CNRS Nantes University US2B US2B
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***  6et7_20240709  ***

elNémo ID: 2407091543422795003

Job options:

ID        	=	 2407091543422795003
JOBID     	=	 6et7_20240709
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 6et7_20240709

ATOM      1  N   ILE A  24      16.264  51.492 480.418  1.00 64.81      A    N  
ANISOU    1  N   ILE A  24     9688   5401   9534   1358  -1227   -839  A    N  
ATOM      2  CA  ILE A  24      15.863  52.743 479.787  1.00 48.90      A    C  
ANISOU    2  CA  ILE A  24     7559   3295   7725   1250  -1085   -899  A    C  
ATOM      3  C   ILE A  24      17.105  53.542 479.408  1.00 60.92      A    C  
ANISOU    3  C   ILE A  24     8850   4666   9632   1122  -1320  -1098  A    C  
ATOM      4  O   ILE A  24      17.331  54.625 479.964  1.00 80.78      A    O  
ANISOU    4  O   ILE A  24    11442   7064  12186   1148  -1479  -1321  A    O  
ATOM      5  CB  ILE A  24      14.931  53.537 480.715  1.00 50.51      A    C  
ANISOU    5  CB  ILE A  24     8058   3485   7649   1394  -1001   -986  A    C  
ATOM      6  CG1 ILE A  24      15.437  53.479 482.160  1.00 58.86      A    C  
ANISOU    6  CG1 ILE A  24     9433   4541   8392   1580  -1301  -1176  A    C  
ATOM      7  CG2 ILE A  24      13.530  52.995 480.642  1.00 49.14      A    C  
ANISOU    7  CG2 ILE A  24     7978   3417   7277   1451   -638   -761  A    C  
ATOM      8  CD1 ILE A  24      14.921  54.556 483.030  1.00 56.24      A    C  
ANISOU    8  CD1 ILE A  24     9379   4135   7854   1703  -1294  -1362  A    C  
ATOM      9  N   PRO A  25      17.937  53.065 478.478  1.00 53.34      A    N  
ANISOU    9  N   PRO A  25     7601   3679   8987    981  -1328  -1039  A    N  
ATOM     10  CA  PRO A  25      19.104  53.846 478.068  1.00 52.73      A    C  
ANISOU   10  CA  PRO A  25     7265   3425   9344    842  -1482  -1220  A    C  
ATOM     11  C   PRO A  25      18.801  54.904 477.021  1.00 54.79      A    C  
ANISOU   11  C   PRO A  25     7403   3557   9859    687  -1224  -1177  A    C  
ATOM     12  O   PRO A  25      19.695  55.685 476.684  1.00 61.03      A    O  
ANISOU   12  O   PRO A  25     7990   4181  11016    557  -1285  -1312  A    O  
ATOM     13  CB  PRO A  25      20.025  52.774 477.484  1.00 49.71      A    C  
ANISOU   13  CB  PRO A  25     6640   3066   9183    774  -1517  -1143  A    C  
ATOM     14  CG  PRO A  25      19.085  51.820 476.856  1.00 46.83      A    C  
ANISOU   14  CG  PRO A  25     6346   2847   8599    779  -1218   -869  A    C  
ATOM     15  CD  PRO A  25      17.879  51.778 477.757  1.00 47.62      A    C  
ANISOU   15  CD  PRO A  25     6770   3060   8265    939  -1172   -818  A    C  
ATOM     16  N   ASN A  26      17.571  54.977 476.530  1.00 56.59      A    N  
ANISOU   16  N   ASN A  26     7745   3856   9902    703   -940   -987  A    N  
ATOM     17  CA  ASN A  26      17.202  55.907 475.460  1.00 72.41      A    C  
ANISOU   17  CA  ASN A  26     9669   5756  12088    583   -699   -898  A    C  
ATOM     18  C   ASN A  26      18.178  55.843 474.277  1.00 66.99      A    C  
ANISOU   18  C   ASN A  26     8730   5068  11656    391   -578   -818  A    C  
ATOM     19  O   ASN A  26      18.502  56.859 473.646  1.00 56.19      A    O  
ANISOU   19  O   ASN A  26     7276   3622  10451    273   -461   -820  A    O  
ATOM     20  CB  ASN A  26      17.060  57.328 476.011  1.00 70.43      A    C  
ANISOU   20  CB  ASN A  26     9508   5384  11867    604   -754  -1069  A    C  
ATOM     21  CG  ASN A  26      15.699  57.563 476.640  1.00 84.45      A    C  
ANISOU   21  CG  ASN A  26    11534   7185  13367    776   -676  -1051  A    C  
ATOM     22  ND2 ASN A  26      15.261  58.819 476.678  1.00100.81      A    N  
ANISOU   22  ND2 ASN A  26    13671   9150  15482    783   -597  -1114  A    N  
ATOM     23  OD1 ASN A  26      15.039  56.616 477.071  1.00 88.07      A    O  
ANISOU   23  OD1 ASN A  26    12109   7826  13525    887   -633   -946  A    O  
ATOM     24  N   ALA A  27      18.608  54.619 473.948  1.00 53.55      A    N  
ANISOU   24  N   ALA A  27     6930   3444   9973    373   -575   -736  A    N  
ATOM     25  CA  ALA A  27      19.521  54.361 472.842  1.00 45.26      A    C  
ANISOU   25  CA  ALA A  27     5661   2395   9139    220   -424   -663  A    C  
ATOM     26  C   ALA A  27      19.419  52.890 472.453  1.00 49.45      A    C  
ANISOU   26  C   ALA A  27     6185   3041   9565    246   -359   -524  A    C  
ATOM     27  O   ALA A  27      18.959  52.048 473.234  1.00 55.18      A    O  
ANISOU   27  O   ALA A  27     7026   3817  10122    378   -493   -518  A    O  
ATOM     28  CB  ALA A  27      20.965  54.732 473.209  1.00 47.90      A    C  
ANISOU   28  CB  ALA A  27     5754   2611   9835    147   -603   -868  A    C  
ATOM     29  N   ILE A  28      19.845  52.590 471.223  1.00 42.97      A    N  
ANISOU   29  N   ILE A  28     5252   2246   8830    128   -135   -411  A    N  
ATOM     30  CA  ILE A  28      19.812  51.231 470.705  1.00 41.59      A    C  
ANISOU   30  CA  ILE A  28     5069   2165   8568    136    -45   -295  A    C  
ATOM     31  C   ILE A  28      21.164  50.892 470.085  1.00 42.94      A    C  
ANISOU   31  C   ILE A  28     5000   2280   9034     39     44   -335  A    C  
ATOM     32  O   ILE A  28      21.931  51.772 469.697  1.00 44.68      A    O  
ANISOU   32  O   ILE A  28     5076   2404   9496    -58    133   -397  A    O  
ATOM     33  CB  ILE A  28      18.695  51.025 469.670  1.00 39.73      A    C  
ANISOU   33  CB  ILE A  28     4998   2027   8070    118    168   -106  A    C  
ATOM     34  CG1 ILE A  28      18.936  51.932 468.462  1.00 40.48      A    C  
ANISOU   34  CG1 ILE A  28     5092   2067   8221      9    380    -49  A    C  
ATOM     35  CG2 ILE A  28      17.348  51.265 470.306  1.00 38.74      A    C  
ANISOU   35  CG2 ILE A  28     5048   1949   7722    224     95    -67  A    C  
ATOM     36  CD1 ILE A  28      18.390  51.372 467.130  1.00 39.47      A    C  
ANISOU   36  CD1 ILE A  28     5092   2006   7899    -20    573    111  A    C  
ATOM     37  N   GLN A  29      21.448  49.586 469.999  1.00 42.40      A    N  
ANISOU   37  N   GLN A  29     4881   2261   8969     72     44   -298  A    N  
ATOM     38  CA  GLN A  29      22.569  49.117 469.205  1.00 43.58      A    C  
ANISOU   38  CA  GLN A  29     4819   2364   9378     -7    207   -308  A    C  
ATOM     39  C   GLN A  29      22.237  49.255 467.721  1.00 42.93      A    C  
ANISOU   39  C   GLN A  29     4850   2313   9150    -97    551   -166  A    C  
ATOM     40  O   GLN A  29      21.094  49.036 467.327  1.00 41.10      A    O  
ANISOU   40  O   GLN A  29     4850   2174   8593    -70    602    -47  A    O  
ATOM     41  CB  GLN A  29      22.879  47.663 469.526  1.00 43.33      A    C  
ANISOU   41  CB  GLN A  29     4729   2362   9371     74    113   -303  A    C  
ATOM     42  CG  GLN A  29      22.919  47.299 471.008  1.00 43.88      A    C  
ANISOU   42  CG  GLN A  29     4809   2412   9450    222   -261   -399  A    C  
ATOM     43  CD  GLN A  29      23.439  45.868 471.232  1.00 44.26      A    C  
ANISOU   43  CD  GLN A  29     4779   2463   9576    314   -346   -382  A    C  
ATOM     44  NE2 GLN A  29      22.582  45.006 471.777  1.00 45.87      A    N  
ANISOU   44  NE2 GLN A  29     5203   2745   9481    435   -427   -282  A    N  
ATOM     45  OE1 GLN A  29      24.587  45.539 470.887  1.00 45.98      A    O  
ANISOU   45  OE1 GLN A  29     4734   2603  10135    279   -310   -449  A    O  
ATOM     46  N   PRO A  30      23.221  49.585 466.864  1.00 49.54      A    N  
ANISOU   46  N   PRO A  30     5532   3059  10234   -190    788   -182  A    N  
ATOM     47  CA  PRO A  30      22.902  49.917 465.464  1.00 48.05      A    C  
ANISOU   47  CA  PRO A  30     5521   2865   9872   -252   1107    -51  A    C  
ATOM     48  C   PRO A  30      22.614  48.751 464.520  1.00 43.91      A    C  
ANISOU   48  C   PRO A  30     5142   2403   9140   -239   1279     44  A    C  
ATOM     49  O   PRO A  30      22.699  48.939 463.300  1.00 59.20      A    O  
ANISOU   49  O   PRO A  30     7206   4291  10997   -286   1563    122  A    O  
ATOM     50  CB  PRO A  30      24.163  50.658 464.999  1.00 47.80      A    C  
ANISOU   50  CB  PRO A  30     5264   2683  10215   -342   1329   -113  A    C  
ATOM     51  CG  PRO A  30      25.246  50.083 465.806  1.00 49.14      A    C  
ANISOU   51  CG  PRO A  30     5093   2802  10774   -326   1178   -263  A    C  
ATOM     52  CD  PRO A  30      24.634  49.875 467.176  1.00 54.34      A    C  
ANISOU   52  CD  PRO A  30     5797   3535  11314   -235    768   -329  A    C  
ATOM     53  N   PHE A  31      22.302  47.552 465.011  1.00 47.04      A    N  
ANISOU   53  N   PHE A  31     5544   2883   9444   -173   1129     38  A    N  
ATOM     54  CA  PHE A  31      21.945  46.506 464.057  1.00 42.93      A    C  
ANISOU   54  CA  PHE A  31     5185   2405   8720   -169   1290    114  A    C  
ATOM     55  C   PHE A  31      20.468  46.552 463.657  1.00 40.12      A    C  
ANISOU   55  C   PHE A  31     5124   2133   7986   -147   1231    219  A    C  
ATOM     56  O   PHE A  31      19.943  45.615 463.041  1.00 41.63      A    O  
ANISOU   56  O   PHE A  31     5463   2361   7994   -137   1279    264  A    O  
ATOM     57  CB  PHE A  31      22.386  45.121 464.567  1.00 41.64      A    C  
ANISOU   57  CB  PHE A  31     4887   2263   8670   -115   1207     64  A    C  
ATOM     58  CG  PHE A  31      21.705  44.633 465.821  1.00 40.08      A    C  
ANISOU   58  CG  PHE A  31     4709   2147   8372    -27    901     61  A    C  
ATOM     59  CD1 PHE A  31      22.176  45.001 467.068  1.00 40.70      A    C  
ANISOU   59  CD1 PHE A  31     4627   2189   8649     26    663    -25  A    C  
ATOM     60  CD2 PHE A  31      20.663  43.706 465.744  1.00 43.85      A    C  
ANISOU   60  CD2 PHE A  31     5369   2713   8581     11    860    135  A    C  
ATOM     61  CE1 PHE A  31      21.584  44.506 468.219  1.00 39.77      A    C  
ANISOU   61  CE1 PHE A  31     4580   2121   8410    134    413    -17  A    C  
ATOM     62  CE2 PHE A  31      20.061  43.205 466.885  1.00 37.51      A    C  
ANISOU   62  CE2 PHE A  31     4593   1964   7696     98    642    150  A    C  
ATOM     63  CZ  PHE A  31      20.522  43.602 468.129  1.00 38.17      A    C  
ANISOU   63  CZ  PHE A  31     4564   2008   7929    170    431     85  A    C  
ATOM     64  N   GLY A  32      19.820  47.670 463.941  1.00 43.78      A    N  
ANISOU   64  N   GLY A  32     5663   2604   8369   -141   1133    249  A    N  
ATOM     65  CA  GLY A  32      18.491  47.933 463.437  1.00 51.09      A    C  
ANISOU   65  CA  GLY A  32     6832   3570   9011   -117   1090    350  A    C  
ATOM     66  C   GLY A  32      18.115  49.365 463.732  1.00 49.73      A    C  
ANISOU   66  C   GLY A  32     6693   3362   8842   -108   1026    368  A    C  
ATOM     67  O   GLY A  32      18.942  50.160 464.185  1.00 57.14      A    O  
ANISOU   67  O   GLY A  32     7485   4233   9994   -140   1045    298  A    O  
ATOM     68  N   ALA A  33      16.842  49.683 463.502  1.00 49.53      A    N  
ANISOU   68  N   ALA A  33     6843   3364   8612    -59    938    452  A    N  
ATOM     69  CA  ALA A  33      16.292  50.996 463.838  1.00 49.83      A    C  
ANISOU   69  CA  ALA A  33     6923   3364   8646    -25    862    474  A    C  
ATOM     70  C   ALA A  33      15.070  50.790 464.712  1.00 37.24      A    C  
ANISOU   70  C   ALA A  33     5328   1855   6966     64    669    476  A    C  
ATOM     71  O   ALA A  33      14.490  49.707 464.741  1.00 47.06      A    O  
ANISOU   71  O   ALA A  33     6580   3174   8127     88    616    497  A    O  
ATOM     72  CB  ALA A  33      15.916  51.815 462.588  1.00 40.01      A    C  
ANISOU   72  CB  ALA A  33     5901   2028   7274    -27    973    596  A    C  
ATOM     73  N   MET A  34      14.675  51.820 465.430  1.00 37.44      A    N  
ANISOU   73  N   MET A  34     5338   1854   7032    113    587    451  A    N  
ATOM     74  CA  MET A  34      13.556  51.703 466.349  1.00 36.54      A    C  
ANISOU   74  CA  MET A  34     5210   1805   6868    210    455    446  A    C  
ATOM     75  C   MET A  34      12.615  52.891 466.198  1.00 58.59      A    C  
ANISOU   75  C   MET A  34     8088   4544   9630    280    424    500  A    C  
ATOM     76  O   MET A  34      13.059  54.036 466.047  1.00 49.63      A    O  
ANISOU   76  O   MET A  34     6988   3312   8558    259    467    485  A    O  
ATOM     77  CB  MET A  34      14.039  51.603 467.795  1.00 36.38      A    C  
ANISOU   77  CB  MET A  34     5080   1796   6948    243    371    324  A    C  
ATOM     78  CG  MET A  34      12.909  51.418 468.781  1.00 35.87      A    C  
ANISOU   78  CG  MET A  34     5030   1779   6820    356    294    327  A    C  
ATOM     79  SD  MET A  34      13.392  51.540 470.513  1.00 36.48      A    S  
ANISOU   79  SD  MET A  34     5087   1810   6962    441    184    181  A    S  
ATOM     80  CE  MET A  34      13.868  49.835 470.852  1.00 35.78      A    C  
ANISOU   80  CE  MET A  34     4956   1786   6853    442    155    198  A    C  
ATOM     81  N   LEU A  35      11.311  52.608 466.238  1.00 49.65      A    N  
ANISOU   81  N   LEU A  35     6969   3460   8436    364    353    562  A    N  
ATOM     82  CA  LEU A  35      10.275  53.626 466.344  1.00 44.62      A    C  
ANISOU   82  CA  LEU A  35     6363   2778   7813    467    303    600  A    C  
ATOM     83  C   LEU A  35       9.504  53.403 467.630  1.00 37.22      A    C  
ANISOU   83  C   LEU A  35     5322   1897   6922    557    268    543  A    C  
ATOM     84  O   LEU A  35       9.285  52.263 468.032  1.00 36.40      A    O  
ANISOU   84  O   LEU A  35     5152   1871   6809    553    269    541  A    O  
ATOM     85  CB  LEU A  35       9.285  53.601 465.170  1.00 38.30      A    C  
ANISOU   85  CB  LEU A  35     5650   1947   6954    519    243    734  A    C  
ATOM     86  CG  LEU A  35       9.684  53.867 463.720  1.00 39.39      A    C  
ANISOU   86  CG  LEU A  35     5985   1988   6993    481    278    837  A    C  
ATOM     87  CD1 LEU A  35       8.461  53.688 462.849  1.00 40.35      A    C  
ANISOU   87  CD1 LEU A  35     6187   2072   7072    582    134    958  A    C  
ATOM     88  CD2 LEU A  35      10.243  55.269 463.561  1.00 40.71      A    C  
ANISOU   88  CD2 LEU A  35     6247   2041   7180    475    351    847  A    C  
ATOM     89  N   ILE A  36       9.122  54.505 468.277  1.00 38.11      A    N  
ANISOU   89  N   ILE A  36     5443   1951   7086    642    265    498  A    N  
ATOM     90  CA  ILE A  36       8.213  54.509 469.416  1.00 38.39      A    C  
ANISOU   90  CA  ILE A  36     5419   2007   7162    760    282    453  A    C  
ATOM     91  C   ILE A  36       7.015  55.370 469.056  1.00 47.91      A    C  
ANISOU   91  C   ILE A  36     6604   3168   8431    868    264    515  A    C  
ATOM     92  O   ILE A  36       7.165  56.571 468.782  1.00 46.19      A    O  
ANISOU   92  O   ILE A  36     6462   2856   8232    891    251    509  A    O  
ATOM     93  CB  ILE A  36       8.876  55.013 470.706  1.00 45.50      A    C  
ANISOU   93  CB  ILE A  36     6367   2850   8072    793    298    305  A    C  
ATOM     94  CG1 ILE A  36      10.056  54.111 471.084  1.00 38.09      A    C  
ANISOU   94  CG1 ILE A  36     5427   1939   7105    712    266    242  A    C  
ATOM     95  CG2 ILE A  36       7.834  55.092 471.832  1.00 39.70      A    C  
ANISOU   95  CG2 ILE A  36     5627   2109   7347    945    372    266  A    C  
ATOM     96  CD1 ILE A  36      10.777  54.540 472.321  1.00 39.03      A    C  
ANISOU   96  CD1 ILE A  36     5607   1973   7249    760    211     76  A    C  
ATOM     97  N   VAL A  37       5.828  54.757 469.114  1.00 49.94      A    N  
ANISOU   97  N   VAL A  37     6741   3477   8759    940    267    571  A    N  
ATOM     98  CA  VAL A  37       4.566  55.330 468.666  1.00 52.87      A    C  
ANISOU   98  CA  VAL A  37     7027   3812   9249   1054    213    637  A    C  
ATOM     99  C   VAL A  37       3.628  55.426 469.857  1.00 54.94      A    C  
ANISOU   99  C   VAL A  37     7168   4078   9628   1175    342    579  A    C  
ATOM    100  O   VAL A  37       3.538  54.494 470.659  1.00 41.79      A    O  
ANISOU  100  O   VAL A  37     5452   2482   7946   1160    456    548  A    O  
ATOM    101  CB  VAL A  37       3.913  54.477 467.556  1.00 52.90      A    C  
ANISOU  101  CB  VAL A  37     6944   3846   9308   1035     81    744  A    C  
ATOM    102  CG1 VAL A  37       2.651  55.166 467.012  1.00 43.42      A    C  
ANISOU  102  CG1 VAL A  37     5643   2593   8263   1174    -46    806  A    C  
ATOM    103  CG2 VAL A  37       4.902  54.198 466.452  1.00 49.22      A    C  
ANISOU  103  CG2 VAL A  37     6645   3368   8690    920     11    795  A    C  
ATOM    104  N   GLU A  38       2.936  56.556 469.980  1.00 53.57      A    N  
ANISOU  104  N   GLU A  38     6971   3835   9548   1298    350    564  A    N  
ATOM    105  CA  GLU A  38       1.897  56.685 470.991  1.00 52.94      A    C  
ANISOU  105  CA  GLU A  38     6762   3746   9605   1429    511    513  A    C  
ATOM    106  C   GLU A  38       0.665  55.922 470.526  1.00 53.76      A    C  
ANISOU  106  C   GLU A  38     6606   3893   9928   1463    481    595  A    C  
ATOM    107  O   GLU A  38       0.175  56.149 469.418  1.00 54.02      A    O  
ANISOU  107  O   GLU A  38     6559   3908  10057   1485    278    673  A    O  
ATOM    108  CB  GLU A  38       1.577  58.158 471.251  1.00 47.21      A    C  
ANISOU  108  CB  GLU A  38     6088   2921   8929   1551    533    457  A    C  
ATOM    109  CG  GLU A  38       2.608  58.803 472.153  1.00 47.00      A    C  
ANISOU  109  CG  GLU A  38     6277   2829   8751   1536    606    321  A    C  
ATOM    110  CD  GLU A  38       2.135  60.057 472.854  1.00 69.28      A    C  
ANISOU  110  CD  GLU A  38     9146   5543  11636   1676    699    221  A    C  
ATOM    111  OE1 GLU A  38       1.240  60.762 472.319  1.00 70.30      A    O  
ANISOU  111  OE1 GLU A  38     9172   5626  11914   1771    659    280  A    O  
ATOM    112  OE2 GLU A  38       2.680  60.333 473.952  1.00 73.05      A    O1-
ANISOU  112  OE2 GLU A  38     9779   5968  12008   1703    796     71  A    O1-
ATOM    113  N   LYS A  39       0.178  55.004 471.369  1.00 46.55      A    N  
ANISOU  113  N   LYS A  39     5572   3031   9085   1464    676    574  A    N  
ATOM    114  CA  LYS A  39      -0.936  54.141 470.980  1.00 47.64      A    C  
ANISOU  114  CA  LYS A  39     5424   3220   9458   1448    656    627  A    C  
ATOM    115  C   LYS A  39      -2.183  54.950 470.620  1.00 58.38      A    C  
ANISOU  115  C   LYS A  39     6546   4492  11145   1601    590    644  A    C  
ATOM    116  O   LYS A  39      -2.831  54.681 469.601  1.00 51.19      A    O  
ANISOU  116  O   LYS A  39     5445   3586  10421   1597    349    696  A    O  
ATOM    117  CB  LYS A  39      -1.240  53.140 472.099  1.00 56.09      A    C  
ANISOU  117  CB  LYS A  39     6430   4346  10536   1416    952    604  A    C  
ATOM    118  CG  LYS A  39      -2.291  52.084 471.736  1.00 58.22      A    C  
ANISOU  118  CG  LYS A  39     6380   4646  11095   1354    961    647  A    C  
ATOM    119  CD  LYS A  39      -2.771  51.282 472.941  1.00 63.78      A    C  
ANISOU  119  CD  LYS A  39     7016   5352  11866   1350   1344    645  A    C  
ATOM    120  CE  LYS A  39      -3.705  50.132 472.500  1.00 88.33      A    C  
ANISOU  120  CE  LYS A  39     9788   8463  15310   1246   1347    681  A    C  
ATOM    121  NZ  LYS A  39      -2.990  48.874 472.001  1.00 89.56      A    N1+
ANISOU  121  NZ  LYS A  39    10032   8690  15306   1062   1215    710  A    N1+
ATOM    122  N   ASP A  40      -2.532  55.951 471.440  1.00 62.12      A    N  
ANISOU  122  N   ASP A  40     7044   4918  11640   1725    770    580  A    N  
ATOM    123  CA  ASP A  40      -3.790  56.680 471.242  1.00 63.31      A    C  
ANISOU  123  CA  ASP A  40     6948   5023  12083   1858    737    580  A    C  
ATOM    124  C   ASP A  40      -3.762  57.570 470.002  1.00 68.82      A    C  
ANISOU  124  C   ASP A  40     7705   5682  12762   1906    390    639  A    C  
ATOM    125  O   ASP A  40      -4.684  57.519 469.175  1.00 70.42      A    O  
ANISOU  125  O   ASP A  40     7674   5878  13203   1960    169    687  A    O  
ATOM    126  CB  ASP A  40      -4.138  57.515 472.481  1.00 66.20      A    C  
ANISOU  126  CB  ASP A  40     7360   5334  12459   1982   1050    487  A    C  
ATOM    127  CG  ASP A  40      -2.968  58.342 472.979  1.00 90.72      A    C  
ANISOU  127  CG  ASP A  40    10835   8399  15235   1987   1078    414  A    C  
ATOM    128  OD1 ASP A  40      -1.829  58.078 472.533  1.00 99.05      A    O  
ANISOU  128  OD1 ASP A  40    12088   9482  16066   1869    920    437  A    O  
ATOM    129  OD2 ASP A  40      -3.191  59.265 473.798  1.00101.76      A    O1-
ANISOU  129  OD2 ASP A  40    12314   9727  16623   2102   1253    321  A    O1-
ATOM    130  N   THR A  41      -2.731  58.413 469.865  1.00 68.91      A    N  
ANISOU  130  N   THR A  41     8031   5651  12501   1894    338    636  A    N  
ATOM    131  CA  THR A  41      -2.678  59.358 468.755  1.00 55.52      A    C  
ANISOU  131  CA  THR A  41     6449   3886  10759   1956     77    713  A    C  
ATOM    132  C   THR A  41      -2.082  58.740 467.501  1.00 57.69      A    C  
ANISOU  132  C   THR A  41     6844   4191  10883   1854   -177    814  A    C  
ATOM    133  O   THR A  41      -2.223  59.313 466.416  1.00 80.08      A    O  
ANISOU  133  O   THR A  41     9774   6969  13682   1924   -413    907  A    O  
ATOM    134  CB  THR A  41      -1.885  60.603 469.159  1.00 54.62      A    C  
ANISOU  134  CB  THR A  41     6608   3677  10468   1983    172    662  A    C  
ATOM    135  CG2 THR A  41      -2.319  61.052 470.508  1.00 55.87      A    C  
ANISOU  135  CG2 THR A  41     6704   3803  10720   2071    440    536  A    C  
ATOM    136  OG1 THR A  41      -0.500  60.292 469.289  1.00 62.07      A    O  
ANISOU  136  OG1 THR A  41     7785   4640  11157   1828    214    635  A    O  
ATOM    137  N   GLN A  42      -1.436  57.584 467.635  1.00 51.13      A    N  
ANISOU  137  N   GLN A  42     6038   3437   9952   1705   -124    801  A    N  
ATOM    138  CA  GLN A  42      -0.753  56.897 466.538  1.00 68.96      A    C  
ANISOU  138  CA  GLN A  42     8439   5716  12044   1595   -318    878  A    C  
ATOM    139  C   GLN A  42       0.325  57.764 465.899  1.00 49.26      A    C  
ANISOU  139  C   GLN A  42     6279   3150   9290   1565   -353    932  A    C  
ATOM    140  O   GLN A  42       0.571  57.703 464.690  1.00 66.38      A    O  
ANISOU  140  O   GLN A  42     8606   5283  11332   1554   -542   1033  A    O  
ATOM    141  CB  GLN A  42      -1.737  56.348 465.504  1.00 74.67      A    C  
ANISOU  141  CB  GLN A  42     8985   6447  12940   1647   -620    940  A    C  
ATOM    142  CG  GLN A  42      -2.679  55.315 466.108  1.00 72.62      A    C  
ANISOU  142  CG  GLN A  42     8362   6244  12987   1628   -553    875  A    C  
ATOM    143  CD  GLN A  42      -3.159  54.302 465.103  1.00 71.06      A    C  
ANISOU  143  CD  GLN A  42     8048   6118  12835   1557   -847    877  A    C  
ATOM    144  NE2 GLN A  42      -3.602  53.156 465.598  1.00 90.24      A    N  
ANISOU  144  NE2 GLN A  42    10228   8623  15436   1448   -736    807  A    N  
ATOM    145  OE1 GLN A  42      -3.136  54.538 463.896  1.00 54.16      A    O  
ANISOU  145  OE1 GLN A  42     6062   3949  10569   1602  -1169    939  A    O  
ATOM    146  N   GLN A  43       0.983  58.568 466.724  1.00 48.73      A    N  
ANISOU  146  N   GLN A  43     6328   3041   9144   1552   -162    858  A    N  
ATOM    147  CA  GLN A  43       2.090  59.399 466.287  1.00 48.43      A    C  
ANISOU  147  CA  GLN A  43     6567   2913   8920   1496   -141    884  A    C  
ATOM    148  C   GLN A  43       3.415  58.754 466.651  1.00 46.11      A    C  
ANISOU  148  C   GLN A  43     6369   2670   8480   1316    -24    817  A    C  
ATOM    149  O   GLN A  43       3.575  58.251 467.767  1.00 45.04      A    O  
ANISOU  149  O   GLN A  43     6142   2602   8368   1280     96    708  A    O  
ATOM    150  CB  GLN A  43       2.053  60.789 466.911  1.00 49.81      A    C  
ANISOU  150  CB  GLN A  43     6803   2978   9146   1584    -47    821  A    C  
ATOM    151  CG  GLN A  43       1.753  61.869 465.937  1.00 52.03      A    C  
ANISOU  151  CG  GLN A  43     7223   3126   9420   1696   -163    938  A    C  
ATOM    152  CD  GLN A  43       2.042  63.186 466.549  1.00 70.61      A    C  
ANISOU  152  CD  GLN A  43     9675   5347  11806   1735    -50    862  A    C  
ATOM    153  NE2 GLN A  43       1.903  64.251 465.771  1.00 73.56      A    N  
ANISOU  153  NE2 GLN A  43    10209   5570  12170   1830   -120    965  A    N  
ATOM    154  OE1 GLN A  43       2.418  63.252 467.721  1.00 65.44      A    O  
ANISOU  154  OE1 GLN A  43     8978   4708  11178   1686     93    708  A    O  
ATOM    155  N   ILE A  44       4.354  58.764 465.703  1.00 45.72      A    N  
ANISOU  155  N   ILE A  44     6513   2575   8283   1219    -50    886  A    N  
ATOM    156  CA  ILE A  44       5.738  58.461 466.040  1.00 48.72      A    C  
ANISOU  156  CA  ILE A  44     6968   2975   8569   1056     69    808  A    C  
ATOM    157  C   ILE A  44       6.248  59.545 466.973  1.00 46.30      A    C  
ANISOU  157  C   ILE A  44     6690   2588   8313   1057    163    688  A    C  
ATOM    158  O   ILE A  44       6.230  60.733 466.631  1.00 48.19      A    O  
ANISOU  158  O   ILE A  44     7035   2696   8579   1105    161    721  A    O  
ATOM    159  CB  ILE A  44       6.597  58.346 464.778  1.00 44.23      A    C  
ANISOU  159  CB  ILE A  44     6591   2349   7867    959     68    907  A    C  
ATOM    160  CG1 ILE A  44       6.177  57.106 463.979  1.00 54.51      A    C  
ANISOU  160  CG1 ILE A  44     7882   3720   9108    952    -34    991  A    C  
ATOM    161  CG2 ILE A  44       8.066  58.316 465.148  1.00 43.30      A    C  
ANISOU  161  CG2 ILE A  44     6499   2225   7727    799    201    811  A    C  
ATOM    162  CD1 ILE A  44       6.555  57.129 462.530  1.00 44.86      A    C  
ANISOU  162  CD1 ILE A  44     6912   2400   7732    935    -65   1130  A    C  
ATOM    163  N   VAL A  45       6.635  59.159 468.185  1.00 48.44      A    N  
ANISOU  163  N   VAL A  45     6885   2916   8604   1022    228    548  A    N  
ATOM    164  CA  VAL A  45       7.190  60.116 469.122  1.00 55.43      A    C  
ANISOU  164  CA  VAL A  45     7818   3706   9537   1025    281    406  A    C  
ATOM    165  C   VAL A  45       8.696  59.951 469.278  1.00 60.79      A    C  
ANISOU  165  C   VAL A  45     8533   4363  10199    869    298    318  A    C  
ATOM    166  O   VAL A  45       9.390  60.939 469.549  1.00 45.09      A    O  
ANISOU  166  O   VAL A  45     6599   2248   8283    831    314    226  A    O  
ATOM    167  CB  VAL A  45       6.491  60.058 470.494  1.00 54.72      A    C  
ANISOU  167  CB  VAL A  45     7666   3641   9485   1145    332    286  A    C  
ATOM    168  CG1 VAL A  45       5.062  60.558 470.362  1.00 46.30      A    C  
ANISOU  168  CG1 VAL A  45     6527   2556   8509   1305    342    352  A    C  
ATOM    169  CG2 VAL A  45       6.578  58.665 471.103  1.00 43.38      A    C  
ANISOU  169  CG2 VAL A  45     6164   2331   7989   1117    359    260  A    C  
ATOM    170  N   TYR A  46       9.230  58.745 469.087  1.00 61.31      A    N  
ANISOU  170  N   TYR A  46     8552   4536  10207    778    291    337  A    N  
ATOM    171  CA  TYR A  46      10.675  58.569 469.092  1.00 56.85      A    C  
ANISOU  171  CA  TYR A  46     7980   3946   9673    636    305    263  A    C  
ATOM    172  C   TYR A  46      11.105  57.751 467.887  1.00 41.25      A    C  
ANISOU  172  C   TYR A  46     6010   2027   7636    536    340    383  A    C  
ATOM    173  O   TYR A  46      10.352  56.927 467.374  1.00 40.40      A    O  
ANISOU  173  O   TYR A  46     5902   2008   7441    572    318    485  A    O  
ATOM    174  CB  TYR A  46      11.178  57.888 470.370  1.00 41.53      A    C  
ANISOU  174  CB  TYR A  46     5986   2049   7744    640    257    110  A    C  
ATOM    175  CG  TYR A  46      10.943  58.659 471.653  1.00 42.81      A    C  
ANISOU  175  CG  TYR A  46     6201   2126   7941    745    223    -49  A    C  
ATOM    176  CD1 TYR A  46      11.753  59.729 472.011  1.00 44.45      A    C  
ANISOU  176  CD1 TYR A  46     6439   2190   8260    700    188   -191  A    C  
ATOM    177  CD2 TYR A  46       9.936  58.289 472.536  1.00 42.76      A    C  
ANISOU  177  CD2 TYR A  46     6220   2165   7864    891    246    -72  A    C  
ATOM    178  CE1 TYR A  46      11.534  60.434 473.206  1.00 45.98      A    C  
ANISOU  178  CE1 TYR A  46     6719   2289   8463    806    145   -369  A    C  
ATOM    179  CE2 TYR A  46       9.722  58.984 473.726  1.00 44.33      A    C  
ANISOU  179  CE2 TYR A  46     6515   2267   8063   1010    245   -237  A    C  
ATOM    180  CZ  TYR A  46      10.526  60.050 474.050  1.00 45.91      A    C  
ANISOU  180  CZ  TYR A  46     6774   2325   8343    969    176   -395  A    C  
ATOM    181  OH  TYR A  46      10.314  60.711 475.226  1.00 47.75      A    O  
ANISOU  181  OH  TYR A  46     7137   2453   8553   1093    162   -586  A    O  
ATOM    182  N   ALA A  47      12.299  58.039 467.395  1.00 41.91      A    N  
ANISOU  182  N   ALA A  47     6101   2039   7786    414    408    366  A    N  
ATOM    183  CA  ALA A  47      12.929  57.219 466.377  1.00 41.46      A    C  
ANISOU  183  CA  ALA A  47     6053   2019   7680    317    483    447  A    C  
ATOM    184  C   ALA A  47      14.413  57.159 466.691  1.00 45.97      A    C  
ANISOU  184  C   ALA A  47     6506   2550   8412    196    539    330  A    C  
ATOM    185  O   ALA A  47      14.996  58.143 467.149  1.00 50.14      A    O  
ANISOU  185  O   ALA A  47     6991   2965   9096    161    545    234  A    O  
ATOM    186  CB  ALA A  47      12.694  57.748 464.952  1.00 42.68      A    C  
ANISOU  186  CB  ALA A  47     6376   2088   7754    314    561    611  A    C  
ATOM    187  N   SER A  48      15.014  55.998 466.475  1.00 47.81      A    N  
ANISOU  187  N   SER A  48     6667   2863   8637    137    570    326  A    N  
ATOM    188  CA  SER A  48      16.447  55.895 466.654  1.00 48.38      A    C  
ANISOU  188  CA  SER A  48     6585   2885   8911     32    625    222  A    C  
ATOM    189  C   SER A  48      17.160  56.713 465.585  1.00 43.94      A    C  
ANISOU  189  C   SER A  48     6054   2194   8446    -60    823    286  A    C  
ATOM    190  O   SER A  48      16.681  56.852 464.456  1.00 44.27      A    O  
ANISOU  190  O   SER A  48     6274   2214   8335    -48    933    438  A    O  
ATOM    191  CB  SER A  48      16.882  54.441 466.583  1.00 56.84      A    C  
ANISOU  191  CB  SER A  48     7574   4058   9963      8    629    216  A    C  
ATOM    192  OG  SER A  48      16.638  53.905 465.290  1.00 61.29      A    O  
ANISOU  192  OG  SER A  48     8258   4651  10379    -14    765    353  A    O  
ATOM    193  N   ALA A  49      18.332  57.240 465.955  1.00 45.65      A    N  
ANISOU  193  N   ALA A  49     6098   2308   8938   -147    866    165  A    N  
ATOM    194  CA  ALA A  49      19.025  58.228 465.129  1.00 54.21      A    C  
ANISOU  194  CA  ALA A  49     7188   3236  10176   -234   1081    212  A    C  
ATOM    195  C   ALA A  49      19.298  57.722 463.717  1.00 56.38      A    C  
ANISOU  195  C   ALA A  49     7566   3505  10350   -273   1332    362  A    C  
ATOM    196  O   ALA A  49      19.422  58.521 462.783  1.00 50.67      A    O  
ANISOU  196  O   ALA A  49     6975   2657   9622   -303   1535    474  A    O  
ATOM    197  CB  ALA A  49      20.329  58.638 465.805  1.00 52.52      A    C  
ANISOU  197  CB  ALA A  49     6700   2917  10340   -329   1077     33  A    C  
ATOM    198  N   ASN A  50      19.394  56.412 463.539  1.00 47.24      A    N  
ANISOU  198  N   ASN A  50     6379   2465   9105   -266   1333    367  A    N  
ATOM    199  CA  ASN A  50      19.638  55.820 462.237  1.00 58.82      A    C  
ANISOU  199  CA  ASN A  50     7973   3922  10452   -291   1574    485  A    C  
ATOM    200  C   ASN A  50      18.356  55.419 461.526  1.00 59.57      A    C  
ANISOU  200  C   ASN A  50     8360   4087  10188   -203   1505    630  A    C  
ATOM    201  O   ASN A  50      18.404  54.553 460.644  1.00 56.93      A    O  
ANISOU  201  O   ASN A  50     8147   3777   9707   -204   1630    695  A    O  
ATOM    202  CB  ASN A  50      20.507  54.574 462.382  1.00 58.49      A    C  
ANISOU  202  CB  ASN A  50     7736   3944  10543   -327   1625    397  A    C  
ATOM    203  CG  ASN A  50      19.835  53.509 463.232  1.00 58.18      A    C  
ANISOU  203  CG  ASN A  50     7664   4063  10379   -258   1359    346  A    C  
ATOM    204  ND2 ASN A  50      20.091  52.252 462.912  1.00 68.38      A    N  
ANISOU  204  ND2 ASN A  50     8933   5419  11630   -258   1416    345  A    N  
ATOM    205  OD1 ASN A  50      19.041  53.814 464.119  1.00 60.45      A    O  
ANISOU  205  OD1 ASN A  50     7969   4401  10598   -197   1132    315  A    O  
ATOM    206  N   SER A  51      17.206  55.977 461.920  1.00 45.79      A    N  
ANISOU  206  N   SER A  51     6716   2362   8318   -118   1302    668  A    N  
ATOM    207  CA  SER A  51      15.940  55.457 461.402  1.00 51.72      A    C  
ANISOU  207  CA  SER A  51     7675   3181   8795    -23   1180    779  A    C  
ATOM    208  C   SER A  51      15.803  55.678 459.905  1.00 56.37      A    C  
ANISOU  208  C   SER A  51     8556   3671   9191     -7   1342    947  A    C  
ATOM    209  O   SER A  51      15.112  54.903 459.224  1.00 55.55      A    O  
ANISOU  209  O   SER A  51     8633   3607   8867     50   1285   1025  A    O  
ATOM    210  CB  SER A  51      14.752  56.063 462.152  1.00 57.16      A    C  
ANISOU  210  CB  SER A  51     8374   3894   9451     80    953    779  A    C  
ATOM    211  OG  SER A  51      14.736  55.648 463.511  1.00 60.53      A    O  
ANISOU  211  OG  SER A  51     8593   4421   9983     91    817    636  A    O  
ATOM    212  N   ALA A  52      16.467  56.705 459.371  1.00 49.16      A    N  
ANISOU  212  N   ALA A  52     7712   2614   8354    -50   1553   1003  A    N  
ATOM    213  CA  ALA A  52      16.303  57.010 457.960  1.00 51.61      A    C  
ANISOU  213  CA  ALA A  52     8356   2815   8436     -9   1724   1181  A    C  
ATOM    214  C   ALA A  52      16.753  55.848 457.081  1.00 67.15      A    C  
ANISOU  214  C   ALA A  52    10456   4811  10247    -35   1911   1198  A    C  
ATOM    215  O   ALA A  52      16.032  55.446 456.158  1.00 68.81      A    O  
ANISOU  215  O   ALA A  52    10982   5015  10146     50   1873   1311  A    O  
ATOM    216  CB  ALA A  52      17.075  58.278 457.615  1.00 77.17      A    C  
ANISOU  216  CB  ALA A  52    11623   5879  11816    -62   1974   1231  A    C  
ATOM    217  N   GLU A  53      17.911  55.251 457.380  1.00 63.97      A    N  
ANISOU  217  N   GLU A  53     9818   4431  10056   -136   2093   1073  A    N  
ATOM    218  CA  GLU A  53      18.445  54.265 456.446  1.00 64.45      A    C  
ANISOU  218  CA  GLU A  53    10024   4479   9984   -154   2342   1087  A    C  
ATOM    219  C   GLU A  53      17.632  52.983 456.407  1.00 72.53      A    C  
ANISOU  219  C   GLU A  53    11143   5619  10794   -102   2134   1067  A    C  
ATOM    220  O   GLU A  53      17.699  52.265 455.407  1.00 85.49      A    O  
ANISOU  220  O   GLU A  53    13053   7224  12207    -82   2299   1108  A    O  
ATOM    221  CB  GLU A  53      19.901  53.933 456.769  1.00 61.72      A    C  
ANISOU  221  CB  GLU A  53     9366   4110   9974   -258   2595    955  A    C  
ATOM    222  CG  GLU A  53      20.100  53.204 458.070  1.00 75.17      A    C  
ANISOU  222  CG  GLU A  53    10702   5947  11912   -288   2357    792  A    C  
ATOM    223  CD  GLU A  53      21.568  53.033 458.423  1.00 78.48      A    C  
ANISOU  223  CD  GLU A  53    10785   6316  12719   -371   2567    664  A    C  
ATOM    224  OE1 GLU A  53      22.134  51.939 458.166  1.00 70.93      A    O  
ANISOU  224  OE1 GLU A  53     9762   5379  11809   -381   2706    610  A    O  
ATOM    225  OE2 GLU A  53      22.153  54.011 458.947  1.00 83.15      A    O1-
ANISOU  225  OE2 GLU A  53    11170   6828  13594   -420   2590    612  A    O1-
ATOM    226  N   TYR A  54      16.849  52.682 457.440  1.00 72.46      A    N  
ANISOU  226  N   TYR A  54    10953   5732  10846    -73   1799   1002  A    N  
ATOM    227  CA  TYR A  54      16.000  51.495 457.366  1.00 66.60      A    C  
ANISOU  227  CA  TYR A  54    10301   5073   9930    -24   1614    989  A    C  
ATOM    228  C   TYR A  54      14.635  51.820 456.762  1.00 72.89      A    C  
ANISOU  228  C   TYR A  54    11405   5833  10455     94   1408   1120  A    C  
ATOM    229  O   TYR A  54      14.142  51.069 455.914  1.00 68.18      A    O  
ANISOU  229  O   TYR A  54    11097   5211   9597    143   1373   1159  A    O  
ATOM    230  CB  TYR A  54      15.836  50.846 458.743  1.00 43.72      A    C  
ANISOU  230  CB  TYR A  54     7069   2313   7229    -41   1395    859  A    C  
ATOM    231  CG  TYR A  54      17.093  50.214 459.272  1.00 49.36      A    C  
ANISOU  231  CG  TYR A  54     7517   3065   8171   -121   1533    733  A    C  
ATOM    232  CD1 TYR A  54      18.110  50.996 459.807  1.00 60.87      A    C  
ANISOU  232  CD1 TYR A  54     8758   4483   9886   -175   1636    673  A    C  
ATOM    233  CD2 TYR A  54      17.273  48.837 459.249  1.00 53.35      A    C  
ANISOU  233  CD2 TYR A  54     7980   3625   8665   -135   1546    668  A    C  
ATOM    234  CE1 TYR A  54      19.271  50.427 460.290  1.00 55.44      A    C  
ANISOU  234  CE1 TYR A  54     7808   3807   9451   -229   1731    558  A    C  
ATOM    235  CE2 TYR A  54      18.440  48.255 459.740  1.00 50.44      A    C  
ANISOU  235  CE2 TYR A  54     7357   3275   8533   -183   1654    561  A    C  
ATOM    236  CZ  TYR A  54      19.428  49.061 460.261  1.00 52.49      A    C  
ANISOU  236  CZ  TYR A  54     7393   3492   9057   -224   1735    509  A    C  
ATOM    237  OH  TYR A  54      20.584  48.513 460.747  1.00 61.36      A    O  
ANISOU  237  OH  TYR A  54     8243   4609  10461   -257   1813    402  A    O  
ATOM    238  N   PHE A  55      13.987  52.905 457.215  1.00 70.03      A    N  
ANISOU  238  N   PHE A  55    10994   5458  10155    154   1243   1174  A    N  
ATOM    239  CA  PHE A  55      12.662  53.202 456.688  1.00 47.99      A    C  
ANISOU  239  CA  PHE A  55     8456   2629   7148    296   1009   1297  A    C  
ATOM    240  C   PHE A  55      12.696  53.859 455.325  1.00 62.95      A    C  
ANISOU  240  C   PHE A  55    10766   4398   8753    364   1129   1456  A    C  
ATOM    241  O   PHE A  55      11.641  53.973 454.693  1.00 69.35      A    O  
ANISOU  241  O   PHE A  55    11855   5179   9317    507    894   1559  A    O  
ATOM    242  CB  PHE A  55      11.872  54.039 457.674  1.00 46.94      A    C  
ANISOU  242  CB  PHE A  55     8115   2520   7198    361    792   1293  A    C  
ATOM    243  CG  PHE A  55      11.490  53.273 458.877  1.00 44.27      A    C  
ANISOU  243  CG  PHE A  55     7476   2304   7039    345    646   1164  A    C  
ATOM    244  CD1 PHE A  55      10.406  52.412 458.839  1.00 48.41      A    C  
ANISOU  244  CD1 PHE A  55     8007   2898   7487    418    427   1159  A    C  
ATOM    245  CD2 PHE A  55      12.252  53.343 460.024  1.00 46.70      A    C  
ANISOU  245  CD2 PHE A  55     7495   2686   7563    256    713   1030  A    C  
ATOM    246  CE1 PHE A  55      10.059  51.665 459.943  1.00 41.60      A    C  
ANISOU  246  CE1 PHE A  55     6838   2186   6784    389    322   1040  A    C  
ATOM    247  CE2 PHE A  55      11.911  52.609 461.144  1.00 44.35      A    C  
ANISOU  247  CE2 PHE A  55     6964   2511   7377    257    595    924  A    C  
ATOM    248  CZ  PHE A  55      10.811  51.767 461.105  1.00 47.32      A    C  
ANISOU  248  CZ  PHE A  55     7339   2927   7714    324    440    950  A    C  
ATOM    249  N   SER A  56      13.869  54.288 454.850  1.00 61.11      A    N  
ANISOU  249  N   SER A  56    10591   4087   8539    281   1477   1476  A    N  
ATOM    250  CA  SER A  56      13.970  54.689 453.453  1.00 56.65      A    C  
ANISOU  250  CA  SER A  56    10487   3402   7637    351   1654   1626  A    C  
ATOM    251  C   SER A  56      13.592  53.540 452.532  1.00 66.48      A    C  
ANISOU  251  C   SER A  56    12100   4655   8506    415   1594   1632  A    C  
ATOM    252  O   SER A  56      13.230  53.774 451.373  1.00 60.75      A    O  
ANISOU  252  O   SER A  56    11851   3849   7382    534   1582   1758  A    O  
ATOM    253  CB  SER A  56      15.382  55.183 453.140  1.00 58.58      A    C  
ANISOU  253  CB  SER A  56    10700   3548   8011    241   2105   1625  A    C  
ATOM    254  OG  SER A  56      16.301  54.115 453.051  1.00 58.14      A    O  
ANISOU  254  OG  SER A  56    10560   3519   8011    146   2349   1509  A    O  
ATOM    255  N   VAL A  57      13.687  52.306 453.036  1.00 63.77      A    N  
ANISOU  255  N   VAL A  57    11566   4396   8266    344   1543   1488  A    N  
ATOM    256  CA  VAL A  57      13.367  51.110 452.266  1.00 67.54      A    C  
ANISOU  256  CA  VAL A  57    12381   4858   8423    384   1472   1453  A    C  
ATOM    257  C   VAL A  57      11.855  50.936 452.109  1.00 74.09      A    C  
ANISOU  257  C   VAL A  57    13332   5777   9040    521    953   1460  A    C  
ATOM    258  O   VAL A  57      11.372  50.513 451.051  1.00 58.66      A    O  
ANISOU  258  O   VAL A  57    11769   3835   6684    613    784   1463  A    O  
ATOM    259  CB  VAL A  57      14.020  49.897 452.946  1.00 66.99      A    C  
ANISOU  259  CB  VAL A  57    11992   4856   8606    252   1590   1277  A    C  
ATOM    260  CG1 VAL A  57      13.830  48.685 452.109  1.00 71.32      A    C  
ANISOU  260  CG1 VAL A  57    12813   5443   8841    270   1534   1187  A    C  
ATOM    261  CG2 VAL A  57      15.506  50.162 453.213  1.00 53.58      A    C  
ANISOU  261  CG2 VAL A  57    10017   3149   7193    129   2005   1227  A    C  
ATOM    262  N   ALA A  58      11.089  51.224 453.168  1.00 78.78      A    N  
ANISOU  262  N   ALA A  58    13533   6481   9918    536    668   1424  A    N  
ATOM    263  CA  ALA A  58       9.629  51.218 453.075  1.00 67.21      A    C  
ANISOU  263  CA  ALA A  58    12054   5128   8354    666    175   1415  A    C  
ATOM    264  C   ALA A  58       9.113  52.425 452.314  1.00 70.11      A    C  
ANISOU  264  C   ALA A  58    12779   5365   8493    840     51   1608  A    C  
ATOM    265  O   ALA A  58       8.049  52.361 451.691  1.00 85.34      A    O  
ANISOU  265  O   ALA A  58    14882   7342  10200    983   -357   1620  A    O  
ATOM    266  CB  ALA A  58       8.999  51.198 454.467  1.00 51.40      A    C  
ANISOU  266  CB  ALA A  58     9525   3256   6747    636    -11   1326  A    C  
ATOM    267  N   ASP A  59       9.846  53.531 452.362  1.00 70.71      A    N  
ANISOU  267  N   ASP A  59    12949   5269   8648    832    377   1754  A    N  
ATOM    268  CA  ASP A  59       9.328  54.809 451.892  1.00 72.86      A    C  
ANISOU  268  CA  ASP A  59    13390   5482   8811    978    262   1913  A    C  
ATOM    269  C   ASP A  59      10.512  55.559 451.287  1.00 72.51      A    C  
ANISOU  269  C   ASP A  59    13530   5334   8688    905    729   2005  A    C  
ATOM    270  O   ASP A  59      11.272  56.200 452.020  1.00 76.48      A    O  
ANISOU  270  O   ASP A  59    13712   5812   9534    780    989   1979  A    O  
ATOM    271  CB  ASP A  59       8.708  55.569 453.056  1.00 71.77      A    C  
ANISOU  271  CB  ASP A  59    12824   5378   9066   1004     98   1900  A    C  
ATOM    272  CG  ASP A  59       7.750  56.638 452.604  1.00 80.51      A    C  
ANISOU  272  CG  ASP A  59    14078   6436  10076   1202   -171   2043  A    C  
ATOM    273  OD1 ASP A  59       7.901  57.129 451.460  1.00 84.30      A    O  
ANISOU  273  OD1 ASP A  59    14973   6835  10221   1285   -111   2180  A    O  
ATOM    274  OD2 ASP A  59       6.851  56.991 453.401  1.00 86.88      A    O1-
ANISOU  274  OD2 ASP A  59    14583   7280  11149   1282   -423   2016  A    O1-
ATOM    275  N   ASN A  60      10.658  55.501 449.957  1.00 66.62      A    N  
ANISOU  275  N   ASN A  60    13309   4515   7488    990    815   2100  A    N  
ATOM    276  CA  ASN A  60      11.899  56.106 449.442  1.00 81.78      A    C  
ANISOU  276  CA  ASN A  60    15367   6320   9386    902   1337   2166  A    C  
ATOM    277  C   ASN A  60      11.904  57.655 449.525  1.00 88.63      A    C  
ANISOU  277  C   ASN A  60    16179   7087  10409    941   1413   2305  A    C  
ATOM    278  O   ASN A  60      12.851  58.294 449.034  1.00 96.18      A    O  
ANISOU  278  O   ASN A  60    17271   7917  11355    884   1830   2375  A    O  
ATOM    279  CB  ASN A  60      12.217  55.625 448.009  1.00 72.73      A    C  
ANISOU  279  CB  ASN A  60    14825   5102   7709    977   1518   2216  A    C  
ATOM    280  CG  ASN A  60      11.010  55.668 447.063  1.00 90.71      A    C  
ANISOU  280  CG  ASN A  60    17589   7385   9492   1214   1059   2308  A    C  
ATOM    281  ND2 ASN A  60      11.235  56.109 445.833  1.00 80.85      A    N  
ANISOU  281  ND2 ASN A  60    16880   6028   7810   1327   1232   2425  A    N  
ATOM    282  OD1 ASN A  60       9.898  55.298 447.435  1.00 97.58      A    O  
ANISOU  282  OD1 ASN A  60    18338   8352  10385   1302    543   2258  A    O  
ATOM    283  N   THR A  61      10.909  58.273 450.165  1.00 87.01      A    N  
ANISOU  283  N   THR A  61    15761   6914  10383   1031   1050   2337  A    N  
ATOM    284  CA  THR A  61      10.943  59.707 450.405  1.00 70.79      A    C  
ANISOU  284  CA  THR A  61    13608   4747   8542   1048   1127   2444  A    C  
ATOM    285  C   THR A  61      11.650  60.052 451.709  1.00 67.63      A    C  
ANISOU  285  C   THR A  61    12691   4350   8654    861   1300   2312  A    C  
ATOM    286  O   THR A  61      12.062  61.203 451.893  1.00 74.46      A    O  
ANISOU  286  O   THR A  61    13485   5089   9718    821   1468   2365  A    O  
ATOM    287  CB  THR A  61       9.524  60.279 450.414  1.00 71.82      A    C  
ANISOU  287  CB  THR A  61    13772   4889   8626   1258    663   2538  A    C  
ATOM    288  CG2 THR A  61       8.863  60.005 449.084  1.00 75.68      A    C  
ANISOU  288  CG2 THR A  61    14791   5377   8585   1458    430   2648  A    C  
ATOM    289  OG1 THR A  61       8.750  59.669 451.449  1.00 68.17      A    O  
ANISOU  289  OG1 THR A  61    12927   4562   8414   1263    343   2401  A    O  
ATOM    290  N   ILE A  62      11.837  59.074 452.591  1.00 63.87      A    N  
ANISOU  290  N   ILE A  62    11884   4005   8379    750   1254   2133  A    N  
ATOM    291  CA  ILE A  62      12.615  59.260 453.813  1.00 76.08      A    C  
ANISOU  291  CA  ILE A  62    12979   5573  10355    579   1390   1976  A    C  
ATOM    292  C   ILE A  62      14.081  59.410 453.415  1.00 75.11      A    C  
ANISOU  292  C   ILE A  62    12882   5360  10298    435   1846   1959  A    C  
ATOM    293  O   ILE A  62      14.707  58.460 452.933  1.00 63.29      A    O  
ANISOU  293  O   ILE A  62    11473   3898   8678    378   2046   1914  A    O  
ATOM    294  CB  ILE A  62      12.424  58.087 454.787  1.00 71.11      A    C  
ANISOU  294  CB  ILE A  62    12036   5110   9872    521   1217   1798  A    C  
ATOM    295  CG1 ILE A  62      10.946  57.916 455.179  1.00 73.39      A    C  
ANISOU  295  CG1 ILE A  62    12277   5472  10138    673    804   1811  A    C  
ATOM    296  CG2 ILE A  62      13.336  58.230 455.991  1.00 60.12      A    C  
ANISOU  296  CG2 ILE A  62    10237   3751   8855    363   1341   1625  A    C  
ATOM    297  CD1 ILE A  62      10.296  59.197 455.704  1.00 72.83      A    C  
ANISOU  297  CD1 ILE A  62    12095   5329  10249    762    656   1860  A    C  
ATOM    298  N   HIS A  63      14.632  60.608 453.609  1.00 74.41      A    N  
ANISOU  298  N   HIS A  63    12710   5136  10428    380   2023   1986  A    N  
ATOM    299  CA  HIS A  63      16.036  60.881 453.335  1.00 66.54      A    C  
ANISOU  299  CA  HIS A  63    11666   4027   9587    244   2467   1958  A    C  
ATOM    300  C   HIS A  63      16.801  61.179 454.617  1.00 76.68      A    C  
ANISOU  300  C   HIS A  63    12479   5324  11332     96   2489   1767  A    C  
ATOM    301  O   HIS A  63      17.764  60.483 454.948  1.00 78.95      A    O  
ANISOU  301  O   HIS A  63    12527   5664  11806    -21   2655   1626  A    O  
ATOM    302  CB  HIS A  63      16.153  62.030 452.341  1.00 71.07      A    C  
ANISOU  302  CB  HIS A  63    12585   4397  10023    307   2702   2154  A    C  
ATOM    303  CG  HIS A  63      15.759  61.657 450.946  1.00 73.93      A    C  
ANISOU  303  CG  HIS A  63    13471   4731   9887    448   2770   2322  A    C  
ATOM    304  CD2 HIS A  63      16.503  61.417 449.840  1.00 85.06      A    C  
ANISOU  304  CD2 HIS A  63    15209   6047  11063    448   3172   2390  A    C  
ATOM    305  ND1 HIS A  63      14.444  61.528 450.555  1.00 74.04      A    N  
ANISOU  305  ND1 HIS A  63    13756   4808   9569    632   2386   2430  A    N  
ATOM    306  CE1 HIS A  63      14.395  61.209 449.273  1.00 77.33      A    C  
ANISOU  306  CE1 HIS A  63    14669   5180   9533    740   2509   2550  A    C  
ATOM    307  NE2 HIS A  63      15.631  61.141 448.814  1.00 81.71      A    N  
ANISOU  307  NE2 HIS A  63    15287   5636  10124    632   3006   2529  A    N  
ATOM    308  N   GLU A  64      16.405  62.202 455.353  1.00 82.94      A    N  
ANISOU  308  N   GLU A  64    13143   6058  12312    111   2316   1750  A    N  
ATOM    309  CA  GLU A  64      16.977  62.420 456.669  1.00 86.07      A    C  
ANISOU  309  CA  GLU A  64    13136   6480  13086     -3   2259   1544  A    C  
ATOM    310  C   GLU A  64      16.057  61.858 457.744  1.00 68.37      A    C  
ANISOU  310  C   GLU A  64    10723   4414  10839     56   1870   1425  A    C  
ATOM    311  O   GLU A  64      14.963  61.355 457.477  1.00 64.97      A    O  
ANISOU  311  O   GLU A  64    10446   4072  10168    177   1650   1504  A    O  
ATOM    312  CB  GLU A  64      17.236  63.910 456.905  1.00 82.60      A    C  
ANISOU  312  CB  GLU A  64    12665   5844  12875    -33   2350   1561  A    C  
ATOM    313  CG  GLU A  64      18.037  64.559 455.813  1.00 84.00      A    C  
ANISOU  313  CG  GLU A  64    13036   5820  13059    -75   2761   1701  A    C  
ATOM    314  CD  GLU A  64      17.156  65.246 454.781  1.00102.35      A    C  
ANISOU  314  CD  GLU A  64    15787   8030  15072     76   2748   1950  A    C  
ATOM    315  OE1 GLU A  64      16.112  65.842 455.159  1.00101.12      A    O  
ANISOU  315  OE1 GLU A  64    15675   7864  14881    184   2443   1991  A    O  
ATOM    316  OE2 GLU A  64      17.515  65.173 453.583  1.00104.34      A    O1-
ANISOU  316  OE2 GLU A  64    16340   8195  15109    101   3050   2102  A    O1-
ATOM    317  N   LEU A  65      16.516  61.969 458.987  1.00 68.74      A    N  
ANISOU  317  N   LEU A  65    10453   4498  11166    -23   1794   1230  A    N  
ATOM    318  CA  LEU A  65      15.671  61.642 460.122  1.00 64.60      A    C  
ANISOU  318  CA  LEU A  65     9789   4112  10646     44   1476   1111  A    C  
ATOM    319  C   LEU A  65      14.475  62.576 460.199  1.00 59.12      A    C  
ANISOU  319  C   LEU A  65     9237   3348   9877    182   1292   1195  A    C  
ATOM    320  O   LEU A  65      13.410  62.183 460.684  1.00 56.97      A    O  
ANISOU  320  O   LEU A  65     8947   3185   9513    293   1052   1173  A    O  
ATOM    321  CB  LEU A  65      16.489  61.703 461.409  1.00 68.58      A    C  
ANISOU  321  CB  LEU A  65     9980   4639  11440    -53   1449    888  A    C  
ATOM    322  CG  LEU A  65      15.820  61.224 462.687  1.00 51.00      A    C  
ANISOU  322  CG  LEU A  65     7613   2559   9207     12   1178    745  A    C  
ATOM    323  CD1 LEU A  65      15.316  59.840 462.464  1.00 50.33      A    C  
ANISOU  323  CD1 LEU A  65     7555   2646   8922     57   1093    782  A    C  
ATOM    324  CD2 LEU A  65      16.821  61.235 463.810  1.00 50.93      A    C  
ANISOU  324  CD2 LEU A  65     7337   2548   9466    -82   1160    534  A    C  
ATOM    325  N   SER A  66      14.637  63.823 459.761  1.00 58.02      A    N  
ANISOU  325  N   SER A  66     9222   3016   9808    184   1415   1287  A    N  
ATOM    326  CA  SER A  66      13.551  64.779 459.917  1.00 58.88      A    C  
ANISOU  326  CA  SER A  66     9440   3038   9892    324   1238   1352  A    C  
ATOM    327  C   SER A  66      12.318  64.371 459.123  1.00 58.83      A    C  
ANISOU  327  C   SER A  66     9647   3086   9621    491   1052   1526  A    C  
ATOM    328  O   SER A  66      11.196  64.657 459.548  1.00 72.15      A    O  
ANISOU  328  O   SER A  66    11322   4785  11305    634    819   1525  A    O  
ATOM    329  CB  SER A  66      14.010  66.171 459.492  1.00 68.62      A    C  
ANISOU  329  CB  SER A  66    10786   4030  11255    293   1424   1437  A    C  
ATOM    330  OG  SER A  66      14.765  66.105 458.298  1.00 73.15      A    O  
ANISOU  330  OG  SER A  66    11528   4521  11744    228   1707   1585  A    O  
ATOM    331  N   ASP A  67      12.492  63.654 458.010  1.00 59.50      A    N  
ANISOU  331  N   ASP A  67     9914   3202   9490    487   1148   1659  A    N  
ATOM    332  CA  ASP A  67      11.340  63.251 457.210  1.00 60.00      A    C  
ANISOU  332  CA  ASP A  67    10190   3307   9299    655    942   1820  A    C  
ATOM    333  C   ASP A  67      10.391  62.341 457.970  1.00 59.49      A    C  
ANISOU  333  C   ASP A  67     9943   3413   9246    730    660   1717  A    C  
ATOM    334  O   ASP A  67       9.218  62.239 457.600  1.00 71.20      A    O  
ANISOU  334  O   ASP A  67    11515   4912  10625    899    420   1821  A    O  
ATOM    335  CB  ASP A  67      11.786  62.555 455.933  1.00 67.32      A    C  
ANISOU  335  CB  ASP A  67    11386   4245   9949    638   1116   1947  A    C  
ATOM    336  CG  ASP A  67      12.616  63.440 455.065  1.00 72.45      A    C  
ANISOU  336  CG  ASP A  67    12262   4712  10553    593   1435   2075  A    C  
ATOM    337  OD1 ASP A  67      12.335  64.649 455.035  1.00 71.39      A    O  
ANISOU  337  OD1 ASP A  67    12199   4427  10501    655   1416   2164  A    O  
ATOM    338  OD2 ASP A  67      13.540  62.930 454.406  1.00 86.32      A    O1-
ANISOU  338  OD2 ASP A  67    14130   6463  12204    502   1726   2088  A    O1-
ATOM    339  N   ILE A  68      10.875  61.646 458.996  1.00 54.22      A    N  
ANISOU  339  N   ILE A  68     9022   2872   8709    620    688   1520  A    N  
ATOM    340  CA  ILE A  68       9.985  60.810 459.784  1.00 67.48      A    C  
ANISOU  340  CA  ILE A  68    10535   4701  10404    693    471   1424  A    C  
ATOM    341  C   ILE A  68       8.869  61.660 460.371  1.00 70.16      A    C  
ANISOU  341  C   ILE A  68    10825   4995  10838    851    288   1417  A    C  
ATOM    342  O   ILE A  68       7.729  61.201 460.520  1.00 73.91      A    O  
ANISOU  342  O   ILE A  68    11250   5541  11292    990     88   1428  A    O  
ATOM    343  CB  ILE A  68      10.784  60.080 460.876  1.00 55.73      A    C  
ANISOU  343  CB  ILE A  68     8796   3342   9037    557    558   1220  A    C  
ATOM    344  CG1 ILE A  68      11.831  59.188 460.233  1.00 55.46      A    C  
ANISOU  344  CG1 ILE A  68     8797   3345   8931    425    735   1227  A    C  
ATOM    345  CG2 ILE A  68       9.866  59.182 461.684  1.00 47.04      A    C  
ANISOU  345  CG2 ILE A  68     7537   2394   7942    634    387   1138  A    C  
ATOM    346  CD1 ILE A  68      11.228  58.034 459.495  1.00 58.17      A    C  
ANISOU  346  CD1 ILE A  68     9261   3764   9078    480    642   1307  A    C  
ATOM    347  N   LYS A  69       9.169  62.915 460.685  1.00 53.77      A    N  
ANISOU  347  N   LYS A  69     8759   2786   8886    841    369   1394  A    N  
ATOM    348  CA  LYS A  69       8.158  63.800 461.241  1.00 56.13      A    C  
ANISOU  348  CA  LYS A  69     9026   3023   9278   1001    233   1375  A    C  
ATOM    349  C   LYS A  69       6.984  63.981 460.278  1.00 56.71      A    C  
ANISOU  349  C   LYS A  69     9258   3031   9257   1196     13   1567  A    C  
ATOM    350  O   LYS A  69       5.829  64.043 460.710  1.00 80.16      A    O  
ANISOU  350  O   LYS A  69    12151   6036  12270   1372   -153   1537  A    O  
ATOM    351  CB  LYS A  69       8.819  65.121 461.619  1.00 56.29      A    C  
ANISOU  351  CB  LYS A  69     9059   2878   9451    941    375   1322  A    C  
ATOM    352  CG  LYS A  69       7.985  66.037 462.438  1.00 57.10      A    C  
ANISOU  352  CG  LYS A  69     9103   2917   9676   1082    292   1247  A    C  
ATOM    353  CD  LYS A  69       8.829  67.204 462.906  1.00 75.44      A    C  
ANISOU  353  CD  LYS A  69    11424   5072  12167    986    445   1159  A    C  
ATOM    354  CE  LYS A  69       8.027  68.202 463.721  1.00 78.25      A    C  
ANISOU  354  CE  LYS A  69    11745   5338  12649   1131    385   1074  A    C  
ATOM    355  NZ  LYS A  69       8.957  68.977 464.575  1.00 78.86      A    N1+
ANISOU  355  NZ  LYS A  69    11755   5303  12904   1007    516    902  A    N1+
ATOM    356  N   GLN A  70       7.246  64.018 458.972  1.00 58.70      A    N  
ANISOU  356  N   GLN A  70     9722   3204   9376   1186     34   1768  A    N  
ATOM    357  CA  GLN A  70       6.161  64.105 457.997  1.00 61.09      A    C  
ANISOU  357  CA  GLN A  70    10144   3468   9598   1384   -188   1978  A    C  
ATOM    358  C   GLN A  70       5.439  62.778 457.781  1.00 59.82      A    C  
ANISOU  358  C   GLN A  70     9898   3478   9354   1462   -350   1993  A    C  
ATOM    359  O   GLN A  70       4.414  62.753 457.097  1.00 61.91      A    O  
ANISOU  359  O   GLN A  70    10234   3768   9520   1669   -537   2128  A    O  
ATOM    360  CB  GLN A  70       6.685  64.591 456.646  1.00 64.24      A    C  
ANISOU  360  CB  GLN A  70    10880   3753   9776   1383    -48   2192  A    C  
ATOM    361  CG  GLN A  70       7.679  65.708 456.739  1.00 72.49      A    C  
ANISOU  361  CG  GLN A  70    12004   4626  10911   1261    209   2185  A    C  
ATOM    362  CD  GLN A  70       8.265  66.055 455.386  1.00 85.62      A    C  
ANISOU  362  CD  GLN A  70    14028   6177  12328   1254    407   2394  A    C  
ATOM    363  NE2 GLN A  70       9.341  66.843 455.392  1.00 99.70      A    N  
ANISOU  363  NE2 GLN A  70    15862   7813  14207   1112    710   2384  A    N  
ATOM    364  OE1 GLN A  70       7.762  65.620 454.343  1.00 79.71      A    O  
ANISOU  364  OE1 GLN A  70    13530   5471  11285   1384    296   2551  A    O  
ATOM    365  N   ALA A  71       5.958  61.677 458.312  1.00 69.98      A    N  
ANISOU  365  N   ALA A  71    11075   4893  10621   1321   -277   1842  A    N  
ATOM    366  CA  ALA A  71       5.432  60.369 457.966  1.00 65.24      A    C  
ANISOU  366  CA  ALA A  71    10466   4434   9889   1377   -394   1850  A    C  
ATOM    367  C   ALA A  71       4.192  60.004 458.779  1.00 71.06      A    C  
ANISOU  367  C   ALA A  71    10949   5283  10768   1527   -571   1750  A    C  
ATOM    368  O   ALA A  71       3.920  60.554 459.848  1.00 75.62      A    O  
ANISOU  368  O   ALA A  71    11356   5869  11508   1560   -509   1628  A    O  
ATOM    369  CB  ALA A  71       6.504  59.300 458.173  1.00 65.94      A    C  
ANISOU  369  CB  ALA A  71    10547   4606   9900   1168   -219   1730  A    C  
ATOM    370  N   ASN A  72       3.433  59.061 458.229  1.00 75.77      A    N  
ANISOU  370  N   ASN A  72    11542   5986  11262   1581   -888   1741  A    N  
ATOM    371  CA  ASN A  72       2.302  58.400 458.857  1.00 57.09      A    C  
ANISOU  371  CA  ASN A  72     8824   3752   9117   1635  -1134   1621  A    C  
ATOM    372  C   ASN A  72       2.695  56.939 459.059  1.00 52.76      A    C  
ANISOU  372  C   ASN A  72     8171   3343   8531   1457  -1108   1501  A    C  
ATOM    373  O   ASN A  72       3.369  56.358 458.210  1.00 62.02      A    O  
ANISOU  373  O   ASN A  72     9606   4531   9427   1371  -1082   1528  A    O  
ATOM    374  CB  ASN A  72       1.067  58.539 457.959  1.00 58.50      A    C  
ANISOU  374  CB  ASN A  72     9029   3939   9259   1835  -1542   1693  A    C  
ATOM    375  CG  ASN A  72      -0.184  57.971 458.573  1.00 77.86      A    C  
ANISOU  375  CG  ASN A  72    11042   6502  12038   1893  -1777   1568  A    C  
ATOM    376  ND2 ASN A  72      -1.135  58.844 458.897  1.00 72.13      A    N  
ANISOU  376  ND2 ASN A  72    10113   5760  11532   2054  -1848   1573  A    N  
ATOM    377  OD1 ASN A  72      -0.316  56.758 458.730  1.00 82.93      A    O  
ANISOU  377  OD1 ASN A  72    11513   7256  12740   1782  -1854   1459  A    O  
ATOM    378  N   ILE A  73       2.254  56.321 460.156  1.00 51.02      A    N  
ANISOU  378  N   ILE A  73     7576   3253   8555   1400  -1067   1359  A    N  
ATOM    379  CA  ILE A  73       2.774  54.988 460.475  1.00 55.92      A    C  
ANISOU  379  CA  ILE A  73     8101   4022   9124   1214   -955   1244  A    C  
ATOM    380  C   ILE A  73       2.328  53.954 459.446  1.00 74.81      A    C  
ANISOU  380  C   ILE A  73    10561   6499  11366   1195  -1219   1224  A    C  
ATOM    381  O   ILE A  73       2.974  52.908 459.282  1.00 48.61      A    O  
ANISOU  381  O   ILE A  73     7301   3255   7914   1048  -1129   1159  A    O  
ATOM    382  CB  ILE A  73       2.382  54.562 461.904  1.00 48.93      A    C  
ANISOU  382  CB  ILE A  73     6850   3233   8508   1172   -825   1121  A    C  
ATOM    383  CG1 ILE A  73       0.878  54.377 462.017  1.00 62.79      A    C  
ANISOU  383  CG1 ILE A  73     8310   5034  10514   1284  -1045   1090  A    C  
ATOM    384  CG2 ILE A  73       2.856  55.563 462.916  1.00 46.24      A    C  
ANISOU  384  CG2 ILE A  73     6493   2805   8272   1199   -593   1108  A    C  
ATOM    385  CD1 ILE A  73       0.395  54.231 463.441  1.00 68.85      A    C  
ANISOU  385  CD1 ILE A  73     8759   5849  11553   1282   -847   1001  A    C  
ATOM    386  N   ASN A  74       1.213  54.208 458.761  1.00 69.58      A    N  
ANISOU  386  N   ASN A  74     9884   5815  10739   1351  -1568   1263  A    N  
ATOM    387  CA  ASN A  74       0.763  53.319 457.697  1.00 62.53      A    C  
ANISOU  387  CA  ASN A  74     9093   4980   9684   1350  -1888   1221  A    C  
ATOM    388  C   ASN A  74       1.703  53.333 456.498  1.00 67.00      A    C  
ANISOU  388  C   ASN A  74    10170   5482   9804   1333  -1858   1307  A    C  
ATOM    389  O   ASN A  74       1.734  52.365 455.732  1.00 79.35      A    O  
ANISOU  389  O   ASN A  74    11881   7104  11166   1275  -2008   1235  A    O  
ATOM    390  CB  ASN A  74      -0.665  53.697 457.288  1.00 58.05      A    C  
ANISOU  390  CB  ASN A  74     8368   4389   9299   1544  -2319   1231  A    C  
ATOM    391  CG  ASN A  74      -1.640  53.595 458.453  1.00 61.75      A    C  
ANISOU  391  CG  ASN A  74     8303   4906  10254   1555  -2292   1136  A    C  
ATOM    392  ND2 ASN A  74      -1.725  54.656 459.243  1.00 59.50      A    N  
ANISOU  392  ND2 ASN A  74     7911   4545  10153   1652  -2106   1198  A    N  
ATOM    393  OD1 ASN A  74      -2.284  52.570 458.656  1.00 57.93      A    O  
ANISOU  393  OD1 ASN A  74     7517   4509   9984   1473  -2402   1006  A    O  
ATOM    394  N   SER A  75       2.469  54.405 456.317  1.00 68.50      A    N  
ANISOU  394  N   SER A  75    10643   5534   9850   1381  -1643   1454  A    N  
ATOM    395  CA  SER A  75       3.423  54.460 455.217  1.00 56.87      A    C  
ANISOU  395  CA  SER A  75     9666   3970   7970   1361  -1517   1553  A    C  
ATOM    396  C   SER A  75       4.649  53.603 455.476  1.00 58.01      A    C  
ANISOU  396  C   SER A  75     9822   4164   8055   1145  -1158   1467  A    C  
ATOM    397  O   SER A  75       5.329  53.208 454.528  1.00 74.84      A    O  
ANISOU  397  O   SER A  75    12314   6256   9865   1106  -1062   1494  A    O  
ATOM    398  CB  SER A  75       3.849  55.904 454.983  1.00 58.25      A    C  
ANISOU  398  CB  SER A  75    10115   3944   8075   1469  -1351   1748  A    C  
ATOM    399  OG  SER A  75       2.706  56.714 454.802  1.00 74.27      A    O  
ANISOU  399  OG  SER A  75    12114   5913  10193   1691  -1690   1832  A    O  
ATOM    400  N   LEU A  76       4.980  53.349 456.736  1.00 51.15      A    N  
ANISOU  400  N   LEU A  76     8592   3363   7478   1023   -947   1370  A    N  
ATOM    401  CA  LEU A  76       6.190  52.617 457.067  1.00 48.89      A    C  
ANISOU  401  CA  LEU A  76     8290   3106   7180    842   -626   1295  A    C  
ATOM    402  C   LEU A  76       5.933  51.206 457.558  1.00 54.15      A    C  
ANISOU  402  C   LEU A  76     8691   3931   7953    735   -694   1136  A    C  
ATOM    403  O   LEU A  76       6.761  50.324 457.326  1.00 68.89      A    O  
ANISOU  403  O   LEU A  76    10643   5818   9715    618   -532   1076  A    O  
ATOM    404  CB  LEU A  76       6.996  53.365 458.130  1.00 50.67      A    C  
ANISOU  404  CB  LEU A  76     8358   3264   7631    782   -332   1300  A    C  
ATOM    405  CG  LEU A  76       7.138  54.871 457.938  1.00 48.58      A    C  
ANISOU  405  CG  LEU A  76     8268   2813   7378    879   -251   1441  A    C  
ATOM    406  CD1 LEU A  76       7.603  55.499 459.232  1.00 46.82      A    C  
ANISOU  406  CD1 LEU A  76     7795   2548   7446    827    -64   1379  A    C  
ATOM    407  CD2 LEU A  76       8.092  55.165 456.801  1.00 50.42      A    C  
ANISOU  407  CD2 LEU A  76     8909   2890   7357    853    -35   1563  A    C  
ATOM    408  N   LEU A  77       4.847  50.983 458.217  1.00 46.97      A    N  
ANISOU  408  N   LEU A  77     7469   3109   7270    773   -892   1074  A    N  
ATOM    409  CA  LEU A  77       4.586  49.708 458.860  1.00 45.53      A    C  
ANISOU  409  CA  LEU A  77     7010   3043   7246    665   -898    941  A    C  
ATOM    410  C   LEU A  77       3.622  48.866 458.026  1.00 55.08      A    C  
ANISOU  410  C   LEU A  77     8220   4298   8409    680  -1232    867  A    C  
ATOM    411  O   LEU A  77       2.711  49.406 457.385  1.00 61.32      A    O  
ANISOU  411  O   LEU A  77     9063   5061   9176    813  -1538    904  A    O  
ATOM    412  CB  LEU A  77       3.999  49.944 460.256  1.00 44.60      A    C  
ANISOU  412  CB  LEU A  77     6527   2971   7449    685   -836    913  A    C  
ATOM    413  CG  LEU A  77       4.914  50.712 461.229  1.00 42.80      A    C  
ANISOU  413  CG  LEU A  77     6286   2699   7278    670   -552    940  A    C  
ATOM    414  CD1 LEU A  77       4.612  50.374 462.669  1.00 41.05      A    C  
ANISOU  414  CD1 LEU A  77     5770   2546   7280    650   -437    871  A    C  
ATOM    415  CD2 LEU A  77       6.389  50.481 460.948  1.00 41.39      A    C  
ANISOU  415  CD2 LEU A  77     6307   2478   6940    562   -334    941  A    C  
ATOM    416  N   PRO A  78       3.788  47.541 458.020  1.00 48.98      A    N  
ANISOU  416  N   PRO A  78     7385   3581   7645    553  -1207    751  A    N  
ATOM    417  CA  PRO A  78       2.842  46.682 457.293  1.00 49.80      A    C  
ANISOU  417  CA  PRO A  78     7454   3710   7757    547  -1546    641  A    C  
ATOM    418  C   PRO A  78       1.466  46.645 457.941  1.00 50.13      A    C  
ANISOU  418  C   PRO A  78     7076   3786   8185    584  -1749    593  A    C  
ATOM    419  O   PRO A  78       1.314  46.830 459.150  1.00 54.58      A    O  
ANISOU  419  O   PRO A  78     7349   4373   9016    569  -1543    617  A    O  
ATOM    420  CB  PRO A  78       3.507  45.302 457.340  1.00 48.00      A    C  
ANISOU  420  CB  PRO A  78     7239   3503   7497    387  -1384    529  A    C  
ATOM    421  CG  PRO A  78       4.945  45.584 457.652  1.00 45.77      A    C  
ANISOU  421  CG  PRO A  78     7115   3193   7081    344  -1003    603  A    C  
ATOM    422  CD  PRO A  78       4.952  46.787 458.514  1.00 44.61      A    C  
ANISOU  422  CD  PRO A  78     6836   3041   7072    417   -889    711  A    C  
ATOM    423  N   GLU A  79       0.455  46.373 457.117  1.00 53.21      A    N  
ANISOU  423  N   GLU A  79     7438   4168   8614    636  -2158    512  A    N  
ATOM    424  CA  GLU A  79      -0.900  46.266 457.643  1.00 54.74      A    C  
ANISOU  424  CA  GLU A  79     7178   4371   9251    662  -2357    447  A    C  
ATOM    425  C   GLU A  79      -0.963  45.223 458.747  1.00 62.89      A    C  
ANISOU  425  C   GLU A  79     7868   5429  10599    498  -2084    372  A    C  
ATOM    426  O   GLU A  79      -1.575  45.461 459.795  1.00 65.46      A    O  
ANISOU  426  O   GLU A  79     7844   5757  11270    515  -1935    398  A    O  
ATOM    427  CB  GLU A  79      -1.888  45.940 456.525  1.00 58.77      A    C  
ANISOU  427  CB  GLU A  79     7693   4856   9780    720  -2886    330  A    C  
ATOM    428  CG  GLU A  79      -3.339  45.874 456.975  1.00 77.28      A    C  
ANISOU  428  CG  GLU A  79     9513   7185  12665    752  -3120    249  A    C  
ATOM    429  CD  GLU A  79      -3.977  44.504 456.744  1.00 92.98      A    C  
ANISOU  429  CD  GLU A  79    11258   9154  14916    601  -3332     41  A    C  
ATOM    430  OE1 GLU A  79      -3.237  43.507 456.568  1.00 85.86      A    O  
ANISOU  430  OE1 GLU A  79    10545   8256  13820    449  -3187    -33  A    O  
ATOM    431  OE2 GLU A  79      -5.226  44.430 456.738  1.00106.30      A    O1-
ANISOU  431  OE2 GLU A  79    12544  10803  17044    635  -3641    -57  A    O1-
ATOM    432  N   HIS A  80      -0.305  44.073 458.540  1.00 52.04      A    N  
ANISOU  432  N   HIS A  80     6620   4057   9096    351  -1982    289  A    N  
ATOM    433  CA  HIS A  80      -0.354  42.987 459.518  1.00 50.78      A    C  
ANISOU  433  CA  HIS A  80     6181   3894   9217    202  -1730    234  A    C  
ATOM    434  C   HIS A  80       0.220  43.426 460.862  1.00 61.84      A    C  
ANISOU  434  C   HIS A  80     7505   5326  10667    214  -1318    356  A    C  
ATOM    435  O   HIS A  80      -0.314  43.066 461.921  1.00 47.73      A    O  
ANISOU  435  O   HIS A  80     5415   3529   9190    174  -1131    360  A    O  
ATOM    436  CB  HIS A  80       0.403  41.761 458.983  1.00 79.46      A    C  
ANISOU  436  CB  HIS A  80    10025   7502  12664     67  -1687    135  A    C  
ATOM    437  CG  HIS A  80      -0.079  41.289 457.642  1.00 96.32      A    C  
ANISOU  437  CG  HIS A  80    12306   9599  14692     59  -2101    -16  A    C  
ATOM    438  CD2 HIS A  80      -0.871  40.243 457.295  1.00102.78      A    C  
ANISOU  438  CD2 HIS A  80    12943  10358  15750    -43  -2343   -194  A    C  
ATOM    439  ND1 HIS A  80       0.233  41.939 456.465  1.00104.40      A    N  
ANISOU  439  ND1 HIS A  80    13730  10625  15310    172  -2327     -1  A    N  
ATOM    440  CE1 HIS A  80      -0.342  41.311 455.452  1.00109.23      A    C  
ANISOU  440  CE1 HIS A  80    14432  11196  15872    155  -2716   -169  A    C  
ATOM    441  NE2 HIS A  80      -1.018  40.280 455.928  1.00105.90      A    N  
ANISOU  441  NE2 HIS A  80    13640  10735  15861     18  -2749   -303  A    N  
ATOM    442  N   LEU A  81       1.300  44.221 460.841  1.00 53.14      A    N  
ANISOU  442  N   LEU A  81     6684   4243   9263    271  -1169    450  A    N  
ATOM    443  CA  LEU A  81       1.874  44.735 462.083  1.00 43.71      A    C  
ANISOU  443  CA  LEU A  81     5441   3070   8097    295   -844    537  A    C  
ATOM    444  C   LEU A  81       0.914  45.695 462.793  1.00 52.34      A    C  
ANISOU  444  C   LEU A  81     6299   4160   9427    412   -844    583  A    C  
ATOM    445  O   LEU A  81       0.761  45.636 464.020  1.00 43.79      A    O  
ANISOU  445  O   LEU A  81     5044   3086   8510    412   -597    604  A    O  
ATOM    446  CB  LEU A  81       3.199  45.438 461.791  1.00 42.17      A    C  
ANISOU  446  CB  LEU A  81     5562   2867   7592    321   -726    601  A    C  
ATOM    447  CG  LEU A  81       3.937  45.973 463.015  1.00 40.12      A    C  
ANISOU  447  CG  LEU A  81     5278   2618   7350    342   -448    655  A    C  
ATOM    448  CD1 LEU A  81       4.167  44.829 463.984  1.00 49.59      A    C  
ANISOU  448  CD1 LEU A  81     6350   3841   8652    256   -260    623  A    C  
ATOM    449  CD2 LEU A  81       5.224  46.692 462.662  1.00 39.15      A    C  
ANISOU  449  CD2 LEU A  81     5414   2457   7006    350   -346    699  A    C  
ATOM    450  N   ILE A  82       0.261  46.590 462.050  1.00 46.46      A    N  
ANISOU  450  N   ILE A  82     5569   3392   8692    529  -1108    603  A    N  
ATOM    451  CA  ILE A  82      -0.648  47.528 462.698  1.00 57.73      A    C  
ANISOU  451  CA  ILE A  82     6761   4797  10377    658  -1097    641  A    C  
ATOM    452  C   ILE A  82      -1.861  46.805 463.270  1.00 49.25      A    C  
ANISOU  452  C   ILE A  82     5276   3714   9723    620  -1082    573  A    C  
ATOM    453  O   ILE A  82      -2.201  46.986 464.441  1.00 49.02      A    O  
ANISOU  453  O   ILE A  82     5051   3676   9899    649   -806    596  A    O  
ATOM    454  CB  ILE A  82      -1.046  48.673 461.750  1.00 60.67      A    C  
ANISOU  454  CB  ILE A  82     7252   5123  10675    817  -1397    694  A    C  
ATOM    455  CG1 ILE A  82       0.199  49.439 461.326  1.00 58.72      A    C  
ANISOU  455  CG1 ILE A  82     7408   4851  10053    842  -1307    783  A    C  
ATOM    456  CG2 ILE A  82      -2.007  49.621 462.437  1.00 50.90      A    C  
ANISOU  456  CG2 ILE A  82     5745   3845   9749    964  -1374    724  A    C  
ATOM    457  CD1 ILE A  82      -0.098  50.675 460.491  1.00 72.71      A    C  
ANISOU  457  CD1 ILE A  82     9356   6544  11726   1014  -1539    875  A    C  
ATOM    458  N   SER A  83      -2.530  45.975 462.476  1.00 51.35      A    N  
ANISOU  458  N   SER A  83     5411   3964  10134    554  -1360    479  A    N  
ATOM    459  CA  SER A  83      -3.703  45.294 463.023  1.00 62.29      A    C  
ANISOU  459  CA  SER A  83     6357   5308  12002    499  -1320    408  A    C  
ATOM    460  C   SER A  83      -3.320  44.395 464.199  1.00 62.45      A    C  
ANISOU  460  C   SER A  83     6315   5327  12087    373   -885    427  A    C  
ATOM    461  O   SER A  83      -4.011  44.380 465.229  1.00 68.70      A    O  
ANISOU  461  O   SER A  83     6828   6079  13196    387   -615    449  A    O  
ATOM    462  CB  SER A  83      -4.439  44.515 461.930  1.00 56.37      A    C  
ANISOU  462  CB  SER A  83     5472   4521  11424    433  -1737    272  A    C  
ATOM    463  OG  SER A  83      -3.549  43.827 461.079  1.00 62.91      A    O  
ANISOU  463  OG  SER A  83     6647   5372  11883    338  -1858    223  A    O  
ATOM    464  N   GLY A  84      -2.193  43.683 464.088  1.00 53.55      A    N  
ANISOU  464  N   GLY A  84     5469   4228  10649    268   -788    431  A    N  
ATOM    465  CA  GLY A  84      -1.734  42.863 465.200  1.00 47.96      A    C  
ANISOU  465  CA  GLY A  84     4757   3509   9956    180   -404    471  A    C  
ATOM    466  C   GLY A  84      -1.474  43.654 466.474  1.00 63.59      A    C  
ANISOU  466  C   GLY A  84     6778   5513  11872    286    -79    569  A    C  
ATOM    467  O   GLY A  84      -1.717  43.157 467.579  1.00 47.02      A    O  
ANISOU  467  O   GLY A  84     4572   3379   9915    263    241    608  A    O  
ATOM    468  N   LEU A  85      -0.905  44.867 466.345  1.00 53.53      A    N  
ANISOU  468  N   LEU A  85     5705   4281  10355    402   -142    608  A    N  
ATOM    469  CA  LEU A  85      -0.695  45.712 467.526  1.00 52.14      A    C  
ANISOU  469  CA  LEU A  85     5580   4112  10118    511    124    665  A    C  
ATOM    470  C   LEU A  85      -2.009  46.244 468.081  1.00 53.85      A    C  
ANISOU  470  C   LEU A  85     5498   4280  10682    610    224    665  A    C  
ATOM    471  O   LEU A  85      -2.181  46.340 469.301  1.00 62.33      A    O  
ANISOU  471  O   LEU A  85     6542   5334  11805    661    554    696  A    O  
ATOM    472  CB  LEU A  85       0.263  46.861 467.211  1.00 43.14      A    C  
ANISOU  472  CB  LEU A  85     4712   2994   8683    590     31    688  A    C  
ATOM    473  CG  LEU A  85       1.765  46.520 467.167  1.00 40.78      A    C  
ANISOU  473  CG  LEU A  85     4696   2726   8072    517     79    694  A    C  
ATOM    474  CD1 LEU A  85       2.561  47.645 466.611  1.00 39.99      A    C  
ANISOU  474  CD1 LEU A  85     4807   2611   7774    572    -24    711  A    C  
ATOM    475  CD2 LEU A  85       2.306  46.156 468.527  1.00 39.83      A    C  
ANISOU  475  CD2 LEU A  85     4636   2619   7880    520    353    709  A    C  
ATOM    476  N   ALA A  86      -2.940  46.613 467.202  1.00 62.43      A    N  
ANISOU  476  N   ALA A  86     6375   5338  12009    654    -58    629  A    N  
ATOM    477  CA  ALA A  86      -4.231  47.128 467.657  1.00 65.73      A    C  
ANISOU  477  CA  ALA A  86     6450   5693  12833    759     25    619  A    C  
ATOM    478  C   ALA A  86      -5.004  46.079 468.440  1.00 62.37      A    C  
ANISOU  478  C   ALA A  86     5730   5209  12758    666    322    605  A    C  
ATOM    479  O   ALA A  86      -5.728  46.409 469.385  1.00 72.23      A    O  
ANISOU  479  O   ALA A  86     6786   6400  14258    747    633    624  A    O  
ATOM    480  CB  ALA A  86      -5.059  47.612 466.470  1.00 54.31      A    C  
ANISOU  480  CB  ALA A  86     4818   4217  11600    832   -409    576  A    C  
ATOM    481  N   SER A  87      -4.903  44.817 468.035  1.00 61.10      A    N  
ANISOU  481  N   SER A  87     5533   5040  12644    497    254    570  A    N  
ATOM    482  CA  SER A  87      -5.663  43.769 468.700  1.00 55.77      A    C  
ANISOU  482  CA  SER A  87     4571   4272  12349    389    548    565  A    C  
ATOM    483  C   SER A  87      -5.024  43.292 470.005  1.00 71.40      A    C  
ANISOU  483  C   SER A  87     6776   6244  14108    371   1024    663  A    C  
ATOM    484  O   SER A  87      -5.704  42.651 470.811  1.00 82.45      A    O  
ANISOU  484  O   SER A  87     7980   7543  15805    324   1387    699  A    O  
ATOM    485  CB  SER A  87      -5.856  42.594 467.745  1.00 56.76      A    C  
ANISOU  485  CB  SER A  87     4564   4356  12645    212    277    473  A    C  
ATOM    486  OG  SER A  87      -4.614  41.995 467.407  1.00 61.20      A    O  
ANISOU  486  OG  SER A  87     5499   4978  12778    128    212    484  A    O  
ATOM    487  N   ALA A  88      -3.736  43.553 470.222  1.00 71.56      A    N  
ANISOU  487  N   ALA A  88     7204   6351  13633    409   1029    708  A    N  
ATOM    488  CA  ALA A  88      -3.044  43.021 471.393  1.00 69.89      A    C  
ANISOU  488  CA  ALA A  88     7244   6134  13177    408   1393    794  A    C  
ATOM    489  C   ALA A  88      -3.454  43.769 472.657  1.00 77.93      A    C  
ANISOU  489  C   ALA A  88     8290   7124  14196    559   1762    844  A    C  
ATOM    490  O   ALA A  88      -3.326  44.994 472.734  1.00 91.50      A    O  
ANISOU  490  O   ALA A  88    10094   8886  15785    694   1688    817  A    O  
ATOM    491  CB  ALA A  88      -1.534  43.117 471.206  1.00 64.38      A    C  
ANISOU  491  CB  ALA A  88     6930   5529  12005    412   1235    803  A    C  
ATOM    492  N   ILE A  89      -3.917  43.028 473.662  1.00 70.87      A    N  
ANISOU  492  N   ILE A  89     7360   6138  13430    540   2185    918  A    N  
ATOM    493  CA  ILE A  89      -4.272  43.611 474.952  1.00 69.56      A    C  
ANISOU  493  CA  ILE A  89     7294   5930  13206    693   2604    969  A    C  
ATOM    494  C   ILE A  89      -3.181  43.349 475.981  1.00 68.93      A    C  
ANISOU  494  C   ILE A  89     7689   5883  12619    758   2787   1046  A    C  
ATOM    495  O   ILE A  89      -2.959  44.176 476.873  1.00 81.53      A    O  
ANISOU  495  O   ILE A  89     9531   7497  13949    919   2949   1042  A    O  
ATOM    496  CB  ILE A  89      -5.645  43.104 475.445  1.00 79.12      A    C  
ANISOU  496  CB  ILE A  89     8154   6989  14920    660   3019   1009  A    C  
ATOM    497  CG1 ILE A  89      -5.781  41.589 475.252  1.00 72.55      A    C  
ANISOU  497  CG1 ILE A  89     7203   6062  14302    466   3108   1061  A    C  
ATOM    498  CG2 ILE A  89      -6.773  43.875 474.760  1.00 87.86      A    C  
ANISOU  498  CG2 ILE A  89     8803   8063  16516    694   2860    914  A    C  
ATOM    499  CD1 ILE A  89      -7.127  41.043 475.658  1.00 65.44      A    C  
ANISOU  499  CD1 ILE A  89     5907   4977  13980    400   3527   1094  A    C  
ATOM    500  N   ARG A  90      -2.510  42.201 475.880  1.00 66.66      A    N  
ANISOU  500  N   ARG A  90     7539   5589  12201    647   2747   1104  A    N  
ATOM    501  CA  ARG A  90      -1.350  41.935 476.728  1.00 58.84      A    C  
ANISOU  501  CA  ARG A  90     6996   4634  10728    724   2811   1169  A    C  
ATOM    502  C   ARG A  90      -0.153  42.786 476.323  1.00 58.58      A    C  
ANISOU  502  C   ARG A  90     7169   4729  10360    779   2422   1079  A    C  
ATOM    503  O   ARG A  90       0.089  43.015 475.138  1.00 70.40      A    O  
ANISOU  503  O   ARG A  90     8517   6281  11951    694   2079   1005  A    O  
ATOM    504  CB  ARG A  90      -0.958  40.464 476.663  1.00 53.15      A    C  
ANISOU  504  CB  ARG A  90     6340   3848  10005    602   2856   1258  A    C  
ATOM    505  CG  ARG A  90      -1.340  39.698 477.895  1.00 67.46      A    C  
ANISOU  505  CG  ARG A  90     8323   5530  11779    652   3345   1411  A    C  
ATOM    506  CD  ARG A  90      -1.367  38.199 477.661  1.00 87.09      A    C  
ANISOU  506  CD  ARG A  90    10744   7892  14453    497   3440   1503  A    C  
ATOM    507  NE  ARG A  90      -2.411  37.782 476.726  1.00 98.88      A    N  
ANISOU  507  NE  ARG A  90    11761   9301  16509    312   3414   1438  A    N  
ATOM    508  CZ  ARG A  90      -2.346  36.678 475.986  1.00 97.92      A    C  
ANISOU  508  CZ  ARG A  90    11500   9099  16605    137   3290   1425  A    C  
ATOM    509  NH1 ARG A  90      -1.283  35.883 476.071  1.00103.73      A    N1+
ANISOU  509  NH1 ARG A  90    12530   9827  17054    132   3211   1489  A    N1+
ATOM    510  NH2 ARG A  90      -3.340  36.364 475.163  1.00 85.47      A    N  
ANISOU  510  NH2 ARG A  90     9485   7438  15550    -25   3225   1334  A    N  
ATOM    511  N   GLU A  91       0.592  43.272 477.312  1.00 48.85      A    N  
ANISOU  511  N   GLU A  91     6292   3529   8741    925   2480   1080  A    N  
ATOM    512  CA  GLU A  91       1.810  44.023 477.027  1.00 62.94      A    C  
ANISOU  512  CA  GLU A  91     8256   5405  10254    963   2131    987  A    C  
ATOM    513  C   GLU A  91       3.020  43.102 476.879  1.00 44.88      A    C  
ANISOU  513  C   GLU A  91     6135   3141   7776    905   1951   1018  A    C  
ATOM    514  O   GLU A  91       3.061  41.997 477.413  1.00 45.93      A    O  
ANISOU  514  O   GLU A  91     6379   3219   7853    898   2126   1124  A    O  
ATOM    515  CB  GLU A  91       2.078  45.055 478.119  1.00 47.46      A    C  
ANISOU  515  CB  GLU A  91     6577   3453   8003   1146   2213    928  A    C  
ATOM    516  CG  GLU A  91       1.076  46.176 478.098  1.00 60.22      A    C  
ANISOU  516  CG  GLU A  91     8025   5042   9815   1216   2329    866  A    C  
ATOM    517  CD  GLU A  91       1.362  47.225 479.127  1.00 67.85      A    C  
ANISOU  517  CD  GLU A  91     9288   6000  10494   1395   2399    777  A    C  
ATOM    518  OE1 GLU A  91       2.545  47.594 479.293  1.00 64.37      A    O  
ANISOU  518  OE1 GLU A  91     9084   5601   9774   1427   2140    696  A    O  
ATOM    519  OE2 GLU A  91       0.391  47.668 479.776  1.00 85.45      A    O1-
ANISOU  519  OE2 GLU A  91    11501   8164  12800   1504   2723    774  A    O1-
ATOM    520  N   ASN A  92       4.026  43.597 476.163  1.00 42.66      A    N  
ANISOU  520  N   ASN A  92     5873   2923   7412    872   1622    929  A    N  
ATOM    521  CA  ASN A  92       5.351  42.966 476.080  1.00 52.40      A    C  
ANISOU  521  CA  ASN A  92     7258   4176   8476    848   1434    928  A    C  
ATOM    522  C   ASN A  92       5.335  41.580 475.420  1.00 51.94      A    C  
ANISOU  522  C   ASN A  92     7086   4077   8571    715   1448   1000  A    C  
ATOM    523  O   ASN A  92       6.157  40.721 475.751  1.00 40.95      A    O  
ANISOU  523  O   ASN A  92     5844   2660   7053    731   1422   1048  A    O  
ATOM    524  CB  ASN A  92       6.006  42.893 477.468  1.00 42.71      A    C  
ANISOU  524  CB  ASN A  92     6365   2940   6925   1007   1487    949  A    C  
ATOM    525  CG  ASN A  92       6.234  44.283 478.084  1.00 48.79      A    C  
ANISOU  525  CG  ASN A  92     7280   3737   7520   1135   1409    830  A    C  
ATOM    526  ND2 ASN A  92       7.265  44.969 477.606  1.00 51.22      A    N  
ANISOU  526  ND2 ASN A  92     7573   4075   7812   1110   1114    712  A    N  
ATOM    527  OD1 ASN A  92       5.495  44.730 478.973  1.00 48.41      A    O  
ANISOU  527  OD1 ASN A  92     7356   3664   7373   1251   1635    836  A    O  
ATOM    528  N   GLU A  93       4.413  41.345 474.480  1.00 59.91      A    N  
ANISOU  528  N   GLU A  93     7833   5067   9864    591   1465    996  A    N  
ATOM    529  CA  GLU A  93       4.390  40.137 473.660  1.00 44.35      A    C  
ANISOU  529  CA  GLU A  93     5743   3046   8062    448   1428   1017  A    C  
ATOM    530  C   GLU A  93       4.755  40.525 472.231  1.00 46.32      A    C  
ANISOU  530  C   GLU A  93     5885   3344   8369    357   1145    914  A    C  
ATOM    531  O   GLU A  93       3.870  40.792 471.409  1.00 59.29      A    O  
ANISOU  531  O   GLU A  93     7332   4987  10208    293   1069    871  A    O  
ATOM    532  CB  GLU A  93       3.018  39.467 473.708  1.00 55.44      A    C  
ANISOU  532  CB  GLU A  93     6936   4361   9766    372   1654   1070  A    C  
ATOM    533  CG  GLU A  93       2.781  38.625 474.943  1.00 73.33      A    C  
ANISOU  533  CG  GLU A  93     9343   6530  11990    425   1994   1207  A    C  
ATOM    534  CD  GLU A  93       1.511  37.776 474.834  1.00 91.80      A    C  
ANISOU  534  CD  GLU A  93    11427   8738  14716    303   2238   1256  A    C  
ATOM    535  OE1 GLU A  93       0.808  37.878 473.802  1.00 93.26      A    O  
ANISOU  535  OE1 GLU A  93    11309   8921  15204    186   2085   1160  A    O  
ATOM    536  OE2 GLU A  93       1.207  37.021 475.784  1.00 83.84      A    O1-
ANISOU  536  OE2 GLU A  93    10525   7612  13717    329   2579   1390  A    O1-
ATOM    537  N   PRO A  94       6.034  40.545 471.870  1.00 38.61      A    N  
ANISOU  537  N   PRO A  94     5037   2395   7236    356    985    874  A    N  
ATOM    538  CA  PRO A  94       6.412  41.019 470.536  1.00 44.12      A    C  
ANISOU  538  CA  PRO A  94     5688   3124   7952    285    777    792  A    C  
ATOM    539  C   PRO A  94       5.809  40.196 469.412  1.00 42.74      A    C  
ANISOU  539  C   PRO A  94     5388   2910   7941    157    713    761  A    C  
ATOM    540  O   PRO A  94       5.473  39.025 469.568  1.00 59.85      A    O  
ANISOU  540  O   PRO A  94     7506   5010  10225     94    813    789  A    O  
ATOM    541  CB  PRO A  94       7.935  40.922 470.549  1.00 35.26      A    C  
ANISOU  541  CB  PRO A  94     4709   2004   6685    305    703    765  A    C  
ATOM    542  CG  PRO A  94       8.283  41.154 471.969  1.00 35.75      A    C  
ANISOU  542  CG  PRO A  94     4894   2076   6616    432    774    802  A    C  
ATOM    543  CD  PRO A  94       7.212  40.415 472.742  1.00 37.23      A    C  
ANISOU  543  CD  PRO A  94     5065   2224   6856    450    981    895  A    C  
ATOM    544  N   ILE A  95       5.616  40.870 468.288  1.00 36.62      A    N  
ANISOU  544  N   ILE A  95     4579   2162   7173    127    538    700  A    N  
ATOM    545  CA  ILE A  95       4.979  40.355 467.087  1.00 37.51      A    C  
ANISOU  545  CA  ILE A  95     4608   2247   7399     28    394    638  A    C  
ATOM    546  C   ILE A  95       5.976  40.513 465.948  1.00 40.84      A    C  
ANISOU  546  C   ILE A  95     5201   2674   7641      1    267    583  A    C  
ATOM    547  O   ILE A  95       6.613  41.563 465.817  1.00 35.89      A    O  
ANISOU  547  O   ILE A  95     4679   2079   6880     61    241    595  A    O  
ATOM    548  CB  ILE A  95       3.664  41.099 466.795  1.00 44.75      A    C  
ANISOU  548  CB  ILE A  95     5351   3178   8475     56    283    623  A    C  
ATOM    549  CG1 ILE A  95       2.601  40.680 467.807  1.00 50.26      A    C  
ANISOU  549  CG1 ILE A  95     5840   3834   9421     57    471    666  A    C  
ATOM    550  CG2 ILE A  95       3.201  40.890 465.370  1.00 40.03      A    C  
ANISOU  550  CG2 ILE A  95     4730   2563   7916    -11     24    536  A    C  
ATOM    551  CD1 ILE A  95       1.633  41.820 468.152  1.00 71.21      A    C  
ANISOU  551  CD1 ILE A  95     8342   6510  12206    157    477    682  A    C  
ATOM    552  N   TRP A  96       6.179  39.443 465.193  1.00 42.64      A    N  
ANISOU  552  N   TRP A  96     5472   2850   7878    -90    230    523  A    N  
ATOM    553  CA  TRP A  96       7.202  39.370 464.163  1.00 36.78      A    C  
ANISOU  553  CA  TRP A  96     4920   2089   6964   -116    189    469  A    C  
ATOM    554  C   TRP A  96       6.522  39.368 462.801  1.00 44.48      A    C  
ANISOU  554  C   TRP A  96     5957   3051   7891   -158    -22    385  A    C  
ATOM    555  O   TRP A  96       5.727  38.470 462.511  1.00 47.65      A    O  
ANISOU  555  O   TRP A  96     6268   3408   8429   -232   -114    313  A    O  
ATOM    556  CB  TRP A  96       8.044  38.115 464.379  1.00 36.50      A    C  
ANISOU  556  CB  TRP A  96     4928   1987   6955   -162    321    450  A    C  
ATOM    557  CG  TRP A  96       9.066  37.882 463.385  1.00 36.52      A    C  
ANISOU  557  CG  TRP A  96     5101   1948   6828   -188    339    384  A    C  
ATOM    558  CD1 TRP A  96       9.573  38.783 462.494  1.00 43.39      A    C  
ANISOU  558  CD1 TRP A  96     6122   2834   7531   -164    309    368  A    C  
ATOM    559  CD2 TRP A  96       9.712  36.643 463.117  1.00 38.22      A    C  
ANISOU  559  CD2 TRP A  96     5373   2072   7076   -236    429    327  A    C  
ATOM    560  CE2 TRP A  96      10.607  36.862 462.055  1.00 37.23      A    C  
ANISOU  560  CE2 TRP A  96     5426   1918   6799   -238    468    266  A    C  
ATOM    561  CE3 TRP A  96       9.629  35.367 463.680  1.00 38.15      A    C  
ANISOU  561  CE3 TRP A  96     5292   1982   7220   -272    508    328  A    C  
ATOM    562  NE1 TRP A  96      10.494  38.178 461.686  1.00 43.39      A    N  
ANISOU  562  NE1 TRP A  96     6272   2763   7453   -197    403    302  A    N  
ATOM    563  CZ2 TRP A  96      11.417  35.860 461.548  1.00 37.89      A    C  
ANISOU  563  CZ2 TRP A  96     5603   1903   6888   -268    584    191  A    C  
ATOM    564  CZ3 TRP A  96      10.426  34.374 463.170  1.00 45.22      A    C  
ANISOU  564  CZ3 TRP A  96     6279   2806   8096   -298    584    255  A    C  
ATOM    565  CH2 TRP A  96      11.312  34.625 462.113  1.00 38.15      A    C  
ANISOU  565  CH2 TRP A  96     5549   1862   7085   -296    630    181  A    C  
ATOM    566  N   VAL A  97       6.823  40.368 461.970  1.00 38.45      A    N  
ANISOU  566  N   VAL A  97     5362   2310   6938   -108   -107    392  A    N  
ATOM    567  CA  VAL A  97       6.188  40.516 460.662  1.00 45.48      A    C  
ANISOU  567  CA  VAL A  97     6380   3187   7712   -108   -347    327  A    C  
ATOM    568  C   VAL A  97       7.259  40.918 459.664  1.00 48.11      A    C  
ANISOU  568  C   VAL A  97     7030   3489   7761    -86   -281    329  A    C  
ATOM    569  O   VAL A  97       7.961  41.906 459.880  1.00 59.09      A    O  
ANISOU  569  O   VAL A  97     8484   4884   9083    -33   -152    415  A    O  
ATOM    570  CB  VAL A  97       5.045  41.565 460.677  1.00 50.31      A    C  
ANISOU  570  CB  VAL A  97     6877   3841   8398    -25   -547    370  A    C  
ATOM    571  CG1 VAL A  97       4.633  41.940 459.264  1.00 43.58      A    C  
ANISOU  571  CG1 VAL A  97     6240   2971   7347     19   -827    326  A    C  
ATOM    572  CG2 VAL A  97       3.818  41.068 461.474  1.00 42.06      A    C  
ANISOU  572  CG2 VAL A  97     5497   2800   7683    -56   -596    347  A    C  
ATOM    573  N   GLU A  98       7.361  40.192 458.554  1.00 53.91      A    N  
ANISOU  573  N   GLU A  98     7973   4173   8338   -127   -355    228  A    N  
ATOM    574  CA  GLU A  98       8.400  40.452 457.561  1.00 52.02      A    C  
ANISOU  574  CA  GLU A  98     8068   3879   7817   -106   -221    228  A    C  
ATOM    575  C   GLU A  98       7.821  40.954 456.240  1.00 45.47      A    C  
ANISOU  575  C   GLU A  98     7541   3034   6701    -41   -461    207  A    C  
ATOM    576  O   GLU A  98       6.716  40.586 455.840  1.00 60.92      A    O  
ANISOU  576  O   GLU A  98     9468   5004   8674    -41   -779    118  A    O  
ATOM    577  CB  GLU A  98       9.231  39.186 457.305  1.00 42.98      A    C  
ANISOU  577  CB  GLU A  98     7007   2663   6662   -180    -41    125  A    C  
ATOM    578  CG  GLU A  98       9.969  38.673 458.522  1.00 40.85      A    C  
ANISOU  578  CG  GLU A  98     6495   2389   6638   -214    183    159  A    C  
ATOM    579  CD  GLU A  98      10.710  37.372 458.268  1.00 55.41      A    C  
ANISOU  579  CD  GLU A  98     8401   4140   8511   -269    340     58  A    C  
ATOM    580  OE1 GLU A  98      10.127  36.464 457.633  1.00 55.49      A    O  
ANISOU  580  OE1 GLU A  98     8496   4103   8485   -320    210    -66  A    O  
ATOM    581  OE2 GLU A  98      11.877  37.265 458.710  1.00 58.94      A    O1-
ANISOU  581  OE2 GLU A  98     8801   4550   9045   -257    579     91  A    O1-
ATOM    582  N   THR A  99       8.597  41.773 455.549  1.00 46.15      A    N  
ANISOU  582  N   THR A  99     7928   3073   6533     18   -309    287  A    N  
ATOM    583  CA  THR A  99       8.357  42.159 454.170  1.00 50.68      A    C  
ANISOU  583  CA  THR A  99     8919   3601   6737     98   -462    284  A    C  
ATOM    584  C   THR A  99       9.463  41.549 453.318  1.00 54.50      A    C  
ANISOU  584  C   THR A  99     9739   3991   6978     67   -179    222  A    C  
ATOM    585  O   THR A  99      10.219  40.677 453.769  1.00 61.24      A    O  
ANISOU  585  O   THR A  99    10450   4820   7999    -18     61    154  A    O  
ATOM    586  CB  THR A  99       8.282  43.687 454.016  1.00 49.63      A    C  
ANISOU  586  CB  THR A  99     8912   3453   6491    211   -475    457  A    C  
ATOM    587  CG2 THR A  99       7.430  44.304 455.100  1.00 48.02      A    C  
ANISOU  587  CG2 THR A  99     8323   3325   6596    238   -639    517  A    C  
ATOM    588  OG1 THR A  99       9.591  44.252 454.070  1.00 60.34      A    O  
ANISOU  588  OG1 THR A  99    10380   4731   7815    195    -64    557  A    O  
ATOM    589  N   ASP A 100       9.554  41.989 452.066  1.00 54.42      A    N  
ANISOU  589  N   ASP A 100    10199   3914   6563    153   -196    248  A    N  
ATOM    590  CA  ASP A 100      10.589  41.432 451.201  1.00 71.70      A    C  
ANISOU  590  CA  ASP A 100    12747   5996   8500    137    128    186  A    C  
ATOM    591  C   ASP A 100      11.976  41.960 451.563  1.00 71.63      A    C  
ANISOU  591  C   ASP A 100    12682   5909   8624    105    636    306  A    C  
ATOM    592  O   ASP A 100      12.985  41.292 451.297  1.00 72.00      A    O  
ANISOU  592  O   ASP A 100    12817   5871   8670     59    981    237  A    O  
ATOM    593  CB  ASP A 100      10.265  41.716 449.730  1.00 79.39      A    C  
ANISOU  593  CB  ASP A 100    14311   6906   8946    255    -22    179  A    C  
ATOM    594  CG  ASP A 100       9.910  43.170 449.472  1.00 90.74      A    C  
ANISOU  594  CG  ASP A 100    15926   8334  10215    380   -124    384  A    C  
ATOM    595  OD1 ASP A 100       9.283  43.812 450.351  1.00 92.67      A    O  
ANISOU  595  OD1 ASP A 100    15801   8657  10751    388   -317    467  A    O  
ATOM    596  OD2 ASP A 100      10.254  43.660 448.377  1.00 92.82      A    O1-
ANISOU  596  OD2 ASP A 100    16728   8495  10046    480      8    465  A    O1-
ATOM    597  N   ARG A 101      12.060  43.158 452.136  1.00 63.44      A    N  
ANISOU  597  N   ARG A 101    11494   4882   7730    132    691    469  A    N  
ATOM    598  CA  ARG A 101      13.348  43.716 452.499  1.00 64.44      A    C  
ANISOU  598  CA  ARG A 101    11525   4915   8044     89   1134    561  A    C  
ATOM    599  C   ARG A 101      13.529  43.965 453.980  1.00 61.36      A    C  
ANISOU  599  C   ARG A 101    10626   4592   8096     32   1129    582  A    C  
ATOM    600  O   ARG A 101      14.678  44.047 454.426  1.00 65.15      A    O  
ANISOU  600  O   ARG A 101    10939   5001   8815    -23   1448    591  A    O  
ATOM    601  CB  ARG A 101      13.606  45.042 451.760  1.00 69.38      A    C  
ANISOU  601  CB  ARG A 101    12496   5422   8442    166   1308    737  A    C  
ATOM    602  CG  ARG A 101      13.705  44.942 450.229  1.00 76.38      A    C  
ANISOU  602  CG  ARG A 101    13995   6201   8824    245   1426    751  A    C  
ATOM    603  CD  ARG A 101      13.770  46.340 449.623  1.00 84.49      A    C  
ANISOU  603  CD  ARG A 101    15367   7106   9631    338   1557    967  A    C  
ATOM    604  NE  ARG A 101      13.425  46.425 448.207  1.00100.39      A    N  
ANISOU  604  NE  ARG A 101    18033   9042  11067    470   1502   1015  A    N  
ATOM    605  CZ  ARG A 101      12.185  46.557 447.743  1.00105.85      A    C  
ANISOU  605  CZ  ARG A 101    18948   9810  11458    597    987   1016  A    C  
ATOM    606  NH1 ARG A 101      11.161  46.604 448.590  1.00106.48      A    N1+
ANISOU  606  NH1 ARG A 101    18609  10040  11809    597    529    973  A    N1+
ATOM    607  NH2 ARG A 101      11.967  46.643 446.434  1.00102.43      A    N  
ANISOU  607  NH2 ARG A 101    19165   9293  10460    736    930   1057  A    N  
ATOM    608  N   LEU A 102      12.452  44.045 454.760  1.00 60.75      A    N  
ANISOU  608  N   LEU A 102    10299   4638   8144     49    781    578  A    N  
ATOM    609  CA  LEU A 102      12.548  44.423 456.164  1.00 58.80      A    C  
ANISOU  609  CA  LEU A 102     9649   4449   8245     22    775    607  A    C  
ATOM    610  C   LEU A 102      11.832  43.432 457.066  1.00 55.45      A    C  
ANISOU  610  C   LEU A 102     8928   4139   8003    -11    561    515  A    C  
ATOM    611  O   LEU A 102      10.836  42.816 456.682  1.00 50.19      A    O  
ANISOU  611  O   LEU A 102     8309   3521   7239     -5    314    452  A    O  
ATOM    612  CB  LEU A 102      11.990  45.823 456.407  1.00 43.84      A    C  
ANISOU  612  CB  LEU A 102     7743   2556   6359     93    655    729  A    C  
ATOM    613  CG  LEU A 102      12.806  46.929 455.771  1.00 45.45      A    C  
ANISOU  613  CG  LEU A 102     8188   2610   6469    113    923    846  A    C  
ATOM    614  CD1 LEU A 102      11.996  48.207 455.749  1.00 47.07      A    C  
ANISOU  614  CD1 LEU A 102     8468   2799   6619    209    744    969  A    C  
ATOM    615  CD2 LEU A 102      14.078  47.102 456.577  1.00 44.20      A    C  
ANISOU  615  CD2 LEU A 102     7780   2386   6631     31   1218    826  A    C  
ATOM    616  N   SER A 103      12.353  43.320 458.289  1.00 52.89      A    N  
ANISOU  616  N   SER A 103     8303   3840   7953    -43    656    511  A    N  
ATOM    617  CA  SER A 103      11.865  42.410 459.317  1.00 51.36      A    C  
ANISOU  617  CA  SER A 103     7844   3726   7943    -67    538    457  A    C  
ATOM    618  C   SER A 103      11.518  43.214 460.565  1.00 50.79      A    C  
ANISOU  618  C   SER A 103     7546   3715   8035    -26    468    518  A    C  
ATOM    619  O   SER A 103      12.388  43.887 461.137  1.00 39.54      A    O  
ANISOU  619  O   SER A 103     6050   2258   6716    -17    596    544  A    O  
ATOM    620  CB  SER A 103      12.919  41.343 459.627  1.00 42.87      A    C  
ANISOU  620  CB  SER A 103     6685   2604   6998   -115    727    391  A    C  
ATOM    621  OG  SER A 103      12.380  40.297 460.405  1.00 45.70      A    O  
ANISOU  621  OG  SER A 103     6869   3009   7487   -134    625    353  A    O  
ATOM    622  N   PHE A 104      10.250  43.142 460.974  1.00 49.34      A    N  
ANISOU  622  N   PHE A 104     7247   3606   7893     -2    269    523  A    N  
ATOM    623  CA  PHE A 104       9.675  43.937 462.054  1.00 45.78      A    C  
ANISOU  623  CA  PHE A 104     6622   3207   7565     56    210    573  A    C  
ATOM    624  C   PHE A 104       9.376  43.098 463.290  1.00 41.07      A    C  
ANISOU  624  C   PHE A 104     5819   2659   7127     46    230    556  A    C  
ATOM    625  O   PHE A 104       8.868  41.976 463.184  1.00 49.00      A    O  
ANISOU  625  O   PHE A 104     6774   3667   8177     -3    191    517  A    O  
ATOM    626  CB  PHE A 104       8.374  44.609 461.604  1.00 37.37      A    C  
ANISOU  626  CB  PHE A 104     5568   2166   6463    115      5    606  A    C  
ATOM    627  CG  PHE A 104       8.568  45.696 460.586  1.00 42.97      A    C  
ANISOU  627  CG  PHE A 104     6511   2814   7000    166    -22    666  A    C  
ATOM    628  CD1 PHE A 104       8.883  46.989 460.979  1.00 43.47      A    C  
ANISOU  628  CD1 PHE A 104     6579   2834   7101    221     52    735  A    C  
ATOM    629  CD2 PHE A 104       8.415  45.435 459.234  1.00 43.50      A    C  
ANISOU  629  CD2 PHE A 104     6826   2848   6855    167   -120    653  A    C  
ATOM    630  CE1 PHE A 104       9.046  47.989 460.038  1.00 39.73      A    C  
ANISOU  630  CE1 PHE A 104     6344   2273   6479    271     56    814  A    C  
ATOM    631  CE2 PHE A 104       8.588  46.432 458.295  1.00 41.91      A    C  
ANISOU  631  CE2 PHE A 104     6899   2572   6454    232   -123    737  A    C  
ATOM    632  CZ  PHE A 104       8.897  47.706 458.692  1.00 41.58      A    C  
ANISOU  632  CZ  PHE A 104     6850   2475   6475    282    -22    829  A    C  
ATOM    633  N   LEU A 105       9.658  43.681 464.459  1.00 34.42      A    N  
ANISOU  633  N   LEU A 105     4884   1836   6360     98    290    583  A    N  
ATOM    634  CA  LEU A 105       9.278  43.161 465.772  1.00 34.48      A    C  
ANISOU  634  CA  LEU A 105     4756   1883   6462    127    325    595  A    C  
ATOM    635  C   LEU A 105       8.625  44.292 466.574  1.00 35.80      A    C  
ANISOU  635  C   LEU A 105     4865   2079   6658    214    306    624  A    C  
ATOM    636  O   LEU A 105       9.281  45.279 466.904  1.00 39.35      A    O  
ANISOU  636  O   LEU A 105     5360   2509   7083    258    322    615  A    O  
ATOM    637  CB  LEU A 105      10.512  42.627 466.502  1.00 38.43      A    C  
ANISOU  637  CB  LEU A 105     5262   2361   6980    133    417    578  A    C  
ATOM    638  CG  LEU A 105      10.345  41.840 467.794  1.00 39.84      A    C  
ANISOU  638  CG  LEU A 105     5385   2557   7196    178    465    608  A    C  
ATOM    639  CD1 LEU A 105       9.725  40.481 467.546  1.00 33.86      A    C  
ANISOU  639  CD1 LEU A 105     4592   1774   6500    115    501    622  A    C  
ATOM    640  CD2 LEU A 105      11.681  41.746 468.526  1.00 34.06      A    C  
ANISOU  640  CD2 LEU A 105     4677   1824   6440    225    470    581  A    C  
ATOM    641  N   GLY A 106       7.350  44.166 466.900  1.00 34.76      A    N  
ANISOU  641  N   GLY A 106     4620   1976   6612    239    287    646  A    N  
ATOM    642  CA  GLY A 106       6.660  45.210 467.624  1.00 35.19      A    C  
ANISOU  642  CA  GLY A 106     4616   2043   6712    334    302    665  A    C  
ATOM    643  C   GLY A 106       5.875  44.686 468.807  1.00 35.81      A    C  
ANISOU  643  C   GLY A 106     4589   2139   6880    373    435    690  A    C  
ATOM    644  O   GLY A 106       5.305  43.605 468.774  1.00 36.40      A    O  
ANISOU  644  O   GLY A 106     4570   2205   7055    314    478    705  A    O  
ATOM    645  N   TRP A 107       5.799  45.510 469.843  1.00 38.97      A    N  
ANISOU  645  N   TRP A 107     5017   2543   7249    476    519    690  A    N  
ATOM    646  CA  TRP A 107       5.040  45.130 471.018  1.00 37.15      A    C  
ANISOU  646  CA  TRP A 107     4736   2312   7066    535    704    724  A    C  
ATOM    647  C   TRP A 107       4.431  46.369 471.651  1.00 38.09      A    C  
ANISOU  647  C   TRP A 107     4845   2420   7206    656    769    705  A    C  
ATOM    648  O   TRP A 107       4.849  47.492 471.393  1.00 43.66      A    O  
ANISOU  648  O   TRP A 107     5615   3111   7861    698    665    662  A    O  
ATOM    649  CB  TRP A 107       5.928  44.371 472.009  1.00 36.88      A    C  
ANISOU  649  CB  TRP A 107     4856   2279   6877    556    798    741  A    C  
ATOM    650  CG  TRP A 107       7.031  45.194 472.612  1.00 36.42      A    C  
ANISOU  650  CG  TRP A 107     4964   2227   6647    635    727    682  A    C  
ATOM    651  CD1 TRP A 107       7.008  45.843 473.810  1.00 44.41      A    C  
ANISOU  651  CD1 TRP A 107     6102   3236   7537    760    798    652  A    C  
ATOM    652  CD2 TRP A 107       8.330  45.458 472.041  1.00 37.47      A    C  
ANISOU  652  CD2 TRP A 107     5148   2351   6739    589    570    624  A    C  
ATOM    653  CE2 TRP A 107       9.030  46.271 472.951  1.00 35.74      A    C  
ANISOU  653  CE2 TRP A 107     5047   2118   6413    680    521    551  A    C  
ATOM    654  CE3 TRP A 107       8.962  45.085 470.851  1.00 34.39      A    C  
ANISOU  654  CE3 TRP A 107     4718   1947   6403    482    486    617  A    C  
ATOM    655  NE1 TRP A 107       8.204  46.501 474.017  1.00 49.37      A    N  
ANISOU  655  NE1 TRP A 107     6843   3854   8063    790    647    563  A    N  
ATOM    656  CZ2 TRP A 107      10.327  46.707 472.715  1.00 35.80      A    C  
ANISOU  656  CZ2 TRP A 107     5081   2092   6431    652    384    470  A    C  
ATOM    657  CZ3 TRP A 107      10.252  45.534 470.616  1.00 33.94      A    C  
ANISOU  657  CZ3 TRP A 107     4706   1857   6334    463    403    555  A    C  
ATOM    658  CH2 TRP A 107      10.920  46.331 471.543  1.00 34.41      A    C  
ANISOU  658  CH2 TRP A 107     4830   1896   6349    540    348    482  A    C  
ATOM    659  N   ARG A 108       3.444  46.144 472.497  1.00 39.64      A    N  
ANISOU  659  N   ARG A 108     4964   2600   7496    714    975    738  A    N  
ATOM    660  CA  ARG A 108       2.759  47.198 473.219  1.00 41.01      A    C  
ANISOU  660  CA  ARG A 108     5127   2748   7708    845   1102    715  A    C  
ATOM    661  C   ARG A 108       3.361  47.310 474.615  1.00 41.48      A    C  
ANISOU  661  C   ARG A 108     5442   2806   7514    948   1254    694  A    C  
ATOM    662  O   ARG A 108       3.452  46.317 475.346  1.00 52.71      A    O  
ANISOU  662  O   ARG A 108     6961   4227   8838    949   1410    752  A    O  
ATOM    663  CB  ARG A 108       1.262  46.890 473.292  1.00 43.29      A    C  
ANISOU  663  CB  ARG A 108     5160   2999   8290    854   1278    755  A    C  
ATOM    664  CG  ARG A 108       0.483  47.765 474.225  1.00 55.07      A    C  
ANISOU  664  CG  ARG A 108     6636   4445   9843   1002   1507    736  A    C  
ATOM    665  CD  ARG A 108      -0.943  47.279 474.322  1.00 66.74      A    C  
ANISOU  665  CD  ARG A 108     7813   5866  11679    994   1726    779  A    C  
ATOM    666  NE  ARG A 108      -1.738  48.108 475.221  1.00 69.08      A    N  
ANISOU  666  NE  ARG A 108     8079   6102  12066   1149   2005    758  A    N  
ATOM    667  CZ  ARG A 108      -3.067  48.090 475.253  1.00 88.66      A    C  
ANISOU  667  CZ  ARG A 108    10235   8509  14942   1176   2198    771  A    C  
ATOM    668  NH1 ARG A 108      -3.735  47.292 474.429  1.00100.89      A    N1+
ANISOU  668  NH1 ARG A 108    11458  10040  16835   1049   2093    793  A    N1+
ATOM    669  NH2 ARG A 108      -3.735  48.867 476.098  1.00 92.56      A    N  
ANISOU  669  NH2 ARG A 108    10716   8935  15518   1331   2492    745  A    N  
ATOM    670  N   HIS A 109       3.776  48.514 474.986  1.00 45.41      A    N  
ANISOU  670  N   HIS A 109     6071   3285   7896   1042   1195    609  A    N  
ATOM    671  CA  HIS A 109       4.272  48.779 476.332  1.00 50.19      A    C  
ANISOU  671  CA  HIS A 109     6948   3881   8243   1164   1292    552  A    C  
ATOM    672  C   HIS A 109       3.595  50.035 476.850  1.00 54.55      A    C  
ANISOU  672  C   HIS A 109     7525   4375   8825   1297   1409    476  A    C  
ATOM    673  O   HIS A 109       3.917  51.143 476.407  1.00 53.10      A    O  
ANISOU  673  O   HIS A 109     7334   4153   8688   1307   1245    395  A    O  
ATOM    674  CB  HIS A 109       5.795  48.946 476.373  1.00 49.81      A    C  
ANISOU  674  CB  HIS A 109     7072   3845   8008   1141   1045    470  A    C  
ATOM    675  CG  HIS A 109       6.324  49.175 477.758  1.00 56.82      A    C  
ANISOU  675  CG  HIS A 109     8256   4719   8614   1279   1067    388  A    C  
ATOM    676  CD2 HIS A 109       6.621  50.318 478.425  1.00 52.29      A    C  
ANISOU  676  CD2 HIS A 109     7849   4099   7922   1384   1006    243  A    C  
ATOM    677  ND1 HIS A 109       6.557  48.143 478.644  1.00 43.97      A    N  
ANISOU  677  ND1 HIS A 109     6820   3114   6772   1336   1151    449  A    N  
ATOM    678  CE1 HIS A 109       6.991  48.638 479.790  1.00 49.36      A    C  
ANISOU  678  CE1 HIS A 109     7796   3776   7182   1482   1116    345  A    C  
ATOM    679  NE2 HIS A 109       7.039  49.955 479.684  1.00 56.06      A    N  
ANISOU  679  NE2 HIS A 109     8627   4583   8092   1507   1024    204  A    N  
ATOM    680  N   GLU A 110       2.662  49.857 477.781  1.00 46.48      A    N  
ANISOU  680  N   GLU A 110     6543   3325   7792   1401   1724    508  A    N  
ATOM    681  CA  GLU A 110       1.949  50.957 478.432  1.00 51.63      A    C  
ANISOU  681  CA  GLU A 110     7242   3907   8468   1553   1909    429  A    C  
ATOM    682  C   GLU A 110       1.296  51.808 477.355  1.00 53.93      A    C  
ANISOU  682  C   GLU A 110     7238   4159   9092   1531   1796    421  A    C  
ATOM    683  O   GLU A 110       0.497  51.275 476.563  1.00 57.29      A    O  
ANISOU  683  O   GLU A 110     7368   4596   9802   1455   1804    510  A    O  
ATOM    684  CB  GLU A 110       2.932  51.706 479.324  1.00 52.87      A    C  
ANISOU  684  CB  GLU A 110     7751   4042   8294   1656   1806    284  A    C  
ATOM    685  CG  GLU A 110       3.458  50.918 480.489  1.00 65.59      A    C  
ANISOU  685  CG  GLU A 110     9698   5682   9543   1727   1897    293  A    C  
ATOM    686  CD  GLU A 110       4.306  51.778 481.394  1.00 81.99      A    C  
ANISOU  686  CD  GLU A 110    12120   7723  11308   1851   1750    110  A    C  
ATOM    687  OE1 GLU A 110       4.323  53.017 481.169  1.00 81.26      A    O  
ANISOU  687  OE1 GLU A 110    11986   7566  11324   1877   1651    -23  A    O  
ATOM    688  OE2 GLU A 110       4.976  51.215 482.298  1.00 86.38      A    O1-
ANISOU  688  OE2 GLU A 110    12993   8303  11524   1925   1704     95  A    O1-
ATOM    689  N   ASN A 111       1.622  53.096 477.263  1.00 67.03      A    N  
ANISOU  689  N   ASN A 111     8974   5757  10738   1597   1663    314  A    N  
ATOM    690  CA  ASN A 111       1.048  54.025 476.307  1.00 48.31      A    C  
ANISOU  690  CA  ASN A 111     6383   3321   8650   1614   1548    318  A    C  
ATOM    691  C   ASN A 111       1.559  53.814 474.890  1.00 50.09      A    C  
ANISOU  691  C   ASN A 111     6490   3584   8957   1468   1240    387  A    C  
ATOM    692  O   ASN A 111       1.008  54.417 473.970  1.00 46.40      A    O  
ANISOU  692  O   ASN A 111     5855   3067   8707   1487   1120    425  A    O  
ATOM    693  CB  ASN A 111       1.361  55.453 476.772  1.00 60.48      A    C  
ANISOU  693  CB  ASN A 111     8105   4753  10124   1733   1529    180  A    C  
ATOM    694  CG  ASN A 111       0.526  56.513 476.052  1.00 93.11      A    C  
ANISOU  694  CG  ASN A 111    12035   8778  14563   1814   1491    194  A    C  
ATOM    695  ND2 ASN A 111       0.927  57.778 476.213  1.00 93.48      A    N  
ANISOU  695  ND2 ASN A 111    12231   8725  14564   1877   1417     82  A    N  
ATOM    696  OD1 ASN A 111      -0.471  56.209 475.376  1.00101.03      A    O  
ANISOU  696  OD1 ASN A 111    12751   9794  15841   1815   1500    294  A    O  
ATOM    697  N   TYR A 112       2.613  53.023 474.686  1.00 47.50      A    N  
ANISOU  697  N   TYR A 112     6269   3329   8451   1342   1110    403  A    N  
ATOM    698  CA  TYR A 112       3.301  52.998 473.401  1.00 42.40      A    C  
ANISOU  698  CA  TYR A 112     5584   2692   7832   1219    857    444  A    C  
ATOM    699  C   TYR A 112       3.186  51.666 472.660  1.00 41.36      A    C  
ANISOU  699  C   TYR A 112     5326   2646   7743   1093    802    536  A    C  
ATOM    700  O   TYR A 112       2.836  50.629 473.219  1.00 47.94      A    O  
ANISOU  700  O   TYR A 112     6119   3528   8567   1074    948    569  A    O  
ATOM    701  CB  TYR A 112       4.777  53.360 473.581  1.00 41.35      A    C  
ANISOU  701  CB  TYR A 112     5656   2534   7520   1170    736    360  A    C  
ATOM    702  CG  TYR A 112       5.029  54.598 474.388  1.00 42.61      A    C  
ANISOU  702  CG  TYR A 112     5963   2593   7633   1275    762    231  A    C  
ATOM    703  CD1 TYR A 112       4.947  55.853 473.807  1.00 56.75      A    C  
ANISOU  703  CD1 TYR A 112     7738   4260   9564   1307    694    212  A    C  
ATOM    704  CD2 TYR A 112       5.414  54.513 475.714  1.00 43.54      A    C  
ANISOU  704  CD2 TYR A 112     6272   2721   7552   1348    837    121  A    C  
ATOM    705  CE1 TYR A 112       5.194  57.010 474.542  1.00 44.55      A    C  
ANISOU  705  CE1 TYR A 112     6332   2593   8003   1397    717     72  A    C  
ATOM    706  CE2 TYR A 112       5.669  55.646 476.453  1.00 60.28      A    C  
ANISOU  706  CE2 TYR A 112     8551   4735   9617   1444    833    -33  A    C  
ATOM    707  CZ  TYR A 112       5.568  56.904 475.864  1.00 56.00      A    C  
ANISOU  707  CZ  TYR A 112     7961   4059   9256   1459    777    -67  A    C  
ATOM    708  OH  TYR A 112       5.837  58.051 476.598  1.00 54.13      A    O  
ANISOU  708  OH  TYR A 112     7886   3688   8992   1547    771   -241  A    O  
ATOM    709  N   TYR A 113       3.509  51.742 471.368  1.00 40.41      A    N  
ANISOU  709  N   TYR A 113     5174   2520   7660   1010    600    577  A    N  
ATOM    710  CA  TYR A 113       3.907  50.626 470.523  1.00 39.21      A    C  
ANISOU  710  CA  TYR A 113     4999   2428   7471    876    499    624  A    C  
ATOM    711  C   TYR A 113       5.392  50.852 470.258  1.00 37.86      A    C  
ANISOU  711  C   TYR A 113     5004   2236   7146    807    420    591  A    C  
ATOM    712  O   TYR A 113       5.789  51.916 469.768  1.00 37.99      A    O  
ANISOU  712  O   TYR A 113     5094   2173   7169    824    349    581  A    O  
ATOM    713  CB  TYR A 113       3.186  50.612 469.172  1.00 39.77      A    C  
ANISOU  713  CB  TYR A 113     4949   2490   7670    851    325    681  A    C  
ATOM    714  CG  TYR A 113       1.692  50.492 469.162  1.00 44.40      A    C  
ANISOU  714  CG  TYR A 113     5292   3075   8504    913    332    700  A    C  
ATOM    715  CD1 TYR A 113       1.005  49.827 470.166  1.00 43.68      A    C  
ANISOU  715  CD1 TYR A 113     5061   3002   8532    926    549    692  A    C  
ATOM    716  CD2 TYR A 113       0.958  51.057 468.124  1.00 42.92      A    C  
ANISOU  716  CD2 TYR A 113     5011   2847   8450    967    120    731  A    C  
ATOM    717  CE1 TYR A 113      -0.386  49.734 470.138  1.00 44.63      A    C  
ANISOU  717  CE1 TYR A 113     4900   3096   8963    973    582    701  A    C  
ATOM    718  CE2 TYR A 113      -0.421  50.974 468.084  1.00 45.07      A    C  
ANISOU  718  CE2 TYR A 113     5004   3103   9017   1031     86    732  A    C  
ATOM    719  CZ  TYR A 113      -1.093  50.316 469.092  1.00 53.63      A    C  
ANISOU  719  CZ  TYR A 113     5897   4201  10280   1025    331    710  A    C  
ATOM    720  OH  TYR A 113      -2.472  50.229 469.039  1.00 49.36      A    O  
ANISOU  720  OH  TYR A 113     5023   3621  10111   1079    323    702  A    O  
ATOM    721  N   ILE A 114       6.220  49.877 470.579  1.00 44.04      A    N  
ANISOU  721  N   ILE A 114     5841   3065   7826    735    445    576  A    N  
ATOM    722  CA  ILE A 114       7.633  49.938 470.250  1.00 43.84      A    C  
ANISOU  722  CA  ILE A 114     5920   3011   7728    662    376    539  A    C  
ATOM    723  C   ILE A 114       7.861  48.975 469.102  1.00 39.97      A    C  
ANISOU  723  C   ILE A 114     5405   2547   7236    551    329    591  A    C  
ATOM    724  O   ILE A 114       7.374  47.841 469.145  1.00 38.41      A    O  
ANISOU  724  O   ILE A 114     5141   2405   7049    520    358    621  A    O  
ATOM    725  CB  ILE A 114       8.507  49.612 471.467  1.00 37.16      A    C  
ANISOU  725  CB  ILE A 114     5156   2179   6783    688    403    465  A    C  
ATOM    726  CG1 ILE A 114       8.034  50.449 472.661  1.00 37.13      A    C  
ANISOU  726  CG1 ILE A 114     5220   2154   6734    819    463    401  A    C  
ATOM    727  CG2 ILE A 114       9.974  49.824 471.116  1.00 35.44      A    C  
ANISOU  727  CG2 ILE A 114     4978   1905   6581    616    317    405  A    C  
ATOM    728  CD1 ILE A 114       8.877  50.303 473.892  1.00 39.36      A    C  
ANISOU  728  CD1 ILE A 114     5644   2440   6872    877    433    309  A    C  
ATOM    729  N   ILE A 115       8.532  49.452 468.054  1.00 35.11      A    N  
ANISOU  729  N   ILE A 115     4859   1870   6610    496    279    601  A    N  
ATOM    730  CA  ILE A 115       8.795  48.690 466.843  1.00 34.87      A    C  
ANISOU  730  CA  ILE A 115     4866   1844   6538    406    251    638  A    C  
ATOM    731  C   ILE A 115      10.286  48.703 466.561  1.00 34.51      A    C  
ANISOU  731  C   ILE A 115     4892   1754   6466    332    309    599  A    C  
ATOM    732  O   ILE A 115      10.887  49.774 466.417  1.00 45.44      A    O  
ANISOU  732  O   ILE A 115     6327   3088   7851    328    329    577  A    O  
ATOM    733  CB  ILE A 115       8.033  49.242 465.633  1.00 35.85      A    C  
ANISOU  733  CB  ILE A 115     5049   1935   6638    427    156    702  A    C  
ATOM    734  CG1 ILE A 115       6.531  49.110 465.826  1.00 36.64      A    C  
ANISOU  734  CG1 ILE A 115     5011   2088   6823    494     69    720  A    C  
ATOM    735  CG2 ILE A 115       8.485  48.557 464.367  1.00 37.06      A    C  
ANISOU  735  CG2 ILE A 115     5322   2075   6684    346    138    720  A    C  
ATOM    736  CD1 ILE A 115       5.882  50.384 466.243  1.00 39.58      A    C  
ANISOU  736  CD1 ILE A 115     5346   2413   7279    611     55    736  A    C  
ATOM    737  N   GLU A 116      10.877  47.522 466.457  1.00 34.00      A    N  
ANISOU  737  N   GLU A 116     4812   1722   6386    269    344    579  A    N  
ATOM    738  CA  GLU A 116      12.260  47.368 466.056  1.00 34.03      A    C  
ANISOU  738  CA  GLU A 116     4839   1706   6386    198    412    533  A    C  
ATOM    739  C   GLU A 116      12.267  46.803 464.643  1.00 49.72      A    C  
ANISOU  739  C   GLU A 116     6934   3652   8305    137    464    573  A    C  
ATOM    740  O   GLU A 116      11.478  45.907 464.333  1.00 46.77      A    O  
ANISOU  740  O   GLU A 116     6572   3286   7914    132    420    598  A    O  
ATOM    741  CB  GLU A 116      13.004  46.437 467.015  1.00 33.61      A    C  
ANISOU  741  CB  GLU A 116     4697   1689   6382    202    411    476  A    C  
ATOM    742  CG  GLU A 116      13.094  46.935 468.443  1.00 39.69      A    C  
ANISOU  742  CG  GLU A 116     5429   2455   7198    284    344    429  A    C  
ATOM    743  CD  GLU A 116      13.856  45.983 469.350  1.00 47.44      A    C  
ANISOU  743  CD  GLU A 116     6370   3435   8222    319    306    392  A    C  
ATOM    744  OE1 GLU A 116      14.159  44.860 468.896  1.00 61.94      A    O  
ANISOU  744  OE1 GLU A 116     8186   5291  10059    276    348    412  A    O  
ATOM    745  OE2 GLU A 116      14.156  46.348 470.514  1.00 60.27      A    O1-
ANISOU  745  OE2 GLU A 116     8004   5026   9871    404    218    336  A    O1-
ATOM    746  N   VAL A 117      13.125  47.339 463.770  1.00 35.25      A    N  
ANISOU  746  N   VAL A 117     5195   1753   6446     91    568    576  A    N  
ATOM    747  CA  VAL A 117      13.184  46.875 462.388  1.00 36.16      A    C  
ANISOU  747  CA  VAL A 117     5487   1793   6457     51    653    616  A    C  
ATOM    748  C   VAL A 117      14.626  46.562 462.022  1.00 36.75      A    C  
ANISOU  748  C   VAL A 117     5544   1842   6576    -15    837    562  A    C  
ATOM    749  O   VAL A 117      15.551  47.271 462.430  1.00 50.20      A    O  
ANISOU  749  O   VAL A 117     7138   3535   8402    -35    905    526  A    O  
ATOM    750  CB  VAL A 117      12.563  47.890 461.399  1.00 37.46      A    C  
ANISOU  750  CB  VAL A 117     5868   1855   6508     93    641    717  A    C  
ATOM    751  CG1 VAL A 117      13.357  49.191 461.332  1.00 38.31      A    C  
ANISOU  751  CG1 VAL A 117     5996   1916   6645     79    750    733  A    C  
ATOM    752  CG2 VAL A 117      12.446  47.257 460.024  1.00 41.93      A    C  
ANISOU  752  CG2 VAL A 117     6678   2392   6860     76    672    739  A    C  
ATOM    753  N   GLU A 118      14.811  45.481 461.270  1.00 37.18      A    N  
ANISOU  753  N   GLU A 118     5691   1866   6569    -48    923    545  A    N  
ATOM    754  CA  GLU A 118      16.116  45.016 460.816  1.00 53.30      A    C  
ANISOU  754  CA  GLU A 118     7708   3868   8676    -97   1135    491  A    C  
ATOM    755  C   GLU A 118      16.047  44.686 459.329  1.00 44.31      A    C  
ANISOU  755  C   GLU A 118     6871   2617   7347   -114   1297    521  A    C  
ATOM    756  O   GLU A 118      15.006  44.244 458.838  1.00 40.46      A    O  
ANISOU  756  O   GLU A 118     6581   2094   6698    -93   1185    544  A    O  
ATOM    757  CB  GLU A 118      16.575  43.756 461.604  1.00 51.59      A    C  
ANISOU  757  CB  GLU A 118     7298   3716   8590    -96   1099    412  A    C  
ATOM    758  CG  GLU A 118      16.697  43.963 463.104  1.00 46.89      A    C  
ANISOU  758  CG  GLU A 118     6480   3201   8134    -56    943    384  A    C  
ATOM    759  CD  GLU A 118      17.286  42.769 463.824  1.00 46.51      A    C  
ANISOU  759  CD  GLU A 118     6285   3180   8205    -32    917    331  A    C  
ATOM    760  OE1 GLU A 118      18.244  42.176 463.289  1.00 62.86      A    O  
ANISOU  760  OE1 GLU A 118     8317   5197  10370    -55   1068    287  A    O  
ATOM    761  OE2 GLU A 118      16.800  42.422 464.926  1.00 45.51      A    O1-
ANISOU  761  OE2 GLU A 118     6096   3113   8084     21    765    341  A    O1-
ATOM    762  N   ARG A 119      17.153  44.896 458.606  1.00 51.98      A    N  
ANISOU  762  N   ARG A 119     7902   3510   8340   -147   1574    514  A    N  
ATOM    763  CA  ARG A 119      17.215  44.382 457.239  1.00 56.23      A    C  
ANISOU  763  CA  ARG A 119     8776   3929   8661   -151   1779    523  A    C  
ATOM    764  C   ARG A 119      17.187  42.859 457.263  1.00 43.69      A    C  
ANISOU  764  C   ARG A 119     7165   2349   7087   -162   1757    421  A    C  
ATOM    765  O   ARG A 119      17.651  42.221 458.209  1.00 42.03      A    O  
ANISOU  765  O   ARG A 119     6645   2222   7102   -169   1698    356  A    O  
ATOM    766  CB  ARG A 119      18.456  44.877 456.497  1.00 45.75      A    C  
ANISOU  766  CB  ARG A 119     7506   2500   7379   -180   2156    536  A    C  
ATOM    767  CG  ARG A 119      18.457  46.369 456.246  1.00 52.12      A    C  
ANISOU  767  CG  ARG A 119     8401   3260   8142   -174   2220    645  A    C  
ATOM    768  CD  ARG A 119      19.494  46.769 455.202  1.00 58.01      A    C  
ANISOU  768  CD  ARG A 119     9314   3864   8863   -196   2657    679  A    C  
ATOM    769  NE  ARG A 119      19.773  48.194 455.255  1.00 70.02      A    N  
ANISOU  769  NE  ARG A 119    10786   5342  10476   -207   2738    758  A    N  
ATOM    770  CZ  ARG A 119      20.598  48.737 456.146  1.00 82.86      A    C  
ANISOU  770  CZ  ARG A 119    12018   6990  12475   -259   2755    695  A    C  
ATOM    771  NH1 ARG A 119      21.210  47.962 457.044  1.00 78.58      A    N1+
ANISOU  771  NH1 ARG A 119    11120   6520  12219   -285   2678    567  A    N1+
ATOM    772  NH2 ARG A 119      20.815  50.048 456.146  1.00 83.85      A    N  
ANISOU  772  NH2 ARG A 119    12122   7048  12688   -276   2831    756  A    N  
ATOM    773  N   TYR A 120      16.658  42.273 456.195  1.00 57.62      A    N  
ANISOU  773  N   TYR A 120     9287   4025   8583   -153   1785    402  A    N  
ATOM    774  CA  TYR A 120      16.283  40.868 456.253  1.00 66.51      A    C  
ANISOU  774  CA  TYR A 120    10382   5200   9690   -164   1659    289  A    C  
ATOM    775  C   TYR A 120      16.444  40.187 454.896  1.00 69.44      A    C  
ANISOU  775  C   TYR A 120    11123   5480   9782   -160   1824    209  A    C  
ATOM    776  O   TYR A 120      16.117  40.753 453.846  1.00 62.23      A    O  
ANISOU  776  O   TYR A 120    10579   4532   8534   -124   1841    251  A    O  
ATOM    777  CB  TYR A 120      14.847  40.726 456.756  1.00 58.31      A    C  
ANISOU  777  CB  TYR A 120     9265   4301   8591   -152   1264    290  A    C  
ATOM    778  CG  TYR A 120      14.168  39.472 456.280  1.00 66.58      A    C  
ANISOU  778  CG  TYR A 120    10420   5360   9517   -173   1117    173  A    C  
ATOM    779  CD1 TYR A 120      14.544  38.232 456.787  1.00 68.57      A    C  
ANISOU  779  CD1 TYR A 120    10502   5582   9968   -207   1179     88  A    C  
ATOM    780  CD2 TYR A 120      13.126  39.520 455.350  1.00 66.64      A    C  
ANISOU  780  CD2 TYR A 120    10695   5392   9234   -152    884    140  A    C  
ATOM    781  CE1 TYR A 120      13.923  37.064 456.374  1.00 69.55      A    C  
ANISOU  781  CE1 TYR A 120    10716   5686  10024   -240   1052    -34  A    C  
ATOM    782  CE2 TYR A 120      12.495  38.357 454.929  1.00 75.35      A    C  
ANISOU  782  CE2 TYR A 120    11876   6486  10267   -185    715     -2  A    C  
ATOM    783  CZ  TYR A 120      12.900  37.125 455.450  1.00 79.36      A    C  
ANISOU  783  CZ  TYR A 120    12205   6950  10999   -239    818    -91  A    C  
ATOM    784  OH  TYR A 120      12.288  35.947 455.054  1.00 84.95      A    O  
ANISOU  784  OH  TYR A 120    12981   7617  11679   -286    665   -244  A    O  
ATOM    785  N   HIS A 121      16.955  38.958 454.942  1.00 75.80      A    N  
ANISOU  785  N   HIS A 121    11854   6235  10713   -181   1941     94  A    N  
ATOM    786  CA  HIS A 121      17.252  38.173 453.753  1.00 84.07      A    C  
ANISOU  786  CA  HIS A 121    13240   7173  11532   -173   2141    -17  A    C  
ATOM    787  C   HIS A 121      16.565  36.815 453.850  1.00 76.22      A    C  
ANISOU  787  C   HIS A 121    12222   6206  10532   -196   1912   -158  A    C  
ATOM    788  O   HIS A 121      16.683  36.125 454.871  1.00 75.37      A    O  
ANISOU  788  O   HIS A 121    11779   6118  10738   -218   1849   -177  A    O  
ATOM    789  CB  HIS A 121      18.765  37.998 453.597  1.00 82.41      A    C  
ANISOU  789  CB  HIS A 121    12958   6808  11544   -175   2611    -39  A    C  
ATOM    790  CG  HIS A 121      19.168  37.407 452.285  1.00 89.51      A    C  
ANISOU  790  CG  HIS A 121    14263   7570  12176   -151   2913   -141  A    C  
ATOM    791  CD2 HIS A 121      19.777  36.234 451.985  1.00 96.02      A    C  
ANISOU  791  CD2 HIS A 121    15113   8282  13087   -143   3135   -285  A    C  
ATOM    792  ND1 HIS A 121      18.939  38.041 451.080  1.00 88.60      A    N  
ANISOU  792  ND1 HIS A 121    14638   7406  11621   -113   3026   -101  A    N  
ATOM    793  CE1 HIS A 121      19.393  37.284 450.096  1.00 96.15      A    C  
ANISOU  793  CE1 HIS A 121    15925   8232  12377    -85   3315   -223  A    C  
ATOM    794  NE2 HIS A 121      19.907  36.183 450.618  1.00 97.44      A    N  
ANISOU  794  NE2 HIS A 121    15800   8352  12872   -106   3393   -344  A    N  
ATOM    795  N   VAL A 122      15.855  36.429 452.788  1.00 62.70      A    N  
ANISOU  795  N   VAL A 122    10884   4476   8464   -186   1778   -259  A    N  
ATOM    796  CA  VAL A 122      15.152  35.151 452.797  1.00 74.93      A    C  
ANISOU  796  CA  VAL A 122    12416   6020  10034   -226   1549   -418  A    C  
ATOM    797  C   VAL A 122      16.157  34.005 452.743  1.00 73.03      A    C  
ANISOU  797  C   VAL A 122    12144   5636   9968   -234   1862   -535  A    C  
ATOM    798  O   VAL A 122      17.103  34.017 451.943  1.00 55.85      A    O  
ANISOU  798  O   VAL A 122    10207   3342   7673   -196   2229   -572  A    O  
ATOM    799  CB  VAL A 122      14.147  35.064 451.636  1.00 73.60      A    C  
ANISOU  799  CB  VAL A 122    12661   5855   9449   -209   1272   -531  A    C  
ATOM    800  CG1 VAL A 122      13.086  36.142 451.754  1.00 53.83      A    C  
ANISOU  800  CG1 VAL A 122    10136   3483   6834   -182    920   -416  A    C  
ATOM    801  CG2 VAL A 122      14.852  35.141 450.290  1.00 72.74      A    C  
ANISOU  801  CG2 VAL A 122    13062   5624   8953   -147   1574   -591  A    C  
ATOM    802  N   GLN A 123      15.966  33.015 453.616  1.00 79.98      A    N  
ANISOU  802  N   GLN A 123    12729   6509  11151   -273   1747   -581  A    N  
ATOM    803  CA  GLN A 123      16.685  31.746 453.542  1.00 92.43      A    C  
ANISOU  803  CA  GLN A 123    14290   7931  12898   -271   1969   -711  A    C  
ATOM    804  C   GLN A 123      15.700  30.683 453.073  1.00 82.00      A    C  
ANISOU  804  C   GLN A 123    13136   6557  11465   -327   1720   -893  A    C  
ATOM    805  O   GLN A 123      14.796  30.281 453.821  1.00 67.88      A    O  
ANISOU  805  O   GLN A 123    11119   4816   9857   -386   1436   -882  A    O  
ATOM    806  CB  GLN A 123      17.316  31.347 454.881  1.00100.70      A    C  
ANISOU  806  CB  GLN A 123    14865   9035  14359   -252   2003   -609  A    C  
ATOM    807  CG  GLN A 123      18.617  32.076 455.226  1.00 99.46      A    C  
ANISOU  807  CG  GLN A 123    14490   8945  14357   -191   2252   -495  A    C  
ATOM    808  CD  GLN A 123      18.360  33.339 456.021  1.00 90.31      A    C  
ANISOU  808  CD  GLN A 123    13150   7921  13244   -193   2096   -337  A    C  
ATOM    809  NE2 GLN A 123      18.970  34.453 455.602  1.00 86.57      A    N  
ANISOU  809  NE2 GLN A 123    12746   7435  12711   -180   2298   -276  A    N  
ATOM    810  OE1 GLN A 123      17.604  33.316 456.996  1.00 83.55      A    O  
ANISOU  810  OE1 GLN A 123    12105   7167  12474   -207   1819   -271  A    O  
ATOM    811  N   THR A 124      15.868  30.241 451.833  1.00 77.95      A    N  
ANISOU  811  N   THR A 124    13028   5927  10660   -310   1840  -1070  A    N  
ATOM    812  CA  THR A 124      15.161  29.066 451.346  1.00 71.40      A    C  
ANISOU  812  CA  THR A 124    12363   4995   9771   -364   1643  -1295  A    C  
ATOM    813  C   THR A 124      16.100  27.884 451.512  1.00 75.03      A    C  
ANISOU  813  C   THR A 124    12732   5283  10495   -347   1953  -1387  A    C  
ATOM    814  O   THR A 124      16.952  27.634 450.654  1.00 96.45      A    O  
ANISOU  814  O   THR A 124    15686   7919  13041   -283   2262  -1478  A    O  
ATOM    815  CB  THR A 124      14.773  29.241 449.885  1.00 77.59      A    C  
ANISOU  815  CB  THR A 124    13690   5749  10041   -335   1549  -1460  A    C  
ATOM    816  CG2 THR A 124      14.108  27.988 449.354  1.00 86.74      A    C  
ANISOU  816  CG2 THR A 124    15025   6776  11155   -395   1327  -1739  A    C  
ATOM    817  OG1 THR A 124      13.891  30.356 449.753  1.00 88.21      A    O  
ANISOU  817  OG1 THR A 124    15097   7259  11159   -325   1222  -1354  A    O  
ATOM    818  N   SER A 125      15.942  27.145 452.604  1.00 58.12      A    N  
ANISOU  818  N   SER A 125    10170   3185   8728   -380   1829  -1317  A    N  
ATOM    819  CA  SER A 125      16.689  25.903 452.753  1.00 74.72      A    C  
ANISOU  819  CA  SER A 125    12124   5226  11041   -342   1997  -1368  A    C  
ATOM    820  C   SER A 125      16.119  25.145 453.936  1.00 70.25      A    C  
ANISOU  820  C   SER A 125    11201   4692  10799   -388   1772  -1280  A    C  
ATOM    821  O   SER A 125      15.379  25.705 454.752  1.00 55.37      A    O  
ANISOU  821  O   SER A 125     9129   2908   9000   -431   1562  -1145  A    O  
ATOM    822  CB  SER A 125      18.196  26.150 452.929  1.00 67.76      A    C  
ANISOU  822  CB  SER A 125    11081   4387  10277   -236   2365  -1251  A    C  
ATOM    823  OG  SER A 125      18.507  26.494 454.260  1.00 67.90      A    O  
ANISOU  823  OG  SER A 125    10678   4545  10575   -206   2297  -1035  A    O  
ATOM    824  N   ASN A 126      16.486  23.871 454.030  1.00 59.10      A    N  
ANISOU  824  N   ASN A 126     9714   3185   9554   -368   1846  -1344  A    N  
ATOM    825  CA  ASN A 126      16.067  23.064 455.161  1.00 58.07      A    C  
ANISOU  825  CA  ASN A 126     9294   3067   9702   -393   1696  -1233  A    C  
ATOM    826  C   ASN A 126      17.122  23.016 456.258  1.00 56.49      A    C  
ANISOU  826  C   ASN A 126     8795   2966   9704   -279   1838  -1022  A    C  
ATOM    827  O   ASN A 126      16.965  22.257 457.222  1.00 60.55      A    O  
ANISOU  827  O   ASN A 126     9122   3477  10410   -268   1764   -916  A    O  
ATOM    828  CB  ASN A 126      15.679  21.657 454.698  1.00 60.91      A    C  
ANISOU  828  CB  ASN A 126     9767   3240  10137   -448   1645  -1422  A    C  
ATOM    829  CG  ASN A 126      16.779  20.971 453.940  1.00 63.42      A    C  
ANISOU  829  CG  ASN A 126    10229   3445  10421   -362   1921  -1551  A    C  
ATOM    830  ND2 ASN A 126      16.429  19.926 453.220  1.00 66.43      A    N  
ANISOU  830  ND2 ASN A 126    10803   3651  10788   -409   1879  -1773  A    N  
ATOM    831  OD1 ASN A 126      17.933  21.381 453.992  1.00 67.12      A    O  
ANISOU  831  OD1 ASN A 126    10628   3976  10899   -256   2174  -1462  A    O  
ATOM    832  N   TRP A 127      18.151  23.858 456.158  1.00 55.85      A    N  
ANISOU  832  N   TRP A 127     8673   2963   9583   -196   2029   -960  A    N  
ATOM    833  CA  TRP A 127      19.216  23.890 457.153  1.00 54.84      A    C  
ANISOU  833  CA  TRP A 127     8254   2912   9670    -85   2121   -797  A    C  
ATOM    834  C   TRP A 127      18.668  23.957 458.572  1.00 52.63      A    C  
ANISOU  834  C   TRP A 127     7757   2743   9496    -80   1893   -610  A    C  
ATOM    835  O   TRP A 127      19.150  23.253 459.460  1.00 52.84      A    O  
ANISOU  835  O   TRP A 127     7619   2754   9704      0   1891   -515  A    O  
ATOM    836  CB  TRP A 127      20.122  25.090 456.888  1.00 54.32      A    C  
ANISOU  836  CB  TRP A 127     8150   2924   9566    -37   2300   -756  A    C  
ATOM    837  CG  TRP A 127      21.346  25.130 457.739  1.00 54.09      A    C  
ANISOU  837  CG  TRP A 127     7816   2936   9800     74   2390   -643  A    C  
ATOM    838  CD1 TRP A 127      22.531  24.530 457.489  1.00 56.28      A    C  
ANISOU  838  CD1 TRP A 127     7998   3113  10272    155   2628   -693  A    C  
ATOM    839  CD2 TRP A 127      21.485  25.780 459.006  1.00 61.16      A    C  
ANISOU  839  CD2 TRP A 127     8462   3966  10810    121   2215   -475  A    C  
ATOM    840  CE2 TRP A 127      22.796  25.538 459.452  1.00 53.11      A    C  
ANISOU  840  CE2 TRP A 127     7206   2909  10065    231   2327   -443  A    C  
ATOM    841  CE3 TRP A 127      20.629  26.551 459.804  1.00 49.50      A    C  
ANISOU  841  CE3 TRP A 127     6948   2625   9237     86   1974   -359  A    C  
ATOM    842  NE1 TRP A 127      23.413  24.777 458.501  1.00 55.73      A    N  
ANISOU  842  NE1 TRP A 127     7617   3099  10460    246   2589   -572  A    N  
ATOM    843  CZ2 TRP A 127      23.276  26.035 460.661  1.00 52.01      A    C  
ANISOU  843  CZ2 TRP A 127     6818   2854  10090    308   2168   -314  A    C  
ATOM    844  CZ3 TRP A 127      21.109  27.049 460.997  1.00 48.32      A    C  
ANISOU  844  CZ3 TRP A 127     6573   2567   9221    164   1856   -227  A    C  
ATOM    845  CH2 TRP A 127      22.420  26.789 461.416  1.00 49.62      A    C  
ANISOU  845  CH2 TRP A 127     6528   2682   9643    275   1935   -212  A    C  
ATOM    846  N   PHE A 128      17.652  24.791 458.805  1.00 44.64      A    N  
ANISOU  846  N   PHE A 128     7588   2811   6560    561    482   -752  A    N  
ATOM    847  CA  PHE A 128      17.139  24.997 460.162  1.00 42.33      A    C  
ANISOU  847  CA  PHE A 128     7035   2577   6474    451    304   -674  A    C  
ATOM    848  C   PHE A 128      16.365  23.787 460.678  1.00 47.00      A    C  
ANISOU  848  C   PHE A 128     7685   3075   7099    359     98   -743  A    C  
ATOM    849  O   PHE A 128      16.512  23.392 461.843  1.00 41.32      A    O  
ANISOU  849  O   PHE A 128     6799   2326   6573    331     49   -704  A    O  
ATOM    850  CB  PHE A 128      16.252  26.236 460.186  1.00 41.11      A    C  
ANISOU  850  CB  PHE A 128     6791   2562   6265    358    185   -583  A    C  
ATOM    851  CG  PHE A 128      17.003  27.493 459.986  1.00 43.69      A    C  
ANISOU  851  CG  PHE A 128     7008   2968   6624    425    369   -487  A    C  
ATOM    852  CD1 PHE A 128      17.313  27.932 458.712  1.00 48.39      A    C  
ANISOU  852  CD1 PHE A 128     7797   3568   7020    497    523   -486  A    C  
ATOM    853  CD2 PHE A 128      17.410  28.255 461.076  1.00 44.90      A    C  
ANISOU  853  CD2 PHE A 128     6879   3179   7001    410    390   -394  A    C  
ATOM    854  CE1 PHE A 128      18.037  29.097 458.533  1.00 42.43      A    C  
ANISOU  854  CE1 PHE A 128     6933   2869   6319    547    713   -379  A    C  
ATOM    855  CE2 PHE A 128      18.121  29.427 460.898  1.00 39.04      A    C  
ANISOU  855  CE2 PHE A 128     6025   2487   6319    457    550   -305  A    C  
ATOM    856  CZ  PHE A 128      18.435  29.842 459.627  1.00 40.68      A    C  
ANISOU  856  CZ  PHE A 128     6406   2695   6357    521    720   -291  A    C  
ATOM    857  N   GLU A 129      15.535  23.185 459.830  1.00 43.84      A    N  
ANISOU  857  N   GLU A 129     7530   2615   6512    306    -36   -842  A    N  
ATOM    858  CA  GLU A 129      14.791  22.013 460.261  1.00 44.23      A    C  
ANISOU  858  CA  GLU A 129     7635   2552   6617    203   -230   -906  A    C  
ATOM    859  C   GLU A 129      15.735  20.856 460.550  1.00 45.15      A    C  
ANISOU  859  C   GLU A 129     7805   2505   6844    300   -117   -971  A    C  
ATOM    860  O   GLU A 129      15.554  20.131 461.539  1.00 44.62      A    O  
ANISOU  860  O   GLU A 129     7647   2365   6944    237   -213   -946  A    O  
ATOM    861  CB  GLU A 129      13.750  21.634 459.210  1.00 46.02      A    C  
ANISOU  861  CB  GLU A 129     8118   2732   6634    121   -423  -1010  A    C  
ATOM    862  CG  GLU A 129      12.661  22.690 458.992  1.00 49.55      A    C  
ANISOU  862  CG  GLU A 129     8490   3325   7012     18   -593   -938  A    C  
ATOM    863  CD  GLU A 129      13.134  23.925 458.211  1.00 53.47      A    C  
ANISOU  863  CD  GLU A 129     9030   3937   7350    119   -447   -882  A    C  
ATOM    864  OE1 GLU A 129      14.338  24.029 457.897  1.00 60.27      A    O  
ANISOU  864  OE1 GLU A 129     9948   4778   8173    260   -186   -888  A    O  
ATOM    865  OE2 GLU A 129      12.293  24.804 457.924  1.00 62.14      A    O1-
ANISOU  865  OE2 GLU A 129    10093   5137   8381     56   -590   -821  A    O1-
ATOM    866  N   ILE A 130      16.754  20.682 459.702  1.00 46.75      A    N  
ANISOU  866  N   ILE A 130     8158   2644   6962    461    101  -1046  A    N  
ATOM    867  CA  ILE A 130      17.749  19.636 459.921  1.00 47.93      A    C  
ANISOU  867  CA  ILE A 130     8339   2628   7245    586    234  -1108  A    C  
ATOM    868  C   ILE A 130      18.504  19.880 461.223  1.00 46.26      A    C  
ANISOU  868  C   ILE A 130     7814   2451   7313    622    284   -982  A    C  
ATOM    869  O   ILE A 130      18.645  18.979 462.062  1.00 46.31      A    O  
ANISOU  869  O   ILE A 130     7773   2339   7483    618    207   -975  A    O  
ATOM    870  CB  ILE A 130      18.709  19.569 458.722  1.00 50.22      A    C  
ANISOU  870  CB  ILE A 130     8826   2858   7395    767    506  -1206  A    C  
ATOM    871  CG1 ILE A 130      17.940  19.181 457.473  1.00 52.30      A    C  
ANISOU  871  CG1 ILE A 130     9463   3062   7346    733    418  -1350  A    C  
ATOM    872  CG2 ILE A 130      19.832  18.604 458.995  1.00 51.54      A    C  
ANISOU  872  CG2 ILE A 130     8971   2859   7753    924    671  -1259  A    C  
ATOM    873  CD1 ILE A 130      18.771  19.175 456.254  1.00 54.83      A    C  
ANISOU  873  CD1 ILE A 130    10029   3335   7470    907    701  -1447  A    C  
ATOM    874  N   GLN A 131      18.968  21.116 461.429  1.00 44.96      A    N  
ANISOU  874  N   GLN A 131     7443   2437   7203    649    390   -875  A    N  
ATOM    875  CA  GLN A 131      19.656  21.444 462.674  1.00 45.86      A    C  
ANISOU  875  CA  GLN A 131     7269   2586   7570    672    396   -762  A    C  
ATOM    876  C   GLN A 131      18.795  21.108 463.877  1.00 42.18      A    C  
ANISOU  876  C   GLN A 131     6728   2123   7175    531    160   -703  A    C  
ATOM    877  O   GLN A 131      19.276  20.525 464.853  1.00 42.13      A    O  
ANISOU  877  O   GLN A 131     6628   2037   7342    561    115   -660  A    O  
ATOM    878  CB  GLN A 131      20.051  22.929 462.718  1.00 42.41      A    C  
ANISOU  878  CB  GLN A 131     6635   2309   7171    682    497   -662  A    C  
ATOM    879  CG  GLN A 131      21.217  23.346 461.803  1.00 52.48      A    C  
ANISOU  879  CG  GLN A 131     7902   3575   8463    832    787   -674  A    C  
ATOM    880  CD  GLN A 131      22.236  22.235 461.510  1.00 46.13      A    C  
ANISOU  880  CD  GLN A 131     7157   2604   7768    994    952   -758  A    C  
ATOM    881  NE2 GLN A 131      22.320  21.844 460.241  1.00 48.23      A    N  
ANISOU  881  NE2 GLN A 131     7681   2805   7839   1076   1123   -866  A    N  
ATOM    882  OE1 GLN A 131      22.949  21.770 462.395  1.00 46.17      A    O  
ANISOU  882  OE1 GLN A 131     6987   2534   8022   1053    926   -726  A    O  
ATOM    883  N   PHE A 132      17.518  21.484 463.821  1.00 41.29      A    N  
ANISOU  883  N   PHE A 132     6656   2099   6935    381     12   -690  A    N  
ATOM    884  CA  PHE A 132      16.610  21.299 464.948  1.00 46.59      A    C  
ANISOU  884  CA  PHE A 132     7240   2790   7671    238   -169   -620  A    C  
ATOM    885  C   PHE A 132      16.372  19.823 465.233  1.00 41.37      A    C  
ANISOU  885  C   PHE A 132     6713   1948   7060    202   -262   -665  A    C  
ATOM    886  O   PHE A 132      16.355  19.404 466.399  1.00 41.12      A    O  
ANISOU  886  O   PHE A 132     6593   1915   7115    158   -317   -577  A    O  
ATOM    887  CB  PHE A 132      15.296  22.045 464.682  1.00 39.38      A    C  
ANISOU  887  CB  PHE A 132     6318   2003   6642     99   -282   -601  A    C  
ATOM    888  CG  PHE A 132      14.581  22.472 465.923  1.00 37.93      A    C  
ANISOU  888  CG  PHE A 132     5959   1906   6545    -14   -378   -497  A    C  
ATOM    889  CD1 PHE A 132      15.265  23.093 466.947  1.00 36.76      A    C  
ANISOU  889  CD1 PHE A 132     5644   1821   6504     33   -325   -412  A    C  
ATOM    890  CD2 PHE A 132      13.222  22.265 466.059  1.00 38.03      A    C  
ANISOU  890  CD2 PHE A 132     5977   1933   6539   -168   -519   -488  A    C  
ATOM    891  CE1 PHE A 132      14.614  23.494 468.099  1.00 35.73      A    C  
ANISOU  891  CE1 PHE A 132     5392   1765   6418    -60   -393   -327  A    C  
ATOM    892  CE2 PHE A 132      12.539  22.672 467.205  1.00 38.25      A    C  
ANISOU  892  CE2 PHE A 132     5847   2041   6644   -263   -562   -391  A    C  
ATOM    893  CZ  PHE A 132      13.237  23.281 468.230  1.00 50.96      A    C  
ANISOU  893  CZ  PHE A 132     7331   3713   8319   -204   -491   -315  A    C  
ATOM    894  N   GLN A 133      16.128  19.028 464.188  1.00 43.11      A    N  
ANISOU  894  N   GLN A 133     7159   2048   7172    209   -275   -791  A    N  
ATOM    895  CA  GLN A 133      15.935  17.601 464.402  1.00 44.55      A    C  
ANISOU  895  CA  GLN A 133     7453   2088   7386    168   -333   -827  A    C  
ATOM    896  C   GLN A 133      17.172  16.975 465.019  1.00 56.97      A    C  
ANISOU  896  C   GLN A 133     8973   3593   9080    308   -215   -786  A    C  
ATOM    897  O   GLN A 133      17.070  16.158 465.948  1.00 61.49      A    O  
ANISOU  897  O   GLN A 133     9518   4130   9715    257   -274   -712  A    O  
ATOM    898  CB  GLN A 133      15.585  16.908 463.098  1.00 46.64      A    C  
ANISOU  898  CB  GLN A 133     7973   2241   7508    166   -360   -989  A    C  
ATOM    899  CG  GLN A 133      15.604  15.431 463.200  1.00 48.49      A    C  
ANISOU  899  CG  GLN A 133     8298   2334   7793    151   -376  -1037  A    C  
ATOM    900  CD  GLN A 133      14.732  14.792 462.157  1.00 64.48      A    C  
ANISOU  900  CD  GLN A 133    10537   4283   9678     60   -500  -1177  A    C  
ATOM    901  NE2 GLN A 133      15.198  13.676 461.588  1.00 62.58      A    N  
ANISOU  901  NE2 GLN A 133    10460   3890   9427    141   -446  -1298  A    N  
ATOM    902  OE1 GLN A 133      13.639  15.285 461.865  1.00 50.09      A    O  
ANISOU  902  OE1 GLN A 133     8729   2535   7769    -80   -659  -1178  A    O  
ATOM    903  N   ARG A 134      18.353  17.357 464.525  1.00 45.51      A    N  
ANISOU  903  N   ARG A 134     7507   2120   7665    490    -54   -824  A    N  
ATOM    904  CA  ARG A 134      19.582  16.789 465.056  1.00 46.37      A    C  
ANISOU  904  CA  ARG A 134     7548   2180   7893    639     21   -780  A    C  
ATOM    905  C   ARG A 134      19.765  17.160 466.529  1.00 44.87      A    C  
ANISOU  905  C   ARG A 134     7135   2107   7808    595    -68   -619  A    C  
ATOM    906  O   ARG A 134      20.116  16.308 467.356  1.00 45.61      A    O  
ANISOU  906  O   ARG A 134     7220   2139   7970    618   -122   -557  A    O  
ATOM    907  CB  ARG A 134      20.760  17.255 464.213  1.00 47.32      A    C  
ANISOU  907  CB  ARG A 134     7623   2300   8055    831    212   -843  A    C  
ATOM    908  CG  ARG A 134      22.110  16.921 464.816  1.00 78.83      A    C  
ANISOU  908  CG  ARG A 134    11447   6284  12221    983    275   -780  A    C  
ATOM    909  CD  ARG A 134      23.231  17.027 463.788  1.00 83.15      A    C  
ANISOU  909  CD  ARG A 134    11966   6807  12821   1170    515   -863  A    C  
ATOM    910  NE  ARG A 134      23.740  18.392 463.668  1.00 78.94      A    N  
ANISOU  910  NE  ARG A 134    11221   6417  12355   1190    659   -799  A    N  
ATOM    911  CZ  ARG A 134      24.369  19.029 464.650  1.00 73.52      A    C  
ANISOU  911  CZ  ARG A 134    10260   5831  11843   1189    612   -673  A    C  
ATOM    912  NH1 ARG A 134      24.544  18.422 465.816  1.00 72.89      A    N1+
ANISOU  912  NH1 ARG A 134    10108   5730  11858   1175    433   -598  A    N1+
ATOM    913  NH2 ARG A 134      24.812  20.271 464.474  1.00 74.16      A    N  
ANISOU  913  NH2 ARG A 134    10156   6023  11997   1196    738   -621  A    N  
ATOM    914  N   ALA A 135      19.515  18.427 466.879  1.00 43.00      A    N  
ANISOU  914  N   ALA A 135     6737   2024   7575    534    -90   -553  A    N  
ATOM    915  CA  ALA A 135      19.622  18.862 468.270  1.00 41.77      A    C  
ANISOU  915  CA  ALA A 135     6408   1973   7488    490   -183   -421  A    C  
ATOM    916  C   ALA A 135      18.669  18.093 469.174  1.00 41.73      A    C  
ANISOU  916  C   ALA A 135     6480   1939   7438    352   -314   -359  A    C  
ATOM    917  O   ALA A 135      19.049  17.661 470.269  1.00 42.05      A    O  
ANISOU  917  O   ALA A 135     6482   1960   7534    369   -379   -269  A    O  
ATOM    918  CB  ALA A 135      19.359  20.360 468.378  1.00 39.98      A    C  
ANISOU  918  CB  ALA A 135     6033   1900   7256    439   -177   -383  A    C  
ATOM    919  N   PHE A 136      17.414  17.926 468.741  1.00 41.71      A    N  
ANISOU  919  N   PHE A 136     6578   1926   7342    212   -358   -399  A    N  
ATOM    920  CA  PHE A 136      16.458  17.170 469.547  1.00 41.92      A    C  
ANISOU  920  CA  PHE A 136     6657   1919   7352     68   -454   -333  A    C  
ATOM    921  C   PHE A 136      16.882  15.729 469.733  1.00 43.79      A    C  
ANISOU  921  C   PHE A 136     7012   1995   7631    114   -458   -333  A    C  
ATOM    922  O   PHE A 136      16.754  15.177 470.832  1.00 44.18      A    O  
ANISOU  922  O   PHE A 136     7065   2011   7710     68   -515   -227  A    O  
ATOM    923  CB  PHE A 136      15.078  17.192 468.919  1.00 41.92      A    C  
ANISOU  923  CB  PHE A 136     6714   1930   7284    -90   -509   -384  A    C  
ATOM    924  CG  PHE A 136      14.224  18.274 469.424  1.00 42.73      A    C  
ANISOU  924  CG  PHE A 136     6686   2174   7375   -198   -550   -316  A    C  
ATOM    925  CD1 PHE A 136      14.689  19.578 469.467  1.00 38.93      A    C  
ANISOU  925  CD1 PHE A 136     6079   1811   6900   -128   -507   -300  A    C  
ATOM    926  CD2 PHE A 136      12.954  17.991 469.881  1.00 48.18      A    C  
ANISOU  926  CD2 PHE A 136     7366   2870   8070   -370   -617   -265  A    C  
ATOM    927  CE1 PHE A 136      13.896  20.581 469.954  1.00 37.71      A    C  
ANISOU  927  CE1 PHE A 136     5808   1775   6746   -218   -535   -244  A    C  
ATOM    928  CE2 PHE A 136      12.153  18.992 470.355  1.00 51.94      A    C  
ANISOU  928  CE2 PHE A 136     7712   3465   8556   -458   -632   -204  A    C  
ATOM    929  CZ  PHE A 136      12.626  20.294 470.390  1.00 48.74      A    C  
ANISOU  929  CZ  PHE A 136     7198   3174   8147   -377   -592   -198  A    C  
ATOM    930  N   GLN A 137      17.351  15.082 468.667  1.00 45.22      A    N  
ANISOU  930  N   GLN A 137     7312   2057   7811    206   -390   -451  A    N  
ATOM    931  CA  GLN A 137      17.769  13.696 468.829  1.00 54.48      A    C  
ANISOU  931  CA  GLN A 137     8598   3060   9041    260   -385   -455  A    C  
ATOM    932  C   GLN A 137      18.933  13.593 469.810  1.00 49.31      A    C  
ANISOU  932  C   GLN A 137     7852   2400   8486    395   -391   -352  A    C  
ATOM    933  O   GLN A 137      18.916  12.760 470.734  1.00 49.46      A    O  
ANISOU  933  O   GLN A 137     7906   2339   8549    371   -460   -260  A    O  
ATOM    934  CB  GLN A 137      18.083  13.087 467.457  1.00 49.94      A    C  
ANISOU  934  CB  GLN A 137     8180   2350   8445    347   -291   -619  A    C  
ATOM    935  CG  GLN A 137      16.814  12.453 466.832  1.00 68.04      A    C  
ANISOU  935  CG  GLN A 137    10603   4574  10676    179   -366   -705  A    C  
ATOM    936  CD  GLN A 137      16.810  12.393 465.296  1.00 80.27      A    C  
ANISOU  936  CD  GLN A 137    12295   6056  12150    228   -309   -896  A    C  
ATOM    937  NE2 GLN A 137      15.612  12.318 464.716  1.00 68.31      A    N  
ANISOU  937  NE2 GLN A 137    10859   4550  10547     69   -434   -966  A    N  
ATOM    938  OE1 GLN A 137      17.862  12.406 464.646  1.00 87.77      A    O  
ANISOU  938  OE1 GLN A 137    13285   6944  13120    409   -160   -979  A    O  
ATOM    939  N   LYS A 138      19.907  14.492 469.686  1.00 46.75      A    N  
ANISOU  939  N   LYS A 138     7393   2162   8208    526   -337   -356  A    N  
ATOM    940  CA  LYS A 138      21.080  14.400 470.543  1.00 49.36      A    C  
ANISOU  940  CA  LYS A 138     7606   2485   8662    658   -371   -271  A    C  
ATOM    941  C   LYS A 138      20.730  14.699 471.995  1.00 48.63      A    C  
ANISOU  941  C   LYS A 138     7446   2467   8563    564   -507   -128  A    C  
ATOM    942  O   LYS A 138      21.186  13.995 472.897  1.00 66.08      A    O  
ANISOU  942  O   LYS A 138     9674   4598  10835    609   -592    -40  A    O  
ATOM    943  CB  LYS A 138      22.166  15.329 470.013  1.00 48.74      A    C  
ANISOU  943  CB  LYS A 138     7364   2486   8669    801   -278   -311  A    C  
ATOM    944  CG  LYS A 138      22.724  14.828 468.681  1.00 48.78      A    C  
ANISOU  944  CG  LYS A 138     7465   2382   8688    938   -124   -445  A    C  
ATOM    945  CD  LYS A 138      23.945  15.597 468.216  1.00 80.37      A    C  
ANISOU  945  CD  LYS A 138    11273   6446  12817   1094      0   -469  A    C  
ATOM    946  CE  LYS A 138      24.486  15.016 466.909  1.00 81.75      A    C  
ANISOU  946  CE  LYS A 138    11564   6504  12994   1243    174   -607  A    C  
ATOM    947  NZ  LYS A 138      25.386  15.968 466.190  1.00 85.49      A    N1+
ANISOU  947  NZ  LYS A 138    11855   7065  13563   1353    362   -640  A    N1+
ATOM    948  N   LEU A 139      19.891  15.699 472.249  1.00 44.56      A    N  
ANISOU  948  N   LEU A 139     6878   2088   7966    437   -532   -102  A    N  
ATOM    949  CA  LEU A 139      19.493  15.950 473.631  1.00 44.03      A    C  
ANISOU  949  CA  LEU A 139     6791   2070   7867    352   -643     26  A    C  
ATOM    950  C   LEU A 139      18.658  14.805 474.187  1.00 46.49      A    C  
ANISOU  950  C   LEU A 139     7261   2267   8135    243   -686     93  A    C  
ATOM    951  O   LEU A 139      18.859  14.385 475.337  1.00 47.70      A    O  
ANISOU  951  O   LEU A 139     7459   2368   8298    249   -773    212  A    O  
ATOM    952  CB  LEU A 139      18.734  17.270 473.746  1.00 42.04      A    C  
ANISOU  952  CB  LEU A 139     6456   1974   7544    248   -637     31  A    C  
ATOM    953  CG  LEU A 139      19.585  18.471 473.354  1.00 41.06      A    C  
ANISOU  953  CG  LEU A 139     6164   1957   7479    345   -599    -13  A    C  
ATOM    954  CD1 LEU A 139      18.746  19.713 473.095  1.00 39.29      A    C  
ANISOU  954  CD1 LEU A 139     5875   1865   7187    249   -565    -36  A    C  
ATOM    955  CD2 LEU A 139      20.645  18.713 474.404  1.00 41.56      A    C  
ANISOU  955  CD2 LEU A 139     6132   2027   7631    438   -702     64  A    C  
ATOM    956  N   ARG A 140      17.732  14.272 473.382  1.00 45.47      A    N  
ANISOU  956  N   ARG A 140     7225   2087   7966    140   -634     23  A    N  
ATOM    957  CA  ARG A 140      16.946  13.125 473.821  1.00 46.91      A    C  
ANISOU  957  CA  ARG A 140     7539   2143   8139     26   -663     84  A    C  
ATOM    958  C   ARG A 140      17.831  11.934 474.197  1.00 48.98      A    C  
ANISOU  958  C   ARG A 140     7888   2242   8481    141   -694    128  A    C  
ATOM    959  O   ARG A 140      17.459  11.146 475.070  1.00 54.97      A    O  
ANISOU  959  O   ARG A 140     8739   2904   9242     73   -741    241  A    O  
ATOM    960  CB  ARG A 140      15.939  12.742 472.733  1.00 47.24      A    C  
ANISOU  960  CB  ARG A 140     7646   2146   8156    -94   -625    -24  A    C  
ATOM    961  CG  ARG A 140      14.580  13.446 472.856  1.00 46.10      A    C  
ANISOU  961  CG  ARG A 140     7445   2113   7959   -279   -637      2  A    C  
ATOM    962  CD  ARG A 140      13.553  13.054 471.769  1.00 46.80      A    C  
ANISOU  962  CD  ARG A 140     7581   2159   8041   -405   -646   -106  A    C  
ATOM    963  NE  ARG A 140      13.530  11.622 471.466  1.00 68.76      A    N  
ANISOU  963  NE  ARG A 140    10500   4753  10872   -421   -659   -143  A    N  
ATOM    964  CZ  ARG A 140      12.667  10.751 471.984  1.00 76.86      A    C  
ANISOU  964  CZ  ARG A 140    11577   5681  11944   -571   -687    -70  A    C  
ATOM    965  NH1 ARG A 140      11.730  11.153 472.841  1.00 81.18      A    N1+
ANISOU  965  NH1 ARG A 140    12051   6302  12494   -718   -686     50  A    N1+
ATOM    966  NH2 ARG A 140      12.739   9.473 471.636  1.00 84.67      A    N  
ANISOU  966  NH2 ARG A 140    12694   6488  12990   -573   -701   -117  A    N  
ATOM    967  N   ASN A 141      19.015  11.802 473.592  1.00 49.60      A    N  
ANISOU  967  N   ASN A 141     7933   2278   8634    320   -661     53  A    N  
ATOM    968  CA  ASN A 141      19.893  10.688 473.944  1.00 52.35      A    C  
ANISOU  968  CA  ASN A 141     8345   2464   9081    446   -695     95  A    C  
ATOM    969  C   ASN A 141      20.622  10.852 475.274  1.00 52.18      A    C  
ANISOU  969  C   ASN A 141     8265   2461   9100    519   -819    241  A    C  
ATOM    970  O   ASN A 141      21.152   9.867 475.789  1.00 88.67      A    O  
ANISOU  970  O   ASN A 141    12957   6941  13795    597   -881    312  A    O  
ATOM    971  CB  ASN A 141      20.910  10.448 472.829  1.00 76.15      A    C  
ANISOU  971  CB  ASN A 141    11344   5411  12177    624   -601    -35  A    C  
ATOM    972  CG  ASN A 141      20.340   9.615 471.704  1.00 87.14      A    C  
ANISOU  972  CG  ASN A 141    12893   6675  13542    579   -512   -165  A    C  
ATOM    973  ND2 ASN A 141      20.826   9.843 470.482  1.00 84.04      A    N  
ANISOU  973  ND2 ASN A 141    12511   6273  13147    687   -394   -309  A    N  
ATOM    974  OD1 ASN A 141      19.447   8.789 471.926  1.00 94.61      A    O  
ANISOU  974  OD1 ASN A 141    13956   7524  14469    444   -550   -137  A    O  
ATOM    975  N   CYS A 142      20.663  12.046 475.842  1.00 51.38      A    N  
ANISOU  975  N   CYS A 142     8049   2517   8954    498   -870    287  A    N  
ATOM    976  CA  CYS A 142      21.346  12.272 477.112  1.00 51.10      A    C  
ANISOU  976  CA  CYS A 142     7978   2496   8942    562  -1019    415  A    C  
ATOM    977  C   CYS A 142      20.609  11.663 478.305  1.00 52.13      A    C  
ANISOU  977  C   CYS A 142     8278   2550   8978    452  -1101    569  A    C  
ATOM    978  O   CYS A 142      19.449  11.985 478.565  1.00 60.01      A    O  
ANISOU  978  O   CYS A 142     9339   3600   9861    289  -1057    605  A    O  
ATOM    979  CB  CYS A 142      21.504  13.768 477.330  1.00 49.17      A    C  
ANISOU  979  CB  CYS A 142     7585   2429   8669    556  -1050    403  A    C  
ATOM    980  SG  CYS A 142      22.564  14.539 476.135  1.00 48.48      A    S  
ANISOU  980  SG  CYS A 142     7281   2421   8716    696   -958    263  A    S  
ATOM    981  N   LYS A 143      21.305  10.842 479.086  1.00 73.01      A    N  
ANISOU  981  N   LYS A 143    10994   5071  11675    544  -1220    674  A    N  
ATOM    982  CA  LYS A 143      20.705  10.240 480.271  1.00 66.70      A    C  
ANISOU  982  CA  LYS A 143    10382   4186  10774    452  -1295    843  A    C  
ATOM    983  C   LYS A 143      21.227  10.847 481.568  1.00 56.19      A    C  
ANISOU  983  C   LYS A 143     9076   2906   9368    499  -1479    968  A    C  
ATOM    984  O   LYS A 143      20.733  10.501 482.643  1.00 57.47      A    O  
ANISOU  984  O   LYS A 143     9425   3010   9402    424  -1540   1123  A    O  
ATOM    985  CB  LYS A 143      20.898   8.714 480.245  1.00 65.51      A    C  
ANISOU  985  CB  LYS A 143    10354   3827  10708    498  -1300    889  A    C  
ATOM    986  CG  LYS A 143      20.355   8.065 478.974  1.00 64.83      A    C  
ANISOU  986  CG  LYS A 143    10281   3668  10683    445  -1140    754  A    C  
ATOM    987  CD  LYS A 143      21.343   7.138 478.299  1.00 64.89      A    C  
ANISOU  987  CD  LYS A 143    10280   3529  10847    615  -1131    679  A    C  
ATOM    988  CE  LYS A 143      20.929   6.882 476.848  1.00 65.29      A    C  
ANISOU  988  CE  LYS A 143    10334   3547  10925    583   -973    499  A    C  
ATOM    989  NZ  LYS A 143      21.666   5.761 476.189  1.00 69.74      A    N1+
ANISOU  989  NZ  LYS A 143    10956   3920  11623    727   -933    426  A    N1+
ATOM    990  N   THR A 144      22.170  11.781 481.485  1.00 61.46      A    N  
ANISOU  990  N   THR A 144     9571   3678  10104    610  -1567    904  A    N  
ATOM    991  CA  THR A 144      22.868  12.352 482.629  1.00 56.21      A    C  
ANISOU  991  CA  THR A 144     8915   3048   9396    674  -1789    996  A    C  
ATOM    992  C   THR A 144      22.932  13.871 482.514  1.00 57.53      A    C  
ANISOU  992  C   THR A 144     8935   3385   9541    655  -1798    913  A    C  
ATOM    993  O   THR A 144      22.953  14.421 481.410  1.00 52.25      A    O  
ANISOU  993  O   THR A 144     8088   2801   8964    659  -1656    776  A    O  
ATOM    994  CB  THR A 144      24.281  11.777 482.725  1.00 58.43      A    C  
ANISOU  994  CB  THR A 144     9099   3241   9862    858  -1946   1008  A    C  
ATOM    995  CG2 THR A 144      25.155  12.552 483.700  1.00 82.86      A    C  
ANISOU  995  CG2 THR A 144    12139   6389  12955    930  -2207   1061  A    C  
ATOM    996  OG1 THR A 144      24.191  10.423 483.142  1.00 60.83      A    O  
ANISOU  996  OG1 THR A 144     9583   3374  10157    874  -1979   1119  A    O  
ATOM    997  N   HIS A 145      22.908  14.544 483.671  1.00 54.40      A    N  
ANISOU  997  N   HIS A 145     8643   3027   8999    629  -1964   1000  A    N  
ATOM    998  CA  HIS A 145      23.228  15.966 483.767  1.00 53.01      A    C  
ANISOU  998  CA  HIS A 145     8336   2980   8826    638  -2039    930  A    C  
ATOM    999  C   HIS A 145      24.461  16.365 482.943  1.00 52.78      A    C  
ANISOU  999  C   HIS A 145     8001   2996   9058    766  -2065    812  A    C  
ATOM   1000  O   HIS A 145      24.376  17.218 482.055  1.00 61.66      A    O  
ANISOU 1000  O   HIS A 145     8950   4225  10253    745  -1924    696  A    O  
ATOM   1001  CB  HIS A 145      23.415  16.309 485.253  1.00 54.64      A    C  
ANISOU 1001  CB  HIS A 145     8740   3167   8855    642  -2292   1047  A    C  
ATOM   1002  CG  HIS A 145      23.906  17.700 485.514  1.00 64.59      A    C  
ANISOU 1002  CG  HIS A 145     9888   4524  10128    666  -2434    976  A    C  
ATOM   1003  CD2 HIS A 145      25.150  18.172 485.772  1.00 55.02      A    C  
ANISOU 1003  CD2 HIS A 145     8516   3322   9069    771  -2672    941  A    C  
ATOM   1004  ND1 HIS A 145      23.068  18.798 485.543  1.00 59.32      A    N  
ANISOU 1004  ND1 HIS A 145     9267   3947   9325    566  -2338    929  A    N  
ATOM   1005  CE1 HIS A 145      23.775  19.884 485.798  1.00 51.95      A    C  
ANISOU 1005  CE1 HIS A 145     8221   3067   8451    614  -2510    864  A    C  
ATOM   1006  NE2 HIS A 145      25.041  19.534 485.940  1.00 57.25      A    N  
ANISOU 1006  NE2 HIS A 145     8756   3693   9303    730  -2719    871  A    N  
ATOM   1007  N   ASN A 146      25.606  15.726 483.192  1.00 58.67      A    N  
ANISOU 1007  N   ASN A 146     8677   3657   9959    897  -2228    848  A    N  
ATOM   1008  CA  ASN A 146      26.840  16.041 482.468  1.00 55.40      A    C  
ANISOU 1008  CA  ASN A 146     7957   3270   9822   1018  -2239    754  A    C  
ATOM   1009  C   ASN A 146      26.662  15.952 480.960  1.00 53.86      A    C  
ANISOU 1009  C   ASN A 146     7628   3108   9729   1025  -1943    632  A    C  
ATOM   1010  O   ASN A 146      27.033  16.863 480.215  1.00 52.66      A    O  
ANISOU 1010  O   ASN A 146     7263   3052   9694   1039  -1848    535  A    O  
ATOM   1011  CB  ASN A 146      27.958  15.094 482.909  1.00 58.50      A    C  
ANISOU 1011  CB  ASN A 146     8312   3537  10377   1156  -2427    822  A    C  
ATOM   1012  CG  ASN A 146      28.537  15.455 484.258  1.00 72.43      A    C  
ANISOU 1012  CG  ASN A 146    10132   5287  12101   1179  -2773    911  A    C  
ATOM   1013  ND2 ASN A 146      29.029  14.449 484.976  1.00 70.59      A    N  
ANISOU 1013  ND2 ASN A 146    10009   4927  11883   1257  -2960   1019  A    N  
ATOM   1014  OD1 ASN A 146      28.537  16.624 484.659  1.00 82.57      A    O  
ANISOU 1014  OD1 ASN A 146    11379   6662  13331   1127  -2884    881  A    O  
ATOM   1015  N   ASP A 147      26.157  14.824 480.486  1.00 58.77      A    N  
ANISOU 1015  N   ASP A 147     8383   3636  10310   1019  -1804    636  A    N  
ATOM   1016  CA  ASP A 147      26.016  14.635 479.051  1.00 57.19      A    C  
ANISOU 1016  CA  ASP A 147     8107   3444  10178   1035  -1549    514  A    C  
ATOM   1017  C   ASP A 147      25.113  15.694 478.454  1.00 50.54      A    C  
ANISOU 1017  C   ASP A 147     7243   2740   9219    914  -1401    436  A    C  
ATOM   1018  O   ASP A 147      25.347  16.164 477.334  1.00 57.93      A    O  
ANISOU 1018  O   ASP A 147     8040   3736  10235    946  -1240    328  A    O  
ATOM   1019  CB  ASP A 147      25.490  13.232 478.773  1.00 59.64      A    C  
ANISOU 1019  CB  ASP A 147     8611   3610  10440   1027  -1462    531  A    C  
ATOM   1020  CG  ASP A 147      26.365  12.182 479.399  1.00 76.15      A    C  
ANISOU 1020  CG  ASP A 147    10732   5553  12650   1153  -1613    619  A    C  
ATOM   1021  OD1 ASP A 147      27.527  12.027 478.949  1.00 84.38      A    O1-
ANISOU 1021  OD1 ASP A 147    11596   6558  13906   1307  -1613    572  A    O1-
ATOM   1022  OD2 ASP A 147      25.905  11.550 480.375  1.00 86.11      A    O1-
ANISOU 1022  OD2 ASP A 147    12191   6733  13796   1100  -1732    744  A    O1-
ATOM   1023  N   LEU A 148      24.058  16.071 479.175  1.00 52.31      A    N  
ANISOU 1023  N   LEU A 148     7615   3011   9252    777  -1442    494  A    N  
ATOM   1024  CA  LEU A 148      23.154  17.080 478.645  1.00 47.03      A    C  
ANISOU 1024  CA  LEU A 148     6918   2467   8484    663  -1310    425  A    C  
ATOM   1025  C   LEU A 148      23.838  18.437 478.551  1.00 52.44      A    C  
ANISOU 1025  C   LEU A 148     7394   3269   9262    702  -1345    373  A    C  
ATOM   1026  O   LEU A 148      23.768  19.093 477.511  1.00 67.84      A    O  
ANISOU 1026  O   LEU A 148     9224   5301  11253    695  -1189    279  A    O  
ATOM   1027  CB  LEU A 148      21.896  17.164 479.485  1.00 46.44      A    C  
ANISOU 1027  CB  LEU A 148     7037   2401   8208    515  -1332    506  A    C  
ATOM   1028  CG  LEU A 148      20.941  18.177 478.871  1.00 56.33      A    C  
ANISOU 1028  CG  LEU A 148     8240   3777   9386    404  -1192    430  A    C  
ATOM   1029  CD1 LEU A 148      19.598  17.561 478.686  1.00 51.25      A    C  
ANISOU 1029  CD1 LEU A 148     7742   3098   8633    265  -1081    449  A    C  
ATOM   1030  CD2 LEU A 148      20.824  19.405 479.742  1.00 43.44      A    C  
ANISOU 1030  CD2 LEU A 148     6596   2227   7681    367  -1287    460  A    C  
ATOM   1031  N   ILE A 149      24.514  18.883 479.611  1.00 47.04      A    N  
ANISOU 1031  N   ILE A 149     6672   2585   8615    742  -1559    435  A    N  
ATOM   1032  CA  ILE A 149      25.102  20.219 479.537  1.00 46.30      A    C  
ANISOU 1032  CA  ILE A 149     6377   2590   8626    757  -1601    381  A    C  
ATOM   1033  C   ILE A 149      26.225  20.271 478.496  1.00 46.89      A    C  
ANISOU 1033  C   ILE A 149     6196   2671   8949    866  -1499    309  A    C  
ATOM   1034  O   ILE A 149      26.374  21.272 477.777  1.00 45.76      A    O  
ANISOU 1034  O   ILE A 149     5888   2616   8881    851  -1382    239  A    O  
ATOM   1035  CB  ILE A 149      25.578  20.696 480.919  1.00 47.52      A    C  
ANISOU 1035  CB  ILE A 149     6567   2725   8762    768  -1889    450  A    C  
ATOM   1036  CG1 ILE A 149      26.766  19.865 481.425  1.00 52.09      A    C  
ANISOU 1036  CG1 ILE A 149     7093   3201   9497    889  -2089    509  A    C  
ATOM   1037  CG2 ILE A 149      24.407  20.708 481.894  1.00 47.12      A    C  
ANISOU 1037  CG2 ILE A 149     6806   2663   8436    662  -1944    523  A    C  
ATOM   1038  CD1 ILE A 149      27.431  20.432 482.667  1.00 51.79      A    C  
ANISOU 1038  CD1 ILE A 149     7062   3145   9471    909  -2417    558  A    C  
ATOM   1039  N   ASN A 150      27.004  19.195 478.352  1.00 48.85      A    N  
ANISOU 1039  N   ASN A 150     6414   2817   9330    976  -1517    328  A    N  
ATOM   1040  CA  ASN A 150      28.034  19.221 477.316  1.00 49.70      A    C  
ANISOU 1040  CA  ASN A 150     6289   2920   9674   1084  -1378    260  A    C  
ATOM   1041  C   ASN A 150      27.430  19.148 475.913  1.00 48.38      A    C  
ANISOU 1041  C   ASN A 150     6165   2781   9434   1066  -1087    169  A    C  
ATOM   1042  O   ASN A 150      27.844  19.895 475.014  1.00 47.97      A    O  
ANISOU 1042  O   ASN A 150     5946   2792   9491   1090   -930    106  A    O  
ATOM   1043  CB  ASN A 150      29.019  18.078 477.525  1.00 62.72      A    C  
ANISOU 1043  CB  ASN A 150     7896   4442  11493   1219  -1465    300  A    C  
ATOM   1044  CG  ASN A 150      29.819  18.235 478.793  1.00 68.69      A    C  
ANISOU 1044  CG  ASN A 150     8573   5167  12359   1251  -1778    382  A    C  
ATOM   1045  ND2 ASN A 150      29.866  17.171 479.599  1.00 65.80      A    N  
ANISOU 1045  ND2 ASN A 150     8366   4689  11944   1294  -1945    468  A    N  
ATOM   1046  OD1 ASN A 150      30.385  19.301 479.057  1.00 70.71      A    O  
ANISOU 1046  OD1 ASN A 150     8638   5487  12740   1233  -1884    370  A    O  
ATOM   1047  N   THR A 151      26.438  18.271 475.705  1.00 47.92      A    N  
ANISOU 1047  N   THR A 151     6343   2670   9195   1016  -1018    164  A    N  
ATOM   1048  CA  THR A 151      25.773  18.219 474.408  1.00 46.87      A    C  
ANISOU 1048  CA  THR A 151     6285   2553   8971    986   -789     70  A    C  
ATOM   1049  C   THR A 151      25.192  19.576 474.045  1.00 58.63      A    C  
ANISOU 1049  C   THR A 151     7711   4181  10383    889   -716     33  A    C  
ATOM   1050  O   THR A 151      25.338  20.035 472.904  1.00 54.21      A    O  
ANISOU 1050  O   THR A 151     7082   3658   9856    918   -536    -42  A    O  
ATOM   1051  CB  THR A 151      24.661  17.169 474.401  1.00 46.79      A    C  
ANISOU 1051  CB  THR A 151     6533   2460   8784    908   -776     75  A    C  
ATOM   1052  CG2 THR A 151      23.946  17.158 473.056  1.00 45.95      A    C  
ANISOU 1052  CG2 THR A 151     6517   2361   8581    867   -585    -34  A    C  
ATOM   1053  OG1 THR A 151      25.192  15.865 474.644  1.00 48.98      A    O  
ANISOU 1053  OG1 THR A 151     6883   2588   9138   1003   -826    107  A    O  
ATOM   1054  N   LEU A 152      24.567  20.253 475.016  1.00 43.52      A    N  
ANISOU 1054  N   LEU A 152     5829   2337   8369    784   -848     89  A    N  
ATOM   1055  CA  LEU A 152      23.950  21.543 474.738  1.00 41.61      A    C  
ANISOU 1055  CA  LEU A 152     5537   2218   8057    694   -785     56  A    C  
ATOM   1056  C   LEU A 152      24.988  22.593 474.386  1.00 43.33      A    C  
ANISOU 1056  C   LEU A 152     5514   2493   8458    755   -746     32  A    C  
ATOM   1057  O   LEU A 152      24.794  23.367 473.438  1.00 44.88      A    O  
ANISOU 1057  O   LEU A 152     5650   2753   8648    734   -587    -19  A    O  
ATOM   1058  CB  LEU A 152      23.115  22.012 475.924  1.00 64.32      A    C  
ANISOU 1058  CB  LEU A 152     8510   5135  10795    585   -926    117  A    C  
ATOM   1059  CG  LEU A 152      22.527  23.421 475.720  1.00 38.97      A    C  
ANISOU 1059  CG  LEU A 152     5234   2042   7531    504   -870     82  A    C  
ATOM   1060  CD1 LEU A 152      21.505  23.449 474.592  1.00 37.80      A    C  
ANISOU 1060  CD1 LEU A 152     5150   1933   7279    438   -697     24  A    C  
ATOM   1061  CD2 LEU A 152      21.944  23.972 476.999  1.00 38.58      A    C  
ANISOU 1061  CD2 LEU A 152     5271   2014   7374    427  -1012    134  A    C  
ATOM   1062  N   THR A 153      26.091  22.650 475.135  1.00 49.71      A    N  
ANISOU 1062  N   THR A 153     6177   3269   9442    824   -897     75  A    N  
ATOM   1063  CA  THR A 153      27.129  23.611 474.776  1.00 46.76      A    C  
ANISOU 1063  CA  THR A 153     5542   2934   9292    867   -856     56  A    C  
ATOM   1064  C   THR A 153      27.651  23.361 473.359  1.00 44.47      A    C  
ANISOU 1064  C   THR A 153     5163   2623   9111    952   -595      2  A    C  
ATOM   1065  O   THR A 153      27.786  24.303 472.560  1.00 43.96      A    O  
ANISOU 1065  O   THR A 153     4983   2616   9105    936   -434    -26  A    O  
ATOM   1066  CB  THR A 153      28.256  23.581 475.809  1.00 52.21      A    C  
ANISOU 1066  CB  THR A 153     6080   3571  10184    923  -1094    108  A    C  
ATOM   1067  CG2 THR A 153      29.273  24.610 475.493  1.00 65.57      A    C  
ANISOU 1067  CG2 THR A 153     7484   5292  12138    940  -1064     94  A    C  
ATOM   1068  OG1 THR A 153      27.726  23.881 477.104  1.00 46.44      A    O  
ANISOU 1068  OG1 THR A 153     5482   2849   9314    850  -1335    152  A    O  
ATOM   1069  N   ARG A 154      27.897  22.095 473.007  1.00 48.78      A    N  
ANISOU 1069  N   ARG A 154     5790   3074   9668   1043   -538    -13  A    N  
ATOM   1070  CA  ARG A 154      28.418  21.799 471.671  1.00 62.84      A    C  
ANISOU 1070  CA  ARG A 154     7523   4818  11537   1142   -279    -75  A    C  
ATOM   1071  C   ARG A 154      27.408  22.172 470.575  1.00 45.37      A    C  
ANISOU 1071  C   ARG A 154     5468   2650   9121   1081    -87   -140  A    C  
ATOM   1072  O   ARG A 154      27.765  22.818 469.584  1.00 45.65      A    O  
ANISOU 1072  O   ARG A 154     5411   2713   9222   1113    123   -172  A    O  
ATOM   1073  CB  ARG A 154      28.829  20.319 471.603  1.00 48.93      A    C  
ANISOU 1073  CB  ARG A 154     5848   2927   9816   1258   -277    -88  A    C  
ATOM   1074  CG  ARG A 154      28.958  19.716 470.198  1.00 59.78      A    C  
ANISOU 1074  CG  ARG A 154     7306   4235  11172   1357     -9   -179  A    C  
ATOM   1075  CD  ARG A 154      29.490  18.270 470.199  1.00 64.12      A    C  
ANISOU 1075  CD  ARG A 154     7929   4641  11794   1489    -17   -196  A    C  
ATOM   1076  NE  ARG A 154      28.796  17.360 471.126  1.00 75.95      A    N  
ANISOU 1076  NE  ARG A 154     9627   6072  13160   1437   -227   -150  A    N  
ATOM   1077  CZ  ARG A 154      27.576  16.843 470.934  1.00 74.70      A    C  
ANISOU 1077  CZ  ARG A 154     9740   5879  12763   1347   -228   -183  A    C  
ATOM   1078  NH1 ARG A 154      26.865  17.146 469.845  1.00 71.86      A    N1+
ANISOU 1078  NH1 ARG A 154     9502   5547  12254   1301    -65   -272  A    N1+
ATOM   1079  NH2 ARG A 154      27.060  16.018 471.839  1.00 66.84      A    N  
ANISOU 1079  NH2 ARG A 154     8894   4814  11687   1295   -398   -120  A    N  
ATOM   1080  N   LEU A 155      26.132  21.796 470.756  1.00 70.03      A    N  
ANISOU 1080  N   LEU A 155     8826   5776  12006    986   -158   -151  A    N  
ATOM   1081  CA  LEU A 155      25.082  22.126 469.785  1.00 45.42      A    C  
ANISOU 1081  CA  LEU A 155     5862   2692   8703    916    -28   -212  A    C  
ATOM   1082  C   LEU A 155      24.936  23.632 469.605  1.00 41.31      A    C  
ANISOU 1082  C   LEU A 155     5218   2285   8193    851     22   -195  A    C  
ATOM   1083  O   LEU A 155      24.803  24.122 468.479  1.00 41.25      A    O  
ANISOU 1083  O   LEU A 155     5235   2289   8147    863    206   -238  A    O  
ATOM   1084  CB  LEU A 155      23.744  21.536 470.221  1.00 41.59      A    C  
ANISOU 1084  CB  LEU A 155     5596   2192   8013    800   -151   -209  A    C  
ATOM   1085  CG  LEU A 155      23.450  20.056 470.070  1.00 42.75      A    C  
ANISOU 1085  CG  LEU A 155     5941   2211   8093    823   -167   -242  A    C  
ATOM   1086  CD1 LEU A 155      22.199  19.760 470.846  1.00 41.71      A    C  
ANISOU 1086  CD1 LEU A 155     5946   2088   7814    676   -305   -198  A    C  
ATOM   1087  CD2 LEU A 155      23.296  19.623 468.628  1.00 43.61      A    C  
ANISOU 1087  CD2 LEU A 155     6192   2244   8134    874      3   -354  A    C  
ATOM   1088  N   ILE A 156      24.878  24.378 470.713  1.00 40.37      A    N  
ANISOU 1088  N   ILE A 156     4997   2236   8106    779   -144   -134  A    N  
ATOM   1089  CA  ILE A 156      24.747  25.825 470.610  1.00 39.26      A    C  
ANISOU 1089  CA  ILE A 156     4744   2187   7986    717   -110   -119  A    C  
ATOM   1090  C   ILE A 156      25.916  26.400 469.821  1.00 47.98      A    C  
ANISOU 1090  C   ILE A 156     5649   3280   9301    799     68   -119  A    C  
ATOM   1091  O   ILE A 156      25.738  27.310 469.004  1.00 40.09      A    O  
ANISOU 1091  O   ILE A 156     4628   2317   8286    776    222   -123  A    O  
ATOM   1092  CB  ILE A 156      24.606  26.459 472.004  1.00 42.01      A    C  
ANISOU 1092  CB  ILE A 156     5035   2586   8342    643   -329    -70  A    C  
ATOM   1093  CG1 ILE A 156      23.312  25.965 472.678  1.00 37.42      A    C  
ANISOU 1093  CG1 ILE A 156     4662   2015   7542    555   -441    -62  A    C  
ATOM   1094  CG2 ILE A 156      24.662  28.002 471.929  1.00 37.75      A    C  
ANISOU 1094  CG2 ILE A 156     4359   2119   7864    591   -301    -61  A    C  
ATOM   1095  CD1 ILE A 156      22.016  26.287 471.916  1.00 36.06      A    C  
ANISOU 1095  CD1 ILE A 156     4611   1891   7198    471   -341    -96  A    C  
ATOM   1096  N   GLN A 157      27.129  25.867 470.035  1.00 61.87      A    N  
ANISOU 1096  N   GLN A 157     7256   4980  11274    896     62   -103  A    N  
ATOM   1097  CA  GLN A 157      28.273  26.301 469.229  1.00 44.09      A    C  
ANISOU 1097  CA  GLN A 157     4794   2706   9253    974    272    -97  A    C  
ATOM   1098  C   GLN A 157      28.123  25.938 467.754  1.00 44.78      A    C  
ANISOU 1098  C   GLN A 157     5018   2756   9242   1045    568   -153  A    C  
ATOM   1099  O   GLN A 157      28.442  26.747 466.873  1.00 49.75      A    O  
ANISOU 1099  O   GLN A 157     5569   3397   9936   1058    794   -141  A    O  
ATOM   1100  CB  GLN A 157      29.560  25.691 469.750  1.00 46.32      A    C  
ANISOU 1100  CB  GLN A 157     4875   2924   9800   1065    200    -71  A    C  
ATOM   1101  CG  GLN A 157      30.669  25.887 468.757  1.00 48.49      A    C  
ANISOU 1101  CG  GLN A 157     4952   3163  10310   1154    477    -69  A    C  
ATOM   1102  CD  GLN A 157      32.001  25.794 469.375  1.00 60.32      A    C  
ANISOU 1102  CD  GLN A 157     6157   4614  12146   1203    381    -24  A    C  
ATOM   1103  NE2 GLN A 157      32.475  24.570 469.572  1.00 60.22      A    N  
ANISOU 1103  NE2 GLN A 157     6161   4527  12192   1308    332    -38  A    N  
ATOM   1104  OE1 GLN A 157      32.621  26.811 469.684  1.00 73.34      A    O  
ANISOU 1104  OE1 GLN A 157     7562   6280  14022   1144    337     24  A    O  
ATOM   1105  N   GLU A 158      27.681  24.715 467.461  1.00 45.10      A    N  
ANISOU 1105  N   GLU A 158     5276   2733   9129   1095    574   -214  A    N  
ATOM   1106  CA  GLU A 158      27.531  24.294 466.072  1.00 46.12      A    C  
ANISOU 1106  CA  GLU A 158     5579   2805   9138   1170    834   -290  A    C  
ATOM   1107  C   GLU A 158      26.495  25.160 465.345  1.00 58.09      A    C  
ANISOU 1107  C   GLU A 158     7250   4369  10450   1085    917   -305  A    C  
ATOM   1108  O   GLU A 158      26.650  25.465 464.157  1.00 54.17      A    O  
ANISOU 1108  O   GLU A 158     6826   3849   9905   1142   1182   -332  A    O  
ATOM   1109  CB  GLU A 158      27.174  22.800 466.037  1.00 52.24      A    C  
ANISOU 1109  CB  GLU A 158     6576   3485   9789   1222    768   -362  A    C  
ATOM   1110  CG  GLU A 158      28.380  21.885 466.390  1.00 58.45      A    C  
ANISOU 1110  CG  GLU A 158     7222   4194  10793   1352    765   -354  A    C  
ATOM   1111  CD  GLU A 158      28.031  20.407 466.730  1.00 63.99      A    C  
ANISOU 1111  CD  GLU A 158     8124   4787  11402   1389    627   -397  A    C  
ATOM   1112  OE1 GLU A 158      26.843  20.053 466.876  1.00 58.26      A    O  
ANISOU 1112  OE1 GLU A 158     7627   4048  10460   1291    502   -422  A    O  
ATOM   1113  OE2 GLU A 158      28.971  19.588 466.872  1.00 76.70      A    O1-
ANISOU 1113  OE2 GLU A 158     9651   6315  13177   1513    642   -398  A    O1-
ATOM   1114  N   ILE A 159      25.436  25.567 466.046  1.00 42.44      A    N  
ANISOU 1114  N   ILE A 159     5331   2449   8344    955    704   -281  A    N  
ATOM   1115  CA  ILE A 159      24.392  26.391 465.444  1.00 41.14      A    C  
ANISOU 1115  CA  ILE A 159     5298   2324   8007    871    744   -288  A    C  
ATOM   1116  C   ILE A 159      24.810  27.853 465.349  1.00 40.85      A    C  
ANISOU 1116  C   ILE A 159     5079   2352   8092    846    837   -213  A    C  
ATOM   1117  O   ILE A 159      24.691  28.481 464.295  1.00 41.29      A    O  
ANISOU 1117  O   ILE A 159     5212   2452   8024    845   1019   -204  A    O  
ATOM   1118  CB  ILE A 159      23.088  26.235 466.241  1.00 39.26      A    C  
ANISOU 1118  CB  ILE A 159     5173   2128   7618    742    494   -289  A    C  
ATOM   1119  CG1 ILE A 159      22.665  24.771 466.229  1.00 39.86      A    C  
ANISOU 1119  CG1 ILE A 159     5439   2117   7591    754    422   -355  A    C  
ATOM   1120  CG2 ILE A 159      22.015  27.110 465.671  1.00 38.15      A    C  
ANISOU 1120  CG2 ILE A 159     5133   2095   7265    643    495   -282  A    C  
ATOM   1121  CD1 ILE A 159      21.356  24.500 466.902  1.00 38.49      A    C  
ANISOU 1121  CD1 ILE A 159     5373   1967   7283    620    217   -349  A    C  
ATOM   1122  N   SER A 160      25.252  28.439 466.456  1.00 40.27      A    N  
ANISOU 1122  N   SER A 160     4787   2334   8180    799    680   -152  A    N  
ATOM   1123  CA  SER A 160      25.499  29.877 466.482  1.00 47.12      A    C  
ANISOU 1123  CA  SER A 160     5493   3249   9163    748    722    -87  A    C  
ATOM   1124  C   SER A 160      26.802  30.255 465.794  1.00 59.92      A    C  
ANISOU 1124  C   SER A 160     6925   4822  11020    830    973    -47  A    C  
ATOM   1125  O   SER A 160      26.958  31.404 465.360  1.00 54.68      A    O  
ANISOU 1125  O   SER A 160     6180   4167  10427    798   1100     12  A    O  
ATOM   1126  CB  SER A 160      25.512  30.387 467.915  1.00 38.92      A    C  
ANISOU 1126  CB  SER A 160     4314   2268   8207    666    457    -55  A    C  
ATOM   1127  OG  SER A 160      26.703  29.969 468.544  1.00 48.04      A    O  
ANISOU 1127  OG  SER A 160     5276   3386   9591    721    393    -41  A    O  
ATOM   1128  N   GLY A 161      27.754  29.332 465.733  1.00 43.79      A    N  
ANISOU 1128  N   GLY A 161     4796   2726   9115    930   1049    -67  A    N  
ATOM   1129  CA  GLY A 161      29.022  29.608 465.117  1.00 46.15      A    C  
ANISOU 1129  CA  GLY A 161     4885   2981   9668   1008   1308    -26  A    C  
ATOM   1130  C   GLY A 161      29.991  30.373 465.977  1.00 46.82      A    C  
ANISOU 1130  C   GLY A 161     4633   3073  10084    958   1192     45  A    C  
ATOM   1131  O   GLY A 161      31.051  30.766 465.480  1.00 48.97      A    O  
ANISOU 1131  O   GLY A 161     4687   3304  10617    996   1414     97  A    O  
ATOM   1132  N   TYR A 162      29.679  30.560 467.255  1.00 45.38      A    N  
ANISOU 1132  N   TYR A 162     4407   2929   9904    874    856     45  A    N  
ATOM   1133  CA  TYR A 162      30.500  31.380 468.131  1.00 48.75      A    C  
ANISOU 1133  CA  TYR A 162     4549   3347  10628    812    696     95  A    C  
ATOM   1134  C   TYR A 162      31.746  30.635 468.577  1.00 51.77      A    C  
ANISOU 1134  C   TYR A 162     4709   3671  11292    882    633    103  A    C  
ATOM   1135  O   TYR A 162      31.725  29.420 468.793  1.00 48.67      A    O  
ANISOU 1135  O   TYR A 162     4420   3262  10812    957    563     64  A    O  
ATOM   1136  CB  TYR A 162      29.714  31.814 469.363  1.00 51.02      A    C  
ANISOU 1136  CB  TYR A 162     4914   3685  10784    710    360     79  A    C  
ATOM   1137  CG  TYR A 162      28.900  33.031 469.122  1.00 42.58      A    C  
ANISOU 1137  CG  TYR A 162     3924   2659   9596    619    393     94  A    C  
ATOM   1138  CD1 TYR A 162      27.785  32.968 468.316  1.00 58.35      A    C  
ANISOU 1138  CD1 TYR A 162     6171   4695  11303    616    526     76  A    C  
ATOM   1139  CD2 TYR A 162      29.251  34.253 469.673  1.00 42.82      A    C  
ANISOU 1139  CD2 TYR A 162     3780   2674   9815    535    280    125  A    C  
ATOM   1140  CE1 TYR A 162      27.013  34.081 468.080  1.00 59.60      A    C  
ANISOU 1140  CE1 TYR A 162     6403   4888  11354    538    545     99  A    C  
ATOM   1141  CE2 TYR A 162      28.490  35.381 469.429  1.00 52.47      A    C  
ANISOU 1141  CE2 TYR A 162     5086   3926  10924    457    315    141  A    C  
ATOM   1142  CZ  TYR A 162      27.362  35.273 468.631  1.00 40.18      A    C  
ANISOU 1142  CZ  TYR A 162     3778   2420   9069    462    450    132  A    C  
ATOM   1143  OH  TYR A 162      26.567  36.337 468.357  1.00 53.41      A    O  
ANISOU 1143  OH  TYR A 162     5542   4124  10626    393    474    155  A    O  
ATOM   1144  N   ASP A 163      32.830  31.396 468.752  1.00 55.62      A    N  
ANISOU 1144  N   ASP A 163     4884   4112  12139    847    640    159  A    N  
ATOM   1145  CA  ASP A 163      34.122  30.803 469.083  1.00 60.59      A    C  
ANISOU 1145  CA  ASP A 163     5260   4672  13091    905    593    177  A    C  
ATOM   1146  C   ASP A 163      34.122  30.140 470.458  1.00 65.59      A    C  
ANISOU 1146  C   ASP A 163     5918   5297  13706    904    191    149  A    C  
ATOM   1147  O   ASP A 163      34.868  29.175 470.671  1.00 66.92      A    O  
ANISOU 1147  O   ASP A 163     5999   5413  14015    990    142    149  A    O  
ATOM   1148  CB  ASP A 163      35.215  31.864 469.000  1.00 60.53      A    C  
ANISOU 1148  CB  ASP A 163     4908   4600  13492    836    665    248  A    C  
ATOM   1149  CG  ASP A 163      35.600  32.179 467.568  1.00 74.65      A    C  
ANISOU 1149  CG  ASP A 163     6637   6363  15363    876   1128    299  A    C  
ATOM   1150  OD1 ASP A 163      35.401  31.302 466.693  1.00 72.65      A    O  
ANISOU 1150  OD1 ASP A 163     6558   6125  14920    991   1382    268  A    O  
ATOM   1151  OD2 ASP A 163      36.106  33.299 467.321  1.00 79.47      A    O1-
ANISOU 1151  OD2 ASP A 163     7044   6927  16224    793   1242    372  A    O1-
ATOM   1152  N   ARG A 164      33.320  30.639 471.405  1.00 50.67      A    N  
ANISOU 1152  N   ARG A 164     4157   3450  11646    815    -91    131  A    N  
ATOM   1153  CA  ARG A 164      33.272  30.046 472.736  1.00 50.65      A    C  
ANISOU 1153  CA  ARG A 164     4221   3432  11592    817   -462    115  A    C  
ATOM   1154  C   ARG A 164      31.857  30.067 473.284  1.00 57.18      A    C  
ANISOU 1154  C   ARG A 164     5365   4329  12032    765   -600     82  A    C  
ATOM   1155  O   ARG A 164      31.167  31.086 473.197  1.00 53.42      A    O  
ANISOU 1155  O   ARG A 164     4953   3901  11445    681   -573     73  A    O  
ATOM   1156  CB  ARG A 164      34.193  30.782 473.699  1.00 53.82      A    C  
ANISOU 1156  CB  ARG A 164     4372   3768  12311    752   -747    136  A    C  
ATOM   1157  CG  ARG A 164      34.077  30.329 475.127  1.00 52.55      A    C  
ANISOU 1157  CG  ARG A 164     4324   3583  12060    750  -1156    122  A    C  
ATOM   1158  CD  ARG A 164      35.202  30.942 475.874  1.00 67.60      A    C  
ANISOU 1158  CD  ARG A 164     5962   5397  14328    700  -1423    136  A    C  
ATOM   1159  NE  ARG A 164      35.091  32.391 475.807  1.00 82.56      A    N  
ANISOU 1159  NE  ARG A 164     7764   7287  16319    586  -1421    124  A    N  
ATOM   1160  CZ  ARG A 164      36.041  33.226 476.224  1.00 89.38      A    C  
ANISOU 1160  CZ  ARG A 164     8372   8049  17538    509  -1602    131  A    C  
ATOM   1161  NH1 ARG A 164      37.178  32.725 476.719  1.00 75.82      A    N1+
ANISOU 1161  NH1 ARG A 164     6469   6234  16106    536  -1798    150  A    N1+
ATOM   1162  NH2 ARG A 164      35.860  34.552 476.133  1.00 77.22      A    N  
ANISOU 1162  NH2 ARG A 164     6771   6488  16081    405  -1593    119  A    N  
ATOM   1163  N   VAL A 165      31.451  28.957 473.901  1.00 48.47      A    N  
ANISOU 1163  N   VAL A 165     4455   3219  10742    812   -750     72  A    N  
ATOM   1164  CA  VAL A 165      30.107  28.800 474.451  1.00 50.46      A    C  
ANISOU 1164  CA  VAL A 165     5011   3523  10638    761   -857     53  A    C  
ATOM   1165  C   VAL A 165      30.234  28.149 475.820  1.00 54.67      A    C  
ANISOU 1165  C   VAL A 165     5629   4007  11138    778  -1186     74  A    C  
ATOM   1166  O   VAL A 165      30.943  27.149 475.972  1.00 47.90      A    O  
ANISOU 1166  O   VAL A 165     4719   3084  10397    864  -1246     98  A    O  
ATOM   1167  CB  VAL A 165      29.197  27.964 473.526  1.00 44.02      A    C  
ANISOU 1167  CB  VAL A 165     4417   2736   9571    793   -626     29  A    C  
ATOM   1168  CG1 VAL A 165      27.900  27.617 474.211  1.00 42.27      A    C  
ANISOU 1168  CG1 VAL A 165     4477   2547   9035    733   -751     23  A    C  
ATOM   1169  CG2 VAL A 165      28.922  28.713 472.226  1.00 43.22      A    C  
ANISOU 1169  CG2 VAL A 165     4292   2680   9449    772   -333     11  A    C  
ATOM   1170  N   MET A 166      29.546  28.716 476.810  1.00 45.14      A    N  
ANISOU 1170  N   MET A 166     4569   2819   9763    704  -1394     69  A    N  
ATOM   1171  CA  MET A 166      29.644  28.308 478.199  1.00 46.20      A    C  
ANISOU 1171  CA  MET A 166     4820   2894   9838    714  -1727     96  A    C  
ATOM   1172  C   MET A 166      28.250  28.233 478.798  1.00 44.42      A    C  
ANISOU 1172  C   MET A 166     4919   2704   9254    655  -1762     95  A    C  
ATOM   1173  O   MET A 166      27.319  28.886 478.327  1.00 52.72      A    O  
ANISOU 1173  O   MET A 166     6045   3828  10158    587  -1592     61  A    O  
ATOM   1174  CB  MET A 166      30.499  29.298 478.991  1.00 61.35      A    C  
ANISOU 1174  CB  MET A 166     6567   4763  11978    682  -2002     85  A    C  
ATOM   1175  CG  MET A 166      31.966  29.252 478.646  1.00 61.41      A    C  
ANISOU 1175  CG  MET A 166     6237   4711  12385    728  -2022    100  A    C  
ATOM   1176  SD  MET A 166      32.693  30.902 478.672  1.00 75.40      A    S  
ANISOU 1176  SD  MET A 166     7728   6450  14469    636  -2113     68  A    S  
ATOM   1177  CE  MET A 166      32.359  31.410 480.344  1.00 79.42      A    C  
ANISOU 1177  CE  MET A 166     8457   6905  14813    590  -2576     38  A    C  
ATOM   1178  N   ILE A 167      28.102  27.403 479.822  1.00 45.32      A    N  
ANISOU 1178  N   ILE A 167     5226   2758   9234    681  -1972    141  A    N  
ATOM   1179  CA  ILE A 167      26.899  27.369 480.646  1.00 44.32      A    C  
ANISOU 1179  CA  ILE A 167     5413   2636   8792    621  -2037    157  A    C  
ATOM   1180  C   ILE A 167      27.262  27.825 482.048  1.00 47.47      A    C  
ANISOU 1180  C   ILE A 167     5914   2964   9160    620  -2392    171  A    C  
ATOM   1181  O   ILE A 167      28.147  27.240 482.691  1.00 48.15      A    O  
ANISOU 1181  O   ILE A 167     5977   2972   9345    685  -2637    218  A    O  
ATOM   1182  CB  ILE A 167      26.242  25.979 480.657  1.00 44.20      A    C  
ANISOU 1182  CB  ILE A 167     5606   2592   8598    638  -1958    215  A    C  
ATOM   1183  CG1 ILE A 167      25.655  25.683 479.282  1.00 42.56      A    C  
ANISOU 1183  CG1 ILE A 167     5354   2445   8369    621  -1632    178  A    C  
ATOM   1184  CG2 ILE A 167      25.193  25.873 481.741  1.00 44.01      A    C  
ANISOU 1184  CG2 ILE A 167     5900   2538   8283    577  -2062    261  A    C  
ATOM   1185  CD1 ILE A 167      24.775  24.447 479.223  1.00 53.89      A    C  
ANISOU 1185  CD1 ILE A 167     7008   3846   9624    605  -1544    219  A    C  
ATOM   1186  N   TYR A 168      26.602  28.884 482.509  1.00 45.11      A    N  
ANISOU 1186  N   TYR A 168     5738   2682   8722    550  -2430    124  A    N  
ATOM   1187  CA  TYR A 168      26.762  29.363 483.873  1.00 46.74      A    C  
ANISOU 1187  CA  TYR A 168     6119   2858   8782    532  -2739    113  A    C  
ATOM   1188  C   TYR A 168      25.631  28.809 484.712  1.00 46.59      A    C  
ANISOU 1188  C   TYR A 168     6470   2879   8353    492  -2706    158  A    C  
ATOM   1189  O   TYR A 168      24.464  28.941 484.331  1.00 59.22      A    O  
ANISOU 1189  O   TYR A 168     8158   4575   9766    424  -2431    140  A    O  
ATOM   1190  CB  TYR A 168      26.675  30.876 484.004  1.00 59.43      A    C  
ANISOU 1190  CB  TYR A 168     7673   4524  10383    457  -2756     11  A    C  
ATOM   1191  CG  TYR A 168      27.485  31.717 483.096  1.00 59.72      A    C  
ANISOU 1191  CG  TYR A 168     7362   4543  10786    454  -2702    -36  A    C  
ATOM   1192  CD1 TYR A 168      28.828  31.483 482.903  1.00 58.64      A    C  
ANISOU 1192  CD1 TYR A 168     6952   4304  11023    521  -2866     -6  A    C  
ATOM   1193  CD2 TYR A 168      26.897  32.803 482.457  1.00 62.77      A    C  
ANISOU 1193  CD2 TYR A 168     7685   5010  11153    381  -2481   -102  A    C  
ATOM   1194  CE1 TYR A 168      29.568  32.304 482.060  1.00 75.42      A    C  
ANISOU 1194  CE1 TYR A 168     8742   6444  13472    493  -2762    -40  A    C  
ATOM   1195  CE2 TYR A 168      27.615  33.617 481.614  1.00 65.84      A    C  
ANISOU 1195  CE2 TYR A 168     7773   5374  11870    367  -2408   -127  A    C  
ATOM   1196  CZ  TYR A 168      28.955  33.374 481.418  1.00 77.27      A    C  
ANISOU 1196  CZ  TYR A 168     8945   6739  13674    418  -2537    -94  A    C  
ATOM   1197  OH  TYR A 168      29.674  34.204 480.582  1.00 80.66      A    O  
ANISOU 1197  OH  TYR A 168     9063   7169  14417    385  -2421   -107  A    O  
ATOM   1198  N   GLN A 169      25.963  28.189 485.838  1.00 48.80      A    N  
ANISOU 1198  N   GLN A 169     6962   3079   8501    534  -2982    227  A    N  
ATOM   1199  CA  GLN A 169      24.938  27.800 486.787  1.00 49.19      A    C  
ANISOU 1199  CA  GLN A 169     7391   3161   8139    490  -2949    279  A    C  
ATOM   1200  C   GLN A 169      25.010  28.721 487.993  1.00 50.87      A    C  
ANISOU 1200  C   GLN A 169     7815   3386   8128    466  -3182    219  A    C  
ATOM   1201  O   GLN A 169      26.080  28.883 488.592  1.00 70.45      A    O  
ANISOU 1201  O   GLN A 169    10272   5776  10720    518  -3542    213  A    O  
ATOM   1202  CB  GLN A 169      25.069  26.346 487.221  1.00 50.71      A    C  
ANISOU 1202  CB  GLN A 169     7757   3247   8266    549  -3054    419  A    C  
ATOM   1203  CG  GLN A 169      23.877  25.925 488.030  1.00 51.02      A    C  
ANISOU 1203  CG  GLN A 169     8169   3324   7892    483  -2929    490  A    C  
ATOM   1204  CD  GLN A 169      24.043  24.581 488.629  1.00 70.06      A    C  
ANISOU 1204  CD  GLN A 169    10797   5610  10213    534  -3066    644  A    C  
ATOM   1205  NE2 GLN A 169      23.025  24.146 489.351  1.00 81.27      A    N  
ANISOU 1205  NE2 GLN A 169    12547   7049  11282    471  -2937    730  A    N  
ATOM   1206  OE1 GLN A 169      25.070  23.921 488.449  1.00 71.56      A    O  
ANISOU 1206  OE1 GLN A 169    10854   5677  10659    633  -3275    696  A    O  
ATOM   1207  N   PHE A 170      23.867  29.318 488.338  1.00 50.15      A    N  
ANISOU 1207  N   PHE A 170     7926   3396   7732    392  -2980    169  A    N  
ATOM   1208  CA  PHE A 170      23.761  30.183 489.502  1.00 51.78      A    C  
ANISOU 1208  CA  PHE A 170     8395   3614   7664    373  -3148     95  A    C  
ATOM   1209  C   PHE A 170      23.573  29.344 490.751  1.00 61.72      A    C  
ANISOU 1209  C   PHE A 170    10062   4822   8568    398  -3295    202  A    C  
ATOM   1210  O   PHE A 170      22.864  28.335 490.731  1.00 53.93      A    O  
ANISOU 1210  O   PHE A 170     9206   3843   7442    385  -3098    321  A    O  
ATOM   1211  CB  PHE A 170      22.590  31.149 489.366  1.00 50.20      A    C  
ANISOU 1211  CB  PHE A 170     8250   3533   7291    303  -2840     -3  A    C  
ATOM   1212  CG  PHE A 170      22.806  32.223 488.348  1.00 48.35      A    C  
ANISOU 1212  CG  PHE A 170     7681   3334   7355    279  -2748   -113  A    C  
ATOM   1213  CD1 PHE A 170      23.769  33.187 488.536  1.00 49.48      A    C  
ANISOU 1213  CD1 PHE A 170     7713   3417   7672    287  -3014   -212  A    C  
ATOM   1214  CD2 PHE A 170      22.025  32.282 487.207  1.00 55.85      A    C  
ANISOU 1214  CD2 PHE A 170     8441   4368   8412    242  -2406   -113  A    C  
ATOM   1215  CE1 PHE A 170      23.966  34.184 487.597  1.00 48.00      A    C  
ANISOU 1215  CE1 PHE A 170     7228   3247   7765    256  -2912   -295  A    C  
ATOM   1216  CE2 PHE A 170      22.220  33.276 486.264  1.00 44.27      A    C  
ANISOU 1216  CE2 PHE A 170     6697   2926   7197    223  -2320   -196  A    C  
ATOM   1217  CZ  PHE A 170      23.191  34.226 486.463  1.00 45.39      A    C  
ANISOU 1217  CZ  PHE A 170     6731   3002   7514    229  -2558   -280  A    C  
ATOM   1218  N   ASP A 171      24.181  29.792 491.841  1.00 62.94      A    N  
ANISOU 1218  N   ASP A 171    10432   4917   8564    427  -3643    160  A    N  
ATOM   1219  CA  ASP A 171      24.027  29.219 493.168  1.00 64.54      A    C  
ANISOU 1219  CA  ASP A 171    11093   5071   8359    453  -3815    249  A    C  
ATOM   1220  C   ASP A 171      22.983  30.007 493.944  1.00 74.89      A    C  
ANISOU 1220  C   ASP A 171    12741   6467   9246    404  -3622    164  A    C  
ATOM   1221  O   ASP A 171      22.502  31.045 493.475  1.00 73.36      A    O  
ANISOU 1221  O   ASP A 171    12400   6355   9118    360  -3412     26  A    O  
ATOM   1222  CB  ASP A 171      25.385  29.210 493.887  1.00 63.03      A    C  
ANISOU 1222  CB  ASP A 171    10950   4749   8249    525  -4358    252  A    C  
ATOM   1223  CG  ASP A 171      25.723  30.541 494.560  1.00 75.77      A    C  
ANISOU 1223  CG  ASP A 171    12675   6356   9756    506  -4607     78  A    C  
ATOM   1224  OD1 ASP A 171      25.098  31.572 494.248  1.00 74.47      A    O1-
ANISOU 1224  OD1 ASP A 171    12450   6278   9565    447  -4361    -60  A    O1-
ATOM   1225  OD2 ASP A 171      26.639  30.552 495.411  1.00 79.09      A    O1-
ANISOU 1225  OD2 ASP A 171    13248   6670  10131    553  -5078     77  A    O1-
ATOM   1226  N   PRO A 172      22.584  29.540 495.139  1.00 80.05      A    N  
ANISOU 1226  N   PRO A 172    13864   7098   9453    418  -3666    247  A    N  
ATOM   1227  CA  PRO A 172      21.463  30.206 495.831  1.00 72.35      A    C  
ANISOU 1227  CA  PRO A 172    13214   6209   8067    381  -3389    172  A    C  
ATOM   1228  C   PRO A 172      21.675  31.688 496.080  1.00 64.38      A    C  
ANISOU 1228  C   PRO A 172    12215   5214   7033    380  -3510    -49  A    C  
ATOM   1229  O   PRO A 172      20.692  32.428 496.192  1.00 79.39      A    O  
ANISOU 1229  O   PRO A 172    14217   7198   8749    352  -3191   -147  A    O  
ATOM   1230  CB  PRO A 172      21.357  29.424 497.146  1.00 67.50      A    C  
ANISOU 1230  CB  PRO A 172    13126   5534   6988    413  -3513    310  A    C  
ATOM   1231  CG  PRO A 172      21.845  28.091 496.810  1.00 67.40      A    C  
ANISOU 1231  CG  PRO A 172    13003   5438   7167    438  -3632    502  A    C  
ATOM   1232  CD  PRO A 172      22.964  28.296 495.832  1.00 65.67      A    C  
ANISOU 1232  CD  PRO A 172    12305   5174   7473    468  -3885    434  A    C  
ATOM   1233  N   GLU A 173      22.922  32.142 496.188  1.00 80.67      A    N  
ANISOU 1233  N   GLU A 173    14171   7183   9295    411  -3965   -130  A    N  
ATOM   1234  CA  GLU A 173      23.247  33.549 496.399  1.00 73.14      A    C  
ANISOU 1234  CA  GLU A 173    13210   6210   8369    399  -4132   -344  A    C  
ATOM   1235  C   GLU A 173      23.487  34.304 495.095  1.00 63.23      A    C  
ANISOU 1235  C   GLU A 173    11430   4981   7611    358  -4019   -437  A    C  
ATOM   1236  O   GLU A 173      23.940  35.449 495.135  1.00 63.83      A    O  
ANISOU 1236  O   GLU A 173    11432   5012   7810    340  -4197   -602  A    O  
ATOM   1237  CB  GLU A 173      24.465  33.680 497.325  1.00 70.06      A    C  
ANISOU 1237  CB  GLU A 173    13014   5686   7921    440  -4727   -386  A    C  
ATOM   1238  CG  GLU A 173      24.223  33.174 498.746  1.00 83.97      A    C  
ANISOU 1238  CG  GLU A 173    15385   7411   9108    484  -4873   -321  A    C  
ATOM   1239  CD  GLU A 173      25.362  33.508 499.694  1.00 97.01      A    C  
ANISOU 1239  CD  GLU A 173    17263   8926  10668    521  -5499   -397  A    C  
ATOM   1240  OE1 GLU A 173      26.350  34.129 499.247  1.00100.46      A    O  
ANISOU 1240  OE1 GLU A 173    17347   9293  11532    503  -5818   -500  A    O  
ATOM   1241  OE2 GLU A 173      25.265  33.147 500.888  1.00111.69      A    O1-
ANISOU 1241  OE2 GLU A 173    19660  10744  12032    563  -5676   -349  A    O1-
ATOM   1242  N   TRP A 174      23.250  33.670 493.944  1.00 72.36      A    N  
ANISOU 1242  N   TRP A 174    12241   6195   9056    343  -3748   -330  A    N  
ATOM   1243  CA  TRP A 174      23.374  34.263 492.606  1.00 68.23      A    C  
ANISOU 1243  CA  TRP A 174    11250   5708   8969    308  -3582   -388  A    C  
ATOM   1244  C   TRP A 174      24.817  34.438 492.154  1.00 67.98      A    C  
ANISOU 1244  C   TRP A 174    10882   5575   9373    320  -3933   -405  A    C  
ATOM   1245  O   TRP A 174      25.087  35.193 491.222  1.00 56.06      A    O  
ANISOU 1245  O   TRP A 174     9026   4070   8205    287  -3851   -474  A    O  
ATOM   1246  CB  TRP A 174      22.614  35.586 492.501  1.00 72.85      A    C  
ANISOU 1246  CB  TRP A 174    11847   6348   9483    270  -3357   -548  A    C  
ATOM   1247  CG  TRP A 174      21.171  35.316 492.604  1.00 65.82      A    C  
ANISOU 1247  CG  TRP A 174    11144   5566   8297    261  -2936   -508  A    C  
ATOM   1248  CD1 TRP A 174      20.357  35.570 493.670  1.00 57.31      A    C  
ANISOU 1248  CD1 TRP A 174    10474   4514   6787    274  -2821   -558  A    C  
ATOM   1249  CD2 TRP A 174      20.370  34.656 491.627  1.00 52.68      A    C  
ANISOU 1249  CD2 TRP A 174     9270   3992   6754    235  -2574   -401  A    C  
ATOM   1250  CE2 TRP A 174      19.067  34.570 492.146  1.00 53.06      A    C  
ANISOU 1250  CE2 TRP A 174     9573   4117   6470    225  -2252   -386  A    C  
ATOM   1251  CE3 TRP A 174      20.624  34.145 490.356  1.00 50.22      A    C  
ANISOU 1251  CE3 TRP A 174     8588   3697   6798    221  -2488   -324  A    C  
ATOM   1252  NE1 TRP A 174      19.085  35.135 493.398  1.00 55.92      A    N  
ANISOU 1252  NE1 TRP A 174    10313   4441   6493    255  -2387   -481  A    N  
ATOM   1253  CZ2 TRP A 174      18.018  33.986 491.435  1.00 51.07      A    C  
ANISOU 1253  CZ2 TRP A 174     9185   3952   6266    189  -1882   -292  A    C  
ATOM   1254  CZ3 TRP A 174      19.582  33.574 489.648  1.00 59.61      A    C  
ANISOU 1254  CZ3 TRP A 174     9685   4972   7992    189  -2132   -244  A    C  
ATOM   1255  CH2 TRP A 174      18.296  33.493 490.191  1.00 48.66      A    C  
ANISOU 1255  CH2 TRP A 174     8529   3656   6304    168  -1850   -226  A    C  
ATOM   1256  N   ASN A 175      25.746  33.728 492.783  1.00 72.75      A    N  
ANISOU 1256  N   ASN A 175    11573   6081   9988    370  -4316   -329  A    N  
ATOM   1257  CA  ASN A 175      27.049  33.521 492.182  1.00 66.93      A    C  
ANISOU 1257  CA  ASN A 175    10445   5254   9732    396  -4577   -293  A    C  
ATOM   1258  C   ASN A 175      26.914  32.536 491.026  1.00 57.97      A    C  
ANISOU 1258  C   ASN A 175     9027   4161   8838    421  -4280   -164  A    C  
ATOM   1259  O   ASN A 175      25.962  31.753 490.951  1.00 56.70      A    O  
ANISOU 1259  O   ASN A 175     9034   4068   8443    422  -3995    -76  A    O  
ATOM   1260  CB  ASN A 175      28.027  32.969 493.216  1.00 64.20      A    C  
ANISOU 1260  CB  ASN A 175    10277   4784   9334    457  -5088   -237  A    C  
ATOM   1261  CG  ASN A 175      28.289  33.933 494.338  1.00 72.43      A    C  
ANISOU 1261  CG  ASN A 175    11607   5763  10148    434  -5444   -379  A    C  
ATOM   1262  ND2 ASN A 175      28.058  33.483 495.561  1.00 75.79      A    N  
ANISOU 1262  ND2 ASN A 175    12523   6163  10112    472  -5639   -340  A    N  
ATOM   1263  OD1 ASN A 175      28.669  35.082 494.114  1.00 76.48      A    O  
ANISOU 1263  OD1 ASN A 175    11933   6245  10882    379  -5537   -525  A    O  
ATOM   1264  N   GLY A 176      27.897  32.544 490.132  1.00 57.55      A    N  
ANISOU 1264  N   GLY A 176     8548   4054   9265    440  -4350   -153  A    N  
ATOM   1265  CA  GLY A 176      27.856  31.703 488.951  1.00 59.10      A    C  
ANISOU 1265  CA  GLY A 176     8475   4277   9705    472  -4066    -58  A    C  
ATOM   1266  C   GLY A 176      29.095  30.835 488.833  1.00 63.93      A    C  
ANISOU 1266  C   GLY A 176     8866   4768  10658    563  -4329     35  A    C  
ATOM   1267  O   GLY A 176      30.193  31.230 489.234  1.00 66.42      A    O  
ANISOU 1267  O   GLY A 176     9040   4985  11212    584  -4702      4  A    O  
ATOM   1268  N   ARG A 177      28.909  29.650 488.250  1.00 56.18      A    N  
ANISOU 1268  N   ARG A 177     7840   3782   9724    620  -4135    145  A    N  
ATOM   1269  CA  ARG A 177      30.004  28.741 487.935  1.00 62.60      A    C  
ANISOU 1269  CA  ARG A 177     8409   4475  10899    727  -4302    234  A    C  
ATOM   1270  C   ARG A 177      29.910  28.327 486.478  1.00 55.35      A    C  
ANISOU 1270  C   ARG A 177     7194   3632  10206    729  -3881    237  A    C  
ATOM   1271  O   ARG A 177      28.827  27.959 486.012  1.00 53.09      A    O  
ANISOU 1271  O   ARG A 177     7054   3400   9718    705  -3571    258  A    O  
ATOM   1272  CB  ARG A 177      29.964  27.498 488.835  1.00 72.63      A    C  
ANISOU 1272  CB  ARG A 177     9981   5688  11925    787  -4485    355  A    C  
ATOM   1273  CG  ARG A 177      31.200  26.628 488.715  1.00 82.93      A    C  
ANISOU 1273  CG  ARG A 177    11025   6953  13529    847  -4624    397  A    C  
ATOM   1274  CD  ARG A 177      31.252  25.527 489.767  1.00 84.41      A    C  
ANISOU 1274  CD  ARG A 177    11531   7072  13468    899  -4858    511  A    C  
ATOM   1275  NE  ARG A 177      30.422  24.367 489.484  1.00 79.72      A    N  
ANISOU 1275  NE  ARG A 177    11112   6491  12686    919  -4577    613  A    N  
ATOM   1276  CZ  ARG A 177      30.686  23.158 489.969  1.00 82.65      A    C  
ANISOU 1276  CZ  ARG A 177    11619   6796  12989    976  -4686    722  A    C  
ATOM   1277  NH1 ARG A 177      31.745  22.984 490.748  1.00 89.68      A    N1+
ANISOU 1277  NH1 ARG A 177    12489   7610  13976   1022  -5065    740  A    N1+
ATOM   1278  NH2 ARG A 177      29.903  22.130 489.684  1.00 76.63      A    N  
ANISOU 1278  NH2 ARG A 177    11009   6030  12076    981  -4424    811  A    N  
ATOM   1279  N   VAL A 178      31.036  28.362 485.766  1.00 56.21      A    N  
ANISOU 1279  N   VAL A 178     6902   3743  10713    749  -3862    214  A    N  
ATOM   1280  CA  VAL A 178      31.082  27.826 484.406  1.00 64.65      A    C  
ANISOU 1280  CA  VAL A 178     7729   4879  11957    769  -3473    221  A    C  
ATOM   1281  C   VAL A 178      31.228  26.311 484.517  1.00 60.14      A    C  
ANISOU 1281  C   VAL A 178     7249   4270  11331    849  -3471    309  A    C  
ATOM   1282  O   VAL A 178      32.270  25.806 484.933  1.00 58.48      A    O  
ANISOU 1282  O   VAL A 178     6924   3987  11308    906  -3704    342  A    O  
ATOM   1283  CB  VAL A 178      32.224  28.437 483.587  1.00 55.52      A    C  
ANISOU 1283  CB  VAL A 178     6138   3722  11235    761  -3409    175  A    C  
ATOM   1284  CG1 VAL A 178      32.276  27.818 482.208  1.00 54.34      A    C  
ANISOU 1284  CG1 VAL A 178     5804   3630  11212    799  -3004    186  A    C  
ATOM   1285  CG2 VAL A 178      32.044  29.911 483.481  1.00 54.57      A    C  
ANISOU 1285  CG2 VAL A 178     5941   3621  11174    676  -3406     98  A    C  
ATOM   1286  N   ILE A 179      30.192  25.586 484.106  1.00 55.19      A    N  
ANISOU 1286  N   ILE A 179     6816   3682  10471    847  -3205    342  A    N  
ATOM   1287  CA  ILE A 179      30.101  24.149 484.334  1.00 58.67      A    C  
ANISOU 1287  CA  ILE A 179     7417   4067  10806    910  -3209    430  A    C  
ATOM   1288  C   ILE A 179      30.218  23.330 483.054  1.00 64.83      A    C  
ANISOU 1288  C   ILE A 179     8028   4867  11739    960  -2883    420  A    C  
ATOM   1289  O   ILE A 179      30.340  22.097 483.128  1.00 55.29      A    O  
ANISOU 1289  O   ILE A 179     6904   3591  10513   1026  -2885    483  A    O  
ATOM   1290  CB  ILE A 179      28.800  23.808 485.081  1.00 53.99      A    C  
ANISOU 1290  CB  ILE A 179     7240   3465   9807    859  -3206    493  A    C  
ATOM   1291  CG1 ILE A 179      27.601  24.268 484.243  1.00 50.86      A    C  
ANISOU 1291  CG1 ILE A 179     6883   3158   9284    775  -2859    439  A    C  
ATOM   1292  CG2 ILE A 179      28.839  24.441 486.462  1.00 55.59      A    C  
ANISOU 1292  CG2 ILE A 179     7672   3622   9827    840  -3563    513  A    C  
ATOM   1293  CD1 ILE A 179      26.267  23.865 484.785  1.00 50.07      A    C  
ANISOU 1293  CD1 ILE A 179     7144   3044   8836    709  -2780    503  A    C  
ATOM   1294  N   ALA A 180      30.201  23.971 481.897  1.00 69.96      A    N  
ANISOU 1294  N   ALA A 180     8466   5593  12523    935  -2610    344  A    N  
ATOM   1295  CA  ALA A 180      30.390  23.333 480.611  1.00 52.00      A    C  
ANISOU 1295  CA  ALA A 180     6048   3330  10378    990  -2302    319  A    C  
ATOM   1296  C   ALA A 180      30.862  24.414 479.653  1.00 61.51      A    C  
ANISOU 1296  C   ALA A 180     6967   4602  11804    966  -2123    248  A    C  
ATOM   1297  O   ALA A 180      30.601  25.604 479.853  1.00 50.28      A    O  
ANISOU 1297  O   ALA A 180     5518   3230  10355    885  -2170    215  A    O  
ATOM   1298  CB  ALA A 180      29.109  22.676 480.101  1.00 49.99      A    C  
ANISOU 1298  CB  ALA A 180     6038   3101   9855    954  -2062    319  A    C  
ATOM   1299  N   GLU A 181      31.606  23.988 478.645  1.00 53.73      A    N  
ANISOU 1299  N   GLU A 181     5775   3598  11040   1042  -1919    230  A    N  
ATOM   1300  CA  GLU A 181      32.258  24.910 477.736  1.00 52.34      A    C  
ANISOU 1300  CA  GLU A 181     5312   3462  11113   1029  -1737    187  A    C  
ATOM   1301  C   GLU A 181      32.553  24.146 476.460  1.00 60.01      A    C  
ANISOU 1301  C   GLU A 181     6213   4417  12172   1121  -1415    166  A    C  
ATOM   1302  O   GLU A 181      32.764  22.933 476.489  1.00 65.31      A    O  
ANISOU 1302  O   GLU A 181     6956   5016  12841   1215  -1423    186  A    O  
ATOM   1303  CB  GLU A 181      33.540  25.463 478.360  1.00 54.89      A    C  
ANISOU 1303  CB  GLU A 181     5357   3728  11771   1031  -1987    204  A    C  
ATOM   1304  CG  GLU A 181      34.369  26.374 477.503  1.00 55.66      A    C  
ANISOU 1304  CG  GLU A 181     5124   3835  12187   1007  -1805    180  A    C  
ATOM   1305  CD  GLU A 181      35.742  26.624 478.120  1.00 83.47      A    C  
ANISOU 1305  CD  GLU A 181     8358   7267  16088   1011  -2062    202  A    C  
ATOM   1306  OE1 GLU A 181      36.286  25.691 478.770  1.00 84.84      A    O  
ANISOU 1306  OE1 GLU A 181     8542   7365  16329   1087  -2274    237  A    O  
ATOM   1307  OE2 GLU A 181      36.280  27.747 477.952  1.00 89.94      A    O1-
ANISOU 1307  OE2 GLU A 181     8945   8078  17151    932  -2058    188  A    O1-
ATOM   1308  N   SER A 182      32.569  24.864 475.343  1.00 57.68      A    N  
ANISOU 1308  N   SER A 182     5796   4176  11943   1099  -1131    127  A    N  
ATOM   1309  CA  SER A 182      32.919  24.275 474.054  1.00 52.87      A    C  
ANISOU 1309  CA  SER A 182     5130   3544  11412   1193   -806     99  A    C  
ATOM   1310  C   SER A 182      33.604  25.410 473.310  1.00 53.47      A    C  
ANISOU 1310  C   SER A 182     4935   3650  11733   1161   -616     95  A    C  
ATOM   1311  O   SER A 182      32.945  26.360 472.874  1.00 51.58      A    O  
ANISOU 1311  O   SER A 182     4744   3481  11373   1077   -497     79  A    O  
ATOM   1312  CB  SER A 182      31.680  23.751 473.324  1.00 50.80      A    C  
ANISOU 1312  CB  SER A 182     5170   3312  10818   1187   -612     55  A    C  
ATOM   1313  OG  SER A 182      31.980  23.052 472.138  1.00 51.92      A    O  
ANISOU 1313  OG  SER A 182     5319   3409  10998   1292   -329     12  A    O  
ATOM   1314  N   VAL A 183      34.928  25.322 473.201  1.00 56.36      A    N  
ANISOU 1314  N   VAL A 183     5009   3949  12455   1224   -593    120  A    N  
ATOM   1315  CA  VAL A 183      35.762  26.474 472.880  1.00 64.51      A    C  
ANISOU 1315  CA  VAL A 183     5735   4980  13798   1164   -502    143  A    C  
ATOM   1316  C   VAL A 183      36.877  26.051 471.937  1.00 72.30      A    C  
ANISOU 1316  C   VAL A 183     6494   5902  15073   1268   -216    154  A    C  
ATOM   1317  O   VAL A 183      37.617  25.107 472.235  1.00101.49      A    O  
ANISOU 1317  O   VAL A 183    10107   9524  18932   1368   -303    164  A    O  
ATOM   1318  CB  VAL A 183      36.346  27.143 474.143  1.00 64.21      A    C  
ANISOU 1318  CB  VAL A 183     5521   4902  13972   1081   -886    172  A    C  
ATOM   1319  CG1 VAL A 183      37.118  26.151 475.008  1.00 65.68      A    C  
ANISOU 1319  CG1 VAL A 183     5645   5001  14310   1162  -1158    197  A    C  
ATOM   1320  CG2 VAL A 183      37.226  28.323 473.768  1.00 62.34      A    C  
ANISOU 1320  CG2 VAL A 183     4961   4634  14090   1003   -787    198  A    C  
ATOM   1321  N   ARG A 184      36.938  26.670 470.765  1.00 70.31      A    N  
ANISOU 1321  N   ARG A 184     6178   5675  14862   1258    146    154  A    N  
ATOM   1322  CA  ARG A 184      38.110  26.516 469.914  1.00 70.94      A    C  
ANISOU 1322  CA  ARG A 184     6006   5688  15258   1338    440    179  A    C  
ATOM   1323  C   ARG A 184      39.298  27.163 470.624  1.00 83.32      A    C  
ANISOU 1323  C   ARG A 184     7209   7185  17265   1268    243    239  A    C  
ATOM   1324  O   ARG A 184      39.136  28.152 471.343  1.00 88.15      A    O  
ANISOU 1324  O   ARG A 184     7763   7808  17921   1135      3    256  A    O  
ATOM   1325  CB  ARG A 184      37.831  27.182 468.579  1.00 63.32      A    C  
ANISOU 1325  CB  ARG A 184     5090   4764  14207   1324    862    181  A    C  
ATOM   1326  CG  ARG A 184      36.450  26.778 468.109  1.00 60.36      A    C  
ANISOU 1326  CG  ARG A 184     5108   4457  13370   1348    941    115  A    C  
ATOM   1327  CD  ARG A 184      35.958  27.556 466.931  1.00 62.71      A    C  
ANISOU 1327  CD  ARG A 184     5511   4798  13520   1319   1286    119  A    C  
ATOM   1328  NE  ARG A 184      34.621  27.100 466.582  1.00 71.68      A    N  
ANISOU 1328  NE  ARG A 184     7029   5980  14225   1335   1297     48  A    N  
ATOM   1329  CZ  ARG A 184      33.906  27.598 465.582  1.00 81.84      A    C  
ANISOU 1329  CZ  ARG A 184     8506   7302  15287   1320   1545     35  A    C  
ATOM   1330  NH1 ARG A 184      34.409  28.578 464.836  1.00 92.16      A    N1+
ANISOU 1330  NH1 ARG A 184     9664   8604  16747   1295   1826     99  A    N1+
ATOM   1331  NH2 ARG A 184      32.692  27.126 465.338  1.00 53.80      A    N  
ANISOU 1331  NH2 ARG A 184     5298   3776  11369   1323   1506    -35  A    N  
ATOM   1332  N   GLN A 185      40.527  26.609 470.422  1.00 93.24      A    N  
ANISOU 1332  N   GLN A 185     8214   8348  18865   1360    336    266  A    N  
ATOM   1333  CA  GLN A 185      41.659  27.166 471.211  1.00 86.81      A    C  
ANISOU 1333  CA  GLN A 185     7057   7440  18486   1285     85    319  A    C  
ATOM   1334  C   GLN A 185      42.065  28.589 470.738  1.00 92.23      A    C  
ANISOU 1334  C   GLN A 185     7527   8103  19414   1151    260    372  A    C  
ATOM   1335  O   GLN A 185      43.122  29.152 471.106  1.00102.51      A    O  
ANISOU 1335  O   GLN A 185     8520   9299  21132   1084    142    422  A    O  
ATOM   1336  CB  GLN A 185      42.872  26.231 471.186  1.00 92.64      A    C  
ANISOU 1336  CB  GLN A 185     7566   8072  19559   1416    113    340  A    C  
ATOM   1337  CG  GLN A 185      43.952  26.550 472.250  1.00102.84      A    C  
ANISOU 1337  CG  GLN A 185     8552   9252  21270   1353   -264    385  A    C  
ATOM   1338  CD  GLN A 185      45.286  25.844 471.978  1.00 95.65      A    C  
ANISOU 1338  CD  GLN A 185     7344   8224  20774   1476   -150    420  A    C  
ATOM   1339  NE2 GLN A 185      45.751  25.055 472.940  1.00 86.61      A    N  
ANISOU 1339  NE2 GLN A 185     6148   7008  19753   1544   -511    423  A    N  
ATOM   1340  OE1 GLN A 185      45.884  26.013 470.917  1.00 88.63      A    O  
ANISOU 1340  OE1 GLN A 185     6283   7304  20090   1513    263    448  A    O  
ATOM   1341  N   LEU A 186      41.186  29.175 469.926  1.00 95.14      A    N  
ANISOU 1341  N   LEU A 186     8077   8555  19515   1111    530    365  A    N  
ATOM   1342  CA  LEU A 186      41.196  30.588 469.579  1.00106.31      A    C  
ANISOU 1342  CA  LEU A 186     9385   9960  21048    973    655    415  A    C  
ATOM   1343  C   LEU A 186      40.924  31.473 470.811  1.00101.97      A    C  
ANISOU 1343  C   LEU A 186     8819   9396  20530    827    207    404  A    C  
ATOM   1344  O   LEU A 186      41.006  32.708 470.718  1.00 82.33      A    O  
ANISOU 1344  O   LEU A 186     6227   6868  18187    703    235    442  A    O  
ATOM   1345  CB  LEU A 186      40.128  30.832 468.496  1.00102.73      A    C  
ANISOU 1345  CB  LEU A 186     9201   9607  20226    988   1004    403  A    C  
ATOM   1346  CG  LEU A 186      40.195  29.995 467.204  1.00 85.85      A    C  
ANISOU 1346  CG  LEU A 186     7174   7482  17961   1137   1455    392  A    C  
ATOM   1347  CD1 LEU A 186      38.913  30.167 466.385  1.00 69.53      A    C  
ANISOU 1347  CD1 LEU A 186     5452   5513  15453   1148   1672    358  A    C  
ATOM   1348  CD2 LEU A 186      41.428  30.307 466.356  1.00 77.95      A    C  
ANISOU 1348  CD2 LEU A 186     5898   6388  17333   1156   1820    473  A    C  
ATOM   1349  N   PHE A 187      40.624  30.828 471.947  1.00102.47      A    N  
ANISOU 1349  N   PHE A 187     9001   9477  20455    850   -196    353  A    N  
ATOM   1350  CA  PHE A 187      40.331  31.416 473.248  1.00 89.67      A    C  
ANISOU 1350  CA  PHE A 187     7428   7840  18801    743   -659    323  A    C  
ATOM   1351  C   PHE A 187      40.896  30.488 474.330  1.00 92.36      A    C  
ANISOU 1351  C   PHE A 187     7736   8119  19236    806  -1036    310  A    C  
ATOM   1352  O   PHE A 187      41.173  29.307 474.077  1.00 97.26      A    O  
ANISOU 1352  O   PHE A 187     8368   8740  19848    939   -938    315  A    O  
ATOM   1353  CB  PHE A 187      38.822  31.608 473.440  1.00 76.77      A    C  
ANISOU 1353  CB  PHE A 187     6136   6331  16700    716   -719    273  A    C  
ATOM   1354  CG  PHE A 187      38.324  32.970 473.044  1.00 89.00      A    C  
ANISOU 1354  CG  PHE A 187     7688   7901  18226    599   -596    282  A    C  
ATOM   1355  CD1 PHE A 187      38.853  34.125 473.624  1.00 98.79      A    C  
ANISOU 1355  CD1 PHE A 187     8747   9039  19749    473   -812    293  A    C  
ATOM   1356  CD2 PHE A 187      37.289  33.099 472.119  1.00 91.20      A    C  
ANISOU 1356  CD2 PHE A 187     8177   8283  18192    619   -288    277  A    C  
ATOM   1357  CE1 PHE A 187      38.378  35.389 473.261  1.00 91.05      A    C  
ANISOU 1357  CE1 PHE A 187     7779   8060  18757    372   -700    304  A    C  
ATOM   1358  CE2 PHE A 187      36.804  34.358 471.755  1.00 86.33      A    C  
ANISOU 1358  CE2 PHE A 187     7570   7677  17553    521   -180    294  A    C  
ATOM   1359  CZ  PHE A 187      37.351  35.501 472.327  1.00 84.54      A    C  
ANISOU 1359  CZ  PHE A 187     7146   7349  17626    399   -380    311  A    C  
ATOM   1360  N   THR A 188      41.108  31.034 475.532  1.00 90.43      A    N  
ANISOU 1360  N   THR A 188     7462   7806  19090    716  -1475    293  A    N  
ATOM   1361  CA  THR A 188      41.551  30.227 476.671  1.00 98.11      A    C  
ANISOU 1361  CA  THR A 188     8454   8716  20106    770  -1883    285  A    C  
ATOM   1362  C   THR A 188      40.365  29.535 477.357  1.00 99.79      A    C  
ANISOU 1362  C   THR A 188     9046   9028  19842    818  -2075    248  A    C  
ATOM   1363  O   THR A 188      39.228  30.020 477.314  1.00 96.89      A    O  
ANISOU 1363  O   THR A 188     8908   8756  19151    767  -2025    216  A    O  
ATOM   1364  CB  THR A 188      42.307  31.098 477.675  1.00 92.34      A    C  
ANISOU 1364  CB  THR A 188     7570   7849  19664    660  -2289    279  A    C  
ATOM   1365  CG2 THR A 188      42.916  30.234 478.793  1.00 89.18      A    C  
ANISOU 1365  CG2 THR A 188     7178   7366  19342    726  -2710    283  A    C  
ATOM   1366  OG1 THR A 188      43.383  31.764 477.003  1.00 95.28      A    O  
ANISOU 1366  OG1 THR A 188     7597   8111  20491    612  -2087    326  A    O  
ATOM   1367  N   SER A 189      40.639  28.383 477.989  1.00 90.38      A    N  
ANISOU 1367  N   SER A 189     7922   7799  18619    920  -2287    262  A    N  
ATOM   1368  CA  SER A 189      39.598  27.591 478.651  1.00 89.05      A    C  
ANISOU 1368  CA  SER A 189     8122   7696  18018    973  -2452    250  A    C  
ATOM   1369  C   SER A 189      39.084  28.250 479.929  1.00 87.05      A    C  
ANISOU 1369  C   SER A 189     8068   7435  17571    880  -2870    223  A    C  
ATOM   1370  O   SER A 189      39.859  28.500 480.860  1.00 90.53      A    O  
ANISOU 1370  O   SER A 189     8417   7769  18210    846  -3244    224  A    O  
ATOM   1371  CB  SER A 189      40.119  26.199 478.986  1.00 94.58      A    C  
ANISOU 1371  CB  SER A 189     8836   8332  18768   1109  -2566    288  A    C  
ATOM   1372  OG  SER A 189      39.141  25.480 479.718  1.00 83.58      A    O  
ANISOU 1372  OG  SER A 189     7810   6976  16969   1146  -2743    294  A    O  
ATOM   1373  N   MET A 190      37.759  28.446 479.996  1.00 81.05      A    N  
ANISOU 1373  N   MET A 190     7613   6778  16406    852  -2813    197  A    N  
ATOM   1374  CA  MET A 190      37.058  29.066 481.119  1.00 76.67      A    C  
ANISOU 1374  CA  MET A 190     7309   6228  15595    780  -3147    165  A    C  
ATOM   1375  C   MET A 190      36.359  28.068 482.037  1.00 62.73      A    C  
ANISOU 1375  C   MET A 190     5902   4470  13463    846  -3356    194  A    C  
ATOM   1376  O   MET A 190      35.664  28.489 482.961  1.00 61.94      A    O  
ANISOU 1376  O   MET A 190     6068   4377  13091    801  -3598    175  A    O  
ATOM   1377  CB  MET A 190      36.009  30.065 480.605  1.00 74.25      A    C  
ANISOU 1377  CB  MET A 190     7105   6016  15091    703  -2930    122  A    C  
ATOM   1378  CG  MET A 190      36.558  31.334 479.991  1.00 79.16      A    C  
ANISOU 1378  CG  MET A 190     7437   6610  16032    608  -2807     98  A    C  
ATOM   1379  SD  MET A 190      37.543  32.262 481.174  1.00 89.38      A    S  
ANISOU 1379  SD  MET A 190     8597   7748  17616    516  -3298     63  A    S  
ATOM   1380  CE  MET A 190      36.360  32.443 482.505  1.00 83.40      A    C  
ANISOU 1380  CE  MET A 190     8286   7021  16382    507  -3656     13  A    C  
ATOM   1381  N   LEU A 191      36.507  26.769 481.803  1.00 63.40      A    N  
ANISOU 1381  N   LEU A 191     6020   4543  13527    953  -3257    244  A    N  
ATOM   1382  CA  LEU A 191      35.786  25.771 482.585  1.00 63.02      A    C  
ANISOU 1382  CA  LEU A 191     6326   4488  13130   1009  -3406    291  A    C  
ATOM   1383  C   LEU A 191      36.130  25.846 484.074  1.00 74.67      A    C  
ANISOU 1383  C   LEU A 191     7947   5879  14546    993  -3903    311  A    C  
ATOM   1384  O   LEU A 191      37.302  25.943 484.453  1.00 75.09      A    O  
ANISOU 1384  O   LEU A 191     7782   5839  14909    999  -4149    313  A    O  
ATOM   1385  CB  LEU A 191      36.086  24.378 482.033  1.00 69.78      A    C  
ANISOU 1385  CB  LEU A 191     7150   5313  14050   1130  -3226    338  A    C  
ATOM   1386  CG  LEU A 191      35.407  23.156 482.660  1.00 70.84      A    C  
ANISOU 1386  CG  LEU A 191     7629   5417  13870   1194  -3318    403  A    C  
ATOM   1387  CD1 LEU A 191      33.929  23.400 482.923  1.00 71.34      A    C  
ANISOU 1387  CD1 LEU A 191     8044   5553  13510   1121  -3254    401  A    C  
ATOM   1388  CD2 LEU A 191      35.585  21.989 481.719  1.00 64.17      A    C  
ANISOU 1388  CD2 LEU A 191     6723   4546  13111   1304  -3029    420  A    C  
ATOM   1389  N   ASN A 192      35.087  25.798 484.911  1.00 76.20      A    N  
ANISOU 1389  N   ASN A 192     8531   6094  14327    972  -4043    329  A    N  
ATOM   1390  CA  ASN A 192      35.104  25.798 486.381  1.00 66.26      A    C  
ANISOU 1390  CA  ASN A 192     7549   4764  12862    963  -4490    355  A    C  
ATOM   1391  C   ASN A 192      35.470  27.123 487.027  1.00 78.48      A    C  
ANISOU 1391  C   ASN A 192     9058   6274  14485    876  -4792    278  A    C  
ATOM   1392  O   ASN A 192      35.740  27.151 488.236  1.00 69.96      A    O  
ANISOU 1392  O   ASN A 192     8187   5116  13277    872  -5201    286  A    O  
ATOM   1393  CB  ASN A 192      36.013  24.723 486.968  1.00 71.73      A    C  
ANISOU 1393  CB  ASN A 192     8226   5354  13676   1048  -4740    428  A    C  
ATOM   1394  CG  ASN A 192      35.243  23.496 487.370  1.00 85.93      A    C  
ANISOU 1394  CG  ASN A 192    10375   7144  15130   1113  -4707    524  A    C  
ATOM   1395  ND2 ASN A 192      34.527  23.589 488.486  1.00 95.43      A    N  
ANISOU 1395  ND2 ASN A 192    11984   8335  15939   1081  -4935    559  A    N  
ATOM   1396  OD1 ASN A 192      35.255  22.487 486.669  1.00 93.35      A    O  
ANISOU 1396  OD1 ASN A 192    11243   8081  16146   1187  -4462    567  A    O  
ATOM   1397  N   HIS A 193      35.469  28.219 486.280  1.00 72.45      A    N  
ANISOU 1397  N   HIS A 193     8065   5554  13908    804  -4609    202  A    N  
ATOM   1398  CA  HIS A 193      35.656  29.525 486.877  1.00 66.77      A    C  
ANISOU 1398  CA  HIS A 193     7349   4787  13234    716  -4880    120  A    C  
ATOM   1399  C   HIS A 193      34.341  29.990 487.496  1.00 64.75      A    C  
ANISOU 1399  C   HIS A 193     7510   4580  12514    695  -4926     96  A    C  
ATOM   1400  O   HIS A 193      33.262  29.691 486.978  1.00 70.30      A    O  
ANISOU 1400  O   HIS A 193     8362   5370  12980    713  -4603    124  A    O  
ATOM   1401  CB  HIS A 193      36.156  30.497 485.813  1.00 66.10      A    C  
ANISOU 1401  CB  HIS A 193     6864   4712  13540    646  -4642     64  A    C  
ATOM   1402  CG  HIS A 193      35.697  31.908 486.009  1.00 85.83      A    C  
ANISOU 1402  CG  HIS A 193     9424   7208  15979    555  -4719    -23  A    C  
ATOM   1403  CD2 HIS A 193      34.581  32.548 485.580  1.00 78.88      A    C  
ANISOU 1403  CD2 HIS A 193     8668   6416  14888    529  -4483    -56  A    C  
ATOM   1404  ND1 HIS A 193      36.435  32.843 486.706  1.00 81.60      A    N  
ANISOU 1404  ND1 HIS A 193     8827   6551  15625    482  -5067    -91  A    N  
ATOM   1405  CE1 HIS A 193      35.787  33.994 486.704  1.00 92.87      A    C  
ANISOU 1405  CE1 HIS A 193    10338   7997  16950    417  -5050   -167  A    C  
ATOM   1406  NE2 HIS A 193      34.656  33.840 486.033  1.00 84.56      A    N  
ANISOU 1406  NE2 HIS A 193     9390   7071  15667    450  -4704   -144  A    N  
ATOM   1407  N   HIS A 194      34.430  30.622 488.666  1.00 68.46      A    N  
ANISOU 1407  N   HIS A 194     8207   4978  12826    661  -5332     46  A    N  
ATOM   1408  CA  HIS A 194      33.289  31.220 489.351  1.00 65.52      A    C  
ANISOU 1408  CA  HIS A 194     8246   4633  12016    647  -5409     10  A    C  
ATOM   1409  C   HIS A 194      33.328  32.745 489.227  1.00 65.20      A    C  
ANISOU 1409  C   HIS A 194     8079   4577  12118    566  -5474   -113  A    C  
ATOM   1410  O   HIS A 194      34.402  33.351 489.254  1.00 67.45      A    O  
ANISOU 1410  O   HIS A 194     8094   4781  12753    503  -5660   -176  A    O  
ATOM   1411  CB  HIS A 194      33.273  30.868 490.843  1.00 74.91      A    C  
ANISOU 1411  CB  HIS A 194     9871   5760  12830    672  -5821     31  A    C  
ATOM   1412  CG  HIS A 194      33.236  29.403 491.147  1.00 93.27      A    C  
ANISOU 1412  CG  HIS A 194    12367   8080  14991    747  -5809    162  A    C  
ATOM   1413  CD2 HIS A 194      32.233  28.610 491.593  1.00 99.73      A    C  
ANISOU 1413  CD2 HIS A 194    13593   8929  15371    789  -5710    259  A    C  
ATOM   1414  ND1 HIS A 194      34.348  28.591 491.043  1.00102.94      A    N  
ANISOU 1414  ND1 HIS A 194    13341   9243  16530    783  -5908    210  A    N  
ATOM   1415  CE1 HIS A 194      34.027  27.359 491.397  1.00103.07      A    C  
ANISOU 1415  CE1 HIS A 194    13596   9257  16308    851  -5885    326  A    C  
ATOM   1416  NE2 HIS A 194      32.752  27.345 491.741  1.00103.84      A    N  
ANISOU 1416  NE2 HIS A 194    14096   9409  15950    847  -5761    362  A    N  
ATOM   1417  N   PHE A 195      32.149  33.370 489.137  1.00 63.36      A    N  
ANISOU 1417  N   PHE A 195     8079   4451  11543    500  -5191   -182  A    N  
ATOM   1418  CA  PHE A 195      32.020  34.828 489.215  1.00 62.62      A    C  
ANISOU 1418  CA  PHE A 195     7973   4365  11455    391  -5208   -328  A    C  
ATOM   1419  C   PHE A 195      31.063  35.226 490.336  1.00 63.02      A    C  
ANISOU 1419  C   PHE A 195     8541   4460  10945    356  -5281   -414  A    C  
ATOM   1420  O   PHE A 195      30.119  34.486 490.646  1.00 92.30      A    O  
ANISOU 1420  O   PHE A 195    12574   8250  14247    390  -5096   -354  A    O  
ATOM   1421  CB  PHE A 195      31.540  35.461 487.894  1.00 73.77      A    C  
ANISOU 1421  CB  PHE A 195     9131   5862  13035    333  -4731   -355  A    C  
ATOM   1422  CG  PHE A 195      30.125  35.064 487.461  1.00 70.06      A    C  
ANISOU 1422  CG  PHE A 195     8888   5539  12193    336  -4284   -327  A    C  
ATOM   1423  CD1 PHE A 195      29.020  35.812 487.860  1.00 55.11      A    C  
ANISOU 1423  CD1 PHE A 195     7292   3722   9927    277  -4145   -419  A    C  
ATOM   1424  CD2 PHE A 195      29.921  33.972 486.611  1.00 64.79      A    C  
ANISOU 1424  CD2 PHE A 195     8113   4919  11586    398  -4005   -216  A    C  
ATOM   1425  CE1 PHE A 195      27.750  35.459 487.455  1.00 63.16      A    C  
ANISOU 1425  CE1 PHE A 195     8468   4867  10664    276  -3754   -388  A    C  
ATOM   1426  CE2 PHE A 195      28.648  33.612 486.192  1.00 61.49      A    C  
ANISOU 1426  CE2 PHE A 195     7876   4621  10867    387  -3632   -193  A    C  
ATOM   1427  CZ  PHE A 195      27.558  34.355 486.611  1.00 68.25      A    C  
ANISOU 1427  CZ  PHE A 195     8995   5556  11379    323  -3509   -273  A    C  
ATOM   1428  N   PRO A 196      31.280  36.381 490.959  1.00 64.80      A    N  
ANISOU 1428  N   PRO A 196     8856   4623  11141    286  -5536   -557  A    N  
ATOM   1429  CA  PRO A 196      30.398  36.828 492.044  1.00 70.34      A    C  
ANISOU 1429  CA  PRO A 196    10070   5356  11299    265  -5587   -660  A    C  
ATOM   1430  C   PRO A 196      29.093  37.432 491.537  1.00 70.90      A    C  
ANISOU 1430  C   PRO A 196    10238   5552  11147    221  -5094   -722  A    C  
ATOM   1431  O   PRO A 196      29.004  37.980 490.435  1.00 62.85      A    O  
ANISOU 1431  O   PRO A 196     8894   4565  10421    178  -4811   -735  A    O  
ATOM   1432  CB  PRO A 196      31.238  37.891 492.754  1.00 72.89      A    C  
ANISOU 1432  CB  PRO A 196    10402   5539  11754    207  -6056   -807  A    C  
ATOM   1433  CG  PRO A 196      32.052  38.478 491.650  1.00 74.76      A    C  
ANISOU 1433  CG  PRO A 196    10082   5725  12597    154  -5986   -805  A    C  
ATOM   1434  CD  PRO A 196      32.385  37.325 490.728  1.00 66.58      A    C  
ANISOU 1434  CD  PRO A 196     8721   4728  11848    222  -5796   -634  A    C  
ATOM   1435  N   ALA A 197      28.083  37.380 492.410  1.00 74.13      A    N  
ANISOU 1435  N   ALA A 197    11116   6022  11029    237  -5006   -760  A    N  
ATOM   1436  CA  ALA A 197      26.754  37.861 492.043  1.00 60.27      A    C  
ANISOU 1436  CA  ALA A 197     9469   4384   9049    211  -4541   -810  A    C  
ATOM   1437  C   ALA A 197      26.773  39.312 491.596  1.00 59.75      A    C  
ANISOU 1437  C   ALA A 197     9228   4280   9195    144  -4483   -960  A    C  
ATOM   1438  O   ALA A 197      25.932  39.717 490.788  1.00 57.10      A    O  
ANISOU 1438  O   ALA A 197     8779   4029   8888    125  -4086   -969  A    O  
ATOM   1439  CB  ALA A 197      25.785  37.686 493.212  1.00 61.61      A    C  
ANISOU 1439  CB  ALA A 197    10174   4600   8636    241  -4484   -841  A    C  
ATOM   1440  N   SER A 198      27.722  40.106 492.105  1.00 87.31      A    N  
ANISOU 1440  N   SER A 198    12693   7630  12849    106  -4893  -1075  A    N  
ATOM   1441  CA  SER A 198      27.821  41.518 491.749  1.00 75.93      A    C  
ANISOU 1441  CA  SER A 198    11099   6117  11634     32  -4877  -1219  A    C  
ATOM   1442  C   SER A 198      28.053  41.739 490.258  1.00 77.51      A    C  
ANISOU 1442  C   SER A 198    10803   6340  12307     -7  -4601  -1140  A    C  
ATOM   1443  O   SER A 198      27.744  42.824 489.749  1.00 81.36      A    O  
ANISOU 1443  O   SER A 198    11170   6851  12893    -44  -4388  -1195  A    O  
ATOM   1444  CB  SER A 198      28.958  42.151 492.539  1.00 66.22      A    C  
ANISOU 1444  CB  SER A 198     9862   4776  10524     20  -5335  -1284  A    C  
ATOM   1445  OG  SER A 198      30.216  41.782 491.996  1.00 66.91      A    O  
ANISOU 1445  OG  SER A 198     9518   4810  11095     19  -5519  -1165  A    O  
ATOM   1446  N   ASP A 199      28.571  40.727 489.552  1.00 75.02      A    N  
ANISOU 1446  N   ASP A 199    10205   6063  12238     24  -4546   -981  A    N  
ATOM   1447  CA  ASP A 199      28.987  40.846 488.157  1.00 56.89      A    C  
ANISOU 1447  CA  ASP A 199     7449   3773  10395     -4  -4312   -898  A    C  
ATOM   1448  C   ASP A 199      27.827  40.819 487.183  1.00 60.19      A    C  
ANISOU 1448  C   ASP A 199     7849   4329  10692      6  -3808   -850  A    C  
ATOM   1449  O   ASP A 199      28.011  41.182 486.013  1.00 52.01      A    O  
ANISOU 1449  O   ASP A 199     6495   3296   9969    -24  -3585   -803  A    O  
ATOM   1450  CB  ASP A 199      29.998  39.751 487.812  1.00 65.53      A    C  
ANISOU 1450  CB  ASP A 199     8270   4842  11787     45  -4438   -761  A    C  
ATOM   1451  CG  ASP A 199      31.413  40.105 488.264  1.00 73.64      A    C  
ANISOU 1451  CG  ASP A 199     9084   5717  13178     17  -4892   -789  A    C  
ATOM   1452  OD1 ASP A 199      31.607  41.180 488.897  1.00 78.22      A    O  
ANISOU 1452  OD1 ASP A 199     9758   6265  13695     -9  -5056   -880  A    O  
ATOM   1453  OD2 ASP A 199      32.335  39.311 487.980  1.00 74.74      A    O1-
ANISOU 1453  OD2 ASP A 199     8952   5803  13645     56  -5025   -690  A    O1-
ATOM   1454  N   ILE A 200      26.679  40.307 487.605  1.00 67.78      A    N  
ANISOU 1454  N   ILE A 200     9131   5400  11223     50  -3628   -843  A    N  
ATOM   1455  CA  ILE A 200      25.420  40.472 486.893  1.00 60.26      A    C  
ANISOU 1455  CA  ILE A 200     8207   4566  10123     52  -3200   -828  A    C  
ATOM   1456  C   ILE A 200      24.402  41.065 487.861  1.00 56.57      A    C  
ANISOU 1456  C   ILE A 200     8115   4121   9258     59  -3161   -948  A    C  
ATOM   1457  O   ILE A 200      23.878  40.372 488.735  1.00 57.57      A    O  
ANISOU 1457  O   ILE A 200     8552   4297   9026     99  -3175   -935  A    O  
ATOM   1458  CB  ILE A 200      24.921  39.151 486.279  1.00 47.57      A    C  
ANISOU 1458  CB  ILE A 200     6565   3073   8436     98  -2952   -686  A    C  
ATOM   1459  CG1 ILE A 200      26.069  38.417 485.598  1.00 47.75      A    C  
ANISOU 1459  CG1 ILE A 200     6280   3049   8814    118  -3044   -584  A    C  
ATOM   1460  CG2 ILE A 200      23.870  39.422 485.239  1.00 44.92      A    C  
ANISOU 1460  CG2 ILE A 200     6143   2838   8086     86  -2555   -663  A    C  
ATOM   1461  CD1 ILE A 200      25.657  37.101 484.988  1.00 56.42      A    C  
ANISOU 1461  CD1 ILE A 200     7359   4229   9847    166  -2823   -461  A    C  
ATOM   1462  N   PRO A 201      24.129  42.364 487.761  1.00 59.13      A    N  
ANISOU 1462  N   PRO A 201     8431   4396   9639     25  -3106  -1066  A    N  
ATOM   1463  CA  PRO A 201      23.211  42.998 488.711  1.00 59.61      A    C  
ANISOU 1463  CA  PRO A 201     8852   4459   9340     47  -3060  -1201  A    C  
ATOM   1464  C   PRO A 201      21.812  42.422 488.591  1.00 51.65      A    C  
ANISOU 1464  C   PRO A 201     7981   3601   8045     94  -2680  -1140  A    C  
ATOM   1465  O   PRO A 201      21.443  41.819 487.583  1.00 52.55      A    O  
ANISOU 1465  O   PRO A 201     7883   3808   8276     94  -2437  -1015  A    O  
ATOM   1466  CB  PRO A 201      23.238  44.475 488.305  1.00 62.33      A    C  
ANISOU 1466  CB  PRO A 201     9073   4706   9904      5  -3033  -1316  A    C  
ATOM   1467  CG  PRO A 201      24.506  44.629 487.536  1.00 64.35      A    C  
ANISOU 1467  CG  PRO A 201     8942   4917  10592    -51  -3176  -1237  A    C  
ATOM   1468  CD  PRO A 201      24.720  43.336 486.828  1.00 49.97      A    C  
ANISOU 1468  CD  PRO A 201     6944   3154   8888    -34  -3092  -1081  A    C  
ATOM   1469  N   ALA A 202      21.032  42.597 489.658  1.00 54.21      A    N  
ANISOU 1469  N   ALA A 202     8671   3940   7987    133  -2633  -1232  A    N  
ATOM   1470  CA  ALA A 202      19.702  42.008 489.677  1.00 49.97      A    C  
ANISOU 1470  CA  ALA A 202     8261   3537   7190    171  -2273  -1167  A    C  
ATOM   1471  C   ALA A 202      18.916  42.448 488.457  1.00 47.41      A    C  
ANISOU 1471  C   ALA A 202     7661   3278   7076    164  -1949  -1133  A    C  
ATOM   1472  O   ALA A 202      18.197  41.653 487.848  1.00 62.65      A    O  
ANISOU 1472  O   ALA A 202     9489   5318   8995    167  -1703  -1013  A    O  
ATOM   1473  CB  ALA A 202      18.978  42.383 490.967  1.00 52.36      A    C  
ANISOU 1473  CB  ALA A 202     8984   3830   7080    219  -2223  -1290  A    C  
ATOM   1474  N   GLN A 203      19.075  43.708 488.066  1.00 68.36      A    N  
ANISOU 1474  N   GLN A 203    10191   5847   9933    153  -1970  -1233  A    N  
ATOM   1475  CA  GLN A 203      18.351  44.241 486.923  1.00 45.38      A    C  
ANISOU 1475  CA  GLN A 203     7044   2981   7218    155  -1695  -1198  A    C  
ATOM   1476  C   GLN A 203      18.718  43.512 485.633  1.00 48.90      A    C  
ANISOU 1476  C   GLN A 203     7176   3487   7917    119  -1634  -1038  A    C  
ATOM   1477  O   GLN A 203      17.861  43.300 484.771  1.00 56.71      A    O  
ANISOU 1477  O   GLN A 203     8038   4568   8943    129  -1378   -959  A    O  
ATOM   1478  CB  GLN A 203      18.624  45.736 486.832  1.00 67.22      A    C  
ANISOU 1478  CB  GLN A 203     9766   5612  10164    146  -1776  -1328  A    C  
ATOM   1479  CG  GLN A 203      17.515  46.511 486.180  1.00 85.95      A    C  
ANISOU 1479  CG  GLN A 203    12051   8009  12598    186  -1485  -1341  A    C  
ATOM   1480  CD  GLN A 203      17.777  47.995 486.209  1.00 96.74      A    C  
ANISOU 1480  CD  GLN A 203    13416   9213  14129    183  -1576  -1475  A    C  
ATOM   1481  NE2 GLN A 203      18.746  48.408 487.027  1.00101.37      A    N  
ANISOU 1481  NE2 GLN A 203    14139   9664  14713    147  -1884  -1594  A    N  
ATOM   1482  OE1 GLN A 203      17.101  48.769 485.528  1.00 97.58      A    O  
ANISOU 1482  OE1 GLN A 203    13408   9301  14366    212  -1390  -1473  A    O  
ATOM   1483  N   ALA A 204      19.979  43.098 485.491  1.00 51.79      A    N  
ANISOU 1483  N   ALA A 204     7421   3797   8460     84  -1870   -991  A    N  
ATOM   1484  CA  ALA A 204      20.409  42.396 484.285  1.00 41.64      A    C  
ANISOU 1484  CA  ALA A 204     5857   2555   7408     64  -1796   -852  A    C  
ATOM   1485  C   ALA A 204      19.955  40.945 484.282  1.00 40.72      A    C  
ANISOU 1485  C   ALA A 204     5806   2547   7120     85  -1691   -745  A    C  
ATOM   1486  O   ALA A 204      19.589  40.412 483.233  1.00 40.24      A    O  
ANISOU 1486  O   ALA A 204     5589   2557   7143     83  -1501   -650  A    O  
ATOM   1487  CB  ALA A 204      21.928  42.462 484.134  1.00 42.67      A    C  
ANISOU 1487  CB  ALA A 204     5805   2578   7829     29  -2057   -839  A    C  
ATOM   1488  N   ARG A 205      20.030  40.267 485.421  1.00 42.66      A    N  
ANISOU 1488  N   ARG A 205     6293   2790   7127    102  -1830   -755  A    N  
ATOM   1489  CA  ARG A 205      19.448  38.934 485.503  1.00 41.54      A    C  
ANISOU 1489  CA  ARG A 205     6244   2733   6805    115  -1708   -648  A    C  
ATOM   1490  C   ARG A 205      17.952  38.966 485.223  1.00 40.37      A    C  
ANISOU 1490  C   ARG A 205     6133   2687   6518    116  -1384   -635  A    C  
ATOM   1491  O   ARG A 205      17.419  38.074 484.553  1.00 50.52      A    O  
ANISOU 1491  O   ARG A 205     7334   4042   7818    103  -1221   -535  A    O  
ATOM   1492  CB  ARG A 205      19.759  38.335 486.880  1.00 43.74      A    C  
ANISOU 1492  CB  ARG A 205     6819   2976   6823    135  -1917   -654  A    C  
ATOM   1493  CG  ARG A 205      21.251  38.035 487.067  1.00 45.01      A    C  
ANISOU 1493  CG  ARG A 205     6902   3037   7164    140  -2266   -636  A    C  
ATOM   1494  CD  ARG A 205      21.608  37.275 488.343  1.00 67.04      A    C  
ANISOU 1494  CD  ARG A 205     9989   5784   9697    168  -2511   -611  A    C  
ATOM   1495  NE  ARG A 205      21.508  38.077 489.560  1.00 77.81      A    N  
ANISOU 1495  NE  ARG A 205    11662   7102  10799    176  -2664   -740  A    N  
ATOM   1496  CZ  ARG A 205      20.407  38.225 490.290  1.00 70.32      A    C  
ANISOU 1496  CZ  ARG A 205    11014   6209   9494    190  -2470   -781  A    C  
ATOM   1497  NH1 ARG A 205      19.269  37.628 489.938  1.00 74.65      A    N1+
ANISOU 1497  NH1 ARG A 205    11566   6863   9934    187  -2120   -695  A    N1+
ATOM   1498  NH2 ARG A 205      20.444  38.972 491.383  1.00 52.82      A    N  
ANISOU 1498  NH2 ARG A 205     9099   3934   7037    208  -2625   -914  A    N  
ATOM   1499  N   ALA A 206      17.278  40.029 485.644  1.00 41.02      A    N  
ANISOU 1499  N   ALA A 206     6314   2766   6505    132  -1294   -740  A    N  
ATOM   1500  CA  ALA A 206      15.838  40.129 485.438  1.00 44.13      A    C  
ANISOU 1500  CA  ALA A 206     6714   3248   6804    144   -991   -730  A    C  
ATOM   1501  C   ALA A 206      15.460  40.289 483.967  1.00 42.88      A    C  
ANISOU 1501  C   ALA A 206     6269   3135   6890    128   -842   -669  A    C  
ATOM   1502  O   ALA A 206      14.331  39.955 483.590  1.00 37.48      A    O  
ANISOU 1502  O   ALA A 206     5539   2532   6170    125   -624   -618  A    O  
ATOM   1503  CB  ALA A 206      15.281  41.292 486.256  1.00 48.43      A    C  
ANISOU 1503  CB  ALA A 206     7431   3759   7213    186   -931   -870  A    C  
ATOM   1504  N   MET A 207      16.362  40.814 483.126  1.00 47.46      A    N  
ANISOU 1504  N   MET A 207     6659   3657   7718    116   -954   -669  A    N  
ATOM   1505  CA  MET A 207      16.003  41.026 481.724  1.00 41.79      A    C  
ANISOU 1505  CA  MET A 207     5716   2975   7189    107   -812   -607  A    C  
ATOM   1506  C   MET A 207      15.691  39.717 481.030  1.00 34.63      A    C  
ANISOU 1506  C   MET A 207     4744   2146   6268     86   -721   -495  A    C  
ATOM   1507  O   MET A 207      14.865  39.693 480.119  1.00 50.20      A    O  
ANISOU 1507  O   MET A 207     6609   4175   8288     81   -570   -449  A    O  
ATOM   1508  CB  MET A 207      17.114  41.740 480.951  1.00 41.45      A    C  
ANISOU 1508  CB  MET A 207     5497   2847   7403     92   -923   -607  A    C  
ATOM   1509  CG  MET A 207      17.403  43.189 481.325  1.00 63.46      A    C  
ANISOU 1509  CG  MET A 207     8302   5531  10279     98  -1007   -712  A    C  
ATOM   1510  SD  MET A 207      16.100  44.409 481.031  1.00 60.06      A    S  
ANISOU 1510  SD  MET A 207     7867   5103   9850    139   -814   -761  A    S  
ATOM   1511  CE  MET A 207      15.247  44.455 482.627  1.00 56.90      A    C  
ANISOU 1511  CE  MET A 207     7748   4719   9152    186   -777   -884  A    C  
ATOM   1512  N   TYR A 208      16.325  38.615 481.448  1.00 46.20      A    N  
ANISOU 1512  N   TYR A 208     6282   3601   7671     75   -829   -451  A    N  
ATOM   1513  CA  TYR A 208      16.060  37.323 480.807  1.00 34.06      A    C  
ANISOU 1513  CA  TYR A 208     4702   2112   6129     55   -751   -354  A    C  
ATOM   1514  C   TYR A 208      14.599  36.907 480.936  1.00 33.92      A    C  
ANISOU 1514  C   TYR A 208     4745   2173   5970     32   -565   -326  A    C  
ATOM   1515  O   TYR A 208      14.058  36.253 480.041  1.00 37.04      A    O  
ANISOU 1515  O   TYR A 208     5050   2609   6415      5   -470   -264  A    O  
ATOM   1516  CB  TYR A 208      16.986  36.251 481.383  1.00 34.82      A    C  
ANISOU 1516  CB  TYR A 208     4885   2160   6188     60   -911   -313  A    C  
ATOM   1517  CG  TYR A 208      18.419  36.433 480.964  1.00 38.16      A    C  
ANISOU 1517  CG  TYR A 208     5167   2506   6827     81  -1072   -316  A    C  
ATOM   1518  CD1 TYR A 208      18.810  36.197 479.646  1.00 36.50      A    C  
ANISOU 1518  CD1 TYR A 208     4769   2293   6805     86   -997   -270  A    C  
ATOM   1519  CD2 TYR A 208      19.377  36.860 481.868  1.00 36.47      A    C  
ANISOU 1519  CD2 TYR A 208     5005   2215   6637     96  -1294   -367  A    C  
ATOM   1520  CE1 TYR A 208      20.122  36.379 479.246  1.00 34.45      A    C  
ANISOU 1520  CE1 TYR A 208     4356   1961   6773    107  -1099   -265  A    C  
ATOM   1521  CE2 TYR A 208      20.684  37.044 481.481  1.00 36.94      A    C  
ANISOU 1521  CE2 TYR A 208     4890   2196   6947    108  -1438   -364  A    C  
ATOM   1522  CZ  TYR A 208      21.056  36.799 480.172  1.00 45.91      A    C  
ANISOU 1522  CZ  TYR A 208     5819   3336   8290    115  -1320   -308  A    C  
ATOM   1523  OH  TYR A 208      22.372  36.974 479.795  1.00 44.15      A    O  
ANISOU 1523  OH  TYR A 208     5400   3032   8341    129  -1425   -296  A    O  
ATOM   1524  N   SER A 209      13.937  37.293 482.020  1.00 35.07      A    N  
ANISOU 1524  N   SER A 209     5041   2334   5950     42   -506   -373  A    N  
ATOM   1525  CA  SER A 209      12.523  37.001 482.149  1.00 35.28      A    C  
ANISOU 1525  CA  SER A 209     5085   2432   5889     21   -297   -342  A    C  
ATOM   1526  C   SER A 209      11.668  37.813 481.176  1.00 38.14      A    C  
ANISOU 1526  C   SER A 209     5257   2833   6400     31   -173   -356  A    C  
ATOM   1527  O   SER A 209      10.594  37.343 480.780  1.00 37.25      A    O  
ANISOU 1527  O   SER A 209     5066   2778   6310     -2    -37   -303  A    O  
ATOM   1528  CB  SER A 209      12.095  37.235 483.593  1.00 37.13      A    C  
ANISOU 1528  CB  SER A 209     5544   2666   5899     43   -232   -390  A    C  
ATOM   1529  OG  SER A 209      12.661  36.243 484.429  1.00 38.10      A    O  
ANISOU 1529  OG  SER A 209     5861   2757   5857     26   -335   -340  A    O  
ATOM   1530  N   ILE A 210      12.146  38.976 480.719  1.00 34.08      A    N  
ANISOU 1530  N   ILE A 210     4660   2280   6010     69   -237   -415  A    N  
ATOM   1531  CA  ILE A 210      11.411  39.740 479.708  1.00 33.44      A    C  
ANISOU 1531  CA  ILE A 210     4410   2222   6074     87   -149   -409  A    C  
ATOM   1532  C   ILE A 210      11.708  39.209 478.310  1.00 35.41      A    C  
ANISOU 1532  C   ILE A 210     4526   2485   6443     56   -190   -331  A    C  
ATOM   1533  O   ILE A 210      10.801  38.975 477.508  1.00 49.85      A    O  
ANISOU 1533  O   ILE A 210     6258   4363   8321     40   -118   -284  A    O  
ATOM   1534  CB  ILE A 210      11.727  41.248 479.821  1.00 33.90      A    C  
ANISOU 1534  CB  ILE A 210     4456   2211   6212    141   -187   -495  A    C  
ATOM   1535  CG1 ILE A 210      11.147  41.851 481.099  1.00 35.49      A    C  
ANISOU 1535  CG1 ILE A 210     4803   2398   6283    186   -105   -591  A    C  
ATOM   1536  CG2 ILE A 210      11.148  41.994 478.656  1.00 43.49      A    C  
ANISOU 1536  CG2 ILE A 210     5505   3432   7589    164   -130   -464  A    C  
ATOM   1537  CD1 ILE A 210      12.166  42.181 482.103  1.00 36.51      A    C  
ANISOU 1537  CD1 ILE A 210     5108   2449   6315    196   -253   -679  A    C  
ATOM   1538  N   ASN A 211      12.961  39.003 477.997  1.00 31.70      A    N  
ANISOU 1538  N   ASN A 211     4054   1968   6024     52   -307   -320  A    N  
ATOM   1539  CA  ASN A 211      13.351  38.404 476.727  1.00 30.80      A    C  
ANISOU 1539  CA  ASN A 211     3852   1858   5993     34   -320   -255  A    C  
ATOM   1540  C   ASN A 211      14.475  37.408 477.000  1.00 30.87      A    C  
ANISOU 1540  C   ASN A 211     3913   1828   5989     26   -414   -238  A    C  
ATOM   1541  O   ASN A 211      15.518  37.764 477.553  1.00 49.54      A    O  
ANISOU 1541  O   ASN A 211     6293   4133   8399     44   -519   -270  A    O  
ATOM   1542  CB  ASN A 211      13.768  39.481 475.720  1.00 30.49      A    C  
ANISOU 1542  CB  ASN A 211     3708   1784   6095     60   -322   -248  A    C  
ATOM   1543  CG  ASN A 211      14.052  38.915 474.332  1.00 29.90      A    C  
ANISOU 1543  CG  ASN A 211     3578   1718   6065     52   -299   -181  A    C  
ATOM   1544  ND2 ASN A 211      13.885  39.742 473.302  1.00 29.81      A    N  
ANISOU 1544  ND2 ASN A 211     3504   1700   6123     70   -261   -149  A    N  
ATOM   1545  OD1 ASN A 211      14.425  37.755 474.189  1.00 29.74      A    O  
ANISOU 1545  OD1 ASN A 211     3592   1701   6007     36   -314   -160  A    O  
ATOM   1546  N   PRO A 212      14.284  36.138 476.660  1.00 34.37      A    N  
ANISOU 1546  N   PRO A 212     4382   2289   6388     -1   -395   -189  A    N  
ATOM   1547  CA  PRO A 212      15.278  35.123 477.030  1.00 38.98      A    C  
ANISOU 1547  CA  PRO A 212     5024   2821   6966      5   -486   -169  A    C  
ATOM   1548  C   PRO A 212      16.608  35.256 476.315  1.00 39.27      A    C  
ANISOU 1548  C   PRO A 212     4964   2800   7158     43   -539   -165  A    C  
ATOM   1549  O   PRO A 212      17.577  34.615 476.744  1.00 40.07      A    O  
ANISOU 1549  O   PRO A 212     5083   2843   7299     66   -637   -155  A    O  
ATOM   1550  CB  PRO A 212      14.586  33.806 476.659  1.00 38.53      A    C  
ANISOU 1550  CB  PRO A 212     5013   2782   6846    -35   -433   -122  A    C  
ATOM   1551  CG  PRO A 212      13.496  34.190 475.711  1.00 30.29      A    C  
ANISOU 1551  CG  PRO A 212     3893   1796   5819    -61   -339   -118  A    C  
ATOM   1552  CD  PRO A 212      13.062  35.552 476.096  1.00 30.36      A    C  
ANISOU 1552  CD  PRO A 212     3860   1836   5839    -41   -307   -155  A    C  
ATOM   1553  N   ILE A 213      16.703  36.062 475.263  1.00 33.83      A    N  
ANISOU 1553  N   ILE A 213     4170   2116   6567     55   -473   -162  A    N  
ATOM   1554  CA  ILE A 213      17.931  36.178 474.488  1.00 40.75      A    C  
ANISOU 1554  CA  ILE A 213     4944   2936   7602     88   -468   -143  A    C  
ATOM   1555  C   ILE A 213      18.426  37.614 474.561  1.00 39.03      A    C  
ANISOU 1555  C   ILE A 213     4636   2682   7511     90   -490   -162  A    C  
ATOM   1556  O   ILE A 213      17.628  38.558 474.583  1.00 49.40      A    O  
ANISOU 1556  O   ILE A 213     5960   4021   8787     77   -457   -180  A    O  
ATOM   1557  CB  ILE A 213      17.750  35.740 473.024  1.00 41.81      A    C  
ANISOU 1557  CB  ILE A 213     5064   3089   7731     98   -346   -106  A    C  
ATOM   1558  CG1 ILE A 213      19.112  35.663 472.350  1.00 41.98      A    C  
ANISOU 1558  CG1 ILE A 213     4992   3046   7912    143   -302    -84  A    C  
ATOM   1559  CG2 ILE A 213      16.846  36.726 472.271  1.00 32.16      A    C  
ANISOU 1559  CG2 ILE A 213     3830   1915   6476     84   -274    -94  A    C  
ATOM   1560  CD1 ILE A 213      19.257  34.472 471.465  1.00 33.17      A    C  
ANISOU 1560  CD1 ILE A 213     3927   1918   6759    175   -222    -71  A    C  
ATOM   1561  N   ARG A 214      19.745  37.768 474.661  1.00 31.85      A    N  
ANISOU 1561  N   ARG A 214     3627   1722   6753    104   -550   -158  A    N  
ATOM   1562  CA  ARG A 214      20.415  39.059 474.616  1.00 32.51      A    C  
ANISOU 1562  CA  ARG A 214     3597   1777   6978     90   -569   -164  A    C  
ATOM   1563  C   ARG A 214      21.506  38.995 473.562  1.00 39.61      A    C  
ANISOU 1563  C   ARG A 214     4346   2652   8050    106   -470   -104  A    C  
ATOM   1564  O   ARG A 214      22.321  38.066 473.568  1.00 62.12      A    O  
ANISOU 1564  O   ARG A 214     7146   5474  10983    137   -491    -90  A    O  
ATOM   1565  CB  ARG A 214      20.992  39.407 475.990  1.00 33.53      A    C  
ANISOU 1565  CB  ARG A 214     3738   1844   7157     78   -771   -227  A    C  
ATOM   1566  CG  ARG A 214      21.673  40.747 476.119  1.00 34.53      A    C  
ANISOU 1566  CG  ARG A 214     3756   1920   7443     48   -831   -250  A    C  
ATOM   1567  CD  ARG A 214      20.775  41.928 475.801  1.00 34.07      A    C  
ANISOU 1567  CD  ARG A 214     3734   1884   7328     33   -737   -264  A    C  
ATOM   1568  NE  ARG A 214      21.317  43.158 476.365  1.00 43.59      A    N  
ANISOU 1568  NE  ARG A 214     4892   3018   8652      2   -850   -316  A    N  
ATOM   1569  CZ  ARG A 214      21.186  44.358 475.813  1.00 43.16      A    C  
ANISOU 1569  CZ  ARG A 214     4783   2947   8669    -16   -772   -297  A    C  
ATOM   1570  NH1 ARG A 214      20.536  44.483 474.665  1.00 37.12      A    N1+
ANISOU 1570  NH1 ARG A 214     4010   2232   7862     -1   -592   -222  A    N1+
ATOM   1571  NH2 ARG A 214      21.720  45.428 476.403  1.00 49.56      A    N  
ANISOU 1571  NH2 ARG A 214     5560   3677   9594    -49   -893   -353  A    N  
ATOM   1572  N   ILE A 215      21.530  39.966 472.653  1.00 38.36      A    N  
ANISOU 1572  N   ILE A 215     4124   2489   7961     92   -349    -63  A    N  
ATOM   1573  CA  ILE A 215      22.495  39.970 471.555  1.00 45.40      A    C  
ANISOU 1573  CA  ILE A 215     4890   3337   9022    108   -200      7  A    C  
ATOM   1574  C   ILE A 215      23.283  41.280 471.546  1.00 50.60      A    C  
ANISOU 1574  C   ILE A 215     5399   3932   9896     66   -202     33  A    C  
ATOM   1575  O   ILE A 215      22.695  42.370 471.554  1.00 57.00      A    O  
ANISOU 1575  O   ILE A 215     6248   4748  10663     35   -207     31  A    O  
ATOM   1576  CB  ILE A 215      21.798  39.748 470.206  1.00 33.58      A    C  
ANISOU 1576  CB  ILE A 215     3493   1863   7403    134    -13     62  A    C  
ATOM   1577  CG1 ILE A 215      20.915  38.511 470.300  1.00 40.30      A    C  
ANISOU 1577  CG1 ILE A 215     4492   2764   8059    158    -45     25  A    C  
ATOM   1578  CG2 ILE A 215      22.817  39.616 469.102  1.00 50.18      A    C  
ANISOU 1578  CG2 ILE A 215     5504   3898   9662    166    179    133  A    C  
ATOM   1579  CD1 ILE A 215      19.613  38.679 469.597  1.00 46.28      A    C  
ANISOU 1579  CD1 ILE A 215     5376   3557   8652    152      6     40  A    C  
ATOM   1580  N   ILE A 216      24.609  41.164 471.504  1.00 47.73      A    N  
ANISOU 1580  N   ILE A 216     4850   3495   9791     66   -194     60  A    N  
ATOM   1581  CA  ILE A 216      25.525  42.292 471.364  1.00 45.50      A    C  
ANISOU 1581  CA  ILE A 216     4380   3127   9779     16   -174    100  A    C  
ATOM   1582  C   ILE A 216      26.425  42.021 470.167  1.00 39.61      A    C  
ANISOU 1582  C   ILE A 216     3495   2318   9238     41     75    199  A    C  
ATOM   1583  O   ILE A 216      27.454  41.358 470.332  1.00 50.11      A    O  
ANISOU 1583  O   ILE A 216     4660   3591  10788     67     63    204  A    O  
ATOM   1584  CB  ILE A 216      26.362  42.481 472.631  1.00 39.55      A    C  
ANISOU 1584  CB  ILE A 216     3498   2312   9216    -17   -432     35  A    C  
ATOM   1585  CG1 ILE A 216      25.470  42.738 473.820  1.00 38.63      A    C  
ANISOU 1585  CG1 ILE A 216     3564   2240   8875    -30   -645    -65  A    C  
ATOM   1586  CG2 ILE A 216      27.311  43.623 472.481  1.00 65.16      A    C  
ANISOU 1586  CG2 ILE A 216     6530   5458  12769    -77   -427     75  A    C  
ATOM   1587  CD1 ILE A 216      26.243  42.758 475.091  1.00 40.01      A    C  
ANISOU 1587  CD1 ILE A 216     3673   2342   9186    -49   -927   -136  A    C  
ATOM   1588  N   PRO A 217      26.070  42.454 468.950  1.00 39.63      A    N  
ANISOU 1588  N   PRO A 217     3569   2314   9175     46    311    285  A    N  
ATOM   1589  CA  PRO A 217      26.853  42.048 467.763  1.00 41.05      A    C  
ANISOU 1589  CA  PRO A 217     3670   2420   9506     90    601    382  A    C  
ATOM   1590  C   PRO A 217      28.209  42.713 467.642  1.00 45.86      A    C  
ANISOU 1590  C   PRO A 217     3997   2910  10517     45    697    455  A    C  
ATOM   1591  O   PRO A 217      29.016  42.286 466.804  1.00 45.04      A    O  
ANISOU 1591  O   PRO A 217     3789   2728  10596     91    959    533  A    O  
ATOM   1592  CB  PRO A 217      25.941  42.430 466.588  1.00 40.55      A    C  
ANISOU 1592  CB  PRO A 217     3820   2372   9214    104    794    457  A    C  
ATOM   1593  CG  PRO A 217      24.552  42.427 467.191  1.00 38.42      A    C  
ANISOU 1593  CG  PRO A 217     3740   2209   8649     97    582    373  A    C  
ATOM   1594  CD  PRO A 217      24.743  42.973 468.573  1.00 38.27      A    C  
ANISOU 1594  CD  PRO A 217     3607   2204   8728     41    330    291  A    C  
ATOM   1595  N   ASP A 218      28.471  43.772 468.398  1.00 51.43      A    N  
ANISOU 1595  N   ASP A 218     4578   3589  11373    -37    515    434  A    N  
ATOM   1596  CA  ASP A 218      29.730  44.489 468.251  1.00 50.25      A    C  
ANISOU 1596  CA  ASP A 218     4143   3322  11629    -91    596    508  A    C  
ATOM   1597  C   ASP A 218      29.905  45.383 469.469  1.00 54.69      A    C  
ANISOU 1597  C   ASP A 218     4614   3868  12299   -159    272    426  A    C  
ATOM   1598  O   ASP A 218      29.183  46.378 469.606  1.00 54.34      A    O  
ANISOU 1598  O   ASP A 218     4703   3851  12092   -198    204    408  A    O  
ATOM   1599  CB  ASP A 218      29.717  45.290 466.960  1.00 47.70      A    C  
ANISOU 1599  CB  ASP A 218     3856   2955  11312   -112    916    650  A    C  
ATOM   1600  CG  ASP A 218      31.082  45.702 466.525  1.00 50.73      A    C  
ANISOU 1600  CG  ASP A 218     3942   3220  12112   -144   1110    756  A    C  
ATOM   1601  OD1 ASP A 218      31.997  45.748 467.369  1.00 52.08      A    O  
ANISOU 1601  OD1 ASP A 218     3855   3335  12599   -166    920    708  A    O  
ATOM   1602  OD2 ASP A 218      31.240  45.930 465.313  1.00 51.99      A    O1-
ANISOU 1602  OD2 ASP A 218     4140   3342  12273   -137   1458    892  A    O1-
ATOM   1603  N   VAL A 219      30.835  45.026 470.356  1.00 51.99      A    N  
ANISOU 1603  N   VAL A 219     4062   3467  12224   -163     63    372  A    N  
ATOM   1604  CA  VAL A 219      31.107  45.880 471.507  1.00 58.27      A    C  
ANISOU 1604  CA  VAL A 219     4793   4221  13125   -217   -259    291  A    C  
ATOM   1605  C   VAL A 219      31.507  47.288 471.091  1.00 61.79      A    C  
ANISOU 1605  C   VAL A 219     5134   4590  13755   -280   -172    360  A    C  
ATOM   1606  O   VAL A 219      31.355  48.229 471.874  1.00 65.91      A    O  
ANISOU 1606  O   VAL A 219     5705   5086  14254   -327   -398    288  A    O  
ATOM   1607  CB  VAL A 219      32.194  45.270 472.416  1.00 50.95      A    C  
ANISOU 1607  CB  VAL A 219     3643   3214  12502   -201   -512    243  A    C  
ATOM   1608  CG1 VAL A 219      31.744  43.927 472.945  1.00 63.75      A    C  
ANISOU 1608  CG1 VAL A 219     5404   4903  13915   -142   -634    174  A    C  
ATOM   1609  CG2 VAL A 219      33.513  45.167 471.672  1.00 53.64      A    C  
ANISOU 1609  CG2 VAL A 219     3656   3435  13290   -184   -307    357  A    C  
ATOM   1610  N   ASN A 220      32.043  47.457 469.888  1.00 63.20      A    N  
ANISOU 1610  N   ASN A 220     5186   4716  14112   -280    160    499  A    N  
ATOM   1611  CA  ASN A 220      32.538  48.752 469.458  1.00 69.29      A    C  
ANISOU 1611  CA  ASN A 220     5851   5396  15080   -339    259    584  A    C  
ATOM   1612  C   ASN A 220      31.586  49.457 468.513  1.00 67.04      A    C  
ANISOU 1612  C   ASN A 220     5789   5154  14529   -358    480    663  A    C  
ATOM   1613  O   ASN A 220      31.902  50.557 468.045  1.00 55.43      A    O  
ANISOU 1613  O   ASN A 220     4265   3605  13192   -409    587    750  A    O  
ATOM   1614  CB  ASN A 220      33.903  48.594 468.800  1.00 57.62      A    C  
ANISOU 1614  CB  ASN A 220     4078   3806  14010   -325    485    701  A    C  
ATOM   1615  CG  ASN A 220      34.917  48.050 469.748  1.00 61.04      A    C  
ANISOU 1615  CG  ASN A 220     4278   4160  14754   -301    228    634  A    C  
ATOM   1616  ND2 ASN A 220      35.655  47.046 469.305  1.00 85.68      A    N  
ANISOU 1616  ND2 ASN A 220     7238   7237  18080   -235    407    689  A    N  
ATOM   1617  OD1 ASN A 220      35.020  48.499 470.886  1.00 59.59      A    O  
ANISOU 1617  OD1 ASN A 220     4084   3943  14612   -336   -136    531  A    O  
ATOM   1618  N   ALA A 221      30.418  48.882 468.250  1.00 50.96      A    N  
ANISOU 1618  N   ALA A 221     4013   3227  12124   -314    528    638  A    N  
ATOM   1619  CA  ALA A 221      29.417  49.625 467.503  1.00 60.40      A    C  
ANISOU 1619  CA  ALA A 221     5438   4450  13061   -322    657    703  A    C  
ATOM   1620  C   ALA A 221      28.954  50.827 468.326  1.00 58.90      A    C  
ANISOU 1620  C   ALA A 221     5313   4237  12831   -372    411    622  A    C  
ATOM   1621  O   ALA A 221      28.840  50.756 469.556  1.00 49.43      A    O  
ANISOU 1621  O   ALA A 221     4117   3057  11608   -376    122    479  A    O  
ATOM   1622  CB  ALA A 221      28.241  48.732 467.134  1.00 47.55      A    C  
ANISOU 1622  CB  ALA A 221     4071   2933  11062   -254    711    682  A    C  
ATOM   1623  N   GLU A 222      28.725  51.943 467.632  1.00 61.79      A    N  
ANISOU 1623  N   GLU A 222     5743   4544  13190   -406    537    721  A    N  
ATOM   1624  CA  GLU A 222      28.342  53.202 468.259  1.00 51.53      A    C  
ANISOU 1624  CA  GLU A 222     4504   3188  11886   -451    348    661  A    C  
ATOM   1625  C   GLU A 222      26.843  53.204 468.502  1.00 49.08      A    C  
ANISOU 1625  C   GLU A 222     4462   2965  11221   -401    252    584  A    C  
ATOM   1626  O   GLU A 222      26.074  53.132 467.534  1.00 52.35      A    O  
ANISOU 1626  O   GLU A 222     5036   3415  11439   -361    421    679  A    O  
ATOM   1627  CB  GLU A 222      28.715  54.372 467.353  1.00 57.27      A    C  
ANISOU 1627  CB  GLU A 222     5194   3801  12767   -506    534    813  A    C  
ATOM   1628  CG  GLU A 222      28.568  55.767 467.969  1.00 71.37      A    C  
ANISOU 1628  CG  GLU A 222     7004   5483  14629   -563    351    760  A    C  
ATOM   1629  CD  GLU A 222      28.666  56.889 466.928  1.00 89.02      A    C  
ANISOU 1629  CD  GLU A 222     9268   7609  16948   -609    554    930  A    C  
ATOM   1630  OE1 GLU A 222      28.162  56.706 465.792  1.00 82.18      A    O  
ANISOU 1630  OE1 GLU A 222     8545   6777  15904   -571    786   1067  A    O  
ATOM   1631  OE2 GLU A 222      29.242  57.960 467.248  1.00103.11      A    O1-
ANISOU 1631  OE2 GLU A 222    10949   9260  18967   -683    471    930  A    O1-
ATOM   1632  N   PRO A 223      26.378  53.285 469.752  1.00 48.15      A    N  
ANISOU 1632  N   PRO A 223     4410   2873  11011   -393    -10    420  A    N  
ATOM   1633  CA  PRO A 223      24.927  53.270 469.982  1.00 46.10      A    C  
ANISOU 1633  CA  PRO A 223     4386   2692  10440   -333    -68    352  A    C  
ATOM   1634  C   PRO A 223      24.267  54.455 469.312  1.00 62.14      A    C  
ANISOU 1634  C   PRO A 223     6526   4656  12429   -333     16    434  A    C  
ATOM   1635  O   PRO A 223      24.873  55.514 469.139  1.00 87.56      A    O  
ANISOU 1635  O   PRO A 223     9665   7753  15850   -393     34    489  A    O  
ATOM   1636  CB  PRO A 223      24.796  53.339 471.509  1.00 45.88      A    C  
ANISOU 1636  CB  PRO A 223     4392   2664  10378   -335   -338    168  A    C  
ATOM   1637  CG  PRO A 223      26.102  53.821 472.008  1.00 48.20      A    C  
ANISOU 1637  CG  PRO A 223     4493   2848  10972   -408   -455    148  A    C  
ATOM   1638  CD  PRO A 223      27.143  53.403 471.003  1.00 49.25      A    C  
ANISOU 1638  CD  PRO A 223     4425   2961  11327   -432   -260    295  A    C  
ATOM   1639  N   GLN A 224      23.020  54.258 468.904  1.00 52.45      A    N  
ANISOU 1639  N   GLN A 224     5478   3497  10953   -263     61    450  A    N  
ATOM   1640  CA  GLN A 224      22.237  55.326 468.290  1.00 47.21      A    C  
ANISOU 1640  CA  GLN A 224     4936   2767  10236   -242    111    529  A    C  
ATOM   1641  C   GLN A 224      21.177  55.800 469.271  1.00 49.93      A    C  
ANISOU 1641  C   GLN A 224     5391   3116  10464   -193    -56    385  A    C  
ATOM   1642  O   GLN A 224      20.374  54.984 469.743  1.00 53.51      A    O  
ANISOU 1642  O   GLN A 224     5918   3677  10738   -133   -111    296  A    O  
ATOM   1643  CB  GLN A 224      21.591  54.862 466.991  1.00 45.14      A    C  
ANISOU 1643  CB  GLN A 224     4795   2552   9806   -187    277    673  A    C  
ATOM   1644  CG  GLN A 224      22.575  54.220 466.035  1.00 55.63      A    C  
ANISOU 1644  CG  GLN A 224     6049   3878  11211   -218    481    805  A    C  
ATOM   1645  CD  GLN A 224      23.663  55.165 465.587  1.00 70.97      A    C  
ANISOU 1645  CD  GLN A 224     7872   5692  13402   -297    598    920  A    C  
ATOM   1646  NE2 GLN A 224      24.906  54.734 465.743  1.00 78.81      A    N  
ANISOU 1646  NE2 GLN A 224     8667   6671  14606   -348    660    920  A    N  
ATOM   1647  OE1 GLN A 224      23.398  56.260 465.091  1.00 82.49      A    O  
ANISOU 1647  OE1 GLN A 224     9407   7056  14879   -308    635   1015  A    O  
ATOM   1648  N   PRO A 225      21.158  57.074 469.646  1.00 55.80      A    N  
ANISOU 1648  N   PRO A 225     6149   3738  11315   -215   -128    352  A    N  
ATOM   1649  CA  PRO A 225      20.156  57.552 470.606  1.00 63.14      A    C  
ANISOU 1649  CA  PRO A 225     7193   4653  12143   -156   -257    207  A    C  
ATOM   1650  C   PRO A 225      18.778  57.717 469.984  1.00 45.59      A    C  
ANISOU 1650  C   PRO A 225     5096   2457   9768    -59   -198    265  A    C  
ATOM   1651  O   PRO A 225      18.628  57.908 468.778  1.00 45.98      A    O  
ANISOU 1651  O   PRO A 225     5173   2485   9812    -47    -86    430  A    O  
ATOM   1652  CB  PRO A 225      20.716  58.906 471.054  1.00 52.89      A    C  
ANISOU 1652  CB  PRO A 225     5870   3187  11039   -214   -338    168  A    C  
ATOM   1653  CG  PRO A 225      21.606  59.317 469.949  1.00 50.16      A    C  
ANISOU 1653  CG  PRO A 225     5424   2766  10867   -286   -209    348  A    C  
ATOM   1654  CD  PRO A 225      22.191  58.084 469.369  1.00 49.07      A    C  
ANISOU 1654  CD  PRO A 225     5194   2741  10709   -301    -99    428  A    C  
ATOM   1655  N   LEU A 226      17.760  57.639 470.845  1.00 44.80      A    N  
ANISOU 1655  N   LEU A 226     5076   2395   9550     17   -276    129  A    N  
ATOM   1656  CA  LEU A 226      16.390  57.950 470.437  1.00 59.11      A    C  
ANISOU 1656  CA  LEU A 226     6976   4212  11272    121   -248    164  A    C  
ATOM   1657  C   LEU A 226      16.178  59.461 470.354  1.00 64.43      A    C  
ANISOU 1657  C   LEU A 226     7695   4723  12063    140   -267    184  A    C  
ATOM   1658  O   LEU A 226      16.466  60.198 471.306  1.00 66.75      A    O  
ANISOU 1658  O   LEU A 226     8005   4918  12439    119   -344     58  A    O  
ATOM   1659  CB  LEU A 226      15.377  57.332 471.406  1.00 43.39      A    C  
ANISOU 1659  CB  LEU A 226     5031   2307   9148    200   -294     16  A    C  
ATOM   1660  CG  LEU A 226      15.465  55.826 471.674  1.00 53.88      A    C  
ANISOU 1660  CG  LEU A 226     6334   3783  10354    186   -290    -22  A    C  
ATOM   1661  CD1 LEU A 226      14.472  55.391 472.729  1.00 45.56      A    C  
ANISOU 1661  CD1 LEU A 226     5336   2781   9193    260   -319   -167  A    C  
ATOM   1662  CD2 LEU A 226      15.222  55.056 470.397  1.00 40.52      A    C  
ANISOU 1662  CD2 LEU A 226     4627   2172   8597    198   -210    130  A    C  
ATOM   1663  N   HIS A 227      15.666  59.916 469.218  1.00 47.27      A    N  
ANISOU 1663  N   HIS A 227     5561   2507   9891    184   -207    343  A    N  
ATOM   1664  CA  HIS A 227      15.358  61.315 469.008  1.00 49.34      A    C  
ANISOU 1664  CA  HIS A 227     5879   2607  10260    217   -222    386  A    C  
ATOM   1665  C   HIS A 227      13.864  61.564 469.091  1.00 57.10      A    C  
ANISOU 1665  C   HIS A 227     6920   3596  11181    358   -253    354  A    C  
ATOM   1666  O   HIS A 227      13.054  60.726 468.679  1.00 48.05      A    O  
ANISOU 1666  O   HIS A 227     5769   2568   9920    425   -241    395  A    O  
ATOM   1667  CB  HIS A 227      15.892  61.797 467.665  1.00 72.60      A    C  
ANISOU 1667  CB  HIS A 227     8844   5470  13270    170   -138    605  A    C  
ATOM   1668  CG  HIS A 227      17.377  61.933 467.641  1.00 72.14      A    C  
ANISOU 1668  CG  HIS A 227     8702   5357  13352     33    -93    639  A    C  
ATOM   1669  CD2 HIS A 227      18.353  61.038 467.368  1.00 74.07      A    C  
ANISOU 1669  CD2 HIS A 227     8858   5682  13604    -47    -20    683  A    C  
ATOM   1670  ND1 HIS A 227      18.013  63.113 467.950  1.00 53.77      A    N  
ANISOU 1670  ND1 HIS A 227     6358   2862  11212    -32   -125    623  A    N  
ATOM   1671  CE1 HIS A 227      19.318  62.942 467.864  1.00 65.49      A    C  
ANISOU 1671  CE1 HIS A 227     7727   4329  12825   -151    -79    662  A    C  
ATOM   1672  NE2 HIS A 227      19.552  61.693 467.511  1.00 67.68      A    N  
ANISOU 1672  NE2 HIS A 227     7957   4759  13001   -156     -8    699  A    N  
ATOM   1673  N   MET A 228      13.500  62.720 469.632  1.00 51.08      A    N  
ANISOU 1673  N   MET A 228     6202   2694  10513    407   -295    279  A    N  
ATOM   1674  CA  MET A 228      12.092  63.075 469.684  1.00 54.22      A    C  
ANISOU 1674  CA  MET A 228     6631   3076  10893    556   -311    255  A    C  
ATOM   1675  C   MET A 228      11.632  63.529 468.305  1.00 52.62      A    C  
ANISOU 1675  C   MET A 228     6464   2820  10711    607   -304    470  A    C  
ATOM   1676  O   MET A 228      12.269  64.365 467.671  1.00 54.22      A    O  
ANISOU 1676  O   MET A 228     6714   2890  10999    553   -289    591  A    O  
ATOM   1677  CB  MET A 228      11.852  64.149 470.729  1.00 53.38      A    C  
ANISOU 1677  CB  MET A 228     6577   2825  10879    606   -345     96  A    C  
ATOM   1678  CG  MET A 228      10.426  64.586 470.846  1.00 54.32      A    C  
ANISOU 1678  CG  MET A 228     6710   2914  11014    773   -343     64  A    C  
ATOM   1679  SD  MET A 228      10.188  65.525 472.367  1.00 67.29      A    S  
ANISOU 1679  SD  MET A 228     8439   4409  12718    841   -350   -182  A    S  
ATOM   1680  CE  MET A 228      10.899  64.434 473.591  1.00 74.22      A    C  
ANISOU 1680  CE  MET A 228     9331   5406  13465    752   -355   -366  A    C  
ATOM   1681  N   ILE A 229      10.569  62.916 467.810  1.00 56.03      A    N  
ANISOU 1681  N   ILE A 229     6876   3352  11061    705   -319    528  A    N  
ATOM   1682  CA  ILE A 229      10.049  63.247 466.495  1.00 53.02      A    C  
ANISOU 1682  CA  ILE A 229     6550   2924  10673    768   -347    735  A    C  
ATOM   1683  C   ILE A 229       8.906  64.224 466.712  1.00 58.37      A    C  
ANISOU 1683  C   ILE A 229     7226   3499  11451    912   -404    706  A    C  
ATOM   1684  O   ILE A 229       8.959  65.390 466.300  1.00 57.10      A    O  
ANISOU 1684  O   ILE A 229     7138   3171  11385    939   -422    794  A    O  
ATOM   1685  CB  ILE A 229       9.570  61.987 465.764  1.00 51.48      A    C  
ANISOU 1685  CB  ILE A 229     6335   2885  10338    791   -366    821  A    C  
ATOM   1686  CG1 ILE A 229      10.717  60.998 465.630  1.00 49.77      A    C  
ANISOU 1686  CG1 ILE A 229     6121   2760  10031    659   -293    833  A    C  
ATOM   1687  CG2 ILE A 229       9.027  62.336 464.394  1.00 53.03      A    C  
ANISOU 1687  CG2 ILE A 229     6623   3021  10503    863   -427   1041  A    C  
ATOM   1688  CD1 ILE A 229      11.829  61.496 464.764  1.00 67.89      A    C  
ANISOU 1688  CD1 ILE A 229     8499   4954  12344    567   -223    992  A    C  
ATOM   1689  N   HIS A 230       7.856  63.734 467.348  1.00 62.37      A    N  
ANISOU 1689  N   HIS A 230     7645   4102  11952   1010   -422    588  A    N  
ATOM   1690  CA  HIS A 230       6.736  64.539 467.784  1.00 56.05      A    C  
ANISOU 1690  CA  HIS A 230     6809   3221  11267   1159   -447    521  A    C  
ATOM   1691  C   HIS A 230       6.731  64.545 469.303  1.00 64.59      A    C  
ANISOU 1691  C   HIS A 230     7865   4307  12369   1168   -380    279  A    C  
ATOM   1692  O   HIS A 230       7.363  63.711 469.958  1.00 64.48      A    O  
ANISOU 1692  O   HIS A 230     7845   4392  12263   1075   -340    175  A    O  
ATOM   1693  CB  HIS A 230       5.431  63.990 467.216  1.00 56.14      A    C  
ANISOU 1693  CB  HIS A 230     6725   3331  11276   1278   -514    597  A    C  
ATOM   1694  CG  HIS A 230       5.324  64.151 465.735  1.00 57.13      A    C  
ANISOU 1694  CG  HIS A 230     6918   3419  11369   1296   -611    836  A    C  
ATOM   1695  CD2 HIS A 230       5.038  65.231 464.974  1.00 59.61      A    C  
ANISOU 1695  CD2 HIS A 230     7309   3584  11757   1373   -679    979  A    C  
ATOM   1696  ND1 HIS A 230       5.578  63.119 464.856  1.00 55.74      A    N  
ANISOU 1696  ND1 HIS A 230     6771   3356  11052   1234   -647    958  A    N  
ATOM   1697  CE1 HIS A 230       5.422  63.550 463.618  1.00 57.40      A    C  
ANISOU 1697  CE1 HIS A 230     7086   3489  11233   1276   -736   1167  A    C  
ATOM   1698  NE2 HIS A 230       5.091  64.828 463.663  1.00 59.74      A    N  
ANISOU 1698  NE2 HIS A 230     7410   3629  11661   1359   -760   1188  A    N  
ATOM   1699  N   LYS A 231       5.982  65.414 469.843  1.00 64.88      A    N  
ANISOU 1699  N   LYS A 231     7900   4238  12514   1291   -369    194  A    N  
ATOM   1700  CA  LYS A 231       6.062  65.579 471.284  1.00 60.03      A    C  
ANISOU 1700  CA  LYS A 231     7320   3589  11900   1308   -298    -37  A    C  
ATOM   1701  C   LYS A 231       5.141  64.583 471.990  1.00 63.42      A    C  
ANISOU 1701  C   LYS A 231     7647   4173  12277   1384   -228   -151  A    C  
ATOM   1702  O   LYS A 231       3.981  64.420 471.588  1.00 57.56      A    O  
ANISOU 1702  O   LYS A 231     6786   3483  11601   1499   -232    -90  A    O  
ATOM   1703  CB  LYS A 231       5.697  67.005 471.652  1.00 60.90      A    C  
ANISOU 1703  CB  LYS A 231     7499   3493  12146   1417   -293    -99  A    C  
ATOM   1704  CG  LYS A 231       6.214  67.474 472.981  1.00 72.33      A    C  
ANISOU 1704  CG  LYS A 231     9064   4836  13582   1400   -247   -320  A    C  
ATOM   1705  CD  LYS A 231       5.143  67.256 474.029  1.00 80.44      A    C  
ANISOU 1705  CD  LYS A 231    10064   5902  14595   1551   -145   -497  A    C  
ATOM   1706  CE  LYS A 231       5.317  68.130 475.257  1.00 90.82      A    C  
ANISOU 1706  CE  LYS A 231    11542   7045  15919   1605    -98   -713  A    C  
ATOM   1707  NZ  LYS A 231       4.098  68.029 476.128  1.00 96.34      A    N1+
ANISOU 1707  NZ  LYS A 231    12216   7770  16620   1790     38   -863  A    N1+
ATOM   1708  N   PRO A 232       5.636  63.860 472.988  1.00 55.57      A    N  
ANISOU 1708  N   PRO A 232     6690   3252  11173   1317   -171   -302  A    N  
ATOM   1709  CA  PRO A 232       4.779  62.949 473.744  1.00 62.21      A    C  
ANISOU 1709  CA  PRO A 232     7451   4219  11967   1389    -77   -413  A    C  
ATOM   1710  C   PRO A 232       4.066  63.584 474.928  1.00 57.12      A    C  
ANISOU 1710  C   PRO A 232     6853   3484  11366   1531     35   -602  A    C  
ATOM   1711  O   PRO A 232       4.572  64.478 475.602  1.00 58.58      A    O  
ANISOU 1711  O   PRO A 232     7190   3518  11550   1538     38   -721  A    O  
ATOM   1712  CB  PRO A 232       5.774  61.882 474.228  1.00 52.65      A    C  
ANISOU 1712  CB  PRO A 232     6294   3112  10600   1247    -75   -475  A    C  
ATOM   1713  CG  PRO A 232       7.034  62.594 474.371  1.00 53.05      A    C  
ANISOU 1713  CG  PRO A 232     6474   3041  10641   1143   -139   -500  A    C  
ATOM   1714  CD  PRO A 232       7.060  63.640 473.283  1.00 54.38      A    C  
ANISOU 1714  CD  PRO A 232     6634   3093  10933   1155   -202   -341  A    C  
ATOM   1715  N   GLN A 233       2.874  63.056 475.200  1.00 57.52      A    N  
ANISOU 1715  N   GLN A 233     6771   3628  11456   1646    136   -634  A    N  
ATOM   1716  CA  GLN A 233       2.130  63.434 476.396  1.00 68.97      A    C  
ANISOU 1716  CA  GLN A 233     8258   5021  12926   1791    295   -822  A    C  
ATOM   1717  C   GLN A 233       2.837  63.030 477.680  1.00 59.17      A    C  
ANISOU 1717  C   GLN A 233     7200   3776  11505   1740    371  -1018  A    C  
ATOM   1718  O   GLN A 233       2.486  63.531 478.747  1.00 73.21      A    O  
ANISOU 1718  O   GLN A 233     9095   5464  13255   1854    496  -1199  A    O  
ATOM   1719  CB  GLN A 233       0.736  62.816 476.366  1.00 72.59      A    C  
ANISOU 1719  CB  GLN A 233     8497   5602  13484   1906    407   -796  A    C  
ATOM   1720  CG  GLN A 233       0.180  62.717 474.972  1.00 86.17      A    C  
ANISOU 1720  CG  GLN A 233    10026   7377  15338   1906    275   -579  A    C  
ATOM   1721  CD  GLN A 233      -1.272  62.319 474.955  1.00 88.23      A    C  
ANISOU 1721  CD  GLN A 233    10046   7728  15751   2027    362   -555  A    C  
ATOM   1722  NE2 GLN A 233      -1.568  61.151 474.367  1.00 78.96      A    N  
ANISOU 1722  NE2 GLN A 233     8714   6709  14578   1953    310   -446  A    N  
ATOM   1723  OE1 GLN A 233      -2.128  63.059 475.454  1.00 86.30      A    O  
ANISOU 1723  OE1 GLN A 233     9748   7408  15634   2185    473   -632  A    O  
ATOM   1724  N   ASN A 234       3.780  62.101 477.612  1.00 82.93      A    N  
ANISOU 1724  N   ASN A 234    10248   6878  14384   1581    302   -991  A    N  
ATOM   1725  CA  ASN A 234       4.548  61.647 478.764  1.00 67.36      A    C  
ANISOU 1725  CA  ASN A 234     8461   4900  12233   1519    331  -1161  A    C  
ATOM   1726  C   ASN A 234       6.023  61.762 478.435  1.00 60.87      A    C  
ANISOU 1726  C   ASN A 234     7733   4034  11360   1345    157  -1113  A    C  
ATOM   1727  O   ASN A 234       6.472  61.275 477.391  1.00 67.89      A    O  
ANISOU 1727  O   ASN A 234     8510   5010  12275   1238     67   -941  A    O  
ATOM   1728  CB  ASN A 234       4.208  60.206 479.147  1.00 75.16      A    C  
ANISOU 1728  CB  ASN A 234     9383   6055  13121   1499    433  -1182  A    C  
ATOM   1729  CG  ASN A 234       5.250  59.600 480.070  1.00 84.69      A    C  
ANISOU 1729  CG  ASN A 234    10785   7260  14132   1396    399  -1310  A    C  
ATOM   1730  ND2 ASN A 234       5.996  58.594 479.568  1.00 81.22      A    N  
ANISOU 1730  ND2 ASN A 234    10294   6930  13637   1252    298  -1207  A    N  
ATOM   1731  OD1 ASN A 234       5.391  60.029 481.219  1.00 71.32      A    O  
ANISOU 1731  OD1 ASN A 234     9303   5463  12332   1450    453  -1503  A    O  
ATOM   1732  N   THR A 235       6.768  62.427 479.303  1.00 56.35      A    N  
ANISOU 1732  N   THR A 235     7365   3321  10726   1319    113  -1264  A    N  
ATOM   1733  CA  THR A 235       8.155  62.748 479.007  1.00 55.84      A    C  
ANISOU 1733  CA  THR A 235     7357   3191  10670   1156    -52  -1218  A    C  
ATOM   1734  C   THR A 235       9.165  61.753 479.578  1.00 57.68      A    C  
ANISOU 1734  C   THR A 235     7659   3500  10756   1023   -126  -1278  A    C  
ATOM   1735  O   THR A 235      10.361  61.893 479.308  1.00 53.92      A    O  
ANISOU 1735  O   THR A 235     7186   2991  10311    880   -262  -1228  A    O  
ATOM   1736  CB  THR A 235       8.456  64.153 479.530  1.00 58.62      A    C  
ANISOU 1736  CB  THR A 235     7874   3320  11079   1186    -95  -1336  A    C  
ATOM   1737  CG2 THR A 235       7.314  65.077 479.163  1.00 73.88      A    C  
ANISOU 1737  CG2 THR A 235     9755   5169  13146   1352     -5  -1305  A    C  
ATOM   1738  OG1 THR A 235       8.539  64.115 480.958  1.00 60.92      A    O  
ANISOU 1738  OG1 THR A 235     8385   3544  11217   1225    -61  -1572  A    O  
ATOM   1739  N   GLU A 236       8.726  60.752 480.338  1.00 53.69      A    N  
ANISOU 1739  N   GLU A 236     7200   3092  10109   1066    -37  -1375  A    N  
ATOM   1740  CA  GLU A 236       9.656  59.796 480.932  1.00 61.44      A    C  
ANISOU 1740  CA  GLU A 236     8265   4132  10946    951   -122  -1433  A    C  
ATOM   1741  C   GLU A 236      10.193  58.798 479.911  1.00 62.09      A    C  
ANISOU 1741  C   GLU A 236     8166   4367  11057    831   -186  -1244  A    C  
ATOM   1742  O   GLU A 236       9.532  58.463 478.922  1.00 77.77      A    O  
ANISOU 1742  O   GLU A 236     9984   6451  13116    860   -121  -1093  A    O  
ATOM   1743  CB  GLU A 236       8.995  59.040 482.078  1.00 65.57      A    C  
ANISOU 1743  CB  GLU A 236     8921   4694  11297   1041      8  -1597  A    C  
ATOM   1744  CG  GLU A 236       8.424  59.932 483.146  1.00 76.80      A    C  
ANISOU 1744  CG  GLU A 236    10555   5971  12653   1179    110  -1803  A    C  
ATOM   1745  CD  GLU A 236       7.456  59.198 484.045  1.00 90.04      A    C  
ANISOU 1745  CD  GLU A 236    12317   7711  14185   1304    324  -1932  A    C  
ATOM   1746  OE1 GLU A 236       7.608  57.962 484.193  1.00 93.85      A    O  
ANISOU 1746  OE1 GLU A 236    12779   8311  14568   1243    336  -1911  A    O  
ATOM   1747  OE2 GLU A 236       6.541  59.859 484.590  1.00 92.42      A    O1-
ANISOU 1747  OE2 GLU A 236    12698   7940  14478   1465    496  -2049  A    O1-
ATOM   1748  N   ALA A 237      11.415  58.326 480.174  1.00 62.73      A    N  
ANISOU 1748  N   ALA A 237     8292   4461  11081    699   -323  -1257  A    N  
ATOM   1749  CA  ALA A 237      12.124  57.429 479.266  1.00 53.42      A    C  
ANISOU 1749  CA  ALA A 237     6960   3408   9929    585   -382  -1092  A    C  
ATOM   1750  C   ALA A 237      11.350  56.134 479.072  1.00 54.34      A    C  
ANISOU 1750  C   ALA A 237     7005   3675   9966    624   -279  -1040  A    C  
ATOM   1751  O   ALA A 237      10.798  55.565 480.019  1.00 59.86      A    O  
ANISOU 1751  O   ALA A 237     7805   4389  10548    685   -209  -1165  A    O  
ATOM   1752  CB  ALA A 237      13.515  57.107 479.816  1.00 47.02      A    C  
ANISOU 1752  CB  ALA A 237     6205   2578   9081    460   -545  -1143  A    C  
ATOM   1753  N   VAL A 238      11.348  55.649 477.863  1.00 51.88      A    N  
ANISOU 1753  N   VAL A 238     6535   3464   9713    584   -267   -863  A    N  
ATOM   1754  CA  VAL A 238      10.558  54.473 477.558  1.00 42.10      A    C  
ANISOU 1754  CA  VAL A 238     5217   2354   8425    614   -180   -804  A    C  
ATOM   1755  C   VAL A 238      11.419  53.245 477.806  1.00 56.57      A    C  
ANISOU 1755  C   VAL A 238     7071   4263  10159    519   -244   -801  A    C  
ATOM   1756  O   VAL A 238      12.621  53.231 477.524  1.00 67.36      A    O  
ANISOU 1756  O   VAL A 238     8420   5627  11547    421   -348   -753  A    O  
ATOM   1757  CB  VAL A 238      10.027  54.533 476.116  1.00 41.39      A    C  
ANISOU 1757  CB  VAL A 238     4975   2321   8430    629   -153   -624  A    C  
ATOM   1758  CG1 VAL A 238       9.105  53.381 475.844  1.00 52.52      A    C  
ANISOU 1758  CG1 VAL A 238     6299   3844   9812    662    -82   -576  A    C  
ATOM   1759  CG2 VAL A 238       9.294  55.823 475.886  1.00 43.04      A    C  
ANISOU 1759  CG2 VAL A 238     5169   2435   8749    724   -123   -619  A    C  
ATOM   1760  N   ASN A 239      10.798  52.227 478.381  1.00 55.19      A    N  
ANISOU 1760  N   ASN A 239     6928   4146   9896    552   -172   -855  A    N  
ATOM   1761  CA  ASN A 239      11.433  50.953 478.669  1.00 49.57      A    C  
ANISOU 1761  CA  ASN A 239     6248   3498   9087    477   -226   -851  A    C  
ATOM   1762  C   ASN A 239      11.592  50.171 477.368  1.00 49.76      A    C  
ANISOU 1762  C   ASN A 239     6128   3630   9149    421   -228   -677  A    C  
ATOM   1763  O   ASN A 239      10.623  49.997 476.625  1.00 60.92      A    O  
ANISOU 1763  O   ASN A 239     7444   5091  10610    465   -147   -597  A    O  
ATOM   1764  CB  ASN A 239      10.545  50.216 479.680  1.00 39.52      A    C  
ANISOU 1764  CB  ASN A 239     5069   2288   7657    529   -110   -940  A    C  
ATOM   1765  CG  ASN A 239      11.185  48.995 480.280  1.00 38.89      A    C  
ANISOU 1765  CG  ASN A 239     5083   2300   7393    453   -173   -941  A    C  
ATOM   1766  ND2 ASN A 239      10.951  48.792 481.556  1.00 40.14      A    N  
ANISOU 1766  ND2 ASN A 239     5425   2471   7355    481   -130  -1055  A    N  
ATOM   1767  OD1 ASN A 239      11.890  48.252 479.616  1.00 37.54      A    O  
ANISOU 1767  OD1 ASN A 239     4834   2179   7249    378   -253   -839  A    O  
ATOM   1768  N   LEU A 240      12.808  49.710 477.076  1.00 36.67      A    N  
ANISOU 1768  N   LEU A 240     4454   2001   7478    330   -323   -622  A    N  
ATOM   1769  CA  LEU A 240      13.077  49.013 475.822  1.00 39.98      A    C  
ANISOU 1769  CA  LEU A 240     4766   2506   7918    286   -308   -473  A    C  
ATOM   1770  C   LEU A 240      13.381  47.516 475.970  1.00 34.31      A    C  
ANISOU 1770  C   LEU A 240     4062   1858   7115    244   -324   -458  A    C  
ATOM   1771  O   LEU A 240      13.778  46.882 474.984  1.00 39.90      A    O  
ANISOU 1771  O   LEU A 240     4705   2625   7829    208   -313   -353  A    O  
ATOM   1772  CB  LEU A 240      14.238  49.690 475.099  1.00 35.67      A    C  
ANISOU 1772  CB  LEU A 240     4160   1930   7464    228   -356   -398  A    C  
ATOM   1773  CG  LEU A 240      14.369  51.198 475.033  1.00 37.02      A    C  
ANISOU 1773  CG  LEU A 240     4328   2000   7738    238   -371   -408  A    C  
ATOM   1774  CD1 LEU A 240      15.689  51.530 474.367  1.00 37.38      A    C  
ANISOU 1774  CD1 LEU A 240     4296   2015   7891    159   -404   -324  A    C  
ATOM   1775  CD2 LEU A 240      13.184  51.787 474.250  1.00 40.90      A    C  
ANISOU 1775  CD2 LEU A 240     4792   2487   8262    313   -293   -340  A    C  
ATOM   1776  N   SER A 241      13.198  46.930 477.152  1.00 34.57      A    N  
ANISOU 1776  N   SER A 241     4198   1893   7043    251   -339   -556  A    N  
ATOM   1777  CA  SER A 241      13.773  45.620 477.456  1.00 50.57      A    C  
ANISOU 1777  CA  SER A 241     6261   3994   8958    200   -388   -537  A    C  
ATOM   1778  C   SER A 241      13.124  44.438 476.729  1.00 44.12      A    C  
ANISOU 1778  C   SER A 241     5394   3302   8067    187   -307   -441  A    C  
ATOM   1779  O   SER A 241      13.687  43.340 476.770  1.00 61.68      A    O  
ANISOU 1779  O   SER A 241     7639   5566  10230    148   -347   -411  A    O  
ATOM   1780  CB  SER A 241      13.719  45.361 478.964  1.00 55.45      A    C  
ANISOU 1780  CB  SER A 241     7044   4614   9411    210   -427   -648  A    C  
ATOM   1781  OG  SER A 241      12.437  45.572 479.502  1.00 56.68      A    O  
ANISOU 1781  OG  SER A 241     7258   4811   9466    265   -292   -697  A    O  
ATOM   1782  N   SER A 242      11.968  44.604 476.093  1.00 32.65      A    N  
ANISOU 1782  N   SER A 242     3877   1898   6631    218   -215   -398  A    N  
ATOM   1783  CA  SER A 242      11.285  43.470 475.471  1.00 31.93      A    C  
ANISOU 1783  CA  SER A 242     3745   1911   6475    193   -169   -323  A    C  
ATOM   1784  C   SER A 242      11.836  43.058 474.101  1.00 37.67      A    C  
ANISOU 1784  C   SER A 242     4421   2646   7244    165   -200   -228  A    C  
ATOM   1785  O   SER A 242      11.581  41.924 473.664  1.00 35.92      A    O  
ANISOU 1785  O   SER A 242     4204   2491   6951    132   -194   -186  A    O  
ATOM   1786  CB  SER A 242       9.796  43.778 475.344  1.00 32.46      A    C  
ANISOU 1786  CB  SER A 242     3743   2022   6567    234    -85   -314  A    C  
ATOM   1787  OG  SER A 242       9.145  43.437 476.555  1.00 46.52      A    O  
ANISOU 1787  OG  SER A 242     5579   3840   8255    241     -2   -378  A    O  
ATOM   1788  N   GLY A 243      12.524  43.955 473.392  1.00 31.30      A    N  
ANISOU 1788  N   GLY A 243     3581   1764   6547    177   -219   -193  A    N  
ATOM   1789  CA  GLY A 243      13.121  43.655 472.108  1.00 30.96      A    C  
ANISOU 1789  CA  GLY A 243     3518   1720   6524    160   -211   -102  A    C  
ATOM   1790  C   GLY A 243      14.560  43.170 472.234  1.00 51.66      A    C  
ANISOU 1790  C   GLY A 243     6142   4304   9183    127   -230   -105  A    C  
ATOM   1791  O   GLY A 243      15.003  42.678 473.278  1.00 44.55      A    O  
ANISOU 1791  O   GLY A 243     5268   3401   8257    111   -284   -169  A    O  
ATOM   1792  N   VAL A 244      15.299  43.296 471.136  1.00 35.77      A    N  
ANISOU 1792  N   VAL A 244     4102   2267   7222    123   -182    -27  A    N  
ATOM   1793  CA  VAL A 244      16.705  42.916 471.121  1.00 36.76      A    C  
ANISOU 1793  CA  VAL A 244     4185   2380   7403    100   -174    -17  A    C  
ATOM   1794  C   VAL A 244      17.657  44.085 470.927  1.00 35.81      A    C  
ANISOU 1794  C   VAL A 244     3983   2201   7421     83   -154     15  A    C  
ATOM   1795  O   VAL A 244      18.859  43.920 471.195  1.00 46.25      A    O  
ANISOU 1795  O   VAL A 244     5228   3497   8849     60   -172      9  A    O  
ATOM   1796  CB  VAL A 244      16.974  41.841 470.055  1.00 41.16      A    C  
ANISOU 1796  CB  VAL A 244     4771   2944   7923    110    -95     41  A    C  
ATOM   1797  CG1 VAL A 244      16.204  40.580 470.404  1.00 30.39      A    C  
ANISOU 1797  CG1 VAL A 244     3479   1657   6411    106   -136     -2  A    C  
ATOM   1798  CG2 VAL A 244      16.580  42.385 468.696  1.00 49.04      A    C  
ANISOU 1798  CG2 VAL A 244     5810   3936   8889    128     -9    130  A    C  
ATOM   1799  N   LEU A 245      17.174  45.258 470.484  1.00 41.50      A    N  
ANISOU 1799  N   LEU A 245     4707   2888   8172     93   -126     55  A    N  
ATOM   1800  CA  LEU A 245      18.045  46.374 470.109  1.00 33.81      A    C  
ANISOU 1800  CA  LEU A 245     3662   1842   7343     66    -87    109  A    C  
ATOM   1801  C   LEU A 245      18.517  47.231 471.276  1.00 34.53      A    C  
ANISOU 1801  C   LEU A 245     3703   1886   7532     36   -196     22  A    C  
ATOM   1802  O   LEU A 245      19.441  48.014 471.078  1.00 35.69      A    O  
ANISOU 1802  O   LEU A 245     3764   1962   7835     -3   -182     59  A    O  
ATOM   1803  CB  LEU A 245      17.336  47.274 469.112  1.00 34.27      A    C  
ANISOU 1803  CB  LEU A 245     3768   1861   7391     92    -23    201  A    C  
ATOM   1804  CG  LEU A 245      17.071  46.707 467.723  1.00 34.25      A    C  
ANISOU 1804  CG  LEU A 245     3841   1858   7313    120     80    314  A    C  
ATOM   1805  CD1 LEU A 245      16.412  47.756 466.863  1.00 35.08      A    C  
ANISOU 1805  CD1 LEU A 245     4008   1904   7418    150    104    416  A    C  
ATOM   1806  CD2 LEU A 245      18.372  46.273 467.099  1.00 34.92      A    C  
ANISOU 1806  CD2 LEU A 245     3884   1907   7476     94    206    377  A    C  
ATOM   1807  N   ARG A 246      17.920  47.104 472.466  1.00 46.19      A    N  
ANISOU 1807  N   ARG A 246     5241   3383   8926     52   -298    -91  A    N  
ATOM   1808  CA  ARG A 246      18.253  47.957 473.608  1.00 35.14      A    C  
ANISOU 1808  CA  ARG A 246     3847   1917   7589     33   -414   -190  A    C  
ATOM   1809  C   ARG A 246      19.762  48.071 473.829  1.00 46.24      A    C  
ANISOU 1809  C   ARG A 246     5140   3265   9164    -25   -488   -189  A    C  
ATOM   1810  O   ARG A 246      20.498  47.086 473.762  1.00 45.43      A    O  
ANISOU 1810  O   ARG A 246     4978   3190   9096    -37   -497   -167  A    O  
ATOM   1811  CB  ARG A 246      17.569  47.421 474.867  1.00 34.78      A    C  
ANISOU 1811  CB  ARG A 246     3914   1891   7408     62   -493   -309  A    C  
ATOM   1812  CG  ARG A 246      18.011  48.055 476.171  1.00 39.38      A    C  
ANISOU 1812  CG  ARG A 246     4554   2391   8017     46   -636   -433  A    C  
ATOM   1813  CD  ARG A 246      17.266  47.446 477.345  1.00 41.02      A    C  
ANISOU 1813  CD  ARG A 246     4916   2604   8066     83   -681   -543  A    C  
ATOM   1814  NE  ARG A 246      17.335  45.989 477.332  1.00 49.29      A    N  
ANISOU 1814  NE  ARG A 246     5972   3719   9036     79   -679   -506  A    N  
ATOM   1815  CZ  ARG A 246      18.274  45.260 477.933  1.00 64.54      A    C  
ANISOU 1815  CZ  ARG A 246     7916   5634  10973     52   -809   -527  A    C  
ATOM   1816  NH1 ARG A 246      19.249  45.837 478.620  1.00 36.73      A    N1+
ANISOU 1816  NH1 ARG A 246     4388   2033   7536     21   -973   -589  A    N1+
ATOM   1817  NH2 ARG A 246      18.229  43.934 477.852  1.00 57.63      A    N  
ANISOU 1817  NH2 ARG A 246     7057   4810  10028     56   -794   -484  A    N  
ATOM   1818  N   ALA A 247      20.215  49.289 474.115  1.00 45.87      A    N  
ANISOU 1818  N   ALA A 247     5056   3126   9248    -57   -548   -216  A    N  
ATOM   1819  CA  ALA A 247      21.643  49.544 474.227  1.00 47.55      A    C  
ANISOU 1819  CA  ALA A 247     5123   3265   9679   -119   -623   -203  A    C  
ATOM   1820  C   ALA A 247      22.229  48.858 475.448  1.00 39.46      A    C  
ANISOU 1820  C   ALA A 247     4109   2232   8653   -130   -816   -306  A    C  
ATOM   1821  O   ALA A 247      21.544  48.586 476.438  1.00 42.43      A    O  
ANISOU 1821  O   ALA A 247     4642   2624   8854    -99   -908   -411  A    O  
ATOM   1822  CB  ALA A 247      21.932  51.045 474.314  1.00 40.74      A    C  
ANISOU 1822  CB  ALA A 247     4228   2289   8964   -158   -664   -214  A    C  
ATOM   1823  N   VAL A 248      23.531  48.625 475.371  1.00 40.58      A    N  
ANISOU 1823  N   VAL A 248     4078   2329   9011   -171   -877   -270  A    N  
ATOM   1824  CA  VAL A 248      24.297  47.885 476.369  1.00 41.31      A    C  
ANISOU 1824  CA  VAL A 248     4144   2398   9154   -179  -1084   -339  A    C  
ATOM   1825  C   VAL A 248      24.984  48.898 477.265  1.00 43.48      A    C  
ANISOU 1825  C   VAL A 248     4390   2557   9575   -228  -1303   -425  A    C  
ATOM   1826  O   VAL A 248      25.506  49.910 476.783  1.00 44.78      A    O  
ANISOU 1826  O   VAL A 248     4423   2647   9942   -273  -1265   -380  A    O  
ATOM   1827  CB  VAL A 248      25.339  46.953 475.706  1.00 41.57      A    C  
ANISOU 1827  CB  VAL A 248     3976   2436   9383   -181  -1027   -245  A    C  
ATOM   1828  CG1 VAL A 248      26.023  46.079 476.731  1.00 42.34      A    C  
ANISOU 1828  CG1 VAL A 248     4056   2504   9528   -172  -1263   -307  A    C  
ATOM   1829  CG2 VAL A 248      24.728  46.137 474.609  1.00 39.83      A    C  
ANISOU 1829  CG2 VAL A 248     3792   2308   9032   -138   -787   -156  A    C  
ATOM   1830  N   SER A 249      24.997  48.620 478.563  1.00 57.31      A    N  
ANISOU 1830  N   SER A 249     6277   4279  11218   -219  -1537   -546  A    N  
ATOM   1831  CA  SER A 249      25.751  49.410 479.530  1.00 54.25      A    C  
ANISOU 1831  CA  SER A 249     5885   3772  10954   -263  -1801   -643  A    C  
ATOM   1832  C   SER A 249      27.221  49.515 479.113  1.00 55.20      A    C  
ANISOU 1832  C   SER A 249     5705   3820  11448   -313  -1875   -563  A    C  
ATOM   1833  O   SER A 249      27.884  48.476 478.934  1.00 51.09      A    O  
ANISOU 1833  O   SER A 249     5045   3320  11046   -297  -1900   -503  A    O  
ATOM   1834  CB  SER A 249      25.635  48.759 480.908  1.00 58.18      A    C  
ANISOU 1834  CB  SER A 249     6595   4257  11255   -237  -2049   -767  A    C  
ATOM   1835  OG  SER A 249      26.621  49.236 481.796  1.00 63.81      A    O  
ANISOU 1835  OG  SER A 249     7281   4855  12110   -277  -2356   -844  A    O  
ATOM   1836  N   PRO A 250      27.764  50.731 478.958  1.00 57.75      A    N  
ANISOU 1836  N   PRO A 250     5914   4042  11985   -369  -1906   -557  A    N  
ATOM   1837  CA  PRO A 250      29.173  50.868 478.543  1.00 52.37      A    C  
ANISOU 1837  CA  PRO A 250     4923   3275  11700   -414  -1953   -470  A    C  
ATOM   1838  C   PRO A 250      30.155  50.180 479.464  1.00 54.13      A    C  
ANISOU 1838  C   PRO A 250     5063   3442  12062   -408  -2264   -518  A    C  
ATOM   1839  O   PRO A 250      31.215  49.726 478.997  1.00 55.28      A    O  
ANISOU 1839  O   PRO A 250     4931   3547  12524   -409  -2252   -423  A    O  
ATOM   1840  CB  PRO A 250      29.375  52.384 478.529  1.00 54.31      A    C  
ANISOU 1840  CB  PRO A 250     5141   3406  12090   -477  -1981   -490  A    C  
ATOM   1841  CG  PRO A 250      28.007  52.925 478.265  1.00 53.79      A    C  
ANISOU 1841  CG  PRO A 250     5304   3394  11738   -453  -1800   -516  A    C  
ATOM   1842  CD  PRO A 250      27.078  52.031 479.012  1.00 55.60      A    C  
ANISOU 1842  CD  PRO A 250     5777   3720  11627   -388  -1857   -611  A    C  
ATOM   1843  N   LEU A 251      29.808  50.043 480.749  1.00 57.99      A    N  
ANISOU 1843  N   LEU A 251     5797   3918  12317   -392  -2533   -658  A    N  
ATOM   1844  CA  LEU A 251      30.607  49.235 481.669  1.00 69.36      A    C  
ANISOU 1844  CA  LEU A 251     7216   5311  13826   -372  -2855   -698  A    C  
ATOM   1845  C   LEU A 251      30.792  47.820 481.151  1.00 54.70      A    C  
ANISOU 1845  C   LEU A 251     5238   3527  12020   -320  -2752   -601  A    C  
ATOM   1846  O   LEU A 251      31.910  47.299 481.104  1.00 56.36      A    O  
ANISOU 1846  O   LEU A 251     5206   3669  12537   -309  -2877   -540  A    O  
ATOM   1847  CB  LEU A 251      29.954  49.185 483.052  1.00 69.73      A    C  
ANISOU 1847  CB  LEU A 251     7627   5351  13514   -352  -3105   -856  A    C  
ATOM   1848  CG  LEU A 251      30.787  48.375 484.056  1.00 70.52      A    C  
ANISOU 1848  CG  LEU A 251     7747   5390  13657   -327  -3482   -890  A    C  
ATOM   1849  CD1 LEU A 251      32.123  49.053 484.267  1.00 74.62      A    C  
ANISOU 1849  CD1 LEU A 251     8032   5766  14555   -370  -3730   -881  A    C  
ATOM   1850  CD2 LEU A 251      30.081  48.183 485.391  1.00 70.85      A    C  
ANISOU 1850  CD2 LEU A 251     8202   5434  13285   -298  -3702  -1036  A    C  
ATOM   1851  N   HIS A 252      29.697  47.186 480.744  1.00 60.08      A    N  
ANISOU 1851  N   HIS A 252     6082   4330  12415   -282  -2519   -584  A    N  
ATOM   1852  CA  HIS A 252      29.777  45.796 480.323  1.00 59.46      A    C  
ANISOU 1852  CA  HIS A 252     5935   4310  12346   -232  -2429   -507  A    C  
ATOM   1853  C   HIS A 252      30.458  45.644 478.965  1.00 57.55      A    C  
ANISOU 1853  C   HIS A 252     5373   4068  12426   -233  -2163   -368  A    C  
ATOM   1854  O   HIS A 252      31.199  44.674 478.749  1.00 61.66      A    O  
ANISOU 1854  O   HIS A 252     5714   4561  13153   -198  -2182   -308  A    O  
ATOM   1855  CB  HIS A 252      28.387  45.177 480.310  1.00 62.05      A    C  
ANISOU 1855  CB  HIS A 252     6546   4757  12275   -189  -2260   -530  A    C  
ATOM   1856  CG  HIS A 252      28.379  43.793 479.765  1.00 61.85      A    C  
ANISOU 1856  CG  HIS A 252     6471   4789  12241   -136  -2132   -447  A    C  
ATOM   1857  CD2 HIS A 252      27.734  43.259 478.702  1.00 55.00      A    C  
ANISOU 1857  CD2 HIS A 252     5607   4018  11271   -105  -1816   -369  A    C  
ATOM   1858  ND1 HIS A 252      29.155  42.786 480.294  1.00 50.89      A    N  
ANISOU 1858  ND1 HIS A 252     5022   3341  10974   -104  -2352   -438  A    N  
ATOM   1859  CE1 HIS A 252      28.963  41.682 479.596  1.00 46.20      A    C  
ANISOU 1859  CE1 HIS A 252     4401   2805  10346    -51  -2156   -361  A    C  
ATOM   1860  NE2 HIS A 252      28.112  41.943 478.620  1.00 44.21      A    N  
ANISOU 1860  NE2 HIS A 252     4194   2654   9951    -52  -1831   -322  A    N  
ATOM   1861  N   MET A 253      30.224  46.582 478.036  1.00 50.08      A    N  
ANISOU 1861  N   MET A 253     4362   3137  11529   -268  -1908   -313  A    N  
ATOM   1862  CA  MET A 253      31.027  46.605 476.816  1.00 62.93      A    C  
ANISOU 1862  CA  MET A 253     5695   4731  13485   -275  -1662   -180  A    C  
ATOM   1863  C   MET A 253      32.511  46.595 477.169  1.00 70.14      A    C  
ANISOU 1863  C   MET A 253     6319   5507  14825   -281  -1866   -158  A    C  
ATOM   1864  O   MET A 253      33.303  45.844 476.581  1.00 54.72      A    O  
ANISOU 1864  O   MET A 253     4132   3516  13145   -244  -1752    -70  A    O  
ATOM   1865  CB  MET A 253      30.689  47.835 475.957  1.00 50.75      A    C  
ANISOU 1865  CB  MET A 253     4148   3187  11950   -321  -1427   -125  A    C  
ATOM   1866  CG  MET A 253      29.272  47.902 475.392  1.00 48.05      A    C  
ANISOU 1866  CG  MET A 253     4053   2961  11244   -302  -1204   -119  A    C  
ATOM   1867  SD  MET A 253      28.843  46.590 474.213  1.00 45.95      A    S  
ANISOU 1867  SD  MET A 253     3808   2801  10852   -239   -893    -20  A    S  
ATOM   1868  CE  MET A 253      28.050  47.426 472.850  1.00 45.04      A    C  
ANISOU 1868  CE  MET A 253     3779   2722  10614   -250   -567     82  A    C  
ATOM   1869  N   GLN A 254      32.901  47.397 478.162  1.00 71.38      A    N  
ANISOU 1869  N   GLN A 254     6502   5574  15047   -319  -2174   -241  A    N  
ATOM   1870  CA  GLN A 254      34.299  47.385 478.573  1.00 71.85      A    C  
ANISOU 1870  CA  GLN A 254     6307   5486  15507   -317  -2406   -220  A    C  
ATOM   1871  C   GLN A 254      34.691  46.036 479.165  1.00 59.53      A    C  
ANISOU 1871  C   GLN A 254     4729   3910  13979   -248  -2616   -233  A    C  
ATOM   1872  O   GLN A 254      35.819  45.568 478.954  1.00 61.64      A    O  
ANISOU 1872  O   GLN A 254     4732   4066  14623   -214  -2641   -159  A    O  
ATOM   1873  CB  GLN A 254      34.576  48.518 479.561  1.00 75.17      A    C  
ANISOU 1873  CB  GLN A 254     6803   5805  15954   -375  -2719   -318  A    C  
ATOM   1874  CG  GLN A 254      36.059  48.766 479.807  1.00 65.50      A    C  
ANISOU 1874  CG  GLN A 254     5297   4403  15187   -390  -2923   -279  A    C  
ATOM   1875  CD  GLN A 254      36.850  48.775 478.512  1.00 70.29      A    C  
ANISOU 1875  CD  GLN A 254     5571   4956  16180   -389  -2583   -123  A    C  
ATOM   1876  NE2 GLN A 254      37.930  47.997 478.467  1.00 68.48      A    N  
ANISOU 1876  NE2 GLN A 254     5109   4624  16286   -344  -2635    -59  A    N  
ATOM   1877  OE1 GLN A 254      36.502  49.488 477.567  1.00 67.87      A    O  
ANISOU 1877  OE1 GLN A 254     5237   4685  15866   -428  -2269    -58  A    O  
ATOM   1878  N   TYR A 255      33.787  45.400 479.921  1.00 60.57      A    N  
ANISOU 1878  N   TYR A 255     5156   4131  13728   -224  -2762   -320  A    N  
ATOM   1879  CA  TYR A 255      34.115  44.095 480.491  1.00 58.05      A    C  
ANISOU 1879  CA  TYR A 255     4846   3788  13424   -160  -2975   -323  A    C  
ATOM   1880  C   TYR A 255      34.462  43.108 479.381  1.00 59.77      A    C  
ANISOU 1880  C   TYR A 255     4826   4015  13868   -109  -2684   -207  A    C  
ATOM   1881  O   TYR A 255      35.495  42.430 479.435  1.00 59.33      A    O  
ANISOU 1881  O   TYR A 255     4564   3838  14141    -60  -2790   -157  A    O  
ATOM   1882  CB  TYR A 255      32.959  43.566 481.353  1.00 60.82      A    C  
ANISOU 1882  CB  TYR A 255     5588   4231  13288   -147  -3106   -420  A    C  
ATOM   1883  CG  TYR A 255      33.356  42.370 482.209  1.00 57.18      A    C  
ANISOU 1883  CG  TYR A 255     5189   3714  12823    -89  -3424   -431  A    C  
ATOM   1884  CD1 TYR A 255      33.393  41.080 481.707  1.00 56.12      A    C  
ANISOU 1884  CD1 TYR A 255     4972   3596  12755    -33  -3305   -359  A    C  
ATOM   1885  CD2 TYR A 255      33.727  42.561 483.528  1.00 59.60      A    C  
ANISOU 1885  CD2 TYR A 255     5655   3934  13056    -88  -3854   -512  A    C  
ATOM   1886  CE1 TYR A 255      33.802  40.015 482.508  1.00 76.43      A    C  
ANISOU 1886  CE1 TYR A 255     7599   6092  15348     21  -3625   -361  A    C  
ATOM   1887  CE2 TYR A 255      34.125  41.519 484.336  1.00 69.54      A    C  
ANISOU 1887  CE2 TYR A 255     6996   5129  14297    -32  -4173   -509  A    C  
ATOM   1888  CZ  TYR A 255      34.169  40.245 483.835  1.00 75.35      A    C  
ANISOU 1888  CZ  TYR A 255     7630   5879  15123     22  -4069   -431  A    C  
ATOM   1889  OH  TYR A 255      34.585  39.226 484.685  1.00 76.71      A    O  
ANISOU 1889  OH  TYR A 255     7896   5982  15267     83  -4409   -420  A    O  
ATOM   1890  N   LEU A 256      33.630  43.065 478.334  1.00 54.71      A    N  
ANISOU 1890  N   LEU A 256     4238   3495  13055   -119  -2297   -164  A    N  
ATOM   1891  CA  LEU A 256      33.874  42.176 477.200  1.00 54.10      A    C  
ANISOU 1891  CA  LEU A 256     3977   3430  13148    -74  -1978    -64  A    C  
ATOM   1892  C   LEU A 256      35.137  42.555 476.432  1.00 56.72      A    C  
ANISOU 1892  C   LEU A 256     3952   3623  13974    -63  -1814     37  A    C  
ATOM   1893  O   LEU A 256      35.832  41.681 475.907  1.00 57.70      A    O  
ANISOU 1893  O   LEU A 256     3915   3655  14354    -16  -1669    105  A    O  
ATOM   1894  CB  LEU A 256      32.668  42.187 476.268  1.00 51.12      A    C  
ANISOU 1894  CB  LEU A 256     3811   3198  12412    -81  -1610    -42  A    C  
ATOM   1895  CG  LEU A 256      31.387  41.618 476.875  1.00 49.85      A    C  
ANISOU 1895  CG  LEU A 256     4032   3154  11755    -51  -1684   -117  A    C  
ATOM   1896  CD1 LEU A 256      30.213  41.854 475.940  1.00 46.15      A    C  
ANISOU 1896  CD1 LEU A 256     3750   2811  10973    -51  -1350    -90  A    C  
ATOM   1897  CD2 LEU A 256      31.563  40.128 477.207  1.00 48.57      A    C  
ANISOU 1897  CD2 LEU A 256     3910   2989  11555     34  -1778   -110  A    C  
ATOM   1898  N   ARG A 257      35.417  43.851 476.291  1.00 58.01      A    N  
ANISOU 1898  N   ARG A 257     4054   3744  14243   -122  -1781     52  A    N  
ATOM   1899  CA  ARG A 257      36.675  44.261 475.679  1.00 61.03      A    C  
ANISOU 1899  CA  ARG A 257     4146   3972  15072   -128  -1634    150  A    C  
ATOM   1900  C   ARG A 257      37.871  43.669 476.418  1.00 64.00      A    C  
ANISOU 1900  C   ARG A 257     4374   4185  15760   -106  -1916    143  A    C  
ATOM   1901  O   ARG A 257      38.769  43.088 475.798  1.00 65.79      A    O  
ANISOU 1901  O   ARG A 257     4397   4321  16280    -93  -1722    225  A    O  
ATOM   1902  CB  ARG A 257      36.768  45.784 475.630  1.00 62.25      A    C  
ANISOU 1902  CB  ARG A 257     4276   4097  15282   -208  -1634    154  A    C  
ATOM   1903  CG  ARG A 257      35.998  46.410 474.509  1.00 60.47      A    C  
ANISOU 1903  CG  ARG A 257     4123   3971  14882   -241  -1252    217  A    C  
ATOM   1904  CD  ARG A 257      36.246  47.903 474.446  1.00 62.24      A    C  
ANISOU 1904  CD  ARG A 257     4300   4125  15222   -323  -1259    235  A    C  
ATOM   1905  NE  ARG A 257      35.066  48.568 473.913  1.00 59.86      A    N  
ANISOU 1905  NE  ARG A 257     4221   3939  14585   -361  -1066    236  A    N  
ATOM   1906  CZ  ARG A 257      34.147  49.156 474.678  1.00 67.41      A    C  
ANISOU 1906  CZ  ARG A 257     5427   4953  15234   -397  -1269    123  A    C  
ATOM   1907  NH1 ARG A 257      34.297  49.163 476.000  1.00 64.37      A    N1+
ANISOU 1907  NH1 ARG A 257     5111   4528  14820   -403  -1662      0  A    N1+
ATOM   1908  NH2 ARG A 257      33.083  49.738 474.131  1.00 56.56      A    N  
ANISOU 1908  NH2 ARG A 257     4253   3660  13578   -421  -1079    135  A    N  
ATOM   1909  N   ASN A 258      37.906  43.824 477.747  1.00 64.88      A    N  
ANISOU 1909  N   ASN A 258     4604   4263  15784   -117  -2368     44  A    N  
ATOM   1910  CA  ASN A 258      39.030  43.316 478.527  1.00 68.05      A    C  
ANISOU 1910  CA  ASN A 258     4890   4511  16454   -107  -2681     35  A    C  
ATOM   1911  C   ASN A 258      39.192  41.811 478.403  1.00 67.60      A    C  
ANISOU 1911  C   ASN A 258     4821   4464  16401    -59  -2629     59  A    C  
ATOM   1912  O   ASN A 258      40.287  41.285 478.617  1.00 77.31      A    O  
ANISOU 1912  O   ASN A 258     5871   5584  17919    -55  -2743     88  A    O  
ATOM   1913  CB  ASN A 258      38.855  43.716 479.990  1.00 68.92      A    C  
ANISOU 1913  CB  ASN A 258     5208   4602  16375   -121  -3176    -82  A    C  
ATOM   1914  CG  ASN A 258      38.860  45.210 480.172  1.00 70.07      A    C  
ANISOU 1914  CG  ASN A 258     5356   4723  16543   -194  -3246   -119  A    C  
ATOM   1915  ND2 ASN A 258      38.640  45.657 481.400  1.00 92.93      A    N  
ANISOU 1915  ND2 ASN A 258     8471   7605  19234   -216  -3643   -234  A    N  
ATOM   1916  OD1 ASN A 258      39.058  45.962 479.217  1.00 70.38      A    O  
ANISOU 1916  OD1 ASN A 258     5222   4750  16769   -234  -2940    -46  A    O  
ATOM   1917  N   PHE A 259      38.127  41.123 478.050  1.00 67.99      A    N  
ANISOU 1917  N   PHE A 259     5043   4654  16134    -29  -2458     45  A    N  
ATOM   1918  CA  PHE A 259      38.072  39.687 477.891  1.00 63.44      A    C  
ANISOU 1918  CA  PHE A 259     4486   4154  15462      7  -2383     57  A    C  
ATOM   1919  C   PHE A 259      38.436  39.231 476.481  1.00 67.45      A    C  
ANISOU 1919  C   PHE A 259     4800   4710  16118     26  -1894    156  A    C  
ATOM   1920  O   PHE A 259      38.487  38.022 476.230  1.00 69.76      A    O  
ANISOU 1920  O   PHE A 259     5094   5094  16316     99  -1784    174  A    O  
ATOM   1921  CB  PHE A 259      36.657  39.230 478.249  1.00 59.95      A    C  
ANISOU 1921  CB  PHE A 259     4344   3874  14560     29  -2450    -10  A    C  
ATOM   1922  CG  PHE A 259      36.566  37.814 478.725  1.00 67.09      A    C  
ANISOU 1922  CG  PHE A 259     5365   4872  15254    114  -2574    -17  A    C  
ATOM   1923  CD1 PHE A 259      37.701  37.049 478.928  1.00 65.25      A    C  
ANISOU 1923  CD1 PHE A 259     4970   4560  15261    152  -2675     19  A    C  
ATOM   1924  CD2 PHE A 259      35.324  37.241 478.952  1.00 62.79      A    C  
ANISOU 1924  CD2 PHE A 259     5125   4479  14254    181  -2565    -47  A    C  
ATOM   1925  CE1 PHE A 259      37.604  35.743 479.346  1.00 71.48      A    C  
ANISOU 1925  CE1 PHE A 259     5886   5418  15855    248  -2781     24  A    C  
ATOM   1926  CE2 PHE A 259      35.218  35.938 479.371  1.00 56.67      A    C  
ANISOU 1926  CE2 PHE A 259     4503   3758  13270    277  -2653    -34  A    C  
ATOM   1927  CZ  PHE A 259      36.357  35.191 479.577  1.00 74.13      A    C  
ANISOU 1927  CZ  PHE A 259     6538   5892  15735    310  -2772      0  A    C  
ATOM   1928  N   GLY A 260      38.669  40.153 475.549  1.00 70.34      A    N  
ANISOU 1928  N   GLY A 260     5031   5023  16673     -8  -1587    225  A    N  
ATOM   1929  CA  GLY A 260      38.932  39.761 474.179  1.00 64.31      A    C  
ANISOU 1929  CA  GLY A 260     4137   4305  15993     22  -1100    321  A    C  
ATOM   1930  C   GLY A 260      37.704  39.391 473.380  1.00 79.73      A    C  
ANISOU 1930  C   GLY A 260     6285   6439  17569     57   -802    322  A    C  
ATOM   1931  O   GLY A 260      37.831  38.781 472.312  1.00 78.66      A    O  
ANISOU 1931  O   GLY A 260     6113   6367  17407    122   -420    384  A    O  
ATOM   1932  N   VAL A 261      36.514  39.747 473.859  1.00 58.05      A    N  
ANISOU 1932  N   VAL A 261     3761   3777  14517     31   -962    252  A    N  
ATOM   1933  CA  VAL A 261      35.253  39.398 473.218  1.00 54.87      A    C  
ANISOU 1933  CA  VAL A 261     3595   3557  13697     91   -726    245  A    C  
ATOM   1934  C   VAL A 261      34.762  40.607 472.425  1.00 63.37      A    C  
ANISOU 1934  C   VAL A 261     4673   4624  14781     32   -485    294  A    C  
ATOM   1935  O   VAL A 261      34.751  41.733 472.939  1.00 54.55      A    O  
ANISOU 1935  O   VAL A 261     3505   3461  13759    -20   -674    272  A    O  
ATOM   1936  CB  VAL A 261      34.211  38.974 474.265  1.00 52.56      A    C  
ANISOU 1936  CB  VAL A 261     3612   3367  12992    126  -1033    146  A    C  
ATOM   1937  CG1 VAL A 261      32.949  38.499 473.600  1.00 49.65      A    C  
ANISOU 1937  CG1 VAL A 261     3560   3149  12156    185   -784    142  A    C  
ATOM   1938  CG2 VAL A 261      34.774  37.944 475.192  1.00 53.80      A    C  
ANISOU 1938  CG2 VAL A 261     3753   3500  13187    175  -1325    113  A    C  
ATOM   1939  N   SER A 262      34.388  40.388 471.164  1.00 59.00      A    N  
ANISOU 1939  N   SER A 262     4211   4137  14068     90    -72    362  A    N  
ATOM   1940  CA  SER A 262      33.868  41.452 470.318  1.00 52.67      A    C  
ANISOU 1940  CA  SER A 262     3485   3329  13197     39    177    425  A    C  
ATOM   1941  C   SER A 262      32.358  41.368 470.113  1.00 66.51      A    C  
ANISOU 1941  C   SER A 262     5645   5238  14387     57    212    379  A    C  
ATOM   1942  O   SER A 262      31.727  42.373 469.765  1.00 72.82      A    O  
ANISOU 1942  O   SER A 262     6565   6069  15032     -7    286    404  A    O  
ATOM   1943  CB  SER A 262      34.573  41.430 468.957  1.00 57.29      A    C  
ANISOU 1943  CB  SER A 262     3896   3845  14029     84    638    555  A    C  
ATOM   1944  OG  SER A 262      35.886  41.967 469.030  1.00 57.88      A    O  
ANISOU 1944  OG  SER A 262     3688   3776  14528     30    637    616  A    O  
ATOM   1945  N   ALA A 263      31.764  40.201 470.315  1.00 59.81      A    N  
ANISOU 1945  N   ALA A 263     5000   4491  13234    142    155    316  A    N  
ATOM   1946  CA  ALA A 263      30.324  40.061 470.219  1.00 45.15      A    C  
ANISOU 1946  CA  ALA A 263     3492   2765  10899    152    154    271  A    C  
ATOM   1947  C   ALA A 263      29.918  38.929 471.132  1.00 43.98      A    C  
ANISOU 1947  C   ALA A 263     3485   2689  10535    203    -79    185  A    C  
ATOM   1948  O   ALA A 263      30.737  38.078 471.473  1.00 45.23      A    O  
ANISOU 1948  O   ALA A 263     3508   2810  10869    258   -157    178  A    O  
ATOM   1949  CB  ALA A 263      29.864  39.792 468.788  1.00 54.46      A    C  
ANISOU 1949  CB  ALA A 263     4817   3972  11902    211    516    336  A    C  
ATOM   1950  N   SER A 264      28.690  38.988 471.620  1.00 41.88      A    N  
ANISOU 1950  N   SER A 264     3478   2517   9916    180   -204    126  A    N  
ATOM   1951  CA  SER A 264      28.201  37.907 472.457  1.00 53.64      A    C  
ANISOU 1951  CA  SER A 264     5129   4063  11187    223   -390     64  A    C  
ATOM   1952  C   SER A 264      26.710  37.737 472.230  1.00 50.19      A    C  
ANISOU 1952  C   SER A 264     4975   3732  10363    220   -327     38  A    C  
ATOM   1953  O   SER A 264      26.031  38.605 471.668  1.00 50.55      A    O  
ANISOU 1953  O   SER A 264     5090   3810  10308    180   -214     56  A    O  
ATOM   1954  CB  SER A 264      28.477  38.126 473.949  1.00 63.89      A    C  
ANISOU 1954  CB  SER A 264     6404   5320  12549    187   -740      4  A    C  
ATOM   1955  OG  SER A 264      27.831  39.279 474.446  1.00 66.54      A    O  
ANISOU 1955  OG  SER A 264     6834   5674  12773    113   -839    -39  A    O  
ATOM   1956  N   THR A 265      26.224  36.584 472.677  1.00 46.00      A    N  
ANISOU 1956  N   THR A 265     4595   3242   9642    262   -409      5  A    N  
ATOM   1957  CA  THR A 265      24.816  36.252 472.784  1.00 37.78      A    C  
ANISOU 1957  CA  THR A 265     3797   2282   8277    249   -411    -24  A    C  
ATOM   1958  C   THR A 265      24.640  35.507 474.093  1.00 39.04      A    C  
ANISOU 1958  C   THR A 265     4058   2435   8340    256   -639    -62  A    C  
ATOM   1959  O   THR A 265      25.503  34.719 474.459  1.00 37.16      A    O  
ANISOU 1959  O   THR A 265     3747   2144   8229    304   -733    -53  A    O  
ATOM   1960  CB  THR A 265      24.386  35.333 471.640  1.00 49.28      A    C  
ANISOU 1960  CB  THR A 265     5356   3762   9608    298   -210     -5  A    C  
ATOM   1961  CG2 THR A 265      22.874  35.153 471.630  1.00 55.55      A    C  
ANISOU 1961  CG2 THR A 265     6361   4623  10121    266   -216    -29  A    C  
ATOM   1962  OG1 THR A 265      24.809  35.882 470.390  1.00 60.68      A    O  
ANISOU 1962  OG1 THR A 265     6715   5175  11164    314     16     42  A    O  
ATOM   1963  N   SER A 266      23.559  35.743 474.824  1.00 38.65      A    N  
ANISOU 1963  N   SER A 266     4178   2426   8081    215   -725    -98  A    N  
ATOM   1964  CA  SER A 266      23.315  34.858 475.956  1.00 35.16      A    C  
ANISOU 1964  CA  SER A 266     3878   1960   7521    228   -897   -114  A    C  
ATOM   1965  C   SER A 266      21.838  34.501 476.002  1.00 33.82      A    C  
ANISOU 1965  C   SER A 266     3905   1846   7099    198   -825   -123  A    C  
ATOM   1966  O   SER A 266      20.981  35.291 475.599  1.00 32.93      A    O  
ANISOU 1966  O   SER A 266     3816   1784   6912    161   -725   -137  A    O  
ATOM   1967  CB  SER A 266      23.756  35.455 477.293  1.00 37.38      A    C  
ANISOU 1967  CB  SER A 266     4172   2177   7854    209  -1149   -154  A    C  
ATOM   1968  OG  SER A 266      23.332  36.786 477.409  1.00 44.87      A    O  
ANISOU 1968  OG  SER A 266     5124   3142   8781    157  -1138   -198  A    O  
ATOM   1969  N   ILE A 267      21.557  33.280 476.458  1.00 40.51      A    N  
ANISOU 1969  N   ILE A 267     4880   2669   7844    214   -877   -105  A    N  
ATOM   1970  CA  ILE A 267      20.199  32.763 476.603  1.00 35.39      A    C  
ANISOU 1970  CA  ILE A 267     4398   2079   6968    171   -811   -100  A    C  
ATOM   1971  C   ILE A 267      19.991  32.345 478.050  1.00 33.82      A    C  
ANISOU 1971  C   ILE A 267     4358   1866   6624    157   -958    -93  A    C  
ATOM   1972  O   ILE A 267      20.878  31.738 478.661  1.00 42.00      A    O  
ANISOU 1972  O   ILE A 267     5411   2827   7720    200  -1112    -69  A    O  
ATOM   1973  CB  ILE A 267      19.918  31.582 475.649  1.00 32.74      A    C  
ANISOU 1973  CB  ILE A 267     4095   1734   6610    185   -697    -74  A    C  
ATOM   1974  CG1 ILE A 267      20.152  31.997 474.217  1.00 32.37      A    C  
ANISOU 1974  CG1 ILE A 267     3939   1709   6650    206   -544    -81  A    C  
ATOM   1975  CG2 ILE A 267      18.494  31.130 475.758  1.00 32.11      A    C  
ANISOU 1975  CG2 ILE A 267     4150   1712   6337    119   -638    -66  A    C  
ATOM   1976  CD1 ILE A 267      20.586  30.886 473.361  1.00 32.84      A    C  
ANISOU 1976  CD1 ILE A 267     4008   1733   6737    257   -464    -74  A    C  
ATOM   1977  N   GLY A 268      18.824  32.682 478.598  1.00 33.44      A    N  
ANISOU 1977  N   GLY A 268     4430   1886   6390    105   -906   -107  A    N  
ATOM   1978  CA  GLY A 268      18.489  32.263 479.949  1.00 34.41      A    C  
ANISOU 1978  CA  GLY A 268     4745   2001   6328     90   -995    -90  A    C  
ATOM   1979  C   GLY A 268      17.964  30.835 479.977  1.00 39.88      A    C  
ANISOU 1979  C   GLY A 268     5550   2676   6928     69   -946    -19  A    C  
ATOM   1980  O   GLY A 268      17.253  30.387 479.076  1.00 39.08      A    O  
ANISOU 1980  O   GLY A 268     5407   2602   6839     35   -808     -5  A    O  
ATOM   1981  N   ILE A 269      18.349  30.111 481.017  1.00 43.15      A    N  
ANISOU 1981  N   ILE A 269     6115   3028   7252     86  -1082     29  A    N  
ATOM   1982  CA  ILE A 269      17.868  28.758 481.250  1.00 36.45      A    C  
ANISOU 1982  CA  ILE A 269     5405   2136   6307     59  -1049    112  A    C  
ATOM   1983  C   ILE A 269      16.870  28.833 482.390  1.00 37.27      A    C  
ANISOU 1983  C   ILE A 269     5711   2285   6167      2   -989    143  A    C  
ATOM   1984  O   ILE A 269      17.248  29.042 483.548  1.00 38.66      A    O  
ANISOU 1984  O   ILE A 269     6046   2437   6206     28  -1120    151  A    O  
ATOM   1985  CB  ILE A 269      19.000  27.798 481.602  1.00 37.74      A    C  
ANISOU 1985  CB  ILE A 269     5614   2179   6546    129  -1236    168  A    C  
ATOM   1986  CG1 ILE A 269      20.114  27.905 480.576  1.00 37.34      A    C  
ANISOU 1986  CG1 ILE A 269     5341   2085   6761    202  -1274    128  A    C  
ATOM   1987  CG2 ILE A 269      18.436  26.381 481.661  1.00 40.75      A    C  
ANISOU 1987  CG2 ILE A 269     6133   2496   6854     94  -1180    257  A    C  
ATOM   1988  CD1 ILE A 269      21.358  27.152 480.998  1.00 41.65      A    C  
ANISOU 1988  CD1 ILE A 269     5884   2506   7433    293  -1481    175  A    C  
ATOM   1989  N   PHE A 270      15.605  28.615 482.093  1.00 47.41      A    N  
ANISOU 1989  N   PHE A 270     6997   3624   7394    -74   -793    164  A    N  
ATOM   1990  CA  PHE A 270      14.576  28.802 483.090  1.00 37.74      A    C  
ANISOU 1990  CA  PHE A 270     5926   2449   5964   -125   -674    191  A    C  
ATOM   1991  C   PHE A 270      14.047  27.460 483.550  1.00 49.92      A    C  
ANISOU 1991  C   PHE A 270     7625   3932   7412   -186   -615    311  A    C  
ATOM   1992  O   PHE A 270      13.693  26.601 482.731  1.00 45.81      A    O  
ANISOU 1992  O   PHE A 270     7026   3375   7006   -235   -558    348  A    O  
ATOM   1993  CB  PHE A 270      13.465  29.683 482.550  1.00 36.77      A    C  
ANISOU 1993  CB  PHE A 270     5665   2428   5877   -167   -484    135  A    C  
ATOM   1994  CG  PHE A 270      13.841  31.110 482.520  1.00 46.11      A    C  
ANISOU 1994  CG  PHE A 270     6771   3656   7094   -111   -527     32  A    C  
ATOM   1995  CD1 PHE A 270      13.677  31.899 483.642  1.00 42.32      A    C  
ANISOU 1995  CD1 PHE A 270     6435   3198   6447    -89   -516    -12  A    C  
ATOM   1996  CD2 PHE A 270      14.430  31.656 481.397  1.00 46.95      A    C  
ANISOU 1996  CD2 PHE A 270     6684   3764   7391    -79   -579    -21  A    C  
ATOM   1997  CE1 PHE A 270      14.049  33.211 483.622  1.00 37.10      A    C  
ANISOU 1997  CE1 PHE A 270     5713   2551   5832    -41   -571   -115  A    C  
ATOM   1998  CE2 PHE A 270      14.816  32.974 481.376  1.00 34.58      A    C  
ANISOU 1998  CE2 PHE A 270     5048   2215   5877    -38   -622   -104  A    C  
ATOM   1999  CZ  PHE A 270      14.625  33.747 482.488  1.00 35.67      A    C  
ANISOU 1999  CZ  PHE A 270     5318   2364   5870    -21   -629   -155  A    C  
ATOM   2000  N   ASN A 271      14.032  27.292 484.864  1.00 52.72      A    N  
ANISOU 2000  N   ASN A 271     8220   4262   7547   -183   -640    371  A    N  
ATOM   2001  CA  ASN A 271      13.304  26.237 485.545  1.00 42.36      A    C  
ANISOU 2001  CA  ASN A 271     7095   2903   6095   -255   -526    502  A    C  
ATOM   2002  C   ASN A 271      11.991  26.882 485.983  1.00 42.89      A    C  
ANISOU 2002  C   ASN A 271     7178   3072   6046   -316   -264    492  A    C  
ATOM   2003  O   ASN A 271      11.947  27.661 486.943  1.00 44.00      A    O  
ANISOU 2003  O   ASN A 271     7473   3256   5988   -277   -236    456  A    O  
ATOM   2004  CB  ASN A 271      14.114  25.694 486.712  1.00 63.92      A    C  
ANISOU 2004  CB  ASN A 271    10106   5542   8638   -204   -708    586  A    C  
ATOM   2005  CG  ASN A 271      13.428  24.535 487.398  1.00 66.17      A    C  
ANISOU 2005  CG  ASN A 271    10607   5756   8778   -281   -587    748  A    C  
ATOM   2006  ND2 ASN A 271      14.167  23.833 488.245  1.00 65.86      A    N  
ANISOU 2006  ND2 ASN A 271    10815   5609   8599   -235   -770    849  A    N  
ATOM   2007  OD1 ASN A 271      12.241  24.280 487.178  1.00 63.99      A    O  
ANISOU 2007  OD1 ASN A 271    10272   5514   8527   -384   -338    790  A    O  
ATOM   2008  N   GLU A 272      10.937  26.611 485.222  1.00 52.72      A    N  
ANISOU 2008  N   GLU A 272     8250   4349   7434   -405    -81    510  A    N  
ATOM   2009  CA  GLU A 272       9.663  27.315 485.351  1.00 61.64      A    C  
ANISOU 2009  CA  GLU A 272     9292   5577   8551   -453    171    487  A    C  
ATOM   2010  C   GLU A 272      10.018  28.787 485.192  1.00 61.28      A    C  
ANISOU 2010  C   GLU A 272     9157   5611   8518   -360    118    342  A    C  
ATOM   2011  O   GLU A 272      10.544  29.155 484.124  1.00 52.03      A    O  
ANISOU 2011  O   GLU A 272     7798   4447   7525   -327     -8    269  A    O  
ATOM   2012  CB  GLU A 272       8.952  26.924 486.650  1.00 70.75      A    C  
ANISOU 2012  CB  GLU A 272    10679   6722   9481   -501    370    596  A    C  
ATOM   2013  CG  GLU A 272       8.723  25.403 486.840  1.00 71.87      A    C  
ANISOU 2013  CG  GLU A 272    10933   6753   9620   -600    404    762  A    C  
ATOM   2014  CD  GLU A 272       7.994  24.735 485.672  1.00 77.10      A    C  
ANISOU 2014  CD  GLU A 272    11342   7390  10562   -709    461    784  A    C  
ATOM   2015  OE1 GLU A 272       6.957  25.257 485.198  1.00 82.96      A    O  
ANISOU 2015  OE1 GLU A 272    11864   8214  11443   -761    628    744  A    O  
ATOM   2016  OE2 GLU A 272       8.481  23.681 485.218  1.00 74.90      A    O1-
ANISOU 2016  OE2 GLU A 272    11090   6998  10372   -738    319    836  A    O1-
ATOM   2017  N   ASP A 273       9.795  29.640 486.192  1.00 62.14      A    N  
ANISOU 2017  N   ASP A 273     9407   5765   8439   -315    210    298  A    N  
ATOM   2018  CA  ASP A 273      10.123  31.059 486.080  1.00 57.40      A    C  
ANISOU 2018  CA  ASP A 273     8736   5213   7860   -231    153    155  A    C  
ATOM   2019  C   ASP A 273      11.457  31.416 486.716  1.00 60.64      A    C  
ANISOU 2019  C   ASP A 273     9327   5570   8142   -152   -104     99  A    C  
ATOM   2020  O   ASP A 273      11.843  32.583 486.673  1.00 56.57      A    O  
ANISOU 2020  O   ASP A 273     8768   5071   7656    -92   -180    -22  A    O  
ATOM   2021  CB  ASP A 273       9.023  31.922 486.707  1.00 60.68      A    C  
ANISOU 2021  CB  ASP A 273     9179   5697   8180   -218    413    108  A    C  
ATOM   2022  CG  ASP A 273       7.663  31.649 486.110  1.00 79.87      A    C  
ANISOU 2022  CG  ASP A 273    11386   8178  10783   -295    657    164  A    C  
ATOM   2023  OD1 ASP A 273       7.587  31.314 484.906  1.00 76.16      A    O1-
ANISOU 2023  OD1 ASP A 273    10686   7708  10543   -340    584    179  A    O1-
ATOM   2024  OD2 ASP A 273       6.665  31.773 486.851  1.00 96.04      A    O1-
ANISOU 2024  OD2 ASP A 273    13492  10261  12739   -309    922    191  A    O1-
ATOM   2025  N   GLU A 274      12.170  30.452 487.302  1.00 67.09      A    N  
ANISOU 2025  N   GLU A 274    10342   6311   8840   -152   -257    186  A    N  
ATOM   2026  CA  GLU A 274      13.427  30.733 487.986  1.00 60.43      A    C  
ANISOU 2026  CA  GLU A 274     9669   5407   7886    -78   -540    142  A    C  
ATOM   2027  C   GLU A 274      14.600  30.651 487.018  1.00 56.15      A    C  
ANISOU 2027  C   GLU A 274     8914   4815   7606    -46   -779    115  A    C  
ATOM   2028  O   GLU A 274      14.737  29.667 486.280  1.00 45.11      A    O  
ANISOU 2028  O   GLU A 274     7403   3379   6356    -72   -790    192  A    O  
ATOM   2029  CB  GLU A 274      13.648  29.748 489.127  1.00 66.39      A    C  
ANISOU 2029  CB  GLU A 274    10751   6092   8382    -81   -613    262  A    C  
ATOM   2030  CG  GLU A 274      12.579  29.778 490.190  1.00 88.82      A    C  
ANISOU 2030  CG  GLU A 274    13849   8972  10929   -108   -351    305  A    C  
ATOM   2031  CD  GLU A 274      13.005  29.018 491.426  1.00105.23      A    C  
ANISOU 2031  CD  GLU A 274    16314  10971  12698    -91   -472    416  A    C  
ATOM   2032  OE1 GLU A 274      14.232  28.907 491.652  1.00103.96      A    O  
ANISOU 2032  OE1 GLU A 274    16239  10735  12527    -31   -817    406  A    O  
ATOM   2033  OE2 GLU A 274      12.125  28.498 492.145  1.00112.21      A    O1-
ANISOU 2033  OE2 GLU A 274    17408  11862  13366   -139   -225    525  A    O1-
ATOM   2034  N   LEU A 275      15.474  31.659 487.069  1.00 56.89      A    N  
ANISOU 2034  N   LEU A 275     8964   4895   7758     12   -967      4  A    N  
ATOM   2035  CA  LEU A 275      16.689  31.669 486.265  1.00 49.06      A    C  
ANISOU 2035  CA  LEU A 275     7766   3849   7026     47  -1180    -18  A    C  
ATOM   2036  C   LEU A 275      17.708  30.724 486.899  1.00 79.90      A    C  
ANISOU 2036  C   LEU A 275    11815   7655  10889     85  -1438     61  A    C  
ATOM   2037  O   LEU A 275      18.237  30.983 487.989  1.00 71.55      A    O  
ANISOU 2037  O   LEU A 275    10970   6553   9662    121  -1641     41  A    O  
ATOM   2038  CB  LEU A 275      17.255  33.076 486.140  1.00 41.18      A    C  
ANISOU 2038  CB  LEU A 275     6658   2852   6136     79  -1287   -149  A    C  
ATOM   2039  CG  LEU A 275      18.473  33.161 485.210  1.00 40.93      A    C  
ANISOU 2039  CG  LEU A 275     6370   2767   6415    107  -1454   -162  A    C  
ATOM   2040  CD1 LEU A 275      18.088  32.811 483.778  1.00 42.61      A    C  
ANISOU 2040  CD1 LEU A 275     6349   3021   6820     84  -1263   -127  A    C  
ATOM   2041  CD2 LEU A 275      19.188  34.510 485.278  1.00 40.60      A    C  
ANISOU 2041  CD2 LEU A 275     6241   2694   6493    125  -1601   -277  A    C  
ATOM   2042  N   TRP A 276      17.944  29.605 486.233  1.00 42.41      A    N  
ANISOU 2042  N   TRP A 276     6969   2859   6285     84  -1438    151  A    N  
ATOM   2043  CA  TRP A 276      18.832  28.578 486.726  1.00 43.94      A    C  
ANISOU 2043  CA  TRP A 276     7278   2943   6475    131  -1665    243  A    C  
ATOM   2044  C   TRP A 276      20.273  28.831 486.309  1.00 52.45      A    C  
ANISOU 2044  C   TRP A 276     8151   3953   7825    205  -1920    198  A    C  
ATOM   2045  O   TRP A 276      21.208  28.504 487.054  1.00 45.91      A    O  
ANISOU 2045  O   TRP A 276     7424   3033   6985    263  -2202    236  A    O  
ATOM   2046  CB  TRP A 276      18.335  27.230 486.202  1.00 43.53      A    C  
ANISOU 2046  CB  TRP A 276     7221   2851   6465     96  -1526    355  A    C  
ATOM   2047  CG  TRP A 276      19.092  26.050 486.679  1.00 45.23      A    C  
ANISOU 2047  CG  TRP A 276     7570   2935   6680    148  -1728    468  A    C  
ATOM   2048  CD1 TRP A 276      18.815  25.299 487.775  1.00 47.32      A    C  
ANISOU 2048  CD1 TRP A 276     8143   3142   6694    135  -1771    589  A    C  
ATOM   2049  CD2 TRP A 276      20.248  25.464 486.069  1.00 45.27      A    C  
ANISOU 2049  CD2 TRP A 276     7407   2838   6957    230  -1904    483  A    C  
ATOM   2050  CE2 TRP A 276      20.615  24.365 486.850  1.00 47.39      A    C  
ANISOU 2050  CE2 TRP A 276     7888   2983   7137    269  -2071    611  A    C  
ATOM   2051  CE3 TRP A 276      21.005  25.764 484.933  1.00 57.73      A    C  
ANISOU 2051  CE3 TRP A 276     8678   4410   8845    279  -1916    405  A    C  
ATOM   2052  NE1 TRP A 276      19.720  24.280 487.884  1.00 48.60      A    N  
ANISOU 2052  NE1 TRP A 276     8344   3165   6958    205  -1989    681  A    N  
ATOM   2053  CZ2 TRP A 276      21.707  23.565 486.538  1.00 52.43      A    C  
ANISOU 2053  CZ2 TRP A 276     8422   3489   8012    367  -2263    656  A    C  
ATOM   2054  CZ3 TRP A 276      22.083  24.965 484.623  1.00 44.85      A    C  
ANISOU 2054  CZ3 TRP A 276     6944   2656   7441    372  -2074    446  A    C  
ATOM   2055  CH2 TRP A 276      22.425  23.883 485.419  1.00 46.93      A    C  
ANISOU 2055  CH2 TRP A 276     7403   2794   7635    420  -2252    566  A    C  
ATOM   2056  N   GLY A 277      20.455  29.404 485.129  1.00 45.26      A    N  
ANISOU 2056  N   GLY A 277     6952   3079   7164    203  -1821    127  A    N  
ATOM   2057  CA  GLY A 277      21.771  29.627 484.572  1.00 51.27      A    C  
ANISOU 2057  CA  GLY A 277     7474   3776   8229    266  -1992     95  A    C  
ATOM   2058  C   GLY A 277      21.654  30.398 483.276  1.00 53.79      A    C  
ANISOU 2058  C   GLY A 277     7530   4159   8751    245  -1800     26  A    C  
ATOM   2059  O   GLY A 277      20.603  30.963 482.959  1.00 57.12      A    O  
ANISOU 2059  O   GLY A 277     7965   4672   9067    188  -1593    -12  A    O  
ATOM   2060  N   ILE A 278      22.750  30.420 482.519  1.00 40.85      A    N  
ANISOU 2060  N   ILE A 278     5647   2462   7411    297  -1864     17  A    N  
ATOM   2061  CA  ILE A 278      22.783  31.114 481.238  1.00 42.70      A    C  
ANISOU 2061  CA  ILE A 278     5646   2740   7836    285  -1678    -30  A    C  
ATOM   2062  C   ILE A 278      23.611  30.310 480.245  1.00 42.81      A    C  
ANISOU 2062  C   ILE A 278     5476   2688   8100    353  -1628      7  A    C  
ATOM   2063  O   ILE A 278      24.565  29.621 480.622  1.00 55.13      A    O  
ANISOU 2063  O   ILE A 278     7000   4151   9795    423  -1806     48  A    O  
ATOM   2064  CB  ILE A 278      23.351  32.547 481.431  1.00 41.90      A    C  
ANISOU 2064  CB  ILE A 278     5425   2637   7859    268  -1783   -105  A    C  
ATOM   2065  CG1 ILE A 278      22.298  33.434 482.083  1.00 45.22      A    C  
ANISOU 2065  CG1 ILE A 278     6023   3131   8030    208  -1735   -164  A    C  
ATOM   2066  CG2 ILE A 278      23.843  33.185 480.128  1.00 38.48      A    C  
ANISOU 2066  CG2 ILE A 278     4718   2205   7696    271  -1635   -123  A    C  
ATOM   2067  CD1 ILE A 278      22.870  34.417 483.037  1.00 53.60      A    C  
ANISOU 2067  CD1 ILE A 278     7127   4143   9095    202  -1968   -237  A    C  
ATOM   2068  N   VAL A 279      23.257  30.408 478.966  1.00 37.57      A    N  
ANISOU 2068  N   VAL A 279     4705   2071   7500    342  -1388     -9  A    N  
ATOM   2069  CA  VAL A 279      24.131  29.971 477.885  1.00 37.90      A    C  
ANISOU 2069  CA  VAL A 279     4551   2118   7732    401  -1273      1  A    C  
ATOM   2070  C   VAL A 279      24.806  31.209 477.303  1.00 41.41      A    C  
ANISOU 2070  C   VAL A 279     4772   2590   8371    392  -1218    -31  A    C  
ATOM   2071  O   VAL A 279      24.156  32.022 476.638  1.00 44.84      A    O  
ANISOU 2071  O   VAL A 279     5198   3091   8749    343  -1060    -56  A    O  
ATOM   2072  CB  VAL A 279      23.363  29.194 476.812  1.00 36.82      A    C  
ANISOU 2072  CB  VAL A 279     4482   2022   7488    396  -1045      4  A    C  
ATOM   2073  CG1 VAL A 279      24.312  28.796 475.694  1.00 37.51      A    C  
ANISOU 2073  CG1 VAL A 279     4404   2095   7754    471   -911      0  A    C  
ATOM   2074  CG2 VAL A 279      22.707  27.948 477.422  1.00 38.21      A    C  
ANISOU 2074  CG2 VAL A 279     4869   2148   7501    387  -1103     45  A    C  
ATOM   2075  N   ALA A 280      26.109  31.369 477.544  1.00 44.96      A    N  
ANISOU 2075  N   ALA A 280     5032   2979   9074    435  -1355    -23  A    N  
ATOM   2076  CA  ALA A 280      26.861  32.524 477.067  1.00 40.14      A    C  
ANISOU 2076  CA  ALA A 280     4186   2364   8702    413  -1314    -40  A    C  
ATOM   2077  C   ALA A 280      27.699  32.147 475.852  1.00 46.78      A    C  
ANISOU 2077  C   ALA A 280     4820   3198   9756    470  -1101    -12  A    C  
ATOM   2078  O   ALA A 280      28.390  31.126 475.857  1.00 49.40      A    O  
ANISOU 2078  O   ALA A 280     5094   3484  10191    545  -1130     12  A    O  
ATOM   2079  CB  ALA A 280      27.742  33.098 478.170  1.00 41.93      A    C  
ANISOU 2079  CB  ALA A 280     4318   2504   9111    404  -1625    -55  A    C  
ATOM   2080  N   CYS A 281      27.638  32.976 474.818  1.00 40.32      A    N  
ANISOU 2080  N   CYS A 281     3906   2414   8998    440   -878    -11  A    N  
ATOM   2081  CA  CYS A 281      28.360  32.775 473.573  1.00 41.20      A    C  
ANISOU 2081  CA  CYS A 281     3854   2509   9292    493   -625     18  A    C  
ATOM   2082  C   CYS A 281      29.196  34.022 473.320  1.00 59.02      A    C  
ANISOU 2082  C   CYS A 281     5859   4722  11845    449   -586     40  A    C  
ATOM   2083  O   CYS A 281      28.646  35.117 473.160  1.00 49.48      A    O  
ANISOU 2083  O   CYS A 281     4686   3541  10573    377   -544     35  A    O  
ATOM   2084  CB  CYS A 281      27.395  32.533 472.411  1.00 39.73      A    C  
ANISOU 2084  CB  CYS A 281     3840   2382   8874    500   -362     12  A    C  
ATOM   2085  SG  CYS A 281      26.086  31.328 472.730  1.00 38.21      A    S  
ANISOU 2085  SG  CYS A 281     3956   2231   8332    504   -421    -17  A    S  
ATOM   2086  N   HIS A 282      30.516  33.855 473.293  1.00 60.85      A    N  
ANISOU 2086  N   HIS A 282     5829   4876  12417    487   -601     69  A    N  
ATOM   2087  CA  HIS A 282      31.453  34.918 472.974  1.00 46.27      A    C  
ANISOU 2087  CA  HIS A 282     3697   2959  10925    439   -538    105  A    C  
ATOM   2088  C   HIS A 282      32.119  34.609 471.642  1.00 47.59      A    C  
ANISOU 2088  C   HIS A 282     3720   3104  11259    502   -175    158  A    C  
ATOM   2089  O   HIS A 282      32.361  33.440 471.313  1.00 48.19      A    O  
ANISOU 2089  O   HIS A 282     3829   3185  11297    597    -78    154  A    O  
ATOM   2090  CB  HIS A 282      32.504  35.063 474.067  1.00 49.87      A    C  
ANISOU 2090  CB  HIS A 282     3936   3321  11691    416   -861     99  A    C  
ATOM   2091  CG  HIS A 282      31.926  35.318 475.425  1.00 64.50      A    C  
ANISOU 2091  CG  HIS A 282     5966   5174  13365    373  -1226     42  A    C  
ATOM   2092  CD2 HIS A 282      30.660  35.603 475.815  1.00 45.41      A    C  
ANISOU 2092  CD2 HIS A 282     3838   2828  10589    338  -1274     -1  A    C  
ATOM   2093  ND1 HIS A 282      32.676  35.240 476.582  1.00 61.36      A    N  
ANISOU 2093  ND1 HIS A 282     5475   4689  13149    367  -1594     23  A    N  
ATOM   2094  CE1 HIS A 282      31.902  35.504 477.622  1.00 52.98      A    C  
ANISOU 2094  CE1 HIS A 282     4659   3636  11834    339  -1847    -30  A    C  
ATOM   2095  NE2 HIS A 282      30.674  35.727 477.183  1.00 46.05      A    N  
ANISOU 2095  NE2 HIS A 282     4009   2858  10631    318  -1639    -46  A    N  
ATOM   2096  N   HIS A 283      32.392  35.663 470.874  1.00 48.23      A    N  
ANISOU 2096  N   HIS A 283     3663   3148  11516    454     37    210  A    N  
ATOM   2097  CA  HIS A 283      33.102  35.585 469.602  1.00 67.32      A    C  
ANISOU 2097  CA  HIS A 283     5936   5525  14118    508    420    276  A    C  
ATOM   2098  C   HIS A 283      34.224  36.616 469.599  1.00 67.92      A    C  
ANISOU 2098  C   HIS A 283     5668   5490  14648    430    452    345  A    C  
ATOM   2099  O   HIS A 283      34.108  37.694 470.189  1.00 73.62      A    O  
ANISOU 2099  O   HIS A 283     6327   6171  15473    327    260    343  A    O  
ATOM   2100  CB  HIS A 283      32.171  35.843 468.394  1.00 54.98      A    C  
ANISOU 2100  CB  HIS A 283     4607   4008  12274    531    734    297  A    C  
ATOM   2101  CG  HIS A 283      32.660  35.254 467.103  1.00 57.21      A    C  
ANISOU 2101  CG  HIS A 283     4879   4268  12590    635   1132    335  A    C  
ATOM   2102  CD2 HIS A 283      32.894  35.823 465.896  1.00 68.53      A    C  
ANISOU 2102  CD2 HIS A 283     6287   5660  14091    657   1512    413  A    C  
ATOM   2103  ND1 HIS A 283      33.015  33.928 466.970  1.00 60.91      A    N  
ANISOU 2103  ND1 HIS A 283     5380   4744  13019    742   1182    293  A    N  
ATOM   2104  CE1 HIS A 283      33.405  33.697 465.729  1.00 52.82      A    C  
ANISOU 2104  CE1 HIS A 283     4365   3691  12012    826   1576    327  A    C  
ATOM   2105  NE2 HIS A 283      33.352  34.833 465.058  1.00 78.76      A    N  
ANISOU 2105  NE2 HIS A 283     7618   6949  15357    777   1792    405  A    N  
ATOM   2106  N   THR A 284      35.309  36.290 468.919  1.00 72.03      A    N  
ANISOU 2106  N   THR A 284     5976   5949  15443    474    702    403  A    N  
ATOM   2107  CA  THR A 284      36.488  37.149 468.949  1.00 77.71      A    C  
ANISOU 2107  CA  THR A 284     6363   6538  16625    386    728    477  A    C  
ATOM   2108  C   THR A 284      36.468  38.249 467.879  1.00 72.14      A    C  
ANISOU 2108  C   THR A 284     5615   5788  16009    338   1085    576  A    C  
ATOM   2109  O   THR A 284      37.404  39.053 467.818  1.00 67.34      A    O  
ANISOU 2109  O   THR A 284     4767   5049  15771    259   1134    651  A    O  
ATOM   2110  CB  THR A 284      37.751  36.274 468.829  1.00 72.56      A    C  
ANISOU 2110  CB  THR A 284     5504   5820  16247    451    810    501  A    C  
ATOM   2111  CG2 THR A 284      37.802  35.571 467.476  1.00 61.89      A    C  
ANISOU 2111  CG2 THR A 284     4239   4508  14768    574   1278    535  A    C  
ATOM   2112  OG1 THR A 284      38.926  37.074 469.024  1.00 83.71      A    O  
ANISOU 2112  OG1 THR A 284     6612   7078  18116    362    768    567  A    O  
ATOM   2113  N   LYS A 285      35.434  38.306 467.048  1.00 56.62      A    N  
ANISOU 2113  N   LYS A 285     3904   3905  13704    391   1320    583  A    N  
ATOM   2114  CA  LYS A 285      35.185  39.418 466.146  1.00 68.52      A    C  
ANISOU 2114  CA  LYS A 285     5424   5374  15236    351   1612    681  A    C  
ATOM   2115  C   LYS A 285      33.679  39.633 466.104  1.00 69.93      A    C  
ANISOU 2115  C   LYS A 285     5978   5643  14949    349   1520    632  A    C  
ATOM   2116  O   LYS A 285      32.913  38.745 466.495  1.00 55.24      A    O  
ANISOU 2116  O   LYS A 285     4346   3864  12781    410   1346    534  A    O  
ATOM   2117  CB  LYS A 285      35.724  39.179 464.726  1.00 67.55      A    C  
ANISOU 2117  CB  LYS A 285     5295   5236  15135    428   2129    777  A    C  
ATOM   2118  CG  LYS A 285      35.339  37.873 464.077  1.00 82.24      A    C  
ANISOU 2118  CG  LYS A 285     7406   7181  16662    582   2313    714  A    C  
ATOM   2119  CD  LYS A 285      36.266  37.552 462.894  1.00 94.72      A    C  
ANISOU 2119  CD  LYS A 285     8922   8720  18350    656   2787    794  A    C  
ATOM   2120  CE  LYS A 285      35.929  36.194 462.269  1.00 95.07      A    C  
ANISOU 2120  CE  LYS A 285     9230   8829  18062    817   2954    708  A    C  
ATOM   2121  NZ  LYS A 285      35.942  35.083 463.272  1.00 94.53      A    N1+
ANISOU 2121  NZ  LYS A 285     9147   8795  17976    853   2592    590  A    N1+
ATOM   2122  N   PRO A 286      33.220  40.793 465.623  1.00 70.21      A    N  
ANISOU 2122  N   PRO A 286     6114   5678  14884    250   1623    704  A    N  
ATOM   2123  CA  PRO A 286      31.773  41.029 465.564  1.00 61.25      A    C  
ANISOU 2123  CA  PRO A 286     5348   4645  13279    225   1514    663  A    C  
ATOM   2124  C   PRO A 286      31.075  39.907 464.813  1.00 52.91      A    C  
ANISOU 2124  C   PRO A 286     4585   3692  11826    341   1668    621  A    C  
ATOM   2125  O   PRO A 286      31.678  39.212 463.991  1.00 56.60      A    O  
ANISOU 2125  O   PRO A 286     5025   4146  12334    437   1964    650  A    O  
ATOM   2126  CB  PRO A 286      31.654  42.367 464.825  1.00 67.25      A    C  
ANISOU 2126  CB  PRO A 286     6137   5359  14056    132   1706    786  A    C  
ATOM   2127  CG  PRO A 286      33.059  42.737 464.396  1.00 54.67      A    C  
ANISOU 2127  CG  PRO A 286     4202   3644  12926    106   1969    901  A    C  
ATOM   2128  CD  PRO A 286      33.978  42.011 465.304  1.00 55.61      A    C  
ANISOU 2128  CD  PRO A 286     4023   3717  13391    142   1779    827  A    C  
ATOM   2129  N   ARG A 287      29.802  39.713 465.136  1.00 46.69      A    N  
ANISOU 2129  N   ARG A 287     4073   2998  10668    333   1459    545  A    N  
ATOM   2130  CA  ARG A 287      29.056  38.558 464.649  1.00 45.56      A    C  
ANISOU 2130  CA  ARG A 287     4201   2941  10168    425   1511    480  A    C  
ATOM   2131  C   ARG A 287      27.575  38.845 464.779  1.00 44.08      A    C  
ANISOU 2131  C   ARG A 287     4285   2843   9619    376   1331    442  A    C  
ATOM   2132  O   ARG A 287      27.092  39.091 465.891  1.00 46.13      A    O  
ANISOU 2132  O   ARG A 287     4526   3119   9882    319   1040    384  A    O  
ATOM   2133  CB  ARG A 287      29.427  37.308 465.432  1.00 53.67      A    C  
ANISOU 2133  CB  ARG A 287     5149   3957  11286    498   1352    388  A    C  
ATOM   2134  CG  ARG A 287      28.626  36.083 465.066  1.00 59.89      A    C  
ANISOU 2134  CG  ARG A 287     6215   4809  11731    577   1363    311  A    C  
ATOM   2135  CD  ARG A 287      29.434  34.819 465.358  1.00 61.42      A    C  
ANISOU 2135  CD  ARG A 287     6295   4942  12098    686   1365    259  A    C  
ATOM   2136  NE  ARG A 287      28.825  33.628 464.771  1.00 45.02      A    N  
ANISOU 2136  NE  ARG A 287     4488   2894   9725    768   1441    188  A    N  
ATOM   2137  CZ  ARG A 287      28.941  33.302 463.490  1.00 46.44      A    C  
ANISOU 2137  CZ  ARG A 287     4810   3065   9769    846   1758    194  A    C  
ATOM   2138  NH1 ARG A 287      29.638  34.082 462.676  1.00 61.03      A    N1+
ANISOU 2138  NH1 ARG A 287     6555   4888  11747    852   2054    284  A    N1+
ATOM   2139  NH2 ARG A 287      28.365  32.205 463.019  1.00 46.22      A    N  
ANISOU 2139  NH2 ARG A 287     5044   3045   9472    913   1785    109  A    N  
ATOM   2140  N   ALA A 288      26.860  38.792 463.660  1.00 43.04      A    N  
ANISOU 2140  N   ALA A 288     4409   2765   9179    403   1500    472  A    N  
ATOM   2141  CA  ALA A 288      25.414  38.949 463.648  1.00 41.09      A    C  
ANISOU 2141  CA  ALA A 288     4406   2602   8604    370   1335    440  A    C  
ATOM   2142  C   ALA A 288      24.714  37.599 463.618  1.00 44.87      A    C  
ANISOU 2142  C   ALA A 288     5077   3143   8830    426   1252    340  A    C  
ATOM   2143  O   ALA A 288      25.209  36.621 463.060  1.00 69.08      A    O  
ANISOU 2143  O   ALA A 288     8191   6188  11867    507   1410    312  A    O  
ATOM   2144  CB  ALA A 288      24.958  39.760 462.438  1.00 52.68      A    C  
ANISOU 2144  CB  ALA A 288     6053   4080   9882    360   1512    542  A    C  
ATOM   2145  N   ILE A 289      23.536  37.565 464.210  1.00 45.61      A    N  
ANISOU 2145  N   ILE A 289     5277   3300   8751    381   1015    285  A    N  
ATOM   2146  CA  ILE A 289      22.702  36.379 464.251  1.00 37.22      A    C  
ANISOU 2146  CA  ILE A 289     4390   2287   7463    404    908    199  A    C  
ATOM   2147  C   ILE A 289      21.287  36.798 463.871  1.00 36.25      A    C  
ANISOU 2147  C   ILE A 289     4451   2235   7086    360    808    206  A    C  
ATOM   2148  O   ILE A 289      20.708  37.677 464.523  1.00 44.78      A    O  
ANISOU 2148  O   ILE A 289     5471   3340   8205    302    668    221  A    O  
ATOM   2149  CB  ILE A 289      22.744  35.759 465.653  1.00 50.54      A    C  
ANISOU 2149  CB  ILE A 289     5971   3969   9262    387    694    129  A    C  
ATOM   2150  CG1 ILE A 289      23.947  34.846 465.803  1.00 50.63      A    C  
ANISOU 2150  CG1 ILE A 289     5866   3908   9463    462    769    107  A    C  
ATOM   2151  CG2 ILE A 289      21.469  35.043 466.007  1.00 57.48      A    C  
ANISOU 2151  CG2 ILE A 289     7013   4908   9919    357    524     66  A    C  
ATOM   2152  CD1 ILE A 289      23.857  34.075 467.104  1.00 65.98      A    C  
ANISOU 2152  CD1 ILE A 289     7772   5842  11456    454    537     49  A    C  
ATOM   2153  N   GLY A 290      20.732  36.176 462.816  1.00 47.45      A    N  
ANISOU 2153  N   GLY A 290     6096   3678   8255    392    868    189  A    N  
ATOM   2154  CA  GLY A 290      19.395  36.520 462.347  1.00 36.32      A    C  
ANISOU 2154  CA  GLY A 290     4852   2328   6621    355    747    200  A    C  
ATOM   2155  C   GLY A 290      18.289  36.009 463.267  1.00 50.83      A    C  
ANISOU 2155  C   GLY A 290     6681   4215   8418    301    506    127  A    C  
ATOM   2156  O   GLY A 290      18.519  35.224 464.195  1.00 43.76      A    O  
ANISOU 2156  O   GLY A 290     5706   3306   7614    294    439     66  A    O  
ATOM   2157  N   ARG A 291      17.047  36.438 462.970  1.00 32.88      A    N  
ANISOU 2157  N   ARG A 291     3371   2436   6687    771   1393   -291  A    N  
ATOM   2158  CA  ARG A 291      15.916  36.040 463.807  1.00 32.73      A    C  
ANISOU 2158  CA  ARG A 291     3387   2451   6596    809   1387   -284  A    C  
ATOM   2159  C   ARG A 291      15.717  34.527 463.827  1.00 31.85      A    C  
ANISOU 2159  C   ARG A 291     3265   2380   6458    809   1254   -271  A    C  
ATOM   2160  O   ARG A 291      15.387  33.968 464.875  1.00 34.70      A    O  
ANISOU 2160  O   ARG A 291     3645   2751   6788    822   1205   -291  A    O  
ATOM   2161  CB  ARG A 291      14.629  36.735 463.351  1.00 33.27      A    C  
ANISOU 2161  CB  ARG A 291     3476   2548   6618    872   1505   -207  A    C  
ATOM   2162  CG  ARG A 291      14.621  38.238 463.447  1.00 34.52      A    C  
ANISOU 2162  CG  ARG A 291     3693   2654   6768    918   1642   -219  A    C  
ATOM   2163  CD  ARG A 291      13.184  38.766 463.496  1.00 47.24      A    C  
ANISOU 2163  CD  ARG A 291     5347   4316   8288   1042   1754   -141  A    C  
ATOM   2164  NE  ARG A 291      13.068  40.203 463.245  1.00 41.29      A    N  
ANISOU 2164  NE  ARG A 291     4674   3508   7506   1119   1895   -133  A    N  
ATOM   2165  CZ  ARG A 291      13.386  41.156 464.117  1.00 49.31      A    C  
ANISOU 2165  CZ  ARG A 291     5806   4446   8484   1183   1955   -217  A    C  
ATOM   2166  NH1 ARG A 291      13.868  40.855 465.316  1.00 49.33      A    N1+
ANISOU 2166  NH1 ARG A 291     5852   4421   8472   1175   1885   -317  A    N1+
ATOM   2167  NH2 ARG A 291      13.254  42.426 463.771  1.00 55.38      A    N  
ANISOU 2167  NH2 ARG A 291     6672   5149   9222   1266   2079   -209  A    N  
ATOM   2168  N   ARG A 292      15.995  33.838 462.725  1.00 32.18      A    N  
ANISOU 2168  N   ARG A 292     3299   2429   6497    816   1186   -245  A    N  
ATOM   2169  CA  ARG A 292      15.749  32.398 462.695  1.00 42.87      A    C  
ANISOU 2169  CA  ARG A 292     4693   3792   7804    849   1046   -240  A    C  
ATOM   2170  C   ARG A 292      16.777  31.656 463.537  1.00 49.80      A    C  
ANISOU 2170  C   ARG A 292     5605   4644   8674    854    942   -301  A    C  
ATOM   2171  O   ARG A 292      16.440  30.661 464.191  1.00 52.67      A    O  
ANISOU 2171  O   ARG A 292     6021   4994   9000    871    843   -306  A    O  
ATOM   2172  CB  ARG A 292      15.719  31.880 461.258  1.00 42.43      A    C  
ANISOU 2172  CB  ARG A 292     4677   3736   7710    904    994   -209  A    C  
ATOM   2173  CG  ARG A 292      14.440  32.296 460.598  1.00 47.61      A    C  
ANISOU 2173  CG  ARG A 292     5302   4421   8365    908   1064   -137  A    C  
ATOM   2174  CD  ARG A 292      14.314  31.965 459.137  1.00 41.95      A    C  
ANISOU 2174  CD  ARG A 292     4629   3702   7607    970   1022   -110  A    C  
ATOM   2175  NE  ARG A 292      12.923  32.204 458.732  1.00 48.59      A    N  
ANISOU 2175  NE  ARG A 292     5428   4579   8455    977   1069    -29  A    N  
ATOM   2176  CZ  ARG A 292      12.432  33.414 458.451  1.00 52.01      A    C  
ANISOU 2176  CZ  ARG A 292     5800   5048   8912    967   1224     30  A    C  
ATOM   2177  NH1 ARG A 292      13.224  34.475 458.495  1.00 50.76      A    N1+
ANISOU 2177  NH1 ARG A 292     5636   4868   8783    936   1330      6  A    N1+
ATOM   2178  NH2 ARG A 292      11.160  33.562 458.096  1.00 52.91      A    N  
ANISOU 2178  NH2 ARG A 292     5871   5214   9019   1004   1263    124  A    N  
ATOM   2179  N   ILE A 293      18.037  32.113 463.515  1.00 43.60      A    N  
ANISOU 2179  N   ILE A 293     4793   3844   7927    849    959   -335  A    N  
ATOM   2180  CA  ILE A 293      19.061  31.505 464.362  1.00 46.80      A    C  
ANISOU 2180  CA  ILE A 293     5220   4232   8330    870    871   -380  A    C  
ATOM   2181  C   ILE A 293      18.775  31.801 465.837  1.00 40.40      A    C  
ANISOU 2181  C   ILE A 293     4399   3412   7538    817    886   -425  A    C  
ATOM   2182  O   ILE A 293      18.938  30.942 466.702  1.00 49.62      A    O  
ANISOU 2182  O   ILE A 293     5614   4568   8672    837    793   -448  A    O  
ATOM   2183  CB  ILE A 293      20.454  32.061 463.971  1.00 40.17      A    C  
ANISOU 2183  CB  ILE A 293     4327   3386   7549    886    899   -383  A    C  
ATOM   2184  CG1 ILE A 293      21.028  31.411 462.717  1.00 32.54      A    C  
ANISOU 2184  CG1 ILE A 293     3411   2434   6520   1008    856   -341  A    C  
ATOM   2185  CG2 ILE A 293      21.478  31.728 465.047  1.00 32.25      A    C  
ANISOU 2185  CG2 ILE A 293     3317   2369   6567    900    831   -423  A    C  
ATOM   2186  CD1 ILE A 293      21.503  30.014 462.886  1.00 35.42      A    C  
ANISOU 2186  CD1 ILE A 293     3895   2789   6773   1143    724   -349  A    C  
ATOM   2187  N   ARG A 294      18.317  33.009 466.146  1.00 41.25      A    N  
ANISOU 2187  N   ARG A 294     4480   3515   7678    778   1003   -437  A    N  
ATOM   2188  CA  ARG A 294      17.898  33.322 467.508  1.00 35.47      A    C  
ANISOU 2188  CA  ARG A 294     3787   2771   6921    779   1026   -483  A    C  
ATOM   2189  C   ARG A 294      16.818  32.377 467.989  1.00 31.31      A    C  
ANISOU 2189  C   ARG A 294     3291   2273   6331    811    980   -447  A    C  
ATOM   2190  O   ARG A 294      16.903  31.829 469.091  1.00 31.25      A    O  
ANISOU 2190  O   ARG A 294     3324   2254   6296    824    917   -479  A    O  
ATOM   2191  CB  ARG A 294      17.403  34.761 467.595  1.00 45.64      A    C  
ANISOU 2191  CB  ARG A 294     5100   4038   8205    794   1167   -495  A    C  
ATOM   2192  CG  ARG A 294      18.428  35.765 467.284  1.00 33.12      A    C  
ANISOU 2192  CG  ARG A 294     3500   2395   6691    761   1208   -534  A    C  
ATOM   2193  CD  ARG A 294      17.764  37.060 467.106  1.00 48.08      A    C  
ANISOU 2193  CD  ARG A 294     5454   4255   8557    801   1344   -530  A    C  
ATOM   2194  NE  ARG A 294      18.608  37.989 466.377  1.00 48.32      A    N  
ANISOU 2194  NE  ARG A 294     5458   4228   8674    764   1391   -536  A    N  
ATOM   2195  CZ  ARG A 294      18.156  39.123 465.877  1.00 35.47      A    C  
ANISOU 2195  CZ  ARG A 294     3883   2559   7033    800   1511   -517  A    C  
ATOM   2196  NH1 ARG A 294      16.881  39.436 466.048  1.00 39.53      A    N1+
ANISOU 2196  NH1 ARG A 294     4478   3099   7445    892   1594   -488  A    N1+
ATOM   2197  NH2 ARG A 294      18.964  39.927 465.211  1.00 35.97      A    N  
ANISOU 2197  NH2 ARG A 294     3919   2561   7187    763   1551   -517  A    N  
ATOM   2198  N   ARG A 295      15.769  32.207 467.181  1.00 47.93      A    N  
ANISOU 2198  N   ARG A 295     5378   4412   8421    828   1010   -370  A    N  
ATOM   2199  CA  ARG A 295      14.670  31.343 467.582  1.00 37.15      A    C  
ANISOU 2199  CA  ARG A 295     4022   3071   7022    860    965   -311  A    C  
ATOM   2200  C   ARG A 295      15.150  29.906 467.717  1.00 30.36      A    C  
ANISOU 2200  C   ARG A 295     3224   2161   6150    852    794   -319  A    C  
ATOM   2201  O   ARG A 295      14.758  29.209 468.656  1.00 30.26      A    O  
ANISOU 2201  O   ARG A 295     3250   2130   6118    865    731   -301  A    O  
ATOM   2202  CB  ARG A 295      13.512  31.429 466.582  1.00 45.18      A    C  
ANISOU 2202  CB  ARG A 295     4994   4131   8041    884   1015   -212  A    C  
ATOM   2203  CG  ARG A 295      12.940  32.831 466.227  1.00 31.92      A    C  
ANISOU 2203  CG  ARG A 295     3283   2496   6349    923   1186   -179  A    C  
ATOM   2204  CD  ARG A 295      12.261  33.466 467.367  1.00 50.70      A    C  
ANISOU 2204  CD  ARG A 295     5670   4927   8667   1015   1288   -170  A    C  
ATOM   2205  NE  ARG A 295      11.397  34.582 466.984  1.00 64.12      A    N  
ANISOU 2205  NE  ARG A 295     7359   6687  10319   1108   1441   -103  A    N  
ATOM   2206  CZ  ARG A 295      11.831  35.812 466.714  1.00 59.72      A    C  
ANISOU 2206  CZ  ARG A 295     6866   6075   9750   1124   1537   -151  A    C  
ATOM   2207  NH1 ARG A 295      13.124  36.096 466.753  1.00 56.48      A    N1+
ANISOU 2207  NH1 ARG A 295     6502   5567   9391   1039   1496   -255  A    N1+
ATOM   2208  NH2 ARG A 295      10.967  36.765 466.417  1.00 60.25      A    N  
ANISOU 2208  NH2 ARG A 295     6944   6194   9756   1238   1674    -81  A    N  
ATOM   2209  N   LEU A 296      15.975  29.433 466.771  1.00 30.37      A    N  
ANISOU 2209  N   LEU A 296     3263   2132   6143    859    718   -334  A    N  
ATOM   2210  CA  LEU A 296      16.494  28.068 466.842  1.00 30.48      A    C  
ANISOU 2210  CA  LEU A 296     3407   2075   6100    900    555   -339  A    C  
ATOM   2211  C   LEU A 296      17.325  27.829 468.092  1.00 37.83      A    C  
ANISOU 2211  C   LEU A 296     4364   2987   7023    899    514   -390  A    C  
ATOM   2212  O   LEU A 296      17.141  26.826 468.793  1.00 42.25      A    O  
ANISOU 2212  O   LEU A 296     5033   3482   7539    909    407   -372  A    O  
ATOM   2213  CB  LEU A 296      17.344  27.796 465.607  1.00 30.93      A    C  
ANISOU 2213  CB  LEU A 296     3527   2113   6111    970    513   -347  A    C  
ATOM   2214  CG  LEU A 296      18.213  26.533 465.496  1.00 40.46      A    C  
ANISOU 2214  CG  LEU A 296     4929   3236   7209   1083    372   -355  A    C  
ATOM   2215  CD1 LEU A 296      17.467  25.215 465.674  1.00 34.58      A    C  
ANISOU 2215  CD1 LEU A 296     4406   2359   6375   1097    227   -311  A    C  
ATOM   2216  CD2 LEU A 296      18.917  26.536 464.151  1.00 34.38      A    C  
ANISOU 2216  CD2 LEU A 296     4218   2469   6377   1202    376   -354  A    C  
ATOM   2217  N   LEU A 297      18.144  28.799 468.460  1.00 30.75      A    N  
ANISOU 2217  N   LEU A 297     3382   2127   6174    877    594   -445  A    N  
ATOM   2218  CA  LEU A 297      18.910  28.717 469.696  1.00 30.93      A    C  
ANISOU 2218  CA  LEU A 297     3422   2131   6199    876    558   -497  A    C  
ATOM   2219  C   LEU A 297      17.982  28.621 470.910  1.00 30.77      A    C  
ANISOU 2219  C   LEU A 297     3434   2102   6155    860    565   -498  A    C  
ATOM   2220  O   LEU A 297      18.115  27.722 471.748  1.00 38.21      A    O  
ANISOU 2220  O   LEU A 297     4460   2998   7058    876    470   -496  A    O  
ATOM   2221  CB  LEU A 297      19.868  29.914 469.803  1.00 32.10      A    C  
ANISOU 2221  CB  LEU A 297     3485   2294   6417    847    635   -551  A    C  
ATOM   2222  CG  LEU A 297      21.075  29.991 468.838  1.00 31.65      A    C  
ANISOU 2222  CG  LEU A 297     3382   2245   6398    882    624   -536  A    C  
ATOM   2223  CD1 LEU A 297      21.876  31.240 469.084  1.00 35.35      A    C  
ANISOU 2223  CD1 LEU A 297     3768   2701   6964    833    692   -577  A    C  
ATOM   2224  CD2 LEU A 297      21.972  28.778 468.816  1.00 32.03      A    C  
ANISOU 2224  CD2 LEU A 297     3501   2280   6387    989    510   -513  A    C  
ATOM   2225  N   VAL A 298      17.074  29.588 471.054  1.00 30.82      A    N  
ANISOU 2225  N   VAL A 298     3392   2149   6171    855    688   -494  A    N  
ATOM   2226  CA  VAL A 298      16.233  29.638 472.247  1.00 31.25      A    C  
ANISOU 2226  CA  VAL A 298     3456   2195   6221    886    737   -492  A    C  
ATOM   2227  C   VAL A 298      15.359  28.397 472.357  1.00 33.23      A    C  
ANISOU 2227  C   VAL A 298     3658   2366   6602    869    691   -400  A    C  
ATOM   2228  O   VAL A 298      15.221  27.820 473.442  1.00 32.63      A    O  
ANISOU 2228  O   VAL A 298     3564   2202   6632    864    675   -394  A    O  
ATOM   2229  CB  VAL A 298      15.385  30.923 472.235  1.00 31.72      A    C  
ANISOU 2229  CB  VAL A 298     3492   2320   6239    944    897   -486  A    C  
ATOM   2230  CG1 VAL A 298      14.358  30.898 473.332  1.00 33.16      A    C  
ANISOU 2230  CG1 VAL A 298     3618   2484   6495   1018   1025   -452  A    C  
ATOM   2231  CG2 VAL A 298      16.272  32.119 472.354  1.00 32.25      A    C  
ANISOU 2231  CG2 VAL A 298     3606   2359   6290    937    946   -582  A    C  
ATOM   2232  N   ARG A 299      14.838  27.908 471.227  1.00 39.70      A    N  
ANISOU 2232  N   ARG A 299     4470   3179   7435    852    644   -318  A    N  
ATOM   2233  CA  ARG A 299      14.009  26.704 471.252  1.00 38.14      A    C  
ANISOU 2233  CA  ARG A 299     4243   2837   7414    809    556   -196  A    C  
ATOM   2234  C   ARG A 299      14.847  25.520 471.710  1.00 42.08      A    C  
ANISOU 2234  C   ARG A 299     4905   3211   7874    776    361   -225  A    C  
ATOM   2235  O   ARG A 299      14.346  24.601 472.372  1.00 33.73      A    O  
ANISOU 2235  O   ARG A 299     3859   1992   6965    707    255   -125  A    O  
ATOM   2236  CB  ARG A 299      13.394  26.404 469.887  1.00 35.18      A    C  
ANISOU 2236  CB  ARG A 299     3875   2437   7056    790    504   -107  A    C  
ATOM   2237  CG  ARG A 299      12.430  27.398 469.315  1.00 32.20      A    C  
ANISOU 2237  CG  ARG A 299     3332   2172   6729    827    685    -34  A    C  
ATOM   2238  CD  ARG A 299      11.122  27.498 470.043  1.00 33.80      A    C  
ANISOU 2238  CD  ARG A 299     3297   2374   7172    861    837    168  A    C  
ATOM   2239  NE  ARG A 299      11.229  28.475 471.123  1.00 35.51      A    N  
ANISOU 2239  NE  ARG A 299     3490   2724   7276    953   1020     88  A    N  
ATOM   2240  CZ  ARG A 299      11.147  29.791 470.909  1.00 42.44      A    C  
ANISOU 2240  CZ  ARG A 299     4406   3760   7959   1031   1159     19  A    C  
ATOM   2241  NH1 ARG A 299      10.965  30.234 469.665  1.00 33.23      A    N1+
ANISOU 2241  NH1 ARG A 299     3256   2651   6716   1021   1154     30  A    N1+
ATOM   2242  NH2 ARG A 299      11.253  30.662 471.908  1.00 34.42      A    N  
ANISOU 2242  NH2 ARG A 299     3442   2817   6818   1125   1274    -59  A    N  
ATOM   2243  N   THR A 300      16.113  25.488 471.284  1.00 37.02      A    N  
ANISOU 2243  N   THR A 300     4403   2632   7030    828    303   -316  A    N  
ATOM   2244  CA  THR A 300      16.996  24.400 471.674  1.00 36.11      A    C  
ANISOU 2244  CA  THR A 300     4461   2420   6840    849    157   -328  A    C  
ATOM   2245  C   THR A 300      17.273  24.427 473.173  1.00 32.83      A    C  
ANISOU 2245  C   THR A 300     3976   1969   6528    824    166   -371  A    C  
ATOM   2246  O   THR A 300      17.145  23.404 473.852  1.00 33.82      A    O  
ANISOU 2246  O   THR A 300     4188   1950   6712    782     38   -322  A    O  
ATOM   2247  CB  THR A 300      18.295  24.515 470.888  1.00 31.59      A    C  
ANISOU 2247  CB  THR A 300     3996   1939   6066    958    155   -373  A    C  
ATOM   2248  CG2 THR A 300      19.251  23.439 471.266  1.00 32.42      A    C  
ANISOU 2248  CG2 THR A 300     4275   1953   6088   1035     57   -366  A    C  
ATOM   2249  OG1 THR A 300      18.007  24.422 469.496  1.00 31.67      A    O  
ANISOU 2249  OG1 THR A 300     4055   1940   6039    991    148   -342  A    O  
ATOM   2250  N   VAL A 301      17.598  25.599 473.721  1.00 45.58      A    N  
ANISOU 2250  N   VAL A 301     5469   3689   8160    838    298   -455  A    N  
ATOM   2251  CA  VAL A 301      17.815  25.694 475.167  1.00 41.80      A    C  
ANISOU 2251  CA  VAL A 301     4951   3160   7771    827    313   -514  A    C  
ATOM   2252  C   VAL A 301      16.548  25.294 475.914  1.00 34.35      A    C  
ANISOU 2252  C   VAL A 301     3943   2112   6996    793    335   -430  A    C  
ATOM   2253  O   VAL A 301      16.599  24.601 476.933  1.00 41.42      A    O  
ANISOU 2253  O   VAL A 301     4868   2892   7977    768    249   -413  A    O  
ATOM   2254  CB  VAL A 301      18.275  27.110 475.570  1.00 39.86      A    C  
ANISOU 2254  CB  VAL A 301     4647   2998   7500    844    445   -621  A    C  
ATOM   2255  CG1 VAL A 301      18.250  27.252 477.075  1.00 34.48      A    C  
ANISOU 2255  CG1 VAL A 301     3961   2241   6899    848    476   -696  A    C  
ATOM   2256  CG2 VAL A 301      19.650  27.446 475.009  1.00 32.81      A    C  
ANISOU 2256  CG2 VAL A 301     3768   2157   6542    855    404   -661  A    C  
ATOM   2257  N   GLU A 302      15.386  25.644 475.367  1.00 37.03      A    N  
ANISOU 2257  N   GLU A 302     4179   2477   7415    795    443   -335  A    N  
ATOM   2258  CA  GLU A 302      14.138  25.304 476.035  1.00 35.82      A    C  
ANISOU 2258  CA  GLU A 302     3897   2224   7490    790    500   -159  A    C  
ATOM   2259  C   GLU A 302      13.887  23.807 476.025  1.00 36.68      A    C  
ANISOU 2259  C   GLU A 302     4120   2233   7585    598    217     26  A    C  
ATOM   2260  O   GLU A 302      13.422  23.254 477.028  1.00 38.07      A    O  
ANISOU 2260  O   GLU A 302     4284   2563   7620    455    138    181  A    O  
ATOM   2261  CB  GLU A 302      12.980  26.034 475.368  1.00 36.03      A    C  
ANISOU 2261  CB  GLU A 302     3745   2361   7585    862    698    -29  A    C  
ATOM   2262  CG  GLU A 302      12.862  27.434 475.830  1.00 36.22      A    C  
ANISOU 2262  CG  GLU A 302     3720   2577   7463   1006    959   -134  A    C  
ATOM   2263  CD  GLU A 302      11.943  28.231 474.979  1.00 50.88      A    C  
ANISOU 2263  CD  GLU A 302     5463   4598   9269   1079   1128    -32  A    C  
ATOM   2264  OE1 GLU A 302      11.567  27.740 473.898  1.00 57.56      A    O  
ANISOU 2264  OE1 GLU A 302     6251   5404  10214   1007   1041     83  A    O  
ATOM   2265  OE2 GLU A 302      11.639  29.370 475.377  1.00 57.04      A    O1-
ANISOU 2265  OE2 GLU A 302     6260   5534   9880   1210   1323    -74  A    O1-
ATOM   2266  N   PHE A 303      14.149  23.131 474.903  1.00 41.47      A    N  
ANISOU 2266  N   PHE A 303     4882   2684   8191    560     46     30  A    N  
ATOM   2267  CA  PHE A 303      13.994  21.681 474.919  1.00 37.44      A    C  
ANISOU 2267  CA  PHE A 303     4590   1994   7643    371   -263    193  A    C  
ATOM   2268  C   PHE A 303      15.031  21.047 475.816  1.00 49.76      A    C  
ANISOU 2268  C   PHE A 303     6313   3495   9099    403   -374     90  A    C  
ATOM   2269  O   PHE A 303      14.735  20.081 476.527  1.00 51.93      A    O  
ANISOU 2269  O   PHE A 303     6704   3738   9291    223   -569    249  A    O  
ATOM   2270  CB  PHE A 303      14.093  21.083 473.528  1.00 37.30      A    C  
ANISOU 2270  CB  PHE A 303     4793   1930   7450    349   -400    188  A    C  
ATOM   2271  CG  PHE A 303      13.824  19.604 473.509  1.00 43.04      A    C  
ANISOU 2271  CG  PHE A 303     5823   2473   8057    132   -723    356  A    C  
ATOM   2272  CD1 PHE A 303      12.547  19.118 473.708  1.00 45.62      A    C  
ANISOU 2272  CD1 PHE A 303     6116   2759   8457   -200   -924    680  A    C  
ATOM   2273  CD2 PHE A 303      14.857  18.690 473.327  1.00 39.45      A    C  
ANISOU 2273  CD2 PHE A 303     5685   1951   7352    233   -807    240  A    C  
ATOM   2274  CE1 PHE A 303      12.305  17.748 473.699  1.00 50.85      A    C  
ANISOU 2274  CE1 PHE A 303     7107   3299   8915   -458  -1252    839  A    C  
ATOM   2275  CE2 PHE A 303      14.611  17.342 473.319  1.00 41.51      A    C  
ANISOU 2275  CE2 PHE A 303     6255   2056   7463     53  -1073    372  A    C  
ATOM   2276  CZ  PHE A 303      13.335  16.869 473.509  1.00 43.38      A    C  
ANISOU 2276  CZ  PHE A 303     6504   2243   7733   -304  -1315    649  A    C  
ATOM   2277  N   ALA A 304      16.233  21.622 475.847  1.00 52.44      A    N  
ANISOU 2277  N   ALA A 304     6644   3971   9308    582   -243   -130  A    N  
ATOM   2278  CA  ALA A 304      17.302  21.059 476.663  1.00 49.04      A    C  
ANISOU 2278  CA  ALA A 304     6331   3505   8796    633   -336   -199  A    C  
ATOM   2279  C   ALA A 304      17.003  21.252 478.139  1.00 45.70      A    C  
ANISOU 2279  C   ALA A 304     5788   3028   8548    583   -327   -184  A    C  
ATOM   2280  O   ALA A 304      17.260  20.362 478.956  1.00 44.32      A    O  
ANISOU 2280  O   ALA A 304     5737   2823   8277    514   -491   -120  A    O  
ATOM   2281  CB  ALA A 304      18.643  21.697 476.305  1.00 49.08      A    C  
ANISOU 2281  CB  ALA A 304     6310   3670   8668    790   -220   -350  A    C  
ATOM   2282  N   ALA A 305      16.418  22.394 478.490  1.00 37.50      A    N  
ANISOU 2282  N   ALA A 305     4542   2164   7543    600   -103   -215  A    N  
ATOM   2283  CA  ALA A 305      16.104  22.661 479.884  1.00 44.45      A    C  
ANISOU 2283  CA  ALA A 305     5347   3256   8287    549    -31   -185  A    C  
ATOM   2284  C   ALA A 305      15.060  21.683 480.422  1.00 47.31      A    C  
ANISOU 2284  C   ALA A 305     5719   3759   8498    340   -162     99  A    C  
ATOM   2285  O   ALA A 305      15.291  21.035 481.448  1.00 61.65      A    O  
ANISOU 2285  O   ALA A 305     7608   5621  10195    268   -276    150  A    O  
ATOM   2286  CB  ALA A 305      15.626  24.107 480.045  1.00 38.46      A    C  
ANISOU 2286  CB  ALA A 305     4436   2645   7531    663    253   -266  A    C  
ATOM   2287  N   GLU A 306      13.925  21.525 479.728  1.00 40.66      A    N  
ANISOU 2287  N   GLU A 306     4798   2998   7653    218   -168    315  A    N  
ATOM   2288  CA  GLU A 306      12.948  20.515 480.145  1.00 43.23      A    C  
ANISOU 2288  CA  GLU A 306     5124   3465   7837    -47   -342    641  A    C  
ATOM   2289  C   GLU A 306      13.578  19.127 480.321  1.00 43.68      A    C  
ANISOU 2289  C   GLU A 306     5473   3281   7841   -181   -653    672  A    C  
ATOM   2290  O   GLU A 306      13.298  18.427 481.303  1.00 44.93      A    O  
ANISOU 2290  O   GLU A 306     5661   3550   7859   -337   -766    845  A    O  
ATOM   2291  CB  GLU A 306      11.799  20.413 479.129  1.00 43.27      A    C  
ANISOU 2291  CB  GLU A 306     5029   3552   7859   -210   -380    885  A    C  
ATOM   2292  CG  GLU A 306      11.026  21.716 478.876  1.00 74.57      A    C  
ANISOU 2292  CG  GLU A 306     8701   7783  11848    -56    -67    914  A    C  
ATOM   2293  CD  GLU A 306      10.362  22.326 480.100  1.00 74.90      A    C  
ANISOU 2293  CD  GLU A 306     8526   8202  11731     30    157   1044  A    C  
ATOM   2294  OE1 GLU A 306       9.398  21.744 480.618  1.00 72.61      A    O  
ANISOU 2294  OE1 GLU A 306     8100   8194  11295   -169     84   1395  A    O  
ATOM   2295  OE2 GLU A 306      10.796  23.426 480.523  1.00 71.64      A    O1-
ANISOU 2295  OE2 GLU A 306     8096   7806  11321    303    407    808  A    O1-
ATOM   2296  N   ARG A 307      14.504  18.756 479.437  1.00 42.25      A    N  
ANISOU 2296  N   ARG A 307     5524   2778   7753    -74   -772    503  A    N  
ATOM   2297  CA  ARG A 307      15.207  17.480 479.570  1.00 43.14      A    C  
ANISOU 2297  CA  ARG A 307     5969   2635   7787   -111  -1041    515  A    C  
ATOM   2298  C   ARG A 307      16.016  17.434 480.863  1.00 44.19      A    C  
ANISOU 2298  C   ARG A 307     6087   2851   7853    -14  -1013    419  A    C  
ATOM   2299  O   ARG A 307      15.967  16.447 481.610  1.00 44.92      A    O  
ANISOU 2299  O   ARG A 307     6337   2921   7809   -149  -1195    561  A    O  
ATOM   2300  CB  ARG A 307      16.077  17.242 478.336  1.00 44.11      A    C  
ANISOU 2300  CB  ARG A 307     6331   2435   7993     86  -1115    354  A    C  
ATOM   2301  CG  ARG A 307      16.734  15.873 478.192  1.00 43.56      A    C  
ANISOU 2301  CG  ARG A 307     6652   2189   7711    114  -1327    369  A    C  
ATOM   2302  CD  ARG A 307      15.808  14.727 477.978  1.00 45.77      A    C  
ANISOU 2302  CD  ARG A 307     7197   2363   7832   -189  -1591    607  A    C  
ATOM   2303  NE  ARG A 307      16.512  13.468 478.137  1.00 47.42      A    N  
ANISOU 2303  NE  ARG A 307     7751   2455   7810   -121  -1738    593  A    N  
ATOM   2304  CZ  ARG A 307      15.915  12.302 478.320  1.00 61.97      A    C  
ANISOU 2304  CZ  ARG A 307     9871   4201   9474   -383  -1999    784  A    C  
ATOM   2305  NH1 ARG A 307      14.600  12.241 478.367  1.00 67.96      A    N1+
ANISOU 2305  NH1 ARG A 307    10565   5011  10244   -767  -2145   1037  A    N1+
ATOM   2306  NH2 ARG A 307      16.632  11.195 478.475  1.00 72.91      A    N  
ANISOU 2306  NH2 ARG A 307    11579   5466  10657   -272  -2112    750  A    N  
ATOM   2307  N   LEU A 308      16.778  18.493 481.132  1.00 42.72      A    N  
ANISOU 2307  N   LEU A 308     5729   2752   7751    201   -805    186  A    N  
ATOM   2308  CA  LEU A 308      17.620  18.547 482.324  1.00 42.33      A    C  
ANISOU 2308  CA  LEU A 308     5663   2790   7632    283   -793     82  A    C  
ATOM   2309  C   LEU A 308      16.785  18.463 483.598  1.00 43.78      A    C  
ANISOU 2309  C   LEU A 308     5751   3225   7659    125   -769    245  A    C  
ATOM   2310  O   LEU A 308      17.219  17.866 484.589  1.00 44.81      A    O  
ANISOU 2310  O   LEU A 308     5965   3387   7673    106   -874    272  A    O  
ATOM   2311  CB  LEU A 308      18.462  19.817 482.310  1.00 50.33      A    C  
ANISOU 2311  CB  LEU A 308     6515   3853   8754    471   -599   -170  A    C  
ATOM   2312  CG  LEU A 308      19.516  19.943 483.398  1.00 47.08      A    C  
ANISOU 2312  CG  LEU A 308     6092   3519   8277    542   -622   -290  A    C  
ATOM   2313  CD1 LEU A 308      20.389  18.704 483.365  1.00 42.27      A    C  
ANISOU 2313  CD1 LEU A 308     5675   2767   7619    607   -838   -237  A    C  
ATOM   2314  CD2 LEU A 308      20.352  21.213 483.167  1.00 40.69      A    C  
ANISOU 2314  CD2 LEU A 308     5149   2725   7585    663   -477   -511  A    C  
ATOM   2315  N   TRP A 309      15.642  19.156 483.637  1.00 44.03      A    N  
ANISOU 2315  N   TRP A 309     5585   3473   7671     58   -602    356  A    N  
ATOM   2316  CA  TRP A 309      14.781  19.044 484.809  1.00 45.82      A    C  
ANISOU 2316  CA  TRP A 309     5702   3986   7721    -54   -559    563  A    C  
ATOM   2317  C   TRP A 309      14.220  17.634 484.945  1.00 54.58      A    C  
ANISOU 2317  C   TRP A 309     6937   5070   8731   -321   -818    867  A    C  
ATOM   2318  O   TRP A 309      14.041  17.148 486.066  1.00 49.14      A    O  
ANISOU 2318  O   TRP A 309     6249   4535   7890   -405   -871   1010  A    O  
ATOM   2319  CB  TRP A 309      13.640  20.070 484.795  1.00 49.89      A    C  
ANISOU 2319  CB  TRP A 309     5970   4785   8201    -11   -302    667  A    C  
ATOM   2320  CG  TRP A 309      13.981  21.514 484.412  1.00 44.79      A    C  
ANISOU 2320  CG  TRP A 309     5253   4113   7650    232    -49    397  A    C  
ATOM   2321  CD1 TRP A 309      13.145  22.390 483.807  1.00 44.65      A    C  
ANISOU 2321  CD1 TRP A 309     5080   4223   7663    315    160    451  A    C  
ATOM   2322  CD2 TRP A 309      15.231  22.206 484.576  1.00 43.65      A    C  
ANISOU 2322  CD2 TRP A 309     5204   3808   7575    394     -3     66  A    C  
ATOM   2323  CE2 TRP A 309      15.058  23.495 484.055  1.00 42.93      A    C  
ANISOU 2323  CE2 TRP A 309     5040   3720   7552    549    228    -71  A    C  
ATOM   2324  CE3 TRP A 309      16.473  21.861 485.114  1.00 43.49      A    C  
ANISOU 2324  CE3 TRP A 309     5312   3659   7552    411   -144    -98  A    C  
ATOM   2325  NE1 TRP A 309      13.775  23.578 483.593  1.00 56.56      A    N  
ANISOU 2325  NE1 TRP A 309     6618   5622   9250    524    336    161  A    N  
ATOM   2326  CZ2 TRP A 309      16.074  24.445 484.054  1.00 47.53      A    C  
ANISOU 2326  CZ2 TRP A 309     5696   4160   8205    675    299   -363  A    C  
ATOM   2327  CZ3 TRP A 309      17.481  22.797 485.112  1.00 42.76      A    C  
ANISOU 2327  CZ3 TRP A 309     5244   3472   7530    534    -74   -367  A    C  
ATOM   2328  CH2 TRP A 309      17.277  24.077 484.586  1.00 45.90      A    C  
ANISOU 2328  CH2 TRP A 309     5589   3852   8000    643    136   -497  A    C  
ATOM   2329  N   LEU A 310      13.878  16.977 483.828  1.00 58.53      A    N  
ANISOU 2329  N   LEU A 310     7567   5376   9296   -474   -992    986  A    N  
ATOM   2330  CA  LEU A 310      13.465  15.577 483.926  1.00 49.69      A    C  
ANISOU 2330  CA  LEU A 310     6665   4149   8065   -764  -1294   1263  A    C  
ATOM   2331  C   LEU A 310      14.591  14.711 484.480  1.00 49.98      A    C  
ANISOU 2331  C   LEU A 310     6997   3954   8040   -680  -1465   1149  A    C  
ATOM   2332  O   LEU A 310      14.350  13.779 485.256  1.00 51.96      A    O  
ANISOU 2332  O   LEU A 310     7371   4225   8147   -865  -1637   1359  A    O  
ATOM   2333  CB  LEU A 310      13.007  15.049 482.564  1.00 49.98      A    C  
ANISOU 2333  CB  LEU A 310     6880   3953   8159   -941  -1486   1375  A    C  
ATOM   2334  CG  LEU A 310      12.588  13.567 482.508  1.00 60.51      A    C  
ANISOU 2334  CG  LEU A 310     8546   5085   9359  -1288  -1858   1660  A    C  
ATOM   2335  CD1 LEU A 310      11.504  13.214 483.538  1.00 55.14      A    C  
ANISOU 2335  CD1 LEU A 310     7664   4755   8533  -1605  -1907   2046  A    C  
ATOM   2336  CD2 LEU A 310      12.102  13.219 481.120  1.00 59.00      A    C  
ANISOU 2336  CD2 LEU A 310     8550   4662   9204  -1466  -2047   1748  A    C  
ATOM   2337  N   ILE A 311      15.833  15.011 484.110  1.00 51.71      A    N  
ANISOU 2337  N   ILE A 311     7314   3980   8355   -395  -1415    847  A    N  
ATOM   2338  CA  ILE A 311      16.946  14.193 484.574  1.00 48.83      A    C  
ANISOU 2338  CA  ILE A 311     7205   3432   7916   -268  -1564    767  A    C  
ATOM   2339  C   ILE A 311      17.178  14.420 486.060  1.00 55.29      A    C  
ANISOU 2339  C   ILE A 311     7867   4510   8633   -239  -1480    755  A    C  
ATOM   2340  O   ILE A 311      17.385  13.466 486.817  1.00 67.99      A    O  
ANISOU 2340  O   ILE A 311     9652   6077  10104   -301  -1643    873  A    O  
ATOM   2341  CB  ILE A 311      18.201  14.462 483.731  1.00 47.30      A    C  
ANISOU 2341  CB  ILE A 311     7103   3034   7836     45  -1525    507  A    C  
ATOM   2342  CG1 ILE A 311      18.022  13.833 482.358  1.00 47.52      A    C  
ANISOU 2342  CG1 ILE A 311     7424   2743   7889     32  -1677    556  A    C  
ATOM   2343  CG2 ILE A 311      19.431  13.964 484.407  1.00 47.89      A    C  
ANISOU 2343  CG2 ILE A 311     7303   3061   7831    244  -1595    424  A    C  
ATOM   2344  CD1 ILE A 311      19.039  14.265 481.351  1.00 46.07      A    C  
ANISOU 2344  CD1 ILE A 311     7269   2415   7822    355  -1588    339  A    C  
ATOM   2345  N   HIS A 312      17.121  15.680 486.505  1.00 48.39      A    N  
ANISOU 2345  N   HIS A 312     6698   3889   7801   -142  -1231    618  A    N  
ATOM   2346  CA  HIS A 312      17.236  15.976 487.932  1.00 58.84      A    C  
ANISOU 2346  CA  HIS A 312     7906   5459   8990   -113  -1150    605  A    C  
ATOM   2347  C   HIS A 312      16.112  15.320 488.727  1.00 57.56      A    C  
ANISOU 2347  C   HIS A 312     7716   5490   8664   -342  -1211    928  A    C  
ATOM   2348  O   HIS A 312      16.341  14.745 489.796  1.00 52.74      A    O  
ANISOU 2348  O   HIS A 312     7172   4957   7909   -369  -1294   1006  A    O  
ATOM   2349  CB  HIS A 312      17.261  17.487 488.191  1.00 48.29      A    C  
ANISOU 2349  CB  HIS A 312     6347   4311   7690     31   -883    403  A    C  
ATOM   2350  CG  HIS A 312      18.484  18.168 487.664  1.00 50.98      A    C  
ANISOU 2350  CG  HIS A 312     6692   4508   8169    214   -843    112  A    C  
ATOM   2351  CD2 HIS A 312      19.634  17.663 487.150  1.00 59.79      A    C  
ANISOU 2351  CD2 HIS A 312     7928   5429   9362    317   -978     19  A    C  
ATOM   2352  ND1 HIS A 312      18.605  19.537 487.607  1.00 45.92      A    N  
ANISOU 2352  ND1 HIS A 312     5922   3940   7587    317   -642    -85  A    N  
ATOM   2353  CE1 HIS A 312      19.786  19.847 487.097  1.00 63.13      A    C  
ANISOU 2353  CE1 HIS A 312     8113   5984   9887    424   -674   -274  A    C  
ATOM   2354  NE2 HIS A 312      20.428  18.729 486.808  1.00 45.12      A    N  
ANISOU 2354  NE2 HIS A 312     5957   3568   7619    448   -864   -205  A    N  
ATOM   2355  N   SER A 313      14.880  15.439 488.246  1.00 51.88      A    N  
ANISOU 2355  N   SER A 313     6866   4892   7955   -511  -1164   1147  A    N  
ATOM   2356  CA  SER A 313      13.761  14.888 488.992  1.00 54.29      A    C  
ANISOU 2356  CA  SER A 313     7076   5455   8099   -745  -1211   1515  A    C  
ATOM   2357  C   SER A 313      13.890  13.373 489.150  1.00 64.66      A    C  
ANISOU 2357  C   SER A 313     8680   6557   9331   -971  -1533   1716  A    C  
ATOM   2358  O   SER A 313      13.565  12.829 490.213  1.00 75.71      A    O  
ANISOU 2358  O   SER A 313    10063   8134  10569  -1091  -1590   1935  A    O  
ATOM   2359  CB  SER A 313      12.451  15.268 488.306  1.00 54.85      A    C  
ANISOU 2359  CB  SER A 313     6920   5723   8197   -896  -1122   1758  A    C  
ATOM   2360  OG  SER A 313      11.358  15.219 489.211  1.00 64.11      A    O  
ANISOU 2360  OG  SER A 313     7857   7308   9194  -1022  -1044   2112  A    O  
ATOM   2361  N   ARG A 314      14.384  12.670 488.119  1.00 66.14      A    N  
ANISOU 2361  N   ARG A 314     9177   6351   9604  -1008  -1745   1647  A    N  
ATOM   2362  CA  ARG A 314      14.572  11.222 488.262  1.00 65.88      A    C  
ANISOU 2362  CA  ARG A 314     9521   6051   9459  -1184  -2060   1819  A    C  
ATOM   2363  C   ARG A 314      15.729  10.907 489.207  1.00 68.60      A    C  
ANISOU 2363  C   ARG A 314     9998   6345   9724   -957  -2075   1658  A    C  
ATOM   2364  O   ARG A 314      15.714   9.870 489.887  1.00 78.27      A    O  
ANISOU 2364  O   ARG A 314    11434   7504  10802  -1092  -2265   1850  A    O  
ATOM   2365  CB  ARG A 314      14.849  10.649 486.872  1.00 57.53      A    C  
ANISOU 2365  CB  ARG A 314     8822   4560   8475  -1202  -2260   1754  A    C  
ATOM   2366  CG  ARG A 314      13.598  10.362 486.060  1.00 58.99      A    C  
ANISOU 2366  CG  ARG A 314     9026   4725   8662  -1573  -2408   2040  A    C  
ATOM   2367  CD  ARG A 314      13.980  10.127 484.590  1.00 66.25      A    C  
ANISOU 2367  CD  ARG A 314    10282   5228   9662  -1497  -2542   1886  A    C  
ATOM   2368  NE  ARG A 314      12.864   9.690 483.754  1.00 78.48      A    N  
ANISOU 2368  NE  ARG A 314    11942   6694  11184  -1893  -2760   2163  A    N  
ATOM   2369  CZ  ARG A 314      12.888   9.715 482.420  1.00 71.31      A    C  
ANISOU 2369  CZ  ARG A 314    11178   5618  10298  -1820  -2790   2004  A    C  
ATOM   2370  NH1 ARG A 314      13.961  10.165 481.775  1.00 58.71      A    N1+
ANISOU 2370  NH1 ARG A 314     9655   3862   8789  -1396  -2630   1644  A    N1+
ATOM   2371  NH2 ARG A 314      11.825   9.333 481.727  1.00 75.38      A    N  
ANISOU 2371  NH2 ARG A 314    11695   6230  10716  -2144  -2944   2193  A    N  
ATOM   2372  N   ASN A 315      16.705  11.820 489.299  1.00 64.46      A    N  
ANISOU 2372  N   ASN A 315     9333   5876   9283   -635  -1882   1332  A    N  
ATOM   2373  CA  ASN A 315      17.818  11.683 490.237  1.00 55.58      A    C  
ANISOU 2373  CA  ASN A 315     8259   4780   8078   -426  -1885   1190  A    C  
ATOM   2374  C   ASN A 315      17.343  11.817 491.677  1.00 56.94      A    C  
ANISOU 2374  C   ASN A 315     8249   5291   8095   -510  -1808   1324  A    C  
ATOM   2375  O   ASN A 315      17.829  11.114 492.564  1.00 65.21      A    O  
ANISOU 2375  O   ASN A 315     9428   6341   9008   -484  -1918   1381  A    O  
ATOM   2376  CB  ASN A 315      18.928  12.685 489.914  1.00 53.47      A    C  
ANISOU 2376  CB  ASN A 315     7860   4520   7938   -129  -1728    852  A    C  
ATOM   2377  CG  ASN A 315      19.765  12.261 488.716  1.00 70.55      A    C  
ANISOU 2377  CG  ASN A 315    10255   6357  10195     46  -1830    744  A    C  
ATOM   2378  ND2 ASN A 315      20.572  13.188 488.184  1.00 52.08      A    N  
ANISOU 2378  ND2 ASN A 315     7758   4039   7991    261  -1690    505  A    N  
ATOM   2379  OD1 ASN A 315      19.684  11.108 488.269  1.00 75.54      A    O  
ANISOU 2379  OD1 ASN A 315    11230   6713  10757     -7  -2038    889  A    O  
ATOM   2380  N   VAL A 316      16.384  12.710 491.918  1.00 56.85      A    N  
ANISOU 2380  N   VAL A 316     7945   5577   8079   -578  -1607   1390  A    N  
ATOM   2381  CA  VAL A 316      15.755  12.822 493.231  1.00 58.61      A    C  
ANISOU 2381  CA  VAL A 316     8002   6150   8117   -633  -1514   1569  A    C  
ATOM   2382  C   VAL A 316      15.105  11.499 493.600  1.00 81.67      A    C  
ANISOU 2382  C   VAL A 316    11062   9058  10912   -918  -1735   1950  A    C  
ATOM   2383  O   VAL A 316      15.210  11.030 494.742  1.00 81.48      A    O  
ANISOU 2383  O   VAL A 316    11066   9170  10722   -928  -1778   2065  A    O  
ATOM   2384  CB  VAL A 316      14.742  13.983 493.249  1.00 59.99      A    C  
ANISOU 2384  CB  VAL A 316     7868   6644   8282   -603  -1242   1616  A    C  
ATOM   2385  CG1 VAL A 316      14.037  14.062 494.587  1.00 60.77      A    C  
ANISOU 2385  CG1 VAL A 316     7809   7132   8150   -608  -1126   1840  A    C  
ATOM   2386  CG2 VAL A 316      15.428  15.299 492.915  1.00 56.33      A    C  
ANISOU 2386  CG2 VAL A 316     7335   6141   7926   -338  -1045   1233  A    C  
ATOM   2387  N   GLU A 317      14.432  10.873 492.632  1.00 77.26      A    N  
ANISOU 2387  N   GLU A 317    10614   8322  10418  -1175  -1901   2160  A    N  
ATOM   2388  CA  GLU A 317      13.820   9.569 492.860  1.00 74.20      A    C  
ANISOU 2388  CA  GLU A 317    10423   7861   9911  -1516  -2168   2542  A    C  
ATOM   2389  C   GLU A 317      14.871   8.538 493.254  1.00 65.23      A    C  
ANISOU 2389  C   GLU A 317     9674   6416   8695  -1432  -2378   2465  A    C  
ATOM   2390  O   GLU A 317      14.720   7.838 494.263  1.00 72.20      A    O  
ANISOU 2390  O   GLU A 317    10617   7401   9416  -1547  -2473   2687  A    O  
ATOM   2391  CB  GLU A 317      13.124   9.119 491.578  1.00 80.23      A    C  
ANISOU 2391  CB  GLU A 317    11326   8396  10760  -1806  -2357   2716  A    C  
ATOM   2392  CG  GLU A 317      11.623   9.179 491.552  1.00 87.06      A    C  
ANISOU 2392  CG  GLU A 317    11903   9599  11577  -2159  -2354   3140  A    C  
ATOM   2393  CD  GLU A 317      11.098   8.793 490.182  1.00 87.77      A    C  
ANISOU 2393  CD  GLU A 317    12166   9425  11756  -2442  -2571   3260  A    C  
ATOM   2394  OE1 GLU A 317      10.830   7.585 489.961  1.00 95.43      A    O  
ANISOU 2394  OE1 GLU A 317    13491  10124  12643  -2800  -2921   3518  A    O  
ATOM   2395  OE2 GLU A 317      10.994   9.699 489.319  1.00 71.01      A    O1-
ANISOU 2395  OE2 GLU A 317     9868   7338   9775  -2305  -2404   3084  A    O1-
ATOM   2396  N   ARG A 318      15.955   8.441 492.480  1.00 63.62      A    N  
ANISOU 2396  N   ARG A 318     9726   5859   8587  -1198  -2438   2172  A    N  
ATOM   2397  CA  ARG A 318      16.995   7.476 492.825  1.00 77.09      A    C  
ANISOU 2397  CA  ARG A 318    11799   7300  10193  -1047  -2614   2117  A    C  
ATOM   2398  C   ARG A 318      17.617   7.775 494.186  1.00 77.27      A    C  
ANISOU 2398  C   ARG A 318    11640   7607  10112   -850  -2487   2028  A    C  
ATOM   2399  O   ARG A 318      17.986   6.845 494.918  1.00 79.05      A    O  
ANISOU 2399  O   ARG A 318    12091   7757  10187   -846  -2635   2149  A    O  
ATOM   2400  CB  ARG A 318      18.064   7.441 491.735  1.00 78.28      A    C  
ANISOU 2400  CB  ARG A 318    12197   7100  10444   -756  -2651   1842  A    C  
ATOM   2401  CG  ARG A 318      17.534   6.898 490.430  1.00 79.42      A    C  
ANISOU 2401  CG  ARG A 318    12655   6889  10633   -937  -2834   1939  A    C  
ATOM   2402  CD  ARG A 318      18.600   6.765 489.363  1.00 83.68      A    C  
ANISOU 2402  CD  ARG A 318    13488   7081  11227   -595  -2866   1695  A    C  
ATOM   2403  NE  ARG A 318      17.965   6.423 488.095  1.00 95.73      A    N  
ANISOU 2403  NE  ARG A 318    15293   8294  12786   -779  -3023   1772  A    N  
ATOM   2404  CZ  ARG A 318      17.526   7.320 487.211  1.00 92.96      A    C  
ANISOU 2404  CZ  ARG A 318    14696   8024  12601   -815  -2890   1675  A    C  
ATOM   2405  NH1 ARG A 318      17.675   8.620 487.448  1.00 90.27      A    N1+
ANISOU 2405  NH1 ARG A 318    13856   8038  12407   -666  -2593   1491  A    N1+
ATOM   2406  NH2 ARG A 318      16.944   6.916 486.083  1.00 83.24      A    N  
ANISOU 2406  NH2 ARG A 318    13686   6594  11346   -985  -3018   1720  A    N  
ATOM   2407  N   TYR A 319      17.721   9.056 494.551  1.00 67.76      A    N  
ANISOU 2407  N   TYR A 319    10067   6715   8965   -694  -2227   1825  A    N  
ATOM   2408  CA  TYR A 319      18.263   9.419 495.857  1.00 66.65      A    C  
ANISOU 2408  CA  TYR A 319     9781   6845   8700   -532  -2124   1733  A    C  
ATOM   2409  C   TYR A 319      17.343   8.985 496.992  1.00 80.86      A    C  
ANISOU 2409  C   TYR A 319    11505   8908  10311   -732  -2135   2054  A    C  
ATOM   2410  O   TYR A 319      17.820   8.524 498.035  1.00 84.66      A    O  
ANISOU 2410  O   TYR A 319    12057   9471  10638   -661  -2191   2093  A    O  
ATOM   2411  CB  TYR A 319      18.503  10.923 495.929  1.00 64.43      A    C  
ANISOU 2411  CB  TYR A 319     9203   6784   8494   -351  -1872   1447  A    C  
ATOM   2412  CG  TYR A 319      19.026  11.393 497.267  1.00 68.33      A    C  
ANISOU 2412  CG  TYR A 319     9589   7542   8831   -207  -1786   1336  A    C  
ATOM   2413  CD1 TYR A 319      20.360  11.214 497.617  1.00 72.50      A    C  
ANISOU 2413  CD1 TYR A 319    10209   8009   9327    -24  -1878   1163  A    C  
ATOM   2414  CD2 TYR A 319      18.181  12.016 498.185  1.00 71.73      A    C  
ANISOU 2414  CD2 TYR A 319     9832   8306   9117   -237  -1616   1426  A    C  
ATOM   2415  CE1 TYR A 319      20.843  11.647 498.843  1.00 81.39      A    C  
ANISOU 2415  CE1 TYR A 319    11252   9379  10293     75  -1832   1067  A    C  
ATOM   2416  CE2 TYR A 319      18.649  12.455 499.419  1.00 77.42      A    C  
ANISOU 2416  CE2 TYR A 319    10513   9246   9659    -98  -1552   1313  A    C  
ATOM   2417  CZ  TYR A 319      19.982  12.270 499.744  1.00 84.28      A    C  
ANISOU 2417  CZ  TYR A 319    11485  10029  10509     32  -1676   1125  A    C  
ATOM   2418  OH  TYR A 319      20.460  12.706 500.967  1.00 85.30      A    O  
ANISOU 2418  OH  TYR A 319    11590  10376  10445    140  -1646   1017  A    O  
ATOM   2419  N   MET A 320      16.026   9.137 496.824  1.00 81.58      A    N  
ANISOU 2419  N   MET A 320    11424   9174  10400   -972  -2076   2313  A    N  
ATOM   2420  CA  MET A 320      15.112   8.674 497.864  1.00 84.05      A    C  
ANISOU 2420  CA  MET A 320    11631   9782  10523  -1169  -2086   2686  A    C  
ATOM   2421  C   MET A 320      15.129   7.154 497.993  1.00 84.05      A    C  
ANISOU 2421  C   MET A 320    11971   9528  10434  -1405  -2394   2962  A    C  
ATOM   2422  O   MET A 320      15.054   6.616 499.111  1.00 87.27      A    O  
ANISOU 2422  O   MET A 320    12394  10100  10664  -1450  -2437   3161  A    O  
ATOM   2423  CB  MET A 320      13.691   9.173 497.581  1.00 94.04      A    C  
ANISOU 2423  CB  MET A 320    12591  11345  11795  -1366  -1952   2961  A    C  
ATOM   2424  CG  MET A 320      13.438  10.652 497.889  1.00103.48      A    C  
ANISOU 2424  CG  MET A 320    13456  12891  12970  -1102  -1606   2784  A    C  
ATOM   2425  SD  MET A 320      14.289  11.243 499.381  1.00121.13      A    S  
ANISOU 2425  SD  MET A 320    15678  15333  15011   -759  -1448   2529  A    S  
ATOM   2426  CE  MET A 320      13.481  10.298 500.688  1.00112.21      A    C  
ANISOU 2426  CE  MET A 320    14486  14533  13615   -936  -1507   3016  A    C  
ATOM   2427  N   VAL A 321      15.264   6.446 496.868  1.00 79.10      A    N  
ANISOU 2427  N   VAL A 321    11668   8477   9910  -1537  -2617   2971  A    N  
ATOM   2428  CA  VAL A 321      15.463   5.000 496.931  1.00 79.94      A    C  
ANISOU 2428  CA  VAL A 321    12225   8241   9908  -1706  -2929   3177  A    C  
ATOM   2429  C   VAL A 321      16.738   4.664 497.699  1.00 84.45      A    C  
ANISOU 2429  C   VAL A 321    12976   8730  10382  -1378  -2943   2980  A    C  
ATOM   2430  O   VAL A 321      16.755   3.757 498.542  1.00 83.66      A    O  
ANISOU 2430  O   VAL A 321    13059   8613  10113  -1466  -3083   3200  A    O  
ATOM   2431  CB  VAL A 321      15.469   4.395 495.517  1.00 75.19      A    C  
ANISOU 2431  CB  VAL A 321    12019   7151   9401  -1839  -3159   3166  A    C  
ATOM   2432  CG1 VAL A 321      15.948   2.961 495.564  1.00 78.12      A    C  
ANISOU 2432  CG1 VAL A 321    12973   7083   9627  -1893  -3470   3290  A    C  
ATOM   2433  CG2 VAL A 321      14.078   4.475 494.913  1.00 76.53      A    C  
ANISOU 2433  CG2 VAL A 321    12033   7428   9618  -2266  -3220   3473  A    C  
ATOM   2434  N   THR A 322      17.815   5.409 497.443  1.00 83.46      A    N  
ANISOU 2434  N   THR A 322    12773   8584  10352  -1008  -2800   2590  A    N  
ATOM   2435  CA  THR A 322      19.067   5.193 498.165  1.00 78.40      A    C  
ANISOU 2435  CA  THR A 322    12231   7941   9616   -692  -2808   2423  A    C  
ATOM   2436  C   THR A 322      18.907   5.409 499.670  1.00 77.40      A    C  
ANISOU 2436  C   THR A 322    11867   8215   9326   -691  -2705   2518  A    C  
ATOM   2437  O   THR A 322      19.375   4.598 500.482  1.00 81.61      A    O  
ANISOU 2437  O   THR A 322    12585   8725   9699   -630  -2821   2624  A    O  
ATOM   2438  CB  THR A 322      20.136   6.135 497.603  1.00 71.79      A    C  
ANISOU 2438  CB  THR A 322    11254   7103   8921   -357  -2665   2037  A    C  
ATOM   2439  CG2 THR A 322      21.423   6.050 498.406  1.00 79.49      A    C  
ANISOU 2439  CG2 THR A 322    12236   8176   9791    -54  -2667   1896  A    C  
ATOM   2440  OG1 THR A 322      20.402   5.797 496.240  1.00 67.95      A    O  
ANISOU 2440  OG1 THR A 322    11033   6236   8551   -298  -2764   1965  A    O  
ATOM   2441  N   VAL A 323      18.236   6.492 500.061  1.00 73.17      A    N  
ANISOU 2441  N   VAL A 323    10952   8047   8804   -729  -2483   2488  A    N  
ATOM   2442  CA  VAL A 323      18.012   6.758 501.478  1.00 77.58      A    C  
ANISOU 2442  CA  VAL A 323    11313   8995   9171   -694  -2368   2579  A    C  
ATOM   2443  C   VAL A 323      17.235   5.611 502.110  1.00 89.18      A    C  
ANISOU 2443  C   VAL A 323    12906  10499  10480   -962  -2519   3014  A    C  
ATOM   2444  O   VAL A 323      17.547   5.161 503.224  1.00 89.43      A    O  
ANISOU 2444  O   VAL A 323    12987  10664  10330   -894  -2554   3106  A    O  
ATOM   2445  CB  VAL A 323      17.303   8.113 501.672  1.00 76.18      A    C  
ANISOU 2445  CB  VAL A 323    10774   9173   8999   -652  -2091   2497  A    C  
ATOM   2446  CG1 VAL A 323      16.672   8.203 503.061  1.00 81.09      A    C  
ANISOU 2446  CG1 VAL A 323    11232  10204   9376   -655  -1975   2715  A    C  
ATOM   2447  CG2 VAL A 323      18.272   9.267 501.437  1.00 69.84      A    C  
ANISOU 2447  CG2 VAL A 323     9886   8359   8290   -377  -1961   2057  A    C  
ATOM   2448  N   GLN A 324      16.243   5.078 501.387  1.00 96.28      A    N  
ANISOU 2448  N   GLN A 324    13876  11269  11439  -1294  -2637   3307  A    N  
ATOM   2449  CA  GLN A 324      15.456   3.999 501.974  1.00 99.44      A    C  
ANISOU 2449  CA  GLN A 324    14386  11713  11685  -1616  -2808   3769  A    C  
ATOM   2450  C   GLN A 324      16.249   2.702 502.058  1.00 99.09      A    C  
ANISOU 2450  C   GLN A 324    14828  11262  11560  -1608  -3082   3812  A    C  
ATOM   2451  O   GLN A 324      16.048   1.914 502.991  1.00102.70      A    O  
ANISOU 2451  O   GLN A 324    15382  11799  11839  -1732  -3185   4100  A    O  
ATOM   2452  CB  GLN A 324      14.189   3.764 501.153  1.00106.46      A    C  
ANISOU 2452  CB  GLN A 324    15224  12578  12646  -2034  -2906   4107  A    C  
ATOM   2453  CG  GLN A 324      13.192   4.905 501.229  1.00121.18      A    C  
ANISOU 2453  CG  GLN A 324    16584  14928  14531  -2049  -2626   4195  A    C  
ATOM   2454  CD  GLN A 324      12.749   5.205 502.642  1.00131.42      A    C  
ANISOU 2454  CD  GLN A 324    17577  16743  15612  -1959  -2431   4398  A    C  
ATOM   2455  NE2 GLN A 324      12.217   6.407 502.850  1.00133.13      A    N  
ANISOU 2455  NE2 GLN A 324    17406  17373  15802  -1773  -2119   4346  A    N  
ATOM   2456  OE1 GLN A 324      12.903   4.378 503.544  1.00133.14      A    O  
ANISOU 2456  OE1 GLN A 324    17934  16983  15670  -2020  -2550   4596  A    O  
ATOM   2457  N   ALA A 325      17.179   2.481 501.130  1.00 98.25      A    N  
ANISOU 2457  N   ALA A 325    15037  10735  11560  -1421  -3186   3540  A    N  
ATOM   2458  CA  ALA A 325      18.033   1.303 501.215  1.00101.13      A    C  
ANISOU 2458  CA  ALA A 325    15893  10720  11811  -1305  -3412   3563  A    C  
ATOM   2459  C   ALA A 325      18.988   1.391 502.402  1.00105.46      A    C  
ANISOU 2459  C   ALA A 325    16347  11500  12224   -974  -3317   3433  A    C  
ATOM   2460  O   ALA A 325      19.285   0.374 503.046  1.00102.55      A    O  
ANISOU 2460  O   ALA A 325    16272  11008  11684   -962  -3473   3614  A    O  
ATOM   2461  CB  ALA A 325      18.802   1.126 499.903  1.00 98.44      A    C  
ANISOU 2461  CB  ALA A 325    15894   9922  11586  -1105  -3506   3314  A    C  
ATOM   2462  N   ALA A 326      19.479   2.603 502.702  1.00105.18      A    N  
ANISOU 2462  N   ALA A 326    15925  11788  12249   -719  -3079   3128  A    N  
ATOM   2463  CA  ALA A 326      20.316   2.825 503.886  1.00 94.50      A    C  
ANISOU 2463  CA  ALA A 326    14443  10710  10752   -453  -2999   3009  A    C  
ATOM   2464  C   ALA A 326      19.563   2.607 505.201  1.00 95.22      A    C  
ANISOU 2464  C   ALA A 326    14400  11134  10646   -615  -2965   3299  A    C  
ATOM   2465  O   ALA A 326      20.105   2.001 506.131  1.00 90.70      A    O  
ANISOU 2465  O   ALA A 326    13949  10616   9897   -496  -3038   3377  A    O  
ATOM   2466  CB  ALA A 326      20.922   4.228 503.847  1.00 84.14      A    C  
ANISOU 2466  CB  ALA A 326    12793   9639   9538   -218  -2791   2630  A    C  
ATOM   2467  N   ARG A 327      18.346   3.154 505.338  1.00103.70      A    N  
ANISOU 2467  N   ARG A 327    15191  12482  11726   -843  -2832   3470  A    N  
ATOM   2468  CA  ARG A 327      17.635   2.965 506.608  1.00105.33      A    C  
ANISOU 2468  CA  ARG A 327    15244  13057  11718   -952  -2774   3780  A    C  
ATOM   2469  C   ARG A 327      17.292   1.498 506.872  1.00110.45      A    C  
ANISOU 2469  C   ARG A 327    16206  13508  12252  -1215  -3023   4193  A    C  
ATOM   2470  O   ARG A 327      17.177   1.089 508.035  1.00112.90      A    O  
ANISOU 2470  O   ARG A 327    16488  14049  12358  -1217  -3023   4412  A    O  
ATOM   2471  CB  ARG A 327      16.392   3.853 506.668  1.00104.20      A    C  
ANISOU 2471  CB  ARG A 327    14719  13295  11578  -1087  -2556   3924  A    C  
ATOM   2472  CG  ARG A 327      16.784   5.309 506.553  1.00102.68      A    C  
ANISOU 2472  CG  ARG A 327    14293  13271  11451   -798  -2315   3508  A    C  
ATOM   2473  CD  ARG A 327      15.690   6.299 506.893  1.00105.01      A    C  
ANISOU 2473  CD  ARG A 327    14238  13996  11664   -790  -2047   3620  A    C  
ATOM   2474  NE  ARG A 327      15.065   6.019 508.179  1.00114.02      A    N  
ANISOU 2474  NE  ARG A 327    15259  15526  12536   -803  -1973   3955  A    N  
ATOM   2475  CZ  ARG A 327      13.819   6.355 508.495  1.00115.65      A    C  
ANISOU 2475  CZ  ARG A 327    15182  16135  12625   -877  -1791   4289  A    C  
ATOM   2476  NH1 ARG A 327      13.058   6.997 507.616  1.00112.13      A    N1+
ANISOU 2476  NH1 ARG A 327    14540  15755  12311   -948  -1666   4325  A    N1+
ATOM   2477  NH2 ARG A 327      13.341   6.065 509.698  1.00118.23      A    N  
ANISOU 2477  NH2 ARG A 327    15403  16833  12686   -850  -1719   4607  A    N  
ATOM   2478  N   GLU A 328      17.107   0.698 505.819  1.00111.32      A    N  
ANISOU 2478  N   GLU A 328    16649  13178  12470  -1445  -3246   4313  A    N  
ATOM   2479  CA  GLU A 328      16.879  -0.733 506.004  1.00114.00      A    C  
ANISOU 2479  CA  GLU A 328    17398  13233  12684  -1705  -3526   4685  A    C  
ATOM   2480  C   GLU A 328      18.176  -1.436 506.394  1.00113.47      A    C  
ANISOU 2480  C   GLU A 328    17696  12913  12503  -1374  -3635   4528  A    C  
ATOM   2481  O   GLU A 328      18.180  -2.359 507.223  1.00117.46      A    O  
ANISOU 2481  O   GLU A 328    18414  13394  12822  -1442  -3763   4798  A    O  
ATOM   2482  CB  GLU A 328      16.292  -1.350 504.734  1.00116.73      A    C  
ANISOU 2482  CB  GLU A 328    18067  13142  13144  -2061  -3762   4848  A    C  
ATOM   2483  CG  GLU A 328      15.944  -2.831 504.886  1.00130.07      A    C  
ANISOU 2483  CG  GLU A 328    20201  14512  14708  -2382  -4046   5191  A    C  
ATOM   2484  CD  GLU A 328      16.752  -3.741 503.972  1.00133.06      A    C  
ANISOU 2484  CD  GLU A 328    21137  14287  15132  -2226  -4201   4905  A    C  
ATOM   2485  OE1 GLU A 328      17.028  -3.340 502.816  1.00137.70      A    O  
ANISOU 2485  OE1 GLU A 328    21820  14635  15864  -2119  -4201   4649  A    O  
ATOM   2486  OE2 GLU A 328      17.110  -4.856 504.418  1.00124.08      A    O1-
ANISOU 2486  OE2 GLU A 328    20341  12936  13868  -2184  -4304   4940  A    O1-
ATOM   2487  N   GLN A 329      19.290  -0.977 505.823  1.00106.95      A    N  
ANISOU 2487  N   GLN A 329    16916  11942  11779  -1000  -3573   4118  A    N  
ATOM   2488  CA  GLN A 329      20.609  -1.484 506.181  1.00105.69      A    C  
ANISOU 2488  CA  GLN A 329    17010  11643  11507   -615  -3635   3968  A    C  
ATOM   2489  C   GLN A 329      20.907  -1.288 507.662  1.00107.48      A    C  
ANISOU 2489  C   GLN A 329    16985  12301  11551   -466  -3527   3998  A    C  
ATOM   2490  O   GLN A 329      21.431  -2.198 508.310  1.00114.99      A    O  
ANISOU 2490  O   GLN A 329    18207  13160  12324   -343  -3648   4135  A    O  
ATOM   2491  CB  GLN A 329      21.665  -0.808 505.305  1.00105.89      A    C  
ANISOU 2491  CB  GLN A 329    16987  11566  11682   -258  -3549   3560  A    C  
ATOM   2492  CG  GLN A 329      23.099  -1.174 505.627  1.00116.47      A    C  
ANISOU 2492  CG  GLN A 329    18483  12864  12905    184  -3582   3417  A    C  
ATOM   2493  CD  GLN A 329      23.429  -2.614 505.285  1.00127.47      A    C  
ANISOU 2493  CD  GLN A 329    20501  13770  14163    274  -3812   3610  A    C  
ATOM   2494  NE2 GLN A 329      23.227  -2.984 504.022  1.00123.82      A    N  
ANISOU 2494  NE2 GLN A 329    20397  12858  13789    212  -3924   3601  A    N  
ATOM   2495  OE1 GLN A 329      23.835  -3.398 506.157  1.00129.37      A    O  
ANISOU 2495  OE1 GLN A 329    20938  14021  14197    404  -3894   3771  A    O  
ATOM   2496  N   LEU A 330      20.622  -0.105 508.208  1.00104.87      A    N  
ANISOU 2496  N   LEU A 330    16180  12426  11239   -442  -3301   3861  A    N  
ATOM   2497  CA  LEU A 330      20.807   0.119 509.643  1.00104.60      A    C  
ANISOU 2497  CA  LEU A 330    15940  12806  10998   -312  -3204   3895  A    C  
ATOM   2498  C   LEU A 330      20.074  -0.941 510.461  1.00109.75      A    C  
ANISOU 2498  C   LEU A 330    16748  13489  11462   -548  -3317   4347  A    C  
ATOM   2499  O   LEU A 330      20.633  -1.522 511.406  1.00115.71      A    O  
ANISOU 2499  O   LEU A 330    17623  14317  12024   -395  -3377   4432  A    O  
ATOM   2500  CB  LEU A 330      20.309   1.522 510.001  1.00102.80      A    C  
ANISOU 2500  CB  LEU A 330    15267  13005  10786   -298  -2952   3731  A    C  
ATOM   2501  CG  LEU A 330      20.709   2.268 511.272  1.00100.98      A    C  
ANISOU 2501  CG  LEU A 330    14807  13201  10358    -74  -2810   3583  A    C  
ATOM   2502  CD1 LEU A 330      20.300   3.724 511.102  1.00 95.70      A    C  
ANISOU 2502  CD1 LEU A 330    13834  12772   9756    -36  -2584   3341  A    C  
ATOM   2503  CD2 LEU A 330      20.080   1.677 512.534  1.00106.75      A    C  
ANISOU 2503  CD2 LEU A 330    15524  14202  10834   -160  -2805   3944  A    C  
ATOM   2504  N   SER A 331      18.817  -1.218 510.094  1.00114.83      A    N  
ANISOU 2504  N   SER A 331    17383  14093  12156   -941  -3359   4671  A    N  
ATOM   2505  CA  SER A 331      18.037  -2.223 510.807  1.00118.22      A    C  
ANISOU 2505  CA  SER A 331    17939  14565  12414  -1237  -3487   5160  A    C  
ATOM   2506  C   SER A 331      18.659  -3.609 510.673  1.00123.78      A    C  
ANISOU 2506  C   SER A 331    19214  14779  13038  -1234  -3767   5288  A    C  
ATOM   2507  O   SER A 331      18.622  -4.405 511.621  1.00134.82      A    O  
ANISOU 2507  O   SER A 331    20754  16235  14237  -1279  -3853   5572  A    O  
ATOM   2508  CB  SER A 331      16.597  -2.231 510.292  1.00119.47      A    C  
ANISOU 2508  CB  SER A 331    17954  14785  12654  -1701  -3509   5513  A    C  
ATOM   2509  OG  SER A 331      15.862  -3.299 510.867  1.00130.50      A    O  
ANISOU 2509  OG  SER A 331    19502  16187  13896  -2053  -3682   6037  A    O  
ATOM   2510  N   THR A 332      19.222  -3.924 509.499  1.00118.92      A    N  
ANISOU 2510  N   THR A 332    18961  13671  12553  -1155  -3905   5095  A    N  
ATOM   2511  CA  THR A 332      19.889  -5.215 509.325  1.00122.74      A    C  
ANISOU 2511  CA  THR A 332    20033  13665  12936  -1051  -4127   5159  A    C  
ATOM   2512  C   THR A 332      21.162  -5.314 510.169  1.00122.38      A    C  
ANISOU 2512  C   THR A 332    20035  13742  12721   -574  -4091   5012  A    C  
ATOM   2513  O   THR A 332      21.458  -6.374 510.739  1.00122.29      A    O  
ANISOU 2513  O   THR A 332    20315  13590  12561   -501  -4167   5153  A    O  
ATOM   2514  CB  THR A 332      20.193  -5.453 507.844  1.00118.43      A    C  
ANISOU 2514  CB  THR A 332    19802  12624  12571   -996  -4190   4901  A    C  
ATOM   2515  CG2 THR A 332      20.498  -6.922 507.589  1.00118.94      A    C  
ANISOU 2515  CG2 THR A 332    20386  12227  12579   -961  -4301   4893  A    C  
ATOM   2516  OG1 THR A 332      19.054  -5.078 507.059  1.00118.76      A    O  
ANISOU 2516  OG1 THR A 332    19681  12656  12785  -1412  -4192   4978  A    O  
ATOM   2517  N   THR A 333      21.920  -4.215 510.261  1.00119.15      A    N  
ANISOU 2517  N   THR A 333    19234  13651  12387   -240  -3886   4634  A    N  
ATOM   2518  CA  THR A 333      23.174  -4.173 511.015  1.00120.79      A    C  
ANISOU 2518  CA  THR A 333    19387  14051  12455    198  -3838   4462  A    C  
ATOM   2519  C   THR A 333      22.951  -4.295 512.521  1.00122.46      A    C  
ANISOU 2519  C   THR A 333    19422  14659  12449    166  -3792   4666  A    C  
ATOM   2520  O   THR A 333      23.788  -4.884 513.223  1.00117.67      A    O  
ANISOU 2520  O   THR A 333    18974  14080  11657    436  -3853   4709  A    O  
ATOM   2521  CB  THR A 333      23.942  -2.889 510.681  1.00114.95      A    C  
ANISOU 2521  CB  THR A 333    18258  13561  11857    462  -3665   4039  A    C  
ATOM   2522  CG2 THR A 333      25.235  -2.800 511.480  1.00115.27      A    C  
ANISOU 2522  CG2 THR A 333    18194  13859  11743    861  -3644   3897  A    C  
ATOM   2523  OG1 THR A 333      24.262  -2.873 509.282  1.00115.39      A    O  
ANISOU 2523  OG1 THR A 333    18501  13247  12094    545  -3707   3870  A    O  
ATOM   2524  N   ALA A 334      21.847  -3.739 513.036  1.00122.72      A    N  
ANISOU 2524  N   ALA A 334    19122  15028  12479   -124  -3672   4808  A    N  
ATOM   2525  CA  ALA A 334      21.594  -3.790 514.477  1.00127.96      A    C  
ANISOU 2525  CA  ALA A 334    19604  16103  12911   -122  -3603   5007  A    C  
ATOM   2526  C   ALA A 334      21.629  -5.222 515.019  1.00130.51      A    C  
ANISOU 2526  C   ALA A 334    20339  16204  13045   -181  -3800   5378  A    C  
ATOM   2527  O   ALA A 334      22.102  -5.463 516.139  1.00123.87      A    O  
ANISOU 2527  O   ALA A 334    19472  15604  11990     16  -3785   5443  A    O  
ATOM   2528  CB  ALA A 334      20.243  -3.140 514.780  1.00122.77      A    C  
ANISOU 2528  CB  ALA A 334    18586  15799  12262   -423  -3446   5194  A    C  
ATOM   2529  N   ASP A 335      21.155  -6.183 514.231  1.00131.78      A    N  
ANISOU 2529  N   ASP A 335    20920  15885  13264   -454  -4001   5623  A    N  
ATOM   2530  CA  ASP A 335      21.082  -7.578 514.652  1.00129.84      A    C  
ANISOU 2530  CA  ASP A 335    21032  15387  12914   -530  -4099   5864  A    C  
ATOM   2531  C   ASP A 335      22.473  -8.206 514.736  1.00124.40      A    C  
ANISOU 2531  C   ASP A 335    20668  14477  12120    -61  -4152   5688  A    C  
ATOM   2532  O   ASP A 335      23.081  -8.248 515.810  1.00124.14      A    O  
ANISOU 2532  O   ASP A 335    20559  14729  11879    198  -4130   5734  A    O  
ATOM   2533  CB  ASP A 335      20.188  -8.370 513.687  1.00133.75      A    C  
ANISOU 2533  CB  ASP A 335    21774  15448  13595   -936  -4181   5964  A    C  
ATOM   2534  CG  ASP A 335      18.860  -7.667 513.401  1.00131.44      A    C  
ANISOU 2534  CG  ASP A 335    21109  15399  13433  -1374  -4122   6124  A    C  
ATOM   2535  OD1 ASP A 335      18.311  -7.026 514.326  1.00133.76      A    O  
ANISOU 2535  OD1 ASP A 335    20988  16217  13617  -1441  -3994   6316  A    O  
ATOM   2536  OD2 ASP A 335      18.368  -7.749 512.252  1.00118.09      A    O1-
ANISOU 2536  OD2 ASP A 335    19527  13405  11936  -1626  -4190   6060  A    O1-
ATOM   2537  N   LYS A 337      25.672  -6.774 515.973  1.00127.52      A    N  
ANISOU 2537  N   LYS A 337    20598  15619  12233   1110  -4017   5076  A    N  
ATOM   2538  CA  LYS A 337      26.364  -5.799 516.810  1.00125.98      A    C  
ANISOU 2538  CA  LYS A 337    19944  15959  11963   1337  -3886   4836  A    C  
ATOM   2539  C   LYS A 337      25.701  -5.729 518.176  1.00131.26      A    C  
ANISOU 2539  C   LYS A 337    20421  17016  12438   1181  -3824   5037  A    C  
ATOM   2540  O   LYS A 337      24.494  -5.956 518.313  1.00130.96      A    O  
ANISOU 2540  O   LYS A 337    20407  16947  12405    832  -3812   5301  A    O  
ATOM   2541  CB  LYS A 337      26.376  -4.410 516.158  1.00121.36      A    C  
ANISOU 2541  CB  LYS A 337    18968  15543  11600   1296  -3749   4470  A    C  
ATOM   2542  CG  LYS A 337      26.764  -4.417 514.692  1.00127.51      A    C  
ANISOU 2542  CG  LYS A 337    19914  15936  12598   1384  -3788   4303  A    C  
ATOM   2543  CD  LYS A 337      28.033  -5.227 514.456  1.00132.74      A    C  
ANISOU 2543  CD  LYS A 337    20866  16416  13152   1810  -3894   4320  A    C  
ATOM   2544  CE  LYS A 337      28.366  -5.308 512.973  1.00132.57      A    C  
ANISOU 2544  CE  LYS A 337    21060  15998  13312   1939  -3921   4187  A    C  
ATOM   2545  NZ  LYS A 337      29.422  -6.325 512.724  1.00138.47      A    N1+
ANISOU 2545  NZ  LYS A 337    22203  16509  13899   2389  -4017   4293  A    N1+
ATOM   2546  N   HIS A 338      26.510  -5.412 519.187  1.00134.15      A    N  
ANISOU 2546  N   HIS A 338    20585  17774  12613   1445  -3792   4934  A    N  
ATOM   2547  CA  HIS A 338      26.055  -5.302 520.565  1.00138.18      A    C  
ANISOU 2547  CA  HIS A 338    20923  18689  12891   1383  -3727   5093  A    C  
ATOM   2548  C   HIS A 338      25.930  -3.859 521.040  1.00139.50      A    C  
ANISOU 2548  C   HIS A 338    20663  19302  13039   1375  -3567   4806  A    C  
ATOM   2549  O   HIS A 338      25.369  -3.626 522.118  1.00142.46      A    O  
ANISOU 2549  O   HIS A 338    20898  20018  13211   1323  -3479   4926  A    O  
ATOM   2550  CB  HIS A 338      27.018  -6.058 521.491  1.00135.63      A    C  
ANISOU 2550  CB  HIS A 338    20740  18487  12305   1690  -3826   5215  A    C  
ATOM   2551  CG  HIS A 338      26.480  -6.306 522.868  1.00139.52      A    C  
ANISOU 2551  CG  HIS A 338    21173  19302  12534   1623  -3788   5475  A    C  
ATOM   2552  CD2 HIS A 338      26.695  -5.661 524.040  1.00143.69      A    C  
ANISOU 2552  CD2 HIS A 338    21433  20320  12841   1742  -3715   5385  A    C  
ATOM   2553  ND1 HIS A 338      25.629  -7.350 523.158  1.00145.95      A    N  
ANISOU 2553  ND1 HIS A 338    22250  19937  13268   1412  -3842   5900  A    N  
ATOM   2554  CE1 HIS A 338      25.337  -7.335 524.448  1.00148.53      A    C  
ANISOU 2554  CE1 HIS A 338    22434  20657  13344   1424  -3779   6073  A    C  
ATOM   2555  NE2 HIS A 338      25.971  -6.320 525.006  1.00147.84      A    N  
ANISOU 2555  NE2 HIS A 338    22042  20973  13159   1639  -3699   5754  A    N  
ATOM   2556  N   SER A 339      26.430  -2.893 520.272  1.00132.12      A    N  
ANISOU 2556  N   SER A 339    19552  18360  12286   1436  -3528   4441  A    N  
ATOM   2557  CA  SER A 339      26.474  -1.501 520.696  1.00128.60      A    C  
ANISOU 2557  CA  SER A 339    18785  18279  11796   1450  -3411   4136  A    C  
ATOM   2558  C   SER A 339      25.921  -0.593 519.608  1.00127.22      A    C  
ANISOU 2558  C   SER A 339    18483  17963  11892   1282  -3303   3920  A    C  
ATOM   2559  O   SER A 339      25.745  -0.987 518.451  1.00132.47      A    O  
ANISOU 2559  O   SER A 339    19278  18262  12793   1189  -3338   3956  A    O  
ATOM   2560  CB  SER A 339      27.902  -1.060 521.046  1.00127.46      A    C  
ANISOU 2560  CB  SER A 339    18526  18354  11550   1706  -3506   3881  A    C  
ATOM   2561  OG  SER A 339      28.017   0.354 520.987  1.00121.08      A    O  
ANISOU 2561  OG  SER A 339    17482  17742  10781   1662  -3436   3532  A    O  
ATOM   2562  N   SER A 340      25.661   0.652 520.007  1.00122.47      A    N  
ANISOU 2562  N   SER A 340    17659  17647  11226   1264  -3174   3689  A    N  
ATOM   2563  CA  SER A 340      25.211   1.669 519.067  1.00121.02      A    C  
ANISOU 2563  CA  SER A 340    17344  17370  11269   1146  -3057   3453  A    C  
ATOM   2564  C   SER A 340      26.376   2.247 518.270  1.00119.56      A    C  
ANISOU 2564  C   SER A 340    17095  17078  11256   1248  -3142   3116  A    C  
ATOM   2565  O   SER A 340      26.252   2.484 517.062  1.00106.03      A    O  
ANISOU 2565  O   SER A 340    15366  15108   9813   1168  -3114   3008  A    O  
ATOM   2566  CB  SER A 340      24.472   2.772 519.826  1.00120.57      A    C  
ANISOU 2566  CB  SER A 340    17139  17639  11032   1134  -2877   3350  A    C  
ATOM   2567  OG  SER A 340      24.189   3.878 518.987  1.00119.06      A    O  
ANISOU 2567  OG  SER A 340    16839  17373  11028   1069  -2764   3082  A    O  
ATOM   2568  N   HIS A 341      27.516   2.475 518.931  1.00127.08      A    N  
ANISOU 2568  N   HIS A 341    17990  18251  12045   1415  -3255   2974  A    N  
ATOM   2569  CA  HIS A 341      28.708   2.987 518.266  1.00119.16      A    C  
ANISOU 2569  CA  HIS A 341    16876  17225  11176   1500  -3357   2721  A    C  
ATOM   2570  C   HIS A 341      29.335   1.973 517.322  1.00114.85      A    C  
ANISOU 2570  C   HIS A 341    16440  16400  10798   1629  -3450   2857  A    C  
ATOM   2571  O   HIS A 341      30.213   2.343 516.537  1.00109.58      A    O  
ANISOU 2571  O   HIS A 341    15662  15695  10279   1713  -3503   2694  A    O  
ATOM   2572  CB  HIS A 341      29.734   3.435 519.312  1.00124.92      A    C  
ANISOU 2572  CB  HIS A 341    17500  18314  11648   1606  -3484   2600  A    C  
ATOM   2573  CG  HIS A 341      29.371   4.718 519.993  1.00128.49      A    C  
ANISOU 2573  CG  HIS A 341    17896  18983  11941   1502  -3421   2357  A    C  
ATOM   2574  CD2 HIS A 341      28.469   4.990 520.966  1.00127.00      A    C  
ANISOU 2574  CD2 HIS A 341    17785  18956  11514   1482  -3306   2398  A    C  
ATOM   2575  ND1 HIS A 341      29.952   5.924 519.663  1.00127.83      A    N  
ANISOU 2575  ND1 HIS A 341    17702  18951  11917   1424  -3475   2039  A    N  
ATOM   2576  CE1 HIS A 341      29.428   6.882 520.408  1.00124.59      A    C  
ANISOU 2576  CE1 HIS A 341    17358  18682  11298   1364  -3407   1872  A    C  
ATOM   2577  NE2 HIS A 341      28.524   6.342 521.205  1.00123.29      A    N  
ANISOU 2577  NE2 HIS A 341    17300  18602  10943   1426  -3289   2084  A    N  
ATOM   2578  N   GLU A 342      28.907   0.711 517.380  1.00125.47      A    N  
ANISOU 2578  N   GLU A 342    18027  17545  12101   1658  -3474   3166  A    N  
ATOM   2579  CA  GLU A 342      29.444  -0.292 516.470  1.00120.17      A    C  
ANISOU 2579  CA  GLU A 342    17568  16548  11543   1821  -3562   3296  A    C  
ATOM   2580  C   GLU A 342      28.875  -0.083 515.076  1.00108.74      A    C  
ANISOU 2580  C   GLU A 342    16181  14746  10389   1683  -3497   3208  A    C  
ATOM   2581  O   GLU A 342      29.584  -0.221 514.075  1.00109.48      A    O  
ANISOU 2581  O   GLU A 342    16324  14650  10622   1848  -3537   3136  A    O  
ATOM   2582  CB  GLU A 342      29.068  -1.685 516.985  1.00126.86      A    C  
ANISOU 2582  CB  GLU A 342    18739  17235  12228   1857  -3627   3655  A    C  
ATOM   2583  CG  GLU A 342      29.885  -2.194 518.183  1.00124.27      A    C  
ANISOU 2583  CG  GLU A 342    18414  17195  11607   2088  -3717   3786  A    C  
ATOM   2584  CD  GLU A 342      31.215  -2.797 517.814  1.00128.50      A    C  
ANISOU 2584  CD  GLU A 342    19031  17692  12103   2451  -3823   3825  A    C  
ATOM   2585  OE1 GLU A 342      31.459  -3.029 516.610  1.00131.43      A    O  
ANISOU 2585  OE1 GLU A 342    19536  17750  12653   2555  -3827   3791  A    O  
ATOM   2586  OE2 GLU A 342      32.017  -3.044 518.741  1.00135.99      A    O1-
ANISOU 2586  OE2 GLU A 342    19906  18946  12817   2659  -3896   3908  A    O1-
ATOM   2587  N   ILE A 343      27.577   0.218 515.013  1.00112.95      A    N  
ANISOU 2587  N   ILE A 343    16706  15214  10997   1400  -3392   3246  A    N  
ATOM   2588  CA  ILE A 343      26.840   0.451 513.770  1.00114.16      A    C  
ANISOU 2588  CA  ILE A 343    16899  15064  11412   1219  -3329   3191  A    C  
ATOM   2589  C   ILE A 343      27.336   1.698 513.029  1.00107.67      A    C  
ANISOU 2589  C   ILE A 343    15823  14309  10776   1254  -3258   2840  A    C  
ATOM   2590  O   ILE A 343      27.452   1.705 511.797  1.00 97.72      A    O  
ANISOU 2590  O   ILE A 343    14625  12773   9733   1268  -3260   2760  A    O  
ATOM   2591  CB  ILE A 343      25.337   0.545 514.105  1.00113.51      A    C  
ANISOU 2591  CB  ILE A 343    16787  15029  11311    918  -3227   3369  A    C  
ATOM   2592  CG1 ILE A 343      24.792  -0.833 514.506  1.00122.90      A    C  
ANISOU 2592  CG1 ILE A 343    18273  16053  12371    814  -3332   3773  A    C  
ATOM   2593  CG2 ILE A 343      24.551   1.152 512.955  1.00100.37      A    C  
ANISOU 2593  CG2 ILE A 343    15050  13185   9902    720  -3133   3270  A    C  
ATOM   2594  CD1 ILE A 343      23.432  -0.788 515.175  1.00125.36      A    C  
ANISOU 2594  CD1 ILE A 343    18480  16561  12588    543  -3237   4032  A    C  
ATOM   2595  N   VAL A 344      27.588   2.782 513.772  1.00114.99      A    N  
ANISOU 2595  N   VAL A 344    16497  15587  11606   1253  -3203   2632  A    N  
ATOM   2596  CA  VAL A 344      28.106   4.045 513.229  1.00106.08      A    C  
ANISOU 2596  CA  VAL A 344    15145  14542  10617   1250  -3161   2305  A    C  
ATOM   2597  C   VAL A 344      29.460   3.877 512.546  1.00102.24      A    C  
ANISOU 2597  C   VAL A 344    14612  14013  10222   1458  -3274   2236  A    C  
ATOM   2598  O   VAL A 344      29.708   4.458 511.481  1.00104.29      A    O  
ANISOU 2598  O   VAL A 344    14774  14152  10699   1450  -3240   2070  A    O  
ATOM   2599  CB  VAL A 344      28.175   5.113 514.340  1.00 99.27      A    C  
ANISOU 2599  CB  VAL A 344    14125  14038   9555   1207  -3131   2126  A    C  
ATOM   2600  CG1 VAL A 344      28.867   6.372 513.832  1.00 91.81      A    C  
ANISOU 2600  CG1 VAL A 344    13000  13157   8727   1178  -3142   1804  A    C  
ATOM   2601  CG2 VAL A 344      26.785   5.431 514.871  1.00102.62      A    C  
ANISOU 2601  CG2 VAL A 344    14576  14529   9884   1065  -2968   2193  A    C  
ATOM   2602  N   ILE A 345      30.361   3.100 513.148  1.00102.96      A    N  
ANISOU 2602  N   ILE A 345    14751  14237  10134   1670  -3398   2385  A    N  
ATOM   2603  CA  ILE A 345      31.682   2.877 512.564  1.00100.06      A    C  
ANISOU 2603  CA  ILE A 345    14305  13905   9807   1929  -3489   2387  A    C  
ATOM   2604  C   ILE A 345      31.595   2.146 511.226  1.00 99.68      A    C  
ANISOU 2604  C   ILE A 345    14480  13451   9943   2061  -3463   2474  A    C  
ATOM   2605  O   ILE A 345      32.399   2.400 510.318  1.00 96.53      A    O  
ANISOU 2605  O   ILE A 345    13966  13040   9671   2224  -3467   2397  A    O  
ATOM   2606  CB  ILE A 345      32.555   2.126 513.597  1.00100.71      A    C  
ANISOU 2606  CB  ILE A 345    14402  14248   9615   2155  -3614   2578  A    C  
ATOM   2607  CG1 ILE A 345      33.109   3.097 514.640  1.00 98.27      A    C  
ANISOU 2607  CG1 ILE A 345    13811  14385   9142   2057  -3687   2432  A    C  
ATOM   2608  CG2 ILE A 345      33.703   1.383 512.941  1.00112.17      A    C  
ANISOU 2608  CG2 ILE A 345    15884  15669  11065   2519  -3680   2721  A    C  
ATOM   2609  CD1 ILE A 345      33.885   2.422 515.743  1.00101.29      A    C  
ANISOU 2609  CD1 ILE A 345    14184  15063   9237   2249  -3814   2624  A    C  
ATOM   2610  N   GLU A 346      30.611   1.261 511.065  1.00104.78      A    N  
ANISOU 2610  N   GLU A 346    15457  13762  10594   1978  -3448   2646  A    N  
ATOM   2611  CA  GLU A 346      30.491   0.451 509.853  1.00103.39      A    C  
ANISOU 2611  CA  GLU A 346    15601  13143  10539   2093  -3463   2741  A    C  
ATOM   2612  C   GLU A 346      29.957   1.228 508.644  1.00 93.01      A    C  
ANISOU 2612  C   GLU A 346    14207  11632   9500   1922  -3371   2549  A    C  
ATOM   2613  O   GLU A 346      30.386   0.963 507.517  1.00 93.93      A    O  
ANISOU 2613  O   GLU A 346    14458  11507   9725   2114  -3377   2532  A    O  
ATOM   2614  CB  GLU A 346      29.617  -0.772 510.140  1.00107.51      A    C  
ANISOU 2614  CB  GLU A 346    16544  13358  10946   1995  -3528   3016  A    C  
ATOM   2615  CG  GLU A 346      29.373  -1.679 508.949  1.00109.19      A    C  
ANISOU 2615  CG  GLU A 346    17204  13045  11237   2063  -3588   3125  A    C  
ATOM   2616  CD  GLU A 346      28.856  -3.039 509.367  1.00121.39      A    C  
ANISOU 2616  CD  GLU A 346    19231  14292  12602   2015  -3713   3435  A    C  
ATOM   2617  OE1 GLU A 346      28.206  -3.125 510.432  1.00124.42      A    O  
ANISOU 2617  OE1 GLU A 346    19544  14854  12876   1784  -3719   3571  A    O  
ATOM   2618  OE2 GLU A 346      29.079  -4.019 508.624  1.00129.47      A    O1-
ANISOU 2618  OE2 GLU A 346    20732  14886  13574   2210  -3809   3553  A    O1-
ATOM   2619  N   HIS A 347      29.050   2.191 508.835  1.00 91.01      A    N  
ANISOU 2619  N   HIS A 347    13751  11487   9343   1608  -3273   2411  A    N  
ATOM   2620  CA  HIS A 347      28.301   2.788 507.726  1.00 98.58      A    C  
ANISOU 2620  CA  HIS A 347    14682  12229  10547   1423  -3180   2281  A    C  
ATOM   2621  C   HIS A 347      28.546   4.278 507.488  1.00 99.18      A    C  
ANISOU 2621  C   HIS A 347    14396  12526  10762   1354  -3078   1985  A    C  
ATOM   2622  O   HIS A 347      27.941   4.842 506.563  1.00 96.69      A    O  
ANISOU 2622  O   HIS A 347    14041  12047  10649   1219  -2988   1871  A    O  
ATOM   2623  CB  HIS A 347      26.788   2.554 507.897  1.00104.96      A    C  
ANISOU 2623  CB  HIS A 347    15611  12906  11361   1104  -3141   2433  A    C  
ATOM   2624  CG  HIS A 347      26.388   1.109 507.888  1.00116.07      A    C  
ANISOU 2624  CG  HIS A 347    17430  14005  12668   1077  -3270   2740  A    C  
ATOM   2625  CD2 HIS A 347      25.312   0.478 508.416  1.00120.59      A    C  
ANISOU 2625  CD2 HIS A 347    18154  14520  13146    820  -3309   3007  A    C  
ATOM   2626  ND1 HIS A 347      27.126   0.134 507.249  1.00119.01      A    N  
ANISOU 2626  ND1 HIS A 347    18144  14066  13009   1332  -3389   2821  A    N  
ATOM   2627  CE1 HIS A 347      26.531  -1.037 507.396  1.00116.92      A    C  
ANISOU 2627  CE1 HIS A 347    18277  13518  12630   1220  -3512   3100  A    C  
ATOM   2628  NE2 HIS A 347      25.430  -0.857 508.104  1.00121.82      A    N  
ANISOU 2628  NE2 HIS A 347    18767  14299  13221    881  -3474   3230  A    N  
ATOM   2629  N   ALA A 348      29.429   4.931 508.256  1.00 99.69      A    N  
ANISOU 2629  N   ALA A 348    14219  12941  10716   1429  -3107   1866  A    N  
ATOM   2630  CA  ALA A 348      29.514   6.392 508.203  1.00 90.60      A    C  
ANISOU 2630  CA  ALA A 348    12794  11974   9656   1292  -3036   1594  A    C  
ATOM   2631  C   ALA A 348      30.106   6.896 506.884  1.00 96.80      A    C  
ANISOU 2631  C   ALA A 348    13461  12643  10677   1362  -3012   1457  A    C  
ATOM   2632  O   ALA A 348      29.822   8.029 506.487  1.00 97.38      A    O  
ANISOU 2632  O   ALA A 348    13387  12726  10885   1206  -2926   1248  A    O  
ATOM   2633  CB  ALA A 348      30.334   6.920 509.381  1.00 85.98      A    C  
ANISOU 2633  CB  ALA A 348    12036  11770   8861   1307  -3125   1520  A    C  
ATOM   2634  N   ALA A 349      30.961   6.113 506.218  1.00 97.00      A    N  
ANISOU 2634  N   ALA A 349    13551  12574  10729   1626  -3078   1578  A    N  
ATOM   2635  CA  ALA A 349      31.440   6.506 504.892  1.00 87.27      A    C  
ANISOU 2635  CA  ALA A 349    12221  11226   9710   1727  -3034   1485  A    C  
ATOM   2636  C   ALA A 349      30.293   6.557 503.884  1.00 85.24      A    C  
ANISOU 2636  C   ALA A 349    12131  10605   9649   1584  -2927   1430  A    C  
ATOM   2637  O   ALA A 349      30.188   7.501 503.080  1.00 84.97      A    O  
ANISOU 2637  O   ALA A 349    11941  10535   9810   1491  -2842   1253  A    O  
ATOM   2638  CB  ALA A 349      32.528   5.543 504.421  1.00 89.72      A    C  
ANISOU 2638  CB  ALA A 349    12614  11521   9955   2116  -3103   1669  A    C  
ATOM   2639  N   ASP A 350      29.377   5.584 503.968  1.00 88.78      A    N  
ANISOU 2639  N   ASP A 350    12892  10799  10040   1526  -2945   1597  A    N  
ATOM   2640  CA  ASP A 350      28.161   5.643 503.167  1.00 88.09      A    C  
ANISOU 2640  CA  ASP A 350    12939  10421  10110   1317  -2872   1586  A    C  
ATOM   2641  C   ASP A 350      27.346   6.869 503.526  1.00 88.73      A    C  
ANISOU 2641  C   ASP A 350    12778  10679  10255   1050  -2745   1425  A    C  
ATOM   2642  O   ASP A 350      26.782   7.522 502.638  1.00 88.21      A    O  
ANISOU 2642  O   ASP A 350    12648  10490  10376    937  -2645   1311  A    O  
ATOM   2643  CB  ASP A 350      27.319   4.380 503.366  1.00 89.84      A    C  
ANISOU 2643  CB  ASP A 350    13528  10385  10223   1230  -2957   1843  A    C  
ATOM   2644  CG  ASP A 350      27.941   3.153 502.730  1.00 99.33      A    C  
ANISOU 2644  CG  ASP A 350    15104  11277  11360   1507  -3077   1989  A    C  
ATOM   2645  OD1 ASP A 350      28.361   3.250 501.559  1.00106.93      A    O  
ANISOU 2645  OD1 ASP A 350    16121  12058  12449   1676  -3055   1902  A    O  
ATOM   2646  OD2 ASP A 350      27.988   2.088 503.389  1.00 98.76      A    O1-
ANISOU 2646  OD2 ASP A 350    15304  11129  11093   1577  -3187   2199  A    O1-
ATOM   2647  N   TRP A 351      27.207   7.161 504.826  1.00 87.70      A    N  
ANISOU 2647  N   TRP A 351    12548  10827   9947    969  -2738   1428  A    N  
ATOM   2648  CA  TRP A 351      26.425   8.337 505.195  1.00 89.25      A    C  
ANISOU 2648  CA  TRP A 351    12578  11181  10151    783  -2600   1278  A    C  
ATOM   2649  C   TRP A 351      27.065   9.615 504.657  1.00 89.18      A    C  
ANISOU 2649  C   TRP A 351    12365  11241  10280    794  -2550    999  A    C  
ATOM   2650  O   TRP A 351      26.355  10.531 504.228  1.00 88.32      A    O  
ANISOU 2650  O   TRP A 351    12186  11091  10281    676  -2414    865  A    O  
ATOM   2651  CB  TRP A 351      26.280   8.407 506.711  1.00 90.77      A    C  
ANISOU 2651  CB  TRP A 351    12748  11659  10080    754  -2609   1326  A    C  
ATOM   2652  CG  TRP A 351      25.573   7.223 507.277  1.00 92.29      A    C  
ANISOU 2652  CG  TRP A 351    13121  11809  10137    711  -2650   1626  A    C  
ATOM   2653  CD1 TRP A 351      24.886   6.271 506.584  1.00 92.34      A    C  
ANISOU 2653  CD1 TRP A 351    13315  11537  10232    627  -2682   1843  A    C  
ATOM   2654  CD2 TRP A 351      25.496   6.849 508.656  1.00 99.88      A    C  
ANISOU 2654  CD2 TRP A 351    14114  13002  10834    725  -2685   1761  A    C  
ATOM   2655  CE2 TRP A 351      24.744   5.660 508.724  1.00102.36      A    C  
ANISOU 2655  CE2 TRP A 351    14618  13171  11103    639  -2730   2077  A    C  
ATOM   2656  CE3 TRP A 351      25.986   7.408 509.840  1.00102.48      A    C  
ANISOU 2656  CE3 TRP A 351    14352  13639  10945    786  -2698   1653  A    C  
ATOM   2657  NE1 TRP A 351      24.386   5.327 507.444  1.00 94.98      A    N  
ANISOU 2657  NE1 TRP A 351    13792  11913  10382    562  -2743   2120  A    N  
ATOM   2658  CZ2 TRP A 351      24.469   5.019 509.928  1.00108.49      A    C  
ANISOU 2658  CZ2 TRP A 351    15464  14120  11639    628  -2766   2298  A    C  
ATOM   2659  CZ3 TRP A 351      25.712   6.770 511.036  1.00110.76      A    C  
ANISOU 2659  CZ3 TRP A 351    15478  14860  11745    801  -2728   1855  A    C  
ATOM   2660  CH2 TRP A 351      24.960   5.589 511.071  1.00114.44      A    C  
ANISOU 2660  CH2 TRP A 351    16101  15194  12185    729  -2751   2180  A    C  
ATOM   2661  N   CYS A 352      28.403   9.659 504.598  1.00 85.04      A    N  
ANISOU 2661  N   CYS A 352    11739  10822   9751    937  -2660    941  A    N  
ATOM   2662  CA  CYS A 352      29.095  10.825 504.056  1.00 78.85      A    C  
ANISOU 2662  CA  CYS A 352    10750  10111   9097    908  -2645    723  A    C  
ATOM   2663  C   CYS A 352      28.776  10.983 502.585  1.00 78.39      A    C  
ANISOU 2663  C   CYS A 352    10692   9791   9300    920  -2548    675  A    C  
ATOM   2664  O   CYS A 352      28.635  12.108 502.087  1.00 76.04      A    O  
ANISOU 2664  O   CYS A 352    10278   9479   9135    812  -2461    486  A    O  
ATOM   2665  CB  CYS A 352      30.599  10.737 504.277  1.00 80.00      A    C  
ANISOU 2665  CB  CYS A 352    10739  10483   9174   1044  -2799    753  A    C  
ATOM   2666  SG  CYS A 352      31.043  11.185 505.941  1.00 88.77      A    S  
ANISOU 2666  SG  CYS A 352    11787  11946   9994    937  -2924    705  A    S  
ATOM   2667  N   LYS A 353      28.644   9.863 501.874  1.00 81.58      A    N  
ANISOU 2667  N   LYS A 353    11271   9964   9762   1052  -2570    844  A    N  
ATOM   2668  CA  LYS A 353      28.206   9.982 500.495  1.00 79.18      A    C  
ANISOU 2668  CA  LYS A 353    11012   9392   9679   1050  -2486    802  A    C  
ATOM   2669  C   LYS A 353      26.762  10.458 500.499  1.00 79.05      A    C  
ANISOU 2669  C   LYS A 353    11025   9296   9713    815  -2360    765  A    C  
ATOM   2670  O   LYS A 353      26.422  11.467 499.872  1.00 97.11      A    O  
ANISOU 2670  O   LYS A 353    13192  11554  12151    729  -2243    604  A    O  
ATOM   2671  CB  LYS A 353      28.283   8.617 499.793  1.00 80.16      A    C  
ANISOU 2671  CB  LYS A 353    11418   9238   9800   1236  -2563    996  A    C  
ATOM   2672  CG  LYS A 353      29.652   7.931 499.695  1.00 79.20      A    C  
ANISOU 2672  CG  LYS A 353    11320   9182   9588   1570  -2662   1095  A    C  
ATOM   2673  CD  LYS A 353      30.786   8.806 499.214  1.00 86.57      A    C  
ANISOU 2673  CD  LYS A 353    11937  10333  10621   1694  -2635    982  A    C  
ATOM   2674  CE  LYS A 353      32.043   7.956 498.998  1.00 94.77      A    C  
ANISOU 2674  CE  LYS A 353    13005  11456  11548   2089  -2711   1159  A    C  
ATOM   2675  NZ  LYS A 353      33.279   8.767 498.778  1.00 96.47      A    N1+
ANISOU 2675  NZ  LYS A 353    12829  12012  11814   2190  -2712   1131  A    N1+
ATOM   2676  N   LEU A 354      25.920   9.760 501.265  1.00 77.16      A    N  
ANISOU 2676  N   LEU A 354    10927   9061   9328    719  -2379    942  A    N  
ATOM   2677  CA  LEU A 354      24.506  10.083 501.435  1.00 78.13      A    C  
ANISOU 2677  CA  LEU A 354    11041   9199   9447    516  -2258    997  A    C  
ATOM   2678  C   LEU A 354      24.253  11.550 501.788  1.00 85.41      A    C  
ANISOU 2678  C   LEU A 354    11772  10318  10361    460  -2104    780  A    C  
ATOM   2679  O   LEU A 354      23.272  12.145 501.324  1.00 75.85      A    O  
ANISOU 2679  O   LEU A 354    10508   9076   9235    366  -1958    760  A    O  
ATOM   2680  CB  LEU A 354      23.911   9.152 502.487  1.00 78.03      A    C  
ANISOU 2680  CB  LEU A 354    11155   9268   9226    441  -2319   1250  A    C  
ATOM   2681  CG  LEU A 354      22.398   9.004 502.441  1.00 82.13      A    C  
ANISOU 2681  CG  LEU A 354    11686   9778   9741    228  -2236   1453  A    C  
ATOM   2682  CD1 LEU A 354      21.973   8.493 501.091  1.00 82.75      A    C  
ANISOU 2682  CD1 LEU A 354    11898   9537  10006    135  -2288   1541  A    C  
ATOM   2683  CD2 LEU A 354      21.985   8.021 503.517  1.00 89.37      A    C  
ANISOU 2683  CD2 LEU A 354    12716  10798  10443    155  -2319   1737  A    C  
ATOM   2684  N   PHE A 355      25.125  12.158 502.600  1.00101.12      A    N  
ANISOU 2684  N   PHE A 355    13684  12506  12230    519  -2144    625  A    N  
ATOM   2685  CA  PHE A 355      24.867  13.501 503.111  1.00104.61      A    C  
ANISOU 2685  CA  PHE A 355    14057  13098  12593    468  -2027    421  A    C  
ATOM   2686  C   PHE A 355      25.774  14.538 502.474  1.00107.35      A    C  
ANISOU 2686  C   PHE A 355    14303  13406  13079    467  -2045    173  A    C  
ATOM   2687  O   PHE A 355      25.654  15.727 502.791  1.00111.29      A    O  
ANISOU 2687  O   PHE A 355    14806  13967  13511    415  -1972    -21  A    O  
ATOM   2688  CB  PHE A 355      25.114  13.579 504.630  1.00107.17      A    C  
ANISOU 2688  CB  PHE A 355    14429  13670  12622    486  -2086    415  A    C  
ATOM   2689  CG  PHE A 355      24.269  12.651 505.464  1.00105.98      A    C  
ANISOU 2689  CG  PHE A 355    14360  13616  12292    485  -2065    674  A    C  
ATOM   2690  CD1 PHE A 355      22.896  12.600 505.321  1.00100.78      A    C  
ANISOU 2690  CD1 PHE A 355    13701  12956  11635    425  -1904    831  A    C  
ATOM   2691  CD2 PHE A 355      24.861  11.903 506.480  1.00101.08      A    C  
ANISOU 2691  CD2 PHE A 355    13795  13136  11476    539  -2207    783  A    C  
ATOM   2692  CE1 PHE A 355      22.144  11.749 506.103  1.00 97.89      A    C  
ANISOU 2692  CE1 PHE A 355    13378  12717  11098    394  -1898   1116  A    C  
ATOM   2693  CE2 PHE A 355      24.110  11.068 507.278  1.00 98.97      A    C  
ANISOU 2693  CE2 PHE A 355    13601  12967  11036    527  -2192   1038  A    C  
ATOM   2694  CZ  PHE A 355      22.748  10.993 507.092  1.00102.64      A    C  
ANISOU 2694  CZ  PHE A 355    14055  13427  11515    443  -2040   1213  A    C  
ATOM   2695  N   ARG A 356      26.631  14.122 501.550  1.00104.55      A    N  
ANISOU 2695  N   ARG A 356    13881  12943  12901    534  -2135    193  A    N  
ATOM   2696  CA  ARG A 356      27.570  14.995 500.861  1.00 97.88      A    C  
ANISOU 2696  CA  ARG A 356    12896  12094  12200    526  -2165     23  A    C  
ATOM   2697  C   ARG A 356      28.295  15.901 501.857  1.00 88.55      A    C  
ANISOU 2697  C   ARG A 356    11675  11124  10848    430  -2264   -128  A    C  
ATOM   2698  O   ARG A 356      28.308  17.127 501.737  1.00 88.16      A    O  
ANISOU 2698  O   ARG A 356    11619  11053  10824    316  -2224   -325  A    O  
ATOM   2699  CB  ARG A 356      26.821  15.794 499.793  1.00 94.33      A    C  
ANISOU 2699  CB  ARG A 356    12429  11462  11952    472  -1996    -94  A    C  
ATOM   2700  CG  ARG A 356      26.241  14.864 498.738  1.00 98.30      A    C  
ANISOU 2700  CG  ARG A 356    12986  11750  12613    540  -1950     62  A    C  
ATOM   2701  CD  ARG A 356      25.618  15.538 497.525  1.00102.74      A    C  
ANISOU 2701  CD  ARG A 356    13508  12138  13389    504  -1803    -28  A    C  
ATOM   2702  NE  ARG A 356      24.266  15.013 497.313  1.00109.89      A    N  
ANISOU 2702  NE  ARG A 356    14509  12943  14299    446  -1716    122  A    N  
ATOM   2703  CZ  ARG A 356      23.946  14.094 496.401  1.00106.40      A    C  
ANISOU 2703  CZ  ARG A 356    14163  12298  13965    462  -1757    270  A    C  
ATOM   2704  NH1 ARG A 356      24.877  13.604 495.587  1.00101.69      A    N1+
ANISOU 2704  NH1 ARG A 356    13604  11564  13470    602  -1851    270  A    N1+
ATOM   2705  NH2 ARG A 356      22.690  13.674 496.290  1.00 97.35      A    N  
ANISOU 2705  NH2 ARG A 356    13086  11098  12805    341  -1711    439  A    N  
ATOM   2706  N   CYS A 357      28.908  15.271 502.857  1.00 88.00      A    N  
ANISOU 2706  N   CYS A 357    11611  11244  10583    468  -2413    -25  A    N  
ATOM   2707  CA  CYS A 357      29.664  15.968 503.888  1.00 96.08      A    C  
ANISOU 2707  CA  CYS A 357    12619  12484  11405    357  -2561   -135  A    C  
ATOM   2708  C   CYS A 357      31.022  15.294 504.036  1.00103.76      A    C  
ANISOU 2708  C   CYS A 357    13419  13661  12342    431  -2763     17  A    C  
ATOM   2709  O   CYS A 357      31.206  14.137 503.646  1.00108.41      A    O  
ANISOU 2709  O   CYS A 357    13981  14221  12988    623  -2766    214  A    O  
ATOM   2710  CB  CYS A 357      28.929  15.997 505.242  1.00 92.06      A    C  
ANISOU 2710  CB  CYS A 357    12301  12070  10606    337  -2534   -153  A    C  
ATOM   2711  SG  CYS A 357      28.559  14.388 505.978  1.00 88.35      A    S  
ANISOU 2711  SG  CYS A 357    11895  11683   9993    486  -2551    131  A    S  
ATOM   2712  N   ASP A 358      31.986  16.037 504.585  1.00104.92      A    N  
ANISOU 2712  N   ASP A 358    13470  14018  12377    280  -2942    -61  A    N  
ATOM   2713  CA  ASP A 358      33.352  15.541 504.729  1.00103.77      A    C  
ANISOU 2713  CA  ASP A 358    13094  14149  12184    337  -3142    117  A    C  
ATOM   2714  C   ASP A 358      33.603  14.745 506.008  1.00 99.32      A    C  
ANISOU 2714  C   ASP A 358    12585  13804  11347    410  -3266    249  A    C  
ATOM   2715  O   ASP A 358      34.613  14.036 506.081  1.00 97.32      A    O  
ANISOU 2715  O   ASP A 358    12147  13782  11046    548  -3394    458  A    O  
ATOM   2716  CB  ASP A 358      34.341  16.706 504.641  1.00108.61      A    C  
ANISOU 2716  CB  ASP A 358    13530  14925  12811     84  -3315     27  A    C  
ATOM   2717  CG  ASP A 358      34.093  17.577 503.425  1.00109.12      A    C  
ANISOU 2717  CG  ASP A 358    13555  14772  13135     -4  -3194   -106  A    C  
ATOM   2718  OD1 ASP A 358      34.519  17.177 502.320  1.00107.00      A    O  
ANISOU 2718  OD1 ASP A 358    13082  14500  13074    154  -3136     30  A    O  
ATOM   2719  OD2 ASP A 358      33.455  18.644 503.566  1.00108.10      A    O1-
ANISOU 2719  OD2 ASP A 358    13624  14468  12980   -196  -3144   -340  A    O1-
ATOM   2720  N   GLY A 359      32.724  14.832 507.005  1.00 98.96      A    N  
ANISOU 2720  N   GLY A 359    12779  13716  11105    355  -3220    158  A    N  
ATOM   2721  CA  GLY A 359      32.962  14.152 508.268  1.00 94.23      A    C  
ANISOU 2721  CA  GLY A 359    12237  13335  10230    416  -3340    279  A    C  
ATOM   2722  C   GLY A 359      31.720  14.091 509.130  1.00 91.91      A    C  
ANISOU 2722  C   GLY A 359    12213  12954   9757    424  -3210    222  A    C  
ATOM   2723  O   GLY A 359      30.793  14.895 508.987  1.00 89.26      A    O  
ANISOU 2723  O   GLY A 359    12023  12450   9443    346  -3060     48  A    O  
ATOM   2724  N   ILE A 360      31.717  13.110 510.032  1.00101.73      A    N  
ANISOU 2724  N   ILE A 360    13510  14337  10805    548  -3259    399  A    N  
ATOM   2725  CA  ILE A 360      30.610  12.865 510.954  1.00103.13      A    C  
ANISOU 2725  CA  ILE A 360    13903  14502  10780    585  -3142    424  A    C  
ATOM   2726  C   ILE A 360      31.143  12.555 512.352  1.00 98.81      A    C  
ANISOU 2726  C   ILE A 360    13402  14235   9906    607  -3309    494  A    C  
ATOM   2727  O   ILE A 360      32.183  11.905 512.497  1.00 99.02      A    O  
ANISOU 2727  O   ILE A 360    13284  14437   9901    676  -3478    643  A    O  
ATOM   2728  CB  ILE A 360      29.704  11.722 510.431  1.00 99.34      A    C  
ANISOU 2728  CB  ILE A 360    13474  13836  10435    718  -2983    640  A    C  
ATOM   2729  CG1 ILE A 360      28.797  12.237 509.316  1.00 94.96      A    C  
ANISOU 2729  CG1 ILE A 360    12931  13024  10124    660  -2792    546  A    C  
ATOM   2730  CG2 ILE A 360      28.884  11.077 511.543  1.00103.04      A    C  
ANISOU 2730  CG2 ILE A 360    14094  14398  10660    773  -2926    797  A    C  
ATOM   2731  CD1 ILE A 360      28.287  11.152 508.406  1.00 98.48      A    C  
ANISOU 2731  CD1 ILE A 360    13400  13252  10767    739  -2719    751  A    C  
ATOM   2732  N   GLY A 361      30.441  13.043 513.383  1.00 98.28      A    N  
ANISOU 2732  N   GLY A 361    13541  14229   9573    577  -3256    397  A    N  
ATOM   2733  CA  GLY A 361      30.742  12.617 514.740  1.00100.54      A    C  
ANISOU 2733  CA  GLY A 361    13905  14767   9531    628  -3384    488  A    C  
ATOM   2734  C   GLY A 361      29.442  12.244 515.432  1.00101.94      A    C  
ANISOU 2734  C   GLY A 361    14260  14936   9535    744  -3182    590  A    C  
ATOM   2735  O   GLY A 361      28.450  12.973 515.353  1.00103.07      A    O  
ANISOU 2735  O   GLY A 361    14534  14976   9653    739  -2994    472  A    O  
ATOM   2736  N   TYR A 362      29.445  11.087 516.100  1.00105.73      A    N  
ANISOU 2736  N   TYR A 362    14736  15547   9889    863  -3215    843  A    N  
ATOM   2737  CA  TYR A 362      28.340  10.573 516.909  1.00103.88      A    C  
ANISOU 2737  CA  TYR A 362    14633  15380   9457    963  -3058   1019  A    C  
ATOM   2738  C   TYR A 362      28.695  10.474 518.386  1.00103.45      A    C  
ANISOU 2738  C   TYR A 362    14687  15607   9015   1029  -3178   1048  A    C  
ATOM   2739  O   TYR A 362      29.658   9.788 518.741  1.00109.70      A    O  
ANISOU 2739  O   TYR A 362    15398  16534   9748   1062  -3370   1161  A    O  
ATOM   2740  CB  TYR A 362      27.897   9.208 516.373  1.00109.62      A    C  
ANISOU 2740  CB  TYR A 362    15304  15977  10371   1020  -2992   1334  A    C  
ATOM   2741  CG  TYR A 362      26.872   8.463 517.202  1.00109.17      A    C  
ANISOU 2741  CG  TYR A 362    15340  16020  10120   1083  -2873   1606  A    C  
ATOM   2742  CD1 TYR A 362      25.584   8.957 517.361  1.00104.97      A    C  
ANISOU 2742  CD1 TYR A 362    14853  15519   9513   1076  -2648   1634  A    C  
ATOM   2743  CD2 TYR A 362      27.182   7.239 517.782  1.00109.98      A    C  
ANISOU 2743  CD2 TYR A 362    15473  16200  10114   1160  -2977   1872  A    C  
ATOM   2744  CE1 TYR A 362      24.641   8.264 518.094  1.00110.94      A    C  
ANISOU 2744  CE1 TYR A 362    15643  16417  10091   1123  -2537   1940  A    C  
ATOM   2745  CE2 TYR A 362      26.249   6.540 518.514  1.00112.38      A    C  
ANISOU 2745  CE2 TYR A 362    15850  16599  10249   1187  -2879   2155  A    C  
ATOM   2746  CZ  TYR A 362      24.980   7.052 518.669  1.00115.82      A    C  
ANISOU 2746  CZ  TYR A 362    16292  17099  10616   1156  -2661   2200  A    C  
ATOM   2747  OH  TYR A 362      24.054   6.351 519.413  1.00122.51      A    O  
ANISOU 2747  OH  TYR A 362    17167  18098  11284   1175  -2562   2536  A    O  
ATOM   2748  N   LEU A 363      27.943  11.158 519.246  1.00101.87      A    N  
ANISOU 2748  N   LEU A 363    14675  15506   8526   1079  -3062    957  A    N  
ATOM   2749  CA  LEU A 363      28.244  11.185 520.672  1.00104.60      A    C  
ANISOU 2749  CA  LEU A 363    15170  16111   8462   1154  -3176    954  A    C  
ATOM   2750  C   LEU A 363      27.074  10.526 521.389  1.00104.20      A    C  
ANISOU 2750  C   LEU A 363    15185  16182   8226   1318  -2962   1222  A    C  
ATOM   2751  O   LEU A 363      25.913  10.848 521.114  1.00103.90      A    O  
ANISOU 2751  O   LEU A 363    15178  16083   8214   1372  -2711   1261  A    O  
ATOM   2752  CB  LEU A 363      28.427  12.607 521.199  1.00106.43      A    C  
ANISOU 2752  CB  LEU A 363    15648  16364   8425   1105  -3244    615  A    C  
ATOM   2753  CG  LEU A 363      29.838  13.142 521.403  1.00110.11      A    C  
ANISOU 2753  CG  LEU A 363    16123  16902   8813    921  -3585    419  A    C  
ATOM   2754  CD1 LEU A 363      30.702  12.870 520.179  1.00110.63      A    C  
ANISOU 2754  CD1 LEU A 363    15883  16867   9286    778  -3702    453  A    C  
ATOM   2755  CD2 LEU A 363      29.783  14.621 521.738  1.00112.10      A    C  
ANISOU 2755  CD2 LEU A 363    16709  17067   8818    836  -3636     76  A    C  
ATOM   2756  N   ARG A 364      27.373   9.628 522.328  1.00106.65      A    N  
ANISOU 2756  N   ARG A 364    15498  16694   8331   1400  -3059   1433  A    N  
ATOM   2757  CA  ARG A 364      26.300   8.961 523.062  1.00112.62      A    C  
ANISOU 2757  CA  ARG A 364    16295  17598   8896   1538  -2869   1732  A    C  
ATOM   2758  C   ARG A 364      26.819   8.581 524.452  1.00118.79      A    C  
ANISOU 2758  C   ARG A 364    17179  18658   9298   1649  -3009   1810  A    C  
ATOM   2759  O   ARG A 364      27.507   7.565 524.609  1.00117.09      A    O  
ANISOU 2759  O   ARG A 364    16874  18492   9123   1648  -3166   1995  A    O  
ATOM   2760  CB  ARG A 364      25.763   7.762 522.288  1.00107.28      A    C  
ANISOU 2760  CB  ARG A 364    15465  16775   8521   1482  -2788   2070  A    C  
ATOM   2761  CG  ARG A 364      24.905   6.855 523.134  1.00115.49      A    C  
ANISOU 2761  CG  ARG A 364    16522  17999   9358   1567  -2673   2451  A    C  
ATOM   2762  CD  ARG A 364      23.438   7.227 522.986  1.00113.59      A    C  
ANISOU 2762  CD  ARG A 364    16249  17811   9100   1586  -2385   2591  A    C  
ATOM   2763  NE  ARG A 364      22.567   6.259 523.645  1.00119.72      A    N  
ANISOU 2763  NE  ARG A 364    16984  18777   9729   1616  -2281   3037  A    N  
ATOM   2764  CZ  ARG A 364      21.243   6.256 523.551  1.00118.12      A    C  
ANISOU 2764  CZ  ARG A 364    16681  18689   9510   1607  -2045   3312  A    C  
ATOM   2765  NH1 ARG A 364      20.630   7.169 522.807  1.00112.20      A    N1+
ANISOU 2765  NH1 ARG A 364    15873  17875   8883   1602  -1876   3171  A    N1+
ATOM   2766  NH2 ARG A 364      20.537   5.338 524.202  1.00116.40      A    N  
ANISOU 2766  NH2 ARG A 364    16406  18675   9146   1600  -1982   3758  A    N  
ATOM   2767  N   GLY A 365      26.490   9.398 525.448  1.00119.75      A    N  
ANISOU 2767  N   GLY A 365    17517  18955   9029   1773  -2949   1671  A    N  
ATOM   2768  CA  GLY A 365      27.029   9.214 526.788  1.00128.64      A    C  
ANISOU 2768  CA  GLY A 365    18779  20346   9755   1877  -3102   1693  A    C  
ATOM   2769  C   GLY A 365      28.537   9.402 526.867  1.00130.01      A    C  
ANISOU 2769  C   GLY A 365    18936  20544   9917   1736  -3451   1492  A    C  
ATOM   2770  O   GLY A 365      29.054  10.502 526.634  1.00124.85      A    O  
ANISOU 2770  O   GLY A 365    18394  19800   9242   1608  -3584   1164  A    O  
ATOM   2771  N   GLU A 366      29.270   8.344 527.222  1.00135.88      A    N  
ANISOU 2771  N   GLU A 366    19544  21430  10655   1754  -3615   1712  A    N  
ATOM   2772  CA  GLU A 366      30.720   8.448 527.349  1.00142.94      A    C  
ANISOU 2772  CA  GLU A 366    20361  22435  11513   1639  -3948   1597  A    C  
ATOM   2773  C   GLU A 366      31.489   8.156 526.062  1.00145.93      A    C  
ANISOU 2773  C   GLU A 366    20474  22652  12319   1516  -4046   1613  A    C  
ATOM   2774  O   GLU A 366      32.715   8.323 526.044  1.00146.53      A    O  
ANISOU 2774  O   GLU A 366    20427  22861  12387   1414  -4314   1547  A    O  
ATOM   2775  CB  GLU A 366      31.201   7.466 528.420  1.00145.32      A    C  
ANISOU 2775  CB  GLU A 366    20642  23019  11554   1772  -4074   1847  A    C  
ATOM   2776  CG  GLU A 366      30.767   7.788 529.836  1.00149.80      A    C  
ANISOU 2776  CG  GLU A 366    21475  23813  11630   1903  -4050   1818  A    C  
ATOM   2777  CD  GLU A 366      30.320   6.545 530.594  1.00152.91      A    C  
ANISOU 2777  CD  GLU A 366    21841  24375  11881   2102  -3939   2196  A    C  
ATOM   2778  OE1 GLU A 366      30.104   5.498 529.945  1.00146.90      A    O  
ANISOU 2778  OE1 GLU A 366    20910  23488  11418   2121  -3845   2471  A    O  
ATOM   2779  OE2 GLU A 366      30.210   6.608 531.840  1.00159.50      A    O1-
ANISOU 2779  OE2 GLU A 366    22854  25455  12291   2236  -3962   2223  A    O1-
ATOM   2780  N   GLU A 367      30.814   7.698 525.013  1.00143.47      A    N  
ANISOU 2780  N   GLU A 367    20067  22089  12356   1530  -3843   1729  A    N  
ATOM   2781  CA  GLU A 367      31.429   7.300 523.750  1.00137.35      A    C  
ANISOU 2781  CA  GLU A 367    19080  21137  11968   1476  -3898   1775  A    C  
ATOM   2782  C   GLU A 367      31.383   8.407 522.695  1.00133.87      A    C  
ANISOU 2782  C   GLU A 367    18604  20487  11776   1310  -3862   1493  A    C  
ATOM   2783  O   GLU A 367      30.381   9.120 522.573  1.00129.92      A    O  
ANISOU 2783  O   GLU A 367    18239  19853  11272   1279  -3672   1355  A    O  
ATOM   2784  CB  GLU A 367      30.787   6.020 523.215  1.00136.82      A    C  
ANISOU 2784  CB  GLU A 367    18989  20886  12109   1584  -3740   2089  A    C  
ATOM   2785  CG  GLU A 367      31.031   4.794 524.069  1.00138.67      A    C  
ANISOU 2785  CG  GLU A 367    19258  21284  12148   1746  -3807   2398  A    C  
ATOM   2786  CD  GLU A 367      32.240   4.007 523.593  1.00138.44      A    C  
ANISOU 2786  CD  GLU A 367    19096  21265  12239   1852  -3978   2531  A    C  
ATOM   2787  OE1 GLU A 367      32.882   4.438 522.610  1.00128.65      A    O  
ANISOU 2787  OE1 GLU A 367    17712  19936  11234   1796  -4040   2392  A    O  
ATOM   2788  OE2 GLU A 367      32.558   2.968 524.209  1.00147.24      A    O1-
ANISOU 2788  OE2 GLU A 367    20251  22496  13199   2016  -4042   2791  A    O1-
ATOM   2789  N   LEU A 368      32.478   8.545 521.936  1.00133.23      A    N  
ANISOU 2789  N   LEU A 368    18326  20400  11894   1224  -4034   1436  A    N  
ATOM   2790  CA  LEU A 368      32.574   9.497 520.830  1.00123.55      A    C  
ANISOU 2790  CA  LEU A 368    17030  18978  10935   1061  -4018   1207  A    C  
ATOM   2791  C   LEU A 368      33.218   8.752 519.667  1.00117.11      A    C  
ANISOU 2791  C   LEU A 368    15976  18068  10451   1127  -4039   1368  A    C  
ATOM   2792  O   LEU A 368      34.300   8.179 519.816  1.00118.97      A    O  
ANISOU 2792  O   LEU A 368    16047  18517  10640   1209  -4217   1527  A    O  
ATOM   2793  CB  LEU A 368      33.403  10.731 521.213  1.00132.51      A    C  
ANISOU 2793  CB  LEU A 368    18193  20259  11898    846  -4259    947  A    C  
ATOM   2794  CG  LEU A 368      33.128  11.418 522.566  1.00144.40      A    C  
ANISOU 2794  CG  LEU A 368    19999  21901  12966    808  -4331    789  A    C  
ATOM   2795  CD1 LEU A 368      33.772  10.690 523.763  1.00137.44      A    C  
ANISOU 2795  CD1 LEU A 368    19098  21353  11770    897  -4519    973  A    C  
ATOM   2796  CD2 LEU A 368      33.584  12.877 522.533  1.00150.37      A    C  
ANISOU 2796  CD2 LEU A 368    20900  22608  13627    540  -4519    466  A    C  
ATOM   2797  N   THR A 369      32.566   8.798 518.506  1.00118.06      A    N  
ANISOU 2797  N   THR A 369    16087  17887  10883   1115  -3856   1333  A    N  
ATOM   2798  CA  THR A 369      33.046   8.221 517.251  1.00117.47      A    C  
ANISOU 2798  CA  THR A 369    15850  17662  11122   1198  -3845   1447  A    C  
ATOM   2799  C   THR A 369      33.181   9.255 516.139  1.00121.01      A    C  
ANISOU 2799  C   THR A 369    16190  17958  11829   1043  -3820   1224  A    C  
ATOM   2800  O   THR A 369      32.279  10.078 515.953  1.00122.48      A    O  
ANISOU 2800  O   THR A 369    16498  17976  12065    920  -3681   1030  A    O  
ATOM   2801  CB  THR A 369      32.104   7.104 516.781  1.00112.08      A    C  
ANISOU 2801  CB  THR A 369    15298  16711  10576   1331  -3664   1659  A    C  
ATOM   2802  CG2 THR A 369      32.606   6.505 515.478  1.00108.83      A    C  
ANISOU 2802  CG2 THR A 369    14803  16106  10443   1453  -3661   1760  A    C  
ATOM   2803  OG1 THR A 369      32.061   6.063 517.761  1.00122.10      A    O  
ANISOU 2803  OG1 THR A 369    16671  18108  11613   1472  -3702   1902  A    O  
ATOM   2804  N   THR A 370      34.308   9.236 515.411  1.00121.71      A    N  
ANISOU 2804  N   THR A 370    16046  18134  12065   1069  -3945   1271  A    N  
ATOM   2805  CA  THR A 370      34.523  10.195 514.332  1.00115.99      A    C  
ANISOU 2805  CA  THR A 370    15194  17289  11589    918  -3931   1091  A    C  
ATOM   2806  C   THR A 370      34.873   9.437 513.055  1.00101.66      A    C  
ANISOU 2806  C   THR A 370    13245  15336  10046   1119  -3859   1256  A    C  
ATOM   2807  O   THR A 370      35.491   8.370 513.087  1.00103.84      A    O  
ANISOU 2807  O   THR A 370    13462  15723  10270   1366  -3910   1506  A    O  
ATOM   2808  CB  THR A 370      35.660  11.193 514.648  1.00121.04      A    C  
ANISOU 2808  CB  THR A 370    15653  18216  12121    698  -4185    985  A    C  
ATOM   2809  CG2 THR A 370      35.419  11.880 515.978  1.00122.92      A    C  
ANISOU 2809  CG2 THR A 370    16101  18575  12028    523  -4297    822  A    C  
ATOM   2810  OG1 THR A 370      36.916  10.499 514.705  1.00126.84      A    O  
ANISOU 2810  OG1 THR A 370    16119  19269  12804    838  -4356   1242  A    O  
ATOM   2811  N   TYR A 371      34.446  10.001 511.926  1.00 97.16      A    N  
ANISOU 2811  N   TYR A 371    12663  14512   9744   1041  -3731   1116  A    N  
ATOM   2812  CA  TYR A 371      34.818   9.565 510.585  1.00 99.97      A    C  
ANISOU 2812  CA  TYR A 371    12901  14725  10356   1211  -3666   1219  A    C  
ATOM   2813  C   TYR A 371      35.126  10.729 509.657  1.00 98.11      A    C  
ANISOU 2813  C   TYR A 371    12489  14455  10332   1034  -3664   1039  A    C  
ATOM   2814  O   TYR A 371      34.369  11.704 509.607  1.00 97.56      A    O  
ANISOU 2814  O   TYR A 371    12524  14228  10318    813  -3588    802  A    O  
ATOM   2815  CB  TYR A 371      33.726   8.721 509.923  1.00100.83      A    C  
ANISOU 2815  CB  TYR A 371    13250  14455  10607   1341  -3476   1290  A    C  
ATOM   2816  CG  TYR A 371      34.089   8.394 508.496  1.00 96.19      A    C  
ANISOU 2816  CG  TYR A 371    12601  13687  10259   1517  -3415   1356  A    C  
ATOM   2817  CD1 TYR A 371      35.080   7.471 508.200  1.00 97.16      A    C  
ANISOU 2817  CD1 TYR A 371    12663  13916  10337   1836  -3480   1589  A    C  
ATOM   2818  CD2 TYR A 371      33.476   9.063 507.443  1.00 91.06      A    C  
ANISOU 2818  CD2 TYR A 371    11960  12784   9857   1398  -3286   1190  A    C  
ATOM   2819  CE1 TYR A 371      35.422   7.192 506.891  1.00 96.39      A    C  
ANISOU 2819  CE1 TYR A 371    12544  13659  10421   2051  -3411   1653  A    C  
ATOM   2820  CE2 TYR A 371      33.819   8.799 506.135  1.00 92.74      A    C  
ANISOU 2820  CE2 TYR A 371    12130  12837  10268   1573  -3230   1245  A    C  
ATOM   2821  CZ  TYR A 371      34.787   7.860 505.864  1.00 93.14      A    C  
ANISOU 2821  CZ  TYR A 371    12148  12984  10255   1907  -3291   1474  A    C  
ATOM   2822  OH  TYR A 371      35.132   7.598 504.561  1.00 91.77      A    O  
ANISOU 2822  OH  TYR A 371    11969  12658  10243   2136  -3221   1535  A    O  
ATOM   2823  N   GLY A 372      36.204  10.614 508.884  1.00 96.03      A    N  
ANISOU 2823  N   GLY A 372    11967  14341  10179   1159  -3730   1172  A    N  
ATOM   2824  CA  GLY A 372      36.490  11.711 507.990  1.00 96.93      A    C  
ANISOU 2824  CA  GLY A 372    11902  14431  10496    975  -3729   1029  A    C  
ATOM   2825  C   GLY A 372      37.090  12.909 508.693  1.00100.88      A    C  
ANISOU 2825  C   GLY A 372    12272  15190  10869    628  -3940    901  A    C  
ATOM   2826  O   GLY A 372      37.620  12.819 509.803  1.00105.35      A    O  
ANISOU 2826  O   GLY A 372    12803  16045  11180    563  -4126    972  A    O  
ATOM   2827  N   GLU A 373      37.039  14.047 508.006  1.00100.38      A    N  
ANISOU 2827  N   GLU A 373    12156  15011  10973    390  -3928    718  A    N  
ATOM   2828  CA  GLU A 373      37.703  15.236 508.511  1.00111.61      A    C  
ANISOU 2828  CA  GLU A 373    13489  16635  12281     17  -4167    609  A    C  
ATOM   2829  C   GLU A 373      36.863  15.797 509.647  1.00111.66      A    C  
ANISOU 2829  C   GLU A 373    13865  16507  12054   -167  -4190    362  A    C  
ATOM   2830  O   GLU A 373      35.718  16.211 509.440  1.00104.42      A    O  
ANISOU 2830  O   GLU A 373    13216  15257  11202   -176  -3992    151  A    O  
ATOM   2831  CB  GLU A 373      37.828  16.276 507.397  1.00113.54      A    C  
ANISOU 2831  CB  GLU A 373    13622  16746  12773   -179  -4138    493  A    C  
ATOM   2832  CG  GLU A 373      38.456  15.783 506.101  1.00111.72      A    C  
ANISOU 2832  CG  GLU A 373    13064  16595  12790     57  -4048    718  A    C  
ATOM   2833  CD  GLU A 373      39.959  15.609 506.193  1.00119.86      A    C  
ANISOU 2833  CD  GLU A 373    13670  18131  13739     56  -4275   1030  A    C  
ATOM   2834  OE1 GLU A 373      40.558  15.998 507.223  1.00123.46      A    O  
ANISOU 2834  OE1 GLU A 373    14066  18876  13967   -211  -4542   1060  A    O  
ATOM   2835  OE2 GLU A 373      40.541  15.082 505.223  1.00120.34      A    O1-
ANISOU 2835  OE2 GLU A 373    13458  18320  13945    337  -4187   1265  A    O1-
ATOM   2836  N   THR A 374      37.436  15.825 510.840  1.00118.22      A    N  
ANISOU 2836  N   THR A 374    14710  17618  12589   -292  -4428    406  A    N  
ATOM   2837  CA  THR A 374      36.747  16.371 511.993  1.00115.95      A    C  
ANISOU 2837  CA  THR A 374    14801  17234  12021   -433  -4469    182  A    C  
ATOM   2838  C   THR A 374      37.733  17.141 512.857  1.00128.19      A    C  
ANISOU 2838  C   THR A 374    16341  19057  13310   -778  -4837    153  A    C  
ATOM   2839  O   THR A 374      38.937  16.861 512.840  1.00137.39      A    O  
ANISOU 2839  O   THR A 374    17148  20588  14465   -845  -5060    395  A    O  
ATOM   2840  CB  THR A 374      36.139  15.196 512.782  1.00111.55      A    C  
ANISOU 2840  CB  THR A 374    14370  16708  11305   -138  -4344    303  A    C  
ATOM   2841  CG2 THR A 374      35.528  15.599 514.096  1.00112.70      A    C  
ANISOU 2841  CG2 THR A 374    14874  16840  11107   -215  -4384    134  A    C  
ATOM   2842  OG1 THR A 374      35.135  14.554 511.990  1.00117.42      A    O  
ANISOU 2842  OG1 THR A 374    15173  17168  12275    106  -4038    332  A    O  
ATOM   2843  N   PRO A 375      37.246  18.102 513.640  1.00128.21      A    N  
ANISOU 2843  N   PRO A 375    16747  18899  13066   -992  -4917   -120  A    N  
ATOM   2844  CA  PRO A 375      38.070  18.717 514.685  1.00128.85      A    C  
ANISOU 2844  CA  PRO A 375    16930  19211  12816  -1322  -5301   -155  A    C  
ATOM   2845  C   PRO A 375      38.429  17.683 515.740  1.00125.10      A    C  
ANISOU 2845  C   PRO A 375    16362  19073  12098  -1150  -5401     53  A    C  
ATOM   2846  O   PRO A 375      37.893  16.574 515.776  1.00120.48      A    O  
ANISOU 2846  O   PRO A 375    15726  18485  11568   -781  -5160    184  A    O  
ATOM   2847  CB  PRO A 375      37.180  19.829 515.241  1.00126.39      A    C  
ANISOU 2847  CB  PRO A 375    17197  18553  12270  -1457  -5276   -518  A    C  
ATOM   2848  CG  PRO A 375      36.294  20.182 514.103  1.00121.46      A    C  
ANISOU 2848  CG  PRO A 375    16630  17567  11951  -1338  -4955   -653  A    C  
ATOM   2849  CD  PRO A 375      36.025  18.890 513.385  1.00120.75      A    C  
ANISOU 2849  CD  PRO A 375    16188  17540  12154   -979  -4683   -414  A    C  
ATOM   2850  N   ASP A 376      39.364  18.031 516.606  1.00128.52      A    N  
ANISOU 2850  N   ASP A 376    16779  19803  12250  -1438  -5779    103  A    N  
ATOM   2851  CA  ASP A 376      39.713  17.004 517.565  1.00130.95      A    C  
ANISOU 2851  CA  ASP A 376    16972  20448  12334  -1244  -5858    321  A    C  
ATOM   2852  C   ASP A 376      38.611  16.935 518.633  1.00129.49      A    C  
ANISOU 2852  C   ASP A 376    17279  20068  11854  -1076  -5716    119  A    C  
ATOM   2853  O   ASP A 376      37.717  17.784 518.694  1.00129.62      A    O  
ANISOU 2853  O   ASP A 376    17716  19736  11796  -1131  -5599   -179  A    O  
ATOM   2854  CB  ASP A 376      41.116  17.252 518.125  1.00135.07      A    C  
ANISOU 2854  CB  ASP A 376    17244  21427  12651  -1583  -6311    507  A    C  
ATOM   2855  CG  ASP A 376      41.223  18.544 518.901  1.00144.09      A    C  
ANISOU 2855  CG  ASP A 376    18806  22466  13475  -2049  -6643    241  A    C  
ATOM   2856  OD1 ASP A 376      40.246  19.323 518.900  1.00143.28      A    O  
ANISOU 2856  OD1 ASP A 376    19194  21920  13324  -2076  -6499    -99  A    O  
ATOM   2857  OD2 ASP A 376      42.291  18.780 519.508  1.00151.01      A    O1-
ANISOU 2857  OD2 ASP A 376    19541  23709  14128  -2383  -7059    386  A    O1-
ATOM   2858  N   GLN A 377      38.668  15.887 519.459  1.00125.62      A    N  
ANISOU 2858  N   GLN A 377    16724  19821  11185   -830  -5706    311  A    N  
ATOM   2859  CA  GLN A 377      37.605  15.587 520.424  1.00125.43      A    C  
ANISOU 2859  CA  GLN A 377    17084  19671  10902   -600  -5524    205  A    C  
ATOM   2860  C   GLN A 377      37.242  16.805 521.278  1.00135.70      A    C  
ANISOU 2860  C   GLN A 377    18906  20813  11841   -823  -5665   -121  A    C  
ATOM   2861  O   GLN A 377      36.056  17.076 521.529  1.00138.35      A    O  
ANISOU 2861  O   GLN A 377    19620  20880  12067   -643  -5407   -307  A    O  
ATOM   2862  CB  GLN A 377      38.028  14.382 521.269  1.00125.81      A    C  
ANISOU 2862  CB  GLN A 377    16962  20070  10771   -382  -5589    489  A    C  
ATOM   2863  CG  GLN A 377      37.183  14.084 522.487  1.00127.13      A    C  
ANISOU 2863  CG  GLN A 377    17489  20220  10595   -190  -5484    432  A    C  
ATOM   2864  CD  GLN A 377      37.293  12.618 522.914  1.00124.86      A    C  
ANISOU 2864  CD  GLN A 377    16998  20167  10275    127  -5405    757  A    C  
ATOM   2865  NE2 GLN A 377      38.295  11.921 522.388  1.00124.56      A    N  
ANISOU 2865  NE2 GLN A 377    16547  20366  10415    179  -5509   1026  A    N  
ATOM   2866  OE1 GLN A 377      36.488  12.126 523.702  1.00121.20      A    O  
ANISOU 2866  OE1 GLN A 377    16757  19679   9613    340  -5246    785  A    O  
ATOM   2867  N   THR A 378      38.254  17.555 521.721  1.00141.02      A    N  
ANISOU 2867  N   THR A 378    19622  21657  12303  -1209  -6082   -172  A    N  
ATOM   2868  CA  THR A 378      38.043  18.716 522.586  1.00140.06      A    C  
ANISOU 2868  CA  THR A 378    20079  21360  11776  -1444  -6284   -484  A    C  
ATOM   2869  C   THR A 378      37.181  19.768 521.898  1.00144.20      A    C  
ANISOU 2869  C   THR A 378    20968  21415  12408  -1479  -6086   -790  A    C  
ATOM   2870  O   THR A 378      36.238  20.301 522.498  1.00146.42      A    O  
ANISOU 2870  O   THR A 378    21789  21444  12400  -1328  -5943  -1033  A    O  
ATOM   2871  CB  THR A 378      39.383  19.338 522.953  1.00134.01      A    C  
ANISOU 2871  CB  THR A 378    19252  20844  10821  -1943  -6817   -446  A    C  
ATOM   2872  CG2 THR A 378      39.194  20.352 524.066  1.00138.06      A    C  
ANISOU 2872  CG2 THR A 378    20453  21181  10820  -2155  -7070   -750  A    C  
ATOM   2873  OG1 THR A 378      40.273  18.313 523.384  1.00134.65      A    O  
ANISOU 2873  OG1 THR A 378    18881  21417  10863  -1887  -6981   -102  A    O  
ATOM   2874  N   THR A 379      37.495  20.078 520.633  1.00138.78      A    N  
ANISOU 2874  N   THR A 379    19989  20623  12118  -1644  -6062   -762  A    N  
ATOM   2875  CA  THR A 379      36.702  21.039 519.873  1.00127.94      A    C  
ANISOU 2875  CA  THR A 379    18919  18811  10880  -1662  -5859  -1027  A    C  
ATOM   2876  C   THR A 379      35.265  20.554 519.749  1.00123.31      A    C  
ANISOU 2876  C   THR A 379    18458  18029  10365  -1187  -5367  -1067  A    C  
ATOM   2877  O   THR A 379      34.324  21.356 519.781  1.00123.88      A    O  
ANISOU 2877  O   THR A 379    18984  17780  10305  -1084  -5181  -1317  A    O  
ATOM   2878  CB  THR A 379      37.317  21.248 518.489  1.00122.08      A    C  
ANISOU 2878  CB  THR A 379    17751  18050  10583  -1876  -5891   -928  A    C  
ATOM   2879  CG2 THR A 379      36.535  22.290 517.714  1.00119.72      A    C  
ANISOU 2879  CG2 THR A 379    17779  17299  10412  -1908  -5699  -1202  A    C  
ATOM   2880  OG1 THR A 379      38.664  21.710 518.628  1.00128.35      A    O  
ANISOU 2880  OG1 THR A 379    18382  19090  11295  -2349  -6364   -832  A    O  
ATOM   2881  N   ILE A 380      35.080  19.243 519.581  1.00118.91      A    N  
ANISOU 2881  N   ILE A 380    17506  17665  10007   -894  -5158   -797  A    N  
ATOM   2882  CA  ILE A 380      33.736  18.681 519.497  1.00114.87      A    C  
ANISOU 2882  CA  ILE A 380    17071  17015   9558   -498  -4729   -767  A    C  
ATOM   2883  C   ILE A 380      32.986  18.961 520.795  1.00114.89      A    C  
ANISOU 2883  C   ILE A 380    17564  17006   9083   -324  -4669   -900  A    C  
ATOM   2884  O   ILE A 380      31.780  19.256 520.792  1.00112.33      A    O  
ANISOU 2884  O   ILE A 380    17505  16490   8687    -77  -4351   -999  A    O  
ATOM   2885  CB  ILE A 380      33.810  17.173 519.193  1.00113.26      A    C  
ANISOU 2885  CB  ILE A 380    16417  17016   9602   -274  -4596   -430  A    C  
ATOM   2886  CG1 ILE A 380      34.096  16.937 517.712  1.00112.05      A    C  
ANISOU 2886  CG1 ILE A 380    15881  16766   9925   -310  -4511   -330  A    C  
ATOM   2887  CG2 ILE A 380      32.515  16.476 519.578  1.00107.41      A    C  
ANISOU 2887  CG2 ILE A 380    15798  16226   8785     73  -4254   -339  A    C  
ATOM   2888  CD1 ILE A 380      34.176  15.475 517.350  1.00111.80      A    C  
ANISOU 2888  CD1 ILE A 380    15505  16869  10107    -68  -4392    -14  A    C  
ATOM   2889  N   ASN A 381      33.705  18.936 521.924  1.00121.53      A    N  
ANISOU 2889  N   ASN A 381    18540  18074   9563   -441  -4979   -894  A    N  
ATOM   2890  CA  ASN A 381      33.069  19.241 523.204  1.00120.85      A    C  
ANISOU 2890  CA  ASN A 381    18961  17984   8972   -258  -4942  -1027  A    C  
ATOM   2891  C   ASN A 381      32.773  20.735 523.345  1.00122.89      A    C  
ANISOU 2891  C   ASN A 381    19826  17914   8953   -371  -5007  -1389  A    C  
ATOM   2892  O   ASN A 381      31.755  21.114 523.942  1.00124.14      A    O  
ANISOU 2892  O   ASN A 381    20435  17946   8787    -67  -4775  -1519  A    O  
ATOM   2893  CB  ASN A 381      33.953  18.754 524.355  1.00124.04      A    C  
ANISOU 2893  CB  ASN A 381    19344  18728   9059   -351  -5272   -911  A    C  
ATOM   2894  CG  ASN A 381      34.082  17.232 524.401  1.00122.25      A    C  
ANISOU 2894  CG  ASN A 381    18628  18803   9016   -143  -5163   -550  A    C  
ATOM   2895  ND2 ASN A 381      34.497  16.708 525.551  1.00125.17      A    N  
ANISOU 2895  ND2 ASN A 381    19038  19465   9058    -95  -5340   -434  A    N  
ATOM   2896  OD1 ASN A 381      33.808  16.542 523.422  1.00118.24      A    O  
ANISOU 2896  OD1 ASN A 381    17755  18248   8922    -23  -4931   -380  A    O  
ATOM   2897  N   LYS A 382      33.646  21.602 522.813  1.00124.65      A    N  
ANISOU 2897  N   LYS A 382    20090  17999   9272   -791  -5321  -1534  A    N  
ATOM   2898  CA  LYS A 382      33.326  23.030 522.746  1.00132.58      A    C  
ANISOU 2898  CA  LYS A 382    21703  18611  10061   -906  -5368  -1875  A    C  
ATOM   2899  C   LYS A 382      32.072  23.303 521.914  1.00137.47      A    C  
ANISOU 2899  C   LYS A 382    22394  18952  10887   -580  -4895  -1951  A    C  
ATOM   2900  O   LYS A 382      31.257  24.161 522.274  1.00145.06      A    O  
ANISOU 2900  O   LYS A 382    23944  19652  11519   -370  -4742  -2181  A    O  
ATOM   2901  CB  LYS A 382      34.500  23.813 522.152  1.00134.70      A    C  
ANISOU 2901  CB  LYS A 382    21915  18792  10474  -1464  -5788  -1952  A    C  
ATOM   2902  CG  LYS A 382      35.875  23.395 522.619  1.00141.12      A    C  
ANISOU 2902  CG  LYS A 382    22410  19979  11232  -1837  -6251  -1763  A    C  
ATOM   2903  CD  LYS A 382      36.951  24.273 521.990  1.00143.82      A    C  
ANISOU 2903  CD  LYS A 382    22691  20250  11705  -2417  -6660  -1802  A    C  
ATOM   2904  CE  LYS A 382      38.303  24.063 522.663  1.00151.98      A    C  
ANISOU 2904  CE  LYS A 382    23506  21681  12559  -2831  -7181  -1615  A    C  
ATOM   2905  NZ  LYS A 382      39.304  25.079 522.233  1.00156.15      A    N1+
ANISOU 2905  NZ  LYS A 382    23958  22124  13250  -3372  -7472  -1634  A    N1+
ATOM   2906  N   LEU A 383      31.905  22.594 520.793  1.00130.71      A    N  
ANISOU 2906  N   LEU A 383    20965  18150  10548   -515  -4664  -1750  A    N  
ATOM   2907  CA  LEU A 383      30.706  22.747 519.968  1.00126.46      A    C  
ANISOU 2907  CA  LEU A 383    20428  17398  10225   -222  -4225  -1775  A    C  
ATOM   2908  C   LEU A 383      29.459  22.310 520.724  1.00128.45      A    C  
ANISOU 2908  C   LEU A 383    20854  17745  10206    252  -3867  -1691  A    C  
ATOM   2909  O   LEU A 383      28.482  23.064 520.823  1.00132.54      A    O  
ANISOU 2909  O   LEU A 383    21785  18071  10503    516  -3614  -1841  A    O  
ATOM   2910  CB  LEU A 383      30.849  21.990 518.646  1.00123.13      A    C  
ANISOU 2910  CB  LEU A 383    19372  17025  10385   -272  -4095  -1560  A    C  
ATOM   2911  CG  LEU A 383      31.766  22.680 517.633  1.00126.58      A    C  
ANISOU 2911  CG  LEU A 383    19669  17312  11114   -662  -4327  -1654  A    C  
ATOM   2912  CD1 LEU A 383      31.895  21.859 516.362  1.00119.27      A    C  
ANISOU 2912  CD1 LEU A 383    18145  16452  10721   -643  -4180  -1429  A    C  
ATOM   2913  CD2 LEU A 383      31.255  24.082 517.312  1.00130.12      A    C  
ANISOU 2913  CD2 LEU A 383    20617  17372  11449   -701  -4257  -1957  A    C  
ATOM   2914  N   VAL A 384      29.460  21.067 521.219  1.00123.97      A    N  
ANISOU 2914  N   VAL A 384    19952  17493   9656    385  -3826  -1416  A    N  
ATOM   2915  CA  VAL A 384      28.313  20.541 521.962  1.00120.92      A    C  
ANISOU 2915  CA  VAL A 384    19662  17259   9023    806  -3499  -1265  A    C  
ATOM   2916  C   VAL A 384      27.914  21.527 523.051  1.00128.88      A    C  
ANISOU 2916  C   VAL A 384    21348  18180   9439    998  -3499  -1504  A    C  
ATOM   2917  O   VAL A 384      26.763  21.981 523.122  1.00128.37      A    O  
ANISOU 2917  O   VAL A 384    21553  18035   9187   1356  -3155  -1538  A    O  
ATOM   2918  CB  VAL A 384      28.638  19.157 522.551  1.00122.34      A    C  
ANISOU 2918  CB  VAL A 384    19483  17778   9222    846  -3566   -959  A    C  
ATOM   2919  CG1 VAL A 384      27.596  18.756 523.585  1.00126.82      A    C  
ANISOU 2919  CG1 VAL A 384    20228  18535   9424   1237  -3302   -811  A    C  
ATOM   2920  CG2 VAL A 384      28.739  18.118 521.449  1.00120.79      A    C  
ANISOU 2920  CG2 VAL A 384    18711  17621   9564    777  -3479   -702  A    C  
ATOM   2921  N   GLU A 385      28.875  21.868 523.917  1.00140.72      A    N  
ANISOU 2921  N   GLU A 385    23147  19711  10611    777  -3893  -1656  A    N  
ATOM   2922  CA  GLU A 385      28.622  22.813 525.001  1.00141.44      A    C  
ANISOU 2922  CA  GLU A 385    23976  19681  10084    941  -3956  -1909  A    C  
ATOM   2923  C   GLU A 385      28.068  24.144 524.479  1.00142.41      A    C  
ANISOU 2923  C   GLU A 385    24601  19400  10107   1023  -3820  -2197  A    C  
ATOM   2924  O   GLU A 385      27.134  24.696 525.072  1.00143.40      A    O  
ANISOU 2924  O   GLU A 385    25244  19444   9799   1446  -3567  -2297  A    O  
ATOM   2925  CB  GLU A 385      29.873  22.982 525.871  1.00142.17      A    C  
ANISOU 2925  CB  GLU A 385    24292  19846   9879    586  -4476  -2024  A    C  
ATOM   2926  CG  GLU A 385      30.233  21.664 526.603  1.00148.07      A    C  
ANISOU 2926  CG  GLU A 385    24627  21022  10612    636  -4545  -1725  A    C  
ATOM   2927  CD  GLU A 385      31.514  21.720 527.441  1.00153.51      A    C  
ANISOU 2927  CD  GLU A 385    25442  21857  11029    276  -5070  -1782  A    C  
ATOM   2928  OE1 GLU A 385      31.911  22.826 527.870  1.00152.38      A    O  
ANISOU 2928  OE1 GLU A 385    25894  21488  10517     63  -5372  -2076  A    O  
ATOM   2929  OE2 GLU A 385      32.114  20.647 527.690  1.00151.75      A    O1-
ANISOU 2929  OE2 GLU A 385    24746  21975  10937    207  -5189  -1519  A    O1-
ATOM   2930  N   TRP A 386      28.645  24.704 523.404  1.00141.60      A    N  
ANISOU 2930  N   TRP A 386    24389  19048  10363    652  -3984  -2324  A    N  
ATOM   2931  CA  TRP A 386      28.116  25.976 522.900  1.00141.37      A    C  
ANISOU 2931  CA  TRP A 386    24868  18614  10233    739  -3853  -2593  A    C  
ATOM   2932  C   TRP A 386      26.675  25.844 522.412  1.00139.27      A    C  
ANISOU 2932  C   TRP A 386    24480  18365  10071   1247  -3289  -2462  A    C  
ATOM   2933  O   TRP A 386      25.877  26.783 522.573  1.00140.49      A    O  
ANISOU 2933  O   TRP A 386    25203  18295   9883   1584  -3068  -2638  A    O  
ATOM   2934  CB  TRP A 386      29.004  26.476 521.752  1.00136.44      A    C  
ANISOU 2934  CB  TRP A 386    24045  17762  10034    231  -4118  -2694  A    C  
ATOM   2935  CG  TRP A 386      28.580  27.777 521.105  1.00135.12      A    C  
ANISOU 2935  CG  TRP A 386    24372  17148   9818    257  -4018  -2961  A    C  
ATOM   2936  CD1 TRP A 386      28.956  29.043 521.459  1.00135.32      A    C  
ANISOU 2936  CD1 TRP A 386    25165  16797   9455     62  -4308  -3284  A    C  
ATOM   2937  CD2 TRP A 386      27.727  27.920 519.959  1.00132.90      A    C  
ANISOU 2937  CD2 TRP A 386    23863  16740   9892    474  -3620  -2915  A    C  
ATOM   2938  CE2 TRP A 386      27.616  29.299 519.688  1.00131.94      A    C  
ANISOU 2938  CE2 TRP A 386    24390  16171   9572    436  -3663  -3218  A    C  
ATOM   2939  CE3 TRP A 386      27.037  27.015 519.144  1.00128.05      A    C  
ANISOU 2939  CE3 TRP A 386    22593  16336   9724    686  -3248  -2640  A    C  
ATOM   2940  NE1 TRP A 386      28.374  29.962 520.618  1.00136.51      A    N  
ANISOU 2940  NE1 TRP A 386    25594  16582   9690    177  -4092  -3443  A    N  
ATOM   2941  CZ2 TRP A 386      26.843  29.793 518.639  1.00127.30      A    C  
ANISOU 2941  CZ2 TRP A 386    23773  15371   9223    633  -3324  -3248  A    C  
ATOM   2942  CZ3 TRP A 386      26.271  27.509 518.103  1.00125.50      A    C  
ANISOU 2942  CZ3 TRP A 386    22238  15812   9636    850  -2934  -2670  A    C  
ATOM   2943  CH2 TRP A 386      26.180  28.884 517.860  1.00124.00      A    C  
ANISOU 2943  CH2 TRP A 386    22661  15206   9248    838  -2962  -2968  A    C  
ATOM   2944  N   LEU A 387      26.303  24.688 521.862  1.00135.58      A    N  
ANISOU 2944  N   LEU A 387    23312  18174  10030   1325  -3055  -2135  A    N  
ATOM   2945  CA  LEU A 387      24.921  24.507 521.433  1.00134.81      A    C  
ANISOU 2945  CA  LEU A 387    23055  18148  10019   1759  -2551  -1955  A    C  
ATOM   2946  C   LEU A 387      24.000  24.472 522.643  1.00140.05      A    C  
ANISOU 2946  C   LEU A 387    24066  19016  10129   2266  -2298  -1869  A    C  
ATOM   2947  O   LEU A 387      23.062  25.272 522.759  1.00140.76      A    O  
ANISOU 2947  O   LEU A 387    24574  19003   9906   2675  -1998  -1951  A    O  
ATOM   2948  CB  LEU A 387      24.768  23.247 520.588  1.00126.03      A    C  
ANISOU 2948  CB  LEU A 387    21166  17257   9463   1669  -2416  -1613  A    C  
ATOM   2949  CG  LEU A 387      25.239  23.501 519.167  1.00122.25      A    C  
ANISOU 2949  CG  LEU A 387    20405  16543   9502   1345  -2498  -1692  A    C  
ATOM   2950  CD1 LEU A 387      25.399  22.194 518.425  1.00117.84      A    C  
ANISOU 2950  CD1 LEU A 387    19160  16170   9445   1204  -2476  -1386  A    C  
ATOM   2951  CD2 LEU A 387      24.253  24.427 518.476  1.00127.06      A    C  
ANISOU 2951  CD2 LEU A 387    21232  16929  10115   1588  -2173  -1796  A    C  
ATOM   2952  N   GLU A 388      24.277  23.549 523.572  1.00140.84      A    N  
ANISOU 2952  N   GLU A 388    24006  19426  10080   2274  -2409  -1688  A    N  
ATOM   2953  CA  GLU A 388      23.459  23.412 524.771  1.00144.48      A    C  
ANISOU 2953  CA  GLU A 388    24749  20135  10011   2756  -2176  -1565  A    C  
ATOM   2954  C   GLU A 388      23.473  24.675 525.624  1.00144.79      A    C  
ANISOU 2954  C   GLU A 388    25669  19933   9409   2974  -2258  -1915  A    C  
ATOM   2955  O   GLU A 388      22.631  24.814 526.517  1.00150.13      A    O  
ANISOU 2955  O   GLU A 388    26687  20771   9584   3487  -1989  -1842  A    O  
ATOM   2956  CB  GLU A 388      23.929  22.200 525.589  1.00148.93      A    C  
ANISOU 2956  CB  GLU A 388    24992  21046  10548   2661  -2340  -1324  A    C  
ATOM   2957  CG  GLU A 388      24.024  20.888 524.784  1.00144.97      A    C  
ANISOU 2957  CG  GLU A 388    23706  20730  10645   2434  -2308   -986  A    C  
ATOM   2958  CD  GLU A 388      24.169  19.640 525.658  1.00145.36      A    C  
ANISOU 2958  CD  GLU A 388    23482  21140  10607   2471  -2363   -684  A    C  
ATOM   2959  OE1 GLU A 388      24.933  19.673 526.650  1.00144.52      A    O  
ANISOU 2959  OE1 GLU A 388    23642  21103  10165   2402  -2649   -801  A    O  
ATOM   2960  OE2 GLU A 388      23.509  18.622 525.346  1.00143.36      A    O1-
ANISOU 2960  OE2 GLU A 388    22761  21095  10614   2554  -2134   -318  A    O1-
ATOM   2961  N   GLU A 389      24.404  25.597 525.365  1.00144.06      A    N  
ANISOU 2961  N   GLU A 389    25977  19457   9302   2599  -2630  -2274  A    N  
ATOM   2962  CA  GLU A 389      24.410  26.883 526.055  1.00153.50      A    C  
ANISOU 2962  CA  GLU A 389    28113  20325   9884   2770  -2739  -2634  A    C  
ATOM   2963  C   GLU A 389      23.503  27.895 525.367  1.00154.75      A    C  
ANISOU 2963  C   GLU A 389    28623  20191   9984   3106  -2397  -2763  A    C  
ATOM   2964  O   GLU A 389      22.774  28.636 526.039  1.00155.42      A    O  
ANISOU 2964  O   GLU A 389    29247  20166   9640   3575  -2146  -2836  A    O  
ATOM   2965  CB  GLU A 389      25.833  27.436 526.137  1.00156.44      A    C  
ANISOU 2965  CB  GLU A 389    28798  20411  10229   2158  -3342  -2933  A    C  
ATOM   2966  CG  GLU A 389      26.601  27.043 527.381  1.00158.51      A    C  
ANISOU 2966  CG  GLU A 389    29179  20861  10185   1993  -3682  -2926  A    C  
ATOM   2967  CD  GLU A 389      27.978  27.671 527.412  1.00159.18      A    C  
ANISOU 2967  CD  GLU A 389    29402  20692  10387   1324  -4224  -3137  A    C  
ATOM   2968  OE1 GLU A 389      28.372  28.273 526.387  1.00159.06      A    O  
ANISOU 2968  OE1 GLU A 389    29346  20391  10697    976  -4356  -3263  A    O  
ATOM   2969  OE2 GLU A 389      28.665  27.562 528.452  1.00158.15      A    O1-
ANISOU 2969  OE2 GLU A 389    29390  20671  10028   1141  -4511  -3149  A    O1-
ATOM   2970  N   ASN A 390      23.539  27.947 524.030  1.00152.00      A    N  
ANISOU 2970  N   ASN A 390    27837  19706  10209   2852  -2339  -2737  A    N  
ATOM   2971  CA  ASN A 390      22.708  28.905 523.305  1.00148.07      A    C  
ANISOU 2971  CA  ASN A 390    27640  18936   9683   3159  -2018  -2848  A    C  
ATOM   2972  C   ASN A 390      21.214  28.665 523.486  1.00148.98      A    C  
ANISOU 2972  C   ASN A 390    27640  19363   9601   3857  -1433  -2561  A    C  
ATOM   2973  O   ASN A 390      20.417  29.477 523.002  1.00150.44      A    O  
ANISOU 2973  O   ASN A 390    28106  19377   9679   4216  -1119  -2620  A    O  
ATOM   2974  CB  ASN A 390      23.035  28.867 521.812  1.00140.67      A    C  
ANISOU 2974  CB  ASN A 390    26166  17849   9432   2745  -2061  -2830  A    C  
ATOM   2975  CG  ASN A 390      23.933  30.007 521.379  1.00139.30      A    C  
ANISOU 2975  CG  ASN A 390    26497  17173   9259   2323  -2436  -3204  A    C  
ATOM   2976  ND2 ASN A 390      23.909  30.320 520.084  1.00136.75      A    N  
ANISOU 2976  ND2 ASN A 390    25900  16658   9402   2141  -2359  -3222  A    N  
ATOM   2977  OD1 ASN A 390      24.642  30.599 522.195  1.00135.69      A    O  
ANISOU 2977  OD1 ASN A 390    26662  16501   8393   2136  -2804  -3455  A    O  
ATOM   2978  N   GLY A 391      20.813  27.590 524.164  1.00149.69      A    N  
ANISOU 2978  N   GLY A 391    27321  19924   9630   4058  -1278  -2225  A    N  
ATOM   2979  CA  GLY A 391      19.438  27.142 524.123  1.00149.27      A    C  
ANISOU 2979  CA  GLY A 391    26915  20261   9539   4594   -743  -1836  A    C  
ATOM   2980  C   GLY A 391      19.024  26.523 522.806  1.00142.25      A    C  
ANISOU 2980  C   GLY A 391    25233  19496   9321   4402   -557  -1562  A    C  
ATOM   2981  O   GLY A 391      17.886  26.052 522.686  1.00143.36      A    O  
ANISOU 2981  O   GLY A 391    24984  20001   9486   4761   -146  -1179  A    O  
ATOM   2982  N   LYS A 392      19.912  26.505 521.818  1.00134.01      A    N  
ANISOU 2982  N   LYS A 392    23937  18178   8801   3844   -855  -1722  A    N  
ATOM   2983  CA  LYS A 392      19.640  25.941 520.507  1.00133.00      A    C  
ANISOU 2983  CA  LYS A 392    23116  18110   9307   3629   -727  -1504  A    C  
ATOM   2984  C   LYS A 392      19.793  24.427 520.463  1.00132.13      A    C  
ANISOU 2984  C   LYS A 392    22294  18341   9570   3379   -797  -1148  A    C  
ATOM   2985  O   LYS A 392      19.708  23.851 519.370  1.00127.79      A    O  
ANISOU 2985  O   LYS A 392    21198  17805   9552   3142   -759   -978  A    O  
ATOM   2986  CB  LYS A 392      20.567  26.580 519.469  1.00131.30      A    C  
ANISOU 2986  CB  LYS A 392    22963  17460   9466   3167  -1015  -1819  A    C  
ATOM   2987  CG  LYS A 392      20.397  28.085 519.323  1.00135.38      A    C  
ANISOU 2987  CG  LYS A 392    24189  17577   9674   3367   -953  -2160  A    C  
ATOM   2988  CD  LYS A 392      20.932  28.539 517.977  1.00133.24      A    C  
ANISOU 2988  CD  LYS A 392    23757  16970   9899   2965  -1095  -2324  A    C  
ATOM   2989  CE  LYS A 392      20.584  29.985 517.659  1.00132.16      A    C  
ANISOU 2989  CE  LYS A 392    24276  16432   9506   3194   -970  -2609  A    C  
ATOM   2990  NZ  LYS A 392      21.079  30.370 516.296  1.00118.77      A    N1+
ANISOU 2990  NZ  LYS A 392    22364  14439   8324   2794  -1093  -2730  A    N1+
ATOM   2991  N   LYS A 393      20.004  23.771 521.611  1.00138.60      A    N  
ANISOU 2991  N   LYS A 393    23145  19413  10104   3438   -900  -1031  A    N  
ATOM   2992  CA  LYS A 393      20.332  22.346 521.594  1.00139.55      A    C  
ANISOU 2992  CA  LYS A 393    22669  19788  10564   3161  -1028   -729  A    C  
ATOM   2993  C   LYS A 393      19.150  21.506 521.132  1.00143.13      A    C  
ANISOU 2993  C   LYS A 393    22585  20556  11243   3326   -673   -268  A    C  
ATOM   2994  O   LYS A 393      19.318  20.603 520.308  1.00146.32      A    O  
ANISOU 2994  O   LYS A 393    22478  20975  12143   3010   -751    -78  A    O  
ATOM   2995  CB  LYS A 393      20.830  21.884 522.972  1.00136.46      A    C  
ANISOU 2995  CB  LYS A 393    22469  19595   9784   3202  -1221   -709  A    C  
ATOM   2996  CG  LYS A 393      19.838  21.105 523.845  1.00138.88      A    C  
ANISOU 2996  CG  LYS A 393    22607  20350   9812   3581   -927   -301  A    C  
ATOM   2997  CD  LYS A 393      20.556  20.228 524.876  1.00139.62      A    C  
ANISOU 2997  CD  LYS A 393    22654  20641   9753   3454  -1187   -213  A    C  
ATOM   2998  CE  LYS A 393      19.604  19.656 525.930  1.00137.97      A    C  
ANISOU 2998  CE  LYS A 393    22400  20868   9153   3872   -903    158  A    C  
ATOM   2999  NZ  LYS A 393      20.324  18.939 527.029  1.00134.34      A    N1+
ANISOU 2999  NZ  LYS A 393    21985  20584   8476   3787  -1158    206  A    N1+
ATOM   3000  N   SER A 394      17.940  21.815 521.612  1.00139.44      A    N  
ANISOU 3000  N   SER A 394    22238  20341  10402   3821   -288    -67  A    N  
ATOM   3001  CA  SER A 394      16.802  20.941 521.346  1.00135.28      A    C  
ANISOU 3001  CA  SER A 394    21170  20199  10032   3945     19    450  A    C  
ATOM   3002  C   SER A 394      16.332  21.031 519.898  1.00138.81      A    C  
ANISOU 3002  C   SER A 394    21264  20527  10951   3793    150    532  A    C  
ATOM   3003  O   SER A 394      15.789  20.057 519.364  1.00139.34      A    O  
ANISOU 3003  O   SER A 394    20799  20803  11343   3633    228    926  A    O  
ATOM   3004  CB  SER A 394      15.661  21.273 522.298  1.00134.22      A    C  
ANISOU 3004  CB  SER A 394    21228  20440   9330   4544    403    691  A    C  
ATOM   3005  OG  SER A 394      16.091  21.120 523.635  1.00140.22      A    O  
ANISOU 3005  OG  SER A 394    22310  21318   9649   4685    277    630  A    O  
ATOM   3006  N   LEU A 395      16.515  22.179 519.254  1.00136.37      A    N  
ANISOU 3006  N   LEU A 395    21266  19877  10672   3829    162    179  A    N  
ATOM   3007  CA  LEU A 395      16.156  22.308 517.853  1.00134.47      A    C  
ANISOU 3007  CA  LEU A 395    20710  19502  10882   3676    265    227  A    C  
ATOM   3008  C   LEU A 395      17.239  21.676 516.990  1.00124.88      A    C  
ANISOU 3008  C   LEU A 395    19215  18020  10213   3116    -94    102  A    C  
ATOM   3009  O   LEU A 395      18.344  21.391 517.461  1.00118.04      A    O  
ANISOU 3009  O   LEU A 395    18466  17040   9346   2875   -422    -81  A    O  
ATOM   3010  CB  LEU A 395      15.968  23.780 517.476  1.00142.60      A    C  
ANISOU 3010  CB  LEU A 395    22198  20252  11731   3936    416    -98  A    C  
ATOM   3011  CG  LEU A 395      14.645  24.411 517.920  1.00148.50      A    C  
ANISOU 3011  CG  LEU A 395    23125  21285  12012   4567    872    108  A    C  
ATOM   3012  CD1 LEU A 395      14.629  25.913 517.647  1.00149.57      A    C  
ANISOU 3012  CD1 LEU A 395    23856  21063  11912   4844    978   -273  A    C  
ATOM   3013  CD2 LEU A 395      13.467  23.716 517.248  1.00144.93      A    C  
ANISOU 3013  CD2 LEU A 395    22027  21229  11812   4622   1168    632  A    C  
ATOM   3014  N   PHE A 396      16.931  21.478 515.708  1.00123.91      A    N  
ANISOU 3014  N   PHE A 396    18727  17814  10540   2933    -29    213  A    N  
ATOM   3015  CA  PHE A 396      18.018  21.088 514.836  1.00121.18      A    C  
ANISOU 3015  CA  PHE A 396    18205  17177  10661   2478   -349     43  A    C  
ATOM   3016  C   PHE A 396      18.811  22.358 514.599  1.00122.39      A    C  
ANISOU 3016  C   PHE A 396    18779  16961  10763   2430   -485   -426  A    C  
ATOM   3017  O   PHE A 396      18.250  23.457 514.607  1.00133.44      A    O  
ANISOU 3017  O   PHE A 396    20508  18277  11915   2722   -272   -567  A    O  
ATOM   3018  CB  PHE A 396      17.404  20.545 513.550  1.00123.97      A    C  
ANISOU 3018  CB  PHE A 396    18104  17538  11460   2326   -236    296  A    C  
ATOM   3019  CG  PHE A 396      16.039  21.149 513.265  1.00135.86      A    C  
ANISOU 3019  CG  PHE A 396    19567  19222  12832   2657    153    483  A    C  
ATOM   3020  CD1 PHE A 396      15.909  22.351 512.574  1.00139.38      A    C  
ANISOU 3020  CD1 PHE A 396    20225  19438  13297   2788    283    226  A    C  
ATOM   3021  CD2 PHE A 396      14.885  20.542 513.765  1.00138.75      A    C  
ANISOU 3021  CD2 PHE A 396    19686  20021  13011   2862    394    946  A    C  
ATOM   3022  CE1 PHE A 396      14.644  22.913 512.348  1.00140.57      A    C  
ANISOU 3022  CE1 PHE A 396    20332  19790  13287   3148    660    425  A    C  
ATOM   3023  CE2 PHE A 396      13.630  21.098 513.551  1.00142.30      A    C  
ANISOU 3023  CE2 PHE A 396    20054  20713  13303   3199    763   1172  A    C  
ATOM   3024  CZ  PHE A 396      13.507  22.281 512.839  1.00143.99      A    C  
ANISOU 3024  CZ  PHE A 396    20476  20699  13536   3362    904    909  A    C  
ATOM   3025  N   TRP A 397      20.098  22.230 514.300  1.00115.53      A    N  
ANISOU 3025  N   TRP A 397    17895  15867  10135   2062   -836   -643  A    N  
ATOM   3026  CA  TRP A 397      20.819  23.444 513.959  1.00117.01      A    C  
ANISOU 3026  CA  TRP A 397    18445  15708  10306   1949   -983  -1041  A    C  
ATOM   3027  C   TRP A 397      21.818  23.248 512.825  1.00109.41      A    C  
ANISOU 3027  C   TRP A 397    17202  14532   9836   1543  -1230  -1136  A    C  
ATOM   3028  O   TRP A 397      22.519  22.233 512.794  1.00106.73      A    O  
ANISOU 3028  O   TRP A 397    16557  14289   9709   1318  -1439  -1008  A    O  
ATOM   3029  CB  TRP A 397      21.441  24.013 515.241  1.00123.96      A    C  
ANISOU 3029  CB  TRP A 397    19842  16548  10708   1996  -1183  -1281  A    C  
ATOM   3030  CG  TRP A 397      21.983  25.374 515.096  1.00122.67      A    C  
ANISOU 3030  CG  TRP A 397    20182  16023  10406   1911  -1324  -1669  A    C  
ATOM   3031  CD1 TRP A 397      21.295  26.531 515.312  1.00124.16      A    C  
ANISOU 3031  CD1 TRP A 397    20893  16051  10230   2246  -1111  -1840  A    C  
ATOM   3032  CD2 TRP A 397      23.317  25.753 514.778  1.00122.46      A    C  
ANISOU 3032  CD2 TRP A 397    20232  15752  10546   1474  -1717  -1913  A    C  
ATOM   3033  CE2 TRP A 397      23.360  27.161 514.785  1.00127.73      A    C  
ANISOU 3033  CE2 TRP A 397    21493  16082  10956   1512  -1747  -2233  A    C  
ATOM   3034  CE3 TRP A 397      24.477  25.043 514.468  1.00120.73      A    C  
ANISOU 3034  CE3 TRP A 397    19636  15583  10654   1067  -2043  -1864  A    C  
ATOM   3035  NE1 TRP A 397      22.107  27.611 515.109  1.00128.84      A    N  
ANISOU 3035  NE1 TRP A 397    21925  16260  10767   2014  -1364  -2196  A    N  
ATOM   3036  CZ2 TRP A 397      24.516  27.870 514.497  1.00130.46      A    C  
ANISOU 3036  CZ2 TRP A 397    22047  16142  11379   1092  -2118  -2489  A    C  
ATOM   3037  CZ3 TRP A 397      25.622  25.748 514.182  1.00122.21      A    C  
ANISOU 3037  CZ3 TRP A 397    19978  15543  10914    692  -2384  -2098  A    C  
ATOM   3038  CH2 TRP A 397      25.636  27.148 514.199  1.00126.47      A    C  
ANISOU 3038  CH2 TRP A 397    21093  15749  11210    673  -2433  -2401  A    C  
ATOM   3039  N   HIS A 398      21.894  24.202 511.899  1.00106.80      A    N  
ANISOU 3039  N   HIS A 398    16984  13924   9670   1477  -1199  -1343  A    N  
ATOM   3040  CA  HIS A 398      22.736  24.018 510.724  1.00103.80      A    C  
ANISOU 3040  CA  HIS A 398    16300  13377   9761   1138  -1384  -1390  A    C  
ATOM   3041  C   HIS A 398      23.212  25.388 510.252  1.00108.32      A    C  
ANISOU 3041  C   HIS A 398    17211  13620  10326   1019  -1473  -1717  A    C  
ATOM   3042  O   HIS A 398      22.513  26.393 510.404  1.00112.60      A    O  
ANISOU 3042  O   HIS A 398    18147  14030  10607   1261  -1276  -1855  A    O  
ATOM   3043  CB  HIS A 398      22.032  23.222 509.616  1.00100.78      A    C  
ANISOU 3043  CB  HIS A 398    15456  13062   9773   1158  -1185  -1125  A    C  
ATOM   3044  CG  HIS A 398      20.897  23.940 508.956  1.00105.07      A    C  
ANISOU 3044  CG  HIS A 398    16053  13538  10332   1386   -857  -1114  A    C  
ATOM   3045  CD2 HIS A 398      20.796  24.523 507.739  1.00 99.84      A    C  
ANISOU 3045  CD2 HIS A 398    15318  12665   9950   1328   -774  -1205  A    C  
ATOM   3046  ND1 HIS A 398      19.654  24.057 509.540  1.00111.58      A    N  
ANISOU 3046  ND1 HIS A 398    16975  14569  10851   1742   -551   -949  A    N  
ATOM   3047  CE1 HIS A 398      18.845  24.709 508.725  1.00106.34      A    C  
ANISOU 3047  CE1 HIS A 398    16301  13832  10271   1901   -295   -941  A    C  
ATOM   3048  NE2 HIS A 398      19.512  24.999 507.623  1.00100.81      A    N  
ANISOU 3048  NE2 HIS A 398    15509  12864   9931   1648   -428  -1106  A    N  
ATOM   3049  N   SER A 399      24.423  25.406 509.688  1.00108.85      A    N  
ANISOU 3049  N   SER A 399    17129  13568  10662    654  -1772  -1813  A    N  
ATOM   3050  CA  SER A 399      25.084  26.601 509.175  1.00108.20      A    C  
ANISOU 3050  CA  SER A 399    17306  13183  10624    432  -1930  -2080  A    C  
ATOM   3051  C   SER A 399      26.105  26.213 508.106  1.00105.72      A    C  
ANISOU 3051  C   SER A 399    16551  12852  10766    101  -2131  -2017  A    C  
ATOM   3052  O   SER A 399      26.754  25.170 508.216  1.00 98.28      A    O  
ANISOU 3052  O   SER A 399    15259  12122   9959    -12  -2290  -1843  A    O  
ATOM   3053  CB  SER A 399      25.765  27.384 510.304  1.00106.72      A    C  
ANISOU 3053  CB  SER A 399    17643  12896  10008    300  -2212  -2312  A    C  
ATOM   3054  OG  SER A 399      26.695  28.319 509.789  1.00106.29      A    O  
ANISOU 3054  OG  SER A 399    17752  12582  10050    -57  -2477  -2509  A    O  
ATOM   3055  N   HIS A 400      26.219  27.040 507.062  1.00110.41      A    N  
ANISOU 3055  N   HIS A 400    17169  13203  11579    -14  -2103  -2139  A    N  
ATOM   3056  CA  HIS A 400      27.276  26.927 506.057  1.00111.08      A    C  
ANISOU 3056  CA  HIS A 400    16898  13263  12045   -325  -2304  -2098  A    C  
ATOM   3057  C   HIS A 400      28.310  28.048 506.200  1.00115.10      A    C  
ANISOU 3057  C   HIS A 400    17698  13593  12440   -682  -2626  -2301  A    C  
ATOM   3058  O   HIS A 400      29.027  28.360 505.243  1.00115.51      A    O  
ANISOU 3058  O   HIS A 400    17537  13570  12781   -929  -2745  -2291  A    O  
ATOM   3059  CB  HIS A 400      26.725  26.885 504.630  1.00108.72      A    C  
ANISOU 3059  CB  HIS A 400    16323  12857  12128   -228  -2054  -2028  A    C  
ATOM   3060  CG  HIS A 400      25.904  28.075 504.244  1.00108.46      A    C  
ANISOU 3060  CG  HIS A 400    16640  12554  12017    -92  -1834  -2207  A    C  
ATOM   3061  CD2 HIS A 400      26.229  29.167 503.513  1.00104.46      A    C  
ANISOU 3061  CD2 HIS A 400    16299  11780  11613   -255  -1881  -2373  A    C  
ATOM   3062  ND1 HIS A 400      24.572  28.214 504.566  1.00107.86      A    N  
ANISOU 3062  ND1 HIS A 400    16768  12483  11733    271  -1511  -2195  A    N  
ATOM   3063  CE1 HIS A 400      24.119  29.351 504.069  1.00105.97      A    C  
ANISOU 3063  CE1 HIS A 400    16825  11985  11455    359  -1360  -2357  A    C  
ATOM   3064  NE2 HIS A 400      25.105  29.948 503.425  1.00104.13      A    N  
ANISOU 3064  NE2 HIS A 400    16594  11559  11412     32  -1586  -2479  A    N  
ATOM   3065  N   MET A 401      28.390  28.656 507.382  1.00115.33      A    N  
ANISOU 3065  N   MET A 401    18230  13554  12036   -722  -2781  -2468  A    N  
ATOM   3066  CA  MET A 401      29.386  29.667 507.719  1.00123.46      A    C  
ANISOU 3066  CA  MET A 401    19613  14413  12885  -1121  -3159  -2645  A    C  
ATOM   3067  C   MET A 401      29.559  29.737 509.233  1.00122.19      A    C  
ANISOU 3067  C   MET A 401    19878  14313  12234  -1137  -3368  -2740  A    C  
ATOM   3068  O   MET A 401      29.061  30.648 509.906  1.00123.06      A    O  
ANISOU 3068  O   MET A 401    20647  14170  11941  -1021  -3344  -2966  A    O  
ATOM   3069  CB  MET A 401      28.957  31.030 507.156  1.00130.63      A    C  
ANISOU 3069  CB  MET A 401    20981  14908  13745  -1128  -3060  -2873  A    C  
ATOM   3070  CG  MET A 401      29.782  32.243 507.624  1.00147.01      A    C  
ANISOU 3070  CG  MET A 401    23614  16707  15536  -1540  -3454  -3088  A    C  
ATOM   3071  SD  MET A 401      31.585  32.288 507.523  1.00162.51      A    S  
ANISOU 3071  SD  MET A 401    25270  18826  17649  -2230  -4023  -2969  A    S  
ATOM   3072  CE  MET A 401      31.793  33.046 505.919  1.00150.55      A    C  
ANISOU 3072  CE  MET A 401    23565  17079  16557  -2437  -3963  -2959  A    C  
ATOM   3073  N   LEU A 402      30.236  28.712 509.768  1.00115.14      A    N  
ANISOU 3073  N   LEU A 402    18622  13767  11360  -1234  -3555  -2553  A    N  
ATOM   3074  CA  LEU A 402      30.507  28.622 511.199  1.00123.47      A    C  
ANISOU 3074  CA  LEU A 402    20001  14939  11972  -1267  -3780  -2605  A    C  
ATOM   3075  C   LEU A 402      31.215  29.847 511.757  1.00129.23      A    C  
ANISOU 3075  C   LEU A 402    21314  15422  12366  -1650  -4170  -2838  A    C  
ATOM   3076  O   LEU A 402      30.886  30.298 512.857  1.00133.13      A    O  
ANISOU 3076  O   LEU A 402    22410  15796  12377  -1538  -4228  -3014  A    O  
ATOM   3077  CB  LEU A 402      31.316  27.362 511.493  1.00126.70      A    C  
ANISOU 3077  CB  LEU A 402    19864  15764  12511  -1365  -3955  -2340  A    C  
ATOM   3078  CG  LEU A 402      30.419  26.127 511.517  1.00117.37      A    C  
ANISOU 3078  CG  LEU A 402    18365  14789  11443   -939  -3603  -2143  A    C  
ATOM   3079  CD1 LEU A 402      31.233  24.860 511.355  1.00109.06      A    C  
ANISOU 3079  CD1 LEU A 402    16721  14079  10637  -1012  -3730  -1858  A    C  
ATOM   3080  CD2 LEU A 402      29.631  26.108 512.818  1.00120.11      A    C  
ANISOU 3080  CD2 LEU A 402    19144  15166  11324   -651  -3494  -2219  A    C  
ATOM   3081  N   LYS A 403      32.208  30.387 511.041  1.00132.83      A    N  
ANISOU 3081  N   LYS A 403    21623  15804  13043  -2116  -4463  -2824  A    N  
ATOM   3082  CA  LYS A 403      32.977  31.471 511.649  1.00138.46      A    C  
ANISOU 3082  CA  LYS A 403    22890  16302  13415  -2573  -4914  -3003  A    C  
ATOM   3083  C   LYS A 403      32.138  32.733 511.851  1.00140.01      A    C  
ANISOU 3083  C   LYS A 403    23949  15986  13265  -2419  -4798  -3333  A    C  
ATOM   3084  O   LYS A 403      32.401  33.490 512.793  1.00144.74      A    O  
ANISOU 3084  O   LYS A 403    25182  16383  13429  -2596  -5069  -3506  A    O  
ATOM   3085  CB  LYS A 403      34.259  31.763 510.863  1.00143.16      A    C  
ANISOU 3085  CB  LYS A 403    23100  16982  14313  -3150  -5278  -2855  A    C  
ATOM   3086  CG  LYS A 403      35.265  30.609 510.923  1.00146.68      A    C  
ANISOU 3086  CG  LYS A 403    22798  17968  14965  -3304  -5469  -2520  A    C  
ATOM   3087  CD  LYS A 403      36.596  30.947 510.262  1.00149.69      A    C  
ANISOU 3087  CD  LYS A 403    22788  18510  15577  -3874  -5852  -2321  A    C  
ATOM   3088  CE  LYS A 403      37.540  29.747 510.259  1.00145.84      A    C  
ANISOU 3088  CE  LYS A 403    21526  18603  15284  -3915  -5977  -1949  A    C  
ATOM   3089  NZ  LYS A 403      38.927  30.134 509.858  1.00148.31      A    N1+
ANISOU 3089  NZ  LYS A 403    21473  19161  15718  -4498  -6409  -1707  A    N1+
ATOM   3090  N   GLU A 404      31.140  32.990 510.996  1.00138.39      A    N  
ANISOU 3090  N   GLU A 404    23761  15573  13247  -2060  -4370  -3391  A    N  
ATOM   3091  CA  GLU A 404      30.238  34.119 511.233  1.00136.72      A    C  
ANISOU 3091  CA  GLU A 404    24379  14905  12663  -1791  -4196  -3679  A    C  
ATOM   3092  C   GLU A 404      28.958  33.759 511.988  1.00135.20      A    C  
ANISOU 3092  C   GLU A 404    24436  14784  12151  -1134  -3783  -3713  A    C  
ATOM   3093  O   GLU A 404      28.444  34.596 512.740  1.00142.26      A    O  
ANISOU 3093  O   GLU A 404    26127  15383  12542   -905  -3747  -3940  A    O  
ATOM   3094  CB  GLU A 404      29.864  34.807 509.918  1.00134.69      A    C  
ANISOU 3094  CB  GLU A 404    24093  14362  12722  -1764  -3975  -3727  A    C  
ATOM   3095  CG  GLU A 404      30.959  35.715 509.380  1.00144.14      A    C  
ANISOU 3095  CG  GLU A 404    25286  15369  14112  -2353  -4316  -3712  A    C  
ATOM   3096  CD  GLU A 404      30.575  36.420 508.089  1.00147.86      A    C  
ANISOU 3096  CD  GLU A 404    25715  15569  14896  -2301  -4072  -3738  A    C  
ATOM   3097  OE1 GLU A 404      29.410  36.282 507.648  1.00145.06      A    O  
ANISOU 3097  OE1 GLU A 404    25433  15126  14557  -1806  -3658  -3811  A    O  
ATOM   3098  OE2 GLU A 404      31.435  37.141 507.536  1.00150.29      A    O1-
ANISOU 3098  OE2 GLU A 404    25919  15769  15415  -2748  -4290  -3665  A    O1-
ATOM   3099  N   ASP A 405      28.439  32.532 511.867  1.00130.77      A    N  
ANISOU 3099  N   ASP A 405    23238  14616  11834   -818  -3479  -3469  A    N  
ATOM   3100  CA  ASP A 405      27.248  32.180 512.642  1.00130.11      A    C  
ANISOU 3100  CA  ASP A 405    23354  14655  11426   -231  -3109  -3446  A    C  
ATOM   3101  C   ASP A 405      27.628  31.868 514.085  1.00133.47      A    C  
ANISOU 3101  C   ASP A 405    24063  15242  11409   -255  -3358  -3474  A    C  
ATOM   3102  O   ASP A 405      27.078  32.456 515.022  1.00137.10      A    O  
ANISOU 3102  O   ASP A 405    25219  15542  11329     50  -3290  -3646  A    O  
ATOM   3103  CB  ASP A 405      26.490  31.010 511.999  1.00121.36      A    C  
ANISOU 3103  CB  ASP A 405    21510  13887  10715     73  -2717  -3152  A    C  
ATOM   3104  CG  ASP A 405      25.523  31.462 510.911  1.00118.50      A    C  
ANISOU 3104  CG  ASP A 405    21100  13356  10568    349  -2325  -3151  A    C  
ATOM   3105  OD1 ASP A 405      25.034  32.607 510.996  1.00112.02      A    O  
ANISOU 3105  OD1 ASP A 405    20914  12206   9441    542  -2218  -3367  A    O  
ATOM   3106  OD2 ASP A 405      25.234  30.674 509.984  1.00125.16      A    O1-
ANISOU 3106  OD2 ASP A 405    21308  14389  11859    392  -2127  -2932  A    O1-
ATOM   3107  N   ALA A 406      28.534  30.911 514.286  1.00131.20      A    N  
ANISOU 3107  N   ALA A 406    23245  15286  11318   -563  -3624  -3289  A    N  
ATOM   3108  CA  ALA A 406      29.126  30.621 515.590  1.00135.13      A    C  
ANISOU 3108  CA  ALA A 406    23958  15955  11432   -686  -3940  -3303  A    C  
ATOM   3109  C   ALA A 406      30.499  31.291 515.683  1.00138.39      A    C  
ANISOU 3109  C   ALA A 406    24573  16223  11785  -1329  -4510  -3419  A    C  
ATOM   3110  O   ALA A 406      31.529  30.636 515.451  1.00137.28      A    O  
ANISOU 3110  O   ALA A 406    23850  16372  11938  -1708  -4784  -3220  A    O  
ATOM   3111  CB  ALA A 406      29.245  29.108 515.791  1.00131.72      A    C  
ANISOU 3111  CB  ALA A 406    22815  16006  11228   -598  -3871  -2992  A    C  
ATOM   3112  N   PRO A 407      30.584  32.578 516.030  1.00142.79      A    N  
ANISOU 3112  N   PRO A 407    25938  16354  11960  -1477  -4713  -3703  A    N  
ATOM   3113  CA  PRO A 407      31.892  33.247 516.001  1.00147.71      A    C  
ANISOU 3113  CA  PRO A 407    26502  16894  12727  -2116  -5143  -3671  A    C  
ATOM   3114  C   PRO A 407      32.859  32.680 517.035  1.00150.53      A    C  
ANISOU 3114  C   PRO A 407    26690  17587  12918  -2410  -5525  -3547  A    C  
ATOM   3115  O   PRO A 407      32.476  32.352 518.161  1.00153.50      A    O  
ANISOU 3115  O   PRO A 407    27351  18069  12904  -2117  -5475  -3590  A    O  
ATOM   3116  CB  PRO A 407      31.543  34.713 516.290  1.00154.58      A    C  
ANISOU 3116  CB  PRO A 407    28110  17266  13356  -2044  -5060  -3874  A    C  
ATOM   3117  CG  PRO A 407      30.312  34.632 517.116  1.00154.50      A    C  
ANISOU 3117  CG  PRO A 407    28571  17210  12921  -1384  -4695  -3987  A    C  
ATOM   3118  CD  PRO A 407      29.527  33.494 516.503  1.00146.75      A    C  
ANISOU 3118  CD  PRO A 407    27128  16521  12108  -1004  -4375  -3886  A    C  
ATOM   3119  N   GLY A 408      34.129  32.587 516.642  1.00148.19      A    N  
ANISOU 3119  N   GLY A 408    25903  17487  12916  -2974  -5892  -3365  A    N  
ATOM   3120  CA  GLY A 408      35.200  32.181 517.535  1.00147.03      A    C  
ANISOU 3120  CA  GLY A 408    25544  17676  12646  -3311  -6278  -3210  A    C  
ATOM   3121  C   GLY A 408      35.203  30.730 517.976  1.00147.84      A    C  
ANISOU 3121  C   GLY A 408    25202  18265  12704  -3105  -6282  -3032  A    C  
ATOM   3122  O   GLY A 408      35.014  30.440 519.160  1.00135.51      A    O  
ANISOU 3122  O   GLY A 408    23914  16811  10761  -2909  -6306  -3073  A    O  
ATOM   3123  N   LEU A 409      35.429  29.801 517.040  1.00151.02      A    N  
ANISOU 3123  N   LEU A 409    24927  18966  13486  -3133  -6265  -2812  A    N  
ATOM   3124  CA  LEU A 409      35.548  28.394 517.410  1.00147.64      A    C  
ANISOU 3124  CA  LEU A 409    23916  19019  13160  -2891  -6163  -2543  A    C  
ATOM   3125  C   LEU A 409      36.686  27.694 516.668  1.00145.85      A    C  
ANISOU 3125  C   LEU A 409    22855  19199  13362  -3186  -6347  -2200  A    C  
ATOM   3126  O   LEU A 409      36.651  26.467 516.517  1.00142.72      A    O  
ANISOU 3126  O   LEU A 409    21890  19139  13199  -2893  -6134  -1952  A    O  
ATOM   3127  CB  LEU A 409      34.216  27.660 517.178  1.00135.17      A    C  
ANISOU 3127  CB  LEU A 409    22205  17429  11724  -2245  -5575  -2520  A    C  
ATOM   3128  CG  LEU A 409      33.171  27.906 518.274  1.00128.80      A    C  
ANISOU 3128  CG  LEU A 409    22067  16458  10414  -1838  -5380  -2727  A    C  
ATOM   3129  CD1 LEU A 409      31.781  27.539 517.796  1.00124.39      A    C  
ANISOU 3129  CD1 LEU A 409    21418  15828  10016  -1277  -4802  -2701  A    C  
ATOM   3130  CD2 LEU A 409      33.524  27.139 519.538  1.00125.79      A    C  
ANISOU 3130  CD2 LEU A 409    21662  16419   9713  -1791  -5561  -2614  A    C  
ATOM   3131  N   LEU A 410      37.691  28.443 516.216  1.00144.99      A    N  
ANISOU 3131  N   LEU A 410    22681  19072  13337  -3746  -6737  -2159  A    N  
ATOM   3132  CA  LEU A 410      38.881  27.892 515.566  1.00134.13      A    C  
ANISOU 3132  CA  LEU A 410    20519  18137  12306  -4039  -6946  -1793  A    C  
ATOM   3133  C   LEU A 410      39.511  26.758 516.369  1.00128.43      A    C  
ANISOU 3133  C   LEU A 410    19379  17942  11475  -3962  -7088  -1520  A    C  
ATOM   3134  O   LEU A 410      40.707  26.781 516.655  1.00131.04      A    O  
ANISOU 3134  O   LEU A 410    19373  18601  11814  -4304  -7389  -1293  A    O  
ATOM   3135  CB  LEU A 410      39.917  28.999 515.350  1.00142.83      A    C  
ANISOU 3135  CB  LEU A 410    21595  19166  13507  -4575  -7209  -1740  A    C  
ATOM   3136  CG  LEU A 410      39.482  30.220 514.537  1.00142.28      A    C  
ANISOU 3136  CG  LEU A 410    21908  18582  13571  -4695  -7084  -1960  A    C  
ATOM   3137  CD1 LEU A 410      40.286  31.448 514.958  1.00146.80      A    C  
ANISOU 3137  CD1 LEU A 410    22793  18969  14014  -5180  -7373  -1983  A    C  
ATOM   3138  CD2 LEU A 410      39.634  29.959 513.047  1.00128.76      A    C  
ANISOU 3138  CD2 LEU A 410    19618  16974  12333  -4713  -6957  -1776  A    C  
ATOM   3139  N   ARG A 415      39.121  26.184 510.383  1.00117.36      A    N  
ANISOU 3139  N   ARG A 415    16174  16361  12056  -3430  -5940  -1048  A    N  
ATOM   3140  CA  ARG A 415      39.290  25.541 509.089  1.00117.48      A    C  
ANISOU 3140  CA  ARG A 415    15609  16523  12505  -3204  -5694   -814  A    C  
ATOM   3141  C   ARG A 415      37.951  25.065 508.478  1.00124.97      A    C  
ANISOU 3141  C   ARG A 415    16664  17164  13654  -2695  -5190   -958  A    C  
ATOM   3142  O   ARG A 415      37.717  25.242 507.275  1.00126.08      A    O  
ANISOU 3142  O   ARG A 415    16640  17151  14114  -2613  -4980   -951  A    O  
ATOM   3143  CB  ARG A 415      40.261  24.366 509.178  1.00119.47      A    C  
ANISOU 3143  CB  ARG A 415    15252  17327  12814  -3084  -5793   -420  A    C  
ATOM   3144  CG  ARG A 415      40.235  23.561 507.901  1.00116.79      A    C  
ANISOU 3144  CG  ARG A 415    14436  17075  12865  -2712  -5475   -212  A    C  
ATOM   3145  CD  ARG A 415      40.563  22.106 508.117  1.00117.43      A    C  
ANISOU 3145  CD  ARG A 415    14147  17524  12947  -2320  -5387     75  A    C  
ATOM   3146  NE  ARG A 415      40.427  21.378 506.861  1.00116.77      A    N  
ANISOU 3146  NE  ARG A 415    13738  17430  13200  -1935  -5074    231  A    N  
ATOM   3147  CZ  ARG A 415      40.445  20.055 506.753  1.00119.18      A    C  
ANISOU 3147  CZ  ARG A 415    13825  17904  13552  -1491  -4901    441  A    C  
ATOM   3148  NH1 ARG A 415      40.597  19.301 507.837  1.00117.83      A    N1+
ANISOU 3148  NH1 ARG A 415    13689  17950  13132  -1373  -4999    534  A    N1+
ATOM   3149  NH2 ARG A 415      40.302  19.491 505.557  1.00118.83      A    N  
ANISOU 3149  NH2 ARG A 415    13574  17788  13786  -1157  -4637    555  A    N  
ATOM   3150  N   PHE A 416      37.104  24.453 509.302  1.00125.66      A    N  
ANISOU 3150  N   PHE A 416    17003  17196  13547  -2375  -5013  -1056  A    N  
ATOM   3151  CA  PHE A 416      35.847  23.873 508.847  1.00110.47      A    C  
ANISOU 3151  CA  PHE A 416    15136  15057  11779  -1926  -4573  -1122  A    C  
ATOM   3152  C   PHE A 416      34.795  24.972 508.754  1.00109.62      A    C  
ANISOU 3152  C   PHE A 416    15549  14512  11591  -1923  -4402  -1444  A    C  
ATOM   3153  O   PHE A 416      34.834  25.954 509.497  1.00116.51      A    O  
ANISOU 3153  O   PHE A 416    16886  15227  12154  -2157  -4601  -1653  A    O  
ATOM   3154  CB  PHE A 416      35.351  22.773 509.804  1.00101.68      A    C  
ANISOU 3154  CB  PHE A 416    14068  14093  10474  -1607  -4463  -1048  A    C  
ATOM   3155  CG  PHE A 416      36.263  21.563 509.916  1.00103.76      A    C  
ANISOU 3155  CG  PHE A 416    13865  14765  10795  -1513  -4581   -722  A    C  
ATOM   3156  CD1 PHE A 416      37.420  21.595 510.685  1.00114.56      A    C  
ANISOU 3156  CD1 PHE A 416    15105  16470  11954  -1775  -4955   -592  A    C  
ATOM   3157  CD2 PHE A 416      35.913  20.364 509.302  1.00 95.34      A    C  
ANISOU 3157  CD2 PHE A 416    12531  13738   9955  -1145  -4321   -536  A    C  
ATOM   3158  CE1 PHE A 416      38.246  20.463 510.809  1.00111.57      A    C  
ANISOU 3158  CE1 PHE A 416    14295  16496  11600  -1628  -5039   -266  A    C  
ATOM   3159  CE2 PHE A 416      36.729  19.235 509.422  1.00 94.15      A    C  
ANISOU 3159  CE2 PHE A 416    12022  13932   9818   -997  -4412   -235  A    C  
ATOM   3160  CZ  PHE A 416      37.896  19.287 510.174  1.00103.78      A    C  
ANISOU 3160  CZ  PHE A 416    13080  15519  10833  -1214  -4755    -95  A    C  
ATOM   3161  N   ALA A 417      33.851  24.806 507.831  1.00 99.21      A    N  
ANISOU 3161  N   ALA A 417    14178  12990  10526  -1642  -4037  -1475  A    N  
ATOM   3162  CA  ALA A 417      32.870  25.852 507.593  1.00 99.34      A    C  
ANISOU 3162  CA  ALA A 417    14632  12623  10488  -1595  -3844  -1740  A    C  
ATOM   3163  C   ALA A 417      31.413  25.428 507.724  1.00108.86      A    C  
ANISOU 3163  C   ALA A 417    16003  13715  11646  -1171  -3453  -1786  A    C  
ATOM   3164  O   ALA A 417      30.574  26.294 508.004  1.00118.18      A    O  
ANISOU 3164  O   ALA A 417    17641  14643  12618  -1076  -3314  -2001  A    O  
ATOM   3165  CB  ALA A 417      33.078  26.451 506.198  1.00 92.64      A    C  
ANISOU 3165  CB  ALA A 417    13599  11610   9988  -1726  -3785  -1746  A    C  
ATOM   3166  N   GLY A 418      31.082  24.152 507.582  1.00102.27      A    N  
ANISOU 3166  N   GLY A 418    14840  13060  10957   -915  -3284  -1574  A    N  
ATOM   3167  CA  GLY A 418      29.698  23.695 507.646  1.00 91.83      A    C  
ANISOU 3167  CA  GLY A 418    13612  11672   9606   -568  -2936  -1551  A    C  
ATOM   3168  C   GLY A 418      29.417  22.775 508.814  1.00 88.98      A    C  
ANISOU 3168  C   GLY A 418    13288  11531   8988   -398  -2933  -1427  A    C  
ATOM   3169  O   GLY A 418      30.244  21.936 509.159  1.00 89.51      A    O  
ANISOU 3169  O   GLY A 418    13119  11829   9061   -459  -3126  -1264  A    O  
ATOM   3170  N   LEU A 419      28.256  22.966 509.438  1.00 91.13      A    N  
ANISOU 3170  N   LEU A 419    13859  11752   9015   -164  -2706  -1486  A    N  
ATOM   3171  CA  LEU A 419      27.841  22.143 510.565  1.00 97.93      A    C  
ANISOU 3171  CA  LEU A 419    14770  12828   9612     21  -2666  -1351  A    C  
ATOM   3172  C   LEU A 419      26.335  21.915 510.550  1.00101.56      A    C  
ANISOU 3172  C   LEU A 419    15282  13282  10025    332  -2297  -1251  A    C  
ATOM   3173  O   LEU A 419      25.560  22.864 510.407  1.00106.66      A    O  
ANISOU 3173  O   LEU A 419    16191  13772  10564    457  -2102  -1396  A    O  
ATOM   3174  CB  LEU A 419      28.246  22.772 511.902  1.00105.09      A    C  
ANISOU 3174  CB  LEU A 419    16079  13781  10069    -49  -2877  -1517  A    C  
ATOM   3175  CG  LEU A 419      27.662  22.058 513.126  1.00109.39      A    C  
ANISOU 3175  CG  LEU A 419    16728  14544  10289    191  -2790  -1389  A    C  
ATOM   3176  CD1 LEU A 419      28.117  20.599 513.183  1.00105.04      A    C  
ANISOU 3176  CD1 LEU A 419    15764  14241   9906    186  -2873  -1103  A    C  
ATOM   3177  CD2 LEU A 419      27.998  22.790 514.410  1.00119.14      A    C  
ANISOU 3177  CD2 LEU A 419    18435  15790  11044    148  -2990  -1584  A    C  
ATOM   3178  N   LEU A 420      25.937  20.648 510.664  1.00100.54      A    N  
ANISOU 3178  N   LEU A 420    14896  13332   9971    450  -2209   -977  A    N  
ATOM   3179  CA  LEU A 420      24.562  20.219 510.912  1.00102.16      A    C  
ANISOU 3179  CA  LEU A 420    15102  13637  10075    704  -1911   -789  A    C  
ATOM   3180  C   LEU A 420      24.536  19.338 512.154  1.00110.24      A    C  
ANISOU 3180  C   LEU A 420    16143  14917  10826    795  -1970   -609  A    C  
ATOM   3181  O   LEU A 420      25.185  18.288 512.181  1.00109.90      A    O  
ANISOU 3181  O   LEU A 420    15880  14968  10910    700  -2136   -448  A    O  
ATOM   3182  CB  LEU A 420      23.954  19.464 509.735  1.00 93.84      A    C  
ANISOU 3182  CB  LEU A 420    13724  12536   9394    711  -1753   -572  A    C  
ATOM   3183  CG  LEU A 420      22.582  18.839 510.054  1.00 92.47      A    C  
ANISOU 3183  CG  LEU A 420    13487  12535   9115    903  -1497   -289  A    C  
ATOM   3184  CD1 LEU A 420      21.616  19.779 510.786  1.00 94.04      A    C  
ANISOU 3184  CD1 LEU A 420    13956  12825   8952   1153  -1259   -351  A    C  
ATOM   3185  CD2 LEU A 420      21.940  18.313 508.795  1.00 95.98      A    C  
ANISOU 3185  CD2 LEU A 420    13668  12890   9911    856  -1371   -104  A    C  
ATOM   3186  N   ALA A 421      23.807  19.766 513.184  1.00112.92      A    N  
ANISOU 3186  N   ALA A 421    16762  15372  10772   1009  -1828   -629  A    N  
ATOM   3187  CA  ALA A 421      23.829  19.113 514.487  1.00110.71      A    C  
ANISOU 3187  CA  ALA A 421    16554  15341  10171   1109  -1890   -491  A    C  
ATOM   3188  C   ALA A 421      22.407  18.669 514.805  1.00110.84      A    C  
ANISOU 3188  C   ALA A 421    16507  15553  10053   1372  -1570   -205  A    C  
ATOM   3189  O   ALA A 421      21.503  19.503 514.920  1.00109.15      A    O  
ANISOU 3189  O   ALA A 421    16490  15348   9635   1602  -1321   -255  A    O  
ATOM   3190  CB  ALA A 421      24.360  20.058 515.565  1.00109.47      A    C  
ANISOU 3190  CB  ALA A 421    16830  15174   9590   1132  -2046   -764  A    C  
ATOM   3191  N   ILE A 422      22.228  17.358 514.956  1.00112.54      A    N  
ANISOU 3191  N   ILE A 422    16457  15938  10364   1342  -1583    120  A    N  
ATOM   3192  CA  ILE A 422      20.942  16.742 515.270  1.00111.12      A    C  
ANISOU 3192  CA  ILE A 422    16148  15994  10078   1515  -1327    479  A    C  
ATOM   3193  C   ILE A 422      20.950  16.364 516.752  1.00110.01      A    C  
ANISOU 3193  C   ILE A 422    16150  16122   9527   1666  -1358    592  A    C  
ATOM   3194  O   ILE A 422      21.718  15.471 517.141  1.00106.87      A    O  
ANISOU 3194  O   ILE A 422    15675  15771   9161   1537  -1582    674  A    O  
ATOM   3195  CB  ILE A 422      20.693  15.494 514.415  1.00106.30      A    C  
ANISOU 3195  CB  ILE A 422    15193  15357   9838   1334  -1350    794  A    C  
ATOM   3196  CG1 ILE A 422      21.085  15.751 512.970  1.00100.61      A    C  
ANISOU 3196  CG1 ILE A 422    14359  14340   9529   1158  -1409    635  A    C  
ATOM   3197  CG2 ILE A 422      19.235  15.066 514.501  1.00108.53      A    C  
ANISOU 3197  CG2 ILE A 422    15316  15872  10048   1445  -1084   1185  A    C  
ATOM   3198  CD1 ILE A 422      20.734  14.621 512.067  1.00104.37      A    C  
ANISOU 3198  CD1 ILE A 422    14582  14744  10327   1003  -1425    925  A    C  
ATOM   3199  N   PRO A 423      20.118  16.978 517.583  1.00113.79      A    N  
ANISOU 3199  N   PRO A 423    16837  16792   9606   1968  -1130    621  A    N  
ATOM   3200  CA  PRO A 423      20.070  16.561 518.984  1.00116.65      A    C  
ANISOU 3200  CA  PRO A 423    17325  17432   9566   2137  -1142    761  A    C  
ATOM   3201  C   PRO A 423      19.321  15.251 519.143  1.00119.28      A    C  
ANISOU 3201  C   PRO A 423    17326  18025   9969   2120  -1043   1252  A    C  
ATOM   3202  O   PRO A 423      18.298  15.009 518.497  1.00122.92      A    O  
ANISOU 3202  O   PRO A 423    17543  18568  10594   2125   -832   1533  A    O  
ATOM   3203  CB  PRO A 423      19.311  17.705 519.654  1.00120.68      A    C  
ANISOU 3203  CB  PRO A 423    18182  18049   9621   2521   -885    650  A    C  
ATOM   3204  CG  PRO A 423      18.382  18.170 518.577  1.00122.07      A    C  
ANISOU 3204  CG  PRO A 423    18204  18164  10011   2589   -620    724  A    C  
ATOM   3205  CD  PRO A 423      19.176  18.072 517.304  1.00116.62      A    C  
ANISOU 3205  CD  PRO A 423    17341  17140   9829   2219   -834    547  A    C  
ATOM   3206  N   LEU A 424      19.854  14.399 520.007  1.00118.54      A    N  
ANISOU 3206  N   LEU A 424    17231  18064   9746   2074  -1217   1373  A    N  
ATOM   3207  CA  LEU A 424      19.266  13.106 520.312  1.00121.44      A    C  
ANISOU 3207  CA  LEU A 424    17345  18660  10138   2031  -1171   1844  A    C  
ATOM   3208  C   LEU A 424      19.010  13.054 521.811  1.00126.49      A    C  
ANISOU 3208  C   LEU A 424    18145  19634  10281   2299  -1091   1974  A    C  
ATOM   3209  O   LEU A 424      19.852  13.487 522.604  1.00129.63      A    O  
ANISOU 3209  O   LEU A 424    18825  20013  10415   2380  -1249   1689  A    O  
ATOM   3210  CB  LEU A 424      20.165  11.958 519.841  1.00116.86      A    C  
ANISOU 3210  CB  LEU A 424    16615  17896   9892   1731  -1459   1913  A    C  
ATOM   3211  CG  LEU A 424      20.498  12.022 518.343  1.00108.71      A    C  
ANISOU 3211  CG  LEU A 424    15457  16526   9322   1505  -1540   1770  A    C  
ATOM   3212  CD1 LEU A 424      21.629  11.064 517.975  1.00103.36      A    C  
ANISOU 3212  CD1 LEU A 424    14719  15661   8890   1306  -1833   1764  A    C  
ATOM   3213  CD2 LEU A 424      19.261  11.772 517.484  1.00103.77      A    C  
ANISOU 3213  CD2 LEU A 424    14613  15913   8904   1439  -1333   2068  A    C  
ATOM   3214  N   LYS A 425      17.850  12.543 522.209  1.00125.61      A    N  
ANISOU 3214  N   LYS A 425    17854  19848  10023   2431   -855   2421  A    N  
ATOM   3215  CA  LYS A 425      17.465  12.588 523.612  1.00131.88      A    C  
ANISOU 3215  CA  LYS A 425    18795  21005  10311   2750   -721   2575  A    C  
ATOM   3216  C   LYS A 425      16.983  11.225 524.079  1.00124.93      A    C  
ANISOU 3216  C   LYS A 425    17644  20394   9429   2651   -717   3108  A    C  
ATOM   3217  O   LYS A 425      16.092  10.631 523.466  1.00123.80      A    O  
ANISOU 3217  O   LYS A 425    17190  20347   9504   2501   -602   3508  A    O  
ATOM   3218  CB  LYS A 425      16.384  13.649 523.845  1.00143.18      A    C  
ANISOU 3218  CB  LYS A 425    20334  22660  11409   3152   -355   2608  A    C  
ATOM   3219  CG  LYS A 425      16.822  15.066 523.462  1.00146.12      A    C  
ANISOU 3219  CG  LYS A 425    21065  22731  11722   3275   -357   2077  A    C  
ATOM   3220  CD  LYS A 425      15.911  16.129 524.073  1.00149.90      A    C  
ANISOU 3220  CD  LYS A 425    21814  23437  11705   3794     -8   2073  A    C  
ATOM   3221  CE  LYS A 425      16.409  17.541 523.774  1.00144.88      A    C  
ANISOU 3221  CE  LYS A 425    21642  22441  10964   3908    -48   1527  A    C  
ATOM   3222  NZ  LYS A 425      15.632  18.575 524.518  1.00147.62      A    N1+
ANISOU 3222  NZ  LYS A 425    22384  22968  10736   4482    273   1489  A    N1+
ATOM   3223  N   SER A 426      17.573  10.739 525.164  1.00128.95      A    N  
ANISOU 3223  N   SER A 426    18287  21025   9683   2712   -859   3126  A    N  
ATOM   3224  CA  SER A 426      17.116   9.518 525.813  1.00134.25      A    C  
ANISOU 3224  CA  SER A 426    18763  21978  10270   2663   -845   3636  A    C  
ATOM   3225  C   SER A 426      17.564   9.576 527.271  1.00130.74      A    C  
ANISOU 3225  C   SER A 426    18567  21758   9349   2928   -885   3567  A    C  
ATOM   3226  O   SER A 426      17.786  10.662 527.818  1.00128.10      A    O  
ANISOU 3226  O   SER A 426    18547  21447   8677   3214   -827   3219  A    O  
ATOM   3227  CB  SER A 426      17.646   8.278 525.074  1.00137.04      A    C  
ANISOU 3227  CB  SER A 426    18947  22060  11060   2251  -1114   3782  A    C  
ATOM   3228  OG  SER A 426      19.022   8.063 525.348  1.00139.33      A    O  
ANISOU 3228  OG  SER A 426    19423  22148  11369   2187  -1411   3473  A    O  
ATOM   3229  N   ASP A 427      17.711   8.413 527.891  1.00131.99      A    N  
ANISOU 3229  N   ASP A 427    18626  22057   9467   2829  -1000   3892  A    N  
ATOM   3230  CA  ASP A 427      18.154   8.336 529.275  1.00135.15      A    C  
ANISOU 3230  CA  ASP A 427    19241  22684   9426   3063  -1056   3863  A    C  
ATOM   3231  C   ASP A 427      19.675   8.442 529.387  1.00127.53      A    C  
ANISOU 3231  C   ASP A 427    18504  21446   8505   2949  -1406   3413  A    C  
ATOM   3232  O   ASP A 427      20.369   8.708 528.404  1.00122.62      A    O  
ANISOU 3232  O   ASP A 427    17880  20480   8230   2728  -1577   3108  A    O  
ATOM   3233  CB  ASP A 427      17.668   7.032 529.912  1.00146.32      A    C  
ANISOU 3233  CB  ASP A 427    20447  24379  10768   3004  -1031   4432  A    C  
ATOM   3234  CG  ASP A 427      16.191   6.767 529.649  1.00154.04      A    C  
ANISOU 3234  CG  ASP A 427    21110  25645  11774   3002   -737   4969  A    C  
ATOM   3235  OD1 ASP A 427      15.519   7.643 529.056  1.00151.35      A    O  
ANISOU 3235  OD1 ASP A 427    20713  25329  11465   3114   -520   4896  A    O  
ATOM   3236  OD2 ASP A 427      15.704   5.682 530.045  1.00160.26      A    O1-
ANISOU 3236  OD2 ASP A 427    21702  26650  12539   2881   -729   5490  A    O1-
ATOM   3237  N   SER A 432      24.125  11.900 522.722  1.00110.66      A    N  
ANISOU 3237  N   SER A 432    16378  17258   8410   1731  -2323   1284  A    N  
ATOM   3238  CA  SER A 432      22.962  12.770 522.652  1.00112.62      A    C  
ANISOU 3238  CA  SER A 432    16736  17528   8526   1904  -2025   1250  A    C  
ATOM   3239  C   SER A 432      23.121  13.793 521.525  1.00116.81      A    C  
ANISOU 3239  C   SER A 432    17303  17770   9310   1794  -2017    938  A    C  
ATOM   3240  O   SER A 432      22.533  14.874 521.569  1.00123.92      A    O  
ANISOU 3240  O   SER A 432    18417  18640  10025   1955  -1839    766  A    O  
ATOM   3241  CB  SER A 432      22.726  13.466 524.005  1.00116.78      A    C  
ANISOU 3241  CB  SER A 432    17601  18270   8500   2176  -1955   1147  A    C  
ATOM   3242  OG  SER A 432      23.918  14.005 524.555  1.00113.19      A    O  
ANISOU 3242  OG  SER A 432    17399  17756   7850   2096  -2253    819  A    O  
ATOM   3243  N   TYR A 433      23.907  13.435 520.508  1.00113.77      A    N  
ANISOU 3243  N   TYR A 433    16723  17175   9330   1551  -2197    883  A    N  
ATOM   3244  CA  TYR A 433      24.145  14.310 519.365  1.00111.03      A    C  
ANISOU 3244  CA  TYR A 433    16370  16558   9257   1423  -2206    616  A    C  
ATOM   3245  C   TYR A 433      24.612  13.494 518.162  1.00105.34      A    C  
ANISOU 3245  C   TYR A 433    15356  15665   9004   1227  -2308    726  A    C  
ATOM   3246  O   TYR A 433      25.226  12.433 518.311  1.00106.36      A    O  
ANISOU 3246  O   TYR A 433    15361  15849   9202   1173  -2469    901  A    O  
ATOM   3247  CB  TYR A 433      25.187  15.388 519.691  1.00107.28      A    C  
ANISOU 3247  CB  TYR A 433    16153  16000   8610   1336  -2437    232  A    C  
ATOM   3248  CG  TYR A 433      24.619  16.706 520.169  1.00109.00      A    C  
ANISOU 3248  CG  TYR A 433    16757  16176   8482   1506  -2298    -12  A    C  
ATOM   3249  CD1 TYR A 433      23.949  17.554 519.297  1.00109.40      A    C  
ANISOU 3249  CD1 TYR A 433    16863  16033   8670   1554  -2091   -135  A    C  
ATOM   3250  CD2 TYR A 433      24.777  17.113 521.485  1.00116.85      A    C  
ANISOU 3250  CD2 TYR A 433    18103  17308   8986   1642  -2379   -123  A    C  
ATOM   3251  CE1 TYR A 433      23.434  18.765 519.731  1.00115.14      A    C  
ANISOU 3251  CE1 TYR A 433    18005  16697   9045   1764  -1952   -355  A    C  
ATOM   3252  CE2 TYR A 433      24.269  18.319 521.928  1.00121.23      A    C  
ANISOU 3252  CE2 TYR A 433    19101  17785   9174   1845  -2253   -356  A    C  
ATOM   3253  CZ  TYR A 433      23.601  19.141 521.049  1.00120.67      A    C  
ANISOU 3253  CZ  TYR A 433    19098  17511   9239   1918  -2035   -469  A    C  
ATOM   3254  OH  TYR A 433      23.100  20.341 521.497  1.00123.22      A    O  
ANISOU 3254  OH  TYR A 433    19921  17737   9162   2171  -1900   -696  A    O  
ATOM   3255  N   LEU A 434      24.313  14.005 516.967  1.00 99.96      A    N  
ANISOU 3255  N   LEU A 434    14597  14768   8617   1154  -2204    623  A    N  
ATOM   3256  CA  LEU A 434      24.930  13.534 515.727  1.00101.35      A    C  
ANISOU 3256  CA  LEU A 434    14563  14738   9209    987  -2318    634  A    C  
ATOM   3257  C   LEU A 434      25.281  14.753 514.890  1.00104.22      A    C  
ANISOU 3257  C   LEU A 434    14971  14902   9727    896  -2329    315  A    C  
ATOM   3258  O   LEU A 434      24.402  15.558 514.566  1.00106.26      A    O  
ANISOU 3258  O   LEU A 434    15314  15085   9976    964  -2116    228  A    O  
ATOM   3259  CB  LEU A 434      24.014  12.593 514.935  1.00 98.68      A    C  
ANISOU 3259  CB  LEU A 434    14051  14319   9122    968  -2170    938  A    C  
ATOM   3260  CG  LEU A 434      24.552  12.126 513.572  1.00 90.16      A    C  
ANISOU 3260  CG  LEU A 434    12822  12989   8445    840  -2268    941  A    C  
ATOM   3261  CD1 LEU A 434      25.802  11.268 513.720  1.00 90.94      A    C  
ANISOU 3261  CD1 LEU A 434    12877  13101   8573    828  -2517    996  A    C  
ATOM   3262  CD2 LEU A 434      23.488  11.379 512.793  1.00 88.93      A    C  
ANISOU 3262  CD2 LEU A 434    12575  12722   8491    791  -2130   1216  A    C  
ATOM   3263  N   LEU A 435      26.556  14.880 514.533  1.00104.02      A    N  
ANISOU 3263  N   LEU A 435    14876  14813   9834    753  -2572    172  A    N  
ATOM   3264  CA  LEU A 435      27.074  16.076 513.889  1.00104.63      A    C  
ANISOU 3264  CA  LEU A 435    15007  14728  10018    622  -2638   -121  A    C  
ATOM   3265  C   LEU A 435      27.598  15.751 512.496  1.00103.24      A    C  
ANISOU 3265  C   LEU A 435    14572  14394  10260    520  -2682    -84  A    C  
ATOM   3266  O   LEU A 435      28.131  14.664 512.251  1.00102.02      A    O  
ANISOU 3266  O   LEU A 435    14235  14286  10242    536  -2781    114  A    O  
ATOM   3267  CB  LEU A 435      28.189  16.712 514.737  1.00103.59      A    C  
ANISOU 3267  CB  LEU A 435    15025  14704   9631    498  -2919   -313  A    C  
ATOM   3268  CG  LEU A 435      27.956  16.760 516.252  1.00104.71      A    C  
ANISOU 3268  CG  LEU A 435    15431  15038   9317    611  -2948   -318  A    C  
ATOM   3269  CD1 LEU A 435      29.115  17.436 516.966  1.00108.39      A    C  
ANISOU 3269  CD1 LEU A 435    16062  15581   9541    427  -3276   -515  A    C  
ATOM   3270  CD2 LEU A 435      26.639  17.441 516.604  1.00106.13      A    C  
ANISOU 3270  CD2 LEU A 435    15886  15167   9271    812  -2661   -389  A    C  
ATOM   3271  N   LEU A 436      27.434  16.709 511.583  1.00 98.25      A    N  
ANISOU 3271  N   LEU A 436    13957  13567   9806    448  -2599   -270  A    N  
ATOM   3272  CA  LEU A 436      27.931  16.609 510.217  1.00 89.40      A    C  
ANISOU 3272  CA  LEU A 436    12615  12293   9062    365  -2627   -266  A    C  
ATOM   3273  C   LEU A 436      28.795  17.829 509.930  1.00 87.12      A    C  
ANISOU 3273  C   LEU A 436    12364  11938   8799    181  -2778   -518  A    C  
ATOM   3274  O   LEU A 436      28.378  18.958 510.201  1.00 87.07      A    O  
ANISOU 3274  O   LEU A 436    12610  11836   8636    145  -2718   -733  A    O  
ATOM   3275  CB  LEU A 436      26.781  16.522 509.211  1.00 92.16      A    C  
ANISOU 3275  CB  LEU A 436    12917  12459   9641    435  -2368   -200  A    C  
ATOM   3276  CG  LEU A 436      25.747  15.400 509.344  1.00 92.98      A    C  
ANISOU 3276  CG  LEU A 436    12988  12603   9738    547  -2223     83  A    C  
ATOM   3277  CD1 LEU A 436      24.686  15.725 510.380  1.00 95.82      A    C  
ANISOU 3277  CD1 LEU A 436    13513  13108   9786    655  -2055    118  A    C  
ATOM   3278  CD2 LEU A 436      25.097  15.132 507.997  1.00 87.23      A    C  
ANISOU 3278  CD2 LEU A 436    12141  11675   9326    532  -2084    174  A    C  
ATOM   3279  N   PHE A 437      29.991  17.601 509.389  1.00 87.84      A    N  
ANISOU 3279  N   PHE A 437    12223  12087   9066     74  -2975   -469  A    N  
ATOM   3280  CA  PHE A 437      30.969  18.654 509.144  1.00 90.62      A    C  
ANISOU 3280  CA  PHE A 437    12553  12434   9443   -160  -3172   -637  A    C  
ATOM   3281  C   PHE A 437      31.270  18.765 507.656  1.00 92.40      A    C  
ANISOU 3281  C   PHE A 437    12539  12528  10042   -192  -3117   -614  A    C  
ATOM   3282  O   PHE A 437      31.452  17.753 506.972  1.00 89.71      A    O  
ANISOU 3282  O   PHE A 437    11971  12212   9903    -48  -3071   -415  A    O  
ATOM   3283  CB  PHE A 437      32.267  18.385 509.899  1.00 94.05      A    C  
ANISOU 3283  CB  PHE A 437    12865  13155   9715   -282  -3487   -545  A    C  
ATOM   3284  CG  PHE A 437      32.080  18.169 511.366  1.00102.50      A    C  
ANISOU 3284  CG  PHE A 437    14155  14380  10409   -238  -3564   -547  A    C  
ATOM   3285  CD1 PHE A 437      31.382  19.087 512.135  1.00108.17      A    C  
ANISOU 3285  CD1 PHE A 437    15263  14989  10846   -267  -3515   -768  A    C  
ATOM   3286  CD2 PHE A 437      32.595  17.040 511.982  1.00109.00      A    C  
ANISOU 3286  CD2 PHE A 437    14825  15456  11135   -131  -3673   -320  A    C  
ATOM   3287  CE1 PHE A 437      31.212  18.890 513.501  1.00109.01      A    C  
ANISOU 3287  CE1 PHE A 437    15593  15250  10577   -195  -3579   -765  A    C  
ATOM   3288  CE2 PHE A 437      32.422  16.834 513.344  1.00112.46      A    C  
ANISOU 3288  CE2 PHE A 437    15464  16048  11219    -83  -3741   -313  A    C  
ATOM   3289  CZ  PHE A 437      31.731  17.762 514.104  1.00109.65      A    C  
ANISOU 3289  CZ  PHE A 437    15487  15594  10583   -118  -3694   -536  A    C  
ATOM   3290  N   ARG A 438      31.347  19.999 507.163  1.00 98.97      A    N  
ANISOU 3290  N   ARG A 438    13458  13204  10940   -369  -3128   -816  A    N  
ATOM   3291  CA  ARG A 438      31.588  20.268 505.752  1.00 97.02      A    C  
ANISOU 3291  CA  ARG A 438    13003  12827  11032   -407  -3064   -811  A    C  
ATOM   3292  C   ARG A 438      32.720  21.278 505.627  1.00105.08      A    C  
ANISOU 3292  C   ARG A 438    13962  13908  12055   -714  -3317   -894  A    C  
ATOM   3293  O   ARG A 438      32.728  22.300 506.321  1.00107.10      A    O  
ANISOU 3293  O   ARG A 438    14514  14095  12085   -917  -3440  -1089  A    O  
ATOM   3294  CB  ARG A 438      30.314  20.777 505.071  1.00 91.81      A    C  
ANISOU 3294  CB  ARG A 438    12507  11884  10493   -310  -2773   -941  A    C  
ATOM   3295  CG  ARG A 438      29.950  20.065 503.773  1.00 93.01      A    C  
ANISOU 3295  CG  ARG A 438    12438  11928  10972   -153  -2594   -804  A    C  
ATOM   3296  CD  ARG A 438      28.447  20.154 503.517  1.00 95.57      A    C  
ANISOU 3296  CD  ARG A 438    12921  12070  11320    -16  -2308   -844  A    C  
ATOM   3297  NE  ARG A 438      28.079  19.876 502.129  1.00 97.71      A    N  
ANISOU 3297  NE  ARG A 438    13038  12184  11905     61  -2158   -776  A    N  
ATOM   3298  CZ  ARG A 438      26.824  19.831 501.688  1.00 94.43      A    C  
ANISOU 3298  CZ  ARG A 438    12684  11641  11555    161  -1927   -752  A    C  
ATOM   3299  NH1 ARG A 438      25.822  20.038 502.531  1.00 85.52      A    N1+
ANISOU 3299  NH1 ARG A 438    11739  10555  10200    227  -1797   -766  A    N1+
ATOM   3300  NH2 ARG A 438      26.569  19.577 500.408  1.00 90.27      A    N  
ANISOU 3300  NH2 ARG A 438    12028  10969  11301    207  -1827   -691  A    N  
ATOM   3301  N   VAL A 439      33.676  20.981 504.748  1.00106.79      A    N  
ANISOU 3301  N   VAL A 439    13814  14258  12503   -744  -3404   -724  A    N  
ATOM   3302  CA  VAL A 439      34.884  21.784 504.588  1.00104.33      A    C  
ANISOU 3302  CA  VAL A 439    13339  14094  12208  -1061  -3673   -703  A    C  
ATOM   3303  C   VAL A 439      34.569  23.038 503.779  1.00105.99      A    C  
ANISOU 3303  C   VAL A 439    13690  14017  12563  -1241  -3602   -901  A    C  
ATOM   3304  O   VAL A 439      33.735  23.026 502.867  1.00110.00      A    O  
ANISOU 3304  O   VAL A 439    14220  14292  13281  -1059  -3328   -960  A    O  
ATOM   3305  CB  VAL A 439      35.985  20.927 503.927  1.00105.56      A    C  
ANISOU 3305  CB  VAL A 439    13015  14555  12536   -952  -3750   -389  A    C  
ATOM   3306  CG1 VAL A 439      37.119  21.784 503.393  1.00119.37      A    C  
ANISOU 3306  CG1 VAL A 439    14504  16470  14383  -1265  -3968   -306  A    C  
ATOM   3307  CG2 VAL A 439      36.524  19.898 504.918  1.00101.63      A    C  
ANISOU 3307  CG2 VAL A 439    12411  14377  11827   -831  -3893   -192  A    C  
ATOM   3308  N   SER A 481      30.835  27.200 503.788  1.00105.42      A    N  
ANISOU 3308  N   SER A 481    15298  12633  12125  -1254  -3009  -1929  A    N  
ATOM   3309  CA  SER A 481      30.724  25.837 503.306  1.00100.10      A    C  
ANISOU 3309  CA  SER A 481    14180  12166  11689  -1027  -2868  -1692  A    C  
ATOM   3310  C   SER A 481      29.667  25.748 502.214  1.00 95.69      A    C  
ANISOU 3310  C   SER A 481    13546  11433  11378   -782  -2523  -1687  A    C  
ATOM   3311  O   SER A 481      28.878  26.671 501.993  1.00 98.69      A    O  
ANISOU 3311  O   SER A 481    14214  11573  11711   -725  -2351  -1858  A    O  
ATOM   3312  CB  SER A 481      30.369  24.887 504.444  1.00 98.65      A    C  
ANISOU 3312  CB  SER A 481    14046  12172  11267   -844  -2855  -1607  A    C  
ATOM   3313  OG  SER A 481      29.848  23.672 503.946  1.00 93.55      A    O  
ANISOU 3313  OG  SER A 481    13115  11613  10818   -587  -2655  -1410  A    O  
ATOM   3314  N   GLN A 482      29.679  24.625 501.513  1.00 95.48      A    N  
ANISOU 3314  N   GLN A 482    13151  11526  11600   -631  -2433  -1480  A    N  
ATOM   3315  CA  GLN A 482      28.583  24.300 500.622  1.00 93.29      A    C  
ANISOU 3315  CA  GLN A 482    12810  11119  11517   -401  -2132  -1437  A    C  
ATOM   3316  C   GLN A 482      27.281  24.334 501.415  1.00 94.23      A    C  
ANISOU 3316  C   GLN A 482    13207  11204  11393   -211  -1930  -1487  A    C  
ATOM   3317  O   GLN A 482      27.200  23.703 502.480  1.00 92.42      A    O  
ANISOU 3317  O   GLN A 482    13038  11138  10940   -151  -1988  -1415  A    O  
ATOM   3318  CB  GLN A 482      28.796  22.916 500.013  1.00 92.41      A    C  
ANISOU 3318  CB  GLN A 482    12363  11131  11616   -266  -2118  -1197  A    C  
ATOM   3319  CG  GLN A 482      27.954  22.654 498.796  1.00 91.30      A    C  
ANISOU 3319  CG  GLN A 482    12127  10835  11727   -113  -1882  -1143  A    C  
ATOM   3320  CD  GLN A 482      28.397  23.493 497.631  1.00 82.78      A    C  
ANISOU 3320  CD  GLN A 482    10946   9623  10882   -206  -1866  -1223  A    C  
ATOM   3321  NE2 GLN A 482      29.680  23.834 497.611  1.00 78.71      A    N  
ANISOU 3321  NE2 GLN A 482    10299   9213  10395   -387  -2085  -1215  A    N  
ATOM   3322  OE1 GLN A 482      27.604  23.832 496.754  1.00 78.88      A    O  
ANISOU 3322  OE1 GLN A 482    10472   8960  10537   -125  -1664  -1266  A    O  
ATOM   3323  N   PRO A 483      26.260  25.061 500.960  1.00100.85      A    N  
ANISOU 3323  N   PRO A 483    14206  11867  12245    -92  -1685  -1584  A    N  
ATOM   3324  CA  PRO A 483      25.034  25.141 501.755  1.00102.54      A    C  
ANISOU 3324  CA  PRO A 483    14658  12115  12188    130  -1475  -1586  A    C  
ATOM   3325  C   PRO A 483      24.339  23.792 501.803  1.00 99.62      A    C  
ANISOU 3325  C   PRO A 483    14055  11923  11873    277  -1366  -1323  A    C  
ATOM   3326  O   PRO A 483      24.437  22.973 500.882  1.00 93.08      A    O  
ANISOU 3326  O   PRO A 483    12945  11091  11328    257  -1369  -1173  A    O  
ATOM   3327  CB  PRO A 483      24.189  26.193 501.019  1.00 92.38      A    C  
ANISOU 3327  CB  PRO A 483    13528  10625  10947    244  -1229  -1704  A    C  
ATOM   3328  CG  PRO A 483      24.975  26.565 499.770  1.00 93.63      A    C  
ANISOU 3328  CG  PRO A 483    13507  10628  11440     57  -1319  -1761  A    C  
ATOM   3329  CD  PRO A 483      26.029  25.524 499.584  1.00 97.96      A    C  
ANISOU 3329  CD  PRO A 483    13725  11326  12171    -85  -1542  -1613  A    C  
ATOM   3330  N   TRP A 484      23.600  23.584 502.886  1.00 93.19      A    N  
ANISOU 3330  N   TRP A 484    13395  11254  10760    428  -1273  -1258  A    N  
ATOM   3331  CA  TRP A 484      22.908  22.323 503.107  1.00 90.40      A    C  
ANISOU 3331  CA  TRP A 484    12854  11084  10410    527  -1195   -978  A    C  
ATOM   3332  C   TRP A 484      21.631  22.328 502.281  1.00 95.13      A    C  
ANISOU 3332  C   TRP A 484    13342  11666  11136    654   -923   -841  A    C  
ATOM   3333  O   TRP A 484      20.625  22.920 502.678  1.00 92.53      A    O  
ANISOU 3333  O   TRP A 484    13154  11411  10592    843   -698   -827  A    O  
ATOM   3334  CB  TRP A 484      22.608  22.120 504.589  1.00 91.60      A    C  
ANISOU 3334  CB  TRP A 484    13186  11436  10183    638  -1196   -926  A    C  
ATOM   3335  CG  TRP A 484      23.814  22.081 505.496  1.00 99.15      A    C  
ANISOU 3335  CG  TRP A 484    14254  12443  10976    506  -1480  -1039  A    C  
ATOM   3336  CD1 TRP A 484      24.343  23.126 506.201  1.00105.77      A    C  
ANISOU 3336  CD1 TRP A 484    15414  13214  11560    453  -1597  -1286  A    C  
ATOM   3337  CD2 TRP A 484      24.652  20.947 505.779  1.00 99.01      A    C  
ANISOU 3337  CD2 TRP A 484    14046  12554  11020    404  -1699   -895  A    C  
ATOM   3338  CE2 TRP A 484      25.656  21.380 506.671  1.00 95.48      A    C  
ANISOU 3338  CE2 TRP A 484    13765  12159  10355    288  -1937  -1049  A    C  
ATOM   3339  CE3 TRP A 484      24.649  19.609 505.367  1.00 92.55      A    C  
ANISOU 3339  CE3 TRP A 484    12972  11797  10396    406  -1727   -645  A    C  
ATOM   3340  NE1 TRP A 484      25.443  22.711 506.917  1.00101.29      A    N  
ANISOU 3340  NE1 TRP A 484    14828  12759  10897    296  -1886  -1291  A    N  
ATOM   3341  CZ2 TRP A 484      26.644  20.527 507.153  1.00 93.73      A    C  
ANISOU 3341  CZ2 TRP A 484    13401  12097  10114    197  -2179   -941  A    C  
ATOM   3342  CZ3 TRP A 484      25.634  18.763 505.850  1.00 89.26      A    C  
ANISOU 3342  CZ3 TRP A 484    12468  11499   9948    347  -1956   -555  A    C  
ATOM   3343  CH2 TRP A 484      26.616  19.226 506.732  1.00 91.63      A    C  
ANISOU 3343  CH2 TRP A 484    12878  11898  10040    254  -2168   -694  A    C  
ATOM   3344  N   ARG A 485      21.669  21.673 501.120  1.00 95.40      A    N  
ANISOU 3344  N   ARG A 485    13132  11617  11498    570   -942   -723  A    N  
ATOM   3345  CA  ARG A 485      20.451  21.478 500.349  1.00 92.64      A    C  
ANISOU 3345  CA  ARG A 485    12648  11284  11266    643   -731   -539  A    C  
ATOM   3346  C   ARG A 485      19.462  20.647 501.164  1.00 97.98      A    C  
ANISOU 3346  C   ARG A 485    13274  12210  11744    716   -648   -246  A    C  
ATOM   3347  O   ARG A 485      19.844  19.870 502.042  1.00 94.06      A    O  
ANISOU 3347  O   ARG A 485    12798  11823  11116    678   -791   -157  A    O  
ATOM   3348  CB  ARG A 485      20.768  20.821 498.998  1.00 92.67      A    C  
ANISOU 3348  CB  ARG A 485    12454  11131  11625    525   -816   -469  A    C  
ATOM   3349  CG  ARG A 485      21.671  21.685 498.100  1.00100.63      A    C  
ANISOU 3349  CG  ARG A 485    13468  11933  12837    469   -866   -714  A    C  
ATOM   3350  CD  ARG A 485      22.503  20.884 497.072  1.00104.85      A    C  
ANISOU 3350  CD  ARG A 485    13840  12347  13652    385  -1024   -660  A    C  
ATOM   3351  NE  ARG A 485      23.730  21.602 496.688  1.00111.00      A    N  
ANISOU 3351  NE  ARG A 485    14603  13032  14541    316  -1138   -857  A    N  
ATOM   3352  CZ  ARG A 485      24.476  21.327 495.614  1.00108.23      A    C  
ANISOU 3352  CZ  ARG A 485    14108  12583  14433    296  -1216   -843  A    C  
ATOM   3353  NH1 ARG A 485      24.130  20.348 494.785  1.00114.26      A    N1+
ANISOU 3353  NH1 ARG A 485    14793  13276  15345    353  -1202   -677  A    N1+
ATOM   3354  NH2 ARG A 485      25.570  22.037 495.360  1.00 92.88      A    N  
ANISOU 3354  NH2 ARG A 485    12114  10614  12563    216  -1319   -976  A    N  
ATOM   3355  N   THR A 486      18.172  20.838 500.877  1.00108.64      A    N  
ANISOU 3355  N   THR A 486    14538  13678  13061    821   -413    -67  A    N  
ATOM   3356  CA  THR A 486      17.113  20.360 501.765  1.00108.90      A    C  
ANISOU 3356  CA  THR A 486    14516  14019  12842    922   -284    235  A    C  
ATOM   3357  C   THR A 486      16.992  18.836 501.748  1.00107.89      A    C  
ANISOU 3357  C   THR A 486    14222  13959  12814    728   -449    547  A    C  
ATOM   3358  O   THR A 486      16.701  18.222 502.782  1.00110.09      A    O  
ANISOU 3358  O   THR A 486    14502  14456  12872    749   -465    750  A    O  
ATOM   3359  CB  THR A 486      15.780  21.017 501.401  1.00103.43      A    C  
ANISOU 3359  CB  THR A 486    13731  13489  12080   1099     18    390  A    C  
ATOM   3360  CG2 THR A 486      14.763  20.729 502.464  1.00 96.92      A    C  
ANISOU 3360  CG2 THR A 486    12849  13045  10931   1259    178    706  A    C  
ATOM   3361  OG1 THR A 486      15.950  22.437 501.340  1.00107.84      A    O  
ANISOU 3361  OG1 THR A 486    14514  13917  12542   1295    161     81  A    O  
ATOM   3362  N   ALA A 487      17.190  18.209 500.582  1.00 97.31      A    N  
ANISOU 3362  N   ALA A 487    12776  12418  11780    547   -575    598  A    N  
ATOM   3363  CA  ALA A 487      17.069  16.756 500.497  1.00 91.65      A    C  
ANISOU 3363  CA  ALA A 487    11994  11693  11135    358   -755    888  A    C  
ATOM   3364  C   ALA A 487      18.065  16.037 501.393  1.00 92.45      A    C  
ANISOU 3364  C   ALA A 487    12219  11777  11132    338   -960    845  A    C  
ATOM   3365  O   ALA A 487      17.773  14.933 501.861  1.00106.29      A    O  
ANISOU 3365  O   ALA A 487    13967  13613  12807    238  -1063   1124  A    O  
ATOM   3366  CB  ALA A 487      17.256  16.295 499.052  1.00 92.65      A    C  
ANISOU 3366  CB  ALA A 487    12085  11543  11574    209   -871    890  A    C  
ATOM   3367  N   GLN A 488      19.253  16.604 501.613  1.00 90.83      A    N  
ANISOU 3367  N   GLN A 488    12118  11469  10924    410  -1040    530  A    N  
ATOM   3368  CA  GLN A 488      20.210  15.926 502.487  1.00 93.02      A    C  
ANISOU 3368  CA  GLN A 488    12482  11777  11084    402  -1238    517  A    C  
ATOM   3369  C   GLN A 488      19.848  16.083 503.968  1.00 95.65      A    C  
ANISOU 3369  C   GLN A 488    12885  12382  11075    501  -1168    580  A    C  
ATOM   3370  O   GLN A 488      20.013  15.135 504.744  1.00 98.40      A    O  
ANISOU 3370  O   GLN A 488    13260  12830  11296    472  -1288    753  A    O  
ATOM   3371  CB  GLN A 488      21.633  16.399 502.201  1.00 99.06      A    C  
ANISOU 3371  CB  GLN A 488    13287  12395  11955    412  -1378    223  A    C  
ATOM   3372  CG  GLN A 488      22.034  16.256 500.747  1.00 97.62      A    C  
ANISOU 3372  CG  GLN A 488    13033  11972  12085    364  -1427    175  A    C  
ATOM   3373  CD  GLN A 488      21.998  17.576 500.025  1.00104.22      A    C  
ANISOU 3373  CD  GLN A 488    13840  12719  13041    384  -1293    -57  A    C  
ATOM   3374  NE2 GLN A 488      21.510  17.563 498.781  1.00105.76      A    N  
ANISOU 3374  NE2 GLN A 488    13959  12763  13461    359  -1216    -13  A    N  
ATOM   3375  OE1 GLN A 488      22.403  18.608 500.579  1.00 99.39      A    O  
ANISOU 3375  OE1 GLN A 488    13304  12155  12305    413  -1272   -272  A    O  
ATOM   3376  N   LEU A 489      19.336  17.254 504.373  1.00 95.14      A    N  
ANISOU 3376  N   LEU A 489    12882  12432  10834    645   -969    452  A    N  
ATOM   3377  CA  LEU A 489      18.947  17.476 505.769  1.00 99.49      A    C  
ANISOU 3377  CA  LEU A 489    13544  13243  11015    798   -877    507  A    C  
ATOM   3378  C   LEU A 489      17.969  16.416 506.253  1.00106.08      A    C  
ANISOU 3378  C   LEU A 489    14247  14318  11742    773   -826    927  A    C  
ATOM   3379  O   LEU A 489      18.120  15.865 507.352  1.00102.18      A    O  
ANISOU 3379  O   LEU A 489    13809  13989  11025    805   -896   1039  A    O  
ATOM   3380  CB  LEU A 489      18.354  18.874 505.983  1.00107.99      A    C  
ANISOU 3380  CB  LEU A 489    14757  14382  11892   1016   -632    344  A    C  
ATOM   3381  CG  LEU A 489      19.014  20.196 505.596  1.00110.58      A    C  
ANISOU 3381  CG  LEU A 489    15281  14480  12253   1055   -632    -50  A    C  
ATOM   3382  CD1 LEU A 489      18.067  21.344 505.868  1.00113.44      A    C  
ANISOU 3382  CD1 LEU A 489    15814  14930  12359   1331   -343   -101  A    C  
ATOM   3383  CD2 LEU A 489      20.240  20.391 506.465  1.00105.59      A    C  
ANISOU 3383  CD2 LEU A 489    14861  13796  11460   1001   -864   -288  A    C  
ATOM   3384  N   TYR A 490      16.928  16.142 505.467  1.00111.03      A    N  
ANISOU 3384  N   TYR A 490    14690  14987  12508    699   -711   1187  A    N  
ATOM   3385  CA  TYR A 490      15.890  15.236 505.949  1.00109.50      A    C  
ANISOU 3385  CA  TYR A 490    14350  15066  12188    636   -663   1638  A    C  
ATOM   3386  C   TYR A 490      16.403  13.801 505.932  1.00104.57      A    C  
ANISOU 3386  C   TYR A 490    13747  14306  11680    402   -939   1808  A    C  
ATOM   3387  O   TYR A 490      16.027  12.996 506.795  1.00105.43      A    O  
ANISOU 3387  O   TYR A 490    13833  14618  11610    358   -976   2108  A    O  
ATOM   3388  CB  TYR A 490      14.641  15.332 505.067  1.00109.39      A    C  
ANISOU 3388  CB  TYR A 490    14115  15160  12289    571   -500   1910  A    C  
ATOM   3389  CG  TYR A 490      13.812  16.595 505.213  1.00118.01      A    C  
ANISOU 3389  CG  TYR A 490    15159  16487  13194    859   -175   1883  A    C  
ATOM   3390  CD1 TYR A 490      13.007  16.831 506.321  1.00126.59      A    C  
ANISOU 3390  CD1 TYR A 490    16205  17976  13916   1098     41   2113  A    C  
ATOM   3391  CD2 TYR A 490      13.781  17.529 504.180  1.00114.47      A    C  
ANISOU 3391  CD2 TYR A 490    14709  15862  12920    920    -67   1659  A    C  
ATOM   3392  CE1 TYR A 490      12.225  17.995 506.418  1.00125.37      A    C  
ANISOU 3392  CE1 TYR A 490    16046  18037  13553   1436    365   2106  A    C  
ATOM   3393  CE2 TYR A 490      13.001  18.673 504.269  1.00110.93      A    C  
ANISOU 3393  CE2 TYR A 490    14255  15610  12284   1221    242   1648  A    C  
ATOM   3394  CZ  TYR A 490      12.233  18.911 505.378  1.00112.98      A    C  
ANISOU 3394  CZ  TYR A 490    14506  16260  12163   1496    461   1867  A    C  
ATOM   3395  OH  TYR A 490      11.476  20.063 505.450  1.00108.93      A    O  
ANISOU 3395  OH  TYR A 490    14030  15934  11425   1866    788   1860  A    O  
ATOM   3396  N   ALA A 491      17.272  13.475 504.966  1.00 96.06      A    N  
ANISOU 3396  N   ALA A 491    12735  12885  10879    280  -1127   1630  A    N  
ATOM   3397  CA  ALA A 491      18.037  12.237 505.029  1.00 95.37      A    C  
ANISOU 3397  CA  ALA A 491    12759  12626  10852    157  -1387   1711  A    C  
ATOM   3398  C   ALA A 491      18.778  12.119 506.357  1.00102.39      A    C  
ANISOU 3398  C   ALA A 491    13750  13660  11495    281  -1457   1635  A    C  
ATOM   3399  O   ALA A 491      18.883  11.023 506.925  1.00110.19      A    O  
ANISOU 3399  O   ALA A 491    14800  14676  12393    212  -1596   1861  A    O  
ATOM   3400  CB  ALA A 491      19.016  12.174 503.859  1.00 94.93      A    C  
ANISOU 3400  CB  ALA A 491    12775  12219  11074    126  -1530   1475  A    C  
ATOM   3401  N   ALA A 492      19.289  13.242 506.876  1.00107.06      A    N  
ANISOU 3401  N   ALA A 492    14388  14332  11957    452  -1376   1326  A    N  
ATOM   3402  CA  ALA A 492      20.056  13.201 508.122  1.00105.54      A    C  
ANISOU 3402  CA  ALA A 492    14310  14275  11516    553  -1470   1232  A    C  
ATOM   3403  C   ALA A 492      19.155  13.009 509.338  1.00101.79      A    C  
ANISOU 3403  C   ALA A 492    13829  14125  10720    640  -1343   1490  A    C  
ATOM   3404  O   ALA A 492      19.460  12.194 510.219  1.00 98.13      A    O  
ANISOU 3404  O   ALA A 492    13417  13767  10099    637  -1462   1636  A    O  
ATOM   3405  CB  ALA A 492      20.902  14.466 508.272  1.00104.34      A    C  
ANISOU 3405  CB  ALA A 492    14258  14081  11306    654  -1472    830  A    C  
ATOM   3406  N   ARG A 493      18.044  13.752 509.415  1.00104.08      A    N  
ANISOU 3406  N   ARG A 493    14053  14604  10889    751  -1087   1572  A    N  
ATOM   3407  CA  ARG A 493      17.121  13.532 510.528  1.00113.90      A    C  
ANISOU 3407  CA  ARG A 493    15254  16211  11812    869   -938   1880  A    C  
ATOM   3408  C   ARG A 493      16.548  12.117 510.513  1.00112.28      A    C  
ANISOU 3408  C   ARG A 493    14909  16080  11671    651  -1034   2340  A    C  
ATOM   3409  O   ARG A 493      16.327  11.528 511.578  1.00107.10      A    O  
ANISOU 3409  O   ARG A 493    14256  15662  10773    687  -1040   2584  A    O  
ATOM   3410  CB  ARG A 493      15.988  14.565 510.514  1.00115.39      A    C  
ANISOU 3410  CB  ARG A 493    15373  16622  11847   1078   -619   1937  A    C  
ATOM   3411  CG  ARG A 493      15.055  14.473 511.729  1.00115.65      A    C  
ANISOU 3411  CG  ARG A 493    15357  17092  11491   1284   -423   2266  A    C  
ATOM   3412  CD  ARG A 493      13.791  15.287 511.532  1.00117.90      A    C  
ANISOU 3412  CD  ARG A 493    15507  17646  11645   1505    -88   2442  A    C  
ATOM   3413  NE  ARG A 493      13.097  14.901 510.307  1.00121.37      A    N  
ANISOU 3413  NE  ARG A 493    15672  18043  12401   1261    -82   2693  A    N  
ATOM   3414  CZ  ARG A 493      12.142  15.622 509.726  1.00119.42      A    C  
ANISOU 3414  CZ  ARG A 493    15268  17953  12151   1393    169   2809  A    C  
ATOM   3415  NH1 ARG A 493      11.764  16.779 510.258  1.00118.71      A    N1+
ANISOU 3415  NH1 ARG A 493    15300  18055  11748   1810    454   2690  A    N1+
ATOM   3416  NH2 ARG A 493      11.569  15.191 508.607  1.00110.58      A    N  
ANISOU 3416  NH2 ARG A 493    13902  16791  11321   1125    128   3046  A    N  
ATOM   3417  N   ASP A 494      16.325  11.545 509.323  1.00105.15      A    N  
ANISOU 3417  N   ASP A 494    13919  14956  11076    411  -1128   2466  A    N  
ATOM   3418  CA  ASP A 494      15.764  10.199 509.253  1.00 97.61      A    C  
ANISOU 3418  CA  ASP A 494    12903  14015  10170    151  -1262   2910  A    C  
ATOM   3419  C   ASP A 494      16.792   9.139 509.614  1.00 95.87      A    C  
ANISOU 3419  C   ASP A 494    12878  13591   9957     79  -1530   2889  A    C  
ATOM   3420  O   ASP A 494      16.462   8.161 510.295  1.00 99.06      A    O  
ANISOU 3420  O   ASP A 494    13298  14115  10224    -28  -1612   3235  A    O  
ATOM   3421  CB  ASP A 494      15.190   9.931 507.867  1.00 98.46      A    C  
ANISOU 3421  CB  ASP A 494    12923  13922  10566    -96  -1309   3047  A    C  
ATOM   3422  CG  ASP A 494      13.790  10.459 507.720  1.00106.67      A    C  
ANISOU 3422  CG  ASP A 494    13698  15293  11538   -102  -1070   3336  A    C  
ATOM   3423  OD1 ASP A 494      13.579  11.654 508.019  1.00110.75      A    O1-
ANISOU 3423  OD1 ASP A 494    14151  16013  11915    184   -816   3156  A    O1-
ATOM   3424  OD2 ASP A 494      12.897   9.675 507.332  1.00110.60      A    O1-
ANISOU 3424  OD2 ASP A 494    14068  15859  12098   -391  -1143   3766  A    O1-
ATOM   3425  N   ILE A 495      18.041   9.298 509.169  1.00 97.92      A    N  
ANISOU 3425  N   ILE A 495    13279  13563  10363    146  -1666   2521  A    N  
ATOM   3426  CA  ILE A 495      19.064   8.350 509.604  1.00 97.60      A    C  
ANISOU 3426  CA  ILE A 495    13410  13389  10283    152  -1893   2516  A    C  
ATOM   3427  C   ILE A 495      19.241   8.438 511.112  1.00 92.88      A    C  
ANISOU 3427  C   ILE A 495    12830  13101   9360    310  -1854   2541  A    C  
ATOM   3428  O   ILE A 495      19.313   7.414 511.803  1.00 91.80      A    O  
ANISOU 3428  O   ILE A 495    12772  13014   9093    266  -1972   2790  A    O  
ATOM   3429  CB  ILE A 495      20.392   8.588 508.860  1.00 91.62      A    C  
ANISOU 3429  CB  ILE A 495    12743  12352   9718    235  -2022   2155  A    C  
ATOM   3430  CG1 ILE A 495      20.285   8.129 507.404  1.00 90.94      A    C  
ANISOU 3430  CG1 ILE A 495    12707  11924   9923     93  -2103   2195  A    C  
ATOM   3431  CG2 ILE A 495      21.523   7.842 509.545  1.00 88.88      A    C  
ANISOU 3431  CG2 ILE A 495    12530  11983   9256    332  -2212   2139  A    C  
ATOM   3432  CD1 ILE A 495      20.206   6.619 507.223  1.00 87.53      A    C  
ANISOU 3432  CD1 ILE A 495    12477  11275   9506    -50  -2303   2506  A    C  
ATOM   3433  N   ALA A 496      19.251   9.668 511.649  1.00 94.83      A    N  
ANISOU 3433  N   ALA A 496    13039  13548   9444    498  -1689   2295  A    N  
ATOM   3434  CA  ALA A 496      19.426   9.880 513.087  1.00 94.90      A    C  
ANISOU 3434  CA  ALA A 496    13112  13843   9103    675  -1652   2280  A    C  
ATOM   3435  C   ALA A 496      18.267   9.301 513.888  1.00 96.49      A    C  
ANISOU 3435  C   ALA A 496    13226  14353   9084    664  -1530   2721  A    C  
ATOM   3436  O   ALA A 496      18.461   8.816 515.008  1.00 96.54      A    O  
ANISOU 3436  O   ALA A 496    13295  14543   8842    740  -1579   2848  A    O  
ATOM   3437  CB  ALA A 496      19.580  11.371 513.385  1.00 91.34      A    C  
ANISOU 3437  CB  ALA A 496    12722  13482   8500    872  -1509   1921  A    C  
ATOM   3438  N   ARG A 497      17.053   9.362 513.339  1.00 98.64      A    N  
ANISOU 3438  N   ARG A 497    13327  14719   9431    570  -1370   2986  A    N  
ATOM   3439  CA  ARG A 497      15.885   8.837 514.037  1.00100.48      A    C  
ANISOU 3439  CA  ARG A 497    13413  15307   9458    535  -1248   3476  A    C  
ATOM   3440  C   ARG A 497      16.056   7.351 514.325  1.00104.39      A    C  
ANISOU 3440  C   ARG A 497    13972  15719   9971    310  -1479   3801  A    C  
ATOM   3441  O   ARG A 497      15.842   6.893 515.454  1.00110.57      A    O  
ANISOU 3441  O   ARG A 497    14750  16774  10486    373  -1458   4053  A    O  
ATOM   3442  CB  ARG A 497      14.639   9.093 513.184  1.00100.31      A    C  
ANISOU 3442  CB  ARG A 497    13158  15392   9563    415  -1083   3736  A    C  
ATOM   3443  CG  ARG A 497      13.325   8.655 513.790  1.00107.90      A    C  
ANISOU 3443  CG  ARG A 497    13884  16795  10316    361   -937   4310  A    C  
ATOM   3444  CD  ARG A 497      12.864   9.632 514.849  1.00114.82      A    C  
ANISOU 3444  CD  ARG A 497    14708  18110  10811    768   -629   4301  A    C  
ATOM   3445  NE  ARG A 497      11.711   9.127 515.588  1.00124.70      A    N  
ANISOU 3445  NE  ARG A 497    15713  19851  11817    759   -486   4898  A    N  
ATOM   3446  CZ  ARG A 497      11.257   9.662 516.719  1.00131.90      A    C  
ANISOU 3446  CZ  ARG A 497    16586  21204  12326   1131   -228   5015  A    C  
ATOM   3447  NH1 ARG A 497      11.848  10.733 517.239  1.00131.82      A    N1+
ANISOU 3447  NH1 ARG A 497    16825  21159  12101   1526   -104   4549  A    N1+
ATOM   3448  NH2 ARG A 497      10.198   9.139 517.323  1.00134.46      A    N  
ANISOU 3448  NH2 ARG A 497    16639  22009  12441   1108    -99   5618  A    N  
ATOM   3449  N   ASP A 498      16.496   6.590 513.321  1.00104.92      A    N  
ANISOU 3449  N   ASP A 498    14145  15389  10330     75  -1705   3786  A    N  
ATOM   3450  CA  ASP A 498      16.724   5.161 513.506  1.00111.63      A    C  
ANISOU 3450  CA  ASP A 498    15151  16076  11187   -121  -1944   4070  A    C  
ATOM   3451  C   ASP A 498      17.891   4.906 514.449  1.00115.28      A    C  
ANISOU 3451  C   ASP A 498    15784  16534  11481     83  -2054   3881  A    C  
ATOM   3452  O   ASP A 498      17.884   3.931 515.207  1.00120.86      A    O  
ANISOU 3452  O   ASP A 498    16580  17306  12035     28  -2159   4170  A    O  
ATOM   3453  CB  ASP A 498      16.963   4.500 512.154  1.00117.47      A    C  
ANISOU 3453  CB  ASP A 498    16044  16351  12239   -356  -2151   4055  A    C  
ATOM   3454  CG  ASP A 498      15.752   4.584 511.255  1.00127.67      A    C  
ANISOU 3454  CG  ASP A 498    17174  17657  13679   -619  -2089   4312  A    C  
ATOM   3455  OD1 ASP A 498      14.972   5.549 511.408  1.00123.96      A    O1-
ANISOU 3455  OD1 ASP A 498    16439  17527  13134   -524  -1838   4338  A    O1-
ATOM   3456  OD2 ASP A 498      15.580   3.695 510.395  1.00138.34      A    O1-
ANISOU 3456  OD2 ASP A 498    18683  18681  15199   -907  -2296   4495  A    O1-
ATOM   3457  N   LEU A 499      18.916   5.758 514.395  1.00113.35      A    N  
ANISOU 3457  N   LEU A 499    15587  16220  11261    297  -2050   3418  A    N  
ATOM   3458  CA  LEU A 499      20.052   5.616 515.297  1.00113.85      A    C  
ANISOU 3458  CA  LEU A 499    15775  16334  11148    480  -2166   3245  A    C  
ATOM   3459  C   LEU A 499      19.616   5.747 516.750  1.00116.32      A    C  
ANISOU 3459  C   LEU A 499    16048  17053  11096    619  -2047   3406  A    C  
ATOM   3460  O   LEU A 499      19.937   4.896 517.590  1.00116.33      A    O  
ANISOU 3460  O   LEU A 499    16140  17132  10930    643  -2159   3590  A    O  
ATOM   3461  CB  LEU A 499      21.105   6.668 514.949  1.00113.20      A    C  
ANISOU 3461  CB  LEU A 499    15705  16158  11147    627  -2185   2758  A    C  
ATOM   3462  CG  LEU A 499      22.560   6.465 515.365  1.00116.12      A    C  
ANISOU 3462  CG  LEU A 499    16178  16490  11453    753  -2381   2555  A    C  
ATOM   3463  CD1 LEU A 499      23.160   5.259 514.676  1.00116.33      A    C  
ANISOU 3463  CD1 LEU A 499    16319  16220  11663    696  -2575   2689  A    C  
ATOM   3464  CD2 LEU A 499      23.336   7.718 515.000  1.00115.73      A    C  
ANISOU 3464  CD2 LEU A 499    16088  16410  11473    827  -2379   2126  A    C  
ATOM   3465  N   LEU A 500      18.860   6.802 517.058  1.00108.55      A    N  
ANISOU 3465  N   LEU A 500    15232  16906   9106    288    663    693  A    N  
ATOM   3466  CA  LEU A 500      18.372   6.991 518.417  1.00109.17      A    C  
ANISOU 3466  CA  LEU A 500    14980  17078   9423    547    614    769  A    C  
ATOM   3467  C   LEU A 500      17.479   5.831 518.845  1.00116.67      A    C  
ANISOU 3467  C   LEU A 500    15816  18182  10333    440    422    846  A    C  
ATOM   3468  O   LEU A 500      17.558   5.370 519.989  1.00118.40      A    O  
ANISOU 3468  O   LEU A 500    15859  18398  10730    583    458    752  A    O  
ATOM   3469  CB  LEU A 500      17.638   8.329 518.527  1.00107.50      A    C  
ANISOU 3469  CB  LEU A 500    14598  16965   9283    738    543   1041  A    C  
ATOM   3470  CG  LEU A 500      17.145   8.713 519.922  1.00104.89      A    C  
ANISOU 3470  CG  LEU A 500    13954  16701   9199   1025    543   1124  A    C  
ATOM   3471  CD1 LEU A 500      18.328   8.844 520.862  1.00106.23      A    C  
ANISOU 3471  CD1 LEU A 500    14109  16690   9562   1190    780    836  A    C  
ATOM   3472  CD2 LEU A 500      16.349  10.006 519.888  1.00104.37      A    C  
ANISOU 3472  CD2 LEU A 500    13753  16713   9190   1207    499   1421  A    C  
ATOM   3473  N   ILE B  24       8.127  -4.652 454.057  1.00 35.43      B    N  
ANISOU 3473  N   ILE B  24     5293   1932   6237   1016    390   -412  B    N  
ATOM   3474  CA  ILE B  24       8.611  -4.925 452.707  1.00 36.27      B    C  
ANISOU 3474  CA  ILE B  24     5361   1993   6425    934    530   -533  B    C  
ATOM   3475  C   ILE B  24       7.441  -5.187 451.771  1.00 35.93      B    C  
ANISOU 3475  C   ILE B  24     5408   1931   6313    789    556   -618  B    C  
ATOM   3476  O   ILE B  24       7.367  -6.268 451.176  1.00 62.28      B    O  
ANISOU 3476  O   ILE B  24     8720   5203   9738    764    722   -709  B    O  
ATOM   3477  CB  ILE B  24       9.572  -6.118 452.705  1.00 45.09      B    C  
ANISOU 3477  CB  ILE B  24     6353   3040   7738   1042    717   -565  B    C  
ATOM   3478  CG1 ILE B  24       9.019  -7.222 453.613  1.00 50.54      B    C  
ANISOU 3478  CG1 ILE B  24     7055   3703   8446   1138    724   -505  B    C  
ATOM   3479  CG2 ILE B  24      10.955  -5.695 453.153  1.00 39.50      B    C  
ANISOU 3479  CG2 ILE B  24     5506   2333   7170   1153    728   -512  B    C  
ATOM   3480  CD1 ILE B  24       9.547  -8.574 453.324  1.00 41.63      B    C  
ANISOU 3480  CD1 ILE B  24     5849   2483   7487   1200    930   -555  B    C  
ATOM   3481  N   PRO B  25       6.543  -4.224 451.550  1.00 46.03      B    N  
ANISOU 3481  N   PRO B  25     6784   3249   7457    682    418   -597  B    N  
ATOM   3482  CA  PRO B  25       5.410  -4.464 450.652  1.00 34.41      B    C  
ANISOU 3482  CA  PRO B  25     5386   1751   5939    546    424   -672  B    C  
ATOM   3483  C   PRO B  25       5.719  -4.281 449.176  1.00 43.22      B    C  
ANISOU 3483  C   PRO B  25     6509   2807   7106    385    553   -810  B    C  
ATOM   3484  O   PRO B  25       4.820  -4.498 448.360  1.00 40.96      B    O  
ANISOU 3484  O   PRO B  25     6293   2493   6777    255    561   -889  B    O  
ATOM   3485  CB  PRO B  25       4.393  -3.434 451.124  1.00 32.85      B    C  
ANISOU 3485  CB  PRO B  25     5263   1600   5618    509    252   -577  B    C  
ATOM   3486  CG  PRO B  25       5.223  -2.301 451.544  1.00 41.02      B    C  
ANISOU 3486  CG  PRO B  25     6305   2681   6599    543    177   -503  B    C  
ATOM   3487  CD  PRO B  25       6.476  -2.878 452.147  1.00 35.33      B    C  
ANISOU 3487  CD  PRO B  25     5479   1955   5990    681    260   -497  B    C  
ATOM   3488  N   ASN B  26       6.952  -3.911 448.803  1.00 47.23      B    N  
ANISOU 3488  N   ASN B  26     6949   3289   7708    375    673   -855  B    N  
ATOM   3489  CA  ASN B  26       7.314  -3.670 447.398  1.00 45.08      B    C  
ANISOU 3489  CA  ASN B  26     6708   2964   7455    192    835  -1008  B    C  
ATOM   3490  C   ASN B  26       6.304  -2.766 446.695  1.00 46.06      B    C  
ANISOU 3490  C   ASN B  26     6965   3101   7434     10    678  -1011  B    C  
ATOM   3491  O   ASN B  26       5.960  -2.975 445.533  1.00 58.70      B    O  
ANISOU 3491  O   ASN B  26     8651   4675   8979   -174    779  -1149  B    O  
ATOM   3492  CB  ASN B  26       7.463  -4.978 446.631  1.00 53.00      B    C  
ANISOU 3492  CB  ASN B  26     7703   3908   8526    145   1101  -1170  B    C  
ATOM   3493  CG  ASN B  26       8.808  -5.618 446.833  1.00 53.19      B    C  
ANISOU 3493  CG  ASN B  26     7589   3891   8731    263   1321  -1203  B    C  
ATOM   3494  ND2 ASN B  26       9.221  -6.439 445.888  1.00 44.03      B    N  
ANISOU 3494  ND2 ASN B  26     6428   2671   7631    177   1604  -1374  B    N  
ATOM   3495  OD1 ASN B  26       9.468  -5.375 447.836  1.00 72.91      B    O  
ANISOU 3495  OD1 ASN B  26     9981   6411  11311    427   1237  -1078  B    O  
ATOM   3496  N   ALA B  27       5.818  -1.759 447.415  1.00 47.11      B    N  
ANISOU 3496  N   ALA B  27     7127   3281   7491     51    433   -857  B    N  
ATOM   3497  CA  ALA B  27       4.887  -0.781 446.878  1.00 34.47      B    C  
ANISOU 3497  CA  ALA B  27     5633   1681   5781   -101    253   -818  B    C  
ATOM   3498  C   ALA B  27       4.914   0.433 447.785  1.00 50.29      B    C  
ANISOU 3498  C   ALA B  27     7664   3732   7711    -32     76   -648  B    C  
ATOM   3499  O   ALA B  27       5.350   0.361 448.938  1.00 50.03      B    O  
ANISOU 3499  O   ALA B  27     7584   3750   7676    133     82   -570  B    O  
ATOM   3500  CB  ALA B  27       3.469  -1.327 446.776  1.00 36.85      B    C  
ANISOU 3500  CB  ALA B  27     5991   1980   6029   -133    160   -821  B    C  
ATOM   3501  N   ILE B  28       4.458   1.558 447.240  1.00 43.91      B    N  
ANISOU 3501  N   ILE B  28     6939   2922   6822   -178    -46   -592  B    N  
ATOM   3502  CA  ILE B  28       4.441   2.816 447.968  1.00 43.65      B    C  
ANISOU 3502  CA  ILE B  28     6937   2984   6666   -158    -24   -441  B    C  
ATOM   3503  C   ILE B  28       3.077   3.453 447.786  1.00 41.36      B    C  
ANISOU 3503  C   ILE B  28     6576   2744   6395   -245     81   -384  B    C  
ATOM   3504  O   ILE B  28       2.318   3.103 446.882  1.00 41.25      B    O  
ANISOU 3504  O   ILE B  28     6537   2691   6446   -369     95   -458  B    O  
ATOM   3505  CB  ILE B  28       5.552   3.786 447.508  1.00 38.76      B    C  
ANISOU 3505  CB  ILE B  28     6300   2311   6114   -258    -35   -446  B    C  
ATOM   3506  CG1 ILE B  28       5.390   4.151 446.034  1.00 43.40      B    C  
ANISOU 3506  CG1 ILE B  28     6827   2842   6821   -472   -168   -510  B    C  
ATOM   3507  CG2 ILE B  28       6.932   3.210 447.755  1.00 34.26      B    C  
ANISOU 3507  CG2 ILE B  28     5605   1688   5725   -161     35   -533  B    C  
ATOM   3508  CD1 ILE B  28       5.999   5.511 445.704  1.00 46.87      B    C  
ANISOU 3508  CD1 ILE B  28     7222   3261   7325   -612    -55   -464  B    C  
ATOM   3509  N   GLN B  29       2.758   4.364 448.694  1.00 36.35      B    N  
ANISOU 3509  N   GLN B  29     5851   2174   5788   -158     40   -269  B    N  
ATOM   3510  CA  GLN B  29       1.623   5.234 448.485  1.00 32.81      B    C  
ANISOU 3510  CA  GLN B  29     5345   1746   5373   -205    -73   -190  B    C  
ATOM   3511  C   GLN B  29       1.970   6.253 447.402  1.00 42.79      B    C  
ANISOU 3511  C   GLN B  29     6632   2978   6648   -359   -228   -158  B    C  
ATOM   3512  O   GLN B  29       3.120   6.684 447.285  1.00 54.58      B    O  
ANISOU 3512  O   GLN B  29     8140   4446   8151   -395   -217   -167  B    O  
ATOM   3513  CB  GLN B  29       1.254   5.952 449.774  1.00 27.64      B    C  
ANISOU 3513  CB  GLN B  29     4626   1192   4682    -74    -95    -87  B    C  
ATOM   3514  CG  GLN B  29       1.218   5.065 450.984  1.00 27.39      B    C  
ANISOU 3514  CG  GLN B  29     4593   1173   4642     67    -47   -100  B    C  
ATOM   3515  CD  GLN B  29       0.634   5.784 452.180  1.00 38.69      B    C  
ANISOU 3515  CD  GLN B  29     5945   2661   6092    151   -138    -26  B    C  
ATOM   3516  NE2 GLN B  29       1.392   5.841 453.269  1.00 27.82      B    N  
ANISOU 3516  NE2 GLN B  29     4550   1311   4711    236   -125    -16  B    N  
ATOM   3517  OE1 GLN B  29      -0.508   6.258 452.134  1.00 27.07      B    O  
ANISOU 3517  OE1 GLN B  29     4441   1201   4642    134   -214     15  B    O  
ATOM   3518  N   PRO B  30       1.014   6.634 446.593  1.00 39.01      B    N  
ANISOU 3518  N   PRO B  30     6193   2493   6135   -463   -390   -104  B    N  
ATOM   3519  CA  PRO B  30       1.338   7.466 445.433  1.00 37.84      B    C  
ANISOU 3519  CA  PRO B  30     6161   2316   5902   -650   -551    -45  B    C  
ATOM   3520  C   PRO B  30       1.524   8.955 445.707  1.00 42.10      B    C  
ANISOU 3520  C   PRO B  30     6680   2896   6418   -630   -649    106  B    C  
ATOM   3521  O   PRO B  30       1.507   9.728 444.745  1.00 60.70      B    O  
ANISOU 3521  O   PRO B  30     9152   5235   8676   -791   -795    205  B    O  
ATOM   3522  CB  PRO B  30       0.143   7.219 444.504  1.00 33.37      B    C  
ANISOU 3522  CB  PRO B  30     5686   1733   5259   -785   -713    -22  B    C  
ATOM   3523  CG  PRO B  30      -0.965   6.899 445.418  1.00 32.20      B    C  
ANISOU 3523  CG  PRO B  30     5411   1615   5208   -619   -687     -5  B    C  
ATOM   3524  CD  PRO B  30      -0.349   6.089 446.515  1.00 35.86      B    C  
ANISOU 3524  CD  PRO B  30     5784   2096   5746   -458   -436   -106  B    C  
ATOM   3525  N   PHE B  31       1.713   9.407 446.951  1.00 46.75      B    N  
ANISOU 3525  N   PHE B  31     7157   3541   7065   -465   -568    129  B    N  
ATOM   3526  CA  PHE B  31       2.030  10.825 447.118  1.00 30.51      B    C  
ANISOU 3526  CA  PHE B  31     5095   1505   4994   -475   -637    235  B    C  
ATOM   3527  C   PHE B  31       3.542  11.133 446.914  1.00 41.60      B    C  
ANISOU 3527  C   PHE B  31     6535   2868   6403   -559   -587    204  B    C  
ATOM   3528  O   PHE B  31       4.026  12.213 447.300  1.00 32.87      B    O  
ANISOU 3528  O   PHE B  31     5409   1773   5309   -555   -603    262  B    O  
ATOM   3529  CB  PHE B  31       1.528  11.348 448.471  1.00 29.17      B    C  
ANISOU 3529  CB  PHE B  31     4823   1406   4852   -314   -583    260  B    C  
ATOM   3530  CG  PHE B  31       2.213  10.765 449.700  1.00 51.23      B    C  
ANISOU 3530  CG  PHE B  31     7564   4240   7659   -197   -434    176  B    C  
ATOM   3531  CD1 PHE B  31       1.770   9.569 450.274  1.00 59.84      B    C  
ANISOU 3531  CD1 PHE B  31     8631   5349   8756   -108   -361    117  B    C  
ATOM   3532  CD2 PHE B  31       3.255  11.439 450.314  1.00 28.23      B    C  
ANISOU 3532  CD2 PHE B  31     4640   1331   4755   -187   -416    173  B    C  
ATOM   3533  CE1 PHE B  31       2.369   9.044 451.414  1.00 38.49      B    C  
ANISOU 3533  CE1 PHE B  31     5901   2664   6060     -7   -302     74  B    C  
ATOM   3534  CE2 PHE B  31       3.850  10.929 451.443  1.00 33.23      B    C  
ANISOU 3534  CE2 PHE B  31     5240   1989   5397    -91   -358    120  B    C  
ATOM   3535  CZ  PHE B  31       3.405   9.721 451.996  1.00 36.23      B    C  
ANISOU 3535  CZ  PHE B  31     5602   2386   5778      3   -312     79  B    C  
ATOM   3536  N   GLY B  32       4.267  10.207 446.293  1.00 43.02      B    N  
ANISOU 3536  N   GLY B  32     6770   2991   6586   -649   -518    100  B    N  
ATOM   3537  CA  GLY B  32       5.634  10.438 445.880  1.00 37.04      B    C  
ANISOU 3537  CA  GLY B  32     6056   2178   5838   -773   -468     63  B    C  
ATOM   3538  C   GLY B  32       6.118   9.314 444.989  1.00 43.85      B    C  
ANISOU 3538  C   GLY B  32     7009   2976   6676   -902   -379    -75  B    C  
ATOM   3539  O   GLY B  32       5.341   8.463 444.556  1.00 54.57      B    O  
ANISOU 3539  O   GLY B  32     8416   4332   7987   -920   -380   -134  B    O  
ATOM   3540  N   ALA B  33       7.416   9.329 444.704  1.00 35.06      B    N  
ANISOU 3540  N   ALA B  33     5928   1809   5584  -1013   -285   -142  B    N  
ATOM   3541  CA  ALA B  33       8.048   8.257 443.948  1.00 36.43      B    C  
ANISOU 3541  CA  ALA B  33     6198   1941   5702  -1135   -100   -317  B    C  
ATOM   3542  C   ALA B  33       9.277   7.751 444.697  1.00 55.30      B    C  
ANISOU 3542  C   ALA B  33     8404   4321   8286   -989     59   -424  B    C  
ATOM   3543  O   ALA B  33       9.822   8.434 445.572  1.00 35.69      B    O  
ANISOU 3543  O   ALA B  33     5816   1812   5933   -903    -18   -354  B    O  
ATOM   3544  CB  ALA B  33       8.433   8.710 442.545  1.00 43.41      B    C  
ANISOU 3544  CB  ALA B  33     7195   2958   6342  -1402    -14   -309  B    C  
ATOM   3545  N   MET B  34       9.704   6.529 444.357  1.00 51.20      B    N  
ANISOU 3545  N   MET B  34     7841   3817   7794   -960    279   -595  B    N  
ATOM   3546  CA  MET B  34      10.819   5.890 445.047  1.00 46.88      B    C  
ANISOU 3546  CA  MET B  34     7098   3253   7463   -794    431   -686  B    C  
ATOM   3547  C   MET B  34      11.765   5.197 444.074  1.00 50.41      B    C  
ANISOU 3547  C   MET B  34     7501   3772   7879   -896    730   -851  B    C  
ATOM   3548  O   MET B  34      11.326   4.569 443.107  1.00 55.77      B    O  
ANISOU 3548  O   MET B  34     8316   4470   8406  -1023    856   -960  B    O  
ATOM   3549  CB  MET B  34      10.325   4.892 446.078  1.00 36.30      B    C  
ANISOU 3549  CB  MET B  34     5698   1822   6271   -540    392   -704  B    C  
ATOM   3550  CG  MET B  34      11.440   4.271 446.861  1.00 48.45      B    C  
ANISOU 3550  CG  MET B  34     7031   3341   8035   -349    512   -754  B    C  
ATOM   3551  SD  MET B  34      10.808   2.918 447.844  1.00 35.83      B    S  
ANISOU 3551  SD  MET B  34     5394   1788   6432    -73    466   -725  B    S  
ATOM   3552  CE  MET B  34      10.368   3.804 449.339  1.00 33.76      B    C  
ANISOU 3552  CE  MET B  34     5138   1607   6081     60    184   -530  B    C  
ATOM   3553  N   LEU B  35      13.068   5.335 444.334  1.00 49.94      B    N  
ANISOU 3553  N   LEU B  35     7249   3756   7968   -852    847   -876  B    N  
ATOM   3554  CA  LEU B  35      14.126   4.591 443.664  1.00 54.61      B    C  
ANISOU 3554  CA  LEU B  35     7735   4390   8623   -889   1165  -1039  B    C  
ATOM   3555  C   LEU B  35      14.928   3.805 444.696  1.00 57.21      B    C  
ANISOU 3555  C   LEU B  35     7813   4657   9269   -619   1235  -1073  B    C  
ATOM   3556  O   LEU B  35      15.157   4.277 445.815  1.00 42.16      B    O  
ANISOU 3556  O   LEU B  35     5777   2741   7500   -475   1038   -955  B    O  
ATOM   3557  CB  LEU B  35      15.072   5.515 442.911  1.00 44.92      B    C  
ANISOU 3557  CB  LEU B  35     6471   3285   7310  -1101   1269  -1028  B    C  
ATOM   3558  CG  LEU B  35      14.487   6.425 441.841  1.00 45.37      B    C  
ANISOU 3558  CG  LEU B  35     6770   3420   7049  -1380   1208   -958  B    C  
ATOM   3559  CD1 LEU B  35      15.623   7.253 441.250  1.00 47.35      B    C  
ANISOU 3559  CD1 LEU B  35     6950   3772   7269  -1563   1355   -948  B    C  
ATOM   3560  CD2 LEU B  35      13.740   5.623 440.778  1.00 55.77      B    C  
ANISOU 3560  CD2 LEU B  35     8301   4748   8140  -1511   1334  -1080  B    C  
ATOM   3561  N   ILE B  36      15.360   2.610 444.318  1.00 44.93      B    N  
ANISOU 3561  N   ILE B  36     6192   3055   7825   -554   1515  -1231  B    N  
ATOM   3562  CA  ILE B  36      16.273   1.814 445.122  1.00 45.78      B    C  
ANISOU 3562  CA  ILE B  36     6038   3104   8252   -301   1621  -1256  B    C  
ATOM   3563  C   ILE B  36      17.503   1.571 444.271  1.00 53.65      B    C  
ANISOU 3563  C   ILE B  36     6886   4160   9337   -390   1950  -1393  B    C  
ATOM   3564  O   ILE B  36      17.401   0.998 443.173  1.00 50.26      B    O  
ANISOU 3564  O   ILE B  36     6587   3718   8793   -532   2219  -1557  B    O  
ATOM   3565  CB  ILE B  36      15.649   0.486 445.571  1.00 52.98      B    C  
ANISOU 3565  CB  ILE B  36     6987   3856   9288    -94   1685  -1311  B    C  
ATOM   3566  CG1 ILE B  36      14.375   0.732 446.376  1.00 49.68      B    C  
ANISOU 3566  CG1 ILE B  36     6721   3375   8781    -23   1386  -1182  B    C  
ATOM   3567  CG2 ILE B  36      16.649  -0.298 446.406  1.00 51.25      B    C  
ANISOU 3567  CG2 ILE B  36     6488   3574   9410    182   1784  -1299  B    C  
ATOM   3568  CD1 ILE B  36      13.655  -0.550 446.766  1.00 42.28      B    C  
ANISOU 3568  CD1 ILE B  36     5810   2457   7798    140   1376  -1160  B    C  
ATOM   3569  N   VAL B  37      18.658   1.979 444.792  1.00 49.67      B    N  
ANISOU 3569  N   VAL B  37     6108   3722   9041   -312   1937  -1334  B    N  
ATOM   3570  CA  VAL B  37      19.923   1.961 444.071  1.00 65.11      B    C  
ANISOU 3570  CA  VAL B  37     7876   5749  11115   -404   2235  -1441  B    C  
ATOM   3571  C   VAL B  37      20.884   1.040 444.810  1.00 64.51      B    C  
ANISOU 3571  C   VAL B  37     7470   5611  11429   -119   2349  -1455  B    C  
ATOM   3572  O   VAL B  37      20.988   1.114 446.039  1.00 69.21      B    O  
ANISOU 3572  O   VAL B  37     7912   6200  12185     91   2091  -1312  B    O  
ATOM   3573  CB  VAL B  37      20.494   3.388 443.956  1.00 52.78      B    C  
ANISOU 3573  CB  VAL B  37     6250   4330   9472   -597   2116  -1350  B    C  
ATOM   3574  CG1 VAL B  37      21.753   3.417 443.142  1.00 55.94      B    C  
ANISOU 3574  CG1 VAL B  37     6465   4806   9985   -722   2447  -1464  B    C  
ATOM   3575  CG2 VAL B  37      19.468   4.275 443.322  1.00 51.28      B    C  
ANISOU 3575  CG2 VAL B  37     6387   4177   8918   -841   1975  -1296  B    C  
ATOM   3576  N   GLU B  38      21.577   0.170 444.066  1.00 56.95      B    N  
ANISOU 3576  N   GLU B  38     6408   4607  10623   -110   2738  -1623  B    N  
ATOM   3577  CA  GLU B  38      22.649  -0.639 444.651  1.00 64.96      B    C  
ANISOU 3577  CA  GLU B  38     7065   5565  12053    158   2878  -1625  B    C  
ATOM   3578  C   GLU B  38      23.890   0.221 444.863  1.00 60.69      B    C  
ANISOU 3578  C   GLU B  38     6205   5174  11679    117   2834  -1557  B    C  
ATOM   3579  O   GLU B  38      24.415   0.794 443.906  1.00 62.27      B    O  
ANISOU 3579  O   GLU B  38     6404   5464  11791   -127   3039  -1649  B    O  
ATOM   3580  CB  GLU B  38      23.020  -1.817 443.748  1.00 69.42      B    C  
ANISOU 3580  CB  GLU B  38     7610   6009  12756    177   3347  -1839  B    C  
ATOM   3581  CG  GLU B  38      22.130  -3.038 443.798  1.00 71.94      B    C  
ANISOU 3581  CG  GLU B  38     8115   6134  13083    315   3444  -1917  B    C  
ATOM   3582  CD  GLU B  38      22.845  -4.320 443.326  1.00 77.65      B    C  
ANISOU 3582  CD  GLU B  38     8701   6758  14045    409   3832  -2046  B    C  
ATOM   3583  OE1 GLU B  38      23.793  -4.249 442.509  1.00 69.21      B    O  
ANISOU 3583  OE1 GLU B  38     7495   5718  13084    301   4170  -2191  B    O  
ATOM   3584  OE2 GLU B  38      22.448  -5.411 443.791  1.00 87.82      B    O1-
ANISOU 3584  OE2 GLU B  38    10034   7991  15343    550   3738  -1947  B    O1-
ATOM   3585  N   LYS B  39      24.392   0.275 446.100  1.00 73.38      B    N  
ANISOU 3585  N   LYS B  39     7539   6810  13532    347   2579  -1401  B    N  
ATOM   3586  CA  LYS B  39      25.554   1.114 446.403  1.00 74.20      B    C  
ANISOU 3586  CA  LYS B  39     7318   7067  13807    300   2491  -1335  B    C  
ATOM   3587  C   LYS B  39      26.773   0.709 445.578  1.00 78.31      B    C  
ANISOU 3587  C   LYS B  39     7561   7600  14593    268   2907  -1475  B    C  
ATOM   3588  O   LYS B  39      27.462   1.561 445.006  1.00 80.91      B    O  
ANISOU 3588  O   LYS B  39     7791   8051  14901     42   3007  -1517  B    O  
ATOM   3589  CB  LYS B  39      25.882   1.048 447.896  1.00 61.92      B    C  
ANISOU 3589  CB  LYS B  39     5512   5543  12472    569   2146  -1152  B    C  
ATOM   3590  CG  LYS B  39      27.032   1.949 448.307  1.00 63.64      B    C  
ANISOU 3590  CG  LYS B  39     5388   5935  12859    505   2001  -1085  B    C  
ATOM   3591  CD  LYS B  39      27.509   1.676 449.737  1.00 64.30      B    C  
ANISOU 3591  CD  LYS B  39     5182   6062  13188    787   1686   -915  B    C  
ATOM   3592  CE  LYS B  39      28.607   2.659 450.148  1.00 69.77      B    C  
ANISOU 3592  CE  LYS B  39     5539   6946  14023    682   1505   -861  B    C  
ATOM   3593  NZ  LYS B  39      28.059   3.971 450.578  1.00 82.72      B    N1+
ANISOU 3593  NZ  LYS B  39     7390   8676  15365    472   1176   -803  B    N1+
ATOM   3594  N   ASP B  40      27.052  -0.591 445.500  1.00 76.71      B    N  
ANISOU 3594  N   ASP B  40     7231   7257  14656    492   3177  -1552  B    N  
ATOM   3595  CA  ASP B  40      28.276  -1.044 444.848  1.00 79.86      B    C  
ANISOU 3595  CA  ASP B  40     7317   7649  15379    508   3585  -1679  B    C  
ATOM   3596  C   ASP B  40      28.235  -0.800 443.339  1.00 89.69      B    C  
ANISOU 3596  C   ASP B  40     8787   8906  16385    181   3976  -1891  B    C  
ATOM   3597  O   ASP B  40      29.196  -0.282 442.761  1.00105.03      B    O  
ANISOU 3597  O   ASP B  40    10533  10948  18427     20   4188  -1956  B    O  
ATOM   3598  CB  ASP B  40      28.537  -2.513 445.191  1.00 80.97      B    C  
ANISOU 3598  CB  ASP B  40     7273   7605  15887    852   3781  -1696  B    C  
ATOM   3599  CG  ASP B  40      27.304  -3.379 445.035  1.00 94.89      B    C  
ANISOU 3599  CG  ASP B  40     9453   9212  17388    873   3785  -1732  B    C  
ATOM   3600  OD1 ASP B  40      26.204  -2.803 444.888  1.00110.29      B    O1-
ANISOU 3600  OD1 ASP B  40    11733  11171  19001    719   3641  -1755  B    O1-
ATOM   3601  OD2 ASP B  40      27.423  -4.626 445.071  1.00 93.15      B    O1-
ANISOU 3601  OD2 ASP B  40     9263   8893  17238   1001   3868  -1702  B    O1-
ATOM   3602  N   THR B  41      27.148  -1.181 442.678  1.00 86.76      B    N  
ANISOU 3602  N   THR B  41     8826   8441  15697     69   4080  -2000  B    N  
ATOM   3603  CA  THR B  41      27.049  -1.023 441.232  1.00 83.67      B    C  
ANISOU 3603  CA  THR B  41     8688   8071  15034   -249   4440  -2201  B    C  
ATOM   3604  C   THR B  41      26.556   0.356 440.803  1.00 74.78      B    C  
ANISOU 3604  C   THR B  41     7823   7102  13489   -576   4230  -2132  B    C  
ATOM   3605  O   THR B  41      26.685   0.698 439.622  1.00 75.66      B    O  
ANISOU 3605  O   THR B  41     8103   7270  13375   -865   4510  -2261  B    O  
ATOM   3606  CB  THR B  41      26.119  -2.098 440.654  1.00 82.57      B    C  
ANISOU 3606  CB  THR B  41     8872   7768  14734   -245   4652  -2366  B    C  
ATOM   3607  CG2 THR B  41      26.574  -3.473 441.085  1.00 74.71      B    C  
ANISOU 3607  CG2 THR B  41     7641   6586  14162     81   4863  -2416  B    C  
ATOM   3608  OG1 THR B  41      24.776  -1.874 441.114  1.00 68.89      B    O  
ANISOU 3608  OG1 THR B  41     7446   6025  12703   -253   4269  -2253  B    O  
ATOM   3609  N   GLN B  42      26.006   1.148 441.728  1.00 73.55      B    N  
ANISOU 3609  N   GLN B  42     7711   7008  13227   -538   3760  -1931  B    N  
ATOM   3610  CA  GLN B  42      25.392   2.453 441.436  1.00 80.92      B    C  
ANISOU 3610  CA  GLN B  42     8910   8054  13782   -815   3525  -1838  B    C  
ATOM   3611  C   GLN B  42      24.254   2.314 440.429  1.00 81.96      B    C  
ANISOU 3611  C   GLN B  42     9488   8153  13500  -1020   3613  -1930  B    C  
ATOM   3612  O   GLN B  42      23.922   3.267 439.711  1.00 85.48      B    O  
ANISOU 3612  O   GLN B  42    10168   8692  13620  -1304   3574  -1898  B    O  
ATOM   3613  CB  GLN B  42      26.424   3.468 440.925  1.00 73.99      B    C  
ANISOU 3613  CB  GLN B  42     7871   7309  12933  -1045   3658  -1839  B    C  
ATOM   3614  CG  GLN B  42      27.590   3.717 441.865  1.00 73.91      B    C  
ANISOU 3614  CG  GLN B  42     7397   7360  13327   -887   3550  -1754  B    C  
ATOM   3615  CD  GLN B  42      27.197   4.492 443.103  1.00 81.37      B    C  
ANISOU 3615  CD  GLN B  42     8315   8349  14251   -802   3046  -1555  B    C  
ATOM   3616  NE2 GLN B  42      26.640   3.797 444.091  1.00 78.26      B    N  
ANISOU 3616  NE2 GLN B  42     7916   7876  13943   -522   2812  -1481  B    N  
ATOM   3617  OE1 GLN B  42      27.402   5.707 443.176  1.00 91.08      B    O  
ANISOU 3617  OE1 GLN B  42     9538   9676  15391   -993   2885  -1474  B    O  
ATOM   3618  N   GLN B  43      23.606   1.152 440.421  1.00 64.61      B    N  
ANISOU 3618  N   GLN B  43     7413   5824  11311   -878   3703  -2027  B    N  
ATOM   3619  CA  GLN B  43      22.564   0.836 439.457  1.00 64.27      B    C  
ANISOU 3619  CA  GLN B  43     7766   5750  10902  -1069   3803  -2145  B    C  
ATOM   3620  C   GLN B  43      21.189   0.979 440.101  1.00 60.67      B    C  
ANISOU 3620  C   GLN B  43     7533   5257  10263  -1004   3399  -2009  B    C  
ATOM   3621  O   GLN B  43      20.942   0.441 441.187  1.00 59.12      B    O  
ANISOU 3621  O   GLN B  43     7216   4962  10284   -726   3221  -1932  B    O  
ATOM   3622  CB  GLN B  43      22.790  -0.584 438.934  1.00 66.75      B    C  
ANISOU 3622  CB  GLN B  43     8069   5929  11365   -987   4222  -2380  B    C  
ATOM   3623  CG  GLN B  43      23.408  -0.619 437.540  1.00 74.91      B    C  
ANISOU 3623  CG  GLN B  43     9190   7015  12258  -1259   4676  -2589  B    C  
ATOM   3624  CD  GLN B  43      23.561  -2.024 436.986  1.00 76.83      B    C  
ANISOU 3624  CD  GLN B  43     9457   7102  12633  -1196   5116  -2851  B    C  
ATOM   3625  NE2 GLN B  43      24.083  -2.130 435.768  1.00 79.37      B    N  
ANISOU 3625  NE2 GLN B  43     9876   7459  12821  -1438   5549  -3060  B    N  
ATOM   3626  OE1 GLN B  43      23.249  -3.003 437.657  1.00 85.17      B    O  
ANISOU 3626  OE1 GLN B  43    10446   7997  13919   -936   5088  -2867  B    O  
ATOM   3627  N   ILE B  44      20.290   1.693 439.424  1.00 59.61      B    N  
ANISOU 3627  N   ILE B  44     7719   5199   9731  -1258   3262  -1971  B    N  
ATOM   3628  CA  ILE B  44      18.902   1.693 439.858  1.00 56.69      B    C  
ANISOU 3628  CA  ILE B  44     7569   4781   9191  -1213   2936  -1875  B    C  
ATOM   3629  C   ILE B  44      18.363   0.283 439.705  1.00 59.20      B    C  
ANISOU 3629  C   ILE B  44     7979   4960   9553  -1111   3114  -2046  B    C  
ATOM   3630  O   ILE B  44      18.270  -0.243 438.588  1.00 61.90      B    O  
ANISOU 3630  O   ILE B  44     8499   5305   9717  -1299   3400  -2240  B    O  
ATOM   3631  CB  ILE B  44      18.077   2.680 439.040  1.00 56.08      B    C  
ANISOU 3631  CB  ILE B  44     7800   4812   8695  -1508   2776  -1798  B    C  
ATOM   3632  CG1 ILE B  44      18.538   4.101 439.268  1.00 55.57      B    C  
ANISOU 3632  CG1 ILE B  44     7658   4849   8609  -1599   2594  -1615  B    C  
ATOM   3633  CG2 ILE B  44      16.638   2.576 439.426  1.00 53.49      B    C  
ANISOU 3633  CG2 ILE B  44     7668   4427   8228  -1456   2472  -1715  B    C  
ATOM   3634  CD1 ILE B  44      18.133   4.983 438.123  1.00 56.45      B    C  
ANISOU 3634  CD1 ILE B  44     8049   5070   8329  -1926   2585  -1568  B    C  
ATOM   3635  N   VAL B  45      17.995  -0.337 440.822  1.00 57.94      B    N  
ANISOU 3635  N   VAL B  45     7716   4675   9624   -828   2956  -1980  B    N  
ATOM   3636  CA  VAL B  45      17.451  -1.678 440.783  1.00 55.84      B    C  
ANISOU 3636  CA  VAL B  45     7533   4248   9434   -720   3119  -2128  B    C  
ATOM   3637  C   VAL B  45      15.945  -1.706 441.013  1.00 53.35      B    C  
ANISOU 3637  C   VAL B  45     7461   3891   8919   -744   2840  -2066  B    C  
ATOM   3638  O   VAL B  45      15.277  -2.610 440.501  1.00 54.08      B    O  
ANISOU 3638  O   VAL B  45     7725   3894   8929   -805   2985  -2228  B    O  
ATOM   3639  CB  VAL B  45      18.170  -2.610 441.770  1.00 56.45      B    C  
ANISOU 3639  CB  VAL B  45     7319   4180   9949   -374   3225  -2118  B    C  
ATOM   3640  CG1 VAL B  45      19.560  -2.902 441.285  1.00 59.72      B    C  
ANISOU 3640  CG1 VAL B  45     7503   4604  10584   -364   3595  -2242  B    C  
ATOM   3641  CG2 VAL B  45      18.217  -2.003 443.153  1.00 54.11      B    C  
ANISOU 3641  CG2 VAL B  45     6848   3908   9804   -159   2855  -1870  B    C  
ATOM   3642  N   TYR B  46      15.377  -0.749 441.734  1.00 50.69      B    N  
ANISOU 3642  N   TYR B  46     7143   3610   8507   -714   2460  -1851  B    N  
ATOM   3643  CA  TYR B  46      13.924  -0.697 441.815  1.00 48.69      B    C  
ANISOU 3643  CA  TYR B  46     7114   3326   8060   -766   2216  -1797  B    C  
ATOM   3644  C   TYR B  46      13.431   0.719 441.561  1.00 51.51      B    C  
ANISOU 3644  C   TYR B  46     7598   3825   8150   -958   1932  -1633  B    C  
ATOM   3645  O   TYR B  46      14.072   1.705 441.932  1.00 46.95      B    O  
ANISOU 3645  O   TYR B  46     6899   3324   7617   -948   1818  -1499  B    O  
ATOM   3646  CB  TYR B  46      13.407  -1.212 443.165  1.00 46.63      B    C  
ANISOU 3646  CB  TYR B  46     6749   2972   7996   -468   2014  -1664  B    C  
ATOM   3647  CG  TYR B  46      13.686  -2.678 443.417  1.00 59.20      B    C  
ANISOU 3647  CG  TYR B  46     8206   4536   9751   -274   2198  -1718  B    C  
ATOM   3648  CD1 TYR B  46      12.877  -3.676 442.861  1.00 48.70      B    C  
ANISOU 3648  CD1 TYR B  46     7003   3217   8285   -339   2278  -1809  B    C  
ATOM   3649  CD2 TYR B  46      14.769  -3.073 444.194  1.00 59.40      B    C  
ANISOU 3649  CD2 TYR B  46     7972   4525  10073    -40   2282  -1665  B    C  
ATOM   3650  CE1 TYR B  46      13.138  -5.027 443.097  1.00 50.14      B    C  
ANISOU 3650  CE1 TYR B  46     7069   3357   8625   -185   2444  -1838  B    C  
ATOM   3651  CE2 TYR B  46      15.040  -4.410 444.426  1.00 50.28      B    C  
ANISOU 3651  CE2 TYR B  46     6700   3341   9061    120   2431  -1677  B    C  
ATOM   3652  CZ  TYR B  46      14.223  -5.391 443.880  1.00 66.81      B    C  
ANISOU 3652  CZ  TYR B  46     8937   5429  11019     42   2518  -1763  B    C  
ATOM   3653  OH  TYR B  46      14.516  -6.726 444.141  1.00 52.63      B    O  
ANISOU 3653  OH  TYR B  46     7032   3581   9382    187   2665  -1763  B    O  
ATOM   3654  N   ALA B  47      12.275   0.810 440.925  1.00 50.40      B    N  
ANISOU 3654  N   ALA B  47     7696   3711   7742  -1136   1816  -1643  B    N  
ATOM   3655  CA  ALA B  47      11.619   2.089 440.753  1.00 45.86      B    C  
ANISOU 3655  CA  ALA B  47     7246   3239   6941  -1284   1520  -1458  B    C  
ATOM   3656  C   ALA B  47      10.127   1.904 440.942  1.00 44.33      B    C  
ANISOU 3656  C   ALA B  47     7195   2989   6661  -1277   1289  -1408  B    C  
ATOM   3657  O   ALA B  47       9.562   0.915 440.472  1.00 67.43      B    O  
ANISOU 3657  O   ALA B  47    10224   5868   9528  -1332   1403  -1566  B    O  
ATOM   3658  CB  ALA B  47      11.901   2.675 439.369  1.00 60.99      B    C  
ANISOU 3658  CB  ALA B  47     9319   5310   8547  -1598   1629  -1497  B    C  
ATOM   3659  N   SER B  48       9.495   2.857 441.630  1.00 56.20      B    N  
ANISOU 3659  N   SER B  48     8696   4487   8171  -1216    978  -1197  B    N  
ATOM   3660  CA  SER B  48       8.049   2.820 441.790  1.00 40.98      B    C  
ANISOU 3660  CA  SER B  48     6882   2511   6177  -1217    751  -1129  B    C  
ATOM   3661  C   SER B  48       7.365   3.120 440.463  1.00 42.56      B    C  
ANISOU 3661  C   SER B  48     7288   2836   6045  -1510    688  -1139  B    C  
ATOM   3662  O   SER B  48       7.847   3.917 439.662  1.00 52.81      B    O  
ANISOU 3662  O   SER B  48     8657   4261   7145  -1697    702  -1085  B    O  
ATOM   3663  CB  SER B  48       7.587   3.822 442.844  1.00 38.68      B    C  
ANISOU 3663  CB  SER B  48     6521   2188   5986  -1072    457   -901  B    C  
ATOM   3664  OG  SER B  48       7.804   5.145 442.428  1.00 38.96      B    O  
ANISOU 3664  OG  SER B  48     6615   2308   5882  -1225    340   -760  B    O  
ATOM   3665  N   ALA B  49       6.203   2.499 440.255  1.00 56.21      B    N  
ANISOU 3665  N   ALA B  49     9114   4533   7711  -1555    603  -1193  B    N  
ATOM   3666  CA  ALA B  49       5.566   2.537 438.944  1.00 49.27      B    C  
ANISOU 3666  CA  ALA B  49     8430   3789   6503  -1845    553  -1238  B    C  
ATOM   3667  C   ALA B  49       5.323   3.963 438.468  1.00 44.85      B    C  
ANISOU 3667  C   ALA B  49     7952   3354   5734  -1990    308  -1001  B    C  
ATOM   3668  O   ALA B  49       5.253   4.206 437.258  1.00 47.12      B    O  
ANISOU 3668  O   ALA B  49     8407   3792   5705  -2253    307  -1012  B    O  
ATOM   3669  CB  ALA B  49       4.262   1.748 438.978  1.00 44.49      B    C  
ANISOU 3669  CB  ALA B  49     7854   3145   5906  -1838    437  -1295  B    C  
ATOM   3670  N   ASN B  50       5.210   4.916 439.392  1.00 42.78      B    N  
ANISOU 3670  N   ASN B  50     7589   3026   5639  -1828    111   -787  B    N  
ATOM   3671  CA  ASN B  50       4.961   6.320 439.066  1.00 58.91      B    C  
ANISOU 3671  CA  ASN B  50     9699   5143   7541  -1934   -115   -542  B    C  
ATOM   3672  C   ASN B  50       6.234   7.178 438.974  1.00 50.37      B    C  
ANISOU 3672  C   ASN B  50     8586   4107   6446  -1975      2   -480  B    C  
ATOM   3673  O   ASN B  50       6.145   8.405 439.067  1.00 43.15      B    O  
ANISOU 3673  O   ASN B  50     7687   3194   5513  -1997   -171   -264  B    O  
ATOM   3674  CB  ASN B  50       4.003   6.906 440.099  1.00 40.76      B    C  
ANISOU 3674  CB  ASN B  50     7321   2725   5443  -1750   -384   -354  B    C  
ATOM   3675  CG  ASN B  50       4.538   6.781 441.501  1.00 38.55      B    C  
ANISOU 3675  CG  ASN B  50     6855   2318   5473  -1471   -312   -373  B    C  
ATOM   3676  ND2 ASN B  50       4.068   7.638 442.398  1.00 36.91      B    N  
ANISOU 3676  ND2 ASN B  50     6502   2114   5410  -1283   -473   -196  B    N  
ATOM   3677  OD1 ASN B  50       5.349   5.892 441.784  1.00 56.20      B    O  
ANISOU 3677  OD1 ASN B  50     9027   4512   7814  -1395    -88   -549  B    O  
ATOM   3678  N   SER B  51       7.412   6.566 438.793  1.00 49.75      B    N  
ANISOU 3678  N   SER B  51     8452   4053   6397  -1986    304   -666  B    N  
ATOM   3679  CA  SER B  51       8.662   7.321 438.874  1.00 50.71      B    C  
ANISOU 3679  CA  SER B  51     8491   4203   6572  -2002    425   -619  B    C  
ATOM   3680  C   SER B  51       8.801   8.341 437.744  1.00 56.66      B    C  
ANISOU 3680  C   SER B  51     9411   5087   7029  -2270    396   -488  B    C  
ATOM   3681  O   SER B  51       9.449   9.385 437.923  1.00 46.89      B    O  
ANISOU 3681  O   SER B  51     8126   3849   5840  -2290    379   -354  B    O  
ATOM   3682  CB  SER B  51       9.856   6.363 438.851  1.00 45.84      B    C  
ANISOU 3682  CB  SER B  51     7758   3586   6075  -1956    769   -850  B    C  
ATOM   3683  OG  SER B  51       9.894   5.510 439.972  1.00 44.16      B    O  
ANISOU 3683  OG  SER B  51     7377   3243   6158  -1689    799   -934  B    O  
ATOM   3684  N   ALA B  52       8.195   8.058 436.584  1.00 58.33      B    N  
ANISOU 3684  N   ALA B  52     9825   5411   6926  -2488    386   -521  B    N  
ATOM   3685  CA  ALA B  52       8.376   8.909 435.414  1.00 51.35      B    C  
ANISOU 3685  CA  ALA B  52     9129   4666   5716  -2760    384   -398  B    C  
ATOM   3686  C   ALA B  52       7.839  10.308 435.657  1.00 56.83      B    C  
ANISOU 3686  C   ALA B  52     9850   5326   6417  -2749     84    -82  B    C  
ATOM   3687  O   ALA B  52       8.464  11.300 435.262  1.00 72.03      B    O  
ANISOU 3687  O   ALA B  52    11829   7289   8252  -2873    125     55  B    O  
ATOM   3688  CB  ALA B  52       7.700   8.285 434.198  1.00 60.29      B    C  
ANISOU 3688  CB  ALA B  52    10485   5936   6488  -2994    386   -490  B    C  
ATOM   3689  N   GLU B  53       6.667  10.414 436.280  1.00 53.69      B    N  
ANISOU 3689  N   GLU B  53     9419   4844   6136  -2606   -201     38  B    N  
ATOM   3690  CA  GLU B  53       6.062  11.730 436.398  1.00 62.15      B    C  
ANISOU 3690  CA  GLU B  53    10530   5869   7213  -2603   -474    341  B    C  
ATOM   3691  C   GLU B  53       6.823  12.619 437.368  1.00 67.95      B    C  
ANISOU 3691  C   GLU B  53    11124   6476   8217  -2465   -444    425  B    C  
ATOM   3692  O   GLU B  53       6.660  13.845 437.312  1.00 68.06      B    O  
ANISOU 3692  O   GLU B  53    11191   6446   8223  -2507   -589    664  B    O  
ATOM   3693  CB  GLU B  53       4.593  11.626 436.800  1.00 47.44      B    C  
ANISOU 3693  CB  GLU B  53     8648   3941   5434  -2485   -767    444  B    C  
ATOM   3694  CG  GLU B  53       4.326  11.114 438.187  1.00 75.88      B    C  
ANISOU 3694  CG  GLU B  53    12063   7384   9386  -2206   -783    352  B    C  
ATOM   3695  CD  GLU B  53       2.834  10.929 438.438  1.00 85.43      B    C  
ANISOU 3695  CD  GLU B  53    13257   8540  10661  -2122  -1040    438  B    C  
ATOM   3696  OE1 GLU B  53       2.277   9.891 437.986  1.00 89.58      B    O  
ANISOU 3696  OE1 GLU B  53    13822   9136  11079  -2188  -1033    293  B    O  
ATOM   3697  OE2 GLU B  53       2.226  11.831 439.071  1.00 74.59      B    O1-
ANISOU 3697  OE2 GLU B  53    11831   7050   9460  -2000  -1236    643  B    O1-
ATOM   3698  N   TYR B  54       7.637  12.039 438.258  1.00 45.56      B    N  
ANISOU 3698  N   TYR B  54     8111   3577   5622  -2305   -268    240  B    N  
ATOM   3699  CA  TYR B  54       8.476  12.869 439.113  1.00 58.17      B    C  
ANISOU 3699  CA  TYR B  54     9574   5083   7444  -2213   -237    297  B    C  
ATOM   3700  C   TYR B  54       9.838  13.138 438.494  1.00 60.03      B    C  
ANISOU 3700  C   TYR B  54     9803   5408   7597  -2382     17    236  B    C  
ATOM   3701  O   TYR B  54      10.258  14.292 438.380  1.00 71.61      B    O  
ANISOU 3701  O   TYR B  54    11296   6853   9058  -2480     -3    389  B    O  
ATOM   3702  CB  TYR B  54       8.660  12.230 440.484  1.00 42.20      B    C  
ANISOU 3702  CB  TYR B  54     7352   2955   5727  -1951   -219    165  B    C  
ATOM   3703  CG  TYR B  54       7.415  12.228 441.310  1.00 40.23      B    C  
ANISOU 3703  CG  TYR B  54     7093   2586   5608  -1774   -454    251  B    C  
ATOM   3704  CD1 TYR B  54       6.399  11.309 441.052  1.00 64.29      B    C  
ANISOU 3704  CD1 TYR B  54    10195   5647   8585  -1748   -515    192  B    C  
ATOM   3705  CD2 TYR B  54       7.239  13.125 442.344  1.00 38.81      B    C  
ANISOU 3705  CD2 TYR B  54     6753   2383   5610  -1569   -560    356  B    C  
ATOM   3706  CE1 TYR B  54       5.242  11.281 441.809  1.00 51.05      B    C  
ANISOU 3706  CE1 TYR B  54     8405   3956   7037  -1526   -674    254  B    C  
ATOM   3707  CE2 TYR B  54       6.081  13.110 443.112  1.00 46.20      B    C  
ANISOU 3707  CE2 TYR B  54     7580   3332   6641  -1341   -682    397  B    C  
ATOM   3708  CZ  TYR B  54       5.086  12.177 442.836  1.00 46.88      B    C  
ANISOU 3708  CZ  TYR B  54     7710   3430   6673  -1319   -736    353  B    C  
ATOM   3709  OH  TYR B  54       3.932  12.129 443.576  1.00 46.98      B    O  
ANISOU 3709  OH  TYR B  54     7606   3466   6778  -1117   -821    387  B    O  
ATOM   3710  N   PHE B  55      10.518  12.095 438.042  1.00 64.10      B    N  
ANISOU 3710  N   PHE B  55    10287   6013   8057  -2429    274     14  B    N  
ATOM   3711  CA  PHE B  55      11.864  12.315 437.552  1.00 58.59      B    C  
ANISOU 3711  CA  PHE B  55     9543   5387   7332  -2571    546    -59  B    C  
ATOM   3712  C   PHE B  55      11.904  12.948 436.177  1.00 65.02      B    C  
ANISOU 3712  C   PHE B  55    10587   6315   7804  -2866    609     51  B    C  
ATOM   3713  O   PHE B  55      12.986  13.374 435.758  1.00 67.57      B    O  
ANISOU 3713  O   PHE B  55    10886   6685   8103  -3008    829     33  B    O  
ATOM   3714  CB  PHE B  55      12.640  11.000 437.554  1.00 57.66      B    C  
ANISOU 3714  CB  PHE B  55     9294   5305   7307  -2508    833   -335  B    C  
ATOM   3715  CG  PHE B  55      12.931  10.515 438.923  1.00 52.57      B    C  
ANISOU 3715  CG  PHE B  55     8403   4556   7014  -2227    803   -414  B    C  
ATOM   3716  CD1 PHE B  55      12.134   9.547 439.518  1.00 54.56      B    C  
ANISOU 3716  CD1 PHE B  55     8631   4739   7360  -2037    712   -490  B    C  
ATOM   3717  CD2 PHE B  55      13.964  11.078 439.648  1.00 47.58      B    C  
ANISOU 3717  CD2 PHE B  55     7568   3898   6614  -2162    844   -397  B    C  
ATOM   3718  CE1 PHE B  55      12.387   9.129 440.804  1.00 44.23      B    C  
ANISOU 3718  CE1 PHE B  55     7117   3336   6353  -1778    674   -535  B    C  
ATOM   3719  CE2 PHE B  55      14.217  10.677 440.928  1.00 45.83      B    C  
ANISOU 3719  CE2 PHE B  55     7130   3598   6684  -1912    782   -448  B    C  
ATOM   3720  CZ  PHE B  55      13.427   9.708 441.514  1.00 48.64      B    C  
ANISOU 3720  CZ  PHE B  55     7482   3885   7113  -1715    697   -508  B    C  
ATOM   3721  N   SER B  56      10.771  13.050 435.474  1.00 52.99      B    N  
ANISOU 3721  N   SER B  56     9279   4839   6015  -2968    418    178  B    N  
ATOM   3722  CA  SER B  56      10.793  13.798 434.222  1.00 68.81      B    C  
ANISOU 3722  CA  SER B  56    11517   6953   7677  -3247    439    335  B    C  
ATOM   3723  C   SER B  56      11.241  15.240 434.438  1.00 83.25      B    C  
ANISOU 3723  C   SER B  56    13331   8701   9599  -3290    387    564  B    C  
ATOM   3724  O   SER B  56      11.774  15.865 433.512  1.00 82.89      B    O  
ANISOU 3724  O   SER B  56    13429   8730   9335  -3522    522    659  B    O  
ATOM   3725  CB  SER B  56       9.420  13.771 433.543  1.00 63.02      B    C  
ANISOU 3725  CB  SER B  56    10995   6285   6665  -3330    171    478  B    C  
ATOM   3726  OG  SER B  56       8.494  14.644 434.159  1.00 55.15      B    O  
ANISOU 3726  OG  SER B  56     9976   5170   5808  -3200   -158    733  B    O  
ATOM   3727  N   VAL B  57      11.062  15.766 435.656  1.00 86.55      B    N  
ANISOU 3727  N   VAL B  57    13586   8961  10337  -3079    215    643  B    N  
ATOM   3728  CA  VAL B  57      11.463  17.136 435.949  1.00 66.68      B    C  
ANISOU 3728  CA  VAL B  57    11052   6340   7941  -3119    170    838  B    C  
ATOM   3729  C   VAL B  57      12.979  17.220 436.045  1.00 71.25      B    C  
ANISOU 3729  C   VAL B  57    11483   6943   8646  -3194    468    694  B    C  
ATOM   3730  O   VAL B  57      13.589  18.217 435.641  1.00 68.85      B    O  
ANISOU 3730  O   VAL B  57    11235   6624   8303  -3365    560    820  B    O  
ATOM   3731  CB  VAL B  57      10.774  17.620 437.237  1.00 62.14      B    C  
ANISOU 3731  CB  VAL B  57    10363   5586   7662  -2882    -87    933  B    C  
ATOM   3732  CG1 VAL B  57      10.996  19.108 437.420  1.00 57.92      B    C  
ANISOU 3732  CG1 VAL B  57     9813   4967   7229  -2893   -145   1130  B    C  
ATOM   3733  CG2 VAL B  57       9.300  17.264 437.203  1.00 50.37      B    C  
ANISOU 3733  CG2 VAL B  57     8964   4082   6094  -2783   -345   1023  B    C  
ATOM   3734  N   ALA B  58      13.607  16.180 436.599  1.00 64.28      B    N  
ANISOU 3734  N   ALA B  58    10395   6089   7938  -3063    625    436  B    N  
ATOM   3735  CA  ALA B  58      15.062  16.104 436.595  1.00 62.95      B    C  
ANISOU 3735  CA  ALA B  58    10054   5966   7898  -3134    922    285  B    C  
ATOM   3736  C   ALA B  58      15.626  15.786 435.209  1.00 62.26      B    C  
ANISOU 3736  C   ALA B  58    10109   6024   7524  -3387   1223    210  B    C  
ATOM   3737  O   ALA B  58      16.697  16.290 434.848  1.00 64.63      B    O  
ANISOU 3737  O   ALA B  58    10356   6353   7847  -3546   1456    199  B    O  
ATOM   3738  CB  ALA B  58      15.518  15.047 437.599  1.00 53.44      B    C  
ANISOU 3738  CB  ALA B  58     8581   4746   6980  -2897    984     57  B    C  
ATOM   3739  N   ASP B  59      14.897  15.024 434.390  1.00 59.10      B    N  
ANISOU 3739  N   ASP B  59     9905   5714   6836  -3451   1226    163  B    N  
ATOM   3740  CA  ASP B  59      15.490  14.428 433.193  1.00 73.17      B    C  
ANISOU 3740  CA  ASP B  59    11805   7636   8358  -3668   1557     12  B    C  
ATOM   3741  C   ASP B  59      14.433  14.437 432.090  1.00 63.65      B    C  
ANISOU 3741  C   ASP B  59    10937   6529   6717  -3848   1427    133  B    C  
ATOM   3742  O   ASP B  59      13.537  13.593 432.079  1.00 75.95      B    O  
ANISOU 3742  O   ASP B  59    12558   8112   8189  -3769   1295     53  B    O  
ATOM   3743  CB  ASP B  59      15.991  13.019 433.499  1.00 80.84      B    C  
ANISOU 3743  CB  ASP B  59    12591   8624   9503  -3526   1784   -298  B    C  
ATOM   3744  CG  ASP B  59      16.975  12.488 432.454  1.00 90.38      B    C  
ANISOU 3744  CG  ASP B  59    13842   9941  10557  -3731   2219   -494  B    C  
ATOM   3745  OD1 ASP B  59      16.902  12.925 431.281  1.00 97.39      B    O  
ANISOU 3745  OD1 ASP B  59    14999  10930  11075  -4007   2312   -412  B    O  
ATOM   3746  OD2 ASP B  59      17.813  11.621 432.804  1.00 82.57      B    O1-
ANISOU 3746  OD2 ASP B  59    12620   8934   9818  -3614   2473   -726  B    O1-
ATOM   3747  N   ASN B  60      14.540  15.394 431.171  1.00 66.24      B    N  
ANISOU 3747  N   ASN B  60    11482   6916   6772  -4096   1456    332  B    N  
ATOM   3748  CA  ASN B  60      13.493  15.525 430.159  1.00 67.98      B    C  
ANISOU 3748  CA  ASN B  60    12023   7240   6566  -4266   1272    497  B    C  
ATOM   3749  C   ASN B  60      13.517  14.416 429.155  1.00 83.89      B    C  
ANISOU 3749  C   ASN B  60    14203   9418   8254  -4434   1492    267  B    C  
ATOM   3750  O   ASN B  60      12.784  14.467 428.155  1.00 89.25      B    O  
ANISOU 3750  O   ASN B  60    15171  10225   8515  -4630   1374    378  B    O  
ATOM   3751  CB  ASN B  60      13.605  16.865 429.427  1.00 72.96      B    C  
ANISOU 3751  CB  ASN B  60    12860   7885   6977  -4487   1242    804  B    C  
ATOM   3752  CG  ASN B  60      15.006  17.138 428.890  1.00 78.40      B    C  
ANISOU 3752  CG  ASN B  60    13542   8616   7632  -4689   1657    719  B    C  
ATOM   3753  ND2 ASN B  60      15.071  17.740 427.714  1.00 77.51      B    N  
ANISOU 3753  ND2 ASN B  60    13719   8601   7130  -4974   1745    892  B    N  
ATOM   3754  OD1 ASN B  60      16.011  16.846 429.538  1.00 83.73      B    O  
ANISOU 3754  OD1 ASN B  60    13946   9234   8634  -4590   1889    517  B    O  
ATOM   3755  N   THR B  61      14.377  13.428 429.373  1.00 88.63      B    N  
ANISOU 3755  N   THR B  61    14628  10017   9030  -4371   1819    -50  B    N  
ATOM   3756  CA  THR B  61      14.383  12.220 428.562  1.00 96.79      B    C  
ANISOU 3756  CA  THR B  61    15795  11167   9815  -4497   2058   -324  B    C  
ATOM   3757  C   THR B  61      13.501  11.123 429.140  1.00 80.58      B    C  
ANISOU 3757  C   THR B  61    13664   9069   7884  -4294   1888   -480  B    C  
ATOM   3758  O   THR B  61      13.172  10.172 428.424  1.00 71.41      B    O  
ANISOU 3758  O   THR B  61    12664   8000   6470  -4418   2000   -678  B    O  
ATOM   3759  CB  THR B  61      15.819  11.715 428.387  1.00 73.83      B    C  
ANISOU 3759  CB  THR B  61    12742   8263   7045  -4547   2554   -588  B    C  
ATOM   3760  CG2 THR B  61      16.634  12.712 427.603  1.00 76.85      B    C  
ANISOU 3760  CG2 THR B  61    13248   8711   7242  -4805   2767   -453  B    C  
ATOM   3761  OG1 THR B  61      16.421  11.513 429.669  1.00 71.05      B    O  
ANISOU 3761  OG1 THR B  61    12015   7769   7211  -4255   2578   -673  B    O  
ATOM   3762  N   ILE B  62      13.121  11.241 430.409  1.00 69.93      B    N  
ANISOU 3762  N   ILE B  62    12085   7577   6908  -4003   1635   -403  B    N  
ATOM   3763  CA  ILE B  62      12.222  10.297 431.066  1.00 70.29      B    C  
ANISOU 3763  CA  ILE B  62    12050   7558   7098  -3798   1456   -515  B    C  
ATOM   3764  C   ILE B  62      10.792  10.537 430.586  1.00 76.18      B    C  
ANISOU 3764  C   ILE B  62    13020   8374   7549  -3892   1093   -333  B    C  
ATOM   3765  O   ILE B  62      10.170  11.541 430.944  1.00 69.03      B    O  
ANISOU 3765  O   ILE B  62    12117   7420   6690  -3831    775    -46  B    O  
ATOM   3766  CB  ILE B  62      12.309  10.426 432.590  1.00 60.14      B    C  
ANISOU 3766  CB  ILE B  62    10463   6103   6286  -3470   1314   -473  B    C  
ATOM   3767  CG1 ILE B  62      13.758  10.285 433.072  1.00 60.23      B    C  
ANISOU 3767  CG1 ILE B  62    10226   6063   6593  -3384   1631   -620  B    C  
ATOM   3768  CG2 ILE B  62      11.411   9.419 433.241  1.00 57.99      B    C  
ANISOU 3768  CG2 ILE B  62    10122   5758   6153  -3271   1168   -587  B    C  
ATOM   3769  CD1 ILE B  62      14.475   9.063 432.570  1.00 62.12      B    C  
ANISOU 3769  CD1 ILE B  62    10438   6343   6823  -3430   2024   -932  B    C  
ATOM   3770  N   HIS B  63      10.239   9.589 429.823  1.00 80.76      B    N  
ANISOU 3770  N   HIS B  63    13772   9059   7854  -4033   1132   -507  B    N  
ATOM   3771  CA  HIS B  63       8.837   9.656 429.419  1.00 78.65      B    C  
ANISOU 3771  CA  HIS B  63    13676   8871   7337  -4113    766   -362  B    C  
ATOM   3772  C   HIS B  63       8.004   8.547 430.058  1.00 71.99      B    C  
ANISOU 3772  C   HIS B  63    12721   7951   6682  -3938    657   -538  B    C  
ATOM   3773  O   HIS B  63       7.086   8.836 430.834  1.00 68.52      B    O  
ANISOU 3773  O   HIS B  63    12172   7423   6439  -3755    331   -372  B    O  
ATOM   3774  CB  HIS B  63       8.688   9.597 427.896  1.00 70.34      B    C  
ANISOU 3774  CB  HIS B  63    12957   8035   5735  -4477    827   -379  B    C  
ATOM   3775  CG  HIS B  63       9.113  10.842 427.172  1.00 83.47      B    C  
ANISOU 3775  CG  HIS B  63    14790   9785   7140  -4673    824   -110  B    C  
ATOM   3776  CD2 HIS B  63       8.386  11.855 426.641  1.00 82.81      B    C  
ANISOU 3776  CD2 HIS B  63    14884   9784   6795  -4796    499    236  B    C  
ATOM   3777  ND1 HIS B  63      10.432  11.130 426.883  1.00 84.02      B    N  
ANISOU 3777  ND1 HIS B  63    14860   9858   7206  -4771   1201   -179  B    N  
ATOM   3778  CE1 HIS B  63      10.498  12.264 426.207  1.00 83.17      B    C  
ANISOU 3778  CE1 HIS B  63    14939   9827   6835  -4957   1120    108  B    C  
ATOM   3779  NE2 HIS B  63       9.270  12.725 426.047  1.00 83.34      B    N  
ANISOU 3779  NE2 HIS B  63    15076   9895   6693  -4969    691    372  B    N  
ATOM   3780  N   GLU B  64       8.296   7.276 429.765  1.00 65.18      B    N  
ANISOU 3780  N   GLU B  64    11880   7103   5783  -3990    943   -875  B    N  
ATOM   3781  CA  GLU B  64       7.659   6.164 430.456  1.00 76.57      B    C  
ANISOU 3781  CA  GLU B  64    13199   8437   7459  -3811    901  -1061  B    C  
ATOM   3782  C   GLU B  64       8.571   5.671 431.579  1.00 70.67      B    C  
ANISOU 3782  C   GLU B  64    12174   7507   7171  -3523   1145  -1203  B    C  
ATOM   3783  O   GLU B  64       9.707   6.128 431.740  1.00 61.01      B    O  
ANISOU 3783  O   GLU B  64    10850   6261   6070  -3486   1350  -1185  B    O  
ATOM   3784  CB  GLU B  64       7.331   5.004 429.501  1.00 80.88      B    C  
ANISOU 3784  CB  GLU B  64    13940   9081   7710  -4038   1058  -1352  B    C  
ATOM   3785  CG  GLU B  64       6.599   5.364 428.221  1.00 87.11      B    C  
ANISOU 3785  CG  GLU B  64    15031  10093   7972  -4376    860  -1255  B    C  
ATOM   3786  CD  GLU B  64       7.541   5.433 427.026  1.00112.85      B    C  
ANISOU 3786  CD  GLU B  64    18522  13502  10855  -4674   1195  -1372  B    C  
ATOM   3787  OE1 GLU B  64       8.458   4.588 426.954  1.00118.04      B    O  
ANISOU 3787  OE1 GLU B  64    19144  14097  11607  -4674   1626  -1680  B    O  
ATOM   3788  OE2 GLU B  64       7.384   6.334 426.170  1.00125.74      B    O1-
ANISOU 3788  OE2 GLU B  64    20367  15302  12106  -4901   1043  -1149  B    O1-
ATOM   3789  N   LEU B  65       8.082   4.664 432.315  1.00 64.03      B    N  
ANISOU 3789  N   LEU B  65    11211   6538   6578  -3333   1133  -1354  B    N  
ATOM   3790  CA  LEU B  65       8.889   4.027 433.352  1.00 60.11      B    C  
ANISOU 3790  CA  LEU B  65    10465   5873   6502  -3057   1358  -1491  B    C  
ATOM   3791  C   LEU B  65      10.133   3.377 432.774  1.00 68.37      B    C  
ANISOU 3791  C   LEU B  65    11510   6933   7533  -3145   1817  -1747  B    C  
ATOM   3792  O   LEU B  65      11.201   3.405 433.392  1.00 77.25      B    O  
ANISOU 3792  O   LEU B  65    12423   7978   8952  -2974   2010  -1769  B    O  
ATOM   3793  CB  LEU B  65       8.063   2.961 434.068  1.00 63.41      B    C  
ANISOU 3793  CB  LEU B  65    10803   6156   7134  -2877   1290  -1612  B    C  
ATOM   3794  CG  LEU B  65       8.712   2.305 435.285  1.00 60.52      B    C  
ANISOU 3794  CG  LEU B  65    10181   5602   7212  -2557   1455  -1698  B    C  
ATOM   3795  CD1 LEU B  65       9.077   3.357 436.344  1.00 59.90      B    C  
ANISOU 3795  CD1 LEU B  65     9916   5474   7369  -2349   1271  -1450  B    C  
ATOM   3796  CD2 LEU B  65       7.840   1.185 435.839  1.00 52.64      B    C  
ANISOU 3796  CD2 LEU B  65     9151   4468   6383  -2420   1418  -1822  B    C  
ATOM   3797  N   SER B  66      10.015   2.792 431.584  1.00 70.07      B    N  
ANISOU 3797  N   SER B  66    11957   7254   7412  -3417   2001  -1946  B    N  
ATOM   3798  CA  SER B  66      11.130   2.055 431.011  1.00 65.55      B    C  
ANISOU 3798  CA  SER B  66    11393   6673   6840  -3502   2482  -2226  B    C  
ATOM   3799  C   SER B  66      12.331   2.953 430.733  1.00 83.45      B    C  
ANISOU 3799  C   SER B  66    13609   9009   9088  -3571   2666  -2133  B    C  
ATOM   3800  O   SER B  66      13.466   2.466 430.715  1.00100.65      B    O  
ANISOU 3800  O   SER B  66    15657  11130  11457  -3520   3058  -2317  B    O  
ATOM   3801  CB  SER B  66      10.648   1.332 429.757  1.00 82.96      B    C  
ANISOU 3801  CB  SER B  66    13898   8987   8637  -3817   2620  -2461  B    C  
ATOM   3802  OG  SER B  66       9.756   2.157 429.024  1.00 87.77      B    O  
ANISOU 3802  OG  SER B  66    14744   9782   8822  -4060   2284  -2262  B    O  
ATOM   3803  N   ASP B  67      12.113   4.262 430.529  1.00 82.03      B    N  
ANISOU 3803  N   ASP B  67    13515   8940   8714  -3679   2400  -1844  B    N  
ATOM   3804  CA  ASP B  67      13.231   5.171 430.267  1.00 67.61      B    C  
ANISOU 3804  CA  ASP B  67    11643   7169   6877  -3763   2576  -1746  B    C  
ATOM   3805  C   ASP B  67      14.185   5.270 431.452  1.00 77.39      B    C  
ANISOU 3805  C   ASP B  67    12525   8269   8612  -3469   2663  -1724  B    C  
ATOM   3806  O   ASP B  67      15.372   5.552 431.265  1.00 80.67      B    O  
ANISOU 3806  O   ASP B  67    12833   8702   9117  -3514   2949  -1766  B    O  
ATOM   3807  CB  ASP B  67      12.716   6.568 429.906  1.00 67.64      B    C  
ANISOU 3807  CB  ASP B  67    11809   7284   6608  -3916   2250  -1414  B    C  
ATOM   3808  CG  ASP B  67      11.850   6.577 428.656  1.00 97.15      B    C  
ANISOU 3808  CG  ASP B  67    15902  11192   9818  -4230   2139  -1396  B    C  
ATOM   3809  OD1 ASP B  67      12.145   5.833 427.686  1.00 93.82      B    O  
ANISOU 3809  OD1 ASP B  67    15660  10857   9131  -4449   2450  -1648  B    O  
ATOM   3810  OD2 ASP B  67      10.853   7.326 428.654  1.00 99.31      B    O1-
ANISOU 3810  OD2 ASP B  67    16274  11514   9944  -4257   1735  -1129  B    O1-
ATOM   3811  N   ILE B  68      13.694   5.046 432.671  1.00 62.19      B    N  
ANISOU 3811  N   ILE B  68    10410   6213   7006  -3176   2421  -1658  B    N  
ATOM   3812  CA  ILE B  68      14.557   5.099 433.853  1.00 65.35      B    C  
ANISOU 3812  CA  ILE B  68    10477   6497   7855  -2897   2465  -1632  B    C  
ATOM   3813  C   ILE B  68      15.693   4.082 433.768  1.00 70.24      B    C  
ANISOU 3813  C   ILE B  68    10929   7061   8696  -2828   2908  -1898  B    C  
ATOM   3814  O   ILE B  68      16.808   4.323 434.261  1.00 62.41      B    O  
ANISOU 3814  O   ILE B  68     9681   6041   7991  -2713   3050  -1887  B    O  
ATOM   3815  CB  ILE B  68      13.698   4.932 435.130  1.00 56.81      B    C  
ANISOU 3815  CB  ILE B  68     9272   5291   7021  -2614   2132  -1526  B    C  
ATOM   3816  CG1 ILE B  68      12.795   6.156 435.297  1.00 55.17      B    C  
ANISOU 3816  CG1 ILE B  68     9173   5120   6666  -2662   1729  -1239  B    C  
ATOM   3817  CG2 ILE B  68      14.543   4.704 436.364  1.00 55.29      B    C  
ANISOU 3817  CG2 ILE B  68     8753   4984   7271  -2318   2187  -1535  B    C  
ATOM   3818  CD1 ILE B  68      11.494   5.862 435.855  1.00 52.98      B    C  
ANISOU 3818  CD1 ILE B  68     8938   4774   6419  -2535   1434  -1176  B    C  
ATOM   3819  N   LYS B  69      15.440   2.936 433.146  1.00 74.89      B    N  
ANISOU 3819  N   LYS B  69    11650   7629   9177  -2900   3136  -2145  B    N  
ATOM   3820  CA  LYS B  69      16.494   1.941 433.002  1.00 75.35      B    C  
ANISOU 3820  CA  LYS B  69    11557   7610   9462  -2833   3591  -2406  B    C  
ATOM   3821  C   LYS B  69      17.662   2.490 432.200  1.00 80.79      B    C  
ANISOU 3821  C   LYS B  69    12233   8401  10064  -3031   3914  -2447  B    C  
ATOM   3822  O   LYS B  69      18.822   2.153 432.463  1.00 75.46      B    O  
ANISOU 3822  O   LYS B  69    11293   7662   9715  -2905   4217  -2552  B    O  
ATOM   3823  CB  LYS B  69      15.935   0.677 432.354  1.00 67.88      B    C  
ANISOU 3823  CB  LYS B  69    10804   6614   8372  -2922   3795  -2679  B    C  
ATOM   3824  CG  LYS B  69      16.906  -0.465 432.372  1.00 69.97      B    C  
ANISOU 3824  CG  LYS B  69    10894   6744   8946  -2795   4259  -2946  B    C  
ATOM   3825  CD  LYS B  69      16.279  -1.725 431.829  1.00 81.21      B    C  
ANISOU 3825  CD  LYS B  69    12515   8085  10255  -2875   4452  -3224  B    C  
ATOM   3826  CE  LYS B  69      17.295  -2.849 431.802  1.00 93.49      B    C  
ANISOU 3826  CE  LYS B  69    13897   9478  12146  -2744   4958  -3493  B    C  
ATOM   3827  NZ  LYS B  69      16.643  -4.182 431.765  1.00 97.37      B    N1+
ANISOU 3827  NZ  LYS B  69    14432   9862  12702  -2682   5012  -3625  B    N1+
ATOM   3828  N   GLN B  70      17.369   3.315 431.202  1.00 70.60      B    N  
ANISOU 3828  N   GLN B  70    11221   7266   8338  -3343   3860  -2359  B    N  
ATOM   3829  CA  GLN B  70      18.377   3.938 430.368  1.00 73.59      B    C  
ANISOU 3829  CA  GLN B  70    11634   7748   8579  -3570   4159  -2373  B    C  
ATOM   3830  C   GLN B  70      19.027   5.145 431.021  1.00 72.25      B    C  
ANISOU 3830  C   GLN B  70    11243   7591   8618  -3495   4007  -2128  B    C  
ATOM   3831  O   GLN B  70      20.071   5.599 430.546  1.00 88.24      B    O  
ANISOU 3831  O   GLN B  70    13202   9670  10655  -3633   4294  -2150  B    O  
ATOM   3832  CB  GLN B  70      17.717   4.314 429.049  1.00 85.07      B    C  
ANISOU 3832  CB  GLN B  70    13507   9364   9452  -3940   4138  -2355  B    C  
ATOM   3833  CG  GLN B  70      16.399   3.553 428.863  1.00 93.61      B    C  
ANISOU 3833  CG  GLN B  70    14812  10444  10311  -3968   3931  -2438  B    C  
ATOM   3834  CD  GLN B  70      16.577   2.096 428.424  1.00 87.95      B    C  
ANISOU 3834  CD  GLN B  70    14143   9654   9619  -3991   4327  -2813  B    C  
ATOM   3835  NE2 GLN B  70      15.474   1.469 428.003  1.00 86.48      B    N  
ANISOU 3835  NE2 GLN B  70    14203   9495   9161  -4107   4194  -2919  B    N  
ATOM   3836  OE1 GLN B  70      17.668   1.528 428.519  1.00 78.98      B    O  
ANISOU 3836  OE1 GLN B  70    12806   8426   8777  -3893   4738  -3003  B    O  
ATOM   3837  N   ALA B  71      18.461   5.657 432.104  1.00 79.46      B    N  
ANISOU 3837  N   ALA B  71    12037   8448   9705  -3289   3587  -1912  B    N  
ATOM   3838  CA  ALA B  71      18.962   6.882 432.704  1.00 86.04      B    C  
ANISOU 3838  CA  ALA B  71    12701   9291  10698  -3252   3414  -1683  B    C  
ATOM   3839  C   ALA B  71      20.127   6.594 433.651  1.00 83.10      B    C  
ANISOU 3839  C   ALA B  71    11915   8838  10821  -3010   3565  -1755  B    C  
ATOM   3840  O   ALA B  71      20.364   5.458 434.080  1.00 79.73      B    O  
ANISOU 3840  O   ALA B  71    11316   8322  10654  -2803   3715  -1929  B    O  
ATOM   3841  CB  ALA B  71      17.850   7.633 433.443  1.00 84.09      B    C  
ANISOU 3841  CB  ALA B  71    12520   9014  10416  -3153   2912  -1427  B    C  
ATOM   3842  N   ASN B  72      20.844   7.665 433.979  1.00 75.67      B    N  
ANISOU 3842  N   ASN B  72    10814   7925  10013  -3044   3510  -1605  B    N  
ATOM   3843  CA  ASN B  72      21.936   7.694 434.938  1.00 75.17      B    C  
ANISOU 3843  CA  ASN B  72    10343   7816  10402  -2846   3563  -1617  B    C  
ATOM   3844  C   ASN B  72      21.482   8.421 436.200  1.00 76.29      B    C  
ANISOU 3844  C   ASN B  72    10375   7908  10702  -2667   3113  -1406  B    C  
ATOM   3845  O   ASN B  72      20.660   9.336 436.134  1.00 83.77      B    O  
ANISOU 3845  O   ASN B  72    11542   8868  11419  -2774   2835  -1221  B    O  
ATOM   3846  CB  ASN B  72      23.140   8.408 434.316  1.00 75.60      B    C  
ANISOU 3846  CB  ASN B  72    10293   7946  10485  -3062   3861  -1628  B    C  
ATOM   3847  CG  ASN B  72      24.334   8.452 435.234  1.00 86.26      B    C  
ANISOU 3847  CG  ASN B  72    11193   9272  12312  -2885   3917  -1647  B    C  
ATOM   3848  ND2 ASN B  72      25.153   9.488 435.085  1.00 88.03      B    N  
ANISOU 3848  ND2 ASN B  72    11304   9550  12592  -3056   3991  -1565  B    N  
ATOM   3849  OD1 ASN B  72      24.524   7.570 436.067  1.00 97.18      B    O  
ANISOU 3849  OD1 ASN B  72    12327  10586  14011  -2603   3891  -1726  B    O  
ATOM   3850  N   ILE B  73      21.982   7.996 437.366  1.00 62.63      B    N  
ANISOU 3850  N   ILE B  73     8316   6117   9365  -2391   3037  -1430  B    N  
ATOM   3851  CA  ILE B  73      21.460   8.595 438.594  1.00 59.55      B    C  
ANISOU 3851  CA  ILE B  73     7860   5678   9089  -2224   2616  -1252  B    C  
ATOM   3852  C   ILE B  73      21.919  10.041 438.749  1.00 79.13      B    C  
ANISOU 3852  C   ILE B  73    10288   8200  11578  -2378   2492  -1097  B    C  
ATOM   3853  O   ILE B  73      21.207  10.866 439.341  1.00 68.80      B    O  
ANISOU 3853  O   ILE B  73     9080   6853  10210  -2359   2159   -929  B    O  
ATOM   3854  CB  ILE B  73      21.831   7.767 439.839  1.00 63.30      B    C  
ANISOU 3854  CB  ILE B  73     8022   6087   9942  -1894   2539  -1300  B    C  
ATOM   3855  CG1 ILE B  73      23.335   7.796 440.085  1.00 65.08      B    C  
ANISOU 3855  CG1 ILE B  73     7870   6359  10499  -1860   2737  -1361  B    C  
ATOM   3856  CG2 ILE B  73      21.335   6.351 439.705  1.00 77.43      B    C  
ANISOU 3856  CG2 ILE B  73     9877   7804  11739  -1742   2671  -1443  B    C  
ATOM   3857  CD1 ILE B  73      23.789   6.794 441.133  1.00 69.32      B    C  
ANISOU 3857  CD1 ILE B  73     8093   6842  11405  -1532   2710  -1411  B    C  
ATOM   3858  N   ASN B  74      23.083  10.395 438.198  1.00 76.42      B    N  
ANISOU 3858  N   ASN B  74     9798   7922  11315  -2544   2775  -1153  B    N  
ATOM   3859  CA  ASN B  74      23.504  11.788 438.265  1.00 70.61      B    C  
ANISOU 3859  CA  ASN B  74     9034   7212  10583  -2722   2683  -1012  B    C  
ATOM   3860  C   ASN B  74      22.560  12.677 437.477  1.00 67.29      B    C  
ANISOU 3860  C   ASN B  74     9005   6790   9773  -2948   2572   -854  B    C  
ATOM   3861  O   ASN B  74      22.437  13.870 437.772  1.00 87.72      B    O  
ANISOU 3861  O   ASN B  74    11638   9345  12345  -3039   2373   -686  B    O  
ATOM   3862  CB  ASN B  74      24.933  11.933 437.750  1.00 82.56      B    C  
ANISOU 3862  CB  ASN B  74    10309   8794  12265  -2873   3046  -1112  B    C  
ATOM   3863  CG  ASN B  74      25.929  11.128 438.564  1.00 93.74      B    C  
ANISOU 3863  CG  ASN B  74    11291  10216  14110  -2639   3133  -1240  B    C  
ATOM   3864  ND2 ASN B  74      27.216  11.423 438.378  1.00106.78      B    N  
ANISOU 3864  ND2 ASN B  74    12656  11925  15990  -2747   3380  -1301  B    N  
ATOM   3865  OD1 ASN B  74      25.550  10.252 439.352  1.00 82.56      B    O  
ANISOU 3865  OD1 ASN B  74     9789   8752  12829  -2363   2980  -1272  B    O  
ATOM   3866  N   SER B  75      21.877  12.111 436.485  1.00 63.44      B    N  
ANISOU 3866  N   SER B  75     8801   6331   8974  -3041   2689   -901  B    N  
ATOM   3867  CA  SER B  75      20.864  12.853 435.757  1.00 63.24      B    C  
ANISOU 3867  CA  SER B  75     9146   6315   8568  -3230   2535   -729  B    C  
ATOM   3868  C   SER B  75      19.604  13.044 436.584  1.00 72.41      B    C  
ANISOU 3868  C   SER B  75    10405   7392   9715  -3054   2114   -586  B    C  
ATOM   3869  O   SER B  75      18.822  13.954 436.292  1.00 89.34      B    O  
ANISOU 3869  O   SER B  75    12783   9515  11646  -3171   1912   -387  B    O  
ATOM   3870  CB  SER B  75      20.523  12.143 434.451  1.00 71.96      B    C  
ANISOU 3870  CB  SER B  75    10520   7498   9324  -3397   2772   -836  B    C  
ATOM   3871  OG  SER B  75      21.692  11.931 433.672  1.00 99.05      B    O  
ANISOU 3871  OG  SER B  75    13869  10998  12768  -3561   3205   -986  B    O  
ATOM   3872  N   LEU B  76      19.386  12.202 437.599  1.00 71.52      B    N  
ANISOU 3872  N   LEU B  76    10119   7223   9833  -2775   1991   -674  B    N  
ATOM   3873  CA  LEU B  76      18.144  12.200 438.364  1.00 54.68      B    C  
ANISOU 3873  CA  LEU B  76     8081   5006   7688  -2601   1637   -567  B    C  
ATOM   3874  C   LEU B  76      18.268  12.832 439.743  1.00 62.05      B    C  
ANISOU 3874  C   LEU B  76     8822   5859   8896  -2432   1387   -477  B    C  
ATOM   3875  O   LEU B  76      17.331  13.501 440.192  1.00 50.87      B    O  
ANISOU 3875  O   LEU B  76     7534   4367   7427  -2393   1104   -321  B    O  
ATOM   3876  CB  LEU B  76      17.634  10.763 438.528  1.00 61.29      B    C  
ANISOU 3876  CB  LEU B  76     8911   5823   8553  -2416   1672   -723  B    C  
ATOM   3877  CG  LEU B  76      17.655   9.868 437.284  1.00 61.17      B    C  
ANISOU 3877  CG  LEU B  76     9049   5880   8313  -2563   1969   -887  B    C  
ATOM   3878  CD1 LEU B  76      17.529   8.413 437.674  1.00 64.75      B    C  
ANISOU 3878  CD1 LEU B  76     9401   6279   8923  -2349   2066  -1075  B    C  
ATOM   3879  CD2 LEU B  76      16.545  10.242 436.305  1.00 56.34      B    C  
ANISOU 3879  CD2 LEU B  76     8790   5318   7300  -2767   1846   -778  B    C  
ATOM   3880  N   LEU B  77      19.372  12.692 440.378  1.00 73.82      B    N  
ANISOU 3880  N   LEU B  77    10019   7365  10665  -2347   1482   -566  B    N  
ATOM   3881  CA  LEU B  77      19.575  13.121 441.753  1.00 63.15      B    C  
ANISOU 3881  CA  LEU B  77     8469   5958   9567  -2183   1249   -515  B    C  
ATOM   3882  C   LEU B  77      20.303  14.457 441.833  1.00 52.94      B    C  
ANISOU 3882  C   LEU B  77     7103   4670   8343  -2363   1231   -430  B    C  
ATOM   3883  O   LEU B  77      21.116  14.786 440.967  1.00 55.45      B    O  
ANISOU 3883  O   LEU B  77     7394   5051   8623  -2573   1477   -457  B    O  
ATOM   3884  CB  LEU B  77      20.379  12.072 442.519  1.00 51.87      B    C  
ANISOU 3884  CB  LEU B  77     6729   4555   8426  -1961   1329   -659  B    C  
ATOM   3885  CG  LEU B  77      19.657  10.749 442.692  1.00 50.52      B    C  
ANISOU 3885  CG  LEU B  77     6610   4341   8244  -1749   1327   -737  B    C  
ATOM   3886  CD1 LEU B  77      20.174  10.059 443.926  1.00 52.42      B    C  
ANISOU 3886  CD1 LEU B  77     6567   4565   8787  -1479   1250   -785  B    C  
ATOM   3887  CD2 LEU B  77      18.146  10.966 442.812  1.00 48.12      B    C  
ANISOU 3887  CD2 LEU B  77     6588   3958   7738  -1721   1077   -624  B    C  
ATOM   3888  N   PRO B  78      20.008  15.250 442.853  1.00 51.41      B    N  
ANISOU 3888  N   PRO B  78     6888   4399   8248  -2298    960   -334  B    N  
ATOM   3889  CA  PRO B  78      20.780  16.475 443.084  1.00 52.74      B    C  
ANISOU 3889  CA  PRO B  78     6955   4555   8528  -2463    943   -281  B    C  
ATOM   3890  C   PRO B  78      22.192  16.133 443.534  1.00 54.43      B    C  
ANISOU 3890  C   PRO B  78     6800   4863   9018  -2433   1069   -418  B    C  
ATOM   3891  O   PRO B  78      22.450  15.058 444.067  1.00 54.00      B    O  
ANISOU 3891  O   PRO B  78     6556   4853   9110  -2221   1075   -521  B    O  
ATOM   3892  CB  PRO B  78      20.000  17.188 444.198  1.00 50.57      B    C  
ANISOU 3892  CB  PRO B  78     6756   4161   8297  -2362    619   -181  B    C  
ATOM   3893  CG  PRO B  78      18.638  16.560 444.195  1.00 50.67      B    C  
ANISOU 3893  CG  PRO B  78     6980   4116   8155  -2202    490   -133  B    C  
ATOM   3894  CD  PRO B  78      18.865  15.133 443.770  1.00 48.61      B    C  
ANISOU 3894  CD  PRO B  78     6637   3948   7886  -2098    673   -269  B    C  
ATOM   3895  N   GLU B  79      23.125  17.062 443.297  1.00 63.66      B    N  
ANISOU 3895  N   GLU B  79     7857   6057  10276  -2651   1177   -410  B    N  
ATOM   3896  CA  GLU B  79      24.511  16.847 443.720  1.00 58.65      B    C  
ANISOU 3896  CA  GLU B  79     6833   5520   9933  -2645   1284   -532  B    C  
ATOM   3897  C   GLU B  79      24.614  16.600 445.224  1.00 58.03      B    C  
ANISOU 3897  C   GLU B  79     6538   5447  10062  -2418    999   -563  B    C  
ATOM   3898  O   GLU B  79      25.324  15.687 445.675  1.00 59.80      B    O  
ANISOU 3898  O   GLU B  79     6469   5759  10494  -2252   1036   -660  B    O  
ATOM   3899  CB  GLU B  79      25.371  18.051 443.333  1.00 80.67      B    C  
ANISOU 3899  CB  GLU B  79     9550   8314  12787  -2937   1406   -505  B    C  
ATOM   3900  CG  GLU B  79      25.947  18.042 441.912  1.00 93.91      B    C  
ANISOU 3900  CG  GLU B  79    11270  10045  14366  -3163   1790   -531  B    C  
ATOM   3901  CD  GLU B  79      26.748  19.319 441.584  1.00103.19      B    C  
ANISOU 3901  CD  GLU B  79    12390  11203  15613  -3466   1910   -486  B    C  
ATOM   3902  OE1 GLU B  79      26.473  20.396 442.176  1.00 98.12      B    O  
ANISOU 3902  OE1 GLU B  79    11825  10463  14991  -3541   1690   -393  B    O  
ATOM   3903  OE2 GLU B  79      27.654  19.241 440.728  1.00109.66      B    O1-
ANISOU 3903  OE2 GLU B  79    13094  12095  16477  -3635   2246   -552  B    O1-
ATOM   3904  N   HIS B  80      23.932  17.425 446.024  1.00 67.63      B    N  
ANISOU 3904  N   HIS B  80     7897   6570  11230  -2412    719   -478  B    N  
ATOM   3905  CA  HIS B  80      24.077  17.303 447.470  1.00 66.68      B    C  
ANISOU 3905  CA  HIS B  80     7596   6466  11273  -2235    451   -512  B    C  
ATOM   3906  C   HIS B  80      23.548  15.963 447.969  1.00 56.37      B    C  
ANISOU 3906  C   HIS B  80     6277   5176   9967  -1928    375   -537  B    C  
ATOM   3907  O   HIS B  80      24.121  15.371 448.887  1.00 53.37      B    O  
ANISOU 3907  O   HIS B  80     5639   4872   9768  -1758    267   -589  B    O  
ATOM   3908  CB  HIS B  80      23.396  18.467 448.191  1.00 66.89      B    C  
ANISOU 3908  CB  HIS B  80     7814   6370  11232  -2303    203   -434  B    C  
ATOM   3909  CG  HIS B  80      23.825  18.612 449.621  1.00 81.55      B    C  
ANISOU 3909  CG  HIS B  80     9472   8267  13247  -2214    -46   -490  B    C  
ATOM   3910  CD2 HIS B  80      24.489  19.607 450.259  1.00 89.33      B    C  
ANISOU 3910  CD2 HIS B  80    10331   9259  14350  -2377   -160   -528  B    C  
ATOM   3911  ND1 HIS B  80      23.593  17.637 450.572  1.00 82.02      B    N  
ANISOU 3911  ND1 HIS B  80     9449   8371  13343  -1941   -210   -515  B    N  
ATOM   3912  CE1 HIS B  80      24.090  18.029 451.733  1.00 82.21      B    C  
ANISOU 3912  CE1 HIS B  80     9314   8444  13477  -1938   -428   -558  B    C  
ATOM   3913  NE2 HIS B  80      24.636  19.222 451.571  1.00 85.34      B    N  
ANISOU 3913  NE2 HIS B  80     9679   8821  13927  -2206   -405   -578  B    N  
ATOM   3914  N   LEU B  81      22.458  15.467 447.381  1.00 51.20      B    N  
ANISOU 3914  N   LEU B  81     5894   4449   9112  -1859    423   -493  B    N  
ATOM   3915  CA  LEU B  81      21.937  14.167 447.794  1.00 49.67      B    C  
ANISOU 3915  CA  LEU B  81     5696   4250   8927  -1584    382   -523  B    C  
ATOM   3916  C   LEU B  81      22.931  13.047 447.490  1.00 51.55      B    C  
ANISOU 3916  C   LEU B  81     5657   4587   9343  -1488    606   -631  B    C  
ATOM   3917  O   LEU B  81      23.119  12.135 448.300  1.00 54.51      B    O  
ANISOU 3917  O   LEU B  81     5859   4984   9867  -1248    529   -658  B    O  
ATOM   3918  CB  LEU B  81      20.597  13.897 447.117  1.00 47.80      B    C  
ANISOU 3918  CB  LEU B  81     5793   3922   8449  -1569    404   -468  B    C  
ATOM   3919  CG  LEU B  81      20.036  12.554 447.560  1.00 46.35      B    C  
ANISOU 3919  CG  LEU B  81     5609   3713   8288  -1300    375   -507  B    C  
ATOM   3920  CD1 LEU B  81      19.977  12.507 449.075  1.00 45.22      B    C  
ANISOU 3920  CD1 LEU B  81     5362   3551   8270  -1103    115   -480  B    C  
ATOM   3921  CD2 LEU B  81      18.664  12.298 446.939  1.00 50.22      B    C  
ANISOU 3921  CD2 LEU B  81     6411   4118   8552  -1299    372   -461  B    C  
ATOM   3922  N   ILE B  82      23.581  13.111 446.329  1.00 53.67      B    N  
ANISOU 3922  N   ILE B  82     5881   4906   9604  -1672    899   -686  B    N  
ATOM   3923  CA  ILE B  82      24.548  12.093 445.937  1.00 55.84      B    C  
ANISOU 3923  CA  ILE B  82     5891   5257  10070  -1595   1165   -800  B    C  
ATOM   3924  C   ILE B  82      25.743  12.088 446.891  1.00 67.58      B    C  
ANISOU 3924  C   ILE B  82     6967   6835  11875  -1505   1070   -826  B    C  
ATOM   3925  O   ILE B  82      26.176  11.030 447.376  1.00 74.62      B    O  
ANISOU 3925  O   ILE B  82     7623   7757  12972  -1269   1088   -866  B    O  
ATOM   3926  CB  ILE B  82      24.992  12.333 444.485  1.00 58.04      B    C  
ANISOU 3926  CB  ILE B  82     6234   5569  10251  -1850   1514   -856  B    C  
ATOM   3927  CG1 ILE B  82      23.780  12.332 443.553  1.00 56.62      B    C  
ANISOU 3927  CG1 ILE B  82     6466   5322   9726  -1946   1565   -816  B    C  
ATOM   3928  CG2 ILE B  82      26.016  11.288 444.076  1.00 60.60      B    C  
ANISOU 3928  CG2 ILE B  82     6272   5954  10798  -1770   1830   -992  B    C  
ATOM   3929  CD1 ILE B  82      24.121  12.479 442.085  1.00 58.95      B    C  
ANISOU 3929  CD1 ILE B  82     6878   5659   9862  -2202   1909   -866  B    C  
ATOM   3930  N   SER B  83      26.327  13.264 447.141  1.00 58.68      B    N  
ANISOU 3930  N   SER B  83     5737   5752  10806  -1699    973   -801  B    N  
ATOM   3931  CA  SER B  83      27.467  13.300 448.054  1.00 76.84      B    C  
ANISOU 3931  CA  SER B  83     7632   8161  13403  -1638    851   -828  B    C  
ATOM   3932  C   SER B  83      27.046  12.870 449.455  1.00 70.71      B    C  
ANISOU 3932  C   SER B  83     6824   7382  12661  -1377    508   -774  B    C  
ATOM   3933  O   SER B  83      27.779  12.142 450.146  1.00 70.14      B    O  
ANISOU 3933  O   SER B  83     6430   7396  12825  -1185    439   -787  B    O  
ATOM   3934  CB  SER B  83      28.126  14.692 448.070  1.00 72.73      B    C  
ANISOU 3934  CB  SER B  83     7022   7680  12930  -1927    805   -825  B    C  
ATOM   3935  OG  SER B  83      27.190  15.756 448.138  1.00 76.06      B    O  
ANISOU 3935  OG  SER B  83     7790   7995  13115  -2071    647   -749  B    O  
ATOM   3936  N   GLY B  84      25.859  13.308 449.885  1.00 56.16      B    N  
ANISOU 3936  N   GLY B  84     5312   5439  10586  -1364    297   -705  B    N  
ATOM   3937  CA  GLY B  84      25.361  12.934 451.199  1.00 59.81      B    C  
ANISOU 3937  CA  GLY B  84     5794   5888  11042  -1133     -4   -653  B    C  
ATOM   3938  C   GLY B  84      25.179  11.439 451.363  1.00 62.79      B    C  
ANISOU 3938  C   GLY B  84     6110   6254  11495   -834     57   -651  B    C  
ATOM   3939  O   GLY B  84      25.544  10.875 452.398  1.00 70.15      B    O  
ANISOU 3939  O   GLY B  84     6843   7244  12566   -627   -121   -619  B    O  
ATOM   3940  N   LEU B  85      24.645  10.768 450.331  1.00 60.16      B    N  
ANISOU 3940  N   LEU B  85     5945   5843  11070   -815    313   -683  B    N  
ATOM   3941  CA  LEU B  85      24.481   9.314 450.402  1.00 64.69      B    C  
ANISOU 3941  CA  LEU B  85     6468   6377  11733   -546    415   -698  B    C  
ATOM   3942  C   LEU B  85      25.825   8.602 450.437  1.00 61.87      B    C  
ANISOU 3942  C   LEU B  85     5695   6114  11698   -433    555   -743  B    C  
ATOM   3943  O   LEU B  85      26.005   7.644 451.199  1.00 57.94      B    O  
ANISOU 3943  O   LEU B  85     5035   5615  11364   -163    475   -702  B    O  
ATOM   3944  CB  LEU B  85      23.656   8.806 449.217  1.00 57.58      B    C  
ANISOU 3944  CB  LEU B  85     5842   5378  10657   -595    672   -750  B    C  
ATOM   3945  CG  LEU B  85      22.141   8.993 449.281  1.00 49.14      B    C  
ANISOU 3945  CG  LEU B  85     5156   4196   9318   -595    531   -692  B    C  
ATOM   3946  CD1 LEU B  85      21.505   8.643 447.960  1.00 48.84      B    C  
ANISOU 3946  CD1 LEU B  85     5354   4103   9101   -709    779   -753  B    C  
ATOM   3947  CD2 LEU B  85      21.561   8.154 450.387  1.00 47.67      B    C  
ANISOU 3947  CD2 LEU B  85     4988   3946   9177   -312    353   -638  B    C  
ATOM   3948  N   ALA B  86      26.787   9.067 449.632  1.00 77.93      B    N  
ANISOU 3948  N   ALA B  86     7542   8224  13842   -634    769   -815  B    N  
ATOM   3949  CA  ALA B  86      28.110   8.451 449.649  1.00 71.20      B    C  
ANISOU 3949  CA  ALA B  86     6255   7462  13338   -532    916   -858  B    C  
ATOM   3950  C   ALA B  86      28.770   8.600 451.012  1.00 71.69      B    C  
ANISOU 3950  C   ALA B  86     6012   7635  13591   -402    576   -775  B    C  
ATOM   3951  O   ALA B  86      29.445   7.680 451.483  1.00 65.04      B    O  
ANISOU 3951  O   ALA B  86     4858   6834  13020   -163    572   -747  B    O  
ATOM   3952  CB  ALA B  86      28.992   9.060 448.560  1.00 73.43      B    C  
ANISOU 3952  CB  ALA B  86     6399   7805  13695   -804   1212   -951  B    C  
ATOM   3953  N   SER B  87      28.550   9.737 451.681  1.00 80.96      B    N  
ANISOU 3953  N   SER B  87     7285   8855  14622   -552    279   -731  B    N  
ATOM   3954  CA  SER B  87      29.215  10.016 452.953  1.00 86.10      B    C  
ANISOU 3954  CA  SER B  87     7664   9636  15414   -487    -60   -672  B    C  
ATOM   3955  C   SER B  87      28.624   9.259 454.150  1.00 79.26      B    C  
ANISOU 3955  C   SER B  87     6871   8747  14495   -191   -337   -565  B    C  
ATOM   3956  O   SER B  87      29.297   9.138 455.183  1.00 75.95      B    O  
ANISOU 3956  O   SER B  87     6180   8455  14224    -75   -597   -501  B    O  
ATOM   3957  CB  SER B  87      29.169  11.522 453.226  1.00 63.19      B    C  
ANISOU 3957  CB  SER B  87     4871   6772  12366   -778   -252   -688  B    C  
ATOM   3958  OG  SER B  87      29.140  11.782 454.619  1.00 63.13      B    O  
ANISOU 3958  OG  SER B  87     4824   6838  12325   -702   -644   -627  B    O  
ATOM   3959  N   ALA B  88      27.395   8.755 454.046  1.00 81.58      B    N  
ANISOU 3959  N   ALA B  88     7524   8892  14582    -75   -293   -539  B    N  
ATOM   3960  CA  ALA B  88      26.728   8.142 455.193  1.00 82.23      B    C  
ANISOU 3960  CA  ALA B  88     7723   8936  14583    177   -542   -434  B    C  
ATOM   3961  C   ALA B  88      27.327   6.774 455.494  1.00 91.65      B    C  
ANISOU 3961  C   ALA B  88     8635  10145  16042    487   -486   -371  B    C  
ATOM   3962  O   ALA B  88      27.379   5.898 454.619  1.00 96.71      B    O  
ANISOU 3962  O   ALA B  88     9241  10697  16808    576   -167   -420  B    O  
ATOM   3963  CB  ALA B  88      25.225   8.014 454.931  1.00 65.28      B    C  
ANISOU 3963  CB  ALA B  88     6024   6616  12164    194   -485   -430  B    C  
ATOM   3964  N   ILE B  89      27.787   6.588 456.728  1.00 85.92      B    N  
ANISOU 3964  N   ILE B  89     7715   9528  15402    648   -793   -260  B    N  
ATOM   3965  CA  ILE B  89      28.240   5.282 457.185  1.00 84.00      B    C  
ANISOU 3965  CA  ILE B  89     7232   9284  15401    978   -791   -152  B    C  
ATOM   3966  C   ILE B  89      27.196   4.626 458.078  1.00 76.51      B    C  
ANISOU 3966  C   ILE B  89     6568   8228  14273   1203   -951    -34  B    C  
ATOM   3967  O   ILE B  89      26.972   3.418 457.999  1.00 73.44      B    O  
ANISOU 3967  O   ILE B  89     6185   7716  14003   1455   -795     22  B    O  
ATOM   3968  CB  ILE B  89      29.606   5.395 457.905  1.00 82.69      B    C  
ANISOU 3968  CB  ILE B  89     6595   9329  15493   1026  -1022    -80  B    C  
ATOM   3969  CG1 ILE B  89      29.605   6.548 458.920  1.00 89.50      B    C  
ANISOU 3969  CG1 ILE B  89     7517  10341  16147    848  -1423    -59  B    C  
ATOM   3970  CG2 ILE B  89      30.736   5.585 456.893  1.00 71.02      B    C  
ANISOU 3970  CG2 ILE B  89     4759   7919  14305    887   -756   -188  B    C  
ATOM   3971  CD1 ILE B  89      30.926   6.740 459.639  1.00 79.96      B    C  
ANISOU 3971  CD1 ILE B  89     5847   9366  15167    855  -1691      1  B    C  
ATOM   3972  N   ARG B  90      26.514   5.432 458.885  1.00 69.56      B    N  
ANISOU 3972  N   ARG B  90     5945   7376  13110   1100  -1227     -8  B    N  
ATOM   3973  CA  ARG B  90      25.405   4.941 459.683  1.00 64.78      B    C  
ANISOU 3973  CA  ARG B  90     5654   6657  12301   1273  -1347     88  B    C  
ATOM   3974  C   ARG B  90      24.216   4.638 458.791  1.00 62.20      B    C  
ANISOU 3974  C   ARG B  90     5665   6121  11847   1248  -1067     12  B    C  
ATOM   3975  O   ARG B  90      23.925   5.379 457.851  1.00 68.10      B    O  
ANISOU 3975  O   ARG B  90     6541   6835  12499   1009   -917   -109  B    O  
ATOM   3976  CB  ARG B  90      25.028   5.972 460.734  1.00 63.95      B    C  
ANISOU 3976  CB  ARG B  90     5731   6635  11932   1140  -1683    109  B    C  
ATOM   3977  CG  ARG B  90      25.479   5.657 462.150  1.00 68.75      B    C  
ANISOU 3977  CG  ARG B  90     6209   7380  12534   1315  -2022    260  B    C  
ATOM   3978  CD  ARG B  90      25.524   6.955 462.914  1.00 79.90      B    C  
ANISOU 3978  CD  ARG B  90     7707   8922  13730   1079  -2316    210  B    C  
ATOM   3979  NE  ARG B  90      26.589   7.815 462.393  1.00 95.61      B    N  
ANISOU 3979  NE  ARG B  90     9403  11054  15871    840  -2321    104  B    N  
ATOM   3980  CZ  ARG B  90      26.547   9.147 462.370  1.00 97.15      B    C  
ANISOU 3980  CZ  ARG B  90     9700  11286  15925    535  -2403    -17  B    C  
ATOM   3981  NH1 ARG B  90      25.466   9.797 462.805  1.00 91.57      B    N1+
ANISOU 3981  NH1 ARG B  90     9386  10476  14929    439  -2476    -53  B    N1+
ATOM   3982  NH2 ARG B  90      27.578   9.832 461.885  1.00 92.82      B    N  
ANISOU 3982  NH2 ARG B  90     8859  10860  15548    326  -2386   -105  B    N  
ATOM   3983  N   GLU B  91      23.522   3.546 459.094  1.00 65.26      B    N  
ANISOU 3983  N   GLU B  91     6198   6369  12230   1489  -1006     92  B    N  
ATOM   3984  CA  GLU B  91      22.361   3.174 458.297  1.00 65.65      B    C  
ANISOU 3984  CA  GLU B  91     6555   6225  12166   1466   -759     18  B    C  
ATOM   3985  C   GLU B  91      21.098   3.882 458.774  1.00 56.51      B    C  
ANISOU 3985  C   GLU B  91     5766   5002  10704   1364   -909     23  B    C  
ATOM   3986  O   GLU B  91      21.013   4.386 459.896  1.00 74.01      B    O  
ANISOU 3986  O   GLU B  91     8039   7288  12794   1375  -1186     99  B    O  
ATOM   3987  CB  GLU B  91      22.144   1.665 458.333  1.00 62.20      B    C  
ANISOU 3987  CB  GLU B  91     6109   5639  11884   1752   -587     82  B    C  
ATOM   3988  CG  GLU B  91      23.240   0.880 457.632  1.00 64.60      B    C  
ANISOU 3988  CG  GLU B  91     6079   5950  12517   1854   -346     49  B    C  
ATOM   3989  CD  GLU B  91      22.918  -0.586 457.571  1.00 80.41      B    C  
ANISOU 3989  CD  GLU B  91     8224   7890  14438   1998   -126     87  B    C  
ATOM   3990  OE1 GLU B  91      21.742  -0.907 457.273  1.00 81.08      B    O  
ANISOU 3990  OE1 GLU B  91     8651   7882  14274   1934     -9     37  B    O  
ATOM   3991  OE2 GLU B  91      23.826  -1.410 457.838  1.00 88.92      B    O1-
ANISOU 3991  OE2 GLU B  91     9078   9031  15678   2160    -85    168  B    O1-
ATOM   3992  N   ASN B  92      20.127   3.967 457.872  1.00 49.40      B    N  
ANISOU 3992  N   ASN B  92     5113   3970   9686   1248   -719    -66  B    N  
ATOM   3993  CA  ASN B  92      18.764   4.389 458.203  1.00 50.78      B    C  
ANISOU 3993  CA  ASN B  92     5633   4038   9623   1196   -802    -55  B    C  
ATOM   3994  C   ASN B  92      18.719   5.806 458.799  1.00 49.36      B    C  
ANISOU 3994  C   ASN B  92     5531   3944   9278   1012  -1043    -56  B    C  
ATOM   3995  O   ASN B  92      17.843   6.119 459.604  1.00 56.47      B    O  
ANISOU 3995  O   ASN B  92     6657   4783  10016   1032  -1182    -13  B    O  
ATOM   3996  CB  ASN B  92      18.102   3.367 459.139  1.00 42.62      B    C  
ANISOU 3996  CB  ASN B  92     4740   2974   8479   1406   -819     52  B    C  
ATOM   3997  CG  ASN B  92      18.067   1.953 458.538  1.00 64.11      B    C  
ANISOU 3997  CG  ASN B  92     7450   5692  11218   1509   -534     41  B    C  
ATOM   3998  ND2 ASN B  92      18.696   0.999 459.229  1.00 77.76      B    N  
ANISOU 3998  ND2 ASN B  92     9046   7484  13016   1706   -544    143  B    N  
ATOM   3999  OD1 ASN B  92      17.514   1.728 457.467  1.00 50.27      B    O  
ANISOU 3999  OD1 ASN B  92     5810   3877   9413   1408   -324    -57  B    O  
ATOM   4000  N   GLU B  93      19.650   6.682 458.395  1.00 57.46      B    N  
ANISOU 4000  N   GLU B  93     6378   5099  10355    822  -1071   -115  B    N  
ATOM   4001  CA  GLU B  93      19.669   8.105 458.753  1.00 53.19      B    C  
ANISOU 4001  CA  GLU B  93     5909   4619   9683    604  -1252   -145  B    C  
ATOM   4002  C   GLU B  93      19.271   8.909 457.523  1.00 48.56      B    C  
ANISOU 4002  C   GLU B  93     5451   3970   9030    365  -1089   -226  B    C  
ATOM   4003  O   GLU B  93      20.131   9.273 456.710  1.00 43.79      B    O  
ANISOU 4003  O   GLU B  93     4671   3446   8522    214   -981   -284  B    O  
ATOM   4004  CB  GLU B  93      21.047   8.569 459.241  1.00 64.49      B    C  
ANISOU 4004  CB  GLU B  93     7033   6241  11228    539  -1417   -148  B    C  
ATOM   4005  CG  GLU B  93      21.427   8.282 460.688  1.00 87.76      B    C  
ANISOU 4005  CG  GLU B  93     9891   9292  14163    698  -1692    -57  B    C  
ATOM   4006  CD  GLU B  93      22.687   9.053 461.123  1.00 96.82      B    C  
ANISOU 4006  CD  GLU B  93    10759  10641  15387    555  -1893    -84  B    C  
ATOM   4007  OE1 GLU B  93      23.261   9.790 460.288  1.00 99.63      B    O  
ANISOU 4007  OE1 GLU B  93    10988  11040  15827    336  -1792   -176  B    O  
ATOM   4008  OE2 GLU B  93      23.109   8.920 462.295  1.00 93.46      B    O1-
ANISOU 4008  OE2 GLU B  93    10241  10337  14932    650  -2154    -12  B    O1-
ATOM   4009  N   PRO B  94      17.991   9.200 457.328  1.00 57.18      B    N  
ANISOU 4009  N   PRO B  94     6840   4921   9965    323  -1063   -221  B    N  
ATOM   4010  CA  PRO B  94      17.581   9.934 456.127  1.00 50.94      B    C  
ANISOU 4010  CA  PRO B  94     6177   4075   9103    106   -926   -267  B    C  
ATOM   4011  C   PRO B  94      18.227  11.305 456.008  1.00 40.30      B    C  
ANISOU 4011  C   PRO B  94     4770   2795   7747   -137   -998   -298  B    C  
ATOM   4012  O   PRO B  94      18.481  11.991 456.997  1.00 40.87      B    O  
ANISOU 4012  O   PRO B  94     4824   2905   7799   -172  -1194   -295  B    O  
ATOM   4013  CB  PRO B  94      16.064  10.054 456.298  1.00 50.22      B    C  
ANISOU 4013  CB  PRO B  94     6390   3826   8865    139   -959   -228  B    C  
ATOM   4014  CG  PRO B  94      15.700   8.800 457.069  1.00 55.73      B    C  
ANISOU 4014  CG  PRO B  94     7097   4482   9597    402   -972   -186  B    C  
ATOM   4015  CD  PRO B  94      16.832   8.636 458.052  1.00 64.66      B    C  
ANISOU 4015  CD  PRO B  94     8006   5745  10818    497  -1115   -163  B    C  
ATOM   4016  N   ILE B  95      18.454  11.682 454.752  1.00 40.71      B    N  
ANISOU 4016  N   ILE B  95     4814   2854   7801   -319   -824   -333  B    N  
ATOM   4017  CA  ILE B  95      19.103  12.903 454.288  1.00 41.97      B    C  
ANISOU 4017  CA  ILE B  95     4917   3058   7969   -577   -813   -361  B    C  
ATOM   4018  C   ILE B  95      18.095  13.634 453.410  1.00 51.76      B    C  
ANISOU 4018  C   ILE B  95     6432   4174   9061   -729   -741   -324  B    C  
ATOM   4019  O   ILE B  95      17.578  13.066 452.442  1.00 56.24      B    O  
ANISOU 4019  O   ILE B  95     7097   4706   9565   -720   -584   -316  B    O  
ATOM   4020  CB  ILE B  95      20.381  12.592 453.487  1.00 44.24      B    C  
ANISOU 4020  CB  ILE B  95     4930   3473   8406   -652   -632   -419  B    C  
ATOM   4021  CG1 ILE B  95      21.533  12.195 454.401  1.00 46.22      B    C  
ANISOU 4021  CG1 ILE B  95     4860   3862   8839   -541   -747   -438  B    C  
ATOM   4022  CG2 ILE B  95      20.755  13.733 452.557  1.00 49.88      B    C  
ANISOU 4022  CG2 ILE B  95     5667   4194   9092   -943   -524   -437  B    C  
ATOM   4023  CD1 ILE B  95      22.468  11.206 453.758  1.00 59.93      B    C  
ANISOU 4023  CD1 ILE B  95     6326   5684  10762   -461   -537   -478  B    C  
ATOM   4024  N   TRP B  96      17.831  14.888 453.735  1.00 54.13      B    N  
ANISOU 4024  N   TRP B  96     6852   4406   9309   -874   -857   -299  B    N  
ATOM   4025  CA  TRP B  96      16.784  15.686 453.113  1.00 39.32      B    C  
ANISOU 4025  CA  TRP B  96     5238   2390   7313   -989   -834   -230  B    C  
ATOM   4026  C   TRP B  96      17.453  16.740 452.238  1.00 40.98      B    C  
ANISOU 4026  C   TRP B  96     5420   2617   7533  -1256   -737   -224  B    C  
ATOM   4027  O   TRP B  96      18.231  17.557 452.740  1.00 42.37      B    O  
ANISOU 4027  O   TRP B  96     5489   2821   7789  -1380   -805   -264  B    O  
ATOM   4028  CB  TRP B  96      15.935  16.325 454.209  1.00 38.18      B    C  
ANISOU 4028  CB  TRP B  96     5254   2174   7079   -918   -989   -198  B    C  
ATOM   4029  CG  TRP B  96      14.864  17.193 453.778  1.00 37.29      B    C  
ANISOU 4029  CG  TRP B  96     5348   2080   6739   -946   -902   -116  B    C  
ATOM   4030  CD1 TRP B  96      14.315  17.271 452.538  1.00 61.41      B    C  
ANISOU 4030  CD1 TRP B  96     8508   5136   9689  -1009   -771    -50  B    C  
ATOM   4031  CD2 TRP B  96      14.191  18.154 454.578  1.00 36.86      B    C  
ANISOU 4031  CD2 TRP B  96     5403   2033   6567   -915   -934    -96  B    C  
ATOM   4032  CE2 TRP B  96      13.229  18.776 453.758  1.00 36.32      B    C  
ANISOU 4032  CE2 TRP B  96     5469   1968   6363   -937   -812    -12  B    C  
ATOM   4033  CE3 TRP B  96      14.316  18.565 455.906  1.00 37.15      B    C  
ANISOU 4033  CE3 TRP B  96     5434   2064   6619   -880  -1051   -148  B    C  
ATOM   4034  NE1 TRP B  96      13.338  18.229 452.509  1.00 36.47      B    N  
ANISOU 4034  NE1 TRP B  96     5489   1985   6384  -1000   -735     20  B    N  
ATOM   4035  CZ2 TRP B  96      12.382  19.759 454.227  1.00 36.01      B    C  
ANISOU 4035  CZ2 TRP B  96     5524   1919   6241   -903   -783     19  B    C  
ATOM   4036  CZ3 TRP B  96      13.474  19.528 456.373  1.00 36.81      B    C  
ANISOU 4036  CZ3 TRP B  96     5516   2011   6458   -865  -1005   -127  B    C  
ATOM   4037  CH2 TRP B  96      12.509  20.114 455.537  1.00 37.30      B    C  
ANISOU 4037  CH2 TRP B  96     5681   2071   6422   -868   -861    -44  B    C  
ATOM   4038  N   VAL B  97      17.177  16.709 450.936  1.00 41.08      B    N  
ANISOU 4038  N   VAL B  97     5534   2617   7459  -1358   -576   -178  B    N  
ATOM   4039  CA  VAL B  97      17.803  17.629 449.994  1.00 42.88      B    C  
ANISOU 4039  CA  VAL B  97     5756   2860   7676  -1616   -451   -154  B    C  
ATOM   4040  C   VAL B  97      16.740  18.108 449.024  1.00 55.50      B    C  
ANISOU 4040  C   VAL B  97     7626   4350   9113  -1706   -414    -29  B    C  
ATOM   4041  O   VAL B  97      16.048  17.287 448.417  1.00 48.90      B    O  
ANISOU 4041  O   VAL B  97     6886   3525   8168  -1624   -360     -7  B    O  
ATOM   4042  CB  VAL B  97      18.967  16.977 449.229  1.00 44.72      B    C  
ANISOU 4042  CB  VAL B  97     5773   3248   7971  -1678   -241   -234  B    C  
ATOM   4043  CG1 VAL B  97      19.346  17.845 448.049  1.00 46.47      B    C  
ANISOU 4043  CG1 VAL B  97     6061   3468   8129  -1949    -73   -187  B    C  
ATOM   4044  CG2 VAL B  97      20.153  16.810 450.144  1.00 46.03      B    C  
ANISOU 4044  CG2 VAL B  97     5634   3524   8332  -1632   -299   -330  B    C  
ATOM   4045  N   GLU B  98      16.620  19.427 448.854  1.00 53.17      B    N  
ANISOU 4045  N   GLU B  98     7445   4013   8745  -1845   -410     47  B    N  
ATOM   4046  CA  GLU B  98      15.573  19.993 448.016  1.00 53.35      B    C  
ANISOU 4046  CA  GLU B  98     7682   4012   8577  -1853   -353    175  B    C  
ATOM   4047  C   GLU B  98      16.141  20.674 446.775  1.00 52.73      B    C  
ANISOU 4047  C   GLU B  98     7644   3914   8478  -2116   -211    252  B    C  
ATOM   4048  O   GLU B  98      17.276  21.146 446.763  1.00 55.67      B    O  
ANISOU 4048  O   GLU B  98     7899   4285   8967  -2307   -143    207  B    O  
ATOM   4049  CB  GLU B  98      14.719  20.997 448.800  1.00 41.92      B    C  
ANISOU 4049  CB  GLU B  98     6313   2542   7072  -1721   -419    217  B    C  
ATOM   4050  CG  GLU B  98      14.027  20.381 449.970  1.00 39.93      B    C  
ANISOU 4050  CG  GLU B  98     6045   2326   6799  -1477   -527    164  B    C  
ATOM   4051  CD  GLU B  98      13.208  21.373 450.774  1.00 59.24      B    C  
ANISOU 4051  CD  GLU B  98     8558   4750   9201  -1373   -555    191  B    C  
ATOM   4052  OE1 GLU B  98      13.689  22.505 451.007  1.00 40.80      B    O  
ANISOU 4052  OE1 GLU B  98     6225   2358   6918  -1493   -532    180  B    O  
ATOM   4053  OE2 GLU B  98      12.086  21.001 451.208  1.00 63.49      B    O1-
ANISOU 4053  OE2 GLU B  98     9135   5324   9665  -1181   -582    213  B    O1-
ATOM   4054  N   THR B  99      15.335  20.687 445.726  1.00 55.86      B    N  
ANISOU 4054  N   THR B  99     8195   4314   8714  -2128   -175    377  B    N  
ATOM   4055  CA  THR B  99      15.497  21.519 444.548  1.00 63.78      B    C  
ANISOU 4055  CA  THR B  99     9300   5313   9619  -2327    -75    510  B    C  
ATOM   4056  C   THR B  99      14.364  22.539 444.579  1.00 46.71      B    C  
ANISOU 4056  C   THR B  99     7251   3099   7397  -2202   -160    652  B    C  
ATOM   4057  O   THR B  99      13.693  22.718 445.610  1.00 49.40      B    O  
ANISOU 4057  O   THR B  99     7564   3415   7791  -1999   -252    613  B    O  
ATOM   4058  CB  THR B  99      15.466  20.688 443.261  1.00 60.97      B    C  
ANISOU 4058  CB  THR B  99     9069   5032   9065  -2466     34    543  B    C  
ATOM   4059  CG2 THR B  99      16.299  19.409 443.420  1.00 47.69      B    C  
ANISOU 4059  CG2 THR B  99     7247   3428   7444  -2477    157    349  B    C  
ATOM   4060  OG1 THR B  99      14.110  20.358 442.914  1.00 61.27      B    O  
ANISOU 4060  OG1 THR B  99     9254   5081   8946  -2327    -82    637  B    O  
ATOM   4061  N   ASP B 100      14.175  23.263 443.475  1.00 57.04      B    N  
ANISOU 4061  N   ASP B 100     8691   4396   8585  -2333   -113    819  B    N  
ATOM   4062  CA  ASP B 100      13.062  24.212 443.478  1.00 68.14      B    C  
ANISOU 4062  CA  ASP B 100    10191   5741   9959  -2209   -197    964  B    C  
ATOM   4063  C   ASP B 100      11.723  23.520 443.254  1.00 65.69      B    C  
ANISOU 4063  C   ASP B 100     9962   5481   9516  -2049   -325   1026  B    C  
ATOM   4064  O   ASP B 100      10.685  24.059 443.646  1.00 72.05      B    O  
ANISOU 4064  O   ASP B 100    10783   6249  10345  -1884   -408   1091  B    O  
ATOM   4065  CB  ASP B 100      13.260  25.346 442.461  1.00 64.07      B    C  
ANISOU 4065  CB  ASP B 100     9788   5176   9381  -2383   -122   1144  B    C  
ATOM   4066  CG  ASP B 100      13.694  24.863 441.103  1.00 78.85      B    C  
ANISOU 4066  CG  ASP B 100    11779   7139  11043  -2606    -34   1221  B    C  
ATOM   4067  OD1 ASP B 100      14.487  23.898 441.050  1.00 87.12      B    O  
ANISOU 4067  OD1 ASP B 100    12764   8262  12075  -2705     58   1080  B    O  
ATOM   4068  OD2 ASP B 100      13.223  25.447 440.101  1.00 79.56      B    O1-
ANISOU 4068  OD2 ASP B 100    12033   7227  10970  -2685    -41   1417  B    O1-
ATOM   4069  N   ARG B 101      11.716  22.356 442.604  1.00 58.50      B    N  
ANISOU 4069  N   ARG B 101     9105   4653   8469  -2113   -326    998  B    N  
ATOM   4070  CA  ARG B 101      10.477  21.651 442.297  1.00 75.38      B    C  
ANISOU 4070  CA  ARG B 101    11323   6840  10479  -1999   -450   1050  B    C  
ATOM   4071  C   ARG B 101      10.340  20.276 442.959  1.00 62.91      B    C  
ANISOU 4071  C   ARG B 101     9657   5299   8945  -1865   -471    879  B    C  
ATOM   4072  O   ARG B 101       9.226  19.737 442.995  1.00 46.67      B    O  
ANISOU 4072  O   ARG B 101     7625   3272   6836  -1731   -577    897  B    O  
ATOM   4073  CB  ARG B 101      10.321  21.529 440.771  1.00 47.77      B    C  
ANISOU 4073  CB  ARG B 101     8026   3402   6721  -2214   -444   1193  B    C  
ATOM   4074  CG  ARG B 101      10.261  22.910 440.169  1.00 59.24      B    C  
ANISOU 4074  CG  ARG B 101     9568   4810   8132  -2303   -444   1393  B    C  
ATOM   4075  CD  ARG B 101      10.369  23.000 438.659  1.00 54.84      B    C  
ANISOU 4075  CD  ARG B 101     9224   4325   7289  -2555   -403   1550  B    C  
ATOM   4076  NE  ARG B 101      10.856  24.343 438.327  1.00 63.34      B    N  
ANISOU 4076  NE  ARG B 101    10331   5335   8399  -2650   -324   1690  B    N  
ATOM   4077  CZ  ARG B 101      10.540  25.039 437.234  1.00 80.26      B    C  
ANISOU 4077  CZ  ARG B 101    12648   7495  10352  -2773   -348   1913  B    C  
ATOM   4078  NH1 ARG B 101       9.712  24.532 436.325  1.00 83.26      B    N1+
ANISOU 4078  NH1 ARG B 101    13194   7974  10466  -2834   -474   2028  B    N1+
ATOM   4079  NH2 ARG B 101      11.071  26.251 437.041  1.00 82.46      B    N  
ANISOU 4079  NH2 ARG B 101    12936   7690  10703  -2847   -247   2024  B    N  
ATOM   4080  N   LEU B 102      11.422  19.692 443.467  1.00 47.51      B    N  
ANISOU 4080  N   LEU B 102     7600   3347   7105  -1900   -374    719  B    N  
ATOM   4081  CA  LEU B 102      11.372  18.373 444.073  1.00 41.47      B    C  
ANISOU 4081  CA  LEU B 102     6759   2602   6398  -1770   -380    565  B    C  
ATOM   4082  C   LEU B 102      12.021  18.436 445.449  1.00 56.94      B    C  
ANISOU 4082  C   LEU B 102     8550   4531   8553  -1647   -377    442  B    C  
ATOM   4083  O   LEU B 102      12.867  19.300 445.718  1.00 43.26      B    O  
ANISOU 4083  O   LEU B 102     6760   2767   6908  -1746   -338    437  B    O  
ATOM   4084  CB  LEU B 102      12.061  17.308 443.195  1.00 42.50      B    C  
ANISOU 4084  CB  LEU B 102     6955   2760   6433  -1957   -249    476  B    C  
ATOM   4085  CG  LEU B 102      11.437  16.988 441.840  1.00 43.70      B    C  
ANISOU 4085  CG  LEU B 102     7317   2968   6320  -2113   -230    555  B    C  
ATOM   4086  CD1 LEU B 102      12.411  16.239 440.975  1.00 45.39      B    C  
ANISOU 4086  CD1 LEU B 102     7536   3294   6415  -2285     20    416  B    C  
ATOM   4087  CD2 LEU B 102      10.183  16.149 442.035  1.00 48.49      B    C  
ANISOU 4087  CD2 LEU B 102     7949   3582   6893  -1934   -362    538  B    C  
ATOM   4088  N   SER B 103      11.559  17.549 446.332  1.00 38.60      B    N  
ANISOU 4088  N   SER B 103     6164   2229   6275  -1438   -425    351  B    N  
ATOM   4089  CA  SER B 103      12.045  17.398 447.699  1.00 45.49      B    C  
ANISOU 4089  CA  SER B 103     6914   3101   7268  -1308   -453    245  B    C  
ATOM   4090  C   SER B 103      12.433  15.941 447.897  1.00 38.10      B    C  
ANISOU 4090  C   SER B 103     5911   2164   6401  -1236   -432    130  B    C  
ATOM   4091  O   SER B 103      11.579  15.055 447.790  1.00 39.32      B    O  
ANISOU 4091  O   SER B 103     6108   2342   6491  -1113   -431    118  B    O  
ATOM   4092  CB  SER B 103      10.971  17.825 448.702  1.00 45.30      B    C  
ANISOU 4092  CB  SER B 103     6893   3115   7205  -1103   -523    274  B    C  
ATOM   4093  OG  SER B 103      11.471  17.922 450.016  1.00 35.71      B    O  
ANISOU 4093  OG  SER B 103     5597   1907   6064  -1022   -566    195  B    O  
ATOM   4094  N   PHE B 104      13.707  15.698 448.195  1.00 43.15      B    N  
ANISOU 4094  N   PHE B 104     6413   2773   7210  -1305   -414     43  B    N  
ATOM   4095  CA  PHE B 104      14.285  14.359 448.251  1.00 38.17      B    C  
ANISOU 4095  CA  PHE B 104     5638   2182   6683  -1209   -330    -78  B    C  
ATOM   4096  C   PHE B 104      14.578  13.947 449.690  1.00 37.38      B    C  
ANISOU 4096  C   PHE B 104     5391   2073   6738  -1006   -440   -135  B    C  
ATOM   4097  O   PHE B 104      15.016  14.762 450.512  1.00 38.11      B    O  
ANISOU 4097  O   PHE B 104     5421   2150   6910  -1032   -552   -127  B    O  
ATOM   4098  CB  PHE B 104      15.578  14.282 447.426  1.00 40.35      B    C  
ANISOU 4098  CB  PHE B 104     5771   2586   6975  -1360   -122   -151  B    C  
ATOM   4099  CG  PHE B 104      15.359  14.404 445.939  1.00 41.47      B    C  
ANISOU 4099  CG  PHE B 104     6069   2764   6925  -1555     26   -114  B    C  
ATOM   4100  CD1 PHE B 104      15.365  15.651 445.321  1.00 42.53      B    C  
ANISOU 4100  CD1 PHE B 104     6323   2871   6966  -1771     19      2  B    C  
ATOM   4101  CD2 PHE B 104      15.144  13.280 445.158  1.00 41.74      B    C  
ANISOU 4101  CD2 PHE B 104     6144   2853   6861  -1532    176   -192  B    C  
ATOM   4102  CE1 PHE B 104      15.148  15.771 443.953  1.00 53.72      B    C  
ANISOU 4102  CE1 PHE B 104     7906   4333   8172  -1956    141     58  B    C  
ATOM   4103  CE2 PHE B 104      14.940  13.386 443.793  1.00 43.07      B    C  
ANISOU 4103  CE2 PHE B 104     6479   3073   6813  -1730    304   -165  B    C  
ATOM   4104  CZ  PHE B 104      14.933  14.628 443.186  1.00 50.02      B    C  
ANISOU 4104  CZ  PHE B 104     7486   3944   7578  -1941    278    -30  B    C  
ATOM   4105  N   LEU B 105      14.310  12.678 449.987  1.00 36.58      B    N  
ANISOU 4105  N   LEU B 105     5251   1979   6668   -813   -410   -190  B    N  
ATOM   4106  CA  LEU B 105      14.688  12.046 451.242  1.00 44.30      B    C  
ANISOU 4106  CA  LEU B 105     6083   2970   7778   -607   -489   -233  B    C  
ATOM   4107  C   LEU B 105      15.354  10.726 450.906  1.00 45.38      B    C  
ANISOU 4107  C   LEU B 105     6061   3184   7998   -502   -316   -320  B    C  
ATOM   4108  O   LEU B 105      14.704   9.837 450.355  1.00 54.84      B    O  
ANISOU 4108  O   LEU B 105     7351   4342   9143   -445   -211   -347  B    O  
ATOM   4109  CB  LEU B 105      13.464  11.811 452.124  1.00 48.42      B    C  
ANISOU 4109  CB  LEU B 105     6740   3498   8160   -423   -584   -176  B    C  
ATOM   4110  CG  LEU B 105      13.744  11.405 453.566  1.00 51.70      B    C  
ANISOU 4110  CG  LEU B 105     7055   3930   8659   -236   -697   -186  B    C  
ATOM   4111  CD1 LEU B 105      14.365  12.582 454.309  1.00 55.50      B    C  
ANISOU 4111  CD1 LEU B 105     7487   4396   9204   -334   -850   -183  B    C  
ATOM   4112  CD2 LEU B 105      12.462  10.940 454.237  1.00 52.72      B    C  
ANISOU 4112  CD2 LEU B 105     7304   4156   8572    -76   -679   -135  B    C  
ATOM   4113  N   GLY B 106      16.630  10.585 451.235  1.00 38.78      B    N  
ANISOU 4113  N   GLY B 106     4979   2449   7307   -478   -282   -368  B    N  
ATOM   4114  CA  GLY B 106      17.359   9.375 450.911  1.00 40.07      B    C  
ANISOU 4114  CA  GLY B 106     4962   2669   7593   -368    -95   -446  B    C  
ATOM   4115  C   GLY B 106      18.082   8.839 452.127  1.00 50.13      B    C  
ANISOU 4115  C   GLY B 106     6012   3988   9047   -159   -202   -436  B    C  
ATOM   4116  O   GLY B 106      18.456   9.586 453.019  1.00 41.02      B    O  
ANISOU 4116  O   GLY B 106     4785   2879   7922   -175   -396   -398  B    O  
ATOM   4117  N   TRP B 107      18.218   7.513 452.188  1.00 41.22      B    N  
ANISOU 4117  N   TRP B 107     4791   2839   8033     39    -83   -467  B    N  
ATOM   4118  CA  TRP B 107      18.987   6.929 453.279  1.00 48.51      B    C  
ANISOU 4118  CA  TRP B 107     5481   3811   9138    252   -184   -430  B    C  
ATOM   4119  C   TRP B 107      19.635   5.630 452.826  1.00 44.08      B    C  
ANISOU 4119  C   TRP B 107     4733   3246   8768    399     54   -486  B    C  
ATOM   4120  O   TRP B 107      19.215   5.007 451.849  1.00 47.58      B    O  
ANISOU 4120  O   TRP B 107     5288   3617   9175    368    286   -563  B    O  
ATOM   4121  CB  TRP B 107      18.127   6.666 454.520  1.00 47.94      B    C  
ANISOU 4121  CB  TRP B 107     5547   3660   9006    438   -391   -342  B    C  
ATOM   4122  CG  TRP B 107      17.138   5.592 454.313  1.00 40.09      B    C  
ANISOU 4122  CG  TRP B 107     4718   2530   7984    576   -269   -347  B    C  
ATOM   4123  CD1 TRP B 107      17.275   4.282 454.639  1.00 40.26      B    C  
ANISOU 4123  CD1 TRP B 107     4652   2496   8148    808   -178   -333  B    C  
ATOM   4124  CD2 TRP B 107      15.846   5.736 453.731  1.00 42.56      B    C  
ANISOU 4124  CD2 TRP B 107     5304   2736   8131    483   -227   -364  B    C  
ATOM   4125  CE2 TRP B 107      15.247   4.461 453.730  1.00 58.92      B    C  
ANISOU 4125  CE2 TRP B 107     7445   4777  10167    634   -102   -367  B    C  
ATOM   4126  CE3 TRP B 107      15.136   6.821 453.205  1.00 45.53      B    C  
ANISOU 4126  CE3 TRP B 107     5866   3096   8338    275   -283   -359  B    C  
ATOM   4127  NE1 TRP B 107      16.143   3.590 454.292  1.00 55.42      B    N  
ANISOU 4127  NE1 TRP B 107     6790   4337   9929    833    -65   -350  B    N  
ATOM   4128  CZ2 TRP B 107      13.966   4.232 453.216  1.00 35.65      B    C  
ANISOU 4128  CZ2 TRP B 107     4734   1872   6941    559    -42   -369  B    C  
ATOM   4129  CZ3 TRP B 107      13.864   6.595 452.694  1.00 53.92      B    C  
ANISOU 4129  CZ3 TRP B 107     7150   4155   9181    237   -227   -349  B    C  
ATOM   4130  CH2 TRP B 107      13.293   5.303 452.704  1.00 46.62      B    C  
ANISOU 4130  CH2 TRP B 107     6276   3268   8170    373   -112   -358  B    C  
ATOM   4131  N   ARG B 108      20.641   5.202 453.581  1.00 45.96      B    N  
ANISOU 4131  N   ARG B 108     4687   3557   9216    564    -10   -444  B    N  
ATOM   4132  CA  ARG B 108      21.360   3.970 453.290  1.00 61.21      B    C  
ANISOU 4132  CA  ARG B 108     6399   5469  11388    740    211   -479  B    C  
ATOM   4133  C   ARG B 108      20.819   2.834 454.138  1.00 57.87      B    C  
ANISOU 4133  C   ARG B 108     6031   4932  11026   1028    159   -395  B    C  
ATOM   4134  O   ARG B 108      20.732   2.951 455.368  1.00 47.18      B    O  
ANISOU 4134  O   ARG B 108     4668   3606   9652   1157   -108   -275  B    O  
ATOM   4135  CB  ARG B 108      22.855   4.108 453.561  1.00 69.95      B    C  
ANISOU 4135  CB  ARG B 108     7115   6723  12740    768    182   -463  B    C  
ATOM   4136  CG  ARG B 108      23.599   2.780 453.483  1.00 62.95      B    C  
ANISOU 4136  CG  ARG B 108     5969   5796  12153   1008    385   -466  B    C  
ATOM   4137  CD  ARG B 108      25.002   2.991 453.924  1.00 66.41      B    C  
ANISOU 4137  CD  ARG B 108     5998   6391  12844   1051    292   -421  B    C  
ATOM   4138  NE  ARG B 108      25.809   1.793 453.808  1.00 73.80      B    N  
ANISOU 4138  NE  ARG B 108     6642   7285  14113   1285    498   -414  B    N  
ATOM   4139  CZ  ARG B 108      27.140   1.831 453.809  1.00100.89      B    C  
ANISOU 4139  CZ  ARG B 108     9663  10839  17833   1311    530   -407  B    C  
ATOM   4140  NH1 ARG B 108      27.756   3.007 453.916  1.00112.97      B    N1+
ANISOU 4140  NH1 ARG B 108    11051  12541  19333   1097    364   -418  B    N1+
ATOM   4141  NH2 ARG B 108      27.858   0.718 453.675  1.00102.97      B    N  
ANISOU 4141  NH2 ARG B 108     9648  11042  18434   1543    740   -395  B    N  
ATOM   4142  N   HIS B 109      20.483   1.731 453.479  1.00 61.26      B    N  
ANISOU 4142  N   HIS B 109     6523   5228  11523   1118    425   -464  B    N  
ATOM   4143  CA  HIS B 109      20.040   0.521 454.160  1.00 67.81      B    C  
ANISOU 4143  CA  HIS B 109     7395   5923  12445   1391    438   -390  B    C  
ATOM   4144  C   HIS B 109      20.773  -0.680 453.568  1.00 76.91      B    C  
ANISOU 4144  C   HIS B 109     8377   7066  13780   1489    736   -447  B    C  
ATOM   4145  O   HIS B 109      20.461  -1.119 452.457  1.00 50.16      B    O  
ANISOU 4145  O   HIS B 109     5102   3601  10355   1383   1015   -589  B    O  
ATOM   4146  CB  HIS B 109      18.529   0.365 454.052  1.00 61.08      B    C  
ANISOU 4146  CB  HIS B 109     6928   5053  11225   1289    424   -393  B    C  
ATOM   4147  CG  HIS B 109      18.001  -0.826 454.785  1.00 62.47      B    C  
ANISOU 4147  CG  HIS B 109     7229   5283  11223   1436    411   -295  B    C  
ATOM   4148  CD2 HIS B 109      17.636  -2.054 454.351  1.00 56.71      B    C  
ANISOU 4148  CD2 HIS B 109     6591   4526  10433   1472    606   -337  B    C  
ATOM   4149  ND1 HIS B 109      17.783  -0.819 456.145  1.00 64.92      B    N  
ANISOU 4149  ND1 HIS B 109     7600   5672  11397   1554    180   -146  B    N  
ATOM   4150  CE1 HIS B 109      17.311  -1.996 456.517  1.00 62.78      B    C  
ANISOU 4150  CE1 HIS B 109     7453   5412  10987   1662    245    -99  B    C  
ATOM   4151  NE2 HIS B 109      17.214  -2.762 455.448  1.00 61.21      B    N  
ANISOU 4151  NE2 HIS B 109     7266   5146  10844   1614    486   -212  B    N  
ATOM   4152  N   GLU B 110      21.728  -1.220 454.324  1.00 73.80      B    N  
ANISOU 4152  N   GLU B 110     7727   6752  13561   1679    666   -331  B    N  
ATOM   4153  CA  GLU B 110      22.553  -2.359 453.910  1.00 65.56      B    C  
ANISOU 4153  CA  GLU B 110     6498   5698  12714   1789    921   -356  B    C  
ATOM   4154  C   GLU B 110      23.225  -1.999 452.592  1.00 58.45      B    C  
ANISOU 4154  C   GLU B 110     5420   4751  12037   1654   1229   -549  B    C  
ATOM   4155  O   GLU B 110      24.024  -1.049 452.569  1.00 58.75      B    O  
ANISOU 4155  O   GLU B 110     5207   4880  12236   1591   1158   -564  B    O  
ATOM   4156  CB  GLU B 110      21.738  -3.655 453.886  1.00 70.78      B    C  
ANISOU 4156  CB  GLU B 110     7420   6297  13175   1842   1040   -345  B    C  
ATOM   4157  CG  GLU B 110      21.325  -4.176 455.243  1.00 78.60      B    C  
ANISOU 4157  CG  GLU B 110     8531   7345  13989   2006    795   -160  B    C  
ATOM   4158  CD  GLU B 110      20.733  -5.564 455.152  1.00 84.26      B    C  
ANISOU 4158  CD  GLU B 110     9432   7992  14591   2067    947   -166  B    C  
ATOM   4159  OE1 GLU B 110      20.773  -6.152 454.051  1.00 84.79      B    O  
ANISOU 4159  OE1 GLU B 110     9499   7971  14745   1990   1234   -306  B    O  
ATOM   4160  OE2 GLU B 110      20.243  -6.076 456.178  1.00 87.17      B    O1-
ANISOU 4160  OE2 GLU B 110     9942   8389  14789   2185    790    -41  B    O1-
ATOM   4161  N   ASN B 111      23.012  -2.753 451.518  1.00 68.53      B    N  
ANISOU 4161  N   ASN B 111     6816   5936  13286   1576   1568   -696  B    N  
ATOM   4162  CA  ASN B 111      23.615  -2.502 450.217  1.00 71.11      B    C  
ANISOU 4162  CA  ASN B 111     7022   6225  13772   1427   1922   -904  B    C  
ATOM   4163  C   ASN B 111      22.927  -1.396 449.443  1.00 63.33      B    C  
ANISOU 4163  C   ASN B 111     6290   5282  12492   1122   1908  -1011  B    C  
ATOM   4164  O   ASN B 111      23.414  -1.020 448.377  1.00 69.96      B    O  
ANISOU 4164  O   ASN B 111     7101   6187  13296    906   2140  -1147  B    O  
ATOM   4165  CB  ASN B 111      23.623  -3.778 449.367  1.00 82.30      B    C  
ANISOU 4165  CB  ASN B 111     8529   7561  15182   1412   2267  -1016  B    C  
ATOM   4166  CG  ASN B 111      24.582  -3.676 448.186  1.00 92.37      B    C  
ANISOU 4166  CG  ASN B 111     9617   8828  16652   1289   2656  -1211  B    C  
ATOM   4167  ND2 ASN B 111      24.437  -4.602 447.240  1.00 96.29      B    N  
ANISOU 4167  ND2 ASN B 111    10258   9237  17091   1206   2980  -1355  B    N  
ATOM   4168  OD1 ASN B 111      25.444  -2.782 448.122  1.00 84.42      B    O  
ANISOU 4168  OD1 ASN B 111     8333   7908  15837   1251   2672  -1236  B    O  
ATOM   4169  N   TYR B 112      21.782  -0.917 449.897  1.00 59.06      B    N  
ANISOU 4169  N   TYR B 112     6029   4731  11680   1067   1644   -937  B    N  
ATOM   4170  CA  TYR B 112      20.980  -0.041 449.068  1.00 51.74      B    C  
ANISOU 4170  CA  TYR B 112     5392   3850  10417    766   1628  -1011  B    C  
ATOM   4171  C   TYR B 112      21.013   1.397 449.561  1.00 50.38      B    C  
ANISOU 4171  C   TYR B 112     5223   3824  10094    625   1310   -901  B    C  
ATOM   4172  O   TYR B 112      21.361   1.692 450.708  1.00 70.96      B    O  
ANISOU 4172  O   TYR B 112     7677   6487  12796    761   1048   -768  B    O  
ATOM   4173  CB  TYR B 112      19.535  -0.547 449.007  1.00 49.52      B    C  
ANISOU 4173  CB  TYR B 112     5441   3429   9945    774   1608  -1033  B    C  
ATOM   4174  CG  TYR B 112      19.420  -1.987 448.583  1.00 61.28      B    C  
ANISOU 4174  CG  TYR B 112     6957   4796  11532    882   1894  -1133  B    C  
ATOM   4175  CD1 TYR B 112      19.395  -2.319 447.238  1.00 69.88      B    C  
ANISOU 4175  CD1 TYR B 112     8154   5833  12565    704   2234  -1343  B    C  
ATOM   4176  CD2 TYR B 112      19.341  -3.023 449.515  1.00 56.98      B    C  
ANISOU 4176  CD2 TYR B 112     6367   4290  10992   1089   1780   -985  B    C  
ATOM   4177  CE1 TYR B 112      19.287  -3.640 446.818  1.00 66.06      B    C  
ANISOU 4177  CE1 TYR B 112     7711   5328  12061    734   2443  -1404  B    C  
ATOM   4178  CE2 TYR B 112      19.234  -4.351 449.102  1.00 52.73      B    C  
ANISOU 4178  CE2 TYR B 112     5876   3714  10445   1122   1992  -1040  B    C  
ATOM   4179  CZ  TYR B 112      19.211  -4.651 447.744  1.00 58.21      B    C  
ANISOU 4179  CZ  TYR B 112     6655   4347  11113    944   2321  -1251  B    C  
ATOM   4180  OH  TYR B 112      19.107  -5.952 447.279  1.00 75.00      B    O  
ANISOU 4180  OH  TYR B 112     8832   6420  13243    953   2539  -1322  B    O  
ATOM   4181  N   TYR B 113      20.660   2.278 448.641  1.00 49.64      B    N  
ANISOU 4181  N   TYR B 113     5316   3789   9758    340   1347   -962  B    N  
ATOM   4182  CA  TYR B 113      20.222   3.635 448.911  1.00 56.26      B    C  
ANISOU 4182  CA  TYR B 113     6286   4704  10386    172   1073   -871  B    C  
ATOM   4183  C   TYR B 113      18.756   3.679 448.517  1.00 45.52      B    C  
ANISOU 4183  C   TYR B 113     5279   3257   8759     83   1025   -875  B    C  
ATOM   4184  O   TYR B 113      18.404   3.316 447.387  1.00 60.06      B    O  
ANISOU 4184  O   TYR B 113     7273   5070  10478    -51   1246   -987  B    O  
ATOM   4185  CB  TYR B 113      20.994   4.657 448.073  1.00 53.58      B    C  
ANISOU 4185  CB  TYR B 113     5876   4488   9995    -95   1170   -915  B    C  
ATOM   4186  CG  TYR B 113      22.469   4.757 448.358  1.00 61.31      B    C  
ANISOU 4186  CG  TYR B 113     6479   5568  11247    -52   1222   -919  B    C  
ATOM   4187  CD1 TYR B 113      22.975   4.560 449.638  1.00 52.20      B    C  
ANISOU 4187  CD1 TYR B 113     5086   4445  10302    171   1005   -821  B    C  
ATOM   4188  CD2 TYR B 113      23.372   4.975 447.321  1.00 54.23      B    C  
ANISOU 4188  CD2 TYR B 113     5456   4742  10406   -234   1503  -1021  B    C  
ATOM   4189  CE1 TYR B 113      24.341   4.636 449.885  1.00 69.94      B    C  
ANISOU 4189  CE1 TYR B 113     6954   6801  12818    207   1032   -819  B    C  
ATOM   4190  CE2 TYR B 113      24.736   5.042 447.553  1.00 56.88      B    C  
ANISOU 4190  CE2 TYR B 113     5412   5172  11027   -198   1566  -1030  B    C  
ATOM   4191  CZ  TYR B 113      25.217   4.872 448.832  1.00 62.85      B    C  
ANISOU 4191  CZ  TYR B 113     5911   5966  12003     25   1319   -927  B    C  
ATOM   4192  OH  TYR B 113      26.572   4.943 449.055  1.00 60.15      B    O  
ANISOU 4192  OH  TYR B 113     5163   5731  11959     56   1358   -929  B    O  
ATOM   4193  N   ILE B 114      17.898   4.099 449.426  1.00 43.29      B    N  
ANISOU 4193  N   ILE B 114     5127   2936   8386    148    745   -761  B    N  
ATOM   4194  CA  ILE B 114      16.498   4.296 449.097  1.00 41.24      B    C  
ANISOU 4194  CA  ILE B 114     5171   2603   7897     56    670   -747  B    C  
ATOM   4195  C   ILE B 114      16.249   5.793 449.007  1.00 40.33      B    C  
ANISOU 4195  C   ILE B 114     5160   2550   7614   -146    484   -667  B    C  
ATOM   4196  O   ILE B 114      16.623   6.549 449.910  1.00 40.05      B    O  
ANISOU 4196  O   ILE B 114     5030   2554   7635   -115    290   -585  B    O  
ATOM   4197  CB  ILE B 114      15.592   3.616 450.131  1.00 46.18      B    C  
ANISOU 4197  CB  ILE B 114     5879   3106   8561    280    535   -683  B    C  
ATOM   4198  CG1 ILE B 114      16.090   2.181 450.376  1.00 40.98      B    C  
ANISOU 4198  CG1 ILE B 114     5071   2375   8125    507    718   -735  B    C  
ATOM   4199  CG2 ILE B 114      14.150   3.656 449.646  1.00 37.91      B    C  
ANISOU 4199  CG2 ILE B 114     5109   1980   7314    181    501   -689  B    C  
ATOM   4200  CD1 ILE B 114      15.238   1.365 451.311  1.00 39.75      B    C  
ANISOU 4200  CD1 ILE B 114     5011   2258   7836    684    598   -631  B    C  
ATOM   4201  N   ILE B 115      15.649   6.225 447.906  1.00 40.17      B    N  
ANISOU 4201  N   ILE B 115     5337   2538   7387   -361    546   -689  B    N  
ATOM   4202  CA  ILE B 115      15.378   7.634 447.669  1.00 39.63      B    C  
ANISOU 4202  CA  ILE B 115     5385   2507   7166   -558    398   -597  B    C  
ATOM   4203  C   ILE B 115      13.891   7.799 447.393  1.00 37.98      B    C  
ANISOU 4203  C   ILE B 115     5437   2220   6772   -607    282   -538  B    C  
ATOM   4204  O   ILE B 115      13.359   7.224 446.437  1.00 38.36      B    O  
ANISOU 4204  O   ILE B 115     5616   2265   6695   -689    406   -602  B    O  
ATOM   4205  CB  ILE B 115      16.197   8.197 446.500  1.00 41.65      B    C  
ANISOU 4205  CB  ILE B 115     5616   2864   7344   -802    579   -641  B    C  
ATOM   4206  CG1 ILE B 115      17.686   8.075 446.781  1.00 43.54      B    C  
ANISOU 4206  CG1 ILE B 115     5558   3182   7804   -759    697   -699  B    C  
ATOM   4207  CG2 ILE B 115      15.844   9.658 446.281  1.00 41.21      B    C  
ANISOU 4207  CG2 ILE B 115     5700   2817   7140   -996    424   -521  B    C  
ATOM   4208  CD1 ILE B 115      18.302   6.926 446.080  1.00 45.40      B    C  
ANISOU 4208  CD1 ILE B 115     5688   3435   8127   -723   1003   -841  B    C  
ATOM   4209  N   GLU B 116      13.240   8.612 448.210  1.00 36.42      B    N  
ANISOU 4209  N   GLU B 116     5311   1964   6563   -568     47   -422  B    N  
ATOM   4210  CA  GLU B 116      11.855   9.016 448.051  1.00 35.04      B    C  
ANISOU 4210  CA  GLU B 116     5348   1711   6254   -612    -91   -337  B    C  
ATOM   4211  C   GLU B 116      11.831  10.484 447.624  1.00 51.12      B    C  
ANISOU 4211  C   GLU B 116     7470   3767   8187   -810   -187   -229  B    C  
ATOM   4212  O   GLU B 116      12.597  11.302 448.140  1.00 59.22      B    O  
ANISOU 4212  O   GLU B 116     8399   4811   9290   -839   -239   -199  B    O  
ATOM   4213  CB  GLU B 116      11.097   8.826 449.373  1.00 33.26      B    C  
ANISOU 4213  CB  GLU B 116     5131   1560   5945   -383   -212   -267  B    C  
ATOM   4214  CG  GLU B 116      10.943   7.386 449.888  1.00 36.53      B    C  
ANISOU 4214  CG  GLU B 116     5495   1988   6396   -181   -136   -325  B    C  
ATOM   4215  CD  GLU B 116      10.215   7.312 451.240  1.00 43.05      B    C  
ANISOU 4215  CD  GLU B 116     6332   2919   7107     -5   -213   -241  B    C  
ATOM   4216  OE1 GLU B 116      10.053   8.375 451.865  1.00 51.94      B    O  
ANISOU 4216  OE1 GLU B 116     7458   4096   8182    -25   -308   -171  B    O  
ATOM   4217  OE2 GLU B 116       9.764   6.217 451.664  1.00 55.70      B    O1-
ANISOU 4217  OE2 GLU B 116     7945   4553   8664    131   -155   -252  B    O1-
ATOM   4218  N   VAL B 117      10.975  10.823 446.670  1.00 48.68      B    N  
ANISOU 4218  N   VAL B 117     7339   3451   7707   -953   -214   -164  B    N  
ATOM   4219  CA  VAL B 117      10.882  12.187 446.170  1.00 36.13      B    C  
ANISOU 4219  CA  VAL B 117     5835   1887   6008  -1125   -283    -35  B    C  
ATOM   4220  C   VAL B 117       9.427  12.629 446.171  1.00 35.09      B    C  
ANISOU 4220  C   VAL B 117     5754   1829   5749  -1037   -379     77  B    C  
ATOM   4221  O   VAL B 117       8.522  11.866 445.808  1.00 40.24      B    O  
ANISOU 4221  O   VAL B 117     6456   2498   6336   -996   -385     59  B    O  
ATOM   4222  CB  VAL B 117      11.493  12.335 444.757  1.00 38.25      B    C  
ANISOU 4222  CB  VAL B 117     6169   2246   6118  -1371   -128    -50  B    C  
ATOM   4223  CG1 VAL B 117      10.705  11.551 443.719  1.00 54.53      B    C  
ANISOU 4223  CG1 VAL B 117     8376   4352   7989  -1442    -74    -85  B    C  
ATOM   4224  CG2 VAL B 117      11.553  13.785 444.358  1.00 39.13      B    C  
ANISOU 4224  CG2 VAL B 117     6371   2342   6155  -1550   -201    104  B    C  
ATOM   4225  N   GLU B 118       9.211  13.880 446.555  1.00 46.16      B    N  
ANISOU 4225  N   GLU B 118     7139   3265   7137  -1021   -451    184  B    N  
ATOM   4226  CA  GLU B 118       7.893  14.482 446.597  1.00 47.29      B    C  
ANISOU 4226  CA  GLU B 118     7308   3458   7202   -941   -540    295  B    C  
ATOM   4227  C   GLU B 118       7.983  15.794 445.843  1.00 35.71      B    C  
ANISOU 4227  C   GLU B 118     5920   1972   5675  -1099   -588    430  B    C  
ATOM   4228  O   GLU B 118       9.026  16.434 445.867  1.00 59.07      B    O  
ANISOU 4228  O   GLU B 118     8865   4896   8682  -1206   -541    427  B    O  
ATOM   4229  CB  GLU B 118       7.428  14.716 448.037  1.00 51.20      B    C  
ANISOU 4229  CB  GLU B 118     7705   4005   7742   -734   -549    277  B    C  
ATOM   4230  CG  GLU B 118       7.266  13.453 448.859  1.00 44.38      B    C  
ANISOU 4230  CG  GLU B 118     6781   3179   6904   -575   -496    178  B    C  
ATOM   4231  CD  GLU B 118       6.701  13.714 450.262  1.00 51.42      B    C  
ANISOU 4231  CD  GLU B 118     7610   4142   7787   -410   -498    180  B    C  
ATOM   4232  OE1 GLU B 118       5.802  14.575 450.403  1.00 69.97      B    O  
ANISOU 4232  OE1 GLU B 118     9965   6517  10106   -389   -527    250  B    O  
ATOM   4233  OE2 GLU B 118       7.136  13.049 451.228  1.00 40.57      B    O1-
ANISOU 4233  OE2 GLU B 118     6188   2790   6436   -310   -469    116  B    O1-
ATOM   4234  N   ARG B 119       6.919  16.164 445.131  1.00 50.46      B    N  
ANISOU 4234  N   ARG B 119     7873   3858   7442  -1127   -684    556  B    N  
ATOM   4235  CA  ARG B 119       6.845  17.513 444.589  1.00 39.95      B    C  
ANISOU 4235  CA  ARG B 119     6611   2504   6064  -1230   -734    712  B    C  
ATOM   4236  C   ARG B 119       6.756  18.497 445.738  1.00 43.15      B    C  
ANISOU 4236  C   ARG B 119     6915   2894   6585  -1088   -716    708  B    C  
ATOM   4237  O   ARG B 119       6.223  18.194 446.808  1.00 54.84      B    O  
ANISOU 4237  O   ARG B 119     8306   4410   8122   -907   -704    632  B    O  
ATOM   4238  CB  ARG B 119       5.634  17.681 443.667  1.00 54.47      B    C  
ANISOU 4238  CB  ARG B 119     8557   4361   7778  -1273   -873    862  B    C  
ATOM   4239  CG  ARG B 119       5.712  16.882 442.390  1.00 50.00      B    C  
ANISOU 4239  CG  ARG B 119     8158   3815   7025  -1483   -899    881  B    C  
ATOM   4240  CD  ARG B 119       4.670  17.326 441.408  1.00 50.42      B    C  
ANISOU 4240  CD  ARG B 119     8343   3888   6925  -1576  -1070   1074  B    C  
ATOM   4241  NE  ARG B 119       4.496  16.378 440.309  1.00 66.93      B    N  
ANISOU 4241  NE  ARG B 119    10617   6018   8795  -1784  -1111   1069  B    N  
ATOM   4242  CZ  ARG B 119       3.771  15.260 440.385  1.00 84.86      B    C  
ANISOU 4242  CZ  ARG B 119    12883   8298  11061  -1734  -1163    971  B    C  
ATOM   4243  NH1 ARG B 119       3.148  14.926 441.517  1.00 75.18      B    N1+
ANISOU 4243  NH1 ARG B 119    11466   7058  10041  -1470  -1171    885  B    N1+
ATOM   4244  NH2 ARG B 119       3.663  14.472 439.322  1.00 88.16      B    N  
ANISOU 4244  NH2 ARG B 119    13500   8750  11248  -1973  -1182    946  B    N  
ATOM   4245  N   TYR B 120       7.288  19.685 445.510  1.00 65.56      B    N  
ANISOU 4245  N   TYR B 120     9787   5680   9441  -1192   -693    787  B    N  
ATOM   4246  CA  TYR B 120       7.512  20.621 446.596  1.00 67.15      B    C  
ANISOU 4246  CA  TYR B 120     9920   5846   9750  -1111   -645    748  B    C  
ATOM   4247  C   TYR B 120       7.494  22.033 446.033  1.00 70.20      B    C  
ANISOU 4247  C   TYR B 120    10375   6156  10141  -1208   -643    891  B    C  
ATOM   4248  O   TYR B 120       8.043  22.280 444.950  1.00 63.34      B    O  
ANISOU 4248  O   TYR B 120     9591   5266   9209  -1392   -634    984  B    O  
ATOM   4249  CB  TYR B 120       8.833  20.292 447.292  1.00 37.65      B    C  
ANISOU 4249  CB  TYR B 120     6114   2103   6090  -1152   -575    606  B    C  
ATOM   4250  CG  TYR B 120       9.501  21.453 447.943  1.00 38.46      B    C  
ANISOU 4250  CG  TYR B 120     6194   2143   6277  -1200   -532    586  B    C  
ATOM   4251  CD1 TYR B 120       9.008  21.991 449.110  1.00 37.70      B    C  
ANISOU 4251  CD1 TYR B 120     6068   2037   6218  -1068   -533    544  B    C  
ATOM   4252  CD2 TYR B 120      10.643  22.013 447.385  1.00 54.89      B    C  
ANISOU 4252  CD2 TYR B 120     8286   4171   8397  -1404   -476    600  B    C  
ATOM   4253  CE1 TYR B 120       9.634  23.056 449.716  1.00 41.11      B    C  
ANISOU 4253  CE1 TYR B 120     6499   2397   6724  -1136   -493    509  B    C  
ATOM   4254  CE2 TYR B 120      11.268  23.088 447.969  1.00 51.26      B    C  
ANISOU 4254  CE2 TYR B 120     7805   3645   8028  -1469   -433    569  B    C  
ATOM   4255  CZ  TYR B 120      10.759  23.608 449.139  1.00 49.93      B    C  
ANISOU 4255  CZ  TYR B 120     7622   3456   7892  -1335   -450    519  B    C  
ATOM   4256  OH  TYR B 120      11.384  24.678 449.749  1.00 67.74      B    O  
ANISOU 4256  OH  TYR B 120     9873   5632  10232  -1421   -406    470  B    O  
ATOM   4257  N   HIS B 121       6.839  22.943 446.762  1.00 73.72      B    N  
ANISOU 4257  N   HIS B 121    10798   6558  10654  -1094   -630    909  B    N  
ATOM   4258  CA  HIS B 121       6.825  24.370 446.456  1.00 63.09      B    C  
ANISOU 4258  CA  HIS B 121     9510   5108   9353  -1158   -597   1027  B    C  
ATOM   4259  C   HIS B 121       7.612  25.127 447.512  1.00 50.18      B    C  
ANISOU 4259  C   HIS B 121     7838   3402   7825  -1170   -496    915  B    C  
ATOM   4260  O   HIS B 121       7.450  24.873 448.708  1.00 45.90      B    O  
ANISOU 4260  O   HIS B 121     7239   2888   7313  -1052   -477    788  B    O  
ATOM   4261  CB  HIS B 121       5.399  24.936 446.432  1.00 71.76      B    C  
ANISOU 4261  CB  HIS B 121    10626   6176  10463  -1030   -643   1136  B    C  
ATOM   4262  CG  HIS B 121       4.633  24.617 445.190  1.00 99.84      B    C  
ANISOU 4262  CG  HIS B 121    14244   9770  13919  -1069   -774   1299  B    C  
ATOM   4263  CD2 HIS B 121       3.758  23.618 444.911  1.00104.62      B    C  
ANISOU 4263  CD2 HIS B 121    14831  10462  14457  -1009   -885   1306  B    C  
ATOM   4264  ND1 HIS B 121       4.707  25.393 444.050  1.00114.88      B    N  
ANISOU 4264  ND1 HIS B 121    16256  11621  15772  -1200   -812   1490  B    N  
ATOM   4265  CE1 HIS B 121       3.921  24.878 443.119  1.00111.13      B    C  
ANISOU 4265  CE1 HIS B 121    15834  11208  15183  -1227   -961   1614  B    C  
ATOM   4266  NE2 HIS B 121       3.335  23.801 443.615  1.00111.60      B    N  
ANISOU 4266  NE2 HIS B 121    15816  11346  15240  -1117  -1010   1498  B    N  
ATOM   4267  N   VAL B 122       8.436  26.075 447.067  1.00 52.43      B    N  
ANISOU 4267  N   VAL B 122     8168   3596   8157  -1328   -431    968  B    N  
ATOM   4268  CA  VAL B 122       9.108  26.985 447.990  1.00 60.48      B    C  
ANISOU 4268  CA  VAL B 122     9169   4523   9287  -1369   -340    870  B    C  
ATOM   4269  C   VAL B 122       8.089  27.943 448.596  1.00 65.87      B    C  
ANISOU 4269  C   VAL B 122     9894   5113  10020  -1244   -297    902  B    C  
ATOM   4270  O   VAL B 122       7.282  28.549 447.880  1.00 77.40      B    O  
ANISOU 4270  O   VAL B 122    11420   6512  11477  -1216   -302   1061  B    O  
ATOM   4271  CB  VAL B 122      10.219  27.762 447.270  1.00 54.22      B    C  
ANISOU 4271  CB  VAL B 122     8406   3647   8547  -1588   -262    922  B    C  
ATOM   4272  CG1 VAL B 122      10.928  28.632 448.241  1.00 47.44      B    C  
ANISOU 4272  CG1 VAL B 122     7522   2693   7809  -1652   -177    799  B    C  
ATOM   4273  CG2 VAL B 122      11.187  26.834 446.593  1.00 46.66      B    C  
ANISOU 4273  CG2 VAL B 122     7411   2778   7540  -1730   -273    896  B    C  
ATOM   4274  N   GLN B 123       8.149  28.121 449.914  1.00 60.09      B    N  
ANISOU 4274  N   GLN B 123     9137   4361   9334  -1184   -252    757  B    N  
ATOM   4275  CA  GLN B 123       7.175  28.934 450.637  1.00 65.84      B    C  
ANISOU 4275  CA  GLN B 123     9919   4997  10102  -1072   -181    759  B    C  
ATOM   4276  C   GLN B 123       7.874  29.611 451.814  1.00 74.39      B    C  
ANISOU 4276  C   GLN B 123    11019   5990  11255  -1141   -103    610  B    C  
ATOM   4277  O   GLN B 123       8.293  28.927 452.754  1.00 89.27      B    O  
ANISOU 4277  O   GLN B 123    12847   7959  13113  -1123   -139    468  B    O  
ATOM   4278  CB  GLN B 123       6.017  28.048 451.106  1.00 64.17      B    C  
ANISOU 4278  CB  GLN B 123     9666   4878   9837   -895   -284    755  B    C  
ATOM   4279  CG  GLN B 123       4.785  28.774 451.637  1.00 84.11      B    C  
ANISOU 4279  CG  GLN B 123    12243   7292  12424   -786   -284    805  B    C  
ATOM   4280  CD  GLN B 123       4.001  27.929 452.648  1.00 87.90      B    C  
ANISOU 4280  CD  GLN B 123    12666   7853  12877   -646   -336    722  B    C  
ATOM   4281  NE2 GLN B 123       3.304  28.598 453.574  1.00 81.69      B    N  
ANISOU 4281  NE2 GLN B 123    11932   6951  12154   -582   -284    692  B    N  
ATOM   4282  OE1 GLN B 123       4.040  26.692 452.604  1.00 88.20      B    O  
ANISOU 4282  OE1 GLN B 123    12628   8044  12841   -603   -403    681  B    O  
ATOM   4283  N   THR B 124       7.964  30.950 451.786  1.00 56.25      B    N  
ANISOU 4283  N   THR B 124     8812   3513   9049  -1225     -1    643  B    N  
ATOM   4284  CA  THR B 124       8.891  31.727 452.620  1.00 57.52      B    C  
ANISOU 4284  CA  THR B 124     8999   3571   9285  -1363     98    496  B    C  
ATOM   4285  C   THR B 124       8.123  32.602 453.613  1.00 55.14      B    C  
ANISOU 4285  C   THR B 124     8796   3129   9027  -1301    142    458  B    C  
ATOM   4286  O   THR B 124       7.522  33.608 453.220  1.00 60.61      B    O  
ANISOU 4286  O   THR B 124     9594   3672   9764  -1290    201    569  B    O  
ATOM   4287  CB  THR B 124       9.796  32.614 451.761  1.00 73.63      B    C  
ANISOU 4287  CB  THR B 124    11061   5503  11411  -1555    165    555  B    C  
ATOM   4288  CG2 THR B 124      10.782  33.376 452.644  1.00 76.36      B    C  
ANISOU 4288  CG2 THR B 124    11397   5786  11830  -1710    221    384  B    C  
ATOM   4289  OG1 THR B 124      10.547  31.815 450.844  1.00 76.49      B    O  
ANISOU 4289  OG1 THR B 124    11340   5978  11745  -1641     84    602  B    O  
ATOM   4290  N   SER B 125       8.150  32.242 454.894  1.00 48.71      B    N  
ANISOU 4290  N   SER B 125     7959   2357   8192  -1265    117    304  B    N  
ATOM   4291  CA  SER B 125       7.535  33.076 455.923  1.00 55.23      B    C  
ANISOU 4291  CA  SER B 125     8885   3055   9045  -1229    181    240  B    C  
ATOM   4292  C   SER B 125       8.020  32.617 457.291  1.00 66.55      B    C  
ANISOU 4292  C   SER B 125    10269   4560  10457  -1250    160     45  B    C  
ATOM   4293  O   SER B 125       8.733  31.619 457.415  1.00 86.50      B    O  
ANISOU 4293  O   SER B 125    12691   7230  12944  -1272     77    -22  B    O  
ATOM   4294  CB  SER B 125       6.013  33.026 455.872  1.00 49.95      B    C  
ANISOU 4294  CB  SER B 125     8282   2335   8362  -1048    159    359  B    C  
ATOM   4295  OG  SER B 125       5.557  31.896 456.565  1.00 49.09      B    O  
ANISOU 4295  OG  SER B 125     8102   2348   8200   -927     91    303  B    O  
ATOM   4296  N   ASN B 126       7.644  33.376 458.321  1.00 61.24      B    N  
ANISOU 4296  N   ASN B 126     9688   3776   9802  -1252    238    -46  B    N  
ATOM   4297  CA  ASN B 126       7.965  33.026 459.699  1.00 53.38      B    C  
ANISOU 4297  CA  ASN B 126     8652   2830   8799  -1270    229   -229  B    C  
ATOM   4298  C   ASN B 126       6.862  32.215 460.384  1.00 49.01      B    C  
ANISOU 4298  C   ASN B 126     8103   2325   8194  -1085    200   -214  B    C  
ATOM   4299  O   ASN B 126       6.867  32.082 461.617  1.00 49.18      B    O  
ANISOU 4299  O   ASN B 126     8114   2352   8221  -1083    221   -354  B    O  
ATOM   4300  CB  ASN B 126       8.289  34.283 460.512  1.00 59.39      B    C  
ANISOU 4300  CB  ASN B 126     9494   3450   9621  -1404    353   -370  B    C  
ATOM   4301  CG  ASN B 126       7.168  35.315 460.521  1.00 55.10      B    C  
ANISOU 4301  CG  ASN B 126     9201   2723   9013  -1352    448   -283  B    C  
ATOM   4302  ND2 ASN B 126       7.494  36.502 460.970  1.00 57.79      B    N  
ANISOU 4302  ND2 ASN B 126     9761   2920   9275  -1508    501   -364  B    N  
ATOM   4303  OD1 ASN B 126       6.029  35.038 460.180  1.00 54.37      B    O  
ANISOU 4303  OD1 ASN B 126     9183   2616   8861  -1192    398   -143  B    O  
ATOM   4304  N   TRP B 127       5.920  31.678 459.606  1.00 64.96      B    N  
ANISOU 4304  N   TRP B 127    10124   4380  10179   -941    155    -54  B    N  
ATOM   4305  CA  TRP B 127       4.814  30.914 460.173  1.00 55.76      B    C  
ANISOU 4305  CA  TRP B 127     8955   3263   8968   -774    138    -35  B    C  
ATOM   4306  C   TRP B 127       5.287  29.798 461.096  1.00 60.32      B    C  
ANISOU 4306  C   TRP B 127     9442   3971   9505   -755     75   -151  B    C  
ATOM   4307  O   TRP B 127       4.772  29.641 462.211  1.00 45.11      B    O  
ANISOU 4307  O   TRP B 127     7536   2032   7571   -695    122   -229  B    O  
ATOM   4308  CB  TRP B 127       3.945  30.328 459.061  1.00 45.46      B    C  
ANISOU 4308  CB  TRP B 127     7616   2010   7647   -652     67    137  B    C  
ATOM   4309  CG  TRP B 127       2.725  29.736 459.644  1.00 58.03      B    C  
ANISOU 4309  CG  TRP B 127     9214   3629   9205   -498     66    151  B    C  
ATOM   4310  CD1 TRP B 127       1.603  30.405 460.001  1.00 46.29      B    C  
ANISOU 4310  CD1 TRP B 127     7844   2020   7724   -426    120    181  B    C  
ATOM   4311  CD2 TRP B 127       2.485  28.353 459.949  1.00 71.54      B    C  
ANISOU 4311  CD2 TRP B 127    10829   5493  10861   -403      3    135  B    C  
ATOM   4312  CE2 TRP B 127       1.184  28.271 460.495  1.00 66.71      B    C  
ANISOU 4312  CE2 TRP B 127    10265   4845  10236   -284     45    153  B    C  
ATOM   4313  CE3 TRP B 127       3.231  27.174 459.800  1.00 56.50      B    C  
ANISOU 4313  CE3 TRP B 127     8796   3780   8893   -405   -108    110  B    C  
ATOM   4314  NE1 TRP B 127       0.674  29.542 460.521  1.00 45.26      B    N  
ANISOU 4314  NE1 TRP B 127     7684   1958   7553   -299    104    179  B    N  
ATOM   4315  CZ2 TRP B 127       0.619  27.061 460.899  1.00 48.43      B    C  
ANISOU 4315  CZ2 TRP B 127     7884   2646   7873   -180     18    145  B    C  
ATOM   4316  CZ3 TRP B 127       2.669  25.986 460.199  1.00 48.09      B    C  
ANISOU 4316  CZ3 TRP B 127     7668   2835   7769   -293   -150    107  B    C  
ATOM   4317  CH2 TRP B 127       1.376  25.936 460.742  1.00 39.59      B    C  
ANISOU 4317  CH2 TRP B 127     6639   1701   6702   -187    -78    123  B    C  
ATOM   4318  N   PHE B 128       6.275  29.015 460.651  1.00 43.40      B    N  
ANISOU 4318  N   PHE B 128     7182   1889   7421     40   -196   -156  B    N  
ATOM   4319  CA  PHE B 128       6.660  27.841 461.425  1.00 41.51      B    C  
ANISOU 4319  CA  PHE B 128     6696   1842   7235     26   -250   -192  B    C  
ATOM   4320  C   PHE B 128       7.394  28.242 462.688  1.00 42.12      B    C  
ANISOU 4320  C   PHE B 128     6708   1898   7398    -51   -302   -298  B    C  
ATOM   4321  O   PHE B 128       7.248  27.588 463.730  1.00 41.02      B    O  
ANISOU 4321  O   PHE B 128     6370   1891   7325     29   -371   -354  B    O  
ATOM   4322  CB  PHE B 128       7.516  26.882 460.605  1.00 40.66      B    C  
ANISOU 4322  CB  PHE B 128     6506   1804   7138   -131   -184   -132  B    C  
ATOM   4323  CG  PHE B 128       6.795  26.213 459.473  1.00 39.85      B    C  
ANISOU 4323  CG  PHE B 128     6445   1748   6948    -58   -150    -41  B    C  
ATOM   4324  CD1 PHE B 128       6.732  26.804 458.232  1.00 41.20      B    C  
ANISOU 4324  CD1 PHE B 128     6868   1764   7022   -119    -63     27  B    C  
ATOM   4325  CD2 PHE B 128       6.208  24.979 459.649  1.00 37.97      B    C  
ANISOU 4325  CD2 PHE B 128     5995   1696   6736     56   -186    -27  B    C  
ATOM   4326  CE1 PHE B 128       6.093  26.188 457.188  1.00 40.70      B    C  
ANISOU 4326  CE1 PHE B 128     6838   1730   6895    -62    -28    105  B    C  
ATOM   4327  CE2 PHE B 128       5.564  24.346 458.601  1.00 44.84      B    C  
ANISOU 4327  CE2 PHE B 128     6910   2600   7528    103   -165     48  B    C  
ATOM   4328  CZ  PHE B 128       5.509  24.966 457.367  1.00 46.54      B    C  
ANISOU 4328  CZ  PHE B 128     7383   2657   7643     47    -99    112  B    C  
ATOM   4329  N   GLU B 129       8.216  29.294 462.605  1.00 44.08      B    N  
ANISOU 4329  N   GLU B 129     7126   1972   7650   -224   -264   -329  B    N  
ATOM   4330  CA  GLU B 129       8.915  29.782 463.789  1.00 45.06      B    C  
ANISOU 4330  CA  GLU B 129     7211   2057   7853   -317   -330   -441  B    C  
ATOM   4331  C   GLU B 129       7.929  30.268 464.844  1.00 47.56      B    C  
ANISOU 4331  C   GLU B 129     7565   2359   8148   -112   -411   -526  B    C  
ATOM   4332  O   GLU B 129       8.040  29.886 466.015  1.00 53.41      B    O  
ANISOU 4332  O   GLU B 129     8165   3186   8943    -81   -496   -611  B    O  
ATOM   4333  CB  GLU B 129       9.873  30.910 463.403  1.00 47.47      B    C  
ANISOU 4333  CB  GLU B 129     7719   2165   8155   -557   -260   -461  B    C  
ATOM   4334  CG  GLU B 129      11.064  30.540 462.533  1.00 47.83      B    C  
ANISOU 4334  CG  GLU B 129     7725   2220   8227   -812   -185   -404  B    C  
ATOM   4335  CD  GLU B 129      10.735  30.192 461.081  1.00 56.34      B    C  
ANISOU 4335  CD  GLU B 129     8925   3285   9198   -802    -86   -283  B    C  
ATOM   4336  OE1 GLU B 129       9.551  30.100 460.701  1.00 59.57      B    O  
ANISOU 4336  OE1 GLU B 129     9397   3699   9539   -586    -64   -236  B    O  
ATOM   4337  OE2 GLU B 129      11.688  30.008 460.298  1.00 68.32      B    O1-
ANISOU 4337  OE2 GLU B 129    10450   4792  10716  -1021    -49   -233  B    O1-
ATOM   4338  N   ILE B 130       6.911  31.045 464.433  1.00 50.59      B    N  
ANISOU 4338  N   ILE B 130     8114   2640   8466     43   -386   -504  B    N  
ATOM   4339  CA  ILE B 130       5.881  31.495 465.373  1.00 46.82      B    C  
ANISOU 4339  CA  ILE B 130     7657   2157   7975    258   -452   -589  B    C  
ATOM   4340  C   ILE B 130       5.129  30.299 465.968  1.00 44.77      B    C  
ANISOU 4340  C   ILE B 130     7177   2116   7718    426   -498   -598  B    C  
ATOM   4341  O   ILE B 130       4.878  30.250 467.181  1.00 44.89      B    O  
ANISOU 4341  O   ILE B 130     7137   2174   7745    508   -550   -705  B    O  
ATOM   4342  CB  ILE B 130       4.938  32.505 464.692  1.00 48.48      B    C  
ANISOU 4342  CB  ILE B 130     8035   2224   8159    400   -432   -552  B    C  
ATOM   4343  CG1 ILE B 130       5.716  33.765 464.329  1.00 54.01      B    C  
ANISOU 4343  CG1 ILE B 130     8939   2691   8891    226   -392   -565  B    C  
ATOM   4344  CG2 ILE B 130       3.792  32.879 465.602  1.00 49.20      B    C  
ANISOU 4344  CG2 ILE B 130     8122   2329   8244    644   -490   -643  B    C  
ATOM   4345  CD1 ILE B 130       4.926  34.805 463.579  1.00 52.92      B    C  
ANISOU 4345  CD1 ILE B 130     8959   2390   8756    349   -411   -516  B    C  
ATOM   4346  N   GLN B 131       4.752  29.326 465.132  1.00 43.11      B    N  
ANISOU 4346  N   GLN B 131     6848   2036   7494    468   -472   -493  B    N  
ATOM   4347  CA  GLN B 131       4.191  28.074 465.645  1.00 41.23      B    C  
ANISOU 4347  CA  GLN B 131     6381   2006   7277    578   -498   -496  B    C  
ATOM   4348  C   GLN B 131       5.094  27.422 466.693  1.00 52.81      B    C  
ANISOU 4348  C   GLN B 131     7699   3548   8819    472   -536   -562  B    C  
ATOM   4349  O   GLN B 131       4.619  26.999 467.751  1.00 40.16      B    O  
ANISOU 4349  O   GLN B 131     5998   2033   7230    578   -572   -636  B    O  
ATOM   4350  CB  GLN B 131       3.959  27.090 464.495  1.00 57.27      B    C  
ANISOU 4350  CB  GLN B 131     8322   4146   9291    572   -461   -375  B    C  
ATOM   4351  CG  GLN B 131       2.747  27.377 463.659  1.00 55.84      B    C  
ANISOU 4351  CG  GLN B 131     8214   3947   9054    727   -465   -317  B    C  
ATOM   4352  CD  GLN B 131       1.610  27.907 464.481  1.00 53.09      B    C  
ANISOU 4352  CD  GLN B 131     7855   3604   8712    936   -507   -399  B    C  
ATOM   4353  NE2 GLN B 131       1.309  29.209 464.320  1.00 52.77      B    N  
ANISOU 4353  NE2 GLN B 131     7998   3392   8660   1002   -518   -420  B    N  
ATOM   4354  OE1 GLN B 131       1.015  27.164 465.282  1.00 43.78      B    O  
ANISOU 4354  OE1 GLN B 131     6503   2574   7557   1036   -518   -448  B    O  
ATOM   4355  N   PHE B 132       6.401  27.337 466.416  1.00 43.78      B    N  
ANISOU 4355  N   PHE B 132     6532   2366   7735    261   -527   -542  B    N  
ATOM   4356  CA  PHE B 132       7.322  26.699 467.354  1.00 43.30      B    C  
ANISOU 4356  CA  PHE B 132     6300   2372   7781    159   -586   -600  B    C  
ATOM   4357  C   PHE B 132       7.344  27.435 468.692  1.00 42.89      B    C  
ANISOU 4357  C   PHE B 132     6336   2240   7721    178   -675   -741  B    C  
ATOM   4358  O   PHE B 132       7.210  26.816 469.758  1.00 41.23      B    O  
ANISOU 4358  O   PHE B 132     6021   2112   7535    241   -741   -808  B    O  
ATOM   4359  CB  PHE B 132       8.747  26.672 466.779  1.00 49.78      B    C  
ANISOU 4359  CB  PHE B 132     7066   3152   8695    -78   -558   -567  B    C  
ATOM   4360  CG  PHE B 132       9.066  25.473 465.918  1.00 58.33      B    C  
ANISOU 4360  CG  PHE B 132     7969   4360   9836   -114   -483   -465  B    C  
ATOM   4361  CD1 PHE B 132       9.104  24.182 466.454  1.00 58.47      B    C  
ANISOU 4361  CD1 PHE B 132     7755   4526   9936    -56   -511   -456  B    C  
ATOM   4362  CD2 PHE B 132       9.394  25.646 464.565  1.00 67.46      B    C  
ANISOU 4362  CD2 PHE B 132     9212   5464  10956   -216   -379   -384  B    C  
ATOM   4363  CE1 PHE B 132       9.421  23.083 465.638  1.00 60.55      B    C  
ANISOU 4363  CE1 PHE B 132     7867   4888  10252    -85   -428   -369  B    C  
ATOM   4364  CE2 PHE B 132       9.709  24.552 463.742  1.00 67.12      B    C  
ANISOU 4364  CE2 PHE B 132     9023   5524  10957   -250   -295   -306  B    C  
ATOM   4365  CZ  PHE B 132       9.723  23.269 464.276  1.00 57.48      B    C  
ANISOU 4365  CZ  PHE B 132     7559   4453   9826   -180   -316   -301  B    C  
ATOM   4366  N   GLN B 133       7.497  28.763 468.656  1.00 43.59      B    N  
ANISOU 4366  N   GLN B 133     6645   2155   7763    122   -675   -794  B    N  
ATOM   4367  CA  GLN B 133       7.559  29.522 469.901  1.00 46.42      B    C  
ANISOU 4367  CA  GLN B 133     7119   2423   8096    125   -757   -944  B    C  
ATOM   4368  C   GLN B 133       6.275  29.363 470.702  1.00 49.18      B    C  
ANISOU 4368  C   GLN B 133     7479   2834   8375    371   -759  -1013  B    C  
ATOM   4369  O   GLN B 133       6.309  29.113 471.913  1.00 45.37      B    O  
ANISOU 4369  O   GLN B 133     6974   2383   7880    396   -833  -1128  B    O  
ATOM   4370  CB  GLN B 133       7.821  31.006 469.619  1.00 47.56      B    C  
ANISOU 4370  CB  GLN B 133     7518   2356   8196     33   -731   -982  B    C  
ATOM   4371  CG  GLN B 133       7.664  31.884 470.860  1.00 51.73      B    C  
ANISOU 4371  CG  GLN B 133     8206   2779   8671     68   -799  -1146  B    C  
ATOM   4372  CD  GLN B 133       8.402  33.191 470.750  1.00 83.75      B    C  
ANISOU 4372  CD  GLN B 133    12470   6631  12722   -118   -795  -1198  B    C  
ATOM   4373  NE2 GLN B 133       7.788  34.260 471.246  1.00 81.07      B    N  
ANISOU 4373  NE2 GLN B 133    12337   6150  12316    -13   -786  -1299  B    N  
ATOM   4374  OE1 GLN B 133       9.516  33.248 470.224  1.00100.98      B    O  
ANISOU 4374  OE1 GLN B 133    14618   8780  14968   -359   -789  -1155  B    O  
ATOM   4375  N   ARG B 134       5.129  29.496 470.031  1.00 45.70      B    N  
ANISOU 4375  N   ARG B 134     7070   2410   7884    550   -680   -952  B    N  
ATOM   4376  CA  ARG B 134       3.850  29.418 470.718  1.00 45.85      B    C  
ANISOU 4376  CA  ARG B 134     7075   2492   7853    784   -657  -1025  B    C  
ATOM   4377  C   ARG B 134       3.601  28.023 471.270  1.00 45.93      B    C  
ANISOU 4377  C   ARG B 134     6871   2693   7889    836   -664  -1023  B    C  
ATOM   4378  O   ARG B 134       3.171  27.870 472.418  1.00 50.61      B    O  
ANISOU 4378  O   ARG B 134     7463   3319   8445    934   -674  -1146  B    O  
ATOM   4379  CB  ARG B 134       2.734  29.835 469.766  1.00 59.11      B    C  
ANISOU 4379  CB  ARG B 134     8795   4157   9508    948   -591   -950  B    C  
ATOM   4380  CG  ARG B 134       1.327  29.534 470.264  1.00 74.48      B    C  
ANISOU 4380  CG  ARG B 134    10647   6215  11437   1192   -551  -1005  B    C  
ATOM   4381  CD  ARG B 134       0.279  30.318 469.487  1.00 85.73      B    C  
ANISOU 4381  CD  ARG B 134    12139   7576  12858   1358   -521   -965  B    C  
ATOM   4382  NE  ARG B 134      -1.081  29.943 469.867  1.00 92.72      B    N  
ANISOU 4382  NE  ARG B 134    12881   8593  13753   1585   -478  -1013  B    N  
ATOM   4383  CZ  ARG B 134      -1.768  28.960 469.295  1.00 92.14      B    C  
ANISOU 4383  CZ  ARG B 134    12615   8689  13706   1645   -469   -926  B    C  
ATOM   4384  NH1 ARG B 134      -1.221  28.251 468.308  1.00 81.69      B    N1+
ANISOU 4384  NH1 ARG B 134    11239   7413  12386   1503   -499   -788  B    N1+
ATOM   4385  NH2 ARG B 134      -3.004  28.690 469.710  1.00 94.29      B    N  
ANISOU 4385  NH2 ARG B 134    12743   9081  14000   1841   -422   -987  B    N  
ATOM   4386  N   ALA B 135       3.846  26.987 470.464  1.00 43.38      B    N  
ANISOU 4386  N   ALA B 135     6379   2485   7617    773   -647   -889  B    N  
ATOM   4387  CA  ALA B 135       3.636  25.630 470.952  1.00 39.80      B    C  
ANISOU 4387  CA  ALA B 135     5731   2194   7195    811   -645   -874  B    C  
ATOM   4388  C   ALA B 135       4.503  25.361 472.156  1.00 46.44      B    C  
ANISOU 4388  C   ALA B 135     6567   3013   8066    720   -739   -973  B    C  
ATOM   4389  O   ALA B 135       4.027  24.830 473.169  1.00 48.46      B    O  
ANISOU 4389  O   ALA B 135     6794   3335   8284    812   -747  -1052  B    O  
ATOM   4390  CB  ALA B 135       3.935  24.612 469.864  1.00 37.96      B    C  
ANISOU 4390  CB  ALA B 135     5345   2065   7012    732   -610   -719  B    C  
ATOM   4391  N   PHE B 136       5.775  25.762 472.078  1.00 56.23      B    N  
ANISOU 4391  N   PHE B 136     7843   4160   9361    531   -816   -977  B    N  
ATOM   4392  CA  PHE B 136       6.685  25.519 473.187  1.00 41.56      B    C  
ANISOU 4392  CA  PHE B 136     5972   2295   7526    422   -946  -1065  B    C  
ATOM   4393  C   PHE B 136       6.250  26.274 474.432  1.00 43.39      B    C  
ANISOU 4393  C   PHE B 136     6391   2489   7605    490   -982  -1228  B    C  
ATOM   4394  O   PHE B 136       6.258  25.711 475.533  1.00 47.13      B    O  
ANISOU 4394  O   PHE B 136     6846   3110   7950    494  -1016  -1265  B    O  
ATOM   4395  CB  PHE B 136       8.103  25.890 472.789  1.00 42.24      B    C  
ANISOU 4395  CB  PHE B 136     6032   2291   7727    193  -1023  -1049  B    C  
ATOM   4396  CG  PHE B 136       8.832  24.783 472.097  1.00 46.91      B    C  
ANISOU 4396  CG  PHE B 136     6386   2995   8443    105  -1004   -919  B    C  
ATOM   4397  CD1 PHE B 136       8.127  23.845 471.331  1.00 40.86      B    C  
ANISOU 4397  CD1 PHE B 136     5509   2332   7683    219   -892   -800  B    C  
ATOM   4398  CD2 PHE B 136      10.212  24.667 472.203  1.00 41.63      B    C  
ANISOU 4398  CD2 PHE B 136     5594   2348   7877    -89  -1091   -918  B    C  
ATOM   4399  CE1 PHE B 136       8.795  22.818 470.662  1.00 40.45      B    C  
ANISOU 4399  CE1 PHE B 136     5262   2363   7746    148   -861   -692  B    C  
ATOM   4400  CE2 PHE B 136      10.887  23.641 471.546  1.00 40.61      B    C  
ANISOU 4400  CE2 PHE B 136     5234   2323   7875   -145  -1053   -810  B    C  
ATOM   4401  CZ  PHE B 136      10.181  22.716 470.776  1.00 38.69      B    C  
ANISOU 4401  CZ  PHE B 136     4915   2150   7636    -23   -932   -699  B    C  
ATOM   4402  N   GLN B 137       5.860  27.543 474.284  1.00 44.81      B    N  
ANISOU 4402  N   GLN B 137     6772   2496   7760    541   -956  -1312  B    N  
ATOM   4403  CA  GLN B 137       5.414  28.304 475.445  1.00 46.82      B    C  
ANISOU 4403  CA  GLN B 137     7233   2672   7884    625   -978  -1497  B    C  
ATOM   4404  C   GLN B 137       4.176  27.665 476.063  1.00 46.48      B    C  
ANISOU 4404  C   GLN B 137     7134   2795   7730    832   -866  -1530  B    C  
ATOM   4405  O   GLN B 137       4.089  27.513 477.290  1.00 47.56      B    O  
ANISOU 4405  O   GLN B 137     7342   3029   7701    835   -870  -1627  B    O  
ATOM   4406  CB  GLN B 137       5.157  29.762 475.054  1.00 50.44      B    C  
ANISOU 4406  CB  GLN B 137     7889   2975   8300    647   -916  -1530  B    C  
ATOM   4407  CG  GLN B 137       4.771  30.706 476.205  1.00 59.75      B    C  
ANISOU 4407  CG  GLN B 137     9307   4052   9344    722   -919  -1729  B    C  
ATOM   4408  CD  GLN B 137       5.851  30.855 477.287  1.00 76.25      B    C  
ANISOU 4408  CD  GLN B 137    11516   6089  11366    528  -1084  -1858  B    C  
ATOM   4409  NE2 GLN B 137       5.804  29.991 478.298  1.00 75.81      B    N  
ANISOU 4409  NE2 GLN B 137    11423   6177  11206    548  -1133  -1917  B    N  
ATOM   4410  OE1 GLN B 137       6.697  31.751 477.222  1.00 80.77      B    O  
ANISOU 4410  OE1 GLN B 137    12209   6530  11948    347  -1150  -1885  B    O  
ATOM   4411  N   LYS B 138       3.230  27.235 475.226  1.00 45.15      B    N  
ANISOU 4411  N   LYS B 138     6835   2683   7638    984   -761  -1443  B    N  
ATOM   4412  CA  LYS B 138       1.996  26.676 475.762  1.00 45.16      B    C  
ANISOU 4412  CA  LYS B 138     6754   2856   7548   1162   -632  -1478  B    C  
ATOM   4413  C   LYS B 138       2.239  25.366 476.484  1.00 44.21      B    C  
ANISOU 4413  C   LYS B 138     6505   2972   7321   1071   -620  -1410  B    C  
ATOM   4414  O   LYS B 138       1.652  25.132 477.545  1.00 54.83      B    O  
ANISOU 4414  O   LYS B 138     7892   4437   8506   1131   -540  -1495  B    O  
ATOM   4415  CB  LYS B 138       0.938  26.515 474.671  1.00 44.24      B    C  
ANISOU 4415  CB  LYS B 138     6503   2769   7539   1322   -542  -1391  B    C  
ATOM   4416  CG  LYS B 138       0.339  27.840 474.301  1.00 45.96      B    C  
ANISOU 4416  CG  LYS B 138     6855   2879   7730   1429   -493  -1424  B    C  
ATOM   4417  CD  LYS B 138      -0.919  27.734 473.518  1.00 45.81      B    C  
ANISOU 4417  CD  LYS B 138     6702   2955   7749   1600   -403  -1350  B    C  
ATOM   4418  CE  LYS B 138      -1.502  29.140 473.314  1.00 76.79      B    C  
ANISOU 4418  CE  LYS B 138    10780   6740  11658   1728   -373  -1401  B    C  
ATOM   4419  NZ  LYS B 138      -1.729  29.954 474.589  1.00 50.57      B    N1+
ANISOU 4419  NZ  LYS B 138     7621   3332   8261   1823   -321  -1613  B    N1+
ATOM   4420  N   LEU B 139       3.112  24.513 475.953  1.00 42.53      B    N  
ANISOU 4420  N   LEU B 139     6155   2820   7186    928   -693  -1261  B    N  
ATOM   4421  CA  LEU B 139       3.431  23.284 476.674  1.00 41.95      B    C  
ANISOU 4421  CA  LEU B 139     5991   2938   7011    849   -711  -1191  B    C  
ATOM   4422  C   LEU B 139       4.189  23.562 477.972  1.00 43.70      B    C  
ANISOU 4422  C   LEU B 139     6371   3160   7075    745   -828  -1289  B    C  
ATOM   4423  O   LEU B 139       3.871  22.971 479.006  1.00 44.40      B    O  
ANISOU 4423  O   LEU B 139     6505   3383   6980    755   -798  -1310  B    O  
ATOM   4424  CB  LEU B 139       4.196  22.335 475.759  1.00 40.04      B    C  
ANISOU 4424  CB  LEU B 139     5568   2739   6908    747   -762  -1022  B    C  
ATOM   4425  CG  LEU B 139       3.322  21.896 474.579  1.00 38.49      B    C  
ANISOU 4425  CG  LEU B 139     5238   2566   6819    845   -647   -927  B    C  
ATOM   4426  CD1 LEU B 139       4.116  21.327 473.405  1.00 37.45      B    C  
ANISOU 4426  CD1 LEU B 139     4978   2407   6843    747   -682   -789  B    C  
ATOM   4427  CD2 LEU B 139       2.277  20.902 475.051  1.00 38.15      B    C  
ANISOU 4427  CD2 LEU B 139     5113   2708   6675    925   -533   -898  B    C  
ATOM   4428  N   ARG B 140       5.169  24.479 477.961  1.00 44.73      B    N  
ANISOU 4428  N   ARG B 140     6603   3135   7257    631   -963  -1354  B    N  
ATOM   4429  CA  ARG B 140       5.847  24.823 479.216  1.00 47.63      B    C  
ANISOU 4429  CA  ARG B 140     7137   3496   7464    525  -1099  -1464  B    C  
ATOM   4430  C   ARG B 140       4.885  25.360 480.258  1.00 48.60      B    C  
ANISOU 4430  C   ARG B 140     7473   3620   7374    640   -998  -1627  B    C  
ATOM   4431  O   ARG B 140       5.166  25.263 481.457  1.00 51.83      B    O  
ANISOU 4431  O   ARG B 140     8028   4088   7579    575  -1074  -1700  B    O  
ATOM   4432  CB  ARG B 140       6.974  25.846 479.025  1.00 48.66      B    C  
ANISOU 4432  CB  ARG B 140     7349   3447   7694    366  -1255  -1530  B    C  
ATOM   4433  CG  ARG B 140       8.311  25.203 478.781  1.00 60.10      B    C  
ANISOU 4433  CG  ARG B 140     8615   4956   9264    191  -1416  -1422  B    C  
ATOM   4434  CD  ARG B 140       9.467  26.171 478.787  1.00 66.11      B    C  
ANISOU 4434  CD  ARG B 140     9438   5570  10111     -3  -1576  -1505  B    C  
ATOM   4435  NE  ARG B 140       9.103  27.551 478.520  1.00 62.73      B    N  
ANISOU 4435  NE  ARG B 140     9223   4918   9694      9  -1519  -1627  B    N  
ATOM   4436  CZ  ARG B 140       8.936  28.036 477.298  1.00 71.37      B    C  
ANISOU 4436  CZ  ARG B 140    10294   5871  10951     25  -1420  -1578  B    C  
ATOM   4437  NH1 ARG B 140       9.085  27.225 476.254  1.00 71.40      B    N1+
ANISOU 4437  NH1 ARG B 140    10069   5954  11107     25  -1355  -1418  B    N1+
ATOM   4438  NH2 ARG B 140       8.624  29.322 477.119  1.00 65.78      B    N  
ANISOU 4438  NH2 ARG B 140     9818   4932  10243     43  -1391  -1688  B    N  
ATOM   4439  N   ASN B 141       3.772  25.962 479.831  1.00 57.18      B    N  
ANISOU 4439  N   ASN B 141     8589   4636   8501    815   -834  -1694  B    N  
ATOM   4440  CA  ASN B 141       2.813  26.481 480.798  1.00 50.77      B    C  
ANISOU 4440  CA  ASN B 141     7956   3829   7505    947   -703  -1868  B    C  
ATOM   4441  C   ASN B 141       1.955  25.404 481.448  1.00 50.61      B    C  
ANISOU 4441  C   ASN B 141     7858   4040   7331   1011   -549  -1835  B    C  
ATOM   4442  O   ASN B 141       1.356  25.670 482.495  1.00 52.86      B    O  
ANISOU 4442  O   ASN B 141     8308   4363   7412   1071   -438  -1981  B    O  
ATOM   4443  CB  ASN B 141       1.914  27.515 480.143  1.00 56.01      B    C  
ANISOU 4443  CB  ASN B 141     8662   4333   8288   1138   -589  -1962  B    C  
ATOM   4444  CG  ASN B 141       2.591  28.848 480.014  1.00 56.86      B    C  
ANISOU 4444  CG  ASN B 141     8986   4174   8446   1078   -712  -2069  B    C  
ATOM   4445  ND2 ASN B 141       2.148  29.651 479.049  1.00 60.11      B    N  
ANISOU 4445  ND2 ASN B 141     9416   4404   9021   1204   -678  -2077  B    N  
ATOM   4446  OD1 ASN B 141       3.499  29.165 480.782  1.00 60.02      B    O  
ANISOU 4446  OD1 ASN B 141     9550   4522   8734    913   -847  -2143  B    O  
ATOM   4447  N   CYS B 142       1.898  24.204 480.875  1.00 50.80      B    N  
ANISOU 4447  N   CYS B 142     7658   4210   7436    986   -528  -1653  B    N  
ATOM   4448  CA  CYS B 142       1.125  23.117 481.467  1.00 48.44      B    C  
ANISOU 4448  CA  CYS B 142     7296   4119   6990   1011   -382  -1605  B    C  
ATOM   4449  C   CYS B 142       1.770  22.607 482.742  1.00 49.74      B    C  
ANISOU 4449  C   CYS B 142     7633   4364   6903    874   -478  -1608  B    C  
ATOM   4450  O   CYS B 142       2.946  22.228 482.751  1.00 49.19      B    O  
ANISOU 4450  O   CYS B 142     7558   4279   6855    738   -691  -1513  B    O  
ATOM   4451  CB  CYS B 142       0.992  21.972 480.487  1.00 45.97      B    C  
ANISOU 4451  CB  CYS B 142     6729   3907   6829   1000   -359  -1409  B    C  
ATOM   4452  SG  CYS B 142       0.020  22.445 479.136  1.00 44.93      B    S  
ANISOU 4452  SG  CYS B 142     6423   3715   6934   1166   -246  -1407  B    S  
ATOM   4453  N   LYS B 143       0.987  22.577 483.816  1.00 52.74      B    N  
ANISOU 4453  N   LYS B 143     8163   4834   7043    913   -318  -1718  B    N  
ATOM   4454  CA  LYS B 143       1.473  22.114 485.099  1.00 59.08      B    C  
ANISOU 4454  CA  LYS B 143     9182   5709   7555    786   -400  -1725  B    C  
ATOM   4455  C   LYS B 143       0.888  20.767 485.475  1.00 59.48      B    C  
ANISOU 4455  C   LYS B 143     9183   5950   7468    754   -266  -1599  B    C  
ATOM   4456  O   LYS B 143       1.310  20.177 486.476  1.00 54.51      B    O  
ANISOU 4456  O   LYS B 143     8741   5382   6588    640   -350  -1560  B    O  
ATOM   4457  CB  LYS B 143       1.124  23.145 486.180  1.00 59.06      B    C  
ANISOU 4457  CB  LYS B 143     9470   5647   7323    822   -317  -1960  B    C  
ATOM   4458  CG  LYS B 143       1.546  24.554 485.823  1.00 66.38      B    C  
ANISOU 4458  CG  LYS B 143    10480   6359   8380    860   -420  -2103  B    C  
ATOM   4459  CD  LYS B 143       2.741  25.020 486.626  1.00 76.52      B    C  
ANISOU 4459  CD  LYS B 143    12014   7549   9510    697   -680  -2171  B    C  
ATOM   4460  CE  LYS B 143       3.350  26.245 485.971  1.00 85.92      B    C  
ANISOU 4460  CE  LYS B 143    13230   8516  10902    688   -815  -2256  B    C  
ATOM   4461  NZ  LYS B 143       2.304  27.262 485.649  1.00 80.94      B    N1+
ANISOU 4461  NZ  LYS B 143    12645   7765  10345    884   -599  -2416  B    N1+
ATOM   4462  N   THR B 144      -0.049  20.264 484.683  1.00 56.15      B    N  
ANISOU 4462  N   THR B 144     8526   5610   7199    838    -76  -1530  B    N  
ATOM   4463  CA  THR B 144      -0.842  19.095 485.015  1.00 51.88      B    C  
ANISOU 4463  CA  THR B 144     7936   5241   6533    802    107  -1439  B    C  
ATOM   4464  C   THR B 144      -0.907  18.188 483.811  1.00 49.17      B    C  
ANISOU 4464  C   THR B 144     7316   4935   6431    801     92  -1254  B    C  
ATOM   4465  O   THR B 144      -1.035  18.669 482.686  1.00 47.63      B    O  
ANISOU 4465  O   THR B 144     6934   4670   6494    893     80  -1256  B    O  
ATOM   4466  CB  THR B 144      -2.266  19.510 485.434  1.00 66.85      B    C  
ANISOU 4466  CB  THR B 144     9827   7227   8345    910    430  -1605  B    C  
ATOM   4467  CG2 THR B 144      -3.233  18.330 485.419  1.00 78.97      B    C  
ANISOU 4467  CG2 THR B 144    11218   8945   9844    868    652  -1504  B    C  
ATOM   4468  OG1 THR B 144      -2.229  20.112 486.734  1.00 56.71      B    O  
ANISOU 4468  OG1 THR B 144     8851   5930   6768    885    479  -1772  B    O  
ATOM   4469  N   HIS B 145      -0.869  16.880 484.067  1.00 59.89      B    N  
ANISOU 4469  N   HIS B 145     8677   6391   7685    695     98  -1097  B    N  
ATOM   4470  CA  HIS B 145      -1.146  15.866 483.055  1.00 46.76      B    C  
ANISOU 4470  CA  HIS B 145     6784   4778   6206    682    133   -933  B    C  
ATOM   4471  C   HIS B 145      -2.340  16.231 482.159  1.00 51.51      B    C  
ANISOU 4471  C   HIS B 145     7147   5423   7003    800    331   -998  B    C  
ATOM   4472  O   HIS B 145      -2.221  16.246 480.925  1.00 44.13      B    O  
ANISOU 4472  O   HIS B 145     6022   4429   6314    848    259   -932  B    O  
ATOM   4473  CB  HIS B 145      -1.359  14.543 483.784  1.00 47.62      B    C  
ANISOU 4473  CB  HIS B 145     6999   4994   6102    557    203   -809  B    C  
ATOM   4474  CG  HIS B 145      -1.815  13.433 482.906  1.00 46.00      B    C  
ANISOU 4474  CG  HIS B 145     6596   4842   6041    523    277   -658  B    C  
ATOM   4475  CD2 HIS B 145      -3.053  12.937 482.675  1.00 46.27      B    C  
ANISOU 4475  CD2 HIS B 145     6491   4994   6096    508    519   -655  B    C  
ATOM   4476  ND1 HIS B 145      -0.947  12.689 482.136  1.00 44.07      B    N  
ANISOU 4476  ND1 HIS B 145     6275   4523   5947    493     89   -496  B    N  
ATOM   4477  CE1 HIS B 145      -1.633  11.784 481.461  1.00 54.37      B    C  
ANISOU 4477  CE1 HIS B 145     7431   5884   7344    460    210   -400  B    C  
ATOM   4478  NE2 HIS B 145      -2.913  11.915 481.767  1.00 65.58      B    N  
ANISOU 4478  NE2 HIS B 145     8802   7424   8690    458    461   -491  B    N  
ATOM   4479  N   ASN B 146      -3.498  16.537 482.760  1.00 54.91      B    N  
ANISOU 4479  N   ASN B 146     7583   5957   7325    851    578  -1133  B    N  
ATOM   4480  CA  ASN B 146      -4.664  16.954 481.974  1.00 63.80      B    C  
ANISOU 4480  CA  ASN B 146     8459   7132   8650    987    745  -1212  B    C  
ATOM   4481  C   ASN B 146      -4.338  18.139 481.073  1.00 47.09      B    C  
ANISOU 4481  C   ASN B 146     6281   4855   6755   1133    605  -1281  B    C  
ATOM   4482  O   ASN B 146      -4.542  18.087 479.855  1.00 45.44      B    O  
ANISOU 4482  O   ASN B 146     5872   4616   6776   1190    556  -1211  B    O  
ATOM   4483  CB  ASN B 146      -5.843  17.331 482.885  1.00 70.61      B    C  
ANISOU 4483  CB  ASN B 146     9339   8120   9371   1045   1032  -1390  B    C  
ATOM   4484  CG  ASN B 146      -6.565  16.129 483.468  1.00 68.24      B    C  
ANISOU 4484  CG  ASN B 146     9016   8003   8910    900   1244  -1322  B    C  
ATOM   4485  ND2 ASN B 146      -7.185  16.324 484.636  1.00 64.09      B    N  
ANISOU 4485  ND2 ASN B 146     8624   7575   8151    881   1480  -1461  B    N  
ATOM   4486  OD1 ASN B 146      -6.577  15.046 482.881  1.00 72.34      B    O  
ANISOU 4486  OD1 ASN B 146     9415   8566   9504    796   1211  -1151  B    O  
ATOM   4487  N   ASP B 147      -3.834  19.226 481.657  1.00 48.31      B    N  
ANISOU 4487  N   ASP B 147     6635   4892   6828   1182    537  -1417  B    N  
ATOM   4488  CA  ASP B 147      -3.568  20.403 480.839  1.00 56.69      B    C  
ANISOU 4488  CA  ASP B 147     7675   5778   8086   1308    419  -1485  B    C  
ATOM   4489  C   ASP B 147      -2.597  20.076 479.716  1.00 53.33      B    C  
ANISOU 4489  C   ASP B 147     7169   5256   7838   1236    206  -1316  B    C  
ATOM   4490  O   ASP B 147      -2.821  20.472 478.568  1.00 44.08      B    O  
ANISOU 4490  O   ASP B 147     5865   4006   6878   1326    171  -1292  B    O  
ATOM   4491  CB  ASP B 147      -3.027  21.569 481.682  1.00 49.61      B    C  
ANISOU 4491  CB  ASP B 147     7045   4747   7060   1332    357  -1652  B    C  
ATOM   4492  CG  ASP B 147      -3.986  22.016 482.771  1.00 75.91      B    C  
ANISOU 4492  CG  ASP B 147    10479   8153  10209   1421    591  -1850  B    C  
ATOM   4493  OD1 ASP B 147      -4.046  21.345 483.823  1.00 87.84      B    O1-
ANISOU 4493  OD1 ASP B 147    12112   9791  11471   1308    688  -1849  B    O1-
ATOM   4494  OD2 ASP B 147      -4.669  23.050 482.591  1.00 72.41      B    O1-
ANISOU 4494  OD2 ASP B 147    10015   7634   9865   1608    683  -2009  B    O1-
ATOM   4495  N   LEU B 148      -1.558  19.284 480.000  1.00 44.24      B    N  
ANISOU 4495  N   LEU B 148     6089   4115   6604   1078     71  -1193  B    N  
ATOM   4496  CA  LEU B 148      -0.589  18.988 478.956  1.00 42.07      B    C  
ANISOU 4496  CA  LEU B 148     5726   3752   6506   1015   -105  -1052  B    C  
ATOM   4497  C   LEU B 148      -1.223  18.217 477.814  1.00 40.39      B    C  
ANISOU 4497  C   LEU B 148     5292   3599   6454   1041    -36   -933  B    C  
ATOM   4498  O   LEU B 148      -1.049  18.580 476.651  1.00 39.16      B    O  
ANISOU 4498  O   LEU B 148     5049   3344   6485   1080   -102   -895  B    O  
ATOM   4499  CB  LEU B 148       0.604  18.214 479.507  1.00 44.59      B    C  
ANISOU 4499  CB  LEU B 148     6133   4083   6728    868   -263   -950  B    C  
ATOM   4500  CG  LEU B 148       1.549  17.917 478.334  1.00 43.06      B    C  
ANISOU 4500  CG  LEU B 148     5808   3805   6747    821   -405   -821  B    C  
ATOM   4501  CD1 LEU B 148       2.937  18.354 478.612  1.00 47.35      B    C  
ANISOU 4501  CD1 LEU B 148     6436   4251   7303    735   -610   -835  B    C  
ATOM   4502  CD2 LEU B 148       1.536  16.461 477.971  1.00 38.51      B    C  
ANISOU 4502  CD2 LEU B 148     5118   3318   6196    767   -386   -656  B    C  
ATOM   4503  N   ILE B 149      -1.959  17.147 478.116  1.00 40.51      B    N  
ANISOU 4503  N   ILE B 149     5236   3770   6387   1001     95   -872  B    N  
ATOM   4504  CA  ILE B 149      -2.475  16.324 477.026  1.00 39.02      B    C  
ANISOU 4504  CA  ILE B 149     4850   3631   6343    994    135   -756  B    C  
ATOM   4505  C   ILE B 149      -3.539  17.072 476.221  1.00 45.83      B    C  
ANISOU 4505  C   ILE B 149     5566   4489   7358   1141    210   -836  B    C  
ATOM   4506  O   ILE B 149      -3.607  16.936 474.990  1.00 43.84      B    O  
ANISOU 4506  O   ILE B 149     5195   4191   7270   1161    151   -758  B    O  
ATOM   4507  CB  ILE B 149      -2.987  14.978 477.552  1.00 44.00      B    C  
ANISOU 4507  CB  ILE B 149     5455   4413   6848    889    252   -670  B    C  
ATOM   4508  CG1 ILE B 149      -4.199  15.188 478.447  1.00 41.54      B    C  
ANISOU 4508  CG1 ILE B 149     5136   4237   6409    928    468   -796  B    C  
ATOM   4509  CG2 ILE B 149      -1.858  14.233 478.259  1.00 39.23      B    C  
ANISOU 4509  CG2 ILE B 149     5014   3784   6106    768    132   -572  B    C  
ATOM   4510  CD1 ILE B 149      -4.905  13.922 478.780  1.00 56.63      B    C  
ANISOU 4510  CD1 ILE B 149     6996   6298   8223    808    619   -714  B    C  
ATOM   4511  N   ASN B 150      -4.364  17.897 476.873  1.00 41.26      B    N  
ANISOU 4511  N   ASN B 150     5004   3947   6728   1258    331   -996  B    N  
ATOM   4512  CA  ASN B 150      -5.336  18.650 476.087  1.00 41.83      B    C  
ANISOU 4512  CA  ASN B 150     4927   3998   6968   1431    368  -1073  B    C  
ATOM   4513  C   ASN B 150      -4.653  19.740 475.264  1.00 43.49      B    C  
ANISOU 4513  C   ASN B 150     5227   3991   7305   1509    199  -1083  B    C  
ATOM   4514  O   ASN B 150      -4.952  19.911 474.078  1.00 46.48      B    O  
ANISOU 4514  O   ASN B 150     5502   4311   7846   1578    132  -1030  B    O  
ATOM   4515  CB  ASN B 150      -6.433  19.197 476.999  1.00 44.47      B    C  
ANISOU 4515  CB  ASN B 150     5231   4432   7233   1555    562  -1253  B    C  
ATOM   4516  CG  ASN B 150      -7.348  18.089 477.550  1.00 45.37      B    C  
ANISOU 4516  CG  ASN B 150     5204   4776   7259   1467    765  -1235  B    C  
ATOM   4517  ND2 ASN B 150      -7.516  18.051 478.870  1.00 47.26      B    N  
ANISOU 4517  ND2 ASN B 150     5567   5102   7289   1423    925  -1331  B    N  
ATOM   4518  OD1 ASN B 150      -7.877  17.275 476.794  1.00 44.55      B    O  
ANISOU 4518  OD1 ASN B 150     4902   4762   7262   1419    778  -1135  B    O  
ATOM   4519  N   THR B 151      -3.694  20.449 475.858  1.00 41.55      B    N  
ANISOU 4519  N   THR B 151     5190   3619   6978   1476    118  -1142  B    N  
ATOM   4520  CA  THR B 151      -2.898  21.424 475.111  1.00 41.04      B    C  
ANISOU 4520  CA  THR B 151     5234   3338   7023   1497    -37  -1140  B    C  
ATOM   4521  C   THR B 151      -2.212  20.768 473.916  1.00 39.96      B    C  
ANISOU 4521  C   THR B 151     5022   3159   7001   1389   -143   -966  B    C  
ATOM   4522  O   THR B 151      -2.114  21.362 472.834  1.00 42.00      B    O  
ANISOU 4522  O   THR B 151     5291   3278   7389   1435   -221   -935  B    O  
ATOM   4523  CB  THR B 151      -1.858  22.064 476.035  1.00 41.89      B    C  
ANISOU 4523  CB  THR B 151     5564   3342   7011   1418   -114  -1221  B    C  
ATOM   4524  CG2 THR B 151      -1.003  23.080 475.302  1.00 41.67      B    C  
ANISOU 4524  CG2 THR B 151     5653   3084   7095   1402   -259  -1223  B    C  
ATOM   4525  OG1 THR B 151      -2.523  22.721 477.113  1.00 52.38      B    O  
ANISOU 4525  OG1 THR B 151     6994   4692   8216   1524     -1  -1399  B    O  
ATOM   4526  N   LEU B 152      -1.719  19.548 474.096  1.00 37.62      B    N  
ANISOU 4526  N   LEU B 152     4673   2971   6650   1247   -144   -854  B    N  
ATOM   4527  CA  LEU B 152      -1.080  18.858 472.991  1.00 49.56      B    C  
ANISOU 4527  CA  LEU B 152     6116   4447   8268   1154   -219   -705  B    C  
ATOM   4528  C   LEU B 152      -2.084  18.573 471.877  1.00 52.62      B    C  
ANISOU 4528  C   LEU B 152     6361   4869   8763   1226   -180   -651  B    C  
ATOM   4529  O   LEU B 152      -1.813  18.849 470.699  1.00 36.70      B    O  
ANISOU 4529  O   LEU B 152     4352   2737   6855   1227   -253   -591  B    O  
ATOM   4530  CB  LEU B 152      -0.442  17.570 473.505  1.00 34.98      B    C  
ANISOU 4530  CB  LEU B 152     4249   2701   6341   1018   -225   -607  B    C  
ATOM   4531  CG  LEU B 152       0.194  16.729 472.423  1.00 33.29      B    C  
ANISOU 4531  CG  LEU B 152     3959   2456   6234    934   -275   -466  B    C  
ATOM   4532  CD1 LEU B 152       1.344  17.519 471.848  1.00 33.01      B    C  
ANISOU 4532  CD1 LEU B 152     3987   2259   6294    892   -380   -468  B    C  
ATOM   4533  CD2 LEU B 152       0.656  15.405 472.989  1.00 40.68      B    C  
ANISOU 4533  CD2 LEU B 152     4881   3483   7094    836   -277   -374  B    C  
ATOM   4534  N   THR B 153      -3.274  18.086 472.239  1.00 35.96      B    N  
ANISOU 4534  N   THR B 153     4128   2916   6617   1281    -66   -681  B    N  
ATOM   4535  CA  THR B 153      -4.299  17.810 471.238  1.00 35.84      B    C  
ANISOU 4535  CA  THR B 153     3954   2953   6709   1345    -50   -642  B    C  
ATOM   4536  C   THR B 153      -4.690  19.073 470.452  1.00 54.85      B    C  
ANISOU 4536  C   THR B 153     6390   5221   9231   1508   -130   -701  B    C  
ATOM   4537  O   THR B 153      -4.774  19.051 469.210  1.00 50.94      B    O  
ANISOU 4537  O   THR B 153     5886   4692   8778   1490   -211   -606  B    O  
ATOM   4538  CB  THR B 153      -5.503  17.180 471.929  1.00 41.90      B    C  
ANISOU 4538  CB  THR B 153     4567   3926   7426   1362     99   -690  B    C  
ATOM   4539  CG2 THR B 153      -6.453  16.697 470.933  1.00 59.52      B    C  
ANISOU 4539  CG2 THR B 153     6615   6232   9770   1385     93   -639  B    C  
ATOM   4540  OG1 THR B 153      -5.064  16.024 472.638  1.00 58.85      B    O  
ANISOU 4540  OG1 THR B 153     6745   6166   9450   1200    159   -618  B    O  
ATOM   4541  N   ARG B 154      -4.908  20.196 471.147  1.00 40.11      B    N  
ANISOU 4541  N   ARG B 154     4603   3292   7345   1640   -110   -841  B    N  
ATOM   4542  CA  ARG B 154      -5.273  21.409 470.429  1.00 47.41      B    C  
ANISOU 4542  CA  ARG B 154     5614   4130   8268   1749   -181   -850  B    C  
ATOM   4543  C   ARG B 154      -4.133  21.892 469.548  1.00 40.71      B    C  
ANISOU 4543  C   ARG B 154     4957   3137   7373   1622   -291   -740  B    C  
ATOM   4544  O   ARG B 154      -4.358  22.300 468.403  1.00 38.38      B    O  
ANISOU 4544  O   ARG B 154     4706   2804   7072   1633   -358   -659  B    O  
ATOM   4545  CB  ARG B 154      -5.695  22.501 471.399  1.00 52.09      B    C  
ANISOU 4545  CB  ARG B 154     6282   4678   8830   1907   -119  -1019  B    C  
ATOM   4546  CG  ARG B 154      -7.012  22.248 472.106  1.00 73.43      B    C  
ANISOU 4546  CG  ARG B 154     8778   7545  11576   2058     25  -1148  B    C  
ATOM   4547  CD  ARG B 154      -7.317  23.430 473.015  1.00 96.76      B    C  
ANISOU 4547  CD  ARG B 154    11850  10434  14478   2214     98  -1323  B    C  
ATOM   4548  NE  ARG B 154      -8.375  23.178 473.989  1.00108.11      B    N  
ANISOU 4548  NE  ARG B 154    13110  12040  15928   2336    293  -1488  B    N  
ATOM   4549  CZ  ARG B 154      -8.811  24.091 474.855  1.00103.26      B    C  
ANISOU 4549  CZ  ARG B 154    12574  11400  15259   2485    403  -1663  B    C  
ATOM   4550  NH1 ARG B 154      -8.273  25.310 474.865  1.00102.53      B    N1+
ANISOU 4550  NH1 ARG B 154    12743  11103  15112   2529    317  -1687  B    N1+
ATOM   4551  NH2 ARG B 154      -9.775  23.788 475.716  1.00 96.62      B    N  
ANISOU 4551  NH2 ARG B 154    11556  10740  14414   2574    621  -1817  B    N  
ATOM   4552  N   LEU B 155      -2.901  21.868 470.063  1.00 43.66      B    N  
ANISOU 4552  N   LEU B 155     5441   3428   7718   1498   -310   -745  B    N  
ATOM   4553  CA  LEU B 155      -1.758  22.302 469.260  1.00 36.80      B    C  
ANISOU 4553  CA  LEU B 155     4718   2443   6822   1359   -384   -656  B    C  
ATOM   4554  C   LEU B 155      -1.621  21.473 467.986  1.00 61.52      B    C  
ANISOU 4554  C   LEU B 155     7785   5628   9961   1257   -402   -510  B    C  
ATOM   4555  O   LEU B 155      -1.523  22.031 466.884  1.00 35.44      B    O  
ANISOU 4555  O   LEU B 155     4581   2253   6630   1235   -442   -445  B    O  
ATOM   4556  CB  LEU B 155      -0.470  22.224 470.081  1.00 43.50      B    C  
ANISOU 4556  CB  LEU B 155     5634   3223   7670   1235   -410   -692  B    C  
ATOM   4557  CG  LEU B 155      -0.183  23.311 471.114  1.00 42.37      B    C  
ANISOU 4557  CG  LEU B 155     5644   2957   7496   1277   -432   -839  B    C  
ATOM   4558  CD1 LEU B 155       0.963  22.916 472.014  1.00 37.84      B    C  
ANISOU 4558  CD1 LEU B 155     5096   2343   6939   1155   -489   -881  B    C  
ATOM   4559  CD2 LEU B 155       0.093  24.643 470.429  1.00 46.92      B    C  
ANISOU 4559  CD2 LEU B 155     6397   3387   8044   1262   -469   -828  B    C  
ATOM   4560  N   ILE B 156      -1.631  20.136 468.119  1.00 34.07      B    N  
ANISOU 4560  N   ILE B 156     4165   2262   6519   1198   -367   -462  B    N  
ATOM   4561  CA  ILE B 156      -1.500  19.264 466.955  1.00 43.00      B    C  
ANISOU 4561  CA  ILE B 156     5250   3436   7652   1100   -375   -339  B    C  
ATOM   4562  C   ILE B 156      -2.623  19.522 465.948  1.00 52.50      B    C  
ANISOU 4562  C   ILE B 156     6436   4658   8855   1190   -411   -313  B    C  
ATOM   4563  O   ILE B 156      -2.381  19.616 464.737  1.00 33.11      B    O  
ANISOU 4563  O   ILE B 156     4064   2149   6367   1130   -451   -234  B    O  
ATOM   4564  CB  ILE B 156      -1.482  17.787 467.393  1.00 31.76      B    C  
ANISOU 4564  CB  ILE B 156     3687   2111   6271   1042   -326   -301  B    C  
ATOM   4565  CG1 ILE B 156      -0.272  17.480 468.274  1.00 40.26      B    C  
ANISOU 4565  CG1 ILE B 156     4791   3152   7354    957   -326   -308  B    C  
ATOM   4566  CG2 ILE B 156      -1.396  16.891 466.171  1.00 30.68      B    C  
ANISOU 4566  CG2 ILE B 156     3524   2002   6131    946   -329   -190  B    C  
ATOM   4567  CD1 ILE B 156       1.086  17.672 467.604  1.00 36.41      B    C  
ANISOU 4567  CD1 ILE B 156     4382   2597   6855    825   -357   -252  B    C  
ATOM   4568  N   GLN B 157      -3.866  19.674 466.428  1.00 34.61      B    N  
ANISOU 4568  N   GLN B 157     4057   2464   6631   1342   -399   -386  B    N  
ATOM   4569  CA  GLN B 157      -4.960  19.902 465.489  1.00 43.58      B    C  
ANISOU 4569  CA  GLN B 157     5145   3623   7792   1440   -463   -364  B    C  
ATOM   4570  C   GLN B 157      -4.802  21.223 464.753  1.00 53.98      B    C  
ANISOU 4570  C   GLN B 157     6657   4799   9055   1490   -537   -348  B    C  
ATOM   4571  O   GLN B 157      -5.064  21.302 463.545  1.00 56.50      B    O  
ANISOU 4571  O   GLN B 157     7030   5076   9363   1487   -617   -272  B    O  
ATOM   4572  CB  GLN B 157      -6.302  19.849 466.202  1.00 42.46      B    C  
ANISOU 4572  CB  GLN B 157     4803   3605   7724   1599   -423   -461  B    C  
ATOM   4573  CG  GLN B 157      -7.463  20.265 465.324  1.00 38.59      B    C  
ANISOU 4573  CG  GLN B 157     4244   3140   7278   1728   -515   -454  B    C  
ATOM   4574  CD  GLN B 157      -8.764  19.680 465.822  1.00 49.83      B    C  
ANISOU 4574  CD  GLN B 157     5381   4746   8805   1824   -462   -528  B    C  
ATOM   4575  NE2 GLN B 157      -9.329  18.742 465.062  1.00 39.80      B    N  
ANISOU 4575  NE2 GLN B 157     3959   3558   7604   1770   -517   -468  B    N  
ATOM   4576  OE1 GLN B 157      -9.238  20.036 466.902  1.00 59.34      B    O  
ANISOU 4576  OE1 GLN B 157     6496   6019  10031   1934   -358   -648  B    O  
ATOM   4577  N   GLU B 158      -4.418  22.284 465.469  1.00 53.90      B    N  
ANISOU 4577  N   GLU B 158     6769   4697   9015   1540   -515   -420  B    N  
ATOM   4578  CA  GLU B 158      -4.237  23.577 464.819  1.00 44.93      B    C  
ANISOU 4578  CA  GLU B 158     5837   3399   7835   1579   -572   -400  B    C  
ATOM   4579  C   GLU B 158      -3.074  23.565 463.835  1.00 44.96      B    C  
ANISOU 4579  C   GLU B 158     6001   3300   7782   1399   -586   -299  B    C  
ATOM   4580  O   GLU B 158      -3.159  24.168 462.766  1.00 38.56      B    O  
ANISOU 4580  O   GLU B 158     5328   2384   6939   1408   -641   -235  B    O  
ATOM   4581  CB  GLU B 158      -4.085  24.667 465.868  1.00 48.88      B    C  
ANISOU 4581  CB  GLU B 158     6436   3809   8325   1660   -536   -511  B    C  
ATOM   4582  CG  GLU B 158      -5.443  24.961 466.482  1.00 77.59      B    C  
ANISOU 4582  CG  GLU B 158     9942   7523  12014   1879   -516   -610  B    C  
ATOM   4583  CD  GLU B 158      -5.378  25.808 467.725  1.00 93.48      B    C  
ANISOU 4583  CD  GLU B 158    12033   9470  14017   1967   -450   -748  B    C  
ATOM   4584  OE1 GLU B 158      -4.250  26.035 468.223  1.00 93.93      B    O  
ANISOU 4584  OE1 GLU B 158    12228   9431  14029   1841   -437   -771  B    O  
ATOM   4585  OE2 GLU B 158      -6.459  26.263 468.181  1.00 87.08      B    O1-
ANISOU 4585  OE2 GLU B 158    11141   8698  13247   2161   -414   -842  B    O1-
ATOM   4586  N   ILE B 159      -1.996  22.854 464.145  1.00 36.15      B    N  
ANISOU 4586  N   ILE B 159     4863   2213   6658   1239   -533   -282  B    N  
ATOM   4587  CA  ILE B 159      -0.869  22.826 463.223  1.00 35.46      B    C  
ANISOU 4587  CA  ILE B 159     4902   2042   6528   1072   -520   -201  B    C  
ATOM   4588  C   ILE B 159      -1.219  22.025 461.982  1.00 34.81      B    C  
ANISOU 4588  C   ILE B 159     4798   2001   6430   1036   -540   -108  B    C  
ATOM   4589  O   ILE B 159      -1.064  22.507 460.855  1.00 38.07      B    O  
ANISOU 4589  O   ILE B 159     5372   2303   6791   1002   -561    -45  B    O  
ATOM   4590  CB  ILE B 159       0.370  22.253 463.924  1.00 53.51      B    C  
ANISOU 4590  CB  ILE B 159     7133   4359   8840    927   -467   -218  B    C  
ATOM   4591  CG1 ILE B 159       0.741  23.134 465.120  1.00 54.30      B    C  
ANISOU 4591  CG1 ILE B 159     7287   4389   8957    953   -473   -319  B    C  
ATOM   4592  CG2 ILE B 159       1.511  22.061 462.931  1.00 46.62      B    C  
ANISOU 4592  CG2 ILE B 159     6342   3427   7944    757   -430   -143  B    C  
ATOM   4593  CD1 ILE B 159       2.000  22.716 465.825  1.00 49.00      B    C  
ANISOU 4593  CD1 ILE B 159     6564   3723   8330    815   -458   -341  B    C  
ATOM   4594  N   SER B 160      -1.707  20.791 462.170  1.00 33.76      B    N  
ANISOU 4594  N   SER B 160     4481   2008   6338   1038   -532   -100  B    N  
ATOM   4595  CA  SER B 160      -1.974  19.889 461.055  1.00 37.70      B    C  
ANISOU 4595  CA  SER B 160     4960   2536   6829    984   -552    -21  B    C  
ATOM   4596  C   SER B 160      -3.275  20.213 460.327  1.00 48.85      B    C  
ANISOU 4596  C   SER B 160     6373   3934   8256   1117   -665     -5  B    C  
ATOM   4597  O   SER B 160      -3.418  19.892 459.139  1.00 52.82      B    O  
ANISOU 4597  O   SER B 160     6948   4391   8728   1074   -717     68  B    O  
ATOM   4598  CB  SER B 160      -2.073  18.458 461.549  1.00 31.86      B    C  
ANISOU 4598  CB  SER B 160     4032   1929   6145    934   -506    -18  B    C  
ATOM   4599  OG  SER B 160      -3.324  18.317 462.211  1.00 38.58      B    O  
ANISOU 4599  OG  SER B 160     4722   2870   7067   1067   -540    -72  B    O  
ATOM   4600  N   GLY B 161      -4.250  20.792 461.016  1.00 48.06      B    N  
ANISOU 4600  N   GLY B 161     6182   3873   8207   1282   -709    -75  B    N  
ATOM   4601  CA  GLY B 161      -5.500  21.059 460.351  1.00 37.31      B    C  
ANISOU 4601  CA  GLY B 161     4779   2515   6883   1422   -835    -66  B    C  
ATOM   4602  C   GLY B 161      -6.402  19.860 460.215  1.00 55.48      B    C  
ANISOU 4602  C   GLY B 161     6859   4950   9270   1432   -879    -61  B    C  
ATOM   4603  O   GLY B 161      -7.399  19.937 459.484  1.00 52.87      B    O  
ANISOU 4603  O   GLY B 161     6480   4627   8981   1528  -1016    -44  B    O  
ATOM   4604  N   TYR B 162      -6.087  18.762 460.899  1.00 47.13      B    N  
ANISOU 4604  N   TYR B 162     5667   3991   8250   1335   -778    -74  B    N  
ATOM   4605  CA  TYR B 162      -6.862  17.542 460.765  1.00 44.04      B    C  
ANISOU 4605  CA  TYR B 162     5073   3706   7955   1315   -804    -62  B    C  
ATOM   4606  C   TYR B 162      -8.201  17.676 461.479  1.00 36.93      B    C  
ANISOU 4606  C   TYR B 162     3926   2943   7161   1475   -821   -153  B    C  
ATOM   4607  O   TYR B 162      -8.324  18.367 462.490  1.00 61.55      B    O  
ANISOU 4607  O   TYR B 162     7011   6098  10277   1573   -747   -239  B    O  
ATOM   4608  CB  TYR B 162      -6.057  16.359 461.304  1.00 41.62      B    C  
ANISOU 4608  CB  TYR B 162     4722   3438   7655   1162   -676    -39  B    C  
ATOM   4609  CG  TYR B 162      -5.188  15.733 460.248  1.00 41.08      B    C  
ANISOU 4609  CG  TYR B 162     4806   3281   7522   1007   -674     54  B    C  
ATOM   4610  CD1 TYR B 162      -4.076  16.393 459.750  1.00 53.30      B    C  
ANISOU 4610  CD1 TYR B 162     6571   4727   8955    939   -642     85  B    C  
ATOM   4611  CD2 TYR B 162      -5.518  14.506 459.703  1.00 31.95      B    C  
ANISOU 4611  CD2 TYR B 162     3578   2137   6424    929   -695    104  B    C  
ATOM   4612  CE1 TYR B 162      -3.284  15.815 458.764  1.00 53.37      B    C  
ANISOU 4612  CE1 TYR B 162     6712   4671   8896    801   -606    154  B    C  
ATOM   4613  CE2 TYR B 162      -4.741  13.922 458.717  1.00 32.64      B    C  
ANISOU 4613  CE2 TYR B 162     3826   2139   6436    791   -673    176  B    C  
ATOM   4614  CZ  TYR B 162      -3.623  14.580 458.252  1.00 50.90      B    C  
ANISOU 4614  CZ  TYR B 162     6342   4376   8621    733   -618    195  B    C  
ATOM   4615  OH  TYR B 162      -2.854  14.004 457.268  1.00 50.27      B    O  
ANISOU 4615  OH  TYR B 162     6412   4231   8458    604   -562    248  B    O  
ATOM   4616  N   ASP B 163      -9.228  17.033 460.915  1.00 61.47      B    N  
ANISOU 4616  N   ASP B 163     6856   6131  10367   1500   -921   -142  B    N  
ATOM   4617  CA  ASP B 163     -10.581  17.199 461.448  1.00 67.97      B    C  
ANISOU 4617  CA  ASP B 163     7407   7118  11299   1649   -935   -236  B    C  
ATOM   4618  C   ASP B 163     -10.712  16.648 462.868  1.00 70.64      B    C  
ANISOU 4618  C   ASP B 163     7546   7601  11691   1630   -740   -320  B    C  
ATOM   4619  O   ASP B 163     -11.481  17.199 463.661  1.00 41.32      B    O  
ANISOU 4619  O   ASP B 163     3685   3998   8015   1765   -675   -426  B    O  
ATOM   4620  CB  ASP B 163     -11.607  16.525 460.523  1.00 78.56      B    C  
ANISOU 4620  CB  ASP B 163     8567   8539  12745   1647  -1096   -206  B    C  
ATOM   4621  CG  ASP B 163     -11.942  17.354 459.282  1.00 70.05      B    C  
ANISOU 4621  CG  ASP B 163     7639   7351  11625   1743  -1320   -156  B    C  
ATOM   4622  OD1 ASP B 163     -11.815  18.582 459.340  1.00 60.67      B    O1-
ANISOU 4622  OD1 ASP B 163     6606   6076  10369   1864  -1333   -175  B    O1-
ATOM   4623  OD2 ASP B 163     -12.343  16.776 458.248  1.00 62.41      B    O1-
ANISOU 4623  OD2 ASP B 163     6647   6374  10693   1694  -1494    -95  B    O1-
ATOM   4624  N   ARG B 164      -9.954  15.593 463.217  1.00 37.69      B    N  
ANISOU 4624  N   ARG B 164     3384   3420   7518   1470   -635   -274  B    N  
ATOM   4625  CA  ARG B 164      -9.996  14.974 464.537  1.00 37.52      B    C  
ANISOU 4625  CA  ARG B 164     3239   3542   7473   1401   -438   -329  B    C  
ATOM   4626  C   ARG B 164      -8.583  14.596 464.950  1.00 42.17      B    C  
ANISOU 4626  C   ARG B 164     4040   4031   7950   1265   -356   -268  B    C  
ATOM   4627  O   ARG B 164      -7.782  14.152 464.123  1.00 48.50      B    O  
ANISOU 4627  O   ARG B 164     4990   4722   8716   1155   -411   -170  B    O  
ATOM   4628  CB  ARG B 164     -10.901  13.728 464.580  1.00 38.15      B    C  
ANISOU 4628  CB  ARG B 164     3099   3827   7570   1259   -375   -316  B    C  
ATOM   4629  CG  ARG B 164     -10.831  12.970 465.895  1.00 54.10      B    C  
ANISOU 4629  CG  ARG B 164     5068   5979   9510   1135   -159   -343  B    C  
ATOM   4630  CD  ARG B 164     -11.901  11.911 466.041  1.00 53.25      B    C  
ANISOU 4630  CD  ARG B 164     4727   6076   9429    997    -75   -351  B    C  
ATOM   4631  NE  ARG B 164     -11.782  10.842 465.058  1.00 69.89      B    N  
ANISOU 4631  NE  ARG B 164     6884   8152  11518    817   -160   -242  B    N  
ATOM   4632  CZ  ARG B 164     -12.686   9.878 464.888  1.00 75.74      B    C  
ANISOU 4632  CZ  ARG B 164     7448   9040  12291    665   -134   -236  B    C  
ATOM   4633  NH1 ARG B 164     -13.792   9.857 465.626  1.00 77.11      B    N1+
ANISOU 4633  NH1 ARG B 164     7351   9419  12529    667    -13   -330  B    N1+
ATOM   4634  NH2 ARG B 164     -12.496   8.941 463.973  1.00 70.35      B    N  
ANISOU 4634  NH2 ARG B 164     6856   8298  11577    500   -218   -144  B    N  
ATOM   4635  N   VAL B 165      -8.278  14.815 466.228  1.00 41.04      B    N  
ANISOU 4635  N   VAL B 165     3912   3927   7754   1282   -228   -335  B    N  
ATOM   4636  CA  VAL B 165      -6.972  14.544 466.816  1.00 34.00      B    C  
ANISOU 4636  CA  VAL B 165     3195   2958   6766   1176   -172   -294  B    C  
ATOM   4637  C   VAL B 165      -7.162  13.918 468.190  1.00 41.22      B    C  
ANISOU 4637  C   VAL B 165     4050   4022   7592   1107    -14   -333  B    C  
ATOM   4638  O   VAL B 165      -7.920  14.440 469.014  1.00 36.09      B    O  
ANISOU 4638  O   VAL B 165     3304   3469   6939   1205     71   -445  B    O  
ATOM   4639  CB  VAL B 165      -6.135  15.828 466.928  1.00 40.49      B    C  
ANISOU 4639  CB  VAL B 165     4186   3609   7590   1277   -230   -338  B    C  
ATOM   4640  CG1 VAL B 165      -4.923  15.580 467.801  1.00 34.35      B    C  
ANISOU 4640  CG1 VAL B 165     3533   2796   6723   1176   -176   -324  B    C  
ATOM   4641  CG2 VAL B 165      -5.707  16.291 465.533  1.00 33.34      B    C  
ANISOU 4641  CG2 VAL B 165     3427   2583   6660   1250   -356   -260  B    C  
ATOM   4642  N   MET B 166      -6.447  12.822 468.456  1.00 33.35      B    N  
ANISOU 4642  N   MET B 166     3129   3030   6513    946     28   -245  B    N  
ATOM   4643  CA  MET B 166      -6.612  12.077 469.695  1.00 33.97      B    C  
ANISOU 4643  CA  MET B 166     3195   3233   6480    855    165   -254  B    C  
ATOM   4644  C   MET B 166      -5.268  11.700 470.300  1.00 32.93      B    C  
ANISOU 4644  C   MET B 166     3247   3014   6250    777    148   -193  B    C  
ATOM   4645  O   MET B 166      -4.250  11.591 469.617  1.00 31.77      B    O  
ANISOU 4645  O   MET B 166     3191   2738   6144    752     53   -123  B    O  
ATOM   4646  CB  MET B 166      -7.451  10.811 469.503  1.00 40.51      B    C  
ANISOU 4646  CB  MET B 166     3903   4187   7303    715    238   -198  B    C  
ATOM   4647  CG  MET B 166      -8.921  11.096 469.257  1.00 39.68      B    C  
ANISOU 4647  CG  MET B 166     3561   4225   7290    776    277   -281  B    C  
ATOM   4648  SD  MET B 166      -9.727   9.863 468.240  1.00 60.70      B    S  
ANISOU 4648  SD  MET B 166     6085   6963  10014    616    249   -203  B    S  
ATOM   4649  CE  MET B 166      -8.697   9.872 466.770  1.00 61.11      B    C  
ANISOU 4649  CE  MET B 166     6309   6803  10106    621     57   -102  B    C  
ATOM   4650  N   ILE B 167      -5.288  11.484 471.606  1.00 33.86      B    N  
ANISOU 4650  N   ILE B 167     3415   3211   6238    740    243   -223  B    N  
ATOM   4651  CA  ILE B 167      -4.163  10.911 472.320  1.00 33.36      B    C  
ANISOU 4651  CA  ILE B 167     3516   3093   6067    658    212   -155  B    C  
ATOM   4652  C   ILE B 167      -4.589   9.503 472.705  1.00 43.79      B    C  
ANISOU 4652  C   ILE B 167     4842   4499   7296    513    305    -70  B    C  
ATOM   4653  O   ILE B 167      -5.536   9.308 473.477  1.00 41.92      B    O  
ANISOU 4653  O   ILE B 167     4561   4397   6969    469    447   -115  B    O  
ATOM   4654  CB  ILE B 167      -3.806  11.727 473.558  1.00 34.39      B    C  
ANISOU 4654  CB  ILE B 167     3758   3228   6081    711    223   -246  B    C  
ATOM   4655  CG1 ILE B 167      -3.357  13.123 473.142  1.00 40.86      B    C  
ANISOU 4655  CG1 ILE B 167     4596   3934   6994    836    127   -330  B    C  
ATOM   4656  CG2 ILE B 167      -2.733  11.009 474.333  1.00 35.92      B    C  
ANISOU 4656  CG2 ILE B 167     4113   3382   6155    623    163   -165  B    C  
ATOM   4657  CD1 ILE B 167      -2.060  13.142 472.444  1.00 36.44      B    C  
ANISOU 4657  CD1 ILE B 167     4100   3230   6515    809    -12   -257  B    C  
ATOM   4658  N   TYR B 168      -3.913   8.518 472.144  1.00 32.76      B    N  
ANISOU 4658  N   TYR B 168     3504   3018   5925    434    240     48  B    N  
ATOM   4659  CA  TYR B 168      -4.196   7.121 472.413  1.00 38.30      B    C  
ANISOU 4659  CA  TYR B 168     4254   3754   6545    290    309    143  B    C  
ATOM   4660  C   TYR B 168      -3.110   6.582 473.338  1.00 33.44      B    C  
ANISOU 4660  C   TYR B 168     3831   3065   5807    260    249    217  B    C  
ATOM   4661  O   TYR B 168      -1.934   6.552 472.967  1.00 38.83      B    O  
ANISOU 4661  O   TYR B 168     4570   3626   6557    307    121    262  B    O  
ATOM   4662  CB  TYR B 168      -4.255   6.385 471.077  1.00 32.24      B    C  
ANISOU 4662  CB  TYR B 168     3435   2921   5893    237    269    213  B    C  
ATOM   4663  CG  TYR B 168      -4.670   4.958 471.148  1.00 48.40      B    C  
ANISOU 4663  CG  TYR B 168     5533   4980   7878     77    338    303  B    C  
ATOM   4664  CD1 TYR B 168      -5.950   4.616 471.538  1.00 46.46      B    C  
ANISOU 4664  CD1 TYR B 168     5197   4878   7578    -31    474    277  B    C  
ATOM   4665  CD2 TYR B 168      -3.782   3.935 470.800  1.00 32.23      B    C  
ANISOU 4665  CD2 TYR B 168     3620   2791   5833     31    274    410  B    C  
ATOM   4666  CE1 TYR B 168      -6.343   3.293 471.590  1.00 52.35      B    C  
ANISOU 4666  CE1 TYR B 168     6008   5620   8263   -209    542    362  B    C  
ATOM   4667  CE2 TYR B 168      -4.165   2.632 470.852  1.00 33.00      B    C  
ANISOU 4667  CE2 TYR B 168     3798   2870   5871   -117    332    492  B    C  
ATOM   4668  CZ  TYR B 168      -5.452   2.308 471.240  1.00 46.08      B    C  
ANISOU 4668  CZ  TYR B 168     5383   4662   7462   -251    465    472  B    C  
ATOM   4669  OH  TYR B 168      -5.850   0.989 471.299  1.00 48.05      B    O  
ANISOU 4669  OH  TYR B 168     5730   4880   7646   -431    530    557  B    O  
ATOM   4670  N   GLN B 169      -3.496   6.113 474.513  1.00 34.98      B    N  
ANISOU 4670  N   GLN B 169     4129   3336   5826    177    340    233  B    N  
ATOM   4671  CA  GLN B 169      -2.528   5.605 475.473  1.00 38.11      B    C  
ANISOU 4671  CA  GLN B 169     4735   3663   6082    155    256    311  B    C  
ATOM   4672  C   GLN B 169      -2.611   4.091 475.614  1.00 40.14      B    C  
ANISOU 4672  C   GLN B 169     5119   3875   6257     21    287    448  B    C  
ATOM   4673  O   GLN B 169      -3.694   3.531 475.844  1.00 38.71      B    O  
ANISOU 4673  O   GLN B 169     4931   3783   5995   -109    446    459  B    O  
ATOM   4674  CB  GLN B 169      -2.700   6.247 476.845  1.00 37.21      B    C  
ANISOU 4674  CB  GLN B 169     4729   3633   5777    161    309    236  B    C  
ATOM   4675  CG  GLN B 169      -1.578   5.863 477.739  1.00 37.89      B    C  
ANISOU 4675  CG  GLN B 169     5034   3635   5727    157    162    314  B    C  
ATOM   4676  CD  GLN B 169      -1.856   6.215 479.136  1.00 39.91      B    C  
ANISOU 4676  CD  GLN B 169     5454   3970   5739    120    228    260  B    C  
ATOM   4677  NE2 GLN B 169      -0.912   5.911 480.030  1.00 40.91      B    N  
ANISOU 4677  NE2 GLN B 169     5801   4029   5714    114     73    329  B    N  
ATOM   4678  OE1 GLN B 169      -2.927   6.749 479.437  1.00 54.53      B    O  
ANISOU 4678  OE1 GLN B 169     7239   5946   7533    101    416    152  B    O  
ATOM   4679  N   PHE B 170      -1.451   3.451 475.536  1.00 35.84      B    N  
ANISOU 4679  N   PHE B 170     4693   3189   5736     54    136    547  B    N  
ATOM   4680  CA  PHE B 170      -1.353   2.012 475.647  1.00 36.61      B    C  
ANISOU 4680  CA  PHE B 170     4950   3196   5766    -44    132    685  B    C  
ATOM   4681  C   PHE B 170      -1.394   1.584 477.104  1.00 38.73      B    C  
ANISOU 4681  C   PHE B 170     5454   3480   5779   -120    146    746  B    C  
ATOM   4682  O   PHE B 170      -0.843   2.261 477.979  1.00 39.35      B    O  
ANISOU 4682  O   PHE B 170     5612   3581   5757    -52     58    710  B    O  
ATOM   4683  CB  PHE B 170      -0.047   1.536 475.010  1.00 35.70      B    C  
ANISOU 4683  CB  PHE B 170     4862   2913   5791     56    -39    755  B    C  
ATOM   4684  CG  PHE B 170      -0.016   1.642 473.525  1.00 34.01      B    C  
ANISOU 4684  CG  PHE B 170     4478   2655   5788     94    -27    719  B    C  
ATOM   4685  CD1 PHE B 170      -0.849   0.859 472.741  1.00 33.89      B    C  
ANISOU 4685  CD1 PHE B 170     4445   2628   5805    -15     77    748  B    C  
ATOM   4686  CD2 PHE B 170       0.855   2.516 472.907  1.00 32.77      B    C  
ANISOU 4686  CD2 PHE B 170     4201   2465   5785    218   -118    657  B    C  
ATOM   4687  CE1 PHE B 170      -0.819   0.949 471.365  1.00 32.56      B    C  
ANISOU 4687  CE1 PHE B 170     4157   2414   5802     12     78    714  B    C  
ATOM   4688  CE2 PHE B 170       0.882   2.618 471.528  1.00 31.46      B    C  
ANISOU 4688  CE2 PHE B 170     3916   2252   5783    239    -94    628  B    C  
ATOM   4689  CZ  PHE B 170       0.044   1.827 470.758  1.00 31.35      B    C  
ANISOU 4689  CZ  PHE B 170     3904   2226   5783    141     -1    657  B    C  
ATOM   4690  N   ASP B 171      -2.052   0.460 477.358  1.00 40.04      B    N  
ANISOU 4690  N   ASP B 171     5756   3630   5829   -278    254    840  B    N  
ATOM   4691  CA  ASP B 171      -2.008  -0.209 478.651  1.00 43.28      B    C  
ANISOU 4691  CA  ASP B 171     6458   4010   5977   -373    258    938  B    C  
ATOM   4692  C   ASP B 171      -1.013  -1.371 478.582  1.00 42.72      B    C  
ANISOU 4692  C   ASP B 171     6589   3729   5915   -338     79   1095  B    C  
ATOM   4693  O   ASP B 171      -0.412  -1.620 477.534  1.00 41.24      B    O  
ANISOU 4693  O   ASP B 171     6291   3435   5942   -241    -16   1108  B    O  
ATOM   4694  CB  ASP B 171      -3.432  -0.631 479.077  1.00 44.04      B    C  
ANISOU 4694  CB  ASP B 171     6588   4225   5920   -592    520    934  B    C  
ATOM   4695  CG  ASP B 171      -3.869  -1.990 478.555  1.00 58.89      B    C  
ANISOU 4695  CG  ASP B 171     8549   6006   7819   -753    586   1048  B    C  
ATOM   4696  OD1 ASP B 171      -3.244  -2.558 477.645  1.00 57.26      B    O1-
ANISOU 4696  OD1 ASP B 171     8333   5649   7775   -685    458   1107  B    O1-
ATOM   4697  OD2 ASP B 171      -4.891  -2.485 479.079  1.00 63.98      B    O1-
ANISOU 4697  OD2 ASP B 171     9271   6727   8310   -963    789   1069  B    O1-
ATOM   4698  N   PRO B 172      -0.722  -2.036 479.704  1.00 44.92      B    N  
ANISOU 4698  N   PRO B 172     7175   3931   5962   -390     13   1212  B    N  
ATOM   4699  CA  PRO B 172       0.341  -3.061 479.674  1.00 48.02      B    C  
ANISOU 4699  CA  PRO B 172     7757   4105   6383   -304   -200   1358  B    C  
ATOM   4700  C   PRO B 172       0.095  -4.205 478.698  1.00 60.69      B    C  
ANISOU 4700  C   PRO B 172     9375   5570   8114   -367   -141   1433  B    C  
ATOM   4701  O   PRO B 172       1.062  -4.851 478.261  1.00 45.15      B    O  
ANISOU 4701  O   PRO B 172     7460   3420   6275   -234   -311   1505  B    O  
ATOM   4702  CB  PRO B 172       0.391  -3.542 481.124  1.00 48.44      B    C  
ANISOU 4702  CB  PRO B 172     8174   4116   6115   -386   -252   1473  B    C  
ATOM   4703  CG  PRO B 172      -0.056  -2.356 481.907  1.00 48.74      B    C  
ANISOU 4703  CG  PRO B 172     8164   4352   6003   -419   -158   1348  B    C  
ATOM   4704  CD  PRO B 172      -1.114  -1.714 481.089  1.00 47.05      B    C  
ANISOU 4704  CD  PRO B 172     7642   4298   5935   -482     83   1206  B    C  
ATOM   4705  N   GLU B 173      -1.161  -4.493 478.358  1.00 56.63      B    N  
ANISOU 4705  N   GLU B 173     8813   5133   7571   -566     91   1409  B    N  
ATOM   4706  CA  GLU B 173      -1.485  -5.563 477.422  1.00 45.23      B    C  
ANISOU 4706  CA  GLU B 173     7395   3557   6232   -658    150   1466  B    C  
ATOM   4707  C   GLU B 173      -1.564  -5.075 475.986  1.00 42.76      B    C  
ANISOU 4707  C   GLU B 173     6770   3289   6186   -586    174   1350  B    C  
ATOM   4708  O   GLU B 173      -1.940  -5.851 475.106  1.00 42.61      B    O  
ANISOU 4708  O   GLU B 173     6754   3182   6255   -677    234   1369  B    O  
ATOM   4709  CB  GLU B 173      -2.816  -6.218 477.806  1.00 65.43      B    C  
ANISOU 4709  CB  GLU B 173    10073   6170   8617   -948    378   1505  B    C  
ATOM   4710  CG  GLU B 173      -2.802  -6.889 479.163  1.00 77.04      B    C  
ANISOU 4710  CG  GLU B 173    11920   7562   9790  -1063    380   1644  B    C  
ATOM   4711  CD  GLU B 173      -3.004  -5.888 480.290  1.00 89.18      B    C  
ANISOU 4711  CD  GLU B 173    13458   9290  11138  -1065    436   1579  B    C  
ATOM   4712  OE1 GLU B 173      -3.941  -5.061 480.192  1.00 83.98      B    O  
ANISOU 4712  OE1 GLU B 173    12550   8853  10504  -1140    631   1440  B    O  
ATOM   4713  OE2 GLU B 173      -2.226  -5.922 481.269  1.00 99.70      B    O1-
ANISOU 4713  OE2 GLU B 173    15043  10544  12294   -983    276   1661  B    O1-
ATOM   4714  N   TRP B 174      -1.257  -3.798 475.748  1.00 48.92      B    N  
ANISOU 4714  N   TRP B 174     7311   4198   7079   -442    131   1229  B    N  
ATOM   4715  CA  TRP B 174      -1.243  -3.127 474.443  1.00 46.48      B    C  
ANISOU 4715  CA  TRP B 174     6727   3933   6999   -358    138   1119  B    C  
ATOM   4716  C   TRP B 174      -2.643  -2.867 473.902  1.00 38.55      B    C  
ANISOU 4716  C   TRP B 174     5549   3082   6017   -511    317   1037  B    C  
ATOM   4717  O   TRP B 174      -2.812  -2.597 472.720  1.00 37.15      B    O  
ANISOU 4717  O   TRP B 174     5197   2914   6004   -484    322    971  B    O  
ATOM   4718  CB  TRP B 174      -0.379  -3.880 473.423  1.00 40.93      B    C  
ANISOU 4718  CB  TRP B 174     6057   3033   6462   -265     40   1163  B    C  
ATOM   4719  CG  TRP B 174       1.059  -3.801 473.857  1.00 43.35      B    C  
ANISOU 4719  CG  TRP B 174     6425   3235   6811    -67   -151   1203  B    C  
ATOM   4720  CD1 TRP B 174       1.804  -4.795 474.398  1.00 39.96      B    C  
ANISOU 4720  CD1 TRP B 174     6224   2629   6328    -11   -273   1324  B    C  
ATOM   4721  CD2 TRP B 174       1.884  -2.627 473.875  1.00 52.76      B    C  
ANISOU 4721  CD2 TRP B 174     7444   4500   8104     92   -254   1119  B    C  
ATOM   4722  CE2 TRP B 174       3.126  -3.000 474.409  1.00 38.30      B    C  
ANISOU 4722  CE2 TRP B 174     5715   2547   6292    235   -442   1189  B    C  
ATOM   4723  CE3 TRP B 174       1.691  -1.299 473.482  1.00 35.71      B    C  
ANISOU 4723  CE3 TRP B 174     5060   2485   6025    126   -214    992  B    C  
ATOM   4724  NE1 TRP B 174       3.049  -4.328 474.723  1.00 39.97      B    N  
ANISOU 4724  NE1 TRP B 174     6174   2605   6408    184   -457   1317  B    N  
ATOM   4725  CZ2 TRP B 174       4.173  -2.103 474.558  1.00 37.89      B    C  
ANISOU 4725  CZ2 TRP B 174     5523   2530   6342    386   -584   1130  B    C  
ATOM   4726  CZ3 TRP B 174       2.740  -0.412 473.624  1.00 43.25      B    C  
ANISOU 4726  CZ3 TRP B 174     5912   3453   7069    270   -345    940  B    C  
ATOM   4727  CH2 TRP B 174       3.963  -0.819 474.160  1.00 36.32      B    C  
ANISOU 4727  CH2 TRP B 174     5117   2469   6214    387   -525   1005  B    C  
ATOM   4728  N   ASN B 175      -3.656  -2.955 474.753  1.00 40.16      B    N  
ANISOU 4728  N   ASN B 175     5796   3408   6056   -677    465   1039  B    N  
ATOM   4729  CA  ASN B 175      -4.932  -2.331 474.479  1.00 40.18      B    C  
ANISOU 4729  CA  ASN B 175     5560   3612   6095   -773    623    927  B    C  
ATOM   4730  C   ASN B 175      -4.774  -0.834 474.729  1.00 52.89      B    C  
ANISOU 4730  C   ASN B 175     6998   5354   7742   -605    597    805  B    C  
ATOM   4731  O   ASN B 175      -3.802  -0.388 475.352  1.00 45.70      B    O  
ANISOU 4731  O   ASN B 175     6188   4395   6779   -472    482    815  B    O  
ATOM   4732  CB  ASN B 175      -6.027  -2.915 475.366  1.00 49.94      B    C  
ANISOU 4732  CB  ASN B 175     6883   4943   7148  -1010    818    958  B    C  
ATOM   4733  CG  ASN B 175      -6.235  -4.403 475.140  1.00 46.96      B    C  
ANISOU 4733  CG  ASN B 175     6704   4415   6724  -1207    849   1080  B    C  
ATOM   4734  ND2 ASN B 175      -6.262  -5.171 476.222  1.00 46.06      B    N  
ANISOU 4734  ND2 ASN B 175     6874   4236   6390  -1344    911   1190  B    N  
ATOM   4735  OD1 ASN B 175      -6.396  -4.850 474.014  1.00 58.66      B    O  
ANISOU 4735  OD1 ASN B 175     8108   5829   8350  -1245    820   1074  B    O  
ATOM   4736  N   GLY B 176      -5.704  -0.047 474.206  1.00 52.24      B    N  
ANISOU 4736  N   GLY B 176     6658   5428   7763   -605    684    686  B    N  
ATOM   4737  CA  GLY B 176      -5.591   1.398 474.279  1.00 58.48      B    C  
ANISOU 4737  CA  GLY B 176     7295   6313   8613   -434    654    564  B    C  
ATOM   4738  C   GLY B 176      -6.830   2.096 474.794  1.00 51.66      B    C  
ANISOU 4738  C   GLY B 176     6262   5658   7710   -475    829    446  B    C  
ATOM   4739  O   GLY B 176      -7.942   1.585 474.709  1.00 62.76      B    O  
ANISOU 4739  O   GLY B 176     7565   7168   9115   -634    974    436  B    O  
ATOM   4740  N   ARG B 177      -6.617   3.273 475.361  1.00 56.35      B    N  
ANISOU 4740  N   ARG B 177     6824   6309   8277   -332    820    349  B    N  
ATOM   4741  CA  ARG B 177      -7.718   4.161 475.724  1.00 58.73      B    C  
ANISOU 4741  CA  ARG B 177     6936   6797   8584   -307    979    205  B    C  
ATOM   4742  C   ARG B 177      -7.428   5.533 475.139  1.00 39.29      B    C  
ANISOU 4742  C   ARG B 177     4336   4320   6274    -89    867     96  B    C  
ATOM   4743  O   ARG B 177      -6.279   5.979 475.159  1.00 54.53      B    O  
ANISOU 4743  O   ARG B 177     6388   6128   8204     21    715    114  B    O  
ATOM   4744  CB  ARG B 177      -7.902   4.264 477.243  1.00 54.01      B    C  
ANISOU 4744  CB  ARG B 177     6492   6282   7748   -365   1129    173  B    C  
ATOM   4745  CG  ARG B 177      -9.189   4.946 477.649  1.00 68.99      B    C  
ANISOU 4745  CG  ARG B 177     8181   8384   9649   -368   1352     19  B    C  
ATOM   4746  CD  ARG B 177      -9.426   4.881 479.156  1.00 81.16      B    C  
ANISOU 4746  CD  ARG B 177     9909  10007  10919   -466   1545     -9  B    C  
ATOM   4747  NE  ARG B 177      -8.615   5.863 479.872  1.00 87.08      B    N  
ANISOU 4747  NE  ARG B 177    10819  10703  11562   -309   1457    -76  B    N  
ATOM   4748  CZ  ARG B 177      -8.937   6.380 481.054  1.00 98.53      B    C  
ANISOU 4748  CZ  ARG B 177    12375  12247  12813   -315   1624   -180  B    C  
ATOM   4749  NH1 ARG B 177     -10.062   6.011 481.665  1.00 95.53      B    N1+
ANISOU 4749  NH1 ARG B 177    11943  12030  12324   -470   1914   -228  B    N1+
ATOM   4750  NH2 ARG B 177      -8.135   7.270 481.628  1.00104.75      B    N  
ANISOU 4750  NH2 ARG B 177    13325  12966  13507   -181   1511   -243  B    N  
ATOM   4751  N   VAL B 178      -8.439   6.176 474.564  1.00 39.72      B    N  
ANISOU 4751  N   VAL B 178     4136   4488   6468    -30    926    -11  B    N  
ATOM   4752  CA  VAL B 178      -8.301   7.571 474.147  1.00 38.98      B    C  
ANISOU 4752  CA  VAL B 178     3941   4374   6498    182    836   -121  B    C  
ATOM   4753  C   VAL B 178      -8.487   8.486 475.355  1.00 46.92      B    C  
ANISOU 4753  C   VAL B 178     4986   5456   7386    266    951   -246  B    C  
ATOM   4754  O   VAL B 178      -9.559   8.508 475.971  1.00 46.45      B    O  
ANISOU 4754  O   VAL B 178     4810   5558   7280    224   1150   -332  B    O  
ATOM   4755  CB  VAL B 178      -9.293   7.938 473.041  1.00 39.14      B    C  
ANISOU 4755  CB  VAL B 178     3691   4465   6714    242    819   -183  B    C  
ATOM   4756  CG1 VAL B 178      -9.157   9.425 472.717  1.00 39.27      B    C  
ANISOU 4756  CG1 VAL B 178     3649   4435   6837    471    725   -291  B    C  
ATOM   4757  CG2 VAL B 178      -9.064   7.098 471.815  1.00 37.72      B    C  
ANISOU 4757  CG2 VAL B 178     3510   4196   6626    156    696    -71  B    C  
ATOM   4758  N   ILE B 179      -7.451   9.257 475.683  1.00 39.72      B    N  
ANISOU 4758  N   ILE B 179     4233   4430   6430    378    833   -269  B    N  
ATOM   4759  CA  ILE B 179      -7.446  10.062 476.896  1.00 41.27      B    C  
ANISOU 4759  CA  ILE B 179     4534   4667   6478    441    921   -385  B    C  
ATOM   4760  C   ILE B 179      -7.576  11.553 476.615  1.00 52.40      B    C  
ANISOU 4760  C   ILE B 179     5857   6046   8009    648    878   -532  B    C  
ATOM   4761  O   ILE B 179      -7.757  12.333 477.569  1.00 42.97      B    O  
ANISOU 4761  O   ILE B 179     4733   4888   6706    718    975   -662  B    O  
ATOM   4762  CB  ILE B 179      -6.186   9.788 477.739  1.00 47.35      B    C  
ANISOU 4762  CB  ILE B 179     5592   5334   7066    388    814   -309  B    C  
ATOM   4763  CG1 ILE B 179      -4.924  10.217 476.989  1.00 53.03      B    C  
ANISOU 4763  CG1 ILE B 179     6355   5883   7909    476    575   -264  B    C  
ATOM   4764  CG2 ILE B 179      -6.081   8.315 478.037  1.00 41.22      B    C  
ANISOU 4764  CG2 ILE B 179     4932   4562   6167    203    845   -156  B    C  
ATOM   4765  CD1 ILE B 179      -3.658  10.125 477.815  1.00 38.87      B    C  
ANISOU 4765  CD1 ILE B 179     4797   4000   5973    449    438   -214  B    C  
ATOM   4766  N   ALA B 180      -7.496  11.981 475.350  1.00 48.71      B    N  
ANISOU 4766  N   ALA B 180     5266   5496   7745    746    740   -519  B    N  
ATOM   4767  CA  ALA B 180      -7.704  13.379 474.978  1.00 48.74      B    C  
ANISOU 4767  CA  ALA B 180     5203   5445   7871    946    689   -645  B    C  
ATOM   4768  C   ALA B 180      -8.080  13.438 473.505  1.00 39.20      B    C  
ANISOU 4768  C   ALA B 180     3824   4200   6871   1005    578   -602  B    C  
ATOM   4769  O   ALA B 180      -7.679  12.582 472.718  1.00 48.74      B    O  
ANISOU 4769  O   ALA B 180     5040   5363   8116    897    492   -471  B    O  
ATOM   4770  CB  ALA B 180      -6.470  14.246 475.258  1.00 39.45      B    C  
ANISOU 4770  CB  ALA B 180     4239   4102   6648   1009    552   -669  B    C  
ATOM   4771  N   GLU B 181      -8.843  14.463 473.143  1.00 40.33      B    N  
ANISOU 4771  N   GLU B 181     3833   4351   7139   1184    573   -717  B    N  
ATOM   4772  CA  GLU B 181      -9.457  14.525 471.825  1.00 49.77      B    C  
ANISOU 4772  CA  GLU B 181     4855   5539   8516   1249    466   -686  B    C  
ATOM   4773  C   GLU B 181      -9.780  15.982 471.475  1.00 56.94      B    C  
ANISOU 4773  C   GLU B 181     5734   6357   9543   1492    386   -800  B    C  
ATOM   4774  O   GLU B 181      -9.963  16.829 472.356  1.00 42.66      B    O  
ANISOU 4774  O   GLU B 181     3962   4552   7697   1615    476   -937  B    O  
ATOM   4775  CB  GLU B 181     -10.715  13.646 471.806  1.00 41.49      B    C  
ANISOU 4775  CB  GLU B 181     3555   4699   7511   1164    591   -692  B    C  
ATOM   4776  CG  GLU B 181     -11.511  13.629 470.525  1.00 41.78      B    C  
ANISOU 4776  CG  GLU B 181     3384   4763   7728   1218    468   -672  B    C  
ATOM   4777  CD  GLU B 181     -12.879  12.956 470.702  1.00 81.16      B    C  
ANISOU 4777  CD  GLU B 181     8074   9985  12778   1144    608   -722  B    C  
ATOM   4778  OE1 GLU B 181     -13.470  13.084 471.796  1.00 82.38      B    O  
ANISOU 4778  OE1 GLU B 181     8136  10281  12885   1157    817   -835  B    O  
ATOM   4779  OE2 GLU B 181     -13.374  12.304 469.753  1.00 75.90      B    O1-
ANISOU 4779  OE2 GLU B 181     7269   9365  12205   1059    516   -656  B    O1-
ATOM   4780  N   SER B 182      -9.800  16.270 470.175  1.00 49.19      B    N  
ANISOU 4780  N   SER B 182     4726   5273   8691   1558    210   -741  B    N  
ATOM   4781  CA  SER B 182     -10.112  17.601 469.660  1.00 41.55      B    C  
ANISOU 4781  CA  SER B 182     3761   4185   7842   1791     96   -821  B    C  
ATOM   4782  C   SER B 182     -10.713  17.415 468.274  1.00 54.26      B    C  
ANISOU 4782  C   SER B 182     5245   5793   9579   1821    -63   -745  B    C  
ATOM   4783  O   SER B 182     -10.012  16.955 467.369  1.00 58.14      B    O  
ANISOU 4783  O   SER B 182     5855   6184  10052   1701   -177   -615  B    O  
ATOM   4784  CB  SER B 182      -8.862  18.484 469.609  1.00 50.06      B    C  
ANISOU 4784  CB  SER B 182     5123   5028   8871   1818     -3   -807  B    C  
ATOM   4785  OG  SER B 182      -9.156  19.813 469.213  1.00 64.31      B    O  
ANISOU 4785  OG  SER B 182     7031   6750  10654   1968    -93   -842  B    O  
ATOM   4786  N   VAL B 183     -11.984  17.770 468.088  1.00 56.95      B    N  
ANISOU 4786  N   VAL B 183     5385   6263   9989   1947    -73   -811  B    N  
ATOM   4787  CA  VAL B 183     -12.746  17.354 466.907  1.00 59.98      B    C  
ANISOU 4787  CA  VAL B 183     5621   6714  10456   1928   -218   -739  B    C  
ATOM   4788  C   VAL B 183     -13.433  18.584 466.313  1.00 63.22      B    C  
ANISOU 4788  C   VAL B 183     6059   7085  10876   2128   -356   -764  B    C  
ATOM   4789  O   VAL B 183     -14.521  18.957 466.755  1.00 72.16      B    O  
ANISOU 4789  O   VAL B 183     6982   8359  12077   2267   -291   -869  B    O  
ATOM   4790  CB  VAL B 183     -13.777  16.284 467.274  1.00 52.91      B    C  
ANISOU 4790  CB  VAL B 183     4372   6060   9670   1849    -90   -789  B    C  
ATOM   4791  CG1 VAL B 183     -13.127  14.976 467.421  1.00 43.55      B    C  
ANISOU 4791  CG1 VAL B 183     3264   4903   8381   1579     -7   -684  B    C  
ATOM   4792  CG2 VAL B 183     -14.410  16.626 468.621  1.00 66.33      B    C  
ANISOU 4792  CG2 VAL B 183     5920   7910  11372   1940    142   -951  B    C  
ATOM   4793  N   ARG B 184     -12.861  19.153 465.238  1.00 56.62      B    N  
ANISOU 4793  N   ARG B 184     5467   6064   9982   2136   -541   -663  B    N  
ATOM   4794  CA  ARG B 184     -13.499  20.289 464.569  1.00 64.10      B    C  
ANISOU 4794  CA  ARG B 184     6462   6949  10945   2320   -686   -666  B    C  
ATOM   4795  C   ARG B 184     -14.812  19.902 463.903  1.00 87.37      B    C  
ANISOU 4795  C   ARG B 184     9127  10054  14017   2379   -799   -670  B    C  
ATOM   4796  O   ARG B 184     -15.885  20.388 464.288  1.00102.78      B    O  
ANISOU 4796  O   ARG B 184    10873  12126  16052   2546   -766   -763  B    O  
ATOM   4797  CB  ARG B 184     -12.569  20.961 463.551  1.00 46.83      B    C  
ANISOU 4797  CB  ARG B 184     4611   4526   8656   2289   -837   -553  B    C  
ATOM   4798  CG  ARG B 184     -11.308  21.534 464.120  1.00 45.34      B    C  
ANISOU 4798  CG  ARG B 184     4691   4183   8352   2231   -746   -552  B    C  
ATOM   4799  CD  ARG B 184     -10.405  22.049 463.030  1.00 51.87      B    C  
ANISOU 4799  CD  ARG B 184     5817   4807   9086   2154   -867   -437  B    C  
ATOM   4800  NE  ARG B 184      -9.217  22.714 463.570  1.00 62.27      B    N  
ANISOU 4800  NE  ARG B 184     7370   5985  10305   2091   -783   -444  B    N  
ATOM   4801  CZ  ARG B 184      -8.279  23.316 462.831  1.00 66.20      B    C  
ANISOU 4801  CZ  ARG B 184     8134   6304  10715   2007   -836   -362  B    C  
ATOM   4802  NH1 ARG B 184      -8.388  23.342 461.503  1.00 55.70      B    N1+
ANISOU 4802  NH1 ARG B 184     6895   4902   9366   1984   -968   -265  B    N1+
ATOM   4803  NH2 ARG B 184      -7.239  23.916 463.418  1.00 60.51      B    N  
ANISOU 4803  NH2 ARG B 184     7590   5474   9926   1941   -756   -384  B    N  
ATOM   4804  N   GLN B 185     -14.753  19.068 462.872  1.00 81.36      B    N  
ANISOU 4804  N   GLN B 185     8352   9285  13274   2248   -940   -573  B    N  
ATOM   4805  CA  GLN B 185     -15.965  18.770 462.126  1.00 77.53      B    C  
ANISOU 4805  CA  GLN B 185     7620   8934  12904   2296  -1094   -573  B    C  
ATOM   4806  C   GLN B 185     -16.869  17.849 462.942  1.00 75.93      B    C  
ANISOU 4806  C   GLN B 185     7033   9002  12814   2233   -934   -666  B    C  
ATOM   4807  O   GLN B 185     -16.519  17.400 464.037  1.00 86.97      B    O  
ANISOU 4807  O   GLN B 185     8382  10469  14192   2149   -705   -720  B    O  
ATOM   4808  CB  GLN B 185     -15.604  18.187 460.766  1.00 80.02      B    C  
ANISOU 4808  CB  GLN B 185     8067   9142  13194   2169  -1306   -447  B    C  
ATOM   4809  CG  GLN B 185     -14.680  19.113 459.996  1.00 90.95      B    C  
ANISOU 4809  CG  GLN B 185     9844  10265  14448   2204  -1421   -359  B    C  
ATOM   4810  CD  GLN B 185     -15.045  19.236 458.532  1.00 98.34      B    C  
ANISOU 4810  CD  GLN B 185    10872  11115  15377   2228  -1700   -272  B    C  
ATOM   4811  NE2 GLN B 185     -14.389  20.163 457.831  1.00 86.87      B    N  
ANISOU 4811  NE2 GLN B 185     9758   9441  13805   2267  -1795   -198  B    N  
ATOM   4812  OE1 GLN B 185     -15.907  18.504 458.033  1.00107.77      B    O  
ANISOU 4812  OE1 GLN B 185    11842  12441  16665   2198  -1832   -271  B    O  
ATOM   4813  N   LEU B 186     -18.054  17.573 462.402  1.00 66.82      B    N  
ANISOU 4813  N   LEU B 186     5605   8009  11775   2263  -1054   -683  B    N  
ATOM   4814  CA  LEU B 186     -18.961  16.613 463.020  1.00 69.28      B    C  
ANISOU 4814  CA  LEU B 186     5537   8594  12193   2151   -905   -760  B    C  
ATOM   4815  C   LEU B 186     -18.350  15.215 462.977  1.00 68.06      B    C  
ANISOU 4815  C   LEU B 186     5382   8454  12024   1870   -843   -697  B    C  
ATOM   4816  O   LEU B 186     -18.181  14.618 461.909  1.00 68.48      B    O  
ANISOU 4816  O   LEU B 186     5492   8441  12086   1754  -1038   -602  B    O  
ATOM   4817  CB  LEU B 186     -20.332  16.659 462.348  1.00 75.69      B    C  
ANISOU 4817  CB  LEU B 186     6059   9569  13132   2229  -1075   -785  B    C  
ATOM   4818  CG  LEU B 186     -21.089  18.005 462.419  1.00 75.62      B    C  
ANISOU 4818  CG  LEU B 186     5999   9557  13176   2527  -1131   -848  B    C  
ATOM   4819  CD1 LEU B 186     -22.281  18.050 461.474  1.00 74.56      B    C  
ANISOU 4819  CD1 LEU B 186     5627   9537  13165   2606  -1375   -840  B    C  
ATOM   4820  CD2 LEU B 186     -21.568  18.286 463.843  1.00 68.66      B    C  
ANISOU 4820  CD2 LEU B 186     4921   8833  12335   2611   -830   -986  B    C  
ATOM   4821  N   PHE B 187     -17.996  14.732 464.166  1.00 75.10      B    N  
ANISOU 4821  N   PHE B 187     6228   9416  12889   1767   -570   -748  B    N  
ATOM   4822  CA  PHE B 187     -17.446  13.423 464.487  1.00 73.80      B    C  
ANISOU 4822  CA  PHE B 187     6042   9279  12719   1506   -434   -701  B    C  
ATOM   4823  C   PHE B 187     -18.049  13.041 465.828  1.00 73.77      B    C  
ANISOU 4823  C   PHE B 187     5796   9499  12735   1434   -128   -814  B    C  
ATOM   4824  O   PHE B 187     -18.341  13.917 466.648  1.00 76.73      B    O  
ANISOU 4824  O   PHE B 187     6147   9920  13087   1607     -0   -920  B    O  
ATOM   4825  CB  PHE B 187     -15.911  13.449 464.676  1.00 68.72      B    C  
ANISOU 4825  CB  PHE B 187     5799   8409  11904   1447   -387   -610  B    C  
ATOM   4826  CG  PHE B 187     -15.089  12.903 463.536  1.00 75.99      B    C  
ANISOU 4826  CG  PHE B 187     6982   9161  12731   1303   -555   -460  B    C  
ATOM   4827  CD1 PHE B 187     -15.238  11.589 463.110  1.00 82.83      B    C  
ANISOU 4827  CD1 PHE B 187     7819  10098  13554   1045   -553   -386  B    C  
ATOM   4828  CD2 PHE B 187     -14.062  13.661 462.982  1.00 81.14      B    C  
ANISOU 4828  CD2 PHE B 187     7941   9571  13319   1402   -675   -397  B    C  
ATOM   4829  CE1 PHE B 187     -14.415  11.051 462.093  1.00 72.38      B    C  
ANISOU 4829  CE1 PHE B 187     6764   8607  12129    913   -675   -262  B    C  
ATOM   4830  CE2 PHE B 187     -13.241  13.136 461.966  1.00 77.98      B    C  
ANISOU 4830  CE2 PHE B 187     7791   9019  12820   1258   -784   -270  B    C  
ATOM   4831  CZ  PHE B 187     -13.422  11.826 461.523  1.00 64.42      B    C  
ANISOU 4831  CZ  PHE B 187     6040   7375  11062   1024   -781   -207  B    C  
ATOM   4832  N   THR B 188     -18.196  11.745 466.085  1.00 67.45      B    N  
ANISOU 4832  N   THR B 188     4927   8823  11878   1139     10   -769  B    N  
ATOM   4833  CA  THR B 188     -18.592  11.352 467.426  1.00 60.89      B    C  
ANISOU 4833  CA  THR B 188     3959   8174  11003   1030    333   -855  B    C  
ATOM   4834  C   THR B 188     -17.352  11.338 468.304  1.00 64.78      B    C  
ANISOU 4834  C   THR B 188     4817   8520  11277    982    479   -804  B    C  
ATOM   4835  O   THR B 188     -16.232  11.097 467.834  1.00 71.43      B    O  
ANISOU 4835  O   THR B 188     5972   9163  12004    919    361   -676  B    O  
ATOM   4836  CB  THR B 188     -19.267   9.975 467.447  1.00 73.01      B    C  
ANISOU 4836  CB  THR B 188     5311   9890  12539    708    439   -822  B    C  
ATOM   4837  CG2 THR B 188     -19.688   9.593 468.871  1.00 71.96      B    C  
ANISOU 4837  CG2 THR B 188     5065   9942  12337    577    800   -907  B    C  
ATOM   4838  OG1 THR B 188     -20.433   9.983 466.610  1.00 83.28      B    O  
ANISOU 4838  OG1 THR B 188     6245  11341  14055    739    274   -877  B    O  
ATOM   4839  N   SER B 189     -17.550  11.635 469.580  1.00 52.09      B    N  
ANISOU 4839  N   SER B 189     3164   7014   9615   1021    735   -913  B    N  
ATOM   4840  CA  SER B 189     -16.437  11.650 470.515  1.00 50.27      B    C  
ANISOU 4840  CA  SER B 189     3271   6660   9168    976    859   -876  B    C  
ATOM   4841  C   SER B 189     -15.990  10.223 470.804  1.00 55.07      B    C  
ANISOU 4841  C   SER B 189     4039   7275   9611    655    956   -744  B    C  
ATOM   4842  O   SER B 189     -16.798   9.374 471.182  1.00 77.87      B    O  
ANISOU 4842  O   SER B 189     6749  10342  12496    458   1126   -759  B    O  
ATOM   4843  CB  SER B 189     -16.852  12.357 471.796  1.00 52.48      B    C  
ANISOU 4843  CB  SER B 189     3477   7049   9413   1099   1106  -1041  B    C  
ATOM   4844  OG  SER B 189     -15.828  12.311 472.760  1.00 70.16      B    O  
ANISOU 4844  OG  SER B 189     6047   9185  11424   1032   1213  -1008  B    O  
ATOM   4845  N   MET B 190     -14.714   9.948 470.586  1.00 51.22      B    N  
ANISOU 4845  N   MET B 190     3879   6585   8998    602    844   -616  B    N  
ATOM   4846  CA  MET B 190     -14.101   8.686 470.981  1.00 56.00      B    C  
ANISOU 4846  CA  MET B 190     4692   7150   9434    345    924   -489  B    C  
ATOM   4847  C   MET B 190     -13.445   8.791 472.347  1.00 52.30      B    C  
ANISOU 4847  C   MET B 190     4446   6657   8769    332   1084   -502  B    C  
ATOM   4848  O   MET B 190     -12.693   7.895 472.741  1.00 63.60      B    O  
ANISOU 4848  O   MET B 190     6112   8009  10043    166   1109   -387  B    O  
ATOM   4849  CB  MET B 190     -13.064   8.230 469.931  1.00 53.41      B    C  
ANISOU 4849  CB  MET B 190     4582   6618   9095    299    710   -345  B    C  
ATOM   4850  CG  MET B 190     -13.650   7.861 468.576  1.00 46.70      B    C  
ANISOU 4850  CG  MET B 190     3581   5779   8384    251    550   -312  B    C  
ATOM   4851  SD  MET B 190     -14.796   6.476 468.732  1.00 59.45      B    S  
ANISOU 4851  SD  MET B 190     4998   7584  10005    -48    695   -299  B    S  
ATOM   4852  CE  MET B 190     -15.586   6.442 467.117  1.00 77.26      B    C  
ANISOU 4852  CE  MET B 190     7040   9868  12448    -44    453   -302  B    C  
ATOM   4853  N   LEU B 191     -13.708   9.875 473.063  1.00 46.41      B    N  
ANISOU 4853  N   LEU B 191     3644   5966   8025    511   1179   -643  B    N  
ATOM   4854  CA  LEU B 191     -13.060  10.126 474.340  1.00 46.57      B    C  
ANISOU 4854  CA  LEU B 191     3902   5952   7842    514   1303   -672  B    C  
ATOM   4855  C   LEU B 191     -13.390   9.017 475.326  1.00 48.08      B    C  
ANISOU 4855  C   LEU B 191     4151   6263   7855    263   1533   -631  B    C  
ATOM   4856  O   LEU B 191     -14.561   8.678 475.513  1.00 60.12      B    O  
ANISOU 4856  O   LEU B 191     5433   7981   9431    168   1720   -698  B    O  
ATOM   4857  CB  LEU B 191     -13.533  11.472 474.886  1.00 48.37      B    C  
ANISOU 4857  CB  LEU B 191     4031   6232   8115    748   1391   -860  B    C  
ATOM   4858  CG  LEU B 191     -12.884  11.918 476.178  1.00 48.81      B    C  
ANISOU 4858  CG  LEU B 191     4349   6242   7954    771   1502   -917  B    C  
ATOM   4859  CD1 LEU B 191     -11.376  11.754 476.090  1.00 46.09      B    C  
ANISOU 4859  CD1 LEU B 191     4323   5689   7499    730   1304   -783  B    C  
ATOM   4860  CD2 LEU B 191     -13.272  13.334 476.508  1.00 74.74      B    C  
ANISOU 4860  CD2 LEU B 191     7561   9531  11306   1028   1553  -1110  B    C  
ATOM   4861  N   ASN B 192     -12.356   8.458 475.964  1.00 54.59      B    N  
ANISOU 4861  N   ASN B 192     5299   6972   8472    153   1515   -521  B    N  
ATOM   4862  CA  ASN B 192     -12.468   7.405 476.974  1.00 54.31      B    C  
ANISOU 4862  CA  ASN B 192     5418   6999   8217    -87   1705   -455  B    C  
ATOM   4863  C   ASN B 192     -12.934   6.079 476.396  1.00 59.76      B    C  
ANISOU 4863  C   ASN B 192     6034   7722   8951   -321   1726   -338  B    C  
ATOM   4864  O   ASN B 192     -13.371   5.196 477.155  1.00 59.12      B    O  
ANISOU 4864  O   ASN B 192     6024   7723   8717   -547   1925   -297  B    O  
ATOM   4865  CB  ASN B 192     -13.400   7.789 478.123  1.00 53.74      B    C  
ANISOU 4865  CB  ASN B 192     5262   7117   8041   -105   2004   -605  B    C  
ATOM   4866  CG  ASN B 192     -12.660   8.358 479.283  1.00 78.08      B    C  
ANISOU 4866  CG  ASN B 192     8639  10135  10894    -39   2041   -647  B    C  
ATOM   4867  ND2 ASN B 192     -12.419   9.664 479.246  1.00 78.77      B    N  
ANISOU 4867  ND2 ASN B 192     8701  10172  11055    208   1962   -775  B    N  
ATOM   4868  OD1 ASN B 192     -12.293   7.635 480.215  1.00 99.53      B    O  
ANISOU 4868  OD1 ASN B 192    11628  12832  13357   -212   2128   -563  B    O  
ATOM   4869  N   HIS B 193     -12.928   5.937 475.078  1.00 46.98      B    N  
ANISOU 4869  N   HIS B 193     4282   6042   7525   -288   1539   -291  B    N  
ATOM   4870  CA  HIS B 193     -13.228   4.659 474.462  1.00 52.34      B    C  
ANISOU 4870  CA  HIS B 193     4940   6713   8233   -516   1526   -179  B    C  
ATOM   4871  C   HIS B 193     -11.980   3.774 474.464  1.00 45.67      B    C  
ANISOU 4871  C   HIS B 193     4444   5654   7255   -599   1402     -9  B    C  
ATOM   4872  O   HIS B 193     -10.858   4.245 474.248  1.00 43.03      B    O  
ANISOU 4872  O   HIS B 193     4263   5165   6921   -439   1228     24  B    O  
ATOM   4873  CB  HIS B 193     -13.771   4.868 473.043  1.00 46.42      B    C  
ANISOU 4873  CB  HIS B 193     3925   5987   7727   -450   1368   -209  B    C  
ATOM   4874  CG  HIS B 193     -15.169   5.408 473.004  1.00 55.84      B    C  
ANISOU 4874  CG  HIS B 193     4735   7409   9074   -412   1485   -360  B    C  
ATOM   4875  CD2 HIS B 193     -16.195   5.170 472.153  1.00 62.92      B    C  
ANISOU 4875  CD2 HIS B 193     5325   8427  10153   -478   1446   -398  B    C  
ATOM   4876  ND1 HIS B 193     -15.648   6.307 473.934  1.00 70.70      B    N  
ANISOU 4876  ND1 HIS B 193     6501   9424  10937   -284   1663   -505  B    N  
ATOM   4877  CE1 HIS B 193     -16.909   6.596 473.660  1.00 53.16      B    C  
ANISOU 4877  CE1 HIS B 193     3898   7401   8899   -258   1739   -628  B    C  
ATOM   4878  NE2 HIS B 193     -17.266   5.919 472.585  1.00 52.89      B    N  
ANISOU 4878  NE2 HIS B 193     3733   7369   8992   -378   1596   -562  B    N  
ATOM   4879  N   HIS B 194     -12.184   2.482 474.701  1.00 46.15      B    N  
ANISOU 4879  N   HIS B 194     4622   5701   7213   -851   1493     95  B    N  
ATOM   4880  CA  HIS B 194     -11.099   1.515 474.668  1.00 44.84      B    C  
ANISOU 4880  CA  HIS B 194     4777   5322   6939   -924   1375    258  B    C  
ATOM   4881  C   HIS B 194     -11.058   0.848 473.311  1.00 43.60      B    C  
ANISOU 4881  C   HIS B 194     4572   5064   6930   -979   1231    320  B    C  
ATOM   4882  O   HIS B 194     -12.097   0.595 472.698  1.00 44.68      B    O  
ANISOU 4882  O   HIS B 194     4485   5312   7180  -1099   1279    276  B    O  
ATOM   4883  CB  HIS B 194     -11.256   0.431 475.728  1.00 46.91      B    C  
ANISOU 4883  CB  HIS B 194     5270   5578   6978  -1165   1543    352  B    C  
ATOM   4884  CG  HIS B 194     -11.239   0.946 477.125  1.00 55.09      B    C  
ANISOU 4884  CG  HIS B 194     6424   6694   7812  -1143   1692    304  B    C  
ATOM   4885  CD2 HIS B 194     -10.282   0.889 478.080  1.00 48.45      B    C  
ANISOU 4885  CD2 HIS B 194     5905   5742   6761  -1104   1643    377  B    C  
ATOM   4886  ND1 HIS B 194     -12.310   1.606 477.688  1.00 56.28      B    N  
ANISOU 4886  ND1 HIS B 194     6358   7069   7958  -1160   1918    158  B    N  
ATOM   4887  CE1 HIS B 194     -12.009   1.944 478.929  1.00 63.66      B    C  
ANISOU 4887  CE1 HIS B 194     7500   8019   8669  -1140   2020    138  B    C  
ATOM   4888  NE2 HIS B 194     -10.787   1.515 479.193  1.00 60.71      B    N  
ANISOU 4888  NE2 HIS B 194     7460   7445   8161  -1112   1841    275  B    N  
ATOM   4889  N   PHE B 195      -9.850   0.559 472.856  1.00 41.59      B    N  
ANISOU 4889  N   PHE B 195     4526   4601   6675   -896   1056    413  B    N  
ATOM   4890  CA  PHE B 195      -9.595  -0.177 471.639  1.00 40.48      B    C  
ANISOU 4890  CA  PHE B 195     4422   4324   6636   -946    929    479  B    C  
ATOM   4891  C   PHE B 195      -8.763  -1.401 471.961  1.00 40.53      B    C  
ANISOU 4891  C   PHE B 195     4747   4133   6518  -1045    904    623  B    C  
ATOM   4892  O   PHE B 195      -7.938  -1.373 472.883  1.00 44.02      B    O  
ANISOU 4892  O   PHE B 195     5386   4504   6836   -973    888    676  B    O  
ATOM   4893  CB  PHE B 195      -8.865   0.684 470.601  1.00 47.01      B    C  
ANISOU 4893  CB  PHE B 195     5188   5068   7605   -725    747    441  B    C  
ATOM   4894  CG  PHE B 195      -9.672   1.856 470.124  1.00 49.80      B    C  
ANISOU 4894  CG  PHE B 195     5257   5575   8090   -611    733    314  B    C  
ATOM   4895  CD1 PHE B 195     -10.031   2.873 470.999  1.00 39.10      B    C  
ANISOU 4895  CD1 PHE B 195     3788   4357   6712   -503    821    217  B    C  
ATOM   4896  CD2 PHE B 195     -10.079   1.936 468.812  1.00 37.86      B    C  
ANISOU 4896  CD2 PHE B 195     3611   4058   6716   -605    624    288  B    C  
ATOM   4897  CE1 PHE B 195     -10.775   3.918 470.578  1.00 39.50      B    C  
ANISOU 4897  CE1 PHE B 195     3588   4528   6894   -376    801    100  B    C  
ATOM   4898  CE2 PHE B 195     -10.828   2.996 468.385  1.00 50.50      B    C  
ANISOU 4898  CE2 PHE B 195     4965   5786   8438   -483    583    182  B    C  
ATOM   4899  CZ  PHE B 195     -11.175   3.991 469.266  1.00 39.10      B    C  
ANISOU 4899  CZ  PHE B 195     3399   4469   6990   -358    671     87  B    C  
ATOM   4900  N   PRO B 196      -8.972  -2.490 471.237  1.00 40.88      B    N  
ANISOU 4900  N   PRO B 196     4862   4079   6593  -1205    888    685  B    N  
ATOM   4901  CA  PRO B 196      -8.220  -3.718 471.495  1.00 41.25      B    C  
ANISOU 4901  CA  PRO B 196     5230   3908   6534  -1287    860    821  B    C  
ATOM   4902  C   PRO B 196      -6.826  -3.676 470.885  1.00 39.23      B    C  
ANISOU 4902  C   PRO B 196     5101   3455   6350  -1079    685    860  B    C  
ATOM   4903  O   PRO B 196      -6.553  -2.945 469.938  1.00 37.57      B    O  
ANISOU 4903  O   PRO B 196     4746   3252   6278   -936    594    791  B    O  
ATOM   4904  CB  PRO B 196      -9.089  -4.785 470.826  1.00 49.10      B    C  
ANISOU 4904  CB  PRO B 196     6225   4876   7555  -1541    914    843  B    C  
ATOM   4905  CG  PRO B 196      -9.700  -4.044 469.675  1.00 49.79      B    C  
ANISOU 4905  CG  PRO B 196     6014   5086   7815  -1489    853    728  B    C  
ATOM   4906  CD  PRO B 196      -9.960  -2.657 470.161  1.00 41.31      B    C  
ANISOU 4906  CD  PRO B 196     4711   4210   6776  -1324    884    627  B    C  
ATOM   4907  N   ALA B 197      -5.937  -4.497 471.450  1.00 39.69      B    N  
ANISOU 4907  N   ALA B 197     5438   3330   6312  -1065    640    974  B    N  
ATOM   4908  CA  ALA B 197      -4.554  -4.562 470.970  1.00 38.26      B    C  
ANISOU 4908  CA  ALA B 197     5362   2963   6213   -864    487   1009  B    C  
ATOM   4909  C   ALA B 197      -4.456  -4.952 469.496  1.00 37.35      B    C  
ANISOU 4909  C   ALA B 197     5215   2737   6238   -865    442    982  B    C  
ATOM   4910  O   ALA B 197      -3.507  -4.562 468.817  1.00 35.90      B    O  
ANISOU 4910  O   ALA B 197     5003   2472   6165   -686    350    955  B    O  
ATOM   4911  CB  ALA B 197      -3.748  -5.530 471.828  1.00 39.52      B    C  
ANISOU 4911  CB  ALA B 197     5824   2938   6253   -854    436   1140  B    C  
ATOM   4912  N   SER B 198      -5.422  -5.708 468.981  1.00 38.39      B    N  
ANISOU 4912  N   SER B 198     5359   2867   6361  -1078    512    983  B    N  
ATOM   4913  CA  SER B 198      -5.409  -6.134 467.586  1.00 37.86      B    C  
ANISOU 4913  CA  SER B 198     5300   2691   6396  -1106    467    952  B    C  
ATOM   4914  C   SER B 198      -5.398  -4.965 466.612  1.00 45.76      B    C  
ANISOU 4914  C   SER B 198     6073   3795   7518   -974    407    846  B    C  
ATOM   4915  O   SER B 198      -5.061  -5.151 465.437  1.00 35.50      B    O  
ANISOU 4915  O   SER B 198     4814   2385   6291   -944    355    819  B    O  
ATOM   4916  CB  SER B 198      -6.616  -7.026 467.314  1.00 39.62      B    C  
ANISOU 4916  CB  SER B 198     5548   2930   6576  -1393    544    957  B    C  
ATOM   4917  OG  SER B 198      -7.790  -6.246 467.218  1.00 54.48      B    O  
ANISOU 4917  OG  SER B 198     7144   5061   8494  -1479    588    869  B    O  
ATOM   4918  N   ASP B 199      -5.760  -3.764 467.068  1.00 45.42      B    N  
ANISOU 4918  N   ASP B 199     5819   3948   7489   -895    417    785  B    N  
ATOM   4919  CA  ASP B 199      -5.945  -2.658 466.136  1.00 49.15      B    C  
ANISOU 4919  CA  ASP B 199     6095   4513   8068   -792    354    692  B    C  
ATOM   4920  C   ASP B 199      -4.627  -2.087 465.660  1.00 32.76      B    C  
ANISOU 4920  C   ASP B 199     4067   2321   6060   -584    276    684  B    C  
ATOM   4921  O   ASP B 199      -4.573  -1.542 464.555  1.00 39.99      B    O  
ANISOU 4921  O   ASP B 199     4920   3224   7048   -529    222    631  B    O  
ATOM   4922  CB  ASP B 199      -6.780  -1.560 466.792  1.00 47.80      B    C  
ANISOU 4922  CB  ASP B 199     5695   4568   7898   -760    394    622  B    C  
ATOM   4923  CG  ASP B 199      -8.237  -1.915 466.847  1.00 47.67      B    C  
ANISOU 4923  CG  ASP B 199     5536   4704   7871   -963    471    591  B    C  
ATOM   4924  OD1 ASP B 199      -8.583  -3.041 466.425  1.00 56.72      B    O  
ANISOU 4924  OD1 ASP B 199     6783   5774   8996  -1152    486    632  B    O  
ATOM   4925  OD2 ASP B 199      -9.019  -1.099 467.360  1.00 50.54      B    O1-
ANISOU 4925  OD2 ASP B 199     5691   5260   8252   -938    524    520  B    O1-
ATOM   4926  N   ILE B 200      -3.574  -2.199 466.467  1.00 39.71      B    N  
ANISOU 4926  N   ILE B 200     5057   3117   6914   -477    264    735  B    N  
ATOM   4927  CA  ILE B 200      -2.200  -1.938 466.037  1.00 37.46      B    C  
ANISOU 4927  CA  ILE B 200     4820   2703   6711   -306    201    734  B    C  
ATOM   4928  C   ILE B 200      -1.345  -3.133 466.443  1.00 34.06      B    C  
ANISOU 4928  C   ILE B 200     4591   2092   6256   -289    191    821  B    C  
ATOM   4929  O   ILE B 200      -0.932  -3.212 467.610  1.00 32.84      B    O  
ANISOU 4929  O   ILE B 200     4496   1939   6041   -241    164    874  B    O  
ATOM   4930  CB  ILE B 200      -1.640  -0.650 466.664  1.00 39.03      B    C  
ANISOU 4930  CB  ILE B 200     4904   2989   6935   -154    158    693  B    C  
ATOM   4931  CG1 ILE B 200      -2.719   0.430 466.692  1.00 44.92      B    C  
ANISOU 4931  CG1 ILE B 200     5474   3918   7675   -173    178    617  B    C  
ATOM   4932  CG2 ILE B 200      -0.405  -0.170 465.899  1.00 29.62      B    C  
ANISOU 4932  CG2 ILE B 200     3699   1696   5859    -13    109    665  B    C  
ATOM   4933  CD1 ILE B 200      -2.299   1.703 467.365  1.00 48.90      B    C  
ANISOU 4933  CD1 ILE B 200     5894   4496   8189    -39    143    567  B    C  
ATOM   4934  N   PRO B 201      -1.055  -4.068 465.535  1.00 46.57      B    N  
ANISOU 4934  N   PRO B 201     6303   3529   7860   -316    201    828  B    N  
ATOM   4935  CA  PRO B 201      -0.229  -5.228 465.883  1.00 33.63      B    C  
ANISOU 4935  CA  PRO B 201     4868   1774   6138   -264    175    874  B    C  
ATOM   4936  C   PRO B 201       1.202  -4.822 466.203  1.00 37.53      B    C  
ANISOU 4936  C   PRO B 201     5322   2275   6663    -50    103    853  B    C  
ATOM   4937  O   PRO B 201       1.659  -3.730 465.861  1.00 37.38      B    O  
ANISOU 4937  O   PRO B 201     5139   2355   6710     43     87    783  B    O  
ATOM   4938  CB  PRO B 201      -0.262  -6.083 464.618  1.00 33.99      B    C  
ANISOU 4938  CB  PRO B 201     5032   1756   6127   -318    200    818  B    C  
ATOM   4939  CG  PRO B 201      -1.425  -5.594 463.839  1.00 52.12      B    C  
ANISOU 4939  CG  PRO B 201     7219   4130   8455   -463    234    775  B    C  
ATOM   4940  CD  PRO B 201      -1.509  -4.133 464.140  1.00 54.36      B    C  
ANISOU 4940  CD  PRO B 201     7279   4533   8841   -385    218    754  B    C  
ATOM   4941  N   ALA B 202       1.917  -5.741 466.858  1.00 34.54      B    N  
ANISOU 4941  N   ALA B 202     5102   1786   6237     19     53    915  B    N  
ATOM   4942  CA  ALA B 202       3.275  -5.452 467.308  1.00 35.39      B    C  
ANISOU 4942  CA  ALA B 202     5156   1898   6394    214    -34    904  B    C  
ATOM   4943  C   ALA B 202       4.162  -4.956 466.174  1.00 40.64      B    C  
ANISOU 4943  C   ALA B 202     5682   2629   7130    316    -10    789  B    C  
ATOM   4944  O   ALA B 202       4.952  -4.025 466.353  1.00 42.30      B    O  
ANISOU 4944  O   ALA B 202     5731   2923   7417    415    -52    750  B    O  
ATOM   4945  CB  ALA B 202       3.880  -6.697 467.939  1.00 36.60      B    C  
ANISOU 4945  CB  ALA B 202     5521   1898   6489    284    -96    983  B    C  
ATOM   4946  N   GLN B 203       4.020  -5.548 464.994  1.00 47.12      B    N  
ANISOU 4946  N   GLN B 203     6574   3406   7922    269     62    737  B    N  
ATOM   4947  CA  GLN B 203       4.857  -5.180 463.863  1.00 42.60      B    C  
ANISOU 4947  CA  GLN B 203     5906   2870   7408    344    108    641  B    C  
ATOM   4948  C   GLN B 203       4.693  -3.710 463.512  1.00 41.62      B    C  
ANISOU 4948  C   GLN B 203     5595   2891   7329    322    128    588  B    C  
ATOM   4949  O   GLN B 203       5.638  -3.060 463.055  1.00 50.12      B    O  
ANISOU 4949  O   GLN B 203     6551   4015   8478    397    147    530  B    O  
ATOM   4950  CB  GLN B 203       4.491  -6.054 462.665  1.00 41.03      B    C  
ANISOU 4950  CB  GLN B 203     5857   2584   7147    267    177    602  B    C  
ATOM   4951  CG  GLN B 203       5.584  -6.199 461.638  1.00 54.96      B    C  
ANISOU 4951  CG  GLN B 203     7601   4313   8969    365    234    523  B    C  
ATOM   4952  CD  GLN B 203       5.117  -6.997 460.427  1.00 72.36      B    C  
ANISOU 4952  CD  GLN B 203     9974   6420  11100    274    292    481  B    C  
ATOM   4953  NE2 GLN B 203       3.950  -7.683 460.557  1.00 58.01      B    N  
ANISOU 4953  NE2 GLN B 203     8312   4544   9184    127    263    526  B    N  
ATOM   4954  OE1 GLN B 203       5.781  -6.979 459.371  1.00 64.57      B    O  
ANISOU 4954  OE1 GLN B 203     8977   5407  10150    318    367    407  B    O  
ATOM   4955  N   ALA B 204       3.477  -3.192 463.662  1.00 66.93      B    N  
ANISOU 4955  N   ALA B 204     8777   6152  10502    211    130    607  B    N  
ATOM   4956  CA  ALA B 204       3.174  -1.790 463.387  1.00 39.42      B    C  
ANISOU 4956  CA  ALA B 204     5141   2782   7055    199    133    562  B    C  
ATOM   4957  C   ALA B 204       3.572  -0.886 464.537  1.00 29.56      B    C  
ANISOU 4957  C   ALA B 204     3774   1593   5863    272     67    578  B    C  
ATOM   4958  O   ALA B 204       4.069   0.209 464.304  1.00 50.83      B    O  
ANISOU 4958  O   ALA B 204     6352   4359   8603    314     60    524  B    O  
ATOM   4959  CB  ALA B 204       1.688  -1.615 463.088  1.00 34.28      B    C  
ANISOU 4959  CB  ALA B 204     4495   2149   6381     68    150    573  B    C  
ATOM   4960  N   ARG B 205       3.333  -1.290 465.784  1.00 30.23      B    N  
ANISOU 4960  N   ARG B 205     3910   1637   5940    274     15    655  B    N  
ATOM   4961  CA  ARG B 205       3.849  -0.485 466.881  1.00 30.26      B    C  
ANISOU 4961  CA  ARG B 205     3832   1679   5988    353    -68    666  B    C  
ATOM   4962  C   ARG B 205       5.348  -0.354 466.767  1.00 37.72      B    C  
ANISOU 4962  C   ARG B 205     4707   2634   6991    465   -114    625  B    C  
ATOM   4963  O   ARG B 205       5.928   0.653 467.177  1.00 43.12      B    O  
ANISOU 4963  O   ARG B 205     5276   3375   7734    513   -171    591  B    O  
ATOM   4964  CB  ARG B 205       3.504  -1.085 468.227  1.00 31.35      B    C  
ANISOU 4964  CB  ARG B 205     4083   1740   6090    339   -125    774  B    C  
ATOM   4965  CG  ARG B 205       2.039  -1.167 468.511  1.00 35.83      B    C  
ANISOU 4965  CG  ARG B 205     4693   2320   6602    198    -55    816  B    C  
ATOM   4966  CD  ARG B 205       1.855  -1.471 469.960  1.00 39.66      B    C  
ANISOU 4966  CD  ARG B 205     5290   2843   6937    168    -97    884  B    C  
ATOM   4967  NE  ARG B 205       2.395  -2.784 470.295  1.00 52.04      B    N  
ANISOU 4967  NE  ARG B 205     7048   4246   8480    187   -149    989  B    N  
ATOM   4968  CZ  ARG B 205       1.764  -3.936 470.122  1.00 52.55      B    C  
ANISOU 4968  CZ  ARG B 205     7270   4219   8478     67    -84   1053  B    C  
ATOM   4969  NH1 ARG B 205       0.545  -3.957 469.608  1.00 61.70      B    N1+
ANISOU 4969  NH1 ARG B 205     8392   5456   9595    -96     35   1020  B    N1+
ATOM   4970  NH2 ARG B 205       2.360  -5.066 470.466  1.00 37.69      B    N  
ANISOU 4970  NH2 ARG B 205     5584   2159   6579    112   -149   1150  B    N  
ATOM   4971  N   ALA B 206       5.991  -1.366 466.205  1.00 45.97      B    N  
ANISOU 4971  N   ALA B 206     5815   3612   8038    504    -86    623  B    N  
ATOM   4972  CA  ALA B 206       7.429  -1.336 466.064  1.00 42.11      B    C  
ANISOU 4972  CA  ALA B 206     5230   3120   7649    614   -115    585  B    C  
ATOM   4973  C   ALA B 206       7.874  -0.276 465.068  1.00 35.70      B    C  
ANISOU 4973  C   ALA B 206     4274   2382   6910    591    -41    496  B    C  
ATOM   4974  O   ALA B 206       9.024   0.164 465.134  1.00 32.43      B    O  
ANISOU 4974  O   ALA B 206     3724   1982   6616    656    -68    461  B    O  
ATOM   4975  CB  ALA B 206       7.923  -2.726 465.671  1.00 33.44      B    C  
ANISOU 4975  CB  ALA B 206     4246   1911   6550    674    -89    600  B    C  
ATOM   4976  N   MET B 207       6.987   0.165 464.170  1.00 42.21      B    N  
ANISOU 4976  N   MET B 207     5126   3242   7670    496     43    466  B    N  
ATOM   4977  CA  MET B 207       7.385   1.139 463.157  1.00 44.28      B    C  
ANISOU 4977  CA  MET B 207     5300   3546   7980    468    116    398  B    C  
ATOM   4978  C   MET B 207       7.777   2.472 463.786  1.00 45.42      B    C  
ANISOU 4978  C   MET B 207     5312   3752   8194    479     53    375  B    C  
ATOM   4979  O   MET B 207       8.729   3.128 463.343  1.00 29.59      B    O  
ANISOU 4979  O   MET B 207     3200   1746   6296    486     89    328  B    O  
ATOM   4980  CB  MET B 207       6.257   1.340 462.149  1.00 49.89      B    C  
ANISOU 4980  CB  MET B 207     6098   4270   8589    374    179    383  B    C  
ATOM   4981  CG  MET B 207       6.144   0.228 461.133  1.00 49.24      B    C  
ANISOU 4981  CG  MET B 207     6145   4109   8455    347    256    376  B    C  
ATOM   4982  SD  MET B 207       7.642  -0.013 460.140  1.00 54.62      B    S  
ANISOU 4982  SD  MET B 207     6787   4725   9239    404    370    316  B    S  
ATOM   4983  CE  MET B 207       7.131  -1.255 458.967  1.00 59.24      B    C  
ANISOU 4983  CE  MET B 207     7580   5207   9721    355    450    302  B    C  
ATOM   4984  N   TYR B 208       7.062   2.885 464.826  1.00 28.89      B    N  
ANISOU 4984  N   TYR B 208     3228   1693   6055    475    -32    404  B    N  
ATOM   4985  CA  TYR B 208       7.324   4.195 465.406  1.00 34.36      B    C  
ANISOU 4985  CA  TYR B 208     3827   2428   6800    481    -95    371  B    C  
ATOM   4986  C   TYR B 208       8.773   4.318 465.851  1.00 30.32      B    C  
ANISOU 4986  C   TYR B 208     3196   1895   6430    541   -160    353  B    C  
ATOM   4987  O   TYR B 208       9.339   5.418 465.831  1.00 44.80      B    O  
ANISOU 4987  O   TYR B 208     4931   3738   8354    525   -178    303  B    O  
ATOM   4988  CB  TYR B 208       6.360   4.445 466.566  1.00 28.51      B    C  
ANISOU 4988  CB  TYR B 208     3132   1703   5999    486   -171    403  B    C  
ATOM   4989  CG  TYR B 208       4.939   4.525 466.100  1.00 35.46      B    C  
ANISOU 4989  CG  TYR B 208     4070   2601   6803    429   -108    408  B    C  
ATOM   4990  CD1 TYR B 208       4.498   5.609 465.354  1.00 31.91      B    C  
ANISOU 4990  CD1 TYR B 208     3594   2189   6343    398    -75    355  B    C  
ATOM   4991  CD2 TYR B 208       4.044   3.496 466.358  1.00 36.67      B    C  
ANISOU 4991  CD2 TYR B 208     4306   2717   6911    400    -89    470  B    C  
ATOM   4992  CE1 TYR B 208       3.194   5.704 464.911  1.00 26.69      B    C  
ANISOU 4992  CE1 TYR B 208     2961   1536   5643    363    -45    358  B    C  
ATOM   4993  CE2 TYR B 208       2.736   3.573 465.905  1.00 42.76      B    C  
ANISOU 4993  CE2 TYR B 208     5091   3494   7661    339    -40    472  B    C  
ATOM   4994  CZ  TYR B 208       2.318   4.689 465.176  1.00 46.12      B    C  
ANISOU 4994  CZ  TYR B 208     5464   3966   8094    332    -27    413  B    C  
ATOM   4995  OH  TYR B 208       1.024   4.795 464.700  1.00 43.45      B    O  
ANISOU 4995  OH  TYR B 208     5116   3625   7770    290     -6    413  B    O  
ATOM   4996  N   SER B 209       9.395   3.204 466.241  1.00 39.75      B    N  
ANISOU 4996  N   SER B 209     4396   3047   7661    613   -204    391  B    N  
ATOM   4997  CA  SER B 209      10.803   3.233 466.613  1.00 32.27      B    C  
ANISOU 4997  CA  SER B 209     3304   2079   6879    687   -284    372  B    C  
ATOM   4998  C   SER B 209      11.737   3.438 465.433  1.00 32.72      B    C  
ANISOU 4998  C   SER B 209     3233   2114   7086    672   -160    307  B    C  
ATOM   4999  O   SER B 209      12.857   3.906 465.627  1.00 42.49      B    O  
ANISOU 4999  O   SER B 209     4295   3342   8508    701   -208    267  B    O  
ATOM   5000  CB  SER B 209      11.139   1.982 467.364  1.00 33.60      B    C  
ANISOU 5000  CB  SER B 209     3530   2200   7036    787   -382    436  B    C  
ATOM   5001  OG  SER B 209      10.483   2.102 468.598  1.00 48.12      B    O  
ANISOU 5001  OG  SER B 209     5464   4044   8776    793   -510    494  B    O  
ATOM   5002  N   ILE B 210      11.314   3.106 464.221  1.00 32.10      B    N  
ANISOU 5002  N   ILE B 210     3234   2018   6946    623     -3    294  B    N  
ATOM   5003  CA  ILE B 210      12.111   3.448 463.057  1.00 32.64      B    C  
ANISOU 5003  CA  ILE B 210     3203   2048   7150    594    143    232  B    C  
ATOM   5004  C   ILE B 210      11.815   4.871 462.603  1.00 31.73      B    C  
ANISOU 5004  C   ILE B 210     3075   1952   7031    494    190    198  B    C  
ATOM   5005  O   ILE B 210      12.725   5.671 462.367  1.00 44.32      B    O  
ANISOU 5005  O   ILE B 210     4524   3509   8806    469    234    148  B    O  
ATOM   5006  CB  ILE B 210      11.866   2.443 461.926  1.00 42.96      B    C  
ANISOU 5006  CB  ILE B 210     4630   3305   8389    592    288    228  B    C  
ATOM   5007  CG1 ILE B 210      12.434   1.070 462.298  1.00 34.18      B    C  
ANISOU 5007  CG1 ILE B 210     3523   2142   7323    710    251    248  B    C  
ATOM   5008  CG2 ILE B 210      12.445   2.990 460.634  1.00 33.20      B    C  
ANISOU 5008  CG2 ILE B 210     3337   2021   7257    536    471    165  B    C  
ATOM   5009  CD1 ILE B 210      11.404   0.051 462.588  1.00 33.68      B    C  
ANISOU 5009  CD1 ILE B 210     3663   2060   7072    716    203    309  B    C  
ATOM   5010  N   ASN B 211      10.549   5.217 462.490  1.00 30.33      B    N  
ANISOU 5010  N   ASN B 211     3044   1817   6663    440    179    221  B    N  
ATOM   5011  CA  ASN B 211      10.156   6.562 462.093  1.00 30.11      B    C  
ANISOU 5011  CA  ASN B 211     3042   1802   6598    365    200    194  B    C  
ATOM   5012  C   ASN B 211       8.955   6.999 462.926  1.00 28.63      B    C  
ANISOU 5012  C   ASN B 211     2934   1676   6268    365     88    218  B    C  
ATOM   5013  O   ASN B 211       7.905   6.349 462.888  1.00 27.99      B    O  
ANISOU 5013  O   ASN B 211     2957   1624   6055    367     84    253  B    O  
ATOM   5014  CB  ASN B 211       9.844   6.574 460.597  1.00 29.46      B    C  
ANISOU 5014  CB  ASN B 211     3072   1686   6435    304    342    182  B    C  
ATOM   5015  CG  ASN B 211       9.554   7.951 460.069  1.00 33.91      B    C  
ANISOU 5015  CG  ASN B 211     3695   2240   6951    234    359    161  B    C  
ATOM   5016  ND2 ASN B 211       9.783   8.144 458.784  1.00 40.13      B    N  
ANISOU 5016  ND2 ASN B 211     4563   2966   7718    174    492    144  B    N  
ATOM   5017  OD1 ASN B 211       9.115   8.832 460.800  1.00 45.13      B    O  
ANISOU 5017  OD1 ASN B 211     5114   3693   8340    235    257    161  B    O  
ATOM   5018  N   PRO B 212       9.058   8.087 463.692  1.00 28.68      B    N  
ANISOU 5018  N   PRO B 212     2892   1690   6316    363      3    194  B    N  
ATOM   5019  CA  PRO B 212       7.979   8.421 464.638  1.00 28.08      B    C  
ANISOU 5019  CA  PRO B 212     2880   1658   6132    385    -90    206  B    C  
ATOM   5020  C   PRO B 212       6.677   8.853 463.988  1.00 28.81      B    C  
ANISOU 5020  C   PRO B 212     3079   1776   6091    358    -52    207  B    C  
ATOM   5021  O   PRO B 212       5.652   8.906 464.682  1.00 27.74      B    O  
ANISOU 5021  O   PRO B 212     2976   1670   5893    386   -100    216  B    O  
ATOM   5022  CB  PRO B 212       8.587   9.555 465.477  1.00 28.68      B    C  
ANISOU 5022  CB  PRO B 212     2888   1706   6305    390   -182    161  B    C  
ATOM   5023  CG  PRO B 212       9.718  10.051 464.692  1.00 29.37      B    C  
ANISOU 5023  CG  PRO B 212     2889   1733   6539    340   -119    125  B    C  
ATOM   5024  CD  PRO B 212      10.248   8.921 463.900  1.00 29.65      B    C  
ANISOU 5024  CD  PRO B 212     2884   1760   6623    347    -19    148  B    C  
ATOM   5025  N   ILE B 213       6.665   9.151 462.698  1.00 27.12      B    N  
ANISOU 5025  N   ILE B 213     2919   1539   5847    311     28    197  B    N  
ATOM   5026  CA  ILE B 213       5.469   9.647 462.037  1.00 32.06      B    C  
ANISOU 5026  CA  ILE B 213     3646   2172   6362    298     28    200  B    C  
ATOM   5027  C   ILE B 213       5.077   8.688 460.916  1.00 26.52      B    C  
ANISOU 5027  C   ILE B 213     3024   1458   5596    267     93    228  B    C  
ATOM   5028  O   ILE B 213       5.934   8.169 460.190  1.00 26.91      B    O  
ANISOU 5028  O   ILE B 213     3083   1468   5673    239    176    225  B    O  
ATOM   5029  CB  ILE B 213       5.687  11.092 461.525  1.00 33.24      B    C  
ANISOU 5029  CB  ILE B 213     3847   2273   6508    273     27    167  B    C  
ATOM   5030  CG1 ILE B 213       4.375  11.704 461.059  1.00 38.02      B    C  
ANISOU 5030  CG1 ILE B 213     4554   2876   7016    294    -16    172  B    C  
ATOM   5031  CG2 ILE B 213       6.665  11.141 460.386  1.00 27.55      B    C  
ANISOU 5031  CG2 ILE B 213     3160   1488   5818    208    128    164  B    C  
ATOM   5032  CD1 ILE B 213       4.223  13.123 461.470  1.00 27.24      B    C  
ANISOU 5032  CD1 ILE B 213     3221   1478   5651    324    -75    135  B    C  
ATOM   5033  N   ARG B 214       3.779   8.436 460.797  1.00 26.22      B    N  
ANISOU 5033  N   ARG B 214     3031   1436   5494    272     56    248  B    N  
ATOM   5034  CA  ARG B 214       3.223   7.627 459.722  1.00 29.21      B    C  
ANISOU 5034  CA  ARG B 214     3503   1783   5812    229     90    270  B    C  
ATOM   5035  C   ARG B 214       2.112   8.418 459.059  1.00 34.28      B    C  
ANISOU 5035  C   ARG B 214     4212   2403   6412    228     29    271  B    C  
ATOM   5036  O   ARG B 214       1.204   8.894 459.751  1.00 37.95      B    O  
ANISOU 5036  O   ARG B 214     4607   2895   6915    276    -44    268  B    O  
ATOM   5037  CB  ARG B 214       2.694   6.279 460.261  1.00 26.22      B    C  
ANISOU 5037  CB  ARG B 214     3103   1417   5442    225     88    302  B    C  
ATOM   5038  CG  ARG B 214       2.143   5.338 459.202  1.00 26.49      B    C  
ANISOU 5038  CG  ARG B 214     3247   1401   5419    164    117    318  B    C  
ATOM   5039  CD  ARG B 214       3.156   4.976 458.088  1.00 26.91      B    C  
ANISOU 5039  CD  ARG B 214     3400   1397   5427    135    208    297  B    C  
ATOM   5040  NE  ARG B 214       2.734   3.760 457.394  1.00 27.35      B    N  
ANISOU 5040  NE  ARG B 214     3573   1395   5426     80    235    307  B    N  
ATOM   5041  CZ  ARG B 214       2.940   3.456 456.112  1.00 27.97      B    C  
ANISOU 5041  CZ  ARG B 214     3798   1396   5431     28    291    288  B    C  
ATOM   5042  NH1 ARG B 214       3.573   4.278 455.295  1.00 28.26      B    N1+
ANISOU 5042  NH1 ARG B 214     3892   1400   5445     18    338    265  B    N1+
ATOM   5043  NH2 ARG B 214       2.487   2.299 455.635  1.00 41.57      B    N  
ANISOU 5043  NH2 ARG B 214     5636   3058   7101    -29    301    292  B    N  
ATOM   5044  N   ILE B 215       2.158   8.545 457.731  1.00 26.80      B    N  
ANISOU 5044  N   ILE B 215     3402   1388   5394    182     54    275  B    N  
ATOM   5045  CA  ILE B 215       1.188   9.367 457.012  1.00 36.76      B    C  
ANISOU 5045  CA  ILE B 215     4750   2599   6617    191    -31    286  B    C  
ATOM   5046  C   ILE B 215       0.497   8.521 455.956  1.00 27.73      B    C  
ANISOU 5046  C   ILE B 215     3717   1394   5425    131    -48    311  B    C  
ATOM   5047  O   ILE B 215       1.151   7.871 455.134  1.00 41.18      B    O  
ANISOU 5047  O   ILE B 215     5543   3048   7057     64     38    309  B    O  
ATOM   5048  CB  ILE B 215       1.827  10.605 456.353  1.00 28.29      B    C  
ANISOU 5048  CB  ILE B 215     3801   1459   5489    181    -17    277  B    C  
ATOM   5049  CG1 ILE B 215       2.712  11.362 457.313  1.00 35.67      B    C  
ANISOU 5049  CG1 ILE B 215     4641   2431   6482    208      8    246  B    C  
ATOM   5050  CG2 ILE B 215       0.773  11.583 455.921  1.00 36.09      B    C  
ANISOU 5050  CG2 ILE B 215     4866   2392   6453    230   -137    292  B    C  
ATOM   5051  CD1 ILE B 215       3.935  11.865 456.605  1.00 45.28      B    C  
ANISOU 5051  CD1 ILE B 215     5952   3574   7677    139     98    237  B    C  
ATOM   5052  N   ILE B 216      -0.821   8.578 455.953  1.00 28.09      B    N  
ANISOU 5052  N   ILE B 216     3718   1430   5526    153   -170    330  B    N  
ATOM   5053  CA  ILE B 216      -1.671   7.960 454.953  1.00 28.87      B    C  
ANISOU 5053  CA  ILE B 216     3912   1452   5607     87   -243    356  B    C  
ATOM   5054  C   ILE B 216      -2.535   9.093 454.403  1.00 45.33      B    C  
ANISOU 5054  C   ILE B 216     6036   3478   7710    147   -412    373  B    C  
ATOM   5055  O   ILE B 216      -3.581   9.395 454.991  1.00 41.90      B    O  
ANISOU 5055  O   ILE B 216     5440   3072   7407    227   -546    372  B    O  
ATOM   5056  CB  ILE B 216      -2.496   6.838 455.599  1.00 28.83      B    C  
ANISOU 5056  CB  ILE B 216     3770   1478   5708     49   -273    367  B    C  
ATOM   5057  CG1 ILE B 216      -1.546   5.785 456.193  1.00 28.13      B    C  
ANISOU 5057  CG1 ILE B 216     3675   1435   5579     15   -121    357  B    C  
ATOM   5058  CG2 ILE B 216      -3.502   6.271 454.620  1.00 33.54      B    C  
ANISOU 5058  CG2 ILE B 216     4442   2014   6287    -44   -391    386  B    C  
ATOM   5059  CD1 ILE B 216      -2.197   4.743 457.041  1.00 28.18      B    C  
ANISOU 5059  CD1 ILE B 216     3572   1462   5672    -29   -122    377  B    C  
ATOM   5060  N   PRO B 217      -2.117   9.804 453.344  1.00 37.34      B    N  
ANISOU 5060  N   PRO B 217     5236   2377   6576    128   -412    388  B    N  
ATOM   5061  CA  PRO B 217      -2.875  10.997 452.921  1.00 42.90      B    C  
ANISOU 5061  CA  PRO B 217     5996   3023   7282    213   -593    412  B    C  
ATOM   5062  C   PRO B 217      -4.176  10.676 452.235  1.00 37.41      B    C  
ANISOU 5062  C   PRO B 217     5321   2268   6626    210   -830    446  B    C  
ATOM   5063  O   PRO B 217      -5.035  11.562 452.110  1.00 39.68      B    O  
ANISOU 5063  O   PRO B 217     5582   2566   6930    323  -1022    454  B    O  
ATOM   5064  CB  PRO B 217      -1.913  11.710 451.963  1.00 32.13      B    C  
ANISOU 5064  CB  PRO B 217     4891   1558   5760    161   -493    429  B    C  
ATOM   5065  CG  PRO B 217      -0.554  11.216 452.363  1.00 39.45      B    C  
ANISOU 5065  CG  PRO B 217     5802   2530   6659     95   -262    392  B    C  
ATOM   5066  CD  PRO B 217      -0.781   9.777 452.729  1.00 41.03      B    C  
ANISOU 5066  CD  PRO B 217     5880   2796   6912     54   -233    378  B    C  
ATOM   5067  N   ASP B 218      -4.359   9.435 451.807  1.00 42.70      B    N  
ANISOU 5067  N   ASP B 218     6020   2964   7242     84   -806    444  B    N  
ATOM   5068  CA  ASP B 218      -5.536   9.061 451.031  1.00 43.76      B    C  
ANISOU 5068  CA  ASP B 218     6178   3145   7304     37  -1008    453  B    C  
ATOM   5069  C   ASP B 218      -5.703   7.558 451.188  1.00 41.00      B    C  
ANISOU 5069  C   ASP B 218     5762   2864   6952   -101   -928    429  B    C  
ATOM   5070  O   ASP B 218      -4.940   6.784 450.603  1.00 37.28      B    O  
ANISOU 5070  O   ASP B 218     5485   2288   6392   -216   -796    429  B    O  
ATOM   5071  CB  ASP B 218      -5.365   9.449 449.563  1.00 43.57      B    C  
ANISOU 5071  CB  ASP B 218     6490   2963   7102    -20  -1099    497  B    C  
ATOM   5072  CG  ASP B 218      -6.671   9.462 448.791  1.00 46.48      B    C  
ANISOU 5072  CG  ASP B 218     6879   3378   7402    -24  -1389    513  B    C  
ATOM   5073  OD1 ASP B 218      -7.685   8.872 449.244  1.00 38.26      B    O  
ANISOU 5073  OD1 ASP B 218     5589   2500   6450    -31  -1492    479  B    O  
ATOM   5074  OD2 ASP B 218      -6.649  10.030 447.682  1.00 46.28      B    O1-
ANISOU 5074  OD2 ASP B 218     7138   3223   7225    -37  -1513    560  B    O1-
ATOM   5075  N   VAL B 219      -6.700   7.168 451.981  1.00 38.21      B    N  
ANISOU 5075  N   VAL B 219     5141   2679   6698    -90   -995    402  B    N  
ATOM   5076  CA  VAL B 219      -7.037   5.771 452.199  1.00 34.42      B    C  
ANISOU 5076  CA  VAL B 219     4594   2264   6218   -237   -940    383  B    C  
ATOM   5077  C   VAL B 219      -7.357   5.057 450.891  1.00 42.16      B    C  
ANISOU 5077  C   VAL B 219     5791   3170   7056   -391  -1043    386  B    C  
ATOM   5078  O   VAL B 219      -7.087   3.853 450.752  1.00 49.95      B    O  
ANISOU 5078  O   VAL B 219     6875   4109   7995   -533   -937    373  B    O  
ATOM   5079  CB  VAL B 219      -8.213   5.726 453.193  1.00 43.49      B    C  
ANISOU 5079  CB  VAL B 219     5413   3618   7493   -206  -1010    352  B    C  
ATOM   5080  CG1 VAL B 219      -8.964   4.438 453.090  1.00 44.00      B    C  
ANISOU 5080  CG1 VAL B 219     5421   3755   7542   -391  -1034    336  B    C  
ATOM   5081  CG2 VAL B 219      -7.721   5.979 454.610  1.00 33.53      B    C  
ANISOU 5081  CG2 VAL B 219     3992   2415   6334   -110   -843    340  B    C  
ATOM   5082  N   ASN B 220      -7.872   5.777 449.890  1.00 37.29      B    N  
ANISOU 5082  N   ASN B 220     5292   2520   6354   -364  -1254    404  B    N  
ATOM   5083  CA  ASN B 220      -8.277   5.143 448.633  1.00 38.98      B    C  
ANISOU 5083  CA  ASN B 220     5730   2672   6409   -518  -1390    404  B    C  
ATOM   5084  C   ASN B 220      -7.287   5.352 447.505  1.00 43.10      B    C  
ANISOU 5084  C   ASN B 220     6641   2990   6745   -559  -1317    429  B    C  
ATOM   5085  O   ASN B 220      -7.563   4.942 446.374  1.00 40.80      B    O  
ANISOU 5085  O   ASN B 220     6593   2626   6283   -684  -1432    427  B    O  
ATOM   5086  CB  ASN B 220      -9.644   5.636 448.184  1.00 41.14      B    C  
ANISOU 5086  CB  ASN B 220     5887   3053   6690   -487  -1716    407  B    C  
ATOM   5087  CG  ASN B 220     -10.726   5.261 449.141  1.00 48.81      B    C  
ANISOU 5087  CG  ASN B 220     6468   4240   7837   -491  -1774    365  B    C  
ATOM   5088  ND2 ASN B 220     -11.583   6.221 449.462  1.00 53.92      B    N  
ANISOU 5088  ND2 ASN B 220     6870   5010   8605   -329  -1952    359  B    N  
ATOM   5089  OD1 ASN B 220     -10.799   4.115 449.598  1.00 51.32      B    O  
ANISOU 5089  OD1 ASN B 220     6708   4608   8184   -640  -1651    336  B    O  
ATOM   5090  N   ALA B 221      -6.140   5.967 447.783  1.00 46.98      B    N  
ANISOU 5090  N   ALA B 221     7200   3390   7259   -472  -1121    445  B    N  
ATOM   5091  CA  ALA B 221      -5.122   6.092 446.755  1.00 53.15      B    C  
ANISOU 5091  CA  ALA B 221     8336   3986   7872   -535   -994    458  B    C  
ATOM   5092  C   ALA B 221      -4.582   4.717 446.388  1.00 38.18      B    C  
ANISOU 5092  C   ALA B 221     6591   2016   5900   -685   -810    411  B    C  
ATOM   5093  O   ALA B 221      -4.351   3.864 447.250  1.00 37.03      B    O  
ANISOU 5093  O   ALA B 221     6273   1920   5877   -693   -671    380  B    O  
ATOM   5094  CB  ALA B 221      -4.001   7.020 447.215  1.00 36.90      B    C  
ANISOU 5094  CB  ALA B 221     6272   1863   5885   -430   -810    476  B    C  
ATOM   5095  N   GLU B 222      -4.347   4.529 445.107  1.00 46.10      B    N  
ANISOU 5095  N   GLU B 222     7942   2883   6689   -798   -806    405  B    N  
ATOM   5096  CA  GLU B 222      -3.918   3.245 444.582  1.00 57.73      B    C  
ANISOU 5096  CA  GLU B 222     9559   4320   8054   -920   -627    338  B    C  
ATOM   5097  C   GLU B 222      -2.410   3.097 444.765  1.00 63.16      B    C  
ANISOU 5097  C   GLU B 222    10185   5021   8793   -847   -267    297  B    C  
ATOM   5098  O   GLU B 222      -1.651   3.940 444.270  1.00 65.34      B    O  
ANISOU 5098  O   GLU B 222    10553   5271   9003   -810   -165    311  B    O  
ATOM   5099  CB  GLU B 222      -4.307   3.161 443.110  1.00 69.52      B    C  
ANISOU 5099  CB  GLU B 222    11420   5719   9277  -1053   -766    334  B    C  
ATOM   5100  CG  GLU B 222      -4.182   1.802 442.436  1.00 76.81      B    C  
ANISOU 5100  CG  GLU B 222    12524   6602  10059  -1194   -656    255  B    C  
ATOM   5101  CD  GLU B 222      -4.357   1.915 440.906  1.00 83.46      B    C  
ANISOU 5101  CD  GLU B 222    13784   7340  10587  -1319   -763    249  B    C  
ATOM   5102  OE1 GLU B 222      -3.895   2.935 440.321  1.00 74.23      B    O  
ANISOU 5102  OE1 GLU B 222    12779   6128   9298  -1275   -735    292  B    O  
ATOM   5103  OE2 GLU B 222      -4.951   0.991 440.296  1.00 83.19      B    O1-
ANISOU 5103  OE2 GLU B 222    13930   7264  10415  -1472   -878    203  B    O1-
ATOM   5104  N   PRO B 223      -1.937   2.095 445.506  1.00 51.15      B    N  
ANISOU 5104  N   PRO B 223     8491   3535   7407   -825   -103    255  B    N  
ATOM   5105  CA  PRO B 223      -0.489   1.949 445.685  1.00 37.60      B    C  
ANISOU 5105  CA  PRO B 223     6690   1830   5766   -746    147    221  B    C  
ATOM   5106  C   PRO B 223       0.219   1.701 444.358  1.00 50.05      B    C  
ANISOU 5106  C   PRO B 223     8546   3333   7138   -817    291    170  B    C  
ATOM   5107  O   PRO B 223      -0.343   1.133 443.418  1.00 47.81      B    O  
ANISOU 5107  O   PRO B 223     8515   2986   6667   -933    234    141  B    O  
ATOM   5108  CB  PRO B 223      -0.362   0.746 446.627  1.00 40.19      B    C  
ANISOU 5108  CB  PRO B 223     6844   2192   6234   -719    197    196  B    C  
ATOM   5109  CG  PRO B 223      -1.651   0.032 446.548  1.00 37.48      B    C  
ANISOU 5109  CG  PRO B 223     6569   1830   5842   -834     53    194  B    C  
ATOM   5110  CD  PRO B 223      -2.698   1.041 446.195  1.00 49.12      B    C  
ANISOU 5110  CD  PRO B 223     8123   3307   7233   -880   -177    241  B    C  
ATOM   5111  N   GLN B 224       1.466   2.159 444.284  1.00 46.14      B    N  
ANISOU 5111  N   GLN B 224     8023   2843   6665   -762    482    152  B    N  
ATOM   5112  CA  GLN B 224       2.314   1.950 443.122  1.00 47.11      B    C  
ANISOU 5112  CA  GLN B 224     8402   2890   6608   -827    692     91  B    C  
ATOM   5113  C   GLN B 224       3.384   0.919 443.452  1.00 41.07      B    C  
ANISOU 5113  C   GLN B 224     7541   2122   5940   -767    920     13  B    C  
ATOM   5114  O   GLN B 224       4.188   1.142 444.367  1.00 46.92      B    O  
ANISOU 5114  O   GLN B 224     8041   2926   6862   -664   1000     16  B    O  
ATOM   5115  CB  GLN B 224       2.944   3.280 442.706  1.00 48.84      B    C  
ANISOU 5115  CB  GLN B 224     8690   3097   6768   -831    772    122  B    C  
ATOM   5116  CG  GLN B 224       1.920   4.370 442.435  1.00 41.68      B    C  
ANISOU 5116  CG  GLN B 224     7888   2178   5771   -860    529    208  B    C  
ATOM   5117  CD  GLN B 224       1.092   4.073 441.199  1.00 69.71      B    C  
ANISOU 5117  CD  GLN B 224    11804   5642   9039   -986    409    206  B    C  
ATOM   5118  NE2 GLN B 224      -0.225   3.961 441.379  1.00 64.61      B    N  
ANISOU 5118  NE2 GLN B 224    11157   5004   8387  -1002    125    246  B    N  
ATOM   5119  OE1 GLN B 224       1.632   3.894 440.101  1.00 67.56      B    O  
ANISOU 5119  OE1 GLN B 224    11827   5294   8548  -1080    569    162  B    O  
ATOM   5120  N   PRO B 225       3.430  -0.220 442.774  1.00 47.53      B    N  
ANISOU 5120  N   PRO B 225     8552   2865   6644   -823   1021    -59  B    N  
ATOM   5121  CA  PRO B 225       4.461  -1.214 443.089  1.00 55.37      B    C  
ANISOU 5121  CA  PRO B 225     9464   3832   7743   -743   1243   -135  B    C  
ATOM   5122  C   PRO B 225       5.833  -0.818 442.562  1.00 54.04      B    C  
ANISOU 5122  C   PRO B 225     9351   3617   7564   -726   1559   -197  B    C  
ATOM   5123  O   PRO B 225       5.984  -0.035 441.617  1.00 45.32      B    O  
ANISOU 5123  O   PRO B 225     8458   2470   6292   -818   1647   -199  B    O  
ATOM   5124  CB  PRO B 225       3.951  -2.493 442.411  1.00 44.46      B    C  
ANISOU 5124  CB  PRO B 225     8313   2360   6218   -822   1241   -197  B    C  
ATOM   5125  CG  PRO B 225       3.028  -2.020 441.348  1.00 45.60      B    C  
ANISOU 5125  CG  PRO B 225     8743   2468   6116   -970   1107   -177  B    C  
ATOM   5126  CD  PRO B 225       2.397  -0.764 441.875  1.00 44.00      B    C  
ANISOU 5126  CD  PRO B 225     8380   2351   5985   -953    893    -74  B    C  
ATOM   5127  N   LEU B 226       6.848  -1.372 443.215  1.00 44.01      B    N  
ANISOU 5127  N   LEU B 226     7889   2347   6486   -609   1736   -246  B    N  
ATOM   5128  CA  LEU B 226       8.212  -1.235 442.739  1.00 45.64      B    C  
ANISOU 5128  CA  LEU B 226     8119   2488   6736   -591   2090   -329  B    C  
ATOM   5129  C   LEU B 226       8.444  -2.198 441.586  1.00 53.43      B    C  
ANISOU 5129  C   LEU B 226     9412   3338   7551   -654   2314   -434  B    C  
ATOM   5130  O   LEU B 226       8.159  -3.397 441.697  1.00 48.61      B    O  
ANISOU 5130  O   LEU B 226     8841   2684   6945   -615   2266   -469  B    O  
ATOM   5131  CB  LEU B 226       9.200  -1.510 443.864  1.00 44.98      B    C  
ANISOU 5131  CB  LEU B 226     7702   2440   6947   -433   2189   -347  B    C  
ATOM   5132  CG  LEU B 226       8.923  -0.719 445.127  1.00 42.52      B    C  
ANISOU 5132  CG  LEU B 226     7105   2264   6785   -369   1952   -251  B    C  
ATOM   5133  CD1 LEU B 226       9.921  -1.098 446.177  1.00 42.30      B    C  
ANISOU 5133  CD1 LEU B 226     6783   2261   7027   -219   2042   -273  B    C  
ATOM   5134  CD2 LEU B 226       8.980   0.761 444.827  1.00 42.25      B    C  
ANISOU 5134  CD2 LEU B 226     7090   2265   6697   -451   1955   -209  B    C  
ATOM   5135  N   HIS B 227       8.964  -1.669 440.484  1.00 50.21      B    N  
ANISOU 5135  N   HIS B 227     9243   2853   6980   -760   2564   -487  B    N  
ATOM   5136  CA  HIS B 227       9.294  -2.452 439.310  1.00 53.06      B    C  
ANISOU 5136  CA  HIS B 227     9934   3076   7150   -835   2830   -600  B    C  
ATOM   5137  C   HIS B 227      10.799  -2.676 439.291  1.00 68.97      B    C  
ANISOU 5137  C   HIS B 227    11826   5019   9359   -758   3253   -710  B    C  
ATOM   5138  O   HIS B 227      11.567  -1.819 439.733  1.00 70.28      B    O  
ANISOU 5138  O   HIS B 227    11765   5226   9711   -729   3380   -699  B    O  
ATOM   5139  CB  HIS B 227       8.850  -1.728 438.041  1.00 54.59      B    C  
ANISOU 5139  CB  HIS B 227    10524   3220   6999  -1024   2845   -589  B    C  
ATOM   5140  CG  HIS B 227       7.365  -1.676 437.855  1.00 60.66      B    C  
ANISOU 5140  CG  HIS B 227    11448   4027   7572  -1105   2448   -502  B    C  
ATOM   5141  CD2 HIS B 227       6.438  -0.812 438.332  1.00 68.81      B    C  
ANISOU 5141  CD2 HIS B 227    12365   5159   8621  -1112   2108   -381  B    C  
ATOM   5142  ND1 HIS B 227       6.671  -2.600 437.104  1.00 70.19      B    N  
ANISOU 5142  ND1 HIS B 227    12956   5156   8555  -1192   2377   -548  B    N  
ATOM   5143  CE1 HIS B 227       5.385  -2.302 437.117  1.00 65.63      B    C  
ANISOU 5143  CE1 HIS B 227    12433   4630   7872  -1258   2009   -458  B    C  
ATOM   5144  NE2 HIS B 227       5.217  -1.222 437.855  1.00 65.20      B    N  
ANISOU 5144  NE2 HIS B 227    12125   4680   7967  -1203   1848   -357  B    N  
ATOM   5145  N   MET B 228      11.222  -3.847 438.838  1.00 65.37      B    N  
ANISOU 5145  N   MET B 228    11494   4453   8891   -719   3465   -821  B    N  
ATOM   5146  CA  MET B 228      12.650  -4.091 438.717  1.00 61.75      B    C  
ANISOU 5146  CA  MET B 228    10911   3915   8634   -641   3888   -940  B    C  
ATOM   5147  C   MET B 228      13.192  -3.384 437.489  1.00 61.70      B    C  
ANISOU 5147  C   MET B 228    11193   3822   8429   -816   4252  -1014  B    C  
ATOM   5148  O   MET B 228      12.657  -3.534 436.386  1.00 78.35      B    O  
ANISOU 5148  O   MET B 228    13726   5856  10189   -967   4281  -1037  B    O  
ATOM   5149  CB  MET B 228      12.979  -5.572 438.633  1.00 60.99      B    C  
ANISOU 5149  CB  MET B 228    10843   3726   8604   -522   3997  -1037  B    C  
ATOM   5150  CG  MET B 228      14.460  -5.765 438.445  1.00 73.09      B    C  
ANISOU 5150  CG  MET B 228    12217   5188  10365   -433   4428  -1167  B    C  
ATOM   5151  SD  MET B 228      15.041  -7.422 438.764  1.00 80.78      B    S  
ANISOU 5151  SD  MET B 228    13070   6084  11540   -207   4482  -1260  B    S  
ATOM   5152  CE  MET B 228      14.302  -7.692 440.378  1.00 71.81      B    C  
ANISOU 5152  CE  MET B 228    11637   5064  10583    -59   3986  -1113  B    C  
ATOM   5153  N   ILE B 229      14.240  -2.594 437.688  1.00 62.29      B    N  
ANISOU 5153  N   ILE B 229    11049   3901   8716   -814   4526  -1050  B    N  
ATOM   5154  CA  ILE B 229      14.838  -1.846 436.596  1.00 64.93      B    C  
ANISOU 5154  CA  ILE B 229    11645   4145   8879  -1005   4912  -1122  B    C  
ATOM   5155  C   ILE B 229      16.058  -2.600 436.084  1.00 81.52      B    C  
ANISOU 5155  C   ILE B 229    13711   6139  11123   -964   5390  -1294  B    C  
ATOM   5156  O   ILE B 229      16.031  -3.182 434.991  1.00 82.17      B    O  
ANISOU 5156  O   ILE B 229    14163   6115  10944  -1060   5589  -1372  B    O  
ATOM   5157  CB  ILE B 229      15.198  -0.425 437.057  1.00 63.75      B    C  
ANISOU 5157  CB  ILE B 229    11295   4061   8866  -1069   4924  -1059  B    C  
ATOM   5158  CG1 ILE B 229      13.936   0.307 437.533  1.00 60.51      B    C  
ANISOU 5158  CG1 ILE B 229    10905   3782   8306  -1089   4402   -879  B    C  
ATOM   5159  CG2 ILE B 229      15.882   0.324 435.964  1.00 66.79      B    C  
ANISOU 5159  CG2 ILE B 229    11957   4339   9081  -1287   5353  -1140  B    C  
ATOM   5160  CD1 ILE B 229      12.904   0.538 436.444  1.00 61.21      B    C  
ANISOU 5160  CD1 ILE B 229    11480   3840   7937  -1256   4238   -825  B    C  
ATOM   5161  N   HIS B 230      17.098  -2.676 436.907  1.00 80.00      B    N  
ANISOU 5161  N   HIS B 230    13050   5991  11356   -803   5527  -1348  B    N  
ATOM   5162  CA  HIS B 230      18.283  -3.465 436.616  1.00 72.11      B    C  
ANISOU 5162  CA  HIS B 230    11888   4944  10566   -706   5882  -1498  B    C  
ATOM   5163  C   HIS B 230      18.239  -4.688 437.511  1.00 74.08      B    C  
ANISOU 5163  C   HIS B 230    11876   5233  11038   -438   5624  -1487  B    C  
ATOM   5164  O   HIS B 230      17.428  -4.768 438.435  1.00 76.08      B    O  
ANISOU 5164  O   HIS B 230    12028   5557  11320   -351   5221  -1366  B    O  
ATOM   5165  CB  HIS B 230      19.574  -2.672 436.868  1.00 80.42      B    C  
ANISOU 5165  CB  HIS B 230    12561   6047  11948   -716   6181  -1571  B    C  
ATOM   5166  CG  HIS B 230      19.853  -1.607 435.848  1.00 84.24      B    C  
ANISOU 5166  CG  HIS B 230    13324   6465  12218   -999   6523  -1613  B    C  
ATOM   5167  CD2 HIS B 230      19.145  -0.512 435.479  1.00 84.82      B    C  
ANISOU 5167  CD2 HIS B 230    13736   6496  11995  -1219   6481  -1532  B    C  
ATOM   5168  ND1 HIS B 230      20.990  -1.604 435.071  1.00 85.16      B    N  
ANISOU 5168  ND1 HIS B 230    13402   6551  12403  -1084   6939  -1750  B    N  
ATOM   5169  CE1 HIS B 230      20.969  -0.556 434.266  1.00 87.96      B    C  
ANISOU 5169  CE1 HIS B 230    14072   6842  12506  -1361   7143  -1746  B    C  
ATOM   5170  NE2 HIS B 230      19.859   0.123 434.492  1.00 77.67      B    N  
ANISOU 5170  NE2 HIS B 230    13022   5521  10970  -1447   6887  -1615  B    N  
ATOM   5171  N   LYS B 231      19.061  -5.659 437.211  1.00 74.36      B    N  
ANISOU 5171  N   LYS B 231    11833   5218  11203   -315   5840  -1610  B    N  
ATOM   5172  CA  LYS B 231      18.852  -6.787 438.108  1.00 73.30      B    C  
ANISOU 5172  CA  LYS B 231    11519   5103  11230    -71   5539  -1578  B    C  
ATOM   5173  C   LYS B 231      19.767  -6.652 439.319  1.00 89.50      B    C  
ANISOU 5173  C   LYS B 231    13017   7268  13719    135   5458  -1569  B    C  
ATOM   5174  O   LYS B 231      20.959  -6.364 439.153  1.00 96.70      B    O  
ANISOU 5174  O   LYS B 231    13672   8213  14858    160   5744  -1671  B    O  
ATOM   5175  CB  LYS B 231      19.098  -8.117 437.421  1.00 78.55      B    C  
ANISOU 5175  CB  LYS B 231    12379   5648  11820     18   5685  -1697  B    C  
ATOM   5176  CG  LYS B 231      18.341  -9.230 438.110  1.00 81.79      B    C  
ANISOU 5176  CG  LYS B 231    12825   6032  12218    175   5316  -1634  B    C  
ATOM   5177  CD  LYS B 231      18.913 -10.608 437.864  1.00 91.65      B    C  
ANISOU 5177  CD  LYS B 231    14102   7172  13551    360   5429  -1758  B    C  
ATOM   5178  CE  LYS B 231      18.175 -11.620 438.749  1.00 92.37      B    C  
ANISOU 5178  CE  LYS B 231    14200   7234  13662    510   5032  -1679  B    C  
ATOM   5179  NZ  LYS B 231      18.894 -12.928 438.905  1.00 98.95      B    N1+
ANISOU 5179  NZ  LYS B 231    14953   7968  14677    762   5077  -1786  B    N1+
ATOM   5180  N   PRO B 232      19.245  -6.803 440.536  1.00 73.52      B    N  
ANISOU 5180  N   PRO B 232    10802   5320  11812    266   5060  -1447  B    N  
ATOM   5181  CA  PRO B 232      20.094  -6.759 441.730  1.00 71.43      B    C  
ANISOU 5181  CA  PRO B 232    10043   5164  11935    467   4935  -1430  B    C  
ATOM   5182  C   PRO B 232      20.699  -8.114 442.059  1.00 71.95      B    C  
ANISOU 5182  C   PRO B 232     9978   5189  12170    726   4888  -1499  B    C  
ATOM   5183  O   PRO B 232      20.142  -9.171 441.762  1.00 72.46      B    O  
ANISOU 5183  O   PRO B 232    10322   5145  12062    776   4812  -1512  B    O  
ATOM   5184  CB  PRO B 232      19.118  -6.307 442.826  1.00 65.30      B    C  
ANISOU 5184  CB  PRO B 232     9207   4474  11132    463   4518  -1260  B    C  
ATOM   5185  CG  PRO B 232      17.811  -6.855 442.379  1.00 63.94      B    C  
ANISOU 5185  CG  PRO B 232     9454   4227  10614    373   4352  -1206  B    C  
ATOM   5186  CD  PRO B 232      17.812  -6.814 440.881  1.00 66.30      B    C  
ANISOU 5186  CD  PRO B 232    10115   4417  10658    199   4690  -1309  B    C  
ATOM   5187  N   GLN B 233      21.875  -8.055 442.687  1.00 73.66      B    N  
ANISOU 5187  N   GLN B 233     9764   5493  12731    893   4920  -1547  B    N  
ATOM   5188  CA  GLN B 233      22.556  -9.253 443.146  1.00 76.15      B    C  
ANISOU 5188  CA  GLN B 233     9912   5782  13239   1175   4837  -1608  B    C  
ATOM   5189  C   GLN B 233      21.763 -10.019 444.190  1.00 80.06      B    C  
ANISOU 5189  C   GLN B 233    10471   6255  13692   1315   4412  -1484  B    C  
ATOM   5190  O   GLN B 233      22.015 -11.213 444.390  1.00 94.77      B    O  
ANISOU 5190  O   GLN B 233    12363   8035  15613   1528   4331  -1529  B    O  
ATOM   5191  CB  GLN B 233      23.911  -8.887 443.739  1.00 78.29      B    C  
ANISOU 5191  CB  GLN B 233     9683   6184  13881   1316   4885  -1666  B    C  
ATOM   5192  CG  GLN B 233      24.569  -7.700 443.081  1.00100.19      B    C  
ANISOU 5192  CG  GLN B 233    12313   9032  16723   1115   5218  -1739  B    C  
ATOM   5193  CD  GLN B 233      25.989  -7.501 443.566  1.00103.33      B    C  
ANISOU 5193  CD  GLN B 233    12207   9563  17490   1257   5274  -1823  B    C  
ATOM   5194  NE2 GLN B 233      26.242  -6.368 444.218  1.00 80.99      B    N  
ANISOU 5194  NE2 GLN B 233     9090   6869  14814   1161   5177  -1763  B    N  
ATOM   5195  OE1 GLN B 233      26.853  -8.361 443.354  1.00114.82      B    O  
ANISOU 5195  OE1 GLN B 233    13533  11003  19091   1455   5394  -1948  B    O  
ATOM   5196  N   ASN B 234      20.838  -9.363 444.880  1.00 70.84      B    N  
ANISOU 5196  N   ASN B 234     9331   5157  12428   1205   4140  -1332  B    N  
ATOM   5197  CA  ASN B 234      19.989 -10.020 445.865  1.00 67.48      B    C  
ANISOU 5197  CA  ASN B 234     8992   4718  11930   1294   3746  -1208  B    C  
ATOM   5198  C   ASN B 234      18.549  -9.638 445.565  1.00 73.20      B    C  
ANISOU 5198  C   ASN B 234    10041   5431  12341   1066   3629  -1112  B    C  
ATOM   5199  O   ASN B 234      18.210  -8.449 445.568  1.00 82.96      B    O  
ANISOU 5199  O   ASN B 234    11233   6758  13529    902   3629  -1052  B    O  
ATOM   5200  CB  ASN B 234      20.394  -9.612 447.285  1.00 77.64      B    C  
ANISOU 5200  CB  ASN B 234     9913   6140  13447   1421   3474  -1115  B    C  
ATOM   5201  CG  ASN B 234      19.364 -10.003 448.325  1.00 87.77      B    C  
ANISOU 5201  CG  ASN B 234    11315   7428  14606   1444   3080   -967  B    C  
ATOM   5202  ND2 ASN B 234      18.654  -9.001 448.879  1.00 90.72      B    N  
ANISOU 5202  ND2 ASN B 234    11646   7914  14910   1299   2911   -849  B    N  
ATOM   5203  OD1 ASN B 234      19.193 -11.186 448.621  1.00 64.37      B    O  
ANISOU 5203  OD1 ASN B 234     8492   4361  11605   1585   2937   -964  B    O  
ATOM   5204  N   THR B 235      17.700 -10.635 445.343  1.00 64.21      B    N  
ANISOU 5204  N   THR B 235     9219   4182  10997   1057   3507  -1100  B    N  
ATOM   5205  CA  THR B 235      16.333 -10.404 444.896  1.00 61.90      B    C  
ANISOU 5205  CA  THR B 235     9245   3880  10395    836   3396  -1031  B    C  
ATOM   5206  C   THR B 235      15.344 -10.349 446.049  1.00 58.68      B    C  
ANISOU 5206  C   THR B 235     8800   3552   9942    821   3001   -878  B    C  
ATOM   5207  O   THR B 235      14.137 -10.229 445.813  1.00 56.85      B    O  
ANISOU 5207  O   THR B 235     8793   3332   9474    652   2854   -816  B    O  
ATOM   5208  CB  THR B 235      15.914 -11.465 443.881  1.00 80.06      B    C  
ANISOU 5208  CB  THR B 235    11920   6018  12480    790   3498  -1116  B    C  
ATOM   5209  CG2 THR B 235      14.796 -10.933 442.987  1.00 78.26      B    C  
ANISOU 5209  CG2 THR B 235    12012   5795  11929    527   3497  -1088  B    C  
ATOM   5210  OG1 THR B 235      17.033 -11.761 443.046  1.00 92.12      B    O  
ANISOU 5210  OG1 THR B 235    13436   7464  14101    870   3857  -1270  B    O  
ATOM   5211  N   GLU B 236      15.817 -10.482 447.282  1.00 58.25      B    N  
ANISOU 5211  N   GLU B 236     8478   3557  10099    992   2819   -820  B    N  
ATOM   5212  CA  GLU B 236      14.924 -10.371 448.423  1.00 55.41      B    C  
ANISOU 5212  CA  GLU B 236     8089   3279   9686    966   2472   -677  B    C  
ATOM   5213  C   GLU B 236      14.507  -8.913 448.626  1.00 54.78      B    C  
ANISOU 5213  C   GLU B 236     7887   3356   9573    819   2420   -600  B    C  
ATOM   5214  O   GLU B 236      15.284  -7.976 448.389  1.00 52.98      B    O  
ANISOU 5214  O   GLU B 236     7469   3185   9476    808   2604   -640  B    O  
ATOM   5215  CB  GLU B 236      15.608 -10.982 449.649  1.00 56.25      B    C  
ANISOU 5215  CB  GLU B 236     7994   3384   9996   1194   2301   -643  B    C  
ATOM   5216  CG  GLU B 236      15.964 -12.449 449.340  1.00 97.73      B    C  
ANISOU 5216  CG  GLU B 236    13413   8454  15266   1346   2347   -727  B    C  
ATOM   5217  CD  GLU B 236      17.023 -13.049 450.242  1.00 96.64      B    C  
ANISOU 5217  CD  GLU B 236    13070   8290  15360   1619   2256   -739  B    C  
ATOM   5218  OE1 GLU B 236      17.160 -12.569 451.384  1.00 94.30      B    O  
ANISOU 5218  OE1 GLU B 236    12568   8107  15156   1675   2056   -643  B    O  
ATOM   5219  OE2 GLU B 236      17.709 -14.009 449.799  1.00 82.46      B    O1-
ANISOU 5219  OE2 GLU B 236    11331   6356  13644   1782   2377   -847  B    O1-
ATOM   5220  N   ALA B 237      13.262  -8.741 449.080  1.00 51.47      B    N  
ANISOU 5220  N   ALA B 237     7575   2996   8984    703   2167   -495  B    N  
ATOM   5221  CA  ALA B 237      12.631  -7.426 449.157  1.00 47.62      B    C  
ANISOU 5221  CA  ALA B 237     7034   2643   8417    556   2090   -426  B    C  
ATOM   5222  C   ALA B 237      13.407  -6.474 450.058  1.00 63.64      B    C  
ANISOU 5222  C   ALA B 237     8734   4788  10658    632   2068   -390  B    C  
ATOM   5223  O   ALA B 237      13.952  -6.870 451.097  1.00 47.16      B    O  
ANISOU 5223  O   ALA B 237     6467   2721   8729    783   1953   -361  B    O  
ATOM   5224  CB  ALA B 237      11.196  -7.561 449.674  1.00 45.48      B    C  
ANISOU 5224  CB  ALA B 237     6890   2423   7967    453   1800   -325  B    C  
ATOM   5225  N   VAL B 238      13.451  -5.194 449.654  1.00 45.94      B    N  
ANISOU 5225  N   VAL B 238     6430   2613   8410    519   2166   -390  B    N  
ATOM   5226  CA  VAL B 238      14.215  -4.202 450.397  1.00 45.44      B    C  
ANISOU 5226  CA  VAL B 238     6060   2644   8559    563   2165   -370  B    C  
ATOM   5227  C   VAL B 238      13.317  -3.595 451.459  1.00 42.72      B    C  
ANISOU 5227  C   VAL B 238     5662   2427   8140    523   1867   -252  B    C  
ATOM   5228  O   VAL B 238      12.142  -3.325 451.209  1.00 48.38      B    O  
ANISOU 5228  O   VAL B 238     6562   3178   8642    402   1748   -203  B    O  
ATOM   5229  CB  VAL B 238      14.785  -3.131 449.450  1.00 53.09      B    C  
ANISOU 5229  CB  VAL B 238     7003   3594   9574    454   2441   -438  B    C  
ATOM   5230  CG1 VAL B 238      15.636  -2.114 450.218  1.00 46.06      B    C  
ANISOU 5230  CG1 VAL B 238     5779   2783   8939    484   2445   -430  B    C  
ATOM   5231  CG2 VAL B 238      15.602  -3.795 448.347  1.00 49.24      B    C  
ANISOU 5231  CG2 VAL B 238     6601   2977   9130    479   2773   -569  B    C  
ATOM   5232  N   ASN B 239      13.872  -3.367 452.645  1.00 50.80      B    N  
ANISOU 5232  N   ASN B 239     6435   3527   9342    624   1744   -214  B    N  
ATOM   5233  CA  ASN B 239      13.117  -2.766 453.741  1.00 49.93      B    C  
ANISOU 5233  CA  ASN B 239     6269   3536   9165    592   1488   -114  B    C  
ATOM   5234  C   ASN B 239      12.881  -1.272 453.500  1.00 59.93      B    C  
ANISOU 5234  C   ASN B 239     7489   4874  10407    468   1510   -102  B    C  
ATOM   5235  O   ASN B 239      13.824  -0.509 453.251  1.00 61.36      B    O  
ANISOU 5235  O   ASN B 239     7508   5042  10764    457   1668   -152  B    O  
ATOM   5236  CB  ASN B 239      13.871  -2.965 455.052  1.00 40.61      B    C  
ANISOU 5236  CB  ASN B 239     4861   2402   8167    734   1353    -85  B    C  
ATOM   5237  CG  ASN B 239      13.033  -2.641 456.241  1.00 50.65      B    C  
ANISOU 5237  CG  ASN B 239     6133   3776   9337    711   1103     11  B    C  
ATOM   5238  ND2 ASN B 239      13.288  -3.325 457.345  1.00 39.18      B    N  
ANISOU 5238  ND2 ASN B 239     4629   2327   7931    829    950     54  B    N  
ATOM   5239  OD1 ASN B 239      12.178  -1.752 456.189  1.00 62.62      B    O  
ANISOU 5239  OD1 ASN B 239     7699   5363  10730    594   1050     45  B    O  
ATOM   5240  N   LEU B 240      11.628  -0.835 453.608  1.00 36.92      B    N  
ANISOU 5240  N   LEU B 240     4711   2029   7290    374   1349    -38  B    N  
ATOM   5241  CA  LEU B 240      11.308   0.557 453.321  1.00 40.91      B    C  
ANISOU 5241  CA  LEU B 240     5216   2588   7739    268   1344    -24  B    C  
ATOM   5242  C   LEU B 240      10.918   1.357 454.546  1.00 34.88      B    C  
ANISOU 5242  C   LEU B 240     4319   1943   6990    279   1140     40  B    C  
ATOM   5243  O   LEU B 240      10.547   2.525 454.402  1.00 49.59      B    O  
ANISOU 5243  O   LEU B 240     6200   3849   8792    203   1103     56  B    O  
ATOM   5244  CB  LEU B 240      10.169   0.660 452.308  1.00 35.39      B    C  
ANISOU 5244  CB  LEU B 240     4784   1870   6792    150   1316    -12  B    C  
ATOM   5245  CG  LEU B 240      10.130  -0.256 451.104  1.00 36.82      B    C  
ANISOU 5245  CG  LEU B 240     5180   1936   6875    114   1460    -67  B    C  
ATOM   5246  CD1 LEU B 240       8.861  -0.008 450.326  1.00 44.82      B    C  
ANISOU 5246  CD1 LEU B 240     6431   2948   7650    -10   1347    -38  B    C  
ATOM   5247  CD2 LEU B 240      11.333   0.070 450.269  1.00 38.65      B    C  
ANISOU 5247  CD2 LEU B 240     5381   2083   7221    101   1752   -148  B    C  
ATOM   5248  N   SER B 241      11.046   0.797 455.744  1.00 34.09      B    N  
ANISOU 5248  N   SER B 241     4105   1885   6964    373   1011     74  B    N  
ATOM   5249  CA  SER B 241      10.334   1.382 456.880  1.00 48.08      B    C  
ANISOU 5249  CA  SER B 241     5826   3762   8678    367    815    134  B    C  
ATOM   5250  C   SER B 241      10.873   2.742 457.352  1.00 48.84      B    C  
ANISOU 5250  C   SER B 241     5753   3908   8895    350    794    127  B    C  
ATOM   5251  O   SER B 241      10.199   3.388 458.162  1.00 58.06      B    O  
ANISOU 5251  O   SER B 241     6909   5156   9995    335    650    164  B    O  
ATOM   5252  CB  SER B 241      10.286   0.376 458.036  1.00 40.01      B    C  
ANISOU 5252  CB  SER B 241     4780   2754   7670    457    689    177  B    C  
ATOM   5253  OG  SER B 241      11.550  -0.162 458.300  1.00 44.23      B    O  
ANISOU 5253  OG  SER B 241     5178   3237   8390    564    734    149  B    O  
ATOM   5254  N   SER B 242      12.044   3.198 456.884  1.00 33.57      B    N  
ANISOU 5254  N   SER B 242     3690   1916   7149    346    944     72  B    N  
ATOM   5255  CA  SER B 242      12.602   4.465 457.352  1.00 42.20      B    C  
ANISOU 5255  CA  SER B 242     4622   3028   8382    314    921     58  B    C  
ATOM   5256  C   SER B 242      11.964   5.710 456.721  1.00 49.46      B    C  
ANISOU 5256  C   SER B 242     5674   3956   9162    200    936     63  B    C  
ATOM   5257  O   SER B 242      12.081   6.807 457.289  1.00 48.93      B    O  
ANISOU 5257  O   SER B 242     5529   3914   9150    170    860     65  B    O  
ATOM   5258  CB  SER B 242      14.118   4.507 457.120  1.00 40.97      B    C  
ANISOU 5258  CB  SER B 242     4251   2790   8525    339   1088    -14  B    C  
ATOM   5259  OG  SER B 242      14.813   3.978 458.236  1.00 47.14      B    O  
ANISOU 5259  OG  SER B 242     4835   3603   9473    454    960    -11  B    O  
ATOM   5260  N   GLY B 243      11.327   5.591 455.564  1.00 35.41      B    N  
ANISOU 5260  N   GLY B 243     4109   2144   7201    137   1013     65  B    N  
ATOM   5261  CA  GLY B 243      10.725   6.727 454.912  1.00 39.11      B    C  
ANISOU 5261  CA  GLY B 243     4734   2609   7516     41    996     79  B    C  
ATOM   5262  C   GLY B 243       9.285   6.930 455.321  1.00 37.63      B    C  
ANISOU 5262  C   GLY B 243     4659   2501   7138     53    790    132  B    C  
ATOM   5263  O   GLY B 243       8.822   6.426 456.344  1.00 48.56      B    O  
ANISOU 5263  O   GLY B 243     5968   3958   8527    119    668    156  B    O  
ATOM   5264  N   VAL B 244       8.564   7.681 454.497  1.00 32.49      B    N  
ANISOU 5264  N   VAL B 244     4195   1823   6327    -16    758    149  B    N  
ATOM   5265  CA  VAL B 244       7.139   7.888 454.692  1.00 40.14      B    C  
ANISOU 5265  CA  VAL B 244     5263   2839   7149     -3    584    189  B    C  
ATOM   5266  C   VAL B 244       6.306   7.242 453.593  1.00 34.56      B    C  
ANISOU 5266  C   VAL B 244     4761   2078   6294    -50    574    204  B    C  
ATOM   5267  O   VAL B 244       5.098   7.048 453.792  1.00 37.83      B    O  
ANISOU 5267  O   VAL B 244     5219   2521   6634    -35    444    232  B    O  
ATOM   5268  CB  VAL B 244       6.792   9.388 454.791  1.00 29.50      B    C  
ANISOU 5268  CB  VAL B 244     3964   1484   5759    -21    497    203  B    C  
ATOM   5269  CG1 VAL B 244       7.453  10.018 455.987  1.00 31.74      B    C  
ANISOU 5269  CG1 VAL B 244     4061   1816   6184     17    475    184  B    C  
ATOM   5270  CG2 VAL B 244       7.206  10.071 453.528  1.00 30.69      B    C  
ANISOU 5270  CG2 VAL B 244     4291   1528   5842   -117    585    202  B    C  
ATOM   5271  N   LEU B 245       6.906   6.870 452.465  1.00 34.68      B    N  
ANISOU 5271  N   LEU B 245     4891   2006   6280   -112    717    180  B    N  
ATOM   5272  CA  LEU B 245       6.121   6.441 451.318  1.00 42.85      B    C  
ANISOU 5272  CA  LEU B 245     6154   2967   7161   -178    687    193  B    C  
ATOM   5273  C   LEU B 245       5.652   5.001 451.410  1.00 42.68      B    C  
ANISOU 5273  C   LEU B 245     6143   2950   7122   -159    669    185  B    C  
ATOM   5274  O   LEU B 245       4.736   4.643 450.660  1.00 55.19      B    O  
ANISOU 5274  O   LEU B 245     7899   4478   8591   -220    590    201  B    O  
ATOM   5275  CB  LEU B 245       6.900   6.641 450.003  1.00 33.26      B    C  
ANISOU 5275  CB  LEU B 245     5094   1647   5897   -269    867    166  B    C  
ATOM   5276  CG  LEU B 245       7.155   8.095 449.544  1.00 33.93      B    C  
ANISOU 5276  CG  LEU B 245     5267   1684   5939   -337    875    188  B    C  
ATOM   5277  CD1 LEU B 245       7.791   8.211 448.153  1.00 38.42      B    C  
ANISOU 5277  CD1 LEU B 245     6036   2145   6415   -451   1078    166  B    C  
ATOM   5278  CD2 LEU B 245       5.915   8.958 449.598  1.00 33.36      B    C  
ANISOU 5278  CD2 LEU B 245     5297   1604   5773   -331    629    251  B    C  
ATOM   5279  N   ARG B 246       6.206   4.203 452.331  1.00 41.72      B    N  
ANISOU 5279  N   ARG B 246     5854   2879   7119    -82    718    168  B    N  
ATOM   5280  CA  ARG B 246       5.863   2.783 452.429  1.00 42.60      B    C  
ANISOU 5280  CA  ARG B 246     6002   2971   7211    -68    708    163  B    C  
ATOM   5281  C   ARG B 246       4.349   2.552 452.401  1.00 46.52      B    C  
ANISOU 5281  C   ARG B 246     6603   3474   7599   -121    544    201  B    C  
ATOM   5282  O   ARG B 246       3.580   3.257 453.070  1.00 45.90      B    O  
ANISOU 5282  O   ARG B 246     6450   3463   7528   -106    428    236  B    O  
ATOM   5283  CB  ARG B 246       6.457   2.194 453.710  1.00 40.28      B    C  
ANISOU 5283  CB  ARG B 246     5515   2735   7055     31    715    165  B    C  
ATOM   5284  CG  ARG B 246       5.993   0.804 454.020  1.00 31.05      B    C  
ANISOU 5284  CG  ARG B 246     4401   1540   5857     45    676    176  B    C  
ATOM   5285  CD  ARG B 246       6.620   0.260 455.287  1.00 30.97      B    C  
ANISOU 5285  CD  ARG B 246     4234   1565   5970    146    662    191  B    C  
ATOM   5286  NE  ARG B 246       6.444   1.123 456.448  1.00 39.91      B    N  
ANISOU 5286  NE  ARG B 246     5212   2800   7150    177    562    227  B    N  
ATOM   5287  CZ  ARG B 246       5.411   1.052 457.288  1.00 45.84      B    C  
ANISOU 5287  CZ  ARG B 246     5956   3606   7854    164    447    271  B    C  
ATOM   5288  NH1 ARG B 246       4.451   0.157 457.094  1.00 29.30      B    N1+
ANISOU 5288  NH1 ARG B 246     3987   1471   5675    106    414    291  B    N1+
ATOM   5289  NH2 ARG B 246       5.339   1.871 458.332  1.00 43.69      B    N  
ANISOU 5289  NH2 ARG B 246     5553   3417   7633    197    374    292  B    N  
ATOM   5290  N   ALA B 247       3.936   1.540 451.629  1.00 34.13      B    N  
ANISOU 5290  N   ALA B 247     5194   1821   5952   -186    549    188  B    N  
ATOM   5291  CA  ALA B 247       2.528   1.249 451.405  1.00 31.64      B    C  
ANISOU 5291  CA  ALA B 247     4985   1478   5559   -269    406    219  B    C  
ATOM   5292  C   ALA B 247       1.860   0.741 452.680  1.00 30.83      B    C  
ANISOU 5292  C   ALA B 247     4751   1448   5515   -241    338    250  B    C  
ATOM   5293  O   ALA B 247       2.513   0.289 453.617  1.00 53.10      B    O  
ANISOU 5293  O   ALA B 247     7451   4315   8409   -163    389    250  B    O  
ATOM   5294  CB  ALA B 247       2.366   0.218 450.299  1.00 33.02      B    C  
ANISOU 5294  CB  ALA B 247     5352   1537   5656   -358    433    189  B    C  
ATOM   5295  N   VAL B 248       0.538   0.872 452.722  1.00 31.74      B    N  
ANISOU 5295  N   VAL B 248     4878   1565   5619   -310    227    280  B    N  
ATOM   5296  CA  VAL B 248      -0.272   0.514 453.882  1.00 30.31      B    C  
ANISOU 5296  CA  VAL B 248     4546   1450   5523   -312    173    314  B    C  
ATOM   5297  C   VAL B 248      -0.940  -0.833 453.649  1.00 40.36      B    C  
ANISOU 5297  C   VAL B 248     5936   2645   6755   -434    159    315  B    C  
ATOM   5298  O   VAL B 248      -1.516  -1.071 452.579  1.00 46.08      B    O  
ANISOU 5298  O   VAL B 248     6821   3279   7408   -549    116    299  B    O  
ATOM   5299  CB  VAL B 248      -1.341   1.584 454.155  1.00 30.00      B    C  
ANISOU 5299  CB  VAL B 248     4368   1461   5569   -309     52    343  B    C  
ATOM   5300  CG1 VAL B 248      -2.115   1.252 455.422  1.00 29.75      B    C  
ANISOU 5300  CG1 VAL B 248     4150   1494   5659   -317      6    376  B    C  
ATOM   5301  CG2 VAL B 248      -0.726   2.967 454.213  1.00 29.35      B    C  
ANISOU 5301  CG2 VAL B 248     4228   1425   5498   -204     57    337  B    C  
ATOM   5302  N   SER B 249      -0.924  -1.687 454.672  1.00 35.41      B    N  
ANISOU 5302  N   SER B 249     5245   2040   6168   -426    183    337  B    N  
ATOM   5303  CA  SER B 249      -1.658  -2.938 454.639  1.00 32.25      B    C  
ANISOU 5303  CA  SER B 249     4952   1569   5735   -563    165    346  B    C  
ATOM   5304  C   SER B 249      -3.112  -2.675 454.309  1.00 37.71      B    C  
ANISOU 5304  C   SER B 249     5587   2265   6475   -712     57    357  B    C  
ATOM   5305  O   SER B 249      -3.769  -1.928 455.045  1.00 39.90      B    O  
ANISOU 5305  O   SER B 249     5647   2634   6880   -696    -16    391  B    O  
ATOM   5306  CB  SER B 249      -1.582  -3.629 455.996  1.00 39.30      B    C  
ANISOU 5306  CB  SER B 249     5766   2490   6677   -538    191    389  B    C  
ATOM   5307  OG  SER B 249      -2.590  -4.623 456.137  1.00 42.33      B    O  
ANISOU 5307  OG  SER B 249     6216   2822   7045   -710    164    412  B    O  
ATOM   5308  N   PRO B 250      -3.664  -3.274 453.252  1.00 39.08      B    N  
ANISOU 5308  N   PRO B 250     5934   2342   6573   -863     18    327  B    N  
ATOM   5309  CA  PRO B 250      -5.084  -3.049 452.946  1.00 35.05      B    C  
ANISOU 5309  CA  PRO B 250     5325   1858   6133  -1022   -166    339  B    C  
ATOM   5310  C   PRO B 250      -6.003  -3.389 454.095  1.00 35.31      B    C  
ANISOU 5310  C   PRO B 250     5147   2021   6247  -1103   -203    371  B    C  
ATOM   5311  O   PRO B 250      -7.106  -2.847 454.155  1.00 35.88      B    O  
ANISOU 5311  O   PRO B 250     5028   2266   6338  -1150   -337    363  B    O  
ATOM   5312  CB  PRO B 250      -5.328  -3.948 451.734  1.00 36.66      B    C  
ANISOU 5312  CB  PRO B 250     5783   1950   6197  -1179   -183    287  B    C  
ATOM   5313  CG  PRO B 250      -4.012  -4.052 451.091  1.00 36.37      B    C  
ANISOU 5313  CG  PRO B 250     5903   1811   6105  -1047     12    244  B    C  
ATOM   5314  CD  PRO B 250      -3.013  -4.096 452.224  1.00 36.27      B    C  
ANISOU 5314  CD  PRO B 250     5863   1850   6069   -901     66    284  B    C  
ATOM   5315  N   LEU B 251      -5.590  -4.264 455.013  1.00 35.18      B    N  
ANISOU 5315  N   LEU B 251     5162   1954   6249  -1108    -81    401  B    N  
ATOM   5316  CA  LEU B 251      -6.357  -4.460 456.238  1.00 41.70      B    C  
ANISOU 5316  CA  LEU B 251     5798   2907   7139  -1180    -81    441  B    C  
ATOM   5317  C   LEU B 251      -6.588  -3.140 456.953  1.00 42.49      B    C  
ANISOU 5317  C   LEU B 251     5633   3202   7309  -1037   -116    446  B    C  
ATOM   5318  O   LEU B 251      -7.707  -2.829 457.366  1.00 46.63      B    O  
ANISOU 5318  O   LEU B 251     5945   3909   7863  -1104   -177    434  B    O  
ATOM   5319  CB  LEU B 251      -5.637  -5.432 457.167  1.00 44.91      B    C  
ANISOU 5319  CB  LEU B 251     6325   3225   7514  -1155     51    484  B    C  
ATOM   5320  CG  LEU B 251      -5.480  -6.878 456.692  1.00 50.97      B    C  
ANISOU 5320  CG  LEU B 251     7376   3852   8138  -1270    101    464  B    C  
ATOM   5321  CD1 LEU B 251      -5.137  -7.709 457.886  1.00 49.46      B    C  
ANISOU 5321  CD1 LEU B 251     7253   3626   7914  -1260    170    526  B    C  
ATOM   5322  CD2 LEU B 251      -6.722  -7.415 455.977  1.00 38.52      B    C  
ANISOU 5322  CD2 LEU B 251     5816   2265   6553  -1531     28    430  B    C  
ATOM   5323  N   HIS B 252      -5.529  -2.359 457.127  1.00 46.54      B    N  
ANISOU 5323  N   HIS B 252     6149   3675   7859   -841    -69    453  B    N  
ATOM   5324  CA  HIS B 252      -5.639  -1.094 457.842  1.00 44.67      B    C  
ANISOU 5324  CA  HIS B 252     5698   3590   7682   -700    -96    450  B    C  
ATOM   5325  C   HIS B 252      -6.302  -0.003 456.997  1.00 47.40      B    C  
ANISOU 5325  C   HIS B 252     5954   4024   8031   -661   -232    410  B    C  
ATOM   5326  O   HIS B 252      -6.989   0.871 457.546  1.00 32.48      B    O  
ANISOU 5326  O   HIS B 252     3854   2294   6195   -594   -287    393  B    O  
ATOM   5327  CB  HIS B 252      -4.265  -0.628 458.307  1.00 33.89      B    C  
ANISOU 5327  CB  HIS B 252     4372   2147   6359   -526    -15    467  B    C  
ATOM   5328  CG  HIS B 252      -4.320   0.646 459.074  1.00 36.06      B    C  
ANISOU 5328  CG  HIS B 252     4463   2553   6684   -393    -41    456  B    C  
ATOM   5329  CD2 HIS B 252      -3.787   1.864 458.827  1.00 29.27      B    C  
ANISOU 5329  CD2 HIS B 252     3574   1690   5858   -258    -69    434  B    C  
ATOM   5330  ND1 HIS B 252      -5.053   0.768 460.234  1.00 30.41      B    N  
ANISOU 5330  ND1 HIS B 252     3587   1989   5981   -405    -31    459  B    N  
ATOM   5331  CE1 HIS B 252      -4.943   2.004 460.683  1.00 31.36      B    C  
ANISOU 5331  CE1 HIS B 252     3588   2187   6141   -266    -54    432  B    C  
ATOM   5332  NE2 HIS B 252      -4.188   2.689 459.844  1.00 31.56      B    N  
ANISOU 5332  NE2 HIS B 252     3692   2115   6182   -179    -86    419  B    N  
ATOM   5333  N   MET B 253      -6.057   0.014 455.675  1.00 44.40      B    N  
ANISOU 5333  N   MET B 253     5750   3531   7589   -686   -288    394  B    N  
ATOM   5334  CA  MET B 253      -6.842   0.883 454.800  1.00 33.41      B    C  
ANISOU 5334  CA  MET B 253     4312   2208   6175   -674   -457    370  B    C  
ATOM   5335  C   MET B 253      -8.333   0.619 454.999  1.00 46.76      B    C  
ANISOU 5335  C   MET B 253     5803   4069   7896   -792   -574    349  B    C  
ATOM   5336  O   MET B 253      -9.126   1.553 455.139  1.00 55.80      B    O  
ANISOU 5336  O   MET B 253     6741   5357   9102   -710   -690    329  B    O  
ATOM   5337  CB  MET B 253      -6.447   0.692 453.334  1.00 33.95      B    C  
ANISOU 5337  CB  MET B 253     4651   2119   6129   -732   -496    359  B    C  
ATOM   5338  CG  MET B 253      -5.016   1.066 452.979  1.00 71.25      B    C  
ANISOU 5338  CG  MET B 253     9551   6689  10830   -628   -365    366  B    C  
ATOM   5339  SD  MET B 253      -4.601   2.804 453.184  1.00 54.99      B    S  
ANISOU 5339  SD  MET B 253     7398   4671   8825   -436   -396    378  B    S  
ATOM   5340  CE  MET B 253      -3.757   3.232 451.670  1.00 47.58      B    C  
ANISOU 5340  CE  MET B 253     6766   3554   7759   -449   -367    375  B    C  
ATOM   5341  N   GLN B 254      -8.721  -0.658 455.066  1.00 36.81      B    N  
ANISOU 5341  N   GLN B 254     4588   2790   6606   -984   -538    349  B    N  
ATOM   5342  CA  GLN B 254     -10.112  -1.023 455.304  1.00 37.65      B    C  
ANISOU 5342  CA  GLN B 254     4485   3066   6755  -1137   -625    324  B    C  
ATOM   5343  C   GLN B 254     -10.557  -0.613 456.698  1.00 47.50      B    C  
ANISOU 5343  C   GLN B 254     5455   4493   8102  -1073   -541    323  B    C  
ATOM   5344  O   GLN B 254     -11.694  -0.169 456.892  1.00 54.05      B    O  
ANISOU 5344  O   GLN B 254     6015   5514   9008  -1086   -627    283  B    O  
ATOM   5345  CB  GLN B 254     -10.288  -2.531 455.127  1.00 46.09      B    C  
ANISOU 5345  CB  GLN B 254     5709   4042   7762  -1380   -577    328  B    C  
ATOM   5346  CG  GLN B 254     -11.721  -2.955 455.063  1.00 41.04      B    C  
ANISOU 5346  CG  GLN B 254     4876   3560   7156  -1587   -690    292  B    C  
ATOM   5347  CD  GLN B 254     -12.512  -2.089 454.115  1.00 50.15      B    C  
ANISOU 5347  CD  GLN B 254     5904   4822   8328  -1544   -929    250  B    C  
ATOM   5348  NE2 GLN B 254     -13.524  -1.419 454.646  1.00 57.93      B    N  
ANISOU 5348  NE2 GLN B 254     6538   6037   9437  -1499  -1000    220  B    N  
ATOM   5349  OE1 GLN B 254     -12.183  -1.970 452.935  1.00 42.29      B    O  
ANISOU 5349  OE1 GLN B 254     5132   3701   7235  -1533  -1046    245  B    O  
ATOM   5350  N   TYR B 255      -9.683  -0.797 457.685  1.00 52.13      B    N  
ANISOU 5350  N   TYR B 255     6102   5020   8685  -1007   -372    361  B    N  
ATOM   5351  CA  TYR B 255      -9.981  -0.384 459.052  1.00 55.92      B    C  
ANISOU 5351  CA  TYR B 255     6371   5652   9224   -945   -276    358  B    C  
ATOM   5352  C   TYR B 255     -10.320   1.093 459.110  1.00 61.47      B    C  
ANISOU 5352  C   TYR B 255     6874   6482  10001   -749   -359    312  B    C  
ATOM   5353  O   TYR B 255     -11.290   1.488 459.765  1.00 37.10      B    O  
ANISOU 5353  O   TYR B 255     3527   3584   6984   -740   -351    267  B    O  
ATOM   5354  CB  TYR B 255      -8.789  -0.716 459.947  1.00 49.97      B    C  
ANISOU 5354  CB  TYR B 255     5771   4782   8433   -878   -127    411  B    C  
ATOM   5355  CG  TYR B 255      -8.849  -0.200 461.365  1.00 34.54      B    C  
ANISOU 5355  CG  TYR B 255     3669   2954   6501   -794    -30    411  B    C  
ATOM   5356  CD1 TYR B 255      -8.472   1.103 461.648  1.00 33.54      B    C  
ANISOU 5356  CD1 TYR B 255     3457   2871   6416   -585    -52    380  B    C  
ATOM   5357  CD2 TYR B 255      -9.232  -1.011 462.416  1.00 35.54      B    C  
ANISOU 5357  CD2 TYR B 255     3779   3136   6588   -932     90    440  B    C  
ATOM   5358  CE1 TYR B 255      -8.490   1.604 462.931  1.00 33.52      B    C  
ANISOU 5358  CE1 TYR B 255     3351   2972   6415   -508     36    367  B    C  
ATOM   5359  CE2 TYR B 255      -9.246  -0.527 463.715  1.00 35.56      B    C  
ANISOU 5359  CE2 TYR B 255     3686   3247   6579   -860    188    435  B    C  
ATOM   5360  CZ  TYR B 255      -8.876   0.790 463.963  1.00 56.43      B    C  
ANISOU 5360  CZ  TYR B 255     6241   5938   9262   -643    158    392  B    C  
ATOM   5361  OH  TYR B 255      -8.893   1.307 465.246  1.00 57.09      B    O  
ANISOU 5361  OH  TYR B 255     6253   6123   9318   -573    253    374  B    O  
ATOM   5362  N   LEU B 256      -9.506   1.925 458.446  1.00 48.94      B    N  
ANISOU 5362  N   LEU B 256     5412   4781   8402   -589   -424    318  B    N  
ATOM   5363  CA  LEU B 256      -9.772   3.356 458.395  1.00 47.00      B    C  
ANISOU 5363  CA  LEU B 256     5030   4609   8219   -398   -519    280  B    C  
ATOM   5364  C   LEU B 256     -11.057   3.657 457.630  1.00 37.41      B    C  
ANISOU 5364  C   LEU B 256     3651   3510   7052   -421   -707    239  B    C  
ATOM   5365  O   LEU B 256     -11.839   4.514 458.049  1.00 39.25      B    O  
ANISOU 5365  O   LEU B 256     3644   3889   7379   -301   -758    189  B    O  
ATOM   5366  CB  LEU B 256      -8.581   4.084 457.779  1.00 44.06      B    C  
ANISOU 5366  CB  LEU B 256     4867   4065   7809   -266   -538    305  B    C  
ATOM   5367  CG  LEU B 256      -7.301   4.065 458.615  1.00 47.06      B    C  
ANISOU 5367  CG  LEU B 256     5343   4358   8179   -202   -382    331  B    C  
ATOM   5368  CD1 LEU B 256      -6.129   4.696 457.860  1.00 47.18      B    C  
ANISOU 5368  CD1 LEU B 256     5548   4208   8168   -113   -388    348  B    C  
ATOM   5369  CD2 LEU B 256      -7.541   4.793 459.915  1.00 51.43      B    C  
ANISOU 5369  CD2 LEU B 256     5714   5039   8789    -91   -328    298  B    C  
ATOM   5370  N   ARG B 257     -11.314   2.937 456.537  1.00 37.49      B    N  
ANISOU 5370  N   ARG B 257     3781   3459   7003   -572   -816    251  B    N  
ATOM   5371  CA  ARG B 257     -12.593   3.081 455.850  1.00 39.70      B    C  
ANISOU 5371  CA  ARG B 257     3888   3865   7332   -619  -1024    212  B    C  
ATOM   5372  C   ARG B 257     -13.756   2.854 456.807  1.00 41.34      B    C  
ANISOU 5372  C   ARG B 257     3744   4304   7657   -687   -974    159  B    C  
ATOM   5373  O   ARG B 257     -14.656   3.695 456.911  1.00 50.68      B    O  
ANISOU 5373  O   ARG B 257     4656   5643   8957   -564  -1083    104  B    O  
ATOM   5374  CB  ARG B 257     -12.669   2.114 454.671  1.00 40.56      B    C  
ANISOU 5374  CB  ARG B 257     4204   3872   7336   -821  -1130    228  B    C  
ATOM   5375  CG  ARG B 257     -11.884   2.584 453.471  1.00 39.91      B    C  
ANISOU 5375  CG  ARG B 257     4427   3601   7138   -745  -1230    259  B    C  
ATOM   5376  CD  ARG B 257     -12.094   1.709 452.248  1.00 41.23      B    C  
ANISOU 5376  CD  ARG B 257     4808   3676   7182   -943  -1354    258  B    C  
ATOM   5377  NE  ARG B 257     -10.942   1.760 451.348  1.00 49.65      B    N  
ANISOU 5377  NE  ARG B 257     6244   4521   8101   -918  -1310    289  B    N  
ATOM   5378  CZ  ARG B 257     -10.016   0.816 451.280  1.00 41.86      B    C  
ANISOU 5378  CZ  ARG B 257     5491   3379   7035  -1014  -1126    297  B    C  
ATOM   5379  NH1 ARG B 257     -10.129  -0.248 452.049  1.00 54.31      B    N1+
ANISOU 5379  NH1 ARG B 257     6998   4983   8655  -1142   -998    291  B    N1+
ATOM   5380  NH2 ARG B 257      -8.998   0.931 450.444  1.00 38.66      B    N  
ANISOU 5380  NH2 ARG B 257     5391   2789   6510   -984  -1067    311  B    N  
ATOM   5381  N   ASN B 258     -13.737   1.725 457.535  1.00 42.50      B    N  
ANISOU 5381  N   ASN B 258     3899   4471   7779   -880   -797    173  B    N  
ATOM   5382  CA  ASN B 258     -14.786   1.388 458.497  1.00 43.09      B    C  
ANISOU 5382  CA  ASN B 258     3668   4761   7945   -993   -698    126  B    C  
ATOM   5383  C   ASN B 258     -14.895   2.420 459.608  1.00 42.88      B    C  
ANISOU 5383  C   ASN B 258     3432   4862   7999   -787   -587     83  B    C  
ATOM   5384  O   ASN B 258     -15.916   2.465 460.308  1.00 61.54      B    O  
ANISOU 5384  O   ASN B 258     5487   7436  10460   -829   -517     18  B    O  
ATOM   5385  CB  ASN B 258     -14.535   0.022 459.144  1.00 44.71      B    C  
ANISOU 5385  CB  ASN B 258     4005   4911   8071  -1233   -505    170  B    C  
ATOM   5386  CG  ASN B 258     -14.473  -1.105 458.148  1.00 43.54      B    C  
ANISOU 5386  CG  ASN B 258     4079   4624   7841  -1455   -589    198  B    C  
ATOM   5387  ND2 ASN B 258     -14.291  -2.314 458.652  1.00 43.77      B    N  
ANISOU 5387  ND2 ASN B 258     4249   4578   7805  -1663   -438    238  B    N  
ATOM   5388  OD1 ASN B 258     -14.631  -0.907 456.951  1.00 44.02      B    O  
ANISOU 5388  OD1 ASN B 258     4200   4638   7888  -1447   -791    183  B    O  
ATOM   5389  N   PHE B 259     -13.845   3.204 459.825  1.00 40.79      B    N  
ANISOU 5389  N   PHE B 259     3333   4473   7693   -582   -550    109  B    N  
ATOM   5390  CA  PHE B 259     -13.814   4.211 460.867  1.00 40.54      B    C  
ANISOU 5390  CA  PHE B 259     3163   4527   7715   -386   -448     62  B    C  
ATOM   5391  C   PHE B 259     -14.344   5.564 460.377  1.00 52.77      B    C  
ANISOU 5391  C   PHE B 259     4550   6128   9371   -150   -624      2  B    C  
ATOM   5392  O   PHE B 259     -14.514   6.491 461.185  1.00 44.92      B    O  
ANISOU 5392  O   PHE B 259     3414   5214   8441     30   -555    -61  B    O  
ATOM   5393  CB  PHE B 259     -12.377   4.306 461.384  1.00 38.10      B    C  
ANISOU 5393  CB  PHE B 259     3122   4048   7306   -310   -333    119  B    C  
ATOM   5394  CG  PHE B 259     -12.260   4.715 462.822  1.00 49.79      B    C  
ANISOU 5394  CG  PHE B 259     4522   5612   8782   -229   -157     86  B    C  
ATOM   5395  CD1 PHE B 259     -13.385   4.931 463.592  1.00 39.99      B    C  
ANISOU 5395  CD1 PHE B 259     2997   4585   7614   -232    -71      4  B    C  
ATOM   5396  CD2 PHE B 259     -11.000   4.831 463.423  1.00 52.21      B    C  
ANISOU 5396  CD2 PHE B 259     5043   5788   9007   -162    -73    130  B    C  
ATOM   5397  CE1 PHE B 259     -13.269   5.306 464.922  1.00 40.11      B    C  
ANISOU 5397  CE1 PHE B 259     2975   4671   7596   -166    107    -36  B    C  
ATOM   5398  CE2 PHE B 259     -10.869   5.199 464.757  1.00 44.38      B    C  
ANISOU 5398  CE2 PHE B 259     4012   4866   7984    -99     70     97  B    C  
ATOM   5399  CZ  PHE B 259     -12.010   5.445 465.510  1.00 46.69      B    C  
ANISOU 5399  CZ  PHE B 259     4055   5363   8324   -102    167     13  B    C  
ATOM   5400  N   GLY B 260     -14.657   5.681 459.082  1.00 42.19      B    N  
ANISOU 5400  N   GLY B 260     3244   4740   8045   -147   -856     15  B    N  
ATOM   5401  CA  GLY B 260     -15.069   6.944 458.514  1.00 43.19      B    C  
ANISOU 5401  CA  GLY B 260     3280   4873   8256     87  -1058    -22  B    C  
ATOM   5402  C   GLY B 260     -13.932   7.885 458.221  1.00 41.28      B    C  
ANISOU 5402  C   GLY B 260     3317   4423   7943    265  -1088     23  B    C  
ATOM   5403  O   GLY B 260     -14.165   9.077 458.006  1.00 42.05      B    O  
ANISOU 5403  O   GLY B 260     3370   4501   8107    487  -1219     -6  B    O  
ATOM   5404  N   VAL B 261     -12.709   7.376 458.199  1.00 39.06      B    N  
ANISOU 5404  N   VAL B 261     3320   3982   7539    173   -971     90  B    N  
ATOM   5405  CA  VAL B 261     -11.503   8.167 458.042  1.00 37.29      B    C  
ANISOU 5405  CA  VAL B 261     3346   3570   7254    301   -953    128  B    C  
ATOM   5406  C   VAL B 261     -10.985   8.047 456.619  1.00 46.51      B    C  
ANISOU 5406  C   VAL B 261     4787   4564   8320    242  -1086    192  B    C  
ATOM   5407  O   VAL B 261     -10.892   6.946 456.071  1.00 49.29      B    O  
ANISOU 5407  O   VAL B 261     5247   4883   8598     55  -1077    224  B    O  
ATOM   5408  CB  VAL B 261     -10.444   7.733 459.054  1.00 35.40      B    C  
ANISOU 5408  CB  VAL B 261     3204   3283   6963    251   -727    148  B    C  
ATOM   5409  CG1 VAL B 261      -9.252   8.608 458.913  1.00 33.95      B    C  
ANISOU 5409  CG1 VAL B 261     3230   2928   6743    371   -716    173  B    C  
ATOM   5410  CG2 VAL B 261     -11.023   7.818 460.445  1.00 36.05      B    C  
ANISOU 5410  CG2 VAL B 261     3052   3538   7109    288   -594     84  B    C  
ATOM   5411  N   SER B 262     -10.661   9.183 456.011  1.00 44.57      B    N  
ANISOU 5411  N   SER B 262     4681   4197   8059    395  -1203    209  B    N  
ATOM   5412  CA  SER B 262     -10.158   9.205 454.650  1.00 37.05      B    C  
ANISOU 5412  CA  SER B 262     4021   3072   6984    341  -1315    270  B    C  
ATOM   5413  C   SER B 262      -8.658   9.438 454.576  1.00 48.77      B    C  
ANISOU 5413  C   SER B 262     5769   4373   8389    336  -1164    310  B    C  
ATOM   5414  O   SER B 262      -8.030   9.053 453.582  1.00 35.95      B    O  
ANISOU 5414  O   SER B 262     4399   2614   6647    229  -1160    354  B    O  
ATOM   5415  CB  SER B 262     -10.888  10.290 453.852  1.00 38.97      B    C  
ANISOU 5415  CB  SER B 262     4276   3286   7243    494  -1576    274  B    C  
ATOM   5416  OG  SER B 262     -12.192   9.858 453.498  1.00 46.00      B    O  
ANISOU 5416  OG  SER B 262     4964   4328   8188    453  -1761    247  B    O  
ATOM   5417  N   ALA B 263      -8.068  10.035 455.609  1.00 48.40      B    N  
ANISOU 5417  N   ALA B 263     5663   4324   8404    438  -1034    287  B    N  
ATOM   5418  CA  ALA B 263      -6.628  10.205 455.662  1.00 32.55      B    C  
ANISOU 5418  CA  ALA B 263     3849   2168   6349    418   -887    315  B    C  
ATOM   5419  C   ALA B 263      -6.207  10.268 457.121  1.00 31.48      B    C  
ANISOU 5419  C   ALA B 263     3568   2105   6288    469   -736    277  B    C  
ATOM   5420  O   ALA B 263      -6.916  10.826 457.949  1.00 32.08      B    O  
ANISOU 5420  O   ALA B 263     3461   2290   6437    581   -762    225  B    O  
ATOM   5421  CB  ALA B 263      -6.214  11.459 454.894  1.00 33.03      B    C  
ANISOU 5421  CB  ALA B 263     4113   2069   6369    508   -976    341  B    C  
ATOM   5422  N   SER B 264      -5.019   9.761 457.429  1.00 35.35      B    N  
ANISOU 5422  N   SER B 264     4148   2527   6757    397   -585    296  B    N  
ATOM   5423  CA  SER B 264      -4.562   9.776 458.811  1.00 39.72      B    C  
ANISOU 5423  CA  SER B 264     4590   3141   7360    437   -470    267  B    C  
ATOM   5424  C   SER B 264      -3.073  10.075 458.908  1.00 43.77      B    C  
ANISOU 5424  C   SER B 264     5231   3569   7832    423   -372    274  B    C  
ATOM   5425  O   SER B 264      -2.319   9.945 457.947  1.00 54.53      B    O  
ANISOU 5425  O   SER B 264     6753   4882   9085    349   -332    296  B    O  
ATOM   5426  CB  SER B 264      -4.862   8.446 459.511  1.00 29.18      B    C  
ANISOU 5426  CB  SER B 264     3153   1916   6018    335   -386    274  B    C  
ATOM   5427  OG  SER B 264      -4.276   7.370 458.821  1.00 46.18      B    O  
ANISOU 5427  OG  SER B 264     5440   3981   8125    213   -336    319  B    O  
ATOM   5428  N   THR B 265      -2.671  10.529 460.083  1.00 27.99      B    N  
ANISOU 5428  N   THR B 265     3158   1633   5843    478   -321    237  B    N  
ATOM   5429  CA  THR B 265      -1.269  10.618 460.443  1.00 46.95      B    C  
ANISOU 5429  CA  THR B 265     5624   4051   8164    436   -232    230  B    C  
ATOM   5430  C   THR B 265      -1.151  10.279 461.916  1.00 48.47      B    C  
ANISOU 5430  C   THR B 265     5707   4302   8410    463   -194    213  B    C  
ATOM   5431  O   THR B 265      -2.011  10.663 462.709  1.00 41.84      B    O  
ANISOU 5431  O   THR B 265     4767   3491   7639    545   -223    179  B    O  
ATOM   5432  CB  THR B 265      -0.673  12.004 460.161  1.00 41.63      B    C  
ANISOU 5432  CB  THR B 265     5047   3344   7427    468   -251    202  B    C  
ATOM   5433  CG2 THR B 265       0.827  11.991 460.389  1.00 41.35      B    C  
ANISOU 5433  CG2 THR B 265     5045   3309   7357    408   -168    196  B    C  
ATOM   5434  OG1 THR B 265      -0.924  12.363 458.800  1.00 49.85      B    O  
ANISOU 5434  OG1 THR B 265     6222   4306   8411    451   -296    228  B    O  
ATOM   5435  N   SER B 266      -0.102   9.551 462.290  1.00 49.51      B    N  
ANISOU 5435  N   SER B 266     5856   4444   8513    409   -131    233  B    N  
ATOM   5436  CA  SER B 266       0.116   9.331 463.703  1.00 26.54      B    C  
ANISOU 5436  CA  SER B 266     2880   1563   5641    440   -120    226  B    C  
ATOM   5437  C   SER B 266       1.581   9.508 464.038  1.00 26.34      B    C  
ANISOU 5437  C   SER B 266     2881   1537   5590    424   -110    217  B    C  
ATOM   5438  O   SER B 266       2.466   9.247 463.221  1.00 26.16      B    O  
ANISOU 5438  O   SER B 266     2899   1498   5544    376    -74    229  B    O  
ATOM   5439  CB  SER B 266      -0.405   7.966 464.149  1.00 26.67      B    C  
ANISOU 5439  CB  SER B 266     2863   1567   5703    405    -86    280  B    C  
ATOM   5440  OG  SER B 266      -0.072   6.987 463.217  1.00 38.17      B    O  
ANISOU 5440  OG  SER B 266     4389   2997   7117    327    -53    319  B    O  
ATOM   5441  N   ILE B 267       1.808  10.006 465.247  1.00 26.64      B    N  
ANISOU 5441  N   ILE B 267     2886   1582   5654    473   -143    186  B    N  
ATOM   5442  CA  ILE B 267       3.126  10.226 465.812  1.00 35.49      B    C  
ANISOU 5442  CA  ILE B 267     4000   2687   6796    468   -170    172  B    C  
ATOM   5443  C   ILE B 267       3.198   9.401 467.086  1.00 38.09      B    C  
ANISOU 5443  C   ILE B 267     4310   3012   7150    497   -200    204  B    C  
ATOM   5444  O   ILE B 267       2.256   9.420 467.892  1.00 32.49      B    O  
ANISOU 5444  O   ILE B 267     3596   2302   6445    542   -203    198  B    O  
ATOM   5445  CB  ILE B 267       3.361  11.726 466.102  1.00 27.70      B    C  
ANISOU 5445  CB  ILE B 267     3031   1675   5821    496   -214    103  B    C  
ATOM   5446  CG1 ILE B 267       3.169  12.543 464.833  1.00 27.11      B    C  
ANISOU 5446  CG1 ILE B 267     3015   1576   5708    472   -192     91  B    C  
ATOM   5447  CG2 ILE B 267       4.751  11.981 466.671  1.00 27.67      B    C  
ANISOU 5447  CG2 ILE B 267     2996   1632   5884    475   -261     83  B    C  
ATOM   5448  CD1 ILE B 267       2.659  13.933 465.090  1.00 38.92      B    C  
ANISOU 5448  CD1 ILE B 267     4559   3039   7189    530   -236     30  B    C  
ATOM   5449  N   GLY B 268       4.316   8.698 467.278  1.00 27.41      B    N  
ANISOU 5449  N   GLY B 268     2945   1643   5825    484   -223    237  B    N  
ATOM   5450  CA  GLY B 268       4.480   7.919 468.487  1.00 28.06      B    C  
ANISOU 5450  CA  GLY B 268     3045   1698   5920    520   -285    285  B    C  
ATOM   5451  C   GLY B 268       4.927   8.778 469.654  1.00 39.62      B    C  
ANISOU 5451  C   GLY B 268     4507   3157   7388    559   -387    237  B    C  
ATOM   5452  O   GLY B 268       5.767   9.668 469.514  1.00 44.81      B    O  
ANISOU 5452  O   GLY B 268     5120   3777   8130    561   -436    183  B    O  
ATOM   5453  N   ILE B 269       4.375   8.481 470.828  1.00 29.50      B    N  
ANISOU 5453  N   ILE B 269     3297   1953   5960    559   -410    250  B    N  
ATOM   5454  CA  ILE B 269       4.737   9.166 472.066  1.00 30.53      B    C  
ANISOU 5454  CA  ILE B 269     3474   2122   6004    573   -509    197  B    C  
ATOM   5455  C   ILE B 269       5.633   8.228 472.861  1.00 31.53      B    C  
ANISOU 5455  C   ILE B 269     3644   2234   6103    582   -630    271  B    C  
ATOM   5456  O   ILE B 269       5.203   7.156 473.298  1.00 45.34      B    O  
ANISOU 5456  O   ILE B 269     5481   4000   7748    568   -610    352  B    O  
ATOM   5457  CB  ILE B 269       3.507   9.583 472.877  1.00 31.04      B    C  
ANISOU 5457  CB  ILE B 269     3612   2280   5900    568   -440    146  B    C  
ATOM   5458  CG1 ILE B 269       2.559  10.412 472.035  1.00 30.33      B    C  
ANISOU 5458  CG1 ILE B 269     3463   2200   5861    591   -340     79  B    C  
ATOM   5459  CG2 ILE B 269       3.913  10.389 474.072  1.00 39.63      B    C  
ANISOU 5459  CG2 ILE B 269     4779   3392   6886    578   -534     73  B    C  
ATOM   5460  CD1 ILE B 269       1.246  10.654 472.738  1.00 31.09      B    C  
ANISOU 5460  CD1 ILE B 269     3585   2403   5823    602   -244     24  B    C  
ATOM   5461  N   PHE B 270       6.888   8.616 473.023  1.00 32.16      B    N  
ANISOU 5461  N   PHE B 270     3661   2275   6283    602   -763    246  B    N  
ATOM   5462  CA  PHE B 270       7.909   7.769 473.613  1.00 38.44      B    C  
ANISOU 5462  CA  PHE B 270     4457   3045   7104    638   -915    313  B    C  
ATOM   5463  C   PHE B 270       8.323   8.262 474.989  1.00 34.95      B    C  
ANISOU 5463  C   PHE B 270     4099   2647   6534    633  -1089    279  B    C  
ATOM   5464  O   PHE B 270       8.594   9.448 475.174  1.00 35.21      B    O  
ANISOU 5464  O   PHE B 270     4103   2693   6582    605  -1135    179  B    O  
ATOM   5465  CB  PHE B 270       9.131   7.686 472.706  1.00 33.36      B    C  
ANISOU 5465  CB  PHE B 270     3639   2333   6704    668   -947    308  B    C  
ATOM   5466  CG  PHE B 270       8.944   6.782 471.546  1.00 36.58      B    C  
ANISOU 5466  CG  PHE B 270     4010   2680   7208    686   -809    363  B    C  
ATOM   5467  CD1 PHE B 270       9.140   5.415 471.688  1.00 33.07      B    C  
ANISOU 5467  CD1 PHE B 270     3614   2188   6765    742   -842    458  B    C  
ATOM   5468  CD2 PHE B 270       8.587   7.284 470.309  1.00 31.15      B    C  
ANISOU 5468  CD2 PHE B 270     3275   1996   6565    634   -648    315  B    C  
ATOM   5469  CE1 PHE B 270       8.975   4.564 470.612  1.00 32.41      B    C  
ANISOU 5469  CE1 PHE B 270     3535   2111   6670    718   -688    477  B    C  
ATOM   5470  CE2 PHE B 270       8.420   6.425 469.226  1.00 36.13      B    C  
ANISOU 5470  CE2 PHE B 270     3914   2647   7168    606   -509    343  B    C  
ATOM   5471  CZ  PHE B 270       8.627   5.067 469.379  1.00 31.13      B    C  
ANISOU 5471  CZ  PHE B 270     3326   1988   6513    648   -526    416  B    C  
ATOM   5472  N   ASN B 271       8.338   7.356 475.954  1.00 36.62      B    N  
ANISOU 5472  N   ASN B 271     4446   2867   6600    651  -1189    364  B    N  
ATOM   5473  CA  ASN B 271       8.993   7.588 477.230  1.00 42.72      B    C  
ANISOU 5473  CA  ASN B 271     5312   3664   7255    655  -1407    354  B    C  
ATOM   5474  C   ASN B 271      10.318   6.838 477.149  1.00 52.03      B    C  
ANISOU 5474  C   ASN B 271     6379   4784   8605    733  -1600    422  B    C  
ATOM   5475  O   ASN B 271      10.356   5.616 477.308  1.00 53.25      B    O  
ANISOU 5475  O   ASN B 271     6615   4891   8729    788  -1642    538  B    O  
ATOM   5476  CB  ASN B 271       8.116   7.112 478.383  1.00 54.05      B    C  
ANISOU 5476  CB  ASN B 271     7003   5143   8390    619  -1392    407  B    C  
ATOM   5477  CG  ASN B 271       8.697   7.453 479.735  1.00 60.34      B    C  
ANISOU 5477  CG  ASN B 271     7946   5965   9014    608  -1618    387  B    C  
ATOM   5478  ND2 ASN B 271       7.881   7.314 480.780  1.00 51.81      B    N  
ANISOU 5478  ND2 ASN B 271     7116   4932   7638    553  -1573    403  B    N  
ATOM   5479  OD1 ASN B 271       9.871   7.835 479.846  1.00 64.77      B    O  
ANISOU 5479  OD1 ASN B 271     8399   6508   9703    637  -1831    354  B    O  
ATOM   5480  N   GLU B 272      11.398   7.568 476.869  1.00 58.40      B    N  
ANISOU 5480  N   GLU B 272     6992   5588   9607    739  -1711    344  B    N  
ATOM   5481  CA  GLU B 272      12.706   6.984 476.550  1.00 41.39      B    C  
ANISOU 5481  CA  GLU B 272     4643   3392   7691    823  -1860    379  B    C  
ATOM   5482  C   GLU B 272      12.516   6.072 475.346  1.00 47.90      B    C  
ANISOU 5482  C   GLU B 272     5389   4149   8662    878  -1670    437  B    C  
ATOM   5483  O   GLU B 272      12.140   6.574 474.270  1.00 64.16      B    O  
ANISOU 5483  O   GLU B 272     7365   6201  10811    826  -1462    380  B    O  
ATOM   5484  CB  GLU B 272      13.266   6.342 477.808  1.00 45.40      B    C  
ANISOU 5484  CB  GLU B 272     5267   3900   8084    887  -2145    455  B    C  
ATOM   5485  CG  GLU B 272      13.353   7.318 478.955  1.00 68.76      B    C  
ANISOU 5485  CG  GLU B 272     8341   6924  10862    809  -2317    381  B    C  
ATOM   5486  CD  GLU B 272      14.191   8.546 478.615  1.00 87.31      B    C  
ANISOU 5486  CD  GLU B 272    10465   9304  13407    744  -2375    245  B    C  
ATOM   5487  OE1 GLU B 272      15.330   8.369 478.116  1.00 90.12      B    O  
ANISOU 5487  OE1 GLU B 272    10557   9648  14038    793  -2475    236  B    O  
ATOM   5488  OE2 GLU B 272      13.686   9.681 478.806  1.00 85.48      B    O1-
ANISOU 5488  OE2 GLU B 272    10317   9099  13061    642  -2302    142  B    O1-
ATOM   5489  N   ASP B 273      12.730   4.768 475.461  1.00 53.71      B    N  
ANISOU 5489  N   ASP B 273     6177   4820   9412    978  -1734    546  B    N  
ATOM   5490  CA  ASP B 273      12.587   3.860 474.330  1.00 53.61      B    C  
ANISOU 5490  CA  ASP B 273     6114   4723   9530   1029  -1558    590  B    C  
ATOM   5491  C   ASP B 273      11.222   3.186 474.265  1.00 46.25      B    C  
ANISOU 5491  C   ASP B 273     5412   3765   8396    977  -1394    664  B    C  
ATOM   5492  O   ASP B 273      10.981   2.393 473.348  1.00 37.60      B    O  
ANISOU 5492  O   ASP B 273     4322   2640   7324    974  -1224    683  B    O  
ATOM   5493  CB  ASP B 273      13.696   2.799 474.382  1.00 70.00      B    C  
ANISOU 5493  CB  ASP B 273     8120   6788  11688   1137  -1664    628  B    C  
ATOM   5494  CG  ASP B 273      15.093   3.407 474.340  1.00 83.41      B    C  
ANISOU 5494  CG  ASP B 273     9543   8540  13608   1168  -1798    540  B    C  
ATOM   5495  OD1 ASP B 273      15.288   4.445 473.655  1.00 69.89      B    O1-
ANISOU 5495  OD1 ASP B 273     7658   6862  12034   1088  -1694    439  B    O1-
ATOM   5496  OD2 ASP B 273      15.988   2.848 475.013  1.00 95.67      B    O1-
ANISOU 5496  OD2 ASP B 273    11058  10094  15198   1268  -2014    574  B    O1-
ATOM   5497  N   GLU B 274      10.336   3.474 475.217  1.00 44.03      B    N  
ANISOU 5497  N   GLU B 274     5323   3547   7858    898  -1406    679  B    N  
ATOM   5498  CA  GLU B 274       9.017   2.856 475.289  1.00 42.83      B    C  
ANISOU 5498  CA  GLU B 274     5369   3391   7512    824  -1248    743  B    C  
ATOM   5499  C   GLU B 274       7.954   3.661 474.547  1.00 50.81      B    C  
ANISOU 5499  C   GLU B 274     6327   4472   8507    729  -1026    659  B    C  
ATOM   5500  O   GLU B 274       7.854   4.883 474.709  1.00 43.15      B    O  
ANISOU 5500  O   GLU B 274     5299   3578   7520    696  -1022    561  B    O  
ATOM   5501  CB  GLU B 274       8.614   2.680 476.750  1.00 42.38      B    C  
ANISOU 5501  CB  GLU B 274     5554   3372   7178    783  -1356    802  B    C  
ATOM   5502  CG  GLU B 274       9.521   1.736 477.495  1.00 63.09      B    C  
ANISOU 5502  CG  GLU B 274     8283   5905   9783    882  -1596    913  B    C  
ATOM   5503  CD  GLU B 274       8.978   1.377 478.856  1.00 89.03      B    C  
ANISOU 5503  CD  GLU B 274    11876   9204  12747    819  -1673    997  B    C  
ATOM   5504  OE1 GLU B 274       7.749   1.514 479.056  1.00 88.29      B    O  
ANISOU 5504  OE1 GLU B 274    11910   9176  12462    692  -1474    985  B    O  
ATOM   5505  OE2 GLU B 274       9.778   0.937 479.713  1.00100.50      B    O1-
ANISOU 5505  OE2 GLU B 274    13443  10603  14140    897  -1930   1074  B    O1-
ATOM   5506  N   LEU B 275       7.147   2.967 473.753  1.00 34.70      B    N  
ANISOU 5506  N   LEU B 275     4319   2396   6470    689   -859    697  B    N  
ATOM   5507  CA  LEU B 275       5.999   3.597 473.117  1.00 37.18      B    C  
ANISOU 5507  CA  LEU B 275     4596   2779   6751    606   -677    632  B    C  
ATOM   5508  C   LEU B 275       4.895   3.707 474.168  1.00 43.35      B    C  
ANISOU 5508  C   LEU B 275     5521   3656   7295    526   -627    637  B    C  
ATOM   5509  O   LEU B 275       4.310   2.700 474.596  1.00 34.60      B    O  
ANISOU 5509  O   LEU B 275     4561   2532   6054    468   -584    725  B    O  
ATOM   5510  CB  LEU B 275       5.560   2.810 471.884  1.00 32.26      B    C  
ANISOU 5510  CB  LEU B 275     3953   2088   6215    580   -540    663  B    C  
ATOM   5511  CG  LEU B 275       4.460   3.398 471.003  1.00 30.89      B    C  
ANISOU 5511  CG  LEU B 275     3719   1975   6044    508   -386    600  B    C  
ATOM   5512  CD1 LEU B 275       4.910   4.733 470.397  1.00 34.24      B    C  
ANISOU 5512  CD1 LEU B 275     4004   2417   6587    542   -392    502  B    C  
ATOM   5513  CD2 LEU B 275       4.054   2.443 469.894  1.00 30.40      B    C  
ANISOU 5513  CD2 LEU B 275     3679   1837   6035    466   -285    640  B    C  
ATOM   5514  N   TRP B 276       4.652   4.939 474.615  1.00 33.73      B    N  
ANISOU 5514  N   TRP B 276     4269   2527   6019    518   -625    539  B    N  
ATOM   5515  CA  TRP B 276       3.695   5.189 475.679  1.00 34.65      B    C  
ANISOU 5515  CA  TRP B 276     4512   2743   5911    455   -561    516  B    C  
ATOM   5516  C   TRP B 276       2.291   5.286 475.119  1.00 48.02      B    C  
ANISOU 5516  C   TRP B 276     6146   4509   7588    392   -357    477  B    C  
ATOM   5517  O   TRP B 276       1.326   4.849 475.762  1.00 34.83      B    O  
ANISOU 5517  O   TRP B 276     4572   2910   5752    309   -246    500  B    O  
ATOM   5518  CB  TRP B 276       4.086   6.475 476.400  1.00 35.20      B    C  
ANISOU 5518  CB  TRP B 276     4582   2860   5932    486   -648    409  B    C  
ATOM   5519  CG  TRP B 276       3.220   6.872 477.545  1.00 36.45      B    C  
ANISOU 5519  CG  TRP B 276     4881   3117   5852    435   -574    358  B    C  
ATOM   5520  CD1 TRP B 276       3.393   6.544 478.847  1.00 43.16      B    C  
ANISOU 5520  CD1 TRP B 276     5936   3984   6480    402   -655    397  B    C  
ATOM   5521  CD2 TRP B 276       2.062   7.721 477.497  1.00 36.23      B    C  
ANISOU 5521  CD2 TRP B 276     4804   3181   5781    421   -399    246  B    C  
ATOM   5522  CE2 TRP B 276       1.583   7.846 478.809  1.00 38.05      B    C  
ANISOU 5522  CE2 TRP B 276     5207   3487   5762    374   -352    213  B    C  
ATOM   5523  CE3 TRP B 276       1.387   8.383 476.468  1.00 44.41      B    C  
ANISOU 5523  CE3 TRP B 276     5673   4237   6964    452   -284    171  B    C  
ATOM   5524  NE1 TRP B 276       2.406   7.111 479.617  1.00 39.29      B    N  
ANISOU 5524  NE1 TRP B 276     5536   3595   5796    352   -512    312  B    N  
ATOM   5525  CZ2 TRP B 276       0.465   8.608 479.123  1.00 44.32      B    C  
ANISOU 5525  CZ2 TRP B 276     5986   4384   6471    368   -172     93  B    C  
ATOM   5526  CZ3 TRP B 276       0.272   9.135 476.782  1.00 35.52      B    C  
ANISOU 5526  CZ3 TRP B 276     4527   3207   5761    458   -138     63  B    C  
ATOM   5527  CH2 TRP B 276      -0.179   9.238 478.095  1.00 37.35      B    C  
ANISOU 5527  CH2 TRP B 276     4907   3520   5765    421    -72     18  B    C  
ATOM   5528  N   GLY B 277       2.198   5.834 473.914  1.00 48.83      B    N  
ANISOU 5528  N   GLY B 277     6093   4596   7864    423   -311    423  B    N  
ATOM   5529  CA  GLY B 277       0.948   6.046 473.223  1.00 31.81      B    C  
ANISOU 5529  CA  GLY B 277     3850   2507   5730    385   -164    379  B    C  
ATOM   5530  C   GLY B 277       1.262   6.627 471.864  1.00 30.42      B    C  
ANISOU 5530  C   GLY B 277     3548   2268   5741    435   -178    341  B    C  
ATOM   5531  O   GLY B 277       2.409   6.607 471.400  1.00 38.59      B    O  
ANISOU 5531  O   GLY B 277     4565   3209   6889    474   -263    360  B    O  
ATOM   5532  N   ILE B 278       0.233   7.152 471.218  1.00 34.19      B    N  
ANISOU 5532  N   ILE B 278     3939   2801   6251    432    -94    284  B    N  
ATOM   5533  CA  ILE B 278       0.389   7.788 469.921  1.00 41.66      B    C  
ANISOU 5533  CA  ILE B 278     4806   3683   7340    471   -109    252  B    C  
ATOM   5534  C   ILE B 278      -0.538   8.990 469.873  1.00 29.20      B    C  
ANISOU 5534  C   ILE B 278     3162   2171   5762    525    -77    154  B    C  
ATOM   5535  O   ILE B 278      -1.519   9.085 470.614  1.00 48.98      B    O  
ANISOU 5535  O   ILE B 278     5644   4787   8180    523     -7    111  B    O  
ATOM   5536  CB  ILE B 278       0.121   6.834 468.723  1.00 44.04      B    C  
ANISOU 5536  CB  ILE B 278     5093   3936   7704    414    -70    316  B    C  
ATOM   5537  CG1 ILE B 278      -1.348   6.489 468.592  1.00 36.08      B    C  
ANISOU 5537  CG1 ILE B 278     4034   3030   6647    353     10    309  B    C  
ATOM   5538  CG2 ILE B 278       0.935   5.530 468.827  1.00 46.44      B    C  
ANISOU 5538  CG2 ILE B 278     5479   4160   8008    378    -89    408  B    C  
ATOM   5539  CD1 ILE B 278      -1.576   5.408 467.591  1.00 52.70      B    C  
ANISOU 5539  CD1 ILE B 278     6157   5081   8785    269     32    372  B    C  
ATOM   5540  N   VAL B 279      -0.194   9.926 469.007  1.00 32.15      B    N  
ANISOU 5540  N   VAL B 279     3513   2466   6236    578   -122    115  B    N  
ATOM   5541  CA  VAL B 279      -1.096  10.997 468.613  1.00 34.86      B    C  
ANISOU 5541  CA  VAL B 279     3804   2831   6609    650   -113     38  B    C  
ATOM   5542  C   VAL B 279      -1.752  10.555 467.310  1.00 28.49      B    C  
ANISOU 5542  C   VAL B 279     2949   2014   5862    622   -105     81  B    C  
ATOM   5543  O   VAL B 279      -1.091  10.455 466.280  1.00 27.76      B    O  
ANISOU 5543  O   VAL B 279     2902   1815   5830    597   -137    124  B    O  
ATOM   5544  CB  VAL B 279      -0.344  12.331 468.465  1.00 28.88      B    C  
ANISOU 5544  CB  VAL B 279     3099   1969   5907    713   -181    -23  B    C  
ATOM   5545  CG1 VAL B 279      -1.258  13.457 467.987  1.00 29.43      B    C  
ANISOU 5545  CG1 VAL B 279     3145   2024   6013    810   -191    -94  B    C  
ATOM   5546  CG2 VAL B 279       0.321  12.699 469.786  1.00 29.53      B    C  
ANISOU 5546  CG2 VAL B 279     3238   2065   5918    720   -210    -71  B    C  
ATOM   5547  N   ALA B 280      -3.048  10.283 467.329  1.00 29.18      B    N  
ANISOU 5547  N   ALA B 280     2944   2214   5930    617    -60     63  B    N  
ATOM   5548  CA  ALA B 280      -3.759   9.845 466.130  1.00 29.11      B    C  
ANISOU 5548  CA  ALA B 280     2884   2206   5968    578    -81     98  B    C  
ATOM   5549  C   ALA B 280      -4.485  11.017 465.496  1.00 29.72      B    C  
ANISOU 5549  C   ALA B 280     2905   2277   6108    692   -149     36  B    C  
ATOM   5550  O   ALA B 280      -5.185  11.751 466.183  1.00 30.75      B    O  
ANISOU 5550  O   ALA B 280     2953   2487   6243    787   -129    -47  B    O  
ATOM   5551  CB  ALA B 280      -4.769   8.756 466.464  1.00 29.86      B    C  
ANISOU 5551  CB  ALA B 280     2891   2432   6021    480     -8    118  B    C  
ATOM   5552  N   CYS B 281      -4.330  11.183 464.188  1.00 37.42      B    N  
ANISOU 5552  N   CYS B 281     3942   3150   7125    689   -228     73  B    N  
ATOM   5553  CA  CYS B 281      -4.967  12.272 463.458  1.00 30.13      B    C  
ANISOU 5553  CA  CYS B 281     3007   2188   6253    803   -328     35  B    C  
ATOM   5554  C   CYS B 281      -5.781  11.721 462.300  1.00 33.41      B    C  
ANISOU 5554  C   CYS B 281     3387   2626   6681    754   -403     76  B    C  
ATOM   5555  O   CYS B 281      -5.221  11.122 461.384  1.00 40.46      B    O  
ANISOU 5555  O   CYS B 281     4399   3430   7545    655   -417    143  B    O  
ATOM   5556  CB  CYS B 281      -3.932  13.284 462.955  1.00 31.62      B    C  
ANISOU 5556  CB  CYS B 281     3373   2239   6402    824   -370     41  B    C  
ATOM   5557  SG  CYS B 281      -2.811  13.865 464.204  1.00 29.30      B    S  
ANISOU 5557  SG  CYS B 281     3142   1943   6049    823   -306     -6  B    S  
ATOM   5558  N   HIS B 282      -7.091  11.959 462.329  1.00 37.70      B    N  
ANISOU 5558  N   HIS B 282     3763   3289   7272    827   -454     26  B    N  
ATOM   5559  CA  HIS B 282      -8.030  11.584 461.278  1.00 35.94      B    C  
ANISOU 5559  CA  HIS B 282     3474   3107   7074    795   -569     50  B    C  
ATOM   5560  C   HIS B 282      -8.563  12.807 460.564  1.00 34.23      B    C  
ANISOU 5560  C   HIS B 282     3266   2826   6912    963   -735     24  B    C  
ATOM   5561  O   HIS B 282      -8.833  13.838 461.188  1.00 43.72      B    O  
ANISOU 5561  O   HIS B 282     4407   4036   8169   1130   -739    -49  B    O  
ATOM   5562  CB  HIS B 282      -9.235  10.841 461.841  1.00 35.77      B    C  
ANISOU 5562  CB  HIS B 282     3208   3294   7090    739   -519      9  B    C  
ATOM   5563  CG  HIS B 282      -8.879   9.583 462.542  1.00 43.53      B    C  
ANISOU 5563  CG  HIS B 282     4201   4331   8007    566   -368     44  B    C  
ATOM   5564  CD2 HIS B 282      -7.771   8.813 462.464  1.00 31.89      B    C  
ANISOU 5564  CD2 HIS B 282     2909   2747   6462    454   -310    116  B    C  
ATOM   5565  ND1 HIS B 282      -9.738   8.950 463.411  1.00 48.73      B    N  
ANISOU 5565  ND1 HIS B 282     4675   5166   8673    490   -259      7  B    N  
ATOM   5566  CE1 HIS B 282      -9.158   7.857 463.866  1.00 54.76      B    C  
ANISOU 5566  CE1 HIS B 282     5540   5910   9356    336   -151     66  B    C  
ATOM   5567  NE2 HIS B 282      -7.965   7.750 463.304  1.00 55.71      B    N  
ANISOU 5567  NE2 HIS B 282     5873   5857   9437    326   -188    130  B    N  
ATOM   5568  N   HIS B 283      -8.775  12.649 459.258  1.00 34.65      B    N  
ANISOU 5568  N   HIS B 283     3412   2813   6943    922   -879     81  B    N  
ATOM   5569  CA  HIS B 283      -9.391  13.664 458.418  1.00 41.93      B    C  
ANISOU 5569  CA  HIS B 283     4365   3665   7901   1074  -1082     78  B    C  
ATOM   5570  C   HIS B 283     -10.489  13.024 457.579  1.00 40.15      B    C  
ANISOU 5570  C   HIS B 283     4021   3541   7693   1020  -1237     94  B    C  
ATOM   5571  O   HIS B 283     -10.340  11.888 457.124  1.00 51.10      B    O  
ANISOU 5571  O   HIS B 283     5457   4947   9012    828  -1208    140  B    O  
ATOM   5572  CB  HIS B 283      -8.328  14.337 457.532  1.00 35.59      B    C  
ANISOU 5572  CB  HIS B 283     3884   2624   7013   1071  -1132    146  B    C  
ATOM   5573  CG  HIS B 283      -8.742  15.686 457.027  1.00 69.53      B    C  
ANISOU 5573  CG  HIS B 283     8279   6844  11295   1237  -1290    138  B    C  
ATOM   5574  CD2 HIS B 283      -8.703  16.222 455.784  1.00 49.00      B    C  
ANISOU 5574  CD2 HIS B 283     5911   4111   8596   1241  -1443    203  B    C  
ATOM   5575  ND1 HIS B 283      -9.290  16.653 457.845  1.00 53.49      B    N  
ANISOU 5575  ND1 HIS B 283     6132   4897   9294   1398  -1274     53  B    N  
ATOM   5576  CE1 HIS B 283      -9.572  17.722 457.125  1.00 40.02      B    C  
ANISOU 5576  CE1 HIS B 283     4575   3104   7527   1504  -1415     71  B    C  
ATOM   5577  NE2 HIS B 283      -9.224  17.487 455.873  1.00 39.96      B    N  
ANISOU 5577  NE2 HIS B 283     4781   2967   7437   1410  -1524    165  B    N  
ATOM   5578  N   THR B 284     -11.584  13.754 457.352  1.00 48.18      B    N  
ANISOU 5578  N   THR B 284     4885   4614   8806   1192  -1416     51  B    N  
ATOM   5579  CA  THR B 284     -12.738  13.174 456.655  1.00 55.49      B    C  
ANISOU 5579  CA  THR B 284     5639   5669   9775   1145  -1591     50  B    C  
ATOM   5580  C   THR B 284     -12.659  13.314 455.152  1.00 51.15      B    C  
ANISOU 5580  C   THR B 284     5341   4967   9126   1118  -1825    135  B    C  
ATOM   5581  O   THR B 284     -13.646  13.023 454.476  1.00 46.51      B    O  
ANISOU 5581  O   THR B 284     4631   4469   8570   1104  -2030    134  B    O  
ATOM   5582  CB  THR B 284     -14.066  13.787 457.113  1.00 44.39      B    C  
ANISOU 5582  CB  THR B 284     3890   4429   8547   1347  -1690    -48  B    C  
ATOM   5583  CG2 THR B 284     -14.372  13.406 458.546  1.00 44.23      B    C  
ANISOU 5583  CG2 THR B 284     3596   4604   8607   1324  -1441   -141  B    C  
ATOM   5584  OG1 THR B 284     -14.007  15.211 456.988  1.00 61.15      B    O  
ANISOU 5584  OG1 THR B 284     6118   6406  10710   1605  -1811    -61  B    O  
ATOM   5585  N   LYS B 285     -11.570  13.860 454.634  1.00 44.58      B    N  
ANISOU 5585  N   LYS B 285     4850   3911   8176   1120  -1811    202  B    N  
ATOM   5586  CA  LYS B 285     -11.263  13.869 453.213  1.00 41.87      B    C  
ANISOU 5586  CA  LYS B 285     4821   3403   7685   1043  -1972    293  B    C  
ATOM   5587  C   LYS B 285      -9.757  13.722 453.080  1.00 39.65      B    C  
ANISOU 5587  C   LYS B 285     4838   2953   7275    910  -1766    344  B    C  
ATOM   5588  O   LYS B 285      -9.039  13.832 454.076  1.00 38.04      B    O  
ANISOU 5588  O   LYS B 285     4583   2752   7117    920  -1559    311  B    O  
ATOM   5589  CB  LYS B 285     -11.800  15.147 452.562  1.00 44.15      B    C  
ANISOU 5589  CB  LYS B 285     5209   3577   7990   1260  -2242    317  B    C  
ATOM   5590  CG  LYS B 285     -11.512  16.380 453.393  1.00 66.56      B    C  
ANISOU 5590  CG  LYS B 285     8042   6349  10898   1455  -2158    272  B    C  
ATOM   5591  CD  LYS B 285     -12.447  17.553 453.086  1.00 58.36      B    C  
ANISOU 5591  CD  LYS B 285     6982   5332   9858   1657  -2349    245  B    C  
ATOM   5592  CE  LYS B 285     -12.153  18.723 454.031  1.00 69.14      B    C  
ANISOU 5592  CE  LYS B 285     8361   6694  11214   1779  -2169    179  B    C  
ATOM   5593  NZ  LYS B 285     -12.235  18.375 455.484  1.00 62.29      B    N1+
ANISOU 5593  NZ  LYS B 285     7205   5998  10464   1794  -1946     76  B    N1+
ATOM   5594  N   PRO B 286      -9.253  13.390 451.892  1.00 39.72      B    N  
ANISOU 5594  N   PRO B 286     5145   2825   7121    771  -1808    416  B    N  
ATOM   5595  CA  PRO B 286      -7.798  13.261 451.747  1.00 61.70      B    C  
ANISOU 5595  CA  PRO B 286     8179   5459   9804    648  -1588    451  B    C  
ATOM   5596  C   PRO B 286      -7.081  14.546 452.132  1.00 50.65      B    C  
ANISOU 5596  C   PRO B 286     6889   3922   8434    769  -1531    455  B    C  
ATOM   5597  O   PRO B 286      -7.617  15.651 452.010  1.00 59.39      B    O  
ANISOU 5597  O   PRO B 286     8018   5015   9533    919  -1674    452  B    O  
ATOM   5598  CB  PRO B 286      -7.605  12.916 450.263  1.00 38.91      B    C  
ANISOU 5598  CB  PRO B 286     5614   2443   6728    510  -1675    517  B    C  
ATOM   5599  CG  PRO B 286      -8.958  12.998 449.633  1.00 41.24      B    C  
ANISOU 5599  CG  PRO B 286     5847   2806   7016    574  -1985    527  B    C  
ATOM   5600  CD  PRO B 286      -9.956  12.828 450.731  1.00 49.56      B    C  
ANISOU 5600  CD  PRO B 286     6480   4082   8269    679  -2017    451  B    C  
ATOM   5601  N   ARG B 287      -5.850  14.383 452.606  1.00 50.09      B    N  
ANISOU 5601  N   ARG B 287     6860   3861   8311    665  -1261    437  B    N  
ATOM   5602  CA  ARG B 287      -5.090  15.498 453.159  1.00 36.93      B    C  
ANISOU 5602  CA  ARG B 287     5240   2197   6596    713  -1126    409  B    C  
ATOM   5603  C   ARG B 287      -3.618  15.124 453.191  1.00 40.48      B    C  
ANISOU 5603  C   ARG B 287     5790   2632   6957    558   -869    409  B    C  
ATOM   5604  O   ARG B 287      -3.235  14.159 453.859  1.00 46.04      B    O  
ANISOU 5604  O   ARG B 287     6353   3423   7717    497   -745    381  B    O  
ATOM   5605  CB  ARG B 287      -5.583  15.841 454.557  1.00 39.87      B    C  
ANISOU 5605  CB  ARG B 287     5346   2696   7108    851  -1116    332  B    C  
ATOM   5606  CG  ARG B 287      -4.767  16.926 455.241  1.00 34.87      B    C  
ANISOU 5606  CG  ARG B 287     4775   2052   6423    880   -986    296  B    C  
ATOM   5607  CD  ARG B 287      -5.569  17.678 456.287  1.00 51.62      B    C  
ANISOU 5607  CD  ARG B 287     6722   4255   8638   1055  -1039    222  B    C  
ATOM   5608  NE  ARG B 287      -4.857  18.883 456.689  1.00 64.19      B    N  
ANISOU 5608  NE  ARG B 287     8445   5782  10164   1080   -960    199  B    N  
ATOM   5609  CZ  ARG B 287      -4.866  20.030 456.011  1.00 61.72      B    C  
ANISOU 5609  CZ  ARG B 287     8331   5339   9779   1131  -1031    231  B    C  
ATOM   5610  NH1 ARG B 287      -5.572  20.155 454.888  1.00 57.20      B    N1+
ANISOU 5610  NH1 ARG B 287     7858   4698   9177   1176  -1202    289  B    N1+
ATOM   5611  NH2 ARG B 287      -4.162  21.053 456.468  1.00 61.50      B    N  
ANISOU 5611  NH2 ARG B 287     8414   5240   9712   1132   -945    208  B    N  
ATOM   5612  N   ALA B 288      -2.796  15.869 452.469  1.00 34.62      B    N  
ANISOU 5612  N   ALA B 288     5285   1782   6088    498   -787    441  B    N  
ATOM   5613  CA  ALA B 288      -1.357  15.695 452.538  1.00 40.09      B    C  
ANISOU 5613  CA  ALA B 288     6047   2462   6723    372   -544    427  B    C  
ATOM   5614  C   ALA B 288      -0.756  16.800 453.391  1.00 38.26      B    C  
ANISOU 5614  C   ALA B 288     5791   2233   6513    418   -482    389  B    C  
ATOM   5615  O   ALA B 288      -1.266  17.926 453.426  1.00 39.74      B    O  
ANISOU 5615  O   ALA B 288     6031   2366   6703    517   -586    396  B    O  
ATOM   5616  CB  ALA B 288      -0.719  15.705 451.147  1.00 40.89      B    C  
ANISOU 5616  CB  ALA B 288     6417   2426   6694    242   -449    479  B    C  
ATOM   5617  N   ILE B 289       0.354  16.474 454.056  1.00 39.16      B    N  
ANISOU 5617  N   ILE B 289     5836   2403   6642    343   -332    348  B    N  
ATOM   5618  CA  ILE B 289       1.095  17.425 454.877  1.00 42.66      B    C  
ANISOU 5618  CA  ILE B 289     6262   2839   7107    350   -285    307  B    C  
ATOM   5619  C   ILE B 289       2.553  17.340 454.463  1.00 40.36      B    C  
ANISOU 5619  C   ILE B 289     6075   2490   6768    195   -138    304  B    C  
ATOM   5620  O   ILE B 289       3.096  16.231 454.329  1.00 40.80      B    O  
ANISOU 5620  O   ILE B 289     6055   2607   6839    122    -63    298  B    O  
ATOM   5621  CB  ILE B 289       0.935  17.175 456.393  1.00 46.97      B    C  
ANISOU 5621  CB  ILE B 289     6554   3528   7764    425   -310    247  B    C  
ATOM   5622  CG1 ILE B 289       1.221  15.707 456.756  1.00 37.79      B    C  
ANISOU 5622  CG1 ILE B 289     5226   2482   6651    371   -244    240  B    C  
ATOM   5623  CG2 ILE B 289      -0.450  17.680 456.899  1.00 31.85      B    C  
ANISOU 5623  CG2 ILE B 289     4555   1646   5902    586   -452    228  B    C  
ATOM   5624  CD1 ILE B 289       1.312  15.461 458.226  1.00 29.18      B    C  
ANISOU 5624  CD1 ILE B 289     3930   1504   5653    416   -240    193  B    C  
ATOM   5625  N   GLY B 290       3.161  18.515 454.196  1.00 37.30      B    N  
ANISOU 5625  N   GLY B 290     5865   1974   6333    142   -102    308  B    N  
ATOM   5626  CA  GLY B 290       4.535  18.589 453.728  1.00 34.12      B    C  
ANISOU 5626  CA  GLY B 290     5559   1502   5904    -29     -2    304  B    C  
ATOM   5627  C   GLY B 290       5.545  18.192 454.792  1.00 33.23      B    C  
ANISOU 5627  C   GLY B 290     5176   1506   5944    -64     62    247  B    C  
ATOM   5628  O   GLY B 290       5.230  18.031 455.969  1.00 32.25      B    O  
ANISOU 5628  O   GLY B 290     4854   1490   5909     35     16    211  B    O  
ATOM   5629  N   ARG B 291       6.810  18.093 454.367  1.00 31.47      B    N  
ANISOU 5629  N   ARG B 291     4689   1943   5325    192   -674  -1263  B    N  
ATOM   5630  CA  ARG B 291       7.875  17.678 455.282  1.00 31.23      B    C  
ANISOU 5630  CA  ARG B 291     4590   2021   5256    252   -519  -1306  B    C  
ATOM   5631  C   ARG B 291       8.034  18.621 456.466  1.00 29.95      B    C  
ANISOU 5631  C   ARG B 291     4404   1882   5094    415   -491  -1232  B    C  
ATOM   5632  O   ARG B 291       8.310  18.168 457.587  1.00 29.18      B    O  
ANISOU 5632  O   ARG B 291     4220   1869   4999    514   -431  -1209  B    O  
ATOM   5633  CB  ARG B 291       9.207  17.624 454.532  1.00 30.80      B    C  
ANISOU 5633  CB  ARG B 291     4610   2008   5086     74   -412  -1426  B    C  
ATOM   5634  CG  ARG B 291       9.277  16.631 453.386  1.00 31.47      B    C  
ANISOU 5634  CG  ARG B 291     4710   2116   5131   -124   -398  -1517  B    C  
ATOM   5635  CD  ARG B 291      10.725  16.271 453.069  1.00 39.85      B    C  
ANISOU 5635  CD  ARG B 291     5796   3260   6086   -229   -287  -1612  B    C  
ATOM   5636  NE  ARG B 291      10.806  15.621 451.772  1.00 48.06      B    N  
ANISOU 5636  NE  ARG B 291     6875   4331   7053   -448   -288  -1693  B    N  
ATOM   5637  CZ  ARG B 291      10.439  14.367 451.543  1.00 45.24      B    C  
ANISOU 5637  CZ  ARG B 291     6429   4007   6753   -480   -281  -1723  B    C  
ATOM   5638  NH1 ARG B 291       9.948  13.638 452.540  1.00 35.62      B    N1+
ANISOU 5638  NH1 ARG B 291     5093   2776   5666   -307   -282  -1673  B    N1+
ATOM   5639  NH2 ARG B 291      10.530  13.860 450.312  1.00 33.80      B    N  
ANISOU 5639  NH2 ARG B 291     5007   2607   5227   -690   -282  -1795  B    N  
ATOM   5640  N   ARG B 292       7.807  19.920 456.258  1.00 30.51      B    N  
ANISOU 5640  N   ARG B 292     4554   1874   5164    434   -543  -1189  B    N  
ATOM   5641  CA  ARG B 292       8.017  20.891 457.330  1.00 30.14      B    C  
ANISOU 5641  CA  ARG B 292     4485   1857   5110    560   -492  -1138  B    C  
ATOM   5642  C   ARG B 292       6.924  20.789 458.378  1.00 29.83      B    C  
ANISOU 5642  C   ARG B 292     4337   1858   5139    723   -534  -1034  B    C  
ATOM   5643  O   ARG B 292       7.192  20.934 459.577  1.00 53.38      B    O  
ANISOU 5643  O   ARG B 292     7259   4926   8097    804   -457  -1017  B    O  
ATOM   5644  CB  ARG B 292       8.103  22.308 456.771  1.00 38.57      B    C  
ANISOU 5644  CB  ARG B 292     5672   2813   6169    526   -527  -1122  B    C  
ATOM   5645  CG  ARG B 292       9.413  22.567 456.067  1.00 32.69      B    C  
ANISOU 5645  CG  ARG B 292     5035   2064   5322    354   -431  -1237  B    C  
ATOM   5646  CD  ARG B 292       9.455  23.926 455.412  1.00 32.46      B    C  
ANISOU 5646  CD  ARG B 292     5147   1901   5287    290   -477  -1217  B    C  
ATOM   5647  NE  ARG B 292      10.820  24.226 454.984  1.00 43.70      B    N  
ANISOU 5647  NE  ARG B 292     6661   3351   6591    123   -342  -1338  B    N  
ATOM   5648  CZ  ARG B 292      11.359  23.757 453.866  1.00 33.20      B    C  
ANISOU 5648  CZ  ARG B 292     5413   2035   5168    -98   -314  -1433  B    C  
ATOM   5649  NH1 ARG B 292      10.623  23.012 453.060  1.00 49.33      B    N1+
ANISOU 5649  NH1 ARG B 292     7454   4058   7230   -181   -422  -1422  B    N1+
ATOM   5650  NH2 ARG B 292      12.614  24.044 453.546  1.00 33.46      B    N  
ANISOU 5650  NH2 ARG B 292     5547   2109   5058   -247   -191  -1530  B    N  
ATOM   5651  N   ILE B 293       5.683  20.546 457.952  1.00 30.36      B    N  
ANISOU 5651  N   ILE B 293     4384   1869   5283    757   -658   -967  B    N  
ATOM   5652  CA  ILE B 293       4.627  20.356 458.938  1.00 36.28      B    C  
ANISOU 5652  CA  ILE B 293     5022   2679   6084    890   -678   -883  B    C  
ATOM   5653  C   ILE B 293       4.854  19.062 459.710  1.00 30.13      B    C  
ANISOU 5653  C   ILE B 293     4163   2000   5284    892   -605   -912  B    C  
ATOM   5654  O   ILE B 293       4.714  19.041 460.936  1.00 39.16      B    O  
ANISOU 5654  O   ILE B 293     5242   3224   6411    972   -550   -878  B    O  
ATOM   5655  CB  ILE B 293       3.238  20.397 458.254  1.00 31.14      B    C  
ANISOU 5655  CB  ILE B 293     4358   1947   5525    926   -838   -799  B    C  
ATOM   5656  CG1 ILE B 293       2.802  21.840 458.004  1.00 32.18      B    C  
ANISOU 5656  CG1 ILE B 293     4539   1996   5694    985   -918   -716  B    C  
ATOM   5657  CG2 ILE B 293       2.168  19.736 459.083  1.00 30.97      B    C  
ANISOU 5657  CG2 ILE B 293     4210   2006   5551   1020   -844   -746  B    C  
ATOM   5658  CD1 ILE B 293       2.422  22.580 459.257  1.00 32.13      B    C  
ANISOU 5658  CD1 ILE B 293     4444   2067   5698   1109   -840   -676  B    C  
ATOM   5659  N   ARG B 294       5.315  18.004 459.033  1.00 29.18      B    N  
ANISOU 5659  N   ARG B 294     4058   1870   5161    792   -597   -981  B    N  
ATOM   5660  CA  ARG B 294       5.697  16.765 459.711  1.00 28.59      B    C  
ANISOU 5660  CA  ARG B 294     3920   1867   5077    790   -532  -1003  B    C  
ATOM   5661  C   ARG B 294       6.758  17.018 460.777  1.00 33.85      B    C  
ANISOU 5661  C   ARG B 294     4577   2610   5674    825   -440  -1013  B    C  
ATOM   5662  O   ARG B 294       6.608  16.590 461.935  1.00 37.05      B    O  
ANISOU 5662  O   ARG B 294     4926   3074   6078    895   -418   -971  B    O  
ATOM   5663  CB  ARG B 294       6.219  15.748 458.703  1.00 31.06      B    C  
ANISOU 5663  CB  ARG B 294     4253   2151   5398    661   -520  -1093  B    C  
ATOM   5664  CG  ARG B 294       5.239  15.286 457.648  1.00 34.04      B    C  
ANISOU 5664  CG  ARG B 294     4638   2452   5845    593   -610  -1105  B    C  
ATOM   5665  CD  ARG B 294       6.046  14.568 456.607  1.00 29.72      B    C  
ANISOU 5665  CD  ARG B 294     4127   1897   5270    423   -559  -1224  B    C  
ATOM   5666  NE  ARG B 294       5.341  14.478 455.345  1.00 42.46      B    N  
ANISOU 5666  NE  ARG B 294     5785   3439   6909    289   -646  -1262  B    N  
ATOM   5667  CZ  ARG B 294       5.949  14.124 454.219  1.00 50.38      B    C  
ANISOU 5667  CZ  ARG B 294     6839   4454   7849     87   -601  -1374  B    C  
ATOM   5668  NH1 ARG B 294       7.245  13.839 454.243  1.00 53.61      B    N1+
ANISOU 5668  NH1 ARG B 294     7254   4930   8187     37   -475  -1448  B    N1+
ATOM   5669  NH2 ARG B 294       5.288  14.073 453.073  1.00 44.77      B    N  
ANISOU 5669  NH2 ARG B 294     6172   3706   7131    -81   -690  -1406  B    N  
ATOM   5670  N   ARG B 295       7.832  17.733 460.419  1.00 28.00      B    N  
ANISOU 5670  N   ARG B 295     3898   1864   4875    770   -391  -1072  B    N  
ATOM   5671  CA  ARG B 295       8.878  17.961 461.406  1.00 27.56      B    C  
ANISOU 5671  CA  ARG B 295     3829   1879   4763    798   -317  -1088  B    C  
ATOM   5672  C   ARG B 295       8.323  18.767 462.568  1.00 36.21      B    C  
ANISOU 5672  C   ARG B 295     4894   3009   5854    901   -310  -1021  B    C  
ATOM   5673  O   ARG B 295       8.631  18.486 463.734  1.00 27.18      B    O  
ANISOU 5673  O   ARG B 295     3705   1930   4692    950   -280  -1008  B    O  
ATOM   5674  CB  ARG B 295      10.085  18.693 460.798  1.00 34.13      B    C  
ANISOU 5674  CB  ARG B 295     4736   2700   5533    716   -263  -1167  B    C  
ATOM   5675  CG  ARG B 295      10.754  18.121 459.547  1.00 33.21      B    C  
ANISOU 5675  CG  ARG B 295     4664   2555   5398    584   -249  -1258  B    C  
ATOM   5676  CD  ARG B 295      11.444  16.809 459.832  1.00 35.10      B    C  
ANISOU 5676  CD  ARG B 295     4834   2848   5655    573   -228  -1295  B    C  
ATOM   5677  NE  ARG B 295      12.393  16.411 458.801  1.00 48.17      B    N  
ANISOU 5677  NE  ARG B 295     6520   4501   7279    447   -191  -1397  B    N  
ATOM   5678  CZ  ARG B 295      12.021  15.845 457.653  1.00 60.98      B    C  
ANISOU 5678  CZ  ARG B 295     8169   6085   8915    341   -205  -1443  B    C  
ATOM   5679  NH1 ARG B 295      10.728  15.646 457.396  1.00 56.81      B    N1+
ANISOU 5679  NH1 ARG B 295     7638   5506   8442    355   -266  -1395  B    N1+
ATOM   5680  NH2 ARG B 295      12.935  15.491 456.760  1.00 63.78      B    N  
ANISOU 5680  NH2 ARG B 295     8549   6457   9228    216   -163  -1541  B    N  
ATOM   5681  N   LEU B 296       7.509  19.784 462.273  1.00 39.28      B    N  
ANISOU 5681  N   LEU B 296     5307   3350   6267    934   -343   -983  B    N  
ATOM   5682  CA  LEU B 296       6.934  20.582 463.344  1.00 28.01      B    C  
ANISOU 5682  CA  LEU B 296     3841   1955   4845   1026   -325   -933  B    C  
ATOM   5683  C   LEU B 296       6.070  19.741 464.280  1.00 27.90      B    C  
ANISOU 5683  C   LEU B 296     3746   1996   4858   1089   -341   -884  B    C  
ATOM   5684  O   LEU B 296       6.115  19.907 465.515  1.00 27.82      B    O  
ANISOU 5684  O   LEU B 296     3697   2045   4827   1142   -299   -878  B    O  
ATOM   5685  CB  LEU B 296       6.151  21.732 462.738  1.00 28.76      B    C  
ANISOU 5685  CB  LEU B 296     3969   1971   4988   1055   -372   -898  B    C  
ATOM   5686  CG  LEU B 296       5.290  22.557 463.688  1.00 29.47      B    C  
ANISOU 5686  CG  LEU B 296     4004   2083   5110   1153   -360   -851  B    C  
ATOM   5687  CD1 LEU B 296       6.124  23.091 464.806  1.00 28.91      B    C  
ANISOU 5687  CD1 LEU B 296     3930   2071   4983   1167   -263   -891  B    C  
ATOM   5688  CD2 LEU B 296       4.685  23.683 462.888  1.00 30.20      B    C  
ANISOU 5688  CD2 LEU B 296     4136   2072   5266   1177   -420   -814  B    C  
ATOM   5689  N   LEU B 297       5.312  18.804 463.715  1.00 28.01      B    N  
ANISOU 5689  N   LEU B 297     3738   1985   4920   1078   -403   -860  B    N  
ATOM   5690  CA  LEU B 297       4.526  17.860 464.510  1.00 28.02      B    C  
ANISOU 5690  CA  LEU B 297     3671   2025   4950   1124   -416   -821  B    C  
ATOM   5691  C   LEU B 297       5.425  17.018 465.416  1.00 28.86      B    C  
ANISOU 5691  C   LEU B 297     3768   2178   5021   1118   -372   -841  B    C  
ATOM   5692  O   LEU B 297       5.245  16.994 466.643  1.00 34.59      B    O  
ANISOU 5692  O   LEU B 297     4456   2950   5737   1177   -351   -822  B    O  
ATOM   5693  CB  LEU B 297       3.709  16.976 463.581  1.00 32.06      B    C  
ANISOU 5693  CB  LEU B 297     4168   2487   5526   1094   -487   -806  B    C  
ATOM   5694  CG  LEU B 297       2.596  17.772 462.905  1.00 34.33      B    C  
ANISOU 5694  CG  LEU B 297     4443   2729   5870   1127   -562   -768  B    C  
ATOM   5695  CD1 LEU B 297       1.829  16.895 461.965  1.00 29.31      B    C  
ANISOU 5695  CD1 LEU B 297     3789   2040   5306   1092   -647   -762  B    C  
ATOM   5696  CD2 LEU B 297       1.692  18.440 463.915  1.00 40.24      B    C  
ANISOU 5696  CD2 LEU B 297     5126   3526   6636   1222   -549   -726  B    C  
ATOM   5697  N   VAL B 298       6.408  16.316 464.836  1.00 27.39      B    N  
ANISOU 5697  N   VAL B 298     3610   1973   4824   1051   -366   -885  B    N  
ATOM   5698  CA  VAL B 298       7.208  15.410 465.661  1.00 28.25      B    C  
ANISOU 5698  CA  VAL B 298     3699   2109   4926   1059   -348   -896  B    C  
ATOM   5699  C   VAL B 298       7.957  16.176 466.745  1.00 35.83      B    C  
ANISOU 5699  C   VAL B 298     4655   3124   5836   1100   -309   -912  B    C  
ATOM   5700  O   VAL B 298       8.000  15.740 467.905  1.00 37.38      B    O  
ANISOU 5700  O   VAL B 298     4817   3349   6037   1153   -315   -894  B    O  
ATOM   5701  CB  VAL B 298       8.181  14.585 464.803  1.00 27.27      B    C  
ANISOU 5701  CB  VAL B 298     3591   1954   4816    982   -347   -955  B    C  
ATOM   5702  CG1 VAL B 298       9.143  13.831 465.710  1.00 27.40      B    C  
ANISOU 5702  CG1 VAL B 298     3581   1991   4840   1007   -343   -968  B    C  
ATOM   5703  CG2 VAL B 298       7.434  13.627 463.901  1.00 27.52      B    C  
ANISOU 5703  CG2 VAL B 298     3616   1928   4913    938   -383   -952  B    C  
ATOM   5704  N   ARG B 299       8.468  17.371 466.422  1.00 27.05      B    N  
ANISOU 5704  N   ARG B 299     3577   2020   4682   1078   -273   -948  B    N  
ATOM   5705  CA  ARG B 299       9.172  18.172 467.430  1.00 32.98      B    C  
ANISOU 5705  CA  ARG B 299     4321   2821   5390   1109   -232   -976  B    C  
ATOM   5706  C   ARG B 299       8.217  18.581 468.543  1.00 33.43      B    C  
ANISOU 5706  C   ARG B 299     4335   2909   5456   1186   -228   -941  B    C  
ATOM   5707  O   ARG B 299       8.586  18.604 469.723  1.00 27.53      B    O  
ANISOU 5707  O   ARG B 299     3556   2208   4696   1228   -217   -962  B    O  
ATOM   5708  CB  ARG B 299       9.760  19.436 466.793  1.00 34.68      B    C  
ANISOU 5708  CB  ARG B 299     4588   3021   5566   1067   -189  -1019  B    C  
ATOM   5709  CG  ARG B 299      10.820  19.215 465.751  1.00 34.54      B    C  
ANISOU 5709  CG  ARG B 299     4606   2979   5539    986   -189  -1086  B    C  
ATOM   5710  CD  ARG B 299      12.115  18.697 466.290  1.00 39.53      B    C  
ANISOU 5710  CD  ARG B 299     5193   3654   6174    979   -198  -1157  B    C  
ATOM   5711  NE  ARG B 299      12.066  17.249 466.365  1.00 35.92      B    N  
ANISOU 5711  NE  ARG B 299     4700   3191   5758    986   -235  -1134  B    N  
ATOM   5712  CZ  ARG B 299      12.241  16.443 465.339  1.00 36.56      B    C  
ANISOU 5712  CZ  ARG B 299     4790   3235   5867    926   -247  -1158  B    C  
ATOM   5713  NH1 ARG B 299      12.472  16.960 464.133  1.00 36.76      B    N1+
ANISOU 5713  NH1 ARG B 299     4866   3231   5870    849   -222  -1205  B    N1+
ATOM   5714  NH2 ARG B 299      12.166  15.126 465.527  1.00 36.96      B    N  
ANISOU 5714  NH2 ARG B 299     4806   3270   5968    939   -277  -1136  B    N  
ATOM   5715  N   THR B 300       6.975  18.910 468.183  1.00 31.86      B    N  
ANISOU 5715  N   THR B 300     4129   2685   5290   1208   -243   -900  B    N  
ATOM   5716  CA  THR B 300       6.026  19.324 469.201  1.00 28.02      B    C  
ANISOU 5716  CA  THR B 300     3589   2232   4824   1280   -233   -885  B    C  
ATOM   5717  C   THR B 300       5.683  18.167 470.135  1.00 34.15      B    C  
ANISOU 5717  C   THR B 300     4320   3035   5623   1320   -261   -866  B    C  
ATOM   5718  O   THR B 300       5.698  18.334 471.361  1.00 35.33      B    O  
ANISOU 5718  O   THR B 300     4428   3229   5765   1371   -246   -895  B    O  
ATOM   5719  CB  THR B 300       4.775  19.850 468.526  1.00 32.46      B    C  
ANISOU 5719  CB  THR B 300     4139   2758   5435   1300   -257   -849  B    C  
ATOM   5720  CG2 THR B 300       3.833  20.408 469.591  1.00 29.05      B    C  
ANISOU 5720  CG2 THR B 300     3638   2365   5035   1374   -236   -857  B    C  
ATOM   5721  OG1 THR B 300       5.139  20.945 467.690  1.00 28.42      B    O  
ANISOU 5721  OG1 THR B 300     3681   2202   4915   1272   -243   -863  B    O  
ATOM   5722  N   VAL B 301       5.382  16.983 469.573  1.00 28.16      B    N  
ANISOU 5722  N   VAL B 301     3565   2237   4896   1298   -306   -827  B    N  
ATOM   5723  CA  VAL B 301       5.110  15.795 470.396  1.00 28.54      B    C  
ANISOU 5723  CA  VAL B 301     3583   2284   4977   1335   -340   -801  B    C  
ATOM   5724  C   VAL B 301       6.324  15.436 471.261  1.00 28.64      B    C  
ANISOU 5724  C   VAL B 301     3599   2314   4967   1351   -346   -828  B    C  
ATOM   5725  O   VAL B 301       6.183  15.030 472.421  1.00 29.23      B    O  
ANISOU 5725  O   VAL B 301     3643   2406   5059   1414   -374   -824  B    O  
ATOM   5726  CB  VAL B 301       4.689  14.604 469.515  1.00 28.52      B    C  
ANISOU 5726  CB  VAL B 301     3593   2220   5023   1295   -381   -760  B    C  
ATOM   5727  CG1 VAL B 301       4.670  13.355 470.325  1.00 29.03      B    C  
ANISOU 5727  CG1 VAL B 301     3645   2257   5130   1327   -418   -727  B    C  
ATOM   5728  CG2 VAL B 301       3.309  14.824 468.883  1.00 34.33      B    C  
ANISOU 5728  CG2 VAL B 301     4300   2942   5800   1299   -399   -736  B    C  
ATOM   5729  N   GLU B 302       7.535  15.612 470.730  1.00 28.22      B    N  
ANISOU 5729  N   GLU B 302     3580   2260   4883   1302   -332   -865  B    N  
ATOM   5730  CA  GLU B 302       8.724  15.287 471.518  1.00 28.48      B    C  
ANISOU 5730  CA  GLU B 302     3602   2311   4908   1324   -353   -900  B    C  
ATOM   5731  C   GLU B 302       8.903  16.269 472.673  1.00 35.52      B    C  
ANISOU 5731  C   GLU B 302     4463   3270   5763   1376   -332   -951  B    C  
ATOM   5732  O   GLU B 302       9.226  15.860 473.798  1.00 30.87      B    O  
ANISOU 5732  O   GLU B 302     3842   2703   5184   1440   -378   -968  B    O  
ATOM   5733  CB  GLU B 302       9.964  15.313 470.629  1.00 28.09      B    C  
ANISOU 5733  CB  GLU B 302     3579   2251   4843   1257   -339   -948  B    C  
ATOM   5734  CG  GLU B 302      10.137  14.050 469.818  1.00 39.82      B    C  
ANISOU 5734  CG  GLU B 302     5073   3674   6380   1218   -372   -931  B    C  
ATOM   5735  CD  GLU B 302      11.180  14.160 468.706  1.00 43.38      B    C  
ANISOU 5735  CD  GLU B 302     5543   4118   6822   1140   -348   -998  B    C  
ATOM   5736  OE1 GLU B 302      11.655  15.273 468.398  1.00 39.15      B    O  
ANISOU 5736  OE1 GLU B 302     5027   3616   6232   1109   -305  -1044  B    O  
ATOM   5737  OE2 GLU B 302      11.429  13.129 468.045  1.00 57.66      B    O1-
ANISOU 5737  OE2 GLU B 302     7347   5878   8684   1105   -369  -1008  B    O1-
ATOM   5738  N   PHE B 303       8.685  17.575 472.420  1.00 49.98      B    N  
ANISOU 5738  N   PHE B 303     6303   5128   7559   1355   -269   -982  B    N  
ATOM   5739  CA  PHE B 303       8.766  18.556 473.498  1.00 28.89      B    C  
ANISOU 5739  CA  PHE B 303     3596   2519   4860   1397   -235  -1046  B    C  
ATOM   5740  C   PHE B 303       7.654  18.350 474.497  1.00 37.94      B    C  
ANISOU 5740  C   PHE B 303     4687   3694   6036   1470   -250  -1045  B    C  
ATOM   5741  O   PHE B 303       7.886  18.433 475.709  1.00 37.22      B    O  
ANISOU 5741  O   PHE B 303     4549   3661   5931   1527   -262  -1112  B    O  
ATOM   5742  CB  PHE B 303       8.711  19.974 472.918  1.00 42.98      B    C  
ANISOU 5742  CB  PHE B 303     5409   4300   6619   1358   -163  -1069  B    C  
ATOM   5743  CG  PHE B 303       8.889  21.072 473.947  1.00 33.92      B    C  
ANISOU 5743  CG  PHE B 303     4229   3211   5449   1386   -112  -1150  B    C  
ATOM   5744  CD1 PHE B 303       7.806  21.513 474.701  1.00 29.76      B    C  
ANISOU 5744  CD1 PHE B 303     3647   2714   4947   1437    -87  -1174  B    C  
ATOM   5745  CD2 PHE B 303      10.135  21.622 474.194  1.00 29.09      B    C  
ANISOU 5745  CD2 PHE B 303     3628   2631   4794   1359    -87  -1219  B    C  
ATOM   5746  CE1 PHE B 303       7.970  22.483 475.671  1.00 30.39      B    C  
ANISOU 5746  CE1 PHE B 303     3685   2853   5007   1456    -32  -1269  B    C  
ATOM   5747  CE2 PHE B 303      10.300  22.599 475.157  1.00 29.66      B    C  
ANISOU 5747  CE2 PHE B 303     3665   2761   4844   1379    -37  -1305  B    C  
ATOM   5748  CZ  PHE B 303       9.227  23.021 475.901  1.00 30.32      B    C  
ANISOU 5748  CZ  PHE B 303     3695   2874   4951   1425     -7  -1333  B    C  
ATOM   5749  N   ALA B 304       6.473  17.962 474.015  1.00 42.49      B    N  
ANISOU 5749  N   ALA B 304     5259   4234   6653   1473   -259   -984  B    N  
ATOM   5750  CA  ALA B 304       5.352  17.762 474.922  1.00 33.60      B    C  
ANISOU 5750  CA  ALA B 304     4066   3138   5563   1540   -269   -999  B    C  
ATOM   5751  C   ALA B 304       5.595  16.525 475.777  1.00 38.30      B    C  
ANISOU 5751  C   ALA B 304     4649   3729   6177   1597   -348   -984  B    C  
ATOM   5752  O   ALA B 304       5.282  16.505 476.969  1.00 35.71      B    O  
ANISOU 5752  O   ALA B 304     4260   3457   5850   1672   -365  -1046  B    O  
ATOM   5753  CB  ALA B 304       4.043  17.645 474.144  1.00 30.34      B    C  
ANISOU 5753  CB  ALA B 304     3640   2689   5200   1530   -268   -945  B    C  
ATOM   5754  N   ALA B 305       6.185  15.491 475.196  1.00 30.67      B    N  
ANISOU 5754  N   ALA B 305     3734   2693   5227   1567   -403   -912  B    N  
ATOM   5755  CA  ALA B 305       6.425  14.291 475.974  1.00 33.20      B    C  
ANISOU 5755  CA  ALA B 305     4055   2979   5582   1629   -499   -871  B    C  
ATOM   5756  C   ALA B 305       7.421  14.527 477.108  1.00 35.75      B    C  
ANISOU 5756  C   ALA B 305     4355   3362   5866   1699   -547   -939  B    C  
ATOM   5757  O   ALA B 305       7.117  14.237 478.273  1.00 45.89      B    O  
ANISOU 5757  O   ALA B 305     5605   4682   7150   1799   -617   -955  B    O  
ATOM   5758  CB  ALA B 305       6.892  13.152 475.068  1.00 31.20      B    C  
ANISOU 5758  CB  ALA B 305     3856   2631   5369   1575   -538   -787  B    C  
ATOM   5759  N   GLU B 306       8.589  15.105 476.816  1.00 31.62      B    N  
ANISOU 5759  N   GLU B 306     3845   2867   5304   1657   -517   -993  B    N  
ATOM   5760  CA  GLU B 306       9.501  15.418 477.914  1.00 34.15      B    C  
ANISOU 5760  CA  GLU B 306     4129   3262   5583   1729   -564  -1080  B    C  
ATOM   5761  C   GLU B 306       8.812  16.206 479.012  1.00 35.89      B    C  
ANISOU 5761  C   GLU B 306     4285   3592   5759   1798   -530  -1184  B    C  
ATOM   5762  O   GLU B 306       8.926  15.866 480.193  1.00 34.23      B    O  
ANISOU 5762  O   GLU B 306     4039   3463   5503   1885   -609  -1208  B    O  
ATOM   5763  CB  GLU B 306      10.696  16.232 477.409  1.00 44.12      B    C  
ANISOU 5763  CB  GLU B 306     5401   4555   6809   1659   -507  -1153  B    C  
ATOM   5764  CG  GLU B 306      11.511  15.564 476.313  1.00 58.05      B    C  
ANISOU 5764  CG  GLU B 306     7205   6243   8609   1591   -523  -1102  B    C  
ATOM   5765  CD  GLU B 306      12.095  14.238 476.721  1.00 68.36      B    C  
ANISOU 5765  CD  GLU B 306     8505   7494   9974   1654   -650  -1050  B    C  
ATOM   5766  OE1 GLU B 306      12.991  14.232 477.571  1.00 71.36      B    O  
ANISOU 5766  OE1 GLU B 306     8850   7919  10346   1725   -728  -1106  B    O  
ATOM   5767  OE2 GLU B 306      11.669  13.199 476.161  1.00 74.02      B    O1-
ANISOU 5767  OE2 GLU B 306     9253   8121  10752   1634   -676   -953  B    O1-
ATOM   5768  N   ARG B 307       7.946  17.138 478.624  1.00 43.42      B    N  
ANISOU 5768  N   ARG B 307     5221   4567   6709   1741   -414  -1217  B    N  
ATOM   5769  CA  ARG B 307       7.173  17.909 479.587  1.00 33.35      B    C  
ANISOU 5769  CA  ARG B 307     3863   3404   5406   1785   -350  -1339  B    C  
ATOM   5770  C   ARG B 307       6.269  17.002 480.407  1.00 44.95      B    C  
ANISOU 5770  C   ARG B 307     5303   4944   6833   1793   -392  -1270  B    C  
ATOM   5771  O   ARG B 307       6.199  17.123 481.632  1.00 59.29      B    O  
ANISOU 5771  O   ARG B 307     7080   6949   8500   1724   -361  -1280  B    O  
ATOM   5772  CB  ARG B 307       6.390  18.974 478.844  1.00 44.96      B    C  
ANISOU 5772  CB  ARG B 307     5329   4853   6899   1704   -233  -1338  B    C  
ATOM   5773  CG  ARG B 307       5.693  19.992 479.694  1.00 42.17      B    C  
ANISOU 5773  CG  ARG B 307     4881   4608   6532   1715   -135  -1476  B    C  
ATOM   5774  CD  ARG B 307       6.611  20.878 480.451  1.00 38.06      B    C  
ANISOU 5774  CD  ARG B 307     4333   4185   5941   1702    -84  -1605  B    C  
ATOM   5775  NE  ARG B 307       5.835  21.621 481.439  1.00 39.24      B    N  
ANISOU 5775  NE  ARG B 307     4370   4465   6073   1702     19  -1759  B    N  
ATOM   5776  CZ  ARG B 307       6.360  22.248 482.477  1.00 40.11      B    C  
ANISOU 5776  CZ  ARG B 307     4415   4722   6102   1689     82  -1919  B    C  
ATOM   5777  NH1 ARG B 307       7.672  22.225 482.674  1.00 41.00      B    N1+
ANISOU 5777  NH1 ARG B 307     4565   4865   6148   1694     35  -1943  B    N1+
ATOM   5778  NH2 ARG B 307       5.568  22.886 483.326  1.00 50.61      B    N  
ANISOU 5778  NH2 ARG B 307     5631   6185   7413   1656    199  -2067  B    N  
ATOM   5779  N   LEU B 308       5.547  16.099 479.745  1.00 46.67      B    N  
ANISOU 5779  N   LEU B 308     5558   5058   7115   1776   -433  -1141  B    N  
ATOM   5780  CA  LEU B 308       4.630  15.210 480.451  1.00 45.61      B    C  
ANISOU 5780  CA  LEU B 308     5427   5021   6884   1676   -439  -1003  B    C  
ATOM   5781  C   LEU B 308       5.362  14.324 481.449  1.00 46.74      B    C  
ANISOU 5781  C   LEU B 308     5620   5246   6892   1626   -532   -876  B    C  
ATOM   5782  O   LEU B 308       4.920  14.194 482.598  1.00 40.95      B    O  
ANISOU 5782  O   LEU B 308     4870   4694   5997   1521   -505   -830  B    O  
ATOM   5783  CB  LEU B 308       3.878  14.336 479.446  1.00 34.80      B    C  
ANISOU 5783  CB  LEU B 308     4096   3506   5621   1666   -471   -894  B    C  
ATOM   5784  CG  LEU B 308       2.768  13.451 480.013  1.00 40.62      B    C  
ANISOU 5784  CG  LEU B 308     4835   4325   6274   1550   -457   -766  B    C  
ATOM   5785  CD1 LEU B 308       1.814  14.270 480.806  1.00 59.49      B    C  
ANISOU 5785  CD1 LEU B 308     7128   6898   8578   1486   -339   -867  B    C  
ATOM   5786  CD2 LEU B 308       2.018  12.797 478.877  1.00 35.33      B    C  
ANISOU 5786  CD2 LEU B 308     4185   3512   5726   1545   -470   -703  B    C  
ATOM   5787  N   TRP B 309       6.520  13.768 481.056  1.00 36.10      B    N  
ANISOU 5787  N   TRP B 309     4329   3777   5610   1696   -644   -828  B    N  
ATOM   5788  CA  TRP B 309       7.308  12.946 481.976  1.00 43.85      B    C  
ANISOU 5788  CA  TRP B 309     5352   4820   6488   1671   -763   -697  B    C  
ATOM   5789  C   TRP B 309       7.835  13.779 483.135  1.00 55.19      B    C  
ANISOU 5789  C   TRP B 309     6737   6474   7760   1641   -735   -789  B    C  
ATOM   5790  O   TRP B 309       7.898  13.301 484.272  1.00 60.79      B    O  
ANISOU 5790  O   TRP B 309     7465   7334   8300   1555   -792   -672  B    O  
ATOM   5791  CB  TRP B 309       8.470  12.265 481.243  1.00 39.37      B    C  
ANISOU 5791  CB  TRP B 309     4827   4064   6066   1770   -886   -664  B    C  
ATOM   5792  CG  TRP B 309       8.125  11.643 479.902  1.00 35.92      B    C  
ANISOU 5792  CG  TRP B 309     4427   3409   5813   1800   -891   -637  B    C  
ATOM   5793  CD1 TRP B 309       8.958  11.517 478.841  1.00 34.99      B    C  
ANISOU 5793  CD1 TRP B 309     4317   3119   5859   1881   -929   -713  B    C  
ATOM   5794  CD2 TRP B 309       6.880  11.034 479.504  1.00 43.04      B    C  
ANISOU 5794  CD2 TRP B 309     5355   4256   6742   1730   -853   -540  B    C  
ATOM   5795  CE2 TRP B 309       7.038  10.598 478.178  1.00 41.01      B    C  
ANISOU 5795  CE2 TRP B 309     5120   3798   6663   1775   -871   -564  B    C  
ATOM   5796  CE3 TRP B 309       5.644  10.830 480.135  1.00 50.92      B    C  
ANISOU 5796  CE3 TRP B 309     6352   5369   7627   1621   -796   -453  B    C  
ATOM   5797  NE1 TRP B 309       8.310  10.920 477.794  1.00 34.37      B    N  
ANISOU 5797  NE1 TRP B 309     4272   2944   5843   1794   -872   -645  B    N  
ATOM   5798  CZ2 TRP B 309       6.010   9.963 477.469  1.00 46.43      B    C  
ANISOU 5798  CZ2 TRP B 309     5828   4398   7415   1718   -840   -496  B    C  
ATOM   5799  CZ3 TRP B 309       4.621  10.202 479.424  1.00 36.51      B    C  
ANISOU 5799  CZ3 TRP B 309     4545   3451   5874   1571   -765   -390  B    C  
ATOM   5800  CH2 TRP B 309       4.813   9.778 478.109  1.00 35.48      B    C  
ANISOU 5800  CH2 TRP B 309     4438   3124   5920   1622   -790   -409  B    C  
ATOM   5801  N   LEU B 310       8.231  15.023 482.868  1.00 51.60      B    N  
ANISOU 5801  N   LEU B 310     6222   6041   7345   1700   -649   -996  B    N  
ATOM   5802  CA  LEU B 310       8.618  15.896 483.964  1.00 43.32      B    C  
ANISOU 5802  CA  LEU B 310     5110   5209   6139   1655   -595  -1113  B    C  
ATOM   5803  C   LEU B 310       7.457  16.118 484.911  1.00 39.45      B    C  
ANISOU 5803  C   LEU B 310     4577   4914   5497   1520   -492  -1111  B    C  
ATOM   5804  O   LEU B 310       7.647  16.143 486.131  1.00 40.98      B    O  
ANISOU 5804  O   LEU B 310     4751   5325   5494   1421   -497  -1097  B    O  
ATOM   5805  CB  LEU B 310       9.128  17.230 483.428  1.00 49.30      B    C  
ANISOU 5805  CB  LEU B 310     5814   5931   6989   1732   -498  -1347  B    C  
ATOM   5806  CG  LEU B 310       9.495  18.219 484.529  1.00 45.18      B    C  
ANISOU 5806  CG  LEU B 310     5215   5633   6317   1677   -417  -1503  B    C  
ATOM   5807  CD1 LEU B 310      10.521  17.561 485.425  1.00 53.71      B    C  
ANISOU 5807  CD1 LEU B 310     6312   6843   7252   1650   -553  -1408  B    C  
ATOM   5808  CD2 LEU B 310      10.048  19.504 483.944  1.00 43.59      B    C  
ANISOU 5808  CD2 LEU B 310     4975   5365   6224   1750   -321  -1731  B    C  
ATOM   5809  N   ILE B 311       6.237  16.211 484.379  1.00 45.02      B    N  
ANISOU 5809  N   ILE B 311     5264   5556   6285   1503   -404  -1123  B    N  
ATOM   5810  CA  ILE B 311       5.087  16.476 485.239  1.00 46.30      B    C  
ANISOU 5810  CA  ILE B 311     5362   5906   6323   1370   -289  -1161  B    C  
ATOM   5811  C   ILE B 311       4.813  15.258 486.102  1.00 51.42      B    C  
ANISOU 5811  C   ILE B 311     6077   6663   6796   1234   -367   -947  B    C  
ATOM   5812  O   ILE B 311       4.532  15.376 487.301  1.00 55.35      B    O  
ANISOU 5812  O   ILE B 311     6544   7397   7090   1088   -316   -960  B    O  
ATOM   5813  CB  ILE B 311       3.848  16.890 484.422  1.00 48.11      B    C  
ANISOU 5813  CB  ILE B 311     5537   6039   6705   1396   -186  -1237  B    C  
ATOM   5814  CG1 ILE B 311       4.016  18.312 483.876  1.00 45.94      B    C  
ANISOU 5814  CG1 ILE B 311     5187   5700   6570   1500    -92  -1457  B    C  
ATOM   5815  CG2 ILE B 311       2.584  16.780 485.259  1.00 51.04      B    C  
ANISOU 5815  CG2 ILE B 311     5845   6589   6957   1245    -87  -1243  B    C  
ATOM   5816  CD1 ILE B 311       2.992  18.700 482.832  1.00 47.43      B    C  
ANISOU 5816  CD1 ILE B 311     5333   5742   6945   1564    -39  -1504  B    C  
ATOM   5817  N   HIS B 312       4.907  14.070 485.510  1.00 45.85      B    N  
ANISOU 5817  N   HIS B 312     5469   5787   6166   1267   -490   -751  B    N  
ATOM   5818  CA  HIS B 312       4.760  12.845 486.281  1.00 45.51      B    C  
ANISOU 5818  CA  HIS B 312     5512   5807   5973   1144   -586   -521  B    C  
ATOM   5819  C   HIS B 312       5.827  12.754 487.364  1.00 48.04      B    C  
ANISOU 5819  C   HIS B 312     5857   6281   6116   1105   -688   -458  B    C  
ATOM   5820  O   HIS B 312       5.528  12.451 488.524  1.00 50.58      B    O  
ANISOU 5820  O   HIS B 312     6199   6808   6211    939   -693   -365  B    O  
ATOM   5821  CB  HIS B 312       4.771  11.655 485.333  1.00 46.00      B    C  
ANISOU 5821  CB  HIS B 312     5666   5620   6193   1206   -694   -348  B    C  
ATOM   5822  CG  HIS B 312       3.564  11.619 484.450  1.00 47.53      B    C  
ANISOU 5822  CG  HIS B 312     5835   5715   6510   1198   -597   -387  B    C  
ATOM   5823  CD2 HIS B 312       2.386  12.289 484.535  1.00 45.85      B    C  
ANISOU 5823  CD2 HIS B 312     5535   5613   6273   1131   -449   -512  B    C  
ATOM   5824  ND1 HIS B 312       3.448  10.777 483.365  1.00 54.63      B    N  
ANISOU 5824  ND1 HIS B 312     6790   6388   7578   1256   -655   -294  B    N  
ATOM   5825  CE1 HIS B 312       2.266  10.957 482.796  1.00 57.14      B    C  
ANISOU 5825  CE1 HIS B 312     7061   6691   7960   1224   -552   -355  B    C  
ATOM   5826  NE2 HIS B 312       1.599  11.861 483.493  1.00 54.10      B    N  
ANISOU 5826  NE2 HIS B 312     6585   6502   7467   1156   -432   -485  B    N  
ATOM   5827  N   SER B 313       7.073  13.036 487.010  1.00 53.53      B    N  
ANISOU 5827  N   SER B 313     6545   6895   6900   1243   -771   -515  B    N  
ATOM   5828  CA  SER B 313       8.160  12.925 487.975  1.00 51.09      B    C  
ANISOU 5828  CA  SER B 313     6246   6729   6436   1222   -891   -456  B    C  
ATOM   5829  C   SER B 313       7.976  13.874 489.155  1.00 56.68      B    C  
ANISOU 5829  C   SER B 313     6877   7747   6913   1085   -777   -594  B    C  
ATOM   5830  O   SER B 313       8.253  13.505 490.300  1.00 71.31      B    O  
ANISOU 5830  O   SER B 313     8757   9798   8538    960   -857   -475  B    O  
ATOM   5831  CB  SER B 313       9.488  13.197 487.288  1.00 49.03      B    C  
ANISOU 5831  CB  SER B 313     5964   6332   6334   1398   -973   -547  B    C  
ATOM   5832  OG  SER B 313      10.537  12.626 488.024  1.00 53.35      B    O  
ANISOU 5832  OG  SER B 313     6538   6950   6784   1403  -1150   -417  B    O  
ATOM   5833  N   ARG B 314       7.466  15.084 488.908  1.00 58.15      B    N  
ANISOU 5833  N   ARG B 314     6964   7978   7152   1093   -590   -843  B    N  
ATOM   5834  CA  ARG B 314       7.232  16.017 490.007  1.00 53.67      B    C  
ANISOU 5834  CA  ARG B 314     6307   7698   6388    954   -456  -1010  B    C  
ATOM   5835  C   ARG B 314       6.082  15.560 490.887  1.00 55.20      B    C  
ANISOU 5835  C   ARG B 314     6512   8075   6389    742   -393   -922  B    C  
ATOM   5836  O   ARG B 314       6.032  15.893 492.077  1.00 59.63      B    O  
ANISOU 5836  O   ARG B 314     7029   8917   6709    570   -336   -979  B    O  
ATOM   5837  CB  ARG B 314       6.968  17.401 489.416  1.00 53.99      B    C  
ANISOU 5837  CB  ARG B 314     6238   7690   6587   1035   -276  -1299  B    C  
ATOM   5838  CG  ARG B 314       8.263  18.133 489.127  1.00 58.83      B    C  
ANISOU 5838  CG  ARG B 314     6822   8259   7271   1159   -303  -1439  B    C  
ATOM   5839  CD  ARG B 314       8.132  19.380 488.264  1.00 66.13      B    C  
ANISOU 5839  CD  ARG B 314     7676   9051   8401   1268   -157  -1682  B    C  
ATOM   5840  NE  ARG B 314       9.425  20.073 488.243  1.00 79.05      B    N  
ANISOU 5840  NE  ARG B 314     9286  10698  10050   1340   -171  -1823  B    N  
ATOM   5841  CZ  ARG B 314       9.776  21.033 487.392  1.00 66.14      B    C  
ANISOU 5841  CZ  ARG B 314     7625   8912   8594   1451    -93  -2003  B    C  
ATOM   5842  NH1 ARG B 314       8.933  21.435 486.450  1.00 64.18      B    N1+
ANISOU 5842  NH1 ARG B 314     7373   8478   8533   1515    -11  -2050  B    N1+
ATOM   5843  NH2 ARG B 314      10.978  21.588 487.488  1.00 64.79      B    N  
ANISOU 5843  NH2 ARG B 314     7431   8779   8407   1489   -103  -2132  B    N  
ATOM   5844  N   ASN B 315       5.159  14.790 490.329  1.00 54.14      B    N  
ANISOU 5844  N   ASN B 315     6432   7797   6343    732   -396   -793  B    N  
ATOM   5845  CA  ASN B 315       4.082  14.242 491.134  1.00 57.97      B    C  
ANISOU 5845  CA  ASN B 315     6938   8448   6641    515   -339   -700  B    C  
ATOM   5846  C   ASN B 315       4.614  13.213 492.129  1.00 62.52      B    C  
ANISOU 5846  C   ASN B 315     7631   9149   6976    380   -505   -437  B    C  
ATOM   5847  O   ASN B 315       4.170  13.159 493.286  1.00 64.91      B    O  
ANISOU 5847  O   ASN B 315     7933   9718   7011    151   -453   -415  B    O  
ATOM   5848  CB  ASN B 315       3.068  13.589 490.209  1.00 59.20      B    C  
ANISOU 5848  CB  ASN B 315     7128   8401   6963    546   -318   -618  B    C  
ATOM   5849  CG  ASN B 315       2.212  14.589 489.490  1.00 61.40      B    C  
ANISOU 5849  CG  ASN B 315     7280   8625   7425    618   -145   -862  B    C  
ATOM   5850  ND2 ASN B 315       1.542  14.133 488.434  1.00 59.67      B    N  
ANISOU 5850  ND2 ASN B 315     7080   8198   7391    694   -150   -807  B    N  
ATOM   5851  OD1 ASN B 315       2.189  15.771 489.836  1.00 71.58      B    O  
ANISOU 5851  OD1 ASN B 315     8450  10045   8703    612    -15  -1100  B    O  
ATOM   5852  N   VAL B 316       5.587  12.401 491.695  1.00 62.21      B    N  
ANISOU 5852  N   VAL B 316     7689   8918   7029    514   -710   -240  B    N  
ATOM   5853  CA  VAL B 316       6.263  11.470 492.595  1.00 63.91      B    C  
ANISOU 5853  CA  VAL B 316     8012   9222   7049    423   -906     23  B    C  
ATOM   5854  C   VAL B 316       6.977  12.201 493.721  1.00 73.82      B    C  
ANISOU 5854  C   VAL B 316     9206  10777   8064    329   -910    -71  B    C  
ATOM   5855  O   VAL B 316       6.875  11.808 494.890  1.00 93.50      B    O  
ANISOU 5855  O   VAL B 316    11751  13505  10269    118   -961     70  B    O  
ATOM   5856  CB  VAL B 316       7.229  10.566 491.810  1.00 59.60      B    C  
ANISOU 5856  CB  VAL B 316     7549   8385   6710    621  -1121    207  B    C  
ATOM   5857  CG1 VAL B 316       7.979   9.644 492.758  1.00 60.50      B    C  
ANISOU 5857  CG1 VAL B 316     7765   8576   6648    548  -1349    487  B    C  
ATOM   5858  CG2 VAL B 316       6.478   9.782 490.747  1.00 57.68      B    C  
ANISOU 5858  CG2 VAL B 316     7367   7864   6684    681  -1108    297  B    C  
ATOM   5859  N   GLU B 317       7.687  13.284 493.407  1.00 67.42      B    N  
ANISOU 5859  N   GLU B 317     8287   9977   7353    463   -850   -315  B    N  
ATOM   5860  CA  GLU B 317       8.341  14.033 494.474  1.00 72.04      B    C  
ANISOU 5860  CA  GLU B 317     8801  10864   7708    361   -834   -435  B    C  
ATOM   5861  C   GLU B 317       7.321  14.574 495.473  1.00 75.72      B    C  
ANISOU 5861  C   GLU B 317     9206  11634   7930    101   -638   -565  B    C  
ATOM   5862  O   GLU B 317       7.499  14.443 496.689  1.00 81.10      B    O  
ANISOU 5862  O   GLU B 317     9904  12605   8305   -104   -681   -491  B    O  
ATOM   5863  CB  GLU B 317       9.189  15.165 493.896  1.00 81.47      B    C  
ANISOU 5863  CB  GLU B 317     9885  12002   9069    539   -770   -704  B    C  
ATOM   5864  CG  GLU B 317      10.383  14.712 493.057  1.00 91.85      B    C  
ANISOU 5864  CG  GLU B 317    11239  13070  10590    768   -960   -615  B    C  
ATOM   5865  CD  GLU B 317      11.146  15.884 492.436  1.00 98.81      B    C  
ANISOU 5865  CD  GLU B 317    12017  13897  11630    918   -869   -901  B    C  
ATOM   5866  OE1 GLU B 317      10.624  16.523 491.498  1.00 96.08      B    O  
ANISOU 5866  OE1 GLU B 317    11634  13386  11485   1005   -718  -1069  B    O  
ATOM   5867  OE2 GLU B 317      12.282  16.159 492.890  1.00100.31      B    O1-
ANISOU 5867  OE2 GLU B 317    12165  14209  11738    943   -956   -952  B    O1-
ATOM   5868  N   ARG B 318       6.236  15.176 494.979  1.00 72.74      B    N  
ANISOU 5868  N   ARG B 318     8751  11204   7685     98   -425   -763  B    N  
ATOM   5869  CA  ARG B 318       5.227  15.711 495.889  1.00 75.26      B    C  
ANISOU 5869  CA  ARG B 318     8986  11805   7804   -147   -222   -927  B    C  
ATOM   5870  C   ARG B 318       4.656  14.613 496.787  1.00 83.99      B    C  
ANISOU 5870  C   ARG B 318    10206  13072   8635   -400   -291   -671  B    C  
ATOM   5871  O   ARG B 318       4.443  14.820 497.996  1.00 85.17      B    O  
ANISOU 5871  O   ARG B 318    10328  13554   8480   -659   -218   -720  B    O  
ATOM   5872  CB  ARG B 318       4.121  16.397 495.086  1.00 72.29      B    C  
ANISOU 5872  CB  ARG B 318     8505  11297   7666    -78    -14  -1156  B    C  
ATOM   5873  CG  ARG B 318       3.447  17.562 495.803  1.00 84.23      B    C  
ANISOU 5873  CG  ARG B 318     9851  13062   9089   -235    236  -1482  B    C  
ATOM   5874  CD  ARG B 318       2.751  18.519 494.823  1.00 97.16      B    C  
ANISOU 5874  CD  ARG B 318    11362  14510  11046    -72    405  -1740  B    C  
ATOM   5875  NE  ARG B 318       3.674  19.154 493.874  1.00103.92      B    N  
ANISOU 5875  NE  ARG B 318    12207  15137  12142    187    354  -1818  B    N  
ATOM   5876  CZ  ARG B 318       3.653  18.962 492.554  1.00 95.96      B    C  
ANISOU 5876  CZ  ARG B 318    11244  13810  11406    404    286  -1746  B    C  
ATOM   5877  NH1 ARG B 318       2.745  18.154 492.016  1.00 99.03      B    N1+
ANISOU 5877  NH1 ARG B 318    11685  14070  11874    405    259  -1599  B    N1+
ATOM   5878  NH2 ARG B 318       4.533  19.582 491.768  1.00 76.27      B    N  
ANISOU 5878  NH2 ARG B 318     8744  11137   9097    603    251  -1830  B    N  
ATOM   5879  N   TYR B 319       4.431  13.426 496.216  1.00 77.01      B    N  
ANISOU 5879  N   TYR B 319     9457  11956   7847   -342   -429   -396  B    N  
ATOM   5880  CA  TYR B 319       3.899  12.310 496.992  1.00 72.38      B    C  
ANISOU 5880  CA  TYR B 319     9003  11481   7016   -580   -504   -125  B    C  
ATOM   5881  C   TYR B 319       4.883  11.836 498.051  1.00 74.61      B    C  
ANISOU 5881  C   TYR B 319     9379  11953   7017   -697   -705     96  B    C  
ATOM   5882  O   TYR B 319       4.481  11.490 499.167  1.00 74.32      B    O  
ANISOU 5882  O   TYR B 319     9399  12184   6655   -988   -697    204  B    O  
ATOM   5883  CB  TYR B 319       3.533  11.154 496.076  1.00 66.44      B    C  
ANISOU 5883  CB  TYR B 319     8374  10407   6461   -475   -610    113  B    C  
ATOM   5884  CG  TYR B 319       3.010   9.952 496.816  1.00 66.26      B    C  
ANISOU 5884  CG  TYR B 319     8508  10462   6207   -719   -692    410  B    C  
ATOM   5885  CD1 TYR B 319       1.710   9.928 497.303  1.00 67.36      B    C  
ANISOU 5885  CD1 TYR B 319     8630  10777   6189   -975   -507    338  B    C  
ATOM   5886  CD2 TYR B 319       3.809   8.834 497.012  1.00 65.28      B    C  
ANISOU 5886  CD2 TYR B 319     8548  10222   6035   -695   -956    759  B    C  
ATOM   5887  CE1 TYR B 319       1.225   8.828 497.971  1.00 69.29      B    C  
ANISOU 5887  CE1 TYR B 319     9029  11089   6209  -1220   -573    611  B    C  
ATOM   5888  CE2 TYR B 319       3.331   7.732 497.677  1.00 67.59      B    C  
ANISOU 5888  CE2 TYR B 319     9000  10562   6120   -923  -1038   1048  B    C  
ATOM   5889  CZ  TYR B 319       2.042   7.736 498.155  1.00 69.27      B    C  
ANISOU 5889  CZ  TYR B 319     9206  10957   6155  -1195   -841    976  B    C  
ATOM   5890  OH  TYR B 319       1.560   6.639 498.817  1.00 74.58      B    O  
ANISOU 5890  OH  TYR B 319    10051  11678   6610  -1445   -914   1265  B    O  
ATOM   5891  N   MET B 320       6.172  11.794 497.719  1.00 75.04      B    N  
ANISOU 5891  N   MET B 320     9448  11879   7185   -484   -893    168  B    N  
ATOM   5892  CA  MET B 320       7.169  11.399 498.710  1.00 77.56      B    C  
ANISOU 5892  CA  MET B 320     9834  12383   7251   -573  -1106    372  B    C  
ATOM   5893  C   MET B 320       7.276  12.419 499.841  1.00 79.01      B    C  
ANISOU 5893  C   MET B 320     9906  12977   7136   -783   -977    151  B    C  
ATOM   5894  O   MET B 320       7.520  12.041 500.995  1.00 82.22      B    O  
ANISOU 5894  O   MET B 320    10380  13653   7206  -1010  -1088    324  B    O  
ATOM   5895  CB  MET B 320       8.517  11.184 498.029  1.00 79.03      B    C  
ANISOU 5895  CB  MET B 320    10028  12334   7663   -281  -1325    454  B    C  
ATOM   5896  CG  MET B 320       8.596   9.887 497.242  1.00 83.63      B    C  
ANISOU 5896  CG  MET B 320    10748  12559   8468   -131  -1514    748  B    C  
ATOM   5897  SD  MET B 320      10.248   9.549 496.609  1.00100.90      B    S  
ANISOU 5897  SD  MET B 320    12930  14505  10904    182  -1784    839  B    S  
ATOM   5898  CE  MET B 320      10.478  10.891 495.440  1.00100.65      B    C  
ANISOU 5898  CE  MET B 320    12730  14355  11159    407  -1576    422  B    C  
ATOM   5899  N   VAL B 321       7.120  13.713 499.532  1.00 83.55      B    N  
ANISOU 5899  N   VAL B 321    10313  13603   7828   -719   -748   -228  B    N  
ATOM   5900  CA  VAL B 321       7.030  14.723 500.592  1.00 87.70      B    C  
ANISOU 5900  CA  VAL B 321    10716  14517   8089   -946   -575   -484  B    C  
ATOM   5901  C   VAL B 321       5.841  14.436 501.502  1.00 81.42      B    C  
ANISOU 5901  C   VAL B 321     9950  13976   7011  -1289   -442   -458  B    C  
ATOM   5902  O   VAL B 321       5.940  14.561 502.729  1.00 87.05      B    O  
ANISOU 5902  O   VAL B 321    10657  15055   7363  -1568   -430   -461  B    O  
ATOM   5903  CB  VAL B 321       6.964  16.143 500.003  1.00 82.18      B    C  
ANISOU 5903  CB  VAL B 321     9833  13771   7618   -804   -339   -899  B    C  
ATOM   5904  CG1 VAL B 321       6.587  17.152 501.091  1.00 82.02      B    C  
ANISOU 5904  CG1 VAL B 321     9675  14139   7349  -1070   -111  -1197  B    C  
ATOM   5905  CG2 VAL B 321       8.297  16.508 499.398  1.00 76.89      B    C  
ANISOU 5905  CG2 VAL B 321     9136  12948   7133   -539   -466   -941  B    C  
ATOM   5906  N   THR B 322       4.694  14.071 500.922  1.00 75.74      B    N  
ANISOU 5906  N   THR B 322     9254  13085   6437  -1293   -333   -449  B    N  
ATOM   5907  CA  THR B 322       3.552  13.708 501.763  1.00 77.55      B    C  
ANISOU 5907  CA  THR B 322     9516  13551   6399  -1633   -207   -421  B    C  
ATOM   5908  C   THR B 322       3.897  12.509 502.644  1.00 79.60      B    C  
ANISOU 5908  C   THR B 322     9974  13938   6334  -1840   -442    -18  B    C  
ATOM   5909  O   THR B 322       3.503  12.455 503.816  1.00 82.93      B    O  
ANISOU 5909  O   THR B 322    10416  14710   6385  -2190   -378     -6  B    O  
ATOM   5910  CB  THR B 322       2.298  13.429 500.938  1.00 81.73      B    C  
ANISOU 5910  CB  THR B 322    10037  13863   7153  -1591    -70   -465  B    C  
ATOM   5911  CG2 THR B 322       1.774  14.711 500.316  1.00 76.74      B    C  
ANISOU 5911  CG2 THR B 322     9194  13179   6784  -1457    182   -879  B    C  
ATOM   5912  OG1 THR B 322       2.583  12.460 499.923  1.00 97.89      B    O  
ANISOU 5912  OG1 THR B 322    12219  15534   9441  -1353   -269   -187  B    O  
ATOM   5913  N   VAL B 323       4.556  11.498 502.074  1.00 78.58      B    N  
ANISOU 5913  N   VAL B 323     9994  13516   6346  -1642   -711    318  B    N  
ATOM   5914  CA  VAL B 323       4.951  10.335 502.865  1.00 78.33      B    C  
ANISOU 5914  CA  VAL B 323    10158  13560   6043  -1809   -967    731  B    C  
ATOM   5915  C   VAL B 323       5.857  10.749 504.029  1.00 82.46      B    C  
ANISOU 5915  C   VAL B 323    10656  14445   6231  -1967  -1065    737  B    C  
ATOM   5916  O   VAL B 323       5.697  10.252 505.148  1.00 91.26      B    O  
ANISOU 5916  O   VAL B 323    11877  15835   6962  -2287  -1135    936  B    O  
ATOM   5917  CB  VAL B 323       5.609   9.279 501.959  1.00 75.87      B    C  
ANISOU 5917  CB  VAL B 323     9981  12835   6012  -1522  -1238   1047  B    C  
ATOM   5918  CG1 VAL B 323       6.405   8.296 502.769  1.00 78.94      B    C  
ANISOU 5918  CG1 VAL B 323    10538  13287   6169  -1618  -1551   1451  B    C  
ATOM   5919  CG2 VAL B 323       4.559   8.569 501.169  1.00 74.62      B    C  
ANISOU 5919  CG2 VAL B 323     9897  12406   6050  -1498  -1161   1125  B    C  
ATOM   5920  N   GLN B 324       6.797  11.683 503.813  1.00 85.10      B    N  
ANISOU 5920  N   GLN B 324    10848  14804   6681  -1771  -1063    513  B    N  
ATOM   5921  CA  GLN B 324       7.661  12.064 504.935  1.00 91.70      B    C  
ANISOU 5921  CA  GLN B 324    11651  16005   7185  -1934  -1158    513  B    C  
ATOM   5922  C   GLN B 324       6.895  12.882 505.963  1.00 93.30      B    C  
ANISOU 5922  C   GLN B 324    11750  16638   7061  -2298   -884    234  B    C  
ATOM   5923  O   GLN B 324       7.174  12.789 507.166  1.00109.43      B    O  
ANISOU 5923  O   GLN B 324    13832  19048   8699  -2588   -960    335  B    O  
ATOM   5924  CB  GLN B 324       8.875  12.892 504.500  1.00102.28      B    C  
ANISOU 5924  CB  GLN B 324    12857  17291   8716  -1658  -1209    316  B    C  
ATOM   5925  CG  GLN B 324       9.981  12.233 503.691  1.00114.16      B    C  
ANISOU 5925  CG  GLN B 324    14426  18456  10495  -1318  -1500    546  B    C  
ATOM   5926  CD  GLN B 324      10.881  13.287 503.036  1.00116.90      B    C  
ANISOU 5926  CD  GLN B 324    14606  18725  11085  -1054  -1440    234  B    C  
ATOM   5927  NE2 GLN B 324      12.099  12.897 502.663  1.00116.02      B    N  
ANISOU 5927  NE2 GLN B 324    14512  18448  11122   -815  -1699    382  B    N  
ATOM   5928  OE1 GLN B 324      10.485  14.447 502.903  1.00116.64      B    O  
ANISOU 5928  OE1 GLN B 324    14428  18786  11106  -1076  -1162   -142  B    O  
ATOM   5929  N   ALA B 325       5.892  13.644 505.525  1.00 82.44      B    N  
ANISOU 5929  N   ALA B 325    10242  15230   5852  -2303   -571   -112  B    N  
ATOM   5930  CA  ALA B 325       5.078  14.367 506.493  1.00 85.34      B    C  
ANISOU 5930  CA  ALA B 325    10496  15994   5935  -2659   -295   -398  B    C  
ATOM   5931  C   ALA B 325       4.267  13.392 507.330  1.00 94.36      B    C  
ANISOU 5931  C   ALA B 325    11796  17324   6733  -3025   -321   -141  B    C  
ATOM   5932  O   ALA B 325       4.061  13.609 508.532  1.00 95.14      B    O  
ANISOU 5932  O   ALA B 325    11875  17845   6427  -3401   -233   -211  B    O  
ATOM   5933  CB  ALA B 325       4.158  15.362 505.785  1.00 81.07      B    C  
ANISOU 5933  CB  ALA B 325     9768  15340   5696  -2557     30   -820  B    C  
ATOM   5934  N   ALA B 326       3.813  12.304 506.707  1.00 90.06      B    N  
ANISOU 5934  N   ALA B 326    11411  16474   6335  -2936   -439    154  B    N  
ATOM   5935  CA  ALA B 326       3.132  11.248 507.444  1.00 88.21      B    C  
ANISOU 5935  CA  ALA B 326    11360  16373   5784  -3274   -496    451  B    C  
ATOM   5936  C   ALA B 326       4.062  10.558 508.434  1.00 99.01      B    C  
ANISOU 5936  C   ALA B 326    12893  17941   6784  -3444   -798    828  B    C  
ATOM   5937  O   ALA B 326       3.651  10.258 509.557  1.00112.53      B    O  
ANISOU 5937  O   ALA B 326    14690  19997   8069  -3854   -775    932  B    O  
ATOM   5938  CB  ALA B 326       2.547  10.225 506.477  1.00 86.68      B    C  
ANISOU 5938  CB  ALA B 326    11300  15770   5863  -3112   -568    686  B    C  
ATOM   5939  N   ARG B 327       5.281  10.195 508.012  1.00 96.65      B    N  
ANISOU 5939  N   ARG B 327    12655  17417   6649  -3141  -1099   1064  B    N  
ATOM   5940  CA  ARG B 327       6.174   9.513 508.947  1.00 99.86      B    C  
ANISOU 5940  CA  ARG B 327    13212  18004   6726  -3285  -1416   1441  B    C  
ATOM   5941  C   ARG B 327       6.572  10.424 510.111  1.00105.46      B    C  
ANISOU 5941  C   ARG B 327    13803  19221   7046  -3558  -1337   1230  B    C  
ATOM   5942  O   ARG B 327       6.777   9.947 511.242  1.00108.92      B    O  
ANISOU 5942  O   ARG B 327    14365  19970   7049  -3878  -1494   1488  B    O  
ATOM   5943  CB  ARG B 327       7.398   8.995 508.191  1.00 95.16      B    C  
ANISOU 5943  CB  ARG B 327    12669  17050   6437  -2878  -1743   1688  B    C  
ATOM   5944  CG  ARG B 327       7.003   8.022 507.082  1.00 92.66      B    C  
ANISOU 5944  CG  ARG B 327    12474  16244   6489  -2641  -1820   1900  B    C  
ATOM   5945  CD  ARG B 327       8.144   7.233 506.472  1.00 96.13      B    C  
ANISOU 5945  CD  ARG B 327    12998  16331   7196  -2299  -2170   2208  B    C  
ATOM   5946  NE  ARG B 327       8.988   6.543 507.435  1.00106.21      B    N  
ANISOU 5946  NE  ARG B 327    14408  17762   8186  -2421  -2507   2591  B    N  
ATOM   5947  CZ  ARG B 327      10.268   6.252 507.232  1.00106.92      B    C  
ANISOU 5947  CZ  ARG B 327    14493  17699   8431  -2151  -2813   2764  B    C  
ATOM   5948  NH1 ARG B 327      10.853   6.597 506.093  1.00104.20      B    N1+
ANISOU 5948  NH1 ARG B 327    14023  17051   8518  -1759  -2805   2573  B    N1+
ATOM   5949  NH2 ARG B 327      10.949   5.577 508.144  1.00109.51      B    N  
ANISOU 5949  NH2 ARG B 327    14946  18169   8492  -2275  -3134   3137  B    N  
ATOM   5950  N   GLU B 328       6.625  11.742 509.876  1.00108.93      B    N  
ANISOU 5950  N   GLU B 328    14006  19760   7621  -3463  -1083    758  B    N  
ATOM   5951  CA  GLU B 328       6.900  12.661 510.980  1.00116.45      B    C  
ANISOU 5951  CA  GLU B 328    14829  21206   8211  -3749   -961    505  B    C  
ATOM   5952  C   GLU B 328       5.690  12.809 511.882  1.00115.83      B    C  
ANISOU 5952  C   GLU B 328    14740  21486   7784  -4217   -690    350  B    C  
ATOM   5953  O   GLU B 328       5.823  12.908 513.106  1.00117.96      B    O  
ANISOU 5953  O   GLU B 328    15019  22181   7620  -4583   -695    369  B    O  
ATOM   5954  CB  GLU B 328       7.305  14.045 510.474  1.00120.57      B    C  
ANISOU 5954  CB  GLU B 328    15102  21714   8996  -3521   -754     32  B    C  
ATOM   5955  CG  GLU B 328       7.671  14.999 511.623  1.00132.06      B    C  
ANISOU 5955  CG  GLU B 328    16413  23679  10083  -3818   -628   -244  B    C  
ATOM   5956  CD  GLU B 328       8.288  16.307 511.151  1.00137.55      B    C  
ANISOU 5956  CD  GLU B 328    16882  24343  11038  -3578   -469   -669  B    C  
ATOM   5957  OE1 GLU B 328       8.196  16.611 509.937  1.00129.21      B    O  
ANISOU 5957  OE1 GLU B 328    15765  22888  10442  -3220   -392   -808  B    O  
ATOM   5958  OE2 GLU B 328       8.864  17.027 512.000  1.00145.35      B    O1-
ANISOU 5958  OE2 GLU B 328    17757  25710  11758  -3764   -421   -863  B    O1-
ATOM   5959  N   GLN B 329       4.500  12.815 511.284  1.00116.53      B    N  
ANISOU 5959  N   GLN B 329    14797  21392   8088  -4206   -450    187  B    N  
ATOM   5960  CA  GLN B 329       3.268  12.846 512.054  1.00118.01      B    C  
ANISOU 5960  CA  GLN B 329    14973  21887   7980  -4645   -189     39  B    C  
ATOM   5961  C   GLN B 329       3.178  11.628 512.966  1.00109.76      B    C  
ANISOU 5961  C   GLN B 329    14187  21017   6500  -4995   -407    504  B    C  
ATOM   5962  O   GLN B 329       2.878  11.749 514.162  1.00118.48      B    O  
ANISOU 5962  O   GLN B 329    15249  22399   7371  -5356   -301    441  B    O  
ATOM   5963  CB  GLN B 329       2.110  12.887 511.050  1.00126.40      B    C  
ANISOU 5963  CB  GLN B 329    15969  22636   9422  -4490     39   -152  B    C  
ATOM   5964  CG  GLN B 329       0.715  12.930 511.582  1.00134.64      B    C  
ANISOU 5964  CG  GLN B 329    16968  23917  10272  -4876    336   -356  B    C  
ATOM   5965  CD  GLN B 329       0.346  14.278 512.163  1.00137.63      B    C  
ANISOU 5965  CD  GLN B 329    17080  24653  10560  -5076    681   -901  B    C  
ATOM   5966  NE2 GLN B 329       0.358  15.303 511.310  1.00129.25      B    N  
ANISOU 5966  NE2 GLN B 329    15804  23384   9922  -4745    846  -1269  B    N  
ATOM   5967  OE1 GLN B 329       0.030  14.400 513.353  1.00135.33      B    O  
ANISOU 5967  OE1 GLN B 329    16739  24669  10011  -5458    784   -979  B    O  
ATOM   5968  N   LEU B 330       3.447  10.443 512.410  1.00103.42      B    N  
ANISOU 5968  N   LEU B 330    13601  19852   5844  -4796   -702    961  B    N  
ATOM   5969  CA  LEU B 330       3.492   9.224 513.206  1.00107.28      B    C  
ANISOU 5969  CA  LEU B 330    14342  20388   6030  -5054   -950   1447  B    C  
ATOM   5970  C   LEU B 330       4.478   9.370 514.359  1.00116.39      B    C  
ANISOU 5970  C   LEU B 330    15474  21776   6972  -5179  -1117   1550  B    C  
ATOM   5971  O   LEU B 330       4.174   9.010 515.500  1.00125.71      B    O  
ANISOU 5971  O   LEU B 330    16716  23160   7887  -5541  -1109   1667  B    O  
ATOM   5972  CB  LEU B 330       3.848   8.018 512.326  1.00105.97      B    C  
ANISOU 5972  CB  LEU B 330    14395  19771   6098  -4758  -1270   1908  B    C  
ATOM   5973  CG  LEU B 330       3.532   6.589 512.810  1.00109.35      B    C  
ANISOU 5973  CG  LEU B 330    15103  20082   6364  -4971  -1474   2404  B    C  
ATOM   5974  CD1 LEU B 330       3.653   5.592 511.683  1.00107.19      B    C  
ANISOU 5974  CD1 LEU B 330    14988  19307   6431  -4641  -1689   2730  B    C  
ATOM   5975  CD2 LEU B 330       4.407   6.126 513.964  1.00120.57      B    C  
ANISOU 5975  CD2 LEU B 330    16613  21616   7581  -5100  -1742   2707  B    C  
ATOM   5976  N   SER B 331       5.679   9.891 514.073  1.00109.12      B    N  
ANISOU 5976  N   SER B 331    14460  20835   6163  -4889  -1274   1503  B    N  
ATOM   5977  CA  SER B 331       6.672  10.047 515.135  1.00114.16      B    C  
ANISOU 5977  CA  SER B 331    15066  21700   6608  -4991  -1436   1594  B    C  
ATOM   5978  C   SER B 331       6.237  11.029 516.233  1.00124.72      B    C  
ANISOU 5978  C   SER B 331    16211  23455   7721  -5362  -1123   1206  B    C  
ATOM   5979  O   SER B 331       6.538  10.810 517.414  1.00124.90      B    O  
ANISOU 5979  O   SER B 331    16269  23708   7479  -5636  -1217   1357  B    O  
ATOM   5980  CB  SER B 331       8.006  10.469 514.514  1.00114.41      B    C  
ANISOU 5980  CB  SER B 331    15012  21619   6838  -4593  -1639   1570  B    C  
ATOM   5981  OG  SER B 331       8.967  10.781 515.506  1.00122.49      B    O  
ANISOU 5981  OG  SER B 331    15967  22888   7683  -4685  -1757   1589  B    O  
ATOM   5982  N   THR B 332       5.556  12.126 515.871  1.00123.62      B    N  
ANISOU 5982  N   THR B 332    15857  23408   7705  -5372   -756    701  B    N  
ATOM   5983  CA  THR B 332       5.063  13.073 516.881  1.00121.20      B    C  
ANISOU 5983  CA  THR B 332    15342  23461   7247  -5721   -443    306  B    C  
ATOM   5984  C   THR B 332       3.949  12.482 517.737  1.00121.81      B    C  
ANISOU 5984  C   THR B 332    15501  23687   7095  -6158   -329    390  B    C  
ATOM   5985  O   THR B 332       3.878  12.758 518.940  1.00133.80      B    O  
ANISOU 5985  O   THR B 332    16939  25523   8374  -6516   -245    299  B    O  
ATOM   5986  CB  THR B 332       4.617  14.394 516.250  1.00118.95      B    C  
ANISOU 5986  CB  THR B 332    14792  23182   7222  -5589    -86   -262  B    C  
ATOM   5987  CG2 THR B 332       4.484  15.493 517.320  1.00114.11      B    C  
ANISOU 5987  CG2 THR B 332    13930  22918   6508  -5889    182   -667  B    C  
ATOM   5988  OG1 THR B 332       5.584  14.810 515.275  1.00123.56      B    O  
ANISOU 5988  OG1 THR B 332    15334  23574   8041  -5163   -206   -313  B    O  
ATOM   5989  N   THR B 333       3.057  11.690 517.141  1.00117.31      B    N  
ANISOU 5989  N   THR B 333    15079  22899   6595  -6151   -314    545  B    N  
ATOM   5990  CA  THR B 333       1.978  11.095 517.929  1.00123.90      B    C  
ANISOU 5990  CA  THR B 333    15994  23865   7218  -6574   -205    616  B    C  
ATOM   5991  C   THR B 333       2.496  10.065 518.923  1.00135.97      B    C  
ANISOU 5991  C   THR B 333    17742  25468   8453  -6796   -512   1098  B    C  
ATOM   5992  O   THR B 333       2.046  10.033 520.075  1.00147.57      B    O  
ANISOU 5992  O   THR B 333    19191  27221   9660  -7222   -418   1057  B    O  
ATOM   5993  CB  THR B 333       0.934  10.452 517.018  1.00125.03      B    C  
ANISOU 5993  CB  THR B 333    16249  23743   7515  -6505   -123    676  B    C  
ATOM   5994  CG2 THR B 333      -0.189   9.832 517.841  1.00122.46      B    C  
ANISOU 5994  CG2 THR B 333    16002  23555   6974  -6955     -6    730  B    C  
ATOM   5995  OG1 THR B 333       0.388  11.443 516.142  1.00130.72      B    O  
ANISOU 5995  OG1 THR B 333    16750  24407   8511  -6314    175    207  B    O  
ATOM   5996  N   ALA B 334       3.424   9.206 518.503  1.00124.83      B    N  
ANISOU 5996  N   ALA B 334    16535  23797   7099  -6517   -883   1551  B    N  
ATOM   5997  CA  ALA B 334       3.932   8.175 519.404  1.00134.35      B    C  
ANISOU 5997  CA  ALA B 334    17953  25026   8068  -6692  -1195   2027  B    C  
ATOM   5998  C   ALA B 334       4.598   8.759 520.653  1.00137.68      B    C  
ANISOU 5998  C   ALA B 334    18255  25828   8229  -6934  -1212   1939  B    C  
ATOM   5999  O   ALA B 334       4.497   8.171 521.738  1.00137.78      B    O  
ANISOU 5999  O   ALA B 334    18380  26012   7958  -7284  -1309   2169  B    O  
ATOM   6000  CB  ALA B 334       4.913   7.284 518.646  1.00127.88      B    C  
ANISOU 6000  CB  ALA B 334    17325  23826   7437  -6283  -1590   2476  B    C  
ATOM   6001  N   ASP B 335       5.264   9.912 520.527  1.00142.71      B    N  
ANISOU 6001  N   ASP B 335    18664  26603   8955  -6770  -1112   1602  B    N  
ATOM   6002  CA  ASP B 335       5.923  10.536 521.676  1.00148.95      B    C  
ANISOU 6002  CA  ASP B 335    19320  27760   9513  -6995  -1110   1490  B    C  
ATOM   6003  C   ASP B 335       4.915  11.127 522.661  1.00153.65      B    C  
ANISOU 6003  C   ASP B 335    19759  28717   9902  -7487   -769   1143  B    C  
ATOM   6004  O   ASP B 335       5.150  11.119 523.877  1.00152.27      B    O  
ANISOU 6004  O   ASP B 335    19571  28850   9434  -7830   -814   1208  B    O  
ATOM   6005  CB  ASP B 335       6.909  11.607 521.192  1.00149.03      B    C  
ANISOU 6005  CB  ASP B 335    19127  27789   9709  -6668  -1085   1210  B    C  
ATOM   6006  CG  ASP B 335       8.145  11.016 520.503  1.00149.97      B    C  
ANISOU 6006  CG  ASP B 335    19381  27619   9983  -6233  -1476   1571  B    C  
ATOM   6007  OD1 ASP B 335       8.499   9.855 520.801  1.00154.01      B    O  
ANISOU 6007  OD1 ASP B 335    20119  28003  10394  -6240  -1803   2058  B    O  
ATOM   6008  OD2 ASP B 335       8.739  11.700 519.636  1.00143.21      B    O1-
ANISOU 6008  OD2 ASP B 335    18398  26642   9374  -5878  -1457   1359  B    O1-
ATOM   6009  N   ASP B 336       3.791  11.657 522.159  1.00155.45      B    N  
ANISOU 6009  N   ASP B 336    19856  28917  10292  -7529   -431    760  B    N  
ATOM   6010  CA  ASP B 336       2.785  12.243 523.046  1.00156.29      B    C  
ANISOU 6010  CA  ASP B 336    19786  29344  10253  -7983   -103    389  B    C  
ATOM   6011  C   ASP B 336       1.986  11.166 523.771  1.00154.42      B    C  
ANISOU 6011  C   ASP B 336    19748  29169   9754  -8380   -163    674  B    C  
ATOM   6012  O   ASP B 336       1.622  11.338 524.940  1.00156.92      B    O  
ANISOU 6012  O   ASP B 336    19990  29821   9810  -8833    -52    558  B    O  
ATOM   6013  CB  ASP B 336       1.838  13.161 522.262  1.00154.93      B    C  
ANISOU 6013  CB  ASP B 336    19391  29096  10380  -7877    265   -127  B    C  
ATOM   6014  CG  ASP B 336       2.349  14.597 522.157  1.00152.52      B    C  
ANISOU 6014  CG  ASP B 336    18788  28906  10255  -7724    455   -585  B    C  
ATOM   6015  OD1 ASP B 336       2.336  15.317 523.183  1.00144.74      B    O  
ANISOU 6015  OD1 ASP B 336    17614  28253   9129  -8042    610   -852  B    O  
ATOM   6016  OD2 ASP B 336       2.744  15.009 521.041  1.00153.49      B    O1-
ANISOU 6016  OD2 ASP B 336    18867  28782  10672  -7294    455   -688  B    O1-
ATOM   6017  N   LYS B 337       1.695  10.057 523.098  1.00150.64      B    N  
ANISOU 6017  N   LYS B 337    19520  28370   9346  -8232   -332   1035  B    N  
ATOM   6018  CA  LYS B 337       0.903   8.989 523.694  1.00151.09      B    C  
ANISOU 6018  CA  LYS B 337    19781  28442   9182  -8592   -386   1308  B    C  
ATOM   6019  C   LYS B 337       1.706   7.699 523.809  1.00151.27      B    C  
ANISOU 6019  C   LYS B 337    20116  28262   9098  -8490   -816   1937  B    C  
ATOM   6020  O   LYS B 337       1.138   6.606 523.809  1.00151.33      B    O  
ANISOU 6020  O   LYS B 337    20351  28101   9045  -8614   -917   2246  B    O  
ATOM   6021  CB  LYS B 337      -0.359   8.744 522.871  1.00149.28      B    C  
ANISOU 6021  CB  LYS B 337    19572  28009   9141  -8567   -175   1159  B    C  
ATOM   6022  CG  LYS B 337      -1.076  10.017 522.465  1.00148.39      B    C  
ANISOU 6022  CG  LYS B 337    19144  27996   9242  -8535    218    542  B    C  
ATOM   6023  CD  LYS B 337      -2.197   9.720 521.483  1.00146.86      B    C  
ANISOU 6023  CD  LYS B 337    18978  27553   9271  -8428    385    435  B    C  
ATOM   6024  CE  LYS B 337      -2.978  10.978 521.137  1.00140.28      B    C  
ANISOU 6024  CE  LYS B 337    17818  26810   8673  -8403    772   -189  B    C  
ATOM   6025  NZ  LYS B 337      -4.244  10.670 520.412  1.00134.72      B    N1+
ANISOU 6025  NZ  LYS B 337    17119  25928   8141  -8396    959   -326  B    N1+
ATOM   6026  N   SER B 340      -0.240   1.328 520.476  1.00144.01      B    N  
ANISOU 6026  N   SER B 340    20524  25367   8827  -7892  -1610   3839  B    N  
ATOM   6027  CA  SER B 340       0.107   1.544 519.070  1.00141.79      B    C  
ANISOU 6027  CA  SER B 340    20191  24768   8916  -7396  -1634   3788  B    C  
ATOM   6028  C   SER B 340      -1.148   1.619 518.195  1.00139.07      B    C  
ANISOU 6028  C   SER B 340    19801  24310   8729  -7407  -1331   3527  B    C  
ATOM   6029  O   SER B 340      -1.189   2.330 517.175  1.00130.56      B    O  
ANISOU 6029  O   SER B 340    18569  23146   7889  -7115  -1186   3255  B    O  
ATOM   6030  CB  SER B 340       1.033   0.431 518.571  1.00139.63      B    C  
ANISOU 6030  CB  SER B 340    20142  24062   8850  -7051  -2038   4305  B    C  
ATOM   6031  OG  SER B 340       0.340  -0.796 518.445  1.00140.28      B    O  
ANISOU 6031  OG  SER B 340    20458  23873   8967  -7165  -2097   4600  B    O  
ATOM   6032  N   HIS B 341      -2.180   0.872 518.594  1.00144.69      B    N  
ANISOU 6032  N   HIS B 341    20646  25023   9305  -7750  -1236   3607  B    N  
ATOM   6033  CA  HIS B 341      -3.480   1.043 517.957  1.00142.04      B    C  
ANISOU 6033  CA  HIS B 341    20232  24663   9075  -7835   -906   3294  B    C  
ATOM   6034  C   HIS B 341      -4.008   2.458 518.168  1.00140.57      B    C  
ANISOU 6034  C   HIS B 341    19727  24851   8832  -7973   -544   2703  B    C  
ATOM   6035  O   HIS B 341      -4.724   2.989 517.306  1.00130.89      B    O  
ANISOU 6035  O   HIS B 341    18350  23575   7807  -7849   -285   2366  B    O  
ATOM   6036  CB  HIS B 341      -4.469   0.003 518.489  1.00140.76      B    C  
ANISOU 6036  CB  HIS B 341    20261  24473   8748  -8218   -871   3465  B    C  
ATOM   6037  CG  HIS B 341      -3.931  -1.399 518.507  1.00144.17      B    C  
ANISOU 6037  CG  HIS B 341    21004  24559   9214  -8131  -1231   4044  B    C  
ATOM   6038  CD2 HIS B 341      -3.340  -2.114 519.493  1.00149.46      B    C  
ANISOU 6038  CD2 HIS B 341    21855  25258   9676  -8302  -1505   4419  B    C  
ATOM   6039  ND1 HIS B 341      -3.990  -2.237 517.413  1.00145.52      B    N  
ANISOU 6039  ND1 HIS B 341    21327  24281   9684  -7837  -1338   4285  B    N  
ATOM   6040  CE1 HIS B 341      -3.454  -3.404 517.723  1.00147.92      B    C  
ANISOU 6040  CE1 HIS B 341    21883  24336   9983  -7817  -1658   4770  B    C  
ATOM   6041  NE2 HIS B 341      -3.052  -3.357 518.980  1.00149.33      B    N  
ANISOU 6041  NE2 HIS B 341    22088  24799   9853  -8093  -1769   4867  B    N  
ATOM   6042  N   GLU B 342      -3.652   3.085 519.301  1.00142.80      B    N  
ANISOU 6042  N   GLU B 342    19894  25500   8865  -8223   -523   2565  B    N  
ATOM   6043  CA  GLU B 342      -3.931   4.505 519.489  1.00140.04      B    C  
ANISOU 6043  CA  GLU B 342    19219  25473   8516  -8297   -209   2002  B    C  
ATOM   6044  C   GLU B 342      -3.344   5.317 518.346  1.00150.42      B    C  
ANISOU 6044  C   GLU B 342    20382  26634  10136  -7816   -181   1815  B    C  
ATOM   6045  O   GLU B 342      -3.972   6.256 517.841  1.00150.46      B    O  
ANISOU 6045  O   GLU B 342    20151  26712  10305  -7751    124   1349  B    O  
ATOM   6046  CB  GLU B 342      -3.289   4.988 520.792  1.00140.04      B    C  
ANISOU 6046  CB  GLU B 342    19140  25836   8234  -8560   -269   1967  B    C  
ATOM   6047  CG  GLU B 342      -3.971   4.633 522.089  1.00148.22      B    C  
ANISOU 6047  CG  GLU B 342    20224  27159   8933  -9115   -200   1970  B    C  
ATOM   6048  CD  GLU B 342      -3.105   5.018 523.276  1.00151.55      B    C  
ANISOU 6048  CD  GLU B 342    20593  27900   9088  -9318   -322   2017  B    C  
ATOM   6049  OE1 GLU B 342      -1.921   5.357 523.057  1.00147.61      B    O  
ANISOU 6049  OE1 GLU B 342    20066  27351   8670  -9002   -507   2127  B    O  
ATOM   6050  OE2 GLU B 342      -3.603   4.979 524.420  1.00161.48      B    O1-
ANISOU 6050  OE2 GLU B 342    21836  29464  10055  -9800   -235   1940  B    O1-
ATOM   6051  N   ILE B 343      -2.121   4.968 517.943  1.00152.55      B    N  
ANISOU 6051  N   ILE B 343    20779  26686  10497  -7473   -507   2168  B    N  
ATOM   6052  CA  ILE B 343      -1.426   5.654 516.859  1.00135.03      B    C  
ANISOU 6052  CA  ILE B 343    18442  24309   8556  -7011   -529   2035  B    C  
ATOM   6053  C   ILE B 343      -2.164   5.445 515.541  1.00132.56      B    C  
ANISOU 6053  C   ILE B 343    18146  23701   8518  -6786   -404   1965  B    C  
ATOM   6054  O   ILE B 343      -2.313   6.369 514.729  1.00129.35      B    O  
ANISOU 6054  O   ILE B 343    17542  23288   8317  -6561   -204   1599  B    O  
ATOM   6055  CB  ILE B 343       0.027   5.152 516.793  1.00131.13      B    C  
ANISOU 6055  CB  ILE B 343    18095  23630   8098  -6724   -941   2464  B    C  
ATOM   6056  CG1 ILE B 343       0.800   5.660 518.011  1.00132.11      B    C  
ANISOU 6056  CG1 ILE B 343    18134  24093   7971  -6912  -1016   2429  B    C  
ATOM   6057  CG2 ILE B 343       0.715   5.642 515.515  1.00129.19      B    C  
ANISOU 6057  CG2 ILE B 343    17767  23153   8166  -6229  -1004   2380  B    C  
ATOM   6058  CD1 ILE B 343       2.098   4.951 518.214  1.00131.70      B    C  
ANISOU 6058  CD1 ILE B 343    18248  23885   7906  -6719  -1436   2894  B    C  
ATOM   6059  N   VAL B 344      -2.619   4.210 515.307  1.00135.31      B    N  
ANISOU 6059  N   VAL B 344    18735  23794   8885  -6842   -523   2320  B    N  
ATOM   6060  CA  VAL B 344      -3.388   3.863 514.108  1.00125.94      B    C  
ANISOU 6060  CA  VAL B 344    17586  22324   7943  -6673   -408   2292  B    C  
ATOM   6061  C   VAL B 344      -4.688   4.668 513.983  1.00121.55      B    C  
ANISOU 6061  C   VAL B 344    16798  21970   7416  -6853     21   1762  B    C  
ATOM   6062  O   VAL B 344      -5.004   5.192 512.909  1.00113.38      B    O  
ANISOU 6062  O   VAL B 344    15632  20821   6628  -6601    187   1512  B    O  
ATOM   6063  CB  VAL B 344      -3.670   2.344 514.120  1.00127.20      B    C  
ANISOU 6063  CB  VAL B 344    18045  22198   8086  -6774   -605   2766  B    C  
ATOM   6064  CG1 VAL B 344      -4.605   1.949 513.007  1.00117.92      B    C  
ANISOU 6064  CG1 VAL B 344    16903  20764   7137  -6675   -450   2718  B    C  
ATOM   6065  CG2 VAL B 344      -2.373   1.547 514.047  1.00127.45      B    C  
ANISOU 6065  CG2 VAL B 344    18278  21951   8196  -6511  -1035   3269  B    C  
ATOM   6066  N   ILE B 345      -5.427   4.825 515.087  1.00131.94      B    N  
ANISOU 6066  N   ILE B 345    18040  23592   8498  -7283    203   1564  B    N  
ATOM   6067  CA  ILE B 345      -6.699   5.567 515.113  1.00128.40      B    C  
ANISOU 6067  CA  ILE B 345    17347  23340   8097  -7480    600   1040  B    C  
ATOM   6068  C   ILE B 345      -6.595   7.069 514.817  1.00122.55      B    C  
ANISOU 6068  C   ILE B 345    16278  22756   7529  -7295    831    522  B    C  
ATOM   6069  O   ILE B 345      -7.504   7.645 514.205  1.00117.96      B    O  
ANISOU 6069  O   ILE B 345    15497  22162   7159  -7233   1116    126  B    O  
ATOM   6070  CB  ILE B 345      -7.394   5.313 516.463  1.00134.29      B    C  
ANISOU 6070  CB  ILE B 345    18106  24375   8542  -8002    690    983  B    C  
ATOM   6071  CG1 ILE B 345      -8.107   3.960 516.434  1.00139.21      B    C  
ANISOU 6071  CG1 ILE B 345    18987  24812   9095  -8191    617   1309  B    C  
ATOM   6072  CG2 ILE B 345      -8.400   6.402 516.772  1.00132.47      B    C  
ANISOU 6072  CG2 ILE B 345    17552  24423   8356  -8203   1070    371  B    C  
ATOM   6073  CD1 ILE B 345      -8.523   3.457 517.808  1.00142.83      B    C  
ANISOU 6073  CD1 ILE B 345    19541  25516   9212  -8699    604   1393  B    C  
ATOM   6074  N   GLU B 346      -5.499   7.721 515.187  1.00125.05      B    N  
ANISOU 6074  N   GLU B 346    16525  23196   7792  -7180    712    507  B    N  
ATOM   6075  CA  GLU B 346      -5.409   9.174 515.031  1.00121.31      B    C  
ANISOU 6075  CA  GLU B 346    15733  22873   7485  -7038    941     -4  B    C  
ATOM   6076  C   GLU B 346      -5.223   9.616 513.590  1.00119.98      B    C  
ANISOU 6076  C   GLU B 346    15489  22447   7652  -6576    984   -131  B    C  
ATOM   6077  O   GLU B 346      -5.682  10.702 513.214  1.00108.83      B    O  
ANISOU 6077  O   GLU B 346    13801  21083   6465  -6466   1257   -615  B    O  
ATOM   6078  CB  GLU B 346      -4.253   9.727 515.860  1.00122.42      B    C  
ANISOU 6078  CB  GLU B 346    15825  23221   7469  -7060    802     19  B    C  
ATOM   6079  CG  GLU B 346      -4.614  10.013 517.297  1.00140.97      B    C  
ANISOU 6079  CG  GLU B 346    18072  25932   9557  -7525    921   -155  B    C  
ATOM   6080  CD  GLU B 346      -5.578  11.176 517.436  1.00143.48      B    C  
ANISOU 6080  CD  GLU B 346    18058  26429  10030  -7651   1303   -773  B    C  
ATOM   6081  OE1 GLU B 346      -5.722  11.951 516.461  1.00140.11      B    O  
ANISOU 6081  OE1 GLU B 346    17454  25855   9929  -7326   1459  -1081  B    O  
ATOM   6082  OE2 GLU B 346      -6.186  11.310 518.524  1.00143.03      B    O1-
ANISOU 6082  OE2 GLU B 346    17913  26648   9785  -8073   1435   -952  B    O1-
ATOM   6083  N   HIS B 347      -4.527   8.825 512.788  1.00117.51      B    N  
ANISOU 6083  N   HIS B 347    15403  21850   7397  -6298    707    288  B    N  
ATOM   6084  CA  HIS B 347      -4.040   9.268 511.499  1.00108.09      B    C  
ANISOU 6084  CA  HIS B 347    14115  20326   6629  -5786    660    200  B    C  
ATOM   6085  C   HIS B 347      -4.632   8.517 510.320  1.00105.27      B    C  
ANISOU 6085  C   HIS B 347    13830  19517   6651  -5526    627    340  B    C  
ATOM   6086  O   HIS B 347      -4.271   8.820 509.180  1.00106.94      B    O  
ANISOU 6086  O   HIS B 347    13951  19370   7310  -5067    570    273  B    O  
ATOM   6087  CB  HIS B 347      -2.521   9.131 511.487  1.00110.76      B    C  
ANISOU 6087  CB  HIS B 347    14563  20554   6966  -5534    313    511  B    C  
ATOM   6088  CG  HIS B 347      -1.873   9.949 512.550  1.00118.21      B    C  
ANISOU 6088  CG  HIS B 347    15411  21935   7569  -5752    343    346  B    C  
ATOM   6089  CD2 HIS B 347      -1.240   9.576 513.686  1.00121.71      B    C  
ANISOU 6089  CD2 HIS B 347    15956  22547   7740  -5973    147    603  B    C  
ATOM   6090  ND1 HIS B 347      -1.875  11.325 512.544  1.00119.42      B    N  
ANISOU 6090  ND1 HIS B 347    15276  22252   7847  -5681    595   -164  B    N  
ATOM   6091  CE1 HIS B 347      -1.273  11.766 513.634  1.00119.05      B    C  
ANISOU 6091  CE1 HIS B 347    15157  22463   7615  -5862    558   -214  B    C  
ATOM   6092  NE2 HIS B 347      -0.860  10.725 514.333  1.00124.35      B    N  
ANISOU 6092  NE2 HIS B 347    16061  23153   8032  -6038    284    248  B    N  
ATOM   6093  N   ALA B 348      -5.557   7.581 510.547  1.00106.67      B    N  
ANISOU 6093  N   ALA B 348    14160  19711   6660  -5822    677    509  B    N  
ATOM   6094  CA  ALA B 348      -5.959   6.672 509.479  1.00107.32      B    C  
ANISOU 6094  CA  ALA B 348    14357  19354   7065  -5590    590    724  B    C  
ATOM   6095  C   ALA B 348      -6.746   7.368 508.374  1.00100.41      B    C  
ANISOU 6095  C   ALA B 348    13228  18278   6643  -5308    826    317  B    C  
ATOM   6096  O   ALA B 348      -6.693   6.922 507.223  1.00 95.91      B    O  
ANISOU 6096  O   ALA B 348    12699  17293   6448  -4959    715    449  B    O  
ATOM   6097  CB  ALA B 348      -6.789   5.530 510.066  1.00110.89      B    C  
ANISOU 6097  CB  ALA B 348    15035  19899   7200  -6016    607    986  B    C  
ATOM   6098  N   ALA B 349      -7.468   8.448 508.673  1.00104.22      B    N  
ANISOU 6098  N   ALA B 349    13445  19039   7116  -5446   1143   -176  B    N  
ATOM   6099  CA  ALA B 349      -8.107   9.183 507.585  1.00105.06      B    C  
ANISOU 6099  CA  ALA B 349    13300  18933   7685  -5132   1329   -547  B    C  
ATOM   6100  C   ALA B 349      -7.059   9.775 506.652  1.00112.46      B    C  
ANISOU 6100  C   ALA B 349    14168  19568   8996  -4625   1169   -553  B    C  
ATOM   6101  O   ALA B 349      -7.228   9.770 505.426  1.00120.25      B    O  
ANISOU 6101  O   ALA B 349    15097  20195  10396  -4270   1145   -582  B    O  
ATOM   6102  CB  ALA B 349      -9.012  10.286 508.132  1.00109.43      B    C  
ANISOU 6102  CB  ALA B 349    13563  19834   8180  -5364   1688  -1088  B    C  
ATOM   6103  N   ASP B 350      -5.969  10.295 507.221  1.00113.18      B    N  
ANISOU 6103  N   ASP B 350    14257  19814   8932  -4604   1062   -533  B    N  
ATOM   6104  CA  ASP B 350      -4.827  10.725 506.421  1.00102.03      B    C  
ANISOU 6104  CA  ASP B 350    12817  18126   7825  -4156    880   -487  B    C  
ATOM   6105  C   ASP B 350      -4.184   9.558 505.674  1.00 94.16      B    C  
ANISOU 6105  C   ASP B 350    12060  16741   6978  -3909    564    -20  B    C  
ATOM   6106  O   ASP B 350      -3.810   9.698 504.503  1.00 92.31      B    O  
ANISOU 6106  O   ASP B 350    11782  16152   7142  -3503    482    -26  B    O  
ATOM   6107  CB  ASP B 350      -3.819  11.416 507.335  1.00117.70      B    C  
ANISOU 6107  CB  ASP B 350    14762  20404   9552  -4249    831   -550  B    C  
ATOM   6108  CG  ASP B 350      -4.318  12.769 507.834  1.00127.06      B    C  
ANISOU 6108  CG  ASP B 350    15666  21903  10707  -4396   1155  -1080  B    C  
ATOM   6109  OD1 ASP B 350      -5.200  12.775 508.730  1.00128.31      B    O  
ANISOU 6109  OD1 ASP B 350    15780  22400  10571  -4812   1362  -1239  B    O  
ATOM   6110  OD2 ASP B 350      -3.826  13.815 507.347  1.00123.97      B    O1-
ANISOU 6110  OD2 ASP B 350    15099  21418  10587  -4111   1207  -1343  B    O1-
ATOM   6111  N   TRP B 351      -3.988   8.415 506.351  1.00 94.31      B    N  
ANISOU 6111  N   TRP B 351    12332  16819   6682  -4153    378    390  B    N  
ATOM   6112  CA  TRP B 351      -3.369   7.263 505.692  1.00 93.15      B    C  
ANISOU 6112  CA  TRP B 351    12409  16290   6693  -3927     76    833  B    C  
ATOM   6113  C   TRP B 351      -4.198   6.723 504.536  1.00102.05      B    C  
ANISOU 6113  C   TRP B 351    13542  17067   8163  -3754    137    837  B    C  
ATOM   6114  O   TRP B 351      -3.632   6.210 503.564  1.00108.39      B    O  
ANISOU 6114  O   TRP B 351    14425  17489   9270  -3422    -55   1037  B    O  
ATOM   6115  CB  TRP B 351      -3.044   6.118 506.657  1.00 92.98      B    C  
ANISOU 6115  CB  TRP B 351    12666  16378   6283  -4228   -145   1289  B    C  
ATOM   6116  CG  TRP B 351      -2.058   6.450 507.740  1.00 95.31      B    C  
ANISOU 6116  CG  TRP B 351    12992  16985   6234  -4374   -283   1379  B    C  
ATOM   6117  CD1 TRP B 351      -1.280   7.571 507.834  1.00 94.08      B    C  
ANISOU 6117  CD1 TRP B 351    12656  16970   6121  -4217   -260   1123  B    C  
ATOM   6118  CD2 TRP B 351      -1.594   5.563 508.756  1.00 99.14      B    C  
ANISOU 6118  CD2 TRP B 351    13721  17625   6323  -4656   -519   1801  B    C  
ATOM   6119  CE2 TRP B 351      -0.611   6.248 509.492  1.00101.65      B    C  
ANISOU 6119  CE2 TRP B 351    13974  18221   6427  -4684   -612   1753  B    C  
ATOM   6120  CE3 TRP B 351      -1.953   4.274 509.149  1.00102.01      B    C  
ANISOU 6120  CE3 TRP B 351    14354  17930   6478  -4909   -653   2211  B    C  
ATOM   6121  NE1 TRP B 351      -0.445   7.480 508.916  1.00 97.04      B    N  
ANISOU 6121  NE1 TRP B 351    13127  17627   6119  -4419   -439   1323  B    N  
ATOM   6122  CZ2 TRP B 351       0.018   5.684 510.597  1.00108.19      B    C  
ANISOU 6122  CZ2 TRP B 351    14991  19283   6836  -4952   -849   2110  B    C  
ATOM   6123  CZ3 TRP B 351      -1.330   3.716 510.240  1.00105.89      B    C  
ANISOU 6123  CZ3 TRP B 351    15043  18629   6560  -5173   -889   2577  B    C  
ATOM   6124  CH2 TRP B 351      -0.354   4.418 510.953  1.00114.65      B    C  
ANISOU 6124  CH2 TRP B 351    16078  20028   7457  -5191   -993   2529  B    C  
ATOM   6125  N   CYS B 352      -5.527   6.809 504.612  1.00103.41      B    N  
ANISOU 6125  N   CYS B 352    13625  17369   8295  -3980    401    609  B    N  
ATOM   6126  CA  CYS B 352      -6.337   6.312 503.505  1.00 95.23      B    C  
ANISOU 6126  CA  CYS B 352    12581  16022   7579  -3823    459    599  B    C  
ATOM   6127  C   CYS B 352      -6.058   7.117 502.249  1.00 95.14      B    C  
ANISOU 6127  C   CYS B 352    12384  15742   8024  -3371    475    369  B    C  
ATOM   6128  O   CYS B 352      -6.025   6.565 501.142  1.00100.29      B    O  
ANISOU 6128  O   CYS B 352    13090  16032   8983  -3108    373    502  B    O  
ATOM   6129  CB  CYS B 352      -7.815   6.322 503.874  1.00 97.74      B    C  
ANISOU 6129  CB  CYS B 352    12810  16563   7761  -4161    746    364  B    C  
ATOM   6130  SG  CYS B 352      -8.233   4.904 504.918  1.00101.70      B    S  
ANISOU 6130  SG  CYS B 352    13615  17214   7811  -4653    681    756  B    S  
ATOM   6131  N   LYS B 353      -5.830   8.420 502.404  1.00 89.75      B    N  
ANISOU 6131  N   LYS B 353    11487  15230   7385  -3288    602     26  B    N  
ATOM   6132  CA  LYS B 353      -5.409   9.224 501.268  1.00 86.60      B    C  
ANISOU 6132  CA  LYS B 353    10936  14576   7393  -2866    592   -161  B    C  
ATOM   6133  C   LYS B 353      -4.002   8.823 500.849  1.00 86.64      B    C  
ANISOU 6133  C   LYS B 353    11085  14332   7500  -2591    297    137  B    C  
ATOM   6134  O   LYS B 353      -3.740   8.593 499.661  1.00 83.85      B    O  
ANISOU 6134  O   LYS B 353    10747  13628   7485  -2272    196    207  B    O  
ATOM   6135  CB  LYS B 353      -5.472  10.717 501.595  1.00 85.84      B    C  
ANISOU 6135  CB  LYS B 353    10584  14712   7318  -2859    799   -594  B    C  
ATOM   6136  CG  LYS B 353      -6.855  11.239 501.924  1.00 91.25      B    C  
ANISOU 6136  CG  LYS B 353    11078  15624   7970  -3090   1104   -950  B    C  
ATOM   6137  CD  LYS B 353      -6.813  12.727 502.241  1.00 96.74      B    C  
ANISOU 6137  CD  LYS B 353    11518  16515   8722  -3061   1297  -1379  B    C  
ATOM   6138  CE  LYS B 353      -8.157  13.220 502.730  1.00100.11      B    C  
ANISOU 6138  CE  LYS B 353    11740  17200   9096  -3326   1602  -1749  B    C  
ATOM   6139  NZ  LYS B 353      -9.216  13.085 501.668  1.00 93.04      B    N1+
ANISOU 6139  NZ  LYS B 353    10746  16069   8536  -3165   1683  -1852  B    N1+
ATOM   6140  N   LEU B 354      -3.075   8.764 501.814  1.00 86.40      B    N  
ANISOU 6140  N   LEU B 354    11150  14495   7183  -2716    157    298  B    N  
ATOM   6141  CA  LEU B 354      -1.704   8.354 501.516  1.00 81.23      B    C  
ANISOU 6141  CA  LEU B 354    10620  13629   6616  -2469   -135    578  B    C  
ATOM   6142  C   LEU B 354      -1.632   7.069 500.696  1.00 80.77      B    C  
ANISOU 6142  C   LEU B 354    10745  13192   6754  -2320   -327    920  B    C  
ATOM   6143  O   LEU B 354      -0.789   6.952 499.798  1.00 84.77      B    O  
ANISOU 6143  O   LEU B 354    11267  13398   7545  -1988   -489   1004  B    O  
ATOM   6144  CB  LEU B 354      -0.909   8.181 502.806  1.00 81.33      B    C  
ANISOU 6144  CB  LEU B 354    10740  13927   6234  -2697   -282    773  B    C  
ATOM   6145  CG  LEU B 354       0.579   8.265 502.489  1.00 80.65      B    C  
ANISOU 6145  CG  LEU B 354    10679  13680   6283  -2395   -533    906  B    C  
ATOM   6146  CD1 LEU B 354       0.895   9.606 501.843  1.00 76.33      B    C  
ANISOU 6146  CD1 LEU B 354     9906  13100   5995  -2132   -395    520  B    C  
ATOM   6147  CD2 LEU B 354       1.413   8.036 503.724  1.00 86.88      B    C  
ANISOU 6147  CD2 LEU B 354    11574  14745   6693  -2602   -715   1126  B    C  
ATOM   6148  N   PHE B 355      -2.509   6.102 500.963  1.00 78.31      B    N  
ANISOU 6148  N   PHE B 355    10568  12883   6304  -2568   -298   1100  B    N  
ATOM   6149  CA  PHE B 355      -2.391   4.807 500.307  1.00 80.33      B    C  
ANISOU 6149  CA  PHE B 355    11014  12785   6723  -2459   -486   1442  B    C  
ATOM   6150  C   PHE B 355      -3.487   4.566 499.295  1.00 81.12      B    C  
ANISOU 6150  C   PHE B 355    11059  12681   7081  -2395   -328   1317  B    C  
ATOM   6151  O   PHE B 355      -3.479   3.516 498.641  1.00 80.46      B    O  
ANISOU 6151  O   PHE B 355    11116  12289   7166  -2303   -453   1561  B    O  
ATOM   6152  CB  PHE B 355      -2.470   3.652 501.307  1.00 89.19      B    C  
ANISOU 6152  CB  PHE B 355    12380  14000   7510  -2785   -618   1821  B    C  
ATOM   6153  CG  PHE B 355      -1.410   3.651 502.351  1.00 98.00      B    C  
ANISOU 6153  CG  PHE B 355    13586  15310   8340  -2880   -821   2025  B    C  
ATOM   6154  CD1 PHE B 355      -0.076   3.751 502.011  1.00100.92      B    C  
ANISOU 6154  CD1 PHE B 355    13953  15511   8881  -2569  -1053   2129  B    C  
ATOM   6155  CD2 PHE B 355      -1.747   3.454 503.681  1.00 98.32      B    C  
ANISOU 6155  CD2 PHE B 355    13727  15703   7928  -3299   -793   2136  B    C  
ATOM   6156  CE1 PHE B 355       0.899   3.721 502.990  1.00 96.70      B    C  
ANISOU 6156  CE1 PHE B 355    13494  15169   8078  -2659  -1257   2324  B    C  
ATOM   6157  CE2 PHE B 355      -0.777   3.413 504.654  1.00 97.64      B    C  
ANISOU 6157  CE2 PHE B 355    13730  15811   7557  -3401  -1000   2347  B    C  
ATOM   6158  CZ  PHE B 355       0.548   3.545 504.308  1.00 92.39      B    C  
ANISOU 6158  CZ  PHE B 355    13048  14981   7076  -3072  -1238   2444  B    C  
ATOM   6159  N   ARG B 356      -4.384   5.529 499.105  1.00 90.61      B    N  
ANISOU 6159  N   ARG B 356    12050  14033   8344  -2422    -67    936  B    N  
ATOM   6160  CA  ARG B 356      -5.495   5.406 498.167  1.00 88.36      B    C  
ANISOU 6160  CA  ARG B 356    11681  13594   8297  -2368     88    786  B    C  
ATOM   6161  C   ARG B 356      -6.173   4.049 498.357  1.00 90.80      B    C  
ANISOU 6161  C   ARG B 356    12185  13832   8481  -2611     62   1059  B    C  
ATOM   6162  O   ARG B 356      -6.278   3.237 497.435  1.00 90.15      B    O  
ANISOU 6162  O   ARG B 356    12186  13435   8631  -2469    -16   1208  B    O  
ATOM   6163  CB  ARG B 356      -4.999   5.598 496.735  1.00 82.55      B    C  
ANISOU 6163  CB  ARG B 356    10882  12506   7977  -1956      4    740  B    C  
ATOM   6164  CG  ARG B 356      -4.428   6.984 496.468  1.00 87.83      B    C  
ANISOU 6164  CG  ARG B 356    11358  13229   8786  -1726     53    452  B    C  
ATOM   6165  CD  ARG B 356      -4.119   7.179 494.999  1.00104.49      B    C  
ANISOU 6165  CD  ARG B 356    13406  15004  11292  -1361     -2    390  B    C  
ATOM   6166  NE  ARG B 356      -4.668   8.419 494.457  1.00114.05      B    N  
ANISOU 6166  NE  ARG B 356    14387  16259  12686  -1235    182     24  B    N  
ATOM   6167  CZ  ARG B 356      -5.776   8.495 493.724  1.00113.42      B    C  
ANISOU 6167  CZ  ARG B 356    14203  16110  12783  -1212    317   -130  B    C  
ATOM   6168  NH1 ARG B 356      -6.453   7.393 493.419  1.00107.79      B    N1+
ANISOU 6168  NH1 ARG B 356    13592  15285  12079  -1314    303     37  B    N1+
ATOM   6169  NH2 ARG B 356      -6.185   9.675 493.268  1.00114.66      B    N  
ANISOU 6169  NH2 ARG B 356    14150  16297  13119  -1080    457   -448  B    N  
ATOM   6170  N   CYS B 357      -6.582   3.790 499.602  1.00 93.36      B    N  
ANISOU 6170  N   CYS B 357    12595  14459   8420  -2999    125   1130  B    N  
ATOM   6171  CA  CYS B 357      -7.257   2.558 499.993  1.00 95.03      B    C  
ANISOU 6171  CA  CYS B 357    13006  14654   8447  -3300    119   1387  B    C  
ATOM   6172  C   CYS B 357      -8.512   2.890 500.788  1.00 93.85      B    C  
ANISOU 6172  C   CYS B 357    12760  14869   8030  -3686    397   1140  B    C  
ATOM   6173  O   CYS B 357      -8.678   4.000 501.297  1.00 96.38      B    O  
ANISOU 6173  O   CYS B 357    12889  15485   8247  -3758    559    822  B    O  
ATOM   6174  CB  CYS B 357      -6.343   1.640 500.813  1.00 99.49      B    C  
ANISOU 6174  CB  CYS B 357    13840  15197   8764  -3430   -142   1827  B    C  
ATOM   6175  SG  CYS B 357      -5.746   2.375 502.341  1.00112.79      B    S  
ANISOU 6175  SG  CYS B 357    15515  17332  10008  -3682   -160   1803  B    S  
ATOM   6176  N   ASP B 358      -9.432   1.935 500.821  1.00 93.56      B    N  
ANISOU 6176  N   ASP B 358    12840  14795   7912  -3929    468   1257  B    N  
ATOM   6177  CA  ASP B 358     -10.713   2.130 501.486  1.00101.28      B    C  
ANISOU 6177  CA  ASP B 358    13724  16101   8657  -4311    745   1011  B    C  
ATOM   6178  C   ASP B 358     -10.714   1.789 502.981  1.00105.59      B    C  
ANISOU 6178  C   ASP B 358    14434  16982   8702  -4771    750   1176  B    C  
ATOM   6179  O   ASP B 358     -11.352   2.495 503.772  1.00105.84      B    O  
ANISOU 6179  O   ASP B 358    14319  17393   8502  -5052    977    877  B    O  
ATOM   6180  CB  ASP B 358     -11.763   1.359 500.712  1.00101.18      B    C  
ANISOU 6180  CB  ASP B 358    13728  15900   8818  -4347    845   1005  B    C  
ATOM   6181  CG  ASP B 358     -11.683   1.673 499.238  1.00 98.18      B    C  
ANISOU 6181  CG  ASP B 358    13199  15200   8905  -3905    815    871  B    C  
ATOM   6182  OD1 ASP B 358     -12.188   2.737 498.821  1.00100.28      B    O  
ANISOU 6182  OD1 ASP B 358    13193  15564   9346  -3771    984    485  B    O  
ATOM   6183  OD2 ASP B 358     -11.080   0.863 498.500  1.00 97.97      B    O1-
ANISOU 6183  OD2 ASP B 358    13328  14821   9075  -3692    615   1154  B    O1-
ATOM   6184  N   GLY B 359     -10.039   0.722 503.392  1.00106.74      B    N  
ANISOU 6184  N   GLY B 359    14877  17001   8678  -4868    508   1637  B    N  
ATOM   6185  CA  GLY B 359     -10.107   0.271 504.768  1.00109.83      B    C  
ANISOU 6185  CA  GLY B 359    15457  17696   8579  -5333    495   1841  B    C  
ATOM   6186  C   GLY B 359      -8.743  -0.038 505.351  1.00113.49      B    C  
ANISOU 6186  C   GLY B 359    16119  18122   8879  -5280    178   2228  B    C  
ATOM   6187  O   GLY B 359      -7.814  -0.440 504.647  1.00114.01      B    O  
ANISOU 6187  O   GLY B 359    16269  17829   9219  -4922    -74   2470  B    O  
ATOM   6188  N   ILE B 360      -8.640   0.148 506.667  1.00116.62      B    N  
ANISOU 6188  N   ILE B 360    16582  18909   8818  -5655    192   2276  B    N  
ATOM   6189  CA  ILE B 360      -7.369  -0.010 507.380  1.00123.66      B    C  
ANISOU 6189  CA  ILE B 360    17635  19850   9499  -5646   -105   2614  B    C  
ATOM   6190  C   ILE B 360      -7.447  -1.093 508.458  1.00109.28      B    C  
ANISOU 6190  C   ILE B 360    16132  18153   7238  -6093   -235   3043  B    C  
ATOM   6191  O   ILE B 360      -8.303  -1.048 509.326  1.00112.19      B    O  
ANISOU 6191  O   ILE B 360    16518  18876   7233  -6557    -28   2930  B    O  
ATOM   6192  CB  ILE B 360      -6.912   1.342 507.986  1.00116.81      B    C  
ANISOU 6192  CB  ILE B 360    16548  19356   8479  -5651    -15   2291  B    C  
ATOM   6193  CG1 ILE B 360      -6.481   2.304 506.868  1.00108.52      B    C  
ANISOU 6193  CG1 ILE B 360    15240  18098   7894  -5143     16   1981  B    C  
ATOM   6194  CG2 ILE B 360      -5.782   1.146 508.990  1.00112.27      B    C  
ANISOU 6194  CG2 ILE B 360    16145  18946   7567  -5772   -292   2630  B    C  
ATOM   6195  CD1 ILE B 360      -5.820   3.564 507.347  1.00104.55      B    C  
ANISOU 6195  CD1 ILE B 360    14544  17881   7300  -5084     58   1710  B    C  
ATOM   6196  N   THR B 369      -8.980  -3.907 515.651  1.00137.80      B    N  
ANISOU 6196  N   THR B 369    20472  22939   8946  -8455   -423   3765  B    N  
ATOM   6197  CA  THR B 369      -8.596  -2.590 515.141  1.00133.61      B    C  
ANISOU 6197  CA  THR B 369    19669  22556   8539  -8193   -298   3421  B    C  
ATOM   6198  C   THR B 369      -8.927  -2.409 513.659  1.00138.25      B    C  
ANISOU 6198  C   THR B 369    20168  22883   9477  -7852   -164   3275  B    C  
ATOM   6199  O   THR B 369      -8.244  -2.961 512.792  1.00130.88      B    O  
ANISOU 6199  O   THR B 369    19366  21570   8793  -7500   -385   3587  B    O  
ATOM   6200  CB  THR B 369      -7.099  -2.335 515.321  1.00137.58      B    C  
ANISOU 6200  CB  THR B 369    20195  23026   9053  -7921   -603   3660  B    C  
ATOM   6201  CG2 THR B 369      -6.756  -0.918 514.880  1.00129.26      B    C  
ANISOU 6201  CG2 THR B 369    18854  22161   8097  -7690   -449   3264  B    C  
ATOM   6202  OG1 THR B 369      -6.748  -2.510 516.698  1.00146.04      B    O  
ANISOU 6202  OG1 THR B 369    21346  24345   9799  -8237   -738   3811  B    O  
ATOM   6203  N   THR B 370      -9.964  -1.621 513.370  1.00131.48      B    N  
ANISOU 6203  N   THR B 370    19074  22229   8655  -7952    195   2789  B    N  
ATOM   6204  CA  THR B 370     -10.453  -1.458 512.007  1.00127.93      B    C  
ANISOU 6204  CA  THR B 370    18524  21563   8519  -7683    358   2620  B    C  
ATOM   6205  C   THR B 370     -10.924  -0.024 511.797  1.00129.18      B    C  
ANISOU 6205  C   THR B 370    18331  22016   8735  -7644    680   2045  B    C  
ATOM   6206  O   THR B 370     -11.328   0.657 512.746  1.00122.04      B    O  
ANISOU 6206  O   THR B 370    17262  21474   7633  -7928    849   1723  B    O  
ATOM   6207  CB  THR B 370     -11.600  -2.431 511.692  1.00127.29      B    C  
ANISOU 6207  CB  THR B 370    18559  21310   8494  -7869    480   2665  B    C  
ATOM   6208  CG2 THR B 370     -11.071  -3.852 511.487  1.00124.66      B    C  
ANISOU 6208  CG2 THR B 370    18560  20566   8241  -7775    164   3228  B    C  
ATOM   6209  OG1 THR B 370     -12.555  -2.416 512.761  1.00127.33      B    O  
ANISOU 6209  OG1 THR B 370    18516  21635   8228  -8331    668   2436  B    O  
ATOM   6210  N   TYR B 371     -10.877   0.419 510.535  1.00124.33      B    N  
ANISOU 6210  N   TYR B 371    17597  21227   8416  -7290    761   1912  B    N  
ATOM   6211  CA  TYR B 371     -11.277   1.767 510.145  1.00114.13      B    C  
ANISOU 6211  CA  TYR B 371    15964  20147   7254  -7177   1055   1373  B    C  
ATOM   6212  C   TYR B 371     -11.555   1.736 508.654  1.00119.23      B    C  
ANISOU 6212  C   TYR B 371    16498  20388   8417  -6738   1081   1272  B    C  
ATOM   6213  O   TYR B 371     -10.749   1.193 507.893  1.00126.09      B    O  
ANISOU 6213  O   TYR B 371    17499  20859   9551  -6374    812   1588  B    O  
ATOM   6214  CB  TYR B 371     -10.201   2.801 510.463  1.00113.77      B    C  
ANISOU 6214  CB  TYR B 371    15794  20276   7159  -7005    971   1266  B    C  
ATOM   6215  CG  TYR B 371     -10.518   4.208 510.000  1.00113.79      B    C  
ANISOU 6215  CG  TYR B 371    15418  20381   7436  -6785   1230    694  B    C  
ATOM   6216  CD1 TYR B 371     -11.168   5.095 510.847  1.00115.66      B    C  
ANISOU 6216  CD1 TYR B 371    15427  21020   7500  -7086   1507    251  B    C  
ATOM   6217  CD2 TYR B 371     -10.152   4.659 508.736  1.00107.22      B    C  
ANISOU 6217  CD2 TYR B 371    14436  19184   7120  -6239   1167    582  B    C  
ATOM   6218  CE1 TYR B 371     -11.446   6.389 510.458  1.00113.50      B    C  
ANISOU 6218  CE1 TYR B 371    14819  20858   7449  -6911   1754   -261  B    C  
ATOM   6219  CE2 TYR B 371     -10.436   5.957 508.333  1.00106.61      B    C  
ANISOU 6219  CE2 TYR B 371    14023  19179   7305  -6036   1387     78  B    C  
ATOM   6220  CZ  TYR B 371     -11.081   6.818 509.203  1.00110.74      B    C  
ANISOU 6220  CZ  TYR B 371    14342  20137   7599  -6370   1679   -339  B    C  
ATOM   6221  OH  TYR B 371     -11.381   8.111 508.828  1.00110.68      B    O  
ANISOU 6221  OH  TYR B 371    13995  20183   7874  -6170   1897   -842  B    O  
ATOM   6222  N   GLY B 372     -12.658   2.363 508.230  1.00125.28      B    N  
ANISOU 6222  N   GLY B 372    16994  21240   9368  -6743   1391    806  B    N  
ATOM   6223  CA  GLY B 372     -12.984   2.343 506.813  1.00118.66      B    C  
ANISOU 6223  CA  GLY B 372    16031  20017   9037  -6326   1404    697  B    C  
ATOM   6224  C   GLY B 372     -13.558   0.984 506.441  1.00113.18      B    C  
ANISOU 6224  C   GLY B 372    15565  19079   8359  -6449   1356    996  B    C  
ATOM   6225  O   GLY B 372     -13.992   0.216 507.307  1.00115.31      B    O  
ANISOU 6225  O   GLY B 372    16037  19528   8250  -6904   1393   1184  B    O  
ATOM   6226  N   GLU B 373     -13.591   0.684 505.147  1.00109.90      B    N  
ANISOU 6226  N   GLU B 373    15119  18262   8377  -6065   1283   1032  B    N  
ATOM   6227  CA  GLU B 373     -14.253  -0.544 504.728  1.00115.19      B    C  
ANISOU 6227  CA  GLU B 373    15969  18706   9093  -6187   1280   1250  B    C  
ATOM   6228  C   GLU B 373     -13.356  -1.741 505.036  1.00114.72      B    C  
ANISOU 6228  C   GLU B 373    16282  18421   8885  -6237    971   1828  B    C  
ATOM   6229  O   GLU B 373     -12.264  -1.868 504.475  1.00116.19      B    O  
ANISOU 6229  O   GLU B 373    16539  18304   9306  -5859    710   2057  B    O  
ATOM   6230  CB  GLU B 373     -14.530  -0.483 503.223  1.00116.62      B    C  
ANISOU 6230  CB  GLU B 373    15995  18536   9782  -5764   1294   1103  B    C  
ATOM   6231  CG  GLU B 373     -15.263   0.769 502.724  1.00116.82      B    C  
ANISOU 6231  CG  GLU B 373    15638  18708  10042  -5606   1540    561  B    C  
ATOM   6232  CD  GLU B 373     -16.731   0.821 503.121  1.00125.51      B    C  
ANISOU 6232  CD  GLU B 373    16595  20100  10992  -5986   1856    237  B    C  
ATOM   6233  OE1 GLU B 373     -17.249  -0.175 503.683  1.00130.21      B    O  
ANISOU 6233  OE1 GLU B 373    17398  20766  11310  -6379   1900    431  B    O  
ATOM   6234  OE2 GLU B 373     -17.374   1.863 502.864  1.00123.13      B    O1-
ANISOU 6234  OE2 GLU B 373    15970  19952  10863  -5894   2062   -218  B    O1-
ATOM   6235  N   THR B 374     -13.809  -2.631 505.910  1.00119.47      B    N  
ANISOU 6235  N   THR B 374    17122  19159   9114  -6703    996   2063  B    N  
ATOM   6236  CA  THR B 374     -13.036  -3.824 506.214  1.00122.06      B    C  
ANISOU 6236  CA  THR B 374    17814  19250   9315  -6765    695   2631  B    C  
ATOM   6237  C   THR B 374     -13.969  -5.009 506.393  1.00122.64      B    C  
ANISOU 6237  C   THR B 374    18108  19261   9231  -7146    784   2819  B    C  
ATOM   6238  O   THR B 374     -15.147  -4.839 506.724  1.00120.04      B    O  
ANISOU 6238  O   THR B 374    17663  19200   8748  -7471   1074   2510  B    O  
ATOM   6239  CB  THR B 374     -12.181  -3.686 507.486  1.00120.57      B    C  
ANISOU 6239  CB  THR B 374    17776  19333   8704  -6989    527   2870  B    C  
ATOM   6240  CG2 THR B 374     -11.460  -2.351 507.556  1.00114.23      B    C  
ANISOU 6240  CG2 THR B 374    16722  18719   7963  -6732    521   2590  B    C  
ATOM   6241  OG1 THR B 374     -13.014  -3.839 508.639  1.00121.35      B    O  
ANISOU 6241  OG1 THR B 374    17895  19748   8464  -7458    678   2751  B    O  
ATOM   6242  N   PRO B 375     -13.458  -6.224 506.211  1.00122.27      B    N  
ANISOU 6242  N   PRO B 375    18364  18848   9244  -7101    531   3303  B    N  
ATOM   6243  CA  PRO B 375     -14.203  -7.433 506.585  1.00123.20      B    C  
ANISOU 6243  CA  PRO B 375    18679  18843   9287  -7385    542   3463  B    C  
ATOM   6244  C   PRO B 375     -14.443  -7.489 508.089  1.00124.37      B    C  
ANISOU 6244  C   PRO B 375    18891  19324   9041  -7778    545   3450  B    C  
ATOM   6245  O   PRO B 375     -13.889  -6.709 508.865  1.00124.66      B    O  
ANISOU 6245  O   PRO B 375    18848  19645   8874  -7816    493   3378  B    O  
ATOM   6246  CB  PRO B 375     -13.279  -8.567 506.127  1.00121.52      B    C  
ANISOU 6246  CB  PRO B 375    18737  18133   9304  -7134    207   3965  B    C  
ATOM   6247  CG  PRO B 375     -12.488  -7.970 505.006  1.00114.54      B    C  
ANISOU 6247  CG  PRO B 375    17724  17043   8751  -6677    118   3936  B    C  
ATOM   6248  CD  PRO B 375     -12.267  -6.537 505.398  1.00111.19      B    C  
ANISOU 6248  CD  PRO B 375    17031  17004   8212  -6609    216   3577  B    C  
ATOM   6249  N   ASP B 376     -15.315  -8.401 508.509  1.00126.08      B    N  
ANISOU 6249  N   ASP B 376    19244  19518   9143  -8093    619   3496  B    N  
ATOM   6250  CA  ASP B 376     -15.598  -8.456 509.933  1.00135.30      B    C  
ANISOU 6250  CA  ASP B 376    20473  21010   9927  -8499    629   3471  B    C  
ATOM   6251  C   ASP B 376     -14.415  -9.161 510.598  1.00142.02      B    C  
ANISOU 6251  C   ASP B 376    21591  21686  10683  -8446    253   3976  B    C  
ATOM   6252  O   ASP B 376     -13.545  -9.717 509.919  1.00140.03      B    O  
ANISOU 6252  O   ASP B 376    21473  21040  10691  -8108      9   4316  B    O  
ATOM   6253  CB  ASP B 376     -16.917  -9.206 510.186  1.00144.49      B    C  
ANISOU 6253  CB  ASP B 376    21702  22214  10985  -8866    826   3351  B    C  
ATOM   6254  CG  ASP B 376     -17.307  -9.296 511.679  1.00154.62      B    C  
ANISOU 6254  CG  ASP B 376    23053  23842  11854  -9335    850   3308  B    C  
ATOM   6255  OD1 ASP B 376     -16.518  -8.892 512.565  1.00158.07      B    O  
ANISOU 6255  OD1 ASP B 376    23512  24467  12080  -9389    692   3416  B    O  
ATOM   6256  OD2 ASP B 376     -18.413  -9.810 511.968  1.00157.75      B    O1-
ANISOU 6256  OD2 ASP B 376    23487  24319  12132  -9665   1023   3167  B    O1-
ATOM   6257  N   GLN B 377     -14.353  -9.103 511.935  1.00150.90      B    N  
ANISOU 6257  N   GLN B 377    22773  23109  11452  -8773    200   4009  B    N  
ATOM   6258  CA  GLN B 377     -13.185  -9.633 512.637  1.00148.74      B    C  
ANISOU 6258  CA  GLN B 377    22715  22720  11080  -8719   -159   4460  B    C  
ATOM   6259  C   GLN B 377     -12.892 -11.072 512.212  1.00152.69      B    C  
ANISOU 6259  C   GLN B 377    23498  22727  11788  -8582   -389   4915  B    C  
ATOM   6260  O   GLN B 377     -11.733 -11.437 511.986  1.00152.05      B    O  
ANISOU 6260  O   GLN B 377    23529  22357  11887  -8263   -695   5266  B    O  
ATOM   6261  CB  GLN B 377     -13.375  -9.528 514.157  1.00145.09      B    C  
ANISOU 6261  CB  GLN B 377    22293  22647  10186  -9168   -157   4430  B    C  
ATOM   6262  CG  GLN B 377     -12.338 -10.302 514.975  1.00149.08      B    C  
ANISOU 6262  CG  GLN B 377    23052  23026  10567  -9182   -527   4927  B    C  
ATOM   6263  CD  GLN B 377     -12.203  -9.806 516.409  1.00156.08      B    C  
ANISOU 6263  CD  GLN B 377    23908  24352  11042  -9546   -546   4861  B    C  
ATOM   6264  NE2 GLN B 377     -11.164 -10.267 517.101  1.00156.25      B    N  
ANISOU 6264  NE2 GLN B 377    24102  24303  10962  -9516   -876   5266  B    N  
ATOM   6265  OE1 GLN B 377     -13.021  -9.020 516.887  1.00153.62      B    O  
ANISOU 6265  OE1 GLN B 377    23410  24436  10523  -9849   -269   4441  B    O  
ATOM   6266  N   THR B 378     -13.935 -11.906 512.109  1.00155.23      B    N  
ANISOU 6266  N   THR B 378    23928  22946  12105  -8815   -242   4896  B    N  
ATOM   6267  CA  THR B 378     -13.747 -13.313 511.756  1.00152.96      B    C  
ANISOU 6267  CA  THR B 378    23907  22194  12017  -8715   -433   5302  B    C  
ATOM   6268  C   THR B 378     -13.159 -13.495 510.355  1.00149.20      B    C  
ANISOU 6268  C   THR B 378    23405  21279  12004  -8223   -531   5412  B    C  
ATOM   6269  O   THR B 378     -12.181 -14.231 510.173  1.00154.56      B    O  
ANISOU 6269  O   THR B 378    24246  21591  12888  -7958   -832   5799  B    O  
ATOM   6270  CB  THR B 378     -15.081 -14.053 511.864  1.00150.44      B    C  
ANISOU 6270  CB  THR B 378    23675  21887  11598  -9074   -208   5190  B    C  
ATOM   6271  CG2 THR B 378     -15.820 -13.644 513.143  1.00151.37      B    C  
ANISOU 6271  CG2 THR B 378    23753  22494  11267  -9575    -48   4959  B    C  
ATOM   6272  OG1 THR B 378     -15.892 -13.739 510.722  1.00147.48      B    O  
ANISOU 6272  OG1 THR B 378    23120  21454  11463  -8957     63   4857  B    O  
ATOM   6273  N   THR B 379     -13.729 -12.821 509.348  1.00135.90      B    N  
ANISOU 6273  N   THR B 379    21507  19626  10505  -8093   -283   5064  B    N  
ATOM   6274  CA  THR B 379     -13.169 -12.925 508.002  1.00137.16      B    C  
ANISOU 6274  CA  THR B 379    21631  19386  11099  -7644   -371   5147  B    C  
ATOM   6275  C   THR B 379     -11.748 -12.383 507.957  1.00139.77      B    C  
ANISOU 6275  C   THR B 379    21924  19653  11528  -7292   -644   5315  B    C  
ATOM   6276  O   THR B 379     -10.877 -12.949 507.283  1.00144.50      B    O  
ANISOU 6276  O   THR B 379    22611  19835  12456  -6937   -883   5587  B    O  
ATOM   6277  CB  THR B 379     -14.060 -12.190 506.992  1.00133.62      B    C  
ANISOU 6277  CB  THR B 379    20941  19033  10797  -7598    -47   4723  B    C  
ATOM   6278  CG2 THR B 379     -13.490 -12.310 505.586  1.00123.06      B    C  
ANISOU 6278  CG2 THR B 379    19571  17280   9905  -7157   -140   4810  B    C  
ATOM   6279  OG1 THR B 379     -15.377 -12.752 507.015  1.00138.22      B    O  
ANISOU 6279  OG1 THR B 379    21548  19664  11307  -7913    199   4558  B    O  
ATOM   6280  N   ILE B 380     -11.500 -11.286 508.679  1.00138.84      B    N  
ANISOU 6280  N   ILE B 380    21661  19951  11140  -7386   -608   5132  B    N  
ATOM   6281  CA  ILE B 380     -10.165 -10.695 508.733  1.00138.63      B    C  
ANISOU 6281  CA  ILE B 380    21583  19918  11170  -7079   -857   5260  B    C  
ATOM   6282  C   ILE B 380      -9.183 -11.688 509.335  1.00145.75      B    C  
ANISOU 6282  C   ILE B 380    22718  20569  12090  -7001  -1223   5726  B    C  
ATOM   6283  O   ILE B 380      -8.021 -11.780 508.914  1.00153.34      B    O  
ANISOU 6283  O   ILE B 380    23694  21264  13303  -6620  -1490   5938  B    O  
ATOM   6284  CB  ILE B 380     -10.188  -9.362 509.513  1.00134.29      B    C  
ANISOU 6284  CB  ILE B 380    20831  19894  10297  -7250   -718   4945  B    C  
ATOM   6285  CG1 ILE B 380     -10.724  -8.221 508.645  1.00128.39      B    C  
ANISOU 6285  CG1 ILE B 380    19813  19314   9657  -7142   -425   4505  B    C  
ATOM   6286  CG2 ILE B 380      -8.807  -8.996 510.020  1.00135.87      B    C  
ANISOU 6286  CG2 ILE B 380    21039  20139  10449  -7050  -1014   5145  B    C  
ATOM   6287  CD1 ILE B 380     -10.762  -6.882 509.366  1.00123.03      B    C  
ANISOU 6287  CD1 ILE B 380    18907  19136   8701  -7288   -266   4152  B    C  
ATOM   6288  N   ASN B 381      -9.647 -12.474 510.305  1.00142.78      B    N  
ANISOU 6288  N   ASN B 381    22521  20264  11465  -7357  -1241   5884  B    N  
ATOM   6289  CA  ASN B 381      -8.788 -13.482 510.910  1.00145.06      B    C  
ANISOU 6289  CA  ASN B 381    23035  20312  11767  -7305  -1581   6334  B    C  
ATOM   6290  C   ASN B 381      -8.569 -14.659 509.968  1.00146.79      B    C  
ANISOU 6290  C   ASN B 381    23397  19968  12407  -7021  -1716   6593  B    C  
ATOM   6291  O   ASN B 381      -7.484 -15.244 509.959  1.00149.46      B    O  
ANISOU 6291  O   ASN B 381    23834  20006  12947  -6746  -2028   6916  B    O  
ATOM   6292  CB  ASN B 381      -9.369 -13.939 512.250  1.00151.52      B    C  
ANISOU 6292  CB  ASN B 381    24006  21390  12174  -7795  -1555   6423  B    C  
ATOM   6293  CG  ASN B 381      -9.362 -12.833 513.311  1.00155.83      B    C  
ANISOU 6293  CG  ASN B 381    24413  22480  12316  -8063  -1475   6201  B    C  
ATOM   6294  ND2 ASN B 381     -10.330 -12.875 514.222  1.00157.70      B    N  
ANISOU 6294  ND2 ASN B 381    24687  23037  12196  -8546  -1291   6064  B    N  
ATOM   6295  OD1 ASN B 381      -8.490 -11.969 513.317  1.00159.01      B    O  
ANISOU 6295  OD1 ASN B 381    24673  23009  12734  -7844  -1575   6145  B    O  
ATOM   6296  N   LYS B 382      -9.578 -15.036 509.176  1.00142.80      B    N  
ANISOU 6296  N   LYS B 382    22892  19311  12053  -7082  -1481   6441  B    N  
ATOM   6297  CA  LYS B 382      -9.335 -16.025 508.118  1.00139.57      B    C  
ANISOU 6297  CA  LYS B 382    22574  18363  12094  -6773  -1583   6626  B    C  
ATOM   6298  C   LYS B 382      -8.290 -15.533 507.116  1.00133.43      B    C  
ANISOU 6298  C   LYS B 382    21654  17354  11689  -6274  -1730   6612  B    C  
ATOM   6299  O   LYS B 382      -7.451 -16.315 506.647  1.00133.77      B    O  
ANISOU 6299  O   LYS B 382    21778  16970  12080  -5953  -1968   6865  B    O  
ATOM   6300  CB  LYS B 382     -10.615 -16.431 507.400  1.00136.82      B    C  
ANISOU 6300  CB  LYS B 382    22225  17920  11843  -6929  -1286   6428  B    C  
ATOM   6301  CG  LYS B 382     -11.631 -17.095 508.281  1.00143.21      B    C  
ANISOU 6301  CG  LYS B 382    23190  18886  12338  -7397  -1154   6456  B    C  
ATOM   6302  CD  LYS B 382     -12.805 -17.502 507.448  1.00141.48      B    C  
ANISOU 6302  CD  LYS B 382    22948  18543  12264  -7499   -872   6248  B    C  
ATOM   6303  CE  LYS B 382     -12.352 -18.721 506.649  1.00140.40      B    C  
ANISOU 6303  CE  LYS B 382    22957  17836  12552  -7213  -1038   6532  B    C  
ATOM   6304  NZ  LYS B 382     -13.277 -19.137 505.578  1.00138.31      B    N1+
ANISOU 6304  NZ  LYS B 382    22649  17369  12533  -7210   -797   6343  B    N1+
ATOM   6305  N   LEU B 383      -8.318 -14.236 506.796  1.00129.41      B    N  
ANISOU 6305  N   LEU B 383    20925  17127  11117  -6207  -1588   6304  B    N  
ATOM   6306  CA  LEU B 383      -7.334 -13.637 505.897  1.00138.55      B    C  
ANISOU 6306  CA  LEU B 383    21940  18114  12590  -5758  -1721   6265  B    C  
ATOM   6307  C   LEU B 383      -5.952 -13.791 506.517  1.00141.74      B    C  
ANISOU 6307  C   LEU B 383    22399  18442  13012  -5550  -2078   6551  B    C  
ATOM   6308  O   LEU B 383      -5.010 -14.320 505.893  1.00141.56      B    O  
ANISOU 6308  O   LEU B 383    22397  18018  13372  -5168  -2309   6732  B    O  
ATOM   6309  CB  LEU B 383      -7.693 -12.165 505.661  1.00137.66      B    C  
ANISOU 6309  CB  LEU B 383    21592  18389  12323  -5795  -1487   5880  B    C  
ATOM   6310  CG  LEU B 383      -8.884 -11.898 504.730  1.00132.28      B    C  
ANISOU 6310  CG  LEU B 383    20799  17726  11735  -5883  -1150   5566  B    C  
ATOM   6311  CD1 LEU B 383      -9.156 -10.403 504.617  1.00126.47      B    C  
ANISOU 6311  CD1 LEU B 383    19820  17400  10835  -5916   -930   5189  B    C  
ATOM   6312  CD2 LEU B 383      -8.650 -12.504 503.360  1.00127.66      B    C  
ANISOU 6312  CD2 LEU B 383    20226  16640  11637  -5540  -1215   5640  B    C  
ATOM   6313  N   VAL B 384      -5.826 -13.313 507.755  1.00142.40      B    N  
ANISOU 6313  N   VAL B 384    22490  18924  12690  -5804  -2114   6567  B    N  
ATOM   6314  CA  VAL B 384      -4.581 -13.411 508.505  1.00145.08      B    C  
ANISOU 6314  CA  VAL B 384    22877  19262  12985  -5665  -2441   6827  B    C  
ATOM   6315  C   VAL B 384      -4.075 -14.840 508.443  1.00148.82      B    C  
ANISOU 6315  C   VAL B 384    23545  19270  13730  -5511  -2692   7200  B    C  
ATOM   6316  O   VAL B 384      -2.925 -15.096 508.065  1.00141.56      B    O  
ANISOU 6316  O   VAL B 384    22603  18060  13123  -5124  -2952   7359  B    O  
ATOM   6317  CB  VAL B 384      -4.783 -12.927 509.954  1.00147.04      B    C  
ANISOU 6317  CB  VAL B 384    23143  20006  12720  -6068  -2409   6804  B    C  
ATOM   6318  CG1 VAL B 384      -3.615 -13.373 510.835  1.00148.79      B    C  
ANISOU 6318  CG1 VAL B 384    23469  20178  12886  -5987  -2764   7147  B    C  
ATOM   6319  CG2 VAL B 384      -4.879 -11.371 509.966  1.00143.57      B    C  
ANISOU 6319  CG2 VAL B 384    22462  20005  12085  -6102  -2215   6423  B    C  
ATOM   6320  N   GLU B 385      -4.936 -15.784 508.820  1.00156.33      B    N  
ANISOU 6320  N   GLU B 385    24680  20151  14567  -5815  -2607   7323  B    N  
ATOM   6321  CA  GLU B 385      -4.598 -17.202 508.829  1.00156.63      B    C  
ANISOU 6321  CA  GLU B 385    24918  19758  14836  -5719  -2813   7673  B    C  
ATOM   6322  C   GLU B 385      -4.066 -17.695 507.488  1.00155.99      B    C  
ANISOU 6322  C   GLU B 385    24784  19173  15312  -5261  -2892   7691  B    C  
ATOM   6323  O   GLU B 385      -3.054 -18.408 507.448  1.00158.93      B    O  
ANISOU 6323  O   GLU B 385    25213  19221  15953  -4981  -3168   7944  B    O  
ATOM   6324  CB  GLU B 385      -5.846 -18.030 509.153  1.00154.46      B    C  
ANISOU 6324  CB  GLU B 385    24820  19479  14388  -6117  -2625   7713  B    C  
ATOM   6325  CG  GLU B 385      -6.505 -17.902 510.504  1.00160.76      B    C  
ANISOU 6325  CG  GLU B 385    25718  20703  14661  -6622  -2544   7728  B    C  
ATOM   6326  CD  GLU B 385      -7.782 -18.745 510.552  1.00164.19      B    C  
ANISOU 6326  CD  GLU B 385    26306  21075  15003  -6967  -2330   7719  B    C  
ATOM   6327  OE1 GLU B 385      -7.885 -19.726 509.781  1.00162.60      B    O  
ANISOU 6327  OE1 GLU B 385    26197  20437  15146  -6801  -2344   7840  B    O  
ATOM   6328  OE2 GLU B 385      -8.699 -18.403 511.329  1.00165.66      B    O1-
ANISOU 6328  OE2 GLU B 385    26504  21654  14784  -7403  -2131   7561  B    O1-
ATOM   6329  N   TRP B 386      -4.727 -17.354 506.371  1.00153.21      B    N  
ANISOU 6329  N   TRP B 386    24315  18743  15154  -5182  -2650   7415  B    N  
ATOM   6330  CA  TRP B 386      -4.179 -17.881 505.125  1.00151.93      B    C  
ANISOU 6330  CA  TRP B 386    24103  18096  15528  -4759  -2732   7430  B    C  
ATOM   6331  C   TRP B 386      -2.793 -17.307 504.876  1.00151.17      B    C  
ANISOU 6331  C   TRP B 386    23858  17940  15640  -4350  -2971   7436  B    C  
ATOM   6332  O   TRP B 386      -1.920 -18.001 504.330  1.00151.71      B    O  
ANISOU 6332  O   TRP B 386    23924  17605  16114  -4001  -3165   7567  B    O  
ATOM   6333  CB  TRP B 386      -5.068 -17.559 503.926  1.00146.12      B    C  
ANISOU 6333  CB  TRP B 386    23253  17292  14972  -4734  -2443   7126  B    C  
ATOM   6334  CG  TRP B 386      -4.502 -18.160 502.654  1.00148.46      B    C  
ANISOU 6334  CG  TRP B 386    23496  17087  15825  -4319  -2523   7129  B    C  
ATOM   6335  CD1 TRP B 386      -4.804 -19.403 502.171  1.00152.15      B    C  
ANISOU 6335  CD1 TRP B 386    24080  17161  16570  -4292  -2498   7240  B    C  
ATOM   6336  CD2 TRP B 386      -3.480 -17.634 501.777  1.00149.01      B    C  
ANISOU 6336  CD2 TRP B 386    23385  16990  16243  -3879  -2649   7020  B    C  
ATOM   6337  CE2 TRP B 386      -3.267 -18.601 500.764  1.00148.62      B    C  
ANISOU 6337  CE2 TRP B 386    23342  16456  16671  -3619  -2674   7044  B    C  
ATOM   6338  CE3 TRP B 386      -2.744 -16.443 501.732  1.00145.21      B    C  
ANISOU 6338  CE3 TRP B 386    22732  16726  15716  -3690  -2727   6884  B    C  
ATOM   6339  NE1 TRP B 386      -4.095 -19.659 501.026  1.00153.70      B    N  
ANISOU 6339  NE1 TRP B 386    24168  16972  17259  -3880  -2577   7179  B    N  
ATOM   6340  CZ2 TRP B 386      -2.360 -18.409 499.717  1.00139.76      B    C  
ANISOU 6340  CZ2 TRP B 386    22053  15072  15976  -3188  -2769   6920  B    C  
ATOM   6341  CZ3 TRP B 386      -1.835 -16.260 500.689  1.00141.49      B    C  
ANISOU 6341  CZ3 TRP B 386    22106  15981  15674  -3253  -2834   6780  B    C  
ATOM   6342  CH2 TRP B 386      -1.656 -17.239 499.698  1.00138.96      B    C  
ANISOU 6342  CH2 TRP B 386    21788  15188  15821  -3011  -2851   6791  B    C  
ATOM   6343  N   LEU B 387      -2.552 -16.055 505.296  1.00150.57      B    N  
ANISOU 6343  N   LEU B 387    23649  18266  15294  -4391  -2957   7282  B    N  
ATOM   6344  CA  LEU B 387      -1.203 -15.524 505.105  1.00149.25      B    C  
ANISOU 6344  CA  LEU B 387    23341  18051  15316  -4010  -3189   7286  B    C  
ATOM   6345  C   LEU B 387      -0.211 -16.270 506.000  1.00151.40      B    C  
ANISOU 6345  C   LEU B 387    23727  18220  15580  -3943  -3508   7620  B    C  
ATOM   6346  O   LEU B 387       0.918 -16.556 505.580  1.00155.09      B    O  
ANISOU 6346  O   LEU B 387    24128  18401  16397  -3559  -3731   7701  B    O  
ATOM   6347  CB  LEU B 387      -1.167 -14.011 505.326  1.00141.93      B    C  
ANISOU 6347  CB  LEU B 387    22242  17577  14108  -4067  -3090   7034  B    C  
ATOM   6348  CG  LEU B 387       0.079 -13.257 504.822  1.00138.57      B    C  
ANISOU 6348  CG  LEU B 387    21628  17106  13914  -3652  -3262   6941  B    C  
ATOM   6349  CD1 LEU B 387      -0.216 -11.778 504.804  1.00137.64      B    C  
ANISOU 6349  CD1 LEU B 387    21345  17410  13541  -3743  -3079   6640  B    C  
ATOM   6350  CD2 LEU B 387       1.329 -13.492 505.682  1.00145.16      B    C  
ANISOU 6350  CD2 LEU B 387    22487  17952  14716  -3523  -3582   7177  B    C  
ATOM   6351  N   GLU B 388      -0.610 -16.586 507.244  1.00144.62      B    N  
ANISOU 6351  N   GLU B 388    23030  17596  14321  -4320  -3531   7806  B    N  
ATOM   6352  CA  GLU B 388       0.284 -17.330 508.128  1.00156.90      B    C  
ANISOU 6352  CA  GLU B 388    24708  19054  15853  -4281  -3842   8147  B    C  
ATOM   6353  C   GLU B 388       0.653 -18.655 507.486  1.00164.58      B    C  
ANISOU 6353  C   GLU B 388    25774  19478  17283  -4019  -3978   8347  B    C  
ATOM   6354  O   GLU B 388       1.769 -19.159 507.665  1.00170.87      B    O  
ANISOU 6354  O   GLU B 388    26578  20064  18282  -3762  -4261   8554  B    O  
ATOM   6355  CB  GLU B 388      -0.335 -17.552 509.511  1.00163.52      B    C  
ANISOU 6355  CB  GLU B 388    25725  20210  16195  -4763  -3827   8317  B    C  
ATOM   6356  CG  GLU B 388      -0.904 -16.329 510.203  1.00161.34      B    C  
ANISOU 6356  CG  GLU B 388    25362  20499  15442  -5097  -3636   8084  B    C  
ATOM   6357  CD  GLU B 388      -1.203 -16.600 511.676  1.00167.40      B    C  
ANISOU 6357  CD  GLU B 388    26294  21568  15742  -5536  -3691   8280  B    C  
ATOM   6358  OE1 GLU B 388      -2.241 -17.232 511.971  1.00164.84      B    O  
ANISOU 6358  OE1 GLU B 388    26128  21247  15255  -5875  -3541   8330  B    O  
ATOM   6359  OE2 GLU B 388      -0.393 -16.192 512.542  1.00174.45      B    O1-
ANISOU 6359  OE2 GLU B 388    27157  22696  16429  -5550  -3883   8380  B    O1-
ATOM   6360  N   GLU B 389      -0.297 -19.255 506.765  1.00162.96      B    N  
ANISOU 6360  N   GLU B 389    25636  19044  17238  -4095  -3769   8278  B    N  
ATOM   6361  CA  GLU B 389      -0.005 -20.491 506.050  1.00162.60      B    C  
ANISOU 6361  CA  GLU B 389    25659  18471  17651  -3846  -3858   8420  B    C  
ATOM   6362  C   GLU B 389       0.991 -20.209 504.936  1.00156.98      B    C  
ANISOU 6362  C   GLU B 389    24737  17503  17404  -3354  -3944   8257  B    C  
ATOM   6363  O   GLU B 389       1.856 -21.042 504.642  1.00162.28      B    O  
ANISOU 6363  O   GLU B 389    25415  17803  18442  -3061  -4140   8401  B    O  
ATOM   6364  CB  GLU B 389      -1.276 -21.132 505.482  1.00157.67      B    C  
ANISOU 6364  CB  GLU B 389    25136  17682  17090  -4048  -3589   8346  B    C  
ATOM   6365  CG  GLU B 389      -2.049 -22.015 506.454  1.00157.65      B    C  
ANISOU 6365  CG  GLU B 389    25386  17722  16791  -4455  -3566   8594  B    C  
ATOM   6366  CD  GLU B 389      -3.308 -22.584 505.826  1.00159.76      B    C  
ANISOU 6366  CD  GLU B 389    25730  17840  17132  -4647  -3280   8481  B    C  
ATOM   6367  OE1 GLU B 389      -3.265 -22.944 504.628  1.00160.51      B    O  
ANISOU 6367  OE1 GLU B 389    25745  17581  17659  -4376  -3207   8358  B    O  
ATOM   6368  OE2 GLU B 389      -4.338 -22.669 506.524  1.00163.39      B    O1-
ANISOU 6368  OE2 GLU B 389    26320  18545  17217  -5076  -3122   8496  B    O1-
ATOM   6369  N   ASN B 390       0.888 -19.038 504.312  1.00145.26      B    N  
ANISOU 6369  N   ASN B 390    23063  16216  15914  -3264  -3797   7947  B    N  
ATOM   6370  CA  ASN B 390       1.595 -18.788 503.072  1.00141.39      B    C  
ANISOU 6370  CA  ASN B 390    22375  15468  15878  -2835  -3815   7741  B    C  
ATOM   6371  C   ASN B 390       2.454 -17.530 503.193  1.00136.29      B    C  
ANISOU 6371  C   ASN B 390    21540  15102  15143  -2659  -3913   7595  B    C  
ATOM   6372  O   ASN B 390       3.268 -17.420 504.117  1.00135.22      B    O  
ANISOU 6372  O   ASN B 390    21418  15119  14842  -2646  -4137   7762  B    O  
ATOM   6373  CB  ASN B 390       0.581 -18.633 501.945  1.00136.65      B    C  
ANISOU 6373  CB  ASN B 390    21718  14772  15428  -2868  -3519   7479  B    C  
ATOM   6374  CG  ASN B 390       0.034 -19.967 501.482  1.00137.23      B    C  
ANISOU 6374  CG  ASN B 390    21928  14457  15755  -2905  -3443   7581  B    C  
ATOM   6375  ND2 ASN B 390       0.607 -20.511 500.415  1.00137.17      B    N  
ANISOU 6375  ND2 ASN B 390    21829  14048  16242  -2556  -3479   7501  B    N  
ATOM   6376  OD1 ASN B 390      -0.888 -20.511 502.093  1.00137.40      B    O  
ANISOU 6376  OD1 ASN B 390    22132  14548  15525  -3255  -3344   7717  B    O  
ATOM   6377  N   LEU B 395       7.651 -11.135 504.833  1.00132.89      B    N  
ANISOU 6377  N   LEU B 395    20150  16295  14048  -1846  -4537   6906  B    N  
ATOM   6378  CA  LEU B 395       7.279 -10.276 503.706  1.00133.52      B    C  
ANISOU 6378  CA  LEU B 395    20083  16366  14282  -1718  -4331   6585  B    C  
ATOM   6379  C   LEU B 395       5.826  -9.840 503.761  1.00135.69      B    C  
ANISOU 6379  C   LEU B 395    20432  16877  14246  -2079  -4046   6486  B    C  
ATOM   6380  O   LEU B 395       5.033 -10.371 504.553  1.00139.87      B    O  
ANISOU 6380  O   LEU B 395    21135  17516  14492  -2424  -3986   6657  B    O  
ATOM   6381  CB  LEU B 395       7.518 -10.975 502.358  1.00129.54      B    C  
ANISOU 6381  CB  LEU B 395    19524  15360  14334  -1379  -4328   6510  B    C  
ATOM   6382  CG  LEU B 395       8.894 -11.044 501.694  1.00124.68      B    C  
ANISOU 6382  CG  LEU B 395    18736  14494  14145   -939  -4502   6414  B    C  
ATOM   6383  CD1 LEU B 395       9.967 -11.521 502.666  1.00130.72      B    C  
ANISOU 6383  CD1 LEU B 395    19526  15286  14855   -874  -4784   6645  B    C  
ATOM   6384  CD2 LEU B 395       8.820 -11.942 500.462  1.00114.47      B    C  
ANISOU 6384  CD2 LEU B 395    17426  12721  13346   -714  -4439   6346  B    C  
ATOM   6385  N   PHE B 396       5.508  -8.827 502.951  1.00132.26      B    N  
ANISOU 6385  N   PHE B 396    19857  16541  13854  -2005  -3870   6198  B    N  
ATOM   6386  CA  PHE B 396       4.138  -8.403 502.701  1.00128.62      B    C  
ANISOU 6386  CA  PHE B 396    19432  16246  13190  -2284  -3577   6054  B    C  
ATOM   6387  C   PHE B 396       3.590  -9.183 501.506  1.00137.04      B    C  
ANISOU 6387  C   PHE B 396    20539  16875  14656  -2155  -3479   6034  B    C  
ATOM   6388  O   PHE B 396       4.322  -9.865 500.781  1.00141.27      B    O  
ANISOU 6388  O   PHE B 396    21038  17008  15630  -1827  -3616   6071  B    O  
ATOM   6389  CB  PHE B 396       4.032  -6.913 502.361  1.00109.91      B    C  
ANISOU 6389  CB  PHE B 396    16877  14194  10689  -2258  -3420   5729  B    C  
ATOM   6390  CG  PHE B 396       4.933  -6.477 501.240  1.00107.84      B    C  
ANISOU 6390  CG  PHE B 396    16403  13695  10877  -1798  -3465   5486  B    C  
ATOM   6391  CD1 PHE B 396       4.355  -5.964 500.085  1.00116.25      B    C  
ANISOU 6391  CD1 PHE B 396    17300  14662  12206  -1647  -3180   5096  B    C  
ATOM   6392  CD2 PHE B 396       6.308  -6.620 501.285  1.00107.48      B    C  
ANISOU 6392  CD2 PHE B 396    16318  13512  11009  -1520  -3774   5628  B    C  
ATOM   6393  CE1 PHE B 396       5.123  -5.563 499.014  1.00112.03      B    C  
ANISOU 6393  CE1 PHE B 396    16581  13916  12068  -1257  -3201   4864  B    C  
ATOM   6394  CE2 PHE B 396       7.087  -6.233 500.212  1.00113.19      B    C  
ANISOU 6394  CE2 PHE B 396    16850  14017  12138  -1127  -3799   5393  B    C  
ATOM   6395  CZ  PHE B 396       6.493  -5.698 499.074  1.00111.57      B    C  
ANISOU 6395  CZ  PHE B 396    16491  13730  12169  -1002  -3502   5004  B    C  
ATOM   6396  N   TRP B 397       2.283  -9.047 501.292  1.00135.48      B    N  
ANISOU 6396  N   TRP B 397    20399  16781  14298  -2427  -3218   5942  B    N  
ATOM   6397  CA  TRP B 397       1.572  -9.567 500.129  1.00127.01      B    C  
ANISOU 6397  CA  TRP B 397    19337  15370  13550  -2354  -3063   5855  B    C  
ATOM   6398  C   TRP B 397       0.573  -8.542 499.609  1.00118.21      B    C  
ANISOU 6398  C   TRP B 397    18018  14510  12387  -2410  -2682   5379  B    C  
ATOM   6399  O   TRP B 397      -0.107  -7.873 500.391  1.00111.84      B    O  
ANISOU 6399  O   TRP B 397    17186  14118  11189  -2704  -2506   5251  B    O  
ATOM   6400  CB  TRP B 397       0.863 -10.909 500.359  1.00129.67      B    C  
ANISOU 6400  CB  TRP B 397    19875  15489  13905  -2563  -3029   6073  B    C  
ATOM   6401  CG  TRP B 397       0.324 -11.508 499.043  1.00128.19      B    C  
ANISOU 6401  CG  TRP B 397    19680  14907  14118  -2433  -2898   5976  B    C  
ATOM   6402  CD1 TRP B 397      -0.811 -12.267 498.898  1.00123.36      B    C  
ANISOU 6402  CD1 TRP B 397    19196  14190  13486  -2681  -2717   6014  B    C  
ATOM   6403  CD2 TRP B 397       0.866 -11.346 497.706  1.00127.44      B    C  
ANISOU 6403  CD2 TRP B 397    19431  14504  14486  -2049  -2920   5795  B    C  
ATOM   6404  CE2 TRP B 397       0.016 -12.046 496.824  1.00126.21      B    C  
ANISOU 6404  CE2 TRP B 397    19319  14071  14563  -2091  -2750   5737  B    C  
ATOM   6405  CE3 TRP B 397       1.994 -10.695 497.175  1.00121.36      B    C  
ANISOU 6405  CE3 TRP B 397    18474  13677  13960  -1678  -3048   5641  B    C  
ATOM   6406  NE1 TRP B 397      -0.993 -12.598 497.573  1.00125.79      B    N  
ANISOU 6406  NE1 TRP B 397    19439  14146  14208  -2476  -2631   5878  B    N  
ATOM   6407  CZ2 TRP B 397       0.256 -12.107 495.445  1.00119.57      B    C  
ANISOU 6407  CZ2 TRP B 397    18325  12922  14183  -1773  -2693   5506  B    C  
ATOM   6408  CZ3 TRP B 397       2.217 -10.747 495.808  1.00117.82      B    C  
ANISOU 6408  CZ3 TRP B 397    17879  12921  13966  -1369  -2983   5407  B    C  
ATOM   6409  CH2 TRP B 397       1.356 -11.450 494.961  1.00116.42      B    C  
ANISOU 6409  CH2 TRP B 397    17743  12488  14005  -1421  -2810   5345  B    C  
ATOM   6410  N   HIS B 398       0.487  -8.418 498.288  1.00117.05      B    N  
ANISOU 6410  N   HIS B 398    17717  14115  12640  -2133  -2558   5112  B    N  
ATOM   6411  CA  HIS B 398      -0.312  -7.373 497.674  1.00114.30      B    C  
ANISOU 6411  CA  HIS B 398    17150  13974  12304  -2117  -2237   4659  B    C  
ATOM   6412  C   HIS B 398      -0.812  -7.896 496.340  1.00117.22      B    C  
ANISOU 6412  C   HIS B 398    17479  13997  13063  -1967  -2113   4529  B    C  
ATOM   6413  O   HIS B 398      -0.056  -8.521 495.588  1.00117.89      B    O  
ANISOU 6413  O   HIS B 398    17580  13701  13511  -1699  -2278   4631  B    O  
ATOM   6414  CB  HIS B 398       0.535  -6.128 497.404  1.00116.88      B    C  
ANISOU 6414  CB  HIS B 398    17245  14452  12711  -1837  -2249   4377  B    C  
ATOM   6415  CG  HIS B 398       1.549  -6.323 496.312  1.00120.39      B    C  
ANISOU 6415  CG  HIS B 398    17608  14526  13608  -1431  -2401   4346  B    C  
ATOM   6416  CD2 HIS B 398       1.532  -5.951 495.008  1.00117.26      B    C  
ANISOU 6416  CD2 HIS B 398    17043  13955  13556  -1173  -2274   4048  B    C  
ATOM   6417  ND1 HIS B 398       2.738  -6.998 496.500  1.00123.37      B    N  
ANISOU 6417  ND1 HIS B 398    18077  14669  14127  -1263  -2720   4640  B    N  
ATOM   6418  CE1 HIS B 398       3.414  -7.022 495.364  1.00118.66      B    C  
ANISOU 6418  CE1 HIS B 398    17362  13775  13948   -921  -2769   4501  B    C  
ATOM   6419  NE2 HIS B 398       2.704  -6.392 494.443  1.00119.94      B    N  
ANISOU 6419  NE2 HIS B 398    17374  13973  14226   -871  -2500   4148  B    N  
ATOM   6420  N   SER B 399      -2.102  -7.682 496.081  1.00120.58      B    N  
ANISOU 6420  N   SER B 399    17848  14561  13404  -2158  -1824   4305  B    N  
ATOM   6421  CA  SER B 399      -2.705  -7.950 494.780  1.00121.02      B    C  
ANISOU 6421  CA  SER B 399    17820  14370  13791  -2033  -1665   4109  B    C  
ATOM   6422  C   SER B 399      -4.149  -7.470 494.771  1.00118.73      B    C  
ANISOU 6422  C   SER B 399    17439  14352  13320  -2279  -1348   3839  B    C  
ATOM   6423  O   SER B 399      -4.818  -7.453 495.813  1.00108.05      B    O  
ANISOU 6423  O   SER B 399    16171  13283  11600  -2620  -1262   3904  B    O  
ATOM   6424  CB  SER B 399      -2.652  -9.420 494.382  1.00119.72      B    C  
ANISOU 6424  CB  SER B 399    17847  13778  13863  -2033  -1785   4397  B    C  
ATOM   6425  OG  SER B 399      -3.432  -9.612 493.209  1.00111.83      B    O  
ANISOU 6425  OG  SER B 399    16757  12615  13117  -1980  -1586   4171  B    O  
ATOM   6426  N   HIS B 400      -4.644  -7.130 493.588  1.00117.18      B    N  
ANISOU 6426  N   HIS B 400    17071  14070  13383  -2120  -1179   3539  B    N  
ATOM   6427  CA  HIS B 400      -6.030  -6.733 493.394  1.00110.28      B    C  
ANISOU 6427  CA  HIS B 400    16083  13409  12408  -2312   -891   3266  B    C  
ATOM   6428  C   HIS B 400      -6.838  -7.926 492.899  1.00111.27      B    C  
ANISOU 6428  C   HIS B 400    16330  13294  12652  -2458   -816   3371  B    C  
ATOM   6429  O   HIS B 400      -6.631  -8.414 491.780  1.00106.91      B    O  
ANISOU 6429  O   HIS B 400    15756  12421  12445  -2250   -847   3348  B    O  
ATOM   6430  CB  HIS B 400      -6.101  -5.558 492.422  1.00103.04      B    C  
ANISOU 6430  CB  HIS B 400    14896  12566  11688  -2053   -764   2877  B    C  
ATOM   6431  CG  HIS B 400      -5.390  -5.805 491.128  1.00108.42      B    C  
ANISOU 6431  CG  HIS B 400    15529  12894  12774  -1716   -865   2848  B    C  
ATOM   6432  CD2 HIS B 400      -5.851  -6.186 489.913  1.00111.87      B    C  
ANISOU 6432  CD2 HIS B 400    15905  13112  13487  -1620   -777   2726  B    C  
ATOM   6433  ND1 HIS B 400      -4.027  -5.644 490.990  1.00103.96      B    N  
ANISOU 6433  ND1 HIS B 400    14962  12182  12357  -1447  -1075   2931  B    N  
ATOM   6434  CE1 HIS B 400      -3.678  -5.923 489.747  1.00101.32      B    C  
ANISOU 6434  CE1 HIS B 400    14570  11549  12376  -1206  -1106   2857  B    C  
ATOM   6435  NE2 HIS B 400      -4.766  -6.252 489.072  1.00106.76      B    N  
ANISOU 6435  NE2 HIS B 400    15227  12194  13144  -1309   -928   2736  B    N  
ATOM   6436  N   MET B 401      -7.737  -8.389 493.761  1.00116.44      B    N  
ANISOU 6436  N   MET B 401    17115  14117  13011  -2835   -710   3477  B    N  
ATOM   6437  CA  MET B 401      -8.653  -9.504 493.535  1.00123.73      B    C  
ANISOU 6437  CA  MET B 401    18171  14875  13965  -3062   -607   3577  B    C  
ATOM   6438  C   MET B 401      -7.940 -10.665 492.842  1.00127.94      B    C  
ANISOU 6438  C   MET B 401    18851  14927  14831  -2883   -793   3830  B    C  
ATOM   6439  O   MET B 401      -8.200 -10.989 491.683  1.00128.14      B    O  
ANISOU 6439  O   MET B 401    18800  14724  15163  -2743   -718   3693  B    O  
ATOM   6440  CB  MET B 401      -9.880  -9.054 492.729  1.00122.87      B    C  
ANISOU 6440  CB  MET B 401    17854  14896  13935  -3100   -328   3201  B    C  
ATOM   6441  CG  MET B 401     -10.990 -10.123 492.580  1.00125.04      B    C  
ANISOU 6441  CG  MET B 401    18245  15070  14193  -3387   -179   3256  B    C  
ATOM   6442  SD  MET B 401     -11.651 -10.821 494.134  1.00137.37      B    S  
ANISOU 6442  SD  MET B 401    20064  16837  15293  -3912   -128   3520  B    S  
ATOM   6443  CE  MET B 401     -13.065  -9.753 494.453  1.00127.04      B    C  
ANISOU 6443  CE  MET B 401    18512  16032  13726  -4158    203   3086  B    C  
ATOM   6444  N   LEU B 402      -6.975 -11.258 493.555  1.00128.28      B    N  
ANISOU 6444  N   LEU B 402    19095  14818  14827  -2874  -1049   4195  B    N  
ATOM   6445  CA  LEU B 402      -6.380 -12.488 493.038  1.00123.93      B    C  
ANISOU 6445  CA  LEU B 402    18702  13794  14592  -2746  -1225   4459  B    C  
ATOM   6446  C   LEU B 402      -7.402 -13.604 492.974  1.00122.00      B    C  
ANISOU 6446  C   LEU B 402    18620  13398  14338  -3038  -1093   4570  B    C  
ATOM   6447  O   LEU B 402      -7.354 -14.444 492.064  1.00114.49      B    O  
ANISOU 6447  O   LEU B 402    17701  12076  13723  -2925  -1104   4598  B    O  
ATOM   6448  CB  LEU B 402      -5.161 -12.945 493.834  1.00123.11      B    C  
ANISOU 6448  CB  LEU B 402    18777  13540  14460  -2674  -1546   4845  B    C  
ATOM   6449  CG  LEU B 402      -3.870 -12.514 493.139  1.00116.33      B    C  
ANISOU 6449  CG  LEU B 402    17772  12504  13923  -2242  -1726   4765  B    C  
ATOM   6450  CD1 LEU B 402      -2.676 -12.812 494.017  1.00122.28      B    C  
ANISOU 6450  CD1 LEU B 402    18667  13175  14619  -2169  -2049   5119  B    C  
ATOM   6451  CD2 LEU B 402      -3.746 -13.149 491.756  1.00105.03      B    C  
ANISOU 6451  CD2 LEU B 402    16282  10666  12957  -2014  -1703   4662  B    C  
ATOM   6452  N   LYS B 403      -8.302 -13.659 493.959  1.00128.66      B    N  
ANISOU 6452  N   LYS B 403    19572  14521  14792  -3430   -967   4634  B    N  
ATOM   6453  CA  LYS B 403      -9.239 -14.765 494.110  1.00129.12      B    C  
ANISOU 6453  CA  LYS B 403    19823  14456  14782  -3763   -853   4782  B    C  
ATOM   6454  C   LYS B 403      -8.498 -16.042 494.459  1.00135.60      B    C  
ANISOU 6454  C   LYS B 403    20933