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***  3blh_a_vs_3lq5_a  ***

elNémo ID: 22051215591366107

Job options:

ID        	=	 22051215591366107
JOBID     	=	 3blh_a_vs_3lq5_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_3lq5_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   
HETATM 2366  N   TRS B 260      12.851   1.543 -16.890  1.00 72.25      C    N  
HETATM 2367  C   TRS B 260      11.898   1.666 -17.985  1.00 74.78      C    C  
HETATM 2368  C1  TRS B 260      11.292   3.076 -17.931  1.00 88.90      C    C  
HETATM 2369  O1  TRS B 260      11.282   3.644 -16.637  1.00 92.56      C    O  
HETATM 2370  C2  TRS B 260      12.627   1.513 -19.312  1.00 71.54      C    C  
HETATM 2371  O2  TRS B 260      12.052   2.330 -20.303  1.00 67.41      C    O  
HETATM 2372  C3  TRS B 260      10.924   0.504 -17.749  1.00 81.60      C    C  
HETATM 2373  O3  TRS B 260      10.829   0.150 -16.374  1.00 69.96      C    O  
HETATM 2374  O   HOH A 331      42.052 -19.542   0.836  1.00 61.27      D    O  
HETATM 2375  O   HOH A 332      59.676  -6.244  -7.029  1.00 63.68      D    O  
HETATM 2376  O   HOH A 333      41.851 -17.269  -5.989  1.00 47.71      D    O  
HETATM 2377  O   HOH A 334      53.214  -8.452  -9.576  1.00 61.90      D    O  
HETATM 2378  O   HOH A 335      48.924  -1.543   2.892  1.00 61.06      D    O  
HETATM 2379  O   HOH A 336      48.219  -5.216  -7.390  1.00 53.37      D    O  
HETATM 2380  O   HOH A 337      57.943  -2.371 -20.677  1.00 56.74      D    O  
HETATM 2381  O   HOH A 338      43.788 -18.085 -14.312  1.00 66.21      D    O  
HETATM 2382  O   HOH A 339      23.567 -22.198 -24.411  1.00 59.32      D    O  
HETATM 2383  O   HOH A 340      46.186  -4.388 -23.953  1.00 56.81      D    O  
HETATM 2384  O   HOH A 341      48.210 -14.805 -10.804  1.00 44.05      D    O  
HETATM 2385  O   HOH A 342      57.150  -4.244  12.272  1.00 56.06      D    O  
HETATM 2386  O   HOH A 343      53.311  -5.736  11.352  1.00 53.65      D    O  
HETATM 2387  O   HOH A 344      45.262 -14.171 -10.855  1.00 43.77      D    O  
HETATM 2388  O   HOH A 345      41.223 -10.105   7.583  1.00 53.20      D    O  
HETATM 2389  O   HOH A 346      37.857 -15.374  -9.623  1.00 63.19      D    O  
HETATM 2390  O   HOH A 347      52.048  -5.606  -7.606  1.00 57.64      D    O  
HETATM 2391  O   HOH A 348      32.609 -12.274  -7.587  1.00 35.64      D    O  
HETATM 2392  O   HOH A 349      59.864  -5.370   1.470  1.00 77.98      D    O  
HETATM 2393  O   HOH A 350      63.618  -0.464 -27.806  1.00 61.77      D    O  
HETATM 2394  O   HOH A 351      50.452  -0.688  -1.675  1.00 53.47      D    O  
HETATM 2395  O   HOH A 352      56.360 -14.412 -29.461  1.00 70.36      D    O  
HETATM 2396  O   HOH A 353      36.201  -6.091   4.933  1.00 72.23      D    O  
HETATM 2397  O   HOH A 354      57.295  -4.744  -6.637  1.00 73.03      D    O  
HETATM 2398  O   HOH A 355      31.510 -16.319  -8.541  1.00 70.64      D    O  
HETATM 2399  O   HOH A 356      54.556  -3.246 -15.032  1.00 70.01      D    O  
HETATM 2400  O   HOH A 357      53.872  -2.066 -17.419  1.00 71.79      D    O  
HETATM 2401  O   HOH A 358      62.643 -19.414  15.468  1.00 69.04      D    O  
HETATM 2402  O   HOH A 359      41.391  -7.139   9.425  1.00 63.29      D    O  
HETATM 2403  O   HOH A 360      48.647  -3.845 -31.313  1.00 60.00      D    O  
HETATM 2404  O   HOH A 361      50.688  -4.724 -29.553  1.00 66.16      D    O  
HETATM 2405  O   HOH A 362      44.684 -40.111  11.135  1.00 77.16      D    O  
HETATM 2406  O   HOH A 363      62.867 -17.728 -15.388  1.00 78.43      D    O  
HETATM 2407  O   HOH A 364      25.667 -18.542 -19.911  1.00 42.91      D    O  
HETATM 2408  O   HOH A 365      25.237 -20.276 -17.969  1.00 56.61      D    O  
HETATM 2409  O   HOH A 366      42.729  -4.812 -23.079  1.00 54.94      D    O  
HETATM 2410  O   HOH A 367      46.367  -6.662 -10.379  1.00 56.64      D    O  
HETATM 2411  O   HOH A 368      40.978 -10.663  15.414  1.00 64.69      D    O  
HETATM 2412  O   HOH A 369      44.158 -23.654  18.556  1.00 78.79      D    O  
HETATM 2413  O   HOH A 370      53.747 -31.792  10.174  1.00 78.98      D    O  
HETATM 2414  O   HOH A 371      53.807 -25.998  -0.111  1.00 83.53      D    O  
HETATM 2415  O   HOH A 372      37.096   4.595 -33.829  1.00 69.22      D    O  
HETATM 2416  O   HOH A 373      36.272   5.925 -36.371  1.00 81.40      D    O  
HETATM 2417  O   HOH A 374      64.715 -19.929  10.926  1.00 85.82      D    O  
HETATM 2418  O   HOH A 375      44.764 -18.726 -30.592  1.00 78.13      D    O  
HETATM 2419  O   HOH A 376      51.053  -9.618  20.577  1.00 64.72      D    O  
HETATM 2420  O   HOH A 377      54.926 -14.908 -12.731  1.00 64.25      D    O  
HETATM 2421  O   HOH A 378      56.058  -4.732   0.813  1.00 64.29      D    O  
HETATM 2422  O   HOH A 379      36.758  -3.420 -15.007  1.00 60.06      D    O  
HETATM 2423  O   HOH A 380      51.331 -14.351 -11.811  1.00 73.12      D    O  
HETATM 2424  O   HOH A 381      39.502 -12.230   8.692  1.00 61.03      D    O  
HETATM 2425  O   HOH A 382      39.930 -14.230  10.541  1.00 62.69      D    O  
HETATM 2426  O   HOH A 383      36.632  -1.789  -3.100  1.00 53.77      D    O  
HETATM 2427  O   HOH A 384      34.469  -6.044  -4.460  1.00 65.11      D    O  
HETATM 2428  O   HOH B 261      24.490 -14.266 -19.708  1.00 42.25      E    O  
HETATM 2429  O   HOH B 262      17.225  21.002  -6.416  1.00 58.34      E    O  
HETATM 2430  O   HOH B 263      31.447   6.228 -20.098  1.00 42.78      E    O  
HETATM 2431  O   HOH B 264      39.607  -1.403 -28.162  1.00 61.15      E    O  
HETATM 2432  O   HOH B 265      34.123   0.134 -20.823  1.00 53.84      E    O  
HETATM 2433  O   HOH B 266      29.405   6.989 -16.837  1.00 54.83      E    O  
HETATM 2434  O   HOH B 267      18.719 -18.659 -15.310  1.00 59.81      E    O  
HETATM 2435  O   HOH B 268       7.999 -10.906 -37.100  1.00 60.18      E    O  
HETATM 2436  O   HOH B 269      29.952  -3.894 -13.786  1.00 46.91      E    O  
HETATM 2437  O   HOH B 270      33.066  -0.160 -36.599  1.00 50.65      E    O  
HETATM 2438  O   HOH B 271       6.559  11.587 -22.084  1.00 48.93      E    O  
HETATM 2439  O   HOH B 272      32.897 -14.704 -26.546  1.00 50.80      E    O  
HETATM 2440  O   HOH B 273      18.699  -3.579 -10.336  1.00 46.89      E    O  
HETATM 2441  O   HOH B 274      31.231  14.824 -14.636  1.00 56.72      E    O  
HETATM 2442  O   HOH B 275      28.907   5.938 -33.479  1.00 52.42      E    O  
HETATM 2443  O   HOH B 276      14.196   2.157 -13.462  1.00 61.13      E    O  
HETATM 2444  O   HOH B 277       2.992  15.318 -11.755  1.00 46.51      E    O  
HETATM 2445  O   HOH B 278      21.347   0.402 -12.094  1.00 60.06      E    O  
HETATM 2446  O   HOH B 279       7.233  19.107 -18.780  1.00 49.41      E    O  
HETATM 2447  O   HOH B 280      13.222  -0.504 -13.652  1.00 44.64      E    O  
HETATM 2448  O   HOH B 281      21.443  -7.566 -10.358  1.00 54.16      E    O  
HETATM 2449  O   HOH B 282      19.342  -0.596 -10.182  1.00 58.57      E    O  
HETATM 2450  O   HOH B 283       0.104   8.931 -14.214  1.00 55.69      E    O  
HETATM 2451  O   HOH B 284      33.178  19.835 -27.454  1.00 68.60      E    O  
HETATM 2452  O   HOH B 285      22.763 -19.715 -16.729  1.00 55.03      E    O  
HETATM 2453  O   HOH B 286       7.350  -6.632 -24.696  1.00 55.24      E    O  
HETATM 2454  O   HOH B 287      32.091 -10.830 -12.627  1.00 62.33      E    O  
HETATM 2455  O   HOH B 288      17.261  11.614 -32.266  1.00 67.50      E    O  
HETATM 2456  O   HOH B 289       6.601  12.323  -8.905  1.00 75.61      E    O  
HETATM 2457  O   HOH B 290      16.215  23.830 -15.977  1.00 73.40      E    O  
HETATM 2458  O   HOH B 291      14.270  21.716 -16.354  1.00 62.21      E    O  
HETATM 2459  O   HOH B 292      11.356  22.010 -14.966  1.00 61.51      E    O  
HETATM 2460  O   HOH B 293      29.022   4.467 -16.188  1.00 55.00      E    O  
HETATM 2461  O   HOH B 294       7.591 -11.748 -29.155  1.00 55.45      E    O  
HETATM 2462  O   HOH B 295      14.529 -16.671 -16.582  1.00 46.53      E    O  
HETATM 2463  O   HOH B 296       0.296  16.866 -11.508  1.00 58.76      E    O  
HETATM 2464  O   HOH B 297      18.670 -14.183 -32.295  1.00 65.02      E    O  
HETATM 2465  O   HOH B 298       4.427  15.442  -9.313  1.00 62.18      E    O  
HETATM 2466  O   HOH B 299      30.791 -12.912 -11.884  1.00 76.14      E    O  
HETATM 2467  O   HOH B 300      21.137  -7.570 -37.002  1.00 63.89      E    O  
HETATM 2468  O   HOH B 301      -3.346  15.926 -11.386  1.00 57.30      E    O  
HETATM 2469  O   HOH B 302      17.023  17.200 -25.101  1.00 59.95      E    O  
HETATM 2470  O   HOH B 303      13.773 -16.616 -14.043  1.00 54.00      E    O  
HETATM 2471  O   HOH B 304      15.722  16.544 -27.407  1.00 69.81      E    O  
HETATM 2472  O   HOH B 305      21.510 -16.727 -13.586  1.00 58.27      E    O  
HETATM 2473  O   HOH B 306      22.232  13.213 -25.351  1.00 61.86      E    O  
HETATM 2474  O   HOH B 307      21.295 -12.476 -31.620  1.00 60.27      E    O  
HETATM 2475  O   HOH B 308       3.891  10.754 -21.148  1.00 38.43      E    O  
HETATM 2476  O   HOH B 309       9.370  -6.954 -22.129  1.00 40.99      E    O  
HETATM 2477  O   HOH B 310      23.044   8.341 -18.284  1.00 43.61      E    O  
HETATM 2478  O   HOH B 311      21.346  -0.136 -35.933  1.00 59.39      E    O  
HETATM 2479  O   HOH B 312      19.322  -5.756 -37.872  1.00 91.68      E    O  
HETATM 2480  O   HOH B 313      25.906   4.744 -15.878  1.00 46.91      E    O  
HETATM 2481  O   HOH B 314      15.326  21.403  -4.785  1.00 68.12      E    O  
HETATM 2482  O   HOH B 315      32.187  -9.695 -37.298  1.00 72.56      E    O  
HETATM 2483  O   HOH B 316      24.944   7.325 -16.497  1.00 47.32      E    O  
HETATM 2484  O   HOH B 317      23.419   7.866 -20.846  1.00 43.43      E    O  
HETATM 2485  O   HOH B 318      19.897  -2.475 -35.590  1.00 52.55      E    O  
HETATM 2486  O   HOH B 319      21.946   0.219 -38.584  1.00 74.84      E    O  
HETATM 2487  O   HOH B 320      39.027   0.421 -20.952  1.00 58.77      E    O  
HETATM 2488  O   HOH B 321      36.995   6.441 -18.458  1.00 55.77      E    O  
HETATM 2489  O   HOH B 322      16.933 -14.049 -13.529  1.00 62.01      E    O  
HETATM 2490  O   HOH B 323       7.052   5.046 -22.213  1.00 62.21      E    O  
HETATM 2491  O   HOH B 324      20.655   7.182 -25.199  1.00 49.95      E    O  
HETATM 2492  O   HOH B 325      33.165   5.684 -14.301  1.00 70.06      E    O  
HETATM 2493  O   HOH B 326      31.588   3.465 -15.003  1.00 64.46      E    O  
HETATM 2494  O   HOH B 327      33.760   1.991 -16.208  1.00 55.13      E    O  
HETATM 2495  O   HOH B 328      20.503 -10.458 -33.207  1.00 56.53      E    O  
HETATM 2496  O   HOH B 329      18.041  -9.340 -36.628  1.00 78.29      E    O  
HETATM 2497  O   HOH B 330      23.828  27.762  -5.500  1.00 84.46      E    O  
HETATM 2498  O   HOH B 331      42.728   6.289 -23.187  1.00 63.15      E    O  
HETATM 2499  O   HOH B 332      28.301  -4.541 -10.375  1.00 72.23      E    O  
HETATM 2500  O   HOH B 333      34.978   4.662 -16.280  1.00 63.23      E    O  
HETATM 2501  O   HOH B 334      17.165  -7.170 -37.334  1.00 66.97      E    O  
HETATM 2502  O   HOH B 335      35.617   8.780 -34.009  1.00 60.03      E    O  
HETATM 2503  O   HOH B 336      27.286  -2.082 -11.778  1.00 67.88      E    O  
HETATM 2504  O   HOH B 337      26.359  -4.679  -7.644  1.00 81.40      E    O  
HETATM 2505  O   HOH B 338      -1.425  17.692  -9.248  1.00 69.00      E    O  
HETATM 2506  O   HOH B 339      11.595   0.883 -22.452  1.00 60.34      E    O  
HETATM 2507  O   HOH B 340       9.551  -2.520 -22.159  1.00 65.65      E    O  
HETATM 2508  O   HOH B 341       9.006  -1.181 -15.274  1.00 75.09      E    O  
HETATM 2509  O   HOH B 342      11.097  -1.256 -23.709  1.00 73.43      E    O  
HETATM 2510  O   HOH B 343       7.807  -4.669 -22.683  1.00 60.40      E    O  
HETATM 2511  O   HOH B 344       7.954  -9.188 -29.767  1.00 63.18      E    O  
HETATM 2512  O   HOH B 345      36.827  -4.174 -11.011  1.00 47.54      E    O  
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
CONECT 2366 2367
CONECT 2367 2366 2368 2370 2372
CONECT 2368 2367 2369
CONECT 2369 2368
CONECT 2370 2367 2371
CONECT 2371 2370
CONECT 2372 2367 2373
CONECT 2373 2372
END


A second structure was input as follows:


CRYST1  173.249  173.249   99.241  90.00  90.00 120.00 H 3           9
ATOM      1  N   ASP A   6      37.845  -7.152 -44.022  1.00181.97      A    N  
ANISOU    1  N   ASP A   6    21825  26992  20322   1019    797  -1354  A    N  
ATOM      2  CA  ASP A   6      37.841  -5.896 -43.274  1.00181.21      A    C  
ANISOU    2  CA  ASP A   6    21729  26814  20307    954    808  -1106  A    C  
ATOM      3  C   ASP A   6      38.294  -6.078 -41.823  1.00174.48      A    C  
ANISOU    3  C   ASP A   6    20882  25712  19702    920    799  -1080  A    C  
ATOM      4  O   ASP A   6      38.202  -7.173 -41.262  1.00173.56      A    O  
ANISOU    4  O   ASP A   6    20785  25448  19711    936    751  -1238  A    O  
ATOM      5  CB  ASP A   6      36.465  -5.213 -43.342  1.00184.76      A    C  
ANISOU    5  CB  ASP A   6    22222  27270  20707    904    724  -1002  A    C  
ATOM      6  CG  ASP A   6      35.311  -6.166 -43.040  1.00187.14      A    C  
ANISOU    6  CG  ASP A   6    22574  27453  21079    892    605  -1168  A    C  
ATOM      7  OD1 ASP A   6      35.565  -7.307 -42.597  1.00190.83      A    O  
ANISOU    7  OD1 ASP A   6    23048  27795  21663    914    588  -1346  A    O  
ATOM      8  OD2 ASP A   6      34.143  -5.768 -43.248  1.00182.49      A    O1-
ANISOU    8  OD2 ASP A   6    22010  26894  20432    861    531  -1116  A    O1-
ATOM      9  N   SER A   7      38.789  -4.995 -41.229  1.00164.48      A    N  
ANISOU    9  N   SER A   7    19594  24399  18501    871    847   -878  A    N  
ATOM     10  CA  SER A   7      39.338  -5.024 -39.877  1.00152.50      A    C  
ANISOU   10  CA  SER A   7    18071  22674  17198    836    845   -835  A    C  
ATOM     11  C   SER A   7      38.524  -4.120 -38.964  1.00147.64      A    C  
ANISOU   11  C   SER A   7    17499  21914  16682    752    791   -674  A    C  
ATOM     12  O   SER A   7      37.872  -3.188 -39.437  1.00147.18      A    O  
ANISOU   12  O   SER A   7    17455  21939  16527    721    790   -546  A    O  
ATOM     13  CB  SER A   7      40.799  -4.565 -39.897  1.00144.79      A    C  
ANISOU   13  CB  SER A   7    17019  21766  16227    849    957   -754  A    C  
ATOM     14  OG  SER A   7      41.326  -4.451 -38.588  1.00138.10      A    O  
ANISOU   14  OG  SER A   7    16160  20737  15574    808    950   -696  A    O  
ATOM     15  N   VAL A   8      38.563  -4.392 -37.660  1.00144.59      A    N  
ANISOU   15  N   VAL A   8    17132  21316  16488    717    749   -677  A    N  
ATOM     16  CA  VAL A   8      37.799  -3.597 -36.692  1.00137.41      A    C  
ANISOU   16  CA  VAL A   8    16267  20256  15685    636    700   -539  A    C  
ATOM     17  C   VAL A   8      38.688  -2.691 -35.838  1.00121.66      A    C  
ANISOU   17  C   VAL A   8    14240  18193  13794    583    757   -388  A    C  
ATOM     18  O   VAL A   8      39.790  -3.076 -35.449  1.00106.52      A    O  
ANISOU   18  O   VAL A   8    12276  16254  11944    604    795   -429  A    O  
ATOM     19  CB  VAL A   8      36.949  -4.478 -35.740  1.00 98.06      A    C  
ANISOU   19  CB  VAL A   8    11343  15071  10844    622    601   -641  A    C  
ATOM     20  CG1 VAL A   8      35.878  -3.636 -35.083  1.00 86.80      A    C  
ANISOU   20  CG1 VAL A   8     9967  13534   9478    547    551   -511  A    C  
ATOM     21  CG2 VAL A   8      36.319  -5.641 -36.487  1.00100.00      A    C  
ANISOU   21  CG2 VAL A   8    11610  15364  11021    678    550   -835  A    C  
ATOM     22  N   GLU A   9      38.180  -1.494 -35.546  1.00116.32      A    N  
ANISOU   22  N   GLU A   9    13583  17480  13131    513    762   -219  A    N  
ATOM     23  CA  GLU A   9      38.852  -0.509 -34.696  1.00104.26      A    C  
ANISOU   23  CA  GLU A   9    12031  15876  11708    445    811    -74  A    C  
ATOM     24  C   GLU A   9      38.980  -1.023 -33.262  1.00 98.32      A    C  
ANISOU   24  C   GLU A   9    11299  14923  11134    416    756   -122  A    C  
ATOM     25  O   GLU A   9      38.020  -1.562 -32.712  1.00101.25      A    O  
ANISOU   25  O   GLU A   9    11732  15169  11570    409    673   -182  A    O  
ATOM     26  CB  GLU A   9      38.031   0.785 -34.708  1.00110.26      A    C  
ANISOU   26  CB  GLU A   9    12822  16619  12451    380    820     99  A    C  
ATOM     27  CG  GLU A   9      38.655   1.967 -33.997  1.00120.22      A    C  
ANISOU   27  CG  GLU A   9    14057  17814  13806    301    884    255  A    C  
ATOM     28  CD  GLU A   9      39.869   2.502 -34.725  1.00137.54      A    C  
ANISOU   28  CD  GLU A   9    16172  20161  15926    312    996    321  A    C  
ATOM     29  OE1 GLU A   9      39.885   2.453 -35.976  1.00138.43      A    O  
ANISOU   29  OE1 GLU A   9    16265  20452  15881    368   1036    317  A    O  
ATOM     30  OE2 GLU A   9      40.808   2.971 -34.045  1.00147.26      A    O1-
ANISOU   30  OE2 GLU A   9    17358  21339  17255    263   1045    374  A    O1-
ATOM     31  N   CYS A  10      40.153  -0.860 -32.650  1.00 98.72      A    N  
ANISOU   31  N   CYS A  10    11295  14949  11264    399    801    -94  A    N  
ATOM     32  CA  CYS A  10      40.366  -1.343 -31.275  1.00 93.62      A    C  
ANISOU   32  CA  CYS A  10    10662  14131  10777    377    747   -132  A    C  
ATOM     33  C   CYS A  10      41.483  -0.626 -30.503  1.00100.56      A    C  
ANISOU   33  C   CYS A  10    11481  14987  11741    323    796    -42  A    C  
ATOM     34  O   CYS A  10      42.572  -1.171 -30.312  1.00114.85      A    O  
ANISOU   34  O   CYS A  10    13227  16824  13586    361    816   -100  A    O  
ATOM     35  CB  CYS A  10      40.617  -2.853 -31.261  1.00 75.86      A    C  
ANISOU   35  CB  CYS A  10     8409  11860   8554    462    708   -305  A    C  
ATOM     36  SG  CYS A  10      40.362  -3.563 -29.638  1.00135.17      A    S  
ANISOU   36  SG  CYS A  10    15967  19146  16244    444    622   -347  A    S  
ATOM     37  N   PRO A  11      41.194   0.589 -30.034  1.00 91.61      A    N  
ANISOU   37  N   PRO A  11    10365  13799  10646    233    814     95  A    N  
ATOM     38  CA  PRO A  11      42.077   1.540 -29.361  1.00 84.32      A    C  
ANISOU   38  CA  PRO A  11     9388  12853   9797    157    865    195  A    C  
ATOM     39  C   PRO A  11      42.600   1.096 -28.002  1.00 83.63      A    C  
ANISOU   39  C   PRO A  11     9290  12645   9841    136    814    152  A    C  
ATOM     40  O   PRO A  11      43.670   1.571 -27.621  1.00 79.32      A    O  
ANISOU   40  O   PRO A  11     8671  12127   9342     97    857    193  A    O  
ATOM     41  CB  PRO A  11      41.169   2.754 -29.150  1.00 89.16      A    C  
ANISOU   41  CB  PRO A  11    10056  13395  10427     72    875    326  A    C  
ATOM     42  CG  PRO A  11      40.130   2.623 -30.163  1.00 96.95      A    C  
ANISOU   42  CG  PRO A  11    11090  14444  11302    117    862    322  A    C  
ATOM     43  CD  PRO A  11      39.858   1.160 -30.222  1.00100.36      A    C  
ANISOU   43  CD  PRO A  11    11546  14864  11722    198    788    161  A    C  
ATOM     44  N   PHE A  12      41.870   0.251 -27.273  1.00 81.61      A    N  
ANISOU   44  N   PHE A  12     9101  12263   9644    157    725     77  A    N  
ATOM     45  CA  PHE A  12      42.306  -0.127 -25.928  1.00 68.21      A    C  
ANISOU   45  CA  PHE A  12     7398  10454   8063    138    674     52  A    C  
ATOM     46  C   PHE A  12      42.580  -1.612 -25.730  1.00 74.33      A    C  
ANISOU   46  C   PHE A  12     8167  11204   8869    233    623    -76  A    C  
ATOM     47  O   PHE A  12      42.485  -2.129 -24.610  1.00 70.85      A    O  
ANISOU   47  O   PHE A  12     7755  10643   8520    232    560   -100  A    O  
ATOM     48  CB  PHE A  12      41.296   0.295 -24.894  1.00 66.30      A    C  
ANISOU   48  CB  PHE A  12     7241  10057   7895     66    621    101  A    C  
ATOM     49  CG  PHE A  12      40.754   1.653 -25.106  1.00 73.86      A    C  
ANISOU   49  CG  PHE A  12     8221  11010   8831    -17    667    218  A    C  
ATOM     50  CD1 PHE A  12      41.590   2.721 -25.271  1.00 65.60      A    C  
ANISOU   50  CD1 PHE A  12     7110  10034   7782    -76    745    306  A    C  
ATOM     51  CD2 PHE A  12      39.393   1.870 -25.099  1.00 84.37      A    C  
ANISOU   51  CD2 PHE A  12     9638  12260  10159    -38    636    245  A    C  
ATOM     52  CE1 PHE A  12      41.076   3.977 -25.448  1.00 63.95      A    C  
ANISOU   52  CE1 PHE A  12     6924   9806   7568   -151    794    420  A    C  
ATOM     53  CE2 PHE A  12      38.881   3.129 -25.268  1.00 79.02      A    C  
ANISOU   53  CE2 PHE A  12     8980  11571   9474   -108    682    361  A    C  
ATOM     54  CZ  PHE A  12      39.726   4.179 -25.443  1.00 70.19      A    C  
ANISOU   54  CZ  PHE A  12     7801  10514   8354   -163    763    450  A    C  
ATOM     55  N   CYS A  13      42.908  -2.308 -26.807  1.00 75.01      A    N  
ANISOU   55  N   CYS A  13     8218  11400   8880    319    653   -156  A    N  
ATOM     56  CA  CYS A  13      43.363  -3.676 -26.667  1.00 79.07      A    C  
ANISOU   56  CA  CYS A  13     8713  11895   9435    413    623   -277  A    C  
ATOM     57  C   CYS A  13      44.449  -3.835 -27.675  1.00 85.88      A    C  
ANISOU   57  C   CYS A  13     9483  12921  10226    475    698   -313  A    C  
ATOM     58  O   CYS A  13      44.208  -3.718 -28.878  1.00 88.75      A    O  
ANISOU   58  O   CYS A  13     9848  13397  10478    499    744   -333  A    O  
ATOM     59  CB  CYS A  13      42.257  -4.669 -26.955  1.00 81.30      A    C  
ANISOU   59  CB  CYS A  13     9075  12106   9707    466    570   -378  A    C  
ATOM     60  SG  CYS A  13      42.392  -6.151 -25.991  1.00 79.46      A    S  
ANISOU   60  SG  CYS A  13     8860  11733   9598    539    504   -480  A    S  
ATOM     61  N   ASP A  14      45.658  -4.061 -27.180  1.00 83.92      A    N  
ANISOU   61  N   ASP A  14     9151  12696  10041    498    713   -318  A    N  
ATOM     62  CA  ASP A  14      46.802  -4.148 -28.058  1.00 82.04      A    C  
ANISOU   62  CA  ASP A  14     8811  12614   9746    553    794   -345  A    C  
ATOM     63  C   ASP A  14      47.009  -5.599 -28.434  1.00 78.88      A    C  
ANISOU   63  C   ASP A  14     8403  12216   9354    675    784   -488  A    C  
ATOM     64  O   ASP A  14      46.693  -6.498 -27.655  1.00 78.75      A    O  
ANISOU   64  O   ASP A  14     8427  12067   9426    712    716   -546  A    O  
ATOM     65  CB  ASP A  14      48.042  -3.559 -27.391  1.00 90.85      A    C  
ANISOU   65  CB  ASP A  14     9825  13767  10928    511    822   -272  A    C  
ATOM     66  CG  ASP A  14      48.069  -2.041 -27.440  1.00100.52      A    C  
ANISOU   66  CG  ASP A  14    11034  15033  12125    395    871   -141  A    C  
ATOM     67  OD1 ASP A  14      47.169  -1.431 -28.071  1.00 98.79      A    O  
ANISOU   67  OD1 ASP A  14    10880  14825  11830    358    891    -96  A    O  
ATOM     68  OD2 ASP A  14      49.004  -1.458 -26.850  1.00104.50      A    O1-
ANISOU   68  OD2 ASP A  14    11456  15560  12688    342    892    -82  A    O1-
ATOM     69  N   GLU A  15      47.510  -5.829 -29.641  1.00 79.02      A    N  
ANISOU   69  N   GLU A  15     8368  12378   9277    738    859   -547  A    N  
ATOM     70  CA  GLU A  15      47.823  -7.181 -30.053  1.00 81.00      A    C  
ANISOU   70  CA  GLU A  15     8601  12636   9538    856    865   -693  A    C  
ATOM     71  C   GLU A  15      49.062  -7.612 -29.286  1.00 79.44      A    C  
ANISOU   71  C   GLU A  15     8310  12424   9451    901    869   -693  A    C  
ATOM     72  O   GLU A  15      50.088  -6.919 -29.279  1.00 73.26      A    O  
ANISOU   72  O   GLU A  15     7429  11741   8667    874    923   -620  A    O  
ATOM     73  CB  GLU A  15      48.058  -7.255 -31.556  1.00 93.14      A    C  
ANISOU   73  CB  GLU A  15    10106  14346  10936    909    951   -758  A    C  
ATOM     74  CG  GLU A  15      47.371  -6.157 -32.338  1.00108.01      A    C  
ANISOU   74  CG  GLU A  15    12028  16322  12688    837    980   -674  A    C  
ATOM     75  CD  GLU A  15      47.499  -6.350 -33.835  1.00127.04      A    C  
ANISOU   75  CD  GLU A  15    14417  18909  14944    899   1057   -748  A    C  
ATOM     76  OE1 GLU A  15      48.455  -7.030 -34.266  1.00131.78      A    O  
ANISOU   76  OE1 GLU A  15    14944  19586  15539    982   1115   -835  A    O  
ATOM     77  OE2 GLU A  15      46.642  -5.827 -34.579  1.00135.92      A    O1-
ANISOU   77  OE2 GLU A  15    15595  20098  15948    867   1060   -718  A    O1-
ATOM     78  N   VAL A  16      48.940  -8.754 -28.622  1.00 77.38      A    N  
ANISOU   78  N   VAL A  16     8076  12035   9291    970    810   -771  A    N  
ATOM     79  CA  VAL A  16      49.997  -9.316 -27.793  1.00 74.00      A    C  
ANISOU   79  CA  VAL A  16     7566  11575   8977   1027    798   -771  A    C  
ATOM     80  C   VAL A  16      51.311  -9.557 -28.562  1.00 75.28      A    C  
ANISOU   80  C   VAL A  16     7601  11888   9113   1107    889   -814  A    C  
ATOM     81  O   VAL A  16      52.321  -9.941 -27.987  1.00 79.66      A    O  
ANISOU   81  O   VAL A  16     8066  12444   9756   1159    888   -807  A    O  
ATOM     82  CB  VAL A  16      49.527 -10.641 -27.208  1.00 62.72      A    C  
ANISOU   82  CB  VAL A  16     6197   9986   7649   1107    735   -859  A    C  
ATOM     83  CG1 VAL A  16      49.652 -11.726 -28.260  1.00 70.41      A    C  
ANISOU   83  CG1 VAL A  16     7161  10996   8594   1220    789  -1011  A    C  
ATOM     84  CG2 VAL A  16      50.325 -11.001 -25.997  1.00 60.09      A    C  
ANISOU   84  CG2 VAL A  16     5804   9586   7440   1139    693   -811  A    C  
ATOM     85  N   SER A  17      51.298  -9.331 -29.865  1.00 70.74      A    N  
ANISOU   85  N   SER A  17     7018  11447   8415   1119    968   -858  A    N  
ATOM     86  CA  SER A  17      52.493  -9.516 -30.671  1.00 71.99      A    C  
ANISOU   86  CA  SER A  17     7059  11757   8537   1192   1066   -900  A    C  
ATOM     87  C   SER A  17      53.543  -8.474 -30.324  1.00 73.38      A    C  
ANISOU   87  C   SER A  17     7123  12028   8731   1127   1104   -774  A    C  
ATOM     88  O   SER A  17      54.625  -8.463 -30.905  1.00 73.43      A    O  
ANISOU   88  O   SER A  17     7016  12168   8717   1173   1190   -787  A    O  
ATOM     89  CB  SER A  17      52.144  -9.401 -32.157  1.00 84.12      A    C  
ANISOU   89  CB  SER A  17     8620  13426   9915   1208   1142   -965  A    C  
ATOM     90  OG  SER A  17      51.683  -8.095 -32.503  1.00 80.88      A    O  
ANISOU   90  OG  SER A  17     8239  13089   9404   1099   1160   -850  A    O  
ATOM     91  N   LYS A  18      53.219  -7.583 -29.393  1.00 66.91      A    N  
ANISOU   91  N   LYS A  18     6331  11140   7952   1016   1045   -657  A    N  
ATOM     92  CA  LYS A  18      54.128  -6.496 -29.067  1.00 74.51      A    C  
ANISOU   92  CA  LYS A  18     7191  12186   8933    935   1081   -543  A    C  
ATOM     93  C   LYS A  18      55.089  -6.980 -28.016  1.00 79.10      A    C  
ANISOU   93  C   LYS A  18     7679  12732   9643    975   1037   -538  A    C  
ATOM     94  O   LYS A  18      56.040  -6.281 -27.651  1.00 83.82      A    O  
ANISOU   94  O   LYS A  18     8166  13404  10278    922   1060   -463  A    O  
ATOM     95  CB  LYS A  18      53.372  -5.255 -28.583  1.00 87.75      A    C  
ANISOU   95  CB  LYS A  18     8935  13809  10595    793   1046   -426  A    C  
ATOM     96  CG  LYS A  18      52.811  -5.316 -27.166  1.00 79.34      A    C  
ANISOU   96  CG  LYS A  18     7936  12580   9629    745    933   -393  A    C  
ATOM     97  CD  LYS A  18      52.330  -3.938 -26.778  1.00 70.67      A    C  
ANISOU   97  CD  LYS A  18     6876  11456   8518    602    926   -276  A    C  
ATOM     98  CE  LYS A  18      51.864  -3.885 -25.355  1.00 73.45      A    C  
ANISOU   98  CE  LYS A  18     7285  11662   8961    546    824   -240  A    C  
ATOM     99  NZ  LYS A  18      50.588  -3.114 -25.243  1.00 72.59      A    N1+
ANISOU   99  NZ  LYS A  18     7296  11467   8819    452    800   -184  A    N1+
ATOM    100  N   TYR A  19      54.811  -8.188 -27.534  1.00 76.99      A    N  
ANISOU  100  N   TYR A  19     7456  12350   9447   1067    974   -617  A    N  
ATOM    101  CA  TYR A  19      55.715  -8.931 -26.672  1.00 74.21      A    C  
ANISOU  101  CA  TYR A  19     7016  11968   9213   1144    935   -627  A    C  
ATOM    102  C   TYR A  19      56.291 -10.088 -27.459  1.00 83.57      A    C  
ANISOU  102  C   TYR A  19     8147  13199  10407   1292    998   -744  A    C  
ATOM    103  O   TYR A  19      55.663 -10.599 -28.383  1.00 92.45      A    O  
ANISOU  103  O   TYR A  19     9345  14318  11466   1340   1035   -840  A    O  
ATOM    104  CB  TYR A  19      54.970  -9.455 -25.449  1.00 67.89      A    C  
ANISOU  104  CB  TYR A  19     6308  10990   8498   1143    820   -615  A    C  
ATOM    105  CG  TYR A  19      54.368  -8.342 -24.643  1.00 74.70      A    C  
ANISOU  105  CG  TYR A  19     7229  11803   9352   1000    762   -510  A    C  
ATOM    106  CD1 TYR A  19      55.129  -7.640 -23.716  1.00 75.96      A    C  
ANISOU  106  CD1 TYR A  19     7302  11998   9562    931    731   -421  A    C  
ATOM    107  CD2 TYR A  19      53.056  -7.958 -24.834  1.00 74.35      A    C  
ANISOU  107  CD2 TYR A  19     7319  11682   9250    931    742   -503  A    C  
ATOM    108  CE1 TYR A  19      54.592  -6.607 -22.985  1.00 71.80      A    C  
ANISOU  108  CE1 TYR A  19     6828  11423   9029    797    684   -336  A    C  
ATOM    109  CE2 TYR A  19      52.512  -6.924 -24.109  1.00 79.66      A    C  
ANISOU  109  CE2 TYR A  19     8043  12304   9921    803    698   -409  A    C  
ATOM    110  CZ  TYR A  19      53.281  -6.254 -23.187  1.00 78.20      A    C  
ANISOU  110  CZ  TYR A  19     7777  12148   9787    736    672   -330  A    C  
ATOM    111  OH  TYR A  19      52.734  -5.226 -22.467  1.00 79.41      A    O  
ANISOU  111  OH  TYR A  19     7984  12247   9941    607    634   -249  A    O  
ATOM    112  N   GLU A  20      57.500 -10.485 -27.104  1.00 86.52      A    N  
ANISOU  112  N   GLU A  20     8388  13624  10863   1364   1012   -740  A    N  
ATOM    113  CA  GLU A  20      58.110 -11.652 -27.696  1.00 88.60      A    C  
ANISOU  113  CA  GLU A  20     8593  13913  11160   1515   1069   -850  A    C  
ATOM    114  C   GLU A  20      58.137 -12.699 -26.607  1.00 91.19      A    C  
ANISOU  114  C   GLU A  20     8930  14096  11622   1601    984   -860  A    C  
ATOM    115  O   GLU A  20      58.683 -12.457 -25.526  1.00 90.31      A    O  
ANISOU  115  O   GLU A  20     8751  13976  11586   1578    921   -770  A    O  
ATOM    116  CB  GLU A  20      59.525 -11.317 -28.149  1.00102.19      A    C  
ANISOU  116  CB  GLU A  20    10141  15808  12880   1542   1159   -829  A    C  
ATOM    117  CG  GLU A  20      60.232 -12.438 -28.882  1.00127.78      A    C  
ANISOU  117  CG  GLU A  20    13309  19093  16148   1700   1239   -946  A    C  
ATOM    118  CD  GLU A  20      61.376 -11.932 -29.741  1.00144.36      A    C  
ANISOU  118  CD  GLU A  20    15262  21389  18198   1708   1359   -938  A    C  
ATOM    119  OE1 GLU A  20      62.064 -10.974 -29.308  1.00143.51      A    O  
ANISOU  119  OE1 GLU A  20    15054  21367  18108   1621   1357   -829  A    O  
ATOM    120  OE2 GLU A  20      61.574 -12.488 -30.849  1.00147.65      A    O1-
ANISOU  120  OE2 GLU A  20    15664  21875  18560   1797   1458  -1045  A    O1-
ATOM    121  N   LYS A  21      57.525 -13.851 -26.862  1.00 87.60      A    N  
ANISOU  121  N   LYS A  21     8560  13526  11198   1698    981   -968  A    N  
ATOM    122  CA  LYS A  21      57.576 -14.934 -25.885  1.00 85.61      A    C  
ANISOU  122  CA  LYS A  21     8315  13129  11084   1794    913   -974  A    C  
ATOM    123  C   LYS A  21      59.018 -15.400 -25.618  1.00 88.48      A    C  
ANISOU  123  C   LYS A  21     8513  13566  11540   1904    942   -958  A    C  
ATOM    124  O   LYS A  21      59.909 -15.280 -26.478  1.00 83.52      A    O  
ANISOU  124  O   LYS A  21     7774  13083  10876   1944   1037   -996  A    O  
ATOM    125  CB  LYS A  21      56.684 -16.096 -26.317  1.00 84.04      A    C  
ANISOU  125  CB  LYS A  21     8232  12790  10910   1876    921  -1103  A    C  
ATOM    126  CG  LYS A  21      55.198 -15.734 -26.385  1.00 91.84      A    C  
ANISOU  126  CG  LYS A  21     9380  13687  11827   1772    874  -1112  A    C  
ATOM    127  CD  LYS A  21      54.324 -16.995 -26.435  1.00 98.70      A    C  
ANISOU  127  CD  LYS A  21    10357  14381  12764   1850    857  -1226  A    C  
ATOM    128  CE  LYS A  21      52.833 -16.680 -26.594  1.00 94.90      A    C  
ANISOU  128  CE  LYS A  21    10024  13819  12214   1750    814  -1247  A    C  
ATOM    129  NZ  LYS A  21      52.431 -16.275 -27.983  1.00 89.88      A    N1+
ANISOU  129  NZ  LYS A  21     9416  13302  11432   1713    880  -1334  A    N1+
ATOM    130  N   LEU A  22      59.258 -15.912 -24.417  1.00 89.52      A    N  
ANISOU  130  N   LEU A  22     8622  13605  11787   1954    860   -895  A    N  
ATOM    131  CA  LEU A  22      60.612 -16.337 -24.060  1.00 87.45      A    C  
ANISOU  131  CA  LEU A  22     8194  13414  11618   2060    873   -864  A    C  
ATOM    132  C   LEU A  22      60.677 -17.725 -23.445  1.00 93.52      A    C  
ANISOU  132  C   LEU A  22     8971  14036  12525   2212    840   -887  A    C  
ATOM    133  O   LEU A  22      61.678 -18.422 -23.605  1.00100.14      A    O  
ANISOU  133  O   LEU A  22     9689  14917  13443   2345    888   -914  A    O  
ATOM    134  CB  LEU A  22      61.291 -15.329 -23.127  1.00 72.80      A    C  
ANISOU  134  CB  LEU A  22     6238  11659   9765   1966    808   -728  A    C  
ATOM    135  CG  LEU A  22      61.591 -13.979 -23.766  1.00 75.00      A    C  
ANISOU  135  CG  LEU A  22     6462  12100   9935   1834    864   -699  A    C  
ATOM    136  CD1 LEU A  22      62.476 -13.144 -22.865  1.00 71.91      A    C  
ANISOU  136  CD1 LEU A  22     5940  11811   9572   1759    809   -585  A    C  
ATOM    137  CD2 LEU A  22      62.229 -14.169 -25.139  1.00 81.13      A    C  
ANISOU  137  CD2 LEU A  22     7158  12997  10670   1903    998   -790  A    C  
ATOM    138  N   ALA A  23      59.624 -18.125 -22.739  1.00 82.03      A    N  
ANISOU  138  N   ALA A  23     7655  12408  11106   2196    762   -871  A    N  
ATOM    139  CA  ALA A  23      59.644 -19.414 -22.071  1.00 87.67      A    C  
ANISOU  139  CA  ALA A  23     8383  12969  11959   2336    731   -873  A    C  
ATOM    140  C   ALA A  23      58.343 -19.698 -21.347  1.00100.02      A    C  
ANISOU  140  C   ALA A  23    10114  14345  13546   2291    653   -851  A    C  
ATOM    141  O   ALA A  23      57.735 -18.794 -20.789  1.00112.63      A    O  
ANISOU  141  O   ALA A  23    11775  15944  15075   2155    584   -774  A    O  
ATOM    142  CB  ALA A  23      60.802 -19.464 -21.089  1.00 90.86      A    C  
ANISOU  142  CB  ALA A  23     8640  13441  12444   2399    680   -758  A    C  
ATOM    143  N   LYS A  24      57.921 -20.957 -21.357  1.00 97.77      A    N  
ANISOU  143  N   LYS A  24     9896  13891  13364   2405    670   -920  A    N  
ATOM    144  CA  LYS A  24      56.797 -21.391 -20.542  1.00 99.63      A    C  
ANISOU  144  CA  LYS A  24    10273  13933  13650   2382    599   -887  A    C  
ATOM    145  C   LYS A  24      57.223 -21.297 -19.079  1.00 95.25      A    C  
ANISOU  145  C   LYS A  24     9671  13368  13151   2393    502   -724  A    C  
ATOM    146  O   LYS A  24      58.408 -21.357 -18.783  1.00 96.37      A    O  
ANISOU  146  O   LYS A  24     9670  13613  13334   2470    499   -666  A    O  
ATOM    147  CB  LYS A  24      56.409 -22.830 -20.902  1.00112.87      A    C  
ANISOU  147  CB  LYS A  24    12011  15429  15445   2513    652  -1000  A    C  
ATOM    148  CG  LYS A  24      54.991 -23.241 -20.496  1.00131.44      A    C  
ANISOU  148  CG  LYS A  24    14531  17579  17831   2466    608  -1014  A    C  
ATOM    149  CD  LYS A  24      54.391 -24.250 -21.483  1.00146.21      A    C  
ANISOU  149  CD  LYS A  24    16475  19325  19754   2529    688  -1192  A    C  
ATOM    150  CE  LYS A  24      54.254 -23.657 -22.895  1.00149.39      A    C  
ANISOU  150  CE  LYS A  24    16878  19867  20017   2462    756  -1324  A    C  
ATOM    151  NZ  LYS A  24      53.881 -24.661 -23.946  1.00143.81      A    N1+
ANISOU  151  NZ  LYS A  24    16217  19073  19352   2535    841  -1516  A    N1+
ATOM    152  N   ILE A  25      56.276 -21.120 -18.161  1.00 98.62      A    N  
ANISOU  152  N   ILE A  25    10214  13684  13573   2316    420   -650  A    N  
ATOM    153  CA  ILE A  25      56.614 -21.151 -16.737  1.00103.05      A    C  
ANISOU  153  CA  ILE A  25    10742  14229  14182   2337    327   -499  A    C  
ATOM    154  C   ILE A  25      55.534 -21.783 -15.844  1.00107.63      A    C  
ANISOU  154  C   ILE A  25    11463  14604  14826   2342    273   -451  A    C  
ATOM    155  O   ILE A  25      55.819 -22.160 -14.703  1.00104.93      A    O  
ANISOU  155  O   ILE A  25    11099  14222  14546   2403    208   -333  A    O  
ATOM    156  CB  ILE A  25      57.067 -19.766 -16.197  1.00 82.36      A    C  
ANISOU  156  CB  ILE A  25     8053  11783  11456   2205    264   -401  A    C  
ATOM    157  CG1 ILE A  25      55.889 -18.827 -15.970  1.00 74.28      A    C  
ANISOU  157  CG1 ILE A  25     7164  10723  10337   2034    222   -383  A    C  
ATOM    158  CG2 ILE A  25      58.070 -19.109 -17.136  1.00 82.86      A    C  
ANISOU  158  CG2 ILE A  25     7980  12042  11460   2188    328   -449  A    C  
ATOM    159  CD1 ILE A  25      56.335 -17.412 -15.697  1.00 69.68      A    C  
ANISOU  159  CD1 ILE A  25     6513  10310   9652   1897    185   -317  A    C  
ATOM    160  N   GLY A  26      54.314 -21.916 -16.371  1.00108.72      A    N  
ANISOU  160  N   GLY A  26    11741  14618  14949   2283    301   -541  A    N  
ATOM    161  CA  GLY A  26      53.234 -22.621 -15.689  1.00119.08      A    C  
ANISOU  161  CA  GLY A  26    13188  15721  16336   2292    269   -515  A    C  
ATOM    162  C   GLY A  26      52.233 -23.170 -16.697  1.00134.89      A    C  
ANISOU  162  C   GLY A  26    15296  17596  18361   2285    335   -668  A    C  
ATOM    163  O   GLY A  26      52.350 -22.841 -17.882  1.00134.40      A    O  
ANISOU  163  O   GLY A  26    15207  17630  18229   2257    396   -784  A    O  
ATOM    164  N   GLN A  27      51.258 -23.992 -16.284  1.00145.42      A    N  
ANISOU  164  N   GLN A  27    16745  18722  19787   2306    328   -675  A    N  
ATOM    165  CA  GLN A  27      51.026 -24.463 -14.903  1.00141.68      A    C  
ANISOU  165  CA  GLN A  27    16314  18120  19396   2343    266   -536  A    C  
ATOM    166  C   GLN A  27      50.481 -23.404 -13.940  1.00133.90      A    C  
ANISOU  166  C   GLN A  27    15385  17178  18312   2203    180   -415  A    C  
ATOM    167  O   GLN A  27      49.320 -23.465 -13.523  1.00120.32      A    O  
ANISOU  167  O   GLN A  27    13789  15324  16604   2137    158   -400  A    O  
ATOM    168  CB  GLN A  27      52.252 -25.179 -14.312  1.00141.26      A    C  
ANISOU  168  CB  GLN A  27    16145  18084  19441   2503    263   -448  A    C  
ATOM    169  CG  GLN A  27      52.447 -26.605 -14.833  1.00149.07      A    C  
ANISOU  169  CG  GLN A  27    17125  18925  20589   2663    346   -539  A    C  
ATOM    170  CD  GLN A  27      53.505 -26.708 -15.924  1.00149.08      A    C  
ANISOU  170  CD  GLN A  27    17002  19053  20587   2742    420   -646  A    C  
ATOM    171  NE2 GLN A  27      53.074 -27.040 -17.140  1.00145.18      A    N  
ANISOU  171  NE2 GLN A  27    16550  18515  20099   2737    501   -824  A    N  
ATOM    172  OE1 GLN A  27      54.696 -26.501 -15.673  1.00148.20      A    O  
ANISOU  172  OE1 GLN A  27    16757  19084  20469   2807    405   -571  A    O  
ATOM    173  N   PHE A  30      46.533 -24.548 -14.368  1.00171.87      A    N  
ANISOU  173  N   PHE A  30    20581  21481  23241   2054    224   -601  A    N  
ATOM    174  CA  PHE A  30      45.844 -23.379 -14.921  1.00175.03      A    C  
ANISOU  174  CA  PHE A  30    21022  21981  23502   1901    208   -647  A    C  
ATOM    175  C   PHE A  30      46.668 -22.092 -14.788  1.00169.49      A    C  
ANISOU  175  C   PHE A  30    20236  21498  22665   1836    170   -570  A    C  
ATOM    176  O   PHE A  30      46.862 -21.571 -13.686  1.00167.02      A    O  
ANISOU  176  O   PHE A  30    19918  21221  22323   1801    109   -433  A    O  
ATOM    177  CB  PHE A  30      44.458 -23.211 -14.280  1.00174.69      A    C  
ANISOU  177  CB  PHE A  30    21106  21805  23465   1799    172   -605  A    C  
ATOM    178  CG  PHE A  30      43.719 -21.978 -14.733  1.00171.81      A    C  
ANISOU  178  CG  PHE A  30    20781  21534  22963   1646    152   -632  A    C  
ATOM    179  CD1 PHE A  30      42.951 -21.246 -13.838  1.00169.60      A    C  
ANISOU  179  CD1 PHE A  30    20572  21228  22639   1540     99   -530  A    C  
ATOM    180  CD2 PHE A  30      43.799 -21.547 -16.051  1.00172.00      A    C  
ANISOU  180  CD2 PHE A  30    20772  21676  22905   1614    190   -754  A    C  
ATOM    181  CE1 PHE A  30      42.271 -20.112 -14.249  1.00171.53      A    C  
ANISOU  181  CE1 PHE A  30    20852  21552  22770   1407     86   -549  A    C  
ATOM    182  CE2 PHE A  30      43.124 -20.414 -16.472  1.00172.76      A    C  
ANISOU  182  CE2 PHE A  30    20904  21858  22880   1482    174   -764  A    C  
ATOM    183  CZ  PHE A  30      42.358 -19.694 -15.569  1.00174.19      A    C  
ANISOU  183  CZ  PHE A  30    21154  22003  23029   1380    123   -661  A    C  
ATOM    184  N   GLY A  31      47.148 -21.584 -15.920  1.00159.57      A    N  
ANISOU  184  N   GLY A  31    18915  20389  21327   1818    211   -661  A    N  
ATOM    185  CA  GLY A  31      46.908 -22.211 -17.207  1.00153.90      A    C  
ANISOU  185  CA  GLY A  31    18206  19639  20630   1860    282   -828  A    C  
ATOM    186  C   GLY A  31      48.176 -22.363 -18.027  1.00145.35      A    C  
ANISOU  186  C   GLY A  31    17000  18693  19535   1951    338   -890  A    C  
ATOM    187  O   GLY A  31      49.042 -23.188 -17.703  1.00134.51      A    O  
ANISOU  187  O   GLY A  31    15558  17287  18262   2082    355   -867  A    O  
ATOM    188  N   GLU A  32      48.275 -21.569 -19.095  1.00144.01      A    N  
ANISOU  188  N   GLU A  32    16800  18676  19242   1887    371   -964  A    N  
ATOM    189  CA  GLU A  32      49.464 -21.539 -19.948  1.00137.60      A    C  
ANISOU  189  CA  GLU A  32    15867  18019  18396   1957    432  -1021  A    C  
ATOM    190  C   GLU A  32      50.163 -20.172 -19.862  1.00120.57      A    C  
ANISOU  190  C   GLU A  32    13630  16064  16118   1872    410   -926  A    C  
ATOM    191  O   GLU A  32      49.689 -19.187 -20.426  1.00112.93      A    O  
ANISOU  191  O   GLU A  32    12691  15185  15031   1758    414   -940  A    O  
ATOM    192  CB  GLU A  32      49.093 -21.861 -21.397  1.00141.59      A    C  
ANISOU  192  CB  GLU A  32    16395  18544  18859   1967    505  -1200  A    C  
ATOM    193  CG  GLU A  32      50.275 -22.281 -22.256  1.00151.69      A    C  
ANISOU  193  CG  GLU A  32    17560  19931  20144   2079    586  -1285  A    C  
ATOM    194  CD  GLU A  32      49.932 -22.349 -23.734  1.00161.01      A    C  
ANISOU  194  CD  GLU A  32    18760  21178  21240   2068    656  -1457  A    C  
ATOM    195  OE1 GLU A  32      48.842 -21.867 -24.119  1.00161.51      A    O  
ANISOU  195  OE1 GLU A  32    18914  21236  21218   1961    634  -1495  A    O  
ATOM    196  OE2 GLU A  32      50.759 -22.877 -24.512  1.00162.24      A    O1-
ANISOU  196  OE2 GLU A  32    18838  21397  21410   2168    734  -1555  A    O1-
ATOM    197  N   VAL A  33      51.309 -20.140 -19.180  1.00111.25      A    N  
ANISOU  197  N   VAL A  33    12342  14954  14975   1931    392   -832  A    N  
ATOM    198  CA  VAL A  33      51.925 -18.899 -18.702  1.00 92.96      A    C  
ANISOU  198  CA  VAL A  33     9952  12794  12573   1842    351   -718  A    C  
ATOM    199  C   VAL A  33      53.384 -18.713 -19.143  1.00 85.24      A    C  
ANISOU  199  C   VAL A  33     8814  11991  11582   1904    396   -719  A    C  
ATOM    200  O   VAL A  33      54.246 -19.495 -18.745  1.00 78.54      A    O  
ANISOU  200  O   VAL A  33     7883  11132  10829   2029    398   -695  A    O  
ATOM    201  CB  VAL A  33      51.894 -18.891 -17.166  1.00 80.70      A    C  
ANISOU  201  CB  VAL A  33     8417  11173  11072   1832    262   -578  A    C  
ATOM    202  CG1 VAL A  33      52.328 -17.538 -16.605  1.00 73.29      A    C  
ANISOU  202  CG1 VAL A  33     7424  10381  10042   1714    213   -474  A    C  
ATOM    203  CG2 VAL A  33      50.515 -19.266 -16.689  1.00 76.79      A    C  
ANISOU  203  CG2 VAL A  33     8074  10491  10612   1793    228   -577  A    C  
ATOM    204  N   PHE A  34      53.650 -17.662 -19.929  1.00 82.03      A    N  
ANISOU  204  N   PHE A  34     8361  11745  11061   1817    434   -736  A    N  
ATOM    205  CA  PHE A  34      54.977 -17.382 -20.489  1.00 82.67      A    C  
ANISOU  205  CA  PHE A  34     8288  12002  11120   1860    491   -744  A    C  
ATOM    206  C   PHE A  34      55.660 -16.153 -19.901  1.00 82.66      A    C  
ANISOU  206  C   PHE A  34     8199  12144  11064   1759    451   -628  A    C  
ATOM    207  O   PHE A  34      55.020 -15.148 -19.625  1.00 87.08      A    O  
ANISOU  207  O   PHE A  34     8823  12712  11552   1621    415   -576  A    O  
ATOM    208  CB  PHE A  34      54.889 -17.097 -21.990  1.00101.28      A    C  
ANISOU  208  CB  PHE A  34    10644  14454  13382   1840    585   -856  A    C  
ATOM    209  CG  PHE A  34      54.038 -18.057 -22.766  1.00122.37      A    C  
ANISOU  209  CG  PHE A  34    13415  17008  16072   1899    626   -993  A    C  
ATOM    210  CD1 PHE A  34      54.614 -19.147 -23.412  1.00128.03      A    C  
ANISOU  210  CD1 PHE A  34    14078  17711  16855   2042    698  -1101  A    C  
ATOM    211  CD2 PHE A  34      52.669 -17.842 -22.895  1.00123.38      A    C  
ANISOU  211  CD2 PHE A  34    13683  17044  16150   1809    598  -1021  A    C  
ATOM    212  CE1 PHE A  34      53.837 -20.022 -24.145  1.00131.28      A    C  
ANISOU  212  CE1 PHE A  34    14579  18016  17285   2089    738  -1243  A    C  
ATOM    213  CE2 PHE A  34      51.883 -18.712 -23.624  1.00126.79      A    C  
ANISOU  213  CE2 PHE A  34    14199  17376  16599   1855    632  -1157  A    C  
ATOM    214  CZ  PHE A  34      52.469 -19.806 -24.252  1.00133.95      A    C  
ANISOU  214  CZ  PHE A  34    15055  18268  17572   1993    702  -1273  A    C  
ATOM    215  N   LYS A  35      56.976 -16.220 -19.759  1.00 88.17      A    N  
ANISOU  215  N   LYS A  35     8743  12957  11800   1827    464   -595  A    N  
ATOM    216  CA  LYS A  35      57.774 -15.015 -19.622  1.00 79.54      A    C  
ANISOU  216  CA  LYS A  35     7540  12034  10648   1730    459   -524  A    C  
ATOM    217  C   LYS A  35      57.845 -14.403 -21.010  1.00 79.73      A    C  
ANISOU  217  C   LYS A  35     7543  12172  10578   1682    560   -595  A    C  
ATOM    218  O   LYS A  35      57.866 -15.118 -22.008  1.00 84.48      A    O  
ANISOU  218  O   LYS A  35     8148  12769  11182   1774    637   -699  A    O  
ATOM    219  CB  LYS A  35      59.180 -15.355 -19.146  1.00 75.49      A    C  
ANISOU  219  CB  LYS A  35     6855  11618  10209   1826    448   -477  A    C  
ATOM    220  CG  LYS A  35      60.063 -14.141 -18.885  1.00 83.11      A    C  
ANISOU  220  CG  LYS A  35     7693  12758  11128   1721    434   -404  A    C  
ATOM    221  CD  LYS A  35      61.549 -14.535 -18.798  1.00 85.91      A    C  
ANISOU  221  CD  LYS A  35     7853  13236  11553   1831    450   -386  A    C  
ATOM    222  CE  LYS A  35      62.392 -13.472 -18.084  1.00 87.28      A    C  
ANISOU  222  CE  LYS A  35     7898  13557  11708   1727    398   -296  A    C  
ATOM    223  NZ  LYS A  35      63.818 -13.886 -17.870  1.00 90.65      A    N1+
ANISOU  223  NZ  LYS A  35     8127  14106  12210   1835    398   -271  A    N1+
ATOM    224  N   ALA A  36      57.877 -13.083 -21.087  1.00 75.34      A    N  
ANISOU  224  N   ALA A  36     6968  11717   9939   1540    564   -541  A    N  
ATOM    225  CA  ALA A  36      58.013 -12.432 -22.379  1.00 73.36      A    C  
ANISOU  225  CA  ALA A  36     6690  11586   9595   1495    664   -588  A    C  
ATOM    226  C   ALA A  36      58.649 -11.052 -22.260  1.00 76.08      A    C  
ANISOU  226  C   ALA A  36     6942  12072   9893   1367    675   -504  A    C  
ATOM    227  O   ALA A  36      58.738 -10.470 -21.177  1.00 68.35      A    O  
ANISOU  227  O   ALA A  36     5948  11084   8938   1286    597   -419  A    O  
ATOM    228  CB  ALA A  36      56.674 -12.345 -23.079  1.00 71.48      A    C  
ANISOU  228  CB  ALA A  36     6609  11269   9280   1446    683   -645  A    C  
ATOM    229  N   ARG A  37      59.100 -10.539 -23.393  1.00 76.53      A    N  
ANISOU  229  N   ARG A  37     6935  12260   9882   1348    777   -532  A    N  
ATOM    230  CA  ARG A  37      59.831  -9.292 -23.414  1.00 67.70      A    C  
ANISOU  230  CA  ARG A  37     5711  11280   8733   1235    809   -458  A    C  
ATOM    231  C   ARG A  37      59.194  -8.311 -24.371  1.00 64.85      A    C  
ANISOU  231  C   ARG A  37     5419  10961   8261   1130    881   -452  A    C  
ATOM    232  O   ARG A  37      58.885  -8.646 -25.509  1.00 77.58      A    O  
ANISOU  232  O   ARG A  37     7072  12599   9806   1183    956   -523  A    O  
ATOM    233  CB  ARG A  37      61.270  -9.552 -23.841  1.00 68.98      A    C  
ANISOU  233  CB  ARG A  37     5690  11587   8934   1319    880   -476  A    C  
ATOM    234  CG  ARG A  37      61.825  -8.472 -24.723  1.00 62.38      A    C  
ANISOU  234  CG  ARG A  37     4769  10904   8028   1232    983   -451  A    C  
ATOM    235  CD  ARG A  37      63.173  -8.842 -25.198  1.00 61.74      A    C  
ANISOU  235  CD  ARG A  37     4512  10960   7987   1326   1060   -478  A    C  
ATOM    236  NE  ARG A  37      64.144  -7.863 -24.767  1.00 74.66      A    N  
ANISOU  236  NE  ARG A  37     6001  12713   9655   1229   1063   -398  A    N  
ATOM    237  CZ  ARG A  37      64.484  -6.809 -25.489  1.00 89.85      A    C  
ANISOU  237  CZ  ARG A  37     7867  14751  11521   1131   1157   -363  A    C  
ATOM    238  NH1 ARG A  37      63.917  -6.616 -26.677  1.00 59.81      A    N1+
ANISOU  238  NH1 ARG A  37     4145  10968   7614   1125   1252   -395  A    N1+
ATOM    239  NH2 ARG A  37      65.389  -5.957 -25.021  1.00 90.00      A    N  
ANISOU  239  NH2 ARG A  37     7745  14866  11586   1038   1157   -296  A    N  
ATOM    240  N   HIS A  38      59.009  -7.087 -23.909  1.00 59.50      A    N  
ANISOU  240  N   HIS A  38     4752  10294   7563    982    858   -366  A    N  
ATOM    241  CA  HIS A  38      58.389  -6.069 -24.731  1.00 69.99      A    C  
ANISOU  241  CA  HIS A  38     6144  11654   8793    878    924   -339  A    C  
ATOM    242  C   HIS A  38      59.350  -5.677 -25.835  1.00 78.93      A    C  
ANISOU  242  C   HIS A  38     7153  12955   9881    889   1048   -342  A    C  
ATOM    243  O   HIS A  38      60.453  -5.210 -25.572  1.00 82.23      A    O  
ANISOU  243  O   HIS A  38     7427  13472  10346    856   1072   -299  A    O  
ATOM    244  CB  HIS A  38      58.036  -4.855 -23.885  1.00 81.34      A    C  
ANISOU  244  CB  HIS A  38     7614  13051  10240    720    875   -244  A    C  
ATOM    245  CG  HIS A  38      57.353  -3.771 -24.648  1.00 84.06      A    C  
ANISOU  245  CG  HIS A  38     8028  13413  10498    615    941   -201  A    C  
ATOM    246  CD2 HIS A  38      56.053  -3.404 -24.701  1.00 91.26      A    C  
ANISOU  246  CD2 HIS A  38     9088  14225  11361    556    917   -182  A    C  
ATOM    247  ND1 HIS A  38      58.031  -2.912 -25.483  1.00 89.78      A    N  
ANISOU  247  ND1 HIS A  38     8661  14271  11181    563   1049   -161  A    N  
ATOM    248  CE1 HIS A  38      57.176  -2.063 -26.022  1.00 99.87      A    C  
ANISOU  248  CE1 HIS A  38    10031  15530  12386    480   1089   -114  A    C  
ATOM    249  NE2 HIS A  38      55.967  -2.341 -25.567  1.00 99.06      A    N  
ANISOU  249  NE2 HIS A  38    10073  15289  12278    476   1008   -128  A    N  
ATOM    250  N   ARG A  39      58.918  -5.858 -27.076  1.00 79.96      A    N  
ANISOU  250  N   ARG A  39     7338  13126   9917    932   1129   -394  A    N  
ATOM    251  CA  ARG A  39      59.809  -5.695 -28.217  1.00 74.78      A    C  
ANISOU  251  CA  ARG A  39     6571  12634   9207    968   1256   -410  A    C  
ATOM    252  C   ARG A  39      60.553  -4.372 -28.267  1.00 73.26      A    C  
ANISOU  252  C   ARG A  39     6272  12551   9013    847   1320   -309  A    C  
ATOM    253  O   ARG A  39      61.586  -4.275 -28.914  1.00 89.77      A    O  
ANISOU  253  O   ARG A  39     8231  14780  11097    877   1417   -312  A    O  
ATOM    254  CB  ARG A  39      59.072  -5.953 -29.545  1.00 78.16      A    C  
ANISOU  254  CB  ARG A  39     7092  13095   9509   1016   1328   -476  A    C  
ATOM    255  CG  ARG A  39      58.769  -7.429 -29.781  1.00 83.38      A    C  
ANISOU  255  CG  ARG A  39     7806  13692  10182   1163   1305   -608  A    C  
ATOM    256  CD  ARG A  39      58.424  -7.774 -31.217  1.00 85.09      A    C  
ANISOU  256  CD  ARG A  39     8068  13991  10272   1226   1395   -696  A    C  
ATOM    257  NE  ARG A  39      57.407  -8.819 -31.216  1.00100.99      A    N  
ANISOU  257  NE  ARG A  39    10209  15876  12285   1296   1332   -802  A    N  
ATOM    258  CZ  ARG A  39      57.668 -10.120 -31.170  1.00112.28      A    C  
ANISOU  258  CZ  ARG A  39    11624  17253  13783   1427   1324   -915  A    C  
ATOM    259  NH1 ARG A  39      58.927 -10.538 -31.153  1.00122.98      A    N1+
ANISOU  259  NH1 ARG A  39    12839  18681  15205   1509   1376   -934  A    N1+
ATOM    260  NH2 ARG A  39      56.672 -11.003 -31.152  1.00102.71      A    N  
ANISOU  260  NH2 ARG A  39    10533  15914  12580   1475   1269  -1009  A    N  
ATOM    261  N   LYS A  40      60.043  -3.353 -27.593  1.00 75.61      A    N  
ANISOU  261  N   LYS A  40     6622  12783   9324    709   1273   -223  A    N  
ATOM    262  CA  LYS A  40      60.601  -2.016 -27.764  1.00 80.27      A    C  
ANISOU  262  CA  LYS A  40     7127  13461   9910    581   1347   -129  A    C  
ATOM    263  C   LYS A  40      61.462  -1.533 -26.595  1.00 81.02      A    C  
ANISOU  263  C   LYS A  40     7105  13561  10118    501   1293    -82  A    C  
ATOM    264  O   LYS A  40      62.348  -0.699 -26.778  1.00 75.08      A    O  
ANISOU  264  O   LYS A  40     6226  12910   9389    426   1368    -29  A    O  
ATOM    265  CB  LYS A  40      59.488  -1.001 -28.064  1.00 74.65      A    C  
ANISOU  265  CB  LYS A  40     6545  12692   9126    471   1365    -60  A    C  
ATOM    266  CG  LYS A  40      58.931  -1.063 -29.491  1.00 69.08      A    C  
ANISOU  266  CG  LYS A  40     5908  12052   8287    521   1457    -77  A    C  
ATOM    267  CD  LYS A  40      58.113   0.182 -29.817  1.00 79.18      A    C  
ANISOU  267  CD  LYS A  40     7273  13307   9506    401   1495     24  A    C  
ATOM    268  CE  LYS A  40      57.846   0.310 -31.312  1.00 95.87      A    C  
ANISOU  268  CE  LYS A  40     9416  15533  11479    443   1605     31  A    C  
ATOM    269  NZ  LYS A  40      58.639   1.416 -31.943  1.00107.95      A    N1+
ANISOU  269  NZ  LYS A  40    10842  17185  12988    368   1737    132  A    N1+
ATOM    270  N   THR A  41      61.210  -2.072 -25.406  1.00 82.09      A    N  
ANISOU  270  N   THR A  41     7277  13591  10322    518   1166   -102  A    N  
ATOM    271  CA  THR A  41      61.799  -1.540 -24.184  1.00 76.87      A    C  
ANISOU  271  CA  THR A  41     6531  12925   9751    427   1094    -58  A    C  
ATOM    272  C   THR A  41      62.553  -2.592 -23.384  1.00 74.97      A    C  
ANISOU  272  C   THR A  41     6198  12697   9590    534   1011   -101  A    C  
ATOM    273  O   THR A  41      63.418  -2.279 -22.548  1.00 80.16      A    O  
ANISOU  273  O   THR A  41     6730  13407  10319    484    966    -74  A    O  
ATOM    274  CB  THR A  41      60.720  -0.886 -23.302  1.00 76.21      A    C  
ANISOU  274  CB  THR A  41     6584  12703   9669    311   1011    -15  A    C  
ATOM    275  CG2 THR A  41      60.046   0.216 -24.078  1.00 76.24      A    C  
ANISOU  275  CG2 THR A  41     6665  12697   9607    207   1098     40  A    C  
ATOM    276  OG1 THR A  41      59.742  -1.859 -22.900  1.00 73.98      A    O  
ANISOU  276  OG1 THR A  41     6440  12294   9376    395    922    -60  A    O  
ATOM    277  N   GLY A  42      62.224  -3.843 -23.648  1.00 68.77      A    N  
ANISOU  277  N   GLY A  42     5472  11864   8793    682    991   -169  A    N  
ATOM    278  CA  GLY A  42      62.901  -4.934 -22.991  1.00 81.17      A    C  
ANISOU  278  CA  GLY A  42     6960  13439  10442    805    924   -204  A    C  
ATOM    279  C   GLY A  42      62.172  -5.326 -21.731  1.00 79.91      A    C  
ANISOU  279  C   GLY A  42     6904  13139  10319    803    787   -192  A    C  
ATOM    280  O   GLY A  42      62.430  -6.387 -21.157  1.00 78.43      A    O  
ANISOU  280  O   GLY A  42     6691  12917  10189    921    722   -216  A    O  
ATOM    281  N   GLN A  43      61.247  -4.479 -21.298  1.00 70.26      A    N  
ANISOU  281  N   GLN A  43     5798  11833   9064    672    750   -149  A    N  
ATOM    282  CA  GLN A  43      60.494  -4.806 -20.102  1.00 74.17      A    C  
ANISOU  282  CA  GLN A  43     6399  12196   9585    664    627   -136  A    C  
ATOM    283  C   GLN A  43      60.052  -6.263 -20.131  1.00 77.26      A    C  
ANISOU  283  C   GLN A  43     6865  12496   9996    824    592   -192  A    C  
ATOM    284  O   GLN A  43      59.424  -6.705 -21.088  1.00 75.44      A    O  
ANISOU  284  O   GLN A  43     6718  12225   9720    882    650   -245  A    O  
ATOM    285  CB  GLN A  43      59.280  -3.912 -19.970  1.00 77.44      A    C  
ANISOU  285  CB  GLN A  43     6964  12510   9949    534    617   -102  A    C  
ATOM    286  CG  GLN A  43      58.497  -4.185 -18.705  1.00 87.17      A    C  
ANISOU  286  CG  GLN A  43     8304  13610  11206    517    498    -86  A    C  
ATOM    287  CD  GLN A  43      57.114  -3.585 -18.758  1.00 91.59      A    C  
ANISOU  287  CD  GLN A  43     9032  14052  11716    426    497    -68  A    C  
ATOM    288  NE2 GLN A  43      56.338  -3.775 -17.689  1.00 78.78      A    N  
ANISOU  288  NE2 GLN A  43     7512  12309  10110    405    404    -53  A    N  
ATOM    289  OE1 GLN A  43      56.743  -2.954 -19.754  1.00 95.17      A    O  
ANISOU  289  OE1 GLN A  43     9520  14525  12116    378    583    -64  A    O  
ATOM    290  N   LYS A  44      60.397  -7.017 -19.095  1.00 77.44      A    N  
ANISOU  290  N   LYS A  44     6852  12487  10087    897    500   -182  A    N  
ATOM    291  CA  LYS A  44      59.917  -8.388 -18.992  1.00 77.71      A    C  
ANISOU  291  CA  LYS A  44     6964  12408  10154   1043    465   -226  A    C  
ATOM    292  C   LYS A  44      58.510  -8.424 -18.388  1.00 82.31      A    C  
ANISOU  292  C   LYS A  44     7731  12826  10717    995    398   -213  A    C  
ATOM    293  O   LYS A  44      58.159  -7.607 -17.529  1.00 84.54      A    O  
ANISOU  293  O   LYS A  44     8053  13082  10985    874    338   -156  A    O  
ATOM    294  CB  LYS A  44      60.873  -9.220 -18.151  1.00 68.47      A    C  
ANISOU  294  CB  LYS A  44     5676  11271   9069   1154    400   -206  A    C  
ATOM    295  CG  LYS A  44      62.314  -9.041 -18.552  1.00 69.48      A    C  
ANISOU  295  CG  LYS A  44     5604  11572   9225   1184    455   -206  A    C  
ATOM    296  CD  LYS A  44      62.681  -9.743 -19.847  1.00 65.56      A    C  
ANISOU  296  CD  LYS A  44     5064  11117   8730   1306    567   -283  A    C  
ATOM    297  CE  LYS A  44      64.186  -9.647 -20.085  1.00 82.57      A    C  
ANISOU  297  CE  LYS A  44     7003  13442  10927   1347    615   -275  A    C  
ATOM    298  NZ  LYS A  44      64.766  -8.294 -19.776  1.00 87.33      A    N1+
ANISOU  298  NZ  LYS A  44     7505  14164  11512   1187    611   -215  A    N1+
ATOM    299  N   VAL A  45      57.706  -9.378 -18.842  1.00 73.49      A    N  
ANISOU  299  N   VAL A  45     6724  11597   9602   1087    411   -272  A    N  
ATOM    300  CA  VAL A  45      56.343  -9.512 -18.359  1.00 68.09      A    C  
ANISOU  300  CA  VAL A  45     6211  10754   8907   1050    355   -266  A    C  
ATOM    301  C   VAL A  45      55.983 -10.985 -18.268  1.00 69.98      A    C  
ANISOU  301  C   VAL A  45     6509  10872   9209   1197    334   -316  A    C  
ATOM    302  O   VAL A  45      56.700 -11.836 -18.776  1.00 78.85      A    O  
ANISOU  302  O   VAL A  45     7553  12033  10376   1324    376   -366  A    O  
ATOM    303  CB  VAL A  45      55.336  -8.817 -19.309  1.00 63.65      A    C  
ANISOU  303  CB  VAL A  45     5755  10168   8261    963    415   -293  A    C  
ATOM    304  CG1 VAL A  45      55.668  -7.336 -19.487  1.00 56.06      A    C  
ANISOU  304  CG1 VAL A  45     4739   9315   7247    819    452   -238  A    C  
ATOM    305  CG2 VAL A  45      55.332  -9.498 -20.642  1.00 62.35      A    C  
ANISOU  305  CG2 VAL A  45     5590  10030   8071   1060    500   -384  A    C  
ATOM    306  N   ALA A  46      54.871 -11.286 -17.613  1.00 70.40      A    N  
ANISOU  306  N   ALA A  46     6700  10773   9275   1180    274   -302  A    N  
ATOM    307  CA  ALA A  46      54.300 -12.624 -17.666  1.00 68.29      A    C  
ANISOU  307  CA  ALA A  46     6513  10367   9069   1302    268   -358  A    C  
ATOM    308  C   ALA A  46      52.966 -12.526 -18.391  1.00 70.60      A    C  
ANISOU  308  C   ALA A  46     6947  10568   9311   1250    298   -416  A    C  
ATOM    309  O   ALA A  46      52.209 -11.587 -18.156  1.00 77.85      A    O  
ANISOU  309  O   ALA A  46     7939  11466  10174   1124    276   -375  A    O  
ATOM    310  CB  ALA A  46      54.105 -13.183 -16.261  1.00 59.50      A    C  
ANISOU  310  CB  ALA A  46     5438   9146   8023   1336    175   -288  A    C  
ATOM    311  N   LEU A  47      52.691 -13.477 -19.282  1.00 63.96      A    N  
ANISOU  311  N   LEU A  47     6137   9675   8488   1347    349   -517  A    N  
ATOM    312  CA  LEU A  47      51.411 -13.531 -19.984  1.00 60.21      A    C  
ANISOU  312  CA  LEU A  47     5791   9118   7969   1309    370   -585  A    C  
ATOM    313  C   LEU A  47      50.660 -14.805 -19.628  1.00 73.38      A    C  
ANISOU  313  C   LEU A  47     7551  10603   9726   1393    341   -633  A    C  
ATOM    314  O   LEU A  47      51.163 -15.900 -19.852  1.00 79.38      A    O  
ANISOU  314  O   LEU A  47     8269  11332  10559   1522    369   -695  A    O  
ATOM    315  CB  LEU A  47      51.617 -13.524 -21.498  1.00 54.83      A    C  
ANISOU  315  CB  LEU A  47     5075   8540   7218   1337    462   -683  A    C  
ATOM    316  CG  LEU A  47      52.623 -12.575 -22.128  1.00 62.92      A    C  
ANISOU  316  CG  LEU A  47     5981   9755   8170   1297    522   -656  A    C  
ATOM    317  CD1 LEU A  47      52.988 -13.062 -23.505  1.00 70.52      A    C  
ANISOU  317  CD1 LEU A  47     6901  10802   9091   1380    615   -768  A    C  
ATOM    318  CD2 LEU A  47      52.078 -11.170 -22.198  1.00 75.02      A    C  
ANISOU  318  CD2 LEU A  47     7555  11336   9613   1145    519   -587  A    C  
ATOM    319  N   LYS A  48      49.457 -14.660 -19.081  1.00 74.79      A    N  
ANISOU  319  N   LYS A  48     7853  10659   9906   1321    291   -606  A    N  
ATOM    320  CA  LYS A  48      48.541 -15.780 -18.912  1.00 72.38      A    C  
ANISOU  320  CA  LYS A  48     7647  10175   9680   1380    276   -661  A    C  
ATOM    321  C   LYS A  48      47.576 -15.779 -20.084  1.00 73.74      A    C  
ANISOU  321  C   LYS A  48     7893  10332   9793   1347    317   -770  A    C  
ATOM    322  O   LYS A  48      46.811 -14.833 -20.261  1.00 79.22      A    O  
ANISOU  322  O   LYS A  48     8644  11051  10407   1233    306   -744  A    O  
ATOM    323  CB  LYS A  48      47.732 -15.622 -17.624  1.00 77.95      A    C  
ANISOU  323  CB  LYS A  48     8442  10755  10419   1317    201   -568  A    C  
ATOM    324  CG  LYS A  48      48.252 -16.390 -16.427  1.00 92.09      A    C  
ANISOU  324  CG  LYS A  48    10208  12472  12309   1401    154   -495  A    C  
ATOM    325  CD  LYS A  48      47.326 -16.186 -15.224  1.00107.74      A    C  
ANISOU  325  CD  LYS A  48    12291  14337  14307   1330     88   -406  A    C  
ATOM    326  CE  LYS A  48      47.774 -16.987 -13.998  1.00117.19      A    C  
ANISOU  326  CE  LYS A  48    13472  15461  15594   1419     40   -322  A    C  
ATOM    327  NZ  LYS A  48      46.846 -16.787 -12.842  1.00123.27      A    N1+
ANISOU  327  NZ  LYS A  48    14345  16123  16369   1349    -17   -237  A    N1+
ATOM    328  N   LYS A  49      47.600 -16.827 -20.893  1.00 71.45      A    N  
ANISOU  328  N   LYS A  49     7600  10004   9542   1446    365   -894  A    N  
ATOM    329  CA  LYS A  49      46.578 -16.986 -21.919  1.00 79.43      A    C  
ANISOU  329  CA  LYS A  49     8688  10988  10502   1418    393  -1009  A    C  
ATOM    330  C   LYS A  49      45.263 -17.324 -21.228  1.00 76.29      A    C  
ANISOU  330  C   LYS A  49     8411  10408  10166   1374    338   -997  A    C  
ATOM    331  O   LYS A  49      45.262 -18.036 -20.227  1.00 81.57      A    O  
ANISOU  331  O   LYS A  49     9101  10944  10947   1423    306   -953  A    O  
ATOM    332  CB  LYS A  49      46.971 -18.115 -22.869  1.00 88.80      A    C  
ANISOU  332  CB  LYS A  49     9840  12171  11727   1539    458  -1158  A    C  
ATOM    333  CG  LYS A  49      46.207 -18.181 -24.177  1.00 89.94      A    C  
ANISOU  333  CG  LYS A  49    10034  12353  11788   1515    497  -1296  A    C  
ATOM    334  CD  LYS A  49      46.839 -19.235 -25.079  1.00104.78      A    C  
ANISOU  334  CD  LYS A  49    11861  14251  13700   1639    570  -1445  A    C  
ATOM    335  CE  LYS A  49      46.461 -19.055 -26.543  1.00111.28      A    C  
ANISOU  335  CE  LYS A  49    12696  15192  14392   1617    620  -1576  A    C  
ATOM    336  NZ  LYS A  49      47.438 -19.746 -27.441  1.00113.53      A    N1+
ANISOU  336  NZ  LYS A  49    12900  15560  14676   1731    706  -1698  A    N1+
ATOM    337  N   VAL A  50      44.151 -16.796 -21.734  1.00 77.32      A    N  
ANISOU  337  N   VAL A  50     8617  10537  10223   1283    329  -1028  A    N  
ATOM    338  CA  VAL A  50      42.832 -17.252 -21.289  1.00 85.07      A    C  
ANISOU  338  CA  VAL A  50     9708  11346  11268   1248    289  -1045  A    C  
ATOM    339  C   VAL A  50      42.347 -18.414 -22.149  1.00 97.85      A    C  
ANISOU  339  C   VAL A  50    11358  12887  12934   1314    323  -1212  A    C  
ATOM    340  O   VAL A  50      42.131 -18.266 -23.370  1.00 90.54      A    O  
ANISOU  340  O   VAL A  50    10425  12060  11916   1302    357  -1317  A    O  
ATOM    341  CB  VAL A  50      41.754 -16.144 -21.291  1.00 68.54      A    C  
ANISOU  341  CB  VAL A  50     7681   9271   9089   1115    257   -991  A    C  
ATOM    342  CG1 VAL A  50      40.370 -16.770 -21.146  1.00 49.54      A    C  
ANISOU  342  CG1 VAL A  50     5375   6699   6747   1091    229  -1047  A    C  
ATOM    343  CG2 VAL A  50      41.983 -15.191 -20.151  1.00 67.32      A    C  
ANISOU  343  CG2 VAL A  50     7523   9129   8927   1045    217   -835  A    C  
ATOM    344  N   LEU A  51      42.163 -19.553 -21.480  1.00105.24      A    N  
ANISOU  344  N   LEU A  51    12328  13644  14014   1381    314  -1232  A    N  
ATOM    345  CA  LEU A  51      41.872 -20.827 -22.121  1.00124.73      A    C  
ANISOU  345  CA  LEU A  51    14817  16008  16565   1458    352  -1392  A    C  
ATOM    346  C   LEU A  51      40.409 -20.936 -22.548  1.00129.19      A    C  
ANISOU  346  C   LEU A  51    15472  16494  17121   1381    333  -1480  A    C  
ATOM    347  O   LEU A  51      39.527 -21.146 -21.714  1.00122.83      A    O  
ANISOU  347  O   LEU A  51    14737  15534  16397   1340    294  -1430  A    O  
ATOM    348  CB  LEU A  51      42.218 -21.963 -21.159  1.00135.66      A    C  
ANISOU  348  CB  LEU A  51    16205  17219  18121   1556    354  -1360  A    C  
ATOM    349  CG  LEU A  51      43.048 -21.596 -19.922  1.00140.09      A    C  
ANISOU  349  CG  LEU A  51    16724  17796  18709   1577    319  -1184  A    C  
ATOM    350  CD1 LEU A  51      42.947 -22.705 -18.894  1.00139.49      A    C  
ANISOU  350  CD1 LEU A  51    16683  17519  18799   1654    310  -1139  A    C  
ATOM    351  CD2 LEU A  51      44.514 -21.317 -20.269  1.00144.41      A    C  
ANISOU  351  CD2 LEU A  51    17151  18513  19206   1644    352  -1167  A    C  
ATOM    352  N   MET A  52      40.160 -20.797 -23.849  1.00135.93      A    N  
ANISOU  352  N   MET A  52    16316  17459  17872   1364    360  -1609  A    N  
ATOM    353  CA  MET A  52      38.802 -20.854 -24.391  1.00142.42      A    C  
ANISOU  353  CA  MET A  52    17208  18237  18668   1290    337  -1704  A    C  
ATOM    354  C   MET A  52      38.426 -22.274 -24.809  1.00152.74      A    C  
ANISOU  354  C   MET A  52    18540  19403  20091   1353    366  -1882  A    C  
ATOM    355  O   MET A  52      37.612 -22.481 -25.717  1.00151.58      A    O  
ANISOU  355  O   MET A  52    18420  19273  19899   1318    366  -2023  A    O  
ATOM    356  CB  MET A  52      38.660 -19.900 -25.576  1.00142.28      A    C  
ANISOU  356  CB  MET A  52    17166  18428  18464   1234    344  -1743  A    C  
ATOM    357  CG  MET A  52      38.850 -18.440 -25.206  1.00146.08      A    C  
ANISOU  357  CG  MET A  52    17633  19031  18842   1156    319  -1571  A    C  
ATOM    358  SD  MET A  52      37.371 -17.696 -24.489  1.00167.72      A    S  
ANISOU  358  SD  MET A  52    20461  21682  21585   1030    249  -1470  A    S  
ATOM    359  CE  MET A  52      36.503 -17.160 -25.974  1.00 92.47      A    C  
ANISOU  359  CE  MET A  52    10938  12302  11895    972    248  -1570  A    C  
ATOM    360  N   GLU A  53      39.032 -23.250 -24.139  1.00158.78      A    N  
ANISOU  360  N   GLU A  53    19293  20028  21007   1448    393  -1874  A    N  
ATOM    361  CA  GLU A  53      38.755 -24.653 -24.405  1.00162.01      A    C  
ANISOU  361  CA  GLU A  53    19726  20273  21558   1514    431  -2033  A    C  
ATOM    362  C   GLU A  53      37.714 -25.186 -23.442  1.00159.78      A    C  
ANISOU  362  C   GLU A  53    19523  19765  21421   1475    397  -1992  A    C  
ATOM    363  O   GLU A  53      37.824 -24.989 -22.227  1.00153.61      A    O  
ANISOU  363  O   GLU A  53    18759  18906  20700   1473    369  -1824  A    O  
ATOM    364  CB  GLU A  53      40.017 -25.490 -24.259  1.00165.70      A    C  
ANISOU  364  CB  GLU A  53    20132  20703  22125   1652    489  -2048  A    C  
ATOM    365  CG  GLU A  53      39.711 -26.966 -24.110  1.00169.79      A    C  
ANISOU  365  CG  GLU A  53    20685  20991  22838   1723    528  -2162  A    C  
ATOM    366  CD  GLU A  53      40.828 -27.728 -23.439  1.00170.53      A    C  
ANISOU  366  CD  GLU A  53    20731  20995  23069   1857    570  -2097  A    C  
ATOM    367  OE1 GLU A  53      40.560 -28.826 -22.906  1.00167.65      A    O  
ANISOU  367  OE1 GLU A  53    20402  20409  22887   1912    593  -2119  A    O  
ATOM    368  OE2 GLU A  53      41.972 -27.224 -23.439  1.00171.72      A    O1-
ANISOU  368  OE2 GLU A  53    20803  21295  23148   1908    581  -2019  A    O1-
ATOM    369  N   ASN A  54      36.721 -25.883 -23.987  1.00161.74      A    N  
ANISOU  369  N   ASN A  54    19817  19912  21725   1445    403  -2151  A    N  
ATOM    370  CA  ASN A  54      35.610 -26.378 -23.186  1.00161.67      A    C  
ANISOU  370  CA  ASN A  54    19881  19690  21854   1395    377  -2126  A    C  
ATOM    371  C   ASN A  54      34.783 -25.195 -22.675  1.00149.52      A    C  
ANISOU  371  C   ASN A  54    18381  18208  20222   1276    310  -1987  A    C  
ATOM    372  O   ASN A  54      34.087 -25.292 -21.659  1.00140.38      A    O  
ANISOU  372  O   ASN A  54    17278  16899  19160   1235    284  -1889  A    O  
ATOM    373  CB  ASN A  54      36.123 -27.238 -22.021  1.00163.33      A    C  
ANISOU  373  CB  ASN A  54    20101  19709  22248   1485    404  -2026  A    C  
ATOM    374  CG  ASN A  54      35.380 -28.562 -21.890  1.00161.73      A    C  
ANISOU  374  CG  ASN A  54    19948  19259  22241   1504    437  -2138  A    C  
ATOM    375  ND2 ASN A  54      35.461 -29.172 -20.708  1.00155.76      A    N  
ANISOU  375  ND2 ASN A  54    19221  18316  21644   1553    449  -2016  A    N  
ATOM    376  OD1 ASN A  54      34.746 -29.032 -22.837  1.00161.93      A    O  
ANISOU  376  OD1 ASN A  54    19984  19264  22276   1474    453  -2332  A    O  
ATOM    377  N   GLU A  55      34.875 -24.076 -23.390  1.00137.20      A    N  
ANISOU  377  N   GLU A  55    16790  16863  18475   1223    288  -1976  A    N  
ATOM    378  CA  GLU A  55      34.153 -22.866 -23.023  1.00122.84      A    C  
ANISOU  378  CA  GLU A  55    15001  15112  16561   1114    232  -1848  A    C  
ATOM    379  C   GLU A  55      33.023 -22.597 -24.004  1.00110.58      A    C  
ANISOU  379  C   GLU A  55    13467  13624  14923   1032    205  -1966  A    C  
ATOM    380  O   GLU A  55      33.218 -22.032 -25.080  1.00 98.51      A    O  
ANISOU  380  O   GLU A  55    11901  12287  13242   1021    208  -2028  A    O  
ATOM    381  CB  GLU A  55      35.101 -21.672 -22.932  1.00124.69      A    C  
ANISOU  381  CB  GLU A  55    15187  15532  16658   1111    226  -1712  A    C  
ATOM    382  CG  GLU A  55      36.058 -21.741 -21.751  1.00123.60      A    C  
ANISOU  382  CG  GLU A  55    15031  15337  16595   1169    231  -1565  A    C  
ATOM    383  CD  GLU A  55      35.338 -21.808 -20.416  1.00124.60      A    C  
ANISOU  383  CD  GLU A  55    15223  15293  16825   1126    197  -1443  A    C  
ATOM    384  OE1 GLU A  55      34.094 -21.655 -20.395  1.00128.58      A    O  
ANISOU  384  OE1 GLU A  55    15784  15732  17338   1043    169  -1460  A    O  
ATOM    385  OE2 GLU A  55      36.019 -22.008 -19.385  1.00119.77      A    O1-
ANISOU  385  OE2 GLU A  55    14604  14621  16283   1178    197  -1327  A    O1-
ATOM    386  N   LYS A  56      31.829 -23.007 -23.610  1.00112.83      A    N  
ANISOU  386  N   LYS A  56    13808  13753  15309    974    180  -1991  A    N  
ATOM    387  CA  LYS A  56      30.698 -23.013 -24.516  1.00114.89      A    C  
ANISOU  387  CA  LYS A  56    14081  14051  15522    904    152  -2127  A    C  
ATOM    388  C   LYS A  56      29.717 -21.914 -24.144  1.00 99.14      A    C  
ANISOU  388  C   LYS A  56    12115  12094  13462    799     97  -2003  A    C  
ATOM    389  O   LYS A  56      28.609 -21.841 -24.663  1.00 97.27      A    O  
ANISOU  389  O   LYS A  56    11890  11869  13200    730     63  -2082  A    O  
ATOM    390  CB  LYS A  56      30.042 -24.400 -24.500  1.00121.95      A    C  
ANISOU  390  CB  LYS A  56    15005  14740  16592    916    171  -2279  A    C  
ATOM    391  CG  LYS A  56      30.965 -25.499 -25.042  1.00125.60      A    C  
ANISOU  391  CG  LYS A  56    15436  15169  17119   1023    233  -2428  A    C  
ATOM    392  CD  LYS A  56      30.691 -26.859 -24.419  1.00130.50      A    C  
ANISOU  392  CD  LYS A  56    16091  15523  17970   1060    269  -2489  A    C  
ATOM    393  CE  LYS A  56      31.771 -27.862 -24.821  1.00135.83      A    C  
ANISOU  393  CE  LYS A  56    16732  16160  18717   1179    340  -2606  A    C  
ATOM    394  NZ  LYS A  56      31.566 -29.208 -24.208  1.00136.62      A    N1+
ANISOU  394  NZ  LYS A  56    16866  15988  19057   1225    386  -2656  A    N1+
ATOM    395  N   GLU A  57      30.155 -21.044 -23.251  1.00 87.72      A    N  
ANISOU  395  N   GLU A  57    10674  10671  11985    787     89  -1813  A    N  
ATOM    396  CA  GLU A  57      29.309 -19.982 -22.748  1.00 71.93      A    C  
ANISOU  396  CA  GLU A  57     8704   8687   9938    694     47  -1682  A    C  
ATOM    397  C   GLU A  57      29.939 -18.603 -22.962  1.00 75.72      A    C  
ANISOU  397  C   GLU A  57     9151   9364  10254    674     42  -1563  A    C  
ATOM    398  O   GLU A  57      29.822 -17.712 -22.116  1.00 62.69      A    O  
ANISOU  398  O   GLU A  57     7521   7707   8590    625     26  -1406  A    O  
ATOM    399  CB  GLU A  57      29.032 -20.230 -21.278  1.00 54.53      A    C  
ANISOU  399  CB  GLU A  57     6552   6291   7875    681     45  -1559  A    C  
ATOM    400  CG  GLU A  57      27.799 -21.064 -21.058  1.00 85.32      A    C  
ANISOU  400  CG  GLU A  57    10494  10011  11911    642     36  -1635  A    C  
ATOM    401  CD  GLU A  57      26.506 -20.283 -21.298  1.00107.86      A    C  
ANISOU  401  CD  GLU A  57    13363  12908  14709    539     -7  -1622  A    C  
ATOM    402  OE1 GLU A  57      26.308 -19.210 -20.653  1.00104.00      A    O  
ANISOU  402  OE1 GLU A  57    12892  12456  14167    488    -25  -1467  A    O  
ATOM    403  OE2 GLU A  57      25.688 -20.760 -22.124  1.00109.60      A    O1-
ANISOU  403  OE2 GLU A  57    13575  13125  14943    511    -22  -1771  A    O1-
ATOM    404  N   GLY A  58      30.593 -18.430 -24.107  1.00 77.75      A    N  
ANISOU  404  N   GLY A  58     9357   9797  10389    710     60  -1643  A    N  
ATOM    405  CA  GLY A  58      31.349 -17.221 -24.364  1.00 76.90      A    C  
ANISOU  405  CA  GLY A  58     9210   9871  10137    701     70  -1535  A    C  
ATOM    406  C   GLY A  58      32.526 -17.079 -23.410  1.00 84.98      A    C  
ANISOU  406  C   GLY A  58    10216  10869  11202    744     93  -1415  A    C  
ATOM    407  O   GLY A  58      32.917 -18.040 -22.728  1.00 88.20      A    O  
ANISOU  407  O   GLY A  58    10633  11140  11738    803    107  -1430  A    O  
ATOM    408  N   PHE A  59      33.083 -15.870 -23.370  1.00 80.23      A    N  
ANISOU  408  N   PHE A  59     9586  10403  10496    714     98  -1293  A    N  
ATOM    409  CA  PHE A  59      34.207 -15.519 -22.494  1.00 69.31      A    C  
ANISOU  409  CA  PHE A  59     8174   9028   9132    739    113  -1172  A    C  
ATOM    410  C   PHE A  59      33.972 -15.915 -21.025  1.00 65.26      A    C  
ANISOU  410  C   PHE A  59     7711   8331   8754    733     90  -1088  A    C  
ATOM    411  O   PHE A  59      32.984 -15.515 -20.407  1.00 60.40      A    O  
ANISOU  411  O   PHE A  59     7150   7633   8165    660     61  -1023  A    O  
ATOM    412  CB  PHE A  59      34.505 -14.018 -22.619  1.00 55.46      A    C  
ANISOU  412  CB  PHE A  59     6393   7424   7253    676    117  -1051  A    C  
ATOM    413  CG  PHE A  59      35.727 -13.584 -21.892  1.00 64.18      A    C  
ANISOU  413  CG  PHE A  59     7454   8569   8362    693    132   -945  A    C  
ATOM    414  CD1 PHE A  59      36.965 -13.605 -22.521  1.00 62.55      A    C  
ANISOU  414  CD1 PHE A  59     7171   8496   8100    754    173   -974  A    C  
ATOM    415  CD2 PHE A  59      35.647 -13.160 -20.570  1.00 75.84      A    C  
ANISOU  415  CD2 PHE A  59     8963   9956   9896    648    107   -821  A    C  
ATOM    416  CE1 PHE A  59      38.103 -13.209 -21.852  1.00 59.26      A    C  
ANISOU  416  CE1 PHE A  59     6703   8123   7692    768    184   -881  A    C  
ATOM    417  CE2 PHE A  59      36.781 -12.758 -19.887  1.00 78.92      A    C  
ANISOU  417  CE2 PHE A  59     9306  10395  10286    660    114   -731  A    C  
ATOM    418  CZ  PHE A  59      38.013 -12.786 -20.531  1.00 77.06      A    C  
ANISOU  418  CZ  PHE A  59     8986  10291  10001    719    150   -761  A    C  
ATOM    419  N   PRO A  60      34.896 -16.703 -20.462  1.00 61.11      A    N  
ANISOU  419  N   PRO A  60     7163   7745   8312    814    106  -1084  A    N  
ATOM    420  CA  PRO A  60      34.687 -17.407 -19.189  1.00 56.20      A    C  
ANISOU  420  CA  PRO A  60     6587   6940   7828    834     91  -1026  A    C  
ATOM    421  C   PRO A  60      34.398 -16.492 -18.030  1.00 62.35      A    C  
ANISOU  421  C   PRO A  60     7402   7691   8596    759     60   -870  A    C  
ATOM    422  O   PRO A  60      35.183 -15.600 -17.741  1.00 70.31      A    O  
ANISOU  422  O   PRO A  60     8371   8809   9533    740     58   -778  A    O  
ATOM    423  CB  PRO A  60      36.013 -18.102 -18.952  1.00 49.21      A    C  
ANISOU  423  CB  PRO A  60     5646   6059   6992    941    116  -1026  A    C  
ATOM    424  CG  PRO A  60      36.619 -18.232 -20.326  1.00 61.32      A    C  
ANISOU  424  CG  PRO A  60     7118   7731   8451    989    153  -1149  A    C  
ATOM    425  CD  PRO A  60      36.201 -17.015 -21.065  1.00 61.55      A    C  
ANISOU  425  CD  PRO A  60     7142   7908   8335    901    145  -1135  A    C  
ATOM    426  N   ILE A  61      33.282 -16.735 -17.361  1.00 61.88      A    N  
ANISOU  426  N   ILE A  61     7414   7485   8614    714     41   -846  A    N  
ATOM    427  CA  ILE A  61      32.881 -15.921 -16.225  1.00 64.71      A    C  
ANISOU  427  CA  ILE A  61     7815   7804   8967    641     17   -708  A    C  
ATOM    428  C   ILE A  61      33.999 -15.766 -15.166  1.00 67.14      A    C  
ANISOU  428  C   ILE A  61     8097   8132   9279    676     11   -596  A    C  
ATOM    429  O   ILE A  61      34.246 -14.672 -14.648  1.00 65.88      A    O  
ANISOU  429  O   ILE A  61     7932   8049   9050    616     -3   -497  A    O  
ATOM    430  CB  ILE A  61      31.557 -16.449 -15.619  1.00 58.89      A    C  
ANISOU  430  CB  ILE A  61     7156   6888   8333    604      7   -708  A    C  
ATOM    431  CG1 ILE A  61      30.856 -15.350 -14.833  1.00 67.49      A    C  
ANISOU  431  CG1 ILE A  61     8289   7969   9385    506    -11   -593  A    C  
ATOM    432  CG2 ILE A  61      31.806 -17.645 -14.752  1.00 72.32      A    C  
ANISOU  432  CG2 ILE A  61     8879   8436  10163    678     16   -692  A    C  
ATOM    433  CD1 ILE A  61      29.405 -15.623 -14.601  1.00 79.11      A    C  
ANISOU  433  CD1 ILE A  61     9824   9303  10930    453    -16   -609  A    C  
ATOM    434  N   THR A  62      34.704 -16.848 -14.876  1.00 67.31      A    N  
ANISOU  434  N   THR A  62     8099   8093   9384    775     20   -614  A    N  
ATOM    435  CA  THR A  62      35.732 -16.803 -13.849  1.00 70.15      A    C  
ANISOU  435  CA  THR A  62     8429   8475   9751    816      7   -506  A    C  
ATOM    436  C   THR A  62      36.870 -15.893 -14.261  1.00 67.40      A    C  
ANISOU  436  C   THR A  62     7997   8317   9294    811      8   -484  A    C  
ATOM    437  O   THR A  62      37.452 -15.219 -13.427  1.00 78.46      A    O  
ANISOU  437  O   THR A  62     9378   9777  10657    784    -14   -381  A    O  
ATOM    438  CB  THR A  62      36.278 -18.188 -13.582  1.00 71.76      A    C  
ANISOU  438  CB  THR A  62     8619   8578  10069    937     21   -530  A    C  
ATOM    439  CG2 THR A  62      35.256 -18.991 -12.812  1.00 63.80      A    C  
ANISOU  439  CG2 THR A  62     7695   7370   9177    936     21   -508  A    C  
ATOM    440  OG1 THR A  62      36.511 -18.827 -14.837  1.00 75.59      A    O  
ANISOU  440  OG1 THR A  62     9064   9089  10568    996     56   -671  A    O  
ATOM    441  N   ALA A  63      37.185 -15.878 -15.550  1.00 59.82      A    N  
ANISOU  441  N   ALA A  63     6988   7457   8285    833     37   -584  A    N  
ATOM    442  CA  ALA A  63      38.178 -14.947 -16.079  1.00 58.83      A    C  
ANISOU  442  CA  ALA A  63     6783   7517   8054    818     49   -566  A    C  
ATOM    443  C   ALA A  63      37.733 -13.511 -15.849  1.00 68.33      A    C  
ANISOU  443  C   ALA A  63     8008   8784   9171    698     35   -484  A    C  
ATOM    444  O   ALA A  63      38.562 -12.642 -15.577  1.00 68.40      A    O  
ANISOU  444  O   ALA A  63     7964   8903   9122    667     33   -414  A    O  
ATOM    445  CB  ALA A  63      38.427 -15.193 -17.584  1.00 48.71      A    C  
ANISOU  445  CB  ALA A  63     5454   6330   6725    860     90   -692  A    C  
ATOM    446  N   LEU A  64      36.423 -13.274 -15.963  1.00 64.59      A    N  
ANISOU  446  N   LEU A  64     7608   8237   8698    630     28   -496  A    N  
ATOM    447  CA  LEU A  64      35.849 -11.950 -15.752  1.00 60.17      A    C  
ANISOU  447  CA  LEU A  64     7076   7713   8071    519     21   -421  A    C  
ATOM    448  C   LEU A  64      35.970 -11.570 -14.300  1.00 60.05      A    C  
ANISOU  448  C   LEU A  64     7089   7646   8083    480     -6   -310  A    C  
ATOM    449  O   LEU A  64      36.286 -10.423 -13.968  1.00 64.10      A    O  
ANISOU  449  O   LEU A  64     7583   8236   8534    410     -6   -238  A    O  
ATOM    450  CB  LEU A  64      34.376 -11.929 -16.145  1.00 58.48      A    C  
ANISOU  450  CB  LEU A  64     6931   7421   7869    468     17   -460  A    C  
ATOM    451  CG  LEU A  64      34.093 -12.018 -17.640  1.00 64.61      A    C  
ANISOU  451  CG  LEU A  64     7682   8279   8588    482     37   -565  A    C  
ATOM    452  CD1 LEU A  64      32.598 -12.156 -17.876  1.00 71.56      A    C  
ANISOU  452  CD1 LEU A  64     8625   9068   9495    437     22   -605  A    C  
ATOM    453  CD2 LEU A  64      34.664 -10.812 -18.367  1.00 52.64      A    C  
ANISOU  453  CD2 LEU A  64     6111   6934   6954    443     61   -528  A    C  
ATOM    454  N   ARG A  65      35.686 -12.542 -13.439  1.00 49.78      A    N  
ANISOU  454  N   ARG A  65     5833   6210   6872    525    -24   -298  A    N  
ATOM    455  CA  ARG A  65      35.836 -12.384 -11.999  1.00 58.00      A    C  
ANISOU  455  CA  ARG A  65     6901   7201   7935    505    -52   -195  A    C  
ATOM    456  C   ARG A  65      37.256 -11.956 -11.654  1.00 65.18      A    C  
ANISOU  456  C   ARG A  65     7729   8240   8796    524    -63   -146  A    C  
ATOM    457  O   ARG A  65      37.468 -10.929 -11.011  1.00 62.27      A    O  
ANISOU  457  O   ARG A  65     7356   7929   8374    448    -76    -75  A    O  
ATOM    458  CB  ARG A  65      35.531 -13.716 -11.315  1.00 62.03      A    C  
ANISOU  458  CB  ARG A  65     7456   7558   8552    580    -61   -195  A    C  
ATOM    459  CG  ARG A  65      35.192 -13.633  -9.835  1.00 67.89      A    C  
ANISOU  459  CG  ARG A  65     8259   8218   9319    549    -85    -89  A    C  
ATOM    460  CD  ARG A  65      34.774 -15.010  -9.368  1.00 87.05      A    C  
ANISOU  460  CD  ARG A  65    10732  10483  11860    626    -81    -92  A    C  
ATOM    461  NE  ARG A  65      35.692 -15.999  -9.929  1.00111.27      A    N  
ANISOU  461  NE  ARG A  65    13736  13566  14974    741    -71   -149  A    N  
ATOM    462  CZ  ARG A  65      35.900 -17.207  -9.418  1.00119.01      A    C  
ANISOU  462  CZ  ARG A  65    14727  14439  16054    837    -67   -131  A    C  
ATOM    463  NH1 ARG A  65      35.247 -17.585  -8.322  1.00120.18      A    N1+
ANISOU  463  NH1 ARG A  65    14947  14458  16258    831    -74    -51  A    N1+
ATOM    464  NH2 ARG A  65      36.764 -18.032 -10.001  1.00114.85      A    N  
ANISOU  464  NH2 ARG A  65    14137  13931  15572    943    -52   -188  A    N  
ATOM    465  N   GLU A  66      38.221 -12.762 -12.096  1.00 70.57      A    N  
ANISOU  465  N   GLU A  66     8344   8967   9504    625    -56   -190  A    N  
ATOM    466  CA  GLU A  66      39.632 -12.529 -11.831  1.00 67.41      A    C  
ANISOU  466  CA  GLU A  66     7850   8691   9071    659    -67   -151  A    C  
ATOM    467  C   GLU A  66      40.051 -11.163 -12.325  1.00 66.46      A    C  
ANISOU  467  C   GLU A  66     7678   8717   8856    572    -51   -139  A    C  
ATOM    468  O   GLU A  66      40.626 -10.381 -11.585  1.00 78.95      A    O  
ANISOU  468  O   GLU A  66     9228  10368  10400    520    -72    -70  A    O  
ATOM    469  CB  GLU A  66      40.487 -13.603 -12.491  1.00 65.92      A    C  
ANISOU  469  CB  GLU A  66     7593   8526   8928    785    -48   -217  A    C  
ATOM    470  CG  GLU A  66      41.961 -13.476 -12.189  1.00 75.89      A    C  
ANISOU  470  CG  GLU A  66     8748   9915  10170    832    -61   -175  A    C  
ATOM    471  CD  GLU A  66      42.779 -14.610 -12.792  1.00100.57      A    C  
ANISOU  471  CD  GLU A  66    11806  13051  13356    967    -36   -239  A    C  
ATOM    472  OE1 GLU A  66      42.187 -15.445 -13.520  1.00102.27      A    O  
ANISOU  472  OE1 GLU A  66    12061  13175  13621   1016     -5   -328  A    O  
ATOM    473  OE2 GLU A  66      44.013 -14.669 -12.538  1.00110.82      A    O1-
ANISOU  473  OE2 GLU A  66    13007  14447  14652   1023    -46   -205  A    O1-
ATOM    474  N   ILE A  67      39.760 -10.877 -13.583  1.00 60.39      A    N  
ANISOU  474  N   ILE A  67     6900   7997   8048    555    -13   -206  A    N  
ATOM    475  CA  ILE A  67      40.028  -9.558 -14.141  1.00 53.26      A    C  
ANISOU  475  CA  ILE A  67     5956   7220   7059    471     13   -186  A    C  
ATOM    476  C   ILE A  67      39.308  -8.451 -13.384  1.00 62.33      A    C  
ANISOU  476  C   ILE A  67     7166   8333   8185    353      1   -112  A    C  
ATOM    477  O   ILE A  67      39.747  -7.315 -13.394  1.00 68.29      A    O  
ANISOU  477  O   ILE A  67     7882   9179   8887    278     16    -71  A    O  
ATOM    478  CB  ILE A  67      39.588  -9.474 -15.606  1.00 46.49      A    C  
ANISOU  478  CB  ILE A  67     5098   6410   6158    474     55   -262  A    C  
ATOM    479  CG1 ILE A  67      40.424 -10.411 -16.463  1.00 48.98      A    C  
ANISOU  479  CG1 ILE A  67     5343   6785   6481    584     80   -345  A    C  
ATOM    480  CG2 ILE A  67      39.718  -8.061 -16.126  1.00 42.02      A    C  
ANISOU  480  CG2 ILE A  67     4501   5957   5508    383     87   -221  A    C  
ATOM    481  CD1 ILE A  67      40.045 -10.362 -17.898  1.00 48.05      A    C  
ANISOU  481  CD1 ILE A  67     5222   6730   6306    590    120   -426  A    C  
ATOM    482  N   LYS A  68      38.182  -8.758 -12.752  1.00 69.96      A    N  
ANISOU  482  N   LYS A  68     8226   9162   9194    333    -20    -98  A    N  
ATOM    483  CA  LYS A  68      37.496  -7.727 -11.997  1.00 68.54      A    C  
ANISOU  483  CA  LYS A  68     8102   8943   8995    225    -25    -31  A    C  
ATOM    484  C   LYS A  68      38.405  -7.409 -10.830  1.00 68.50      A    C  
ANISOU  484  C   LYS A  68     8064   8982   8982    206    -55     31  A    C  
ATOM    485  O   LYS A  68      38.771  -6.256 -10.585  1.00 73.40      A    O  
ANISOU  485  O   LYS A  68     8657   9675   9557    121    -47     70  A    O  
ATOM    486  CB  LYS A  68      36.134  -8.210 -11.495  1.00 67.93      A    C  
ANISOU  486  CB  LYS A  68     8128   8710   8974    215    -38    -29  A    C  
ATOM    487  CG  LYS A  68      35.305  -7.121 -10.786  1.00 77.67      A    C  
ANISOU  487  CG  LYS A  68     9425   9897  10191    104    -33     34  A    C  
ATOM    488  CD  LYS A  68      34.040  -7.666 -10.101  1.00 84.52      A    C  
ANISOU  488  CD  LYS A  68    10387  10607  11118     98    -44     45  A    C  
ATOM    489  CE  LYS A  68      34.367  -8.513  -8.876  1.00 85.93      A    C  
ANISOU  489  CE  LYS A  68    10587  10723  11339    148    -76     83  A    C  
ATOM    490  NZ  LYS A  68      33.445  -9.679  -8.720  1.00 86.07      A    N1+
ANISOU  490  NZ  LYS A  68    10669  10595  11440    199    -79     61  A    N1+
ATOM    491  N   ILE A  69      38.800  -8.471 -10.148  1.00 64.34      A    N  
ANISOU  491  N   ILE A  69     7533   8413   8501    290    -89     39  A    N  
ATOM    492  CA  ILE A  69      39.543  -8.387  -8.901  1.00 73.21      A    C  
ANISOU  492  CA  ILE A  69     8632   9569   9616    287   -130    102  A    C  
ATOM    493  C   ILE A  69      40.950  -7.796  -9.069  1.00 74.16      A    C  
ANISOU  493  C   ILE A  69     8636   9851   9691    278   -134    108  A    C  
ATOM    494  O   ILE A  69      41.391  -7.007  -8.231  1.00 75.92      A    O  
ANISOU  494  O   ILE A  69     8837  10132   9877    208   -157    153  A    O  
ATOM    495  CB  ILE A  69      39.595  -9.785  -8.210  1.00 62.91      A    C  
ANISOU  495  CB  ILE A  69     7349   8177   8377    396   -163    119  A    C  
ATOM    496  CG1 ILE A  69      38.173 -10.280  -7.923  1.00 54.64      A    C  
ANISOU  496  CG1 ILE A  69     6417   6964   7381    387   -155    121  A    C  
ATOM    497  CG2 ILE A  69      40.408  -9.736  -6.942  1.00 61.63      A    C  
ANISOU  497  CG2 ILE A  69     7156   8069   8194    403   -212    191  A    C  
ATOM    498  CD1 ILE A  69      38.110 -11.629  -7.270  1.00 58.90      A    C  
ANISOU  498  CD1 ILE A  69     6986   7398   7996    488   -175    144  A    C  
ATOM    499  N   LEU A  70      41.642  -8.162 -10.148  1.00 63.38      A    N  
ANISOU  499  N   LEU A  70     7194   8561   8328    345   -107     56  A    N  
ATOM    500  CA  LEU A  70      43.005  -7.682 -10.387  1.00 54.91      A    C  
ANISOU  500  CA  LEU A  70     6000   7644   7221    344   -103     59  A    C  
ATOM    501  C   LEU A  70      43.053  -6.205 -10.706  1.00 62.67      A    C  
ANISOU  501  C   LEU A  70     6962   8704   8148    220    -69     72  A    C  
ATOM    502  O   LEU A  70      44.088  -5.551 -10.523  1.00 78.40      A    O  
ANISOU  502  O   LEU A  70     8863  10812  10115    181    -72     91  A    O  
ATOM    503  CB  LEU A  70      43.665  -8.421 -11.536  1.00 52.67      A    C  
ANISOU  503  CB  LEU A  70     5642   7419   6952    446    -70     -3  A    C  
ATOM    504  CG  LEU A  70      43.979  -9.891 -11.339  1.00 56.69      A    C  
ANISOU  504  CG  LEU A  70     6139   7872   7528    584    -92    -22  A    C  
ATOM    505  CD1 LEU A  70      44.508 -10.422 -12.651  1.00 62.39      A    C  
ANISOU  505  CD1 LEU A  70     6794   8654   8257    667    -44   -101  A    C  
ATOM    506  CD2 LEU A  70      44.989 -10.081 -10.212  1.00 52.28      A    C  
ANISOU  506  CD2 LEU A  70     5513   7369   6981    619   -146     41  A    C  
ATOM    507  N   GLN A  71      41.938  -5.689 -11.205  1.00 50.18      A    N  
ANISOU  507  N   GLN A  71     5457   7055   6553    159    -35     64  A    N  
ATOM    508  CA  GLN A  71      41.858  -4.291 -11.574  1.00 52.15      A    C  
ANISOU  508  CA  GLN A  71     5696   7358   6760     46      7     84  A    C  
ATOM    509  C   GLN A  71      41.602  -3.484 -10.342  1.00 59.35      A    C  
ANISOU  509  C   GLN A  71     6651   8232   7669    -54    -18    134  A    C  
ATOM    510  O   GLN A  71      41.836  -2.279 -10.305  1.00 71.96      A    O  
ANISOU  510  O   GLN A  71     8222   9878   9242   -154     10    156  A    O  
ATOM    511  CB  GLN A  71      40.741  -4.081 -12.580  1.00 44.03      A    C  
ANISOU  511  CB  GLN A  71     4733   6278   5721     29     50     63  A    C  
ATOM    512  CG  GLN A  71      40.998  -4.847 -13.839  1.00 57.66      A    C  
ANISOU  512  CG  GLN A  71     6417   8055   7436    123     75      2  A    C  
ATOM    513  CD  GLN A  71      39.988  -4.607 -14.915  1.00 58.33      A    C  
ANISOU  513  CD  GLN A  71     6551   8118   7493    108    113    -22  A    C  
ATOM    514  NE2 GLN A  71      40.472  -4.557 -16.144  1.00 55.02      A    N  
ANISOU  514  NE2 GLN A  71     6070   7806   7028    142    156    -56  A    N  
ATOM    515  OE1 GLN A  71      38.783  -4.496 -14.663  1.00 68.00      A    O  
ANISOU  515  OE1 GLN A  71     7864   9238   8734     70    103     -9  A    O  
ATOM    516  N   LEU A  72      41.129  -4.176  -9.323  1.00 61.61      A    N  
ANISOU  516  N   LEU A  72     7003   8426   7981    -24    -66    150  A    N  
ATOM    517  CA  LEU A  72      40.710  -3.531  -8.095  1.00 74.08      A    C  
ANISOU  517  CA  LEU A  72     8640   9956   9551   -112    -88    191  A    C  
ATOM    518  C   LEU A  72      41.839  -3.551  -7.072  1.00 75.44      A    C  
ANISOU  518  C   LEU A  72     8743  10217   9704   -111   -141    212  A    C  
ATOM    519  O   LEU A  72      42.091  -2.560  -6.391  1.00 72.66      A    O  
ANISOU  519  O   LEU A  72     8379   9905   9323   -212   -146    228  A    O  
ATOM    520  CB  LEU A  72      39.458  -4.219  -7.531  1.00 60.71      A    C  
ANISOU  520  CB  LEU A  72     7063   8115   7890    -86   -104    203  A    C  
ATOM    521  CG  LEU A  72      39.266  -3.874  -6.065  1.00 50.01      A    C  
ANISOU  521  CG  LEU A  72     5757   6725   6519   -147   -138    246  A    C  
ATOM    522  CD1 LEU A  72      38.636  -2.517  -5.936  1.00 55.78      A    C  
ANISOU  522  CD1 LEU A  72     6531   7430   7230   -275    -98    255  A    C  
ATOM    523  CD2 LEU A  72      38.450  -4.920  -5.388  1.00 55.52      A    C  
ANISOU  523  CD2 LEU A  72     6541   7303   7251    -85   -163    266  A    C  
ATOM    524  N   LEU A  73      42.509  -4.691  -6.974  1.00 75.03      A    N  
ANISOU  524  N   LEU A  73     8644  10194   9671      3   -179    210  A    N  
ATOM    525  CA  LEU A  73      43.625  -4.852  -6.062  1.00 66.87      A    C  
ANISOU  525  CA  LEU A  73     7532   9257   8619     24   -237    236  A    C  
ATOM    526  C   LEU A  73      44.881  -4.244  -6.636  1.00 62.30      A    C  
ANISOU  526  C   LEU A  73     6819   8829   8022      0   -222    215  A    C  
ATOM    527  O   LEU A  73      45.484  -4.810  -7.531  1.00 76.95      A    O  
ANISOU  527  O   LEU A  73     8604  10736   9898     84   -203    190  A    O  
ATOM    528  CB  LEU A  73      43.854  -6.323  -5.804  1.00 62.69      A    C  
ANISOU  528  CB  LEU A  73     6996   8695   8127    168   -277    251  A    C  
ATOM    529  CG  LEU A  73      42.663  -6.943  -5.082  1.00 66.06      A    C  
ANISOU  529  CG  LEU A  73     7552   8971   8578    188   -290    281  A    C  
ATOM    530  CD1 LEU A  73      43.065  -8.277  -4.497  1.00 67.73      A    C  
ANISOU  530  CD1 LEU A  73     7749   9161   8824    319   -336    318  A    C  
ATOM    531  CD2 LEU A  73      42.180  -6.020  -3.986  1.00 63.89      A    C  
ANISOU  531  CD2 LEU A  73     7338   8681   8255     72   -307    314  A    C  
ATOM    532  N   LYS A  74      45.256  -3.077  -6.126  1.00 58.71      A    N  
ANISOU  532  N   LYS A  74     6332   8442   7534   -119   -225    222  A    N  
ATOM    533  CA  LYS A  74      46.468  -2.392  -6.558  1.00 61.16      A    C  
ANISOU  533  CA  LYS A  74     6509   8895   7833   -161   -209    204  A    C  
ATOM    534  C   LYS A  74      47.349  -2.086  -5.359  1.00 65.51      A    C  
ANISOU  534  C   LYS A  74     6990   9545   8355   -206   -277    218  A    C  
ATOM    535  O   LYS A  74      47.053  -1.191  -4.576  1.00 59.41      A    O  
ANISOU  535  O   LYS A  74     6257   8760   7556   -322   -286    219  A    O  
ATOM    536  CB  LYS A  74      46.131  -1.120  -7.322  1.00 47.84      A    C  
ANISOU  536  CB  LYS A  74     4832   7203   6142   -278   -132    190  A    C  
ATOM    537  CG  LYS A  74      45.396  -1.398  -8.643  1.00 69.86      A    C  
ANISOU  537  CG  LYS A  74     7669   9928   8946   -228    -68    176  A    C  
ATOM    538  CD  LYS A  74      46.132  -2.408  -9.516  1.00 77.29      A    C  
ANISOU  538  CD  LYS A  74     8530  10937   9900    -99    -63    152  A    C  
ATOM    539  CE  LYS A  74      45.501  -2.537 -10.894  1.00 81.47      A    C  
ANISOU  539  CE  LYS A  74     9095  11432  10428    -65      3    127  A    C  
ATOM    540  NZ  LYS A  74      46.523  -2.920 -11.911  1.00 88.45      A    N1+
ANISOU  540  NZ  LYS A  74     9867  12431  11310     11     36     97  A    N1+
ATOM    541  N   HIS A  75      48.440  -2.834  -5.225  1.00 61.56      A    N  
ANISOU  541  N   HIS A  75     6382   9148   7861   -113   -325    225  A    N  
ATOM    542  CA  HIS A  75      49.185  -2.812  -3.982  1.00 54.99      A    C  
ANISOU  542  CA  HIS A  75     5489   8409   6995   -129   -408    245  A    C  
ATOM    543  C   HIS A  75      50.531  -3.547  -4.115  1.00 66.49      A    C  
ANISOU  543  C   HIS A  75     6796  10000   8468    -21   -449    253  A    C  
ATOM    544  O   HIS A  75      50.644  -4.538  -4.841  1.00 68.01      A    O  
ANISOU  544  O   HIS A  75     6972  10168   8701    108   -429    255  A    O  
ATOM    545  CB  HIS A  75      48.303  -3.392  -2.873  1.00 44.45      A    C  
ANISOU  545  CB  HIS A  75     4276   6976   5637    -99   -459    285  A    C  
ATOM    546  CG  HIS A  75      48.977  -3.488  -1.541  1.00 57.65      A    C  
ANISOU  546  CG  HIS A  75     5899   8748   7259   -100   -552    314  A    C  
ATOM    547  CD2 HIS A  75      48.679  -2.917  -0.352  1.00 56.94      A    C  
ANISOU  547  CD2 HIS A  75     5860   8666   7109   -191   -594    322  A    C  
ATOM    548  ND1 HIS A  75      50.082  -4.277  -1.321  1.00 65.27      A    N  
ANISOU  548  ND1 HIS A  75     6746   9827   8227      8   -613    341  A    N  
ATOM    549  CE1 HIS A  75      50.452  -4.171  -0.057  1.00 60.40      A    C  
ANISOU  549  CE1 HIS A  75     6108   9294   7549    -18   -696    368  A    C  
ATOM    550  NE2 HIS A  75      49.620  -3.347   0.551  1.00 53.12      A    N  
ANISOU  550  NE2 HIS A  75     5288   8311   6583   -141   -685    352  A    N  
ATOM    551  N   GLU A  76      51.543  -3.041  -3.408  1.00 67.67      A    N  
ANISOU  551  N   GLU A  76     6834  10290   8588    -77   -504    252  A    N  
ATOM    552  CA  GLU A  76      52.937  -3.443  -3.603  1.00 64.13      A    C  
ANISOU  552  CA  GLU A  76     6215   9993   8157     -3   -535    253  A    C  
ATOM    553  C   GLU A  76      53.187  -4.912  -3.333  1.00 69.64      A    C  
ANISOU  553  C   GLU A  76     6898  10684   8877    176   -588    301  A    C  
ATOM    554  O   GLU A  76      54.213  -5.466  -3.740  1.00 72.99      A    O  
ANISOU  554  O   GLU A  76     7193  11206   9336    273   -595    304  A    O  
ATOM    555  CB  GLU A  76      53.874  -2.610  -2.727  1.00 63.56      A    C  
ANISOU  555  CB  GLU A  76     6030  10073   8045   -107   -597    241  A    C  
ATOM    556  CG  GLU A  76      55.217  -2.311  -3.401  1.00 88.08      A    C  
ANISOU  556  CG  GLU A  76     8951  13332  11184   -113   -578    214  A    C  
ATOM    557  CD  GLU A  76      56.313  -1.942  -2.404  1.00118.79      A    C  
ANISOU  557  CD  GLU A  76    12702  17393  15040   -166   -669    210  A    C  
ATOM    558  OE1 GLU A  76      56.028  -1.133  -1.489  1.00131.12      A    O  
ANISOU  558  OE1 GLU A  76    14306  18962  16551   -294   -707    190  A    O  
ATOM    559  OE2 GLU A  76      57.454  -2.462  -2.534  1.00120.19      A    O1-
ANISOU  559  OE2 GLU A  76    12724  17701  15241    -79   -704    222  A    O1-
ATOM    560  N   ASN A  77      52.252  -5.533  -2.631  1.00 72.38      A    N  
ANISOU  560  N   ASN A  77     7376  10914   9210    222   -619    341  A    N  
ATOM    561  CA  ASN A  77      52.343  -6.945  -2.296  1.00 71.94      A    C  
ANISOU  561  CA  ASN A  77     7326  10825   9184    391   -662    397  A    C  
ATOM    562  C   ASN A  77      51.324  -7.808  -3.049  1.00 70.77      A    C  
ANISOU  562  C   ASN A  77     7297  10500   9094    478   -598    392  A    C  
ATOM    563  O   ASN A  77      51.137  -8.985  -2.770  1.00 70.18      A    O  
ANISOU  563  O   ASN A  77     7258  10352   9056    609   -619    437  A    O  
ATOM    564  CB  ASN A  77      52.191  -7.103  -0.796  1.00 68.70      A    C  
ANISOU  564  CB  ASN A  77     6958  10432   8713    388   -752    459  A    C  
ATOM    565  CG  ASN A  77      53.374  -6.568  -0.057  1.00 81.36      A    C  
ANISOU  565  CG  ASN A  77     8419  12229  10263    341   -830    464  A    C  
ATOM    566  ND2 ASN A  77      54.558  -6.847  -0.582  1.00 84.72      A    N  
ANISOU  566  ND2 ASN A  77     8686  12775  10727    412   -837    458  A    N  
ATOM    567  OD1 ASN A  77      53.240  -5.903   0.969  1.00 90.32      A    O  
ANISOU  567  OD1 ASN A  77     9581  13412  11323    240   -883    468  A    O  
ATOM    568  N   VAL A  78      50.662  -7.209  -4.018  1.00 67.78      A    N  
ANISOU  568  N   VAL A  78     6975  10054   8726    403   -519    337  A    N  
ATOM    569  CA  VAL A  78      49.766  -7.965  -4.849  1.00 62.87      A    C  
ANISOU  569  CA  VAL A  78     6448   9285   8155    476   -460    316  A    C  
ATOM    570  C   VAL A  78      50.219  -7.871  -6.286  1.00 75.30      A    C  
ANISOU  570  C   VAL A  78     7948  10905   9758    497   -388    256  A    C  
ATOM    571  O   VAL A  78      50.506  -6.789  -6.811  1.00 75.57      A    O  
ANISOU  571  O   VAL A  78     7932  11016   9764    391   -350    224  A    O  
ATOM    572  CB  VAL A  78      48.337  -7.459  -4.730  1.00 55.53      A    C  
ANISOU  572  CB  VAL A  78     5672   8219   7206    380   -431    309  A    C  
ATOM    573  CG1 VAL A  78      47.437  -8.164  -5.751  1.00 48.65      A    C  
ANISOU  573  CG1 VAL A  78     4883   7212   6388    445   -369    273  A    C  
ATOM    574  CG2 VAL A  78      47.849  -7.680  -3.320  1.00 45.93      A    C  
ANISOU  574  CG2 VAL A  78     4536   6952   5962    374   -494    371  A    C  
ATOM    575  N   VAL A  79      50.303  -9.036  -6.903  1.00 79.33      A    N  
ANISOU  575  N   VAL A  79     8449  11366  10327    637   -365    241  A    N  
ATOM    576  CA  VAL A  79      50.675  -9.145  -8.291  1.00 71.23      A    C  
ANISOU  576  CA  VAL A  79     7362  10377   9324    678   -292    178  A    C  
ATOM    577  C   VAL A  79      49.919  -8.067  -9.062  1.00 67.94      A    C  
ANISOU  577  C   VAL A  79     7008   9937   8868    550   -230    138  A    C  
ATOM    578  O   VAL A  79      48.843  -7.651  -8.649  1.00 69.01      A    O  
ANISOU  578  O   VAL A  79     7261   9975   8983    470   -236    152  A    O  
ATOM    579  CB  VAL A  79      50.385 -10.572  -8.792  1.00 68.54      A    C  
ANISOU  579  CB  VAL A  79     7059   9929   9054    831   -269    153  A    C  
ATOM    580  CG1 VAL A  79      49.167 -10.600  -9.691  1.00 54.37      A    C  
ANISOU  580  CG1 VAL A  79     5382   8013   7263    803   -208     95  A    C  
ATOM    581  CG2 VAL A  79      51.623 -11.160  -9.454  1.00 76.71      A    C  
ANISOU  581  CG2 VAL A  79     7952  11066  10128    945   -245    126  A    C  
ATOM    582  N   ASN A  80      50.507  -7.591 -10.156  1.00 76.32      A    N  
ANISOU  582  N   ASN A  80     7987  11095   9919    532   -168     97  A    N  
ATOM    583  CA  ASN A  80      50.002  -6.422 -10.880  1.00 72.93      A    C  
ANISOU  583  CA  ASN A  80     7591  10672   9446    408   -107     76  A    C  
ATOM    584  C   ASN A  80      49.607  -6.701 -12.328  1.00 78.90      A    C  
ANISOU  584  C   ASN A  80     8371  11406  10200    454    -29     19  A    C  
ATOM    585  O   ASN A  80      50.453  -7.012 -13.178  1.00 73.63      A    O  
ANISOU  585  O   ASN A  80     7606  10831   9540    523     13    -15  A    O  
ATOM    586  CB  ASN A  80      51.043  -5.298 -10.852  1.00 72.17      A    C  
ANISOU  586  CB  ASN A  80     7372  10724   9324    312    -95     89  A    C  
ATOM    587  CG  ASN A  80      50.589  -4.060 -11.601  1.00 72.54      A    C  
ANISOU  587  CG  ASN A  80     7449  10775   9337    187    -23     80  A    C  
ATOM    588  ND2 ASN A  80      51.142  -3.858 -12.799  1.00 65.55      A    N  
ANISOU  588  ND2 ASN A  80     6486   9977   8444    203     51     54  A    N  
ATOM    589  OD1 ASN A  80      49.754  -3.287 -11.107  1.00 71.26      A    O  
ANISOU  589  OD1 ASN A  80     7378  10541   9157     81    -30    102  A    O  
ATOM    590  N   LEU A  81      48.317  -6.572 -12.613  1.00 81.62      A    N  
ANISOU  590  N   LEU A  81     8842  11637  10531    415     -9      7  A    N  
ATOM    591  CA  LEU A  81      47.849  -6.759 -13.976  1.00 73.86      A    C  
ANISOU  591  CA  LEU A  81     7888  10645   9532    447     58    -49  A    C  
ATOM    592  C   LEU A  81      48.080  -5.476 -14.750  1.00 65.99      A    C  
ANISOU  592  C   LEU A  81     6846   9746   8481    346    121    -39  A    C  
ATOM    593  O   LEU A  81      47.416  -4.484 -14.486  1.00 73.08      A    O  
ANISOU  593  O   LEU A  81     7804  10606   9356    233    126     -3  A    O  
ATOM    594  CB  LEU A  81      46.367  -7.127 -13.992  1.00 58.85      A    C  
ANISOU  594  CB  LEU A  81     6129   8591   7638    445     50    -65  A    C  
ATOM    595  CG  LEU A  81      45.799  -7.226 -15.397  1.00 46.08      A    C  
ANISOU  595  CG  LEU A  81     4542   6976   5991    466    111   -126  A    C  
ATOM    596  CD1 LEU A  81      46.201  -8.548 -16.022  1.00 52.69      A    C  
ANISOU  596  CD1 LEU A  81     5344   7814   6863    605    125   -200  A    C  
ATOM    597  CD2 LEU A  81      44.313  -7.100 -15.333  1.00 50.48      A    C  
ANISOU  597  CD2 LEU A  81     5229   7407   6545    415    102   -125  A    C  
ATOM    598  N   ILE A  82      49.033  -5.499 -15.683  1.00 64.49      A    N  
ANISOU  598  N   ILE A  82     6549   9678   8276    390    174    -67  A    N  
ATOM    599  CA  ILE A  82      49.401  -4.320 -16.477  1.00 65.03      A    C  
ANISOU  599  CA  ILE A  82     6561   9851   8297    303    246    -49  A    C  
ATOM    600  C   ILE A  82      48.358  -3.957 -17.514  1.00 61.69      A    C  
ANISOU  600  C   ILE A  82     6223   9392   7822    274    301    -62  A    C  
ATOM    601  O   ILE A  82      48.004  -2.793 -17.684  1.00 62.29      A    O  
ANISOU  601  O   ILE A  82     6322   9477   7868    167    336    -16  A    O  
ATOM    602  CB  ILE A  82      50.663  -4.562 -17.292  1.00 56.48      A    C  
ANISOU  602  CB  ILE A  82     5340   8909   7209    370    298    -78  A    C  
ATOM    603  CG1 ILE A  82      51.844  -4.845 -16.397  1.00 56.61      A    C  
ANISOU  603  CG1 ILE A  82     5245   8991   7275    401    249    -61  A    C  
ATOM    604  CG2 ILE A  82      50.987  -3.356 -18.111  1.00 46.02      A    C  
ANISOU  604  CG2 ILE A  82     3963   7685   5837    279    380    -50  A    C  
ATOM    605  CD1 ILE A  82      53.013  -5.325 -17.201  1.00 62.40      A    C  
ANISOU  605  CD1 ILE A  82     5845   9849   8014    493    300    -97  A    C  
ATOM    606  N   GLU A  83      47.911  -4.965 -18.246  1.00 66.94      A    N  
ANISOU  606  N   GLU A  83     6929  10025   8480    375    310   -126  A    N  
ATOM    607  CA  GLU A  83      46.927  -4.770 -19.293  1.00 68.89      A    C  
ANISOU  607  CA  GLU A  83     7250  10254   8669    363    353   -149  A    C  
ATOM    608  C   GLU A  83      46.398  -6.108 -19.801  1.00 78.58      A    C  
ANISOU  608  C   GLU A  83     8529  11421   9907    478    341   -238  A    C  
ATOM    609  O   GLU A  83      46.826  -7.169 -19.350  1.00 77.61      A    O  
ANISOU  609  O   GLU A  83     8383  11262   9843    568    308   -276  A    O  
ATOM    610  CB  GLU A  83      47.529  -3.970 -20.439  1.00 55.72      A    C  
ANISOU  610  CB  GLU A  83     5506   8729   6935    336    440   -136  A    C  
ATOM    611  CG  GLU A  83      48.693  -4.637 -21.133  1.00 71.89      A    C  
ANISOU  611  CG  GLU A  83     7443  10895   8976    434    482   -190  A    C  
ATOM    612  CD  GLU A  83      48.950  -4.040 -22.515  1.00 90.20      A    C  
ANISOU  612  CD  GLU A  83     9717  13344  11210    424    576   -189  A    C  
ATOM    613  OE1 GLU A  83      47.975  -3.621 -23.194  1.00101.42      A    O  
ANISOU  613  OE1 GLU A  83    11217  14750  12568    390    600   -180  A    O  
ATOM    614  OE2 GLU A  83      50.125  -3.998 -22.924  1.00 76.59      A    O1-
ANISOU  614  OE2 GLU A  83     7878  11744   9481    454    628   -194  A    O1-
ATOM    615  N   ILE A  84      45.445  -6.053 -20.723  1.00 81.72      A    N  
ANISOU  615  N   ILE A  84     8994  11806  10251    472    368   -271  A    N  
ATOM    616  CA  ILE A  84      44.949  -7.264 -21.355  1.00 70.81      A    C  
ANISOU  616  CA  ILE A  84     7653  10380   8872    571    364   -373  A    C  
ATOM    617  C   ILE A  84      45.122  -7.126 -22.853  1.00 71.55      A    C  
ANISOU  617  C   ILE A  84     7709  10603   8872    599    436   -423  A    C  
ATOM    618  O   ILE A  84      44.936  -6.039 -23.407  1.00 85.27      A    O  
ANISOU  618  O   ILE A  84     9445  12416  10536    525    476   -366  A    O  
ATOM    619  CB  ILE A  84      43.495  -7.546 -20.974  1.00 59.33      A    C  
ANISOU  619  CB  ILE A  84     6322   8776   7443    545    315   -384  A    C  
ATOM    620  CG1 ILE A  84      43.444  -8.045 -19.537  1.00 56.83      A    C  
ANISOU  620  CG1 ILE A  84     6038   8333   7222    552    250   -352  A    C  
ATOM    621  CG2 ILE A  84      42.907  -8.604 -21.870  1.00 62.13      A    C  
ANISOU  621  CG2 ILE A  84     6714   9103   7788    626    322   -498  A    C  
ATOM    622  CD1 ILE A  84      42.119  -7.811 -18.859  1.00 60.50      A    C  
ANISOU  622  CD1 ILE A  84     6613   8663   7711    483    207   -317  A    C  
ATOM    623  N   CYS A  85      45.517  -8.224 -23.492  1.00 58.15      A    N  
ANISOU  623  N   CYS A  85     5981   8934   7178    709    456   -525  A    N  
ATOM    624  CA  CYS A  85      45.894  -8.217 -24.896  1.00 64.75      A    C  
ANISOU  624  CA  CYS A  85     6768   9914   7921    751    530   -585  A    C  
ATOM    625  C   CYS A  85      45.152  -9.289 -25.666  1.00 72.11      A    C  
ANISOU  625  C   CYS A  85     7758  10807   8835    825    527   -714  A    C  
ATOM    626  O   CYS A  85      44.712 -10.296 -25.097  1.00 65.56      A    O  
ANISOU  626  O   CYS A  85     6979   9840   8093    872    479   -772  A    O  
ATOM    627  CB  CYS A  85      47.397  -8.469 -25.059  1.00 74.78      A    C  
ANISOU  627  CB  CYS A  85     7913  11293   9208    817    579   -599  A    C  
ATOM    628  SG  CYS A  85      48.476  -7.126 -24.561  1.00 81.30      A    S  
ANISOU  628  SG  CYS A  85     8638  12221  10032    727    607   -468  A    S  
ATOM    629  N   ARG A  86      45.055  -9.069 -26.975  1.00 75.67      A    N  
ANISOU  629  N   ARG A  86     8197  11384   9171    836    583   -760  A    N  
ATOM    630  CA  ARG A  86      44.412  -9.994 -27.891  1.00 80.36      A    C  
ANISOU  630  CA  ARG A  86     8835  11975   9724    900    588   -899  A    C  
ATOM    631  C   ARG A  86      45.401 -10.510 -28.926  1.00 81.75      A    C  
ANISOU  631  C   ARG A  86     8929  12289   9843    992    665   -992  A    C  
ATOM    632  O   ARG A  86      46.538 -10.058 -28.995  1.00 87.57      A    O  
ANISOU  632  O   ARG A  86     9574  13132  10567   1000    718   -938  A    O  
ATOM    633  CB  ARG A  86      43.271  -9.276 -28.610  1.00 86.07      A    C  
ANISOU  633  CB  ARG A  86     9623  12742  10338    832    582   -879  A    C  
ATOM    634  CG  ARG A  86      43.729  -8.047 -29.350  1.00 90.18      A    C  
ANISOU  634  CG  ARG A  86    10091  13432  10740    785    647   -786  A    C  
ATOM    635  CD  ARG A  86      42.592  -7.140 -29.750  1.00 97.33      A    C  
ANISOU  635  CD  ARG A  86    11060  14358  11561    707    632   -719  A    C  
ATOM    636  NE  ARG A  86      43.120  -5.993 -30.479  1.00108.06      A    N  
ANISOU  636  NE  ARG A  86    12365  15877  12815    670    706   -621  A    N  
ATOM    637  CZ  ARG A  86      43.281  -5.959 -31.798  1.00106.20      A    C  
ANISOU  637  CZ  ARG A  86    12101  15806  12443    711    766   -662  A    C  
ATOM    638  NH1 ARG A  86      42.923  -7.015 -32.525  1.00100.55      A    N1+
ANISOU  638  NH1 ARG A  86    11408  15116  11679    785    754   -814  A    N1+
ATOM    639  NH2 ARG A  86      43.789  -4.872 -32.384  1.00 98.11      A    N  
ANISOU  639  NH2 ARG A  86    11026  14920  11331    674    841   -554  A    N  
ATOM    640  N   THR A  87      44.953 -11.459 -29.732  1.00 86.09      A    N  
ANISOU  640  N   THR A  87     9510  12837  10362   1058    673  -1139  A    N  
ATOM    641  CA  THR A  87      45.678 -11.879 -30.920  1.00 95.27      A    C  
ANISOU  641  CA  THR A  87    10610  14146  11441   1138    753  -1244  A    C  
ATOM    642  C   THR A  87      44.945 -11.294 -32.121  1.00111.02      A    C  
ANISOU  642  C   THR A  87    12640  16275  13269   1099    775  -1262  A    C  
ATOM    643  O   THR A  87      43.840 -10.769 -31.976  1.00121.63      A    O  
ANISOU  643  O   THR A  87    14057  17572  14586   1024    721  -1210  A    O  
ATOM    644  CB  THR A  87      45.704 -13.400 -31.005  1.00 95.89      A    C  
ANISOU  644  CB  THR A  87    10700  14130  11602   1243    751  -1410  A    C  
ATOM    645  CG2 THR A  87      47.005 -13.947 -30.428  1.00 99.03      A    C  
ANISOU  645  CG2 THR A  87    11010  14505  12111   1324    782  -1405  A    C  
ATOM    646  OG1 THR A  87      44.615 -13.927 -30.234  1.00 97.80      A    O  
ANISOU  646  OG1 THR A  87    11034  14182  11942   1218    670  -1431  A    O  
ATOM    647  N   LYS A  88      45.537 -11.367 -33.305  1.00119.72      A    N  
ANISOU  647  N   LYS A  88    13688  17547  14253   1152    854  -1332  A    N  
ATOM    648  CA  LYS A  88      44.870 -10.812 -34.487  1.00135.93      A    C  
ANISOU  648  CA  LYS A  88    15770  19747  16130   1122    875  -1343  A    C  
ATOM    649  C   LYS A  88      44.344 -11.893 -35.438  1.00137.20      A    C  
ANISOU  649  C   LYS A  88    15966  19937  16227   1190    876  -1543  A    C  
ATOM    650  O   LYS A  88      43.318 -11.713 -36.104  1.00129.93      A    O  
ANISOU  650  O   LYS A  88    15102  19069  15197   1157    845  -1577  A    O  
ATOM    651  CB  LYS A  88      45.783  -9.827 -35.231  1.00146.88      A    C  
ANISOU  651  CB  LYS A  88    17077  21335  17395   1112    969  -1248  A    C  
ATOM    652  CG  LYS A  88      47.123 -10.406 -35.680  1.00155.37      A    C  
ANISOU  652  CG  LYS A  88    18056  22506  18471   1205   1058  -1327  A    C  
ATOM    653  CD  LYS A  88      48.072 -10.628 -34.503  1.00160.68      A    C  
ANISOU  653  CD  LYS A  88    18668  23069  19315   1223   1051  -1276  A    C  
ATOM    654  CE  LYS A  88      49.405 -11.191 -34.973  1.00164.86      A    C  
ANISOU  654  CE  LYS A  88    19092  23699  19850   1321   1142  -1350  A    C  
ATOM    655  NZ  LYS A  88      50.288 -11.555 -33.835  1.00160.99      A    N1+
ANISOU  655  NZ  LYS A  88    18537  23102  19529   1352   1124  -1313  A    N1+
ATOM    656  N   GLY A  97      40.693 -17.300 -32.084  1.00 98.49      A    N  
ANISOU  656  N   GLY A  97    11377  13987  12058   1266    569  -2030  A    N  
ATOM    657  CA  GLY A  97      41.288 -16.129 -31.459  1.00115.01      A    C  
ANISOU  657  CA  GLY A  97    13434  16137  14127   1222    570  -1829  A    C  
ATOM    658  C   GLY A  97      41.122 -16.081 -29.943  1.00129.84      A    C  
ANISOU  658  C   GLY A  97    15343  17831  16158   1189    514  -1703  A    C  
ATOM    659  O   GLY A  97      40.059 -16.433 -29.415  1.00128.05      A    O  
ANISOU  659  O   GLY A  97    15189  17453  16009   1150    456  -1719  A    O  
ATOM    660  N   SER A  98      42.170 -15.633 -29.242  1.00132.03      A    N  
ANISOU  660  N   SER A  98    15563  18127  16475   1201    533  -1579  A    N  
ATOM    661  CA  SER A  98      42.185 -15.635 -27.768  1.00117.70      A    C  
ANISOU  661  CA  SER A  98    13769  16155  14797   1180    483  -1462  A    C  
ATOM    662  C   SER A  98      42.676 -14.337 -27.102  1.00100.04      A    C  
ANISOU  662  C   SER A  98    11498  13985  12527   1109    474  -1279  A    C  
ATOM    663  O   SER A  98      42.794 -13.289 -27.736  1.00 97.17      A    O  
ANISOU  663  O   SER A  98    11107  13772  12039   1056    501  -1224  A    O  
ATOM    664  CB  SER A  98      42.990 -16.824 -27.237  1.00110.84      A    C  
ANISOU  664  CB  SER A  98    12865  15179  14069   1288    502  -1516  A    C  
ATOM    665  OG  SER A  98      44.300 -16.820 -27.780  1.00107.43      A    O  
ANISOU  665  OG  SER A  98    12334  14886  13597   1359    570  -1534  A    O  
ATOM    666  N   ILE A  99      42.982 -14.437 -25.814  1.00 82.91      A    N  
ANISOU  666  N   ILE A  99     9328  11703  10472   1109    438  -1189  A    N  
ATOM    667  CA  ILE A  99      43.139 -13.270 -24.961  1.00 73.36      A    C  
ANISOU  667  CA  ILE A  99     8110  10513   9252   1023    411  -1027  A    C  
ATOM    668  C   ILE A  99      44.188 -13.510 -23.867  1.00 78.00      A    C  
ANISOU  668  C   ILE A  99     8639  11060   9937   1066    399   -955  A    C  
ATOM    669  O   ILE A  99      44.158 -14.532 -23.183  1.00 78.05      A    O  
ANISOU  669  O   ILE A  99     8667  10932  10058   1130    372   -983  A    O  
ATOM    670  CB  ILE A  99      41.754 -12.912 -24.349  1.00 58.99      A    C  
ANISOU  670  CB  ILE A  99     6392   8570   7451    933    349   -977  A    C  
ATOM    671  CG1 ILE A  99      41.007 -11.986 -25.291  1.00 64.88      A    C  
ANISOU  671  CG1 ILE A  99     7164   9420   8070    860    361   -970  A    C  
ATOM    672  CG2 ILE A  99      41.854 -12.306 -22.952  1.00 60.80      A    C  
ANISOU  672  CG2 ILE A  99     6633   8727   7741    873    306   -836  A    C  
ATOM    673  CD1 ILE A  99      41.810 -10.810 -25.707  1.00 79.68      A    C  
ANISOU  673  CD1 ILE A  99     8969  11460   9846    821    408   -882  A    C  
ATOM    674  N   TYR A 100      45.119 -12.572 -23.709  1.00 78.86      A    N  
ANISOU  674  N   TYR A 100     8670  11290  10003   1031    418   -861  A    N  
ATOM    675  CA  TYR A 100      46.198 -12.717 -22.729  1.00 75.24      A    C  
ANISOU  675  CA  TYR A 100     8139  10826   9624   1068    403   -793  A    C  
ATOM    676  C   TYR A 100      46.146 -11.669 -21.607  1.00 71.94      A    C  
ANISOU  676  C   TYR A 100     7731  10392   9210    964    354   -655  A    C  
ATOM    677  O   TYR A 100      46.052 -10.472 -21.866  1.00 69.38      A    O  
ANISOU  677  O   TYR A 100     7401  10153   8808    869    371   -594  A    O  
ATOM    678  CB  TYR A 100      47.567 -12.627 -23.415  1.00 76.94      A    C  
ANISOU  678  CB  TYR A 100     8229  11203   9803   1126    470   -812  A    C  
ATOM    679  CG  TYR A 100      47.871 -13.709 -24.440  1.00 86.14      A    C  
ANISOU  679  CG  TYR A 100     9366  12393  10970   1242    527   -953  A    C  
ATOM    680  CD1 TYR A 100      48.241 -14.988 -24.046  1.00 92.83      A    C  
ANISOU  680  CD1 TYR A 100    10198  13140  11934   1357    521  -1012  A    C  
ATOM    681  CD2 TYR A 100      47.823 -13.437 -25.801  1.00 86.51      A    C  
ANISOU  681  CD2 TYR A 100     9400  12568  10902   1240    592  -1026  A    C  
ATOM    682  CE1 TYR A 100      48.536 -15.973 -24.978  1.00 95.64      A    C  
ANISOU  682  CE1 TYR A 100    10527  13511  12300   1463    581  -1150  A    C  
ATOM    683  CE2 TYR A 100      48.114 -14.413 -26.740  1.00 93.61      A    C  
ANISOU  683  CE2 TYR A 100    10274  13497  11796   1344    649  -1167  A    C  
ATOM    684  CZ  TYR A 100      48.470 -15.680 -26.324  1.00100.14      A    C  
ANISOU  684  CZ  TYR A 100    11087  14212  12749   1454    645  -1234  A    C  
ATOM    685  OH  TYR A 100      48.761 -16.652 -27.260  1.00104.15      A    O  
ANISOU  685  OH  TYR A 100    11571  14742  13260   1558    708  -1384  A    O  
ATOM    686  N   LEU A 101      46.211 -12.132 -20.362  1.00 68.34      A    N  
ANISOU  686  N   LEU A 101     7290   9827   8848    985    298   -606  A    N  
ATOM    687  CA  LEU A 101      46.449 -11.263 -19.215  1.00 59.46      A    C  
ANISOU  687  CA  LEU A 101     6155   8707   7731    903    253   -486  A    C  
ATOM    688  C   LEU A 101      47.938 -10.940 -19.141  1.00 66.64      A    C  
ANISOU  688  C   LEU A 101     6928   9756   8636    926    274   -449  A    C  
ATOM    689  O   LEU A 101      48.774 -11.824 -19.311  1.00 72.95      A    O  
ANISOU  689  O   LEU A 101     7655  10580   9481   1038    291   -494  A    O  
ATOM    690  CB  LEU A 101      45.992 -11.951 -17.928  1.00 60.72      A    C  
ANISOU  690  CB  LEU A 101     6378   8711   7981    925    185   -448  A    C  
ATOM    691  CG  LEU A 101      44.535 -11.674 -17.507  1.00 70.28      A    C  
ANISOU  691  CG  LEU A 101     7717   9795   9191    842    151   -426  A    C  
ATOM    692  CD1 LEU A 101      43.573 -11.828 -18.668  1.00 71.17      A    C  
ANISOU  692  CD1 LEU A 101     7888   9887   9264    836    185   -515  A    C  
ATOM    693  CD2 LEU A 101      44.081 -12.543 -16.341  1.00 64.24      A    C  
ANISOU  693  CD2 LEU A 101     7017   8873   8520    882     98   -397  A    C  
ATOM    694  N   VAL A 102      48.282  -9.680 -18.899  1.00 64.43      A    N  
ANISOU  694  N   VAL A 102     6608   9565   8307    821    276   -372  A    N  
ATOM    695  CA  VAL A 102      49.687  -9.290 -18.895  1.00 56.86      A    C  
ANISOU  695  CA  VAL A 102     5511   8749   7345    830    300   -341  A    C  
ATOM    696  C   VAL A 102      50.120  -8.707 -17.557  1.00 64.89      A    C  
ANISOU  696  C   VAL A 102     6494   9769   8390    763    237   -249  A    C  
ATOM    697  O   VAL A 102      49.656  -7.644 -17.164  1.00 68.16      A    O  
ANISOU  697  O   VAL A 102     6951  10175   8772    641    224   -194  A    O  
ATOM    698  CB  VAL A 102      49.992  -8.271 -19.993  1.00 58.82      A    C  
ANISOU  698  CB  VAL A 102     5708   9135   7508    766    377   -340  A    C  
ATOM    699  CG1 VAL A 102      51.471  -8.041 -20.078  1.00 71.94      A    C  
ANISOU  699  CG1 VAL A 102     7216  10939   9177    788    411   -321  A    C  
ATOM    700  CG2 VAL A 102      49.490  -8.763 -21.320  1.00 58.48      A    C  
ANISOU  700  CG2 VAL A 102     5703   9103   7412    823    434   -430  A    C  
ATOM    701  N   PHE A 103      51.021  -9.404 -16.867  1.00 68.11      A    N  
ANISOU  701  N   PHE A 103     6824  10194   8860    846    200   -236  A    N  
ATOM    702  CA  PHE A 103      51.537  -8.954 -15.572  1.00 69.41      A    C  
ANISOU  702  CA  PHE A 103     6944  10382   9046    794    132   -156  A    C  
ATOM    703  C   PHE A 103      52.987  -8.462 -15.628  1.00 74.31      A    C  
ANISOU  703  C   PHE A 103     7400  11171   9664    787    150   -135  A    C  
ATOM    704  O   PHE A 103      53.708  -8.713 -16.597  1.00 75.97      A    O  
ANISOU  704  O   PHE A 103     7522  11471   9872    852    214   -180  A    O  
ATOM    705  CB  PHE A 103      51.474 -10.098 -14.569  1.00 61.57      A    C  
ANISOU  705  CB  PHE A 103     5980   9291   8124    893     63   -138  A    C  
ATOM    706  CG  PHE A 103      50.129 -10.684 -14.424  1.00 63.32      A    C  
ANISOU  706  CG  PHE A 103     6351   9343   8365    906     46   -156  A    C  
ATOM    707  CD1 PHE A 103      49.267 -10.223 -13.450  1.00 62.77      A    C  
ANISOU  707  CD1 PHE A 103     6378   9187   8284    817     -6   -101  A    C  
ATOM    708  CD2 PHE A 103      49.710 -11.685 -15.269  1.00 71.54      A    C  
ANISOU  708  CD2 PHE A 103     7433  10311   9438   1002     87   -236  A    C  
ATOM    709  CE1 PHE A 103      48.014 -10.758 -13.312  1.00 60.44      A    C  
ANISOU  709  CE1 PHE A 103     6215   8736   8013    825    -17   -116  A    C  
ATOM    710  CE2 PHE A 103      48.454 -12.228 -15.140  1.00 75.91      A    C  
ANISOU  710  CE2 PHE A 103     8118  10707  10018   1006     73   -259  A    C  
ATOM    711  CZ  PHE A 103      47.606 -11.764 -14.157  1.00 71.67      A    C  
ANISOU  711  CZ  PHE A 103     7673  10085   9473    918     21   -194  A    C  
ATOM    712  N   ASP A 104      53.413  -7.767 -14.579  1.00 64.77      A    N  
ANISOU  712  N   ASP A 104     6147  10006   8456    706     93    -72  A    N  
ATOM    713  CA  ASP A 104      54.826  -7.526 -14.369  1.00 78.28      A    C  
ANISOU  713  CA  ASP A 104     7693  11868  10184    714     87    -51  A    C  
ATOM    714  C   ASP A 104      55.425  -8.912 -14.172  1.00 83.70      A    C  
ANISOU  714  C   ASP A 104     8322  12547  10935    882     59    -64  A    C  
ATOM    715  O   ASP A 104      54.747  -9.808 -13.683  1.00 81.00      A    O  
ANISOU  715  O   ASP A 104     8074  12077  10626    954     17    -60  A    O  
ATOM    716  CB  ASP A 104      55.040  -6.697 -13.101  1.00 98.10      A    C  
ANISOU  716  CB  ASP A 104    10179  14408  12684    602     12     10  A    C  
ATOM    717  CG  ASP A 104      54.637  -5.245 -13.268  1.00106.21      A    C  
ANISOU  717  CG  ASP A 104    11240  15449  13664    432     49     23  A    C  
ATOM    718  OD1 ASP A 104      54.913  -4.667 -14.345  1.00108.07      A    O  
ANISOU  718  OD1 ASP A 104    11429  15755  13879    397    135      3  A    O  
ATOM    719  OD2 ASP A 104      54.062  -4.679 -12.309  1.00103.60      A    O1-
ANISOU  719  OD2 ASP A 104    10983  15061  13319    336     -4     56  A    O1-
ATOM    720  N   PHE A 105      56.684  -9.110 -14.536  1.00 88.04      A    N  
ANISOU  720  N   PHE A 105     8715  13226  11511    949     87    -74  A    N  
ATOM    721  CA  PHE A 105      57.284 -10.423 -14.342  1.00 80.78      A    C  
ANISOU  721  CA  PHE A 105     7734  12295  10663   1118     65    -81  A    C  
ATOM    722  C   PHE A 105      57.973 -10.488 -12.997  1.00 80.03      A    C  
ANISOU  722  C   PHE A 105     7559  12252  10596   1129    -35     -6  A    C  
ATOM    723  O   PHE A 105      58.714  -9.571 -12.645  1.00 85.79      A    O  
ANISOU  723  O   PHE A 105     8183  13111  11302   1037    -57     24  A    O  
ATOM    724  CB  PHE A 105      58.290 -10.710 -15.440  1.00 85.93      A    C  
ANISOU  724  CB  PHE A 105     8254  13061  11335   1202    150   -133  A    C  
ATOM    725  CG  PHE A 105      59.038 -11.984 -15.247  1.00 93.04      A    C  
ANISOU  725  CG  PHE A 105     9072  13961  12319   1378    135   -137  A    C  
ATOM    726  CD1 PHE A 105      58.449 -13.200 -15.550  1.00 99.45      A    C  
ANISOU  726  CD1 PHE A 105     9973  14634  13180   1503    156   -184  A    C  
ATOM    727  CD2 PHE A 105      60.335 -11.975 -14.773  1.00 88.54      A    C  
ANISOU  727  CD2 PHE A 105     8329  13525  11786   1418    104    -94  A    C  
ATOM    728  CE1 PHE A 105      59.140 -14.383 -15.380  1.00 92.87      A    C  
ANISOU  728  CE1 PHE A 105     9063  13786  12437   1671    151   -185  A    C  
ATOM    729  CE2 PHE A 105      61.029 -13.157 -14.598  1.00 81.63      A    C  
ANISOU  729  CE2 PHE A 105     7373  12648  10996   1591     93    -89  A    C  
ATOM    730  CZ  PHE A 105      60.430 -14.359 -14.901  1.00 82.65      A    C  
ANISOU  730  CZ  PHE A 105     7597  12628  11179   1719    120   -132  A    C  
ATOM    731  N   CYS A 106      57.724 -11.565 -12.249  1.00 79.69      A    N  
ANISOU  731  N   CYS A 106     7564  12111  10604   1241    -94     25  A    N  
ATOM    732  CA  CYS A 106      58.413 -11.816 -10.971  1.00 83.53      A    C  
ANISOU  732  CA  CYS A 106     7971  12654  11115   1282   -193    105  A    C  
ATOM    733  C   CYS A 106      59.479 -12.899 -11.076  1.00 83.68      A    C  
ANISOU  733  C   CYS A 106     7856  12725  11213   1459   -190    113  A    C  
ATOM    734  O   CYS A 106      59.220 -14.002 -11.564  1.00 93.70      A    O  
ANISOU  734  O   CYS A 106     9169  13887  12544   1593   -146     79  A    O  
ATOM    735  CB  CYS A 106      57.426 -12.171  -9.868  1.00 81.55      A    C  
ANISOU  735  CB  CYS A 106     7861  12266  10858   1278   -269    160  A    C  
ATOM    736  SG  CYS A 106      56.425 -10.783  -9.381  1.00 97.11      A    S  
ANISOU  736  SG  CYS A 106     9953  14208  12738   1066   -293    170  A    S  
ATOM    737  N   GLU A 107      60.674 -12.576 -10.593  1.00 77.10      A    N  
ANISOU  737  N   GLU A 107     6855  12056  10384   1460   -236    155  A    N  
ATOM    738  CA  GLU A 107      61.874 -13.358 -10.913  1.00 90.34      A    C  
ANISOU  738  CA  GLU A 107     8368  13822  12135   1613   -214    155  A    C  
ATOM    739  C   GLU A 107      61.911 -14.699 -10.188  1.00 90.80      A    C  
ANISOU  739  C   GLU A 107     8438  13792  12268   1787   -268    215  A    C  
ATOM    740  O   GLU A 107      62.525 -15.643 -10.670  1.00 97.40      A    O  
ANISOU  740  O   GLU A 107     9194  14627  13187   1944   -223    198  A    O  
ATOM    741  CB  GLU A 107      63.166 -12.548 -10.654  1.00 85.51      A    C  
ANISOU  741  CB  GLU A 107     7558  13424  11508   1552   -246    180  A    C  
ATOM    742  CG  GLU A 107      63.228 -11.160 -11.358  1.00157.76      A    C  
ANISOU  742  CG  GLU A 107    16682  22663  20596   1374   -184    130  A    C  
ATOM    743  CD  GLU A 107      62.275 -10.093 -10.768  1.00152.46      A    C  
ANISOU  743  CD  GLU A 107    16141  21941  19846   1191   -226    144  A    C  
ATOM    744  OE1 GLU A 107      61.522 -10.401  -9.825  1.00153.85      A    O  
ANISOU  744  OE1 GLU A 107    16433  22015  20006   1195   -303    187  A    O  
ATOM    745  OE2 GLU A 107      62.272  -8.936 -11.249  1.00142.78      A    O1-
ANISOU  745  OE2 GLU A 107    14902  20771  18577   1043   -177    113  A    O1-
ATOM    746  N   HIS A 108      61.233 -14.778  -9.044  1.00 83.19      A    N  
ANISOU  746  N   HIS A 108     7578  12752  11279   1761   -357    286  A    N  
ATOM    747  CA  HIS A 108      61.263 -15.972  -8.205  1.00 85.99      A    C  
ANISOU  747  CA  HIS A 108     7945  13029  11700   1918   -415    367  A    C  
ATOM    748  C   HIS A 108      59.883 -16.357  -7.741  1.00 91.79      A    C  
ANISOU  748  C   HIS A 108     8883  13567  12427   1903   -430    388  A    C  
ATOM    749  O   HIS A 108      58.970 -15.546  -7.785  1.00104.13      A    O  
ANISOU  749  O   HIS A 108    10564  15082  13919   1755   -423    356  A    O  
ATOM    750  CB  HIS A 108      62.131 -15.734  -6.968  1.00 85.46      A    C  
ANISOU  750  CB  HIS A 108     7753  13115  11604   1921   -532    468  A    C  
ATOM    751  CG  HIS A 108      63.571 -15.511  -7.290  1.00 94.08      A    C  
ANISOU  751  CG  HIS A 108     8624  14403  12721   1956   -529    460  A    C  
ATOM    752  CD2 HIS A 108      64.536 -16.370  -7.692  1.00 93.59      A    C  
ANISOU  752  CD2 HIS A 108     8422  14388  12751   2125   -496    467  A    C  
ATOM    753  ND1 HIS A 108      64.156 -14.263  -7.258  1.00101.62      A    N  
ANISOU  753  ND1 HIS A 108     9474  15530  13609   1804   -551    438  A    N  
ATOM    754  CE1 HIS A 108      65.425 -14.364  -7.607  1.00105.13      A    C  
ANISOU  754  CE1 HIS A 108     9719  16124  14101   1874   -537    435  A    C  
ATOM    755  NE2 HIS A 108      65.680 -15.632  -7.880  1.00108.14      A    N  
ANISOU  755  NE2 HIS A 108    10075  16436  14578   2072   -503    452  A    N  
ATOM    756  N   ASP A 109      59.725 -17.597  -7.294  1.00 83.62      A    N  
ANISOU  756  N   ASP A 109    10282  10715  10776   1296  -2614   1106  A    N  
ATOM    757  CA  ASP A 109      58.585 -17.906  -6.449  1.00 90.91      A    C  
ANISOU  757  CA  ASP A 109    11385  11400  11756   1097  -2580   1108  A    C  
ATOM    758  C   ASP A 109      58.960 -18.770  -5.258  1.00 94.43      A    C  
ANISOU  758  C   ASP A 109    12009  11682  12190   1049  -2684   1188  A    C  
ATOM    759  O   ASP A 109      59.807 -19.657  -5.338  1.00103.36      A    O  
ANISOU  759  O   ASP A 109    13160  12804  13309   1228  -2820   1189  A    O  
ATOM    760  CB  ASP A 109      57.391 -18.448  -7.228  1.00101.63      A    C  
ANISOU  760  CB  ASP A 109    12766  12640  13210   1128  -2560    970  A    C  
ATOM    761  CG  ASP A 109      57.572 -19.860  -7.659  1.00113.63      A    C  
ANISOU  761  CG  ASP A 109    14349  14041  14786   1313  -2702    883  A    C  
ATOM    762  OD1 ASP A 109      57.554 -20.102  -8.885  1.00121.89      A    O  
ANISOU  762  OD1 ASP A 109    15285  15174  15852   1506  -2731    761  A    O  
ATOM    763  OD2 ASP A 109      57.714 -20.722  -6.771  1.00117.66      A    O1-
ANISOU  763  OD2 ASP A 109    15025  14365  15316   1270  -2783    936  A    O1-
ATOM    764  N   LEU A 110      58.316 -18.459  -4.146  1.00 92.19      A    N  
ANISOU  764  N   LEU A 110    11854  11277  11899    812  -2613   1259  A    N  
ATOM    765  CA  LEU A 110      58.685 -18.948  -2.835  1.00 87.06      A    C  
ANISOU  765  CA  LEU A 110    11373  10507  11199    729  -2682   1369  A    C  
ATOM    766  C   LEU A 110      58.805 -20.458  -2.767  1.00 97.40      A    C  
ANISOU  766  C   LEU A 110    12830  11623  12555    860  -2818   1355  A    C  
ATOM    767  O   LEU A 110      59.512 -20.984  -1.918  1.00109.01      A    O  
ANISOU  767  O   LEU A 110    14414  13040  13966    892  -2918   1450  A    O  
ATOM    768  CB  LEU A 110      57.644 -18.480  -1.833  1.00 85.12      A    C  
ANISOU  768  CB  LEU A 110    11251  10140  10950    458  -2561   1418  A    C  
ATOM    769  CG  LEU A 110      57.976 -18.764  -0.387  1.00 92.11      A    C  
ANISOU  769  CG  LEU A 110    12312  10932  11754    350  -2607   1546  A    C  
ATOM    770  CD1 LEU A 110      59.139 -17.880   0.036  1.00 86.31      A    C  
ANISOU  770  CD1 LEU A 110    11477  10410  10906    359  -2637   1617  A    C  
ATOM    771  CD2 LEU A 110      56.740 -18.525   0.465  1.00 94.15      A    C  
ANISOU  771  CD2 LEU A 110    12703  11045  12023     98  -2477   1572  A    C  
ATOM    772  N   ALA A 111      58.097 -21.165  -3.639  1.00 99.57      A    N  
ANISOU  772  N   ALA A 111    13111  11784  12936    938  -2827   1235  A    N  
ATOM    773  CA  ALA A 111      58.201 -22.620  -3.658  1.00100.82      A    C  
ANISOU  773  CA  ALA A 111    13416  11735  13157   1069  -2957   1207  A    C  
ATOM    774  C   ALA A 111      59.599 -23.032  -4.136  1.00107.83      A    C  
ANISOU  774  C   ALA A 111    14220  12759  13991   1350  -3105   1204  A    C  
ATOM    775  O   ALA A 111      60.312 -23.784  -3.456  1.00 98.00      A    O  
ANISOU  775  O   ALA A 111    13102  11427  12708   1434  -3224   1283  A    O  
ATOM    776  CB  ALA A 111      57.120 -23.219  -4.545  1.00 90.22      A    C  
ANISOU  776  CB  ALA A 111    12079  10251  11948   1082  -2935   1054  A    C  
ATOM    777  N   GLY A 112      59.980 -22.513  -5.303  1.00109.63      A    N  
ANISOU  777  N   GLY A 112    14233  13213  14208   1502  -3091   1114  A    N  
ATOM    778  CA  GLY A 112      61.267 -22.797  -5.908  1.00110.10      A    C  
ANISOU  778  CA  GLY A 112    14172  13445  14215   1774  -3208   1093  A    C  
ATOM    779  C   GLY A 112      62.439 -22.270  -5.109  1.00112.65      A    C  
ANISOU  779  C   GLY A 112    14445  13934  14424   1771  -3246   1224  A    C  
ATOM    780  O   GLY A 112      63.588 -22.656  -5.344  1.00116.18      A    O  
ANISOU  780  O   GLY A 112    14815  14506  14823   1992  -3363   1224  A    O  
ATOM    781  N   LEU A 113      62.153 -21.379  -4.166  1.00109.09      A    N  
ANISOU  781  N   LEU A 113    14028  13495  13927   1525  -3151   1323  A    N  
ATOM    782  CA  LEU A 113      63.175 -20.887  -3.250  1.00106.53      A    C  
ANISOU  782  CA  LEU A 113    13674  13308  13495   1489  -3194   1439  A    C  
ATOM    783  C   LEU A 113      63.351 -21.827  -2.073  1.00105.24      A    C  
ANISOU  783  C   LEU A 113    13738  12951  13298   1484  -3309   1531  A    C  
ATOM    784  O   LEU A 113      64.449 -21.978  -1.547  1.00115.01      A    O  
ANISOU  784  O   LEU A 113    14960  14290  14450   1588  -3423   1596  A    O  
ATOM    785  CB  LEU A 113      62.814 -19.503  -2.723  1.00103.65      A    C  
ANISOU  785  CB  LEU A 113    13255  13038  13090   1233  -3048   1495  A    C  
ATOM    786  CG  LEU A 113      62.918 -18.372  -3.729  1.00107.40      A    C  
ANISOU  786  CG  LEU A 113    13499  13738  13570   1237  -2936   1444  A    C  
ATOM    787  CD1 LEU A 113      63.178 -17.104  -2.975  1.00102.08      A    C  
ANISOU  787  CD1 LEU A 113    12769  13186  12831   1034  -2853   1524  A    C  
ATOM    788  CD2 LEU A 113      64.045 -18.647  -4.715  1.00115.05      A    C  
ANISOU  788  CD2 LEU A 113    14286  14907  14520   1504  -3021   1398  A    C  
ATOM    789  N   LEU A 114      62.258 -22.451  -1.656  1.00100.41      A    N  
ANISOU  789  N   LEU A 114    13336  12064  12751   1361  -3275   1538  A    N  
ATOM    790  CA  LEU A 114      62.282 -23.297  -0.479  1.00107.54      A    C  
ANISOU  790  CA  LEU A 114    14483  12759  13618   1327  -3357   1647  A    C  
ATOM    791  C   LEU A 114      62.795 -24.694  -0.804  1.00109.71      A    C  
ANISOU  791  C   LEU A 114    14856  12896  13932   1588  -3521   1620  A    C  
ATOM    792  O   LEU A 114      63.234 -25.415   0.085  1.00109.52      A    O  
ANISOU  792  O   LEU A 114    15010  12752  13852   1643  -3628   1722  A    O  
ATOM    793  CB  LEU A 114      60.901 -23.359   0.176  1.00110.12      A    C  
ANISOU  793  CB  LEU A 114    14996  12850  13995   1067  -3235   1680  A    C  
ATOM    794  CG  LEU A 114      60.469 -22.115   0.956  1.00105.25      A    C  
ANISOU  794  CG  LEU A 114    14354  12330  13308    806  -3095   1742  A    C  
ATOM    795  CD1 LEU A 114      59.153 -22.367   1.683  1.00102.19      A    C  
ANISOU  795  CD1 LEU A 114    14165  11702  12961    572  -2984   1782  A    C  
ATOM    796  CD2 LEU A 114      61.554 -21.670   1.937  1.00100.91      A    C  
ANISOU  796  CD2 LEU A 114    13800  11935  12607    811  -3169   1854  A    C  
ATOM    797  N   SER A 115      62.743 -25.067  -2.079  1.00111.73      A    N  
ANISOU  797  N   SER A 115    15005  13171  14278   1759  -3543   1480  A    N  
ATOM    798  CA  SER A 115      63.254 -26.360  -2.520  1.00117.78      A    C  
ANISOU  798  CA  SER A 115    15848  13815  15087   2031  -3701   1427  A    C  
ATOM    799  C   SER A 115      64.761 -26.288  -2.755  1.00127.51      A    C  
ANISOU  799  C   SER A 115    16917  15308  16223   2288  -3825   1433  A    C  
ATOM    800  O   SER A 115      65.525 -27.080  -2.200  1.00131.07      A    O  
ANISOU  800  O   SER A 115    17482  15694  16626   2450  -3972   1498  A    O  
ATOM    801  CB  SER A 115      62.553 -26.803  -3.799  1.00119.09      A    C  
ANISOU  801  CB  SER A 115    15965  13901  15384   2115  -3678   1254  A    C  
ATOM    802  OG  SER A 115      62.795 -25.879  -4.846  1.00120.16      A    O  
ANISOU  802  OG  SER A 115    15829  14328  15496   2179  -3612   1162  A    O  
ATOM    803  N   ASN A 116      65.182 -25.340  -3.589  1.00129.65      A    N  
ANISOU  803  N   ASN A 116    16918  15878  16466   2329  -3764   1368  A    N  
ATOM    804  CA  ASN A 116      66.602 -25.095  -3.818  1.00130.10      A    C  
ANISOU  804  CA  ASN A 116    16776  16224  16430   2536  -3853   1375  A    C  
ATOM    805  C   ASN A 116      67.338 -24.978  -2.481  1.00129.79      A    C  
ANISOU  805  C   ASN A 116    16809  16223  16281   2485  -3932   1518  A    C  
ATOM    806  O   ASN A 116      66.939 -24.200  -1.609  1.00124.32      A    O  
ANISOU  806  O   ASN A 116    16164  15527  15546   2227  -3843   1606  A    O  
ATOM    807  CB  ASN A 116      66.790 -23.830  -4.659  1.00125.78      A    C  
ANISOU  807  CB  ASN A 116    15946  15981  15863   2489  -3727   1326  A    C  
ATOM    808  CG  ASN A 116      68.226 -23.624  -5.093  1.00127.31      A    C  
ANISOU  808  CG  ASN A 116    15905  16487  15979   2709  -3803   1313  A    C  
ATOM    809  ND2 ASN A 116      68.438 -23.536  -6.399  1.00122.03      A    N  
ANISOU  809  ND2 ASN A 116    15049  15986  15331   2879  -3772   1203  A    N  
ATOM    810  OD1 ASN A 116      69.134 -23.543  -4.267  1.00132.38      A    O  
ANISOU  810  OD1 ASN A 116    16526  17232  16538   2729  -3889   1397  A    O  
ATOM    811  N   VAL A 117      68.408 -25.754  -2.319  1.00128.99      A    N  
ANISOU  811  N   VAL A 117    16716  16166  16127   2742  -4104   1534  A    N  
ATOM    812  CA  VAL A 117      69.035 -25.893  -1.004  1.00125.39      A    C  
ANISOU  812  CA  VAL A 117    16375  15705  15562   2729  -4208   1667  A    C  
ATOM    813  C   VAL A 117      70.172 -24.905  -0.726  1.00132.37      A    C  
ANISOU  813  C   VAL A 117    17012  16946  16334   2727  -4229   1698  A    C  
ATOM    814  O   VAL A 117      70.595 -24.753   0.423  1.00126.95      A    O  
ANISOU  814  O   VAL A 117    16397  16292  15547   2661  -4295   1801  A    O  
ATOM    815  CB  VAL A 117      69.506 -27.339  -0.724  1.00115.04      A    C  
ANISOU  815  CB  VAL A 117    15260  14205  14244   2999  -4398   1691  A    C  
ATOM    816  CG1 VAL A 117      69.225 -27.696   0.730  1.00111.67      A    C  
ANISOU  816  CG1 VAL A 117    15115  13564  13749   2871  -4440   1849  A    C  
ATOM    817  CG2 VAL A 117      68.818 -28.336  -1.659  1.00109.48      A    C  
ANISOU  817  CG2 VAL A 117    14666  13253  13677   3123  -4404   1581  A    C  
ATOM    818  N   LEU A 118      70.657 -24.231  -1.768  1.00143.99      A    N  
ANISOU  818  N   LEU A 118    18197  18688  17823   2792  -4171   1608  A    N  
ATOM    819  CA  LEU A 118      71.665 -23.182  -1.592  1.00149.55      A    C  
ANISOU  819  CA  LEU A 118    18644  19733  18446   2747  -4162   1629  A    C  
ATOM    820  C   LEU A 118      71.031 -21.914  -1.022  1.00144.54      A    C  
ANISOU  820  C   LEU A 118    18001  19119  17800   2397  -4004   1683  A    C  
ATOM    821  O   LEU A 118      71.678 -21.142  -0.316  1.00146.13      A    O  
ANISOU  821  O   LEU A 118    18098  19502  17922   2287  -4017   1731  A    O  
ATOM    822  CB  LEU A 118      72.372 -22.853  -2.912  1.00154.23      A    C  
ANISOU  822  CB  LEU A 118    18934  20607  19061   2918  -4129   1527  A    C  
ATOM    823  CG  LEU A 118      73.179 -23.933  -3.635  1.00152.04      A    C  
ANISOU  823  CG  LEU A 118    18594  20391  18784   3292  -4274   1448  A    C  
ATOM    824  CD1 LEU A 118      72.269 -24.751  -4.552  1.00149.80      A    C  
ANISOU  824  CD1 LEU A 118    18444  19874  18600   3399  -4249   1357  A    C  
ATOM    825  CD2 LEU A 118      74.326 -23.304  -4.425  1.00143.10      A    C  
ANISOU  825  CD2 LEU A 118    17107  19651  17614   3418  -4257   1394  A    C  
ATOM    826  N   VAL A 119      69.763 -21.699  -1.345  1.00136.31      A    N  
ANISOU  826  N   VAL A 119    17062  17892  16839   2227  -3860   1662  A    N  
ATOM    827  CA  VAL A 119      69.027 -20.565  -0.816  1.00129.88      A    C  
ANISOU  827  CA  VAL A 119    16266  17063  16020   1908  -3707   1705  A    C  
ATOM    828  C   VAL A 119      68.936 -20.707   0.692  1.00125.24      A    C  
ANISOU  828  C   VAL A 119    15887  16352  15348   1776  -3768   1811  A    C  
ATOM    829  O   VAL A 119      68.595 -21.774   1.193  1.00124.54      A    O  
ANISOU  829  O   VAL A 119    16035  16030  15256   1845  -3851   1855  A    O  
ATOM    830  CB  VAL A 119      67.606 -20.523  -1.382  1.00128.10      A    C  
ANISOU  830  CB  VAL A 119    16140  16636  15896   1783  -3562   1659  A    C  
ATOM    831  CG1 VAL A 119      67.077 -19.096  -1.353  1.00130.55      A    C  
ANISOU  831  CG1 VAL A 119    16355  17036  16212   1519  -3384   1666  A    C  
ATOM    832  CG2 VAL A 119      67.584 -21.081  -2.800  1.00119.87      A    C  
ANISOU  832  CG2 VAL A 119    14999  15614  14931   2007  -3569   1547  A    C  
ATOM    833  N   LYS A 120      69.244 -19.641   1.420  1.00122.25      A    N  
ANISOU  833  N   LYS A 120    15428  16125  14897   1588  -3727   1852  A    N  
ATOM    834  CA  LYS A 120      69.201 -19.703   2.882  1.00125.42      A    C  
ANISOU  834  CA  LYS A 120    16019  16442  15194   1468  -3788   1948  A    C  
ATOM    835  C   LYS A 120      68.627 -18.424   3.495  1.00118.89      A    C  
ANISOU  835  C   LYS A 120    15186  15645  14342   1157  -3643   1965  A    C  
ATOM    836  O   LYS A 120      68.882 -17.312   3.008  1.00108.52      A    O  
ANISOU  836  O   LYS A 120    13657  14519  13057   1060  -3550   1916  A    O  
ATOM    837  CB  LYS A 120      70.589 -20.016   3.466  1.00128.76      A    C  
ANISOU  837  CB  LYS A 120    16368  17050  15505   1644  -3981   1979  A    C  
ATOM    838  CG  LYS A 120      71.130 -21.405   3.125  1.00129.35      A    C  
ANISOU  838  CG  LYS A 120    16506  17058  15584   1968  -4146   1976  A    C  
ATOM    839  CD  LYS A 120      72.603 -21.556   3.523  1.00133.26      A    C  
ANISOU  839  CD  LYS A 120    16860  17802  15973   2163  -4333   1985  A    C  
ATOM    840  CE  LYS A 120      72.813 -21.367   5.031  1.00132.50      A    C  
ANISOU  840  CE  LYS A 120    16897  17714  15732   2052  -4414   2078  A    C  
ATOM    841  NZ  LYS A 120      74.211 -21.645   5.510  1.00117.97      A    N1+
ANISOU  841  NZ  LYS A 120    14940  16106  13776   2265  -4621   2085  A    N1+
ATOM    842  N   PHE A 121      67.852 -18.594   4.566  1.00113.79      A    N  
ANISOU  842  N   PHE A 121    14785  14808  13641   1006  -3619   2038  A    N  
ATOM    843  CA  PHE A 121      67.123 -17.483   5.172  1.00109.58      A    C  
ANISOU  843  CA  PHE A 121    14284  14266  13087    718  -3473   2047  A    C  
ATOM    844  C   PHE A 121      67.596 -17.160   6.583  1.00103.72      A    C  
ANISOU  844  C   PHE A 121    13621  13597  12191    622  -3551   2110  A    C  
ATOM    845  O   PHE A 121      67.644 -18.032   7.458  1.00103.09      A    O  
ANISOU  845  O   PHE A 121    13746  13406  12017    692  -3658   2194  A    O  
ATOM    846  CB  PHE A 121      65.611 -17.776   5.212  1.00118.07      A    C  
ANISOU  846  CB  PHE A 121    15565  15070  14227    582  -3338   2061  A    C  
ATOM    847  CG  PHE A 121      64.927 -17.717   3.861  1.00124.46      A    C  
ANISOU  847  CG  PHE A 121    16275  15830  15183    607  -3224   1975  A    C  
ATOM    848  CD1 PHE A 121      64.694 -16.494   3.232  1.00123.26      A    C  
ANISOU  848  CD1 PHE A 121    15945  15805  15084    486  -3084   1912  A    C  
ATOM    849  CD2 PHE A 121      64.491 -18.884   3.235  1.00123.21      A    C  
ANISOU  849  CD2 PHE A 121    16213  15491  15109    754  -3258   1955  A    C  
ATOM    850  CE1 PHE A 121      64.065 -16.437   1.999  1.00114.69      A    C  
ANISOU  850  CE1 PHE A 121    14773  14688  14115    526  -2986   1836  A    C  
ATOM    851  CE2 PHE A 121      63.859 -18.836   2.001  1.00120.16      A    C  
ANISOU  851  CE2 PHE A 121    15733  15075  14846    786  -3166   1862  A    C  
ATOM    852  CZ  PHE A 121      63.645 -17.611   1.382  1.00116.63      A    C  
ANISOU  852  CZ  PHE A 121    15104  14775  14434    679  -3031   1805  A    C  
ATOM    853  N   THR A 122      67.931 -15.895   6.805  1.00 98.11      A    N  
ANISOU  853  N   THR A 122    12755  13071  11453    463  -3497   2070  A    N  
ATOM    854  CA  THR A 122      68.179 -15.415   8.155  1.00103.92      A    C  
ANISOU  854  CA  THR A 122    13570  13870  12045    330  -3546   2106  A    C  
ATOM    855  C   THR A 122      66.839 -15.115   8.827  1.00109.26      A    C  
ANISOU  855  C   THR A 122    14460  14353  12702    107  -3397   2138  A    C  
ATOM    856  O   THR A 122      65.816 -14.996   8.159  1.00109.98      A    O  
ANISOU  856  O   THR A 122    14574  14307  12906     29  -3245   2112  A    O  
ATOM    857  CB  THR A 122      69.076 -14.165   8.143  1.00104.64      A    C  
ANISOU  857  CB  THR A 122    13408  14227  12124    234  -3549   2034  A    C  
ATOM    858  CG2 THR A 122      69.462 -13.807   6.717  1.00 99.51      A    C  
ANISOU  858  CG2 THR A 122    12502  13695  11613    308  -3488   1966  A    C  
ATOM    859  OG1 THR A 122      68.385 -13.061   8.738  1.00114.19      A    O  
ANISOU  859  OG1 THR A 122    14667  15406  13313    -31  -3415   2011  A    O  
ATOM    860  N   LEU A 123      66.834 -15.007  10.146  1.00108.84      A    N  
ANISOU  860  N   LEU A 123    14557  14298  12498     12  -3441   2190  A    N  
ATOM    861  CA  LEU A 123      65.606 -14.659  10.846  1.00108.33      A    C  
ANISOU  861  CA  LEU A 123    14681  14079  12399   -201  -3293   2216  A    C  
ATOM    862  C   LEU A 123      65.058 -13.308  10.386  1.00113.89      A    C  
ANISOU  862  C   LEU A 123    15249  14830  13195   -401  -3117   2122  A    C  
ATOM    863  O   LEU A 123      63.850 -13.127  10.287  1.00113.14      A    O  
ANISOU  863  O   LEU A 123    15249  14583  13156   -529  -2957   2117  A    O  
ATOM    864  CB  LEU A 123      65.837 -14.618  12.351  1.00103.14      A    C  
ANISOU  864  CB  LEU A 123    14182  13464  11541   -263  -3374   2275  A    C  
ATOM    865  CG  LEU A 123      64.541 -14.780  13.134  1.00 99.78      A    C  
ANISOU  865  CG  LEU A 123    14014  12840  11058   -419  -3241   2341  A    C  
ATOM    866  CD1 LEU A 123      63.941 -16.153  12.843  1.00 91.86      A    C  
ANISOU  866  CD1 LEU A 123    13191  11601  10112   -305  -3238   2433  A    C  
ATOM    867  CD2 LEU A 123      64.770 -14.588  14.618  1.00101.90      A    C  
ANISOU  867  CD2 LEU A 123    14428  13180  11108   -486  -3308   2390  A    C  
ATOM    868  N   SER A 124      65.950 -12.357  10.123  1.00118.19      A    N  
ANISOU  868  N   SER A 124    15569  15583  13755   -427  -3146   2049  A    N  
ATOM    869  CA  SER A 124      65.546 -11.023   9.695  1.00112.20      A    C  
ANISOU  869  CA  SER A 124    14685  14865  13083   -608  -2987   1967  A    C  
ATOM    870  C   SER A 124      64.864 -11.066   8.343  1.00112.86      A    C  
ANISOU  870  C   SER A 124    14694  14857  13331   -567  -2858   1941  A    C  
ATOM    871  O   SER A 124      63.890 -10.348   8.105  1.00105.94      A    O  
ANISOU  871  O   SER A 124    13836  13898  12518   -709  -2692   1906  A    O  
ATOM    872  CB  SER A 124      66.755 -10.096   9.620  1.00116.83      A    C  
ANISOU  872  CB  SER A 124    15039  15685  13666   -636  -3053   1901  A    C  
ATOM    873  OG  SER A 124      67.215  -9.760  10.914  1.00128.44      A    O  
ANISOU  873  OG  SER A 124    16569  17245  14986   -724  -3146   1894  A    O  
ATOM    874  N   GLU A 125      65.389 -11.905   7.454  1.00119.91      A    N  
ANISOU  874  N   GLU A 125    15500  15776  14285   -359  -2940   1952  A    N  
ATOM    875  CA  GLU A 125      64.809 -12.070   6.126  1.00121.30      A    C  
ANISOU  875  CA  GLU A 125    15605  15882  14603   -286  -2841   1920  A    C  
ATOM    876  C   GLU A 125      63.432 -12.731   6.210  1.00111.75      A    C  
ANISOU  876  C   GLU A 125    14602  14432  13425   -326  -2753   1944  A    C  
ATOM    877  O   GLU A 125      62.507 -12.336   5.510  1.00110.80      A    O  
ANISOU  877  O   GLU A 125    14457  14241  13402   -389  -2610   1899  A    O  
ATOM    878  CB  GLU A 125      65.752 -12.864   5.210  1.00132.44      A    C  
ANISOU  878  CB  GLU A 125    16878  17390  16055    -39  -2962   1916  A    C  
ATOM    879  CG  GLU A 125      67.071 -12.149   4.898  1.00143.53      A    C  
ANISOU  879  CG  GLU A 125    18030  19052  17454     -4  -3018   1882  A    C  
ATOM    880  CD  GLU A 125      67.866 -12.811   3.777  1.00150.75      A    C  
ANISOU  880  CD  GLU A 125    18779  20077  18424    241  -3096   1863  A    C  
ATOM    881  OE1 GLU A 125      68.005 -14.055   3.786  1.00150.09      A    O  
ANISOU  881  OE1 GLU A 125    18791  19918  18318    431  -3217   1890  A    O  
ATOM    882  OE2 GLU A 125      68.361 -12.081   2.888  1.00152.38      A    O1-
ANISOU  882  OE2 GLU A 125    18763  20443  18692    248  -3033   1823  A    O1-
ATOM    883  N   ILE A 126      63.297 -13.724   7.081  1.00106.49      A    N  
ANISOU  883  N   ILE A 126    14138  13647  12677   -291  -2839   2015  A    N  
ATOM    884  CA  ILE A 126      62.022 -14.412   7.273  1.00 99.26      A    C  
ANISOU  884  CA  ILE A 126    13423  12498  11791   -350  -2754   2047  A    C  
ATOM    885  C   ILE A 126      60.946 -13.508   7.871  1.00 94.13      A    C  
ANISOU  885  C   ILE A 126    12849  11793  11122   -588  -2587   2029  A    C  
ATOM    886  O   ILE A 126      59.816 -13.488   7.402  1.00 90.18      A    O  
ANISOU  886  O   ILE A 126    12378  11173  10715   -656  -2454   1995  A    O  
ATOM    887  CB  ILE A 126      62.171 -15.652   8.176  1.00 97.78      A    C  
ANISOU  887  CB  ILE A 126    13456  12188  11509   -270  -2876   2149  A    C  
ATOM    888  CG1 ILE A 126      62.962 -16.744   7.462  1.00103.72      A    C  
ANISOU  888  CG1 ILE A 126    14167  12936  12307    -13  -3027   2158  A    C  
ATOM    889  CG2 ILE A 126      60.810 -16.184   8.576  1.00 85.82      A    C  
ANISOU  889  CG2 ILE A 126    12153  10438  10015   -391  -2761   2190  A    C  
ATOM    890  CD1 ILE A 126      63.122 -17.993   8.276  1.00109.21      A    C  
ANISOU  890  CD1 ILE A 126    15090  13487  12917     87  -3150   2265  A    C  
ATOM    891  N   LYS A 127      61.286 -12.775   8.922  1.00 94.61      A    N  
ANISOU  891  N   LYS A 127    12941  11947  11059   -707  -2598   2044  A    N  
ATOM    892  CA  LYS A 127      60.329 -11.856   9.508  1.00 87.67      A    C  
ANISOU  892  CA  LYS A 127    12127  11030  10154   -920  -2443   2015  A    C  
ATOM    893  C   LYS A 127      59.757 -10.975   8.403  1.00 91.03      A    C  
ANISOU  893  C   LYS A 127    12397  11469  10721   -966  -2300   1925  A    C  
ATOM    894  O   LYS A 127      58.563 -10.659   8.401  1.00 92.65      A    O  
ANISOU  894  O   LYS A 127    12662  11573  10967  -1082  -2150   1896  A    O  
ATOM    895  CB  LYS A 127      60.984 -10.995  10.592  1.00 86.23      A    C  
ANISOU  895  CB  LYS A 127    11947  10987   9830  -1024  -2489   2008  A    C  
ATOM    896  CG  LYS A 127      61.470 -11.776  11.796  1.00 94.48      A    C  
ANISOU  896  CG  LYS A 127    13162  12033  10705   -980  -2626   2098  A    C  
ATOM    897  CD  LYS A 127      61.704 -10.884  13.019  1.00 97.96      A    C  
ANISOU  897  CD  LYS A 127    13649  12581  10990  -1122  -2634   2076  A    C  
ATOM    898  CE  LYS A 127      62.167 -11.728  14.207  1.00 97.93      A    C  
ANISOU  898  CE  LYS A 127    13826  12586  10796  -1054  -2777   2176  A    C  
ATOM    899  NZ  LYS A 127      62.234 -10.983  15.493  1.00101.46      A    N1+
ANISOU  899  NZ  LYS A 127    14356  13127  11066  -1187  -2781   2155  A    N1+
ATOM    900  N   ARG A 128      60.616 -10.594   7.459  1.00 87.94      A    N  
ANISOU  900  N   ARG A 128    11804  11210  10397   -867  -2345   1886  A    N  
ATOM    901  CA  ARG A 128      60.243  -9.652   6.405  1.00 85.57      A    C  
ANISOU  901  CA  ARG A 128    11352  10946  10213   -897  -2216   1815  A    C  
ATOM    902  C   ARG A 128      59.249 -10.265   5.440  1.00 87.23      A    C  
ANISOU  902  C   ARG A 128    11574  11032  10535   -823  -2141   1791  A    C  
ATOM    903  O   ARG A 128      58.173  -9.725   5.201  1.00 92.72      A    O  
ANISOU  903  O   ARG A 128    12283  11662  11286   -916  -1997   1747  A    O  
ATOM    904  CB  ARG A 128      61.466  -9.216   5.621  1.00 80.09      A    C  
ANISOU  904  CB  ARG A 128    10444  10429   9557   -799  -2281   1795  A    C  
ATOM    905  CG  ARG A 128      61.167  -8.138   4.629  1.00 75.67      A    C  
ANISOU  905  CG  ARG A 128     9742   9912   9097   -838  -2143   1742  A    C  
ATOM    906  CD  ARG A 128      60.961  -6.824   5.342  1.00 86.56      A    C  
ANISOU  906  CD  ARG A 128    11140  11305  10444  -1040  -2049   1712  A    C  
ATOM    907  NE  ARG A 128      60.417  -5.833   4.427  1.00102.86      A    N  
ANISOU  907  NE  ARG A 128    13114  13362  12606  -1076  -1898   1670  A    N  
ATOM    908  CZ  ARG A 128      59.165  -5.393   4.465  1.00 99.63      A    C  
ANISOU  908  CZ  ARG A 128    12790  12838  12225  -1162  -1760   1638  A    C  
ATOM    909  NH1 ARG A 128      58.336  -5.845   5.395  1.00 94.02      A    N1+
ANISOU  909  NH1 ARG A 128    12252  12018  11455  -1238  -1745   1640  A    N1+
ATOM    910  NH2 ARG A 128      58.752  -4.491   3.582  1.00 96.58      A    N  
ANISOU  910  NH2 ARG A 128    12320  12455  11922  -1168  -1634   1606  A    N  
ATOM    911  N   VAL A 129      59.632 -11.393   4.870  1.00 78.80      A    N  
ANISOU  911  N   VAL A 129    10497   9942   9503   -646  -2247   1811  A    N  
ATOM    912  CA  VAL A 129      58.741 -12.142   4.014  1.00 76.32      A    C  
ANISOU  912  CA  VAL A 129    10204   9502   9291   -569  -2203   1777  A    C  
ATOM    913  C   VAL A 129      57.342 -12.249   4.594  1.00 83.07      A    C  
ANISOU  913  C   VAL A 129    11215  10194  10155   -723  -2085   1772  A    C  
ATOM    914  O   VAL A 129      56.360 -11.929   3.920  1.00 90.24      A    O  
ANISOU  914  O   VAL A 129    12078  11060  11151   -756  -1966   1706  A    O  
ATOM    915  CB  VAL A 129      59.271 -13.542   3.784  1.00 72.99      A    C  
ANISOU  915  CB  VAL A 129     9830   9026   8879   -385  -2351   1808  A    C  
ATOM    916  CG1 VAL A 129      58.125 -14.522   3.659  1.00 61.91      A    C  
ANISOU  916  CG1 VAL A 129     8562   7413   7546   -392  -2312   1795  A    C  
ATOM    917  CG2 VAL A 129      60.153 -13.565   2.558  1.00 83.85      A    C  
ANISOU  917  CG2 VAL A 129    11009  10542  10309   -191  -2415   1767  A    C  
ATOM    918  N   MET A 130      57.258 -12.718   5.835  1.00 79.92      A    N  
ANISOU  918  N   MET A 130    10993   9712   9659   -809  -2117   1843  A    N  
ATOM    919  CA  MET A 130      55.974 -12.894   6.505  1.00 78.70      A    C  
ANISOU  919  CA  MET A 130    10993   9411   9499   -963  -2000   1852  A    C  
ATOM    920  C   MET A 130      55.256 -11.569   6.652  1.00 77.01      A    C  
ANISOU  920  C   MET A 130    10728   9249   9283  -1119  -1844   1793  A    C  
ATOM    921  O   MET A 130      54.029 -11.482   6.514  1.00 75.78      A    O  
ANISOU  921  O   MET A 130    10596   9009   9187  -1204  -1713   1747  A    O  
ATOM    922  CB  MET A 130      56.165 -13.514   7.882  1.00 74.37      A    C  
ANISOU  922  CB  MET A 130    10646   8795   8816  -1023  -2060   1957  A    C  
ATOM    923  CG  MET A 130      56.568 -14.958   7.825  1.00 86.90      A    C  
ANISOU  923  CG  MET A 130    12334  10269  10414   -881  -2192   2025  A    C  
ATOM    924  SD  MET A 130      55.455 -15.921   6.793  1.00 89.24      A    S  
ANISOU  924  SD  MET A 130    12641  10377  10889   -844  -2131   1968  A    S  
ATOM    925  CE  MET A 130      53.913 -15.714   7.685  1.00 85.06      A    C  
ANISOU  925  CE  MET A 130    12251   9726  10344  -1096  -1939   1980  A    C  
ATOM    926  N   GLN A 131      56.030 -10.534   6.933  1.00 66.33      A    N  
ANISOU  926  N   GLN A 131     9301   8036   7865  -1153  -1860   1786  A    N  
ATOM    927  CA  GLN A 131      55.449  -9.236   7.123  1.00 66.65      A    C  
ANISOU  927  CA  GLN A 131     9307   8115   7902  -1291  -1722   1728  A    C  
ATOM    928  C   GLN A 131      54.790  -8.778   5.827  1.00 69.13      A    C  
ANISOU  928  C   GLN A 131     9487   8431   8351  -1241  -1621   1650  A    C  
ATOM    929  O   GLN A 131      53.625  -8.408   5.828  1.00 69.57      A    O  
ANISOU  929  O   GLN A 131     9566   8425   8441  -1326  -1488   1601  A    O  
ATOM    930  CB  GLN A 131      56.495  -8.245   7.609  1.00 74.41      A    C  
ANISOU  930  CB  GLN A 131    10232   9236   8806  -1336  -1771   1727  A    C  
ATOM    931  CG  GLN A 131      55.900  -6.893   7.873  1.00 87.72      A    C  
ANISOU  931  CG  GLN A 131    11904  10938  10488  -1480  -1631   1662  A    C  
ATOM    932  CD  GLN A 131      56.748  -6.061   8.784  1.00 89.02      A    C  
ANISOU  932  CD  GLN A 131    12074  11199  10548  -1573  -1680   1657  A    C  
ATOM    933  NE2 GLN A 131      56.179  -5.686   9.939  1.00 96.23      A    N  
ANISOU  933  NE2 GLN A 131    13123  12080  11359  -1712  -1619   1642  A    N  
ATOM    934  OE1 GLN A 131      57.903  -5.747   8.463  1.00 70.05      A    O  
ANISOU  934  OE1 GLN A 131     9550   8909   8156  -1522  -1772   1657  A    O  
ATOM    935  N   MET A 132      55.527  -8.823   4.721  1.00 75.06      A    N  
ANISOU  935  N   MET A 132    10092   9261   9168  -1091  -1685   1639  A    N  
ATOM    936  CA  MET A 132      54.974  -8.470   3.414  1.00 70.61      A    C  
ANISOU  936  CA  MET A 132     9401   8712   8716  -1012  -1604   1573  A    C  
ATOM    937  C   MET A 132      53.743  -9.307   3.083  1.00 77.31      A    C  
ANISOU  937  C   MET A 132    10305   9435   9635   -998  -1555   1531  A    C  
ATOM    938  O   MET A 132      52.775  -8.812   2.517  1.00 79.23      A    O  
ANISOU  938  O   MET A 132    10496   9665   9941  -1013  -1442   1463  A    O  
ATOM    939  CB  MET A 132      56.013  -8.664   2.313  1.00 63.24      A    C  
ANISOU  939  CB  MET A 132     8318   7887   7824   -832  -1695   1578  A    C  
ATOM    940  CG  MET A 132      57.217  -7.761   2.410  1.00 68.79      A    C  
ANISOU  940  CG  MET A 132     8922   8733   8484   -847  -1727   1607  A    C  
ATOM    941  SD  MET A 132      58.307  -7.965   0.992  1.00 82.01      A    S  
ANISOU  941  SD  MET A 132    10398  10551  10211   -633  -1800   1610  A    S  
ATOM    942  CE  MET A 132      59.077  -9.523   1.399  1.00118.93      A    C  
ANISOU  942  CE  MET A 132    15139  15208  14842   -509  -1990   1652  A    C  
ATOM    943  N   LEU A 133      53.781 -10.585   3.429  1.00 75.64      A    N  
ANISOU  943  N   LEU A 133    10196   9128   9416   -966  -1643   1569  A    N  
ATOM    944  CA  LEU A 133      52.682 -11.477   3.099  1.00 69.73      A    C  
ANISOU  944  CA  LEU A 133     9495   8248   8751   -964  -1606   1524  A    C  
ATOM    945  C   LEU A 133      51.440 -11.222   3.936  1.00 69.49      A    C  
ANISOU  945  C   LEU A 133     9564   8134   8706  -1150  -1469   1509  A    C  
ATOM    946  O   LEU A 133      50.337 -11.212   3.406  1.00 73.03      A    O  
ANISOU  946  O   LEU A 133     9967   8542   9239  -1170  -1377   1429  A    O  
ATOM    947  CB  LEU A 133      53.123 -12.925   3.216  1.00 76.46      A    C  
ANISOU  947  CB  LEU A 133    10442   8999   9611   -877  -1738   1574  A    C  
ATOM    948  CG  LEU A 133      52.007 -13.945   3.076  1.00 73.48      A    C  
ANISOU  948  CG  LEU A 133    10142   8454   9324   -911  -1703   1534  A    C  
ATOM    949  CD1 LEU A 133      52.469 -15.129   2.248  1.00 78.64      A    C  
ANISOU  949  CD1 LEU A 133    10781   9046  10052   -730  -1836   1514  A    C  
ATOM    950  CD2 LEU A 133      51.592 -14.379   4.450  1.00 75.77      A    C  
ANISOU  950  CD2 LEU A 133    10625   8622   9543  -1077  -1667   1619  A    C  
ATOM    951  N   LEU A 134      51.614 -11.013   5.238  1.00 71.91      A    N  
ANISOU  951  N   LEU A 134     9996   8430   8898  -1280  -1456   1579  A    N  
ATOM    952  CA  LEU A 134      50.494 -10.607   6.097  1.00 71.10      A    C  
ANISOU  952  CA  LEU A 134     9978   8278   8758  -1457  -1312   1564  A    C  
ATOM    953  C   LEU A 134      49.925  -9.224   5.727  1.00 69.23      A    C  
ANISOU  953  C   LEU A 134     9631   8126   8546  -1496  -1186   1477  A    C  
ATOM    954  O   LEU A 134      48.749  -8.944   5.914  1.00 69.26      A    O  
ANISOU  954  O   LEU A 134     9646   8097   8573  -1591  -1055   1421  A    O  
ATOM    955  CB  LEU A 134      50.884 -10.673   7.578  1.00 58.43      A    C  
ANISOU  955  CB  LEU A 134     8537   6661   7002  -1569  -1333   1658  A    C  
ATOM    956  CG  LEU A 134      51.039 -12.131   8.036  1.00 71.68      A    C  
ANISOU  956  CG  LEU A 134    10363   8214   8660  -1550  -1420   1751  A    C  
ATOM    957  CD1 LEU A 134      51.592 -12.273   9.448  1.00 61.49      A    C  
ANISOU  957  CD1 LEU A 134     9240   6926   7197  -1622  -1467   1860  A    C  
ATOM    958  CD2 LEU A 134      49.697 -12.865   7.908  1.00 79.24      A    C  
ANISOU  958  CD2 LEU A 134    11367   9031   9712  -1631  -1314   1722  A    C  
ATOM    959  N   ASN A 135      50.766  -8.359   5.192  1.00 63.48      A    N  
ANISOU  959  N   ASN A 135     8796   7506   7816  -1419  -1221   1466  A    N  
ATOM    960  CA  ASN A 135      50.304  -7.068   4.738  1.00 66.88      A    C  
ANISOU  960  CA  ASN A 135     9134   7998   8279  -1434  -1109   1395  A    C  
ATOM    961  C   ASN A 135      49.481  -7.239   3.464  1.00 71.29      A    C  
ANISOU  961  C   ASN A 135     9580   8550   8958  -1328  -1062   1317  A    C  
ATOM    962  O   ASN A 135      48.388  -6.691   3.327  1.00 67.31      A    O  
ANISOU  962  O   ASN A 135     9048   8038   8489  -1369   -942   1245  A    O  
ATOM    963  CB  ASN A 135      51.502  -6.158   4.480  1.00 68.91      A    C  
ANISOU  963  CB  ASN A 135     9312   8361   8511  -1387  -1160   1418  A    C  
ATOM    964  CG  ASN A 135      51.174  -4.706   4.666  1.00 72.90      A    C  
ANISOU  964  CG  ASN A 135     9798   8898   9003  -1469  -1043   1372  A    C  
ATOM    965  ND2 ASN A 135      51.580  -3.883   3.716  1.00 74.25      A    N  
ANISOU  965  ND2 ASN A 135     9850   9134   9229  -1388  -1024   1358  A    N  
ATOM    966  OD1 ASN A 135      50.553  -4.324   5.652  1.00 82.22      A    O  
ANISOU  966  OD1 ASN A 135    11076  10043  10123  -1600   -965   1351  A    O  
ATOM    967  N   GLY A 136      50.024  -8.004   2.528  1.00 80.68      A    N  
ANISOU  967  N   GLY A 136    10699   9751  10204  -1179  -1166   1323  A    N  
ATOM    968  CA  GLY A 136      49.323  -8.317   1.301  1.00 82.12      A    C  
ANISOU  968  CA  GLY A 136    10777   9935  10490  -1061  -1148   1240  A    C  
ATOM    969  C   GLY A 136      47.934  -8.838   1.594  1.00 77.09      A    C  
ANISOU  969  C   GLY A 136    10186   9203   9901  -1155  -1067   1176  A    C  
ATOM    970  O   GLY A 136      46.972  -8.445   0.935  1.00 75.85      A    O  
ANISOU  970  O   GLY A 136     9942   9072   9805  -1126   -985   1084  A    O  
ATOM    971  N   LEU A 137      47.823  -9.718   2.587  1.00 64.22      A    N  
ANISOU  971  N   LEU A 137     8691   7469   8240  -1268  -1088   1228  A    N  
ATOM    972  CA  LEU A 137      46.513 -10.219   3.000  1.00 61.06      A    C  
ANISOU  972  CA  LEU A 137     8339   6978   7884  -1392   -994   1179  A    C  
ATOM    973  C   LEU A 137      45.597  -9.126   3.564  1.00 64.17      A    C  
ANISOU  973  C   LEU A 137     8726   7414   8240  -1512   -838   1135  A    C  
ATOM    974  O   LEU A 137      44.512  -8.909   3.048  1.00 76.23      A    O  
ANISOU  974  O   LEU A 137    10164   8959   9841  -1509   -751   1034  A    O  
ATOM    975  CB  LEU A 137      46.647 -11.387   3.976  1.00 46.05      A    C  
ANISOU  975  CB  LEU A 137     6601   4947   5949  -1490  -1040   1267  A    C  
ATOM    976  CG  LEU A 137      47.058 -12.722   3.343  1.00 51.14      A    C  
ANISOU  976  CG  LEU A 137     7259   5501   6673  -1379  -1171   1275  A    C  
ATOM    977  CD1 LEU A 137      47.204 -13.806   4.398  1.00 49.86      A    C  
ANISOU  977  CD1 LEU A 137     7284   5192   6467  -1477  -1208   1382  A    C  
ATOM    978  CD2 LEU A 137      46.078 -13.174   2.258  1.00 52.28      A    C  
ANISOU  978  CD2 LEU A 137     7289   5614   6961  -1328  -1148   1143  A    C  
ATOM    979  N   TYR A 138      46.041  -8.433   4.606  1.00 64.52      A    N  
ANISOU  979  N   TYR A 138     8860   7484   8169  -1606   -808   1200  A    N  
ATOM    980  CA  TYR A 138      45.292  -7.312   5.169  1.00 60.37      A    C  
ANISOU  980  CA  TYR A 138     8337   7002   7597  -1704   -667   1152  A    C  
ATOM    981  C   TYR A 138      44.674  -6.465   4.062  1.00 63.94      A    C  
ANISOU  981  C   TYR A 138     8639   7525   8132  -1600   -603   1047  A    C  
ATOM    982  O   TYR A 138      43.529  -6.041   4.146  1.00 67.34      A    O  
ANISOU  982  O   TYR A 138     9033   7967   8584  -1648   -482    966  A    O  
ATOM    983  CB  TYR A 138      46.218  -6.444   6.025  1.00 61.05      A    C  
ANISOU  983  CB  TYR A 138     8500   7135   7561  -1755   -685   1214  A    C  
ATOM    984  CG  TYR A 138      45.575  -5.186   6.570  1.00 77.16      A    C  
ANISOU  984  CG  TYR A 138    10549   9216   9552  -1837   -550   1154  A    C  
ATOM    985  CD1 TYR A 138      44.958  -5.183   7.815  1.00 82.36      A    C  
ANISOU  985  CD1 TYR A 138    11321   9854  10119  -1987   -460   1159  A    C  
ATOM    986  CD2 TYR A 138      45.593  -3.996   5.846  1.00 80.75      A    C  
ANISOU  986  CD2 TYR A 138    10907   9729  10046  -1757   -510   1096  A    C  
ATOM    987  CE1 TYR A 138      44.374  -4.031   8.334  1.00 79.86      A    C  
ANISOU  987  CE1 TYR A 138    11015   9577   9752  -2049   -338   1091  A    C  
ATOM    988  CE2 TYR A 138      45.000  -2.840   6.350  1.00 79.85      A    C  
ANISOU  988  CE2 TYR A 138    10813   9635   9891  -1820   -390   1035  A    C  
ATOM    989  CZ  TYR A 138      44.389  -2.866   7.596  1.00 82.03      A    C  
ANISOU  989  CZ  TYR A 138    11197   9895  10078  -1963   -307   1025  A    C  
ATOM    990  OH  TYR A 138      43.789  -1.734   8.111  1.00 84.14      A    O  
ANISOU  990  OH  TYR A 138    11485  10185  10299  -2013   -188    951  A    O  
ATOM    991  N   TYR A 139      45.439  -6.219   3.013  1.00 62.23      A    N  
ANISOU  991  N   TYR A 139     8332   7361   7953  -1447   -683   1051  A    N  
ATOM    992  CA  TYR A 139      44.981  -5.322   1.977  1.00 60.45      A    C  
ANISOU  992  CA  TYR A 139     7981   7207   7782  -1331   -625    974  A    C  
ATOM    993  C   TYR A 139      43.770  -5.864   1.276  1.00 61.64      A    C  
ANISOU  993  C   TYR A 139     8042   7353   8024  -1285   -587    868  A    C  
ATOM    994  O   TYR A 139      42.782  -5.152   1.093  1.00 62.48      A    O  
ANISOU  994  O   TYR A 139     8088   7499   8152  -1276   -483    785  A    O  
ATOM    995  CB  TYR A 139      46.080  -5.068   0.951  1.00 61.45      A    C  
ANISOU  995  CB  TYR A 139     8029   7397   7922  -1172   -715   1014  A    C  
ATOM    996  CG  TYR A 139      45.590  -4.299  -0.247  1.00 52.22      A    C  
ANISOU  996  CG  TYR A 139     6737   6299   6805  -1028   -661    947  A    C  
ATOM    997  CD1 TYR A 139      45.309  -2.949  -0.151  1.00 46.44      A    C  
ANISOU  997  CD1 TYR A 139     6003   5593   6049  -1039   -557    933  A    C  
ATOM    998  CD2 TYR A 139      45.406  -4.926  -1.475  1.00 55.23      A    C  
ANISOU  998  CD2 TYR A 139     7013   6720   7252   -868   -718    896  A    C  
ATOM    999  CE1 TYR A 139      44.852  -2.241  -1.239  1.00 56.07      A    C  
ANISOU  999  CE1 TYR A 139     7126   6872   7305   -892   -509    885  A    C  
ATOM   1000  CE2 TYR A 139      44.965  -4.222  -2.576  1.00 59.75      A    C  
ANISOU 1000  CE2 TYR A 139     7479   7370   7852   -718   -674    841  A    C  
ATOM   1001  CZ  TYR A 139      44.686  -2.880  -2.449  1.00 61.55      A    C  
ANISOU 1001  CZ  TYR A 139     7715   7620   8052   -729   -567    843  A    C  
ATOM   1002  OH  TYR A 139      44.230  -2.163  -3.526  1.00 61.87      A    O  
ANISOU 1002  OH  TYR A 139     7665   7732   8111   -566   -522    801  A    O  
ATOM   1003  N   ILE A 140      43.853  -7.127   0.868  1.00 70.67      A    N  
ANISOU 1003  N   ILE A 140     9174   8451   9228  -1247   -678    863  A    N  
ATOM   1004  CA  ILE A 140      42.817  -7.715   0.023  1.00 68.69      A    C  
ANISOU 1004  CA  ILE A 140     8817   8203   9079  -1186   -669    745  A    C  
ATOM   1005  C   ILE A 140      41.565  -8.007   0.832  1.00 62.87      A    C  
ANISOU 1005  C   ILE A 140     8108   7415   8366  -1356   -560    689  A    C  
ATOM   1006  O   ILE A 140      40.451  -7.782   0.378  1.00 66.39      A    O  
ANISOU 1006  O   ILE A 140     8446   7909   8871  -1335   -488    571  A    O  
ATOM   1007  CB  ILE A 140      43.316  -8.963  -0.758  1.00 59.09      A    C  
ANISOU 1007  CB  ILE A 140     7576   6946   7929  -1082   -808    737  A    C  
ATOM   1008  CG1 ILE A 140      43.148 -10.237   0.025  1.00 71.34      A    C  
ANISOU 1008  CG1 ILE A 140     9238   8360   9510  -1220   -836    767  A    C  
ATOM   1009  CG2 ILE A 140      44.785  -8.876  -1.087  1.00 58.77      A    C  
ANISOU 1009  CG2 ILE A 140     7552   6942   7837   -966   -916    832  A    C  
ATOM   1010  CD1 ILE A 140      43.897 -11.363  -0.648  1.00 76.62      A    C  
ANISOU 1010  CD1 ILE A 140     9909   8974  10228  -1102   -986    776  A    C  
ATOM   1011  N   HIS A 141      41.762  -8.484   2.051  1.00 61.63      A    N  
ANISOU 1011  N   HIS A 141     8092   7171   8153  -1519   -544    775  A    N  
ATOM   1012  CA  HIS A 141      40.669  -8.651   2.989  1.00 57.95      A    C  
ANISOU 1012  CA  HIS A 141     7668   6667   7684  -1699   -418    747  A    C  
ATOM   1013  C   HIS A 141      39.942  -7.341   3.246  1.00 61.26      A    C  
ANISOU 1013  C   HIS A 141     8037   7179   8059  -1718   -283    683  A    C  
ATOM   1014  O   HIS A 141      38.713  -7.306   3.274  1.00 76.04      A    O  
ANISOU 1014  O   HIS A 141     9832   9080   9980  -1774   -179    583  A    O  
ATOM   1015  CB  HIS A 141      41.199  -9.212   4.294  1.00 60.15      A    C  
ANISOU 1015  CB  HIS A 141     8128   6853   7872  -1849   -425    877  A    C  
ATOM   1016  CG  HIS A 141      41.621 -10.640   4.195  1.00 67.63      A    C  
ANISOU 1016  CG  HIS A 141     9144   7680   8873  -1853   -533    933  A    C  
ATOM   1017  CD2 HIS A 141      41.463 -11.546   3.200  1.00 69.74      A    C  
ANISOU 1017  CD2 HIS A 141     9335   7897   9266  -1769   -613    867  A    C  
ATOM   1018  ND1 HIS A 141      42.296 -11.289   5.207  1.00 74.66      A    N  
ANISOU 1018  ND1 HIS A 141    10208   8479   9681  -1941   -576   1068  A    N  
ATOM   1019  CE1 HIS A 141      42.530 -12.537   4.839  1.00 86.61      A    C  
ANISOU 1019  CE1 HIS A 141    11756   9878  11273  -1910   -673   1090  A    C  
ATOM   1020  NE2 HIS A 141      42.034 -12.718   3.626  1.00 78.77      A    N  
ANISOU 1020  NE2 HIS A 141    10613   8905  10410  -1810   -698    963  A    N  
ATOM   1021  N   ARG A 142      40.708  -6.274   3.439  1.00 51.82      A    N  
ANISOU 1021  N   ARG A 142     6882   6029   6777  -1672   -287    736  A    N  
ATOM   1022  CA  ARG A 142      40.171  -4.919   3.619  1.00 51.10      A    C  
ANISOU 1022  CA  ARG A 142     6759   6010   6645  -1664   -172    677  A    C  
ATOM   1023  C   ARG A 142      39.354  -4.514   2.412  1.00 59.88      A    C  
ANISOU 1023  C   ARG A 142     7708   7199   7846  -1515   -146    557  A    C  
ATOM   1024  O   ARG A 142      38.444  -3.696   2.516  1.00 65.98      A    O  
ANISOU 1024  O   ARG A 142     8431   8027   8613  -1510    -35    475  A    O  
ATOM   1025  CB  ARG A 142      41.327  -3.930   3.825  1.00 53.79      A    C  
ANISOU 1025  CB  ARG A 142     7169   6367   6903  -1626   -210    755  A    C  
ATOM   1026  CG  ARG A 142      40.974  -2.458   3.900  1.00 65.96      A    C  
ANISOU 1026  CG  ARG A 142     8694   7957   8411  -1596   -109    702  A    C  
ATOM   1027  CD  ARG A 142      42.157  -1.627   3.376  1.00 96.11      A    C  
ANISOU 1027  CD  ARG A 142    12516  11788  12213  -1496   -177    763  A    C  
ATOM   1028  NE  ARG A 142      42.076  -0.219   3.741  1.00120.91      A    N  
ANISOU 1028  NE  ARG A 142    15694  14936  15309  -1506    -89    736  A    N  
ATOM   1029  CZ  ARG A 142      42.483   0.267   4.912  1.00143.93      A    C  
ANISOU 1029  CZ  ARG A 142    18730  17824  18134  -1635    -65    764  A    C  
ATOM   1030  NH1 ARG A 142      42.990  -0.548   5.827  1.00146.95      A    N1+
ANISOU 1030  NH1 ARG A 142    19204  18182  18450  -1757   -121    829  A    N1+
ATOM   1031  NH2 ARG A 142      42.380   1.564   5.175  1.00154.50      A    N  
ANISOU 1031  NH2 ARG A 142    20103  19156  19444  -1635     12    724  A    N  
ATOM   1032  N   ASN A 143      39.694  -5.097   1.265  1.00 66.42      A    N  
ANISOU 1032  N   ASN A 143     8454   8037   8747  -1378   -253    544  A    N  
ATOM   1033  CA  ASN A 143      39.003  -4.826   0.016  1.00 64.71      A    C  
ANISOU 1033  CA  ASN A 143     8081   7904   8601  -1211   -253    431  A    C  
ATOM   1034  C   ASN A 143      37.980  -5.892  -0.296  1.00 73.50      A    C  
ANISOU 1034  C   ASN A 143     9100   9012   9814  -1245   -256    320  A    C  
ATOM   1035  O   ASN A 143      37.583  -6.075  -1.450  1.00 85.76      A    O  
ANISOU 1035  O   ASN A 143    10521  10629  11435  -1098   -305    222  A    O  
ATOM   1036  CB  ASN A 143      39.996  -4.741  -1.127  1.00 70.00      A    C  
ANISOU 1036  CB  ASN A 143     8709   8609   9279  -1023   -366    473  A    C  
ATOM   1037  CG  ASN A 143      40.469  -3.344  -1.366  1.00 76.66      A    C  
ANISOU 1037  CG  ASN A 143     9561   9501  10063   -929   -326    518  A    C  
ATOM   1038  ND2 ASN A 143      41.440  -2.909  -0.565  1.00 61.70      A    N  
ANISOU 1038  ND2 ASN A 143     7783   7561   8099  -1019   -328    627  A    N  
ATOM   1039  OD1 ASN A 143      39.963  -2.647  -2.259  1.00 82.70      A    O  
ANISOU 1039  OD1 ASN A 143    10233  10343  10846   -776   -294    456  A    O  
ATOM   1040  N   LYS A 144      37.569  -6.612   0.738  1.00 72.40      A    N  
ANISOU 1040  N   LYS A 144     9032   8797   9679  -1443   -203    335  A    N  
ATOM   1041  CA  LYS A 144      36.467  -7.547   0.620  1.00 73.99      A    C  
ANISOU 1041  CA  LYS A 144     9145   8984   9983  -1523   -175    226  A    C  
ATOM   1042  C   LYS A 144      36.772  -8.687  -0.326  1.00 72.34      A    C  
ANISOU 1042  C   LYS A 144     8888   8728   9870  -1444   -313    192  A    C  
ATOM   1043  O   LYS A 144      35.854  -9.304  -0.847  1.00 79.62      A    O  
ANISOU 1043  O   LYS A 144     9691   9665  10897  -1451   -313     61  A    O  
ATOM   1044  CB  LYS A 144      35.213  -6.820   0.142  1.00 79.50      A    C  
ANISOU 1044  CB  LYS A 144     9679   9808  10718  -1455    -85     74  A    C  
ATOM   1045  CG  LYS A 144      34.748  -5.730   1.075  1.00 86.30      A    C  
ANISOU 1045  CG  LYS A 144    10579  10717  11495  -1526     60     80  A    C  
ATOM   1046  CD  LYS A 144      34.624  -6.264   2.498  1.00100.79      A    C  
ANISOU 1046  CD  LYS A 144    12540  12469  13286  -1769    145    153  A    C  
ATOM   1047  CE  LYS A 144      33.992  -5.209   3.373  1.00117.26      A    C  
ANISOU 1047  CE  LYS A 144    14642  14623  15289  -1829    297    126  A    C  
ATOM   1048  NZ  LYS A 144      33.019  -4.398   2.566  1.00126.43      A    N1+
ANISOU 1048  NZ  LYS A 144    15628  15913  16496  -1678    345    -25  A    N1+
ATOM   1049  N   ILE A 145      38.050  -8.978  -0.551  1.00 67.11      A    N  
ANISOU 1049  N   ILE A 145     8312   8014   9173  -1367   -431    297  A    N  
ATOM   1050  CA  ILE A 145      38.405 -10.120  -1.386  1.00 68.36      A    C  
ANISOU 1050  CA  ILE A 145     8440   8117   9415  -1285   -566    264  A    C  
ATOM   1051  C   ILE A 145      38.970 -11.265  -0.557  1.00 73.09      A    C  
ANISOU 1051  C   ILE A 145     9197   8554  10021  -1426   -614    370  A    C  
ATOM   1052  O   ILE A 145      39.747 -11.019   0.365  1.00 72.94      A    O  
ANISOU 1052  O   ILE A 145     9318   8495   9902  -1495   -604    510  A    O  
ATOM   1053  CB  ILE A 145      39.415  -9.750  -2.479  1.00 62.28      A    C  
ANISOU 1053  CB  ILE A 145     7629   7423   8614  -1052   -678    286  A    C  
ATOM   1054  CG1 ILE A 145      38.833  -8.688  -3.396  1.00 63.71      A    C  
ANISOU 1054  CG1 ILE A 145     7665   7757   8787   -892   -635    190  A    C  
ATOM   1055  CG2 ILE A 145      39.741 -10.959  -3.321  1.00 68.87      A    C  
ANISOU 1055  CG2 ILE A 145     8433   8206   9528   -958   -817    235  A    C  
ATOM   1056  CD1 ILE A 145      37.469  -9.042  -3.897  1.00 73.09      A    C  
ANISOU 1056  CD1 ILE A 145     8708   8991  10071   -891   -607     13  A    C  
ATOM   1057  N   LEU A 146      38.551 -12.498  -0.878  1.00 68.70      A    N  
ANISOU 1057  N   LEU A 146     8620   7902   9581  -1466   -667    298  A    N  
ATOM   1058  CA  LEU A 146      39.175 -13.722  -0.354  1.00 69.91      A    C  
ANISOU 1058  CA  LEU A 146     8927   7880   9756  -1551   -742    395  A    C  
ATOM   1059  C   LEU A 146      40.058 -14.372  -1.422  1.00 77.02      A    C  
ANISOU 1059  C   LEU A 146     9807   8759  10698  -1354   -913    371  A    C  
ATOM   1060  O   LEU A 146      39.611 -14.598  -2.544  1.00 85.04      A    O  
ANISOU 1060  O   LEU A 146    10683   9827  11802  -1236   -967    222  A    O  
ATOM   1061  CB  LEU A 146      38.117 -14.736   0.075  1.00 67.85      A    C  
ANISOU 1061  CB  LEU A 146     8678   7492   9610  -1749   -678    336  A    C  
ATOM   1062  CG  LEU A 146      37.179 -14.443   1.241  1.00 62.82      A    C  
ANISOU 1062  CG  LEU A 146     8074   6850   8944  -1977   -500    363  A    C  
ATOM   1063  CD1 LEU A 146      36.383 -15.672   1.500  1.00 55.53      A    C  
ANISOU 1063  CD1 LEU A 146     7171   5776   8151  -2159   -464    322  A    C  
ATOM   1064  CD2 LEU A 146      37.935 -14.078   2.475  1.00 57.40      A    C  
ANISOU 1064  CD2 LEU A 146     7572   6133   8106  -2058   -459    549  A    C  
ATOM   1065  N   HIS A 147      41.304 -14.688  -1.083  1.00 72.68      A    N  
ANISOU 1065  N   HIS A 147     9390   8145  10081  -1309  -1004    509  A    N  
ATOM   1066  CA  HIS A 147      42.226 -15.215  -2.090  1.00 69.52      A    C  
ANISOU 1066  CA  HIS A 147     8963   7748   9703  -1101  -1162    488  A    C  
ATOM   1067  C   HIS A 147      41.930 -16.665  -2.445  1.00 67.00      A    C  
ANISOU 1067  C   HIS A 147     8671   7269   9518  -1114  -1247    407  A    C  
ATOM   1068  O   HIS A 147      41.980 -17.049  -3.620  1.00 71.16      A    O  
ANISOU 1068  O   HIS A 147     9095   7830  10111   -947  -1346    283  A    O  
ATOM   1069  CB  HIS A 147      43.673 -15.074  -1.627  1.00 71.90      A    C  
ANISOU 1069  CB  HIS A 147     9377   8049   9891  -1038  -1236    651  A    C  
ATOM   1070  CG  HIS A 147      44.674 -15.627  -2.592  1.00 72.47      A    C  
ANISOU 1070  CG  HIS A 147     9420   8138   9978   -821  -1392    636  A    C  
ATOM   1071  CD2 HIS A 147      45.454 -15.019  -3.514  1.00 76.11      A    C  
ANISOU 1071  CD2 HIS A 147     9776   8753  10388   -618  -1450    626  A    C  
ATOM   1072  ND1 HIS A 147      44.967 -16.970  -2.674  1.00 73.99      A    N  
ANISOU 1072  ND1 HIS A 147     9697   8175  10241   -793  -1503    629  A    N  
ATOM   1073  CE1 HIS A 147      45.882 -17.166  -3.602  1.00 75.66      A    C  
ANISOU 1073  CE1 HIS A 147     9852   8454  10442   -572  -1627    606  A    C  
ATOM   1074  NE2 HIS A 147      46.197 -15.997  -4.128  1.00 77.63      A    N  
ANISOU 1074  NE2 HIS A 147     9983   8898  10615   -467  -1593    608  A    N  
ATOM   1075  N   ARG A 148      41.668 -17.462  -1.413  1.00 61.75      A    N  
ANISOU 1075  N   ARG A 148     8154   6424   8884  -1310  -1207    483  A    N  
ATOM   1076  CA  ARG A 148      41.179 -18.831  -1.559  1.00 74.47      A    C  
ANISOU 1076  CA  ARG A 148     9812   7844  10641  -1383  -1254    411  A    C  
ATOM   1077  C   ARG A 148      42.160 -19.790  -2.202  1.00 72.76      A    C  
ANISOU 1077  C   ARG A 148     9654   7531  10461  -1206  -1430    408  A    C  
ATOM   1078  O   ARG A 148      41.777 -20.893  -2.604  1.00 73.27      A    O  
ANISOU 1078  O   ARG A 148     9734   7443  10663  -1223  -1491    309  A    O  
ATOM   1079  CB  ARG A 148      39.890 -18.860  -2.377  1.00 75.38      A    C  
ANISOU 1079  CB  ARG A 148     9742   8011  10886  -1408  -1211    198  A    C  
ATOM   1080  CG  ARG A 148      38.705 -18.213  -1.737  1.00 64.53      A    C  
ANISOU 1080  CG  ARG A 148     8304   6700   9515  -1603  -1035    171  A    C  
ATOM   1081  CD  ARG A 148      37.679 -17.995  -2.805  1.00 72.37      A    C  
ANISOU 1081  CD  ARG A 148     9074   7817  10607  -1540  -1029    -51  A    C  
ATOM   1082  NE  ARG A 148      36.587 -18.954  -2.759  1.00 80.28      A    N  
ANISOU 1082  NE  ARG A 148    10036   8692  11773  -1720   -992   -174  A    N  
ATOM   1083  CZ  ARG A 148      35.645 -19.038  -3.693  1.00 98.51      A    C  
ANISOU 1083  CZ  ARG A 148    12148  11085  14196  -1683  -1009   -394  A    C  
ATOM   1084  NH1 ARG A 148      35.685 -18.239  -4.750  1.00102.96      A    N1+
ANISOU 1084  NH1 ARG A 148    12553  11857  14710  -1454  -1066   -501  A    N1+
ATOM   1085  NH2 ARG A 148      34.666 -19.924  -3.579  1.00105.49      A    N  
ANISOU 1085  NH2 ARG A 148    12992  11848  15240  -1874   -971   -506  A    N  
ATOM   1086  N   ASP A 149      43.410 -19.375  -2.324  1.00 70.32      A    N  
ANISOU 1086  N   ASP A 149     9371   7313  10036  -1036  -1513    505  A    N  
ATOM   1087  CA  ASP A 149      44.414 -20.268  -2.863  1.00 80.65      A    C  
ANISOU 1087  CA  ASP A 149    10736   8545  11364   -855  -1679    509  A    C  
ATOM   1088  C   ASP A 149      45.785 -20.036  -2.238  1.00 85.19      A    C  
ANISOU 1088  C   ASP A 149    11420   9149  11798   -778  -1738    691  A    C  
ATOM   1089  O   ASP A 149      46.800 -19.971  -2.935  1.00 82.38      A    O  
ANISOU 1089  O   ASP A 149    11012   8891  11397   -563  -1849    689  A    O  
ATOM   1090  CB  ASP A 149      44.475 -20.174  -4.385  1.00 83.37      A    C  
ANISOU 1090  CB  ASP A 149    10901   9025  11750   -625  -1767    338  A    C  
ATOM   1091  CG  ASP A 149      45.073 -21.421  -5.016  1.00 95.12      A    C  
ANISOU 1091  CG  ASP A 149    12443  10384  13313   -470  -1929    278  A    C  
ATOM   1092  OD1 ASP A 149      45.318 -22.400  -4.269  1.00 98.53      A    O  
ANISOU 1092  OD1 ASP A 149    13057  10596  13784   -555  -1969    364  A    O  
ATOM   1093  OD2 ASP A 149      45.293 -21.422  -6.250  1.00 97.08      A    O1-
ANISOU 1093  OD2 ASP A 149    12561  10751  13575   -255  -2016    145  A    O1-
ATOM   1094  N   MET A 150      45.812 -19.926  -0.916  1.00 85.44      A    N  
ANISOU 1094  N   MET A 150    11600   9109  11757   -954  -1663    844  A    N  
ATOM   1095  CA  MET A 150      47.076 -19.765  -0.222  1.00 87.47      A    C  
ANISOU 1095  CA  MET A 150    11964   9393  11878   -894  -1728   1009  A    C  
ATOM   1096  C   MET A 150      47.956 -20.978  -0.429  1.00 92.89      A    C  
ANISOU 1096  C   MET A 150    12756   9941  12596   -747  -1891   1040  A    C  
ATOM   1097  O   MET A 150      47.519 -22.108  -0.237  1.00113.95      A    O  
ANISOU 1097  O   MET A 150    15546  12388  15363   -816  -1912   1031  A    O  
ATOM   1098  CB  MET A 150      46.837 -19.543   1.265  1.00102.65      A    C  
ANISOU 1098  CB  MET A 150    14038  11253  13711  -1110  -1622   1155  A    C  
ATOM   1099  CG  MET A 150      46.467 -18.115   1.605  1.00106.39      A    C  
ANISOU 1099  CG  MET A 150    14421  11905  14097  -1201  -1490   1157  A    C  
ATOM   1100  SD  MET A 150      47.756 -16.971   1.081  1.00 84.91      A    S  
ANISOU 1100  SD  MET A 150    11580   9418  11266  -1007  -1562   1181  A    S  
ATOM   1101  CE  MET A 150      47.128 -16.430  -0.506  1.00124.90      A    C  
ANISOU 1101  CE  MET A 150    16413  14616  16428   -876  -1538    995  A    C  
ATOM   1102  N   LYS A 151      49.190 -20.737  -0.850  1.00 87.35      A    N  
ANISOU 1102  N   LYS A 151    12004   9368  11816   -542  -2002   1072  A    N  
ATOM   1103  CA  LYS A 151      50.208 -21.782  -0.947  1.00 88.96      A    C  
ANISOU 1103  CA  LYS A 151    12308   9472  12022   -374  -2164   1116  A    C  
ATOM   1104  C   LYS A 151      51.499 -21.151  -1.432  1.00 85.39      A    C  
ANISOU 1104  C   LYS A 151    11739   9238  11467   -166  -2250   1141  A    C  
ATOM   1105  O   LYS A 151      51.480 -20.234  -2.247  1.00 86.59      A    O  
ANISOU 1105  O   LYS A 151    11708   9585  11605    -97  -2209   1064  A    O  
ATOM   1106  CB  LYS A 151      49.780 -22.922  -1.881  1.00 85.88      A    C  
ANISOU 1106  CB  LYS A 151    11915   8928  11789   -282  -2242    970  A    C  
ATOM   1107  CG  LYS A 151      49.587 -22.526  -3.338  1.00 82.17      A    C  
ANISOU 1107  CG  LYS A 151    11227   8624  11369   -123  -2261    789  A    C  
ATOM   1108  CD  LYS A 151      49.312 -23.746  -4.204  1.00 83.95      A    C  
ANISOU 1108  CD  LYS A 151    11465   8693  11737    -14  -2365    636  A    C  
ATOM   1109  CE  LYS A 151      49.112 -23.364  -5.663  1.00 90.12      A    C  
ANISOU 1109  CE  LYS A 151    12033   9659  12551    160  -2390    449  A    C  
ATOM   1110  NZ  LYS A 151      49.078 -24.541  -6.588  1.00 93.47      A    N1+
ANISOU 1110  NZ  LYS A 151    12463   9959  13093    315  -2520    287  A    N1+
ATOM   1111  N   ALA A 152      52.624 -21.628  -0.922  1.00 86.40      A    N  
ANISOU 1111  N   ALA A 152    11969   9339  11520    -65  -2365   1254  A    N  
ATOM   1112  CA  ALA A 152      53.903 -21.019  -1.258  1.00 92.63      A    C  
ANISOU 1112  CA  ALA A 152    12638  10349  12209    111  -2440   1286  A    C  
ATOM   1113  C   ALA A 152      54.064 -20.815  -2.765  1.00 91.36      A    C  
ANISOU 1113  C   ALA A 152    12276  10339  12098    308  -2472   1143  A    C  
ATOM   1114  O   ALA A 152      54.665 -19.839  -3.213  1.00 94.16      A    O  
ANISOU 1114  O   ALA A 152    12474  10918  12383    384  -2452   1146  A    O  
ATOM   1115  CB  ALA A 152      55.046 -21.850  -0.706  1.00 95.23      A    C  
ANISOU 1115  CB  ALA A 152    13093  10612  12476    239  -2589   1391  A    C  
ATOM   1116  N   ALA A 153      53.518 -21.730  -3.551  1.00 83.98      A    N  
ANISOU 1116  N   ALA A 153    11349   9279  11282    388  -2518   1016  A    N  
ATOM   1117  CA  ALA A 153      53.720 -21.672  -4.989  1.00 80.90      A    C  
ANISOU 1117  CA  ALA A 153    10783   9032  10922    604  -2565    875  A    C  
ATOM   1118  C   ALA A 153      53.089 -20.417  -5.619  1.00 80.99      A    C  
ANISOU 1118  C   ALA A 153    10618   9235  10918    555  -2436    811  A    C  
ATOM   1119  O   ALA A 153      53.399 -20.063  -6.760  1.00 82.29      A    O  
ANISOU 1119  O   ALA A 153    10622   9577  11066    736  -2454    728  A    O  
ATOM   1120  CB  ALA A 153      53.208 -22.954  -5.638  1.00 81.94      A    C  
ANISOU 1120  CB  ALA A 153    10973   8975  11187    690  -2650    734  A    C  
ATOM   1121  N   ASN A 154      52.223 -19.746  -4.856  1.00 77.99      A    N  
ANISOU 1121  N   ASN A 154    10276   8821  10535    321  -2303    855  A    N  
ATOM   1122  CA  ASN A 154      51.479 -18.569  -5.318  1.00 75.29      A    C  
ANISOU 1122  CA  ASN A 154     9795   8628  10186    261  -2174    799  A    C  
ATOM   1123  C   ASN A 154      52.005 -17.272  -4.698  1.00 84.94      A    C  
ANISOU 1123  C   ASN A 154    10983   9997  11293    179  -2091    924  A    C  
ATOM   1124  O   ASN A 154      51.392 -16.199  -4.785  1.00 80.41      A    O  
ANISOU 1124  O   ASN A 154    10332   9517  10703     94  -1969    908  A    O  
ATOM   1125  CB  ASN A 154      49.989 -18.729  -5.009  1.00 71.37      A    C  
ANISOU 1125  CB  ASN A 154     9343   7992   9781     66  -2077    726  A    C  
ATOM   1126  CG  ASN A 154      49.271 -19.578  -6.031  1.00 85.22      A    C  
ANISOU 1126  CG  ASN A 154    11044   9677  11657    157  -2131    546  A    C  
ATOM   1127  ND2 ASN A 154      48.045 -19.965  -5.716  1.00 89.92      A    N  
ANISOU 1127  ND2 ASN A 154    11684  10127  12353    -20  -2067    476  A    N  
ATOM   1128  OD1 ASN A 154      49.807 -19.877  -7.098  1.00 95.98      A    O  
ANISOU 1128  OD1 ASN A 154    12320  11125  13023    382  -2228    462  A    O  
ATOM   1129  N   VAL A 155      53.164 -17.389  -4.074  1.00 88.04      A    N  
ANISOU 1129  N   VAL A 155    11433  10408  11608    211  -2166   1041  A    N  
ATOM   1130  CA  VAL A 155      53.786 -16.280  -3.385  1.00 77.01      A    C  
ANISOU 1130  CA  VAL A 155    10015   9136  10107    125  -2111   1154  A    C  
ATOM   1131  C   VAL A 155      55.079 -15.967  -4.127  1.00 73.84      A    C  
ANISOU 1131  C   VAL A 155     9476   8928   9651    322  -2182   1172  A    C  
ATOM   1132  O   VAL A 155      56.080 -16.635  -3.939  1.00 85.36      A    O  
ANISOU 1132  O   VAL A 155    10966  10388  11078    431  -2303   1219  A    O  
ATOM   1133  CB  VAL A 155      54.069 -16.706  -1.939  1.00 69.30      A    C  
ANISOU 1133  CB  VAL A 155     9220   8033   9078    -11  -2144   1274  A    C  
ATOM   1134  CG1 VAL A 155      54.794 -15.650  -1.188  1.00 58.42      A    C  
ANISOU 1134  CG1 VAL A 155     7822   6784   7590    -93  -2112   1373  A    C  
ATOM   1135  CG2 VAL A 155      52.766 -17.049  -1.241  1.00 71.58      A    C  
ANISOU 1135  CG2 VAL A 155     9640   8138   9420   -210  -2056   1261  A    C  
ATOM   1136  N   LEU A 156      55.050 -14.976  -5.003  1.00 69.55      A    N  
ANISOU 1136  N   LEU A 156     8778   8553   9096    379  -2104   1135  A    N  
ATOM   1137  CA  LEU A 156      56.219 -14.683  -5.819  1.00 70.75      A    C  
ANISOU 1137  CA  LEU A 156     8784   8899   9200    565  -2152   1151  A    C  
ATOM   1138  C   LEU A 156      57.095 -13.680  -5.114  1.00 78.10      A    C  
ANISOU 1138  C   LEU A 156     9681   9942  10050    466  -2117   1265  A    C  
ATOM   1139  O   LEU A 156      56.607 -12.881  -4.321  1.00 77.15      A    O  
ANISOU 1139  O   LEU A 156     9616   9784   9913    271  -2022   1307  A    O  
ATOM   1140  CB  LEU A 156      55.807 -14.095  -7.167  1.00 63.25      A    C  
ANISOU 1140  CB  LEU A 156     7685   8081   8266    685  -2079   1068  A    C  
ATOM   1141  CG  LEU A 156      54.686 -14.841  -7.880  1.00 63.67      A    C  
ANISOU 1141  CG  LEU A 156     7753   8038   8401    750  -2092    929  A    C  
ATOM   1142  CD1 LEU A 156      54.503 -14.313  -9.296  1.00 59.74      A    C  
ANISOU 1142  CD1 LEU A 156     7098   7710   7890    921  -2046    851  A    C  
ATOM   1143  CD2 LEU A 156      54.995 -16.318  -7.878  1.00 61.99      A    C  
ANISOU 1143  CD2 LEU A 156     7619   7701   8232    859  -2240    881  A    C  
ATOM   1144  N   ILE A 157      58.390 -13.713  -5.409  1.00 84.57      A    N  
ANISOU 1144  N   ILE A 157    10403  10909  10823    601  -2194   1305  A    N  
ATOM   1145  CA  ILE A 157      59.272 -12.633  -4.987  1.00 80.30      A    C  
ANISOU 1145  CA  ILE A 157     9782  10511  10218    517  -2153   1393  A    C  
ATOM   1146  C   ILE A 157      60.012 -12.000  -6.148  1.00 82.10      A    C  
ANISOU 1146  C   ILE A 157     9813  10952  10428    660  -2115   1392  A    C  
ATOM   1147  O   ILE A 157      60.357 -12.672  -7.113  1.00 90.10      A    O  
ANISOU 1147  O   ILE A 157    10747  12038  11448    873  -2179   1340  A    O  
ATOM   1148  CB  ILE A 157      60.262 -13.081  -3.945  1.00 70.89      A    C  
ANISOU 1148  CB  ILE A 157     8649   9316   8971    493  -2270   1465  A    C  
ATOM   1149  CG1 ILE A 157      59.536 -13.923  -2.888  1.00 68.68      A    C  
ANISOU 1149  CG1 ILE A 157     8581   8813   8700    386  -2314   1476  A    C  
ATOM   1150  CG2 ILE A 157      60.914 -11.858  -3.328  1.00 70.14      A    C  
ANISOU 1150  CG2 ILE A 157     8489   9340   8822    345  -2214   1536  A    C  
ATOM   1151  CD1 ILE A 157      60.278 -14.047  -1.569  1.00 60.10      A    C  
ANISOU 1151  CD1 ILE A 157     7588   7715   7534    301  -2397   1565  A    C  
ATOM   1152  N   THR A 158      60.230 -10.694  -6.052  1.00 78.86      A    N  
ANISOU 1152  N   THR A 158     9330  10638   9995    539  -2005   1448  A    N  
ATOM   1153  CA  THR A 158      60.891  -9.947  -7.110  1.00 85.41      A    C  
ANISOU 1153  CA  THR A 158     9980  11665  10808    643  -1939   1469  A    C  
ATOM   1154  C   THR A 158      62.381  -9.754  -6.829  1.00 99.53      A    C  
ANISOU 1154  C   THR A 158    11654  13611  12552    652  -1997   1536  A    C  
ATOM   1155  O   THR A 158      62.801  -9.744  -5.674  1.00102.57      A    O  
ANISOU 1155  O   THR A 158    12100  13956  12915    520  -2056   1575  A    O  
ATOM   1156  CB  THR A 158      60.208  -8.583  -7.355  1.00 78.25      A    C  
ANISOU 1156  CB  THR A 158     9055  10763   9913    520  -1769   1491  A    C  
ATOM   1157  CG2 THR A 158      58.726  -8.780  -7.475  1.00 71.04      A    C  
ANISOU 1157  CG2 THR A 158     8249   9704   9041    500  -1722   1417  A    C  
ATOM   1158  OG1 THR A 158      60.485  -7.674  -6.275  1.00 79.40      A    O  
ANISOU 1158  OG1 THR A 158     9239  10883  10046    298  -1724   1556  A    O  
ATOM   1159  N   ARG A 159      63.166  -9.613  -7.897  1.00100.44      A    N  
ANISOU 1159  N   ARG A 159    11596  13917  12649    813  -1981   1544  A    N  
ATOM   1160  CA  ARG A 159      64.606  -9.396  -7.805  1.00100.26      A    C  
ANISOU 1160  CA  ARG A 159    11422  14080  12591    835  -2022   1598  A    C  
ATOM   1161  C   ARG A 159      64.978  -8.366  -6.723  1.00 94.18      A    C  
ANISOU 1161  C   ARG A 159    10660  13306  11818    582  -1979   1663  A    C  
ATOM   1162  O   ARG A 159      65.888  -8.600  -5.918  1.00 93.33      A    O  
ANISOU 1162  O   ARG A 159    10524  13253  11682    544  -2084   1683  A    O  
ATOM   1163  CB  ARG A 159      65.154  -8.970  -9.172  1.00109.55      A    C  
ANISOU 1163  CB  ARG A 159    12407  15467  13751    988  -1938   1614  A    C  
ATOM   1164  CG  ARG A 159      66.685  -8.931  -9.287  1.00123.14      A    C  
ANISOU 1164  CG  ARG A 159    13935  17413  15438   1053  -1983   1655  A    C  
ATOM   1165  CD  ARG A 159      67.137  -8.534 -10.699  1.00130.82      A    C  
ANISOU 1165  CD  ARG A 159    14724  18597  16386   1209  -1878   1677  A    C  
ATOM   1166  NE  ARG A 159      66.621  -7.221 -11.093  1.00144.25      A    N  
ANISOU 1166  NE  ARG A 159    16417  20287  18103   1074  -1692   1740  A    N  
ATOM   1167  CZ  ARG A 159      65.540  -7.023 -11.849  1.00149.11      A    C  
ANISOU 1167  CZ  ARG A 159    17103  20833  18719   1136  -1603   1719  A    C  
ATOM   1168  NH1 ARG A 159      64.849  -8.057 -12.316  1.00152.98      A    N1+
ANISOU 1168  NH1 ARG A 159    17665  21262  19200   1319  -1683   1624  A    N1+
ATOM   1169  NH2 ARG A 159      65.148  -5.787 -12.145  1.00141.79      A    N  
ANISOU 1169  NH2 ARG A 159    16175  19895  17804   1020  -1437   1788  A    N  
ATOM   1170  N   ASP A 160      64.278  -7.233  -6.693  1.00 72.21      A    N  
ANISOU 1170  N   ASP A 160     7915  10459   9061    419  -1833   1688  A    N  
ATOM   1171  CA  ASP A 160      64.567  -6.206  -5.694  1.00 72.40      A    C  
ANISOU 1171  CA  ASP A 160     7956  10464   9089    176  -1788   1732  A    C  
ATOM   1172  C   ASP A 160      64.001  -6.564  -4.318  1.00 77.01      A    C  
ANISOU 1172  C   ASP A 160     8728  10875   9657     36  -1861   1709  A    C  
ATOM   1173  O   ASP A 160      63.945  -5.709  -3.424  1.00 78.92      A    O  
ANISOU 1173  O   ASP A 160     9023  11067   9896   -171  -1817   1726  A    O  
ATOM   1174  CB  ASP A 160      64.060  -4.828  -6.138  1.00 94.35      A    C  
ANISOU 1174  CB  ASP A 160    10720  13225  11905     59  -1604   1766  A    C  
ATOM   1175  CG  ASP A 160      64.472  -4.472  -7.568  1.00116.48      A    C  
ANISOU 1175  CG  ASP A 160    13359  16188  14710    207  -1511   1804  A    C  
ATOM   1176  OD1 ASP A 160      65.386  -5.125  -8.114  1.00123.44      A    O  
ANISOU 1176  OD1 ASP A 160    14105  17231  15565    370  -1583   1805  A    O  
ATOM   1177  OD2 ASP A 160      63.878  -3.534  -8.150  1.00120.58      A    O1-
ANISOU 1177  OD2 ASP A 160    13889  16676  15251    172  -1361   1835  A    O1-
ATOM   1178  N   GLY A 161      63.564  -7.816  -4.165  1.00 77.94      A    N  
ANISOU 1178  N   GLY A 161     8954  10897   9764    149  -1966   1671  A    N  
ATOM   1179  CA  GLY A 161      63.168  -8.365  -2.871  1.00 91.13      A    C  
ANISOU 1179  CA  GLY A 161    10803  12417  11404     44  -2047   1667  A    C  
ATOM   1180  C   GLY A 161      61.776  -8.076  -2.309  1.00 92.03      A    C  
ANISOU 1180  C   GLY A 161    11088  12343  11535   -109  -1957   1646  A    C  
ATOM   1181  O   GLY A 161      61.565  -8.160  -1.093  1.00 91.69      A    O  
ANISOU 1181  O   GLY A 161    11181  12206  11453   -247  -1991   1658  A    O  
ATOM   1182  N   VAL A 162      60.828  -7.747  -3.183  1.00 78.27      A    N  
ANISOU 1182  N   VAL A 162     9338  10560   9843    -75  -1842   1611  A    N  
ATOM   1183  CA  VAL A 162      59.473  -7.425  -2.759  1.00 71.26      A    C  
ANISOU 1183  CA  VAL A 162     8584   9516   8976   -204  -1746   1581  A    C  
ATOM   1184  C   VAL A 162      58.567  -8.595  -3.048  1.00 79.66      A    C  
ANISOU 1184  C   VAL A 162     9732  10463  10072   -105  -1788   1524  A    C  
ATOM   1185  O   VAL A 162      58.620  -9.166  -4.134  1.00 84.45      A    O  
ANISOU 1185  O   VAL A 162    10260  11119  10707     80  -1819   1487  A    O  
ATOM   1186  CB  VAL A 162      58.892  -6.242  -3.541  1.00 76.89      A    C  
ANISOU 1186  CB  VAL A 162     9235  10255   9726   -228  -1589   1571  A    C  
ATOM   1187  CG1 VAL A 162      57.689  -5.679  -2.808  1.00 74.46      A    C  
ANISOU 1187  CG1 VAL A 162     9058   9807   9427   -394  -1491   1543  A    C  
ATOM   1188  CG2 VAL A 162      59.932  -5.161  -3.768  1.00 80.86      A    C  
ANISOU 1188  CG2 VAL A 162     9609  10893  10221   -271  -1540   1628  A    C  
ATOM   1189  N   LEU A 163      57.711  -8.927  -2.090  1.00 82.01      A    N  
ANISOU 1189  N   LEU A 163    10188  10608  10366   -233  -1780   1513  A    N  
ATOM   1190  CA  LEU A 163      56.800 -10.062  -2.219  1.00 78.05      A    C  
ANISOU 1190  CA  LEU A 163     9777   9971   9907   -180  -1814   1459  A    C  
ATOM   1191  C   LEU A 163      55.455  -9.740  -2.896  1.00 76.17      A    C  
ANISOU 1191  C   LEU A 163     9528   9683   9732   -186  -1696   1381  A    C  
ATOM   1192  O   LEU A 163      54.841  -8.701  -2.650  1.00 81.45      A    O  
ANISOU 1192  O   LEU A 163    10204  10345  10397   -308  -1576   1378  A    O  
ATOM   1193  CB  LEU A 163      56.507 -10.622  -0.843  1.00 76.57      A    C  
ANISOU 1193  CB  LEU A 163     9766   9644   9682   -322  -1851   1494  A    C  
ATOM   1194  CG  LEU A 163      55.445 -11.702  -0.878  1.00 74.27      A    C  
ANISOU 1194  CG  LEU A 163     9580   9190   9450   -314  -1858   1444  A    C  
ATOM   1195  CD1 LEU A 163      56.210 -12.963  -1.048  1.00 86.46      A    C  
ANISOU 1195  CD1 LEU A 163    11148  10707  10996   -159  -2012   1460  A    C  
ATOM   1196  CD2 LEU A 163      54.677 -11.724   0.408  1.00 68.83      A    C  
ANISOU 1196  CD2 LEU A 163     9053   8371   8727   -514  -1802   1474  A    C  
ATOM   1197  N   LYS A 164      54.985 -10.648  -3.734  1.00 62.26      A    N  
ANISOU 1197  N   LYS A 164     7746   7884   8026    -48  -1739   1309  A    N  
ATOM   1198  CA  LYS A 164      53.698 -10.459  -4.367  1.00 62.13      A    C  
ANISOU 1198  CA  LYS A 164     7709   7831   8068    -43  -1648   1219  A    C  
ATOM   1199  C   LYS A 164      52.852 -11.725  -4.217  1.00 69.34      A    C  
ANISOU 1199  C   LYS A 164     8714   8588   9044    -51  -1699   1149  A    C  
ATOM   1200  O   LYS A 164      53.386 -12.834  -4.273  1.00 79.55      A    O  
ANISOU 1200  O   LYS A 164    10043   9832  10350     42  -1821   1149  A    O  
ATOM   1201  CB  LYS A 164      53.865 -10.124  -5.853  1.00 51.71      A    C  
ANISOU 1201  CB  LYS A 164     6235   6655   6759    154  -1632   1174  A    C  
ATOM   1202  CG  LYS A 164      54.917  -9.077  -6.207  1.00 42.18      A    C  
ANISOU 1202  CG  LYS A 164     4922   5608   5498    194  -1593   1255  A    C  
ATOM   1203  CD  LYS A 164      54.800  -7.779  -5.426  1.00 80.33      A    C  
ANISOU 1203  CD  LYS A 164     9788  10430  10304      6  -1480   1315  A    C  
ATOM   1204  CE  LYS A 164      55.334  -6.577  -6.226  1.00 64.64      A    C  
ANISOU 1204  CE  LYS A 164     7681   8583   8296     63  -1393   1364  A    C  
ATOM   1205  NZ  LYS A 164      54.511  -6.370  -7.472  1.00 71.83      A    N1+
ANISOU 1205  NZ  LYS A 164     8525   9540   9227    212  -1328   1303  A    N1+
ATOM   1206  N   LEU A 165      51.540 -11.558  -4.027  1.00 60.33      A    N  
ANISOU 1206  N   LEU A 165     7609   7366   7947   -164  -1605   1087  A    N  
ATOM   1207  CA  LEU A 165      50.614 -12.691  -4.012  1.00 62.91      A    C  
ANISOU 1207  CA  LEU A 165     8000   7549   8354   -188  -1635   1004  A    C  
ATOM   1208  C   LEU A 165      50.044 -12.884  -5.416  1.00 70.78      A    C  
ANISOU 1208  C   LEU A 165     8872   8606   9415    -22  -1645    872  A    C  
ATOM   1209  O   LEU A 165      49.896 -11.915  -6.160  1.00 71.15      A    O  
ANISOU 1209  O   LEU A 165     8807   8787   9439     53  -1577    848  A    O  
ATOM   1210  CB  LEU A 165      49.483 -12.482  -2.998  1.00 60.73      A    C  
ANISOU 1210  CB  LEU A 165     7817   7164   8092   -409  -1526   1001  A    C  
ATOM   1211  CG  LEU A 165      49.875 -12.117  -1.562  1.00 70.04      A    C  
ANISOU 1211  CG  LEU A 165     9123   8302   9188   -583  -1495   1120  A    C  
ATOM   1212  CD1 LEU A 165      48.655 -11.846  -0.719  1.00 69.84      A    C  
ANISOU 1212  CD1 LEU A 165     9168   8198   9171   -779  -1369   1099  A    C  
ATOM   1213  CD2 LEU A 165      50.709 -13.204  -0.930  1.00 84.77      A    C  
ANISOU 1213  CD2 LEU A 165    11107  10075  11027   -573  -1618   1200  A    C  
ATOM   1214  N   ALA A 166      49.730 -14.125  -5.787  1.00 65.03      A    N  
ANISOU 1214  N   ALA A 166     8167   7777   8763     41  -1732    785  A    N  
ATOM   1215  CA  ALA A 166      49.342 -14.393  -7.166  1.00 69.18      A    C  
ANISOU 1215  CA  ALA A 166     8570   8377   9338    225  -1769    646  A    C  
ATOM   1216  C   ALA A 166      48.226 -15.429  -7.325  1.00 81.25      A    C  
ANISOU 1216  C   ALA A 166    10126   9762  10982    181  -1796    507  A    C  
ATOM   1217  O   ALA A 166      47.778 -16.041  -6.354  1.00 76.95      A    O  
ANISOU 1217  O   ALA A 166     9706   9045  10488      3  -1784    531  A    O  
ATOM   1218  CB  ALA A 166      50.567 -14.792  -7.979  1.00 79.70      A    C  
ANISOU 1218  CB  ALA A 166     9845   9806  10632    451  -1884    657  A    C  
ATOM   1219  N   ASP A 167      47.801 -15.624  -8.572  1.00 93.83      A    N  
ANISOU 1219  N   ASP A 167    11601  11436  12615    347  -1834    360  A    N  
ATOM   1220  CA  ASP A 167      46.675 -16.492  -8.904  1.00101.79      A    C  
ANISOU 1220  CA  ASP A 167    12596  12337  13741    314  -1861    194  A    C  
ATOM   1221  C   ASP A 167      45.421 -16.061  -8.161  1.00 96.80      A    C  
ANISOU 1221  C   ASP A 167    11978  11646  13154     87  -1733    175  A    C  
ATOM   1222  O   ASP A 167      45.068 -16.612  -7.104  1.00 89.06      A    O  
ANISOU 1222  O   ASP A 167    11121  10493  12226   -116  -1704    219  A    O  
ATOM   1223  CB  ASP A 167      46.972 -17.975  -8.638  1.00110.23      A    C  
ANISOU 1223  CB  ASP A 167    13784  13207  14892    304  -1981    170  A    C  
ATOM   1224  CG  ASP A 167      46.108 -18.908  -9.492  1.00123.95      A    C  
ANISOU 1224  CG  ASP A 167    15466  14878  16752    363  -2050    -41  A    C  
ATOM   1225  OD1 ASP A 167      45.282 -19.663  -8.929  1.00129.67      A    O  
ANISOU 1225  OD1 ASP A 167    16267  15410  17590    182  -2037    -92  A    O  
ATOM   1226  OD2 ASP A 167      46.250 -18.880 -10.734  1.00126.39      A    O1-
ANISOU 1226  OD2 ASP A 167    15651  15329  17040    587  -2116   -158  A    O1-
ATOM   1227  N   PHE A 168      44.752 -15.059  -8.717  1.00 86.24      A    N  
ANISOU 1227  N   PHE A 168    10517  10462  11790    132  -1651    114  A    N  
ATOM   1228  CA  PHE A 168      43.443 -14.686  -8.213  1.00 75.77      A    C  
ANISOU 1228  CA  PHE A 168     9168   9107  10513    -45  -1536     57  A    C  
ATOM   1229  C   PHE A 168      42.380 -15.375  -9.039  1.00 79.92      A    C  
ANISOU 1229  C   PHE A 168     9590   9629  11149     -1  -1580   -154  A    C  
ATOM   1230  O   PHE A 168      41.251 -14.893  -9.190  1.00 82.12      A    O  
ANISOU 1230  O   PHE A 168     9769   9975  11458    -47  -1503   -256  A    O  
ATOM   1231  CB  PHE A 168      43.306 -13.175  -8.178  1.00 68.70      A    C  
ANISOU 1231  CB  PHE A 168     8215   8361   9525    -33  -1417    118  A    C  
ATOM   1232  CG  PHE A 168      44.101 -12.552  -7.076  1.00 77.57      A    C  
ANISOU 1232  CG  PHE A 168     9454   9452  10567   -153  -1359    304  A    C  
ATOM   1233  CD1 PHE A 168      43.510 -12.235  -5.870  1.00 68.01      A    C  
ANISOU 1233  CD1 PHE A 168     8323   8161   9356   -376  -1251    353  A    C  
ATOM   1234  CD2 PHE A 168      45.456 -12.351  -7.216  1.00 92.92      A    C  
ANISOU 1234  CD2 PHE A 168    11424  11448  12433    -46  -1417    419  A    C  
ATOM   1235  CE1 PHE A 168      44.241 -11.699  -4.845  1.00 59.23      A    C  
ANISOU 1235  CE1 PHE A 168     7319   7023   8162   -482  -1209    507  A    C  
ATOM   1236  CE2 PHE A 168      46.193 -11.802  -6.182  1.00 85.94      A    C  
ANISOU 1236  CE2 PHE A 168    10637  10539  11476   -163  -1375    573  A    C  
ATOM   1237  CZ  PHE A 168      45.576 -11.480  -4.998  1.00 69.04      A    C  
ANISOU 1237  CZ  PHE A 168     8582   8318   9332   -379  -1276    612  A    C  
ATOM   1238  N   GLY A 169      42.775 -16.535  -9.559  1.00 80.79      A    N  
ANISOU 1238  N   GLY A 169     9721   9657  11319     93  -1713   -228  A    N  
ATOM   1239  CA  GLY A 169      41.924 -17.343 -10.399  1.00 81.68      A    C  
ANISOU 1239  CA  GLY A 169     9740   9751  11544    146  -1786   -446  A    C  
ATOM   1240  C   GLY A 169      40.818 -17.931  -9.567  1.00 85.37      A    C  
ANISOU 1240  C   GLY A 169    10247  10048  12140   -119  -1723   -504  A    C  
ATOM   1241  O   GLY A 169      39.723 -18.183 -10.072  1.00 89.89      A    O  
ANISOU 1241  O   GLY A 169    10702  10645  12808   -142  -1725   -692  A    O  
ATOM   1242  N   LEU A 170      41.104 -18.141  -8.285  1.00 84.13      A    N  
ANISOU 1242  N   LEU A 170    10252   9731  11983   -320  -1665   -342  A    N  
ATOM   1243  CA  LEU A 170      40.111 -18.698  -7.378  1.00 90.06      A    C  
ANISOU 1243  CA  LEU A 170    11058  10314  12845   -591  -1583   -364  A    C  
ATOM   1244  C   LEU A 170      39.536 -17.660  -6.435  1.00 83.37      A    C  
ANISOU 1244  C   LEU A 170    10210   9531  11936   -762  -1414   -273  A    C  
ATOM   1245  O   LEU A 170      38.543 -17.920  -5.754  1.00 81.91      A    O  
ANISOU 1245  O   LEU A 170    10031   9261  11832   -983  -1318   -306  A    O  
ATOM   1246  CB  LEU A 170      40.691 -19.853  -6.571  1.00102.20      A    C  
ANISOU 1246  CB  LEU A 170    12797  11602  14433   -706  -1634   -257  A    C  
ATOM   1247  CG  LEU A 170      40.945 -21.142  -7.338  1.00 98.82      A    C  
ANISOU 1247  CG  LEU A 170    12390  11041  14114   -595  -1790   -380  A    C  
ATOM   1248  CD1 LEU A 170      41.248 -22.251  -6.347  1.00 99.88      A    C  
ANISOU 1248  CD1 LEU A 170    12741  10894  14313   -756  -1808   -264  A    C  
ATOM   1249  CD2 LEU A 170      39.722 -21.463  -8.160  1.00 95.27      A    C  
ANISOU 1249  CD2 LEU A 170    11779  10620  13799   -614  -1801   -628  A    C  
ATOM   1250  N   ALA A 171      40.165 -16.492  -6.383  1.00 78.66      A    N  
ANISOU 1250  N   ALA A 171     9605   9082  11200   -664  -1374   -160  A    N  
ATOM   1251  CA  ALA A 171      39.670 -15.409  -5.544  1.00 69.68      A    C  
ANISOU 1251  CA  ALA A 171     8467   8012   9995   -800  -1220    -85  A    C  
ATOM   1252  C   ALA A 171      38.201 -15.121  -5.833  1.00 65.57      A    C  
ANISOU 1252  C   ALA A 171     7791   7574   9550   -859  -1135   -254  A    C  
ATOM   1253  O   ALA A 171      37.730 -15.358  -6.927  1.00 67.15      A    O  
ANISOU 1253  O   ALA A 171     7851   7851   9813   -727  -1204   -425  A    O  
ATOM   1254  CB  ALA A 171      40.495 -14.161  -5.768  1.00 62.70      A    C  
ANISOU 1254  CB  ALA A 171     7567   7284   8972   -650  -1205     17  A    C  
ATOM   1255  N   ARG A 172      37.492 -14.603  -4.838  1.00 72.80      A    N  
ANISOU 1255  N   ARG A 172     8727   8485  10450  -1050   -989   -212  A    N  
ATOM   1256  CA  ARG A 172      36.113 -14.151  -4.976  1.00 73.17      A    C  
ANISOU 1256  CA  ARG A 172     8617   8636  10548  -1107   -890   -359  A    C  
ATOM   1257  C   ARG A 172      35.881 -13.051  -3.930  1.00 78.07      A    C  
ANISOU 1257  C   ARG A 172     9283   9308  11070  -1222   -734   -253  A    C  
ATOM   1258  O   ARG A 172      36.602 -12.977  -2.915  1.00 67.05      A    O  
ANISOU 1258  O   ARG A 172     8055   7823   9596  -1326   -699    -81  A    O  
ATOM   1259  CB  ARG A 172      35.141 -15.308  -4.717  1.00 65.74      A    C  
ANISOU 1259  CB  ARG A 172     7647   7568   9763  -1306   -871   -473  A    C  
ATOM   1260  CG  ARG A 172      34.410 -15.178  -3.396  1.00 72.37      A    C  
ANISOU 1260  CG  ARG A 172     8541   8351  10604  -1573   -702   -408  A    C  
ATOM   1261  CD  ARG A 172      33.680 -16.436  -2.959  1.00 94.34      A    C  
ANISOU 1261  CD  ARG A 172    11344  10965  13538  -1806   -671   -466  A    C  
ATOM   1262  NE  ARG A 172      32.441 -16.707  -3.691  1.00113.11      A    N  
ANISOU 1262  NE  ARG A 172    13504  13419  16055  -1827   -667   -702  A    N  
ATOM   1263  CZ  ARG A 172      31.408 -15.871  -3.781  1.00116.07      A    C  
ANISOU 1263  CZ  ARG A 172    13701  13976  16423  -1830   -567   -816  A    C  
ATOM   1264  NH1 ARG A 172      31.465 -14.682  -3.202  1.00122.77      A    N1+
ANISOU 1264  NH1 ARG A 172    14575  14937  17135  -1807   -459   -716  A    N1+
ATOM   1265  NH2 ARG A 172      30.320 -16.218  -4.466  1.00110.20      A    N  
ANISOU 1265  NH2 ARG A 172    12752  13307  15813  -1846   -581  -1042  A    N  
ATOM   1266  N   ALA A 173      34.878 -12.204  -4.153  1.00 70.11      A    N  
ANISOU 1266  N   ALA A 173     8130   8448  10060  -1194   -645   -362  A    N  
ATOM   1267  CA  ALA A 173      34.558 -11.175  -3.164  1.00 60.94      A    C  
ANISOU 1267  CA  ALA A 173     7009   7333   8812  -1297   -493   -286  A    C  
ATOM   1268  C   ALA A 173      33.708 -11.737  -2.026  1.00 68.88      A    C  
ANISOU 1268  C   ALA A 173     8050   8248   9873  -1573   -371   -288  A    C  
ATOM   1269  O   ALA A 173      33.073 -12.773  -2.182  1.00 76.58      A    O  
ANISOU 1269  O   ALA A 173     8966   9154  10975  -1677   -388   -388  A    O  
ATOM   1270  CB  ALA A 173      33.868 -10.014  -3.814  1.00 55.77      A    C  
ANISOU 1270  CB  ALA A 173     6200   6865   8125  -1140   -445   -391  A    C  
ATOM   1271  N   PHE A 174      33.711 -11.069  -0.876  1.00 69.63      A    N  
ANISOU 1271  N   PHE A 174     8245   8340   9870  -1696   -245   -178  A    N  
ATOM   1272  CA  PHE A 174      32.895 -11.515   0.251  1.00 75.23      A    C  
ANISOU 1272  CA  PHE A 174     8990   8986  10609  -1955   -108   -167  A    C  
ATOM   1273  C   PHE A 174      32.206 -10.351   0.957  1.00 96.39      A    C  
ANISOU 1273  C   PHE A 174    11634  11789  13203  -2000     53   -180  A    C  
ATOM   1274  O   PHE A 174      32.603  -9.192   0.801  1.00 91.76      A    O  
ANISOU 1274  O   PHE A 174    11054  11292  12517  -1852     55   -152  A    O  
ATOM   1275  CB  PHE A 174      33.710 -12.347   1.240  1.00 70.06      A    C  
ANISOU 1275  CB  PHE A 174     8557   8147   9916  -2111   -121     12  A    C  
ATOM   1276  CG  PHE A 174      34.601 -11.536   2.138  1.00 84.58      A    C  
ANISOU 1276  CG  PHE A 174    10559   9989  11588  -2111    -89    179  A    C  
ATOM   1277  CD1 PHE A 174      35.880 -11.186   1.740  1.00 90.08      A    C  
ANISOU 1277  CD1 PHE A 174    11327  10686  12213  -1945   -212    267  A    C  
ATOM   1278  CD2 PHE A 174      34.167 -11.140   3.397  1.00 85.55      A    C  
ANISOU 1278  CD2 PHE A 174    10759  10123  11625  -2283     65    241  A    C  
ATOM   1279  CE1 PHE A 174      36.706 -10.440   2.580  1.00 89.42      A    C  
ANISOU 1279  CE1 PHE A 174    11382  10609  11984  -1958   -189    405  A    C  
ATOM   1280  CE2 PHE A 174      34.994 -10.399   4.244  1.00 79.39      A    C  
ANISOU 1280  CE2 PHE A 174    10129   9349  10687  -2284     84    378  A    C  
ATOM   1281  CZ  PHE A 174      36.260 -10.053   3.834  1.00 79.31      A    C  
ANISOU 1281  CZ  PHE A 174    10183   9335  10618  -2127    -47    455  A    C  
ATOM   1282  N   SER A 175      31.160 -10.669   1.720  1.00116.58      A    N  
ANISOU 1282  N   SER A 175    14149  14345  15800  -2206    194   -225  A    N  
ATOM   1283  CA  SER A 175      30.341  -9.655   2.387  1.00122.05      A    C  
ANISOU 1283  CA  SER A 175    14785  15167  16422  -2251    357   -266  A    C  
ATOM   1284  C   SER A 175      29.808 -10.148   3.727  1.00128.05      A    C  
ANISOU 1284  C   SER A 175    15625  15867  17161  -2524    515   -200  A    C  
ATOM   1285  O   SER A 175      30.221 -11.195   4.225  1.00125.42      A    O  
ANISOU 1285  O   SER A 175    15430  15375  16850  -2674    495    -88  A    O  
ATOM   1286  CB  SER A 175      29.181  -9.222   1.486  1.00119.31      A    C  
ANISOU 1286  CB  SER A 175    14183  14991  16160  -2137    379   -479  A    C  
ATOM   1287  OG  SER A 175      28.490 -10.346   0.967  1.00121.16      A    O  
ANISOU 1287  OG  SER A 175    14284  15197  16555  -2224    345   -603  A    O  
ATOM   1288  N   LEU A 176      28.883  -9.390   4.304  1.00142.36      A    N  
ANISOU 1288  N   LEU A 176    17355  17809  18926  -2579    675   -266  A    N  
ATOM   1289  CA  LEU A 176      28.343  -9.714   5.621  1.00153.14      A    C  
ANISOU 1289  CA  LEU A 176    18792  19149  20245  -2827    848   -201  A    C  
ATOM   1290  C   LEU A 176      26.864 -10.104   5.552  1.00159.29      A    C  
ANISOU 1290  C   LEU A 176    19352  20021  21150  -2959    974   -364  A    C  
ATOM   1291  O   LEU A 176      26.171 -10.143   6.570  1.00161.52      A    O  
ANISOU 1291  O   LEU A 176    19638  20340  21390  -3148   1152   -344  A    O  
ATOM   1292  CB  LEU A 176      28.557  -8.530   6.565  1.00156.56      A    C  
ANISOU 1292  CB  LEU A 176    19333  19658  20496  -2805    948   -132  A    C  
ATOM   1293  CG  LEU A 176      29.992  -7.990   6.464  1.00162.20      A    C  
ANISOU 1293  CG  LEU A 176    20220  20305  21103  -2655    812     -5  A    C  
ATOM   1294  CD1 LEU A 176      30.140  -6.616   7.115  1.00162.49      A    C  
ANISOU 1294  CD1 LEU A 176    20323  20431  20985  -2588    889     10  A    C  
ATOM   1295  CD2 LEU A 176      30.993  -8.993   7.041  1.00160.60      A    C  
ANISOU 1295  CD2 LEU A 176    20230  19927  20864  -2772    742    177  A    C  
ATOM   1296  N   ALA A 177      26.395 -10.404   4.342  1.00158.21      A    N  
ANISOU 1296  N   ALA A 177    19016  19933  21162  -2859    879   -529  A    N  
ATOM   1297  CA  ALA A 177      25.013 -10.817   4.124  1.00159.93      A    C  
ANISOU 1297  CA  ALA A 177    18994  20252  21522  -2974    972   -711  A    C  
ATOM   1298  C   ALA A 177      24.620 -11.974   5.039  1.00161.16      A    C  
ANISOU 1298  C   ALA A 177    19213  20280  21742  -3294   1094   -636  A    C  
ATOM   1299  O   ALA A 177      24.057 -12.974   4.587  1.00160.15      A    O  
ANISOU 1299  O   ALA A 177    18965  20098  21788  -3414   1075   -734  A    O  
ATOM   1300  CB  ALA A 177      24.795 -11.193   2.662  1.00155.04      A    C  
ANISOU 1300  CB  ALA A 177    18187  19668  21053  -2824    811   -885  A    C  
ATOM   1301  N   PRO A 182      22.544 -15.794   5.922  1.00146.88      A    N  
ANISOU 1301  N   PRO A 182    17271  18126  20409  -4162   1359   -686  A    N  
ATOM   1302  CA  PRO A 182      23.967 -16.154   5.921  1.00154.85      A    C  
ANISOU 1302  CA  PRO A 182    18566  18925  21346  -4067   1202   -496  A    C  
ATOM   1303  C   PRO A 182      24.452 -16.511   4.520  1.00165.56      A    C  
ANISOU 1303  C   PRO A 182    19857  20224  22823  -3868    963   -616  A    C  
ATOM   1304  O   PRO A 182      23.643 -16.865   3.659  1.00172.51      A    O  
ANISOU 1304  O   PRO A 182    20503  21165  23878  -3879    924   -831  A    O  
ATOM   1305  CB  PRO A 182      24.005 -17.392   6.814  1.00149.44      A    C  
ANISOU 1305  CB  PRO A 182    18066  18004  20712  -4362   1300   -328  A    C  
ATOM   1306  CG  PRO A 182      22.685 -18.025   6.581  1.00150.35      A    C  
ANISOU 1306  CG  PRO A 182    17938  18154  21034  -4577   1408   -505  A    C  
ATOM   1307  CD  PRO A 182      21.711 -16.876   6.470  1.00146.71      A    C  
ANISOU 1307  CD  PRO A 182    17208  18006  20531  -4496   1512   -684  A    C  
ATOM   1308  N   ASN A 183      25.763 -16.427   4.307  1.00161.64      A    N  
ANISOU 1308  N   ASN A 183    19561  19623  22231  -3689    805   -484  A    N  
ATOM   1309  CA  ASN A 183      26.358 -16.645   2.992  1.00151.69      A    C  
ANISOU 1309  CA  ASN A 183    18255  18331  21049  -3464    579   -583  A    C  
ATOM   1310  C   ASN A 183      26.283 -18.097   2.535  1.00145.56      A    C  
ANISOU 1310  C   ASN A 183    17489  17345  20472  -3591    494   -637  A    C  
ATOM   1311  O   ASN A 183      26.017 -18.999   3.332  1.00144.73      A    O  
ANISOU 1311  O   ASN A 183    17490  17068  20434  -3856    600   -544  A    O  
ATOM   1312  CB  ASN A 183      27.821 -16.192   2.989  1.00147.48      A    C  
ANISOU 1312  CB  ASN A 183    17936  17744  20355  -3258    450   -413  A    C  
ATOM   1313  CG  ASN A 183      28.011 -14.814   3.596  1.00148.53      A    C  
ANISOU 1313  CG  ASN A 183    18105  18039  20292  -3164    538   -336  A    C  
ATOM   1314  ND2 ASN A 183      29.118 -14.630   4.320  1.00144.99      A    N  
ANISOU 1314  ND2 ASN A 183    17897  17502  19690  -3142    515   -128  A    N  
ATOM   1315  OD1 ASN A 183      27.180 -13.923   3.414  1.00149.30      A    O  
ANISOU 1315  OD1 ASN A 183    18015  18337  20375  -3106    618   -470  A    O  
ATOM   1316  N   ARG A 184      26.526 -18.312   1.245  1.00134.20      A    N  
ANISOU 1316  N   ARG A 184    15948  15917  19124  -3396    303   -788  A    N  
ATOM   1317  CA  ARG A 184      26.575 -19.654   0.690  1.00127.44      A    C  
ANISOU 1317  CA  ARG A 184    15112  14855  18456  -3475    191   -860  A    C  
ATOM   1318  C   ARG A 184      27.721 -19.772  -0.319  1.00118.30      A    C  
ANISOU 1318  C   ARG A 184    14030  13648  17272  -3194    -42   -866  A    C  
ATOM   1319  O   ARG A 184      27.493 -20.037  -1.498  1.00121.61      A    O  
ANISOU 1319  O   ARG A 184    14286  14116  17802  -3064   -179  -1072  A    O  
ATOM   1320  CB  ARG A 184      25.229 -20.007   0.044  1.00133.28      A    C  
ANISOU 1320  CB  ARG A 184    15559  15688  19394  -3582    217  -1133  A    C  
ATOM   1321  CG  ARG A 184      25.031 -21.500  -0.253  1.00143.12      A    C  
ANISOU 1321  CG  ARG A 184    16826  16689  20865  -3763    153  -1213  A    C  
ATOM   1322  CD  ARG A 184      23.620 -21.813  -0.774  1.00147.81      A    C  
ANISOU 1322  CD  ARG A 184    17111  17390  21661  -3907    198  -1493  A    C  
ATOM   1323  NE  ARG A 184      22.630 -21.941   0.297  1.00150.10      A    N  
ANISOU 1323  NE  ARG A 184    17347  17682  22001  -4234    441  -1451  A    N  
ATOM   1324  CZ  ARG A 184      21.963 -20.924   0.843  1.00146.87      A    C  
ANISOU 1324  CZ  ARG A 184    16806  17514  21483  -4254    607  -1453  A    C  
ATOM   1325  NH1 ARG A 184      22.174 -19.679   0.429  1.00145.59      A    N1+
ANISOU 1325  NH1 ARG A 184    16564  17592  21161  -3965    553  -1490  A    N1+
ATOM   1326  NH2 ARG A 184      21.084 -21.151   1.814  1.00138.24      A    N  
ANISOU 1326  NH2 ARG A 184    15667  16417  20440  -4560    833  -1414  A    N  
ATOM   1327  N   TYR A 185      28.953 -19.569   0.144  1.00114.32      A    N  
ANISOU 1327  N   TYR A 185    13762  13060  16614  -3096    -88   -645  A    N  
ATOM   1328  CA  TYR A 185      30.126 -19.626  -0.738  1.00109.40      A    C  
ANISOU 1328  CA  TYR A 185    13213  12407  15949  -2827   -295   -631  A    C  
ATOM   1329  C   TYR A 185      30.528 -21.073  -0.977  1.00112.11      A    C  
ANISOU 1329  C   TYR A 185    13682  12483  16434  -2888   -411   -629  A    C  
ATOM   1330  O   TYR A 185      30.263 -21.941  -0.149  1.00115.32      A    O  
ANISOU 1330  O   TYR A 185    14214  12686  16918  -3139   -322   -540  A    O  
ATOM   1331  CB  TYR A 185      31.333 -18.839  -0.179  1.00103.27      A    C  
ANISOU 1331  CB  TYR A 185    12623  11656  14959  -2694   -308   -408  A    C  
ATOM   1332  CG  TYR A 185      31.069 -17.381   0.164  1.00 96.95      A    C  
ANISOU 1332  CG  TYR A 185    11743  11084  14011  -2634   -194   -389  A    C  
ATOM   1333  CD1 TYR A 185      30.388 -16.552  -0.713  1.00 98.68      A    C  
ANISOU 1333  CD1 TYR A 185    11726  11525  14243  -2486   -200   -575  A    C  
ATOM   1334  CD2 TYR A 185      31.514 -16.838   1.362  1.00100.39      A    C  
ANISOU 1334  CD2 TYR A 185    12347  11509  14287  -2714    -89   -189  A    C  
ATOM   1335  CE1 TYR A 185      30.136 -15.226  -0.401  1.00107.23      A    C  
ANISOU 1335  CE1 TYR A 185    12750  12794  15197  -2422    -97   -559  A    C  
ATOM   1336  CE2 TYR A 185      31.270 -15.510   1.688  1.00107.62      A    C  
ANISOU 1336  CE2 TYR A 185    13199  12615  15074  -2659     13   -184  A    C  
ATOM   1337  CZ  TYR A 185      30.582 -14.705   0.799  1.00114.94      A    C  
ANISOU 1337  CZ  TYR A 185    13900  13744  16030  -2512     10   -367  A    C  
ATOM   1338  OH  TYR A 185      30.333 -13.378   1.101  1.00116.55      A    O  
ANISOU 1338  OH  TYR A 185    14052  14121  16112  -2443    108   -366  A    O  
HETATM 1339  N   TPO A 186      31.160 -21.304  -2.118  1.00110.66      A    N  
ANISOU 1339  N   TPO A 186    13471  12300  16276  -2651   -605   -724  A    N  
HETATM 1340  CA  TPO A 186      31.701 -22.616  -2.561  1.00101.07      A    C  
ANISOU 1340  CA  TPO A 186    12356  10838  15206  -2659   -745   -767  A    C  
HETATM 1341  C   TPO A 186      32.587 -23.278  -1.567  1.00108.94      A    C  
ANISOU 1341  C   TPO A 186    13653  11598  16139  -2698   -770   -519  A    C  
HETATM 1342  O   TPO A 186      33.366 -22.582  -0.953  1.00111.24      A    O  
ANISOU 1342  O   TPO A 186    14060  11954  16253  -2562   -788   -348  A    O  
HETATM 1343  CB  TPO A 186      32.629 -22.192  -3.670  1.00 89.83      A    C  
ANISOU 1343  CB  TPO A 186    10799   9550  13781  -2349   -934   -940  A    C  
HETATM 1344  CG2 TPO A 186      32.546 -23.056  -4.898  1.00 77.36      A    C  
ANISOU 1344  CG2 TPO A 186     9400   7800  12193  -2186  -1108   -869  A    C  
HETATM 1345  OG1 TPO A 186      32.374 -20.839  -4.008  1.00 98.93      A    O  
ANISOU 1345  OG1 TPO A 186    11858  10970  14760  -2168   -902   -909  A    O  
HETATM 1346  P   TPO A 186      32.104 -20.367  -5.488  1.00111.92      A    P  
ANISOU 1346  P   TPO A 186    13300  12863  16363  -1854  -1029  -1093  A    P  
HETATM 1347  O1P TPO A 186      33.449 -20.262  -6.094  1.00100.27      A    O  
ANISOU 1347  O1P TPO A 186    11962  11350  14787  -1617  -1176   -984  A    O  
HETATM 1348  O2P TPO A 186      31.305 -21.483  -6.024  1.00121.69      A    O1-
ANISOU 1348  O2P TPO A 186    14368  14076  17795  -1901  -1100  -1361  A    O1-
HETATM 1349  O3P TPO A 186      31.364 -19.088  -5.355  1.00 84.74      A    O  
ANISOU 1349  O3P TPO A 186     9742   9652  12801  -1832   -896  -1071  A    O  
ATOM   1350  N   ASN A 187      32.519 -24.597  -1.400  1.00126.05      A    N  
ANISOU 1350  N   ASN A 187    15952  13486  18456  -2881   -773   -498  A    N  
ATOM   1351  CA  ASN A 187      33.423 -25.264  -0.459  1.00130.32      A    C  
ANISOU 1351  CA  ASN A 187    16795  13783  18939  -2943   -777   -246  A    C  
ATOM   1352  C   ASN A 187      34.688 -25.879  -1.069  1.00128.67      A    C  
ANISOU 1352  C   ASN A 187    16725  13446  18717  -2702   -989   -216  A    C  
ATOM   1353  O   ASN A 187      35.697 -26.040  -0.388  1.00119.41      A    O  
ANISOU 1353  O   ASN A 187    15777  12166  17428  -2653  -1020      2  A    O  
ATOM   1354  CB  ASN A 187      32.662 -26.328   0.332  1.00135.45      A    C  
ANISOU 1354  CB  ASN A 187    17553  14171  19741  -3271   -653   -198  A    C  
ATOM   1355  CG  ASN A 187      33.486 -26.916   1.459  1.00139.45      A    C  
ANISOU 1355  CG  ASN A 187    18383  14442  20160  -3346   -628     90  A    C  
ATOM   1356  ND2 ASN A 187      33.141 -26.567   2.689  1.00142.97      A    N  
ANISOU 1356  ND2 ASN A 187    18915  14906  20503  -3547   -437    266  A    N  
ATOM   1357  OD1 ASN A 187      34.423 -27.674   1.225  1.00141.04      A    O  
ANISOU 1357  OD1 ASN A 187    18756  14455  20378  -3213   -781    150  A    O  
ATOM   1358  N   ARG A 188      34.627 -26.214  -2.353  1.00139.97      A    N  
ANISOU 1358  N   ARG A 188    18015  14905  20263  -2541  -1138   -444  A    N  
ATOM   1359  CA  ARG A 188      35.714 -26.916  -3.036  1.00142.17      A    C  
ANISOU 1359  CA  ARG A 188    18405  15060  20554  -2310  -1341   -455  A    C  
ATOM   1360  C   ARG A 188      36.954 -26.049  -3.302  1.00130.91      A    C  
ANISOU 1360  C   ARG A 188    16996  13826  18919  -2017  -1432   -351  A    C  
ATOM   1361  O   ARG A 188      37.560 -26.143  -4.372  1.00127.80      A    O  
ANISOU 1361  O   ARG A 188    16538  13498  18521  -1760  -1593   -465  A    O  
ATOM   1362  CB  ARG A 188      35.192 -27.494  -4.360  1.00152.58      A    C  
ANISOU 1362  CB  ARG A 188    19550  16376  22050  -2225  -1468   -755  A    C  
ATOM   1363  CG  ARG A 188      33.860 -28.239  -4.226  1.00163.64      A    C  
ANISOU 1363  CG  ARG A 188    20877  17625  23674  -2525  -1377   -903  A    C  
ATOM   1364  CD  ARG A 188      33.333 -28.769  -5.564  1.00165.27      A    C  
ANISOU 1364  CD  ARG A 188    20894  17850  24053  -2435  -1517  -1228  A    C  
ATOM   1365  NE  ARG A 188      32.488 -29.954  -5.390  1.00162.10      A    N  
ANISOU 1365  NE  ARG A 188    20522  17170  23899  -2713  -1484  -1336  A    N  
ATOM   1366  CZ  ARG A 188      31.838 -30.570  -6.375  1.00156.34      A    C  
ANISOU 1366  CZ  ARG A 188    19635  16410  23358  -2716  -1586  -1633  A    C  
ATOM   1367  NH1 ARG A 188      31.922 -30.114  -7.617  1.00151.07      A    N1+
ANISOU 1367  NH1 ARG A 188    18769  15986  22644  -2439  -1730  -1850  A    N1+
ATOM   1368  NH2 ARG A 188      31.099 -31.642  -6.118  1.00157.15      A    N  
ANISOU 1368  NH2 ARG A 188    19778  16238  23695  -3000  -1543  -1716  A    N  
ATOM   1369  N   VAL A 189      37.345 -25.216  -2.339  1.00121.56      A    N  
ANISOU 1369  N   VAL A 189    15893  12733  17560  -2056  -1330   -140  A    N  
ATOM   1370  CA  VAL A 189      38.470 -24.304  -2.564  1.00126.29      A    C  
ANISOU 1370  CA  VAL A 189    16487  13526  17971  -1806  -1402    -48  A    C  
ATOM   1371  C   VAL A 189      39.719 -24.597  -1.733  1.00128.56      A    C  
ANISOU 1371  C   VAL A 189    17018  13689  18139  -1758  -1453    192  A    C  
ATOM   1372  O   VAL A 189      39.652 -25.242  -0.684  1.00131.19      A    O  
ANISOU 1372  O   VAL A 189    17545  13815  18486  -1944  -1388    340  A    O  
ATOM   1373  CB  VAL A 189      38.078 -22.813  -2.373  1.00102.40      A    C  
ANISOU 1373  CB  VAL A 189    13315  10775  14816  -1814  -1274    -35  A    C  
ATOM   1374  CG1 VAL A 189      37.431 -22.256  -3.639  1.00104.78      A    C  
ANISOU 1374  CG1 VAL A 189    13357  11288  15168  -1677  -1306   -271  A    C  
ATOM   1375  CG2 VAL A 189      37.185 -22.631  -1.150  1.00 92.20      A    C  
ANISOU 1375  CG2 VAL A 189    12071   9439  13521  -2107  -1078     56  A    C  
ATOM   1376  N   VAL A 190      40.853 -24.098  -2.223  1.00119.03      A    N  
ANISOU 1376  N   VAL A 190    15792  12623  16809  -1501  -1566    229  A    N  
ATOM   1377  CA  VAL A 190      42.152 -24.248  -1.567  1.00109.20      A    C  
ANISOU 1377  CA  VAL A 190    14737  11317  15436  -1410  -1637    436  A    C  
ATOM   1378  C   VAL A 190      42.770 -25.639  -1.732  1.00108.49      A    C  
ANISOU 1378  C   VAL A 190    14812  10975  15435  -1326  -1783    449  A    C  
ATOM   1379  O   VAL A 190      42.168 -26.647  -1.344  1.00 93.85      A    O  
ANISOU 1379  O   VAL A 190    13078   8869  13713  -1499  -1754    447  A    O  
ATOM   1380  CB  VAL A 190      42.095 -23.926  -0.057  1.00 97.67      A    C  
ANISOU 1380  CB  VAL A 190    13432   9812  13864  -1618  -1501    650  A    C  
ATOM   1381  CG1 VAL A 190      43.504 -23.695   0.477  1.00 94.98      A    C  
ANISOU 1381  CG1 VAL A 190    13224   9510  13353  -1477  -1584    836  A    C  
ATOM   1382  CG2 VAL A 190      41.212 -22.725   0.205  1.00 89.02      A    C  
ANISOU 1382  CG2 VAL A 190    12192   8916  12716  -1746  -1335    615  A    C  
ATOM   1383  N   THR A 191      43.975 -25.671  -2.306  1.00111.17      A    N  
ANISOU 1383  N   THR A 191    15154  11383  15702  -1059  -1935    462  A    N  
ATOM   1384  CA  THR A 191      44.834 -26.850  -2.306  1.00103.50      A    C  
ANISOU 1384  CA  THR A 191    14360  10196  14767   -935  -2083    513  A    C  
ATOM   1385  C   THR A 191      44.667 -27.600  -0.992  1.00103.62      A    C  
ANISOU 1385  C   THR A 191    14629   9945  14798  -1148  -2018    696  A    C  
ATOM   1386  O   THR A 191      44.632 -26.994   0.080  1.00103.50      A    O  
ANISOU 1386  O   THR A 191    14682   9984  14661  -1290  -1903    863  A    O  
ATOM   1387  CB  THR A 191      46.311 -26.433  -2.413  1.00111.87      A    C  
ANISOU 1387  CB  THR A 191    15428  11412  15665   -680  -2197    616  A    C  
ATOM   1388  CG2 THR A 191      47.224 -27.646  -2.541  1.00115.71      A    C  
ANISOU 1388  CG2 THR A 191    16076  11699  16189   -508  -2364    645  A    C  
ATOM   1389  OG1 THR A 191      46.487 -25.570  -3.540  1.00116.60      A    O  
ANISOU 1389  OG1 THR A 191    15795  12284  16223   -498  -2227    481  A    O  
ATOM   1390  N   LEU A 192      44.575 -28.920  -1.063  1.00105.95      A    N  
ANISOU 1390  N   LEU A 192    15073   9947  15237  -1166  -2090    668  A    N  
ATOM   1391  CA  LEU A 192      44.370 -29.713   0.143  1.00108.60      A    C  
ANISOU 1391  CA  LEU A 192    15667  10003  15596  -1371  -2021    852  A    C  
ATOM   1392  C   LEU A 192      45.347 -29.368   1.291  1.00109.73      A    C  
ANISOU 1392  C   LEU A 192    15977  10188  15526  -1333  -2019   1115  A    C  
ATOM   1393  O   LEU A 192      44.913 -29.011   2.388  1.00107.79      A    O  
ANISOU 1393  O   LEU A 192    15815   9940  15200  -1545  -1872   1263  A    O  
ATOM   1394  CB  LEU A 192      44.399 -31.208  -0.189  1.00105.89      A    C  
ANISOU 1394  CB  LEU A 192    15482   9321  15430  -1338  -2132    793  A    C  
ATOM   1395  CG  LEU A 192      44.081 -32.199   0.933  1.00102.32      A    C  
ANISOU 1395  CG  LEU A 192    15314   8525  15037  -1557  -2058    973  A    C  
ATOM   1396  CD1 LEU A 192      42.765 -31.838   1.617  1.00 98.52      A    C  
ANISOU 1396  CD1 LEU A 192    14790   8044  14598  -1903  -1834    998  A    C  
ATOM   1397  CD2 LEU A 192      44.051 -33.622   0.391  1.00 96.29      A    C  
ANISOU 1397  CD2 LEU A 192    14682   7423  14479  -1511  -2176    872  A    C  
ATOM   1398  N   TRP A 193      46.654 -29.453   1.047  1.00109.10      A    N  
ANISOU 1398  N   TRP A 193    15937  10167  15350  -1062  -2182   1164  A    N  
ATOM   1399  CA  TRP A 193      47.627 -29.276   2.134  1.00111.49      A    C  
ANISOU 1399  CA  TRP A 193    16406  10495  15460  -1013  -2207   1402  A    C  
ATOM   1400  C   TRP A 193      47.525 -27.940   2.872  1.00101.13      A    C  
ANISOU 1400  C   TRP A 193    15010   9436  13977  -1131  -2076   1495  A    C  
ATOM   1401  O   TRP A 193      48.100 -27.781   3.948  1.00 86.80      A    O  
ANISOU 1401  O   TRP A 193    13344   7633  12003  -1151  -2068   1690  A    O  
ATOM   1402  CB  TRP A 193      49.063 -29.465   1.646  1.00111.81      A    C  
ANISOU 1402  CB  TRP A 193    16448  10611  15424   -687  -2407   1411  A    C  
ATOM   1403  CG  TRP A 193      49.329 -30.779   1.014  1.00116.80      A    C  
ANISOU 1403  CG  TRP A 193    17187  10993  16200   -534  -2551   1332  A    C  
ATOM   1404  CD1 TRP A 193      48.599 -31.922   1.147  1.00119.93      A    C  
ANISOU 1404  CD1 TRP A 193    17752  11051  16765   -672  -2530   1317  A    C  
ATOM   1405  CD2 TRP A 193      50.420 -31.097   0.147  1.00124.80      A    C  
ANISOU 1405  CD2 TRP A 193    18148  12070  17202   -211  -2739   1252  A    C  
ATOM   1406  CE2 TRP A 193      50.286 -32.447  -0.216  1.00117.99      A    C  
ANISOU 1406  CE2 TRP A 193    17436  10892  16505   -155  -2832   1181  A    C  
ATOM   1407  CE3 TRP A 193      51.499 -30.365  -0.363  1.00132.06      A    C  
ANISOU 1407  CE3 TRP A 193    18904  13284  17990     33  -2832   1231  A    C  
ATOM   1408  NE1 TRP A 193      49.165 -32.931   0.406  1.00120.30      A    N  
ANISOU 1408  NE1 TRP A 193    17864  10932  16911   -448  -2701   1224  A    N  
ATOM   1409  CZ2 TRP A 193      51.184 -33.080  -1.064  1.00116.15      A    C  
ANISOU 1409  CZ2 TRP A 193    17195  10636  16300    151  -3018   1082  A    C  
ATOM   1410  CZ3 TRP A 193      52.391 -30.999  -1.208  1.00125.68      A    C  
ANISOU 1410  CZ3 TRP A 193    18077  12466  17209    330  -3008   1140  A    C  
ATOM   1411  CH2 TRP A 193      52.226 -32.340  -1.551  1.00116.97      A    C  
ANISOU 1411  CH2 TRP A 193    17127  11053  16263    395  -3102   1063  A    C  
ATOM   1412  N   TYR A 194      46.810 -26.984   2.287  1.00 99.09      A    N  
ANISOU 1412  N   TYR A 194    14521   9382  13748  -1195  -1981   1349  A    N  
ATOM   1413  CA  TYR A 194      46.665 -25.672   2.896  1.00 97.16      A    C  
ANISOU 1413  CA  TYR A 194    14190   9371  13356  -1297  -1857   1412  A    C  
ATOM   1414  C   TYR A 194      45.221 -25.346   3.242  1.00105.88      A    C  
ANISOU 1414  C   TYR A 194    15241  10462  14526  -1572  -1661   1364  A    C  
ATOM   1415  O   TYR A 194      44.931 -24.249   3.726  1.00107.28      A    O  
ANISOU 1415  O   TYR A 194    15342  10824  14595  -1667  -1542   1393  A    O  
ATOM   1416  CB  TYR A 194      47.183 -24.596   1.964  1.00 89.86      A    C  
ANISOU 1416  CB  TYR A 194    13031   8735  12376  -1113  -1908   1301  A    C  
ATOM   1417  CG  TYR A 194      48.642 -24.705   1.621  1.00 93.14      A    C  
ANISOU 1417  CG  TYR A 194    13455   9227  12709   -845  -2083   1345  A    C  
ATOM   1418  CD1 TYR A 194      49.602 -24.051   2.381  1.00 94.06      A    C  
ANISOU 1418  CD1 TYR A 194    13612   9482  12645   -800  -2107   1492  A    C  
ATOM   1419  CD2 TYR A 194      49.060 -25.431   0.512  1.00 95.55      A    C  
ANISOU 1419  CD2 TYR A 194    13709   9483  13114   -634  -2226   1223  A    C  
ATOM   1420  CE1 TYR A 194      50.941 -24.128   2.054  1.00103.49      A    C  
ANISOU 1420  CE1 TYR A 194    14786  10769  13767   -558  -2265   1522  A    C  
ATOM   1421  CE2 TYR A 194      50.392 -25.520   0.179  1.00 98.18      A    C  
ANISOU 1421  CE2 TYR A 194    14031   9907  13368   -381  -2379   1255  A    C  
ATOM   1422  CZ  TYR A 194      51.331 -24.867   0.950  1.00108.75      A    C  
ANISOU 1422  CZ  TYR A 194    15398  11389  14534   -347  -2396   1407  A    C  
ATOM   1423  OH  TYR A 194      52.666 -24.954   0.615  1.00115.88      A    O  
ANISOU 1423  OH  TYR A 194    16266  12399  15362    -98  -2548   1431  A    O  
ATOM   1424  N   ARG A 195      44.311 -26.279   2.977  1.00107.91      A    N  
ANISOU 1424  N   ARG A 195    15529  10507  14965  -1697  -1625   1278  A    N  
ATOM   1425  CA  ARG A 195      42.909 -26.047   3.296  1.00102.06      A    C  
ANISOU 1425  CA  ARG A 195    14719   9758  14299  -1965  -1435   1222  A    C  
ATOM   1426  C   ARG A 195      42.757 -26.058   4.795  1.00101.36      A    C  
ANISOU 1426  C   ARG A 195    14830   9592  14091  -2166  -1304   1441  A    C  
ATOM   1427  O   ARG A 195      43.395 -26.857   5.475  1.00108.59      A    O  
ANISOU 1427  O   ARG A 195    15981  10320  14956  -2147  -1362   1611  A    O  
ATOM   1428  CB  ARG A 195      41.992 -27.101   2.676  1.00 98.88      A    C  
ANISOU 1428  CB  ARG A 195    14298   9140  14134  -2068  -1432   1072  A    C  
ATOM   1429  CG  ARG A 195      40.630 -26.543   2.276  1.00103.78      A    C  
ANISOU 1429  CG  ARG A 195    14692   9884  14855  -2233  -1292    893  A    C  
ATOM   1430  CD  ARG A 195      39.561 -27.613   2.129  1.00113.80      A    C  
ANISOU 1430  CD  ARG A 195    15978  10915  16348  -2437  -1236    791  A    C  
ATOM   1431  NE  ARG A 195      40.033 -28.799   1.421  1.00123.47      A    N  
ANISOU 1431  NE  ARG A 195    17291  11911  17711  -2309  -1406    719  A    N  
ATOM   1432  CZ  ARG A 195      40.150 -28.886   0.102  1.00123.89      A    C  
ANISOU 1432  CZ  ARG A 195    17181  12033  17857  -2115  -1545    501  A    C  
ATOM   1433  NH1 ARG A 195      39.838 -27.850  -0.657  1.00117.56      A    N1+
ANISOU 1433  NH1 ARG A 195    16124  11522  17019  -2024  -1533    347  A    N1+
ATOM   1434  NH2 ARG A 195      40.588 -30.007  -0.454  1.00129.36      A    N  
ANISOU 1434  NH2 ARG A 195    17977  12504  18670  -2000  -1697    438  A    N  
ATOM   1435  N   PRO A 196      41.928 -25.150   5.317  1.00 98.38      A    N  
ANISOU 1435  N   PRO A 196    14360   9366  13653  -2341  -1127   1436  A    N  
ATOM   1436  CA  PRO A 196      41.644 -25.047   6.750  1.00105.73      A    C  
ANISOU 1436  CA  PRO A 196    15459  10260  14455  -2543   -976   1627  A    C  
ATOM   1437  C   PRO A 196      40.717 -26.168   7.188  1.00118.48      A    C  
ANISOU 1437  C   PRO A 196    17204  11606  16209  -2781   -865   1670  A    C  
ATOM   1438  O   PRO A 196      40.123 -26.828   6.328  1.00114.24      A    O  
ANISOU 1438  O   PRO A 196    16577  10946  15882  -2814   -889   1512  A    O  
ATOM   1439  CB  PRO A 196      40.903 -23.709   6.870  1.00 98.22      A    C  
ANISOU 1439  CB  PRO A 196    14315   9569  13436  -2635   -826   1544  A    C  
ATOM   1440  CG  PRO A 196      41.096 -23.018   5.576  1.00 92.50      A    C  
ANISOU 1440  CG  PRO A 196    13352   9027  12766  -2439   -923   1352  A    C  
ATOM   1441  CD  PRO A 196      41.291 -24.074   4.548  1.00 92.05      A    C  
ANISOU 1441  CD  PRO A 196    13286   8808  12882  -2323  -1069   1249  A    C  
ATOM   1442  N   PRO A 197      40.589 -26.378   8.510  1.00125.44      A    N  
ANISOU 1442  N   PRO A 197    18293  12399  16970  -2950   -743   1879  A    N  
ATOM   1443  CA  PRO A 197      39.629 -27.346   9.052  1.00119.54      A    C  
ANISOU 1443  CA  PRO A 197    17670  11407  16341  -3214   -596   1945  A    C  
ATOM   1444  C   PRO A 197      38.231 -26.944   8.627  1.00120.24      A    C  
ANISOU 1444  C   PRO A 197    17513  11597  16574  -3405   -436   1751  A    C  
ATOM   1445  O   PRO A 197      37.547 -27.692   7.940  1.00128.13      A    O  
ANISOU 1445  O   PRO A 197    18440  12444  17800  -3495   -435   1614  A    O  
ATOM   1446  CB  PRO A 197      39.772 -27.171  10.565  1.00116.64      A    C  
ANISOU 1446  CB  PRO A 197    17519  11049  15751  -3330   -473   2196  A    C  
ATOM   1447  CG  PRO A 197      41.123 -26.569  10.757  1.00122.52      A    C  
ANISOU 1447  CG  PRO A 197    18322  11944  16287  -3080   -630   2282  A    C  
ATOM   1448  CD  PRO A 197      41.334 -25.682   9.573  1.00122.71      A    C  
ANISOU 1448  CD  PRO A 197    18070  12191  16364  -2904   -731   2062  A    C  
ATOM   1449  N   GLU A 198      37.830 -25.750   9.040  1.00117.31      A    N  
ANISOU 1449  N   GLU A 198    17014  11488  16071  -3458   -309   1732  A    N  
ATOM   1450  CA  GLU A 198      36.555 -25.147   8.666  1.00113.81      A    C  
ANISOU 1450  CA  GLU A 198    16313  11201  15730  -3602   -161   1543  A    C  
ATOM   1451  C   GLU A 198      36.003 -25.650   7.339  1.00113.29      A    C  
ANISOU 1451  C   GLU A 198    16055  11071  15919  -3579   -238   1303  A    C  
ATOM   1452  O   GLU A 198      34.841 -26.055   7.247  1.00112.16      A    O  
ANISOU 1452  O   GLU A 198    15811  10864  15940  -3794   -112   1201  A    O  
ATOM   1453  CB  GLU A 198      36.747 -23.639   8.590  1.00107.22      A    C  
ANISOU 1453  CB  GLU A 198    15316  10685  14738  -3471   -153   1477  A    C  
ATOM   1454  CG  GLU A 198      38.099 -23.224   9.120  1.00113.12      A    C  
ANISOU 1454  CG  GLU A 198    16225  11490  15267  -3292   -267   1643  A    C  
ATOM   1455  CD  GLU A 198      38.498 -21.851   8.658  1.00126.88      A    C  
ANISOU 1455  CD  GLU A 198    17793  13508  16908  -3116   -318   1542  A    C  
ATOM   1456  OE1 GLU A 198      37.610 -21.076   8.239  1.00122.12      A    O  
ANISOU 1456  OE1 GLU A 198    16974  13069  16358  -3159   -220   1382  A    O  
ATOM   1457  OE2 GLU A 198      39.707 -21.545   8.717  1.00141.02      A    O1-
ANISOU 1457  OE2 GLU A 198    19662  15350  18568  -2932   -456   1625  A    O1-
ATOM   1458  N   LEU A 199      36.843 -25.612   6.310  1.00109.28      A    N  
ANISOU 1458  N   LEU A 199    15488  10596  15439  -3316   -445   1205  A    N  
ATOM   1459  CA  LEU A 199      36.431 -26.013   4.972  1.00103.90      A    C  
ANISOU 1459  CA  LEU A 199    14620   9886  14970  -3249   -544    962  A    C  
ATOM   1460  C   LEU A 199      36.183 -27.512   4.860  1.00100.08      A    C  
ANISOU 1460  C   LEU A 199    14269   9069  14688  -3372   -576    958  A    C  
ATOM   1461  O   LEU A 199      35.179 -27.945   4.303  1.00102.14      A    O  
ANISOU 1461  O   LEU A 199    14385   9271  15151  -3511   -531    777  A    O  
ATOM   1462  CB  LEU A 199      37.477 -25.581   3.949  1.00100.12      A    C  
ANISOU 1462  CB  LEU A 199    14061   9538  14443  -2923   -751    878  A    C  
ATOM   1463  CG  LEU A 199      37.432 -24.100   3.593  1.00 99.84      A    C  
ANISOU 1463  CG  LEU A 199    13814   9831  14289  -2803   -724    791  A    C  
ATOM   1464  CD1 LEU A 199      38.398 -23.806   2.446  1.00106.93      A    C  
ANISOU 1464  CD1 LEU A 199    14622  10840  15166  -2494   -921    699  A    C  
ATOM   1465  CD2 LEU A 199      36.016 -23.706   3.226  1.00 93.46      A    C  
ANISOU 1465  CD2 LEU A 199    12768   9144  13596  -2948   -591    599  A    C  
ATOM   1466  N   LEU A 200      37.111 -28.297   5.387  1.00 95.86      A    N  
ANISOU 1466  N   LEU A 200    14010   8314  14098  -3316   -659   1153  A    N  
ATOM   1467  CA  LEU A 200      37.003 -29.745   5.348  1.00 98.85      A    C  
ANISOU 1467  CA  LEU A 200    14561   8339  14659  -3416   -698   1177  A    C  
ATOM   1468  C   LEU A 200      35.725 -30.244   6.005  1.00107.11      A    C  
ANISOU 1468  C   LEU A 200    15626   9240  15831  -3775   -479   1202  A    C  
ATOM   1469  O   LEU A 200      35.236 -31.313   5.656  1.00104.33      A    O  
ANISOU 1469  O   LEU A 200    15309   8629  15701  -3904   -488   1122  A    O  
ATOM   1470  CB  LEU A 200      38.215 -30.377   6.018  1.00100.31      A    C  
ANISOU 1470  CB  LEU A 200    15062   8330  14722  -3292   -802   1423  A    C  
ATOM   1471  CG  LEU A 200      39.542 -29.996   5.369  1.00 99.31      A    C  
ANISOU 1471  CG  LEU A 200    14914   8336  14482  -2938  -1022   1400  A    C  
ATOM   1472  CD1 LEU A 200      40.719 -30.427   6.231  1.00108.22      A    C  
ANISOU 1472  CD1 LEU A 200    16337   9334  15447  -2820  -1105   1659  A    C  
ATOM   1473  CD2 LEU A 200      39.644 -30.587   3.971  1.00 95.12      A    C  
ANISOU 1473  CD2 LEU A 200    14269   7728  14145  -2776  -1194   1166  A    C  
ATOM   1474  N   LEU A 201      35.191 -29.474   6.954  1.00117.94      A    N  
ANISOU 1474  N   LEU A 201    16972  10778  17063  -3939   -281   1307  A    N  
ATOM   1475  CA  LEU A 201      33.921 -29.819   7.600  1.00126.95      A    C  
ANISOU 1475  CA  LEU A 201    18096  11833  18308  -4288    -47   1327  A    C  
ATOM   1476  C   LEU A 201      32.715 -29.255   6.845  1.00129.21      A    C  
ANISOU 1476  C   LEU A 201    18030  12327  18737  -4387     34   1047  A    C  
ATOM   1477  O   LEU A 201      31.647 -29.068   7.429  1.00134.48      A    O  
ANISOU 1477  O   LEU A 201    18609  13059  19430  -4646    251   1047  A    O  
ATOM   1478  CB  LEU A 201      33.879 -29.355   9.063  1.00120.55      A    C  
ANISOU 1478  CB  LEU A 201    17439  11095  17269  -4425    143   1581  A    C  
ATOM   1479  CG  LEU A 201      34.975 -29.810  10.030  1.00113.27      A    C  
ANISOU 1479  CG  LEU A 201    16870  10007  16161  -4345     92   1882  A    C  
ATOM   1480  CD1 LEU A 201      34.456 -29.816  11.456  1.00113.80      A    C  
ANISOU 1480  CD1 LEU A 201    17096  10052  16091  -4596    334   2110  A    C  
ATOM   1481  CD2 LEU A 201      35.493 -31.174   9.666  1.00107.61      A    C  
ANISOU 1481  CD2 LEU A 201    16357   8929  15599  -4295    -53   1927  A    C  
ATOM   1482  N   GLY A 202      32.898 -28.980   5.555  1.00119.22      A    N  
ANISOU 1482  N   GLY A 202    16563  11180  17554  -4170   -140    812  A    N  
ATOM   1483  CA  GLY A 202      31.805 -28.595   4.677  1.00114.74      A    C  
ANISOU 1483  CA  GLY A 202    15666  10790  17141  -4227   -104    525  A    C  
ATOM   1484  C   GLY A 202      31.237 -27.207   4.914  1.00112.84      A    C  
ANISOU 1484  C   GLY A 202    15215  10900  16759  -4230     30    476  A    C  
ATOM   1485  O   GLY A 202      30.084 -26.932   4.576  1.00110.89      A    O  
ANISOU 1485  O   GLY A 202    14715  10791  16628  -4359    130    284  A    O  
ATOM   1486  N   GLU A 203      32.045 -26.319   5.482  1.00109.63      A    N  
ANISOU 1486  N   GLU A 203    14906  10642  16107  -4080     25    638  A    N  
ATOM   1487  CA  GLU A 203      31.595 -24.956   5.724  1.00107.99      A    C  
ANISOU 1487  CA  GLU A 203    14522  10752  15758  -4061    142    595  A    C  
ATOM   1488  C   GLU A 203      31.428 -24.141   4.430  1.00107.23      A    C  
ANISOU 1488  C   GLU A 203    14142  10897  15705  -3842     30    341  A    C  
ATOM   1489  O   GLU A 203      32.298 -24.143   3.561  1.00 98.35      A    O  
ANISOU 1489  O   GLU A 203    13021   9774  14574  -3592   -167    290  A    O  
ATOM   1490  CB  GLU A 203      32.536 -24.249   6.694  1.00102.55      A    C  
ANISOU 1490  CB  GLU A 203    14023  10139  14800  -3967    160    828  A    C  
ATOM   1491  CG  GLU A 203      32.192 -22.789   6.911  1.00107.22      A    C  
ANISOU 1491  CG  GLU A 203    14454  11045  15241  -3917    261    778  A    C  
ATOM   1492  CD  GLU A 203      30.880 -22.601   7.639  1.00119.23      A    C  
ANISOU 1492  CD  GLU A 203    15874  12645  16783  -4185    508    754  A    C  
ATOM   1493  OE1 GLU A 203      30.888 -22.651   8.887  1.00121.62      A    O  
ANISOU 1493  OE1 GLU A 203    16356  12905  16950  -4337    652    954  A    O  
ATOM   1494  OE2 GLU A 203      29.843 -22.399   6.969  1.00125.34      A    O1-
ANISOU 1494  OE2 GLU A 203    16385  13539  17700  -4236    559    534  A    O1-
ATOM   1495  N   ARG A 204      30.297 -23.452   4.310  1.00112.41      A    N  
ANISOU 1495  N   ARG A 204    14553  11762  16397  -3932    161    186  A    N  
ATOM   1496  CA  ARG A 204      30.015 -22.628   3.141  1.00113.74      A    C  
ANISOU 1496  CA  ARG A 204    14452  12173  16593  -3727     73    -48  A    C  
ATOM   1497  C   ARG A 204      29.826 -21.159   3.524  1.00112.11      A    C  
ANISOU 1497  C   ARG A 204    14146  12246  16205  -3653    179    -33  A    C  
ATOM   1498  O   ARG A 204      29.577 -20.311   2.672  1.00114.62      A    O  
ANISOU 1498  O   ARG A 204    14255  12780  16515  -3476    128   -200  A    O  
ATOM   1499  CB  ARG A 204      28.777 -23.146   2.395  1.00116.16      A    C  
ANISOU 1499  CB  ARG A 204    14513  12489  17133  -3856     95   -305  A    C  
ATOM   1500  CG  ARG A 204      28.975 -24.477   1.689  1.00120.70      A    C  
ANISOU 1500  CG  ARG A 204    15143  12811  17908  -3871    -53   -389  A    C  
ATOM   1501  CD  ARG A 204      27.723 -24.914   0.930  1.00131.90      A    C  
ANISOU 1501  CD  ARG A 204    16295  14263  19559  -4001    -38   -671  A    C  
ATOM   1502  NE  ARG A 204      27.357 -23.990  -0.145  1.00135.98      A    N  
ANISOU 1502  NE  ARG A 204    16530  15077  20058  -3779   -119   -903  A    N  
ATOM   1503  CZ  ARG A 204      27.800 -24.079  -1.397  1.00136.37      A    C  
ANISOU 1503  CZ  ARG A 204    16501  15165  20147  -3525   -329  -1062  A    C  
ATOM   1504  NH1 ARG A 204      28.639 -25.053  -1.740  1.00137.34      A    N1+
ANISOU 1504  NH1 ARG A 204    16800  15048  20334  -3457   -483  -1027  A    N1+
ATOM   1505  NH2 ARG A 204      27.408 -23.192  -2.308  1.00128.45      A    N  
ANISOU 1505  NH2 ARG A 204    15250  14445  19110  -3325   -384  -1255  A    N  
ATOM   1506  N   ASP A 205      29.929 -20.865   4.812  1.00108.23      A    N  
ANISOU 1506  N   ASP A 205    13813  11747  15562  -3784    328    166  A    N  
ATOM   1507  CA  ASP A 205      29.875 -19.487   5.281  1.00115.38      A    C  
ANISOU 1507  CA  ASP A 205    14665  12891  16282  -3710    422    194  A    C  
ATOM   1508  C   ASP A 205      31.161 -19.144   6.023  1.00113.38      A    C  
ANISOU 1508  C   ASP A 205    14664  12596  15820  -3610    371    423  A    C  
ATOM   1509  O   ASP A 205      31.191 -19.083   7.254  1.00120.39      A    O  
ANISOU 1509  O   ASP A 205    15710  13455  16577  -3754    503    593  A    O  
ATOM   1510  CB  ASP A 205      28.669 -19.263   6.193  1.00126.03      A    C  
ANISOU 1510  CB  ASP A 205    15934  14329  17624  -3957    667    186  A    C  
ATOM   1511  CG  ASP A 205      28.695 -17.903   6.866  1.00130.06      A    C  
ANISOU 1511  CG  ASP A 205    16439  15053  17924  -3888    770    238  A    C  
ATOM   1512  OD1 ASP A 205      28.911 -16.895   6.156  1.00137.72      A    O  
ANISOU 1512  OD1 ASP A 205    17288  16195  18844  -3659    686    134  A    O  
ATOM   1513  OD2 ASP A 205      28.511 -17.845   8.101  1.00122.04      A    O1-
ANISOU 1513  OD2 ASP A 205    15549  14029  16790  -4058    937    383  A    O1-
ATOM   1514  N   TYR A 206      32.228 -18.935   5.265  1.00 98.74      A    N  
ANISOU 1514  N   TYR A 206    12840  10748  13929  -3362    179    423  A    N  
ATOM   1515  CA  TYR A 206      33.523 -18.624   5.847  1.00 93.01      A    C  
ANISOU 1515  CA  TYR A 206    12325   9995  13019  -3251    106    618  A    C  
ATOM   1516  C   TYR A 206      33.985 -17.236   5.416  1.00 92.75      A    C  
ANISOU 1516  C   TYR A 206    12193  10181  12866  -3033     56    568  A    C  
ATOM   1517  O   TYR A 206      33.239 -16.482   4.778  1.00 93.94      A    O  
ANISOU 1517  O   TYR A 206    12130  10503  13061  -2972     96    400  A    O  
ATOM   1518  CB  TYR A 206      34.547 -19.660   5.412  1.00 91.83      A    C  
ANISOU 1518  CB  TYR A 206    12321   9645  12926  -3150    -80    687  A    C  
ATOM   1519  CG  TYR A 206      34.543 -19.875   3.919  1.00 97.02      A    C  
ANISOU 1519  CG  TYR A 206    12805  10325  13734  -2976   -231    492  A    C  
ATOM   1520  CD1 TYR A 206      34.109 -21.078   3.363  1.00 97.53      A    C  
ANISOU 1520  CD1 TYR A 206    12847  10215  13997  -3050   -282    393  A    C  
ATOM   1521  CD2 TYR A 206      34.946 -18.866   3.061  1.00 90.33      A    C  
ANISOU 1521  CD2 TYR A 206    11819   9673  12828  -2739   -319    400  A    C  
ATOM   1522  CE1 TYR A 206      34.098 -21.271   1.992  1.00 88.67      A    C  
ANISOU 1522  CE1 TYR A 206    11564   9127  12999  -2880   -427    199  A    C  
ATOM   1523  CE2 TYR A 206      34.931 -19.045   1.695  1.00 90.02      A    C  
ANISOU 1523  CE2 TYR A 206    11625   9674  12904  -2568   -452    225  A    C  
ATOM   1524  CZ  TYR A 206      34.509 -20.245   1.164  1.00 88.56      A    C  
ANISOU 1524  CZ  TYR A 206    11416   9330  12904  -2633   -510    118  A    C  
ATOM   1525  OH  TYR A 206      34.512 -20.402  -0.202  1.00 83.60      A    O  
ANISOU 1525  OH  TYR A 206    10633   8756  12374  -2447   -651    -69  A    O  
ATOM   1526  N   GLY A 207      35.222 -16.908   5.770  1.00 87.24      A    N  
ANISOU 1526  N   GLY A 207    11652   9476  12019  -2916    -34    715  A    N  
ATOM   1527  CA  GLY A 207      35.800 -15.622   5.432  1.00 74.29      A    C  
ANISOU 1527  CA  GLY A 207     9946   8014  10266  -2726    -81    692  A    C  
ATOM   1528  C   GLY A 207      37.310 -15.610   5.569  1.00 75.51      A    C  
ANISOU 1528  C   GLY A 207    10259   8124  10306  -2589   -227    838  A    C  
ATOM   1529  O   GLY A 207      37.975 -16.645   5.480  1.00 72.90      A    O  
ANISOU 1529  O   GLY A 207    10045   7636  10015  -2565   -341    913  A    O  
ATOM   1530  N   PRO A 208      37.870 -14.422   5.795  1.00 78.87      A    N  
ANISOU 1530  N   PRO A 208    10686   8689  10593  -2497   -225    872  A    N  
ATOM   1531  CA  PRO A 208      39.322 -14.238   5.859  1.00 73.81      A    C  
ANISOU 1531  CA  PRO A 208    10155   8044   9844  -2361   -364    989  A    C  
ATOM   1532  C   PRO A 208      40.081 -15.327   6.596  1.00 79.90      A    C  
ANISOU 1532  C   PRO A 208    11139   8649  10570  -2415   -437   1153  A    C  
ATOM   1533  O   PRO A 208      41.124 -15.739   6.106  1.00 86.00      A    O  
ANISOU 1533  O   PRO A 208    11950   9376  11349  -2268   -596   1194  A    O  
ATOM   1534  CB  PRO A 208      39.450 -12.908   6.566  1.00 68.97      A    C  
ANISOU 1534  CB  PRO A 208     9556   7570   9079  -2374   -280   1019  A    C  
ATOM   1535  CG  PRO A 208      38.265 -12.139   5.990  1.00 69.80      A    C  
ANISOU 1535  CG  PRO A 208     9467   7797   9259  -2369   -168    852  A    C  
ATOM   1536  CD  PRO A 208      37.154 -13.137   5.870  1.00 72.77      A    C  
ANISOU 1536  CD  PRO A 208     9789   8090   9772  -2500   -100    781  A    C  
ATOM   1537  N   PRO A 209      39.565 -15.815   7.730  1.00 83.79      A    N  
ANISOU 1537  N   PRO A 209    11768   9053  11016  -2612   -321   1247  A    N  
ATOM   1538  CA  PRO A 209      40.447 -16.703   8.493  1.00 89.22      A    C  
ANISOU 1538  CA  PRO A 209    12682   9595  11623  -2631   -401   1427  A    C  
ATOM   1539  C   PRO A 209      40.920 -17.932   7.719  1.00 89.21      A    C  
ANISOU 1539  C   PRO A 209    12716   9425  11754  -2536   -553   1429  A    C  
ATOM   1540  O   PRO A 209      41.825 -18.616   8.198  1.00 94.29      A    O  
ANISOU 1540  O   PRO A 209    13540   9957  12331  -2496   -652   1573  A    O  
ATOM   1541  CB  PRO A 209      39.592 -17.098   9.698  1.00 83.92      A    C  
ANISOU 1541  CB  PRO A 209    12136   8851  10900  -2867   -228   1516  A    C  
ATOM   1542  CG  PRO A 209      38.627 -15.984   9.847  1.00 81.35      A    C  
ANISOU 1542  CG  PRO A 209    11665   8697  10547  -2943    -65   1406  A    C  
ATOM   1543  CD  PRO A 209      38.308 -15.545   8.444  1.00 77.16      A    C  
ANISOU 1543  CD  PRO A 209    10900   8253  10165  -2810   -117   1215  A    C  
ATOM   1544  N   ILE A 210      40.345 -18.202   6.549  1.00 82.42      A    N  
ANISOU 1544  N   ILE A 210    11691   8554  11072  -2487   -578   1267  A    N  
ATOM   1545  CA  ILE A 210      40.819 -19.327   5.743  1.00 81.85      A    C  
ANISOU 1545  CA  ILE A 210    11646   8328  11126  -2377   -732   1244  A    C  
ATOM   1546  C   ILE A 210      42.153 -19.006   5.078  1.00 85.54      A    C  
ANISOU 1546  C   ILE A 210    12087   8879  11535  -2126   -909   1254  A    C  
ATOM   1547  O   ILE A 210      42.989 -19.897   4.849  1.00 85.10      A    O  
ANISOU 1547  O   ILE A 210    12131   8700  11504  -2015  -1054   1309  A    O  
ATOM   1548  CB  ILE A 210      39.825 -19.738   4.645  1.00 73.88      A    C  
ANISOU 1548  CB  ILE A 210    10460   7290  10321  -2390   -721   1046  A    C  
ATOM   1549  CG1 ILE A 210      39.842 -18.726   3.496  1.00 74.94      A    C  
ANISOU 1549  CG1 ILE A 210    10368   7636  10469  -2207   -767    888  A    C  
ATOM   1550  CG2 ILE A 210      38.442 -19.916   5.222  1.00 76.65      A    C  
ANISOU 1550  CG2 ILE A 210    10786   7597  10739  -2643   -533   1011  A    C  
ATOM   1551  CD1 ILE A 210      39.105 -19.199   2.249  1.00 71.11      A    C  
ANISOU 1551  CD1 ILE A 210     9710   7139  10170  -2156   -809    683  A    C  
ATOM   1552  N   ASP A 211      42.345 -17.732   4.750  1.00 81.95      A    N  
ANISOU 1552  N   ASP A 211    11496   8632  11007  -2035   -895   1198  A    N  
ATOM   1553  CA  ASP A 211      43.583 -17.318   4.108  1.00 81.35      A    C  
ANISOU 1553  CA  ASP A 211    11374   8657  10877  -1814  -1040   1208  A    C  
ATOM   1554  C   ASP A 211      44.698 -17.267   5.147  1.00 84.17      A    C  
ANISOU 1554  C   ASP A 211    11902   9007  11070  -1808  -1097   1385  A    C  
ATOM   1555  O   ASP A 211      45.867 -17.473   4.831  1.00 82.27      A    O  
ANISOU 1555  O   ASP A 211    11682   8780  10795  -1643  -1245   1431  A    O  
ATOM   1556  CB  ASP A 211      43.414 -15.975   3.395  1.00 69.64      A    C  
ANISOU 1556  CB  ASP A 211     9699   7383   9378  -1727   -998   1100  A    C  
ATOM   1557  CG  ASP A 211      42.698 -16.102   2.061  1.00 74.80      A    C  
ANISOU 1557  CG  ASP A 211    10171   8072  10179  -1637  -1012    921  A    C  
ATOM   1558  OD1 ASP A 211      42.518 -17.248   1.585  1.00 74.55      A    O  
ANISOU 1558  OD1 ASP A 211    10155   7906  10266  -1620  -1082    869  A    O  
ATOM   1559  OD2 ASP A 211      42.325 -15.049   1.484  1.00 75.08      A    O1-
ANISOU 1559  OD2 ASP A 211    10055   8266  10208  -1575   -957    829  A    O1-
ATOM   1560  N   LEU A 212      44.321 -17.022   6.396  1.00 84.96      A    N  
ANISOU 1560  N   LEU A 212    12120   9094  11066  -1983   -980   1479  A    N  
ATOM   1561  CA  LEU A 212      45.297 -16.858   7.459  1.00 86.58      A    C  
ANISOU 1561  CA  LEU A 212    12481   9320  11095  -1983  -1028   1635  A    C  
ATOM   1562  C   LEU A 212      45.803 -18.199   7.926  1.00 84.49      A    C  
ANISOU 1562  C   LEU A 212    12413   8867  10823  -1973  -1122   1765  A    C  
ATOM   1563  O   LEU A 212      46.896 -18.293   8.475  1.00 87.54      A    O  
ANISOU 1563  O   LEU A 212    12910   9267  11083  -1891  -1230   1882  A    O  
ATOM   1564  CB  LEU A 212      44.695 -16.088   8.621  1.00 91.28      A    C  
ANISOU 1564  CB  LEU A 212    13134   9983  11563  -2160   -869   1678  A    C  
ATOM   1565  CG  LEU A 212      44.675 -14.591   8.381  1.00 90.79      A    C  
ANISOU 1565  CG  LEU A 212    12924  10118  11454  -2127   -816   1586  A    C  
ATOM   1566  CD1 LEU A 212      43.610 -13.957   9.245  1.00115.13      A    C  
ANISOU 1566  CD1 LEU A 212    16024  13248  14473  -2307   -627   1568  A    C  
ATOM   1567  CD2 LEU A 212      46.028 -14.063   8.728  1.00 85.83      A    C  
ANISOU 1567  CD2 LEU A 212    12340   9580  10689  -2027   -933   1664  A    C  
ATOM   1568  N   TRP A 213      44.997 -19.233   7.714  1.00 84.76      A    N  
ANISOU 1568  N   TRP A 213    12488   8721  10994  -2056  -1082   1741  A    N  
ATOM   1569  CA  TRP A 213      45.438 -20.604   7.934  1.00 85.26      A    C  
ANISOU 1569  CA  TRP A 213    12737   8567  11089  -2025  -1181   1848  A    C  
ATOM   1570  C   TRP A 213      46.544 -20.923   6.937  1.00 88.11      A    C  
ANISOU 1570  C   TRP A 213    13039   8941  11498  -1773  -1381   1806  A    C  
ATOM   1571  O   TRP A 213      47.622 -21.359   7.322  1.00 91.63      A    O  
ANISOU 1571  O   TRP A 213    13614   9350  11853  -1657  -1510   1924  A    O  
ATOM   1572  CB  TRP A 213      44.277 -21.576   7.762  1.00 80.54      A    C  
ANISOU 1572  CB  TRP A 213    12169   7770  10662  -2177  -1090   1802  A    C  
ATOM   1573  CG  TRP A 213      44.660 -22.980   7.989  1.00 84.77      A    C  
ANISOU 1573  CG  TRP A 213    12912   8052  11245  -2156  -1181   1913  A    C  
ATOM   1574  CD1 TRP A 213      45.111 -23.861   7.057  1.00 90.01      A    C  
ANISOU 1574  CD1 TRP A 213    13571   8588  12041  -1998  -1332   1850  A    C  
ATOM   1575  CD2 TRP A 213      44.631 -23.687   9.234  1.00 98.21      A    C  
ANISOU 1575  CD2 TRP A 213    14870   9587  12857  -2286  -1125   2111  A    C  
ATOM   1576  CE2 TRP A 213      45.085 -24.999   8.978  1.00100.01      A    C  
ANISOU 1576  CE2 TRP A 213    15248   9572  13179  -2196  -1252   2165  A    C  
ATOM   1577  CE3 TRP A 213      44.271 -23.338  10.541  1.00100.03      A    C  
ANISOU 1577  CE3 TRP A 213    15226   9852  12928  -2459   -979   2249  A    C  
ATOM   1578  NE1 TRP A 213      45.375 -25.078   7.641  1.00 95.53      A    N  
ANISOU 1578  NE1 TRP A 213    14513   9034  12748  -2019  -1379   1995  A    N  
ATOM   1579  CZ2 TRP A 213      45.187 -25.966   9.980  1.00 97.93      A    C  
ANISOU 1579  CZ2 TRP A 213    15263   9087  12858  -2275  -1236   2366  A    C  
ATOM   1580  CZ3 TRP A 213      44.374 -24.296  11.537  1.00103.44      A    C  
ANISOU 1580  CZ3 TRP A 213    15928  10083  13291  -2538   -960   2449  A    C  
ATOM   1581  CH2 TRP A 213      44.827 -25.598  11.249  1.00104.55      A    C  
ANISOU 1581  CH2 TRP A 213    16221   9970  13532  -2447  -1087   2512  A    C  
ATOM   1582  N   GLY A 214      46.281 -20.696   5.655  1.00 84.49      A    N  
ANISOU 1582  N   GLY A 214    12380   8551  11170  -1678  -1407   1634  A    N  
ATOM   1583  CA  GLY A 214      47.321 -20.832   4.656  1.00 85.38      A    C  
ANISOU 1583  CA  GLY A 214    12409   8722  11310  -1431  -1579   1582  A    C  
ATOM   1584  C   GLY A 214      48.627 -20.201   5.122  1.00 87.32      A    C  
ANISOU 1584  C   GLY A 214    12677   9115  11384  -1316  -1667   1688  A    C  
ATOM   1585  O   GLY A 214      49.667 -20.849   5.164  1.00 93.42      A    O  
ANISOU 1585  O   GLY A 214    13537   9839  12120  -1169  -1814   1762  A    O  
ATOM   1586  N   ALA A 215      48.576 -18.927   5.481  1.00 85.32      A    N  
ANISOU 1586  N   ALA A 215    12343   9043  11031  -1382  -1580   1687  A    N  
ATOM   1587  CA  ALA A 215      49.775 -18.212   5.899  1.00 84.84      A    C  
ANISOU 1587  CA  ALA A 215    12279   9138  10820  -1295  -1657   1764  A    C  
ATOM   1588  C   ALA A 215      50.512 -18.926   7.030  1.00 92.98      A    C  
ANISOU 1588  C   ALA A 215    13526  10076  11727  -1295  -1741   1931  A    C  
ATOM   1589  O   ALA A 215      51.740 -18.941   7.061  1.00 97.13      A    O  
ANISOU 1589  O   ALA A 215    14053  10679  12173  -1144  -1882   1984  A    O  
ATOM   1590  CB  ALA A 215      49.431 -16.787   6.307  1.00 77.79      A    C  
ANISOU 1590  CB  ALA A 215    11304   8410   9843  -1409  -1531   1739  A    C  
ATOM   1591  N   GLY A 216      49.766 -19.505   7.964  1.00 88.40      A    N  
ANISOU 1591  N   GLY A 216    13122   9340  11124  -1461  -1651   2016  A    N  
ATOM   1592  CA  GLY A 216      50.372 -20.299   9.017  1.00 88.18      A    C  
ANISOU 1592  CA  GLY A 216    13324   9204  10978  -1451  -1726   2187  A    C  
ATOM   1593  C   GLY A 216      51.225 -21.418   8.438  1.00 91.68      A    C  
ANISOU 1593  C   GLY A 216    13820   9530  11486  -1245  -1907   2210  A    C  
ATOM   1594  O   GLY A 216      52.366 -21.612   8.840  1.00 96.54      A    O  
ANISOU 1594  O   GLY A 216    14507  10187  11985  -1108  -2046   2304  A    O  
ATOM   1595  N   CYS A 217      50.672 -22.149   7.476  1.00 92.21      A    N  
ANISOU 1595  N   CYS A 217    13842   9456  11737  -1215  -1910   2112  A    N  
ATOM   1596  CA  CYS A 217      51.370 -23.274   6.864  1.00 96.71      A    C  
ANISOU 1596  CA  CYS A 217    14468   9892  12387  -1016  -2076   2112  A    C  
ATOM   1597  C   CYS A 217      52.621 -22.827   6.148  1.00 95.89      A    C  
ANISOU 1597  C   CYS A 217    14207   9986  12240   -778  -2226   2061  A    C  
ATOM   1598  O   CYS A 217      53.656 -23.492   6.193  1.00107.87      A    O  
ANISOU 1598  O   CYS A 217    15802  11470  13715   -594  -2385   2126  A    O  
ATOM   1599  CB  CYS A 217      50.468 -23.967   5.853  1.00 93.62      A    C  
ANISOU 1599  CB  CYS A 217    14020   9342  12208  -1036  -2046   1974  A    C  
ATOM   1600  SG  CYS A 217      48.892 -24.404   6.527  1.00103.39      A    S  
ANISOU 1600  SG  CYS A 217    15383  10372  13528  -1341  -1849   2002  A    S  
ATOM   1601  N   ILE A 218      52.507 -21.710   5.452  1.00 83.57      A    N  
ANISOU 1601  N   ILE A 218    12424   8633  10697   -777  -2170   1943  A    N  
ATOM   1602  CA  ILE A 218      53.624 -21.188   4.700  1.00 86.62      A    C  
ANISOU 1602  CA  ILE A 218    12639   9223  11052   -573  -2284   1891  A    C  
ATOM   1603  C   ILE A 218      54.675 -20.674   5.671  1.00 92.97      A    C  
ANISOU 1603  C   ILE A 218    13487  10163  11675   -551  -2348   2012  A    C  
ATOM   1604  O   ILE A 218      55.868 -20.862   5.460  1.00 99.99      A    O  
ANISOU 1604  O   ILE A 218    14335  11141  12516   -359  -2497   2033  A    O  
ATOM   1605  CB  ILE A 218      53.163 -20.094   3.735  1.00 83.17      A    C  
ANISOU 1605  CB  ILE A 218    11968   8957  10676   -590  -2190   1750  A    C  
ATOM   1606  CG1 ILE A 218      52.048 -20.649   2.840  1.00 87.73      A    C  
ANISOU 1606  CG1 ILE A 218    12503   9404  11424   -615  -2135   1621  A    C  
ATOM   1607  CG2 ILE A 218      54.336 -19.569   2.909  1.00 65.97      A    C  
ANISOU 1607  CG2 ILE A 218     9610   6989   8468   -384  -2293   1708  A    C  
ATOM   1608  CD1 ILE A 218      51.249 -19.592   2.139  1.00 83.84      A    C  
ANISOU 1608  CD1 ILE A 218    11823   9052  10982   -677  -2010   1498  A    C  
ATOM   1609  N   MET A 219      54.232 -20.055   6.758  1.00 92.92      A    N  
ANISOU 1609  N   MET A 219    13563  10181  11564   -744  -2239   2083  A    N  
ATOM   1610  CA  MET A 219      55.168 -19.574   7.767  1.00 88.27      A    C  
ANISOU 1610  CA  MET A 219    13026   9722  10793   -736  -2304   2186  A    C  
ATOM   1611  C   MET A 219      56.033 -20.714   8.292  1.00 83.30      A    C  
ANISOU 1611  C   MET A 219    12570   8988  10093   -591  -2467   2307  A    C  
ATOM   1612  O   MET A 219      57.229 -20.554   8.509  1.00 88.31      A    O  
ANISOU 1612  O   MET A 219    13166   9764  10623   -454  -2602   2345  A    O  
ATOM   1613  CB  MET A 219      54.438 -18.896   8.925  1.00 83.48      A    C  
ANISOU 1613  CB  MET A 219    12515   9128  10078   -965  -2159   2241  A    C  
ATOM   1614  CG  MET A 219      55.329 -17.962   9.725  1.00 74.75      A    C  
ANISOU 1614  CG  MET A 219    11383   8220   8797   -972  -2207   2283  A    C  
ATOM   1615  SD  MET A 219      54.566 -17.422  11.254  1.00128.72      A    S  
ANISOU 1615  SD  MET A 219    18384  15051  15471  -1210  -2064   2361  A    S  
ATOM   1616  CE  MET A 219      55.947 -16.596  12.034  1.00102.27      A    C  
ANISOU 1616  CE  MET A 219    15000  11932  11927  -1149  -2195   2393  A    C  
ATOM   1617  N   ALA A 220      55.426 -21.871   8.495  1.00 82.47      A    N  
ANISOU 1617  N   ALA A 220    12654   8633  10049   -619  -2454   2367  A    N  
ATOM   1618  CA  ALA A 220      56.183 -23.034   8.923  1.00 91.94      A    C  
ANISOU 1618  CA  ALA A 220    14039   9699  11196   -463  -2607   2486  A    C  
ATOM   1619  C   ALA A 220      57.101 -23.494   7.792  1.00 97.56      A    C  
ANISOU 1619  C   ALA A 220    14623  10451  11994   -199  -2769   2403  A    C  
ATOM   1620  O   ALA A 220      58.287 -23.737   7.985  1.00101.54      A    O  
ANISOU 1620  O   ALA A 220    15136  11040  12405     -9  -2930   2457  A    O  
ATOM   1621  CB  ALA A 220      55.241 -24.142   9.332  1.00 88.50      A    C  
ANISOU 1621  CB  ALA A 220    13838   8959  10827   -573  -2537   2567  A    C  
ATOM   1622  N   GLU A 221      56.537 -23.599   6.602  1.00101.24      A    N  
ANISOU 1622  N   GLU A 221    14961  10873  12633   -180  -2726   2262  A    N  
ATOM   1623  CA  GLU A 221      57.273 -24.057   5.437  1.00107.53      A    C  
ANISOU 1623  CA  GLU A 221    15632  11706  13517     70  -2861   2165  A    C  
ATOM   1624  C   GLU A 221      58.562 -23.263   5.239  1.00114.00      A    C  
ANISOU 1624  C   GLU A 221    16264  12818  14233    223  -2960   2150  A    C  
ATOM   1625  O   GLU A 221      59.377 -23.606   4.392  1.00120.14      A    O  
ANISOU 1625  O   GLU A 221    16932  13667  15048    452  -3083   2087  A    O  
ATOM   1626  CB  GLU A 221      56.370 -23.930   4.211  1.00105.49      A    C  
ANISOU 1626  CB  GLU A 221    15226  11425  13432     35  -2771   1998  A    C  
ATOM   1627  CG  GLU A 221      56.799 -24.674   2.972  1.00103.39      A    C  
ANISOU 1627  CG  GLU A 221    14877  11128  13280    275  -2892   1882  A    C  
ATOM   1628  CD  GLU A 221      55.595 -25.056   2.142  1.00114.14      A    C  
ANISOU 1628  CD  GLU A 221    16214  12337  14816    196  -2808   1747  A    C  
ATOM   1629  OE1 GLU A 221      54.557 -25.378   2.762  1.00118.44      A    O  
ANISOU 1629  OE1 GLU A 221    16906  12687  15409    -14  -2702   1789  A    O  
ATOM   1630  OE2 GLU A 221      55.672 -25.025   0.892  1.00115.06      A    O1-
ANISOU 1630  OE2 GLU A 221    16160  12539  15018    341  -2843   1598  A    O1-
ATOM   1631  N   MET A 222      58.738 -22.199   6.020  1.00117.51      A    N  
ANISOU 1631  N   MET A 222    16666  13433  14548     93  -2904   2200  A    N  
ATOM   1632  CA  MET A 222      59.919 -21.336   5.909  1.00118.13      A    C  
ANISOU 1632  CA  MET A 222    16556  13793  14536    194  -2983   2182  A    C  
ATOM   1633  C   MET A 222      61.123 -21.917   6.654  1.00123.47      A    C  
ANISOU 1633  C   MET A 222    17325  14507  15080    360  -3164   2288  A    C  
ATOM   1634  O   MET A 222      62.274 -21.593   6.353  1.00124.38      A    O  
ANISOU 1634  O   MET A 222    17275  14835  15148    514  -3274   2259  A    O  
ATOM   1635  CB  MET A 222      59.616 -19.925   6.436  1.00108.14      A    C  
ANISOU 1635  CB  MET A 222    15207  12685  13196    -18  -2853   2175  A    C  
ATOM   1636  CG  MET A 222      58.581 -19.137   5.625  1.00101.43      A    C  
ANISOU 1636  CG  MET A 222    14224  11852  12462   -149  -2684   2062  A    C  
ATOM   1637  SD  MET A 222      59.208 -18.428   4.079  1.00 91.79      A    S  
ANISOU 1637  SD  MET A 222    12700  10851  11326      6  -2699   1932  A    S  
ATOM   1638  CE  MET A 222      60.603 -17.485   4.692  1.00209.40      A    C  
ANISOU 1638  CE  MET A 222    27480  26006  26076     24  -2780   1980  A    C  
ATOM   1639  N   TRP A 223      60.851 -22.774   7.631  1.00120.63      A    N  
ANISOU 1639  N   TRP A 223    17229  13946  14658    328  -3191   2413  A    N  
ATOM   1640  CA  TRP A 223      61.910 -23.398   8.408  1.00112.06      A    C  
ANISOU 1640  CA  TRP A 223    16263  12878  13435    497  -3366   2526  A    C  
ATOM   1641  C   TRP A 223      62.046 -24.861   8.052  1.00115.17      A    C  
ANISOU 1641  C   TRP A 223    16810  13041  13906    699  -3479   2557  A    C  
ATOM   1642  O   TRP A 223      62.974 -25.525   8.502  1.00126.02      A    O  
ANISOU 1642  O   TRP A 223    18280  14415  15186    895  -3645   2640  A    O  
ATOM   1643  CB  TRP A 223      61.634 -23.262   9.905  1.00108.35      A    C  
ANISOU 1643  CB  TRP A 223    16003  12367  12798    338  -3327   2667  A    C  
ATOM   1644  CG  TRP A 223      62.006 -21.922  10.428  1.00118.81      A    C  
ANISOU 1644  CG  TRP A 223    17184  13958  14000    222  -3296   2641  A    C  
ATOM   1645  CD1 TRP A 223      63.256 -21.497  10.778  1.00122.90      A    C  
ANISOU 1645  CD1 TRP A 223    17592  14715  14391    339  -3439   2645  A    C  
ATOM   1646  CD2 TRP A 223      61.128 -20.810  10.642  1.00117.25      A    C  
ANISOU 1646  CD2 TRP A 223    16929  13816  13803    -35  -3112   2593  A    C  
ATOM   1647  CE2 TRP A 223      61.914 -19.745  11.128  1.00111.02      A    C  
ANISOU 1647  CE2 TRP A 223    16009  13286  12889    -64  -3156   2570  A    C  
ATOM   1648  CE3 TRP A 223      59.754 -20.613  10.469  1.00109.28      A    C  
ANISOU 1648  CE3 TRP A 223    15961  12668  12894   -237  -2919   2560  A    C  
ATOM   1649  NE1 TRP A 223      63.208 -20.190  11.203  1.00119.56      A    N  
ANISOU 1649  NE1 TRP A 223    17053  14480  13896    159  -3356   2600  A    N  
ATOM   1650  CZ2 TRP A 223      61.372 -18.502  11.443  1.00 98.95      A    C  
ANISOU 1650  CZ2 TRP A 223    14407  11858  11331   -284  -3012   2516  A    C  
ATOM   1651  CZ3 TRP A 223      59.220 -19.384  10.788  1.00105.10      A    C  
ANISOU 1651  CZ3 TRP A 223    15352  12256  12327   -442  -2778   2510  A    C  
ATOM   1652  CH2 TRP A 223      60.028 -18.342  11.271  1.00101.00      A    C  
ANISOU 1652  CH2 TRP A 223    14719  11974  11682   -461  -2825   2489  A    C  
ATOM   1653  N   THR A 224      61.120 -25.363   7.244  1.00104.77      A    N  
ANISOU 1653  N   THR A 224    15518  11528  12764    656  -3396   2482  A    N  
ATOM   1654  CA  THR A 224      61.046 -26.795   7.005  1.00106.72      A    C  
ANISOU 1654  CA  THR A 224    15952  11496  13101    804  -3483   2511  A    C  
ATOM   1655  C   THR A 224      61.254 -27.131   5.543  1.00105.75      A    C  
ANISOU 1655  C   THR A 224    15660  11388  13132    991  -3541   2348  A    C  
ATOM   1656  O   THR A 224      61.292 -28.300   5.169  1.00112.24      A    O  
ANISOU 1656  O   THR A 224    16610  11993  14044   1147  -3630   2336  A    O  
ATOM   1657  CB  THR A 224      59.695 -27.394   7.477  1.00 92.64      A    C  
ANISOU 1657  CB  THR A 224    14407   9398  11394    582  -3344   2576  A    C  
ATOM   1658  CG2 THR A 224      59.393 -27.009   8.918  1.00 77.60      A    C  
ANISOU 1658  CG2 THR A 224    12668   7495   9324    386  -3262   2736  A    C  
ATOM   1659  OG1 THR A 224      58.634 -26.936   6.632  1.00 97.31      A    O  
ANISOU 1659  OG1 THR A 224    14857   9977  12138    421  -3192   2434  A    O  
ATOM   1660  N   ARG A 225      61.381 -26.108   4.714  1.00102.64      A    N  
ANISOU 1660  N   ARG A 225    14988  11244  12766    980  -3487   2221  A    N  
ATOM   1661  CA  ARG A 225      61.503 -26.321   3.273  1.00109.37      A    C  
ANISOU 1661  CA  ARG A 225    15666  12140  13750   1151  -3522   2060  A    C  
ATOM   1662  C   ARG A 225      60.404 -27.219   2.670  1.00110.79      A    C  
ANISOU 1662  C   ARG A 225    15962  12027  14105   1108  -3471   1981  A    C  
ATOM   1663  O   ARG A 225      60.400 -27.473   1.464  1.00112.47      A    O  
ANISOU 1663  O   ARG A 225    16048  12258  14428   1249  -3501   1834  A    O  
ATOM   1664  CB  ARG A 225      62.888 -26.885   2.936  1.00109.00      A    C  
ANISOU 1664  CB  ARG A 225    15560  12199  13656   1476  -3719   2051  A    C  
ATOM   1665  CG  ARG A 225      64.025 -25.979   3.365  1.00106.80      A    C  
ANISOU 1665  CG  ARG A 225    15115  12240  13224   1525  -3777   2097  A    C  
ATOM   1666  CD  ARG A 225      63.719 -24.555   2.984  1.00107.74      A    C  
ANISOU 1666  CD  ARG A 225    15004  12584  13347   1343  -3628   2027  A    C  
ATOM   1667  NE  ARG A 225      64.805 -23.640   3.305  1.00112.65      A    N  
ANISOU 1667  NE  ARG A 225    15448  13510  13845   1371  -3676   2052  A    N  
ATOM   1668  CZ  ARG A 225      65.601 -23.075   2.402  1.00121.32      A    C  
ANISOU 1668  CZ  ARG A 225    16277  14866  14953   1497  -3698   1964  A    C  
ATOM   1669  NH1 ARG A 225      65.439 -23.331   1.108  1.00119.46      A    N1+
ANISOU 1669  NH1 ARG A 225    15927  14634  14830   1625  -3679   1847  A    N1+
ATOM   1670  NH2 ARG A 225      66.562 -22.248   2.796  1.00125.26      A    N  
ANISOU 1670  NH2 ARG A 225    16619  15628  15347   1491  -3736   1989  A    N  
ATOM   1671  N   SER A 226      59.469 -27.686   3.495  1.00106.78      A    N  
ANISOU 1671  N   SER A 226    15688  11262  13622    909  -3390   2073  A    N  
ATOM   1672  CA  SER A 226      58.453 -28.623   3.025  1.00116.22      A    C  
ANISOU 1672  CA  SER A 226    17005  12161  14993    851  -3348   2003  A    C  
ATOM   1673  C   SER A 226      57.062 -28.355   3.626  1.00116.42      A    C  
ANISOU 1673  C   SER A 226    17124  12047  15061    519  -3156   2040  A    C  
ATOM   1674  O   SER A 226      56.948 -28.044   4.814  1.00118.63      A    O  
ANISOU 1674  O   SER A 226    17531  12324  15221    364  -3093   2192  A    O  
ATOM   1675  CB  SER A 226      58.905 -30.060   3.327  1.00127.60      A    C  
ANISOU 1675  CB  SER A 226    18696  13329  16458   1026  -3495   2082  A    C  
ATOM   1676  OG  SER A 226      58.040 -31.031   2.751  1.00131.60      A    O  
ANISOU 1676  OG  SER A 226    19310  13539  17154    993  -3475   1990  A    O  
ATOM   1677  N   PRO A 227      56.001 -28.483   2.800  1.00107.31      A    N  
ANISOU 1677  N   PRO A 227    15903  10792  14076    418  -3066   1894  A    N  
ATOM   1678  CA  PRO A 227      54.605 -28.402   3.255  1.00 99.95      A    C  
ANISOU 1678  CA  PRO A 227    15050   9709  13216    113  -2887   1906  A    C  
ATOM   1679  C   PRO A 227      54.398 -29.328   4.445  1.00114.51      A    C  
ANISOU 1679  C   PRO A 227    17206  11269  15033      8  -2878   2090  A    C  
ATOM   1680  O   PRO A 227      54.672 -30.526   4.351  1.00122.84      A    O  
ANISOU 1680  O   PRO A 227    18432  12082  16160    138  -2988   2115  A    O  
ATOM   1681  CB  PRO A 227      53.812 -28.935   2.062  1.00 91.60      A    C  
ANISOU 1681  CB  PRO A 227    13912   8526  12365    123  -2877   1709  A    C  
ATOM   1682  CG  PRO A 227      54.685 -28.711   0.892  1.00 97.30      A    C  
ANISOU 1682  CG  PRO A 227    14429   9454  13087    397  -2999   1575  A    C  
ATOM   1683  CD  PRO A 227      56.097 -28.835   1.373  1.00103.00      A    C  
ANISOU 1683  CD  PRO A 227    15208  10265  13662    607  -3143   1700  A    C  
ATOM   1684  N   ILE A 228      53.901 -28.781   5.545  1.00117.08      A    N  
ANISOU 1684  N   ILE A 228    17613  11619  15253   -220  -2743   2219  A    N  
ATOM   1685  CA  ILE A 228      53.903 -29.492   6.822  1.00113.87      A    C  
ANISOU 1685  CA  ILE A 228    17505  11002  14760   -299  -2734   2432  A    C  
ATOM   1686  C   ILE A 228      52.803 -30.547   7.021  1.00120.55      A    C  
ANISOU 1686  C   ILE A 228    18555  11491  15760   -482  -2638   2465  A    C  
ATOM   1687  O   ILE A 228      52.915 -31.391   7.913  1.00125.68      A    O  
ANISOU 1687  O   ILE A 228    19480  11914  16359   -499  -2656   2646  A    O  
ATOM   1688  CB  ILE A 228      53.888 -28.495   7.994  1.00110.20      A    C  
ANISOU 1688  CB  ILE A 228    17058  10721  14093   -455  -2632   2563  A    C  
ATOM   1689  CG1 ILE A 228      52.675 -27.564   7.881  1.00111.34      A    C  
ANISOU 1689  CG1 ILE A 228    17050  10962  14291   -716  -2426   2467  A    C  
ATOM   1690  CG2 ILE A 228      55.192 -27.698   8.014  1.00104.91      A    C  
ANISOU 1690  CG2 ILE A 228    16247  10352  13260   -259  -2761   2569  A    C  
ATOM   1691  CD1 ILE A 228      52.393 -26.748   9.127  1.00105.27      A    C  
ANISOU 1691  CD1 ILE A 228    16344  10311  13343   -908  -2297   2593  A    C  
ATOM   1692  N   MET A 229      51.756 -30.510   6.198  1.00123.06      A    N  
ANISOU 1692  N   MET A 229    18737  11757  16262   -618  -2539   2292  A    N  
ATOM   1693  CA  MET A 229      50.663 -31.485   6.296  1.00120.86      A    C  
ANISOU 1693  CA  MET A 229    18618  11147  16157   -815  -2442   2295  A    C  
ATOM   1694  C   MET A 229      50.257 -32.045   4.936  1.00120.24      A    C  
ANISOU 1694  C   MET A 229    18416  10958  16311   -748  -2498   2063  A    C  
ATOM   1695  O   MET A 229      49.283 -31.584   4.338  1.00115.70      A    O  
ANISOU 1695  O   MET A 229    17655  10457  15850   -898  -2388   1900  A    O  
ATOM   1696  CB  MET A 229      49.431 -30.857   6.950  1.00106.98      A    C  
ANISOU 1696  CB  MET A 229    16832   9425  14390  -1146  -2210   2326  A    C  
ATOM   1697  CG  MET A 229      49.644 -30.340   8.353  1.00 95.34      A    C  
ANISOU 1697  CG  MET A 229    15494   8045  12686  -1244  -2131   2545  A    C  
ATOM   1698  SD  MET A 229      48.131 -29.556   8.925  1.00166.11      A    S  
ANISOU 1698  SD  MET A 229    24380  17079  21656  -1613  -1853   2533  A    S  
ATOM   1699  CE  MET A 229      48.736 -28.618  10.322  1.00121.78      A    C  
ANISOU 1699  CE  MET A 229    18850  11691  15729  -1630  -1814   2732  A    C  
ATOM   1700  N   GLN A 230      50.984 -33.050   4.460  1.00122.92      A    N  
ANISOU 1700  N   GLN A 230    18863  11123  16719   -516  -2672   2040  A    N  
ATOM   1701  CA  GLN A 230      50.751 -33.579   3.117  1.00126.15      A    C  
ANISOU 1701  CA  GLN A 230    19153  11450  17330   -408  -2753   1802  A    C  
ATOM   1702  C   GLN A 230      49.797 -34.776   3.099  1.00126.37      A    C  
ANISOU 1702  C   GLN A 230    19358  11081  17575   -581  -2705   1768  A    C  
ATOM   1703  O   GLN A 230      50.227 -35.917   3.205  1.00125.72      A    O  
ANISOU 1703  O   GLN A 230    19504  10711  17555   -464  -2815   1830  A    O  
ATOM   1704  CB  GLN A 230      52.086 -33.936   2.456  1.00123.61      A    C  
ANISOU 1704  CB  GLN A 230    18810  11189  16966    -36  -2974   1755  A    C  
ATOM   1705  CG  GLN A 230      53.080 -32.785   2.472  1.00119.34      A    C  
ANISOU 1705  CG  GLN A 230    18086  11036  16221    124  -3020   1788  A    C  
ATOM   1706  CD  GLN A 230      54.450 -33.180   1.981  1.00118.21      A    C  
ANISOU 1706  CD  GLN A 230    17932  10960  16021    484  -3229   1769  A    C  
ATOM   1707  NE2 GLN A 230      54.939 -32.485   0.963  1.00117.82      A    N  
ANISOU 1707  NE2 GLN A 230    17614  11203  15950    656  -3283   1614  A    N  
ATOM   1708  OE1 GLN A 230      55.070 -34.092   2.517  1.00121.53      A    O  
ANISOU 1708  OE1 GLN A 230    18584  11180  16413    612  -3338   1896  A    O  
ATOM   1709  N   GLY A 231      48.502 -34.506   2.950  1.00129.47      A    N  
ANISOU 1709  N   GLY A 231    19641  11461  18091   -857  -2541   1664  A    N  
ATOM   1710  CA  GLY A 231      47.495 -35.553   2.975  1.00133.27      A    C  
ANISOU 1710  CA  GLY A 231    20263  11582  18791  -1071  -2470   1625  A    C  
ATOM   1711  C   GLY A 231      47.086 -36.050   1.599  1.00139.16      A    C  
ANISOU 1711  C   GLY A 231    20863  12252  19760  -1000  -2555   1333  A    C  
ATOM   1712  O   GLY A 231      47.177 -35.314   0.613  1.00139.41      A    O  
ANISOU 1712  O   GLY A 231    20623  12567  19778   -866  -2603   1140  A    O  
ATOM   1713  N   ASN A 232      46.632 -37.301   1.538  1.00143.25      A    N  
ANISOU 1713  N   ASN A 232    21567  12382  20481  -1091  -2573   1300  A    N  
ATOM   1714  CA  ASN A 232      46.191 -37.915   0.286  1.00148.42      A    C  
ANISOU 1714  CA  ASN A 232    22110  12919  21364  -1041  -2661   1009  A    C  
ATOM   1715  C   ASN A 232      44.736 -37.598  -0.028  1.00147.61      A    C  
ANISOU 1715  C   ASN A 232    21813  12857  21416  -1345  -2502    837  A    C  
ATOM   1716  O   ASN A 232      44.353 -37.521  -1.196  1.00147.56      A    O  
ANISOU 1716  O   ASN A 232    21587  12950  21529  -1281  -2563    558  A    O  
ATOM   1717  CB  ASN A 232      46.386 -39.435   0.312  1.00161.40      A    C  
ANISOU 1717  CB  ASN A 232    24044  14107  23173   -993  -2766   1029  A    C  
ATOM   1718  CG  ASN A 232      47.853 -39.844   0.319  1.00170.97      A    C  
ANISOU 1718  CG  ASN A 232    25412  15290  24260   -624  -2964   1130  A    C  
ATOM   1719  ND2 ASN A 232      48.124 -41.071  -0.120  1.00176.94      A    N  
ANISOU 1719  ND2 ASN A 232    26345  15710  25172   -485  -3105   1049  A    N  
ATOM   1720  OD1 ASN A 232      48.728 -39.076   0.722  1.00170.25      A    O  
ANISOU 1720  OD1 ASN A 232    25280  15472  23938   -467  -2992   1272  A    O  
ATOM   1721  N   THR A 233      43.928 -37.434   1.018  1.00147.23      A    N  
ANISOU 1721  N   THR A 233    21843  12738  21359  -1668  -2301    999  A    N  
ATOM   1722  CA  THR A 233      42.537 -37.001   0.868  1.00145.41      A    C  
ANISOU 1722  CA  THR A 233    21408  12593  21249  -1969  -2129    857  A    C  
ATOM   1723  C   THR A 233      42.036 -36.304   2.123  1.00140.80      A    C  
ANISOU 1723  C   THR A 233    20861  12109  20529  -2228  -1911   1080  A    C  
ATOM   1724  O   THR A 233      42.662 -36.385   3.178  1.00140.92      A    O  
ANISOU 1724  O   THR A 233    21107  12052  20384  -2213  -1888   1352  A    O  
ATOM   1725  CB  THR A 233      41.588 -38.173   0.583  1.00146.15      A    C  
ANISOU 1725  CB  THR A 233    21576  12318  21635  -2187  -2102    720  A    C  
ATOM   1726  CG2 THR A 233      41.749 -38.666  -0.849  1.00143.39      A    C  
ANISOU 1726  CG2 THR A 233    21102  11937  21443  -1970  -2297    411  A    C  
ATOM   1727  OG1 THR A 233      41.860 -39.239   1.503  1.00150.80      A    O  
ANISOU 1727  OG1 THR A 233    22525  12513  22261  -2269  -2088    954  A    O  
ATOM   1728  N   GLU A 234      40.894 -35.635   1.995  1.00133.13      A    N  
ANISOU 1728  N   GLU A 234    19660  11310  19615  -2453  -1755    954  A    N  
ATOM   1729  CA  GLU A 234      40.262 -34.939   3.111  1.00134.45      A    C  
ANISOU 1729  CA  GLU A 234    19829  11590  19665  -2711  -1532   1126  A    C  
ATOM   1730  C   GLU A 234      40.365 -35.709   4.430  1.00145.79      A    C  
ANISOU 1730  C   GLU A 234    21607  12727  21060  -2875  -1437   1425  A    C  
ATOM   1731  O   GLU A 234      40.924 -35.201   5.407  1.00144.32      A    O  
ANISOU 1731  O   GLU A 234    21543  12650  20642  -2842  -1390   1660  A    O  
ATOM   1732  CB  GLU A 234      38.803 -34.637   2.775  1.00135.95      A    C  
ANISOU 1732  CB  GLU A 234    19775  11866  20015  -2981  -1376    928  A    C  
ATOM   1733  CG  GLU A 234      38.640 -33.730   1.564  1.00145.93      A    C  
ANISOU 1733  CG  GLU A 234    20699  13465  21284  -2816  -1452    655  A    C  
ATOM   1734  CD  GLU A 234      37.191 -33.555   1.137  1.00157.05      A    C  
ANISOU 1734  CD  GLU A 234    21859  14945  22867  -3058  -1326    432  A    C  
ATOM   1735  OE1 GLU A 234      36.592 -34.536   0.634  1.00166.09      A    O  
ANISOU 1735  OE1 GLU A 234    23003  15850  24253  -3175  -1356    271  A    O  
ATOM   1736  OE2 GLU A 234      36.656 -32.433   1.299  1.00150.30      A    O1-
ANISOU 1736  OE2 GLU A 234    20808  14388  21911  -3125  -1201    408  A    O1-
ATOM   1737  N   GLN A 235      39.819 -36.926   4.452  1.00151.88      A    N  
ANISOU 1737  N   GLN A 235    22535  13120  22052  -3052  -1410   1414  A    N  
ATOM   1738  CA  GLN A 235      39.945 -37.828   5.597  1.00148.57      A    C  
ANISOU 1738  CA  GLN A 235    22473  12361  21615  -3190  -1333   1701  A    C  
ATOM   1739  C   GLN A 235      41.357 -37.790   6.173  1.00141.17      A    C  
ANISOU 1739  C   GLN A 235    21759  11444  20436  -2905  -1465   1935  A    C  
ATOM   1740  O   GLN A 235      41.553 -37.501   7.358  1.00130.71      A    O  
ANISOU 1740  O   GLN A 235    20596  10159  18910  -2975  -1358   2200  A    O  
ATOM   1741  CB  GLN A 235      39.624 -39.266   5.176  1.00155.17      A    C  
ANISOU 1741  CB  GLN A 235    23469  12754  22736  -3280  -1387   1620  A    C  
ATOM   1742  CG  GLN A 235      38.150 -39.648   5.235  1.00162.79      A    C  
ANISOU 1742  CG  GLN A 235    24353  13564  23938  -3682  -1188   1522  A    C  
ATOM   1743  CD  GLN A 235      37.750 -40.242   6.577  1.00166.60      A    C  
ANISOU 1743  CD  GLN A 235    25126  13769  24404  -3972   -984   1828  A    C  
ATOM   1744  NE2 GLN A 235      37.137 -41.423   6.543  1.00160.33      A    N  
ANISOU 1744  NE2 GLN A 235    24480  12566  23872  -4198   -933   1808  A    N  
ATOM   1745  OE1 GLN A 235      37.986 -39.646   7.630  1.00170.90      A    O  
ANISOU 1745  OE1 GLN A 235    25767  14467  24702  -3996   -871   2078  A    O  
ATOM   1746  N   HIS A 236      42.332 -38.093   5.317  1.00139.47      A    N  
ANISOU 1746  N   HIS A 236    21543  11212  20238  -2578  -1701   1826  A    N  
ATOM   1747  CA  HIS A 236      43.732 -38.167   5.715  1.00135.95      A    C  
ANISOU 1747  CA  HIS A 236    21287  10780  19589  -2275  -1858   2013  A    C  
ATOM   1748  C   HIS A 236      44.209 -36.834   6.250  1.00137.97      A    C  
ANISOU 1748  C   HIS A 236    21419  11438  19563  -2198  -1819   2116  A    C  
ATOM   1749  O   HIS A 236      44.802 -36.763   7.326  1.00140.46      A    O  
ANISOU 1749  O   HIS A 236    21939  11756  19675  -2165  -1802   2376  A    O  
ATOM   1750  CB  HIS A 236      44.606 -38.595   4.532  1.00135.67      A    C  
ANISOU 1750  CB  HIS A 236    21199  10719  19631  -1933  -2109   1824  A    C  
ATOM   1751  CG  HIS A 236      46.052 -38.782   4.884  1.00140.76      A    C  
ANISOU 1751  CG  HIS A 236    22029  11366  20087  -1609  -2282   1998  A    C  
ATOM   1752  CD2 HIS A 236      46.648 -39.161   6.040  1.00141.68      A    C  
ANISOU 1752  CD2 HIS A 236    22445  11339  20049  -1578  -2279   2297  A    C  
ATOM   1753  ND1 HIS A 236      47.074 -38.563   3.983  1.00140.06      A    N  
ANISOU 1753  ND1 HIS A 236    21807  11463  19945  -1257  -2487   1862  A    N  
ATOM   1754  CE1 HIS A 236      48.235 -38.804   4.566  1.00135.47      A    C  
ANISOU 1754  CE1 HIS A 236    21424  10855  19195  -1027  -2607   2059  A    C  
ATOM   1755  NE2 HIS A 236      48.006 -39.167   5.815  1.00137.51      A    N  
ANISOU 1755  NE2 HIS A 236    21949  10915  19385  -1208  -2491   2324  A    N  
ATOM   1756  N   GLN A 237      43.951 -35.779   5.482  1.00138.33      A    N  
ANISOU 1756  N   GLN A 237    21137  11823  19600  -2165  -1811   1908  A    N  
ATOM   1757  CA  GLN A 237      44.353 -34.431   5.856  1.00129.49      A    C  
ANISOU 1757  CA  GLN A 237    19873  11089  18240  -2098  -1775   1968  A    C  
ATOM   1758  C   GLN A 237      43.817 -34.098   7.236  1.00123.92      A    C  
ANISOU 1758  C   GLN A 237    19294  10392  17398  -2358  -1567   2193  A    C  
ATOM   1759  O   GLN A 237      44.577 -34.007   8.193  1.00125.53      A    O  
ANISOU 1759  O   GLN A 237    19685  10617  17392  -2281  -1587   2422  A    O  
ATOM   1760  CB  GLN A 237      43.828 -33.415   4.842  1.00127.86      A    C  
ANISOU 1760  CB  GLN A 237    19306  11192  18085  -2091  -1751   1708  A    C  
ATOM   1761  CG  GLN A 237      44.200 -31.970   5.145  1.00122.36      A    C  
ANISOU 1761  CG  GLN A 237    18452  10879  17160  -2028  -1710   1752  A    C  
ATOM   1762  CD  GLN A 237      45.567 -31.597   4.617  1.00121.73      A    C  
ANISOU 1762  CD  GLN A 237    18314  10982  16956  -1686  -1908   1735  A    C  
ATOM   1763  NE2 GLN A 237      45.928 -30.324   4.754  1.00121.70      A    N  
ANISOU 1763  NE2 GLN A 237    18157  11307  16777  -1627  -1882   1750  A    N  
ATOM   1764  OE1 GLN A 237      46.291 -32.440   4.087  1.00121.49      A    O  
ANISOU 1764  OE1 GLN A 237    18372  10799  16990  -1478  -2078   1704  A    O  
ATOM   1765  N   LEU A 238      42.503 -33.927   7.333  1.00117.61      A    N  
ANISOU 1765  N   LEU A 238    18386   9588  16712  -2659  -1369   2120  A    N  
ATOM   1766  CA  LEU A 238      41.869 -33.574   8.598  1.00120.01      A    C  
ANISOU 1766  CA  LEU A 238    18784   9925  16891  -2921  -1148   2312  A    C  
ATOM   1767  C   LEU A 238      42.511 -34.299   9.777  1.00119.05      A    C  
ANISOU 1767  C   LEU A 238    19027   9581  16626  -2907  -1153   2622  A    C  
ATOM   1768  O   LEU A 238      42.640 -33.748  10.863  1.00117.01      A    O  
ANISOU 1768  O   LEU A 238    18861   9454  16142  -2965  -1054   2814  A    O  
ATOM   1769  CB  LEU A 238      40.374 -33.890   8.551  1.00126.37      A    C  
ANISOU 1769  CB  LEU A 238    19505  10606  17905  -3261   -948   2214  A    C  
ATOM   1770  CG  LEU A 238      39.376 -32.769   8.865  1.00121.75      A    C  
ANISOU 1770  CG  LEU A 238    18693  10308  17259  -3470   -739   2152  A    C  
ATOM   1771  CD1 LEU A 238      37.958 -33.289   8.679  1.00128.40      A    C  
ANISOU 1771  CD1 LEU A 238    19443  10998  18344  -3787   -570   2032  A    C  
ATOM   1772  CD2 LEU A 238      39.564 -32.185  10.269  1.00107.86      A    C  
ANISOU 1772  CD2 LEU A 238    17082   8671  15227  -3544   -606   2410  A    C  
ATOM   1773  N   ALA A 239      42.910 -35.542   9.558  1.00126.43      A    N  
ANISOU 1773  N   ALA A 239    20175  10175  17687  -2818  -1273   2667  A    N  
ATOM   1774  CA  ALA A 239      43.519 -36.334  10.613  1.00128.48      A    C  
ANISOU 1774  CA  ALA A 239    20802  10192  17822  -2781  -1292   2965  A    C  
ATOM   1775  C   ALA A 239      44.908 -35.809  10.990  1.00126.82      A    C  
ANISOU 1775  C   ALA A 239    20652  10194  17341  -2471  -1457   3088  A    C  
ATOM   1776  O   ALA A 239      45.274 -35.811  12.162  1.00130.68      A    O  
ANISOU 1776  O   ALA A 239    21361  10675  17614  -2479  -1413   3345  A    O  
ATOM   1777  CB  ALA A 239      43.582 -37.789  10.200  1.00134.04      A    C  
ANISOU 1777  CB  ALA A 239    21716  10463  18748  -2750  -1386   2963  A    C  
ATOM   1778  N   LEU A 240      45.676 -35.362   9.997  1.00122.08      A    N  
ANISOU 1778  N   LEU A 240    19848   9791  16744  -2200  -1645   2904  A    N  
ATOM   1779  CA  LEU A 240      46.991 -34.765  10.244  1.00118.98      A    C  
ANISOU 1779  CA  LEU A 240    19455   9640  16111  -1914  -1803   2985  A    C  
ATOM   1780  C   LEU A 240      46.877 -33.499  11.072  1.00119.27      A    C  
ANISOU 1780  C   LEU A 240    19395  10004  15919  -2019  -1676   3063  A    C  
ATOM   1781  O   LEU A 240      47.710 -33.234  11.935  1.00116.70      A    O  
ANISOU 1781  O   LEU A 240    19199   9786  15355  -1902  -1732   3243  A    O  
ATOM   1782  CB  LEU A 240      47.686 -34.417   8.933  1.00115.88      A    C  
ANISOU 1782  CB  LEU A 240    18816   9428  15784  -1643  -1992   2749  A    C  
ATOM   1783  CG  LEU A 240      48.705 -35.404   8.386  1.00122.47      A    C  
ANISOU 1783  CG  LEU A 240    19780  10074  16679  -1343  -2222   2739  A    C  
ATOM   1784  CD1 LEU A 240      48.007 -36.695   7.986  1.00125.58      A    C  
ANISOU 1784  CD1 LEU A 240    20322  10058  17335  -1452  -2207   2684  A    C  
ATOM   1785  CD2 LEU A 240      49.436 -34.781   7.203  1.00121.00      A    C  
ANISOU 1785  CD2 LEU A 240    19313  10163  16498  -1078  -2381   2521  A    C  
ATOM   1786  N   ILE A 241      45.846 -32.712  10.771  1.00123.86      A    N  
ANISOU 1786  N   ILE A 241    19740  10749  16573  -2227  -1515   2911  A    N  
ATOM   1787  CA  ILE A 241      45.562 -31.463  11.467  1.00116.52      A    C  
ANISOU 1787  CA  ILE A 241    18696  10122  15455  -2346  -1376   2947  A    C  
ATOM   1788  C   ILE A 241      45.201 -31.721  12.917  1.00120.26      A    C  
ANISOU 1788  C   ILE A 241    19428  10490  15775  -2541  -1215   3205  A    C  
ATOM   1789  O   ILE A 241      45.741 -31.079  13.814  1.00120.75      A    O  
ANISOU 1789  O   ILE A 241    19556  10739  15585  -2490  -1213   3342  A    O  
ATOM   1790  CB  ILE A 241      44.377 -30.717  10.825  1.00113.81      A    C  
ANISOU 1790  CB  ILE A 241    18063   9931  15250  -2537  -1224   2727  A    C  
ATOM   1791  CG1 ILE A 241      44.645 -30.442   9.344  1.00114.54      A    C  
ANISOU 1791  CG1 ILE A 241    17895  10139  15486  -2347  -1370   2468  A    C  
ATOM   1792  CG2 ILE A 241      44.085 -29.425  11.580  1.00115.11      A    C  
ANISOU 1792  CG2 ILE A 241    18125  10394  15217  -2648  -1079   2763  A    C  
ATOM   1793  CD1 ILE A 241      43.525 -29.676   8.656  1.00116.36      A    C  
ANISOU 1793  CD1 ILE A 241    17835  10537  15840  -2498  -1241   2247  A    C  
ATOM   1794  N   SER A 242      44.276 -32.654  13.141  1.00123.72      A    N  
ANISOU 1794  N   SER A 242    20010  10633  16366  -2769  -1077   3268  A    N  
ATOM   1795  CA  SER A 242      43.853 -32.997  14.498  1.00124.25      A    C  
ANISOU 1795  CA  SER A 242    20336  10576  16296  -2970   -902   3528  A    C  
ATOM   1796  C   SER A 242      44.994 -33.658  15.260  1.00124.71      A    C  
ANISOU 1796  C   SER A 242    20715  10498  16172  -2766  -1045   3779  A    C  
ATOM   1797  O   SER A 242      44.933 -33.814  16.475  1.00131.24      A    O  
ANISOU 1797  O   SER A 242    21777  11279  16811  -2861   -936   4022  A    O  
ATOM   1798  CB  SER A 242      42.576 -33.862  14.513  1.00121.38      A    C  
ANISOU 1798  CB  SER A 242    20041   9920  16159  -3281   -708   3535  A    C  
ATOM   1799  OG  SER A 242      42.468 -34.701  13.373  1.00116.65      A    O  
ANISOU 1799  OG  SER A 242    19391   9085  15846  -3236   -817   3365  A    O  
ATOM   1800  N   GLN A 243      46.045 -34.014  14.531  1.00121.64      A    N  
ANISOU 1800  N   GLN A 243    20326  10065  15826  -2470  -1291   3714  A    N  
ATOM   1801  CA  GLN A 243      47.219 -34.651  15.112  1.00129.72      A    C  
ANISOU 1801  CA  GLN A 243    21627  10975  16688  -2227  -1461   3924  A    C  
ATOM   1802  C   GLN A 243      48.246 -33.622  15.590  1.00124.82      A    C  
ANISOU 1802  C   GLN A 243    20932  10712  15780  -2028  -1573   3963  A    C  
ATOM   1803  O   GLN A 243      49.015 -33.879  16.517  1.00123.47      A    O  
ANISOU 1803  O   GLN A 243    20996  10526  15390  -1897  -1649   4180  A    O  
ATOM   1804  CB  GLN A 243      47.846 -35.582  14.077  1.00137.27      A    C  
ANISOU 1804  CB  GLN A 243    22612  11708  17838  -1995  -1674   3821  A    C  
ATOM   1805  CG  GLN A 243      48.882 -36.532  14.626  1.00143.42      A    C  
ANISOU 1805  CG  GLN A 243    23715  12275  18503  -1759  -1838   4041  A    C  
ATOM   1806  CD  GLN A 243      49.127 -37.701  13.696  1.00145.58      A    C  
ANISOU 1806  CD  GLN A 243    24073  12221  19019  -1610  -1986   3953  A    C  
ATOM   1807  NE2 GLN A 243      49.911 -38.671  14.157  1.00153.36      A    N  
ANISOU 1807  NE2 GLN A 243    25371  12963  19938  -1412  -2119   4148  A    N  
ATOM   1808  OE1 GLN A 243      48.610 -37.737  12.579  1.00136.79      A    O  
ANISOU 1808  OE1 GLN A 243    22751  11073  18147  -1664  -1986   3707  A    O  
ATOM   1809  N   LEU A 244      48.245 -32.457  14.946  1.00126.47      A    N  
ANISOU 1809  N   LEU A 244    20816  11241  15996  -2006  -1583   3748  A    N  
ATOM   1810  CA  LEU A 244      49.165 -31.372  15.275  1.00123.61      A    C  
ANISOU 1810  CA  LEU A 244    20342  11229  15397  -1843  -1681   3745  A    C  
ATOM   1811  C   LEU A 244      48.505 -30.317  16.170  1.00128.89      A    C  
ANISOU 1811  C   LEU A 244    20954  12126  15894  -2061  -1483   3784  A    C  
ATOM   1812  O   LEU A 244      49.170 -29.683  16.991  1.00132.26      A    O  
ANISOU 1812  O   LEU A 244    21424  12763  16067  -1981  -1528   3879  A    O  
ATOM   1813  CB  LEU A 244      49.686 -30.712  13.995  1.00115.51      A    C  
ANISOU 1813  CB  LEU A 244    19002  10411  14476  -1664  -1822   3494  A    C  
ATOM   1814  CG  LEU A 244      50.806 -29.678  14.165  1.00111.72      A    C  
ANISOU 1814  CG  LEU A 244    18391  10270  13786  -1471  -1955   3475  A    C  
ATOM   1815  CD1 LEU A 244      52.169 -30.354  14.074  1.00113.79      A    C  
ANISOU 1815  CD1 LEU A 244    18768  10482  13986  -1156  -2203   3549  A    C  
ATOM   1816  CD2 LEU A 244      50.701 -28.542  13.148  1.00 94.47      A    C  
ANISOU 1816  CD2 LEU A 244    15855   8351  11688  -1462  -1949   3230  A    C  
ATOM   1817  N   CYS A 245      47.196 -30.137  16.017  1.00127.52      A    N  
ANISOU 1817  N   CYS A 245    20678  11915  15857  -2333  -1268   3699  A    N  
ATOM   1818  CA  CYS A 245      46.479 -29.098  16.754  1.00125.99      A    C  
ANISOU 1818  CA  CYS A 245    20401  11946  15522  -2535  -1071   3701  A    C  
ATOM   1819  C   CYS A 245      45.444 -29.642  17.745  1.00131.89      A    C  
ANISOU 1819  C   CYS A 245    21356  12519  16237  -2809   -836   3879  A    C  
ATOM   1820  O   CYS A 245      44.614 -28.892  18.259  1.00130.19      A    O  
ANISOU 1820  O   CYS A 245    21056  12463  15946  -3009   -638   3859  A    O  
ATOM   1821  CB  CYS A 245      45.807 -28.132  15.776  1.00120.27      A    C  
ANISOU 1821  CB  CYS A 245    19331  11414  14951  -2612  -1002   3433  A    C  
ATOM   1822  SG  CYS A 245      46.910 -27.511  14.491  1.00130.65      A    S  
ANISOU 1822  SG  CYS A 245    20391  12924  16326  -2313  -1247   3225  A    S  
ATOM   1823  N   GLY A 246      45.495 -30.943  18.013  1.00140.52      A    N  
ANISOU 1823  N   GLY A 246    22722  13283  17385  -2816   -852   4054  A    N  
ATOM   1824  CA  GLY A 246      44.564 -31.563  18.941  1.00143.90      A    C  
ANISOU 1824  CA  GLY A 246    23368  13517  17789  -3078   -624   4247  A    C  
ATOM   1825  C   GLY A 246      43.289 -32.017  18.259  1.00140.52      A    C  
ANISOU 1825  C   GLY A 246    22824  12903  17664  -3333   -459   4118  A    C  
ATOM   1826  O   GLY A 246      43.134 -31.856  17.053  1.00135.07      A    O  
ANISOU 1826  O   GLY A 246    21888  12238  17194  -3291   -533   3873  A    O  
ATOM   1827  N   SER A 247      42.373 -32.593  19.025  1.00145.34      A    N  
ANISOU 1827  N   SER A 247    23606  13334  18282  -3599   -233   4281  A    N  
ATOM   1828  CA  SER A 247      41.120 -33.066  18.453  1.00149.73      A    C  
ANISOU 1828  CA  SER A 247    24048  13711  19131  -3870    -65   4161  A    C  
ATOM   1829  C   SER A 247      40.146 -31.912  18.331  1.00145.29      A    C  
ANISOU 1829  C   SER A 247    23172  13452  18578  -4049    113   3972  A    C  
ATOM   1830  O   SER A 247      40.312 -30.875  18.982  1.00139.87      A    O  
ANISOU 1830  O   SER A 247    22433  13064  17648  -4015    158   3997  A    O  
ATOM   1831  CB  SER A 247      40.511 -34.183  19.304  1.00155.36      A    C  
ANISOU 1831  CB  SER A 247    25066  14096  19867  -4102    120   4416  A    C  
ATOM   1832  OG  SER A 247      41.356 -35.319  19.329  1.00155.52      A    O  
ANISOU 1832  OG  SER A 247    25385  13797  19910  -3930    -47   4582  A    O  
ATOM   1833  N   ILE A 248      39.138 -32.089  17.486  1.00143.66      A    N  
ANISOU 1833  N   ILE A 248    22758  13172  18655  -4229    205   3772  A    N  
ATOM   1834  CA  ILE A 248      38.109 -31.074  17.340  1.00139.17      A    C  
ANISOU 1834  CA  ILE A 248    21888  12875  18115  -4402    381   3588  A    C  
ATOM   1835  C   ILE A 248      36.974 -31.337  18.321  1.00145.52      A    C  
ANISOU 1835  C   ILE A 248    22782  13618  18892  -4736    684   3733  A    C  
ATOM   1836  O   ILE A 248      36.110 -32.181  18.088  1.00149.71      A    O  
ANISOU 1836  O   ILE A 248    23315  13911  19656  -4965    807   3716  A    O  
ATOM   1837  CB  ILE A 248      37.555 -30.986  15.901  1.00126.04      A    C  
ANISOU 1837  CB  ILE A 248    19911  11226  16754  -4412    324   3271  A    C  
ATOM   1838  CG1 ILE A 248      38.610 -30.440  14.935  1.00101.35      A    C  
ANISOU 1838  CG1 ILE A 248    16645   8248  13617  -4083     55   3111  A    C  
ATOM   1839  CG2 ILE A 248      36.332 -30.092  15.864  1.00125.05      A    C  
ANISOU 1839  CG2 ILE A 248    19501  11346  16667  -4620    535   3106  A    C  
ATOM   1840  CD1 ILE A 248      39.513 -31.495  14.331  1.00 94.10      A    C  
ANISOU 1840  CD1 ILE A 248    15885   7056  12813  -3886   -172   3138  A    C  
ATOM   1841  N   THR A 249      37.000 -30.608  19.428  1.00145.80      A    N  
ANISOU 1841  N   THR A 249    22888  13873  18637  -4762    805   3871  A    N  
ATOM   1842  CA  THR A 249      35.988 -30.718  20.460  1.00145.50      A    C  
ANISOU 1842  CA  THR A 249    22930  13834  18518  -5057   1105   4020  A    C  
ATOM   1843  C   THR A 249      35.407 -29.330  20.678  1.00142.06      A    C  
ANISOU 1843  C   THR A 249    22235  13788  17954  -5106   1238   3870  A    C  
ATOM   1844  O   THR A 249      36.098 -28.333  20.491  1.00132.05      A    O  
ANISOU 1844  O   THR A 249    20858  12767  16549  -4885   1091   3766  A    O  
ATOM   1845  CB  THR A 249      36.603 -31.222  21.771  1.00144.51      A    C  
ANISOU 1845  CB  THR A 249    23192  13600  18114  -5026   1136   4367  A    C  
ATOM   1846  CG2 THR A 249      37.272 -32.570  21.562  1.00144.26      A    C  
ANISOU 1846  CG2 THR A 249    23439  13177  18198  -4936    984   4522  A    C  
ATOM   1847  OG1 THR A 249      37.590 -30.287  22.216  1.00142.43      A    O  
ANISOU 1847  OG1 THR A 249    22954  13609  17556  -4775    994   4392  A    O  
ATOM   1848  N   PRO A 250      34.127 -29.259  21.055  1.00145.18      A    N  
ANISOU 1848  N   PRO A 250    22525  14236  18402  -5398   1518   3852  A    N  
ATOM   1849  CA  PRO A 250      33.477 -27.977  21.340  1.00143.62      A    C  
ANISOU 1849  CA  PRO A 250    22090  14400  18078  -5453   1668   3714  A    C  
ATOM   1850  C   PRO A 250      34.072 -27.249  22.548  1.00142.27      A    C  
ANISOU 1850  C   PRO A 250    22090  14442  17524  -5346   1693   3881  A    C  
ATOM   1851  O   PRO A 250      33.719 -26.096  22.789  1.00135.31      A    O  
ANISOU 1851  O   PRO A 250    21032  13867  16514  -5342   1781   3759  A    O  
ATOM   1852  CB  PRO A 250      32.025 -28.376  21.614  1.00146.74      A    C  
ANISOU 1852  CB  PRO A 250    22395  14746  18613  -5805   1974   3713  A    C  
ATOM   1853  CG  PRO A 250      31.848 -29.656  20.883  1.00148.55      A    C  
ANISOU 1853  CG  PRO A 250    22673  14616  19153  -5910   1923   3709  A    C  
ATOM   1854  CD  PRO A 250      33.163 -30.368  21.010  1.00148.13      A    C  
ANISOU 1854  CD  PRO A 250    22943  14329  19012  -5692   1697   3907  A    C  
ATOM   1855  N   GLU A 251      34.952 -27.904  23.298  1.00153.13      A    N  
ANISOU 1855  N   GLU A 251    23805  15661  18718  -5254   1613   4149  A    N  
ATOM   1856  CA  GLU A 251      35.651 -27.224  24.386  1.00162.98      A    C  
ANISOU 1856  CA  GLU A 251    25213  17118  19592  -5116   1592   4291  A    C  
ATOM   1857  C   GLU A 251      36.763 -26.359  23.800  1.00157.82      A    C  
ANISOU 1857  C   GLU A 251    24448  16639  18879  -4811   1311   4135  A    C  
ATOM   1858  O   GLU A 251      37.105 -25.302  24.335  1.00151.66      A    O  
ANISOU 1858  O   GLU A 251    23632  16133  17858  -4709   1294   4100  A    O  
ATOM   1859  CB  GLU A 251      36.226 -28.226  25.392  1.00174.35      A    C  
ANISOU 1859  CB  GLU A 251    27057  18343  20845  -5104   1593   4634  A    C  
ATOM   1860  CG  GLU A 251      37.277 -29.163  24.818  1.00182.11      A    C  
ANISOU 1860  CG  GLU A 251    28211  19043  21939  -4906   1327   4710  A    C  
ATOM   1861  CD  GLU A 251      37.966 -29.999  25.880  1.00189.58      A    C  
ANISOU 1861  CD  GLU A 251    29565  19817  22651  -4839   1302   5052  A    C  
ATOM   1862  OE1 GLU A 251      37.861 -31.246  25.825  1.00191.03      A    O  
ANISOU 1862  OE1 GLU A 251    29954  19650  22979  -4923   1327   5214  A    O  
ATOM   1863  OE2 GLU A 251      38.612 -29.406  26.769  1.00190.22      A    O1-
ANISOU 1863  OE2 GLU A 251    29765  20110  22400  -4696   1255   5155  A    O1-
ATOM   1864  N   VAL A 252      37.312 -26.830  22.685  1.00153.94      A    N  
ANISOU 1864  N   VAL A 252    23897  15980  18612  -4673   1095   4036  A    N  
ATOM   1865  CA  VAL A 252      38.366 -26.139  21.958  1.00141.92      A    C  
ANISOU 1865  CA  VAL A 252    22252  14593  17079  -4392    828   3885  A    C  
ATOM   1866  C   VAL A 252      37.737 -25.246  20.890  1.00140.61      A    C  
ANISOU 1866  C   VAL A 252    21717  14601  17107  -4409    844   3577  A    C  
ATOM   1867  O   VAL A 252      38.026 -24.049  20.804  1.00135.36      A    O  
ANISOU 1867  O   VAL A 252    20897  14202  16333  -4291    790   3442  A    O  
ATOM   1868  CB  VAL A 252      39.309 -27.165  21.295  1.00130.69      A    C  
ANISOU 1868  CB  VAL A 252    20963  12903  15789  -4216    588   3944  A    C  
ATOM   1869  CG1 VAL A 252      40.326 -26.483  20.431  1.00117.01      A    C  
ANISOU 1869  CG1 VAL A 252    19069  11318  14073  -3942    330   3774  A    C  
ATOM   1870  CG2 VAL A 252      39.998 -28.013  22.353  1.00136.31      A    C  
ANISOU 1870  CG2 VAL A 252    22051  13449  16293  -4163    553   4255  A    C  
ATOM   1871  N   TRP A 253      36.858 -25.840  20.093  1.00141.94      A    N  
ANISOU 1871  N   TRP A 253    21752  14614  17565  -4560    921   3466  A    N  
ATOM   1872  CA  TRP A 253      36.186 -25.138  19.005  1.00140.33      A    C  
ANISOU 1872  CA  TRP A 253    21201  14553  17563  -4573    932   3175  A    C  
ATOM   1873  C   TRP A 253      34.669 -25.178  19.193  1.00142.50      A    C  
ANISOU 1873  C   TRP A 253    21339  14854  17950  -4868   1213   3112  A    C  
ATOM   1874  O   TRP A 253      33.989 -26.040  18.636  1.00147.01      A    O  
ANISOU 1874  O   TRP A 253    21856  15228  18774  -5020   1266   3062  A    O  
ATOM   1875  CB  TRP A 253      36.578 -25.779  17.670  1.00137.71      A    C  
ANISOU 1875  CB  TRP A 253    20788  14042  17494  -4447    726   3047  A    C  
ATOM   1876  CG  TRP A 253      35.900 -25.210  16.451  1.00133.24      A    C  
ANISOU 1876  CG  TRP A 253    19879  13600  17147  -4444    719   2751  A    C  
ATOM   1877  CD1 TRP A 253      34.876 -24.298  16.413  1.00136.50      A    C  
ANISOU 1877  CD1 TRP A 253    20050  14239  17575  -4561    889   2593  A    C  
ATOM   1878  CD2 TRP A 253      36.203 -25.525  15.090  1.00123.75      A    C  
ANISOU 1878  CD2 TRP A 253    18540  12310  16170  -4300    529   2578  A    C  
ATOM   1879  CE2 TRP A 253      35.323 -24.772  14.278  1.00126.53      A    C  
ANISOU 1879  CE2 TRP A 253    18572  12847  16657  -4337    592   2323  A    C  
ATOM   1880  CE3 TRP A 253      37.132 -26.371  14.477  1.00116.35      A    C  
ANISOU 1880  CE3 TRP A 253    17720  11165  15323  -4129    310   2609  A    C  
ATOM   1881  NE1 TRP A 253      34.526 -24.029  15.108  1.00129.23      A    N  
ANISOU 1881  NE1 TRP A 253    18854  13375  16870  -4494    810   2337  A    N  
ATOM   1882  CZ2 TRP A 253      35.344 -24.845  12.887  1.00122.73      A    C  
ANISOU 1882  CZ2 TRP A 253    17892  12351  16387  -4213    443   2107  A    C  
ATOM   1883  CZ3 TRP A 253      37.154 -26.442  13.096  1.00119.06      A    C  
ANISOU 1883  CZ3 TRP A 253    17862  11495  15881  -4010    167   2387  A    C  
ATOM   1884  CH2 TRP A 253      36.264 -25.687  12.316  1.00121.97      A    C  
ANISOU 1884  CH2 TRP A 253    17919  12054  16371  -4054    235   2141  A    C  
ATOM   1885  N   PRO A 254      34.132 -24.239  19.985  1.00134.80      A    N  
ANISOU 1885  N   PRO A 254    20299  14129  16788  -4950   1392   3105  A    N  
ATOM   1886  CA  PRO A 254      32.698 -24.198  20.290  1.00130.73      A    C  
ANISOU 1886  CA  PRO A 254    19645  13680  16345  -5225   1676   3052  A    C  
ATOM   1887  C   PRO A 254      31.814 -24.224  19.046  1.00132.27      A    C  
ANISOU 1887  C   PRO A 254    19526  13872  16858  -5297   1687   2787  A    C  
ATOM   1888  O   PRO A 254      32.016 -23.422  18.139  1.00130.17      A    O  
ANISOU 1888  O   PRO A 254    19046  13757  16656  -5121   1548   2575  A    O  
ATOM   1889  CB  PRO A 254      32.544 -22.868  21.028  1.00123.83      A    C  
ANISOU 1889  CB  PRO A 254    18699  13134  15218  -5187   1782   3009  A    C  
ATOM   1890  CG  PRO A 254      33.861 -22.672  21.694  1.00126.87      A    C  
ANISOU 1890  CG  PRO A 254    19331  13539  15337  -4987   1620   3175  A    C  
ATOM   1891  CD  PRO A 254      34.882 -23.207  20.722  1.00129.99      A    C  
ANISOU 1891  CD  PRO A 254    19761  13752  15877  -4790   1339   3154  A    C  
ATOM   1892  N   ASN A 255      30.855 -25.146  19.018  1.00143.31      A    N  
ANISOU 1892  N   ASN A 255    20903  15098  18450  -5555   1849   2804  A    N  
ATOM   1893  CA  ASN A 255      29.861 -25.251  17.942  1.00148.58      A    C  
ANISOU 1893  CA  ASN A 255    21263  15770  19420  -5663   1885   2549  A    C  
ATOM   1894  C   ASN A 255      30.296 -26.047  16.710  1.00143.03      A    C  
ANISOU 1894  C   ASN A 255    20534  14836  18976  -5561   1657   2443  A    C  
ATOM   1895  O   ASN A 255      29.681 -25.939  15.648  1.00138.15      A    O  
ANISOU 1895  O   ASN A 255    19640  14267  18583  -5571   1622   2191  A    O  
ATOM   1896  CB  ASN A 255      29.315 -23.873  17.531  1.00149.17      A    C  
ANISOU 1896  CB  ASN A 255    21019  16189  19470  -5581   1921   2300  A    C  
ATOM   1897  CG  ASN A 255      27.966 -23.563  18.166  1.00152.96      A    C  
ANISOU 1897  CG  ASN A 255    21346  16836  19935  -5833   2224   2260  A    C  
ATOM   1898  ND2 ASN A 255      26.983 -23.220  17.338  1.00151.79      A    N  
ANISOU 1898  ND2 ASN A 255    20866  16821  19988  -5889   2274   1998  A    N  
ATOM   1899  OD1 ASN A 255      27.812 -23.631  19.385  1.00154.38      A    O  
ANISOU 1899  OD1 ASN A 255    21700  17039  19918  -5966   2409   2459  A    O  
ATOM   1900  N   VAL A 256      31.348 -26.844  16.855  1.00140.20      A    N  
ANISOU 1900  N   VAL A 256    20460  14234  18575  -5452   1501   2628  A    N  
ATOM   1901  CA  VAL A 256      31.730 -27.771  15.799  1.00141.41      A    C  
ANISOU 1901  CA  VAL A 256    20626  14130  18972  -5375   1304   2549  A    C  
ATOM   1902  C   VAL A 256      30.651 -28.829  15.600  1.00165.85      A    C  
ANISOU 1902  C   VAL A 256    23678  16997  22340  -5673   1451   2510  A    C  
ATOM   1903  O   VAL A 256      30.346 -29.221  14.470  1.00170.75      A    O  
ANISOU 1903  O   VAL A 256    24124  17529  23225  -5671   1351   2296  A    O  
ATOM   1904  CB  VAL A 256      33.040 -28.492  16.120  1.00127.02      A    C  
ANISOU 1904  CB  VAL A 256    19140  12080  17042  -5205   1125   2775  A    C  
ATOM   1905  CG1 VAL A 256      34.169 -27.820  15.418  1.00121.58      A    C  
ANISOU 1905  CG1 VAL A 256    18390  11528  16278  -4868    863   2676  A    C  
ATOM   1906  CG2 VAL A 256      33.273 -28.554  17.627  1.00122.81      A    C  
ANISOU 1906  CG2 VAL A 256    18894  11538  16230  -5283   1266   3078  A    C  
ATOM   1907  N   ASP A 257      30.082 -29.297  16.709  1.00180.78      A    N  
ANISOU 1907  N   ASP A 257    25730  18796  24162  -5933   1692   2718  A    N  
ATOM   1908  CA  ASP A 257      29.028 -30.308  16.669  1.00184.01      A    C  
ANISOU 1908  CA  ASP A 257    26111  18980  24824  -6259   1866   2709  A    C  
ATOM   1909  C   ASP A 257      27.898 -29.910  15.716  1.00182.03      A    C  
ANISOU 1909  C   ASP A 257    25452  18899  24811  -6368   1921   2376  A    C  
ATOM   1910  O   ASP A 257      27.191 -30.764  15.181  1.00185.79      A    O  
ANISOU 1910  O   ASP A 257    25840  19181  25572  -6569   1961   2269  A    O  
ATOM   1911  CB  ASP A 257      28.496 -30.626  18.083  1.00185.83      A    C  
ANISOU 1911  CB  ASP A 257    26539  19163  24905  -6529   2159   2982  A    C  
ATOM   1912  CG  ASP A 257      28.296 -29.378  18.952  1.00184.72      A    C  
ANISOU 1912  CG  ASP A 257    26323  19395  24466  -6501   2309   3016  A    C  
ATOM   1913  OD1 ASP A 257      28.279 -28.248  18.419  1.00185.76      A    O  
ANISOU 1913  OD1 ASP A 257    26199  19823  24557  -6333   2230   2796  A    O  
ATOM   1914  OD2 ASP A 257      28.147 -29.538  20.183  1.00179.29      A    O1-
ANISOU 1914  OD2 ASP A 257    25844  18698  23580  -6645   2511   3268  A    O1-
ATOM   1915  N   ASN A 258      27.753 -28.608  15.492  1.00171.97      A    N  
ANISOU 1915  N   ASN A 258    23934  17986  23421  -6224   1911   2209  A    N  
ATOM   1916  CA  ASN A 258      26.709 -28.081  14.624  1.00163.62      A    C  
ANISOU 1916  CA  ASN A 258    22482  17136  22549  -6285   1955   1894  A    C  
ATOM   1917  C   ASN A 258      26.831 -28.524  13.161  1.00149.65      A    C  
ANISOU 1917  C   ASN A 258    20560  15250  21050  -6167   1724   1651  A    C  
ATOM   1918  O   ASN A 258      25.902 -28.345  12.372  1.00140.72      A    O  
ANISOU 1918  O   ASN A 258    19112  14242  20113  -6242   1750   1384  A    O  
ATOM   1919  CB  ASN A 258      26.681 -26.552  14.713  1.00164.40      A    C  
ANISOU 1919  CB  ASN A 258    22396  17628  22442  -6108   1971   1788  A    C  
ATOM   1920  CG  ASN A 258      25.453 -26.031  15.431  1.00164.53      A    C  
ANISOU 1920  CG  ASN A 258    22238  17868  22406  -6339   2266   1757  A    C  
ATOM   1921  ND2 ASN A 258      25.393 -24.716  15.626  1.00158.90      A    N  
ANISOU 1921  ND2 ASN A 258    21390  17480  21505  -6195   2299   1678  A    N  
ATOM   1922  OD1 ASN A 258      24.564 -26.800  15.798  1.00169.29      A    O  
ANISOU 1922  OD1 ASN A 258    22826  18353  23144  -6646   2467   1800  A    O  
ATOM   1923  N   TYR A 259      27.976 -29.094  12.798  1.00143.55      A    N  
ANISOU 1923  N   TYR A 259    20006  14256  20281  -5970   1494   1733  A    N  
ATOM   1924  CA  TYR A 259      28.197 -29.510  11.418  1.00144.58      A    C  
ANISOU 1924  CA  TYR A 259    20012  14283  20640  -5826   1263   1506  A    C  
ATOM   1925  C   TYR A 259      27.833 -30.969  11.256  1.00152.66      A    C  
ANISOU 1925  C   TYR A 259    21146  14930  21926  -6053   1284   1523  A    C  
ATOM   1926  O   TYR A 259      28.109 -31.784  12.133  1.00157.43      A    O  
ANISOU 1926  O   TYR A 259    22057  15271  22487  -6184   1364   1788  A    O  
ATOM   1927  CB  TYR A 259      29.654 -29.309  11.000  1.00146.80      A    C  
ANISOU 1927  CB  TYR A 259    20442  14545  20791  -5468    993   1557  A    C  
ATOM   1928  CG  TYR A 259      30.147 -27.875  11.008  1.00144.57      A    C  
ANISOU 1928  CG  TYR A 259    20051  14607  20271  -5224    938   1522  A    C  
ATOM   1929  CD1 TYR A 259      29.258 -26.798  11.030  1.00141.63      A    C  
ANISOU 1929  CD1 TYR A 259    19409  14549  19855  -5278   1080   1377  A    C  
ATOM   1930  CD2 TYR A 259      31.507 -27.602  10.983  1.00139.21      A    C  
ANISOU 1930  CD2 TYR A 259    19538  13935  19420  -4937    742   1630  A    C  
ATOM   1931  CE1 TYR A 259      29.719 -25.493  11.038  1.00134.51      A    C  
ANISOU 1931  CE1 TYR A 259    18427  13933  18748  -5057   1030   1347  A    C  
ATOM   1932  CE2 TYR A 259      31.974 -26.310  10.986  1.00139.70      A    C  
ANISOU 1932  CE2 TYR A 259    19506  14291  19282  -4733    694   1598  A    C  
ATOM   1933  CZ  TYR A 259      31.085 -25.258  11.012  1.00137.96      A    C  
ANISOU 1933  CZ  TYR A 259    19038  14355  19027  -4794    838   1459  A    C  
ATOM   1934  OH  TYR A 259      31.588 -23.973  11.014  1.00132.66      A    O  
ANISOU 1934  OH  TYR A 259    18294  13948  18164  -4588    786   1431  A    O  
ATOM   1935  N   GLU A 260      27.221 -31.303  10.127  1.00162.22      A    N  
ANISOU 1935  N   GLU A 260    22115  16112  23410  -6094   1206   1239  A    N  
ATOM   1936  CA  GLU A 260      26.764 -32.668   9.902  1.00174.43      A    C  
ANISOU 1936  CA  GLU A 260    23734  17300  25240  -6334   1228   1212  A    C  
ATOM   1937  C   GLU A 260      27.930 -33.610   9.612  1.00175.50      A    C  
ANISOU 1937  C   GLU A 260    24174  17095  25413  -6155   1004   1321  A    C  
ATOM   1938  O   GLU A 260      27.944 -34.760  10.062  1.00182.45      A    O  
ANISOU 1938  O   GLU A 260    25307  17611  26405  -6338   1059   1485  A    O  
ATOM   1939  CB  GLU A 260      25.710 -32.725   8.785  1.00181.13      A    C  
ANISOU 1939  CB  GLU A 260    24213  18239  26371  -6437   1207    848  A    C  
ATOM   1940  CG  GLU A 260      26.100 -32.027   7.482  1.00183.13      A    C  
ANISOU 1940  CG  GLU A 260    24237  18716  26628  -6099    956    574  A    C  
ATOM   1941  CD  GLU A 260      25.027 -32.160   6.407  1.00181.39      A    C  
ANISOU 1941  CD  GLU A 260    23660  18582  26680  -6202    930    214  A    C  
ATOM   1942  OE1 GLU A 260      24.083 -32.954   6.609  1.00180.48      A    O  
ANISOU 1942  OE1 GLU A 260    23493  18298  26783  -6541   1080    170  A    O  
ATOM   1943  OE2 GLU A 260      25.127 -31.472   5.365  1.00177.74      A    O1-
ANISOU 1943  OE2 GLU A 260    22967  18357  26209  -5947    762    -23  A    O1-
ATOM   1944  N   LEU A 261      28.912 -33.115   8.868  1.00162.95      A    N  
ANISOU 1944  N   LEU A 261    22562  15625  23728  -5793    756   1236  A    N  
ATOM   1945  CA  LEU A 261      30.066 -33.928   8.515  1.00156.30      A    C  
ANISOU 1945  CA  LEU A 261    21977  14501  22908  -5581    528   1314  A    C  
ATOM   1946  C   LEU A 261      30.917 -34.170   9.761  1.00148.95      A    C  
ANISOU 1946  C   LEU A 261    21424  13422  21748  -5554    576   1687  A    C  
ATOM   1947  O   LEU A 261      31.890 -34.924   9.726  1.00147.96      A    O  
ANISOU 1947  O   LEU A 261    21565  13038  21617  -5397    414   1812  A    O  
ATOM   1948  CB  LEU A 261      30.872 -33.252   7.396  1.00152.71      A    C  
ANISOU 1948  CB  LEU A 261    21372  14256  22396  -5200    269   1124  A    C  
ATOM   1949  CG  LEU A 261      31.856 -34.096   6.580  1.00152.80      A    C  
ANISOU 1949  CG  LEU A 261    21532  14021  22505  -4963      5   1076  A    C  
ATOM   1950  CD1 LEU A 261      33.219 -34.127   7.242  1.00155.73      A    C  
ANISOU 1950  CD1 LEU A 261    22213  14316  22640  -4740    -95   1355  A    C  
ATOM   1951  CD2 LEU A 261      31.328 -35.509   6.389  1.00153.66      A    C  
ANISOU 1951  CD2 LEU A 261    21747  13730  22906  -5192     20   1026  A    C  
ATOM   1952  N   TYR A 262      30.527 -33.541  10.868  1.00143.72      A    N  
ANISOU 1952  N   TYR A 262    20783  12932  20892  -5702    797   1859  A    N  
ATOM   1953  CA  TYR A 262      31.267 -33.654  12.122  1.00152.14      A    C  
ANISOU 1953  CA  TYR A 262    22192  13910  21705  -5676    856   2209  A    C  
ATOM   1954  C   TYR A 262      31.400 -35.100  12.576  1.00158.06      A    C  
ANISOU 1954  C   TYR A 262    23276  14207  22572  -5827    884   2418  A    C  
ATOM   1955  O   TYR A 262      32.501 -35.656  12.585  1.00156.84      A    O  
ANISOU 1955  O   TYR A 262    23385  13847  22358  -5613    701   2555  A    O  
ATOM   1956  CB  TYR A 262      30.610 -32.813  13.220  1.00162.99      A    C  
ANISOU 1956  CB  TYR A 262    23513  15540  22876  -5853   1119   2330  A    C  
ATOM   1957  CG  TYR A 262      31.252 -32.963  14.586  1.00173.11      A    C  
ANISOU 1957  CG  TYR A 262    25148  16740  23885  -5852   1200   2692  A    C  
ATOM   1958  CD1 TYR A 262      32.619 -32.787  14.758  1.00173.79      A    C  
ANISOU 1958  CD1 TYR A 262    25439  16834  23760  -5540    997   2829  A    C  
ATOM   1959  CD2 TYR A 262      30.489 -33.267  15.706  1.00181.06      A    C  
ANISOU 1959  CD2 TYR A 262    26276  17681  24837  -6158   1482   2892  A    C  
ATOM   1960  CE1 TYR A 262      33.210 -32.919  16.004  1.00177.14      A    C  
ANISOU 1960  CE1 TYR A 262    26181  17202  23923  -5523   1057   3150  A    C  
ATOM   1961  CE2 TYR A 262      31.071 -33.400  16.957  1.00184.17      A    C  
ANISOU 1961  CE2 TYR A 262    27000  18015  24961  -6142   1555   3225  A    C  
ATOM   1962  CZ  TYR A 262      32.431 -33.225  17.100  1.00182.05      A    C  
ANISOU 1962  CZ  TYR A 262    26931  17757  24482  -5819   1334   3348  A    C  
ATOM   1963  OH  TYR A 262      33.013 -33.358  18.341  1.00182.90      A    O  
ANISOU 1963  OH  TYR A 262    27363  17821  24311  -5789   1393   3670  A    O  
ATOM   1964  N   GLU A 263      30.276 -35.703  12.953  1.00166.63      A    N  
ANISOU 1964  N   GLU A 263    24349  15137  23827  -6195   1116   2442  A    N  
ATOM   1965  CA  GLU A 263      30.269 -37.088  13.411  1.00173.17      A    C  
ANISOU 1965  CA  GLU A 263    25496  15510  24789  -6382   1176   2647  A    C  
ATOM   1966  C   GLU A 263      30.360 -38.061  12.242  1.00171.65      A    C  
ANISOU 1966  C   GLU A 263    25288  15015  24916  -6340    981   2439  A    C  
ATOM   1967  O   GLU A 263      30.922 -39.149  12.370  1.00174.05      A    O  
ANISOU 1967  O   GLU A 263    25909  14930  25293  -6314    898   2595  A    O  
ATOM   1968  CB  GLU A 263      29.028 -37.375  14.260  1.00181.59      A    C  
ANISOU 1968  CB  GLU A 263    26553  16520  25924  -6810   1514   2757  A    C  
ATOM   1969  CG  GLU A 263      29.321 -37.530  15.751  1.00189.13      A    C  
ANISOU 1969  CG  GLU A 263    27854  17397  26611  -6890   1691   3160  A    C  
ATOM   1970  CD  GLU A 263      30.170 -38.757  16.065  1.00196.93      A    C  
ANISOU 1970  CD  GLU A 263    29274  17933  27615  -6822   1588   3418  A    C  
ATOM   1971  OE1 GLU A 263      30.022 -39.788  15.373  1.00200.32      A    O  
ANISOU 1971  OE1 GLU A 263    29751  18014  28347  -6906   1508   3318  A    O  
ATOM   1972  OE2 GLU A 263      30.982 -38.691  17.012  1.00197.44      A    O1-
ANISOU 1972  OE2 GLU A 263    29636  17993  27390  -6677   1582   3716  A    O1-
ATOM   1973  N   LYS A 264      29.812 -37.661  11.100  1.00169.17      A    N  
ANISOU 1973  N   LYS A 264    24611  14883  24783  -6320    901   2083  A    N  
ATOM   1974  CA  LYS A 264      29.877 -38.486   9.900  1.00173.51      A    C  
ANISOU 1974  CA  LYS A 264    25110  15193  25625  -6258    700   1841  A    C  
ATOM   1975  C   LYS A 264      31.310 -38.601   9.378  1.00178.13      A    C  
ANISOU 1975  C   LYS A 264    25863  15710  26108  -5842    398   1860  A    C  
ATOM   1976  O   LYS A 264      31.535 -38.759   8.179  1.00179.83      A    O  
ANISOU 1976  O   LYS A 264    25938  15915  26477  -5663    186   1594  A    O  
ATOM   1977  CB  LYS A 264      28.954 -37.924   8.813  1.00167.38      A    C  
ANISOU 1977  CB  LYS A 264    23887  14681  25027  -6308    681   1449  A    C  
ATOM   1978  CG  LYS A 264      28.899 -38.766   7.539  1.00165.84      A    C  
ANISOU 1978  CG  LYS A 264    23611  14261  25140  -6262    479   1162  A    C  
ATOM   1979  CD  LYS A 264      28.725 -40.253   7.863  1.00163.64      A    C  
ANISOU 1979  CD  LYS A 264    23620  13463  25093  -6512    536   1285  A    C  
ATOM   1980  CE  LYS A 264      28.763 -41.121   6.607  1.00150.73      A    C  
ANISOU 1980  CE  LYS A 264    21931  11582  23757  -6444    315    993  A    C  
ATOM   1981  NZ  LYS A 264      28.474 -42.550   6.906  1.00142.70      A    N1+
ANISOU 1981  NZ  LYS A 264    21180  10044  22997  -6722    386   1090  A    N1+
ATOM   1982  N   LEU A 265      32.284 -38.520  10.277  1.00177.57      A    N  
ANISOU 1982  N   LEU A 265    26087  15610  25770  -5682    378   2168  A    N  
ATOM   1983  CA  LEU A 265      33.680 -38.603   9.867  1.00172.86      A    C  
ANISOU 1983  CA  LEU A 265    25644  14975  25061  -5286    100   2200  A    C  
ATOM   1984  C   LEU A 265      34.611 -39.068  10.983  1.00168.36      A    C  
ANISOU 1984  C   LEU A 265    25486  14203  24278  -5194     97   2575  A    C  
ATOM   1985  O   LEU A 265      34.411 -38.766  12.162  1.00157.77      A    O  
ANISOU 1985  O   LEU A 265    24269  12934  22743  -5340    294   2824  A    O  
ATOM   1986  CB  LEU A 265      34.155 -37.270   9.270  1.00172.09      A    C  
ANISOU 1986  CB  LEU A 265    25272  15326  24788  -4998    -30   2033  A    C  
ATOM   1987  CG  LEU A 265      35.586 -37.225   8.718  1.00173.57      A    C  
ANISOU 1987  CG  LEU A 265    25551  15536  24862  -4580   -316   2028  A    C  
ATOM   1988  CD1 LEU A 265      35.688 -36.358   7.463  1.00165.44      A    C  
ANISOU 1988  CD1 LEU A 265    24174  14828  23855  -4359   -469   1715  A    C  
ATOM   1989  CD2 LEU A 265      36.564 -36.753   9.785  1.00175.46      A    C  
ANISOU 1989  CD2 LEU A 265    26010  15885  24772  -4422   -320   2328  A    C  
ATOM   1990  N   GLU A 266      35.631 -39.814  10.581  1.00177.41      A    N  
ANISOU 1990  N   GLU A 266    26843  15105  25459  -4936   -134   2606  A    N  
ATOM   1991  CA  GLU A 266      36.604 -40.364  11.504  1.00186.60      A    C  
ANISOU 1991  CA  GLU A 266    28405  16056  26437  -4799   -181   2941  A    C  
ATOM   1992  C   GLU A 266      37.525 -39.261  11.984  1.00193.41      A    C  
ANISOU 1992  C   GLU A 266    29248  17288  26949  -4534   -252   3056  A    C  
ATOM   1993  O   GLU A 266      38.243 -38.648  11.195  1.00192.34      A    O  
ANISOU 1993  O   GLU A 266    28938  17386  26757  -4240   -454   2885  A    O  
ATOM   1994  CB  GLU A 266      37.421 -41.453  10.809  1.00187.39      A    C  
ANISOU 1994  CB  GLU A 266    28702  15806  26692  -4570   -426   2897  A    C  
ATOM   1995  CG  GLU A 266      37.843 -42.600  11.709  1.00192.51      A    C  
ANISOU 1995  CG  GLU A 266    29805  16025  27316  -4598   -403   3225  A    C  
ATOM   1996  CD  GLU A 266      38.440 -43.751  10.922  1.00195.70      A    C  
ANISOU 1996  CD  GLU A 266    30382  16044  27929  -4409   -628   3136  A    C  
ATOM   1997  OE1 GLU A 266      39.345 -43.493  10.099  1.00191.92      A    O  
ANISOU 1997  OE1 GLU A 266    29800  15712  27408  -4055   -878   2975  A    O  
ATOM   1998  OE2 GLU A 266      38.003 -44.908  11.123  1.00198.29      A    O1-
ANISOU 1998  OE2 GLU A 266    30949  15924  28467  -4615   -552   3226  A    O1-
ATOM   1999  N   LEU A 267      37.490 -38.999  13.283  1.00204.83      A    N  
ANISOU 1999  N   LEU A 267    30871  18795  28160  -4645    -81   3343  A    N  
ATOM   2000  CA  LEU A 267      38.433 -38.074  13.894  1.00211.06      A    C  
ANISOU 2000  CA  LEU A 267    31695  19892  28606  -4401   -154   3481  A    C  
ATOM   2001  C   LEU A 267      38.851 -38.597  15.265  1.00213.81      A    C  
ANISOU 2001  C   LEU A 267    32440  20061  28739  -4425    -73   3864  A    C  
ATOM   2002  O   LEU A 267      38.013 -39.039  16.054  1.00218.39      A    O  
ANISOU 2002  O   LEU A 267    33159  20475  29344  -4731    166   4033  A    O  
ATOM   2003  CB  LEU A 267      37.842 -36.660  13.980  1.00214.82      A    C  
ANISOU 2003  CB  LEU A 267    31850  20813  28958  -4489    -20   3354  A    C  
ATOM   2004  CG  LEU A 267      36.428 -36.496  14.545  1.00223.00      A    C  
ANISOU 2004  CG  LEU A 267    32789  21888  30053  -4883    291   3369  A    C  
ATOM   2005  CD1 LEU A 267      36.424 -36.557  16.070  1.00230.20      A    C  
ANISOU 2005  CD1 LEU A 267    33982  22772  30712  -5010    478   3715  A    C  
ATOM   2006  CD2 LEU A 267      35.826 -35.186  14.067  1.00214.77      A    C  
ANISOU 2006  CD2 LEU A 267    31351  21260  28993  -4908    350   3118  A    C  
ATOM   2007  N   VAL A 268      40.152 -38.571  15.531  1.00205.61      A    N  
ANISOU 2007  N   VAL A 268    31578  19057  27486  -4098   -274   4002  A    N  
ATOM   2008  CA  VAL A 268      40.670 -39.033  16.810  1.00201.61      A    C  
ANISOU 2008  CA  VAL A 268    31452  18408  26743  -4066   -232   4364  A    C  
ATOM   2009  C   VAL A 268      39.986 -38.255  17.927  1.00193.08      A    C  
ANISOU 2009  C   VAL A 268    30349  17569  25443  -4297     30   4508  A    C  
ATOM   2010  O   VAL A 268      39.309 -37.260  17.674  1.00194.26      A    O  
ANISOU 2010  O   VAL A 268    30182  18027  25602  -4420    138   4317  A    O  
ATOM   2011  CB  VAL A 268      42.195 -38.847  16.897  1.00202.07      A    C  
ANISOU 2011  CB  VAL A 268    31625  18580  26572  -3653   -500   4446  A    C  
ATOM   2012  CG1 VAL A 268      42.765 -39.620  18.084  1.00205.18      A    C  
ANISOU 2012  CG1 VAL A 268    32452  18744  26764  -3588   -495   4816  A    C  
ATOM   2013  CG2 VAL A 268      42.851 -39.299  15.603  1.00199.67      A    C  
ANISOU 2013  CG2 VAL A 268    31233  18157  26475  -3398   -762   4226  A    C  
ATOM   2014  N   LYS A 269      40.153 -38.705  19.163  1.00181.08      A    N  
ANISOU 2014  N   LYS A 269    29170  15916  23718  -4345    132   4843  A    N  
ATOM   2015  CA  LYS A 269      39.507 -38.038  20.280  1.00172.06      A    C  
ANISOU 2015  CA  LYS A 269    28031  14995  22350  -4559    389   4992  A    C  
ATOM   2016  C   LYS A 269      40.493 -37.730  21.408  1.00170.51      A    C  
ANISOU 2016  C   LYS A 269    28079  14947  21759  -4341    321   5258  A    C  
ATOM   2017  O   LYS A 269      40.223 -36.876  22.250  1.00171.34      A    O  
ANISOU 2017  O   LYS A 269    28139  15344  21619  -4425    470   5329  A    O  
ATOM   2018  CB  LYS A 269      38.334 -38.881  20.789  1.00174.41      A    C  
ANISOU 2018  CB  LYS A 269    28477  14997  22795  -4945    677   5143  A    C  
ATOM   2019  CG  LYS A 269      37.381 -39.357  19.686  1.00166.89      A    C  
ANISOU 2019  CG  LYS A 269    27306  13851  22253  -5168    730   4883  A    C  
ATOM   2020  CD  LYS A 269      36.494 -40.507  20.171  1.00160.18      A    C  
ANISOU 2020  CD  LYS A 269    26686  12598  21576  -5514    965   5073  A    C  
ATOM   2021  CE  LYS A 269      35.703 -41.136  19.032  1.00150.16      A    C  
ANISOU 2021  CE  LYS A 269    25232  11090  20734  -5708    970   4807  A    C  
ATOM   2022  NZ  LYS A 269      34.893 -42.291  19.506  1.00150.56      A    N1+
ANISOU 2022  NZ  LYS A 269    25517  10721  20967  -6054   1195   4996  A    N1+
ATOM   2023  N   GLY A 270      41.637 -38.413  21.413  1.00168.81      A    N  
ANISOU 2023  N   GLY A 270    28117  14543  21482  -4051     88   5389  A    N  
ATOM   2024  CA  GLY A 270      42.647 -38.203  22.440  1.00169.11      A    C  
ANISOU 2024  CA  GLY A 270    28390  14715  21149  -3816    -10   5632  A    C  
ATOM   2025  C   GLY A 270      43.840 -37.357  22.011  1.00164.42      A    C  
ANISOU 2025  C   GLY A 270    27622  14438  20413  -3461   -289   5478  A    C  
ATOM   2026  O   GLY A 270      44.964 -37.581  22.460  1.00159.41      A    O  
ANISOU 2026  O   GLY A 270    27196  13802  19571  -3178   -477   5637  A    O  
ATOM   2027  N   GLN A 271      43.596 -36.368  21.155  1.00163.64      A    N  
ANISOU 2027  N   GLN A 271    27136  14620  20420  -3475   -312   5171  A    N  
ATOM   2028  CA  GLN A 271      44.676 -35.571  20.574  1.00155.51      A    C  
ANISOU 2028  CA  GLN A 271    25908  13875  19305  -3161   -567   4999  A    C  
ATOM   2029  C   GLN A 271      44.938 -34.247  21.292  1.00159.65      A    C  
ANISOU 2029  C   GLN A 271    26311  14825  19523  -3121   -539   4997  A    C  
ATOM   2030  O   GLN A 271      44.012 -33.489  21.582  1.00161.85      A    O  
ANISOU 2030  O   GLN A 271    26435  15289  19771  -3355   -325   4933  A    O  
ATOM   2031  CB  GLN A 271      44.420 -35.332  19.085  1.00143.66      A    C  
ANISOU 2031  CB  GLN A 271    24072  12406  18106  -3149   -646   4663  A    C  
ATOM   2032  CG  GLN A 271      45.002 -36.415  18.205  1.00141.86      A    C  
ANISOU 2032  CG  GLN A 271    23941  11867  18092  -2961   -851   4617  A    C  
ATOM   2033  CD  GLN A 271      46.378 -36.838  18.686  1.00147.18      A    C  
ANISOU 2033  CD  GLN A 271    24869  12494  18559  -2632  -1075   4807  A    C  
ATOM   2034  NE2 GLN A 271      47.333 -35.912  18.650  1.00144.10      A    N  
ANISOU 2034  NE2 GLN A 271    24327  12448  17976  -2392  -1238   4735  A    N  
ATOM   2035  OE1 GLN A 271      46.574 -37.975  19.110  1.00151.78      A    O  
ANISOU 2035  OE1 GLN A 271    25781  12736  19152  -2596  -1097   5021  A    O  
ATOM   2036  N   LYS A 272      46.212 -33.975  21.568  1.00159.24      A    N  
ANISOU 2036  N   LYS A 272    26325  14928  19249  -2820   -761   5056  A    N  
ATOM   2037  CA  LYS A 272      46.608 -32.754  22.266  1.00154.13      A    C  
ANISOU 2037  CA  LYS A 272    25581  14674  18307  -2757   -768   5049  A    C  
ATOM   2038  C   LYS A 272      47.486 -31.873  21.386  1.00148.41      A    C  
ANISOU 2038  C   LYS A 272    24566  14219  17604  -2525   -989   4806  A    C  
ATOM   2039  O   LYS A 272      48.295 -32.378  20.607  1.00148.72      A    O  
ANISOU 2039  O   LYS A 272    24595  14152  17761  -2297  -1206   4746  A    O  
ATOM   2040  CB  LYS A 272      47.325 -33.095  23.573  1.00155.63      A    C  
ANISOU 2040  CB  LYS A 272    26106  14858  18167  -2627   -818   5347  A    C  
ATOM   2041  CG  LYS A 272      46.425 -33.786  24.579  1.00160.12      A    C  
ANISOU 2041  CG  LYS A 272    26960  15215  18663  -2873   -566   5607  A    C  
ATOM   2042  CD  LYS A 272      47.176 -34.222  25.826  1.00159.84      A    C  
ANISOU 2042  CD  LYS A 272    27283  15155  18294  -2713   -630   5917  A    C  
ATOM   2043  CE  LYS A 272      46.212 -34.789  26.864  1.00157.16      A    C  
ANISOU 2043  CE  LYS A 272    27216  14640  17859  -2978   -345   6183  A    C  
ATOM   2044  NZ  LYS A 272      45.314 -35.838  26.291  1.00152.19      A    N1+
ANISOU 2044  NZ  LYS A 272    26655  13608  17563  -3199   -200   6206  A    N1+
ATOM   2045  N   ARG A 273      47.319 -30.559  21.521  1.00147.21      A    N  
ANISOU 2045  N   ARG A 273    24185  14411  17338  -2583   -927   4670  A    N  
ATOM   2046  CA  ARG A 273      47.983 -29.583  20.655  1.00153.73      A    C  
ANISOU 2046  CA  ARG A 273    24707  15501  18203  -2414  -1091   4429  A    C  
ATOM   2047  C   ARG A 273      49.502 -29.642  20.755  1.00143.80      A    C  
ANISOU 2047  C   ARG A 273    23517  14333  16786  -2090  -1367   4484  A    C  
ATOM   2048  O   ARG A 273      50.083 -29.171  21.730  1.00140.56      A    O  
ANISOU 2048  O   ARG A 273    23200  14113  16093  -2014  -1412   4592  A    O  
ATOM   2049  CB  ARG A 273      47.498 -28.162  20.975  1.00169.01      A    C  
ANISOU 2049  CB  ARG A 273    26431  17766  20018  -2550   -955   4305  A    C  
ATOM   2050  CG  ARG A 273      45.979 -27.988  20.909  1.00180.40      A    C  
ANISOU 2050  CG  ARG A 273    27774  19169  21601  -2861   -677   4234  A    C  
ATOM   2051  CD  ARG A 273      45.520 -26.687  21.568  1.00183.73      A    C  
ANISOU 2051  CD  ARG A 273    28069  19900  21840  -2983   -528   4170  A    C  
ATOM   2052  NE  ARG A 273      44.081 -26.680  21.839  1.00183.20      A    N  
ANISOU 2052  NE  ARG A 273    27974  19788  21846  -3279   -244   4167  A    N  
ATOM   2053  CZ  ARG A 273      43.486 -25.880  22.722  1.00180.88      A    C  
ANISOU 2053  CZ  ARG A 273    27665  19695  21367  -3424    -60   4183  A    C  
ATOM   2054  NH1 ARG A 273      44.203 -25.017  23.430  1.00179.50      A    N1+
ANISOU 2054  NH1 ARG A 273    27512  19770  20921  -3304   -137   4200  A    N1+
ATOM   2055  NH2 ARG A 273      42.173 -25.947  22.902  1.00178.54      A    N  
ANISOU 2055  NH2 ARG A 273    27327  19356  21155  -3688    200   4174  A    N  
ATOM   2056  N   LYS A 274      50.138 -30.210  19.734  1.00138.95      A    N  
ANISOU 2056  N   LYS A 274    22846  13596  16353  -1894  -1555   4395  A    N  
ATOM   2057  CA  LYS A 274      51.593 -30.326  19.702  1.00141.98      A    C  
ANISOU 2057  CA  LYS A 274    23264  14068  16616  -1571  -1825   4427  A    C  
ATOM   2058  C   LYS A 274      52.197 -29.333  18.708  1.00137.59      A    C  
ANISOU 2058  C   LYS A 274    22363  13787  16129  -1440  -1954   4176  A    C  
ATOM   2059  O   LYS A 274      53.275 -29.573  18.151  1.00130.77      A    O  
ANISOU 2059  O   LYS A 274    21448  12953  15287  -1177  -2176   4130  A    O  
ATOM   2060  CB  LYS A 274      52.019 -31.756  19.336  1.00147.08      A    C  
ANISOU 2060  CB  LYS A 274    24121  14375  17389  -1404  -1960   4528  A    C  
ATOM   2061  CG  LYS A 274      51.247 -32.864  20.058  1.00149.29      A    C  
ANISOU 2061  CG  LYS A 274    24735  14306  17683  -1569  -1806   4760  A    C  
ATOM   2062  CD  LYS A 274      52.139 -34.066  20.391  1.00150.13      A    C  
ANISOU 2062  CD  LYS A 274    25154  14166  17723  -1321  -1986   4966  A    C  
ATOM   2063  CE  LYS A 274      53.029 -33.807  21.621  1.00142.52      A    C  
ANISOU 2063  CE  LYS A 274    24363  13394  16396  -1157  -2085   5162  A    C  
ATOM   2064  NZ  LYS A 274      53.908 -34.964  21.975  1.00128.39      A    N1+
ANISOU 2064  NZ  LYS A 274    22884  11375  14524   -890  -2268   5369  A    N1+
ATOM   2065  N   VAL A 275      51.502 -28.218  18.493  1.00137.79      A    N  
ANISOU 2065  N   VAL A 275    22153  14014  16187  -1619  -1809   4018  A    N  
ATOM   2066  CA  VAL A 275      51.919 -27.241  17.491  1.00132.14      A    C  
ANISOU 2066  CA  VAL A 275    21111  13539  15559  -1526  -1896   3783  A    C  
ATOM   2067  C   VAL A 275      53.321 -26.721  17.790  1.00133.89      A    C  
ANISOU 2067  C   VAL A 275    21289  14002  15581  -1292  -2104   3795  A    C  
ATOM   2068  O   VAL A 275      54.195 -26.736  16.920  1.00130.99      A    O  
ANISOU 2068  O   VAL A 275    20775  13698  15296  -1083  -2282   3690  A    O  
ATOM   2069  CB  VAL A 275      50.942 -26.052  17.394  1.00125.40      A    C  
ANISOU 2069  CB  VAL A 275    20044  12867  14734  -1753  -1699   3636  A    C  
ATOM   2070  CG1 VAL A 275      51.052 -25.410  16.033  1.00113.08      A    C  
ANISOU 2070  CG1 VAL A 275    18171  11433  13361  -1681  -1756   3396  A    C  
ATOM   2071  CG2 VAL A 275      49.505 -26.499  17.654  1.00130.16      A    C  
ANISOU 2071  CG2 VAL A 275    20742  13276  15439  -2024  -1459   3683  A    C  
ATOM   2072  N   LYS A 276      53.532 -26.269  19.024  1.00134.30      A    N  
ANISOU 2072  N   LYS A 276    21461  14197  15368  -1328  -2082   3917  A    N  
ATOM   2073  CA  LYS A 276      54.834 -25.757  19.437  1.00130.48      A    C  
ANISOU 2073  CA  LYS A 276    20939  13958  14681  -1126  -2279   3925  A    C  
ATOM   2074  C   LYS A 276      55.852 -26.877  19.646  1.00136.37      A    C  
ANISOU 2074  C   LYS A 276    21885  14574  15355   -867  -2489   4077  A    C  
ATOM   2075  O   LYS A 276      57.037 -26.695  19.376  1.00140.26      A    O  
ANISOU 2075  O   LYS A 276    22267  15229  15798   -639  -2698   4022  A    O  
ATOM   2076  CB  LYS A 276      54.716 -24.909  20.706  1.00121.97      A    C  
ANISOU 2076  CB  LYS A 276    19927  13084  13332  -1243  -2196   3989  A    C  
ATOM   2077  CG  LYS A 276      54.146 -23.521  20.496  1.00108.65      A    C  
ANISOU 2077  CG  LYS A 276    17994  11612  11674  -1418  -2059   3803  A    C  
ATOM   2078  CD  LYS A 276      54.410 -22.622  21.702  1.00117.35      A    C  
ANISOU 2078  CD  LYS A 276    19141  12957  12489  -1461  -2049   3835  A    C  
ATOM   2079  CE  LYS A 276      54.092 -21.149  21.383  1.00126.13      A    C  
ANISOU 2079  CE  LYS A 276    19988  14295  13640  -1587  -1958   3624  A    C  
ATOM   2080  NZ  LYS A 276      54.907 -20.138  22.155  1.00119.84      A    N1+
ANISOU 2080  NZ  LYS A 276    19143  13779  12610  -1539  -2058   3579  A    N1+
ATOM   2081  N   ASP A 277      55.392 -28.031  20.121  1.00138.79      A    N  
ANISOU 2081  N   ASP A 277    22485  14587  15661   -901  -2431   4268  A    N  
ATOM   2082  CA  ASP A 277      56.281 -29.176  20.352  1.00149.21      A    C  
ANISOU 2082  CA  ASP A 277    24033  15744  16918   -647  -2622   4429  A    C  
ATOM   2083  C   ASP A 277      56.986 -29.663  19.080  1.00143.26      A    C  
ANISOU 2083  C   ASP A 277    23136  14922  16373   -420  -2803   4299  A    C  
ATOM   2084  O   ASP A 277      58.214 -29.754  19.038  1.00138.63      A    O  
ANISOU 2084  O   ASP A 277    22517  14461  15693   -149  -3027   4300  A    O  
ATOM   2085  CB  ASP A 277      55.524 -30.352  20.989  1.00156.42      A    C  
ANISOU 2085  CB  ASP A 277    25296  16307  17831   -752  -2497   4658  A    C  
ATOM   2086  CG  ASP A 277      55.013 -30.042  22.385  1.00158.30      A    C  
ANISOU 2086  CG  ASP A 277    25725  16614  17809   -922  -2342   4832  A    C  
ATOM   2087  OD1 ASP A 277      54.893 -28.845  22.727  1.00164.24      A    O  
ANISOU 2087  OD1 ASP A 277    26309  17659  18438  -1029  -2275   4733  A    O  
ATOM   2088  OD2 ASP A 277      54.725 -31.001  23.136  1.00153.83      A    O1-
ANISOU 2088  OD2 ASP A 277    25483  15804  17160   -947  -2281   5069  A    O1-
ATOM   2089  N   ARG A 278      56.205 -29.981  18.051  1.00138.76      A    N  
ANISOU 2089  N   ARG A 278    22476  14167  16081   -525  -2707   4180  A    N  
ATOM   2090  CA  ARG A 278      56.747 -30.613  16.852  1.00135.92      A    C  
ANISOU 2090  CA  ARG A 278    22020  13700  15925   -313  -2862   4065  A    C  
ATOM   2091  C   ARG A 278      57.679 -29.701  16.062  1.00125.95      A    C  
ANISOU 2091  C   ARG A 278    20429  12759  14669   -148  -3004   3869  A    C  
ATOM   2092  O   ARG A 278      58.535 -30.182  15.324  1.00121.58      A    O  
ANISOU 2092  O   ARG A 278    19812  12194  14191    106  -3185   3807  A    O  
ATOM   2093  CB  ARG A 278      55.622 -31.152  15.954  1.00142.93      A    C  
ANISOU 2093  CB  ARG A 278    22886  14320  17102   -479  -2722   3968  A    C  
ATOM   2094  CG  ARG A 278      55.574 -32.691  15.864  1.00152.61      A    C  
ANISOU 2094  CG  ARG A 278    24392  15147  18447   -386  -2778   4089  A    C  
ATOM   2095  CD  ARG A 278      54.368 -33.222  15.063  1.00159.67      A    C  
ANISOU 2095  CD  ARG A 278    25268  15768  19631   -589  -2629   3985  A    C  
ATOM   2096  NE  ARG A 278      54.418 -32.864  13.641  1.00164.91      A    N  
ANISOU 2096  NE  ARG A 278    25625  16538  20496   -516  -2686   3718  A    N  
ATOM   2097  CZ  ARG A 278      53.510 -33.221  12.731  1.00157.07      A    C  
ANISOU 2097  CZ  ARG A 278    24553  15367  19760   -645  -2598   3571  A    C  
ATOM   2098  NH1 ARG A 278      52.461 -33.959  13.080  1.00155.31      A    N1+
ANISOU 2098  NH1 ARG A 278    24525  14839  19647   -874  -2442   3659  A    N1+
ATOM   2099  NH2 ARG A 278      53.653 -32.839  11.465  1.00143.11      A    N  
ANISOU 2099  NH2 ARG A 278    22506  13733  18137   -547  -2664   3333  A    N  
ATOM   2100  N   LEU A 279      57.530 -28.392  16.238  1.00126.79      A    N  
ANISOU 2100  N   LEU A 279    20333  13149  14691   -288  -2919   3775  A    N  
ATOM   2101  CA  LEU A 279      58.265 -27.419  15.423  1.00129.14      A    C  
ANISOU 2101  CA  LEU A 279    20303  13742  15021   -182  -3014   3583  A    C  
ATOM   2102  C   LEU A 279      59.489 -26.753  16.064  1.00132.50      A    C  
ANISOU 2102  C   LEU A 279    20657  14467  15218    -34  -3171   3606  A    C  
ATOM   2103  O   LEU A 279      60.188 -25.977  15.400  1.00116.70      A    O  
ANISOU 2103  O   LEU A 279    18385  12710  13247     55  -3254   3456  A    O  
ATOM   2104  CB  LEU A 279      57.316 -26.342  14.905  1.00123.01      A    C  
ANISOU 2104  CB  LEU A 279    19303  13079  14356   -420  -2824   3422  A    C  
ATOM   2105  CG  LEU A 279      56.553 -26.770  13.655  1.00117.03      A    C  
ANISOU 2105  CG  LEU A 279    18448  12143  13873   -463  -2752   3290  A    C  
ATOM   2106  CD1 LEU A 279      55.535 -25.718  13.232  1.00 99.88      A    C  
ANISOU 2106  CD1 LEU A 279    16074  10082  11794   -694  -2560   3145  A    C  
ATOM   2107  CD2 LEU A 279      57.543 -27.053  12.535  1.00120.35      A    C  
ANISOU 2107  CD2 LEU A 279    18710  12620  14396   -191  -2941   3177  A    C  
ATOM   2108  N   LYS A 280      59.744 -27.050  17.338  1.00142.18      A    N  
ANISOU 2108  N   LYS A 280    22124  15682  16217    -10  -3212   3791  A    N  
ATOM   2109  CA  LYS A 280      60.898 -26.491  18.040  1.00140.00      A    C  
ANISOU 2109  CA  LYS A 280    21796  15690  15709    133  -3376   3812  A    C  
ATOM   2110  C   LYS A 280      62.187 -26.816  17.296  1.00139.76      A    C  
ANISOU 2110  C   LYS A 280    21618  15758  15725    439  -3611   3740  A    C  
ATOM   2111  O   LYS A 280      63.107 -26.001  17.248  1.00141.17      A    O  
ANISOU 2111  O   LYS A 280    21577  16237  15823    525  -3725   3642  A    O  
ATOM   2112  CB  LYS A 280      60.982 -27.022  19.476  1.00143.96      A    C  
ANISOU 2112  CB  LYS A 280    22618  16126  15955    158  -3404   4039  A    C  
ATOM   2113  CG  LYS A 280      59.884 -26.529  20.417  1.00137.52      A    C  
ANISOU 2113  CG  LYS A 280    21931  15295  15025   -130  -3180   4113  A    C  
ATOM   2114  CD  LYS A 280      60.035 -27.110  21.834  1.00128.12      A    C  
ANISOU 2114  CD  LYS A 280    21072  14051  13558    -78  -3214   4354  A    C  
ATOM   2115  CE  LYS A 280      59.960 -28.639  21.849  1.00115.34      A    C  
ANISOU 2115  CE  LYS A 280    19749  12081  11995     50  -3254   4543  A    C  
ATOM   2116  NZ  LYS A 280      59.836 -29.180  23.230  1.00107.84      A    N1+
ANISOU 2116  NZ  LYS A 280    19148  11045  10783     50  -3228   4799  A    N1+
ATOM   2117  N   ALA A 281      62.243 -28.014  16.721  1.00139.56      A    N  
ANISOU 2117  N   ALA A 281    21713  15480  15835    600  -3680   3783  A    N  
ATOM   2118  CA  ALA A 281      63.393 -28.452  15.932  1.00136.33      A    C  
ANISOU 2118  CA  ALA A 281    21174  15139  15487    908  -3894   3710  A    C  
ATOM   2119  C   ALA A 281      63.885 -27.390  14.939  1.00133.32      A    C  
ANISOU 2119  C   ALA A 281    20404  15052  15199    920  -3915   3490  A    C  
ATOM   2120  O   ALA A 281      65.019 -26.913  15.038  1.00129.82      A    O  
ANISOU 2120  O   ALA A 281    19795  14887  14645   1074  -4070   3444  A    O  
ATOM   2121  CB  ALA A 281      63.061 -29.751  15.193  1.00130.09      A    C  
ANISOU 2121  CB  ALA A 281    20531  14004  14893   1018  -3910   3732  A    C  
ATOM   2122  N   TYR A 282      63.027 -27.022  13.990  1.00121.93      A    N  
ANISOU 2122  N   TYR A 282    18817  13551  13960    756  -3758   3358  A    N  
ATOM   2123  CA  TYR A 282      63.432 -26.157  12.893  1.00111.55      A    C  
ANISOU 2123  CA  TYR A 282    17157  12471  12755    786  -3767   3163  A    C  
ATOM   2124  C   TYR A 282      63.286 -24.691  13.251  1.00115.68      A    C  
ANISOU 2124  C   TYR A 282    17506  13251  13197    574  -3662   3096  A    C  
ATOM   2125  O   TYR A 282      64.082 -23.850  12.824  1.00112.20      A    O  
ANISOU 2125  O   TYR A 282    16802  13081  12748    631  -3725   2984  A    O  
ATOM   2126  CB  TYR A 282      62.592 -26.438  11.659  1.00110.86      A    C  
ANISOU 2126  CB  TYR A 282    16996  12212  12915    731  -3657   3047  A    C  
ATOM   2127  CG  TYR A 282      62.099 -27.854  11.543  1.00121.65      A    C  
ANISOU 2127  CG  TYR A 282    18617  13219  14385    799  -3670   3126  A    C  
ATOM   2128  CD1 TYR A 282      61.088 -28.323  12.369  1.00124.86      A    C  
ANISOU 2128  CD1 TYR A 282    19296  13375  14771    606  -3541   3263  A    C  
ATOM   2129  CD2 TYR A 282      62.623 -28.717  10.587  1.00126.34      A    C  
ANISOU 2129  CD2 TYR A 282    19177  13721  15105   1050  -3801   3058  A    C  
ATOM   2130  CE1 TYR A 282      60.624 -29.614  12.259  1.00130.53      A    C  
ANISOU 2130  CE1 TYR A 282    20251  13743  15600    647  -3544   3336  A    C  
ATOM   2131  CE2 TYR A 282      62.161 -30.011  10.467  1.00129.14      A    C  
ANISOU 2131  CE2 TYR A 282    19774  13724  15570   1105  -3814   3119  A    C  
ATOM   2132  CZ  TYR A 282      61.160 -30.453  11.306  1.00133.08      A    C  
ANISOU 2132  CZ  TYR A 282    20546  13962  16057    895  -3684   3260  A    C  
ATOM   2133  OH  TYR A 282      60.689 -31.740  11.195  1.00137.68      A    O  
ANISOU 2133  OH  TYR A 282    21375  14175  16764    929  -3689   3324  A    O  
ATOM   2134  N   VAL A 283      62.249 -24.385  14.017  1.00124.12      A    N  
ANISOU 2134  N   VAL A 283    18721  14228  14213    324  -3493   3161  A    N  
ATOM   2135  CA  VAL A 283      61.990 -23.008  14.413  1.00123.48      A    C  
ANISOU 2135  CA  VAL A 283    18502  14358  14055    115  -3381   3093  A    C  
ATOM   2136  C   VAL A 283      62.561 -22.776  15.805  1.00118.45      A    C  
ANISOU 2136  C   VAL A 283    17993  13856  13157    123  -3465   3203  A    C  
ATOM   2137  O   VAL A 283      62.209 -23.465  16.766  1.00103.74      A    O  
ANISOU 2137  O   VAL A 283    16409  11838  11170    102  -3451   3363  A    O  
ATOM   2138  CB  VAL A 283      60.476 -22.675  14.376  1.00110.55      A    C  
ANISOU 2138  CB  VAL A 283    16914  12576  12512   -161  -3136   3070  A    C  
ATOM   2139  CG1 VAL A 283      60.237 -21.220  14.724  1.00105.34      A    C  
ANISOU 2139  CG1 VAL A 283    16110  12134  11783   -355  -3026   2986  A    C  
ATOM   2140  CG2 VAL A 283      59.897 -22.994  13.008  1.00105.94      A    C  
ANISOU 2140  CG2 VAL A 283    16214  11859  12179   -153  -3070   2958  A    C  
ATOM   2141  N   ARG A 284      63.458 -21.810  15.911  1.00129.67      A    N  
ANISOU 2141  N   ARG A 284    19207  15569  14491    154  -3554   3115  A    N  
ATOM   2142  CA  ARG A 284      64.096 -21.551  17.185  1.00145.00      A    C  
ANISOU 2142  CA  ARG A 284    21241  17672  16181    178  -3659   3190  A    C  
ATOM   2143  C   ARG A 284      63.400 -20.416  17.929  1.00147.01      A    C  
ANISOU 2143  C   ARG A 284    21496  18022  16339    -87  -3502   3153  A    C  
ATOM   2144  O   ARG A 284      62.937 -20.601  19.061  1.00143.66      A    O  
ANISOU 2144  O   ARG A 284    21307  17537  15741   -170  -3453   3273  A    O  
ATOM   2145  CB  ARG A 284      65.584 -21.290  16.974  1.00151.99      A    C  
ANISOU 2145  CB  ARG A 284    21912  18823  17016    385  -3877   3116  A    C  
ATOM   2146  CG  ARG A 284      66.294 -22.531  16.475  1.00160.73      A    C  
ANISOU 2146  CG  ARG A 284    23067  19833  18172    678  -4047   3174  A    C  
ATOM   2147  CD  ARG A 284      67.553 -22.226  15.698  1.00170.92      A    C  
ANISOU 2147  CD  ARG A 284    24056  21371  19515    864  -4206   3049  A    C  
ATOM   2148  NE  ARG A 284      68.195 -23.466  15.265  1.00182.93      A    N  
ANISOU 2148  NE  ARG A 284    25639  22792  21074   1163  -4368   3103  A    N  
ATOM   2149  CZ  ARG A 284      68.028 -24.022  14.069  1.00184.80      A    C  
ANISOU 2149  CZ  ARG A 284    25809  22894  21512   1260  -4344   3046  A    C  
ATOM   2150  NH1 ARG A 284      67.247 -23.438  13.167  1.00184.17      A    N1+
ANISOU 2150  NH1 ARG A 284    25591  22776  21610   1084  -4167   2937  A    N1+
ATOM   2151  NH2 ARG A 284      68.652 -25.157  13.771  1.00182.15      A    N  
ANISOU 2151  NH2 ARG A 284    25547  22467  21195   1546  -4503   3091  A    N  
ATOM   2152  N   ASP A 285      63.302 -19.259  17.277  1.00142.14      A    N  
ANISOU 2152  N   ASP A 285    20625  17547  15833   -214  -3418   2991  A    N  
ATOM   2153  CA  ASP A 285      62.656 -18.089  17.870  1.00138.33      A    C  
ANISOU 2153  CA  ASP A 285    20122  17156  15281   -455  -3269   2929  A    C  
ATOM   2154  C   ASP A 285      61.312 -18.446  18.511  1.00134.87      A    C  
ANISOU 2154  C   ASP A 285    19933  16509  14802   -623  -3082   3031  A    C  
ATOM   2155  O   ASP A 285      60.423 -18.982  17.848  1.00133.66      A    O  
ANISOU 2155  O   ASP A 285    19822  16147  14816   -672  -2959   3046  A    O  
ATOM   2156  CB  ASP A 285      62.474 -16.989  16.817  1.00138.45      A    C  
ANISOU 2156  CB  ASP A 285    19861  17263  15481   -563  -3166   2756  A    C  
ATOM   2157  CG  ASP A 285      62.044 -15.661  17.423  1.00141.92      A    C  
ANISOU 2157  CG  ASP A 285    20254  17824  15844   -782  -3046   2671  A    C  
ATOM   2158  OD1 ASP A 285      60.944 -15.600  18.008  1.00142.16      A    O  
ANISOU 2158  OD1 ASP A 285    20446  17742  15826   -941  -2886   2713  A    O  
ATOM   2159  OD2 ASP A 285      62.803 -14.672  17.306  1.00143.82      A    O1-
ANISOU 2159  OD2 ASP A 285    20294  18272  16077   -798  -3108   2557  A    O1-
ATOM   2160  N   PRO A 286      61.166 -18.148  19.810  1.00128.84      A    N  
ANISOU 2160  N   PRO A 286    19327  15814  13812   -712  -3060   3096  A    N  
ATOM   2161  CA  PRO A 286      59.948 -18.435  20.580  1.00131.99      A    C  
ANISOU 2161  CA  PRO A 286    19965  16052  14134   -876  -2877   3203  A    C  
ATOM   2162  C   PRO A 286      58.777 -17.535  20.191  1.00135.03      A    C  
ANISOU 2162  C   PRO A 286    20244  16414  14648  -1109  -2645   3086  A    C  
ATOM   2163  O   PRO A 286      57.632 -17.987  20.231  1.00143.33      A    O  
ANISOU 2163  O   PRO A 286    21425  17278  15758  -1230  -2473   3149  A    O  
ATOM   2164  CB  PRO A 286      60.372 -18.156  22.022  1.00131.09      A    C  
ANISOU 2164  CB  PRO A 286    19997  16095  13718   -875  -2948   3272  A    C  
ATOM   2165  CG  PRO A 286      61.489 -17.187  21.899  1.00128.04      A    C  
ANISOU 2165  CG  PRO A 286    19374  15978  13299   -813  -3102   3123  A    C  
ATOM   2166  CD  PRO A 286      62.213 -17.524  20.634  1.00122.15      A    C  
ANISOU 2166  CD  PRO A 286    18430  15222  12758   -653  -3218   3064  A    C  
ATOM   2167  N   TYR A 287      59.062 -16.283  19.838  1.00131.00      A    N  
ANISOU 2167  N   TYR A 287    19504  16089  14181  -1169  -2640   2919  A    N  
ATOM   2168  CA  TYR A 287      58.044 -15.376  19.316  1.00122.75      A    C  
ANISOU 2168  CA  TYR A 287    18336  15028  13276  -1354  -2438   2794  A    C  
ATOM   2169  C   TYR A 287      57.480 -15.934  18.011  1.00113.77      A    C  
ANISOU 2169  C   TYR A 287    17115  13718  12395  -1331  -2369   2769  A    C  
ATOM   2170  O   TYR A 287      56.271 -15.916  17.791  1.00114.81      A    O  
ANISOU 2170  O   TYR A 287    17272  13727  12625  -1470  -2183   2752  A    O  
ATOM   2171  CB  TYR A 287      58.632 -13.986  19.054  1.00124.69      A    C  
ANISOU 2171  CB  TYR A 287    18350  15486  13540  -1392  -2472   2627  A    C  
ATOM   2172  CG  TYR A 287      58.996 -13.180  20.286  1.00128.14      A    C  
ANISOU 2172  CG  TYR A 287    18841  16099  13746  -1461  -2510   2598  A    C  
ATOM   2173  CD1 TYR A 287      58.024 -12.790  21.199  1.00128.82      A    C  
ANISOU 2173  CD1 TYR A 287    19071  16168  13707  -1623  -2350   2608  A    C  
ATOM   2174  CD2 TYR A 287      60.310 -12.774  20.513  1.00128.75      A    C  
ANISOU 2174  CD2 TYR A 287    18811  16375  13734  -1364  -2706   2546  A    C  
ATOM   2175  CE1 TYR A 287      58.353 -12.034  22.318  1.00133.62      A    C  
ANISOU 2175  CE1 TYR A 287    19730  16945  14096  -1678  -2389   2564  A    C  
ATOM   2176  CE2 TYR A 287      60.652 -12.017  21.628  1.00129.93      A    C  
ANISOU 2176  CE2 TYR A 287    19001  16693  13674  -1428  -2752   2497  A    C  
ATOM   2177  CZ  TYR A 287      59.669 -11.649  22.529  1.00133.00      A    C  
ANISOU 2177  CZ  TYR A 287    19547  17053  13932  -1581  -2596   2505  A    C  
ATOM   2178  OH  TYR A 287      59.995 -10.900  23.644  1.00128.39      A    O  
ANISOU 2178  OH  TYR A 287    19010  16641  13130  -1637  -2645   2443  A    O  
ATOM   2179  N   ALA A 288      58.368 -16.420  17.146  1.00105.64      A    N  
ANISOU 2179  N   ALA A 288    15974  12694  11469  -1147  -2523   2757  A    N  
ATOM   2180  CA  ALA A 288      57.963 -17.024  15.881  1.00100.94      A    C  
ANISOU 2180  CA  ALA A 288    15300  11949  11105  -1092  -2487   2724  A    C  
ATOM   2181  C   ALA A 288      57.020 -18.189  16.122  1.00111.97      A    C  
ANISOU 2181  C   ALA A 288    16920  13092  12531  -1136  -2399   2843  A    C  
ATOM   2182  O   ALA A 288      56.031 -18.351  15.410  1.00123.34      A    O  
ANISOU 2182  O   ALA A 288    18322  14398  14142  -1222  -2264   2793  A    O  
ATOM   2183  CB  ALA A 288      59.175 -17.484  15.091  1.00 92.74      A    C  
ANISOU 2183  CB  ALA A 288    14138  10967  10130   -861  -2683   2707  A    C  
ATOM   2184  N   LEU A 289      57.333 -19.003  17.125  1.00109.51      A    N  
ANISOU 2184  N   LEU A 289    16841  12715  12054  -1079  -2476   3002  A    N  
ATOM   2185  CA  LEU A 289      56.475 -20.124  17.485  1.00103.59      A    C  
ANISOU 2185  CA  LEU A 289    16330  11711  11318  -1137  -2385   3140  A    C  
ATOM   2186  C   LEU A 289      55.121 -19.627  17.949  1.00109.31      A    C  
ANISOU 2186  C   LEU A 289    17103  12396  12034  -1389  -2145   3128  A    C  
ATOM   2187  O   LEU A 289      54.090 -20.035  17.424  1.00115.22      A    O  
ANISOU 2187  O   LEU A 289    17857  12974  12948  -1493  -2006   3109  A    O  
ATOM   2188  CB  LEU A 289      57.126 -20.981  18.562  1.00102.29      A    C  
ANISOU 2188  CB  LEU A 289    16418  11502  10946  -1019  -2513   3328  A    C  
ATOM   2189  CG  LEU A 289      57.986 -22.104  17.983  1.00113.34      A    C  
ANISOU 2189  CG  LEU A 289    17857  12787  12421   -773  -2704   3384  A    C  
ATOM   2190  CD1 LEU A 289      58.810 -22.791  19.056  1.00123.99      A    C  
ANISOU 2190  CD1 LEU A 289    19433  14138  13540   -618  -2859   3560  A    C  
ATOM   2191  CD2 LEU A 289      57.113 -23.110  17.263  1.00113.09      A    C  
ANISOU 2191  CD2 LEU A 289    17906  12462  12602   -810  -2611   3408  A    C  
ATOM   2192  N   ASP A 290      55.127 -18.728  18.924  1.00112.99      A    N  
ANISOU 2192  N   ASP A 290    17593  13032  12308  -1484  -2099   3123  A    N  
ATOM   2193  CA  ASP A 290      53.889 -18.158  19.434  1.00119.67      A    C  
ANISOU 2193  CA  ASP A 290    18474  13874  13123  -1711  -1871   3100  A    C  
ATOM   2194  C   ASP A 290      53.002 -17.626  18.308  1.00124.03      A    C  
ANISOU 2194  C   ASP A 290    18817  14397  13913  -1811  -1732   2939  A    C  
ATOM   2195  O   ASP A 290      51.775 -17.699  18.397  1.00131.87      A    O  
ANISOU 2195  O   ASP A 290    19848  15292  14964  -1976  -1539   2938  A    O  
ATOM   2196  CB  ASP A 290      54.182 -17.047  20.443  1.00123.53      A    C  
ANISOU 2196  CB  ASP A 290    18962  14588  13387  -1769  -1868   3063  A    C  
ATOM   2197  CG  ASP A 290      52.957 -16.648  21.243  1.00129.94      A    C  
ANISOU 2197  CG  ASP A 290    19869  15393  14109  -1980  -1639   3075  A    C  
ATOM   2198  OD1 ASP A 290      52.397 -17.508  21.964  1.00130.71      A    O  
ANISOU 2198  OD1 ASP A 290    20189  15357  14117  -2040  -1553   3234  A    O  
ATOM   2199  OD2 ASP A 290      52.562 -15.467  21.157  1.00130.43      A    O1-
ANISOU 2199  OD2 ASP A 290    19786  15584  14189  -2082  -1542   2927  A    O1-
ATOM   2200  N   LEU A 291      53.611 -17.093  17.250  1.00115.63      A    N  
ANISOU 2200  N   LEU A 291    17527  13427  12980  -1707  -1827   2806  A    N  
ATOM   2201  CA  LEU A 291      52.823 -16.560  16.140  1.00105.05      A    C  
ANISOU 2201  CA  LEU A 291    15989  12075  11851  -1775  -1708   2656  A    C  
ATOM   2202  C   LEU A 291      52.175 -17.663  15.312  1.00106.25      A    C  
ANISOU 2202  C   LEU A 291    16162  12011  12199  -1762  -1672   2671  A    C  
ATOM   2203  O   LEU A 291      50.976 -17.615  15.040  1.00105.43      A    O  
ANISOU 2203  O   LEU A 291    16024  11828  12205  -1902  -1503   2616  A    O  
ATOM   2204  CB  LEU A 291      53.649 -15.641  15.237  1.00 92.10      A    C  
ANISOU 2204  CB  LEU A 291    14108  10600  10285  -1671  -1805   2521  A    C  
ATOM   2205  CG  LEU A 291      52.853 -15.158  14.010  1.00 86.53      A    C  
ANISOU 2205  CG  LEU A 291    13209   9877   9792  -1711  -1691   2378  A    C  
ATOM   2206  CD1 LEU A 291      51.474 -14.635  14.401  1.00 87.44      A    C  
ANISOU 2206  CD1 LEU A 291    13346   9968   9909  -1909  -1474   2334  A    C  
ATOM   2207  CD2 LEU A 291      53.607 -14.114  13.194  1.00 74.41      A    C  
ANISOU 2207  CD2 LEU A 291    11449   8510   8312  -1629  -1757   2259  A    C  
ATOM   2208  N   ILE A 292      52.976 -18.646  14.908  1.00105.73      A    N  
ANISOU 2208  N   ILE A 292    16143  11853  12177  -1588  -1837   2732  A    N  
ATOM   2209  CA  ILE A 292      52.479 -19.791  14.154  1.00104.37      A    C  
ANISOU 2209  CA  ILE A 292    16012  11457  12189  -1559  -1829   2743  A    C  
ATOM   2210  C   ILE A 292      51.302 -20.445  14.869  1.00109.76      A    C  
ANISOU 2210  C   ILE A 292    16885  11953  12865  -1747  -1661   2841  A    C  
ATOM   2211  O   ILE A 292      50.318 -20.860  14.247  1.00112.53      A    O  
ANISOU 2211  O   ILE A 292    17198  12163  13396  -1839  -1553   2782  A    O  
ATOM   2212  CB  ILE A 292      53.574 -20.849  13.962  1.00 93.07      A    C  
ANISOU 2212  CB  ILE A 292    14669   9938  10753  -1338  -2037   2828  A    C  
ATOM   2213  CG1 ILE A 292      54.715 -20.274  13.126  1.00 88.08      A    C  
ANISOU 2213  CG1 ILE A 292    13820   9496  10149  -1151  -2192   2722  A    C  
ATOM   2214  CG2 ILE A 292      52.995 -22.103  13.322  1.00 87.50      A    C  
ANISOU 2214  CG2 ILE A 292    14047   8967  10233  -1324  -2023   2843  A    C  
ATOM   2215  CD1 ILE A 292      55.470 -21.308  12.325  1.00 88.59      A    C  
ANISOU 2215  CD1 ILE A 292    13885   9462  10315   -927  -2361   2729  A    C  
ATOM   2216  N   ASP A 293      51.414 -20.520  16.187  1.00102.62      A    N  
ANISOU 2216  N   ASP A 293    16180  11062  11749  -1805  -1639   2988  A    N  
ATOM   2217  CA  ASP A 293      50.406 -21.162  17.003  1.00109.63      A    C  
ANISOU 2217  CA  ASP A 293    17271  11785  12598  -1982  -1475   3112  A    C  
ATOM   2218  C   ASP A 293      49.081 -20.407  16.965  1.00114.37      A    C  
ANISOU 2218  C   ASP A 293    17757  12437  13263  -2201  -1245   3005  A    C  
ATOM   2219  O   ASP A 293      48.029 -20.998  17.189  1.00125.04      A    O  
ANISOU 2219  O   ASP A 293    19200  13632  14679  -2363  -1087   3056  A    O  
ATOM   2220  CB  ASP A 293      50.910 -21.296  18.440  1.00121.17      A    C  
ANISOU 2220  CB  ASP A 293    18966  13290  13782  -1972  -1509   3294  A    C  
ATOM   2221  CG  ASP A 293      49.967 -22.083  19.319  1.00129.36      A    C  
ANISOU 2221  CG  ASP A 293    20242  14146  14763  -2140  -1341   3458  A    C  
ATOM   2222  OD1 ASP A 293      49.993 -23.332  19.250  1.00139.44      A    O  
ANISOU 2222  OD1 ASP A 293    21689  15182  16109  -2098  -1381   3583  A    O  
ATOM   2223  OD2 ASP A 293      49.206 -21.451  20.085  1.00126.35      A    O1-
ANISOU 2223  OD2 ASP A 293    19882  13859  14266  -2315  -1164   3462  A    O1-
ATOM   2224  N   LYS A 294      49.121 -19.107  16.685  1.00110.40      A    N  
ANISOU 2224  N   LYS A 294    17052  12146  12747  -2208  -1223   2856  A    N  
ATOM   2225  CA  LYS A 294      47.885 -18.328  16.608  1.00105.64      A    C  
ANISOU 2225  CA  LYS A 294    16330  11604  12205  -2388  -1014   2741  A    C  
ATOM   2226  C   LYS A 294      47.329 -18.312  15.199  1.00104.04      A    C  
ANISOU 2226  C   LYS A 294    15915  11354  12259  -2374   -990   2580  A    C  
ATOM   2227  O   LYS A 294      46.186 -17.913  14.983  1.00107.70      A    O  
ANISOU 2227  O   LYS A 294    16277  11833  12812  -2513   -821   2483  A    O  
ATOM   2228  CB  LYS A 294      48.083 -16.911  17.140  1.00 99.19      A    C  
ANISOU 2228  CB  LYS A 294    15433  11022  11232  -2415   -982   2666  A    C  
ATOM   2229  CG  LYS A 294      48.069 -16.852  18.650  1.00104.68      A    C  
ANISOU 2229  CG  LYS A 294    16334  11769  11672  -2500   -921   2798  A    C  
ATOM   2230  CD  LYS A 294      49.124 -15.922  19.210  1.00107.48      A    C  
ANISOU 2230  CD  LYS A 294    16677  12326  11837  -2412  -1045   2774  A    C  
ATOM   2231  CE  LYS A 294      49.170 -16.012  20.732  1.00115.79      A    C  
ANISOU 2231  CE  LYS A 294    17956  13428  12613  -2472  -1006   2913  A    C  
ATOM   2232  NZ  LYS A 294      50.007 -14.937  21.342  1.00121.40      A    N1+
ANISOU 2232  NZ  LYS A 294    18635  14357  13136  -2421  -1101   2851  A    N1+
ATOM   2233  N   LEU A 295      48.148 -18.762  14.253  1.00 95.77      A    N  
ANISOU 2233  N   LEU A 295    14803  10264  11322  -2195  -1164   2550  A    N  
ATOM   2234  CA  LEU A 295      47.741 -18.888  12.863  1.00 79.11      A    C  
ANISOU 2234  CA  LEU A 295    12508   8107   9443  -2148  -1169   2402  A    C  
ATOM   2235  C   LEU A 295      47.122 -20.240  12.634  1.00 82.07      A    C  
ANISOU 2235  C   LEU A 295    12989   8234   9962  -2201  -1143   2447  A    C  
ATOM   2236  O   LEU A 295      46.114 -20.347  11.945  1.00 90.76      A    O  
ANISOU 2236  O   LEU A 295    13975   9276  11233  -2289  -1042   2333  A    O  
ATOM   2237  CB  LEU A 295      48.933 -18.731  11.931  1.00 71.05      A    C  
ANISOU 2237  CB  LEU A 295    11362   7170   8465  -1921  -1363   2342  A    C  
ATOM   2238  CG  LEU A 295      49.429 -17.297  11.769  1.00 79.11      A    C  
ANISOU 2238  CG  LEU A 295    12215   8428   9415  -1878  -1376   2251  A    C  
ATOM   2239  CD1 LEU A 295      50.730 -17.292  11.010  1.00 87.24      A    C  
ANISOU 2239  CD1 LEU A 295    13147   9537  10465  -1662  -1568   2228  A    C  
ATOM   2240  CD2 LEU A 295      48.397 -16.454  11.062  1.00 73.49      A    C  
ANISOU 2240  CD2 LEU A 295    11318   7783   8820  -1961  -1232   2097  A    C  
ATOM   2241  N   LEU A 296      47.735 -21.277  13.199  1.00 78.21      A    N  
ANISOU 2241  N   LEU A 296    12717   7593   9406  -2143  -1239   2609  A    N  
ATOM   2242  CA  LEU A 296      47.196 -22.633  13.081  1.00 82.49      A    C  
ANISOU 2242  CA  LEU A 296    13398   7861  10084  -2202  -1214   2672  A    C  
ATOM   2243  C   LEU A 296      46.290 -22.956  14.261  1.00 92.85      A    C  
ANISOU 2243  C   LEU A 296    14895   9072  11311  -2432  -1027   2809  A    C  
ATOM   2244  O   LEU A 296      46.592 -23.808  15.095  1.00 95.06      A    O  
ANISOU 2244  O   LEU A 296    15423   9202  11492  -2436  -1051   2998  A    O  
ATOM   2245  CB  LEU A 296      48.316 -23.653  12.949  1.00 79.94      A    C  
ANISOU 2245  CB  LEU A 296    13219   7400   9756  -1998  -1420   2771  A    C  
ATOM   2246  CG  LEU A 296      49.182 -23.319  11.741  1.00 92.16      A    C  
ANISOU 2246  CG  LEU A 296    14562   9068  11386  -1773  -1589   2628  A    C  
ATOM   2247  CD1 LEU A 296      50.483 -24.102  11.751  1.00 95.31      A    C  
ANISOU 2247  CD1 LEU A 296    15084   9400  11730  -1541  -1804   2725  A    C  
ATOM   2248  CD2 LEU A 296      48.398 -23.545  10.450  1.00 88.83      A    C  
ANISOU 2248  CD2 LEU A 296    13971   8572  11210  -1791  -1552   2448  A    C  
ATOM   2249  N   VAL A 297      45.179 -22.236  14.318  1.00 98.94      A    N  
ANISOU 2249  N   VAL A 297    15539   9939  12114  -2613   -837   2713  A    N  
ATOM   2250  CA  VAL A 297      44.192 -22.382  15.365  1.00 99.01      A    C  
ANISOU 2250  CA  VAL A 297    15676   9897  12047  -2846   -627   2815  A    C  
ATOM   2251  C   VAL A 297      42.979 -23.000  14.711  1.00105.43      A    C  
ANISOU 2251  C   VAL A 297    16405  10552  13102  -3004   -501   2722  A    C  
ATOM   2252  O   VAL A 297      42.549 -22.543  13.654  1.00111.21      A    O  
ANISOU 2252  O   VAL A 297    16897  11361  13995  -2983   -500   2522  A    O  
ATOM   2253  CB  VAL A 297      43.809 -21.007  15.936  1.00 94.07      A    C  
ANISOU 2253  CB  VAL A 297    14944   9527  11272  -2930   -498   2752  A    C  
ATOM   2254  CG1 VAL A 297      42.692 -21.126  16.957  1.00 84.35      A    C  
ANISOU 2254  CG1 VAL A 297    13818   8266   9967  -3172   -260   2839  A    C  
ATOM   2255  CG2 VAL A 297      45.025 -20.330  16.540  1.00 95.94      A    C  
ANISOU 2255  CG2 VAL A 297    15242   9929  11281  -2781   -633   2815  A    C  
ATOM   2256  N   LEU A 298      42.429 -24.038  15.333  1.00108.25      A    N  
ANISOU 2256  N   LEU A 298    16956  10690  13483  -3162   -396   2866  A    N  
ATOM   2257  CA  LEU A 298      41.319 -24.784  14.745  1.00110.07      A    C  
ANISOU 2257  CA  LEU A 298    17122  10740  13961  -3329   -286   2783  A    C  
ATOM   2258  C   LEU A 298      40.091 -23.906  14.491  1.00111.85      A    C  
ANISOU 2258  C   LEU A 298    17100  11138  14260  -3492   -100   2606  A    C  
ATOM   2259  O   LEU A 298      39.591 -23.825  13.362  1.00106.80      A    O  
ANISOU 2259  O   LEU A 298    16240  10512  13826  -3480   -118   2404  A    O  
ATOM   2260  CB  LEU A 298      40.964 -25.981  15.629  1.00112.51      A    C  
ANISOU 2260  CB  LEU A 298    17705  10783  14259  -3496   -182   2998  A    C  
ATOM   2261  CG  LEU A 298      42.077 -27.030  15.797  1.00114.15      A    C  
ANISOU 2261  CG  LEU A 298    18173  10770  14427  -3328   -368   3172  A    C  
ATOM   2262  CD1 LEU A 298      41.844 -27.908  17.020  1.00127.77      A    C  
ANISOU 2262  CD1 LEU A 298    20212  12294  16043  -3479   -245   3438  A    C  
ATOM   2263  CD2 LEU A 298      42.254 -27.893  14.547  1.00 97.51      A    C  
ANISOU 2263  CD2 LEU A 298    16009   8458  12580  -3222   -518   3051  A    C  
ATOM   2264  N   ASP A 299      39.625 -23.243  15.545  1.00112.62      A    N  
ANISOU 2264  N   ASP A 299    17234  11378  14178  -3626     72   2677  A    N  
ATOM   2265  CA  ASP A 299      38.468 -22.358  15.463  1.00106.62      A    C  
ANISOU 2265  CA  ASP A 299    16253  10799  13457  -3770    259   2521  A    C  
ATOM   2266  C   ASP A 299      38.779 -21.026  14.760  1.00102.84      A    C  
ANISOU 2266  C   ASP A 299    15544  10573  12958  -3604    176   2335  A    C  
ATOM   2267  O   ASP A 299      39.483 -20.169  15.299  1.00 97.70      A    O  
ANISOU 2267  O   ASP A 299    14934  10082  12105  -3505    130   2378  A    O  
ATOM   2268  CB  ASP A 299      37.918 -22.106  16.865  1.00111.87      A    C  
ANISOU 2268  CB  ASP A 299    17047  11537  13920  -3952    471   2662  A    C  
ATOM   2269  CG  ASP A 299      36.657 -21.279  16.851  1.00121.35      A    C  
ANISOU 2269  CG  ASP A 299    18027  12919  15161  -4105    679   2506  A    C  
ATOM   2270  OD1 ASP A 299      36.091 -21.078  15.755  1.00119.92      A    O  
ANISOU 2270  OD1 ASP A 299    17604  12773  15189  -4094    668   2299  A    O  
ATOM   2271  OD2 ASP A 299      36.234 -20.832  17.937  1.00128.57      A    O1-
ANISOU 2271  OD2 ASP A 299    19009  13950  15890  -4224    851   2586  A    O1-
ATOM   2272  N   PRO A 300      38.246 -20.851  13.546  1.00102.29      A    N  
ANISOU 2272  N   PRO A 300    15235  10534  13098  -3573    156   2126  A    N  
ATOM   2273  CA  PRO A 300      38.401 -19.657  12.703  1.00102.20      A    C  
ANISOU 2273  CA  PRO A 300    14993  10737  13101  -3419     90   1943  A    C  
ATOM   2274  C   PRO A 300      38.159 -18.353  13.442  1.00104.72      A    C  
ANISOU 2274  C   PRO A 300    15266  11284  13240  -3453    211   1925  A    C  
ATOM   2275  O   PRO A 300      38.866 -17.375  13.207  1.00106.69      A    O  
ANISOU 2275  O   PRO A 300    15451  11683  13404  -3295    117   1873  A    O  
ATOM   2276  CB  PRO A 300      37.308 -19.838  11.654  1.00 98.11      A    C  
ANISOU 2276  CB  PRO A 300    14249  10206  12823  -3482    147   1744  A    C  
ATOM   2277  CG  PRO A 300      37.189 -21.314  11.527  1.00101.32      A    C  
ANISOU 2277  CG  PRO A 300    14776  10343  13377  -3569    119   1811  A    C  
ATOM   2278  CD  PRO A 300      37.436 -21.888  12.890  1.00100.35      A    C  
ANISOU 2278  CD  PRO A 300    14933  10099  13096  -3691    194   2056  A    C  
ATOM   2279  N   ALA A 301      37.161 -18.345  14.316  1.00106.23      A    N  
ANISOU 2279  N   ALA A 301    15487  11498  13377  -3659    424   1962  A    N  
ATOM   2280  CA  ALA A 301      36.791 -17.143  15.043  1.00105.96      A    C  
ANISOU 2280  CA  ALA A 301    15407  11677  13176  -3699    557   1927  A    C  
ATOM   2281  C   ALA A 301      37.738 -16.875  16.204  1.00105.61      A    C  
ANISOU 2281  C   ALA A 301    15585  11675  12869  -3658    517   2098  A    C  
ATOM   2282  O   ALA A 301      37.625 -15.851  16.876  1.00 99.63      A    O  
ANISOU 2282  O   ALA A 301    14817  11091  11946  -3669    600   2072  A    O  
ATOM   2283  CB  ALA A 301      35.376 -17.254  15.540  1.00108.43      A    C  
ANISOU 2283  CB  ALA A 301    15659  12018  13524  -3926    804   1897  A    C  
ATOM   2284  N   GLN A 302      38.655 -17.809  16.445  1.00107.91      A    N  
ANISOU 2284  N   GLN A 302    16077  11807  13117  -3604    384   2263  A    N  
ATOM   2285  CA  GLN A 302      39.704 -17.620  17.443  1.00105.71      A    C  
ANISOU 2285  CA  GLN A 302    16002  11573  12590  -3529    301   2418  A    C  
ATOM   2286  C   GLN A 302      41.071 -17.540  16.783  1.00109.00      A    C  
ANISOU 2286  C   GLN A 302    16412  11987  13015  -3301     48   2409  A    C  
ATOM   2287  O   GLN A 302      42.075 -17.314  17.455  1.00110.46      A    O  
ANISOU 2287  O   GLN A 302    16731  12231  13010  -3209    -58   2509  A    O  
ATOM   2288  CB  GLN A 302      39.697 -18.746  18.474  1.00106.31      A    C  
ANISOU 2288  CB  GLN A 302    16345  11487  12561  -3644    362   2647  A    C  
ATOM   2289  CG  GLN A 302      38.602 -18.614  19.521  1.00118.30      A    C  
ANISOU 2289  CG  GLN A 302    17916  13067  13966  -3860    621   2700  A    C  
ATOM   2290  CD  GLN A 302      38.593 -19.762  20.517  1.00128.47      A    C  
ANISOU 2290  CD  GLN A 302    19482  14183  15147  -3974    692   2948  A    C  
ATOM   2291  NE2 GLN A 302      39.193 -19.537  21.684  1.00127.50      A    N  
ANISOU 2291  NE2 GLN A 302    19559  14144  14740  -3938    684   3097  A    N  
ATOM   2292  OE1 GLN A 302      38.048 -20.836  20.243  1.00134.30      A    O  
ANISOU 2292  OE1 GLN A 302    20260  14714  16056  -4093    755   3003  A    O  
ATOM   2293  N   ARG A 303      41.101 -17.725  15.465  1.00107.83      A    N  
ANISOU 2293  N   ARG A 303    16100  11785  13084  -3208    -48   2283  A    N  
ATOM   2294  CA  ARG A 303      42.345 -17.656  14.706  1.00 94.76      A    C  
ANISOU 2294  CA  ARG A 303    14408  10141  11455  -2988   -276   2260  A    C  
ATOM   2295  C   ARG A 303      42.716 -16.208  14.427  1.00 88.34      A    C  
ANISOU 2295  C   ARG A 303    13438   9548  10581  -2890   -308   2136  A    C  
ATOM   2296  O   ARG A 303      41.888 -15.425  13.948  1.00 87.97      A    O  
ANISOU 2296  O   ARG A 303    13212   9598  10613  -2931   -201   1986  A    O  
ATOM   2297  CB  ARG A 303      42.237 -18.437  13.391  1.00 92.79      A    C  
ANISOU 2297  CB  ARG A 303    14051   9756  11450  -2916   -363   2171  A    C  
ATOM   2298  CG  ARG A 303      43.586 -18.691  12.718  1.00 94.11      A    C  
ANISOU 2298  CG  ARG A 303    14224   9902  11633  -2688   -598   2186  A    C  
ATOM   2299  CD  ARG A 303      43.455 -19.208  11.285  1.00 90.35      A    C  
ANISOU 2299  CD  ARG A 303    13599   9343  11389  -2592   -683   2053  A    C  
ATOM   2300  NE  ARG A 303      42.938 -20.571  11.232  1.00 90.48      A    N  
ANISOU 2300  NE  ARG A 303    13724   9118  11538  -2681   -662   2101  A    N  
ATOM   2301  CZ  ARG A 303      41.666 -20.860  11.007  1.00 91.19      A    C  
ANISOU 2301  CZ  ARG A 303    13737   9140  11773  -2850   -515   2015  A    C  
ATOM   2302  NH1 ARG A 303      40.811 -19.875  10.817  1.00 94.28      A    N1+
ANISOU 2302  NH1 ARG A 303    13940   9699  12181  -2923   -386   1880  A    N1+
ATOM   2303  NH2 ARG A 303      41.246 -22.118  10.971  1.00 95.47      A    N  
ANISOU 2303  NH2 ARG A 303    14383   9444  12446  -2944   -500   2060  A    N  
ATOM   2304  N   ILE A 304      43.978 -15.885  14.706  1.00 84.29      A    N  
ANISOU 2304  N   ILE A 304    12991   9103   9931  -2757   -461   2198  A    N  
ATOM   2305  CA  ILE A 304      44.529 -14.529  14.618  1.00 77.10      A    C  
ANISOU 2305  CA  ILE A 304    11969   8385   8942  -2676   -504   2106  A    C  
ATOM   2306  C   ILE A 304      44.208 -13.757  13.342  1.00 78.51      A    C  
ANISOU 2306  C   ILE A 304    11905   8639   9286  -2605   -497   1926  A    C  
ATOM   2307  O   ILE A 304      44.301 -14.287  12.227  1.00 69.42      A    O  
ANISOU 2307  O   ILE A 304    10659   7418   8301  -2510   -579   1875  A    O  
ATOM   2308  CB  ILE A 304      46.072 -14.547  14.812  1.00 84.75      A    C  
ANISOU 2308  CB  ILE A 304    13013   9393   9795  -2523   -710   2188  A    C  
ATOM   2309  CG1 ILE A 304      46.584 -13.176  15.251  1.00 78.76      A    C  
ANISOU 2309  CG1 ILE A 304    12204   8824   8897  -2505   -722   2129  A    C  
ATOM   2310  CG2 ILE A 304      46.776 -15.004  13.547  1.00 81.21      A    C  
ANISOU 2310  CG2 ILE A 304    12457   8894   9506  -2353   -872   2147  A    C  
ATOM   2311  CD1 ILE A 304      47.962 -13.211  15.855  1.00 74.37      A    C  
ANISOU 2311  CD1 ILE A 304    11751   8325   8180  -2406   -896   2223  A    C  
ATOM   2312  N   ASP A 305      43.832 -12.492  13.545  1.00 84.07      A    N  
ANISOU 2312  N   ASP A 305    12523   9486   9932  -2643   -400   1831  A    N  
ATOM   2313  CA  ASP A 305      43.598 -11.504  12.491  1.00 77.17      A    C  
ANISOU 2313  CA  ASP A 305    11441   8707   9173  -2565   -386   1673  A    C  
ATOM   2314  C   ASP A 305      44.896 -11.228  11.759  1.00 83.40      A    C  
ANISOU 2314  C   ASP A 305    12168   9538   9981  -2392   -568   1669  A    C  
ATOM   2315  O   ASP A 305      45.970 -11.324  12.358  1.00 90.29      A    O  
ANISOU 2315  O   ASP A 305    13148  10428  10731  -2353   -682   1765  A    O  
ATOM   2316  CB  ASP A 305      43.164 -10.200  13.153  1.00 87.35      A    C  
ANISOU 2316  CB  ASP A 305    12710  10127  10351  -2634   -261   1604  A    C  
ATOM   2317  CG  ASP A 305      42.047  -9.512  12.416  1.00110.45      A    C  
ANISOU 2317  CG  ASP A 305    15459  13106  13401  -2641   -135   1450  A    C  
ATOM   2318  OD1 ASP A 305      40.975 -10.139  12.277  1.00125.03      A    O  
ANISOU 2318  OD1 ASP A 305    17268  14898  15339  -2725    -29   1421  A    O  
ATOM   2319  OD2 ASP A 305      42.226  -8.346  11.990  1.00109.74      A    O1-
ANISOU 2319  OD2 ASP A 305    15268  13110  13317  -2564   -139   1358  A    O1-
ATOM   2320  N   SER A 306      44.819 -10.854  10.482  1.00 82.78      A    N  
ANISOU 2320  N   SER A 306    11912   9494  10048  -2285   -594   1560  A    N  
ATOM   2321  CA  SER A 306      46.027 -10.399   9.770  1.00 89.18      A    C  
ANISOU 2321  CA  SER A 306    12643  10372  10869  -2128   -740   1552  A    C  
ATOM   2322  C   SER A 306      46.586  -9.073  10.333  1.00 84.69      A    C  
ANISOU 2322  C   SER A 306    12075   9926  10178  -2143   -731   1537  A    C  
ATOM   2323  O   SER A 306      47.761  -8.761  10.167  1.00 78.58      A    O  
ANISOU 2323  O   SER A 306    11278   9209   9369  -2056   -854   1564  A    O  
ATOM   2324  CB  SER A 306      45.768 -10.251   8.272  1.00 82.47      A    C  
ANISOU 2324  CB  SER A 306    11609   9542  10185  -2006   -755   1443  A    C  
ATOM   2325  OG  SER A 306      45.338  -8.934   7.978  1.00 87.28      A    O  
ANISOU 2325  OG  SER A 306    12109  10253  10802  -2002   -661   1346  A    O  
ATOM   2326  N   ASP A 307      45.727  -8.298  10.985  1.00 86.54      A    N  
ANISOU 2326  N   ASP A 307    12327  10200  10354  -2257   -583   1484  A    N  
ATOM   2327  CA  ASP A 307      46.133  -7.075  11.663  1.00 89.73      A    C  
ANISOU 2327  CA  ASP A 307    12756  10699  10638  -2291   -563   1457  A    C  
ATOM   2328  C   ASP A 307      46.860  -7.425  12.953  1.00 80.15      A    C  
ANISOU 2328  C   ASP A 307    11714   9493   9245  -2352   -631   1564  A    C  
ATOM   2329  O   ASP A 307      47.991  -7.014  13.182  1.00 89.88      A    O  
ANISOU 2329  O   ASP A 307    12960  10788  10403  -2309   -747   1586  A    O  
ATOM   2330  CB  ASP A 307      44.896  -6.233  11.993  1.00101.77      A    C  
ANISOU 2330  CB  ASP A 307    14257  12259  12153  -2382   -380   1358  A    C  
ATOM   2331  CG  ASP A 307      45.177  -4.737  12.012  1.00111.92      A    C  
ANISOU 2331  CG  ASP A 307    15495  13627  13405  -2364   -356   1275  A    C  
ATOM   2332  OD1 ASP A 307      46.193  -4.283  11.421  1.00123.50      A    O  
ANISOU 2332  OD1 ASP A 307    16898  15120  14905  -2275   -466   1276  A    O  
ATOM   2333  OD2 ASP A 307      44.354  -4.015  12.615  1.00101.01      A    O1-
ANISOU 2333  OD2 ASP A 307    14136  12277  11965  -2440   -221   1204  A    O1-
ATOM   2334  N   ASP A 308      46.209  -8.200  13.798  1.00 73.99      A    N  
ANISOU 2334  N   ASP A 308    11065   8656   8391  -2453   -556   1631  A    N  
ATOM   2335  CA  ASP A 308      46.775  -8.516  15.093  1.00 86.88      A    C  
ANISOU 2335  CA  ASP A 308    12878  10305   9828  -2506   -605   1738  A    C  
ATOM   2336  C   ASP A 308      48.090  -9.274  14.962  1.00 86.96      A    C  
ANISOU 2336  C   ASP A 308    12932  10292   9818  -2395   -806   1840  A    C  
ATOM   2337  O   ASP A 308      48.885  -9.317  15.904  1.00 92.89      A    O  
ANISOU 2337  O   ASP A 308    13802  11093  10400  -2395   -894   1913  A    O  
ATOM   2338  CB  ASP A 308      45.772  -9.316  15.921  1.00 99.65      A    C  
ANISOU 2338  CB  ASP A 308    14629  11853  11382  -2632   -472   1811  A    C  
ATOM   2339  CG  ASP A 308      44.496  -8.540  16.198  1.00108.38      A    C  
ANISOU 2339  CG  ASP A 308    15687  13009  12482  -2742   -267   1707  A    C  
ATOM   2340  OD1 ASP A 308      44.510  -7.701  17.127  1.00107.97      A    O  
ANISOU 2340  OD1 ASP A 308    15699  13052  12271  -2795   -216   1677  A    O  
ATOM   2341  OD2 ASP A 308      43.483  -8.767  15.491  1.00107.28      A    O1-
ANISOU 2341  OD2 ASP A 308    15443  12823  12495  -2767   -164   1646  A    O1-
ATOM   2342  N   ALA A 309      48.321  -9.859  13.791  1.00 76.92      A    N  
ANISOU 2342  N   ALA A 309    11560   8958   8709  -2287   -884   1835  A    N  
ATOM   2343  CA  ALA A 309      49.500 -10.693  13.583  1.00 79.49      A    C  
ANISOU 2343  CA  ALA A 309    11918   9256   9028  -2163  -1071   1925  A    C  
ATOM   2344  C   ALA A 309      50.710  -9.856  13.225  1.00 83.83      A    C  
ANISOU 2344  C   ALA A 309    12356   9932   9564  -2066  -1197   1881  A    C  
ATOM   2345  O   ALA A 309      51.826 -10.158  13.622  1.00 85.73      A    O  
ANISOU 2345  O   ALA A 309    12647  10215   9711  -1997  -1347   1951  A    O  
ATOM   2346  CB  ALA A 309      49.239 -11.711  12.505  1.00 82.84      A    C  
ANISOU 2346  CB  ALA A 309    12286   9561   9626  -2082  -1102   1928  A    C  
ATOM   2347  N   LEU A 310      50.476  -8.802  12.456  1.00 89.11      A    N  
ANISOU 2347  N   LEU A 310    12868  10660  10329  -2061  -1133   1766  A    N  
ATOM   2348  CA  LEU A 310      51.520  -7.862  12.079  1.00 85.92      A    C  
ANISOU 2348  CA  LEU A 310    12347  10369   9928  -1998  -1219   1719  A    C  
ATOM   2349  C   LEU A 310      51.966  -7.066  13.294  1.00 87.68      A    C  
ANISOU 2349  C   LEU A 310    12652  10681   9982  -2089  -1231   1713  A    C  
ATOM   2350  O   LEU A 310      53.020  -6.426  13.295  1.00 96.80      A    O  
ANISOU 2350  O   LEU A 310    13741  11932  11108  -2059  -1330   1689  A    O  
ATOM   2351  CB  LEU A 310      50.976  -6.898  11.033  1.00 77.49      A    C  
ANISOU 2351  CB  LEU A 310    11121   9322   8998  -1984  -1118   1608  A    C  
ATOM   2352  CG  LEU A 310      50.764  -7.363   9.600  1.00 63.11      A    C  
ANISOU 2352  CG  LEU A 310     9170   7462   7346  -1863  -1127   1583  A    C  
ATOM   2353  CD1 LEU A 310      49.896  -6.350   8.905  1.00 67.95      A    C  
ANISOU 2353  CD1 LEU A 310     9674   8092   8050  -1875   -991   1478  A    C  
ATOM   2354  CD2 LEU A 310      52.094  -7.480   8.890  1.00 67.15      A    C  
ANISOU 2354  CD2 LEU A 310     9583   8039   7891  -1727  -1279   1611  A    C  
ATOM   2355  N   ASN A 311      51.130  -7.111  14.319  1.00 84.76      A    N  
ANISOU 2355  N   ASN A 311    12420  10283   9501  -2204  -1125   1726  A    N  
ATOM   2356  CA  ASN A 311      51.330  -6.365  15.541  1.00 95.68      A    C  
ANISOU 2356  CA  ASN A 311    13898  11750  10708  -2296  -1115   1704  A    C  
ATOM   2357  C   ASN A 311      51.995  -7.250  16.579  1.00 93.57      A    C  
ANISOU 2357  C   ASN A 311    13791  11498  10265  -2282  -1233   1824  A    C  
ATOM   2358  O   ASN A 311      52.236  -6.837  17.711  1.00 93.59      A    O  
ANISOU 2358  O   ASN A 311    13896  11579  10087  -2344  -1249   1821  A    O  
ATOM   2359  CB  ASN A 311      49.971  -5.897  16.045  1.00109.32      A    C  
ANISOU 2359  CB  ASN A 311    15681  13453  12402  -2416   -917   1645  A    C  
ATOM   2360  CG  ASN A 311      50.078  -4.947  17.201  1.00115.66      A    C  
ANISOU 2360  CG  ASN A 311    16566  14348  13033  -2504   -890   1588  A    C  
ATOM   2361  ND2 ASN A 311      48.934  -4.507  17.707  1.00114.88      A    N  
ANISOU 2361  ND2 ASN A 311    16516  14244  12889  -2598   -717   1530  A    N  
ATOM   2362  OD1 ASN A 311      51.175  -4.601  17.636  1.00120.33      A    O  
ANISOU 2362  OD1 ASN A 311    17168  15020  13531  -2486  -1024   1584  A    O  
ATOM   2363  N   HIS A 312      52.294  -8.476  16.172  1.00 95.62      A    N  
ANISOU 2363  N   HIS A 312    14077  11681  10575  -2188  -1322   1927  A    N  
ATOM   2364  CA  HIS A 312      52.868  -9.490  17.050  1.00 97.40      A    C  
ANISOU 2364  CA  HIS A 312    14469  11892  10646  -2147  -1436   2062  A    C  
ATOM   2365  C   HIS A 312      54.332  -9.195  17.366  1.00 95.43      A    C  
ANISOU 2365  C   HIS A 312    14186  11777  10295  -2064  -1631   2063  A    C  
ATOM   2366  O   HIS A 312      55.074  -8.720  16.509  1.00102.54      A    O  
ANISOU 2366  O   HIS A 312    14913  12740  11306  -1994  -1711   1996  A    O  
ATOM   2367  CB  HIS A 312      52.739 -10.854  16.373  1.00 95.23      A    C  
ANISOU 2367  CB  HIS A 312    14223  11474  10487  -2059  -1474   2156  A    C  
ATOM   2368  CG  HIS A 312      53.022 -12.019  17.268  1.00 96.44      A    C  
ANISOU 2368  CG  HIS A 312    14585  11562  10497  -2026  -1551   2315  A    C  
ATOM   2369  CD2 HIS A 312      52.189 -12.818  17.977  1.00 99.40      A    C  
ANISOU 2369  CD2 HIS A 312    15146  11820  10801  -2107  -1450   2422  A    C  
ATOM   2370  ND1 HIS A 312      54.293 -12.510  17.472  1.00 91.75      A    N  
ANISOU 2370  ND1 HIS A 312    14025  11018   9819  -1887  -1754   2387  A    N  
ATOM   2371  CE1 HIS A 312      54.233 -13.553  18.281  1.00 96.58      A    C  
ANISOU 2371  CE1 HIS A 312    14849  11539  10307  -1872  -1780   2537  A    C  
ATOM   2372  NE2 HIS A 312      52.969 -13.760  18.603  1.00 98.86      A    N  
ANISOU 2372  NE2 HIS A 312    15238  11721  10603  -2012  -1592   2566  A    N  
ATOM   2373  N   ASP A 313      54.747  -9.494  18.591  1.00 93.87      A    N  
ANISOU 2373  N   ASP A 313    14150  11634   9884  -2070  -1706   2140  A    N  
ATOM   2374  CA  ASP A 313      56.102  -9.175  19.045  1.00100.19      A    C  
ANISOU 2374  CA  ASP A 313    14918  12586  10565  -2000  -1896   2126  A    C  
ATOM   2375  C   ASP A 313      57.186  -9.818  18.180  1.00102.16      A    C  
ANISOU 2375  C   ASP A 313    15053  12847  10915  -1832  -2071   2163  A    C  
ATOM   2376  O   ASP A 313      58.358  -9.475  18.282  1.00104.36      A    O  
ANISOU 2376  O   ASP A 313    15242  13267  11144  -1767  -2228   2127  A    O  
ATOM   2377  CB  ASP A 313      56.288  -9.568  20.514  1.00105.04      A    C  
ANISOU 2377  CB  ASP A 313    15744  13253  10913  -2010  -1952   2217  A    C  
ATOM   2378  CG  ASP A 313      55.317  -8.853  21.438  1.00120.04      A    C  
ANISOU 2378  CG  ASP A 313    17748  15175  12685  -2167  -1784   2167  A    C  
ATOM   2379  OD1 ASP A 313      55.730  -7.880  22.110  1.00119.36      A    O  
ANISOU 2379  OD1 ASP A 313    17646  15230  12475  -2216  -1823   2067  A    O  
ATOM   2380  OD2 ASP A 313      54.135  -9.264  21.489  1.00131.29      A    O1-
ANISOU 2380  OD2 ASP A 313    19266  16481  14137  -2241  -1612   2218  A    O1-
ATOM   2381  N   PHE A 314      56.788 -10.754  17.331  1.00101.69      A    N  
ANISOU 2381  N   PHE A 314    14992  12646  11000  -1760  -2044   2224  A    N  
ATOM   2382  CA  PHE A 314      57.706 -11.379  16.393  1.00 97.24      A    C  
ANISOU 2382  CA  PHE A 314    14314  12086  10547  -1589  -2193   2246  A    C  
ATOM   2383  C   PHE A 314      58.243 -10.343  15.410  1.00 90.44      A    C  
ANISOU 2383  C   PHE A 314    13205  11337   9822  -1579  -2204   2118  A    C  
ATOM   2384  O   PHE A 314      59.417 -10.356  15.037  1.00 88.73      A    O  
ANISOU 2384  O   PHE A 314    12863  11230   9621  -1463  -2356   2106  A    O  
ATOM   2385  CB  PHE A 314      56.973 -12.499  15.653  1.00100.83      A    C  
ANISOU 2385  CB  PHE A 314    14821  12349  11141  -1537  -2135   2310  A    C  
ATOM   2386  CG  PHE A 314      57.701 -13.028  14.449  1.00103.01      A    C  
ANISOU 2386  CG  PHE A 314    14955  12619  11565  -1363  -2252   2298  A    C  
ATOM   2387  CD1 PHE A 314      58.960 -13.581  14.564  1.00104.97      A    C  
ANISOU 2387  CD1 PHE A 314    15195  12943  11745  -1198  -2452   2352  A    C  
ATOM   2388  CD2 PHE A 314      57.102 -13.005  13.202  1.00105.98      A    C  
ANISOU 2388  CD2 PHE A 314    15204  12922  12141  -1352  -2163   2229  A    C  
ATOM   2389  CE1 PHE A 314      59.619 -14.080  13.458  1.00103.25      A    C  
ANISOU 2389  CE1 PHE A 314    14842  12730  11657  -1028  -2553   2334  A    C  
ATOM   2390  CE2 PHE A 314      57.757 -13.504  12.093  1.00104.35      A    C  
ANISOU 2390  CE2 PHE A 314    14871  12721  12057  -1182  -2266   2212  A    C  
ATOM   2391  CZ  PHE A 314      59.017 -14.041  12.223  1.00101.16      A    C  
ANISOU 2391  CZ  PHE A 314    14458  12393  11584  -1021  -2457   2264  A    C  
ATOM   2392  N   PHE A 315      57.376  -9.431  14.999  1.00 86.68      A    N  
ANISOU 2392  N   PHE A 315    12657  10836   9443  -1697  -2038   2025  A    N  
ATOM   2393  CA  PHE A 315      57.766  -8.412  14.040  1.00 91.14      A    C  
ANISOU 2393  CA  PHE A 315    13005  11483  10139  -1696  -2022   1918  A    C  
ATOM   2394  C   PHE A 315      58.426  -7.224  14.720  1.00 93.08      A    C  
ANISOU 2394  C   PHE A 315    13201  11872  10291  -1787  -2059   1839  A    C  
ATOM   2395  O   PHE A 315      59.053  -6.387  14.065  1.00 81.80      A    O  
ANISOU 2395  O   PHE A 315    11597  10529   8955  -1787  -2078   1763  A    O  
ATOM   2396  CB  PHE A 315      56.546  -7.963  13.245  1.00 93.26      A    C  
ANISOU 2396  CB  PHE A 315    13223  11656  10554  -1762  -1835   1855  A    C  
ATOM   2397  CG  PHE A 315      55.957  -9.048  12.410  1.00 90.60      A    C  
ANISOU 2397  CG  PHE A 315    12897  11191  10337  -1673  -1809   1901  A    C  
ATOM   2398  CD1 PHE A 315      54.781  -9.665  12.785  1.00 87.10      A    C  
ANISOU 2398  CD1 PHE A 315    12595  10615   9884  -1743  -1698   1940  A    C  
ATOM   2399  CD2 PHE A 315      56.596  -9.470  11.258  1.00 89.64      A    C  
ANISOU 2399  CD2 PHE A 315    12638  11086  10335  -1523  -1897   1901  A    C  
ATOM   2400  CE1 PHE A 315      54.243 -10.666  12.016  1.00 83.36      A    C  
ANISOU 2400  CE1 PHE A 315    12125  10016   9531  -1675  -1681   1967  A    C  
ATOM   2401  CE2 PHE A 315      56.062 -10.473  10.489  1.00 87.21      A    C  
ANISOU 2401  CE2 PHE A 315    12342  10658  10137  -1438  -1883   1925  A    C  
ATOM   2402  CZ  PHE A 315      54.885 -11.075  10.872  1.00 82.71      A    C  
ANISOU 2402  CZ  PHE A 315    11914   9944   9567  -1519  -1779   1955  A    C  
ATOM   2403  N   TRP A 316      58.283  -7.174  16.042  1.00105.69      A    N  
ANISOU 2403  N   TRP A 316    14959  13494  11702  -1866  -2067   1856  A    N  
ATOM   2404  CA  TRP A 316      58.810  -6.079  16.853  1.00110.05      A    C  
ANISOU 2404  CA  TRP A 316    15492  14176  12144  -1963  -2105   1765  A    C  
ATOM   2405  C   TRP A 316      59.758  -6.557  17.954  1.00114.44      A    C  
ANISOU 2405  C   TRP A 316    16138  14847  12495  -1910  -2288   1816  A    C  
ATOM   2406  O   TRP A 316      59.537  -6.293  19.135  1.00124.83      A    O  
ANISOU 2406  O   TRP A 316    17595  16205  13631  -1990  -2278   1803  A    O  
ATOM   2407  CB  TRP A 316      57.653  -5.295  17.461  1.00102.85      A    C  
ANISOU 2407  CB  TRP A 316    14682  13214  11184  -2116  -1927   1699  A    C  
ATOM   2408  CG  TRP A 316      56.667  -4.899  16.434  1.00 95.72      A    C  
ANISOU 2408  CG  TRP A 316    13699  12203  10466  -2147  -1756   1654  A    C  
ATOM   2409  CD1 TRP A 316      55.475  -5.490  16.178  1.00 95.02      A    C  
ANISOU 2409  CD1 TRP A 316    13684  11990  10431  -2154  -1622   1698  A    C  
ATOM   2410  CD2 TRP A 316      56.802  -3.836  15.488  1.00 98.92      A    C  
ANISOU 2410  CD2 TRP A 316    13932  12623  11031  -2170  -1703   1556  A    C  
ATOM   2411  CE2 TRP A 316      55.643  -3.832  14.703  1.00 94.17      A    C  
ANISOU 2411  CE2 TRP A 316    13312  11909  10559  -2172  -1543   1546  A    C  
ATOM   2412  CE3 TRP A 316      57.791  -2.883  15.236  1.00103.10      A    C  
ANISOU 2412  CE3 TRP A 316    14320  13248  11606  -2193  -1773   1479  A    C  
ATOM   2413  NE1 TRP A 316      54.845  -4.851  15.143  1.00 94.46      A    N  
ANISOU 2413  NE1 TRP A 316    13492  11867  10533  -2168  -1498   1625  A    N  
ATOM   2414  CZ2 TRP A 316      55.447  -2.912  13.683  1.00 94.77      A    C  
ANISOU 2414  CZ2 TRP A 316    13249  11967  10794  -2177  -1455   1470  A    C  
ATOM   2415  CZ3 TRP A 316      57.588  -1.971  14.224  1.00 96.22      A    C  
ANISOU 2415  CZ3 TRP A 316    13315  12343  10901  -2215  -1672   1412  A    C  
ATOM   2416  CH2 TRP A 316      56.430  -1.990  13.462  1.00 93.40      A    C  
ANISOU 2416  CH2 TRP A 316    12958  11875  10657  -2198  -1518   1413  A    C  
ATOM   2417  N   SER A 317      60.809  -7.262  17.551  1.00107.17      A    N  
ANISOU 2417  N   SER A 317    15136  13988  11596  -1762  -2456   1871  A    N  
ATOM   2418  CA  SER A 317      61.835  -7.748  18.464  1.00111.06      A    C  
ANISOU 2418  CA  SER A 317    15686  14608  11903  -1676  -2655   1917  A    C  
ATOM   2419  C   SER A 317      63.024  -8.159  17.609  1.00117.03      A    C  
ANISOU 2419  C   SER A 317    16257  15452  12758  -1519  -2813   1927  A    C  
ATOM   2420  O   SER A 317      62.884  -8.317  16.394  1.00118.65      A    O  
ANISOU 2420  O   SER A 317    16342  15588  13150  -1467  -2755   1928  A    O  
ATOM   2421  CB  SER A 317      61.327  -8.941  19.267  1.00108.59      A    C  
ANISOU 2421  CB  SER A 317    15624  14200  11438  -1615  -2663   2064  A    C  
ATOM   2422  OG  SER A 317      61.212 -10.089  18.445  1.00108.10      A    O  
ANISOU 2422  OG  SER A 317    15574  14009  11491  -1481  -2676   2167  A    O  
ATOM   2423  N   ASP A 318      64.191  -8.330  18.221  1.00113.93      A    N  
ANISOU 2423  N   ASP A 318    15831  15223  12233  -1435  -3012   1928  A    N  
ATOM   2424  CA  ASP A 318      65.380  -8.629  17.430  1.00112.28      A    C  
ANISOU 2424  CA  ASP A 318    15418  15128  12114  -1286  -3161   1920  A    C  
ATOM   2425  C   ASP A 318      65.487 -10.100  17.075  1.00109.24      A    C  
ANISOU 2425  C   ASP A 318    15116  14655  11735  -1077  -3243   2055  A    C  
ATOM   2426  O   ASP A 318      65.074 -10.956  17.851  1.00106.07      A    O  
ANISOU 2426  O   ASP A 318    14945  14161  11196  -1028  -3265   2165  A    O  
ATOM   2427  CB  ASP A 318      66.649  -8.121  18.114  1.00120.61      A    C  
ANISOU 2427  CB  ASP A 318    16355  16419  13051  -1282  -3347   1840  A    C  
ATOM   2428  CG  ASP A 318      66.847  -6.623  17.925  1.00127.22      A    C  
ANISOU 2428  CG  ASP A 318    17014  17345  13980  -1469  -3278   1683  A    C  
ATOM   2429  OD1 ASP A 318      67.027  -6.174  16.766  1.00122.17      A    O  
ANISOU 2429  OD1 ASP A 318    16178  16703  13539  -1487  -3210   1639  A    O  
ATOM   2430  OD2 ASP A 318      66.809  -5.894  18.938  1.00131.90      A    O1-
ANISOU 2430  OD2 ASP A 318    17671  18003  14442  -1598  -3290   1603  A    O1-
ATOM   2431  N   PRO A 319      66.004 -10.393  15.870  1.00113.25      A    N  
ANISOU 2431  N   PRO A 319    15443  15182  12407   -955  -3277   2047  A    N  
ATOM   2432  CA  PRO A 319      66.393  -9.377  14.881  1.00110.32      A    C  
ANISOU 2432  CA  PRO A 319    14808  14905  12202  -1022  -3220   1934  A    C  
ATOM   2433  C   PRO A 319      65.179  -8.722  14.232  1.00100.27      A    C  
ANISOU 2433  C   PRO A 319    13545  13482  11070  -1168  -2991   1897  A    C  
ATOM   2434  O   PRO A 319      64.172  -9.385  14.002  1.00101.02      A    O  
ANISOU 2434  O   PRO A 319    13782  13398  11203  -1148  -2893   1963  A    O  
ATOM   2435  CB  PRO A 319      67.158 -10.187  13.818  1.00110.49      A    C  
ANISOU 2435  CB  PRO A 319    14682  14971  12329   -809  -3318   1967  A    C  
ATOM   2436  CG  PRO A 319      67.422 -11.526  14.428  1.00111.87      A    C  
ANISOU 2436  CG  PRO A 319    15028  15106  12371   -624  -3471   2079  A    C  
ATOM   2437  CD  PRO A 319      66.309 -11.754  15.402  1.00113.74      A    C  
ANISOU 2437  CD  PRO A 319    15547  15177  12493   -730  -3380   2148  A    C  
ATOM   2438  N   MET A 320      65.265  -7.433  13.936  1.00 98.14      A    N  
ANISOU 2438  N   MET A 320    13126  13281  10882  -1313  -2907   1792  A    N  
ATOM   2439  CA  MET A 320      64.175  -6.779  13.228  1.00 99.05      A    C  
ANISOU 2439  CA  MET A 320    13238  13264  11134  -1423  -2698   1756  A    C  
ATOM   2440  C   MET A 320      64.131  -7.294  11.803  1.00109.34      A    C  
ANISOU 2440  C   MET A 320    14423  14520  12601  -1289  -2661   1787  A    C  
ATOM   2441  O   MET A 320      65.137  -7.807  11.296  1.00112.81      A    O  
ANISOU 2441  O   MET A 320    14730  15066  13066  -1140  -2788   1806  A    O  
ATOM   2442  CB  MET A 320      64.343  -5.268  13.238  1.00 93.09      A    C  
ANISOU 2442  CB  MET A 320    12361  12579  10429  -1598  -2623   1642  A    C  
ATOM   2443  CG  MET A 320      64.144  -4.669  14.593  1.00 92.48      A    C  
ANISOU 2443  CG  MET A 320    12417  12523  10198  -1743  -2629   1588  A    C  
ATOM   2444  SD  MET A 320      62.482  -4.991  15.165  1.00104.14      A    S  
ANISOU 2444  SD  MET A 320    14156  13804  11607  -1806  -2468   1634  A    S  
ATOM   2445  CE  MET A 320      61.606  -3.586  14.496  1.00 73.16      A    C  
ANISOU 2445  CE  MET A 320    10163   9796   7840  -1960  -2251   1531  A    C  
ATOM   2446  N   PRO A 321      62.961  -7.173  11.153  1.00107.53      A    N  
ANISOU 2446  N   PRO A 321    14237  14142  12477  -1330  -2491   1784  A    N  
ATOM   2447  CA  PRO A 321      62.822  -7.673   9.782  1.00101.59      A    C  
ANISOU 2447  CA  PRO A 321    13383  13346  11871  -1196  -2455   1801  A    C  
ATOM   2448  C   PRO A 321      63.755  -6.889   8.870  1.00 94.60      A    C  
ANISOU 2448  C   PRO A 321    12253  12609  11083  -1175  -2462   1751  A    C  
ATOM   2449  O   PRO A 321      63.836  -5.670   9.025  1.00 83.22      A    O  
ANISOU 2449  O   PRO A 321    10745  11215   9659  -1325  -2391   1690  A    O  
ATOM   2450  CB  PRO A 321      61.359  -7.372   9.447  1.00 97.44      A    C  
ANISOU 2450  CB  PRO A 321    12941  12662  11420  -1285  -2264   1781  A    C  
ATOM   2451  CG  PRO A 321      60.681  -7.156  10.785  1.00 97.66      A    C  
ANISOU 2451  CG  PRO A 321    13159  12628  11320  -1433  -2220   1782  A    C  
ATOM   2452  CD  PRO A 321      61.724  -6.543  11.647  1.00100.70      A    C  
ANISOU 2452  CD  PRO A 321    13505  13160  11595  -1493  -2329   1752  A    C  
ATOM   2453  N   SER A 322      64.446  -7.569   7.956  1.00 95.12      A    N  
ANISOU 2453  N   SER A 322    12190  12744  11208   -996  -2541   1776  A    N  
ATOM   2454  CA  SER A 322      65.417  -6.918   7.080  1.00 97.72      A    C  
ANISOU 2454  CA  SER A 322    12275  13235  11620   -966  -2546   1742  A    C  
ATOM   2455  C   SER A 322      65.082  -7.125   5.613  1.00 88.61      A    C  
ANISOU 2455  C   SER A 322    11024  12050  10594   -845  -2458   1747  A    C  
ATOM   2456  O   SER A 322      64.310  -8.005   5.280  1.00 97.59      A    O  
ANISOU 2456  O   SER A 322    12267  13060  11752   -747  -2441   1771  A    O  
ATOM   2457  CB  SER A 322      66.820  -7.462   7.354  1.00111.36      A    C  
ANISOU 2457  CB  SER A 322    13893  15139  13281   -846  -2741   1754  A    C  
ATOM   2458  OG  SER A 322      66.926  -8.818   6.952  1.00116.46      A    O  
ANISOU 2458  OG  SER A 322    14577  15751  13921   -626  -2837   1807  A    O  
ATOM   2459  N   ASP A 323      65.679  -6.326   4.736  1.00 90.90      A    N  
ANISOU 2459  N   ASP A 323    11110  12462  10966   -850  -2402   1723  A    N  
ATOM   2460  CA  ASP A 323      65.496  -6.497   3.295  1.00100.65      A    C  
ANISOU 2460  CA  ASP A 323    12236  13705  12302   -714  -2325   1730  A    C  
ATOM   2461  C   ASP A 323      66.062  -7.814   2.744  1.00101.56      A    C  
ANISOU 2461  C   ASP A 323    12302  13876  12409   -471  -2456   1753  A    C  
ATOM   2462  O   ASP A 323      66.665  -8.607   3.478  1.00100.33      A    O  
ANISOU 2462  O   ASP A 323    12193  13754  12172   -399  -2613   1773  A    O  
ATOM   2463  CB  ASP A 323      66.062  -5.298   2.535  1.00114.62      A    C  
ANISOU 2463  CB  ASP A 323    13806  15596  14147   -783  -2226   1715  A    C  
ATOM   2464  CG  ASP A 323      65.069  -4.148   2.451  1.00136.02      A    C  
ANISOU 2464  CG  ASP A 323    16582  18187  16910   -948  -2046   1696  A    C  
ATOM   2465  OD1 ASP A 323      65.491  -3.015   2.124  1.00141.96      A    O  
ANISOU 2465  OD1 ASP A 323    17215  19005  17718  -1053  -1960   1688  A    O  
ATOM   2466  OD2 ASP A 323      63.863  -4.381   2.711  1.00139.91      A    O1-
ANISOU 2466  OD2 ASP A 323    17247  18518  17394   -971  -1989   1687  A    O1-
ATOM   2467  N   LEU A 324      65.848  -8.055   1.453  1.00101.91      A    N  
ANISOU 2467  N   LEU A 324    12260  13929  12530   -331  -2395   1748  A    N  
ATOM   2468  CA  LEU A 324      66.288  -9.308   0.845  1.00105.06      A    C  
ANISOU 2468  CA  LEU A 324    12622  14367  12929    -87  -2510   1754  A    C  
ATOM   2469  C   LEU A 324      67.299  -9.112  -0.283  1.00121.87      A    C  
ANISOU 2469  C   LEU A 324    14504  16705  15097     48  -2509   1746  A    C  
ATOM   2470  O   LEU A 324      67.059  -8.411  -1.276  1.00110.64      A    O  
ANISOU 2470  O   LEU A 324    12979  15323  13738     40  -2372   1739  A    O  
ATOM   2471  CB  LEU A 324      65.110 -10.165   0.385  1.00 99.04      A    C  
ANISOU 2471  CB  LEU A 324    12006  13419  12207      3  -2477   1741  A    C  
ATOM   2472  CG  LEU A 324      64.092 -10.558   1.458  1.00 94.03      A    C  
ANISOU 2472  CG  LEU A 324    11614  12577  11535   -115  -2475   1755  A    C  
ATOM   2473  CD1 LEU A 324      63.239  -9.353   1.832  1.00108.36      A    C  
ANISOU 2473  CD1 LEU A 324    13478  14331  13363   -340  -2319   1742  A    C  
ATOM   2474  CD2 LEU A 324      63.201 -11.693   0.983  1.00 70.06      A    C  
ANISOU 2474  CD2 LEU A 324     8697   9375   8546      4  -2483   1739  A    C  
ATOM   2475  N   LYS A 325      68.449  -9.742  -0.073  1.00143.27      A    N  
ANISOU 2475  N   LYS A 325    17122  19555  17759    178  -2663   1751  A    N  
ATOM   2476  CA  LYS A 325      69.575  -9.730  -0.987  1.00143.93      A    C  
ANISOU 2476  CA  LYS A 325    16959  19867  17861    325  -2688   1742  A    C  
ATOM   2477  C   LYS A 325      70.230 -11.094  -0.785  1.00141.91      A    C  
ANISOU 2477  C   LYS A 325    16722  19647  17550    556  -2882   1738  A    C  
ATOM   2478  O   LYS A 325      71.118 -11.497  -1.539  1.00138.85      A    O  
ANISOU 2478  O   LYS A 325    16158  19433  17166    750  -2939   1722  A    O  
ATOM   2479  CB  LYS A 325      70.526  -8.577  -0.645  1.00143.37      A    C  
ANISOU 2479  CB  LYS A 325    16708  19978  17789    158  -2661   1745  A    C  
ATOM   2480  CG  LYS A 325      69.858  -7.189  -0.681  1.00142.08      A    C  
ANISOU 2480  CG  LYS A 325    16563  19741  17681    -86  -2475   1752  A    C  
ATOM   2481  CD  LYS A 325      70.670  -6.114   0.061  1.00141.20      A    C  
ANISOU 2481  CD  LYS A 325    16339  19746  17566   -299  -2476   1741  A    C  
ATOM   2482  CE  LYS A 325      71.925  -5.673  -0.712  1.00133.22      A    C  
ANISOU 2482  CE  LYS A 325    15035  18986  16595   -264  -2456   1744  A    C  
ATOM   2483  NZ  LYS A 325      72.813  -4.733   0.058  1.00120.46      A    N1+
ANISOU 2483  NZ  LYS A 325    13291  17493  14983   -474  -2480   1718  A    N1+
ATOM   2484  N   GLY A 326      69.771 -11.789   0.258  1.00139.03      A    N  
ANISOU 2484  N   GLY A 326    16581  19114  17131    536  -2978   1757  A    N  
ATOM   2485  CA  GLY A 326      69.972 -13.222   0.404  1.00141.03      A    C  
ANISOU 2485  CA  GLY A 326    16937  19301  17345    761  -3140   1764  A    C  
ATOM   2486  C   GLY A 326      69.085 -13.908  -0.620  1.00138.37      A    C  
ANISOU 2486  C   GLY A 326    16675  18818  17081    893  -3081   1735  A    C  
ATOM   2487  O   GLY A 326      68.053 -14.514  -0.290  1.00122.10      A    O  
ANISOU 2487  O   GLY A 326    14836  16522  15033    865  -3074   1744  A    O  
ATOM   2488  N   MET A 327      69.521 -13.800  -1.874  1.00152.42      A    N  
ANISOU 2488  N   MET A 327    18256  20751  18905   1035  -3038   1696  A    N  
ATOM   2489  CA  MET A 327      68.723 -14.085  -3.064  1.00157.45      A    C  
ANISOU 2489  CA  MET A 327    18903  21310  19611   1140  -2949   1651  A    C  
ATOM   2490  C   MET A 327      68.778 -15.551  -3.496  1.00153.70      A    C  
ANISOU 2490  C   MET A 327    18500  20756  19143   1409  -3081   1609  A    C  
ATOM   2491  O   MET A 327      68.503 -15.878  -4.656  1.00145.39      A    O  
ANISOU 2491  O   MET A 327    17392  19714  18136   1562  -3043   1549  A    O  
ATOM   2492  CB  MET A 327      69.226 -13.197  -4.205  1.00163.38      A    C  
ANISOU 2492  CB  MET A 327    19404  22286  20388   1169  -2832   1635  A    C  
ATOM   2493  CG  MET A 327      70.747 -13.282  -4.394  1.00172.14      A    C  
ANISOU 2493  CG  MET A 327    20286  23664  21457   1311  -2925   1636  A    C  
ATOM   2494  SD  MET A 327      71.484 -12.085  -5.532  1.00229.35      A    S  
ANISOU 2494  SD  MET A 327    27224  31194  28725   1291  -2768   1645  A    S  
ATOM   2495  CE  MET A 327      71.599 -10.618  -4.508  1.00100.41      A    C  
ANISOU 2495  CE  MET A 327    10871  14878  12401    939  -2681   1698  A    C  
TER   
HETATM 2496  CA' SLQ A 331      58.725 -17.063 -11.009  0.99103.45      C    C  
HETATM 2497  C6' SLQ A 331      59.125 -19.207 -12.289  0.99104.00      C    C  
HETATM 2498  C5' SLQ A 331      59.706 -19.863 -13.383  0.99114.93      C    C  
HETATM 2499  C4' SLQ A 331      60.515 -19.137 -14.284  0.99118.84      C    C  
HETATM 2500  C3' SLQ A 331      60.736 -17.767 -14.095  0.99106.37      C    C  
HETATM 2501  C2' SLQ A 331      60.165 -17.110 -13.012  0.99 97.65      C    C  
HETATM 2502  C1' SLQ A 331      59.382 -17.839 -12.121  0.99102.38      C    C  
HETATM 2503  C1B SLQ A 331      61.102 -19.734 -15.393  0.99125.95      C    C  
HETATM 2504  N1  SLQ A 331      55.336 -17.504 -11.365  0.99 90.63      C    N  
HETATM 2505  N1B SLQ A 331      61.824 -18.944 -16.267  0.99118.45      C    N  
HETATM 2506  O1  SLQ A 331      52.564 -20.630 -12.495  0.99115.37      C    O  
HETATM 2507  C2  SLQ A 331      53.986 -17.467 -11.485  0.99 91.04      C    C  
HETATM 2508  C2B SLQ A 331      60.934 -21.108 -15.634  0.99127.96      C    C  
HETATM 2509  N2  SLQ A 331      53.185 -18.583 -11.030  0.99 96.76      C    N  
HETATM 2510  C3B SLQ A 331      61.513 -21.667 -16.746  0.99129.35      C    C  
HETATM 2511  N3  SLQ A 331      53.386 -16.335 -11.937  0.99 97.59      C    N  
HETATM 2512  C4  SLQ A 331      54.122 -15.261 -12.274  0.99 93.44      C    C  
HETATM 2513  C4B SLQ A 331      62.237 -20.874 -17.609  0.99128.52      C    C  
HETATM 2514  C5  SLQ A 331      55.473 -15.304 -12.161  0.99 91.42      C    C  
HETATM 2515  C5B SLQ A 331      62.399 -19.498 -17.376  0.99117.02      C    C  
HETATM 2516  C6  SLQ A 331      56.067 -16.441 -11.700  0.99 93.26      C    C  
HETATM 2517  N6  SLQ A 331      57.489 -16.504 -11.496  0.99 98.72      C    N  
HETATM 2518  N7  SLQ A 331      55.961 -14.132 -12.560  0.99 88.25      C    N  
HETATM 2519  C8  SLQ A 331      54.916 -13.357 -12.926  0.99 85.52      C    C  
HETATM 2520  C9  SLQ A 331      52.420 -13.606 -12.980  0.99 86.45      C    C  
HETATM 2521  N9  SLQ A 331      53.781 -14.061 -12.744  0.99 85.43      C    N  
HETATM 2522  C10 SLQ A 331      51.679 -14.328 -14.104  0.99 88.90      C    C  
HETATM 2523  C11 SLQ A 331      51.593 -13.467 -11.705  0.99 79.25      C    C  
HETATM 2524  C12 SLQ A 331      52.057 -19.299 -10.465  0.99109.34      C    C  
HETATM 2525  C13 SLQ A 331      50.789 -18.439 -10.557  0.99108.99      C    C  
HETATM 2526  C14 SLQ A 331      49.479 -19.114 -10.156  0.99110.16      C    C  
HETATM 2527  C15 SLQ A 331      51.879 -20.558 -11.275  0.99117.92      C    C  
HETATM 2528  O   HOH A 332      62.355  -6.104   0.809  1.00 72.90      D    O  
HETATM 2529  O   HOH A 333      42.660 -10.598   8.086  1.00 43.58      D    O  
HETATM 2530  O   HOH A 334      33.431 -12.365  -6.796  1.00 49.80      D    O  
HETATM 2531  O   HOH A 335      66.983 -19.127   9.823  1.00 69.78      D    O  
HETATM 2532  O   HOH A 336      48.644 -14.349 -10.831  1.00 55.67      D    O  
HETATM 2533  O   HOH B 260      25.616  11.020 -30.075  1.00 62.00      E    O  
HETATM 2534  O   HOH B 261      31.830   3.562 -14.505  1.00 82.88      E    O  
HETATM 2535  O   HOH B 262       8.048  -9.910 -28.664  1.00 75.16      E    O  
HETATM 2536  O   HOH B 263       9.061 -15.394 -31.342  1.00 68.43      E    O  
CONECT 1329 1339
CONECT 1339 1329 1340
CONECT 1340 1339 1341 1343
CONECT 1341 1340 1342 1350
CONECT 1342 1341
CONECT 1343 1340 1344 1345
CONECT 1344 1343
CONECT 1345 1343 1346
CONECT 1346 1345 1347 1348 1349
CONECT 1347 1346
CONECT 1348 1346
CONECT 1349 1346
CONECT 1350 1341
CONECT 2496 2502 2517
CONECT 2497 2498 2502
CONECT 2498 2497 2499
CONECT 2499 2498 2500 2503
CONECT 2500 2499 2501
CONECT 2501 2500 2502
CONECT 2502 2496 2497 2501
CONECT 2503 2499 2505 2508
CONECT 2504 2507 2516
CONECT 2505 2503 2515
CONECT 2506 2527
CONECT 2507 2504 2509 2511
CONECT 2508 2503 2510
CONECT 2509 2507 2524
CONECT 2510 2508 2513
CONECT 2511 2507 2512
CONECT 2512 2511 2514 2521
CONECT 2513 2510 2515
CONECT 2514 2512 2516 2518
CONECT 2515 2505 2513
CONECT 2516 2504 2514 2517
CONECT 2517 2516 2496
CONECT 2518 2514 2519
CONECT 2519 2518 2521
CONECT 2520 2521 2522 2523
CONECT 2521 2512 2519 2520
CONECT 2522 2520
CONECT 2523 2520
CONECT 2524 2509 2525 2527
CONECT 2525 2524 2526
CONECT 2526 2525
CONECT 2527 2506 2524
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.