOU 2154  C   LEU A 279    22177  13930  17223    457  -4360   4121  A    C  
ATOM   2155  O   LEU A 279      60.935 -26.198  14.111  1.00133.12      A    O  
ANISOU 2155  O   LEU A 279    20998  13236  16344    602  -4473   3956  A    O  
ATOM   2156  CB  LEU A 279      57.842 -26.366  13.858  1.00129.33      A    C  
ANISOU 2156  CB  LEU A 279    20698  12371  16069    -23  -3983   3880  A    C  
ATOM   2157  CG  LEU A 279      56.910 -26.742  12.702  1.00126.39      A    C  
ANISOU 2157  CG  LEU A 279    20256  11802  15963   -144  -3844   3691  A    C  
ATOM   2158  CD1 LEU A 279      56.103 -25.535  12.266  1.00119.66      A    C  
ANISOU 2158  CD1 LEU A 279    19178  11186  15103   -371  -3690   3502  A    C  
ATOM   2159  CD2 LEU A 279      57.703 -27.298  11.523  1.00122.97      A    C  
ANISOU 2159  CD2 LEU A 279    19698  11298  15728    118  -3980   3544  A    C  
ATOM   2160  N   LYS A 280      60.257 -26.835  16.159  1.00156.34      A    N  
ANISOU 2160  N   LYS A 280    24402  15989  19012    456  -4395   4353  A    N  
ATOM   2161  CA  LYS A 280      61.422 -26.264  16.841  1.00164.38      A    C  
ANISOU 2161  CA  LYS A 280    25339  17319  19798    631  -4587   4414  A    C  
ATOM   2162  C   LYS A 280      62.738 -26.620  16.143  1.00161.89      A    C  
ANISOU 2162  C   LYS A 280    24878  17062  19571    964  -4802   4350  A    C  
ATOM   2163  O   LYS A 280      63.599 -25.759  15.946  1.00159.13      A    O  
ANISOU 2163  O   LYS A 280    24275  17034  19152   1054  -4924   4229  A    O  
ATOM   2164  CB  LYS A 280      61.473 -26.724  18.302  1.00172.66      A    C  
ANISOU 2164  CB  LYS A 280    26682  18320  20602    662  -4619   4709  A    C  
ATOM   2165  CG  LYS A 280      60.344 -26.198  19.187  1.00175.83      A    C  
ANISOU 2165  CG  LYS A 280    27209  18750  20849    357  -4428   4788  A    C  
ATOM   2166  CD  LYS A 280      60.441 -26.781  20.599  1.00180.58      A    C  
ANISOU 2166  CD  LYS A 280    28117  19290  21206    425  -4462   5098  A    C  
ATOM   2167  CE  LYS A 280      59.240 -26.405  21.455  1.00178.96      A    C  
ANISOU 2167  CE  LYS A 280    28061  19077  20860    127  -4251   5195  A    C  
ATOM   2168  NZ  LYS A 280      59.295 -27.038  22.802  1.00179.93      A    N1+
ANISOU 2168  NZ  LYS A 280    28494  19127  20744    205  -4269   5513  A    N1+
ATOM   2169  N   ALA A 281      62.883 -27.891  15.775  1.00158.32      A    N  
ANISOU 2169  N   ALA A 281    24585  16292  19275   1143  -4840   4429  A    N  
ATOM   2170  CA  ALA A 281      64.086 -28.385  15.103  1.00152.88      A    C  
ANISOU 2170  CA  ALA A 281    23787  15622  18680   1481  -5036   4381  A    C  
ATOM   2171  C   ALA A 281      64.471 -27.609  13.829  1.00146.66      A    C  
ANISOU 2171  C   ALA A 281    22637  15051  18037   1515  -5063   4094  A    C  
ATOM   2172  O   ALA A 281      65.651 -27.538  13.472  1.00144.12      A    O  
ANISOU 2172  O   ALA A 281    22142  14908  17710   1774  -5242   4045  A    O  
ATOM   2173  CB  ALA A 281      63.944 -29.878  14.794  1.00149.52      A    C  
ANISOU 2173  CB  ALA A 281    23607  14767  18437   1628  -5027   4483  A    C  
ATOM   2174  N   TYR A 282      63.486 -27.039  13.139  1.00136.49      A    N  
ANISOU 2174  N   TYR A 282    21231  13754  16874   1263  -4883   3913  A    N  
ATOM   2175  CA  TYR A 282      63.763 -26.336  11.895  1.00133.19      A    C  
ANISOU 2175  CA  TYR A 282    20485  13525  16596   1298  -4885   3654  A    C  
ATOM   2176  C   TYR A 282      63.897 -24.834  12.134  1.00137.94      A    C  
ANISOU 2176  C   TYR A 282    20854  14507  17050   1151  -4864   3560  A    C  
ATOM   2177  O   TYR A 282      64.905 -24.220  11.763  1.00131.70      A    O  
ANISOU 2177  O   TYR A 282    19815  13984  16240   1300  -4987   3464  A    O  
ATOM   2178  CB  TYR A 282      62.674 -26.614  10.862  1.00132.48      A    C  
ANISOU 2178  CB  TYR A 282    20379  13218  16739   1148  -4710   3491  A    C  
ATOM   2179  CG  TYR A 282      62.584 -28.053  10.387  1.00140.31      A    C  
ANISOU 2179  CG  TYR A 282    21559  13831  17922   1295  -4731   3523  A    C  
ATOM   2180  CD1 TYR A 282      61.718 -28.956  11.000  1.00145.07      A    C  
ANISOU 2180  CD1 TYR A 282    22475  14092  18553   1161  -4627   3679  A    C  
ATOM   2181  CD2 TYR A 282      63.343 -28.502   9.308  1.00142.73      A    C  
ANISOU 2181  CD2 TYR A 282    21729  14115  18387   1563  -4842   3391  A    C  
ATOM   2182  CE1 TYR A 282      61.621 -30.270  10.562  1.00151.94      A    C  
ANISOU 2182  CE1 TYR A 282    23525  14590  19614   1282  -4636   3699  A    C  
ATOM   2183  CE2 TYR A 282      63.252 -29.816   8.859  1.00149.28      A    C  
ANISOU 2183  CE2 TYR A 282    22738  14584  19397   1699  -4858   3403  A    C  
ATOM   2184  CZ  TYR A 282      62.390 -30.697   9.491  1.00154.96      A    C  
ANISOU 2184  CZ  TYR A 282    23776  14950  20152   1553  -4755   3554  A    C  
ATOM   2185  OH  TYR A 282      62.295 -32.006   9.057  1.00157.34      A    O  
ANISOU 2185  OH  TYR A 282    24266  14869  20647   1677  -4763   3561  A    O  
ATOM   2186  N   VAL A 283      62.874 -24.246  12.751  1.00145.80      A    N  
ANISOU 2186  N   VAL A 283    21930  15520  17949    857  -4701   3586  A    N  
ATOM   2187  CA  VAL A 283      62.890 -22.827  13.106  1.00144.82      A    C  
ANISOU 2187  CA  VAL A 283    21626  15723  17674    696  -4662   3507  A    C  
ATOM   2188  C   VAL A 283      63.287 -22.628  14.568  1.00147.19      A    C  
ANISOU 2188  C   VAL A 283    22071  16153  17700    688  -4756   3693  A    C  
ATOM   2189  O   VAL A 283      62.621 -23.117  15.484  1.00144.99      A    O  
ANISOU 2189  O   VAL A 283    22062  15711  17316    582  -4688   3870  A    O  
ATOM   2190  CB  VAL A 283      61.527 -22.139  12.837  1.00146.83      A    C  
ANISOU 2190  CB  VAL A 283    21848  15961  17978    385  -4419   3394  A    C  
ATOM   2191  CG1 VAL A 283      60.375 -23.058  13.194  1.00148.30      A    C  
ANISOU 2191  CG1 VAL A 283    22316  15824  18209    238  -4282   3515  A    C  
ATOM   2192  CG2 VAL A 283      61.426 -20.833  13.610  1.00146.75      A    C  
ANISOU 2192  CG2 VAL A 283    21762  16232  17766    204  -4370   3379  A    C  
ATOM   2193  N   ARG A 284      64.379 -21.906  14.781  1.00151.98      A    N  
ANISOU 2193  N   ARG A 284    22490  17064  18190    802  -4910   3651  A    N  
ATOM   2194  CA  ARG A 284      64.893 -21.698  16.126  1.00159.60      A    C  
ANISOU 2194  CA  ARG A 284    23562  18195  18885    825  -5029   3803  A    C  
ATOM   2195  C   ARG A 284      64.186 -20.544  16.834  1.00156.76      A    C  
ANISOU 2195  C   ARG A 284    23195  18006  18362    537  -4897   3763  A    C  
ATOM   2196  O   ARG A 284      63.703 -20.706  17.958  1.00159.11      A    O  
ANISOU 2196  O   ARG A 284    23726  18260  18470    439  -4860   3926  A    O  
ATOM   2197  CB  ARG A 284      66.401 -21.459  16.085  1.00166.45      A    C  
ANISOU 2197  CB  ARG A 284    24223  19327  19695   1072  -5265   3765  A    C  
ATOM   2198  CG  ARG A 284      67.171 -22.574  15.401  1.00173.32      A    C  
ANISOU 2198  CG  ARG A 284    25092  20051  20713   1384  -5403   3804  A    C  
ATOM   2199  CD  ARG A 284      68.647 -22.238  15.283  1.00180.70      A    C  
ANISOU 2199  CD  ARG A 284    25777  21281  21597   1618  -5624   3747  A    C  
ATOM   2200  NE  ARG A 284      69.414 -23.355  14.737  1.00188.89      A    N  
ANISOU 2200  NE  ARG A 284    26833  22185  22750   1943  -5763   3804  A    N  
ATOM   2201  CZ  ARG A 284      70.742 -23.398  14.691  1.00195.50      A    C  
ANISOU 2201  CZ  ARG A 284    27500  23237  23544   2207  -5975   3801  A    C  
ATOM   2202  NH1 ARG A 284      71.456 -22.383  15.161  1.00197.91      A    N1+
ANISOU 2202  NH1 ARG A 284    27596  23901  23700   2169  -6075   3737  A    N1+
ATOM   2203  NH2 ARG A 284      71.358 -24.456  14.179  1.00196.63      A    N  
ANISOU 2203  NH2 ARG A 284    27678  23237  23795   2508  -6086   3856  A    N  
ATOM   2204  N   ASP A 285      64.121 -19.389  16.173  1.00146.48      A    N  
ANISOU 2204  N   ASP A 285    21631  16893  17131    411  -4818   3551  A    N  
ATOM   2205  CA  ASP A 285      63.515 -18.191  16.763  1.00141.05      A    C  
ANISOU 2205  CA  ASP A 285    20915  16378  16301    151  -4691   3487  A    C  
ATOM   2206  C   ASP A 285      62.120 -18.442  17.364  1.00135.92      A    C  
ANISOU 2206  C   ASP A 285    20522  15535  15586    -71  -4494   3596  A    C  
ATOM   2207  O   ASP A 285      61.183 -18.818  16.651  1.00128.51      A    O  
ANISOU 2207  O   ASP A 285    19619  14385  14822   -163  -4333   3560  A    O  
ATOM   2208  CB  ASP A 285      63.460 -17.058  15.734  1.00138.81      A    C  
ANISOU 2208  CB  ASP A 285    20333  16248  16162     53  -4589   3248  A    C  
ATOM   2209  CG  ASP A 285      62.847 -15.788  16.295  1.00134.74      A    C  
ANISOU 2209  CG  ASP A 285    19787  15897  15510   -205  -4449   3172  A    C  
ATOM   2210  OD1 ASP A 285      63.563 -15.028  16.984  1.00135.47      A    O  
ANISOU 2210  OD1 ASP A 285    19801  16229  15441   -212  -4555   3144  A    O  
ATOM   2211  OD2 ASP A 285      61.646 -15.551  16.043  1.00128.11      A    O1-
ANISOU 2211  OD2 ASP A 285    18999  14950  14728   -397  -4234   3133  A    O1-
ATOM   2212  N   PRO A 286      61.981 -18.216  18.683  1.00135.17      A    N  
ANISOU 2212  N   PRO A 286    20596  15529  15232   -157  -4507   3725  A    N  
ATOM   2213  CA  PRO A 286      60.753 -18.520  19.424  1.00130.96      A    C  
ANISOU 2213  CA  PRO A 286    20324  14830  14603   -346  -4333   3865  A    C  
ATOM   2214  C   PRO A 286      59.615 -17.616  19.011  1.00126.88      A    C  
ANISOU 2214  C   PRO A 286    19719  14336  14152   -612  -4094   3717  A    C  
ATOM   2215  O   PRO A 286      58.465 -17.959  19.260  1.00129.03      A    O  
ANISOU 2215  O   PRO A 286    20166  14435  14425   -773  -3918   3800  A    O  
ATOM   2216  CB  PRO A 286      61.139 -18.216  20.868  1.00132.77      A    C  
ANISOU 2216  CB  PRO A 286    20685  15248  14515   -342  -4433   3993  A    C  
ATOM   2217  CG  PRO A 286      62.156 -17.150  20.740  1.00135.74      A    C  
ANISOU 2217  CG  PRO A 286    20794  15938  14843   -292  -4570   3817  A    C  
ATOM   2218  CD  PRO A 286      62.973 -17.548  19.542  1.00137.06      A    C  
ANISOU 2218  CD  PRO A 286    20765  16064  15248    -91  -4680   3724  A    C  
ATOM   2219  N   TYR A 287      59.935 -16.473  18.410  1.00125.88      A    N  
ANISOU 2219  N   TYR A 287    19327  14423  14079   -653  -4083   3507  A    N  
ATOM   2220  CA  TYR A 287      58.918 -15.546  17.922  1.00122.06      A    C  
ANISOU 2220  CA  TYR A 287    18738  13975  13664   -876  -3857   3357  A    C  
ATOM   2221  C   TYR A 287      58.292 -16.079  16.628  1.00119.76      A    C  
ANISOU 2221  C   TYR A 287    18376  13484  13645   -873  -3741   3278  A    C  
ATOM   2222  O   TYR A 287      57.066 -16.085  16.475  1.00122.78      A    O  
ANISOU 2222  O   TYR A 287    18823  13752  14076  -1051  -3540   3268  A    O  
ATOM   2223  CB  TYR A 287      59.504 -14.143  17.694  1.00123.66      A    C  
ANISOU 2223  CB  TYR A 287    18687  14457  13841   -910  -3876   3167  A    C  
ATOM   2224  CG  TYR A 287      59.802 -13.331  18.952  1.00130.66      A    C  
ANISOU 2224  CG  TYR A 287    19629  15558  14456   -991  -3930   3188  A    C  
ATOM   2225  CD1 TYR A 287      58.778 -12.901  19.794  1.00128.58      A    C  
ANISOU 2225  CD1 TYR A 287    19525  15302  14026  -1197  -3768   3234  A    C  
ATOM   2226  CD2 TYR A 287      61.108 -12.962  19.273  1.00137.05      A    C  
ANISOU 2226  CD2 TYR A 287    20317  16579  15178   -863  -4142   3147  A    C  
ATOM   2227  CE1 TYR A 287      59.052 -12.149  20.937  1.00131.12      A    C  
ANISOU 2227  CE1 TYR A 287    19900  15828  14092  -1265  -3821   3237  A    C  
ATOM   2228  CE2 TYR A 287      61.392 -12.208  20.411  1.00138.11      A    C  
ANISOU 2228  CE2 TYR A 287    20492  16921  15063   -941  -4202   3141  A    C  
ATOM   2229  CZ  TYR A 287      60.362 -11.803  21.240  1.00134.74      A    C  
ANISOU 2229  CZ  TYR A 287    20238  16490  14466  -1138  -4042   3183  A    C  
ATOM   2230  OH  TYR A 287      60.648 -11.056  22.370  1.00131.79      A    O  
ANISOU 2230  OH  TYR A 287    19909  16329  13837  -1207  -4105   3163  A    O  
ATOM   2231  N   ALA A 288      59.138 -16.526  15.702  1.00111.80      A    N  
ANISOU 2231  N   ALA A 288    17225  12447  12807   -666  -3872   3215  A    N  
ATOM   2232  CA  ALA A 288      58.665 -17.164  14.473  1.00101.87      A    C  
ANISOU 2232  CA  ALA A 288    15907  10999  11800   -627  -3795   3136  A    C  
ATOM   2233  C   ALA A 288      57.760 -18.357  14.784  1.00114.09      A    C  
ANISOU 2233  C   ALA A 288    17719  12246  13383   -692  -3717   3285  A    C  
ATOM   2234  O   ALA A 288      56.689 -18.511  14.196  1.00116.63      A    O  
ANISOU 2234  O   ALA A 288    18040  12437  13836   -827  -3545   3219  A    O  
ATOM   2235  CB  ALA A 288      59.838 -17.599  13.615  1.00 87.10      A    C  
ANISOU 2235  CB  ALA A 288    13881   9143  10072   -361  -3974   3076  A    C  
ATOM   2236  N   LEU A 289      58.200 -19.202  15.709  1.00118.01      A    N  
ANISOU 2236  N   LEU A 289    18437  12639  13762   -592  -3842   3487  A    N  
ATOM   2237  CA  LEU A 289      57.389 -20.322  16.158  1.00120.18      A    C  
ANISOU 2237  CA  LEU A 289    18986  12619  14055   -661  -3761   3659  A    C  
ATOM   2238  C   LEU A 289      56.002 -19.853  16.595  1.00120.40      A    C  
ANISOU 2238  C   LEU A 289    19095  12635  14016   -953  -3525   3669  A    C  
ATOM   2239  O   LEU A 289      54.996 -20.383  16.131  1.00124.04      A    O  
ANISOU 2239  O   LEU A 289    19612  12891  14628  -1076  -3374   3652  A    O  
ATOM   2240  CB  LEU A 289      58.089 -21.063  17.303  1.00125.03      A    C  
ANISOU 2240  CB  LEU A 289    19834  13180  14493   -516  -3918   3899  A    C  
ATOM   2241  CG  LEU A 289      59.259 -21.973  16.909  1.00127.27      A    C  
ANISOU 2241  CG  LEU A 289    20114  13374  14869   -211  -4133   3943  A    C  
ATOM   2242  CD1 LEU A 289      60.288 -22.137  18.045  1.00124.47      A    C  
ANISOU 2242  CD1 LEU A 289    19876  13143  14274    -35  -4329   4124  A    C  
ATOM   2243  CD2 LEU A 289      58.738 -23.324  16.434  1.00129.25      A    C  
ANISOU 2243  CD2 LEU A 289    20537  13249  15323   -177  -4076   4015  A    C  
ATOM   2244  N   ASP A 290      55.953 -18.853  17.475  1.00117.74      A    N  
ANISOU 2244  N   ASP A 290    18757  12524  13453  -1064  -3494   3686  A    N  
ATOM   2245  CA  ASP A 290      54.684 -18.366  18.021  1.00119.78      A    C  
ANISOU 2245  CA  ASP A 290    19103  12795  13613  -1326  -3273   3710  A    C  
ATOM   2246  C   ASP A 290      53.739 -17.867  16.938  1.00124.80      A    C  
ANISOU 2246  C   ASP A 290    19557  13430  14431  -1471  -3086   3514  A    C  
ATOM   2247  O   ASP A 290      52.528 -18.083  17.012  1.00126.34      A    O  
ANISOU 2247  O   ASP A 290    19840  13504  14657  -1659  -2897   3544  A    O  
ATOM   2248  CB  ASP A 290      54.908 -17.248  19.038  1.00119.77      A    C  
ANISOU 2248  CB  ASP A 290    19099  13066  13342  -1395  -3284   3719  A    C  
ATOM   2249  CG  ASP A 290      53.619 -16.822  19.732  1.00122.06      A    C  
ANISOU 2249  CG  ASP A 290    19508  13367  13503  -1646  -3060   3769  A    C  
ATOM   2250  OD1 ASP A 290      52.889 -17.702  20.240  1.00128.61      A    O  
ANISOU 2250  OD1 ASP A 290    20558  13994  14314  -1724  -2970   3944  A    O  
ATOM   2251  OD2 ASP A 290      53.337 -15.609  19.776  1.00117.08      A    O1-
ANISOU 2251  OD2 ASP A 290    18752  12944  12790  -1763  -2966   3637  A    O1-
ATOM   2252  N   LEU A 291      54.286 -17.181  15.939  1.00122.91      A    N  
ANISOU 2252  N   LEU A 291    19056  13340  14305  -1381  -3133   3316  A    N  
ATOM   2253  CA  LEU A 291      53.462 -16.689  14.841  1.00114.02      A    C  
ANISOU 2253  CA  LEU A 291    17743  12236  13343  -1483  -2965   3127  A    C  
ATOM   2254  C   LEU A 291      52.922 -17.855  14.010  1.00110.28      A    C  
ANISOU 2254  C   LEU A 291    17306  11499  13097  -1465  -2927   3113  A    C  
ATOM   2255  O   LEU A 291      51.714 -17.955  13.790  1.00114.79      A    O  
ANISOU 2255  O   LEU A 291    17896  11985  13735  -1643  -2743   3079  A    O  
ATOM   2256  CB  LEU A 291      54.237 -15.701  13.966  1.00102.00      A    C  
ANISOU 2256  CB  LEU A 291    15937  10933  11884  -1371  -3021   2937  A    C  
ATOM   2257  CG  LEU A 291      53.492 -15.149  12.751  1.00 90.29      A    C  
ANISOU 2257  CG  LEU A 291    14244   9499  10563  -1434  -2856   2743  A    C  
ATOM   2258  CD1 LEU A 291      52.197 -14.483  13.172  1.00 87.26      A    C  
ANISOU 2258  CD1 LEU A 291    13903   9166  10084  -1674  -2629   2735  A    C  
ATOM   2259  CD2 LEU A 291      54.381 -14.179  11.991  1.00 87.66      A    C  
ANISOU 2259  CD2 LEU A 291    13650   9381  10277  -1307  -2915   2589  A    C  
ATOM   2260  N   ILE A 292      53.817 -18.730  13.557  1.00 97.69      A    N  
ANISOU 2260  N   ILE A 292    15716   9781  11620  -1252  -3101   3130  A    N  
ATOM   2261  CA  ILE A 292      53.412 -19.921  12.826  1.00103.50      A    C  
ANISOU 2261  CA  ILE A 292    16511  10244  12573  -1220  -3085   3113  A    C  
ATOM   2262  C   ILE A 292      52.272 -20.612  13.556  1.00108.86      A    C  
ANISOU 2262  C   ILE A 292    17429  10705  13228  -1426  -2939   3260  A    C  
ATOM   2263  O   ILE A 292      51.343 -21.134  12.936  1.00112.48      A    O  
ANISOU 2263  O   ILE A 292    17883  10998  13855  -1537  -2817   3188  A    O  
ATOM   2264  CB  ILE A 292      54.568 -20.928  12.683  1.00109.91      A    C  
ANISOU 2264  CB  ILE A 292    17390  10913  13456   -958  -3303   3186  A    C  
ATOM   2265  CG1 ILE A 292      55.675 -20.353  11.805  1.00115.46      A    C  
ANISOU 2265  CG1 ILE A 292    17834  11819  14216   -747  -3439   3030  A    C  
ATOM   2266  CG2 ILE A 292      54.077 -22.226  12.079  1.00104.37      A    C  
ANISOU 2266  CG2 ILE A 292    16796   9889  12971   -945  -3276   3182  A    C  
ATOM   2267  CD1 ILE A 292      56.457 -21.417  11.060  1.00117.18      A    C  
ANISOU 2267  CD1 ILE A 292    18049  11869  14604   -498  -3594   3011  A    C  
ATOM   2268  N   ASP A 293      52.347 -20.605  14.881  1.00107.72      A    N  
ANISOU 2268  N   ASP A 293    17486  10573  12870  -1478  -2951   3464  A    N  
ATOM   2269  CA  ASP A 293      51.341 -21.255  15.706  1.00114.85      A    C  
ANISOU 2269  CA  ASP A 293    18632  11279  13726  -1666  -2809   3638  A    C  
ATOM   2270  C   ASP A 293      49.981 -20.559  15.641  1.00117.45      A    C  
ANISOU 2270  C   ASP A 293    18888  11694  14045  -1932  -2569   3551  A    C  
ATOM   2271  O   ASP A 293      48.948 -21.214  15.529  1.00125.17      A    O  
ANISOU 2271  O   ASP A 293    19947  12475  15136  -2092  -2423   3575  A    O  
ATOM   2272  CB  ASP A 293      51.817 -21.322  17.155  1.00122.30      A    C  
ANISOU 2272  CB  ASP A 293    19798  12258  14411  -1631  -2884   3879  A    C  
ATOM   2273  CG  ASP A 293      50.978 -22.253  17.998  1.00125.73      A    C  
ANISOU 2273  CG  ASP A 293    20516  12443  14814  -1772  -2761   4102  A    C  
ATOM   2274  OD1 ASP A 293      50.819 -23.418  17.584  1.00125.77      A    O  
ANISOU 2274  OD1 ASP A 293    20624  12150  15014  -1742  -2761   4147  A    O  
ATOM   2275  OD2 ASP A 293      50.485 -21.823  19.066  1.00126.81      A    O1-
ANISOU 2275  OD2 ASP A 293    20772  12678  14733  -1910  -2660   4231  A    O1-
ATOM   2276  N   LYS A 294      49.980 -19.235  15.719  1.00115.88      A    N  
ANISOU 2276  N   LYS A 294    18532  11784  13711  -1979  -2523   3449  A    N  
ATOM   2277  CA  LYS A 294      48.730 -18.487  15.752  1.00115.89      A    C  
ANISOU 2277  CA  LYS A 294    18469  11892  13671  -2211  -2295   3378  A    C  
ATOM   2278  C   LYS A 294      48.085 -18.428  14.374  1.00112.50      A    C  
ANISOU 2278  C   LYS A 294    17822  11451  13470  -2249  -2199   3159  A    C  
ATOM   2279  O   LYS A 294      46.917 -18.042  14.243  1.00110.37      A    O  
ANISOU 2279  O   LYS A 294    17493  11232  13209  -2437  -2001   3094  A    O  
ATOM   2280  CB  LYS A 294      48.957 -17.090  16.337  1.00116.64      A    C  
ANISOU 2280  CB  LYS A 294    18488  12286  13543  -2239  -2275   3344  A    C  
ATOM   2281  CG  LYS A 294      49.382 -17.150  17.798  1.00118.13      A    C  
ANISOU 2281  CG  LYS A 294    18903  12502  13478  -2232  -2346   3557  A    C  
ATOM   2282  CD  LYS A 294      49.593 -15.792  18.435  1.00115.87      A    C  
ANISOU 2282  CD  LYS A 294    18557  12502  12967  -2270  -2330   3509  A    C  
ATOM   2283  CE  LYS A 294      49.815 -15.964  19.936  1.00122.73      A    C  
ANISOU 2283  CE  LYS A 294    19670  13391  13569  -2282  -2380   3726  A    C  
ATOM   2284  NZ  LYS A 294      50.326 -14.737  20.611  1.00125.86      A    N1+
ANISOU 2284  NZ  LYS A 294    20017  14064  13738  -2276  -2426   3671  A    N1+
ATOM   2285  N   LEU A 295      48.849 -18.834  13.359  1.00107.09      A    N  
ANISOU 2285  N   LEU A 295    17018  10710  12961  -2058  -2340   3046  A    N  
ATOM   2286  CA  LEU A 295      48.350 -18.892  11.988  1.00 99.82      A    C  
ANISOU 2286  CA  LEU A 295    15893   9779  12257  -2055  -2276   2832  A    C  
ATOM   2287  C   LEU A 295      47.767 -20.266  11.676  1.00106.30      A    C  
ANISOU 2287  C   LEU A 295    16830  10289  13268  -2112  -2251   2854  A    C  
ATOM   2288  O   LEU A 295      46.787 -20.378  10.936  1.00109.69      A    O  
ANISOU 2288  O   LEU A 295    17153  10690  13836  -2232  -2120   2715  A    O  
ATOM   2289  CB  LEU A 295      49.444 -18.521  10.975  1.00 89.43      A    C  
ANISOU 2289  CB  LEU A 295    14363   8590  11025  -1815  -2425   2678  A    C  
ATOM   2290  CG  LEU A 295      49.760 -17.019  10.842  1.00 90.66      A    C  
ANISOU 2290  CG  LEU A 295    14322   9061  11065  -1789  -2393   2577  A    C  
ATOM   2291  CD1 LEU A 295      51.154 -16.763  10.286  1.00 91.44      A    C  
ANISOU 2291  CD1 LEU A 295    14276   9265  11199  -1542  -2578   2510  A    C  
ATOM   2292  CD2 LEU A 295      48.727 -16.299   9.998  1.00 88.11      A    C  
ANISOU 2292  CD2 LEU A 295    13804   8869  10806  -1896  -2203   2401  A    C  
ATOM   2293  N   LEU A 296      48.362 -21.309  12.250  1.00104.62      A    N  
ANISOU 2293  N   LEU A 296    16839   9846  13065  -2027  -2374   3027  A    N  
ATOM   2294  CA  LEU A 296      47.901 -22.677  12.009  1.00100.18      A    C  
ANISOU 2294  CA  LEU A 296    16417   8950  12697  -2075  -2355   3061  A    C  
ATOM   2295  C   LEU A 296      46.850 -23.087  13.017  1.00102.24      A    C  
ANISOU 2295  C   LEU A 296    16890   9064  12894  -2326  -2187   3240  A    C  
ATOM   2296  O   LEU A 296      46.725 -24.251  13.356  1.00110.26      A    O  
ANISOU 2296  O   LEU A 296    18117   9777  13999  -2356  -2190   3377  A    O  
ATOM   2297  CB  LEU A 296      49.066 -23.662  12.053  1.00102.07      A    C  
ANISOU 2297  CB  LEU A 296    16796   8989  12998  -1839  -2562   3162  A    C  
ATOM   2298  CG  LEU A 296      50.103 -23.502  10.944  1.00103.59      A    C  
ANISOU 2298  CG  LEU A 296    16784   9283  13293  -1577  -2730   2984  A    C  
ATOM   2299  CD1 LEU A 296      51.247 -24.477  11.152  1.00102.49      A    C  
ANISOU 2299  CD1 LEU A 296    16803   8953  13186  -1339  -2930   3112  A    C  
ATOM   2300  CD2 LEU A 296      49.454 -23.709   9.583  1.00101.53      A    C  
ANISOU 2300  CD2 LEU A 296    16338   8979  13260  -1609  -2661   2735  A    C  
ATOM   2301  N   VAL A 297      46.092 -22.118  13.499  1.00104.14      A    N  
ANISOU 2301  N   VAL A 297    17075   9514  12979  -2501  -2031   3243  A    N  
ATOM   2302  CA  VAL A 297      44.986 -22.400  14.400  1.00111.16      A    C  
ANISOU 2302  CA  VAL A 297    18133  10301  13801  -2752  -1844   3399  A    C  
ATOM   2303  C   VAL A 297      43.826 -23.116  13.675  1.00115.81      A    C  
ANISOU 2303  C   VAL A 297    18671  10705  14627  -2937  -1700   3285  A    C  
ATOM   2304  O   VAL A 297      43.493 -22.784  12.531  1.00110.13      A    O  
ANISOU 2304  O   VAL A 297    17711  10091  14044  -2934  -1674   3040  A    O  
ATOM   2305  CB  VAL A 297      44.519 -21.090  15.088  1.00101.23      A    C  
ANISOU 2305  CB  VAL A 297    16815   9344  12301  -2871  -1717   3417  A    C  
ATOM   2306  CG1 VAL A 297      43.096 -21.200  15.606  1.00103.44      A    C  
ANISOU 2306  CG1 VAL A 297    17166   9578  12558  -3153  -1478   3489  A    C  
ATOM   2307  CG2 VAL A 297      45.483 -20.709  16.208  1.00101.90      A    C  
ANISOU 2307  CG2 VAL A 297    17048   9533  12135  -2751  -1837   3597  A    C  
ATOM   2308  N   LEU A 298      43.222 -24.100  14.342  1.00121.64      A    N  
ANISOU 2308  N   LEU A 298    19632  11173  15413  -3095  -1605   3461  A    N  
ATOM   2309  CA  LEU A 298      42.127 -24.874  13.749  1.00124.13      A    C  
ANISOU 2309  CA  LEU A 298    19915  11286  15964  -3294  -1468   3362  A    C  
ATOM   2310  C   LEU A 298      40.846 -24.069  13.497  1.00124.08      A    C  
ANISOU 2310  C   LEU A 298    19708  11501  15935  -3519  -1261   3222  A    C  
ATOM   2311  O   LEU A 298      40.301 -24.085  12.393  1.00125.04      A    O  
ANISOU 2311  O   LEU A 298    19618  11655  16234  -3565  -1223   2982  A    O  
ATOM   2312  CB  LEU A 298      41.803 -26.088  14.618  1.00127.22      A    C  
ANISOU 2312  CB  LEU A 298    20605  11325  16407  -3422  -1399   3609  A    C  
ATOM   2313  CG  LEU A 298      42.777 -27.266  14.546  1.00130.24      A    C  
ANISOU 2313  CG  LEU A 298    21180  11385  16921  -3229  -1571   3705  A    C  
ATOM   2314  CD1 LEU A 298      42.462 -28.288  15.631  1.00137.06      A    C  
ANISOU 2314  CD1 LEU A 298    22366  11931  17779  -3351  -1476   4003  A    C  
ATOM   2315  CD2 LEU A 298      42.764 -27.917  13.168  1.00124.93      A    C  
ANISOU 2315  CD2 LEU A 298    20368  10553  16548  -3179  -1636   3448  A    C  
ATOM   2316  N   ASP A 299      40.362 -23.385  14.527  1.00120.23      A    N  
ANISOU 2316  N   ASP A 299    19288  11173  15223  -3649  -1128   3370  A    N  
ATOM   2317  CA  ASP A 299      39.134 -22.602  14.423  1.00117.21      A    C  
ANISOU 2317  CA  ASP A 299    18733  11010  14793  -3854   -920   3265  A    C  
ATOM   2318  C   ASP A 299      39.357 -21.249  13.702  1.00118.07      A    C  
ANISOU 2318  C   ASP A 299    18572  11472  14817  -3729   -950   3052  A    C  
ATOM   2319  O   ASP A 299      40.025 -20.352  14.218  1.00114.35      A    O  
ANISOU 2319  O   ASP A 299    18116  11194  14137  -3612  -1009   3112  A    O  
ATOM   2320  CB  ASP A 299      38.545 -22.395  15.823  1.00117.51      A    C  
ANISOU 2320  CB  ASP A 299    18954  11081  14612  -4025   -761   3512  A    C  
ATOM   2321  CG  ASP A 299      37.234 -21.639  15.801  1.00127.38      A    C  
ANISOU 2321  CG  ASP A 299    20040  12552  15806  -4239   -534   3423  A    C  
ATOM   2322  OD1 ASP A 299      36.526 -21.707  14.771  1.00134.59      A    O  
ANISOU 2322  OD1 ASP A 299    20741  13493  16906  -4320   -470   3205  A    O  
ATOM   2323  OD2 ASP A 299      36.910 -20.978  16.816  1.00125.01      A    O1-
ANISOU 2323  OD2 ASP A 299    19822  12409  15268  -4315   -421   3567  A    O1-
ATOM   2324  N   PRO A 300      38.786 -21.100  12.502  1.00117.72      A    N  
ANISOU 2324  N   PRO A 300    18278  11513  14935  -3754   -905   2801  A    N  
ATOM   2325  CA  PRO A 300      38.951 -19.883  11.695  1.00114.68      A    C  
ANISOU 2325  CA  PRO A 300    17633  11446  14494  -3624   -918   2598  A    C  
ATOM   2326  C   PRO A 300      38.858 -18.623  12.525  1.00115.74      A    C  
ANISOU 2326  C   PRO A 300    17771  11844  14362  -3648   -825   2683  A    C  
ATOM   2327  O   PRO A 300      39.795 -17.838  12.557  1.00121.30      A    O  
ANISOU 2327  O   PRO A 300    18443  12697  14949  -3471   -933   2673  A    O  
ATOM   2328  CB  PRO A 300      37.753 -19.925  10.750  1.00115.35      A    C  
ANISOU 2328  CB  PRO A 300    17498  11601  14731  -3763   -778   2387  A    C  
ATOM   2329  CG  PRO A 300      37.423 -21.363  10.627  1.00114.40      A    C  
ANISOU 2329  CG  PRO A 300    17489  11149  14829  -3881   -789   2406  A    C  
ATOM   2330  CD  PRO A 300      37.854 -22.060  11.888  1.00116.44      A    C  
ANISOU 2330  CD  PRO A 300    18068  11161  15013  -3923   -819   2697  A    C  
ATOM   2331  N   ALA A 301      37.730 -18.430  13.191  1.00121.08      A    N  
ANISOU 2331  N   ALA A 301    18483  12576  14945  -3868   -623   2760  A    N  
ATOM   2332  CA  ALA A 301      37.505 -17.206  13.948  1.00127.78      A    C  
ANISOU 2332  CA  ALA A 301    19328  13681  15540  -3900   -513   2819  A    C  
ATOM   2333  C   ALA A 301      38.422 -17.060  15.170  1.00129.99      A    C  
ANISOU 2333  C   ALA A 301    19845  13935  15611  -3824   -611   3036  A    C  
ATOM   2334  O   ALA A 301      38.327 -16.073  15.896  1.00130.45      A    O  
ANISOU 2334  O   ALA A 301    19927  14192  15446  -3844   -535   3088  A    O  
ATOM   2335  CB  ALA A 301      36.041 -17.091  14.353  1.00130.55      A    C  
ANISOU 2335  CB  ALA A 301    19656  14103  15844  -4148   -267   2849  A    C  
ATOM   2336  N   GLN A 302      39.301 -18.037  15.395  1.00129.11      A    N  
ANISOU 2336  N   GLN A 302    19906  13585  15565  -3730   -779   3154  A    N  
ATOM   2337  CA  GLN A 302      40.329 -17.931  16.440  1.00126.72      A    C  
ANISOU 2337  CA  GLN A 302    19805  13277  15067  -3615   -910   3341  A    C  
ATOM   2338  C   GLN A 302      41.722 -17.751  15.830  1.00122.13      A    C  
ANISOU 2338  C   GLN A 302    19145  12726  14531  -3357  -1143   3247  A    C  
ATOM   2339  O   GLN A 302      42.690 -17.444  16.525  1.00123.47      A    O  
ANISOU 2339  O   GLN A 302    19418  12956  14537  -3233  -1273   3349  A    O  
ATOM   2340  CB  GLN A 302      40.317 -19.153  17.367  1.00130.44      A    C  
ANISOU 2340  CB  GLN A 302    20560  13468  15532  -3686   -918   3594  A    C  
ATOM   2341  CG  GLN A 302      39.352 -19.064  18.560  1.00137.62      A    C  
ANISOU 2341  CG  GLN A 302    21624  14405  16259  -3895   -716   3782  A    C  
ATOM   2342  CD  GLN A 302      39.256 -20.374  19.358  1.00144.24      A    C  
ANISOU 2342  CD  GLN A 302    22739  14939  17126  -3971   -699   4039  A    C  
ATOM   2343  NE2 GLN A 302      39.545 -20.301  20.656  1.00146.33      A    N  
ANISOU 2343  NE2 GLN A 302    23226  15231  17140  -3954   -701   4273  A    N  
ATOM   2344  OE1 GLN A 302      38.918 -21.431  18.812  1.00142.67      A    O  
ANISOU 2344  OE1 GLN A 302    22556  14483  17170  -4042   -680   4025  A    O  
ATOM   2345  N   ARG A 303      41.810 -17.942  14.521  1.00115.03      A    N  
ANISOU 2345  N   ARG A 303    18053  11802  13851  -3275  -1195   3048  A    N  
ATOM   2346  CA  ARG A 303      43.068 -17.804  13.804  1.00108.45      A    C  
ANISOU 2346  CA  ARG A 303    17118  11004  13083  -3029  -1401   2947  A    C  
ATOM   2347  C   ARG A 303      43.437 -16.328  13.612  1.00104.01      A    C  
ANISOU 2347  C   ARG A 303    16379  10750  12390  -2945  -1395   2829  A    C  
ATOM   2348  O   ARG A 303      42.558 -15.482  13.404  1.00102.55      A    O  
ANISOU 2348  O   ARG A 303    16062  10742  12161  -3051  -1223   2730  A    O  
ATOM   2349  CB  ARG A 303      42.946 -18.492  12.451  1.00102.52      A    C  
ANISOU 2349  CB  ARG A 303    16217  10134  12602  -2972  -1439   2766  A    C  
ATOM   2350  CG  ARG A 303      44.241 -18.662  11.691  1.00107.62      A    C  
ANISOU 2350  CG  ARG A 303    16785  10762  13345  -2711  -1656   2682  A    C  
ATOM   2351  CD  ARG A 303      43.937 -19.382  10.406  1.00110.79      A    C  
ANISOU 2351  CD  ARG A 303    17051  11044  14000  -2677  -1669   2499  A    C  
ATOM   2352  NE  ARG A 303      42.782 -20.240  10.620  1.00124.36      A    N  
ANISOU 2352  NE  ARG A 303    18872  12565  15814  -2901  -1533   2541  A    N  
ATOM   2353  CZ  ARG A 303      42.276 -21.066   9.716  1.00130.67      A    C  
ANISOU 2353  CZ  ARG A 303    19600  13210  16839  -2940  -1518   2400  A    C  
ATOM   2354  NH1 ARG A 303      42.827 -21.150   8.515  1.00131.95      A    N1+
ANISOU 2354  NH1 ARG A 303    19591  13402  17141  -2751  -1635   2206  A    N1+
ATOM   2355  NH2 ARG A 303      41.218 -21.807  10.021  1.00132.51      A    N  
ANISOU 2355  NH2 ARG A 303    19929  13264  17155  -3170  -1384   2448  A    N  
ATOM   2356  N   ILE A 304      44.738 -16.039  13.659  1.00 93.53      A    N  
ANISOU 2356  N   ILE A 304    15046   9481  11011  -2751  -1580   2836  A    N  
ATOM   2357  CA  ILE A 304      45.243 -14.668  13.608  1.00 94.76      A    C  
ANISOU 2357  CA  ILE A 304    15060   9902  11042  -2674  -1587   2745  A    C  
ATOM   2358  C   ILE A 304      44.997 -14.028  12.256  1.00 95.07      A    C  
ANISOU 2358  C   ILE A 304    14824  10080  11219  -2615  -1521   2518  A    C  
ATOM   2359  O   ILE A 304      45.002 -14.713  11.226  1.00 98.51      A    O  
ANISOU 2359  O   ILE A 304    15161  10414  11854  -2539  -1568   2417  A    O  
ATOM   2360  CB  ILE A 304      46.759 -14.625  13.909  1.00 99.56      A    C  
ANISOU 2360  CB  ILE A 304    15708  10530  11588  -2481  -1815   2798  A    C  
ATOM   2361  CG1 ILE A 304      47.218 -13.205  14.251  1.00 92.60      A    C  
ANISOU 2361  CG1 ILE A 304    14739   9906  10539  -2457  -1807   2743  A    C  
ATOM   2362  CG2 ILE A 304      47.554 -15.181  12.748  1.00102.03      A    C  
ANISOU 2362  CG2 ILE A 304    15890  10766  12111  -2285  -1967   2690  A    C  
ATOM   2363  CD1 ILE A 304      48.604 -13.160  14.871  1.00 81.75      A    C  
ANISOU 2363  CD1 ILE A 304    13434   8568   9059  -2312  -2021   2821  A    C  
ATOM   2364  N   ASP A 305      44.767 -12.717  12.255  1.00 85.00      A    N  
ANISOU 2364  N   ASP A 305    13429   9035   9832  -2641  -1407   2438  A    N  
ATOM   2365  CA  ASP A 305      44.542 -12.019  10.990  1.00 85.53      A    C  
ANISOU 2365  CA  ASP A 305    13237   9251  10010  -2566  -1331   2239  A    C  
ATOM   2366  C   ASP A 305      45.763 -11.223  10.533  1.00 89.57      A    C  
ANISOU 2366  C   ASP A 305    13613   9895  10523  -2376  -1448   2161  A    C  
ATOM   2367  O   ASP A 305      46.726 -11.043  11.286  1.00 91.39      A    O  
ANISOU 2367  O   ASP A 305    13940  10135  10648  -2325  -1577   2248  A    O  
ATOM   2368  CB  ASP A 305      43.254 -11.170  11.006  1.00 86.14      A    C  
ANISOU 2368  CB  ASP A 305    13237   9482  10009  -2715  -1088   2180  A    C  
ATOM   2369  CG  ASP A 305      43.344  -9.957  11.924  1.00100.24      A    C  
ANISOU 2369  CG  ASP A 305    15078  11431  11579  -2764  -1013   2227  A    C  
ATOM   2370  OD1 ASP A 305      44.441  -9.688  12.460  1.00110.60      A    O  
ANISOU 2370  OD1 ASP A 305    16459  12757  12808  -2683  -1154   2282  A    O  
ATOM   2371  OD2 ASP A 305      42.314  -9.262  12.104  1.00 95.35      A    O1-
ANISOU 2371  OD2 ASP A 305    14426  10932  10871  -2882   -812   2200  A    O1-
ATOM   2372  N   SER A 306      45.718 -10.769   9.288  1.00 82.36      A    N  
ANISOU 2372  N   SER A 306    12470   9091   9730  -2269  -1402   1996  A    N  
ATOM   2373  CA  SER A 306      46.844 -10.090   8.666  1.00 79.33      A    C  
ANISOU 2373  CA  SER A 306    11932   8825   9384  -2083  -1498   1916  A    C  
ATOM   2374  C   SER A 306      47.331  -8.886   9.477  1.00 84.38      A    C  
ANISOU 2374  C   SER A 306    12599   9607   9854  -2113  -1474   1952  A    C  
ATOM   2375  O   SER A 306      48.535  -8.735   9.717  1.00 86.64      A    O  
ANISOU 2375  O   SER A 306    12889   9911  10119  -2011  -1631   1979  A    O  
ATOM   2376  CB  SER A 306      46.415  -9.658   7.282  1.00 85.50      A    C  
ANISOU 2376  CB  SER A 306    12472   9727  10288  -1992  -1390   1746  A    C  
ATOM   2377  OG  SER A 306      45.360 -10.506   6.866  1.00101.52      A    O  
ANISOU 2377  OG  SER A 306    14501  11663  12409  -2069  -1321   1706  A    O  
ATOM   2378  N   ASP A 307      46.391  -8.030   9.880  1.00 80.09      A    N  
ANISOU 2378  N   ASP A 307    12068   9169   9193  -2251  -1278   1942  A    N  
ATOM   2379  CA  ASP A 307      46.669  -6.891  10.761  1.00 78.91      A    C  
ANISOU 2379  CA  ASP A 307    11972   9140   8870  -2310  -1232   1968  A    C  
ATOM   2380  C   ASP A 307      47.434  -7.327  12.021  1.00 81.54      A    C  
ANISOU 2380  C   ASP A 307    12511   9395   9074  -2343  -1401   2108  A    C  
ATOM   2381  O   ASP A 307      48.591  -6.985  12.198  1.00 87.88      A    O  
ANISOU 2381  O   ASP A 307    13290  10245   9854  -2253  -1543   2103  A    O  
ATOM   2382  CB  ASP A 307      45.347  -6.206  11.142  1.00 89.24      A    C  
ANISOU 2382  CB  ASP A 307    13311  10533  10063  -2467   -993   1961  A    C  
ATOM   2383  CG  ASP A 307      45.533  -4.785  11.655  1.00100.85      A    C  
ANISOU 2383  CG  ASP A 307    14775  12151  11392  -2496   -901   1927  A    C  
ATOM   2384  OD1 ASP A 307      45.634  -3.850  10.822  1.00108.51      A    O  
ANISOU 2384  OD1 ASP A 307    15567  13235  12426  -2409   -811   1812  A    O  
ATOM   2385  OD2 ASP A 307      45.548  -4.603  12.893  1.00102.06      A    O1-
ANISOU 2385  OD2 ASP A 307    15105  12304  11370  -2604   -911   2014  A    O1-
ATOM   2386  N   ASP A 308      46.791  -8.103  12.886  1.00 88.10      A    N  
ANISOU 2386  N   ASP A 308    13541  10114   9820  -2470  -1384   2237  A    N  
ATOM   2387  CA  ASP A 308      47.438  -8.585  14.107  1.00 92.00      A    C  
ANISOU 2387  CA  ASP A 308    14244  10539  10172  -2489  -1535   2388  A    C  
ATOM   2388  C   ASP A 308      48.730  -9.356  13.821  1.00 88.37      A    C  
ANISOU 2388  C   ASP A 308    13771   9993   9812  -2315  -1781   2415  A    C  
ATOM   2389  O   ASP A 308      49.699  -9.259  14.565  1.00 92.71      A    O  
ANISOU 2389  O   ASP A 308    14396  10578  10251  -2263  -1934   2477  A    O  
ATOM   2390  CB  ASP A 308      46.466  -9.435  14.946  1.00 94.80      A    C  
ANISOU 2390  CB  ASP A 308    14809  10766  10444  -2641  -1458   2537  A    C  
ATOM   2391  CG  ASP A 308      45.345  -8.601  15.575  1.00100.07      A    C  
ANISOU 2391  CG  ASP A 308    15524  11547  10952  -2811  -1234   2540  A    C  
ATOM   2392  OD1 ASP A 308      45.475  -7.359  15.619  1.00105.15      A    O  
ANISOU 2392  OD1 ASP A 308    16084  12357  11511  -2808  -1167   2447  A    O  
ATOM   2393  OD2 ASP A 308      44.335  -9.179  16.035  1.00 96.45      A    O1-
ANISOU 2393  OD2 ASP A 308    15186  11008  10452  -2948  -1119   2637  A    O1-
ATOM   2394  N   ALA A 309      48.748 -10.124  12.744  1.00 85.82      A    N  
ANISOU 2394  N   ALA A 309    13349   9568   9693  -2217  -1822   2361  A    N  
ATOM   2395  CA  ALA A 309      49.947 -10.880  12.412  1.00 91.57      A    C  
ANISOU 2395  CA  ALA A 309    14058  10213  10520  -2036  -2047   2382  A    C  
ATOM   2396  C   ALA A 309      51.118  -9.945  12.192  1.00 87.84      A    C  
ANISOU 2396  C   ALA A 309    13432   9908  10034  -1912  -2145   2299  A    C  
ATOM   2397  O   ALA A 309      52.241 -10.264  12.540  1.00 94.67      A    O  
ANISOU 2397  O   ALA A 309    14332  10766  10874  -1799  -2342   2356  A    O  
ATOM   2398  CB  ALA A 309      49.719 -11.740  11.186  1.00100.16      A    C  
ANISOU 2398  CB  ALA A 309    15045  11180  11833  -1946  -2056   2305  A    C  
ATOM   2399  N   LEU A 310      50.844  -8.785  11.610  1.00 86.45      A    N  
ANISOU 2399  N   LEU A 310    13083   9884   9878  -1933  -2001   2168  A    N  
ATOM   2400  CA  LEU A 310      51.883  -7.817  11.281  1.00 83.90      A    C  
ANISOU 2400  CA  LEU A 310    12593   9714   9571  -1833  -2061   2077  A    C  
ATOM   2401  C   LEU A 310      52.403  -7.065  12.505  1.00 88.88      A    C  
ANISOU 2401  C   LEU A 310    13320  10444  10006  -1912  -2110   2121  A    C  
ATOM   2402  O   LEU A 310      53.531  -6.561  12.495  1.00 93.73      A    O  
ANISOU 2402  O   LEU A 310    13833  11155  10623  -1828  -2230   2076  A    O  
ATOM   2403  CB  LEU A 310      51.361  -6.815  10.251  1.00 74.72      A    C  
ANISOU 2403  CB  LEU A 310    11227   8668   8495  -1826  -1868   1934  A    C  
ATOM   2404  CG  LEU A 310      51.599  -7.205   8.799  1.00 76.58      A    C  
ANISOU 2404  CG  LEU A 310    11269   8893   8937  -1654  -1891   1842  A    C  
ATOM   2405  CD1 LEU A 310      50.871  -6.259   7.890  1.00 72.37      A    C  
ANISOU 2405  CD1 LEU A 310    10564   8477   8456  -1656  -1676   1724  A    C  
ATOM   2406  CD2 LEU A 310      53.084  -7.198   8.494  1.00 83.38      A    C  
ANISOU 2406  CD2 LEU A 310    12017   9798   9865  -1484  -2080   1825  A    C  
ATOM   2407  N   ASN A 311      51.565  -6.975  13.538  1.00 83.36      A    N  
ANISOU 2407  N   ASN A 311    12805   9731   9138  -2076  -2013   2199  A    N  
ATOM   2408  CA  ASN A 311      51.915  -6.274  14.764  1.00 90.52      A    C  
ANISOU 2408  CA  ASN A 311    13821  10736   9835  -2161  -2047   2231  A    C  
ATOM   2409  C   ASN A 311      52.529  -7.248  15.744  1.00 98.01      A    C  
ANISOU 2409  C   ASN A 311    14955  11612  10671  -2123  -2252   2383  A    C  
ATOM   2410  O   ASN A 311      52.824  -6.895  16.886  1.00 99.06      A    O  
ANISOU 2410  O   ASN A 311    15210  11824  10605  -2182  -2310   2431  A    O  
ATOM   2411  CB  ASN A 311      50.683  -5.603  15.389  1.00101.66      A    C  
ANISOU 2411  CB  ASN A 311    15335  12190  11101  -2342  -1826   2235  A    C  
ATOM   2412  CG  ASN A 311      51.024  -4.772  16.639  1.00115.40      A    C  
ANISOU 2412  CG  ASN A 311    17184  14047  12615  -2427  -1852   2242  A    C  
ATOM   2413  ND2 ASN A 311      50.123  -4.789  17.621  1.00120.04      A    N  
ANISOU 2413  ND2 ASN A 311    17960  14629  13020  -2563  -1745   2326  A    N  
ATOM   2414  OD1 ASN A 311      52.073  -4.121  16.713  1.00113.42      A    O  
ANISOU 2414  OD1 ASN A 311    16844  13896  12355  -2374  -1965   2165  A    O  
ATOM   2415  N   HIS A 312      52.716  -8.484  15.289  1.00104.58      A    N  
ANISOU 2415  N   HIS A 312    15813  12296  11628  -2016  -2359   2455  A    N  
ATOM   2416  CA  HIS A 312      53.314  -9.526  16.118  1.00107.42      A    C  
ANISOU 2416  CA  HIS A 312    16353  12563  11898  -1949  -2551   2615  A    C  
ATOM   2417  C   HIS A 312      54.804  -9.256  16.395  1.00105.10      A    C  
ANISOU 2417  C   HIS A 312    15984  12394  11554  -1814  -2776   2595  A    C  
ATOM   2418  O   HIS A 312      55.534  -8.752  15.525  1.00 88.66      A    O  
ANISOU 2418  O   HIS A 312    13683  10398   9606  -1716  -2822   2466  A    O  
ATOM   2419  CB  HIS A 312      53.119 -10.905  15.485  1.00101.10      A    C  
ANISOU 2419  CB  HIS A 312    15598  11550  11265  -1863  -2595   2686  A    C  
ATOM   2420  CG  HIS A 312      53.550 -12.037  16.363  1.00103.61      A    C  
ANISOU 2420  CG  HIS A 312    16134  11740  11492  -1798  -2756   2875  A    C  
ATOM   2421  CD2 HIS A 312      52.851 -12.811  17.228  1.00107.28      A    C  
ANISOU 2421  CD2 HIS A 312    16842  12065  11853  -1890  -2708   3047  A    C  
ATOM   2422  ND1 HIS A 312      54.854 -12.485  16.416  1.00102.82      A    N  
ANISOU 2422  ND1 HIS A 312    16015  11653  11400  -1607  -2991   2914  A    N  
ATOM   2423  CE1 HIS A 312      54.937 -13.488  17.269  1.00108.28      A    C  
ANISOU 2423  CE1 HIS A 312    16934  12215  11991  -1573  -3083   3103  A    C  
ATOM   2424  NE2 HIS A 312      53.735 -13.706  17.778  1.00111.53      A    N  
ANISOU 2424  NE2 HIS A 312    17513  12526  12336  -1746  -2911   3192  A    N  
ATOM   2425  N   ASP A 313      55.241  -9.597  17.608  1.00108.12      A    N  
ANISOU 2425  N   ASP A 313    16545  12796  11739  -1807  -2911   2724  A    N  
ATOM   2426  CA  ASP A 313      56.590  -9.272  18.057  1.00111.08      A    C  
ANISOU 2426  CA  ASP A 313    16856  13324  12026  -1701  -3125   2701  A    C  
ATOM   2427  C   ASP A 313      57.644  -9.772  17.073  1.00103.14      A    C  
ANISOU 2427  C   ASP A 313    15676  12298  11215  -1495  -3288   2659  A    C  
ATOM   2428  O   ASP A 313      58.707  -9.177  16.938  1.00 98.75      A    O  
ANISOU 2428  O   ASP A 313    14951  11898  10671  -1419  -3410   2565  A    O  
ATOM   2429  CB  ASP A 313      56.842  -9.831  19.460  1.00120.15      A    C  
ANISOU 2429  CB  ASP A 313    18240  14481  12931  -1689  -3257   2872  A    C  
ATOM   2430  CG  ASP A 313      55.912  -9.232  20.509  1.00128.31      A    C  
ANISOU 2430  CG  ASP A 313    19437  15572  13743  -1880  -3105   2905  A    C  
ATOM   2431  OD1 ASP A 313      55.585  -8.025  20.414  1.00128.18      A    O  
ANISOU 2431  OD1 ASP A 313    19318  15676  13708  -2003  -2971   2758  A    O  
ATOM   2432  OD2 ASP A 313      55.516  -9.972  21.439  1.00132.03      A    O1-
ANISOU 2432  OD2 ASP A 313    20144  15967  14056  -1900  -3115   3085  A    O1-
ATOM   2433  N   PHE A 314      57.335 -10.862  16.381  1.00 99.71      A    N  
ANISOU 2433  N   PHE A 314    15277  11671  10936  -1410  -3283   2721  A    N  
ATOM   2434  CA  PHE A 314      58.214 -11.400  15.350  1.00102.62      A    C  
ANISOU 2434  CA  PHE A 314    15486  12005  11500  -1205  -3417   2675  A    C  
ATOM   2435  C   PHE A 314      58.819 -10.308  14.457  1.00102.07      A    C  
ANISOU 2435  C   PHE A 314    15127  12109  11546  -1170  -3397   2489  A    C  
ATOM   2436  O   PHE A 314      60.026 -10.307  14.202  1.00100.62      A    O  
ANISOU 2436  O   PHE A 314    14801  12022  11408  -1015  -3568   2456  A    O  
ATOM   2437  CB  PHE A 314      57.444 -12.430  14.511  1.00107.58      A    C  
ANISOU 2437  CB  PHE A 314    16163  12405  12308  -1174  -3334   2703  A    C  
ATOM   2438  CG  PHE A 314      58.221 -12.993  13.341  1.00110.46      A    C  
ANISOU 2438  CG  PHE A 314    16364  12726  12881   -959  -3448   2639  A    C  
ATOM   2439  CD1 PHE A 314      59.477 -13.547  13.517  1.00107.62      A    C  
ANISOU 2439  CD1 PHE A 314    15993  12390  12509   -758  -3681   2700  A    C  
ATOM   2440  CD2 PHE A 314      57.671 -12.998  12.063  1.00110.06      A    C  
ANISOU 2440  CD2 PHE A 314    16170  12617  13029   -946  -3322   2517  A    C  
ATOM   2441  CE1 PHE A 314      60.177 -14.074  12.439  1.00105.35      A    C  
ANISOU 2441  CE1 PHE A 314    15555  12065  12406   -550  -3779   2640  A    C  
ATOM   2442  CE2 PHE A 314      58.370 -13.525  10.986  1.00105.46      A    C  
ANISOU 2442  CE2 PHE A 314    15441  12002  12626   -738  -3424   2453  A    C  
ATOM   2443  CZ  PHE A 314      59.622 -14.066  11.176  1.00102.22      A    C  
ANISOU 2443  CZ  PHE A 314    15024  11609  12205   -541  -3649   2515  A    C  
ATOM   2444  N   PHE A 315      57.982  -9.379  13.996  1.00101.60      A    N  
ANISOU 2444  N   PHE A 315    14980  12093  11531  -1309  -3180   2377  A    N  
ATOM   2445  CA  PHE A 315      58.408  -8.336  13.052  1.00 99.13      A    C  
ANISOU 2445  CA  PHE A 315    14401  11919  11344  -1280  -3118   2213  A    C  
ATOM   2446  C   PHE A 315      59.035  -7.125  13.731  1.00100.40      A    C  
ANISOU 2446  C   PHE A 315    14492  12271  11383  -1363  -3143   2143  A    C  
ATOM   2447  O   PHE A 315      59.408  -6.153  13.064  1.00103.28      A    O  
ANISOU 2447  O   PHE A 315    14647  12749  11846  -1361  -3077   2013  A    O  
ATOM   2448  CB  PHE A 315      57.224  -7.862  12.196  1.00 94.09      A    C  
ANISOU 2448  CB  PHE A 315    13696  11245  10811  -1372  -2865   2126  A    C  
ATOM   2449  CG  PHE A 315      56.655  -8.923  11.308  1.00 93.29      A    C  
ANISOU 2449  CG  PHE A 315    13605  10980  10862  -1289  -2835   2145  A    C  
ATOM   2450  CD1 PHE A 315      55.510  -9.618  11.680  1.00 93.07      A    C  
ANISOU 2450  CD1 PHE A 315    13770  10801  10792  -1399  -2742   2229  A    C  
ATOM   2451  CD2 PHE A 315      57.266  -9.236  10.107  1.00 89.21      A    C  
ANISOU 2451  CD2 PHE A 315    12902  10463  10530  -1104  -2898   2074  A    C  
ATOM   2452  CE1 PHE A 315      54.984 -10.598  10.871  1.00 89.66      A    C  
ANISOU 2452  CE1 PHE A 315    13344  10212  10510  -1339  -2717   2227  A    C  
ATOM   2453  CE2 PHE A 315      56.744 -10.217   9.294  1.00 93.82      A    C  
ANISOU 2453  CE2 PHE A 315    13499  10898  11252  -1027  -2877   2071  A    C  
ATOM   2454  CZ  PHE A 315      55.600 -10.901   9.679  1.00 93.15      A    C  
ANISOU 2454  CZ  PHE A 315    13606  10653  11132  -1151  -2789   2142  A    C  
ATOM   2455  N   TRP A 316      59.132  -7.178  15.055  1.00101.16      A    N  
ANISOU 2455  N   TRP A 316    14768  12403  11266  -1438  -3231   2226  A    N  
ATOM   2456  CA  TRP A 316      59.638  -6.053  15.834  1.00106.41      A    C  
ANISOU 2456  CA  TRP A 316    15393  13247  11792  -1538  -3258   2147  A    C  
ATOM   2457  C   TRP A 316      60.670  -6.504  16.884  1.00113.19      A    C  
ANISOU 2457  C   TRP A 316    16330  14191  12484  -1461  -3517   2226  A    C  
ATOM   2458  O   TRP A 316      60.690  -6.016  18.017  1.00107.15      A    O  
ANISOU 2458  O   TRP A 316    15675  13528  11511  -1567  -3548   2228  A    O  
ATOM   2459  CB  TRP A 316      58.472  -5.306  16.485  1.00105.44      A    C  
ANISOU 2459  CB  TRP A 316    15407  13125  11529  -1746  -3051   2130  A    C  
ATOM   2460  CG  TRP A 316      57.378  -4.947  15.521  1.00105.81      A    C  
ANISOU 2460  CG  TRP A 316    15390  13096  11716  -1808  -2799   2069  A    C  
ATOM   2461  CD1 TRP A 316      56.159  -5.535  15.420  1.00108.66      A    C  
ANISOU 2461  CD1 TRP A 316    15883  13323  12081  -1864  -2659   2144  A    C  
ATOM   2462  CD2 TRP A 316      57.409  -3.918  14.519  1.00107.56      A    C  
ANISOU 2462  CD2 TRP A 316    15392  13383  12091  -1814  -2657   1921  A    C  
ATOM   2463  CE2 TRP A 316      56.171  -3.945  13.857  1.00102.86      A    C  
ANISOU 2463  CE2 TRP A 316    14810  12701  11571  -1859  -2440   1915  A    C  
ATOM   2464  CE3 TRP A 316      58.365  -2.978  14.124  1.00103.99      A    C  
ANISOU 2464  CE3 TRP A 316    14733  13058  11721  -1785  -2687   1798  A    C  
ATOM   2465  NE1 TRP A 316      55.425  -4.941  14.423  1.00104.32      A    N  
ANISOU 2465  NE1 TRP A 316    15204  12768  11667  -1897  -2448   2045  A    N  
ATOM   2466  CZ2 TRP A 316      55.865  -3.073  12.822  1.00100.40      A    C  
ANISOU 2466  CZ2 TRP A 316    14318  12430  11397  -1856  -2257   1799  A    C  
ATOM   2467  CZ3 TRP A 316      58.056  -2.117  13.098  1.00 97.75      A    C  
ANISOU 2467  CZ3 TRP A 316    13772  12287  11080  -1793  -2493   1691  A    C  
ATOM   2468  CH2 TRP A 316      56.822  -2.171  12.454  1.00 99.56      A    C  
ANISOU 2468  CH2 TRP A 316    14025  12435  11367  -1818  -2283   1696  A    C  
ATOM   2469  N   SER A 317      61.521  -7.445  16.481  1.00118.01      A    N  
ANISOU 2469  N   SER A 317    16884  14770  13184  -1262  -3702   2287  A    N  
ATOM   2470  CA  SER A 317      62.575  -7.983  17.325  1.00120.24      A    C  
ANISOU 2470  CA  SER A 317    17218  15141  13327  -1142  -3960   2370  A    C  
ATOM   2471  C   SER A 317      63.868  -8.005  16.528  1.00125.40      A    C  
ANISOU 2471  C   SER A 317    17615  15896  14136   -965  -4117   2296  A    C  
ATOM   2472  O   SER A 317      63.847  -7.999  15.299  1.00122.88      A    O  
ANISOU 2472  O   SER A 317    17133  15520  14034   -899  -4035   2230  A    O  
ATOM   2473  CB  SER A 317      62.239  -9.411  17.747  1.00122.64      A    C  
ANISOU 2473  CB  SER A 317    17763  15270  13565  -1042  -4034   2572  A    C  
ATOM   2474  OG  SER A 317      61.019  -9.458  18.458  1.00125.24      A    O  
ANISOU 2474  OG  SER A 317    18325  15502  13759  -1206  -3877   2655  A    O  
ATOM   2475  N   ASP A 318      64.998  -8.027  17.221  1.00131.60      A    N  
ANISOU 2475  N   ASP A 318    18355  16845  14803   -881  -4343   2305  A    N  
ATOM   2476  CA  ASP A 318      66.264  -8.227  16.543  1.00133.67      A    C  
ANISOU 2476  CA  ASP A 318    18383  17206  15198   -690  -4513   2260  A    C  
ATOM   2477  C   ASP A 318      66.339  -9.704  16.177  1.00126.52      A    C  
ANISOU 2477  C   ASP A 318    17582  16132  14358   -471  -4612   2411  A    C  
ATOM   2478  O   ASP A 318      66.026 -10.565  17.002  1.00130.21      A    O  
ANISOU 2478  O   ASP A 318    18297  16501  14675   -435  -4678   2570  A    O  
ATOM   2479  CB  ASP A 318      67.426  -7.799  17.442  1.00144.42      A    C  
ANISOU 2479  CB  ASP A 318    19657  18814  16404   -671  -4729   2216  A    C  
ATOM   2480  CG  ASP A 318      67.364  -6.318  17.805  1.00149.52      A    C  
ANISOU 2480  CG  ASP A 318    20204  19610  16999   -900  -4628   2045  A    C  
ATOM   2481  OD1 ASP A 318      66.695  -5.548  17.075  1.00143.12      A    O  
ANISOU 2481  OD1 ASP A 318    19319  18733  16329  -1029  -4400   1947  A    O  
ATOM   2482  OD2 ASP A 318      67.988  -5.925  18.816  1.00155.47      A    O1-
ANISOU 2482  OD2 ASP A 318    20955  20548  17569   -944  -4777   2005  A    O1-
ATOM   2483  N   PRO A 319      66.717 -10.006  14.926  1.00114.55      A    N  
ANISOU 2483  N   PRO A 319    15885  14572  13068   -322  -4610   2365  A    N  
ATOM   2484  CA  PRO A 319      67.120  -9.067  13.871  1.00111.12      A    C  
ANISOU 2484  CA  PRO A 319    15154  14249  12818   -338  -4523   2198  A    C  
ATOM   2485  C   PRO A 319      65.921  -8.466  13.147  1.00109.54      A    C  
ANISOU 2485  C   PRO A 319    14951  13940  12730   -494  -4243   2123  A    C  
ATOM   2486  O   PRO A 319      64.934  -9.164  12.919  1.00106.36      A    O  
ANISOU 2486  O   PRO A 319    14714  13342  12356   -500  -4141   2195  A    O  
ATOM   2487  CB  PRO A 319      67.892  -9.952  12.881  1.00111.06      A    C  
ANISOU 2487  CB  PRO A 319    15011  14209  12979    -72  -4641   2222  A    C  
ATOM   2488  CG  PRO A 319      67.724 -11.402  13.382  1.00113.03      A    C  
ANISOU 2488  CG  PRO A 319    15518  14283  13146     71  -4765   2401  A    C  
ATOM   2489  CD  PRO A 319      66.664 -11.391  14.433  1.00110.53      A    C  
ANISOU 2489  CD  PRO A 319    15478  13868  12649   -121  -4673   2485  A    C  
ATOM   2490  N   MET A 320      66.019  -7.193  12.774  1.00110.89      A    N  
ANISOU 2490  N   MET A 320    14931  14236  12967   -614  -4119   1980  A    N  
ATOM   2491  CA  MET A 320      64.943  -6.510  12.061  1.00106.80      A    C  
ANISOU 2491  CA  MET A 320    14390  13642  12549   -744  -3849   1905  A    C  
ATOM   2492  C   MET A 320      64.834  -6.970  10.617  1.00114.32      A    C  
ANISOU 2492  C   MET A 320    15209  14511  13716   -587  -3776   1883  A    C  
ATOM   2493  O   MET A 320      65.818  -7.400  10.021  1.00123.79      A    O  
ANISOU 2493  O   MET A 320    16250  15764  15019   -395  -3913   1878  A    O  
ATOM   2494  CB  MET A 320      65.139  -4.995  12.103  1.00105.95      A    C  
ANISOU 2494  CB  MET A 320    14124  13682  12449   -906  -3734   1766  A    C  
ATOM   2495  CG  MET A 320      64.749  -4.384  13.425  1.00111.29      A    C  
ANISOU 2495  CG  MET A 320    14969  14403  12914  -1109  -3717   1759  A    C  
ATOM   2496  SD  MET A 320      63.144  -4.988  13.982  1.00110.56      A    S  
ANISOU 2496  SD  MET A 320    15199  14119  12689  -1214  -3578   1876  A    S  
ATOM   2497  CE  MET A 320      62.121  -3.557  13.641  1.00 70.73      A    C  
ANISOU 2497  CE  MET A 320    10109   9079   7685  -1420  -3266   1749  A    C  
ATOM   2498  N   PRO A 321      63.628  -6.877  10.045  1.00111.92      A    N  
ANISOU 2498  N   PRO A 321    14962  14089  13474   -662  -3561   1864  A    N  
ATOM   2499  CA  PRO A 321      63.496  -7.288   8.648  1.00112.14      A    C  
ANISOU 2499  CA  PRO A 321    14857  14057  13696   -507  -3492   1826  A    C  
ATOM   2500  C   PRO A 321      64.471  -6.517   7.758  1.00106.32      A    C  
ANISOU 2500  C   PRO A 321    13820  13480  13095   -412  -3483   1726  A    C  
ATOM   2501  O   PRO A 321      64.567  -5.291   7.834  1.00 94.79      A    O  
ANISOU 2501  O   PRO A 321    12250  12132  11632   -541  -3371   1648  A    O  
ATOM   2502  CB  PRO A 321      62.042  -6.933   8.314  1.00113.60      A    C  
ANISOU 2502  CB  PRO A 321    15119  14150  13894   -647  -3241   1794  A    C  
ATOM   2503  CG  PRO A 321      61.338  -6.921   9.639  1.00113.43      A    C  
ANISOU 2503  CG  PRO A 321    15346  14072  13678   -836  -3225   1867  A    C  
ATOM   2504  CD  PRO A 321      62.351  -6.424  10.623  1.00112.14      A    C  
ANISOU 2504  CD  PRO A 321    15167  14048  13392   -875  -3377   1871  A    C  
ATOM   2505  N   SER A 322      65.196  -7.255   6.927  1.00110.71      A    N  
ANISOU 2505  N   SER A 322    14250  14041  13774   -184  -3597   1732  A    N  
ATOM   2506  CA  SER A 322      66.174  -6.672   6.028  1.00111.84      A    C  
ANISOU 2506  CA  SER A 322    14103  14339  14054    -67  -3596   1654  A    C  
ATOM   2507  C   SER A 322      65.679  -6.815   4.604  1.00105.44      A    C  
ANISOU 2507  C   SER A 322    13180  13483  13399     59  -3446   1603  A    C  
ATOM   2508  O   SER A 322      64.907  -7.724   4.313  1.00 93.23      A    O  
ANISOU 2508  O   SER A 322    11770  11786  11867    115  -3431   1632  A    O  
ATOM   2509  CB  SER A 322      67.507  -7.413   6.158  1.00113.09      A    C  
ANISOU 2509  CB  SER A 322    14178  14571  14220    129  -3854   1698  A    C  
ATOM   2510  OG  SER A 322      67.427  -8.723   5.605  1.00109.99      A    O  
ANISOU 2510  OG  SER A 322    13857  14047  13888    335  -3941   1751  A    O  
ATOM   2511  N   ASP A 323      66.150  -5.943   3.716  1.00106.15      A    N  
ANISOU 2511  N   ASP A 323    13019  13707  13606    108  -3337   1527  A    N  
ATOM   2512  CA  ASP A 323      65.839  -6.071   2.302  1.00108.61      A    C  
ANISOU 2512  CA  ASP A 323    13196  14013  14057    266  -3210   1480  A    C  
ATOM   2513  C   ASP A 323      66.444  -7.341   1.711  1.00109.12      A    C  
ANISOU 2513  C   ASP A 323    13226  14041  14191    527  -3387   1504  A    C  
ATOM   2514  O   ASP A 323      67.156  -8.074   2.393  1.00116.57      A    O  
ANISOU 2514  O   ASP A 323    14243  14968  15082    591  -3603   1566  A    O  
ATOM   2515  CB  ASP A 323      66.254  -4.817   1.531  1.00119.84      A    C  
ANISOU 2515  CB  ASP A 323    14362  15591  15580    266  -3044   1412  A    C  
ATOM   2516  CG  ASP A 323      65.115  -3.796   1.422  1.00131.01      A    C  
ANISOU 2516  CG  ASP A 323    15819  16984  16976     92  -2778   1372  A    C  
ATOM   2517  OD1 ASP A 323      63.928  -4.199   1.537  1.00134.12      A    O  
ANISOU 2517  OD1 ASP A 323    16394  17255  17310     30  -2705   1383  A    O  
ATOM   2518  OD2 ASP A 323      65.403  -2.594   1.213  1.00131.32      A    O1-
ANISOU 2518  OD2 ASP A 323    15708  17125  17063     20  -2635   1333  A    O1-
ATOM   2519  N   LEU A 324      66.129  -7.622   0.452  1.00112.77      A    N  
ANISOU 2519  N   LEU A 324    13588  14493  14765    688  -3293   1453  A    N  
ATOM   2520  CA  LEU A 324      66.547  -8.877  -0.169  1.00118.49      A    C  
ANISOU 2520  CA  LEU A 324    14304  15159  15557    940  -3444   1459  A    C  
ATOM   2521  C   LEU A 324      67.517  -8.657  -1.329  1.00127.51      A    C  
ANISOU 2521  C   LEU A 324    15159  16466  16823   1168  -3440   1411  A    C  
ATOM   2522  O   LEU A 324      67.234  -7.923  -2.281  1.00117.17      A    O  
ANISOU 2522  O   LEU A 324    13690  15247  15584   1196  -3250   1350  A    O  
ATOM   2523  CB  LEU A 324      65.339  -9.716  -0.605  1.00114.94      A    C  
ANISOU 2523  CB  LEU A 324    14015  14533  15125    958  -3380   1433  A    C  
ATOM   2524  CG  LEU A 324      64.595 -10.494   0.495  1.00109.86      A    C  
ANISOU 2524  CG  LEU A 324    13675  13688  14380    810  -3453   1506  A    C  
ATOM   2525  CD1 LEU A 324      64.020  -9.551   1.530  1.00113.37      A    C  
ANISOU 2525  CD1 LEU A 324    14222  14150  14703    531  -3347   1538  A    C  
ATOM   2526  CD2 LEU A 324      63.489 -11.389  -0.067  1.00 96.96      A    C  
ANISOU 2526  CD2 LEU A 324    12166  11880  12793    838  -3393   1465  A    C  
ATOM   2527  N   LYS A 325      68.677  -9.293  -1.209  1.00145.98      A    N  
ANISOU 2527  N   LYS A 325    17434  18852  19178   1339  -3649   1448  A    N  
ATOM   2528  CA  LYS A 325      69.772  -9.156  -2.159  1.00155.09      A    C  
ANISOU 2528  CA  LYS A 325    18311  20178  20438   1563  -3675   1417  A    C  
ATOM   2529  C   LYS A 325      70.489 -10.498  -2.234  1.00156.39      A    C  
ANISOU 2529  C   LYS A 325    18514  20289  20618   1813  -3906   1450  A    C  
ATOM   2530  O   LYS A 325      71.315 -10.733  -3.117  1.00157.23      A    O  
ANISOU 2530  O   LYS A 325    18422  20508  20811   2055  -3951   1424  A    O  
ATOM   2531  CB  LYS A 325      70.757  -8.073  -1.702  1.00157.73      A    C  
ANISOU 2531  CB  LYS A 325    18458  20702  20770   1463  -3681   1429  A    C  
ATOM   2532  CG  LYS A 325      70.190  -6.655  -1.633  1.00158.86      A    C  
ANISOU 2532  CG  LYS A 325    18550  20897  20912   1224  -3447   1395  A    C  
ATOM   2533  CD  LYS A 325      71.241  -5.678  -1.102  1.00161.77      A    C  
ANISOU 2533  CD  LYS A 325    18743  21433  21290   1114  -3476   1395  A    C  
ATOM   2534  CE  LYS A 325      70.731  -4.242  -1.064  1.00161.40      A    C  
ANISOU 2534  CE  LYS A 325    18648  21420  21257    884  -3233   1356  A    C  
ATOM   2535  NZ  LYS A 325      71.746  -3.327  -0.470  1.00163.36      A    N1+
ANISOU 2535  NZ  LYS A 325    18738  21811  21522    751  -3271   1340  A    N1+
ATOM   2536  N   GLY A 326      70.173 -11.372  -1.285  1.00152.18      A    N  
ANISOU 2536  N   GLY A 326    18242  19582  19998   1759  -4045   1514  A    N  
ATOM   2537  CA  GLY A 326      70.666 -12.731  -1.319  1.00149.02      A    C  
ANISOU 2537  CA  GLY A 326    17931  19079  19610   1992  -4247   1553  A    C  
ATOM   2538  C   GLY A 326      69.934 -13.527  -2.380  1.00151.18      A    C  
ANISOU 2538  C   GLY A 326    18258  19212  19971   2138  -4181   1482  A    C  
ATOM   2539  O   GLY A 326      69.491 -14.645  -2.129  1.00147.97      A    O  
ANISOU 2539  O   GLY A 326    18077  18591  19554   2182  -4270   1509  A    O  
ATOM   2540  N   MET A 327      69.804 -12.945  -3.569  1.00157.78      A    N  
ANISOU 2540  N   MET A 327    18886  20169  20893   2215  -4022   1390  A    N  
ATOM   2541  CA  MET A 327      69.094 -13.587  -4.671  1.00166.37      A    C  
ANISOU 2541  CA  MET A 327    19993  21164  22057   2357  -3949   1296  A    C  
ATOM   2542  C   MET A 327      68.985 -12.667  -5.886  1.00163.85      A    C  
ANISOU 2542  C   MET A 327    19421  21032  21802   2422  -3750   1209  A    C  
ATOM   2543  O   MET A 327      69.663 -12.872  -6.893  1.00162.05      A    O  
ANISOU 2543  O   MET A 327    19005  20920  21646   2680  -3770   1162  A    O  
ATOM   2544  CB  MET A 327      67.703 -14.051  -4.218  1.00173.74      A    C  
ANISOU 2544  CB  MET A 327    21200  21863  22951   2166  -3890   1288  A    C  
ATOM   2545  CG  MET A 327      66.951 -13.050  -3.342  1.00172.78      A    C  
ANISOU 2545  CG  MET A 327    21160  21749  22739   1845  -3756   1329  A    C  
ATOM   2546  SD  MET A 327      65.902 -13.842  -2.098  1.00299.29      A    S  
ANISOU 2546  SD  MET A 327    37551  37493  38673   1622  -3804   1403  A    S  
ATOM   2547  CE  MET A 327      67.093 -14.483  -0.907  1.00 87.31      A    C  
ANISOU 2547  CE  MET A 327    10813  10610  11750   1689  -4067   1543  A    C  
TER   
CONECT 1381 1391
CONECT 1391 1381 1392
CONECT 1392 1391 1393 1395
CONECT 1393 1392 1394 1402
CONECT 1394 1393
CONECT 1395 1392 1396 1397
CONECT 1396 1395
CONECT 1397 1395 1398
CONECT 1398 1397 1399 1400 1401
CONECT 1399 1398
CONECT 1400 1398
CONECT 1401 1398
CONECT 1402 1393
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.