CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 2210061134239865

Job options:

ID        	=	 2210061134239865
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:



ATOM      1  N   VAL A  31      14.803  29.611  60.496  1.00122.89           N  
ANISOU    1  N   VAL A  31    21367  13436  11891  -4519  -1805  -5164       N  
ATOM      2  CA  VAL A  31      15.613  28.402  60.562  1.00121.24           C  
ANISOU    2  CA  VAL A  31    20718  13779  11569  -4554  -2225  -5015       C  
ATOM      3  C   VAL A  31      15.789  27.878  59.130  1.00115.76           C  
ANISOU    3  C   VAL A  31    19647  13079  11259  -4518  -2184  -4728       C  
ATOM      4  O   VAL A  31      15.461  28.574  58.170  1.00114.23           O  
ANISOU    4  O   VAL A  31    19528  12473  11400  -4537  -1879  -4682       O  
ATOM      5  CB  VAL A  31      14.970  27.358  61.518  1.00119.33           C  
ANISOU    5  CB  VAL A  31    20604  13840  10895  -4217  -2287  -4923       C  
ATOM      6  CG1 VAL A  31      13.712  26.756  60.907  1.00113.28           C  
ANISOU    6  CG1 VAL A  31    19944  12887  10209  -3802  -1928  -4658       C  
ATOM      7  CG2 VAL A  31      15.978  26.290  61.972  1.00120.17           C  
ANISOU    7  CG2 VAL A  31    20322  14548  10790  -4284  -2794  -4830       C  
ATOM      8  N   TRP A  32      16.301  26.657  58.987  1.00120.55           N  
ANISOU    8  N   TRP A  32    19861  14137  11807  -4452  -2487  -4527       N  
ATOM      9  CA  TRP A  32      16.697  26.095  57.701  1.00116.34           C  
ANISOU    9  CA  TRP A  32    18915  13677  11612  -4470  -2516  -4280       C  
ATOM     10  C   TRP A  32      15.519  25.522  56.920  1.00110.38           C  
ANISOU   10  C   TRP A  32    18285  12702  10951  -4097  -2191  -4030       C  
ATOM     11  O   TRP A  32      15.727  24.892  55.878  1.00106.69           O  
ANISOU   11  O   TRP A  32    17508  12314  10716  -4066  -2211  -3810       O  
ATOM     12  CB  TRP A  32      17.749  25.007  57.931  1.00119.55           C  
ANISOU   12  CB  TRP A  32    18841  14674  11908  -4525  -2988  -4165       C  
ATOM     13  CG  TRP A  32      18.936  25.491  58.715  1.00125.92           C  
ANISOU   13  CG  TRP A  32    19471  15753  12620  -4872  -3349  -4398       C  
ATOM     14  CD1 TRP A  32      19.252  26.787  59.016  1.00130.88           C  
ANISOU   14  CD1 TRP A  32    20289  16129  13311  -5197  -3291  -4690       C  
ATOM     15  CD2 TRP A  32      19.930  24.681  59.353  1.00128.60           C  
ANISOU   15  CD2 TRP A  32    19426  16669  12767  -4907  -3834  -4356       C  
ATOM     16  NE1 TRP A  32      20.394  26.833  59.776  1.00136.46           N  
ANISOU   16  NE1 TRP A  32    20743  17224  13881  -5462  -3718  -4848       N  
ATOM     17  CE2 TRP A  32      20.830  25.553  59.998  1.00135.21           C  
ANISOU   17  CE2 TRP A  32    20217  17590  13568  -5275  -4061  -4641       C  
ATOM     18  CE3 TRP A  32      20.154  23.303  59.429  1.00126.43           C  
ANISOU   18  CE3 TRP A  32    18841  16842  12354  -4646  -4104  -4088       C  
ATOM     19  CZ2 TRP A  32      21.935  25.092  60.709  1.00139.71           C  
ANISOU   19  CZ2 TRP A  32    20418  18694  13972  -5381  -4557  -4670       C  
ATOM     20  CZ3 TRP A  32      21.252  22.848  60.135  1.00130.86           C  
ANISOU   20  CZ3 TRP A  32    19042  17923  12756  -4721  -4583  -4096       C  
ATOM     21  CH2 TRP A  32      22.128  23.739  60.766  1.00137.44           C  
ANISOU   21  CH2 TRP A  32    19813  18848  13558  -5082  -4811  -4388       C  
ATOM     22  N   VAL A  33      14.296  25.732  57.408  1.00110.70           N  
ANISOU   22  N   VAL A  33    18760  12482  10820  -3815  -1888  -4065       N  
ATOM     23  CA  VAL A  33      13.101  25.170  56.784  1.00105.66           C  
ANISOU   23  CA  VAL A  33    18240  11659  10247  -3437  -1583  -3836       C  
ATOM     24  C   VAL A  33      12.735  25.913  55.502  1.00103.88           C  
ANISOU   24  C   VAL A  33    18039  10996  10435  -3441  -1258  -3761       C  
ATOM     25  O   VAL A  33      12.148  25.323  54.586  1.00102.15           O  
ANISOU   25  O   VAL A  33    17675  10730  10408  -3174  -1096  -3491       O  
ATOM     26  CB  VAL A  33      11.948  25.178  57.806  1.00108.73           C  
ANISOU   26  CB  VAL A  33    19039  11955  10319  -3137  -1356  -3900       C  
ATOM     27  CG1 VAL A  33      10.626  24.847  57.155  1.00105.08           C  
ANISOU   27  CG1 VAL A  33    18705  11247   9972  -2756   -981  -3696       C  
ATOM     28  CG2 VAL A  33      12.235  24.186  58.925  1.00110.02           C  
ANISOU   28  CG2 VAL A  33    19158  12581  10064  -3074  -1665  -3878       C  
ATOM     29  N   VAL A  34      13.083  27.200  55.406  1.00103.89           N  
ANISOU   29  N   VAL A  34    18161  10704  10610  -3689  -1154  -3940       N  
ATOM     30  CA  VAL A  34      12.740  27.995  54.227  1.00102.66           C  
ANISOU   30  CA  VAL A  34    18065  10112  10829  -3676   -837  -3841       C  
ATOM     31  C   VAL A  34      13.296  27.364  52.957  1.00 99.37           C  
ANISOU   31  C   VAL A  34    17250   9822  10682  -3762   -925  -3610       C  
ATOM     32  O   VAL A  34      12.696  27.480  51.881  1.00 97.65           O  
ANISOU   32  O   VAL A  34    17060   9330  10711  -3595   -660  -3417       O  
ATOM     33  CB  VAL A  34      13.241  29.443  54.408  1.00 99.67           C  
ANISOU   33  CB  VAL A  34    17867   9435  10568  -3983   -766  -4069       C  
ATOM     34  CG1 VAL A  34      12.959  30.279  53.167  1.00 98.89           C  
ANISOU   34  CG1 VAL A  34    17836   8892  10846  -3966   -451  -3927       C  
ATOM     35  CG2 VAL A  34      12.608  30.072  55.639  1.00103.54           C  
ANISOU   35  CG2 VAL A  34    18784   9771  10784  -3876   -645  -4305       C  
ATOM     36  N   GLY A  35      14.436  26.677  53.058  1.00 98.21           N  
ANISOU   36  N   GLY A  35    16716  10108  10490  -4005  -1295  -3613       N  
ATOM     37  CA  GLY A  35      14.994  26.017  51.888  1.00 97.81           C  
ANISOU   37  CA  GLY A  35    16176  10256  10729  -3996  -1348  -3339       C  
ATOM     38  C   GLY A  35      14.101  24.909  51.364  1.00 96.48           C  
ANISOU   38  C   GLY A  35    15841  10207  10610  -3484  -1215  -2994       C  
ATOM     39  O   GLY A  35      13.775  24.866  50.176  1.00 95.31           O  
ANISOU   39  O   GLY A  35    15562   9916  10736  -3334  -1001  -2762       O  
ATOM     40  N   MET A  36      13.685  24.000  52.251  1.00 97.37           N  
ANISOU   40  N   MET A  36    15978  10581  10439  -3227  -1339  -2957       N  
ATOM     41  CA  MET A  36      12.822  22.898  51.834  1.00 96.22           C  
ANISOU   41  CA  MET A  36    15689  10544  10328  -2782  -1216  -2646       C  
ATOM     42  C   MET A  36      11.457  23.389  51.373  1.00 94.66           C  
ANISOU   42  C   MET A  36    15777   9958  10230  -2517   -828  -2566       C  
ATOM     43  O   MET A  36      10.842  22.765  50.500  1.00 93.51           O  
ANISOU   43  O   MET A  36    15450   9827  10253  -2240   -686  -2294       O  
ATOM     44  CB  MET A  36      12.662  21.893  52.974  1.00105.77           C  
ANISOU   44  CB  MET A  36    16920  12077  11192  -2598  -1410  -2627       C  
ATOM     45  CG  MET A  36      13.928  21.127  53.308  1.00107.46           C  
ANISOU   45  CG  MET A  36    16769  12734  11325  -2735  -1811  -2604       C  
ATOM     46  SD  MET A  36      13.677  19.917  54.620  1.00108.24           S  
ANISOU   46  SD  MET A  36    16946  13182  10998  -2473  -2023  -2523       S  
ATOM     47  CE  MET A  36      13.587  20.989  56.054  1.00109.05           C  
ANISOU   47  CE  MET A  36    17565  13181  10689  -2730  -2092  -2920       C  
ATOM     48  N   GLY A  37      10.964  24.489  51.945  1.00 91.59           N  
ANISOU   48  N   GLY A  37    15830   9230   9740  -2589   -657  -2802       N  
ATOM     49  CA  GLY A  37       9.696  25.038  51.492  1.00 90.48           C  
ANISOU   49  CA  GLY A  37    15936   8720   9723  -2308   -284  -2717       C  
ATOM     50  C   GLY A  37       9.726  25.426  50.027  1.00 89.52           C  
ANISOU   50  C   GLY A  37    15656   8395   9964  -2308   -135  -2518       C  
ATOM     51  O   GLY A  37       8.811  25.103  49.264  1.00 88.47           O  
ANISOU   51  O   GLY A  37    15435   8212   9969  -1986     51  -2265       O  
ATOM     52  N   ILE A  38      10.784  26.127  49.613  1.00 89.61           N  
ANISOU   52  N   ILE A  38    15626   8301  10119  -2688   -219  -2625       N  
ATOM     53  CA  ILE A  38      10.936  26.479  48.204  1.00 88.82           C  
ANISOU   53  CA  ILE A  38    15382   8029  10335  -2723    -78  -2421       C  
ATOM     54  C   ILE A  38      11.131  25.224  47.365  1.00 88.21           C  
ANISOU   54  C   ILE A  38    14836   8323  10356  -2564   -185  -2131       C  
ATOM     55  O   ILE A  38      10.525  25.073  46.296  1.00 87.07           O  
ANISOU   55  O   ILE A  38    14609   8098  10376  -2340    -16  -1879       O  
ATOM     56  CB  ILE A  38      12.102  27.468  48.023  1.00 89.37           C  
ANISOU   56  CB  ILE A  38    15504   7925  10527  -3217   -133  -2608       C  
ATOM     57  CG1 ILE A  38      11.822  28.758  48.791  1.00 89.93           C  
ANISOU   57  CG1 ILE A  38    16112   7550  10509  -3373     13  -2911       C  
ATOM     58  CG2 ILE A  38      12.324  27.769  46.551  1.00 88.66           C  
ANISOU   58  CG2 ILE A  38    15264   7685  10738  -3266     24  -2371       C  
ATOM     59  CD1 ILE A  38      13.021  29.668  48.899  1.00 92.10           C  
ANISOU   59  CD1 ILE A  38    16359   7761  10874  -3855    -89  -3104       C  
ATOM     60  N   VAL A  39      11.977  24.304  47.836  1.00 86.13           N  
ANISOU   60  N   VAL A  39    14274   8468   9983  -2667   -471  -2163       N  
ATOM     61  CA  VAL A  39      12.215  23.058  47.108  1.00 85.84           C  
ANISOU   61  CA  VAL A  39    13820   8762  10032  -2503   -561  -1911       C  
ATOM     62  C   VAL A  39      10.909  22.301  46.903  1.00 84.53           C  
ANISOU   62  C   VAL A  39    13687   8605   9826  -2082   -416  -1703       C  
ATOM     63  O   VAL A  39      10.585  21.878  45.788  1.00 83.51           O  
ANISOU   63  O   VAL A  39    13389   8488   9854  -1925   -310  -1475       O  
ATOM     64  CB  VAL A  39      13.259  22.196  47.842  1.00 85.55           C  
ANISOU   64  CB  VAL A  39    13499   9146   9862  -2621   -893  -1980       C  
ATOM     65  CG1 VAL A  39      13.361  20.823  47.197  1.00 85.48           C  
ANISOU   65  CG1 VAL A  39    13122   9431   9924  -2379   -950  -1723       C  
ATOM     66  CG2 VAL A  39      14.611  22.886  47.831  1.00 87.02           C  
ANISOU   66  CG2 VAL A  39    13539   9383  10142  -3064  -1046  -2155       C  
ATOM     67  N   MET A  40      10.131  22.132  47.974  1.00 85.53           N  
ANISOU   67  N   MET A  40    14035   8734   9730  -1913   -403  -1786       N  
ATOM     68  CA  MET A  40       8.881  21.389  47.857  1.00 84.60           C  
ANISOU   68  CA  MET A  40    13915   8650   9578  -1548   -260  -1595       C  
ATOM     69  C   MET A  40       7.851  22.156  47.034  1.00 83.58           C  
ANISOU   69  C   MET A  40    13933   8206   9617  -1381     22  -1488       C  
ATOM     70  O   MET A  40       7.087  21.553  46.272  1.00 82.72           O  
ANISOU   70  O   MET A  40    13675   8158   9598  -1149    112  -1262       O  
ATOM     71  CB  MET A  40       8.336  21.057  49.245  1.00 87.44           C  
ANISOU   71  CB  MET A  40    14477   9098   9647  -1430   -285  -1708       C  
ATOM     72  CG  MET A  40       9.199  20.064  50.007  1.00 88.47           C  
ANISOU   72  CG  MET A  40    14444   9583   9587  -1507   -579  -1731       C  
ATOM     73  SD  MET A  40       8.574  19.694  51.655  1.00 89.23           S  
ANISOU   73  SD  MET A  40    14830   9787   9287  -1378   -596  -1842       S  
ATOM     74  CE  MET A  40       9.872  18.626  52.274  1.00 90.60           C  
ANISOU   74  CE  MET A  40    14765  10376   9284  -1487   -999  -1820       C  
ATOM     75  N   SER A  41       7.817  23.485  47.168  1.00 83.25           N  
ANISOU   75  N   SER A  41    14192   7824   9617  -1496    156  -1645       N  
ATOM     76  CA  SER A  41       6.888  24.281  46.370  1.00 82.63           C  
ANISOU   76  CA  SER A  41    14263   7426   9707  -1305    418  -1517       C  
ATOM     77  C   SER A  41       7.195  24.160  44.883  1.00 81.77           C  
ANISOU   77  C   SER A  41    13921   7335   9814  -1334    423  -1282       C  
ATOM     78  O   SER A  41       6.279  24.129  44.053  1.00 81.15           O  
ANISOU   78  O   SER A  41    13803   7195   9835  -1079    560  -1063       O  
ATOM     79  CB  SER A  41       6.933  25.744  46.809  1.00 83.63           C  
ANISOU   79  CB  SER A  41    14798   7134   9844  -1439    567  -1738       C  
ATOM     80  OG  SER A  41       6.489  25.890  48.146  1.00 84.40           O  
ANISOU   80  OG  SER A  41    15159   7195   9714  -1371    610  -1960       O  
ATOM     81  N   LEU A  42       8.480  24.095  44.526  1.00 80.08           N  
ANISOU   81  N   LEU A  42    13539   7227   9661  -1644    275  -1323       N  
ATOM     82  CA  LEU A  42       8.848  23.897  43.128  1.00 79.40           C  
ANISOU   82  CA  LEU A  42    13230   7192   9745  -1681    298  -1108       C  
ATOM     83  C   LEU A  42       8.493  22.495  42.652  1.00 78.66           C  
ANISOU   83  C   LEU A  42    12835   7429   9623  -1462    221   -915       C  
ATOM     84  O   LEU A  42       8.129  22.309  41.484  1.00 77.82           O  
ANISOU   84  O   LEU A  42    12631   7326   9610  -1345    303   -702       O  
ATOM     85  CB  LEU A  42      10.340  24.164  42.932  1.00 80.35           C  
ANISOU   85  CB  LEU A  42    13216   7367   9945  -2076    188  -1213       C  
ATOM     86  CG  LEU A  42      10.815  25.600  43.169  1.00 81.09           C  
ANISOU   86  CG  LEU A  42    13604   7100  10105  -2380    278  -1397       C  
ATOM     87  CD1 LEU A  42      12.330  25.689  43.063  1.00 82.21           C  
ANISOU   87  CD1 LEU A  42    13523   7388  10325  -2805    140  -1508       C  
ATOM     88  CD2 LEU A  42      10.144  26.562  42.201  1.00 80.40           C  
ANISOU   88  CD2 LEU A  42    13766   6622  10160  -2270    540  -1228       C  
ATOM     89  N   ILE A  43       8.595  21.499  43.534  1.00 77.60           N  
ANISOU   89  N   ILE A  43    12579   7561   9345  -1413     64   -984       N  
ATOM     90  CA  ILE A  43       8.207  20.143  43.163  1.00 77.00           C  
ANISOU   90  CA  ILE A  43    12269   7748   9242  -1214     11   -814       C  
ATOM     91  C   ILE A  43       6.705  20.068  42.922  1.00 76.24           C  
ANISOU   91  C   ILE A  43    12256   7571   9140   -926    164   -673       C  
ATOM     92  O   ILE A  43       6.245  19.377  42.006  1.00 75.43           O  
ANISOU   92  O   ILE A  43    11994   7579   9089   -801    184   -491       O  
ATOM     93  CB  ILE A  43       8.664  19.139  44.238  1.00 75.42           C  
ANISOU   93  CB  ILE A  43    11964   7811   8883  -1220   -181   -903       C  
ATOM     94  CG1 ILE A  43      10.191  19.099  44.312  1.00 76.72           C  
ANISOU   94  CG1 ILE A  43    11946   8125   9079  -1479   -362  -1003       C  
ATOM     95  CG2 ILE A  43       8.113  17.749  43.950  1.00 74.90           C  
ANISOU   95  CG2 ILE A  43    11728   7945   8786  -1006   -198   -732       C  
ATOM     96  CD1 ILE A  43      10.723  18.350  45.514  1.00 78.18           C  
ANISOU   96  CD1 ILE A  43    12065   8554   9085  -1488   -583  -1099       C  
ATOM     97  N   VAL A  44       5.918  20.788  43.724  1.00 75.70           N  
ANISOU   97  N   VAL A  44    12432   7321   9010   -822    279   -764       N  
ATOM     98  CA  VAL A  44       4.472  20.809  43.513  1.00 75.66           C  
ANISOU   98  CA  VAL A  44    12460   7258   9027   -533    438   -625       C  
ATOM     99  C   VAL A  44       4.141  21.446  42.169  1.00 75.11           C  
ANISOU   99  C   VAL A  44    12381   7036   9121   -464    538   -443       C  
ATOM    100  O   VAL A  44       3.244  20.988  41.452  1.00 74.95           O  
ANISOU  100  O   VAL A  44    12219   7119   9138   -273    570   -251       O  
ATOM    101  CB  VAL A  44       3.768  21.533  44.676  1.00 75.31           C  
ANISOU  101  CB  VAL A  44    12686   7039   8889   -418    579   -775       C  
ATOM    102  CG1 VAL A  44       2.279  21.660  44.400  1.00 75.84           C  
ANISOU  102  CG1 VAL A  44    12739   7058   9019    -99    766   -618       C  
ATOM    103  CG2 VAL A  44       4.001  20.791  45.980  1.00 75.95           C  
ANISOU  103  CG2 VAL A  44    12789   7311   8756   -468    477   -921       C  
ATOM    104  N   LEU A  45       4.865  22.506  41.801  1.00 74.15           N  
ANISOU  104  N   LEU A  45    12414   6674   9087   -635    581   -493       N  
ATOM    105  CA  LEU A  45       4.636  23.142  40.507  1.00 73.81           C  
ANISOU  105  CA  LEU A  45    12400   6471   9174   -577    678   -293       C  
ATOM    106  C   LEU A  45       5.054  22.230  39.361  1.00 72.95           C  
ANISOU  106  C   LEU A  45    12027   6612   9080   -641    577   -133       C  
ATOM    107  O   LEU A  45       4.293  22.026  38.409  1.00 72.74           O  
ANISOU  107  O   LEU A  45    11920   6645   9072   -467    604     76       O  
ATOM    108  CB  LEU A  45       5.381  24.474  40.432  1.00 73.36           C  
ANISOU  108  CB  LEU A  45    12605   6067   9203   -786    771   -385       C  
ATOM    109  CG  LEU A  45       4.867  25.598  41.329  1.00 74.22           C  
ANISOU  109  CG  LEU A  45    13059   5826   9314   -698    926   -532       C  
ATOM    110  CD1 LEU A  45       5.789  26.802  41.240  1.00 74.57           C  
ANISOU  110  CD1 LEU A  45    13369   5519   9445   -992   1002   -649       C  
ATOM    111  CD2 LEU A  45       3.445  25.974  40.941  1.00 74.62           C  
ANISOU  111  CD2 LEU A  45    13181   5748   9423   -301   1086   -332       C  
ATOM    112  N   ALA A  46       6.270  21.677  39.433  1.00 72.24           N  
ANISOU  112  N   ALA A  46    11796   6680   8973   -884    459   -234       N  
ATOM    113  CA  ALA A  46       6.754  20.798  38.372  1.00 71.61           C  
ANISOU  113  CA  ALA A  46    11485   6822   8903   -937    398   -110       C  
ATOM    114  C   ALA A  46       5.833  19.604  38.164  1.00 71.05           C  
ANISOU  114  C   ALA A  46    11256   6979   8760   -727    344     -1       C  
ATOM    115  O   ALA A  46       5.739  19.077  37.049  1.00 70.53           O  
ANISOU  115  O   ALA A  46    11077   7031   8689   -699    338    140       O  
ATOM    116  CB  ALA A  46       8.172  20.326  38.689  1.00 68.74           C  
ANISOU  116  CB  ALA A  46    10960   6615   8544  -1182    286   -250       C  
ATOM    117  N   ILE A  47       5.147  19.166  39.217  1.00 69.63           N  
ANISOU  117  N   ILE A  47    11084   6861   8511   -600    314    -72       N  
ATOM    118  CA  ILE A  47       4.177  18.086  39.084  1.00 69.40           C  
ANISOU  118  CA  ILE A  47    10917   7023   8428   -434    285     29       C  
ATOM    119  C   ILE A  47       2.892  18.589  38.440  1.00 69.90           C  
ANISOU  119  C   ILE A  47    11005   7023   8529   -235    373    195       C  
ATOM    120  O   ILE A  47       2.406  18.014  37.460  1.00 69.72           O  
ANISOU  120  O   ILE A  47    10853   7142   8496   -183    336    338       O  
ATOM    121  CB  ILE A  47       3.905  17.444  40.455  1.00 70.37           C  
ANISOU  121  CB  ILE A  47    11044   7235   8457   -384    249    -85       C  
ATOM    122  CG1 ILE A  47       5.133  16.671  40.942  1.00 70.32           C  
ANISOU  122  CG1 ILE A  47    10959   7360   8398   -536    116   -193       C  
ATOM    123  CG2 ILE A  47       2.683  16.559  40.388  1.00 70.65           C  
ANISOU  123  CG2 ILE A  47    10968   7417   8460   -226    269     26       C  
ATOM    124  CD1 ILE A  47       5.047  16.238  42.391  1.00 71.33           C  
ANISOU  124  CD1 ILE A  47    11153   7552   8396   -504     68   -303       C  
ATOM    125  N   VAL A  48       2.320  19.665  38.980  1.00 71.01           N  
ANISOU  125  N   VAL A  48    11315   6958   8709   -114    486    174       N  
ATOM    126  CA  VAL A  48       1.037  20.156  38.480  1.00 72.11           C  
ANISOU  126  CA  VAL A  48    11445   7053   8899    134    568    347       C  
ATOM    127  C   VAL A  48       1.193  20.725  37.075  1.00 71.85           C  
ANISOU  127  C   VAL A  48    11442   6945   8912    130    565    529       C  
ATOM    128  O   VAL A  48       0.536  20.275  36.128  1.00 72.29           O  
ANISOU  128  O   VAL A  48    11349   7174   8943    223    502    704       O  
ATOM    129  CB  VAL A  48       0.441  21.195  39.446  1.00 69.01           C  
ANISOU  129  CB  VAL A  48    11249   6427   8544    302    725    271       C  
ATOM    130  CG1 VAL A  48      -0.813  21.814  38.846  1.00 70.40           C  
ANISOU  130  CG1 VAL A  48    11395   6549   8804    601    816    478       C  
ATOM    131  CG2 VAL A  48       0.122  20.547  40.786  1.00 69.70           C  
ANISOU  131  CG2 VAL A  48    11308   6632   8542    326    745    118       C  
ATOM    132  N   PHE A  49       2.065  21.726  36.921  1.00 74.20           N  
ANISOU  132  N   PHE A  49    11945   6986   9261      2    633    491       N  
ATOM    133  CA  PHE A  49       2.224  22.385  35.628  1.00 74.24           C  
ANISOU  133  CA  PHE A  49    12032   6880   9295     -2    666    686       C  
ATOM    134  C   PHE A  49       2.662  21.404  34.547  1.00 73.55           C  
ANISOU  134  C   PHE A  49    11764   7057   9123   -129    557    771       C  
ATOM    135  O   PHE A  49       2.265  21.542  33.384  1.00 74.05           O  
ANISOU  135  O   PHE A  49    11826   7165   9143    -47    543    980       O  
ATOM    136  CB  PHE A  49       3.224  23.536  35.748  1.00 76.84           C  
ANISOU  136  CB  PHE A  49    12619   6878   9698   -191    777    604       C  
ATOM    137  CG  PHE A  49       3.368  24.350  34.494  1.00 77.12           C  
ANISOU  137  CG  PHE A  49    12799   6742   9760   -195    854    827       C  
ATOM    138  CD1 PHE A  49       2.403  25.281  34.143  1.00 78.13           C  
ANISOU  138  CD1 PHE A  49    13096   6656   9935     84    946   1026       C  
ATOM    139  CD2 PHE A  49       4.468  24.189  33.668  1.00 76.60           C  
ANISOU  139  CD2 PHE A  49    12704   6732   9668   -458    851    853       C  
ATOM    140  CE1 PHE A  49       2.532  26.035  32.989  1.00 78.53           C  
ANISOU  140  CE1 PHE A  49    13314   6537   9985     96   1015   1265       C  
ATOM    141  CE2 PHE A  49       4.603  24.940  32.511  1.00 77.04           C  
ANISOU  141  CE2 PHE A  49    12923   6629   9719   -472    945   1077       C  
ATOM    142  CZ  PHE A  49       3.633  25.864  32.172  1.00 77.96           C  
ANISOU  142  CZ  PHE A  49    13239   6519   9863   -196   1018   1291       C  
ATOM    143  N   GLY A  50       3.467  20.405  34.908  1.00 70.48           N  
ANISOU  143  N   GLY A  50    11239   6844   8696   -312    481    614       N  
ATOM    144  CA  GLY A  50       3.921  19.444  33.917  1.00 69.93           C  
ANISOU  144  CA  GLY A  50    11024   6996   8548   -416    413    666       C  
ATOM    145  C   GLY A  50       2.835  18.471  33.498  1.00 70.27           C  
ANISOU  145  C   GLY A  50    10916   7277   8507   -275    317    758       C  
ATOM    146  O   GLY A  50       2.701  18.148  32.314  1.00 70.55           O  
ANISOU  146  O   GLY A  50    10917   7436   8454   -285    279    883       O  
ATOM    147  N   ASN A  51       2.043  17.992  34.459  1.00 69.07           N  
ANISOU  147  N   ASN A  51    10678   7196   8367   -166    283    693       N  
ATOM    148  CA  ASN A  51       1.031  16.985  34.158  1.00 69.84           C  
ANISOU  148  CA  ASN A  51    10607   7528   8402    -89    195    758       C  
ATOM    149  C   ASN A  51      -0.246  17.595  33.594  1.00 71.86           C  
ANISOU  149  C   ASN A  51    10827   7815   8664    115    182    953       C  
ATOM    150  O   ASN A  51      -0.965  16.923  32.847  1.00 73.12           O  
ANISOU  150  O   ASN A  51    10842   8191   8747    130     77   1047       O  
ATOM    151  CB  ASN A  51       0.726  16.163  35.408  1.00 71.08           C  
ANISOU  151  CB  ASN A  51    10680   7759   8567    -81    187    626       C  
ATOM    152  CG  ASN A  51       1.854  15.221  35.764  1.00 69.44           C  
ANISOU  152  CG  ASN A  51    10460   7597   8327   -247    150    481       C  
ATOM    153  OD1 ASN A  51       2.381  14.513  34.906  1.00 68.77           O  
ANISOU  153  OD1 ASN A  51    10331   7605   8194   -347    108    487       O  
ATOM    154  ND2 ASN A  51       2.260  15.236  37.027  1.00 69.18           N  
ANISOU  154  ND2 ASN A  51    10478   7500   8310   -261    170    351       N  
ATOM    155  N   VAL A  52      -0.550  18.849  33.937  1.00 71.63           N  
ANISOU  155  N   VAL A  52    10923   7572   8721    276    280   1014       N  
ATOM    156  CA  VAL A  52      -1.606  19.554  33.219  1.00 73.49           C  
ANISOU  156  CA  VAL A  52    11134   7820   8970    507    265   1243       C  
ATOM    157  C   VAL A  52      -1.163  19.831  31.790  1.00 73.32           C  
ANISOU  157  C   VAL A  52    11203   7804   8851    442    211   1405       C  
ATOM    158  O   VAL A  52      -1.977  19.803  30.859  1.00 74.93           O  
ANISOU  158  O   VAL A  52    11315   8178   8977    563    103   1601       O  
ATOM    159  CB  VAL A  52      -1.996  20.851  33.956  1.00 70.65           C  
ANISOU  159  CB  VAL A  52    10928   7176   8738    729    418   1266       C  
ATOM    160  CG1 VAL A  52      -2.995  21.651  33.136  1.00 72.39           C  
ANISOU  160  CG1 VAL A  52    11133   7388   8984   1016    404   1540       C  
ATOM    161  CG2 VAL A  52      -2.580  20.532  35.317  1.00 71.36           C  
ANISOU  161  CG2 VAL A  52    10928   7302   8883    814    489   1116       C  
ATOM    162  N   LEU A  53       0.131  20.089  31.588  1.00 72.71           N  
ANISOU  162  N   LEU A  53    11295   7568   8762    241    283   1330       N  
ATOM    163  CA  LEU A  53       0.657  20.266  30.239  1.00 72.68           C  
ANISOU  163  CA  LEU A  53    11390   7584   8642    147    270   1474       C  
ATOM    164  C   LEU A  53       0.494  18.992  29.420  1.00 73.01           C  
ANISOU  164  C   LEU A  53    11271   7951   8518     51    129   1472       C  
ATOM    165  O   LEU A  53       0.064  19.034  28.261  1.00 74.24           O  
ANISOU  165  O   LEU A  53    11444   8239   8526     99     45   1655       O  
ATOM    166  CB  LEU A  53       2.127  20.678  30.310  1.00 73.57           C  
ANISOU  166  CB  LEU A  53    11661   7493   8797    -86    402   1364       C  
ATOM    167  CG  LEU A  53       2.837  21.021  29.002  1.00 73.66           C  
ANISOU  167  CG  LEU A  53    11809   7478   8699   -211    461   1509       C  
ATOM    168  CD1 LEU A  53       2.233  22.266  28.370  1.00 74.87           C  
ANISOU  168  CD1 LEU A  53    12167   7437   8842    -24    508   1782       C  
ATOM    169  CD2 LEU A  53       4.325  21.201  29.246  1.00 72.66           C  
ANISOU  169  CD2 LEU A  53    11742   7217   8647   -481    595   1356       C  
ATOM    170  N   VAL A  54       0.845  17.846  30.008  1.00 70.99           N  
ANISOU  170  N   VAL A  54    10887   7817   8268    -86    100   1265       N  
ATOM    171  CA  VAL A  54       0.667  16.563  29.331  1.00 71.25           C  
ANISOU  171  CA  VAL A  54    10803   8113   8156   -187    -13   1226       C  
ATOM    172  C   VAL A  54      -0.807  16.322  29.038  1.00 73.57           C  
ANISOU  172  C   VAL A  54    10945   8613   8394    -52   -163   1350       C  
ATOM    173  O   VAL A  54      -1.183  15.902  27.937  1.00 74.58           O  
ANISOU  173  O   VAL A  54    11048   8939   8349    -95   -283   1435       O  
ATOM    174  CB  VAL A  54       1.255  15.423  30.182  1.00 70.94           C  
ANISOU  174  CB  VAL A  54    10679   8109   8165   -318      3    996       C  
ATOM    175  CG1 VAL A  54       0.935  14.077  29.557  1.00 71.35           C  
ANISOU  175  CG1 VAL A  54    10646   8381   8083   -415    -97    944       C  
ATOM    176  CG2 VAL A  54       2.753  15.600  30.348  1.00 69.35           C  
ANISOU  176  CG2 VAL A  54    10566   7771   8014   -452    120    886       C  
ATOM    177  N   ILE A  55      -1.660  16.579  30.028  1.00 70.54           N  
ANISOU  177  N   ILE A  55    10448   8207   8148    104   -156   1354       N  
ATOM    178  CA  ILE A  55      -3.092  16.345  29.874  1.00 73.33           C  
ANISOU  178  CA  ILE A  55    10586   8789   8488    233   -286   1469       C  
ATOM    179  C   ILE A  55      -3.678  17.241  28.790  1.00 74.89           C  
ANISOU  179  C   ILE A  55    10808   9044   8603    405   -377   1732       C  
ATOM    180  O   ILE A  55      -4.440  16.783  27.931  1.00 76.22           O  
ANISOU  180  O   ILE A  55    10834   9489   8635    395   -560   1834       O  
ATOM    181  CB  ILE A  55      -3.802  16.538  31.224  1.00 70.23           C  
ANISOU  181  CB  ILE A  55    10069   8343   8270    384   -201   1420       C  
ATOM    182  CG1 ILE A  55      -3.586  15.317  32.126  1.00 69.66           C  
ANISOU  182  CG1 ILE A  55     9924   8328   8218    207   -175   1208       C  
ATOM    183  CG2 ILE A  55      -5.255  16.891  31.022  1.00 72.77           C  
ANISOU  183  CG2 ILE A  55    10169   8850   8632    610   -286   1608       C  
ATOM    184  CD1 ILE A  55      -4.052  15.511  33.548  1.00 70.16           C  
ANISOU  184  CD1 ILE A  55     9931   8313   8414    326    -50   1139       C  
ATOM    185  N   THR A  56      -3.332  18.529  28.810  1.00 74.99           N  
ANISOU  185  N   THR A  56    11016   8791   8687    559   -258   1851       N  
ATOM    186  CA  THR A  56      -3.908  19.454  27.839  1.00 76.32           C  
ANISOU  186  CA  THR A  56    11240   8977   8783    770   -332   2142       C  
ATOM    187  C   THR A  56      -3.414  19.163  26.426  1.00 76.55           C  
ANISOU  187  C   THR A  56    11390   9140   8555    610   -434   2230       C  
ATOM    188  O   THR A  56      -4.167  19.330  25.459  1.00 78.27           O  
ANISOU  188  O   THR A  56    11557   9562   8620    729   -607   2453       O  
ATOM    189  CB  THR A  56      -3.584  20.894  28.236  1.00 74.62           C  
ANISOU  189  CB  THR A  56    11265   8375   8713    956   -144   2238       C  
ATOM    190  OG1 THR A  56      -4.103  21.157  29.547  1.00 74.68           O  
ANISOU  190  OG1 THR A  56    11184   8266   8927   1117    -36   2137       O  
ATOM    191  CG2 THR A  56      -4.204  21.875  27.252  1.00 76.05           C  
ANISOU  191  CG2 THR A  56    11532   8538   8823   1220   -212   2579       C  
ATOM    192  N   ALA A  57      -2.162  18.720  26.289  1.00 77.26           N  
ANISOU  192  N   ALA A  57    11631   9140   8584    350   -331   2061       N  
ATOM    193  CA  ALA A  57      -1.638  18.381  24.970  1.00 77.07           C  
ANISOU  193  CA  ALA A  57    11738   9245   8299    191   -381   2116       C  
ATOM    194  C   ALA A  57      -2.429  17.246  24.335  1.00 78.20           C  
ANISOU  194  C   ALA A  57    11704   9759   8249    109   -609   2083       C  
ATOM    195  O   ALA A  57      -2.688  17.259  23.126  1.00 79.19           O  
ANISOU  195  O   ALA A  57    11902  10069   8117     99   -742   2236       O  
ATOM    196  CB  ALA A  57      -0.160  18.011  25.072  1.00 74.64           C  
ANISOU  196  CB  ALA A  57    11564   8796   8000    -56   -199   1912       C  
ATOM    197  N   ILE A  58      -2.820  16.251  25.133  1.00 76.61           N  
ANISOU  197  N   ILE A  58    11290   9667   8150     27   -656   1883       N  
ATOM    198  CA  ILE A  58      -3.623  15.156  24.604  1.00 77.60           C  
ANISOU  198  CA  ILE A  58    11249  10121   8116    -96   -868   1830       C  
ATOM    199  C   ILE A  58      -5.059  15.609  24.369  1.00 79.96           C  
ANISOU  199  C   ILE A  58    11325  10651   8407    110  -1078   2055       C  
ATOM    200  O   ILE A  58      -5.730  15.121  23.452  1.00 81.07           O  
ANISOU  200  O   ILE A  58    11372  11100   8331     31  -1308   2112       O  
ATOM    201  CB  ILE A  58      -3.547  13.945  25.554  1.00 76.65           C  
ANISOU  201  CB  ILE A  58    11000  10004   8120   -265   -823   1559       C  
ATOM    202  CG1 ILE A  58      -2.103  13.448  25.654  1.00 74.30           C  
ANISOU  202  CG1 ILE A  58    10900   9517   7814   -433   -641   1362       C  
ATOM    203  CG2 ILE A  58      -4.455  12.820  25.084  1.00 78.01           C  
ANISOU  203  CG2 ILE A  58    11005  10482   8155   -430  -1029   1490       C  
ATOM    204  CD1 ILE A  58      -1.878  12.434  26.750  1.00 73.38           C  
ANISOU  204  CD1 ILE A  58    10700   9334   7846   -536   -568   1136       C  
ATOM    205  N   ALA A  59      -5.547  16.562  25.165  1.00 79.97           N  
ANISOU  205  N   ALA A  59    11234  10517   8634    381  -1005   2184       N  
ATOM    206  CA  ALA A  59      -6.939  16.988  25.051  1.00 82.03           C  
ANISOU  206  CA  ALA A  59    11227  11008   8934    627  -1183   2404       C  
ATOM    207  C   ALA A  59      -7.190  17.741  23.749  1.00 83.01           C  
ANISOU  207  C   ALA A  59    11456  11248   8835    779  -1348   2703       C  
ATOM    208  O   ALA A  59      -8.128  17.424  23.008  1.00 84.41           O  
ANISOU  208  O   ALA A  59    11426  11795   8851    791  -1624   2825       O  
ATOM    209  CB  ALA A  59      -7.322  17.850  26.255  1.00 78.49           C  
ANISOU  209  CB  ALA A  59    10692  10344   8785    913  -1010   2453       C  
ATOM    210  N   LYS A  60      -6.360  18.743  23.449  1.00 85.56           N  
ANISOU  210  N   LYS A  60    12108  11268   9133    880  -1191   2834       N  
ATOM    211  CA  LYS A  60      -6.623  19.598  22.296  1.00 86.77           C  
ANISOU  211  CA  LYS A  60    12402  11485   9080   1072  -1319   3170       C  
ATOM    212  C   LYS A  60      -6.136  18.977  20.989  1.00 86.80           C  
ANISOU  212  C   LYS A  60    12584  11695   8702    813  -1448   3158       C  
ATOM    213  O   LYS A  60      -6.828  19.060  19.969  1.00 88.23           O  
ANISOU  213  O   LYS A  60    12724  12174   8626    895  -1708   3379       O  
ATOM    214  CB  LYS A  60      -5.981  20.972  22.498  1.00 90.63           C  
ANISOU  214  CB  LYS A  60    13204  11529   9700   1276  -1073   3335       C  
ATOM    215  CG  LYS A  60      -6.652  21.834  23.559  1.00 90.64           C  
ANISOU  215  CG  LYS A  60    13088  11324  10027   1618   -963   3416       C  
ATOM    216  CD  LYS A  60      -6.025  23.220  23.605  1.00 89.84           C  
ANISOU  216  CD  LYS A  60    13361  10751  10024   1794   -726   3585       C  
ATOM    217  CE  LYS A  60      -6.702  24.114  24.631  1.00 89.95           C  
ANISOU  217  CE  LYS A  60    13310  10522  10347   2157   -591   3650       C  
ATOM    218  NZ  LYS A  60      -6.100  25.478  24.651  1.00 89.20           N  
ANISOU  218  NZ  LYS A  60    13629   9917  10347   2305   -350   3803       N  
ATOM    219  N   PHE A  61      -4.957  18.360  20.991  1.00 88.30           N  
ANISOU  219  N   PHE A  61    12968  11747   8835    514  -1271   2905       N  
ATOM    220  CA  PHE A  61      -4.354  17.887  19.751  1.00 87.93           C  
ANISOU  220  CA  PHE A  61    13150  11840   8421    290  -1315   2887       C  
ATOM    221  C   PHE A  61      -4.903  16.516  19.377  1.00 88.04           C  
ANISOU  221  C   PHE A  61    12984  12223   8244     56  -1547   2686       C  
ATOM    222  O   PHE A  61      -4.993  15.619  20.221  1.00 87.24           O  
ANISOU  222  O   PHE A  61    12693  12130   8326    -83  -1519   2422       O  
ATOM    223  CB  PHE A  61      -2.832  17.844  19.881  1.00 87.44           C  
ANISOU  223  CB  PHE A  61    13351  11477   8395     94   -997   2710       C  
ATOM    224  CG  PHE A  61      -2.200  19.202  19.982  1.00 87.23           C  
ANISOU  224  CG  PHE A  61    13558  11095   8488    242   -775   2913       C  
ATOM    225  CD1 PHE A  61      -1.972  19.960  18.844  1.00 88.07           C  
ANISOU  225  CD1 PHE A  61    13947  11181   8334    296   -758   3192       C  
ATOM    226  CD2 PHE A  61      -1.850  19.728  21.213  1.00 86.11           C  
ANISOU  226  CD2 PHE A  61    13382  10633   8703    311   -580   2824       C  
ATOM    227  CE1 PHE A  61      -1.397  21.212  18.934  1.00 87.66           C  
ANISOU  227  CE1 PHE A  61    14139  10764   8404    402   -532   3384       C  
ATOM    228  CE2 PHE A  61      -1.275  20.981  21.309  1.00 85.56           C  
ANISOU  228  CE2 PHE A  61    13553  10208   8747    405   -372   2987       C  
ATOM    229  CZ  PHE A  61      -1.049  21.723  20.167  1.00 86.32           C  
ANISOU  229  CZ  PHE A  61    13930  10257   8610    445   -340   3271       C  
ATOM    230  N   GLU A  62      -5.271  16.360  18.102  1.00 89.95           N  
ANISOU  230  N   GLU A  62    13314  12763   8101      0  -1776   2812       N  
ATOM    231  CA  GLU A  62      -5.942  15.142  17.656  1.00 90.39           C  
ANISOU  231  CA  GLU A  62    13208  13190   7946   -238  -2040   2631       C  
ATOM    232  C   GLU A  62      -4.970  13.973  17.568  1.00 88.73           C  
ANISOU  232  C   GLU A  62    13181  12893   7638   -576  -1867   2268       C  
ATOM    233  O   GLU A  62      -5.250  12.881  18.073  1.00 88.36           O  
ANISOU  233  O   GLU A  62    12967  12916   7689   -770  -1911   2002       O  
ATOM    234  CB  GLU A  62      -6.608  15.374  16.300  1.00100.56           C  
ANISOU  234  CB  GLU A  62    14559  14839   8810   -202  -2360   2872       C  
ATOM    235  CG  GLU A  62      -7.704  16.415  16.311  1.00102.45           C  
ANISOU  235  CG  GLU A  62    14571  15223   9131    167  -2581   3253       C  
ATOM    236  CD  GLU A  62      -7.155  17.816  16.163  1.00102.80           C  
ANISOU  236  CD  GLU A  62    14895  14951   9214    465  -2384   3572       C  
ATOM    237  OE1 GLU A  62      -5.925  17.955  15.996  1.00101.58           O  
ANISOU  237  OE1 GLU A  62    15090  14504   9002    340  -2089   3492       O  
ATOM    238  OE2 GLU A  62      -7.945  18.779  16.212  1.00104.30           O  
ANISOU  238  OE2 GLU A  62    14953  15175   9500    824  -2510   3905       O  
ATOM    239  N   ARG A  63      -3.821  14.181  16.921  1.00 90.42           N  
ANISOU  239  N   ARG A  63    13744  12946   7666   -642  -1650   2261       N  
ATOM    240  CA  ARG A  63      -2.903  13.079  16.661  1.00 89.13           C  
ANISOU  240  CA  ARG A  63    13765  12729   7372   -923  -1479   1934       C  
ATOM    241  C   ARG A  63      -2.241  12.539  17.922  1.00 87.47           C  
ANISOU  241  C   ARG A  63    13448  12242   7543   -974  -1237   1679       C  
ATOM    242  O   ARG A  63      -1.574  11.501  17.851  1.00 86.61           O  
ANISOU  242  O   ARG A  63    13447  12081   7378  -1173  -1105   1399       O  
ATOM    243  CB  ARG A  63      -1.844  13.511  15.645  1.00 96.98           C  
ANISOU  243  CB  ARG A  63    15129  13642   8077   -957  -1273   2015       C  
ATOM    244  CG  ARG A  63      -0.933  14.631  16.105  1.00 96.13           C  
ANISOU  244  CG  ARG A  63    15115  13200   8209   -802   -977   2175       C  
ATOM    245  CD  ARG A  63      -0.030  15.070  14.965  1.00 96.28           C  
ANISOU  245  CD  ARG A  63    15490  13191   7903   -861   -784   2292       C  
ATOM    246  NE  ARG A  63       0.871  16.151  15.349  1.00 95.50           N  
ANISOU  246  NE  ARG A  63    15486  12767   8033   -769   -489   2443       N  
ATOM    247  CZ  ARG A  63       1.737  16.726  14.521  1.00 95.62           C  
ANISOU  247  CZ  ARG A  63    15791  12698   7841   -819   -256   2582       C  
ATOM    248  NH1 ARG A  63       1.815  16.327  13.258  1.00 96.51           N  
ANISOU  248  NH1 ARG A  63    16145  13037   7487   -935   -279   2594       N  
ATOM    249  NH2 ARG A  63       2.521  17.704  14.953  1.00 94.90           N  
ANISOU  249  NH2 ARG A  63    15763  12298   7996   -777      9   2704       N  
ATOM    250  N   LEU A  64      -2.407  13.198  19.066  1.00 83.13           N  
ANISOU  250  N   LEU A  64    12709  11515   7362   -787  -1176   1768       N  
ATOM    251  CA  LEU A  64      -2.004  12.621  20.340  1.00 81.81           C  
ANISOU  251  CA  LEU A  64    12412  11147   7526   -832  -1015   1539       C  
ATOM    252  C   LEU A  64      -3.152  11.938  21.067  1.00 82.66           C  
ANISOU  252  C   LEU A  64    12227  11400   7778   -862  -1202   1455       C  
ATOM    253  O   LEU A  64      -2.942  11.404  22.158  1.00 81.84           O  
ANISOU  253  O   LEU A  64    12023  11147   7925   -897  -1084   1285       O  
ATOM    254  CB  LEU A  64      -1.387  13.687  21.248  1.00 79.84           C  
ANISOU  254  CB  LEU A  64    12163  10599   7573   -652   -807   1639       C  
ATOM    255  CG  LEU A  64      -0.014  14.207  20.830  1.00 78.71           C  
ANISOU  255  CG  LEU A  64    12270  10258   7381   -691   -551   1655       C  
ATOM    256  CD1 LEU A  64       0.422  15.309  21.770  1.00 77.88           C  
ANISOU  256  CD1 LEU A  64    12150   9868   7574   -549   -390   1747       C  
ATOM    257  CD2 LEU A  64       1.002  13.078  20.817  1.00 77.62           C  
ANISOU  257  CD2 LEU A  64    12197  10080   7215   -887   -386   1369       C  
ATOM    258  N   GLN A  65      -4.356  11.944  20.496  1.00 81.16           N  
ANISOU  258  N   GLN A  65    11888  11517   7433   -855  -1490   1582       N  
ATOM    259  CA  GLN A  65      -5.497  11.252  21.093  1.00 82.25           C  
ANISOU  259  CA  GLN A  65    11712  11838   7701   -929  -1665   1504       C  
ATOM    260  C   GLN A  65      -5.495   9.779  20.680  1.00 82.09           C  
ANISOU  260  C   GLN A  65    11762  11925   7504  -1272  -1730   1217       C  
ATOM    261  O   GLN A  65      -6.398   9.281  20.010  1.00 83.30           O  
ANISOU  261  O   GLN A  65    11811  12383   7455  -1436  -1996   1199       O  
ATOM    262  CB  GLN A  65      -6.798  11.940  20.703  1.00 83.53           C  
ANISOU  262  CB  GLN A  65    11624  12308   7806   -763  -1951   1775       C  
ATOM    263  CG  GLN A  65      -6.947  13.332  21.282  1.00 83.93           C  
ANISOU  263  CG  GLN A  65    11596  12208   8087   -393  -1864   2044       C  
ATOM    264  CD  GLN A  65      -8.231  14.013  20.860  1.00 86.00           C  
ANISOU  264  CD  GLN A  65    11597  12778   8303   -170  -2143   2338       C  
ATOM    265  OE1 GLN A  65      -9.004  13.472  20.071  1.00 87.10           O  
ANISOU  265  OE1 GLN A  65    11594  13288   8212   -312  -2438   2351       O  
ATOM    266  NE2 GLN A  65      -8.466  15.211  21.385  1.00 86.54           N  
ANISOU  266  NE2 GLN A  65    11598  12694   8587    187  -2054   2574       N  
ATOM    267  N   THR A  66      -4.442   9.082  21.091  1.00 80.77           N  
ANISOU  267  N   THR A  66    11779  11493   7416  -1380  -1482    986       N  
ATOM    268  CA  THR A  66      -4.288   7.662  20.820  1.00 80.49           C  
ANISOU  268  CA  THR A  66    11871  11457   7255  -1675  -1473    695       C  
ATOM    269  C   THR A  66      -4.752   6.847  22.022  1.00 80.62           C  
ANISOU  269  C   THR A  66    11692  11385   7555  -1764  -1438    558       C  
ATOM    270  O   THR A  66      -5.069   7.383  23.086  1.00 80.93           O  
ANISOU  270  O   THR A  66    11515  11362   7872  -1592  -1391    674       O  
ATOM    271  CB  THR A  66      -2.831   7.327  20.482  1.00 78.39           C  
ANISOU  271  CB  THR A  66    11931  10954   6901  -1706  -1203    536       C  
ATOM    272  OG1 THR A  66      -2.002   7.594  21.618  1.00 77.21           O  
ANISOU  272  OG1 THR A  66    11743  10523   7069  -1547   -963    530       O  
ATOM    273  CG2 THR A  66      -2.351   8.167  19.309  1.00 78.49           C  
ANISOU  273  CG2 THR A  66    12148  11049   6625  -1631  -1195    689       C  
ATOM    274  N   VAL A  67      -4.790   5.526  21.837  1.00 78.92           N  
ANISOU  274  N   VAL A  67    11589  11145   7250  -2044  -1440    305       N  
ATOM    275  CA  VAL A  67      -5.189   4.642  22.927  1.00 78.96           C  
ANISOU  275  CA  VAL A  67    11464  11035   7501  -2163  -1381    179       C  
ATOM    276  C   VAL A  67      -4.148   4.663  24.040  1.00 77.70           C  
ANISOU  276  C   VAL A  67    11384  10541   7597  -1984  -1097    149       C  
ATOM    277  O   VAL A  67      -4.490   4.706  25.228  1.00 78.03           O  
ANISOU  277  O   VAL A  67    11245  10511   7893  -1909  -1041    199       O  
ATOM    278  CB  VAL A  67      -5.428   3.216  22.398  1.00 78.58           C  
ANISOU  278  CB  VAL A  67    11579  10989   7287  -2524  -1434    -90       C  
ATOM    279  CG1 VAL A  67      -5.738   2.273  23.546  1.00 78.30           C  
ANISOU  279  CG1 VAL A  67    11464  10775   7509  -2652  -1328   -203       C  
ATOM    280  CG2 VAL A  67      -6.557   3.213  21.383  1.00 79.97           C  
ANISOU  280  CG2 VAL A  67    11631  11547   7206  -2735  -1765    -65       C  
ATOM    281  N   THR A  68      -2.864   4.636  23.674  1.00 76.51           N  
ANISOU  281  N   THR A  68    11493  10206   7370  -1914   -916     70       N  
ATOM    282  CA  THR A  68      -1.800   4.692  24.671  1.00 75.36           C  
ANISOU  282  CA  THR A  68    11392   9787   7453  -1742   -680     48       C  
ATOM    283  C   THR A  68      -1.829   6.000  25.449  1.00 75.37           C  
ANISOU  283  C   THR A  68    11209   9787   7641  -1502   -668    259       C  
ATOM    284  O   THR A  68      -1.528   6.017  26.648  1.00 74.87           O  
ANISOU  284  O   THR A  68    11081   9565   7802  -1398   -556    257       O  
ATOM    285  CB  THR A  68      -0.440   4.509  23.995  1.00 73.79           C  
ANISOU  285  CB  THR A  68    11450   9452   7135  -1709   -494    -60       C  
ATOM    286  OG1 THR A  68      -0.403   3.240  23.331  1.00 73.76           O  
ANISOU  286  OG1 THR A  68    11659   9405   6962  -1915   -469   -285       O  
ATOM    287  CG2 THR A  68       0.688   4.575  25.013  1.00 72.80           C  
ANISOU  287  CG2 THR A  68    11320   9092   7250  -1532   -284    -74       C  
ATOM    288  N   ASN A  69      -2.200   7.102  24.798  1.00 75.69           N  
ANISOU  288  N   ASN A  69    11189   9988   7580  -1407   -781    443       N  
ATOM    289  CA  ASN A  69      -2.187   8.391  25.473  1.00 75.32           C  
ANISOU  289  CA  ASN A  69    11024   9886   7707  -1173   -743    632       C  
ATOM    290  C   ASN A  69      -3.430   8.629  26.322  1.00 76.87           C  
ANISOU  290  C   ASN A  69    10952  10186   8067  -1103   -845    730       C  
ATOM    291  O   ASN A  69      -3.418   9.534  27.162  1.00 76.54           O  
ANISOU  291  O   ASN A  69    10832  10046   8205   -907   -768    836       O  
ATOM    292  CB  ASN A  69      -2.022   9.517  24.455  1.00 79.98           C  
ANISOU  292  CB  ASN A  69    11700  10553   8135  -1070   -785    815       C  
ATOM    293  CG  ASN A  69      -0.703   9.440  23.715  1.00 78.79           C  
ANISOU  293  CG  ASN A  69    11798  10292   7845  -1121   -622    737       C  
ATOM    294  OD1 ASN A  69      -0.671   9.256  22.499  1.00 79.41           O  
ANISOU  294  OD1 ASN A  69    12025  10502   7646  -1219   -677    733       O  
ATOM    295  ND2 ASN A  69       0.396   9.562  24.449  1.00 77.24           N  
ANISOU  295  ND2 ASN A  69    11640   9878   7829  -1060   -419    669       N  
ATOM    296  N   TYR A  70      -4.499   7.853  26.128  1.00 76.20           N  
ANISOU  296  N   TYR A  70    10725  10300   7929  -1271  -1001    687       N  
ATOM    297  CA  TYR A  70      -5.549   7.828  27.142  1.00 77.96           C  
ANISOU  297  CA  TYR A  70    10674  10598   8348  -1236  -1027    740       C  
ATOM    298  C   TYR A  70      -5.033   7.201  28.427  1.00 77.42           C  
ANISOU  298  C   TYR A  70    10663  10291   8462  -1252   -830    611       C  
ATOM    299  O   TYR A  70      -5.374   7.650  29.527  1.00 78.33           O  
ANISOU  299  O   TYR A  70    10643  10362   8759  -1110   -747    680       O  
ATOM    300  CB  TYR A  70      -6.774   7.067  26.641  1.00 84.52           C  
ANISOU  300  CB  TYR A  70    11312  11712   9091  -1466  -1233    711       C  
ATOM    301  CG  TYR A  70      -7.584   7.791  25.596  1.00 85.57           C  
ANISOU  301  CG  TYR A  70    11290  12156   9066  -1406  -1480    890       C  
ATOM    302  CD1 TYR A  70      -7.370   9.136  25.322  1.00 85.40           C  
ANISOU  302  CD1 TYR A  70    11292  12122   9034  -1111  -1482   1104       C  
ATOM    303  CD2 TYR A  70      -8.583   7.130  24.896  1.00 86.64           C  
ANISOU  303  CD2 TYR A  70    11258  12598   9061  -1651  -1722    855       C  
ATOM    304  CE1 TYR A  70      -8.119   9.796  24.364  1.00 86.46           C  
ANISOU  304  CE1 TYR A  70    11299  12539   9012  -1020  -1719   1305       C  
ATOM    305  CE2 TYR A  70      -9.335   7.780  23.942  1.00 87.68           C  
ANISOU  305  CE2 TYR A  70    11229  13056   9029  -1581  -1987   1037       C  
ATOM    306  CZ  TYR A  70      -9.102   9.111  23.679  1.00 87.66           C  
ANISOU  306  CZ  TYR A  70    11261  13033   9010  -1244  -1985   1276       C  
ATOM    307  OH  TYR A  70      -9.857   9.753  22.725  1.00 88.77           O  
ANISOU  307  OH  TYR A  70    11257  13497   8976  -1141  -2259   1493       O  
ATOM    308  N   PHE A  71      -4.213   6.154  28.306  1.00 78.10           N  
ANISOU  308  N   PHE A  71    10965  10222   8488  -1408   -746    430       N  
ATOM    309  CA  PHE A  71      -3.563   5.584  29.479  1.00 77.12           C  
ANISOU  309  CA  PHE A  71    10928   9862   8514  -1382   -570    338       C  
ATOM    310  C   PHE A  71      -2.635   6.603  30.127  1.00 75.03           C  
ANISOU  310  C   PHE A  71    10708   9449   8350  -1143   -454    404       C  
ATOM    311  O   PHE A  71      -2.576   6.710  31.357  1.00 73.86           O  
ANISOU  311  O   PHE A  71    10520   9198   8343  -1049   -362    413       O  
ATOM    312  CB  PHE A  71      -2.788   4.327  29.084  1.00 76.62           C  
ANISOU  312  CB  PHE A  71    11103   9645   8363  -1542   -500    150       C  
ATOM    313  CG  PHE A  71      -3.654   3.205  28.577  1.00 76.88           C  
ANISOU  313  CG  PHE A  71    11144   9762   8303  -1827   -592     42       C  
ATOM    314  CD1 PHE A  71      -5.014   3.181  28.835  1.00 78.61           C  
ANISOU  314  CD1 PHE A  71    11115  10178   8576  -1945   -708    110       C  
ATOM    315  CD2 PHE A  71      -3.106   2.185  27.818  1.00 75.60           C  
ANISOU  315  CD2 PHE A  71    11235   9485   8005  -1988   -552   -140       C  
ATOM    316  CE1 PHE A  71      -5.807   2.152  28.361  1.00 78.75           C  
ANISOU  316  CE1 PHE A  71    11125  10283   8514  -2262   -804     -4       C  
ATOM    317  CE2 PHE A  71      -3.893   1.156  27.339  1.00 75.88           C  
ANISOU  317  CE2 PHE A  71    11315   9571   7946  -2291   -637   -269       C  
ATOM    318  CZ  PHE A  71      -5.245   1.140  27.610  1.00 77.34           C  
ANISOU  318  CZ  PHE A  71    11239   9961   8187  -2450   -775   -202       C  
ATOM    319  N   ILE A  72      -1.913   7.372  29.309  1.00 75.12           N  
ANISOU  319  N   ILE A  72    10814   9453   8276  -1065   -454    447       N  
ATOM    320  CA  ILE A  72      -1.041   8.417  29.835  1.00 72.76           C  
ANISOU  320  CA  ILE A  72    10555   9014   8075   -889   -351    503       C  
ATOM    321  C   ILE A  72      -1.856   9.543  30.462  1.00 73.54           C  
ANISOU  321  C   ILE A  72    10511   9149   8283   -726   -374    648       C  
ATOM    322  O   ILE A  72      -1.408  10.181  31.424  1.00 72.00           O  
ANISOU  322  O   ILE A  72    10337   8812   8209   -607   -277    650       O  
ATOM    323  CB  ILE A  72      -0.107   8.922  28.718  1.00 75.64           C  
ANISOU  323  CB  ILE A  72    11060   9362   8317   -887   -319    522       C  
ATOM    324  CG1 ILE A  72       0.917   7.840  28.360  1.00 75.09           C  
ANISOU  324  CG1 ILE A  72    11133   9214   8184   -992   -225    354       C  
ATOM    325  CG2 ILE A  72       0.571  10.223  29.106  1.00 74.09           C  
ANISOU  325  CG2 ILE A  72    10885   9041   8222   -746   -233    609       C  
ATOM    326  CD1 ILE A  72       1.742   8.153  27.136  1.00 75.09           C  
ANISOU  326  CD1 ILE A  72    11267   9233   8030  -1019   -164    358       C  
ATOM    327  N   THR A  73      -3.065   9.794  29.953  1.00 71.91           N  
ANISOU  327  N   THR A  73    10154   9136   8033   -712   -502    764       N  
ATOM    328  CA  THR A  73      -3.931  10.801  30.559  1.00 73.43           C  
ANISOU  328  CA  THR A  73    10189   9363   8346   -516   -500    907       C  
ATOM    329  C   THR A  73      -4.246  10.452  32.008  1.00 73.94           C  
ANISOU  329  C   THR A  73    10172   9364   8559   -491   -390    839       C  
ATOM    330  O   THR A  73      -4.069  11.277  32.911  1.00 73.30           O  
ANISOU  330  O   THR A  73    10122   9146   8583   -326   -279    859       O  
ATOM    331  CB  THR A  73      -5.221  10.946  29.750  1.00 74.33           C  
ANISOU  331  CB  THR A  73    10098   9750   8395   -500   -677   1049       C  
ATOM    332  OG1 THR A  73      -4.908  11.382  28.422  1.00 73.61           O  
ANISOU  332  OG1 THR A  73    10122   9720   8126   -500   -781   1138       O  
ATOM    333  CG2 THR A  73      -6.153  11.953  30.408  1.00 76.24           C  
ANISOU  333  CG2 THR A  73    10150  10030   8789   -248   -648   1202       C  
ATOM    334  N   SER A  74      -4.711   9.224  32.252  1.00 74.29           N  
ANISOU  334  N   SER A  74    10141   9490   8595   -669   -409    752       N  
ATOM    335  CA  SER A  74      -4.972   8.799  33.623  1.00 74.42           C  
ANISOU  335  CA  SER A  74    10116   9441   8721   -664   -284    702       C  
ATOM    336  C   SER A  74      -3.685   8.695  34.430  1.00 70.30           C  
ANISOU  336  C   SER A  74     9812   8684   8213   -631   -170    600       C  
ATOM    337  O   SER A  74      -3.692   8.952  35.639  1.00 69.87           O  
ANISOU  337  O   SER A  74     9773   8550   8226   -534    -62    590       O  
ATOM    338  CB  SER A  74      -5.711   7.463  33.633  1.00 74.45           C  
ANISOU  338  CB  SER A  74    10022   9555   8709   -898   -315    645       C  
ATOM    339  OG  SER A  74      -4.887   6.421  33.144  1.00 72.07           O  
ANISOU  339  OG  SER A  74     9922   9145   8317  -1075   -331    516       O  
ATOM    340  N   LEU A  75      -2.578   8.312  33.786  1.00 71.92           N  
ANISOU  340  N   LEU A  75    10178   8801   8346   -705   -192    522       N  
ATOM    341  CA  LEU A  75      -1.289   8.322  34.469  1.00 68.63           C  
ANISOU  341  CA  LEU A  75     9915   8206   7955   -654   -111    443       C  
ATOM    342  C   LEU A  75      -0.917   9.732  34.906  1.00 68.07           C  
ANISOU  342  C   LEU A  75     9866   8057   7941   -497    -69    486       C  
ATOM    343  O   LEU A  75      -0.423   9.935  36.021  1.00 66.89           O  
ANISOU  343  O   LEU A  75     9778   7805   7832   -438     -7    435       O  
ATOM    344  CB  LEU A  75      -0.205   7.739  33.562  1.00 69.73           C  
ANISOU  344  CB  LEU A  75    10175   8296   8023   -738   -122    363       C  
ATOM    345  CG  LEU A  75       1.190   7.613  34.181  1.00 67.42           C  
ANISOU  345  CG  LEU A  75     9981   7864   7770   -684    -56    286       C  
ATOM    346  CD1 LEU A  75       1.180   6.623  35.336  1.00 66.72           C  
ANISOU  346  CD1 LEU A  75     9932   7707   7712   -683    -21    244       C  
ATOM    347  CD2 LEU A  75       2.218   7.215  33.135  1.00 67.30           C  
ANISOU  347  CD2 LEU A  75    10044   7828   7701   -733    -35    223       C  
ATOM    348  N   ALA A  76      -1.149  10.722  34.041  1.00 69.44           N  
ANISOU  348  N   ALA A  76    10014   8266   8103   -436   -106    581       N  
ATOM    349  CA  ALA A  76      -0.885  12.104  34.424  1.00 69.17           C  
ANISOU  349  CA  ALA A  76    10038   8108   8134   -297    -47    624       C  
ATOM    350  C   ALA A  76      -1.868  12.588  35.482  1.00 71.19           C  
ANISOU  350  C   ALA A  76    10223   8361   8467   -157     18    657       C  
ATOM    351  O   ALA A  76      -1.497  13.390  36.345  1.00 70.46           O  
ANISOU  351  O   ALA A  76    10231   8118   8421    -72    103    612       O  
ATOM    352  CB  ALA A  76      -0.930  13.011  33.195  1.00 69.03           C  
ANISOU  352  CB  ALA A  76    10047   8102   8078   -252    -86    751       C  
ATOM    353  N   CYS A  77      -3.117  12.114  35.436  1.00 68.63           N  
ANISOU  353  N   CYS A  77     9722   8205   8150   -146     -9    723       N  
ATOM    354  CA  CYS A  77      -4.074  12.453  36.485  1.00 71.12           C  
ANISOU  354  CA  CYS A  77     9940   8541   8540    -10     94    748       C  
ATOM    355  C   CYS A  77      -3.629  11.901  37.831  1.00 69.57           C  
ANISOU  355  C   CYS A  77     9850   8255   8328    -57    192    624       C  
ATOM    356  O   CYS A  77      -3.709  12.594  38.853  1.00 69.96           O  
ANISOU  356  O   CYS A  77     9971   8210   8402     69    310    590       O  
ATOM    357  CB  CYS A  77      -5.462  11.924  36.128  1.00 70.65           C  
ANISOU  357  CB  CYS A  77     9617   8725   8504    -30     44    843       C  
ATOM    358  SG  CYS A  77      -6.229  12.738  34.718  1.00 72.56           S  
ANISOU  358  SG  CYS A  77     9696   9125   8747     93    -99   1032       S  
ATOM    359  N   ALA A  78      -3.170  10.649  37.855  1.00 72.40           N  
ANISOU  359  N   ALA A  78    10244   8635   8630   -228    150    558       N  
ATOM    360  CA  ALA A  78      -2.652  10.081  39.095  1.00 70.67           C  
ANISOU  360  CA  ALA A  78    10150   8331   8371   -255    220    471       C  
ATOM    361  C   ALA A  78      -1.475  10.895  39.615  1.00 68.63           C  
ANISOU  361  C   ALA A  78    10062   7921   8094   -192    225    389       C  
ATOM    362  O   ALA A  78      -1.315  11.067  40.829  1.00 68.96           O  
ANISOU  362  O   ALA A  78    10206   7905   8092   -142    293    330       O  
ATOM    363  CB  ALA A  78      -2.250   8.624  38.880  1.00 68.17           C  
ANISOU  363  CB  ALA A  78     9873   8022   8008   -418    171    435       C  
ATOM    364  N   ASP A  79      -0.645  11.413  38.708  1.00 68.25           N  
ANISOU  364  N   ASP A  79    10049   7818   8063   -214    155    382       N  
ATOM    365  CA  ASP A  79       0.442  12.293  39.115  1.00 67.15           C  
ANISOU  365  CA  ASP A  79    10042   7545   7929   -198    158    302       C  
ATOM    366  C   ASP A  79      -0.048  13.708  39.400  1.00 68.58           C  
ANISOU  366  C   ASP A  79    10279   7621   8156    -72    242    317       C  
ATOM    367  O   ASP A  79       0.512  14.385  40.268  1.00 68.61           O  
ANISOU  367  O   ASP A  79    10421   7502   8143    -62    278    216       O  
ATOM    368  CB  ASP A  79       1.533  12.314  38.042  1.00 72.65           C  
ANISOU  368  CB  ASP A  79    10746   8220   8638   -291     91    293       C  
ATOM    369  CG  ASP A  79       2.296  11.003  37.953  1.00 71.53           C  
ANISOU  369  CG  ASP A  79    10587   8132   8459   -376     38    244       C  
ATOM    370  OD1 ASP A  79       2.376  10.283  38.970  1.00 71.65           O  
ANISOU  370  OD1 ASP A  79    10633   8154   8437   -365     35    203       O  
ATOM    371  OD2 ASP A  79       2.831  10.702  36.865  1.00 70.92           O  
ANISOU  371  OD2 ASP A  79    10485   8081   8382   -439     15    253       O  
ATOM    372  N   LEU A  80      -1.087  14.168  38.698  1.00 67.65           N  
ANISOU  372  N   LEU A  80    10066   7547   8092     31    268    440       N  
ATOM    373  CA  LEU A  80      -1.614  15.507  38.950  1.00 69.11           C  
ANISOU  373  CA  LEU A  80    10317   7602   8340    203    372    473       C  
ATOM    374  C   LEU A  80      -2.286  15.592  40.314  1.00 71.06           C  
ANISOU  374  C   LEU A  80    10594   7836   8570    312    505    406       C  
ATOM    375  O   LEU A  80      -2.069  16.551  41.064  1.00 71.22           O  
ANISOU  375  O   LEU A  80    10793   7676   8590    387    604    315       O  
ATOM    376  CB  LEU A  80      -2.596  15.908  37.850  1.00 69.50           C  
ANISOU  376  CB  LEU A  80    10228   7732   8447    329    349    654       C  
ATOM    377  CG  LEU A  80      -3.217  17.290  38.042  1.00 70.91           C  
ANISOU  377  CG  LEU A  80    10476   7755   8712    568    471    722       C  
ATOM    378  CD1 LEU A  80      -2.126  18.339  38.082  1.00 68.92           C  
ANISOU  378  CD1 LEU A  80    10490   7222   8476    526    515    647       C  
ATOM    379  CD2 LEU A  80      -4.214  17.589  36.935  1.00 72.77           C  
ANISOU  379  CD2 LEU A  80    10539   8117   8996    725    413    937       C  
ATOM    380  N   VAL A  81      -3.118  14.603  40.648  1.00 68.40           N  
ANISOU  380  N   VAL A  81    10101   7677   8210    304    527    442       N  
ATOM    381  CA  VAL A  81      -3.737  14.575  41.968  1.00 70.80           C  
ANISOU  381  CA  VAL A  81    10440   7991   8472    390    685    385       C  
ATOM    382  C   VAL A  81      -2.677  14.370  43.042  1.00 69.34           C  
ANISOU  382  C   VAL A  81    10479   7710   8156    290    675    229       C  
ATOM    383  O   VAL A  81      -2.824  14.849  44.173  1.00 70.80           O  
ANISOU  383  O   VAL A  81    10812   7822   8266    370    805    136       O  
ATOM    384  CB  VAL A  81      -4.827  13.488  42.019  1.00 68.74           C  
ANISOU  384  CB  VAL A  81     9948   7949   8220    355    721    474       C  
ATOM    385  CG1 VAL A  81      -5.439  13.404  43.407  1.00 71.49           C  
ANISOU  385  CG1 VAL A  81    10340   8318   8506    429    922    426       C  
ATOM    386  CG2 VAL A  81      -5.899  13.765  40.980  1.00 71.27           C  
ANISOU  386  CG2 VAL A  81    10007   8410   8662    453    695    627       C  
ATOM    387  N   MET A  82      -1.592  13.667  42.706  1.00 69.64           N  
ANISOU  387  N   MET A  82    10546   7761   8154    127    520    197       N  
ATOM    388  CA  MET A  82      -0.468  13.545  43.627  1.00 68.84           C  
ANISOU  388  CA  MET A  82    10622   7600   7935     46    462     67       C  
ATOM    389  C   MET A  82       0.072  14.917  44.012  1.00 68.63           C  
ANISOU  389  C   MET A  82    10776   7398   7903     70    491    -56       C  
ATOM    390  O   MET A  82       0.500  15.128  45.152  1.00 69.11           O  
ANISOU  390  O   MET A  82    11009   7416   7834     48    500   -187       O  
ATOM    391  CB  MET A  82       0.637  12.700  42.992  1.00 71.68           C  
ANISOU  391  CB  MET A  82    10933   8003   8297    -91    297     71       C  
ATOM    392  CG  MET A  82       1.759  12.298  43.938  1.00 71.89           C  
ANISOU  392  CG  MET A  82    11075   8036   8206   -155    201    -26       C  
ATOM    393  SD  MET A  82       1.285  11.004  45.103  1.00 73.65           S  
ANISOU  393  SD  MET A  82    11358   8352   8275   -129    241     18       S  
ATOM    394  CE  MET A  82       1.321   9.577  44.022  1.00 70.68           C  
ANISOU  394  CE  MET A  82    10839   8032   7985   -194    182    131       C  
ATOM    395  N   GLY A  83       0.052  15.864  43.077  1.00 68.96           N  
ANISOU  395  N   GLY A  83    10805   7327   8069    105    505    -15       N  
ATOM    396  CA  GLY A  83       0.618  17.179  43.308  1.00 68.53           C  
ANISOU  396  CA  GLY A  83    10949   7055   8033     91    543   -129       C  
ATOM    397  C   GLY A  83      -0.366  18.209  43.820  1.00 70.09           C  
ANISOU  397  C   GLY A  83    11274   7102   8254    287    741   -152       C  
ATOM    398  O   GLY A  83       0.039  19.241  44.360  1.00 69.94           O  
ANISOU  398  O   GLY A  83    11491   6869   8214    271    805   -295       O  
ATOM    399  N   LEU A  84      -1.662  17.949  43.654  1.00 68.67           N  
ANISOU  399  N   LEU A  84    10935   7030   8126    471    847    -19       N  
ATOM    400  CA  LEU A  84      -2.680  18.869  44.148  1.00 70.39           C  
ANISOU  400  CA  LEU A  84    11231   7128   8385    711   1067    -25       C  
ATOM    401  C   LEU A  84      -3.183  18.501  45.541  1.00 71.90           C  
ANISOU  401  C   LEU A  84    11493   7391   8432    765   1214   -131       C  
ATOM    402  O   LEU A  84      -3.430  19.393  46.360  1.00 72.26           O  
ANISOU  402  O   LEU A  84    11757   7264   8433    890   1396   -258       O  
ATOM    403  CB  LEU A  84      -3.858  18.935  43.171  1.00 71.86           C  
ANISOU  403  CB  LEU A  84    11163   7417   8725    911   1109    195       C  
ATOM    404  CG  LEU A  84      -3.628  19.630  41.827  1.00 70.68           C  
ANISOU  404  CG  LEU A  84    11001   7159   8696    943   1020    331       C  
ATOM    405  CD1 LEU A  84      -4.849  19.479  40.934  1.00 72.62           C  
ANISOU  405  CD1 LEU A  84    10952   7592   9046   1134   1010    561       C  
ATOM    406  CD2 LEU A  84      -3.300  21.101  42.035  1.00 70.01           C  
ANISOU  406  CD2 LEU A  84    11219   6718   8662   1041   1149    253       C  
ATOM    407  N   ALA A  85      -3.337  17.205  45.833  1.00 75.30           N  
ANISOU  407  N   ALA A  85    11778   8055   8777    670   1158    -84       N  
ATOM    408  CA  ALA A  85      -3.927  16.762  47.090  1.00 76.69           C  
ANISOU  408  CA  ALA A  85    12011   8322   8804    719   1324   -140       C  
ATOM    409  C   ALA A  85      -2.950  16.110  48.055  1.00 75.53           C  
ANISOU  409  C   ALA A  85    12059   8209   8429    539   1215   -264       C  
ATOM    410  O   ALA A  85      -3.232  16.072  49.255  1.00 75.92           O  
ANISOU  410  O   ALA A  85    12274   8276   8295    581   1361   -351       O  
ATOM    411  CB  ALA A  85      -5.061  15.761  46.825  1.00 75.51           C  
ANISOU  411  CB  ALA A  85    11555   8414   8723    755   1391     35       C  
ATOM    412  N   VAL A  86      -1.826  15.593  47.575  1.00 76.44           N  
ANISOU  412  N   VAL A  86    12155   8349   8539    360    971   -263       N  
ATOM    413  CA  VAL A  86      -0.945  14.746  48.374  1.00 75.61           C  
ANISOU  413  CA  VAL A  86    12163   8329   8237    222    833   -321       C  
ATOM    414  C   VAL A  86       0.326  15.493  48.774  1.00 74.26           C  
ANISOU  414  C   VAL A  86    12196   8046   7971    108    687   -504       C  
ATOM    415  O   VAL A  86       0.583  15.710  49.959  1.00 74.42           O  
ANISOU  415  O   VAL A  86    12447   8059   7772     87    701   -645       O  
ATOM    416  CB  VAL A  86      -0.619  13.430  47.631  1.00 72.96           C  
ANISOU  416  CB  VAL A  86    11631   8127   7965    122    676   -179       C  
ATOM    417  CG1 VAL A  86       0.378  12.594  48.415  1.00 71.96           C  
ANISOU  417  CG1 VAL A  86    11619   8069   7652     28    520   -212       C  
ATOM    418  CG2 VAL A  86      -1.901  12.641  47.363  1.00 74.47           C  
ANISOU  418  CG2 VAL A  86    11636   8433   8227    175    816    -24       C  
ATOM    419  N   VAL A  87       1.125  15.913  47.788  1.00 76.16           N  
ANISOU  419  N   VAL A  87    12359   8213   8366     15    549   -509       N  
ATOM    420  CA  VAL A  87       2.437  16.501  48.087  1.00 75.33           C  
ANISOU  420  CA  VAL A  87    12387   8039   8198   -152    386   -676       C  
ATOM    421  C   VAL A  87       2.335  17.799  48.877  1.00 75.78           C  
ANISOU  421  C   VAL A  87    12728   7898   8165   -148    505   -877       C  
ATOM    422  O   VAL A  87       3.176  18.022  49.763  1.00 75.95           O  
ANISOU  422  O   VAL A  87    12922   7929   8005   -290    382  -1054       O  
ATOM    423  CB  VAL A  87       3.253  16.654  46.797  1.00 74.66           C  
ANISOU  423  CB  VAL A  87    12136   7922   8310   -264    262   -622       C  
ATOM    424  CG1 VAL A  87       4.581  17.352  47.081  1.00 74.49           C  
ANISOU  424  CG1 VAL A  87    12210   7838   8254   -470    113   -797       C  
ATOM    425  CG2 VAL A  87       3.489  15.304  46.155  1.00 74.21           C  
ANISOU  425  CG2 VAL A  87    11849   8049   8297   -274    149   -469       C  
ATOM    426  N   PRO A  88       1.393  18.711  48.603  1.00 78.03           N  
ANISOU  426  N   PRO A  88    13086   7997   8564      7    729   -870       N  
ATOM    427  CA  PRO A  88       1.318  19.918  49.447  1.00 78.51           C  
ANISOU  427  CA  PRO A  88    13475   7829   8525     21    870  -1090       C  
ATOM    428  C   PRO A  88       1.026  19.611  50.906  1.00 79.41           C  
ANISOU  428  C   PRO A  88    13791   8037   8344     57    945  -1218       C  
ATOM    429  O   PRO A  88       1.727  20.111  51.795  1.00 79.52           O  
ANISOU  429  O   PRO A  88    14072   7986   8157    -91    873  -1448       O  
ATOM    430  CB  PRO A  88       0.193  20.731  48.790  1.00 77.11           C  
ANISOU  430  CB  PRO A  88    13287   7459   8551    263   1120   -992       C  
ATOM    431  CG  PRO A  88       0.166  20.268  47.383  1.00 76.45           C  
ANISOU  431  CG  PRO A  88    12897   7468   8682    271   1017   -759       C  
ATOM    432  CD  PRO A  88       0.477  18.806  47.452  1.00 76.28           C  
ANISOU  432  CD  PRO A  88    12668   7744   8570    171    844   -674       C  
ATOM    433  N   PHE A  89       0.008  18.792  51.181  1.00 80.94           N  
ANISOU  433  N   PHE A  89    13869   8394   8489    226   1089  -1077       N  
ATOM    434  CA  PHE A  89      -0.327  18.471  52.563  1.00 81.69           C  
ANISOU  434  CA  PHE A  89    14172   8584   8280    264   1199  -1173       C  
ATOM    435  C   PHE A  89       0.753  17.638  53.243  1.00 81.28           C  
ANISOU  435  C   PHE A  89    14181   8722   7980     71    921  -1213       C  
ATOM    436  O   PHE A  89       0.838  17.648  54.475  1.00 81.76           O  
ANISOU  436  O   PHE A  89    14509   8832   7723     47    945  -1351       O  
ATOM    437  CB  PHE A  89      -1.673  17.754  52.617  1.00 81.51           C  
ANISOU  437  CB  PHE A  89    13975   8701   8293    462   1438   -987       C  
ATOM    438  CG  PHE A  89      -2.833  18.623  52.224  1.00 82.45           C  
ANISOU  438  CG  PHE A  89    14039   8675   8612    703   1733   -959       C  
ATOM    439  CD1 PHE A  89      -3.421  19.480  53.141  1.00 83.12           C  
ANISOU  439  CD1 PHE A  89    14395   8619   8568    857   2020  -1128       C  
ATOM    440  CD2 PHE A  89      -3.320  18.600  50.929  1.00 82.74           C  
ANISOU  440  CD2 PHE A  89    13763   8720   8956    792   1720   -763       C  
ATOM    441  CE1 PHE A  89      -4.488  20.283  52.774  1.00 84.06           C  
ANISOU  441  CE1 PHE A  89    14444   8601   8892   1130   2303  -1085       C  
ATOM    442  CE2 PHE A  89      -4.381  19.399  50.556  1.00 83.79           C  
ANISOU  442  CE2 PHE A  89    13818   8743   9275   1049   1964   -707       C  
ATOM    443  CZ  PHE A  89      -4.966  20.242  51.478  1.00 84.41           C  
ANISOU  443  CZ  PHE A  89    14141   8674   9256   1235   2261   -861       C  
ATOM    444  N   GLY A  90       1.574  16.918  52.475  1.00 81.97           N  
ANISOU  444  N   GLY A  90    14031   8922   8191    -45    662  -1090       N  
ATOM    445  CA  GLY A  90       2.751  16.295  53.051  1.00 81.83           C  
ANISOU  445  CA  GLY A  90    14050   9070   7973   -202    371  -1130       C  
ATOM    446  C   GLY A  90       3.871  17.279  53.299  1.00 81.86           C  
ANISOU  446  C   GLY A  90    14202   8988   7913   -403    187  -1369       C  
ATOM    447  O   GLY A  90       4.699  17.068  54.191  1.00 82.39           O  
ANISOU  447  O   GLY A  90    14387   9197   7720   -526    -29  -1473       O  
ATOM    448  N   ALA A  91       3.915  18.365  52.522  1.00 84.26           N  
ANISOU  448  N   ALA A  91    14506   9063   8446   -452    262  -1451       N  
ATOM    449  CA  ALA A  91       4.896  19.414  52.775  1.00 84.47           C  
ANISOU  449  CA  ALA A  91    14706   8962   8426   -687    129  -1701       C  
ATOM    450  C   ALA A  91       4.543  20.201  54.029  1.00 85.29           C  
ANISOU  450  C   ALA A  91    15220   8942   8245   -693    264  -1957       C  
ATOM    451  O   ALA A  91       5.424  20.528  54.831  1.00 85.94           O  
ANISOU  451  O   ALA A  91    15483   9073   8099   -913     65  -2177       O  
ATOM    452  CB  ALA A  91       4.997  20.343  51.567  1.00 83.67           C  
ANISOU  452  CB  ALA A  91    14530   8610   8650   -740    209  -1690       C  
ATOM    453  N   ALA A  92       3.257  20.510  54.219  1.00 88.37           N  
ANISOU  453  N   ALA A  92    15753   9188   8637   -453    602  -1940       N  
ATOM    454  CA  ALA A  92       2.828  21.153  55.455  1.00 89.22           C  
ANISOU  454  CA  ALA A  92    16267   9186   8445   -418    783  -2183       C  
ATOM    455  C   ALA A  92       3.039  20.242  56.656  1.00 89.80           C  
ANISOU  455  C   ALA A  92    16449   9554   8118   -454    650  -2200       C  
ATOM    456  O   ALA A  92       3.279  20.724  57.769  1.00 90.54           O  
ANISOU  456  O   ALA A  92    16902   9628   7872   -556    637  -2457       O  
ATOM    457  CB  ALA A  92       1.361  21.566  55.355  1.00 85.84           C  
ANISOU  457  CB  ALA A  92    15903   8580   8132   -105   1203  -2124       C  
ATOM    458  N   HIS A  93       2.951  18.926  56.451  1.00 91.61           N  
ANISOU  458  N   HIS A  93    16402  10041   8363   -373    553  -1929       N  
ATOM    459  CA  HIS A  93       3.207  17.982  57.532  1.00 92.12           C  
ANISOU  459  CA  HIS A  93    16574  10375   8051   -392    411  -1891       C  
ATOM    460  C   HIS A  93       4.669  18.006  57.959  1.00 92.57           C  
ANISOU  460  C   HIS A  93    16674  10581   7918   -647     -6  -2030       C  
ATOM    461  O   HIS A  93       4.973  17.965  59.157  1.00 93.42           O  
ANISOU  461  O   HIS A  93    17060  10823   7611   -720   -118  -2167       O  
ATOM    462  CB  HIS A  93       2.798  16.575  57.101  1.00 93.53           C  
ANISOU  462  CB  HIS A  93    16461  10738   8339   -254    416  -1555       C  
ATOM    463  CG  HIS A  93       2.996  15.539  58.162  1.00 93.96           C  
ANISOU  463  CG  HIS A  93    16645  11036   8021   -244    299  -1461       C  
ATOM    464  ND1 HIS A  93       4.181  14.853  58.317  1.00 94.14           N  
ANISOU  464  ND1 HIS A  93    16581  11258   7932   -350    -85  -1396       N  
ATOM    465  CD2 HIS A  93       2.165  15.079  59.127  1.00 94.38           C  
ANISOU  465  CD2 HIS A  93    16913  11165   7781   -127    525  -1402       C  
ATOM    466  CE1 HIS A  93       4.070  14.010  59.328  1.00 94.60           C  
ANISOU  466  CE1 HIS A  93    16816  11491   7636   -285   -108  -1287       C  
ATOM    467  NE2 HIS A  93       2.856  14.128  59.837  1.00 94.66           N  
ANISOU  467  NE2 HIS A  93    17021  11426   7520   -167    268  -1290       N  
ATOM    468  N   ILE A  94       5.588  18.065  56.995  1.00 91.79           N  
ANISOU  468  N   ILE A  94    16288  10486   8104   -787   -241  -1992       N  
ATOM    469  CA  ILE A  94       7.010  18.044  57.323  1.00 92.57           C  
ANISOU  469  CA  ILE A  94    16332  10772   8068  -1031   -649  -2103       C  
ATOM    470  C   ILE A  94       7.438  19.368  57.939  1.00 93.31           C  
ANISOU  470  C   ILE A  94    16745  10715   7994  -1277   -692  -2472       C  
ATOM    471  O   ILE A  94       8.115  19.400  58.973  1.00 94.45           O  
ANISOU  471  O   ILE A  94    17070  11042   7775  -1440   -944  -2641       O  
ATOM    472  CB  ILE A  94       7.846  17.714  56.075  1.00 88.47           C  
ANISOU  472  CB  ILE A  94    15384  10309   7921  -1105   -838  -1952       C  
ATOM    473  CG1 ILE A  94       7.553  16.294  55.599  1.00 87.95           C  
ANISOU  473  CG1 ILE A  94    15054  10400   7962   -885   -833  -1620       C  
ATOM    474  CG2 ILE A  94       9.329  17.894  56.359  1.00 89.64           C  
ANISOU  474  CG2 ILE A  94    15427  10651   7982  -1377  -1237  -2094       C  
ATOM    475  CD1 ILE A  94       8.188  15.978  54.283  1.00 87.51           C  
ANISOU  475  CD1 ILE A  94    14613  10362   8273   -917   -935  -1479       C  
ATOM    476  N   LEU A  95       7.057  20.480  57.310  1.00 95.34           N  
ANISOU  476  N   LEU A  95    17093  10631   8503  -1314   -455  -2601       N  
ATOM    477  CA  LEU A  95       7.553  21.778  57.752  1.00 96.04           C  
ANISOU  477  CA  LEU A  95    17493  10512   8485  -1589   -490  -2963       C  
ATOM    478  C   LEU A  95       7.009  22.131  59.132  1.00 96.84           C  
ANISOU  478  C   LEU A  95    18079  10578   8139  -1557   -353  -3203       C  
ATOM    479  O   LEU A  95       7.755  22.589  60.006  1.00 97.95           O  
ANISOU  479  O   LEU A  95    18410  10801   8005  -1810   -573  -3459       O  
ATOM    480  CB  LEU A  95       7.186  22.854  56.731  1.00 98.09           C  
ANISOU  480  CB  LEU A  95    17779  10363   9126  -1592   -225  -3005       C  
ATOM    481  CG  LEU A  95       7.686  22.624  55.299  1.00 97.23           C  
ANISOU  481  CG  LEU A  95    17238  10264   9439  -1634   -317  -2778       C  
ATOM    482  CD1 LEU A  95       7.269  23.775  54.390  1.00 96.56           C  
ANISOU  482  CD1 LEU A  95    17260   9754   9674  -1625    -43  -2812       C  
ATOM    483  CD2 LEU A  95       9.184  22.357  55.218  1.00 97.93           C  
ANISOU  483  CD2 LEU A  95    17064  10612   9532  -1952   -727  -2818       C  
ATOM    484  N   MET A  96       5.712  21.914  59.351  1.00 97.74           N  
ANISOU  484  N   MET A  96    18327  10607   8203  -1238     17  -3098       N  
ATOM    485  CA  MET A  96       5.092  22.225  60.634  1.00 98.53           C  
ANISOU  485  CA  MET A  96    18849  10683   7905  -1161    220  -3292       C  
ATOM    486  C   MET A  96       5.307  21.136  61.679  1.00 99.19           C  
ANISOU  486  C   MET A  96    18955  11165   7567  -1139     15  -3187       C  
ATOM    487  O   MET A  96       4.958  21.347  62.846  1.00101.93           O  
ANISOU  487  O   MET A  96    19548  11572   7607  -1097    131  -3302       O  
ATOM    488  CB  MET A  96       3.592  22.468  60.443  1.00105.04           C  
ANISOU  488  CB  MET A  96    19785  11266   8858   -819    736  -3221       C  
ATOM    489  CG  MET A  96       3.262  23.694  59.600  1.00104.68           C  
ANISOU  489  CG  MET A  96    19775  10799   9199   -779    976  -3316       C  
ATOM    490  SD  MET A  96       1.487  23.925  59.368  1.00104.61           S  
ANISOU  490  SD  MET A  96    19819  10566   9363   -318   1559  -3195       S  
ATOM    491  CE  MET A  96       1.460  25.319  58.242  1.00104.25           C  
ANISOU  491  CE  MET A  96    19779  10046   9785   -304   1703  -3255       C  
ATOM    492  N   LYS A  97       5.862  19.987  61.289  1.00 98.97           N  
ANISOU  492  N   LYS A  97    18617  11414   7572  -1138   -275  -2929       N  
ATOM    493  CA  LYS A  97       6.140  18.854  62.175  1.00 99.59           C  
ANISOU  493  CA  LYS A  97    18721  11856   7262  -1094   -497  -2774       C  
ATOM    494  C   LYS A  97       4.883  18.302  62.849  1.00 99.47           C  
ANISOU  494  C   LYS A  97    18922  11861   7011   -826   -124  -2641       C  
ATOM    495  O   LYS A  97       4.982  17.541  63.818  1.00100.08           O  
ANISOU  495  O   LYS A  97    19095  12202   6728   -784   -236  -2530       O  
ATOM    496  CB  LYS A  97       7.189  19.209  63.239  1.00101.54           C  
ANISOU  496  CB  LYS A  97    19085  12318   7178  -1339   -857  -2990       C  
ATOM    497  CG  LYS A  97       8.636  19.047  62.782  1.00101.74           C  
ANISOU  497  CG  LYS A  97    18803  12543   7309  -1583  -1357  -2992       C  
ATOM    498  CD  LYS A  97       9.108  20.215  61.928  1.00101.53           C  
ANISOU  498  CD  LYS A  97    18680  12250   7647  -1829  -1360  -3216       C  
ATOM    499  CE  LYS A  97       9.277  21.470  62.774  1.00106.01           C  
ANISOU  499  CE  LYS A  97    19492  12697   8088  -2026  -1318  -3563       C  
ATOM    500  NZ  LYS A  97       9.833  22.614  61.999  1.00106.50           N  
ANISOU  500  NZ  LYS A  97    19469  12491   8505  -2294  -1330  -3765       N  
ATOM    501  N   MET A  98       3.702  18.660  62.353  1.00 99.24           N  
ANISOU  501  N   MET A  98    18879  11583   7243   -630    322  -2605       N  
ATOM    502  CA  MET A  98       2.449  18.121  62.870  1.00 99.27           C  
ANISOU  502  CA  MET A  98    19001  11621   7095   -382    715  -2456       C  
ATOM    503  C   MET A  98       1.384  18.268  61.789  1.00 98.55           C  
ANISOU  503  C   MET A  98    18627  11325   7492   -177   1070  -2304       C  
ATOM    504  O   MET A  98       1.649  18.769  60.693  1.00 98.00           O  
ANISOU  504  O   MET A  98    18318  11089   7828   -219    997  -2308       O  
ATOM    505  CB  MET A  98       2.052  18.802  64.187  1.00103.11           C  
ANISOU  505  CB  MET A  98    19844  12090   7244   -374    916  -2682       C  
ATOM    506  CG  MET A  98       1.810  20.306  64.112  1.00105.20           C  
ANISOU  506  CG  MET A  98    20256  12030   7685   -398   1127  -2988       C  
ATOM    507  SD  MET A  98       0.129  20.781  63.663  1.00104.57           S  
ANISOU  507  SD  MET A  98    20170  11672   7889    -56   1761  -2939       S  
ATOM    508  CE  MET A  98       0.417  22.421  63.007  1.00105.67           C  
ANISOU  508  CE  MET A  98    20384  11395   8369   -138   1794  -3220       C  
ATOM    509  N   TRP A  99       0.171  17.819  62.105  1.00 94.28           N  
ANISOU  509  N   TRP A  99    18104  10819   6899     39   1455  -2158       N  
ATOM    510  CA  TRP A  99      -0.917  17.737  61.138  1.00 93.96           C  
ANISOU  510  CA  TRP A  99    17732  10674   7294    241   1763  -1963       C  
ATOM    511  C   TRP A  99      -1.965  18.790  61.475  1.00 94.66           C  
ANISOU  511  C   TRP A  99    18036  10549   7380    429   2225  -2153       C  
ATOM    512  O   TRP A  99      -2.574  18.749  62.550  1.00 95.38           O  
ANISOU  512  O   TRP A  99    18414  10704   7123    518   2510  -2228       O  
ATOM    513  CB  TRP A  99      -1.532  16.339  61.125  1.00 89.14           C  
ANISOU  513  CB  TRP A  99    16893  10283   6692    328   1851  -1622       C  
ATOM    514  CG  TRP A  99      -2.505  16.122  60.010  1.00 88.98           C  
ANISOU  514  CG  TRP A  99    16464  10211   7134    474   2066  -1410       C  
ATOM    515  CD1 TRP A  99      -3.865  16.084  60.099  1.00 89.67           C  
ANISOU  515  CD1 TRP A  99    16457  10307   7308    662   2497  -1319       C  
ATOM    516  CD2 TRP A  99      -2.187  15.917  58.629  1.00 88.31           C  
ANISOU  516  CD2 TRP A  99    15994  10086   7472    434   1852  -1265       C  
ATOM    517  NE1 TRP A  99      -4.414  15.862  58.858  1.00 89.60           N  
ANISOU  517  NE1 TRP A  99    16013  10282   7749    731   2526  -1125       N  
ATOM    518  CE2 TRP A  99      -3.404  15.757  57.939  1.00 88.73           C  
ANISOU  518  CE2 TRP A  99    15745  10134   7834    594   2137  -1092       C  
ATOM    519  CE3 TRP A  99      -0.989  15.848  57.909  1.00 87.52           C  
ANISOU  519  CE3 TRP A  99    15765   9976   7511    276   1453  -1264       C  
ATOM    520  CZ2 TRP A  99      -3.459  15.535  56.564  1.00 88.43           C  
ANISOU  520  CZ2 TRP A  99    15324  10076   8200    592   2015   -929       C  
ATOM    521  CZ3 TRP A  99      -1.045  15.629  56.546  1.00 87.04           C  
ANISOU  521  CZ3 TRP A  99    15334   9879   7857    287   1375  -1102       C  
ATOM    522  CH2 TRP A  99      -2.271  15.476  55.887  1.00 87.51           C  
ANISOU  522  CH2 TRP A  99    15139   9930   8183    440   1643   -941       C  
ATOM    523  N   THR A 100      -2.176  19.721  60.547  1.00 91.23           N  
ANISOU  523  N   THR A 100    17473   9858   7332    508   2316  -2217       N  
ATOM    524  CA  THR A 100      -3.055  20.866  60.743  1.00 91.90           C  
ANISOU  524  CA  THR A 100    17764   9680   7473    721   2737  -2407       C  
ATOM    525  C   THR A 100      -4.509  20.569  60.393  1.00 92.47           C  
ANISOU  525  C   THR A 100    17533   9807   7793   1026   3142  -2176       C  
ATOM    526  O   THR A 100      -5.409  21.276  60.864  1.00 93.32           O  
ANISOU  526  O   THR A 100    17813   9780   7863   1259   3566  -2303       O  
ATOM    527  CB  THR A 100      -2.541  22.036  59.887  1.00 90.42           C  
ANISOU  527  CB  THR A 100    17603   9163   7590    668   2631  -2558       C  
ATOM    528  OG1 THR A 100      -1.191  22.345  60.257  1.00 90.14           O  
ANISOU  528  OG1 THR A 100    17825   9096   7328    343   2262  -2793       O  
ATOM    529  CG2 THR A 100      -3.396  23.286  60.046  1.00 91.21           C  
ANISOU  529  CG2 THR A 100    17953   8928   7774    921   3067  -2752       C  
ATOM    530  N   PHE A 101      -4.764  19.510  59.629  1.00 89.72           N  
ANISOU  530  N   PHE A 101    16739   9668   7683   1024   3031  -1851       N  
ATOM    531  CA  PHE A 101      -5.972  19.414  58.826  1.00 90.35           C  
ANISOU  531  CA  PHE A 101    16414   9774   8142   1263   3297  -1629       C  
ATOM    532  C   PHE A 101      -7.000  18.425  59.363  1.00 91.08           C  
ANISOU  532  C   PHE A 101    16344  10130   8132   1348   3583  -1436       C  
ATOM    533  O   PHE A 101      -8.038  18.228  58.722  1.00 91.82           O  
ANISOU  533  O   PHE A 101    16043  10305   8538   1513   3786  -1238       O  
ATOM    534  CB  PHE A 101      -5.579  19.049  57.392  1.00 87.61           C  
ANISOU  534  CB  PHE A 101    15665   9446   8177   1176   2973  -1420       C  
ATOM    535  CG  PHE A 101      -4.550  19.975  56.807  1.00 86.80           C  
ANISOU  535  CG  PHE A 101    15698   9094   8189   1063   2713  -1580       C  
ATOM    536  CD1 PHE A 101      -4.910  21.211  56.299  1.00 87.09           C  
ANISOU  536  CD1 PHE A 101    15786   8842   8461   1243   2887  -1669       C  
ATOM    537  CD2 PHE A 101      -3.210  19.619  56.800  1.00 85.81           C  
ANISOU  537  CD2 PHE A 101    15652   9018   7933    778   2309  -1634       C  
ATOM    538  CE1 PHE A 101      -3.956  22.064  55.777  1.00 86.28           C  
ANISOU  538  CE1 PHE A 101    15836   8486   8461   1104   2673  -1807       C  
ATOM    539  CE2 PHE A 101      -2.253  20.468  56.279  1.00 85.14           C  
ANISOU  539  CE2 PHE A 101    15668   8720   7960    635   2091  -1781       C  
ATOM    540  CZ  PHE A 101      -2.627  21.692  55.767  1.00 85.32           C  
ANISOU  540  CZ  PHE A 101    15768   8436   8214    780   2280  -1869       C  
ATOM    541  N   GLY A 102      -6.750  17.802  60.509  1.00 90.04           N  
ANISOU  541  N   GLY A 102    16496  10146   7569   1230   3600  -1476       N  
ATOM    542  CA  GLY A 102      -7.729  16.934  61.132  1.00 90.71           C  
ANISOU  542  CA  GLY A 102    16490  10455   7522   1292   3927  -1301       C  
ATOM    543  C   GLY A 102      -7.577  15.477  60.727  1.00 90.16           C  
ANISOU  543  C   GLY A 102    16139  10595   7522   1112   3702   -997       C  
ATOM    544  O   GLY A 102      -6.922  15.134  59.745  1.00 89.40           O  
ANISOU  544  O   GLY A 102    15820  10481   7667    993   3335   -896       O  
ATOM    545  N   ASN A 103      -8.209  14.600  61.519  1.00 92.95           N  
ANISOU  545  N   ASN A 103    16532  11135   7650   1090   3958   -852       N  
ATOM    546  CA  ASN A 103      -8.162  13.172  61.215  1.00 92.43           C  
ANISOU  546  CA  ASN A 103    16250  11226   7643    917   3804   -559       C  
ATOM    547  C   ASN A 103      -8.955  12.826  59.963  1.00 92.80           C  
ANISOU  547  C   ASN A 103    15747  11321   8192    936   3843   -361       C  
ATOM    548  O   ASN A 103      -8.626  11.849  59.280  1.00 92.10           O  
ANISOU  548  O   ASN A 103    15459  11279   8256    772   3584   -174       O  
ATOM    549  CB  ASN A 103      -8.678  12.336  62.388  1.00 96.25           C  
ANISOU  549  CB  ASN A 103    16944  11871   7756    870   4103   -436       C  
ATOM    550  CG  ASN A 103      -7.738  12.342  63.575  1.00 95.95           C  
ANISOU  550  CG  ASN A 103    17452  11839   7164    801   3953   -566       C  
ATOM    551  OD1 ASN A 103      -8.097  12.796  64.659  1.00 96.86           O  
ANISOU  551  OD1 ASN A 103    17906  11982   6914    883   4266   -710       O  
ATOM    552  ND2 ASN A 103      -6.528  11.826  63.378  1.00 94.98           N  
ANISOU  552  ND2 ASN A 103    17413  11710   6964    656   3472   -515       N  
ATOM    553  N   PHE A 104     -10.008  13.586  59.653  1.00 89.54           N  
ANISOU  553  N   PHE A 104    15086  10904   8031   1140   4161   -396       N  
ATOM    554  CA  PHE A 104     -10.755  13.330  58.426  1.00 90.20           C  
ANISOU  554  CA  PHE A 104    14627  11067   8577   1159   4150   -212       C  
ATOM    555  C   PHE A 104      -9.859  13.481  57.205  1.00 89.40           C  
ANISOU  555  C   PHE A 104    14404  10846   8719   1085   3693   -214       C  
ATOM    556  O   PHE A 104      -9.727  12.557  56.394  1.00 89.01           O  
ANISOU  556  O   PHE A 104    14103  10871   8845    915   3467    -40       O  
ATOM    557  CB  PHE A 104     -11.961  14.262  58.316  1.00 91.32           C  
ANISOU  557  CB  PHE A 104    14521  11233   8943   1446   4540   -251       C  
ATOM    558  CG  PHE A 104     -12.720  14.104  57.025  1.00 92.28           C  
ANISOU  558  CG  PHE A 104    14066  11471   9526   1481   4480    -64       C  
ATOM    559  CD1 PHE A 104     -13.554  13.016  56.822  1.00 92.97           C  
ANISOU  559  CD1 PHE A 104    13776  11801   9747   1328   4591    160       C  
ATOM    560  CD2 PHE A 104     -12.579  15.033  56.004  1.00 92.56           C  
ANISOU  560  CD2 PHE A 104    13951  11373   9845   1645   4299   -108       C  
ATOM    561  CE1 PHE A 104     -14.244  12.865  55.631  1.00 94.02           C  
ANISOU  561  CE1 PHE A 104    13376  12072  10277   1330   4497    316       C  
ATOM    562  CE2 PHE A 104     -13.266  14.887  54.812  1.00 93.63           C  
ANISOU  562  CE2 PHE A 104    13569  11644  10360   1679   4211     73       C  
ATOM    563  CZ  PHE A 104     -14.100  13.803  54.627  1.00 94.41           C  
ANISOU  563  CZ  PHE A 104    13279  12015  10578   1517   4296    275       C  
ATOM    564  N   TRP A 105      -9.233  14.650  57.054  1.00 88.91           N  
ANISOU  564  N   TRP A 105    14537  10582   8662   1198   3574   -418       N  
ATOM    565  CA  TRP A 105      -8.342  14.841  55.918  1.00 88.17           C  
ANISOU  565  CA  TRP A 105    14345  10374   8782   1115   3173   -419       C  
ATOM    566  C   TRP A 105      -7.097  13.973  56.031  1.00 86.70           C  
ANISOU  566  C   TRP A 105    14333  10204   8407    869   2810   -398       C  
ATOM    567  O   TRP A 105      -6.508  13.609  55.008  1.00 86.09           O  
ANISOU  567  O   TRP A 105    14071  10112   8526    759   2506   -315       O  
ATOM    568  CB  TRP A 105      -7.959  16.312  55.769  1.00 86.14           C  
ANISOU  568  CB  TRP A 105    14282   9869   8576   1265   3160   -636       C  
ATOM    569  CG  TRP A 105      -7.093  16.534  54.574  1.00 85.42           C  
ANISOU  569  CG  TRP A 105    14080   9667   8710   1170   2791   -616       C  
ATOM    570  CD1 TRP A 105      -5.766  16.846  54.567  1.00 84.17           C  
ANISOU  570  CD1 TRP A 105    14172   9371   8438   1014   2493   -761       C  
ATOM    571  CD2 TRP A 105      -7.480  16.388  53.203  1.00 86.01           C  
ANISOU  571  CD2 TRP A 105    13750   9790   9139   1201   2680   -431       C  
ATOM    572  NE1 TRP A 105      -5.310  16.937  53.274  1.00 83.79           N  
ANISOU  572  NE1 TRP A 105    13905   9267   8664    957   2242   -676       N  
ATOM    573  CE2 TRP A 105      -6.343  16.659  52.418  1.00 84.95           C  
ANISOU  573  CE2 TRP A 105    13673   9523   9083   1074   2346   -474       C  
ATOM    574  CE3 TRP A 105      -8.682  16.071  52.562  1.00 87.46           C  
ANISOU  574  CE3 TRP A 105    13519  10138   9572   1313   2826   -235       C  
ATOM    575  CZ2 TRP A 105      -6.371  16.622  51.025  1.00 85.28           C  
ANISOU  575  CZ2 TRP A 105    13416   9575   9410   1067   2172   -328       C  
ATOM    576  CZ3 TRP A 105      -8.708  16.035  51.181  1.00 87.96           C  
ANISOU  576  CZ3 TRP A 105    13278  10226   9915   1298   2613    -96       C  
ATOM    577  CH2 TRP A 105      -7.560  16.309  50.427  1.00 86.89           C  
ANISOU  577  CH2 TRP A 105    13253   9941   9820   1182   2298   -142       C  
ATOM    578  N   CYS A 106      -6.686  13.628  57.254  1.00 86.82           N  
ANISOU  578  N   CYS A 106    14699  10258   8031    799   2841   -464       N  
ATOM    579  CA  CYS A 106      -5.594  12.674  57.423  1.00 85.61           C  
ANISOU  579  CA  CYS A 106    14677  10153   7696    609   2508   -395       C  
ATOM    580  C   CYS A 106      -5.915  11.346  56.750  1.00 85.25           C  
ANISOU  580  C   CYS A 106    14336  10214   7841    500   2454   -130       C  
ATOM    581  O   CYS A 106      -5.027  10.697  56.185  1.00 84.19           O  
ANISOU  581  O   CYS A 106    14153  10065   7769    383   2132    -57       O  
ATOM    582  CB  CYS A 106      -5.301  12.468  58.909  1.00 88.17           C  
ANISOU  582  CB  CYS A 106    15422  10539   7538    581   2581   -466       C  
ATOM    583  SG  CYS A 106      -3.987  11.274  59.265  1.00 87.01           S  
ANISOU  583  SG  CYS A 106    15450  10476   7135    410   2173   -342       S  
ATOM    584  N   GLU A 107      -7.181  10.927  56.798  1.00 85.91           N  
ANISOU  584  N   GLU A 107    14216  10402   8023    528   2778      6       N  
ATOM    585  CA  GLU A 107      -7.581   9.688  56.139  1.00 85.64           C  
ANISOU  585  CA  GLU A 107    13908  10450   8181    381   2747    234       C  
ATOM    586  C   GLU A 107      -7.548   9.837  54.621  1.00 85.67           C  
ANISOU  586  C   GLU A 107    13558  10423   8569    362   2535    261       C  
ATOM    587  O   GLU A 107      -6.883   9.060  53.927  1.00 84.51           O  
ANISOU  587  O   GLU A 107    13356  10245   8509    227   2265    341       O  
ATOM    588  CB  GLU A 107      -8.970   9.259  56.617  1.00 91.78           C  
ANISOU  588  CB  GLU A 107    14536  11369   8969    377   3163    359       C  
ATOM    589  CG  GLU A 107      -9.002   8.760  58.057  1.00 91.68           C  
ANISOU  589  CG  GLU A 107    14886  11400   8548    343   3381    398       C  
ATOM    590  CD  GLU A 107     -10.392   8.340  58.508  1.00 92.95           C  
ANISOU  590  CD  GLU A 107    14873  11711   8734    316   3835    531       C  
ATOM    591  OE1 GLU A 107     -11.363   8.585  57.761  1.00 94.12           O  
ANISOU  591  OE1 GLU A 107    14591  11947   9222    351   3980    566       O  
ATOM    592  OE2 GLU A 107     -10.512   7.757  59.608  1.00 92.96           O  
ANISOU  592  OE2 GLU A 107    15156  11755   8408    254   4046    612       O  
ATOM    593  N   PHE A 108      -8.265  10.831  54.086  1.00 83.21           N  
ANISOU  593  N   PHE A 108    13020  10118   8479    515   2662    204       N  
ATOM    594  CA  PHE A 108      -8.269  11.045  52.640  1.00 83.58           C  
ANISOU  594  CA  PHE A 108    12755  10151   8853    511   2458    245       C  
ATOM    595  C   PHE A 108      -6.868  11.302  52.099  1.00 82.27           C  
ANISOU  595  C   PHE A 108    12744   9839   8676    460   2100    154       C  
ATOM    596  O   PHE A 108      -6.476  10.717  51.083  1.00 81.60           O  
ANISOU  596  O   PHE A 108    12502   9758   8744    341   1871    232       O  
ATOM    597  CB  PHE A 108      -9.217  12.184  52.264  1.00 88.45           C  
ANISOU  597  CB  PHE A 108    13145  10785   9675    738   2650    215       C  
ATOM    598  CG  PHE A 108     -10.625  11.733  52.003  1.00 90.04           C  
ANISOU  598  CG  PHE A 108    12944  11200  10068    745   2875    373       C  
ATOM    599  CD1 PHE A 108     -10.986  11.288  50.740  1.00 90.78           C  
ANISOU  599  CD1 PHE A 108    12667  11402  10422    645   2698    502       C  
ATOM    600  CD2 PHE A 108     -11.575  11.721  53.008  1.00 90.88           C  
ANISOU  600  CD2 PHE A 108    13030  11419  10080    827   3261    389       C  
ATOM    601  CE1 PHE A 108     -12.274  10.862  50.475  1.00 92.38           C  
ANISOU  601  CE1 PHE A 108    12459  11837  10806    611   2869    640       C  
ATOM    602  CE2 PHE A 108     -12.868  11.289  52.750  1.00 92.43           C  
ANISOU  602  CE2 PHE A 108    12797  11846  10478    805   3468    539       C  
ATOM    603  CZ  PHE A 108     -13.216  10.861  51.482  1.00 93.20           C  
ANISOU  603  CZ  PHE A 108    12500  12064  10849    687   3255    663       C  
ATOM    604  N   TRP A 109      -6.100  12.180  52.752  1.00 82.07           N  
ANISOU  604  N   TRP A 109    13023   9689   8470    531   2059    -24       N  
ATOM    605  CA  TRP A 109      -4.723  12.413  52.319  1.00 80.88           C  
ANISOU  605  CA  TRP A 109    12994   9428   8309    450   1729   -113       C  
ATOM    606  C   TRP A 109      -3.968  11.099  52.179  1.00 79.44           C  
ANISOU  606  C   TRP A 109    12811   9304   8068    286   1504     -2       C  
ATOM    607  O   TRP A 109      -3.310  10.847  51.164  1.00 78.71           O  
ANISOU  607  O   TRP A 109    12586   9183   8136    212   1274     32       O  
ATOM    608  CB  TRP A 109      -3.993  13.330  53.298  1.00 81.12           C  
ANISOU  608  CB  TRP A 109    13380   9351   8092    483   1713   -329       C  
ATOM    609  CG  TRP A 109      -2.574  13.564  52.901  1.00 80.01           C  
ANISOU  609  CG  TRP A 109    13317   9130   7952    366   1378   -421       C  
ATOM    610  CD1 TRP A 109      -2.129  14.302  51.844  1.00 79.79           C  
ANISOU  610  CD1 TRP A 109    13176   8987   8154    354   1246   -464       C  
ATOM    611  CD2 TRP A 109      -1.409  13.011  53.524  1.00 79.05           C  
ANISOU  611  CD2 TRP A 109    13374   9064   7599    245   1134   -457       C  
ATOM    612  NE1 TRP A 109      -0.756  14.267  51.788  1.00 78.66           N  
ANISOU  612  NE1 TRP A 109    13114   8826   7946    212    959   -541       N  
ATOM    613  CE2 TRP A 109      -0.290  13.478  52.807  1.00 78.37           C  
ANISOU  613  CE2 TRP A 109    13237   8906   7635    154    871   -539       C  
ATOM    614  CE3 TRP A 109      -1.203  12.177  54.627  1.00 78.85           C  
ANISOU  614  CE3 TRP A 109    13543   9151   7265    213   1114   -413       C  
ATOM    615  CZ2 TRP A 109       1.016  13.139  53.156  1.00 77.75           C  
ANISOU  615  CZ2 TRP A 109    13244   8892   7407     39    582   -586       C  
ATOM    616  CZ3 TRP A 109       0.093  11.840  54.972  1.00 78.27           C  
ANISOU  616  CZ3 TRP A 109    13583   9130   7024    121    805   -445       C  
ATOM    617  CH2 TRP A 109       1.186  12.321  54.239  1.00 77.84           C  
ANISOU  617  CH2 TRP A 109    13425   9030   7122     38    539   -536       C  
ATOM    618  N   THR A 110      -4.057  10.248  53.200  1.00 82.71           N  
ANISOU  618  N   THR A 110    13395   9789   8245    243   1589     64       N  
ATOM    619  CA  THR A 110      -3.489   8.910  53.101  1.00 81.37           C  
ANISOU  619  CA  THR A 110    13240   9643   8033    124   1422    205       C  
ATOM    620  C   THR A 110      -4.213   8.085  52.043  1.00 81.15           C  
ANISOU  620  C   THR A 110    12919   9643   8271     37   1464    355       C  
ATOM    621  O   THR A 110      -3.575   7.400  51.234  1.00 79.87           O  
ANISOU  621  O   THR A 110    12684   9441   8222    -45   1258    409       O  
ATOM    622  CB  THR A 110      -3.559   8.217  54.461  1.00 84.06           C  
ANISOU  622  CB  THR A 110    13858  10036   8045    114   1541    276       C  
ATOM    623  OG1 THR A 110      -2.784   8.954  55.417  1.00 84.26           O  
ANISOU  623  OG1 THR A 110    14173  10058   7783    170   1447    117       O  
ATOM    624  CG2 THR A 110      -3.032   6.804  54.362  1.00 82.84           C  
ANISOU  624  CG2 THR A 110    13746   9867   7864     24   1394    451       C  
ATOM    625  N   SER A 111      -5.546   8.149  52.029  1.00 81.11           N  
ANISOU  625  N   SER A 111    12734   9718   8365     47   1732    413       N  
ATOM    626  CA  SER A 111      -6.324   7.342  51.095  1.00 81.25           C  
ANISOU  626  CA  SER A 111    12461   9796   8615    -80   1764    543       C  
ATOM    627  C   SER A 111      -6.074   7.759  49.651  1.00 81.20           C  
ANISOU  627  C   SER A 111    12227   9769   8854    -81   1553    508       C  
ATOM    628  O   SER A 111      -5.930   6.905  48.768  1.00 80.17           O  
ANISOU  628  O   SER A 111    11990   9630   8841   -221   1418    573       O  
ATOM    629  CB  SER A 111      -7.809   7.449  51.434  1.00 83.42           C  
ANISOU  629  CB  SER A 111    12537  10206   8951    -66   2093    606       C  
ATOM    630  OG  SER A 111      -8.090   6.890  52.703  1.00 83.36           O  
ANISOU  630  OG  SER A 111    12743  10224   8706   -101   2322    667       O  
ATOM    631  N   ILE A 112      -6.027   9.067  49.388  1.00 78.15           N  
ANISOU  631  N   ILE A 112    11798   9360   8534     71   1537    405       N  
ATOM    632  CA  ILE A 112      -5.763   9.546  48.035  1.00 78.33           C  
ANISOU  632  CA  ILE A 112    11644   9358   8758     80   1349    392       C  
ATOM    633  C   ILE A 112      -4.324   9.241  47.631  1.00 76.04           C  
ANISOU  633  C   ILE A 112    11500   8964   8427      4   1086    343       C  
ATOM    634  O   ILE A 112      -4.049   8.904  46.473  1.00 74.97           O  
ANISOU  634  O   ILE A 112    11234   8829   8424    -75    933    376       O  
ATOM    635  CB  ILE A 112      -6.081  11.049  47.934  1.00 76.96           C  
ANISOU  635  CB  ILE A 112    11435   9143   8661    280   1430    317       C  
ATOM    636  CG1 ILE A 112      -7.572  11.293  48.176  1.00 79.16           C  
ANISOU  636  CG1 ILE A 112    11493   9556   9029    394   1699    388       C  
ATOM    637  CG2 ILE A 112      -5.666  11.602  46.583  1.00 77.31           C  
ANISOU  637  CG2 ILE A 112    11362   9138   8875    292   1233    321       C  
ATOM    638  CD1 ILE A 112      -7.926  12.750  48.384  1.00 80.74           C  
ANISOU  638  CD1 ILE A 112    11725   9676   9275    648   1848    311       C  
ATOM    639  N   ASP A 113      -3.386   9.355  48.576  1.00 78.13           N  
ANISOU  639  N   ASP A 113    12026   9162   8499     27   1030    261       N  
ATOM    640  CA  ASP A 113      -1.994   9.017  48.293  1.00 76.42           C  
ANISOU  640  CA  ASP A 113    11901   8885   8249    -31    785    225       C  
ATOM    641  C   ASP A 113      -1.867   7.565  47.845  1.00 74.57           C  
ANISOU  641  C   ASP A 113    11620   8659   8054   -138    720    342       C  
ATOM    642  O   ASP A 113      -1.198   7.265  46.850  1.00 73.18           O  
ANISOU  642  O   ASP A 113    11365   8450   7990   -184    566    341       O  
ATOM    643  CB  ASP A 113      -1.134   9.283  49.532  1.00 74.86           C  
ANISOU  643  CB  ASP A 113    11965   8667   7811      5    725    133       C  
ATOM    644  CG  ASP A 113       0.357   9.201  49.247  1.00 74.01           C  
ANISOU  644  CG  ASP A 113    11890   8534   7696    -34    459     81       C  
ATOM    645  OD1 ASP A 113       0.745   8.885  48.103  1.00 73.09           O  
ANISOU  645  OD1 ASP A 113    11615   8400   7756    -78    355    117       O  
ATOM    646  OD2 ASP A 113       1.148   9.471  50.174  1.00 74.27           O  
ANISOU  646  OD2 ASP A 113    12099   8585   7537    -23    356     -2       O  
ATOM    647  N   VAL A 114      -2.509   6.648  48.571  1.00 75.62           N  
ANISOU  647  N   VAL A 114    11825   8817   8091   -182    862    441       N  
ATOM    648  CA  VAL A 114      -2.494   5.244  48.173  1.00 74.29           C  
ANISOU  648  CA  VAL A 114    11655   8604   7969   -298    837    550       C  
ATOM    649  C   VAL A 114      -3.208   5.063  46.839  1.00 74.26           C  
ANISOU  649  C   VAL A 114    11401   8631   8183   -409    840    567       C  
ATOM    650  O   VAL A 114      -2.777   4.274  45.988  1.00 72.91           O  
ANISOU  650  O   VAL A 114    11216   8394   8091   -494    732    580       O  
ATOM    651  CB  VAL A 114      -3.118   4.374  49.281  1.00 76.31           C  
ANISOU  651  CB  VAL A 114    12066   8857   8071   -345   1026    667       C  
ATOM    652  CG1 VAL A 114      -3.217   2.925  48.836  1.00 75.36           C  
ANISOU  652  CG1 VAL A 114    11974   8640   8021   -489   1034    780       C  
ATOM    653  CG2 VAL A 114      -2.301   4.487  50.557  1.00 76.38           C  
ANISOU  653  CG2 VAL A 114    12353   8854   7813   -232    977    661       C  
ATOM    654  N   LEU A 115      -4.302   5.799  46.630  1.00 73.44           N  
ANISOU  654  N   LEU A 115    11099   8636   8170   -396    960    564       N  
ATOM    655  CA  LEU A 115      -5.051   5.695  45.380  1.00 74.27           C  
ANISOU  655  CA  LEU A 115    10941   8821   8456   -498    929    589       C  
ATOM    656  C   LEU A 115      -4.202   6.085  44.176  1.00 72.96           C  
ANISOU  656  C   LEU A 115    10739   8614   8368   -478    720    526       C  
ATOM    657  O   LEU A 115      -4.245   5.418  43.136  1.00 72.38           O  
ANISOU  657  O   LEU A 115    10586   8547   8369   -609    632    536       O  
ATOM    658  CB  LEU A 115      -6.304   6.566  45.450  1.00 73.96           C  
ANISOU  658  CB  LEU A 115    10670   8932   8500   -423   1079    614       C  
ATOM    659  CG  LEU A 115      -7.150   6.625  44.179  1.00 75.93           C  
ANISOU  659  CG  LEU A 115    10606   9321   8922   -500   1011    656       C  
ATOM    660  CD1 LEU A 115      -7.637   5.248  43.796  1.00 75.84           C  
ANISOU  660  CD1 LEU A 115    10521   9346   8949   -766   1009    706       C  
ATOM    661  CD2 LEU A 115      -8.322   7.568  44.373  1.00 79.20           C  
ANISOU  661  CD2 LEU A 115    10774   9894   9425   -355   1162    700       C  
ATOM    662  N   CYS A 116      -3.428   7.165  44.293  1.00 73.64           N  
ANISOU  662  N   CYS A 116    10898   8654   8426   -336    652    453       N  
ATOM    663  CA  CYS A 116      -2.651   7.636  43.152  1.00 72.37           C  
ANISOU  663  CA  CYS A 116    10698   8460   8339   -328    492    408       C  
ATOM    664  C   CYS A 116      -1.497   6.699  42.824  1.00 69.85           C  
ANISOU  664  C   CYS A 116    10490   8058   7990   -396    373    383       C  
ATOM    665  O   CYS A 116      -1.108   6.585  41.657  1.00 68.77           O  
ANISOU  665  O   CYS A 116    10294   7916   7918   -447    280    366       O  
ATOM    666  CB  CYS A 116      -2.129   9.047  43.414  1.00 69.43           C  
ANISOU  666  CB  CYS A 116    10389   8034   7956   -193    477    335       C  
ATOM    667  SG  CYS A 116      -3.412  10.314  43.489  1.00 73.01           S  
ANISOU  667  SG  CYS A 116    10715   8538   8486    -48    626    365       S  
ATOM    668  N   VAL A 117      -0.937   6.026  43.826  1.00 70.81           N  
ANISOU  668  N   VAL A 117    10778   8119   8006   -377    381    390       N  
ATOM    669  CA  VAL A 117       0.163   5.105  43.561  1.00 69.36           C  
ANISOU  669  CA  VAL A 117    10688   7854   7812   -389    280    385       C  
ATOM    670  C   VAL A 117      -0.362   3.786  43.009  1.00 68.89           C  
ANISOU  670  C   VAL A 117    10638   7740   7796   -518    330    437       C  
ATOM    671  O   VAL A 117       0.237   3.196  42.104  1.00 68.00           O  
ANISOU  671  O   VAL A 117    10538   7562   7735   -551    267    407       O  
ATOM    672  CB  VAL A 117       0.999   4.901  44.836  1.00 70.87           C  
ANISOU  672  CB  VAL A 117    11052   8013   7864   -291    240    395       C  
ATOM    673  CG1 VAL A 117       2.139   3.925  44.580  1.00 70.37           C  
ANISOU  673  CG1 VAL A 117    11054   7873   7810   -249    138    414       C  
ATOM    674  CG2 VAL A 117       1.529   6.232  45.334  1.00 72.02           C  
ANISOU  674  CG2 VAL A 117    11200   8207   7956   -216    176    305       C  
ATOM    675  N   THR A 118      -1.494   3.309  43.534  1.00 71.69           N  
ANISOU  675  N   THR A 118    10994   8114   8131   -608    463    506       N  
ATOM    676  CA  THR A 118      -2.078   2.071  43.031  1.00 71.72           C  
ANISOU  676  CA  THR A 118    11017   8050   8184   -787    519    542       C  
ATOM    677  C   THR A 118      -2.562   2.233  41.594  1.00 72.05           C  
ANISOU  677  C   THR A 118    10877   8173   8327   -912    454    484       C  
ATOM    678  O   THR A 118      -2.331   1.358  40.752  1.00 71.45           O  
ANISOU  678  O   THR A 118    10865   8005   8277  -1026    418    443       O  
ATOM    679  CB  THR A 118      -3.225   1.623  43.939  1.00 72.66           C  
ANISOU  679  CB  THR A 118    11145   8194   8267   -891    696    633       C  
ATOM    680  OG1 THR A 118      -2.729   1.392  45.263  1.00 72.40           O  
ANISOU  680  OG1 THR A 118    11331   8086   8092   -775    753    700       O  
ATOM    681  CG2 THR A 118      -3.860   0.345  43.413  1.00 72.94           C  
ANISOU  681  CG2 THR A 118    11205   8142   8366  -1135    760    658       C  
ATOM    682  N   ALA A 119      -3.227   3.351  41.292  1.00 69.41           N  
ANISOU  682  N   ALA A 119    10335   8002   8034   -879    438    483       N  
ATOM    683  CA  ALA A 119      -3.706   3.588  39.936  1.00 70.38           C  
ANISOU  683  CA  ALA A 119    10285   8236   8221   -975    346    455       C  
ATOM    684  C   ALA A 119      -2.571   3.838  38.952  1.00 68.62           C  
ANISOU  684  C   ALA A 119    10130   7957   7984   -918    225    384       C  
ATOM    685  O   ALA A 119      -2.752   3.613  37.751  1.00 69.07           O  
ANISOU  685  O   ALA A 119    10135   8064   8044  -1033    149    349       O  
ATOM    686  CB  ALA A 119      -4.677   4.768  39.916  1.00 70.67           C  
ANISOU  686  CB  ALA A 119    10086   8456   8308   -896    362    506       C  
ATOM    687  N   SER A 120      -1.413   4.302  39.427  1.00 70.00           N  
ANISOU  687  N   SER A 120    10413   8049   8135   -760    206    360       N  
ATOM    688  CA  SER A 120      -0.290   4.556  38.530  1.00 68.69           C  
ANISOU  688  CA  SER A 120    10282   7846   7971   -715    124    298       C  
ATOM    689  C   SER A 120       0.328   3.254  38.036  1.00 67.99           C  
ANISOU  689  C   SER A 120    10326   7639   7870   -782    129    248       C  
ATOM    690  O   SER A 120       0.566   3.086  36.834  1.00 68.03           O  
ANISOU  690  O   SER A 120    10333   7651   7865   -847     95    191       O  
ATOM    691  CB  SER A 120       0.764   5.413  39.230  1.00 68.70           C  
ANISOU  691  CB  SER A 120    10322   7815   7965   -561    100    280       C  
ATOM    692  OG  SER A 120       0.269   6.709  39.510  1.00 69.53           O  
ANISOU  692  OG  SER A 120    10348   7984   8085   -498    112    300       O  
ATOM    693  N   ILE A 121       0.602   2.324  38.952  1.00 68.53           N  
ANISOU  693  N   ILE A 121    10533   7582   7922   -752    183    272       N  
ATOM    694  CA  ILE A 121       1.268   1.084  38.566  1.00 68.35           C  
ANISOU  694  CA  ILE A 121    10672   7396   7903   -764    211    231       C  
ATOM    695  C   ILE A 121       0.349   0.213  37.717  1.00 68.87           C  
ANISOU  695  C   ILE A 121    10781   7421   7968   -990    249    186       C  
ATOM    696  O   ILE A 121       0.802  -0.438  36.768  1.00 68.94           O  
ANISOU  696  O   ILE A 121    10892   7335   7968  -1036    259     96       O  
ATOM    697  CB  ILE A 121       1.787   0.339  39.811  1.00 69.35           C  
ANISOU  697  CB  ILE A 121    10957   7386   8006   -641    252    304       C  
ATOM    698  CG1 ILE A 121       2.587  -0.900  39.396  1.00 69.70           C  
ANISOU  698  CG1 ILE A 121    11179   7230   8076   -589    295    274       C  
ATOM    699  CG2 ILE A 121       0.646  -0.015  40.759  1.00 69.70           C  
ANISOU  699  CG2 ILE A 121    11050   7418   8015   -745    337    393       C  
ATOM    700  CD1 ILE A 121       3.837  -0.596  38.603  1.00 70.15           C  
ANISOU  700  CD1 ILE A 121    11172   7313   8170   -452    251    197       C  
ATOM    701  N   GLU A 122      -0.949   0.186  38.028  1.00 68.73           N  
ANISOU  701  N   GLU A 122    10679   7482   7955  -1148    277    233       N  
ATOM    702  CA  GLU A 122      -1.866  -0.577  37.187  1.00 69.73           C  
ANISOU  702  CA  GLU A 122    10806   7608   8079  -1414    281    175       C  
ATOM    703  C   GLU A 122      -1.991   0.050  35.807  1.00 70.42           C  
ANISOU  703  C   GLU A 122    10768   7860   8130  -1476    165    102       C  
ATOM    704  O   GLU A 122      -2.091  -0.665  34.804  1.00 70.87           O  
ANISOU  704  O   GLU A 122    10917   7872   8138  -1649    142     -3       O  
ATOM    705  CB  GLU A 122      -3.238  -0.701  37.844  1.00 76.83           C  
ANISOU  705  CB  GLU A 122    11581   8601   9010  -1583    340    252       C  
ATOM    706  CG  GLU A 122      -3.267  -1.645  39.027  1.00 76.51           C  
ANISOU  706  CG  GLU A 122    11730   8366   8974  -1603    485    328       C  
ATOM    707  CD  GLU A 122      -4.661  -1.815  39.591  1.00 78.15           C  
ANISOU  707  CD  GLU A 122    11797   8679   9217  -1811    582    402       C  
ATOM    708  OE1 GLU A 122      -5.582  -1.121  39.111  1.00 79.77           O  
ANISOU  708  OE1 GLU A 122    11716   9136   9458  -1900    520    397       O  
ATOM    709  OE2 GLU A 122      -4.834  -2.637  40.516  1.00 78.12           O  
ANISOU  709  OE2 GLU A 122    11960   8516   9205  -1876    727    480       O  
ATOM    710  N   THR A 123      -1.979   1.381  35.734  1.00 70.20           N  
ANISOU  710  N   THR A 123    10562   8006   8106  -1338     95    155       N  
ATOM    711  CA  THR A 123      -1.974   2.042  34.434  1.00 71.21           C  
ANISOU  711  CA  THR A 123    10607   8276   8175  -1361    -12    121       C  
ATOM    712  C   THR A 123      -0.720   1.678  33.649  1.00 70.10           C  
ANISOU  712  C   THR A 123    10646   8010   7978  -1312      8     20       C  
ATOM    713  O   THR A 123      -0.798   1.289  32.479  1.00 71.02           O  
ANISOU  713  O   THR A 123    10830   8155   8002  -1448    -30    -68       O  
ATOM    714  CB  THR A 123      -2.085   3.556  34.610  1.00 68.57           C  
ANISOU  714  CB  THR A 123    10101   8085   7869  -1191    -57    218       C  
ATOM    715  OG1 THR A 123      -3.324   3.872  35.259  1.00 70.50           O  
ANISOU  715  OG1 THR A 123    10160   8457   8169  -1213    -48    305       O  
ATOM    716  CG2 THR A 123      -2.036   4.248  33.264  1.00 70.10           C  
ANISOU  716  CG2 THR A 123    10246   8406   7985  -1199   -160    219       C  
ATOM    717  N   LEU A 124       0.449   1.784  34.287  1.00 70.39           N  
ANISOU  717  N   LEU A 124    10756   7927   8063  -1120     70     27       N  
ATOM    718  CA  LEU A 124       1.679   1.316  33.655  1.00 70.12           C  
ANISOU  718  CA  LEU A 124    10859   7777   8005  -1048    125    -63       C  
ATOM    719  C   LEU A 124       1.622  -0.176  33.363  1.00 70.40           C  
ANISOU  719  C   LEU A 124    11104   7628   8016  -1162    201   -162       C  
ATOM    720  O   LEU A 124       2.273  -0.652  32.426  1.00 70.93           O  
ANISOU  720  O   LEU A 124    11301   7621   8029  -1163    257   -272       O  
ATOM    721  CB  LEU A 124       2.879   1.631  34.542  1.00 68.78           C  
ANISOU  721  CB  LEU A 124    10676   7546   7912   -826    158    -25       C  
ATOM    722  CG  LEU A 124       3.231   3.107  34.688  1.00 68.46           C  
ANISOU  722  CG  LEU A 124    10478   7639   7895   -734    103     30       C  
ATOM    723  CD1 LEU A 124       4.314   3.270  35.729  1.00 68.41           C  
ANISOU  723  CD1 LEU A 124    10452   7587   7953   -567    106     51       C  
ATOM    724  CD2 LEU A 124       3.684   3.667  33.353  1.00 69.26           C  
ANISOU  724  CD2 LEU A 124    10556   7815   7944   -764    109    -10       C  
ATOM    725  N   CYS A 125       0.858  -0.929  34.153  1.00 69.36           N  
ANISOU  725  N   CYS A 125    11030   7401   7921  -1263    230   -127       N  
ATOM    726  CA  CYS A 125       0.681  -2.346  33.867  1.00 69.71           C  
ANISOU  726  CA  CYS A 125    11309   7227   7949  -1415    314   -223       C  
ATOM    727  C   CYS A 125      -0.242  -2.550  32.672  1.00 70.73           C  
ANISOU  727  C   CYS A 125    11440   7455   7977  -1707    247   -337       C  
ATOM    728  O   CYS A 125       0.001  -3.430  31.838  1.00 71.11           O  
ANISOU  728  O   CYS A 125    11708   7352   7957  -1815    304   -488       O  
ATOM    729  CB  CYS A 125       0.140  -3.062  35.103  1.00 72.16           C  
ANISOU  729  CB  CYS A 125    11698   7393   8326  -1460    383   -131       C  
ATOM    730  SG  CYS A 125       0.010  -4.847  34.936  1.00 72.60           S  
ANISOU  730  SG  CYS A 125    12108   7088   8389  -1639    524   -227       S  
ATOM    731  N   VAL A 126      -1.302  -1.744  32.567  1.00 70.33           N  
ANISOU  731  N   VAL A 126    11149   7666   7908  -1829    122   -271       N  
ATOM    732  CA  VAL A 126      -2.192  -1.839  31.413  1.00 71.82           C  
ANISOU  732  CA  VAL A 126    11292   8016   7979  -2099      6   -361       C  
ATOM    733  C   VAL A 126      -1.466  -1.415  30.141  1.00 72.16           C  
ANISOU  733  C   VAL A 126    11407   8132   7879  -2037    -36   -447       C  
ATOM    734  O   VAL A 126      -1.648  -2.019  29.078  1.00 72.83           O  
ANISOU  734  O   VAL A 126    11641   8212   7818  -2241    -67   -598       O  
ATOM    735  CB  VAL A 126      -3.469  -1.010  31.646  1.00 70.37           C  
ANISOU  735  CB  VAL A 126    10784   8126   7827  -2184   -124   -237       C  
ATOM    736  CG1 VAL A 126      -4.305  -0.951  30.378  1.00 72.21           C  
ANISOU  736  CG1 VAL A 126    10923   8593   7919  -2426   -299   -306       C  
ATOM    737  CG2 VAL A 126      -4.287  -1.610  32.773  1.00 70.44           C  
ANISOU  737  CG2 VAL A 126    10738   8071   7956  -2309    -44   -175       C  
ATOM    738  N   ILE A 127      -0.630  -0.376  30.230  1.00 71.53           N  
ANISOU  738  N   ILE A 127    11239   8115   7823  -1778    -25   -359       N  
ATOM    739  CA  ILE A 127       0.150   0.057  29.072  1.00 72.07           C  
ANISOU  739  CA  ILE A 127    11382   8244   7758  -1715    -20   -419       C  
ATOM    740  C   ILE A 127       1.028  -1.080  28.568  1.00 71.70           C  
ANISOU  740  C   ILE A 127    11621   7965   7657  -1722    133   -596       C  
ATOM    741  O   ILE A 127       1.044  -1.393  27.372  1.00 72.51           O  
ANISOU  741  O   ILE A 127    11877   8098   7577  -1854    133   -731       O  
ATOM    742  CB  ILE A 127       0.991   1.300  29.418  1.00 70.03           C  
ANISOU  742  CB  ILE A 127    10988   8046   7573  -1460      3   -294       C  
ATOM    743  CG1 ILE A 127       0.088   2.493  29.722  1.00 71.09           C  
ANISOU  743  CG1 ILE A 127    10886   8384   7739  -1439   -130   -135       C  
ATOM    744  CG2 ILE A 127       1.944   1.635  28.282  1.00 70.77           C  
ANISOU  744  CG2 ILE A 127    11177   8170   7541  -1404     65   -351       C  
ATOM    745  CD1 ILE A 127       0.823   3.684  30.294  1.00 70.52           C  
ANISOU  745  CD1 ILE A 127    10716   8314   7765  -1220    -95    -26       C  
ATOM    746  N   ALA A 128       1.773  -1.715  29.476  1.00 72.54           N  
ANISOU  746  N   ALA A 128    11817   7836   7909  -1561    270   -595       N  
ATOM    747  CA  ALA A 128       2.679  -2.788  29.079  1.00 72.79           C  
ANISOU  747  CA  ALA A 128    12114   7618   7923  -1495    444   -745       C  
ATOM    748  C   ALA A 128       1.924  -3.946  28.437  1.00 73.18           C  
ANISOU  748  C   ALA A 128    12417   7529   7861  -1782    460   -921       C  
ATOM    749  O   ALA A 128       2.367  -4.501  27.425  1.00 73.89           O  
ANISOU  749  O   ALA A 128    12737   7520   7817  -1824    561  -1100       O  
ATOM    750  CB  ALA A 128       3.479  -3.272  30.287  1.00 71.96           C  
ANISOU  750  CB  ALA A 128    12039   7301   8003  -1248    554   -669       C  
ATOM    751  N   VAL A 129       0.780  -4.325  29.011  1.00 75.34           N  
ANISOU  751  N   VAL A 129    12656   7790   8181  -2003    375   -886       N  
ATOM    752  CA  VAL A 129      -0.007  -5.412  28.437  1.00 75.90           C  
ANISOU  752  CA  VAL A 129    12952   7731   8155  -2342    376  -1064       C  
ATOM    753  C   VAL A 129      -0.657  -4.967  27.134  1.00 76.92           C  
ANISOU  753  C   VAL A 129    13030   8143   8055  -2584    206  -1166       C  
ATOM    754  O   VAL A 129      -0.760  -5.746  26.177  1.00 77.52           O  
ANISOU  754  O   VAL A 129    13370   8122   7960  -2804    231  -1385       O  
ATOM    755  CB  VAL A 129      -1.047  -5.911  29.457  1.00 73.81           C  
ANISOU  755  CB  VAL A 129    12630   7396   8020  -2538    349   -981       C  
ATOM    756  CG1 VAL A 129      -1.939  -6.973  28.835  1.00 74.61           C  
ANISOU  756  CG1 VAL A 129    12937   7384   8029  -2961    333  -1175       C  
ATOM    757  CG2 VAL A 129      -0.350  -6.455  30.692  1.00 72.95           C  
ANISOU  757  CG2 VAL A 129    12641   6988   8087  -2291    520   -874       C  
ATOM    758  N   ASP A 130      -1.106  -3.711  27.073  1.00 74.99           N  
ANISOU  758  N   ASP A 130    12467   8243   7785  -2540     31  -1007       N  
ATOM    759  CA  ASP A 130      -1.622  -3.173  25.818  1.00 76.20           C  
ANISOU  759  CA  ASP A 130    12566   8689   7696  -2706   -149  -1056       C  
ATOM    760  C   ASP A 130      -0.555  -3.188  24.732  1.00 76.36           C  
ANISOU  760  C   ASP A 130    12832   8656   7526  -2601    -33  -1189       C  
ATOM    761  O   ASP A 130      -0.837  -3.537  23.579  1.00 77.11           O  
ANISOU  761  O   ASP A 130    13108   8829   7363  -2825    -98  -1358       O  
ATOM    762  CB  ASP A 130      -2.149  -1.756  26.031  1.00 77.40           C  
ANISOU  762  CB  ASP A 130    12354   9170   7885  -2589   -323   -822       C  
ATOM    763  CG  ASP A 130      -2.736  -1.160  24.773  1.00 78.79           C  
ANISOU  763  CG  ASP A 130    12465   9666   7804  -2727   -535   -822       C  
ATOM    764  OD1 ASP A 130      -3.844  -1.579  24.374  1.00 79.69           O  
ANISOU  764  OD1 ASP A 130    12519   9941   7818  -3032   -715   -889       O  
ATOM    765  OD2 ASP A 130      -2.087  -0.272  24.182  1.00 79.00           O  
ANISOU  765  OD2 ASP A 130    12500   9794   7724  -2541   -527   -746       O  
ATOM    766  N   ARG A 131       0.679  -2.817  25.080  1.00 76.70           N  
ANISOU  766  N   ARG A 131    12877   8585   7680  -2275    142  -1121       N  
ATOM    767  CA  ARG A 131       1.753  -2.825  24.093  1.00 77.18           C  
ANISOU  767  CA  ARG A 131    13137   8605   7581  -2160    301  -1238       C  
ATOM    768  C   ARG A 131       2.174  -4.241  23.725  1.00 77.25           C  
ANISOU  768  C   ARG A 131    13518   8298   7534  -2229    499  -1494       C  
ATOM    769  O   ARG A 131       2.708  -4.459  22.632  1.00 77.95           O  
ANISOU  769  O   ARG A 131    13837   8374   7407  -2242    617  -1659       O  
ATOM    770  CB  ARG A 131       2.953  -2.029  24.607  1.00 73.30           C  
ANISOU  770  CB  ARG A 131    12492   8106   7255  -1817    435  -1092       C  
ATOM    771  CG  ARG A 131       2.701  -0.534  24.767  1.00 73.48           C  
ANISOU  771  CG  ARG A 131    12221   8398   7301  -1744    282   -867       C  
ATOM    772  CD  ARG A 131       2.451   0.140  23.427  1.00 74.47           C  
ANISOU  772  CD  ARG A 131    12391   8763   7139  -1854    193   -863       C  
ATOM    773  NE  ARG A 131       1.040   0.131  23.050  1.00 74.91           N  
ANISOU  773  NE  ARG A 131    12402   9011   7049  -2106    -60   -854       N  
ATOM    774  CZ  ARG A 131       0.594   0.390  21.825  1.00 75.74           C  
ANISOU  774  CZ  ARG A 131    12595   9333   6849  -2260   -189   -882       C  
ATOM    775  NH1 ARG A 131       1.449   0.673  20.852  1.00 76.04           N  
ANISOU  775  NH1 ARG A 131    12808   9401   6681  -2192    -56   -921       N  
ATOM    776  NH2 ARG A 131      -0.706   0.362  21.571  1.00 76.38           N  
ANISOU  776  NH2 ARG A 131    12578   9623   6819  -2484   -452   -863       N  
ATOM    777  N   TYR A 132       1.951  -5.215  24.611  1.00 80.07           N  
ANISOU  777  N   TYR A 132    13970   8379   8073  -2266    561  -1529       N  
ATOM    778  CA  TYR A 132       2.268  -6.595  24.262  1.00 80.34           C  
ANISOU  778  CA  TYR A 132    14404   8058   8063  -2337    760  -1773       C  
ATOM    779  C   TYR A 132       1.290  -7.142  23.231  1.00 80.96           C  
ANISOU  779  C   TYR A 132    14702   8185   7872  -2762    642  -2000       C  
ATOM    780  O   TYR A 132       1.700  -7.677  22.195  1.00 81.61           O  
ANISOU  780  O   TYR A 132    15110   8161   7737  -2823    772  -2239       O  
ATOM    781  CB  TYR A 132       2.281  -7.487  25.502  1.00 81.59           C  
ANISOU  781  CB  TYR A 132    14641   7878   8483  -2261    865  -1720       C  
ATOM    782  CG  TYR A 132       2.476  -8.939  25.133  1.00 82.06           C  
ANISOU  782  CG  TYR A 132    15157   7519   8503  -2354   1074  -1970       C  
ATOM    783  CD1 TYR A 132       3.708  -9.402  24.695  1.00 82.70           C  
ANISOU  783  CD1 TYR A 132    15472   7374   8576  -2065   1342  -2092       C  
ATOM    784  CD2 TYR A 132       1.420  -9.839  25.193  1.00 82.07           C  
ANISOU  784  CD2 TYR A 132    15357   7345   8481  -2741   1020  -2092       C  
ATOM    785  CE1 TYR A 132       3.886 -10.724  24.336  1.00 83.24           C  
ANISOU  785  CE1 TYR A 132    15997   7021   8611  -2123   1562  -2333       C  
ATOM    786  CE2 TYR A 132       1.590 -11.164  24.839  1.00 82.57           C  
ANISOU  786  CE2 TYR A 132    15890   6976   8509  -2847   1228  -2338       C  
ATOM    787  CZ  TYR A 132       2.825 -11.600  24.413  1.00 83.11           C  
ANISOU  787  CZ  TYR A 132    16219   6793   8565  -2520   1502  -2459       C  
ATOM    788  OH  TYR A 132       3.004 -12.916  24.056  1.00 83.90           O  
ANISOU  788  OH  TYR A 132    16683   6527   8668  -2540   1709  -2633       O  
ATOM    789  N   PHE A 133      -0.011  -7.027  23.502  1.00 84.00           N  
ANISOU  789  N   PHE A 133    14909   8747   8262  -3068    397  -1939       N  
ATOM    790  CA  PHE A 133      -1.006  -7.490  22.543  1.00 84.83           C  
ANISOU  790  CA  PHE A 133    15162   8961   8108  -3513    229  -2149       C  
ATOM    791  C   PHE A 133      -0.963  -6.697  21.244  1.00 85.61           C  
ANISOU  791  C   PHE A 133    15248   9408   7872  -3548     93  -2190       C  
ATOM    792  O   PHE A 133      -1.414  -7.198  20.209  1.00 86.38           O  
ANISOU  792  O   PHE A 133    15587   9559   7674  -3869      5  -2427       O  
ATOM    793  CB  PHE A 133      -2.403  -7.421  23.162  1.00 88.86           C  
ANISOU  793  CB  PHE A 133    15383   9653   8725  -3812    -12  -2038       C  
ATOM    794  CG  PHE A 133      -2.655  -8.474  24.206  1.00 88.35           C  
ANISOU  794  CG  PHE A 133    15441   9220   8906  -3921    129  -2057       C  
ATOM    795  CD1 PHE A 133      -1.846  -9.595  24.286  1.00 88.03           C  
ANISOU  795  CD1 PHE A 133    15831   8697   8919  -3838    413  -2226       C  
ATOM    796  CD2 PHE A 133      -3.699  -8.342  25.109  1.00 88.40           C  
ANISOU  796  CD2 PHE A 133    15142   9355   9091  -4089      2  -1892       C  
ATOM    797  CE1 PHE A 133      -2.073 -10.566  25.242  1.00 87.70           C  
ANISOU  797  CE1 PHE A 133    15943   8287   9093  -3927    553  -2213       C  
ATOM    798  CE2 PHE A 133      -3.930  -9.311  26.069  1.00 88.03           C  
ANISOU  798  CE2 PHE A 133    15234   8961   9250  -4204    156  -1889       C  
ATOM    799  CZ  PHE A 133      -3.116 -10.424  26.134  1.00 87.65           C  
ANISOU  799  CZ  PHE A 133    15646   8413   9243  -4126    425  -2041       C  
ATOM    800  N   ALA A 134      -0.428  -5.476  21.273  1.00 84.69           N  
ANISOU  800  N   ALA A 134    14880   9519   7778  -3241     75  -1966       N  
ATOM    801  CA  ALA A 134      -0.264  -4.711  20.042  1.00 85.45           C  
ANISOU  801  CA  ALA A 134    15010   9910   7547  -3241    -11  -1972       C  
ATOM    802  C   ALA A 134       0.910  -5.237  19.222  1.00 85.66           C  
ANISOU  802  C   ALA A 134    15423   9727   7398  -3121    289  -2191       C  
ATOM    803  O   ALA A 134       0.788  -5.450  18.010  1.00 86.39           O  
ANISOU  803  O   ALA A 134    15781   9922   7123  -3318    258  -2385       O  
ATOM    804  CB  ALA A 134      -0.078  -3.230  20.366  1.00 81.29           C  
ANISOU  804  CB  ALA A 134    14120   9648   7120  -2969    -97  -1653       C  
ATOM    805  N   ILE A 135       2.057  -5.463  19.870  1.00 83.47           N  
ANISOU  805  N   ILE A 135    15178   9169   7370  -2789    584  -2166       N  
ATOM    806  CA  ILE A 135       3.269  -5.854  19.156  1.00 84.01           C  
ANISOU  806  CA  ILE A 135    15540   9064   7317  -2603    909  -2340       C  
ATOM    807  C   ILE A 135       3.236  -7.302  18.687  1.00 84.34           C  
ANISOU  807  C   ILE A 135    16048   8766   7232  -2785   1075  -2687       C  
ATOM    808  O   ILE A 135       4.108  -7.717  17.914  1.00 84.99           O  
ANISOU  808  O   ILE A 135    16431   8708   7153  -2666   1356  -2884       O  
ATOM    809  CB  ILE A 135       4.499  -5.591  20.053  1.00 85.39           C  
ANISOU  809  CB  ILE A 135    15526   9092   7827  -2173   1145  -2178       C  
ATOM    810  CG1 ILE A 135       5.787  -5.560  19.228  1.00 86.31           C  
ANISOU  810  CG1 ILE A 135    15798   9175   7820  -1944   1466  -2282       C  
ATOM    811  CG2 ILE A 135       4.602  -6.643  21.142  1.00 84.87           C  
ANISOU  811  CG2 ILE A 135    15538   8648   8062  -2081   1255  -2214       C  
ATOM    812  CD1 ILE A 135       6.960  -4.978  19.968  1.00 86.51           C  
ANISOU  812  CD1 ILE A 135    15528   9198   8144  -1560   1633  -2084       C  
ATOM    813  N   THR A 136       2.246  -8.083  19.118  1.00 84.36           N  
ANISOU  813  N   THR A 136    16130   8621   7301  -3082    930  -2777       N  
ATOM    814  CA  THR A 136       2.099  -9.458  18.659  1.00 84.87           C  
ANISOU  814  CA  THR A 136    16553   8382   7313  -3257   1060  -3039       C  
ATOM    815  C   THR A 136       1.041  -9.620  17.577  1.00 88.02           C  
ANISOU  815  C   THR A 136    16993   9042   7409  -3661    804  -3159       C  
ATOM    816  O   THR A 136       1.043 -10.641  16.879  1.00 92.37           O  
ANISOU  816  O   THR A 136    17827   9407   7860  -3778    919  -3373       O  
ATOM    817  CB  THR A 136       1.752 -10.385  19.831  1.00 83.91           C  
ANISOU  817  CB  THR A 136    16455   7904   7524  -3296   1106  -3008       C  
ATOM    818  OG1 THR A 136       0.527  -9.953  20.437  1.00 82.83           O  
ANISOU  818  OG1 THR A 136    16043   7985   7445  -3591    787  -2875       O  
ATOM    819  CG2 THR A 136       2.862 -10.377  20.867  1.00 82.69           C  
ANISOU  819  CG2 THR A 136    16291   7463   7664  -2860   1362  -2890       C  
ATOM    820  N   SER A 137       0.144  -8.653  17.426  1.00 87.58           N  
ANISOU  820  N   SER A 137    16660   9410   7206  -3863    456  -3024       N  
ATOM    821  CA  SER A 137      -0.857  -8.697  16.378  1.00 91.26           C  
ANISOU  821  CA  SER A 137    17115  10183   7376  -4213    175  -3109       C  
ATOM    822  C   SER A 137      -0.248  -8.268  15.047  1.00 93.24           C  
ANISOU  822  C   SER A 137    17536  10626   7266  -4111    240  -3175       C  
ATOM    823  O   SER A 137       0.770  -7.571  15.015  1.00 90.90           O  
ANISOU  823  O   SER A 137    17249  10343   6946  -3795    434  -3084       O  
ATOM    824  CB  SER A 137      -2.030  -7.789  16.738  1.00 92.47           C  
ANISOU  824  CB  SER A 137    16865  10744   7525  -4413   -227  -2901       C  
ATOM    825  OG  SER A 137      -1.640  -6.426  16.729  1.00 90.19           O  
ANISOU  825  OG  SER A 137    16397  10734   7139  -4184   -299  -2687       O  
ATOM    826  N   PRO A 138      -0.846  -8.680  13.925  1.00 97.06           N  
ANISOU  826  N   PRO A 138    18159  11263   7457  -4382     92  -3334       N  
ATOM    827  CA  PRO A 138      -0.378  -8.172  12.626  1.00 99.31           C  
ANISOU  827  CA  PRO A 138    18593  11779   7360  -4303    121  -3369       C  
ATOM    828  C   PRO A 138      -0.562  -6.675  12.472  1.00 96.59           C  
ANISOU  828  C   PRO A 138    17968  11873   6858  -4211   -115  -3085       C  
ATOM    829  O   PRO A 138       0.093  -6.070  11.613  1.00 97.36           O  
ANISOU  829  O   PRO A 138    18179  12121   6693  -4051    -11  -3043       O  
ATOM    830  CB  PRO A 138      -1.224  -8.956  11.616  1.00105.36           C  
ANISOU  830  CB  PRO A 138    19534  12635   7863  -4666    -63  -3591       C  
ATOM    831  CG  PRO A 138      -2.440  -9.340  12.368  1.00105.42           C  
ANISOU  831  CG  PRO A 138    19308  12668   8079  -4971   -334  -3566       C  
ATOM    832  CD  PRO A 138      -1.991  -9.594  13.777  1.00101.11           C  
ANISOU  832  CD  PRO A 138    18693  11764   7959  -4784   -112  -3485       C  
ATOM    833  N   PHE A 139      -1.441  -6.059  13.268  1.00 96.85           N  
ANISOU  833  N   PHE A 139    17644  12112   7043  -4301   -416  -2877       N  
ATOM    834  CA  PHE A 139      -1.471  -4.605  13.423  1.00 93.68           C  
ANISOU  834  CA  PHE A 139    16971  12043   6579  -4134   -584  -2567       C  
ATOM    835  C   PHE A 139      -0.382  -4.207  14.418  1.00 90.37           C  
ANISOU  835  C   PHE A 139    16534  11378   6422  -3809   -283  -2466       C  
ATOM    836  O   PHE A 139      -0.637  -3.848  15.569  1.00 89.73           O  
ANISOU  836  O   PHE A 139    16153  11269   6672  -3720   -354  -2283       O  
ATOM    837  CB  PHE A 139      -2.840  -4.127  13.887  1.00 94.74           C  
ANISOU  837  CB  PHE A 139    16716  12497   6784  -4333  -1012  -2385       C  
ATOM    838  CG  PHE A 139      -3.913  -4.249  12.849  1.00 99.59           C  
ANISOU  838  CG  PHE A 139    17272  13453   7114  -4611  -1355  -2428       C  
ATOM    839  CD1 PHE A 139      -4.009  -3.321  11.826  1.00101.34           C  
ANISOU  839  CD1 PHE A 139    17471  14044   6990  -4529  -1538  -2267       C  
ATOM    840  CD2 PHE A 139      -4.840  -5.275  12.907  1.00102.76           C  
ANISOU  840  CD2 PHE A 139    17639  13810   7595  -4951  -1495  -2614       C  
ATOM    841  CE1 PHE A 139      -4.999  -3.423  10.869  1.00106.22           C  
ANISOU  841  CE1 PHE A 139    18029  14995   7336  -4763  -1875  -2302       C  
ATOM    842  CE2 PHE A 139      -5.833  -5.382  11.953  1.00107.69           C  
ANISOU  842  CE2 PHE A 139    18190  14773   7956  -5214  -1826  -2664       C  
ATOM    843  CZ  PHE A 139      -5.913  -4.454  10.932  1.00109.47           C  
ANISOU  843  CZ  PHE A 139    18387  15379   7827  -5110  -2028  -2510       C  
ATOM    844  N   LYS A 140       0.861  -4.294  13.952  1.00 87.96           N  
ANISOU  844  N   LYS A 140    16477  10901   6042  -3578     79  -2553       N  
ATOM    845  CA  LYS A 140       1.994  -4.019  14.821  1.00 87.25           C  
ANISOU  845  CA  LYS A 140    16320  10581   6253  -3233    394  -2458       C  
ATOM    846  C   LYS A 140       2.002  -2.552  15.238  1.00 87.03           C  
ANISOU  846  C   LYS A 140    15877  10812   6377  -3015    260  -2065       C  
ATOM    847  O   LYS A 140       1.750  -1.656  14.428  1.00 87.56           O  
ANISOU  847  O   LYS A 140    15922  11197   6150  -3049    103  -1918       O  
ATOM    848  CB  LYS A 140       3.308  -4.382  14.128  1.00 84.10           C  
ANISOU  848  CB  LYS A 140    16237   9997   5720  -3039    817  -2634       C  
ATOM    849  CG  LYS A 140       4.520  -4.282  15.042  1.00 80.94           C  
ANISOU  849  CG  LYS A 140    15674   9356   5725  -2649   1146  -2528       C  
ATOM    850  CD  LYS A 140       5.826  -4.539  14.306  1.00 83.24           C  
ANISOU  850  CD  LYS A 140    16224   9526   5878  -2443   1580  -2686       C  
ATOM    851  CE  LYS A 140       6.055  -6.006  14.025  1.00 86.93           C  
ANISOU  851  CE  LYS A 140    17010   9650   6368  -2459   1796  -2996       C  
ATOM    852  NZ  LYS A 140       7.409  -6.211  13.443  1.00 89.11           N  
ANISOU  852  NZ  LYS A 140    17416   9817   6622  -2171   2239  -3090       N  
ATOM    853  N   TYR A 141       2.271  -2.326  16.525  1.00 81.33           N  
ANISOU  853  N   TYR A 141    14857   9940   6107  -2796    320  -1894       N  
ATOM    854  CA  TYR A 141       2.395  -1.027  17.183  1.00 81.02           C  
ANISOU  854  CA  TYR A 141    14442  10046   6295  -2569    248  -1554       C  
ATOM    855  C   TYR A 141       1.059  -0.322  17.380  1.00 81.15           C  
ANISOU  855  C   TYR A 141    14185  10345   6303  -2701   -142  -1350       C  
ATOM    856  O   TYR A 141       1.046   0.856  17.756  1.00 81.03           O  
ANISOU  856  O   TYR A 141    13905  10464   6419  -2523   -217  -1069       O  
ATOM    857  CB  TYR A 141       3.331  -0.067  16.437  1.00 79.42           C  
ANISOU  857  CB  TYR A 141    14278   9970   5928  -2393    421  -1427       C  
ATOM    858  CG  TYR A 141       4.703  -0.615  16.127  1.00 79.69           C  
ANISOU  858  CG  TYR A 141    14528   9790   5960  -2235    834  -1604       C  
ATOM    859  CD1 TYR A 141       5.615  -0.893  17.137  1.00 79.41           C  
ANISOU  859  CD1 TYR A 141    14346   9508   6317  -1992   1063  -1599       C  
ATOM    860  CD2 TYR A 141       5.109  -0.786  14.812  1.00 80.43           C  
ANISOU  860  CD2 TYR A 141    14953   9960   5647  -2308    999  -1758       C  
ATOM    861  CE1 TYR A 141       6.879  -1.379  16.840  1.00 80.00           C  
ANISOU  861  CE1 TYR A 141    14567   9420   6411  -1813   1443  -1744       C  
ATOM    862  CE2 TYR A 141       6.366  -1.257  14.507  1.00 80.90           C  
ANISOU  862  CE2 TYR A 141    15184   9843   5712  -2138   1412  -1916       C  
ATOM    863  CZ  TYR A 141       7.246  -1.557  15.521  1.00 80.75           C  
ANISOU  863  CZ  TYR A 141    14978   9584   6119  -1882   1633  -1905       C  
ATOM    864  OH  TYR A 141       8.496  -2.033  15.202  1.00 81.52           O  
ANISOU  864  OH  TYR A 141    15201   9533   6240  -1683   2048  -2052       O  
ATOM    865  N   GLN A 142      -0.065  -0.994  17.145  1.00 84.17           N  
ANISOU  865  N   GLN A 142    14614  10822   6546  -3007   -386  -1483       N  
ATOM    866  CA  GLN A 142      -1.378  -0.375  17.275  1.00 84.71           C  
ANISOU  866  CA  GLN A 142    14377  11202   6607  -3127   -760  -1291       C  
ATOM    867  C   GLN A 142      -2.208  -1.152  18.288  1.00 84.45           C  
ANISOU  867  C   GLN A 142    14177  11057   6853  -3294   -853  -1359       C  
ATOM    868  O   GLN A 142      -2.320  -2.379  18.195  1.00 84.33           O  
ANISOU  868  O   GLN A 142    14400  10850   6793  -3537   -791  -1635       O  
ATOM    869  CB  GLN A 142      -2.096  -0.310  15.925  1.00 89.01           C  
ANISOU  869  CB  GLN A 142    15063  12080   6676  -3379  -1029  -1349       C  
ATOM    870  CG  GLN A 142      -3.394   0.478  15.959  1.00 89.88           C  
ANISOU  870  CG  GLN A 142    14810  12571   6771  -3437  -1430  -1101       C  
ATOM    871  CD  GLN A 142      -4.030   0.613  14.590  1.00 91.12           C  
ANISOU  871  CD  GLN A 142    15098  13100   6425  -3653  -1728  -1124       C  
ATOM    872  OE1 GLN A 142      -3.521   0.082  13.603  1.00 91.30           O  
ANISOU  872  OE1 GLN A 142    15521  13087   6082  -3790  -1626  -1353       O  
ATOM    873  NE2 GLN A 142      -5.147   1.329  14.524  1.00 92.14           N  
ANISOU  873  NE2 GLN A 142    14891  13599   6521  -3668  -2097   -885       N  
ATOM    874  N   SER A 143      -2.786  -0.433  19.249  1.00 84.87           N  
ANISOU  874  N   SER A 143    13846  11213   7189  -3169   -976  -1110       N  
ATOM    875  CA  SER A 143      -3.521  -1.069  20.333  1.00 84.67           C  
ANISOU  875  CA  SER A 143    13638  11082   7450  -3298  -1015  -1134       C  
ATOM    876  C   SER A 143      -4.766  -1.776  19.815  1.00 85.64           C  
ANISOU  876  C   SER A 143    13739  11402   7398  -3718  -1282  -1281       C  
ATOM    877  O   SER A 143      -5.506  -1.244  18.983  1.00 86.77           O  
ANISOU  877  O   SER A 143    13758  11919   7293  -3830  -1571  -1206       O  
ATOM    878  CB  SER A 143      -3.917  -0.036  21.385  1.00 83.74           C  
ANISOU  878  CB  SER A 143    13118  11072   7625  -3064  -1080   -836       C  
ATOM    879  OG  SER A 143      -4.678  -0.635  22.420  1.00 83.72           O  
ANISOU  879  OG  SER A 143    12938  10997   7874  -3198  -1098   -848       O  
ATOM    880  N   LEU A 144      -4.997  -2.989  20.323  1.00 87.52           N  
ANISOU  880  N   LEU A 144    14097  11387   7767  -3959  -1190  -1484       N  
ATOM    881  CA  LEU A 144      -6.189  -3.741  19.956  1.00 88.45           C  
ANISOU  881  CA  LEU A 144    14178  11664   7766  -4419  -1428  -1645       C  
ATOM    882  C   LEU A 144      -7.452  -3.145  20.559  1.00 89.46           C  
ANISOU  882  C   LEU A 144    13786  12131   8075  -4477  -1681  -1413       C  
ATOM    883  O   LEU A 144      -8.546  -3.377  20.034  1.00 90.69           O  
ANISOU  883  O   LEU A 144    13781  12592   8083  -4829  -1972  -1476       O  
ATOM    884  CB  LEU A 144      -6.045  -5.197  20.396  1.00 90.50           C  
ANISOU  884  CB  LEU A 144    14742  11497   8145  -4664  -1215  -1912       C  
ATOM    885  CG  LEU A 144      -4.925  -5.998  19.732  1.00 89.91           C  
ANISOU  885  CG  LEU A 144    15209  11065   7888  -4641   -952  -2191       C  
ATOM    886  CD1 LEU A 144      -4.817  -7.377  20.362  1.00 89.31           C  
ANISOU  886  CD1 LEU A 144    15421  10515   8000  -4819   -721  -2400       C  
ATOM    887  CD2 LEU A 144      -5.151  -6.103  18.232  1.00 90.97           C  
ANISOU  887  CD2 LEU A 144    15561  11431   7572  -4891  -1131  -2390       C  
ATOM    888  N   LEU A 145      -7.324  -2.388  21.644  1.00 87.50           N  
ANISOU  888  N   LEU A 145    13264  11847   8135  -4144  -1575  -1157       N  
ATOM    889  CA  LEU A 145      -8.475  -1.787  22.299  1.00 88.67           C  
ANISOU  889  CA  LEU A 145    12918  12294   8479  -4141  -1755   -934       C  
ATOM    890  C   LEU A 145      -8.956  -0.574  21.514  1.00 89.99           C  
ANISOU  890  C   LEU A 145    12828  12902   8464  -3992  -2041   -723       C  
ATOM    891  O   LEU A 145      -8.152   0.206  20.996  1.00 89.63           O  
ANISOU  891  O   LEU A 145    12934  12847   8274  -3713  -1998   -630       O  
ATOM    892  CB  LEU A 145      -8.112  -1.367  23.725  1.00 87.00           C  
ANISOU  892  CB  LEU A 145    12562  11872   8623  -3816  -1518   -752       C  
ATOM    893  CG  LEU A 145      -7.670  -2.445  24.719  1.00 85.63           C  
ANISOU  893  CG  LEU A 145    12603  11272   8659  -3888  -1237   -879       C  
ATOM    894  CD1 LEU A 145      -7.211  -1.813  26.029  1.00 84.98           C  
ANISOU  894  CD1 LEU A 145    12390  11045   8853  -3519  -1043   -676       C  
ATOM    895  CD2 LEU A 145      -8.777  -3.452  24.969  1.00 86.27           C  
ANISOU  895  CD2 LEU A 145    12585  11382   8811  -4330  -1303   -994       C  
ATOM    896  N   THR A 146     -10.273  -0.418  21.423  1.00 88.61           N  
ANISOU  896  N   THR A 146    12254  13116   8298  -4176  -2328   -632       N  
ATOM    897  CA  THR A 146     -10.807   0.832  20.911  1.00 89.95           C  
ANISOU  897  CA  THR A 146    12116  13696   8366  -3945  -2591   -360       C  
ATOM    898  C   THR A 146     -10.829   1.879  22.022  1.00 90.30           C  
ANISOU  898  C   THR A 146    11867  13700   8745  -3523  -2448    -75       C  
ATOM    899  O   THR A 146     -10.618   1.583  23.201  1.00 89.75           O  
ANISOU  899  O   THR A 146    11778  13358   8967  -3466  -2193    -94       O  
ATOM    900  CB  THR A 146     -12.203   0.636  20.321  1.00 92.67           C  
ANISOU  900  CB  THR A 146    12106  14521   8582  -4274  -2982   -358       C  
ATOM    901  OG1 THR A 146     -12.659   1.873  19.757  1.00 93.93           O  
ANISOU  901  OG1 THR A 146    11992  15075   8622  -3990  -3246    -64       O  
ATOM    902  CG2 THR A 146     -13.183   0.181  21.381  1.00 93.35           C  
ANISOU  902  CG2 THR A 146    11792  14666   9010  -4458  -2953   -345       C  
ATOM    903  N   LYS A 147     -11.084   3.128  21.629  1.00 89.74           N  
ANISOU  903  N   LYS A 147    11595  13891   8610  -3218  -2612    194       N  
ATOM    904  CA  LYS A 147     -11.030   4.223  22.592  1.00 90.16           C  
ANISOU  904  CA  LYS A 147    11437  13868   8951  -2795  -2461    449       C  
ATOM    905  C   LYS A 147     -12.153   4.115  23.616  1.00 91.52           C  
ANISOU  905  C   LYS A 147    11156  14190   9430  -2835  -2464    524       C  
ATOM    906  O   LYS A 147     -11.925   4.307  24.816  1.00 91.46           O  
ANISOU  906  O   LYS A 147    11103  13947   9700  -2649  -2202    570       O  
ATOM    907  CB  LYS A 147     -11.085   5.561  21.860  1.00 91.74           C  
ANISOU  907  CB  LYS A 147    11570  14282   9005  -2465  -2629    725       C  
ATOM    908  CG  LYS A 147      -9.880   5.809  20.968  1.00 90.40           C  
ANISOU  908  CG  LYS A 147    11855  13936   8556  -2389  -2552    687       C  
ATOM    909  CD  LYS A 147      -9.985   7.137  20.244  1.00 91.11           C  
ANISOU  909  CD  LYS A 147    11904  14219   8493  -2075  -2708    992       C  
ATOM    910  CE  LYS A 147      -8.763   7.376  19.379  1.00 89.84           C  
ANISOU  910  CE  LYS A 147    12200  13879   8055  -2027  -2586    962       C  
ATOM    911  NZ  LYS A 147      -8.678   6.396  18.260  1.00 89.70           N  
ANISOU  911  NZ  LYS A 147    12436  13994   7651  -2384  -2726    728       N  
ATOM    912  N   ASN A 148     -13.370   3.801  23.165  1.00 91.75           N  
ANISOU  912  N   ASN A 148    10835  14626   9399  -3090  -2755    533       N  
ATOM    913  CA  ASN A 148     -14.479   3.631  24.098  1.00 93.05           C  
ANISOU  913  CA  ASN A 148    10527  14968   9860  -3167  -2736    598       C  
ATOM    914  C   ASN A 148     -14.218   2.488  25.070  1.00 92.05           C  
ANISOU  914  C   ASN A 148    10562  14500   9912  -3439  -2450    382       C  
ATOM    915  O   ASN A 148     -14.609   2.565  26.240  1.00 92.65           O  
ANISOU  915  O   ASN A 148    10405  14521  10275  -3344  -2250    464       O  
ATOM    916  CB  ASN A 148     -15.777   3.393  23.327  1.00 94.17           C  
ANISOU  916  CB  ASN A 148    10250  15642   9889  -3455  -3126    622       C  
ATOM    917  CG  ASN A 148     -16.217   4.613  22.541  1.00 95.36           C  
ANISOU  917  CG  ASN A 148    10155  16172   9905  -3112  -3419    910       C  
ATOM    918  OD1 ASN A 148     -16.128   5.743  23.023  1.00 95.84           O  
ANISOU  918  OD1 ASN A 148    10106  16177  10132  -2633  -3298   1159       O  
ATOM    919  ND2 ASN A 148     -16.696   4.390  21.323  1.00 95.90           N  
ANISOU  919  ND2 ASN A 148    10161  16618   9657  -3357  -3809    878       N  
ATOM    920  N   LYS A 149     -13.550   1.430  24.607  1.00 92.68           N  
ANISOU  920  N   LYS A 149    11066  14333   9815  -3757  -2408    114       N  
ATOM    921  CA  LYS A 149     -13.209   0.309  25.476  1.00 91.46           C  
ANISOU  921  CA  LYS A 149    11135  13800   9814  -3987  -2128    -74       C  
ATOM    922  C   LYS A 149     -12.035   0.651  26.384  1.00 90.15           C  
ANISOU  922  C   LYS A 149    11251  13215   9786  -3618  -1799    -25       C  
ATOM    923  O   LYS A 149     -11.997   0.219  27.541  1.00 89.68           O  
ANISOU  923  O   LYS A 149    11201  12928   9944  -3627  -1555    -31       O  
ATOM    924  CB  LYS A 149     -12.887  -0.921  24.630  1.00 91.16           C  
ANISOU  924  CB  LYS A 149    11484  13612   9542  -4420  -2186   -380       C  
ATOM    925  CG  LYS A 149     -12.732  -2.222  25.389  1.00 90.03           C  
ANISOU  925  CG  LYS A 149    11576  13088   9546  -4722  -1932   -575       C  
ATOM    926  CD  LYS A 149     -12.309  -3.323  24.427  1.00 89.14           C  
ANISOU  926  CD  LYS A 149    11912  12782   9175  -5092  -1975   -889       C  
ATOM    927  CE  LYS A 149     -13.437  -3.689  23.474  1.00 90.63           C  
ANISOU  927  CE  LYS A 149    11880  13377   9178  -5560  -2329  -1006       C  
ATOM    928  NZ  LYS A 149     -13.067  -4.810  22.565  1.00 90.35           N  
ANISOU  928  NZ  LYS A 149    12329  13127   8875  -5960  -2354  -1353       N  
ATOM    929  N   ALA A 150     -11.066   1.416  25.875  1.00 87.58           N  
ANISOU  929  N   ALA A 150    11156  12796   9323  -3312  -1791     29       N  
ATOM    930  CA  ALA A 150      -9.968   1.866  26.723  1.00 86.52           C  
ANISOU  930  CA  ALA A 150    11229  12321   9323  -2969  -1515     85       C  
ATOM    931  C   ALA A 150     -10.464   2.791  27.826  1.00 87.98           C  
ANISOU  931  C   ALA A 150    11090  12582   9758  -2678  -1424    303       C  
ATOM    932  O   ALA A 150      -9.912   2.786  28.932  1.00 87.32           O  
ANISOU  932  O   ALA A 150    11114  12229   9836  -2524  -1179    311       O  
ATOM    933  CB  ALA A 150      -8.898   2.562  25.883  1.00 85.84           C  
ANISOU  933  CB  ALA A 150    11409  12160   9045  -2740  -1528    106       C  
ATOM    934  N   ARG A 151     -11.500   3.589  27.550  1.00 87.52           N  
ANISOU  934  N   ARG A 151    10641  12893   9722  -2583  -1616    481       N  
ATOM    935  CA  ARG A 151     -12.105   4.397  28.604  1.00 89.19           C  
ANISOU  935  CA  ARG A 151    10531  13181  10177  -2311  -1501    669       C  
ATOM    936  C   ARG A 151     -12.747   3.510  29.663  1.00 89.32           C  
ANISOU  936  C   ARG A 151    10391  13164  10382  -2541  -1337    604       C  
ATOM    937  O   ARG A 151     -12.719   3.833  30.857  1.00 89.78           O  
ANISOU  937  O   ARG A 151    10402  13088  10621  -2341  -1103    677       O  
ATOM    938  CB  ARG A 151     -13.141   5.358  28.015  1.00 90.82           C  
ANISOU  938  CB  ARG A 151    10328  13803  10376  -2144  -1743    882       C  
ATOM    939  CG  ARG A 151     -12.579   6.421  27.078  1.00 90.55           C  
ANISOU  939  CG  ARG A 151    10449  13788  10167  -1858  -1876   1013       C  
ATOM    940  CD  ARG A 151     -13.680   7.368  26.612  1.00 92.23           C  
ANISOU  940  CD  ARG A 151    10244  14403  10396  -1641  -2109   1265       C  
ATOM    941  NE  ARG A 151     -13.204   8.360  25.650  1.00 91.74           N  
ANISOU  941  NE  ARG A 151    10358  14356  10142  -1380  -2244   1421       N  
ATOM    942  CZ  ARG A 151     -13.292   8.223  24.329  1.00 91.40           C  
ANISOU  942  CZ  ARG A 151    10378  14548   9802  -1526  -2536   1431       C  
ATOM    943  NH1 ARG A 151     -13.852   7.140  23.806  1.00 91.54           N  
ANISOU  943  NH1 ARG A 151    10289  14807   9684  -1946  -2740   1267       N  
ATOM    944  NH2 ARG A 151     -12.832   9.175  23.528  1.00 90.98           N  
ANISOU  944  NH2 ARG A 151    10515  14482   9571  -1270  -2619   1603       N  
ATOM    945  N   VAL A 152     -13.332   2.386  29.242  1.00 88.48           N  
ANISOU  945  N   VAL A 152    10228  13172  10221  -2981  -1449    463       N  
ATOM    946  CA  VAL A 152     -13.898   1.434  30.193  1.00 88.33           C  
ANISOU  946  CA  VAL A 152    10109  13081  10370  -3259  -1269    399       C  
ATOM    947  C   VAL A 152     -12.803   0.826  31.059  1.00 86.22           C  
ANISOU  947  C   VAL A 152    10286  12335  10137  -3223   -979    300       C  
ATOM    948  O   VAL A 152     -13.026   0.530  32.240  1.00 86.10           O  
ANISOU  948  O   VAL A 152    10230  12200  10284  -3231   -745    340       O  
ATOM    949  CB  VAL A 152     -14.701   0.354  29.442  1.00 87.00           C  
ANISOU  949  CB  VAL A 152     9825  13110  10121  -3790  -1465    248       C  
ATOM    950  CG1 VAL A 152     -15.194  -0.722  30.398  1.00 86.71           C  
ANISOU  950  CG1 VAL A 152     9754  12935  10256  -4129  -1245    176       C  
ATOM    951  CG2 VAL A 152     -15.872   0.986  28.707  1.00 89.05           C  
ANISOU  951  CG2 VAL A 152     9564  13911  10361  -3809  -1779    377       C  
ATOM    952  N   ILE A 153     -11.603   0.645  30.504  1.00 86.94           N  
ANISOU  952  N   ILE A 153    10798  12163  10072  -3163   -983    184       N  
ATOM    953  CA  ILE A 153     -10.502   0.106  31.293  1.00 84.69           C  
ANISOU  953  CA  ILE A 153    10903  11450   9823  -3078   -733    111       C  
ATOM    954  C   ILE A 153     -10.032   1.126  32.323  1.00 84.85           C  
ANISOU  954  C   ILE A 153    10894  11389   9957  -2662   -575    263       C  
ATOM    955  O   ILE A 153      -9.731   0.774  33.470  1.00 83.65           O  
ANISOU  955  O   ILE A 153    10869  11014   9899  -2608   -359    276       O  
ATOM    956  CB  ILE A 153      -9.352  -0.343  30.371  1.00 84.57           C  
ANISOU  956  CB  ILE A 153    11299  11211   9624  -3105   -768    -54       C  
ATOM    957  CG1 ILE A 153      -9.844  -1.395  29.374  1.00 84.61           C  
ANISOU  957  CG1 ILE A 153    11385  11273   9491  -3544   -911   -243       C  
ATOM    958  CG2 ILE A 153      -8.189  -0.885  31.190  1.00 82.12           C  
ANISOU  958  CG2 ILE A 153    11346  10486   9369  -2970   -525   -106       C  
ATOM    959  CD1 ILE A 153     -10.362  -2.664  30.019  1.00 84.17           C  
ANISOU  959  CD1 ILE A 153    11395  11041   9546  -3899   -775   -337       C  
ATOM    960  N   ILE A 154      -9.980   2.407  31.942  1.00 83.10           N  
ANISOU  960  N   ILE A 154    10527  11335   9711  -2371   -680    381       N  
ATOM    961  CA  ILE A 154      -9.485   3.439  32.853  1.00 83.54           C  
ANISOU  961  CA  ILE A 154    10599  11284   9859  -1998   -534    495       C  
ATOM    962  C   ILE A 154     -10.358   3.524  34.099  1.00 84.66           C  
ANISOU  962  C   ILE A 154    10505  11497  10166  -1959   -368    587       C  
ATOM    963  O   ILE A 154      -9.850   3.626  35.223  1.00 83.54           O  
ANISOU  963  O   ILE A 154    10514  11151  10077  -1805   -170    599       O  
ATOM    964  CB  ILE A 154      -9.399   4.799  32.136  1.00 83.57           C  
ANISOU  964  CB  ILE A 154    10502  11435   9814  -1723   -670    613       C  
ATOM    965  CG1 ILE A 154      -8.426   4.725  30.959  1.00 82.08           C  
ANISOU  965  CG1 ILE A 154    10586  11162   9441  -1759   -784    528       C  
ATOM    966  CG2 ILE A 154      -8.964   5.884  33.109  1.00 84.58           C  
ANISOU  966  CG2 ILE A 154    10663  11428  10047  -1374   -509    706       C  
ATOM    967  CD1 ILE A 154      -7.010   4.401  31.369  1.00 79.51           C  
ANISOU  967  CD1 ILE A 154    10610  10499   9101  -1693   -622    422       C  
ATOM    968  N   LEU A 155     -11.680   3.484  33.924  1.00 84.72           N  
ANISOU  968  N   LEU A 155    10130  11815  10245  -2100   -445    653       N  
ATOM    969  CA  LEU A 155     -12.574   3.571  35.074  1.00 85.92           C  
ANISOU  969  CA  LEU A 155    10022  12066  10558  -2064   -251    745       C  
ATOM    970  C   LEU A 155     -12.379   2.385  36.010  1.00 83.95           C  
ANISOU  970  C   LEU A 155     9990  11576  10329  -2298    -37    666       C  
ATOM    971  O   LEU A 155     -12.255   2.557  37.228  1.00 83.72           O  
ANISOU  971  O   LEU A 155    10035  11422  10354  -2142    196    717       O  
ATOM    972  CB  LEU A 155     -14.027   3.665  34.609  1.00 84.74           C  
ANISOU  972  CB  LEU A 155     9366  12336  10494  -2198   -384    831       C  
ATOM    973  CG  LEU A 155     -14.390   4.942  33.849  1.00 86.70           C  
ANISOU  973  CG  LEU A 155     9353  12847  10740  -1892   -578    971       C  
ATOM    974  CD1 LEU A 155     -15.827   4.884  33.354  1.00 88.21           C  
ANISOU  974  CD1 LEU A 155     9006  13496  11014  -2045   -748   1060       C  
ATOM    975  CD2 LEU A 155     -14.161   6.174  34.715  1.00 87.88           C  
ANISOU  975  CD2 LEU A 155     9523  12887  10982  -1435   -384   1084       C  
ATOM    976  N   MET A 156     -12.333   1.170  35.456  1.00 84.86           N  
ANISOU  976  N   MET A 156    10251  11606  10386  -2670   -106    542       N  
ATOM    977  CA  MET A 156     -12.138  -0.013  36.290  1.00 83.14           C  
ANISOU  977  CA  MET A 156    10287  11114  10189  -2892    103    487       C  
ATOM    978  C   MET A 156     -10.825   0.057  37.059  1.00 80.84           C  
ANISOU  978  C   MET A 156    10399  10476   9841  -2621    245    482       C  
ATOM    979  O   MET A 156     -10.754  -0.378  38.213  1.00 80.13           O  
ANISOU  979  O   MET A 156    10447  10219   9778  -2616    464    530       O  
ATOM    980  CB  MET A 156     -12.183  -1.282  35.442  1.00 87.98           C  
ANISOU  980  CB  MET A 156    11060  11628  10740  -3318      2    331       C  
ATOM    981  CG  MET A 156     -13.543  -1.611  34.869  1.00 89.92           C  
ANISOU  981  CG  MET A 156    10912  12212  11043  -3692   -129    316       C  
ATOM    982  SD  MET A 156     -13.487  -3.138  33.913  1.00 88.72           S  
ANISOU  982  SD  MET A 156    11046  11874  10789  -4231   -233     83       S  
ATOM    983  CE  MET A 156     -13.285  -4.339  35.228  1.00 87.43           C  
ANISOU  983  CE  MET A 156    11218  11279  10720  -4404    125     91       C  
ATOM    984  N   VAL A 157      -9.773   0.592  36.436  1.00 81.01           N  
ANISOU  984  N   VAL A 157    10604  10405   9773  -2403    122    433       N  
ATOM    985  CA  VAL A 157      -8.505   0.748  37.144  1.00 78.66           C  
ANISOU  985  CA  VAL A 157    10623   9832   9432  -2145    226    431       C  
ATOM    986  C   VAL A 157      -8.686   1.656  38.354  1.00 79.57           C  
ANISOU  986  C   VAL A 157    10636  10001   9597  -1885    370    545       C  
ATOM    987  O   VAL A 157      -8.257   1.331  39.465  1.00 78.21           O  
ANISOU  987  O   VAL A 157    10665   9649   9401  -1815    530    572       O  
ATOM    988  CB  VAL A 157      -7.412   1.275  36.197  1.00 78.94           C  
ANISOU  988  CB  VAL A 157    10803   9809   9380  -1978     78    364       C  
ATOM    989  CG1 VAL A 157      -6.153   1.603  36.980  1.00 76.51           C  
ANISOU  989  CG1 VAL A 157    10733   9286   9053  -1708    167    373       C  
ATOM    990  CG2 VAL A 157      -7.102   0.244  35.126  1.00 77.90           C  
ANISOU  990  CG2 VAL A 157    10856   9573   9169  -2222     -9    225       C  
ATOM    991  N   TRP A 158      -9.347   2.800  38.160  1.00 77.59           N  
ANISOU  991  N   TRP A 158    10087   9994   9398  -1727    319    617       N  
ATOM    992  CA  TRP A 158      -9.597   3.704  39.279  1.00 78.91           C  
ANISOU  992  CA  TRP A 158    10173  10200   9608  -1474    482    701       C  
ATOM    993  C   TRP A 158     -10.637   3.141  40.242  1.00 80.14           C  
ANISOU  993  C   TRP A 158    10181  10442   9826  -1619    694    764       C  
ATOM    994  O   TRP A 158     -10.566   3.408  41.447  1.00 80.26           O  
ANISOU  994  O   TRP A 158    10294  10386   9816  -1469    893    803       O  
ATOM    995  CB  TRP A 158     -10.026   5.074  38.757  1.00 78.88           C  
ANISOU  995  CB  TRP A 158     9917  10395   9659  -1236    392    766       C  
ATOM    996  CG  TRP A 158      -8.904   5.849  38.126  1.00 77.84           C  
ANISOU  996  CG  TRP A 158     9979  10137   9461  -1049    259    729       C  
ATOM    997  CD1 TRP A 158      -8.550   5.852  36.809  1.00 77.74           C  
ANISOU  997  CD1 TRP A 158     9986  10159   9392  -1115     57    701       C  
ATOM    998  CD2 TRP A 158      -8.008   6.755  38.783  1.00 76.75           C  
ANISOU  998  CD2 TRP A 158    10041   9825   9294   -793    332    713       C  
ATOM    999  NE1 TRP A 158      -7.481   6.690  36.606  1.00 76.44           N  
ANISOU  999  NE1 TRP A 158    10011   9850   9182   -916     23    684       N  
ATOM   1000  CE2 TRP A 158      -7.130   7.258  37.802  1.00 75.57           C  
ANISOU 1000  CE2 TRP A 158    10005   9609   9099   -729    179    685       C  
ATOM   1001  CE3 TRP A 158      -7.859   7.185  40.106  1.00 76.62           C  
ANISOU 1001  CE3 TRP A 158    10133   9709   9270   -633    514    710       C  
ATOM   1002  CZ2 TRP A 158      -6.118   8.169  38.101  1.00 73.81           C  
ANISOU 1002  CZ2 TRP A 158     9971   9220   8852   -538    201    656       C  
ATOM   1003  CZ3 TRP A 158      -6.854   8.089  40.401  1.00 75.04           C  
ANISOU 1003  CZ3 TRP A 158    10138   9348   9026   -442    510    663       C  
ATOM   1004  CH2 TRP A 158      -5.997   8.571  39.403  1.00 73.66           C  
ANISOU 1004  CH2 TRP A 158    10045   9107   8836   -407    355    637       C  
ATOM   1005  N   ILE A 159     -11.608   2.374  39.738  1.00 80.83           N  
ANISOU 1005  N   ILE A 159    10038  10692   9982  -1931    661    770       N  
ATOM   1006  CA  ILE A 159     -12.569   1.711  40.619  1.00 81.79           C  
ANISOU 1006  CA  ILE A 159    10021  10885  10172  -2133    888    832       C  
ATOM   1007  C   ILE A 159     -11.860   0.693  41.505  1.00 79.47           C  
ANISOU 1007  C   ILE A 159    10142  10266   9788  -2237   1052    817       C  
ATOM   1008  O   ILE A 159     -11.974   0.727  42.736  1.00 79.77           O  
ANISOU 1008  O   ILE A 159    10263  10252   9793  -2146   1290    890       O  
ATOM   1009  CB  ILE A 159     -13.696   1.054  39.803  1.00 79.19           C  
ANISOU 1009  CB  ILE A 159     9349  10799   9939  -2506    789    823       C  
ATOM   1010  CG1 ILE A 159     -14.592   2.114  39.159  1.00 81.72           C  
ANISOU 1010  CG1 ILE A 159     9189  11504  10357  -2354    650    893       C  
ATOM   1011  CG2 ILE A 159     -14.513   0.115  40.679  1.00 79.69           C  
ANISOU 1011  CG2 ILE A 159     9340  10868  10071  -2806   1045    873       C  
ATOM   1012  CD1 ILE A 159     -15.554   1.553  38.132  1.00 82.65           C  
ANISOU 1012  CD1 ILE A 159     8958  11909  10537  -2717    451    870       C  
ATOM   1013  N   VAL A 160     -11.123  -0.235  40.887  1.00 82.04           N  
ANISOU 1013  N   VAL A 160    10748  10365  10057  -2411    936    728       N  
ATOM   1014  CA  VAL A 160     -10.403  -1.246  41.659  1.00 79.81           C  
ANISOU 1014  CA  VAL A 160    10877   9751   9697  -2470   1077    737       C  
ATOM   1015  C   VAL A 160      -9.376  -0.591  42.574  1.00 78.41           C  
ANISOU 1015  C   VAL A 160    10938   9444   9411  -2102   1126    774       C  
ATOM   1016  O   VAL A 160      -9.209  -0.993  43.732  1.00 77.76           O  
ANISOU 1016  O   VAL A 160    11072   9223   9252  -2065   1309    854       O  
ATOM   1017  CB  VAL A 160      -9.751  -2.280  40.721  1.00 78.35           C  
ANISOU 1017  CB  VAL A 160    10953   9331   9484  -2667    947    621       C  
ATOM   1018  CG1 VAL A 160      -8.859  -3.225  41.510  1.00 76.30           C  
ANISOU 1018  CG1 VAL A 160    11138   8703   9151  -2630   1081    655       C  
ATOM   1019  CG2 VAL A 160     -10.821  -3.067  39.983  1.00 79.69           C  
ANISOU 1019  CG2 VAL A 160    10936   9607   9737  -3104    916    565       C  
ATOM   1020  N   SER A 161      -8.676   0.430  42.074  1.00 79.44           N  
ANISOU 1020  N   SER A 161    11041   9623   9520  -1843    959    720       N  
ATOM   1021  CA  SER A 161      -7.755   1.173  42.927  1.00 78.20           C  
ANISOU 1021  CA  SER A 161    11069   9378   9265  -1531    986    733       C  
ATOM   1022  C   SER A 161      -8.501   1.877  44.053  1.00 80.14           C  
ANISOU 1022  C   SER A 161    11195   9762   9493  -1410   1184    809       C  
ATOM   1023  O   SER A 161      -8.066   1.846  45.209  1.00 79.08           O  
ANISOU 1023  O   SER A 161    11292   9523   9233  -1293   1305    847       O  
ATOM   1024  CB  SER A 161      -6.961   2.181  42.100  1.00 77.57           C  
ANISOU 1024  CB  SER A 161    10956   9328   9188  -1331    788    658       C  
ATOM   1025  OG  SER A 161      -6.146   1.534  41.143  1.00 75.56           O  
ANISOU 1025  OG  SER A 161    10847   8939   8923  -1414    645    582       O  
ATOM   1026  N   GLY A 162      -9.631   2.512  43.733  1.00 80.21           N  
ANISOU 1026  N   GLY A 162    10842  10020   9615  -1422   1221    834       N  
ATOM   1027  CA  GLY A 162     -10.399   3.211  44.747  1.00 82.17           C  
ANISOU 1027  CA  GLY A 162    10955  10405   9861  -1279   1448    896       C  
ATOM   1028  C   GLY A 162     -10.957   2.299  45.819  1.00 82.10           C  
ANISOU 1028  C   GLY A 162    11030  10367   9798  -1453   1712    979       C  
ATOM   1029  O   GLY A 162     -11.202   2.741  46.944  1.00 82.52           O  
ANISOU 1029  O   GLY A 162    11137  10454   9764  -1306   1934   1019       O  
ATOM   1030  N   LEU A 163     -11.166   1.022  45.491  1.00 83.36           N  
ANISOU 1030  N   LEU A 163    11232  10447   9996  -1776   1711   1004       N  
ATOM   1031  CA  LEU A 163     -11.649   0.077  46.489  1.00 83.30           C  
ANISOU 1031  CA  LEU A 163    11351  10367   9934  -1972   1980   1105       C  
ATOM   1032  C   LEU A 163     -10.506  -0.470  47.334  1.00 80.65           C  
ANISOU 1032  C   LEU A 163    11509   9737   9398  -1873   2005   1139       C  
ATOM   1033  O   LEU A 163     -10.633  -0.576  48.558  1.00 80.71           O  
ANISOU 1033  O   LEU A 163    11688   9715   9263  -1822   2235   1233       O  
ATOM   1034  CB  LEU A 163     -12.415  -1.058  45.809  1.00 79.67           C  
ANISOU 1034  CB  LEU A 163    10742   9920   9608  -2395   1987   1116       C  
ATOM   1035  CG  LEU A 163     -13.726  -0.667  45.127  1.00 82.63           C  
ANISOU 1035  CG  LEU A 163    10572  10648  10174  -2544   1974   1112       C  
ATOM   1036  CD1 LEU A 163     -14.324  -1.864  44.409  1.00 82.69           C  
ANISOU 1036  CD1 LEU A 163    10483  10646  10290  -3017   1933   1088       C  
ATOM   1037  CD2 LEU A 163     -14.712  -0.087  46.132  1.00 84.98           C  
ANISOU 1037  CD2 LEU A 163    10609  11179  10502  -2445   2279   1212       C  
ATOM   1038  N   THR A 164      -9.381  -0.810  46.705  1.00 83.45           N  
ANISOU 1038  N   THR A 164    12089   9891   9727  -1826   1774   1073       N  
ATOM   1039  CA  THR A 164      -8.234  -1.307  47.454  1.00 81.32           C  
ANISOU 1039  CA  THR A 164    12245   9371   9282  -1688   1760   1121       C  
ATOM   1040  C   THR A 164      -7.513  -0.212  48.227  1.00 80.79           C  
ANISOU 1040  C   THR A 164    12278   9361   9059  -1356   1715   1096       C  
ATOM   1041  O   THR A 164      -6.662  -0.531  49.065  1.00 79.61           O  
ANISOU 1041  O   THR A 164    12453   9068   8729  -1229   1706   1154       O  
ATOM   1042  CB  THR A 164      -7.247  -1.999  46.514  1.00 78.10           C  
ANISOU 1042  CB  THR A 164    12010   8747   8918  -1714   1546   1054       C  
ATOM   1043  OG1 THR A 164      -6.759  -1.056  45.552  1.00 77.66           O  
ANISOU 1043  OG1 THR A 164    11778   8803   8928  -1568   1322    926       O  
ATOM   1044  CG2 THR A 164      -7.919  -3.157  45.793  1.00 78.59           C  
ANISOU 1044  CG2 THR A 164    12049   8706   9107  -2074   1598   1050       C  
ATOM   1045  N   SER A 165      -7.822   1.059  47.971  1.00 83.06           N  
ANISOU 1045  N   SER A 165    12310   9845   9404  -1214   1678   1013       N  
ATOM   1046  CA  SER A 165      -7.162   2.170  48.646  1.00 82.72           C  
ANISOU 1046  CA  SER A 165    12377   9830   9221   -936   1638    954       C  
ATOM   1047  C   SER A 165      -8.031   2.811  49.722  1.00 84.49           C  
ANISOU 1047  C   SER A 165    12556  10196   9352   -854   1906    983       C  
ATOM   1048  O   SER A 165      -7.566   3.013  50.847  1.00 84.02           O  
ANISOU 1048  O   SER A 165    12767  10094   9064   -724   1975    990       O  
ATOM   1049  CB  SER A 165      -6.733   3.232  47.626  1.00 82.18           C  
ANISOU 1049  CB  SER A 165    12135   9819   9271   -805   1424    832       C  
ATOM   1050  OG  SER A 165      -5.773   2.710  46.723  1.00 80.27           O  
ANISOU 1050  OG  SER A 165    11972   9449   9077   -848   1202    793       O  
ATOM   1051  N   PHE A 166      -9.285   3.141  49.405  1.00 85.55           N  
ANISOU 1051  N   PHE A 166    12345  10513   9646   -919   2059    999       N  
ATOM   1052  CA  PHE A 166     -10.120   3.815  50.395  1.00 87.23           C  
ANISOU 1052  CA  PHE A 166    12492  10867   9786   -803   2352   1016       C  
ATOM   1053  C   PHE A 166     -10.644   2.851  51.453  1.00 87.38           C  
ANISOU 1053  C   PHE A 166    12662  10873   9663   -964   2639   1147       C  
ATOM   1054  O   PHE A 166     -10.643   3.183  52.643  1.00 87.48           O  
ANISOU 1054  O   PHE A 166    12888  10897   9452   -835   2840   1157       O  
ATOM   1055  CB  PHE A 166     -11.294   4.538  49.729  1.00 86.16           C  
ANISOU 1055  CB  PHE A 166    11894  10956   9885   -769   2433   1007       C  
ATOM   1056  CG  PHE A 166     -10.905   5.782  48.980  1.00 86.55           C  
ANISOU 1056  CG  PHE A 166    11843  11015  10026   -534   2234    903       C  
ATOM   1057  CD1 PHE A 166      -9.593   6.217  48.958  1.00 84.69           C  
ANISOU 1057  CD1 PHE A 166    11904  10602   9673   -407   2023    806       C  
ATOM   1058  CD2 PHE A 166     -11.870   6.558  48.360  1.00 88.93           C  
ANISOU 1058  CD2 PHE A 166    11752  11509  10530   -430   2276    916       C  
ATOM   1059  CE1 PHE A 166      -9.239   7.372  48.287  1.00 85.20           C  
ANISOU 1059  CE1 PHE A 166    11901  10649   9824   -222   1871    720       C  
ATOM   1060  CE2 PHE A 166     -11.524   7.718  47.693  1.00 89.46           C  
ANISOU 1060  CE2 PHE A 166    11769  11550  10674   -202   2114    848       C  
ATOM   1061  CZ  PHE A 166     -10.207   8.125  47.658  1.00 87.64           C  
ANISOU 1061  CZ  PHE A 166    11865  11109  10324   -114   1924    747       C  
ATOM   1062  N   LEU A 167     -11.098   1.664  51.043  1.00 89.50           N  
ANISOU 1062  N   LEU A 167    12851  11110  10044  -1261   2673   1245       N  
ATOM   1063  CA  LEU A 167     -11.712   0.738  51.996  1.00 89.93           C  
ANISOU 1063  CA  LEU A 167    13036  11143   9990  -1455   2985   1392       C  
ATOM   1064  C   LEU A 167     -10.780   0.342  53.134  1.00 88.30           C  
ANISOU 1064  C   LEU A 167    13344  10746   9461  -1350   3014   1462       C  
ATOM   1065  O   LEU A 167     -11.198   0.445  54.300  1.00 89.03           O  
ANISOU 1065  O   LEU A 167    13576  10903   9350  -1307   3306   1535       O  
ATOM   1066  CB  LEU A 167     -12.245  -0.497  51.261  1.00 86.64           C  
ANISOU 1066  CB  LEU A 167    12488  10670   9763  -1832   2987   1466       C  
ATOM   1067  CG  LEU A 167     -13.461  -0.307  50.357  1.00 88.98           C  
ANISOU 1067  CG  LEU A 167    12240  11223  10345  -2016   3015   1437       C  
ATOM   1068  CD1 LEU A 167     -13.752  -1.585  49.588  1.00 88.92           C  
ANISOU 1068  CD1 LEU A 167    12188  11111  10485  -2427   2953   1467       C  
ATOM   1069  CD2 LEU A 167     -14.665   0.107  51.186  1.00 91.20           C  
ANISOU 1069  CD2 LEU A 167    12256  11757  10640  -2010   3393   1509       C  
ATOM   1070  N   PRO A 168      -9.541  -0.110  52.897  1.00 90.46           N  
ANISOU 1070  N   PRO A 168    13907  10807   9658  -1293   2735   1455       N  
ATOM   1071  CA  PRO A 168      -8.681  -0.453  54.041  1.00 89.45           C  
ANISOU 1071  CA  PRO A 168    14239  10543   9205  -1164   2739   1547       C  
ATOM   1072  C   PRO A 168      -8.391   0.728  54.948  1.00 89.77           C  
ANISOU 1072  C   PRO A 168    14393  10711   9004   -901   2764   1453       C  
ATOM   1073  O   PRO A 168      -8.151   0.535  56.145  1.00 89.77           O  
ANISOU 1073  O   PRO A 168    14735  10690   8685   -832   2881   1543       O  
ATOM   1074  CB  PRO A 168      -7.401  -0.972  53.376  1.00 86.12           C  
ANISOU 1074  CB  PRO A 168    13985   9917   8819  -1106   2395   1529       C  
ATOM   1075  CG  PRO A 168      -7.816  -1.391  52.019  1.00 86.09           C  
ANISOU 1075  CG  PRO A 168    13700   9880   9130  -1313   2319   1477       C  
ATOM   1076  CD  PRO A 168      -8.874  -0.413  51.619  1.00 87.74           C  
ANISOU 1076  CD  PRO A 168    13491  10345   9502  -1340   2421   1380       C  
ATOM   1077  N   ILE A 169      -8.403   1.951  54.418  1.00 89.47           N  
ANISOU 1077  N   ILE A 169    14111  10793   9091   -756   2660   1275       N  
ATOM   1078  CA  ILE A 169      -8.115   3.112  55.251  1.00 89.86           C  
ANISOU 1078  CA  ILE A 169    14305  10922   8917   -526   2691   1152       C  
ATOM   1079  C   ILE A 169      -9.378   3.608  55.942  1.00 91.67           C  
ANISOU 1079  C   ILE A 169    14413  11314   9104   -507   3095   1155       C  
ATOM   1080  O   ILE A 169      -9.344   3.989  57.115  1.00 92.02           O  
ANISOU 1080  O   ILE A 169    14730  11396   8839   -393   3268   1131       O  
ATOM   1081  CB  ILE A 169      -7.456   4.217  54.411  1.00 90.69           C  
ANISOU 1081  CB  ILE A 169    14265  11026   9168   -375   2412    962       C  
ATOM   1082  CG1 ILE A 169      -6.209   3.681  53.699  1.00 88.92           C  
ANISOU 1082  CG1 ILE A 169    14125  10662   8998   -397   2050    964       C  
ATOM   1083  CG2 ILE A 169      -7.082   5.391  55.300  1.00 91.14           C  
ANISOU 1083  CG2 ILE A 169    14528  11118   8984   -173   2438    811       C  
ATOM   1084  CD1 ILE A 169      -5.123   3.197  54.634  1.00 88.02           C  
ANISOU 1084  CD1 ILE A 169    14397  10467   8578   -328   1916   1021       C  
ATOM   1085  N   GLN A 170     -10.512   3.604  55.235  1.00 90.86           N  
ANISOU 1085  N   GLN A 170    13893  11332   9299   -615   3254   1182       N  
ATOM   1086  CA  GLN A 170     -11.761   4.055  55.839  1.00 92.76           C  
ANISOU 1086  CA  GLN A 170    13946  11757   9542   -579   3663   1196       C  
ATOM   1087  C   GLN A 170     -12.311   3.038  56.831  1.00 93.10           C  
ANISOU 1087  C   GLN A 170    14166  11814   9395   -765   3996   1377       C  
ATOM   1088  O   GLN A 170     -12.950   3.424  57.816  1.00 94.16           O  
ANISOU 1088  O   GLN A 170    14359  12066   9352   -682   4359   1382       O  
ATOM   1089  CB  GLN A 170     -12.793   4.352  54.750  1.00 91.84           C  
ANISOU 1089  CB  GLN A 170    13275  11806   9815   -629   3697   1189       C  
ATOM   1090  CG  GLN A 170     -12.449   5.540  53.863  1.00 92.02           C  
ANISOU 1090  CG  GLN A 170    13125  11832  10007   -404   3446   1035       C  
ATOM   1091  CD  GLN A 170     -12.518   6.861  54.606  1.00 92.66           C  
ANISOU 1091  CD  GLN A 170    13317  11937   9954    -95   3626    900       C  
ATOM   1092  OE1 GLN A 170     -13.400   7.070  55.439  1.00 93.85           O  
ANISOU 1092  OE1 GLN A 170    13418  12211  10027    -26   4011    922       O  
ATOM   1093  NE2 GLN A 170     -11.591   7.762  54.302  1.00 91.91           N  
ANISOU 1093  NE2 GLN A 170    13381  11711   9830     83   3369    750       N  
ATOM   1094  N   MET A 171     -12.081   1.747  56.597  1.00 94.48           N  
ANISOU 1094  N   MET A 171    14451  11852   9596  -1013   3909   1528       N  
ATOM   1095  CA  MET A 171     -12.551   0.704  57.502  1.00 94.85           C  
ANISOU 1095  CA  MET A 171    14712  11862   9463  -1216   4228   1731       C  
ATOM   1096  C   MET A 171     -11.565   0.396  58.621  1.00 93.67           C  
ANISOU 1096  C   MET A 171    15143  11567   8880  -1100   4180   1807       C  
ATOM   1097  O   MET A 171     -11.802  -0.541  59.393  1.00 93.88           O  
ANISOU 1097  O   MET A 171    15433  11522   8715  -1254   4417   2009       O  
ATOM   1098  CB  MET A 171     -12.861  -0.578  56.722  1.00 94.34           C  
ANISOU 1098  CB  MET A 171    14518  11682   9645  -1563   4190   1864       C  
ATOM   1099  CG  MET A 171     -14.043  -0.465  55.768  1.00 96.05           C  
ANISOU 1099  CG  MET A 171    14148  12098  10249  -1754   4281   1825       C  
ATOM   1100  SD  MET A 171     -15.597  -0.119  56.619  1.00 98.59           S  
ANISOU 1100  SD  MET A 171    14156  12723  10579  -1812   4844   1896       S  
ATOM   1101  CE  MET A 171     -15.819   1.621  56.250  1.00 99.54           C  
ANISOU 1101  CE  MET A 171    13916  13077  10827  -1416   4776   1684       C  
ATOM   1102  N   HIS A 172     -10.467   1.149  58.714  1.00 95.24           N  
ANISOU 1102  N   HIS A 172    15542  11726   8918   -848   3872   1662       N  
ATOM   1103  CA  HIS A 172      -9.477   1.035  59.787  1.00 94.47           C  
ANISOU 1103  CA  HIS A 172    15958  11553   8384   -710   3765   1708       C  
ATOM   1104  C   HIS A 172      -8.818  -0.340  59.833  1.00 93.50           C  
ANISOU 1104  C   HIS A 172    16125  11218   8182   -822   3618   1932       C  
ATOM   1105  O   HIS A 172      -8.348  -0.772  60.888  1.00 93.46           O  
ANISOU 1105  O   HIS A 172    16553  11165   7793   -760   3644   2075       O  
ATOM   1106  CB  HIS A 172     -10.098   1.376  61.146  1.00 96.64           C  
ANISOU 1106  CB  HIS A 172    16460  11962   8295   -653   4164   1736       C  
ATOM   1107  CG  HIS A 172     -10.524   2.805  61.268  1.00 97.52           C  
ANISOU 1107  CG  HIS A 172    16399  12237   8416   -466   4298   1494       C  
ATOM   1108  ND1 HIS A 172     -11.292   3.268  62.315  1.00 98.80           N  
ANISOU 1108  ND1 HIS A 172    16678  12539   8324   -399   4727   1470       N  
ATOM   1109  CD2 HIS A 172     -10.293   3.874  60.469  1.00 97.40           C  
ANISOU 1109  CD2 HIS A 172    16130  12241   8635   -320   4085   1270       C  
ATOM   1110  CE1 HIS A 172     -11.516   4.560  62.155  1.00 99.34           C  
ANISOU 1110  CE1 HIS A 172    16573  12690   8482   -203   4772   1231       C  
ATOM   1111  NE2 HIS A 172     -10.921   4.952  61.042  1.00 98.57           N  
ANISOU 1111  NE2 HIS A 172    16256  12514   8683   -157   4381   1116       N  
ATOM   1112  N   TRP A 173      -8.768  -1.035  58.695  1.00 94.87           N  
ANISOU 1112  N   TRP A 173    16091  11255   8701   -974   3461   1966       N  
ATOM   1113  CA  TRP A 173      -8.099  -2.327  58.615  1.00 93.97           C  
ANISOU 1113  CA  TRP A 173    16258  10888   8557  -1050   3322   2160       C  
ATOM   1114  C   TRP A 173      -6.586  -2.203  58.702  1.00 92.82           C  
ANISOU 1114  C   TRP A 173    16359  10667   8242   -795   2909   2127       C  
ATOM   1115  O   TRP A 173      -5.909  -3.215  58.915  1.00 92.36           O  
ANISOU 1115  O   TRP A 173    16605  10411   8078   -768   2799   2316       O  
ATOM   1116  CB  TRP A 173      -8.494  -3.030  57.315  1.00 89.28           C  
ANISOU 1116  CB  TRP A 173    15377  10166   8380  -1291   3283   2156       C  
ATOM   1117  CG  TRP A 173      -9.942  -3.406  57.275  1.00 90.71           C  
ANISOU 1117  CG  TRP A 173    15322  10418   8724  -1599   3670   2229       C  
ATOM   1118  CD1 TRP A 173     -10.815  -3.408  58.324  1.00 92.04           C  
ANISOU 1118  CD1 TRP A 173    15565  10705   8702  -1678   4074   2345       C  
ATOM   1119  CD2 TRP A 173     -10.699  -3.798  56.123  1.00 91.17           C  
ANISOU 1119  CD2 TRP A 173    15004  10470   9167  -1883   3691   2179       C  
ATOM   1120  NE1 TRP A 173     -12.062  -3.797  57.902  1.00 93.39           N  
ANISOU 1120  NE1 TRP A 173    15394  10947   9142  -2000   4353   2382       N  
ATOM   1121  CE2 TRP A 173     -12.018  -4.040  56.554  1.00 92.92           C  
ANISOU 1121  CE2 TRP A 173    15052  10820   9433  -2139   4104   2277       C  
ATOM   1122  CE3 TRP A 173     -10.387  -3.977  54.772  1.00 90.40           C  
ANISOU 1122  CE3 TRP A 173    14701  10286   9360  -1958   3403   2058       C  
ATOM   1123  CZ2 TRP A 173     -13.025  -4.450  55.683  1.00 94.04           C  
ANISOU 1123  CZ2 TRP A 173    14795  11023   9914  -2482   4204   2255       C  
ATOM   1124  CZ3 TRP A 173     -11.389  -4.385  53.908  1.00 91.44           C  
ANISOU 1124  CZ3 TRP A 173    14483  10467   9794  -2292   3499   2029       C  
ATOM   1125  CH2 TRP A 173     -12.692  -4.617  54.367  1.00 93.33           C  
ANISOU 1125  CH2 TRP A 173    14526  10850  10083  -2558   3880   2126       C  
ATOM   1126  N   TYR A 174      -6.046  -0.995  58.536  1.00 93.69           N  
ANISOU 1126  N   TYR A 174    16336  10924   8338   -610   2686   1900       N  
ATOM   1127  CA  TYR A 174      -4.615  -0.763  58.667  1.00 92.97           C  
ANISOU 1127  CA  TYR A 174    16423  10815   8087   -392   2294   1850       C  
ATOM   1128  C   TYR A 174      -4.196  -0.521  60.109  1.00 93.67           C  
ANISOU 1128  C   TYR A 174    16899  11006   7686   -248   2295   1907       C  
ATOM   1129  O   TYR A 174      -3.029  -0.748  60.443  1.00 93.46           O  
ANISOU 1129  O   TYR A 174    17088  10958   7465    -92   1982   1965       O  
ATOM   1130  CB  TYR A 174      -4.203   0.441  57.816  1.00 94.98           C  
ANISOU 1130  CB  TYR A 174    16369  11169   8551   -305   2059   1576       C  
ATOM   1131  CG  TYR A 174      -4.763   1.755  58.322  1.00 95.92           C  
ANISOU 1131  CG  TYR A 174    16422  11468   8553   -247   2220   1390       C  
ATOM   1132  CD1 TYR A 174      -6.035   2.177  57.959  1.00 96.71           C  
ANISOU 1132  CD1 TYR A 174    16235  11644   8866   -341   2521   1332       C  
ATOM   1133  CD2 TYR A 174      -4.014   2.580  59.154  1.00 96.23           C  
ANISOU 1133  CD2 TYR A 174    16687  11602   8275    -94   2068   1265       C  
ATOM   1134  CE1 TYR A 174      -6.551   3.374  58.420  1.00 97.73           C  
ANISOU 1134  CE1 TYR A 174    16318  11908   8905   -243   2698   1166       C  
ATOM   1135  CE2 TYR A 174      -4.522   3.781  59.618  1.00 97.12           C  
ANISOU 1135  CE2 TYR A 174    16790  11833   8278    -37   2242   1071       C  
ATOM   1136  CZ  TYR A 174      -5.791   4.173  59.247  1.00 97.83           C  
ANISOU 1136  CZ  TYR A 174    16608  11966   8596    -91   2572   1027       C  
ATOM   1137  OH  TYR A 174      -6.303   5.367  59.703  1.00 98.83           O  
ANISOU 1137  OH  TYR A 174    16736  12183   8630     11   2773    838       O  
ATOM   1138  N   ARG A 175      -5.120  -0.071  60.959  1.00 94.61           N  
ANISOU 1138  N   ARG A 175    17100  11254   7594   -290   2637   1891       N  
ATOM   1139  CA  ARG A 175      -4.796   0.383  62.308  1.00 95.37           C  
ANISOU 1139  CA  ARG A 175    17567  11483   7187   -160   2652   1882       C  
ATOM   1140  C   ARG A 175      -3.977  -0.644  63.073  1.00 95.41           C  
ANISOU 1140  C   ARG A 175    17933  11415   6905    -81   2463   2129       C  
ATOM   1141  O   ARG A 175      -4.397  -1.793  63.240  1.00 96.14           O  
ANISOU 1141  O   ARG A 175    18078  11374   7076   -179   2620   2361       O  
ATOM   1142  CB  ARG A 175      -6.082   0.700  63.076  1.00 99.68           C  
ANISOU 1142  CB  ARG A 175    18161  12142   7570   -241   3148   1882       C  
ATOM   1143  CG  ARG A 175      -6.902   1.846  62.512  1.00100.09           C  
ANISOU 1143  CG  ARG A 175    17828  12302   7901   -245   3328   1626       C  
ATOM   1144  CD  ARG A 175      -6.179   3.170  62.669  1.00100.08           C  
ANISOU 1144  CD  ARG A 175    17876  12387   7763    -70   3089   1336       C  
ATOM   1145  NE  ARG A 175      -6.990   4.308  62.250  1.00100.72           N  
ANISOU 1145  NE  ARG A 175    17655  12536   8076    -30   3300   1111       N  
ATOM   1146  CZ  ARG A 175      -7.776   5.000  63.068  1.00101.84           C  
ANISOU 1146  CZ  ARG A 175    17898  12785   8010     33   3672   1010       C  
ATOM   1147  NH1 ARG A 175      -7.855   4.668  64.350  1.00102.46           N  
ANISOU 1147  NH1 ARG A 175    18386  12928   7615     36   3875   1106       N  
ATOM   1148  NH2 ARG A 175      -8.481   6.024  62.608  1.00102.51           N  
ANISOU 1148  NH2 ARG A 175    17691  12910   8350    114   3853    821       N  
ATOM   1149  N   ALA A 176      -2.804  -0.221  63.533  1.00 94.35           N  
ANISOU 1149  N   ALA A 176    17957  11380   6511     95   2085   2052       N  
ATOM   1150  CA  ALA A 176      -1.967  -1.054  64.376  1.00 96.22           C  
ANISOU 1150  CA  ALA A 176    18434  11616   6508    216   1841   2256       C  
ATOM   1151  C   ALA A 176      -2.528  -1.096  65.795  1.00100.72           C  
ANISOU 1151  C   ALA A 176    19229  12313   6725    198   2066   2318       C  
ATOM   1152  O   ALA A 176      -3.380  -0.291  66.182  1.00101.52           O  
ANISOU 1152  O   ALA A 176    19308  12531   6735    128   2358   2152       O  
ATOM   1153  CB  ALA A 176      -0.528  -0.536  64.381  1.00 97.36           C  
ANISOU 1153  CB  ALA A 176    18609  11880   6504    392   1343   2146       C  
ATOM   1154  N   THR A 177      -2.038  -2.054  66.580  1.00 98.59           N  
ANISOU 1154  N   THR A 177    19185  12021   6255    280   1938   2568       N  
ATOM   1155  CA  THR A 177      -2.512  -2.254  67.942  1.00103.57           C  
ANISOU 1155  CA  THR A 177    20064  12762   6526    262   2141   2675       C  
ATOM   1156  C   THR A 177      -1.467  -1.908  68.996  1.00106.60           C  
ANISOU 1156  C   THR A 177    20672  13365   6466    425   1781   2651       C  
ATOM   1157  O   THR A 177      -1.701  -2.152  70.184  1.00111.28           O  
ANISOU 1157  O   THR A 177    21510  14062   6711    428   1896   2767       O  
ATOM   1158  CB  THR A 177      -2.988  -3.696  68.136  1.00107.47           C  
ANISOU 1158  CB  THR A 177    20670  13055   7109    188   2352   3012       C  
ATOM   1159  OG1 THR A 177      -1.912  -4.603  67.859  1.00107.49           O  
ANISOU 1159  OG1 THR A 177    20742  12917   7183    339   2005   3214       O  
ATOM   1160  CG2 THR A 177      -4.163  -4.001  67.219  1.00105.38           C  
ANISOU 1160  CG2 THR A 177    20169  12615   7254    -36   2735   3012       C  
ATOM   1161  N   HIS A 178      -0.326  -1.351  68.603  1.00105.29           N  
ANISOU 1161  N   HIS A 178    20419  13290   6297    543   1347   2506       N  
ATOM   1162  CA  HIS A 178       0.666  -0.959  69.591  1.00108.54           C  
ANISOU 1162  CA  HIS A 178    20996  13952   6291    660    981   2459       C  
ATOM   1163  C   HIS A 178       0.404   0.467  70.066  1.00108.92           C  
ANISOU 1163  C   HIS A 178    21079  14194   6111    584   1048   2098       C  
ATOM   1164  O   HIS A 178      -0.267   1.259  69.400  1.00105.77           O  
ANISOU 1164  O   HIS A 178    20525  13729   5933    492   1279   1864       O  
ATOM   1165  CB  HIS A 178       2.089  -1.100  69.042  1.00112.80           C  
ANISOU 1165  CB  HIS A 178    21402  14532   6926    816    459   2490       C  
ATOM   1166  CG  HIS A 178       2.409  -0.168  67.916  1.00107.93           C  
ANISOU 1166  CG  HIS A 178    20522  13904   6582    780    314   2203       C  
ATOM   1167  ND1 HIS A 178       2.046  -0.424  66.612  1.00103.54           N  
ANISOU 1167  ND1 HIS A 178    19761  13115   6466    737    457   2215       N  
ATOM   1168  CD2 HIS A 178       3.081   1.007  67.896  1.00107.12           C  
ANISOU 1168  CD2 HIS A 178    20339  13991   6371    764     33   1899       C  
ATOM   1169  CE1 HIS A 178       2.473   0.558  65.838  1.00100.33           C  
ANISOU 1169  CE1 HIS A 178    19166  12759   6195    714    275   1946       C  
ATOM   1170  NE2 HIS A 178       3.102   1.440  66.593  1.00102.36           N  
ANISOU 1170  NE2 HIS A 178    19494  13260   6138    723     21   1746       N  
ATOM   1171  N   GLN A 179       0.955   0.782  71.243  1.00110.84           N  
ANISOU 1171  N   GLN A 179    21536  14677   5902    629    840   2054       N  
ATOM   1172  CA  GLN A 179       0.546   1.980  71.971  1.00112.83           C  
ANISOU 1172  CA  GLN A 179    21911  15088   5871    547    987   1736       C  
ATOM   1173  C   GLN A 179       0.847   3.252  71.187  1.00108.97           C  
ANISOU 1173  C   GLN A 179    21233  14602   5568    498    851   1355       C  
ATOM   1174  O   GLN A 179       0.006   4.156  71.114  1.00108.19           O  
ANISOU 1174  O   GLN A 179    21123  14457   5525    423   1177   1101       O  
ATOM   1175  CB  GLN A 179       1.235   2.017  73.334  1.00118.68           C  
ANISOU 1175  CB  GLN A 179    22918  16099   6077    593    724   1764       C  
ATOM   1176  CG  GLN A 179       0.756   3.130  74.249  1.00121.89           C  
ANISOU 1176  CG  GLN A 179    23517  16656   6140    507    916   1450       C  
ATOM   1177  CD  GLN A 179      -0.701   2.972  74.649  1.00123.55           C  
ANISOU 1177  CD  GLN A 179    23841  16767   6334    451   1517   1508       C  
ATOM   1178  OE1 GLN A 179      -1.574   3.688  74.158  1.00121.12           O  
ANISOU 1178  OE1 GLN A 179    23411  16348   6260    392   1863   1290       O  
ATOM   1179  NE2 GLN A 179      -0.968   2.028  75.544  1.00128.07           N  
ANISOU 1179  NE2 GLN A 179    24633  17389   6637    473   1646   1813       N  
ATOM   1180  N   GLU A 180       2.041   3.342  70.595  1.00111.04           N  
ANISOU 1180  N   GLU A 180    21338  14913   5939    547    381   1316       N  
ATOM   1181  CA  GLU A 180       2.430   4.563  69.892  1.00108.02           C  
ANISOU 1181  CA  GLU A 180    20792  14534   5715    477    222    953       C  
ATOM   1182  C   GLU A 180       1.480   4.877  68.741  1.00103.34           C  
ANISOU 1182  C   GLU A 180    20017  13704   5543    426    583    862       C  
ATOM   1183  O   GLU A 180       1.156   6.046  68.495  1.00102.15           O  
ANISOU 1183  O   GLU A 180    19833  13520   5460    356    710    540       O  
ATOM   1184  CB  GLU A 180       3.867   4.441  69.382  1.00113.87           C  
ANISOU 1184  CB  GLU A 180    21350  15376   6541    532   -333    975       C  
ATOM   1185  CG  GLU A 180       4.365   5.671  68.641  1.00111.12           C  
ANISOU 1185  CG  GLU A 180    20826  15029   6365    429   -524    608       C  
ATOM   1186  CD  GLU A 180       5.807   5.542  68.194  1.00110.62           C  
ANISOU 1186  CD  GLU A 180    20543  15104   6382    469  -1072    633       C  
ATOM   1187  OE1 GLU A 180       6.433   4.505  68.498  1.00112.59           O  
ANISOU 1187  OE1 GLU A 180    20776  15459   6546    612  -1307    940       O  
ATOM   1188  OE2 GLU A 180       6.308   6.470  67.523  1.00108.58           O  
ANISOU 1188  OE2 GLU A 180    20117  14845   6293    363  -1254    354       O  
ATOM   1189  N   ALA A 181       1.020   3.849  68.023  1.00107.60           N  
ANISOU 1189  N   ALA A 181    20438  14072   6374    459    755   1140       N  
ATOM   1190  CA  ALA A 181       0.083   4.084  66.929  1.00103.73           C  
ANISOU 1190  CA  ALA A 181    19750  13393   6270    398   1093   1075       C  
ATOM   1191  C   ALA A 181      -1.282   4.506  67.454  1.00105.42           C  
ANISOU 1191  C   ALA A 181    20035  13597   6422    341   1611    989       C  
ATOM   1192  O   ALA A 181      -1.937   5.375  66.867  1.00103.43           O  
ANISOU 1192  O   ALA A 181    19648  13280   6372    309   1849    775       O  
ATOM   1193  CB  ALA A 181      -0.040   2.833  66.060  1.00102.45           C  
ANISOU 1193  CB  ALA A 181    19445  13055   6426    415   1134   1386       C  
ATOM   1194  N   ILE A 182      -1.722   3.907  68.563  1.00102.70           N  
ANISOU 1194  N   ILE A 182    19894  13323   5803    342   1796   1160       N  
ATOM   1195  CA  ILE A 182      -3.033   4.227  69.122  1.00105.01           C  
ANISOU 1195  CA  ILE A 182    20236  13628   6033    296   2308   1100       C  
ATOM   1196  C   ILE A 182      -3.077   5.674  69.595  1.00106.39           C  
ANISOU 1196  C   ILE A 182    20507  13892   6024    312   2355    721       C  
ATOM   1197  O   ILE A 182      -4.089   6.366  69.429  1.00106.22           O  
ANISOU 1197  O   ILE A 182    20389  13824   6145    310   2751    562       O  
ATOM   1198  CB  ILE A 182      -3.380   3.244  70.256  1.00105.90           C  
ANISOU 1198  CB  ILE A 182    20574  13807   5858    286   2469   1375       C  
ATOM   1199  CG1 ILE A 182      -3.500   1.820  69.708  1.00104.70           C  
ANISOU 1199  CG1 ILE A 182    20328  13499   5956    252   2495   1738       C  
ATOM   1200  CG2 ILE A 182      -4.666   3.660  70.962  1.00109.17           C  
ANISOU 1200  CG2 ILE A 182    21043  14274   6160    244   2990   1292       C  
ATOM   1201  CD1 ILE A 182      -3.605   0.760  70.781  1.00109.65           C  
ANISOU 1201  CD1 ILE A 182    21205  14158   6298    250   2574   2039       C  
ATOM   1202  N   ASN A 183      -1.981   6.159  70.185  1.00108.14           N  
ANISOU 1202  N   ASN A 183    20905  14240   5942    327   1953    566       N  
ATOM   1203  CA  ASN A 183      -1.945   7.550  70.622  1.00109.78           C  
ANISOU 1203  CA  ASN A 183    21228  14497   5988    313   1975    178       C  
ATOM   1204  C   ASN A 183      -1.983   8.512  69.440  1.00105.53           C  
ANISOU 1204  C   ASN A 183    20468  13803   5824    305   1985    -73       C  
ATOM   1205  O   ASN A 183      -2.547   9.605  69.553  1.00106.45           O  
ANISOU 1205  O   ASN A 183    20621  13860   5964    318   2240   -353       O  
ATOM   1206  CB  ASN A 183      -0.703   7.808  71.477  1.00109.25           C  
ANISOU 1206  CB  ASN A 183    21368  14618   5523    287   1506     68       C  
ATOM   1207  CG  ASN A 183      -0.705   7.006  72.766  1.00114.50           C  
ANISOU 1207  CG  ASN A 183    22291  15458   5756    309   1515    293       C  
ATOM   1208  OD1 ASN A 183       0.161   6.161  72.985  1.00115.47           O  
ANISOU 1208  OD1 ASN A 183    22443  15692   5741    342   1155    529       O  
ATOM   1209  ND2 ASN A 183      -1.686   7.266  73.624  1.00118.26           N  
ANISOU 1209  ND2 ASN A 183    22951  15961   6019    308   1938    231       N  
ATOM   1210  N   CYS A 184      -1.394   8.131  68.304  1.00107.79           N  
ANISOU 1210  N   CYS A 184    20537  14012   6407    297   1722     28       N  
ATOM   1211  CA  CYS A 184      -1.465   8.984  67.122  1.00103.95           C  
ANISOU 1211  CA  CYS A 184    19845  13376   6276    289   1747   -180       C  
ATOM   1212  C   CYS A 184      -2.838   8.916  66.465  1.00102.24           C  
ANISOU 1212  C   CYS A 184    19433  13040   6374    332   2250   -103       C  
ATOM   1213  O   CYS A 184      -3.257   9.873  65.805  1.00101.34           O  
ANISOU 1213  O   CYS A 184    19197  12815   6492    366   2420   -315       O  
ATOM   1214  CB  CYS A 184      -0.375   8.591  66.121  1.00103.30           C  
ANISOU 1214  CB  CYS A 184    19592  13269   6388    265   1306    -96       C  
ATOM   1215  SG  CYS A 184      -0.323   9.614  64.626  1.00102.54           S  
ANISOU 1215  SG  CYS A 184    19142  12994   6823    235   1268   -333       S  
ATOM   1216  N   TYR A 185      -3.549   7.800  66.639  1.00105.53           N  
ANISOU 1216  N   TYR A 185    19802  13479   6813    327   2490    203       N  
ATOM   1217  CA  TYR A 185      -4.859   7.642  66.016  1.00104.36           C  
ANISOU 1217  CA  TYR A 185    19407  13263   6981    332   2953    297       C  
ATOM   1218  C   TYR A 185      -5.885   8.574  66.651  1.00107.30           C  
ANISOU 1218  C   TYR A 185    19812  13666   7293    404   3385     97       C  
ATOM   1219  O   TYR A 185      -6.597   9.300  65.948  1.00105.97           O  
ANISOU 1219  O   TYR A 185    19424  13427   7412    473   3644    -31       O  
ATOM   1220  CB  TYR A 185      -5.299   6.182  66.120  1.00104.31           C  
ANISOU 1220  CB  TYR A 185    19351  13267   7015    258   3081    666       C  
ATOM   1221  CG  TYR A 185      -4.470   5.243  65.273  1.00102.03           C  
ANISOU 1221  CG  TYR A 185    18982  12894   6892    215   2731    872       C  
ATOM   1222  CD1 TYR A 185      -3.743   5.717  64.189  1.00101.27           C  
ANISOU 1222  CD1 TYR A 185    18647  12728   7101    229   2399    732       C  
ATOM   1223  CD2 TYR A 185      -4.377   3.892  65.583  1.00102.53           C  
ANISOU 1223  CD2 TYR A 185    19119  12930   6907    167   2689   1189       C  
ATOM   1224  CE1 TYR A 185      -2.974   4.868  63.416  1.00100.37           C  
ANISOU 1224  CE1 TYR A 185    18375  12539   7222    206   2065    897       C  
ATOM   1225  CE2 TYR A 185      -3.603   3.035  64.820  1.00100.97           C  
ANISOU 1225  CE2 TYR A 185    18860  12624   6878    159   2382   1369       C  
ATOM   1226  CZ  TYR A 185      -2.907   3.529  63.737  1.00100.21           C  
ANISOU 1226  CZ  TYR A 185    18519  12480   7078    184   2074   1215       C  
ATOM   1227  OH  TYR A 185      -2.140   2.681  62.972  1.00 99.39           O  
ANISOU 1227  OH  TYR A 185    18281  12271   7212    193   1770   1368       O  
ATOM   1228  N   ALA A 186      -5.975   8.567  67.983  1.00103.80           N  
ANISOU 1228  N   ALA A 186    19636  13329   6475    408   3473     75       N  
ATOM   1229  CA  ALA A 186      -6.919   9.449  68.662  1.00107.32           C  
ANISOU 1229  CA  ALA A 186    20136  13800   6840    492   3891   -123       C  
ATOM   1230  C   ALA A 186      -6.489  10.908  68.578  1.00107.27           C  
ANISOU 1230  C   ALA A 186    20229  13700   6827    564   3779   -506       C  
ATOM   1231  O   ALA A 186      -7.342  11.803  68.558  1.00108.62           O  
ANISOU 1231  O   ALA A 186    20326  13808   7137    680   4141   -685       O  
ATOM   1232  CB  ALA A 186      -7.080   9.027  70.122  1.00107.76           C  
ANISOU 1232  CB  ALA A 186    20484  13999   6461    466   4008    -43       C  
ATOM   1233  N   GLU A 187      -5.184  11.167  68.529  1.00107.23           N  
ANISOU 1233  N   GLU A 187    20378  13681   6686    496   3288   -631       N  
ATOM   1234  CA  GLU A 187      -4.693  12.534  68.420  1.00107.40           C  
ANISOU 1234  CA  GLU A 187    20499  13586   6723    511   3154   -999       C  
ATOM   1235  C   GLU A 187      -4.988  13.089  67.033  1.00103.28           C  
ANISOU 1235  C   GLU A 187    19692  12883   6666    580   3242  -1068       C  
ATOM   1236  O   GLU A 187      -4.637  12.479  66.018  1.00 99.25           O  
ANISOU 1236  O   GLU A 187    18976  12354   6381    538   3047   -899       O  
ATOM   1237  CB  GLU A 187      -3.193  12.581  68.703  1.00101.41           C  
ANISOU 1237  CB  GLU A 187    19918  12896   5718    381   2585  -1095       C  
ATOM   1238  CG  GLU A 187      -2.582  13.971  68.628  1.00102.09           C  
ANISOU 1238  CG  GLU A 187    20111  12856   5821    331   2412  -1482       C  
ATOM   1239  CD  GLU A 187      -3.101  14.903  69.707  1.00107.37           C  
ANISOU 1239  CD  GLU A 187    21047  13500   6247    371   2694  -1744       C  
ATOM   1240  OE1 GLU A 187      -3.525  14.409  70.772  1.00111.19           O  
ANISOU 1240  OE1 GLU A 187    21700  14140   6407    395   2868  -1643       O  
ATOM   1241  OE2 GLU A 187      -3.081  16.133  69.490  1.00108.00           O  
ANISOU 1241  OE2 GLU A 187    21183  13390   6462    380   2750  -2049       O  
ATOM   1242  N   GLU A 188      -5.637  14.254  66.990  1.00103.74           N  
ANISOU 1242  N   GLU A 188    19748  12801   6866    702   3542  -1310       N  
ATOM   1243  CA  GLU A 188      -6.001  14.853  65.714  1.00100.50           C  
ANISOU 1243  CA  GLU A 188    19072  12215   6898    807   3659  -1365       C  
ATOM   1244  C   GLU A 188      -4.859  15.652  65.098  1.00 98.46           C  
ANISOU 1244  C   GLU A 188    18889  11794   6727    719   3258  -1590       C  
ATOM   1245  O   GLU A 188      -4.870  15.894  63.885  1.00 97.24           O  
ANISOU 1245  O   GLU A 188    18458  11514   6974    759   3203  -1563       O  
ATOM   1246  CB  GLU A 188      -7.246  15.731  65.890  1.00 98.14           C  
ANISOU 1246  CB  GLU A 188    18701  11825   6761   1021   4169  -1487       C  
ATOM   1247  CG  GLU A 188      -7.822  16.268  64.591  1.00 95.34           C  
ANISOU 1247  CG  GLU A 188    18020  11318   6885   1189   4343  -1483       C  
ATOM   1248  CD  GLU A 188      -9.136  16.995  64.784  1.00 98.75           C  
ANISOU 1248  CD  GLU A 188    18314  11702   7503   1445   4855  -1542       C  
ATOM   1249  OE1 GLU A 188      -9.606  17.082  65.937  1.00103.28           O  
ANISOU 1249  OE1 GLU A 188    19063  12356   7824   1478   5094  -1602       O  
ATOM   1250  OE2 GLU A 188      -9.700  17.477  63.779  1.00 97.21           O  
ANISOU 1250  OE2 GLU A 188    17825  11402   7710   1630   5016  -1518       O  
ATOM   1251  N   THR A 189      -3.867  16.044  65.893  1.00102.78           N  
ANISOU 1251  N   THR A 189    19722  12362   6967    576   2937  -1786       N  
ATOM   1252  CA  THR A 189      -2.691  16.731  65.378  1.00101.31           C  
ANISOU 1252  CA  THR A 189    19581  12054   6860    432   2527  -1992       C  
ATOM   1253  C   THR A 189      -1.622  15.771  64.872  1.00 98.79           C  
ANISOU 1253  C   THR A 189    19142  11875   6517    285   2062  -1810       C  
ATOM   1254  O   THR A 189      -0.599  16.226  64.351  1.00 98.39           O  
ANISOU 1254  O   THR A 189    19066  11757   6561    146   1702  -1951       O  
ATOM   1255  CB  THR A 189      -2.086  17.639  66.455  1.00101.01           C  
ANISOU 1255  CB  THR A 189    19863  11996   6519    313   2384  -2301       C  
ATOM   1256  OG1 THR A 189      -1.652  16.845  67.565  1.00103.61           O  
ANISOU 1256  OG1 THR A 189    20356  12595   6417    222   2193  -2204       O  
ATOM   1257  CG2 THR A 189      -3.113  18.654  66.934  1.00104.59           C  
ANISOU 1257  CG2 THR A 189    20457  12277   7006    477   2850  -2496       C  
ATOM   1258  N   CYS A 190      -1.831  14.464  65.010  1.00 99.87           N  
ANISOU 1258  N   CYS A 190    19198  12195   6552    310   2069  -1494       N  
ATOM   1259  CA  CYS A 190      -0.887  13.461  64.540  1.00 99.21           C  
ANISOU 1259  CA  CYS A 190    18930  12234   6531    216   1639  -1268       C  
ATOM   1260  C   CYS A 190      -1.485  12.717  63.356  1.00 98.42           C  
ANISOU 1260  C   CYS A 190    18367  12088   6940    281   1744   -985       C  
ATOM   1261  O   CYS A 190      -2.612  12.215  63.436  1.00 98.59           O  
ANISOU 1261  O   CYS A 190    18315  12129   7016    371   2121   -816       O  
ATOM   1262  CB  CYS A 190      -0.526  12.473  65.653  1.00106.64           C  
ANISOU 1262  CB  CYS A 190    20090  13400   7027    188   1492  -1089       C  
ATOM   1263  SG  CYS A 190       0.733  11.259  65.179  1.00106.09           S  
ANISOU 1263  SG  CYS A 190    19858  13469   6982    130    958   -813       S  
ATOM   1264  N   CYS A 191      -0.731  12.653  62.262  1.00 97.07           N  
ANISOU 1264  N   CYS A 191    17885  11868   7131    217   1419   -944       N  
ATOM   1265  CA  CYS A 191      -1.125  11.917  61.068  1.00 96.34           C  
ANISOU 1265  CA  CYS A 191    17376  11738   7490    248   1449   -700       C  
ATOM   1266  C   CYS A 191      -0.002  10.985  60.640  1.00 95.67           C  
ANISOU 1266  C   CYS A 191    17150  11733   7467    174   1033   -533       C  
ATOM   1267  O   CYS A 191       0.264  10.798  59.449  1.00 94.99           O  
ANISOU 1267  O   CYS A 191    16737  11585   7771    154    897   -459       O  
ATOM   1268  CB  CYS A 191      -1.509  12.872  59.939  1.00 90.00           C  
ANISOU 1268  CB  CYS A 191    16306  10765   7127    286   1549   -816       C  
ATOM   1269  SG  CYS A 191      -2.299  12.105  58.498  1.00 89.53           S  
ANISOU 1269  SG  CYS A 191    15755  10682   7579    325   1651   -546       S  
ATOM   1270  N   ASP A 192       0.693  10.402  61.612  1.00 96.00           N  
ANISOU 1270  N   ASP A 192    17446  11921   7109    153    825   -469       N  
ATOM   1271  CA  ASP A 192       1.697   9.398  61.300  1.00 95.62           C  
ANISOU 1271  CA  ASP A 192    17267  11955   7109    142    463   -270       C  
ATOM   1272  C   ASP A 192       1.020   8.154  60.742  1.00 94.88           C  
ANISOU 1272  C   ASP A 192    17000  11807   7244    195    640     37       C  
ATOM   1273  O   ASP A 192      -0.065   7.766  61.183  1.00 95.00           O  
ANISOU 1273  O   ASP A 192    17125  11809   7163    221    992    151       O  
ATOM   1274  CB  ASP A 192       2.515   9.046  62.541  1.00 98.91           C  
ANISOU 1274  CB  ASP A 192    18007  12558   7016    144    202   -239       C  
ATOM   1275  CG  ASP A 192       3.407  10.184  62.994  1.00 99.73           C  
ANISOU 1275  CG  ASP A 192    18245  12739   6908     36    -72   -555       C  
ATOM   1276  OD1 ASP A 192       3.820  10.994  62.139  1.00 99.45           O  
ANISOU 1276  OD1 ASP A 192    17981  12612   7195    -49   -182   -738       O  
ATOM   1277  OD2 ASP A 192       3.697  10.268  64.206  1.00100.71           O  
ANISOU 1277  OD2 ASP A 192    18721  13017   6529     16   -178   -621       O  
ATOM   1278  N   PHE A 193       1.663   7.530  59.763  1.00 96.99           N  
ANISOU 1278  N   PHE A 193    16998  12038   7815    194    413    159       N  
ATOM   1279  CA  PHE A 193       1.073   6.408  59.038  1.00 96.16           C  
ANISOU 1279  CA  PHE A 193    16719  11839   7977    208    564    403       C  
ATOM   1280  C   PHE A 193       1.656   5.113  59.593  1.00 96.19           C  
ANISOU 1280  C   PHE A 193    16896  11883   7771    274    407    663       C  
ATOM   1281  O   PHE A 193       2.650   4.589  59.089  1.00 95.99           O  
ANISOU 1281  O   PHE A 193    16743  11855   7874    323    117    742       O  
ATOM   1282  CB  PHE A 193       1.316   6.557  57.542  1.00 96.30           C  
ANISOU 1282  CB  PHE A 193    16369  11765   8457    174    462    359       C  
ATOM   1283  CG  PHE A 193       0.716   5.458  56.717  1.00 95.41           C  
ANISOU 1283  CG  PHE A 193    16089  11550   8613    154    601    564       C  
ATOM   1284  CD1 PHE A 193      -0.656   5.352  56.575  1.00 95.38           C  
ANISOU 1284  CD1 PHE A 193    16021  11503   8717    102    951    616       C  
ATOM   1285  CD2 PHE A 193       1.525   4.550  56.055  1.00 94.78           C  
ANISOU 1285  CD2 PHE A 193    15903  11418   8689    180    388    691       C  
ATOM   1286  CE1 PHE A 193      -1.211   4.343  55.811  1.00 94.66           C  
ANISOU 1286  CE1 PHE A 193    15778  11324   8866     32   1060    780       C  
ATOM   1287  CE2 PHE A 193       0.974   3.543  55.284  1.00 93.88           C  
ANISOU 1287  CE2 PHE A 193    15680  11181   8811    136    523    846       C  
ATOM   1288  CZ  PHE A 193      -0.396   3.444  55.159  1.00 93.78           C  
ANISOU 1288  CZ  PHE A 193    15615  11130   8889     39    846    884       C  
ATOM   1289  N   PHE A 194       1.027   4.598  60.647  1.00 97.29           N  
ANISOU 1289  N   PHE A 194    17334  12052   7580    293    622    808       N  
ATOM   1290  CA  PHE A 194       1.369   3.301  61.213  1.00 97.43           C  
ANISOU 1290  CA  PHE A 194    17567  12064   7389    368    545   1106       C  
ATOM   1291  C   PHE A 194       0.327   2.281  60.781  1.00 96.73           C  
ANISOU 1291  C   PHE A 194    17432  11805   7515    306    880   1323       C  
ATOM   1292  O   PHE A 194      -0.877   2.540  60.876  1.00 96.80           O  
ANISOU 1292  O   PHE A 194    17422  11799   7558    213   1249   1288       O  
ATOM   1293  CB  PHE A 194       1.436   3.349  62.740  1.00 99.46           C  
ANISOU 1293  CB  PHE A 194    18246  12469   7076    415    551   1152       C  
ATOM   1294  CG  PHE A 194       2.537   4.210  63.274  1.00100.37           C  
ANISOU 1294  CG  PHE A 194    18442  12772   6923    445    173    947       C  
ATOM   1295  CD1 PHE A 194       3.851   3.776  63.244  1.00100.89           C  
ANISOU 1295  CD1 PHE A 194    18453  12932   6949    542   -270   1042       C  
ATOM   1296  CD2 PHE A 194       2.255   5.441  63.838  1.00100.90           C  
ANISOU 1296  CD2 PHE A 194    18645  12923   6771    372    266    656       C  
ATOM   1297  CE1 PHE A 194       4.867   4.568  63.742  1.00101.98           C  
ANISOU 1297  CE1 PHE A 194    18626  13279   6843    528   -640    846       C  
ATOM   1298  CE2 PHE A 194       3.264   6.233  64.343  1.00101.83           C  
ANISOU 1298  CE2 PHE A 194    18855  13205   6629    347    -90    443       C  
ATOM   1299  CZ  PHE A 194       4.571   5.798  64.294  1.00102.40           C  
ANISOU 1299  CZ  PHE A 194    18833  13404   6670    407   -556    537       C  
ATOM   1300  N   THR A 195       0.791   1.128  60.306  1.00 91.64           N  
ANISOU 1300  N   THR A 195    16762  11032   7024    353    758   1540       N  
ATOM   1301  CA  THR A 195      -0.092   0.047  59.901  1.00 91.05           C  
ANISOU 1301  CA  THR A 195    16684  10765   7146    257   1047   1745       C  
ATOM   1302  C   THR A 195       0.348  -1.251  60.559  1.00 91.42           C  
ANISOU 1302  C   THR A 195    17061  10704   6971    359    995   2066       C  
ATOM   1303  O   THR A 195       1.526  -1.439  60.876  1.00 91.93           O  
ANISOU 1303  O   THR A 195    17228  10828   6875    542    654   2136       O  
ATOM   1304  CB  THR A 195      -0.113  -0.137  58.378  1.00 88.63           C  
ANISOU 1304  CB  THR A 195    16022  10322   7333    185   1007   1673       C  
ATOM   1305  OG1 THR A 195       1.197  -0.492  57.917  1.00 88.46           O  
ANISOU 1305  OG1 THR A 195    15946  10263   7401    330    654   1702       O  
ATOM   1306  CG2 THR A 195      -0.554   1.144  57.698  1.00 88.44           C  
ANISOU 1306  CG2 THR A 195    15687  10393   7521    108   1052   1395       C  
ATOM   1307  N   ASN A 196      -0.614  -2.146  60.767  1.00 88.83           N  
ANISOU 1307  N   ASN A 196    16891  10221   6641    239   1339   2273       N  
ATOM   1308  CA  ASN A 196      -0.278  -3.475  61.245  1.00 89.19           C  
ANISOU 1308  CA  ASN A 196    17258  10088   6541    326   1329   2603       C  
ATOM   1309  C   ASN A 196       0.466  -4.247  60.158  1.00 88.52           C  
ANISOU 1309  C   ASN A 196    17041   9789   6804    408   1126   2661       C  
ATOM   1310  O   ASN A 196       0.452  -3.883  58.979  1.00 87.64           O  
ANISOU 1310  O   ASN A 196    16579   9653   7069    330   1075   2455       O  
ATOM   1311  CB  ASN A 196      -1.536  -4.223  61.704  1.00 88.63           C  
ANISOU 1311  CB  ASN A 196    17268   9906   6502    125   1750   2748       C  
ATOM   1312  CG  ASN A 196      -2.572  -4.385  60.602  1.00 87.81           C  
ANISOU 1312  CG  ASN A 196    16941   9652   6772   -133   2039   2694       C  
ATOM   1313  OD1 ASN A 196      -2.332  -4.046  59.450  1.00 86.97           O  
ANISOU 1313  OD1 ASN A 196    16540   9521   6984   -151   1890   2520       O  
ATOM   1314  ND2 ASN A 196      -3.739  -4.908  60.964  1.00 88.64           N  
ANISOU 1314  ND2 ASN A 196    17051   9706   6921   -347   2409   2789       N  
ATOM   1315  N   GLN A 197       1.137  -5.322  60.573  1.00 88.14           N  
ANISOU 1315  N   GLN A 197    17207   9603   6678    580   1002   2910       N  
ATOM   1316  CA  GLN A 197       1.995  -6.046  59.641  1.00 87.83           C  
ANISOU 1316  CA  GLN A 197    17107   9353   6910    729    810   2979       C  
ATOM   1317  C   GLN A 197       1.197  -6.684  58.512  1.00 86.81           C  
ANISOU 1317  C   GLN A 197    16895   8926   7164    503   1081   2959       C  
ATOM   1318  O   GLN A 197       1.697  -6.790  57.388  1.00 86.22           O  
ANISOU 1318  O   GLN A 197    16587   8755   7416    541    947   2833       O  
ATOM   1319  CB  GLN A 197       2.811  -7.099  60.388  1.00 92.57           C  
ANISOU 1319  CB  GLN A 197    17903   9875   7393    980    649   3239       C  
ATOM   1320  CG  GLN A 197       3.837  -6.500  61.331  1.00 94.39           C  
ANISOU 1320  CG  GLN A 197    18156  10429   7277   1218    285   3251       C  
ATOM   1321  CD  GLN A 197       4.666  -7.549  62.037  1.00 98.71           C  
ANISOU 1321  CD  GLN A 197    18864  10923   7717   1485    108   3535       C  
ATOM   1322  OE1 GLN A 197       4.437  -8.749  61.880  1.00100.53           O  
ANISOU 1322  OE1 GLN A 197    19231  10841   8123   1500    287   3727       O  
ATOM   1323  NE2 GLN A 197       5.641  -7.103  62.820  1.00100.79           N  
ANISOU 1323  NE2 GLN A 197    19111  11494   7692   1690   -251   3559       N  
ATOM   1324  N   ALA A 198      -0.043  -7.100  58.784  1.00 84.53           N  
ANISOU 1324  N   ALA A 198    16667   8545   6906    239   1440   3011       N  
ATOM   1325  CA  ALA A 198      -0.857  -7.724  57.746  1.00 83.86           C  
ANISOU 1325  CA  ALA A 198    16484   8204   7173    -30   1680   2974       C  
ATOM   1326  C   ALA A 198      -1.146  -6.752  56.608  1.00 82.95           C  
ANISOU 1326  C   ALA A 198    15954   8234   7328   -167   1634   2668       C  
ATOM   1327  O   ALA A 198      -1.071  -7.124  55.431  1.00 82.28           O  
ANISOU 1327  O   ALA A 198    15709   7988   7566   -247   1597   2566       O  
ATOM   1328  CB  ALA A 198      -2.158  -8.251  58.347  1.00 83.44           C  
ANISOU 1328  CB  ALA A 198    16500   8101   7101   -308   2052   3068       C  
ATOM   1329  N   TYR A 199      -1.485  -5.504  56.938  1.00 83.53           N  
ANISOU 1329  N   TYR A 199    15827   8620   7290   -189   1629   2496       N  
ATOM   1330  CA  TYR A 199      -1.747  -4.512  55.900  1.00 82.85           C  
ANISOU 1330  CA  TYR A 199    15315   8688   7476   -285   1565   2207       C  
ATOM   1331  C   TYR A 199      -0.486  -4.208  55.102  1.00 82.25           C  
ANISOU 1331  C   TYR A 199    15079   8629   7544    -88   1212   2074       C  
ATOM   1332  O   TYR A 199      -0.512  -4.189  53.867  1.00 81.49           O  
ANISOU 1332  O   TYR A 199    14739   8472   7753   -176   1170   1933       O  
ATOM   1333  CB  TYR A 199      -2.305  -3.231  56.519  1.00 84.36           C  
ANISOU 1333  CB  TYR A 199    15384   9168   7502   -300   1650   2066       C  
ATOM   1334  CG  TYR A 199      -2.613  -2.150  55.511  1.00 83.93           C  
ANISOU 1334  CG  TYR A 199    14919   9256   7714   -366   1596   1799       C  
ATOM   1335  CD1 TYR A 199      -3.767  -2.196  54.744  1.00 83.97           C  
ANISOU 1335  CD1 TYR A 199    14668   9255   7981   -598   1808   1745       C  
ATOM   1336  CD2 TYR A 199      -1.740  -1.089  55.317  1.00 83.72           C  
ANISOU 1336  CD2 TYR A 199    14762   9374   7675   -204   1324   1615       C  
ATOM   1337  CE1 TYR A 199      -4.047  -1.209  53.820  1.00 83.81           C  
ANISOU 1337  CE1 TYR A 199    14289   9372   8185   -626   1742   1535       C  
ATOM   1338  CE2 TYR A 199      -2.012  -0.098  54.396  1.00 83.44           C  
ANISOU 1338  CE2 TYR A 199    14393   9437   7873   -253   1288   1401       C  
ATOM   1339  CZ  TYR A 199      -3.168  -0.163  53.650  1.00 83.48           C  
ANISOU 1339  CZ  TYR A 199    14164   9435   8119   -444   1493   1373       C  
ATOM   1340  OH  TYR A 199      -3.445   0.821  52.729  1.00 83.45           O  
ANISOU 1340  OH  TYR A 199    13842   9536   8330   -462   1441   1194       O  
ATOM   1341  N   ALA A 200       0.631  -3.970  55.795  1.00 81.87           N  
ANISOU 1341  N   ALA A 200    15156   8683   7266    168    956   2121       N  
ATOM   1342  CA  ALA A 200       1.874  -3.629  55.109  1.00 81.74           C  
ANISOU 1342  CA  ALA A 200    14945   8725   7387    349    632   1999       C  
ATOM   1343  C   ALA A 200       2.286  -4.706  54.114  1.00 81.33           C  
ANISOU 1343  C   ALA A 200    14890   8404   7606    389    616   2062       C  
ATOM   1344  O   ALA A 200       2.880  -4.394  53.075  1.00 80.93           O  
ANISOU 1344  O   ALA A 200    14586   8376   7786    429    470   1900       O  
ATOM   1345  CB  ALA A 200       2.987  -3.387  56.127  1.00 83.63           C  
ANISOU 1345  CB  ALA A 200    15323   9132   7319    601    353   2078       C  
ATOM   1346  N   ILE A 201       1.978  -5.970  54.402  1.00 80.12           N  
ANISOU 1346  N   ILE A 201    15042   7977   7422    374    788   2291       N  
ATOM   1347  CA  ILE A 201       2.267  -7.042  53.453  1.00 79.84           C  
ANISOU 1347  CA  ILE A 201    15061   7629   7645    394    823   2330       C  
ATOM   1348  C   ILE A 201       1.240  -7.050  52.327  1.00 78.83           C  
ANISOU 1348  C   ILE A 201    14749   7414   7790     63   1018   2152       C  
ATOM   1349  O   ILE A 201       1.585  -6.912  51.148  1.00 78.27           O  
ANISOU 1349  O   ILE A 201    14464   7323   7952     53    929   1973       O  
ATOM   1350  CB  ILE A 201       2.315  -8.404  54.169  1.00 79.90           C  
ANISOU 1350  CB  ILE A 201    15508   7324   7526    495    949   2646       C  
ATOM   1351  CG1 ILE A 201       3.325  -8.386  55.320  1.00 81.11           C  
ANISOU 1351  CG1 ILE A 201    15840   7609   7372    845    717   2850       C  
ATOM   1352  CG2 ILE A 201       2.647  -9.512  53.178  1.00 79.79           C  
ANISOU 1352  CG2 ILE A 201    15592   6938   7785    533   1005   2662       C  
ATOM   1353  CD1 ILE A 201       4.742  -8.099  54.909  1.00 81.72           C  
ANISOU 1353  CD1 ILE A 201    15697   7817   7536   1159    379   2778       C  
ATOM   1354  N   ALA A 202      -0.041  -7.201  52.680  1.00 79.24           N  
ANISOU 1354  N   ALA A 202    14869   7438   7800   -217   1286   2201       N  
ATOM   1355  CA  ALA A 202      -1.085  -7.369  51.672  1.00 78.74           C  
ANISOU 1355  CA  ALA A 202    14633   7300   7985   -557   1461   2063       C  
ATOM   1356  C   ALA A 202      -1.202  -6.147  50.768  1.00 78.07           C  
ANISOU 1356  C   ALA A 202    14128   7490   8046   -609   1329   1798       C  
ATOM   1357  O   ALA A 202      -1.469  -6.280  49.568  1.00 77.58           O  
ANISOU 1357  O   ALA A 202    13899   7369   8209   -773   1328   1651       O  
ATOM   1358  CB  ALA A 202      -2.423  -7.664  52.348  1.00 78.65           C  
ANISOU 1358  CB  ALA A 202    14715   7273   7895   -844   1771   2180       C  
ATOM   1359  N   SER A 203      -1.015  -4.948  51.323  1.00 77.61           N  
ANISOU 1359  N   SER A 203    13922   7719   7847   -478   1221   1734       N  
ATOM   1360  CA  SER A 203      -1.092  -3.743  50.502  1.00 77.11           C  
ANISOU 1360  CA  SER A 203    13499   7880   7918   -506   1108   1506       C  
ATOM   1361  C   SER A 203       0.065  -3.680  49.513  1.00 76.47           C  
ANISOU 1361  C   SER A 203    13316   7759   7979   -358    876   1393       C  
ATOM   1362  O   SER A 203      -0.135  -3.398  48.326  1.00 75.84           O  
ANISOU 1362  O   SER A 203    13017   7706   8093   -471    847   1241       O  
ATOM   1363  CB  SER A 203      -1.112  -2.498  51.388  1.00 79.44           C  
ANISOU 1363  CB  SER A 203    13724   8434   8023   -399   1069   1456       C  
ATOM   1364  OG  SER A 203      -1.146  -1.317  50.607  1.00 79.11           O  
ANISOU 1364  OG  SER A 203    13376   8564   8119   -408    970   1255       O  
ATOM   1365  N   SER A 204       1.288  -3.937  49.985  1.00 75.50           N  
ANISOU 1365  N   SER A 204    13338   7595   7753    -96    711   1476       N  
ATOM   1366  CA  SER A 204       2.449  -3.886  49.102  1.00 75.41           C  
ANISOU 1366  CA  SER A 204    13200   7570   7883     64    518   1379       C  
ATOM   1367  C   SER A 204       2.371  -4.954  48.020  1.00 75.00           C  
ANISOU 1367  C   SER A 204    13216   7251   8031    -22    615   1359       C  
ATOM   1368  O   SER A 204       2.703  -4.696  46.857  1.00 74.56           O  
ANISOU 1368  O   SER A 204    12975   7215   8137    -42    552   1199       O  
ATOM   1369  CB  SER A 204       3.735  -4.046  49.912  1.00 76.04           C  
ANISOU 1369  CB  SER A 204    13392   7685   7816    371    322   1499       C  
ATOM   1370  OG  SER A 204       3.915  -2.961  50.805  1.00 76.59           O  
ANISOU 1370  OG  SER A 204    13393   8018   7688    422    196   1464       O  
ATOM   1371  N   ILE A 205       1.936  -6.161  48.382  1.00 75.82           N  
ANISOU 1371  N   ILE A 205    13613   7086   8110    -86    783   1516       N  
ATOM   1372  CA  ILE A 205       1.871  -7.251  47.413  1.00 75.67           C  
ANISOU 1372  CA  ILE A 205    13725   6761   8266   -183    891   1480       C  
ATOM   1373  C   ILE A 205       0.784  -6.980  46.380  1.00 74.93           C  
ANISOU 1373  C   ILE A 205    13438   6722   8309   -534    982   1295       C  
ATOM   1374  O   ILE A 205       1.055  -6.885  45.179  1.00 74.52           O  
ANISOU 1374  O   ILE A 205    13256   6666   8390   -570    922   1123       O  
ATOM   1375  CB  ILE A 205       1.648  -8.596  48.126  1.00 75.22           C  
ANISOU 1375  CB  ILE A 205    14074   6361   8146   -186   1066   1704       C  
ATOM   1376  CG1 ILE A 205       2.808  -8.899  49.078  1.00 76.22           C  
ANISOU 1376  CG1 ILE A 205    14387   6446   8126    213    937   1913       C  
ATOM   1377  CG2 ILE A 205       1.478  -9.714  47.112  1.00 75.18           C  
ANISOU 1377  CG2 ILE A 205    14246   5996   8324   -335   1206   1632       C  
ATOM   1378  CD1 ILE A 205       4.151  -9.009  48.395  1.00 76.77           C  
ANISOU 1378  CD1 ILE A 205    14366   6485   8319    523    770   1848       C  
ATOM   1379  N   VAL A 206      -0.462  -6.838  46.837  1.00 74.96           N  
ANISOU 1379  N   VAL A 206    13406   6805   8268   -792   1125   1336       N  
ATOM   1380  CA  VAL A 206      -1.588  -6.746  45.912  1.00 74.84           C  
ANISOU 1380  CA  VAL A 206    13199   6853   8386  -1139   1205   1193       C  
ATOM   1381  C   VAL A 206      -1.511  -5.471  45.080  1.00 74.29           C  
ANISOU 1381  C   VAL A 206    12770   7081   8375  -1109   1040   1014       C  
ATOM   1382  O   VAL A 206      -1.715  -5.500  43.860  1.00 74.06           O  
ANISOU 1382  O   VAL A 206    12620   7057   8461  -1261    998    863       O  
ATOM   1383  CB  VAL A 206      -2.919  -6.840  46.680  1.00 72.45           C  
ANISOU 1383  CB  VAL A 206    12882   6610   8034  -1398   1408   1297       C  
ATOM   1384  CG1 VAL A 206      -4.093  -6.613  45.741  1.00 72.89           C  
ANISOU 1384  CG1 VAL A 206    12649   6813   8233  -1743   1448   1155       C  
ATOM   1385  CG2 VAL A 206      -3.038  -8.192  47.364  1.00 73.00           C  
ANISOU 1385  CG2 VAL A 206    13345   6336   8056  -1479   1601   1484       C  
ATOM   1386  N   SER A 207      -1.207  -4.339  45.711  1.00 73.98           N  
ANISOU 1386  N   SER A 207    12588   7279   8244   -921    946   1027       N  
ATOM   1387  CA  SER A 207      -1.322  -3.056  45.030  1.00 73.65           C  
ANISOU 1387  CA  SER A 207    12231   7496   8258   -917    830    883       C  
ATOM   1388  C   SER A 207      -0.046  -2.611  44.326  1.00 72.96           C  
ANISOU 1388  C   SER A 207    12082   7430   8210   -717    649    784       C  
ATOM   1389  O   SER A 207      -0.131  -1.818  43.382  1.00 72.58           O  
ANISOU 1389  O   SER A 207    11818   7523   8237   -763    572    662       O  
ATOM   1390  CB  SER A 207      -1.758  -1.969  46.019  1.00 75.09           C  
ANISOU 1390  CB  SER A 207    12301   7899   8333   -848    858    920       C  
ATOM   1391  OG  SER A 207      -3.059  -2.230  46.515  1.00 76.12           O  
ANISOU 1391  OG  SER A 207    12409   8064   8451  -1048   1057    996       O  
ATOM   1392  N   PHE A 208       1.128  -3.082  44.750  1.00 70.59           N  
ANISOU 1392  N   PHE A 208    11949   7010   7863   -492    582    846       N  
ATOM   1393  CA  PHE A 208       2.373  -2.660  44.113  1.00 70.59           C  
ANISOU 1393  CA  PHE A 208    11842   7060   7917   -308    431    756       C  
ATOM   1394  C   PHE A 208       3.135  -3.807  43.462  1.00 70.97           C  
ANISOU 1394  C   PHE A 208    12047   6872   8048   -217    456    750       C  
ATOM   1395  O   PHE A 208       3.442  -3.726  42.268  1.00 70.77           O  
ANISOU 1395  O   PHE A 208    11925   6845   8118   -250    440    616       O  
ATOM   1396  CB  PHE A 208       3.277  -1.940  45.120  1.00 67.43           C  
ANISOU 1396  CB  PHE A 208    11408   6806   7406    -84    291    807       C  
ATOM   1397  CG  PHE A 208       4.596  -1.518  44.542  1.00 68.17           C  
ANISOU 1397  CG  PHE A 208    11355   6976   7572     82    143    725       C  
ATOM   1398  CD1 PHE A 208       4.678  -0.434  43.686  1.00 67.77           C  
ANISOU 1398  CD1 PHE A 208    11077   7074   7598      9     91    585       C  
ATOM   1399  CD2 PHE A 208       5.753  -2.219  44.841  1.00 69.64           C  
ANISOU 1399  CD2 PHE A 208    11619   7085   7757    319     69    805       C  
ATOM   1400  CE1 PHE A 208       5.890  -0.050  43.145  1.00 68.97           C  
ANISOU 1400  CE1 PHE A 208    11083   7301   7823    130    -13    517       C  
ATOM   1401  CE2 PHE A 208       6.968  -1.840  44.305  1.00 71.08           C  
ANISOU 1401  CE2 PHE A 208    11613   7368   8025    464    -47    732       C  
ATOM   1402  CZ  PHE A 208       7.037  -0.754  43.456  1.00 70.86           C  
ANISOU 1402  CZ  PHE A 208    11359   7492   8073    350    -78    583       C  
ATOM   1403  N   TYR A 209       3.457  -4.873  44.199  1.00 69.66           N  
ANISOU 1403  N   TYR A 209    12138   6491   7837    -88    511    897       N  
ATOM   1404  CA  TYR A 209       4.400  -5.856  43.672  1.00 70.47           C  
ANISOU 1404  CA  TYR A 209    12386   6362   8026     93    533    899       C  
ATOM   1405  C   TYR A 209       3.793  -6.685  42.547  1.00 69.98           C  
ANISOU 1405  C   TYR A 209    12455   6068   8065   -131    684    779       C  
ATOM   1406  O   TYR A 209       4.473  -6.979  41.558  1.00 70.37           O  
ANISOU 1406  O   TYR A 209    12507   6028   8203    -47    698    661       O  
ATOM   1407  CB  TYR A 209       4.919  -6.759  44.792  1.00 70.99           C  
ANISOU 1407  CB  TYR A 209    12713   6246   8014    334    544   1119       C  
ATOM   1408  CG  TYR A 209       5.939  -6.098  45.696  1.00 72.15           C  
ANISOU 1408  CG  TYR A 209    12728   6624   8060    619    341   1212       C  
ATOM   1409  CD1 TYR A 209       7.253  -5.925  45.275  1.00 73.58           C  
ANISOU 1409  CD1 TYR A 209    12734   6895   8328    876    212   1167       C  
ATOM   1410  CD2 TYR A 209       5.601  -5.671  46.974  1.00 72.18           C  
ANISOU 1410  CD2 TYR A 209    12781   6771   7871    618    282   1339       C  
ATOM   1411  CE1 TYR A 209       8.194  -5.329  46.091  1.00 75.09           C  
ANISOU 1411  CE1 TYR A 209    12771   7328   8430   1097     -1   1242       C  
ATOM   1412  CE2 TYR A 209       6.538  -5.074  47.800  1.00 73.46           C  
ANISOU 1412  CE2 TYR A 209    12838   7160   7911    845     69   1401       C  
ATOM   1413  CZ  TYR A 209       7.832  -4.906  47.352  1.00 74.94           C  
ANISOU 1413  CZ  TYR A 209    12824   7448   8202   1072    -88   1352       C  
ATOM   1414  OH  TYR A 209       8.767  -4.316  48.168  1.00 76.58           O  
ANISOU 1414  OH  TYR A 209    12894   7912   8292   1260   -327   1404       O  
ATOM   1415  N   VAL A 210       2.523  -7.072  42.672  1.00 70.49           N  
ANISOU 1415  N   VAL A 210    12627   6045   8112   -433    805    795       N  
ATOM   1416  CA  VAL A 210       1.890  -7.869  41.618  1.00 70.36           C  
ANISOU 1416  CA  VAL A 210    12739   5821   8175   -706    925    659       C  
ATOM   1417  C   VAL A 210       1.846  -7.120  40.291  1.00 69.88           C  
ANISOU 1417  C   VAL A 210    12436   5963   8152   -822    840    447       C  
ATOM   1418  O   VAL A 210       2.324  -7.667  39.283  1.00 70.18           O  
ANISOU 1418  O   VAL A 210    12587   5841   8236   -810    883    311       O  
ATOM   1419  CB  VAL A 210       0.507  -8.366  42.079  1.00 71.40           C  
ANISOU 1419  CB  VAL A 210    12976   5865   8287  -1048   1060    725       C  
ATOM   1420  CG1 VAL A 210      -0.221  -9.036  40.925  1.00 71.52           C  
ANISOU 1420  CG1 VAL A 210    13071   5730   8374  -1399   1141    546       C  
ATOM   1421  CG2 VAL A 210       0.662  -9.343  43.234  1.00 72.01           C  
ANISOU 1421  CG2 VAL A 210    13389   5655   8316   -933   1185    945       C  
ATOM   1422  N   PRO A 211       1.330  -5.885  40.207  1.00 72.13           N  
ANISOU 1422  N   PRO A 211    12417   6581   8409   -913    734    415       N  
ATOM   1423  CA  PRO A 211       1.390  -5.181  38.916  1.00 71.83           C  
ANISOU 1423  CA  PRO A 211    12185   6720   8388   -987    650    247       C  
ATOM   1424  C   PRO A 211       2.806  -4.829  38.491  1.00 72.07           C  
ANISOU 1424  C   PRO A 211    12165   6780   8439   -701    593    199       C  
ATOM   1425  O   PRO A 211       3.070  -4.751  37.286  1.00 72.17           O  
ANISOU 1425  O   PRO A 211    12149   6816   8457   -748    592     55       O  
ATOM   1426  CB  PRO A 211       0.540  -3.927  39.155  1.00 71.04           C  
ANISOU 1426  CB  PRO A 211    11796   6935   8260  -1086    564    277       C  
ATOM   1427  CG  PRO A 211       0.619  -3.697  40.613  1.00 71.07           C  
ANISOU 1427  CG  PRO A 211    11817   6962   8222   -936    579    434       C  
ATOM   1428  CD  PRO A 211       0.678  -5.058  41.242  1.00 71.54           C  
ANISOU 1428  CD  PRO A 211    12184   6722   8276   -934    704    530       C  
ATOM   1429  N   LEU A 212       3.721  -4.609  39.440  1.00 69.33           N  
ANISOU 1429  N   LEU A 212    11794   6457   8091   -421    544    316       N  
ATOM   1430  CA  LEU A 212       5.113  -4.344  39.088  1.00 70.36           C  
ANISOU 1430  CA  LEU A 212    11831   6636   8266   -159    496    279       C  
ATOM   1431  C   LEU A 212       5.744  -5.550  38.404  1.00 71.37           C  
ANISOU 1431  C   LEU A 212    12175   6488   8453    -51    624    215       C  
ATOM   1432  O   LEU A 212       6.329  -5.431  37.321  1.00 71.98           O  
ANISOU 1432  O   LEU A 212    12193   6594   8561    -15    661     81       O  
ATOM   1433  CB  LEU A 212       5.911  -3.967  40.337  1.00 67.75           C  
ANISOU 1433  CB  LEU A 212    11424   6405   7913     95    389    422       C  
ATOM   1434  CG  LEU A 212       7.378  -3.594  40.104  1.00 69.69           C  
ANISOU 1434  CG  LEU A 212    11493   6764   8221    352    314    397       C  
ATOM   1435  CD1 LEU A 212       7.482  -2.304  39.310  1.00 69.51           C  
ANISOU 1435  CD1 LEU A 212    11214   6982   8215    238    256    278       C  
ATOM   1436  CD2 LEU A 212       8.152  -3.492  41.410  1.00 71.23           C  
ANISOU 1436  CD2 LEU A 212    11642   7045   8376    593    183    547       C  
ATOM   1437  N   VAL A 213       5.644  -6.724  39.034  1.00 72.11           N  
ANISOU 1437  N   VAL A 213    12549   6292   8558     12    719    313       N  
ATOM   1438  CA  VAL A 213       6.227  -7.933  38.458  1.00 73.12           C  
ANISOU 1438  CA  VAL A 213    12935   6094   8752    146    872    256       C  
ATOM   1439  C   VAL A 213       5.589  -8.241  37.110  1.00 72.56           C  
ANISOU 1439  C   VAL A 213    12975   5928   8666   -148    972     34       C  
ATOM   1440  O   VAL A 213       6.270  -8.662  36.166  1.00 73.43           O  
ANISOU 1440  O   VAL A 213    13177   5916   8808    -43   1077   -105       O  
ATOM   1441  CB  VAL A 213       6.093  -9.110  39.441  1.00 67.15           C  
ANISOU 1441  CB  VAL A 213    12505   5005   8004    244    965    429       C  
ATOM   1442  CG1 VAL A 213       6.552 -10.405  38.793  1.00 68.06           C  
ANISOU 1442  CG1 VAL A 213    12947   4714   8199    364   1157    354       C  
ATOM   1443  CG2 VAL A 213       6.905  -8.836  40.695  1.00 68.09           C  
ANISOU 1443  CG2 VAL A 213    12524   5247   8101    581    838    650       C  
ATOM   1444  N   ILE A 214       4.277  -8.025  36.990  1.00 72.86           N  
ANISOU 1444  N   ILE A 214    12996   6042   8644   -518    941     -8       N  
ATOM   1445  CA  ILE A 214       3.619  -8.193  35.697  1.00 72.63           C  
ANISOU 1445  CA  ILE A 214    13030   6000   8567   -828    978   -221       C  
ATOM   1446  C   ILE A 214       4.150  -7.171  34.699  1.00 72.72           C  
ANISOU 1446  C   ILE A 214    12800   6295   8535   -772    899   -334       C  
ATOM   1447  O   ILE A 214       4.507  -7.513  33.567  1.00 73.33           O  
ANISOU 1447  O   ILE A 214    12999   6292   8572   -795    983   -509       O  
ATOM   1448  CB  ILE A 214       2.091  -8.099  35.848  1.00 70.61           C  
ANISOU 1448  CB  ILE A 214    12726   5835   8268  -1228    929   -216       C  
ATOM   1449  CG1 ILE A 214       1.569  -9.264  36.691  1.00 70.87           C  
ANISOU 1449  CG1 ILE A 214    13049   5536   8342  -1338   1060   -118       C  
ATOM   1450  CG2 ILE A 214       1.421  -8.095  34.484  1.00 70.76           C  
ANISOU 1450  CG2 ILE A 214    12744   5934   8208  -1552    898   -431       C  
ATOM   1451  CD1 ILE A 214       0.121  -9.118  37.103  1.00 70.67           C  
ANISOU 1451  CD1 ILE A 214    12912   5640   8300  -1704   1034    -68       C  
ATOM   1452  N   MET A 215       4.216  -5.901  35.109  1.00 70.42           N  
ANISOU 1452  N   MET A 215    12196   6322   8239   -702    756   -237       N  
ATOM   1453  CA  MET A 215       4.723  -4.850  34.229  1.00 70.63           C  
ANISOU 1453  CA  MET A 215    12005   6603   8228   -659    694   -312       C  
ATOM   1454  C   MET A 215       6.122  -5.173  33.721  1.00 72.15           C  
ANISOU 1454  C   MET A 215    12244   6704   8466   -389    807   -377       C  
ATOM   1455  O   MET A 215       6.383  -5.138  32.514  1.00 72.74           O  
ANISOU 1455  O   MET A 215    12355   6807   8477   -440    878   -526       O  
ATOM   1456  CB  MET A 215       4.738  -3.509  34.962  1.00 70.59           C  
ANISOU 1456  CB  MET A 215    11708   6876   8239   -587    552   -184       C  
ATOM   1457  CG  MET A 215       5.209  -2.349  34.107  1.00 70.87           C  
ANISOU 1457  CG  MET A 215    11539   7146   8244   -569    500   -235       C  
ATOM   1458  SD  MET A 215       5.370  -0.825  35.052  1.00 70.32           S  
ANISOU 1458  SD  MET A 215    11189   7319   8210   -476    361   -105       S  
ATOM   1459  CE  MET A 215       6.883  -1.148  35.951  1.00 72.25           C  
ANISOU 1459  CE  MET A 215    11402   7501   8549   -162    373    -42       C  
ATOM   1460  N   VAL A 216       7.041  -5.482  34.638  1.00 73.02           N  
ANISOU 1460  N   VAL A 216    12341   6726   8676    -87    827   -260       N  
ATOM   1461  CA  VAL A 216       8.431  -5.697  34.253  1.00 75.07           C  
ANISOU 1461  CA  VAL A 216    12558   6955   9011    213    930   -296       C  
ATOM   1462  C   VAL A 216       8.575  -6.945  33.389  1.00 75.63           C  
ANISOU 1462  C   VAL A 216    12948   6711   9076    237   1142   -448       C  
ATOM   1463  O   VAL A 216       9.401  -6.976  32.470  1.00 76.98           O  
ANISOU 1463  O   VAL A 216    13099   6898   9253    364   1274   -567       O  
ATOM   1464  CB  VAL A 216       9.316  -5.761  35.512  1.00 73.79           C  
ANISOU 1464  CB  VAL A 216    12279   6805   8951    537    861   -114       C  
ATOM   1465  CG1 VAL A 216      10.757  -6.078  35.145  1.00 76.38           C  
ANISOU 1465  CG1 VAL A 216    12515   7118   9387    875    971   -137       C  
ATOM   1466  CG2 VAL A 216       9.239  -4.445  36.274  1.00 73.52           C  
ANISOU 1466  CG2 VAL A 216    11954   7085   8897    487    659    -13       C  
ATOM   1467  N   PHE A 217       7.771  -7.981  33.641  1.00 77.06           N  
ANISOU 1467  N   PHE A 217    13445   6593   9242     98   1203   -459       N  
ATOM   1468  CA  PHE A 217       7.879  -9.191  32.831  1.00 77.65           C  
ANISOU 1468  CA  PHE A 217    13880   6316   9306     97   1419   -630       C  
ATOM   1469  C   PHE A 217       7.179  -9.042  31.484  1.00 77.09           C  
ANISOU 1469  C   PHE A 217    13902   6313   9077   -255   1442   -865       C  
ATOM   1470  O   PHE A 217       7.702  -9.495  30.460  1.00 78.01           O  
ANISOU 1470  O   PHE A 217    14192   6306   9143   -198   1616  -1052       O  
ATOM   1471  CB  PHE A 217       7.317 -10.396  33.586  1.00 82.86           C  
ANISOU 1471  CB  PHE A 217    14886   6584  10013     53   1494   -558       C  
ATOM   1472  CG  PHE A 217       7.363 -11.672  32.795  1.00 83.46           C  
ANISOU 1472  CG  PHE A 217    15392   6235  10083     23   1731   -751       C  
ATOM   1473  CD1 PHE A 217       8.561 -12.339  32.598  1.00 85.01           C  
ANISOU 1473  CD1 PHE A 217    15720   6201  10377    434   1927   -775       C  
ATOM   1474  CD2 PHE A 217       6.210 -12.198  32.234  1.00 82.68           C  
ANISOU 1474  CD2 PHE A 217    15561   5970   9883   -419   1762   -922       C  
ATOM   1475  CE1 PHE A 217       8.608 -13.510  31.862  1.00 85.55           C  
ANISOU 1475  CE1 PHE A 217    16229   5839  10438    423   2177   -974       C  
ATOM   1476  CE2 PHE A 217       6.251 -13.367  31.498  1.00 83.33           C  
ANISOU 1476  CE2 PHE A 217    16083   5634   9945   -480   1985  -1134       C  
ATOM   1477  CZ  PHE A 217       7.450 -14.025  31.312  1.00 84.67           C  
ANISOU 1477  CZ  PHE A 217    16429   5534  10208    -50   2206  -1166       C  
ATOM   1478  N   VAL A 218       5.999  -8.417  31.462  1.00 75.79           N  
ANISOU 1478  N   VAL A 218    13624   6355   8818   -606   1270   -857       N  
ATOM   1479  CA  VAL A 218       5.258  -8.285  30.210  1.00 75.58           C  
ANISOU 1479  CA  VAL A 218    13673   6429   8615   -948   1243  -1058       C  
ATOM   1480  C   VAL A 218       5.919  -7.269  29.287  1.00 76.19           C  
ANISOU 1480  C   VAL A 218    13544   6804   8601   -858   1228  -1110       C  
ATOM   1481  O   VAL A 218       5.909  -7.440  28.062  1.00 76.74           O  
ANISOU 1481  O   VAL A 218    13774   6876   8509   -991   1304  -1307       O  
ATOM   1482  CB  VAL A 218       3.786  -7.923  30.492  1.00 73.82           C  
ANISOU 1482  CB  VAL A 218    13341   6371   8339  -1319   1053  -1006       C  
ATOM   1483  CG1 VAL A 218       3.047  -7.599  29.204  1.00 74.05           C  
ANISOU 1483  CG1 VAL A 218    13370   6597   8168  -1647    960  -1180       C  
ATOM   1484  CG2 VAL A 218       3.090  -9.069  31.212  1.00 73.59           C  
ANISOU 1484  CG2 VAL A 218    13566   6016   8380  -1481   1120   -987       C  
ATOM   1485  N   TYR A 219       6.511  -6.208  29.836  1.00 74.62           N  
ANISOU 1485  N   TYR A 219    13014   6852   8488   -653   1141   -943       N  
ATOM   1486  CA  TYR A 219       7.079  -5.181  28.971  1.00 75.38           C  
ANISOU 1486  CA  TYR A 219    12921   7220   8502   -613   1140   -973       C  
ATOM   1487  C   TYR A 219       8.505  -5.497  28.543  1.00 77.22           C  
ANISOU 1487  C   TYR A 219    13176   7372   8793   -311   1362  -1041       C  
ATOM   1488  O   TYR A 219       8.942  -5.014  27.490  1.00 78.12           O  
ANISOU 1488  O   TYR A 219    13255   7635   8791   -327   1449  -1131       O  
ATOM   1489  CB  TYR A 219       7.042  -3.808  29.649  1.00 71.35           C  
ANISOU 1489  CB  TYR A 219    12057   6999   8053   -580    960   -786       C  
ATOM   1490  CG  TYR A 219       7.178  -2.677  28.655  1.00 71.90           C  
ANISOU 1490  CG  TYR A 219    11984   7336   8001   -659    931   -804       C  
ATOM   1491  CD1 TYR A 219       6.092  -2.293  27.878  1.00 71.28           C  
ANISOU 1491  CD1 TYR A 219    11947   7394   7741   -937    815   -843       C  
ATOM   1492  CD2 TYR A 219       8.384  -2.016  28.466  1.00 73.49           C  
ANISOU 1492  CD2 TYR A 219    12006   7655   8261   -465   1022   -770       C  
ATOM   1493  CE1 TYR A 219       6.194  -1.275  26.957  1.00 71.99           C  
ANISOU 1493  CE1 TYR A 219    11946   7711   7696   -993    788   -828       C  
ATOM   1494  CE2 TYR A 219       8.496  -0.993  27.540  1.00 74.14           C  
ANISOU 1494  CE2 TYR A 219    11996   7952   8222   -557   1022   -767       C  
ATOM   1495  CZ  TYR A 219       7.395  -0.628  26.791  1.00 73.27           C  
ANISOU 1495  CZ  TYR A 219    11973   7952   7915   -809    906   -787       C  
ATOM   1496  OH  TYR A 219       7.488   0.386  25.869  1.00 74.01           O  
ANISOU 1496  OH  TYR A 219    12009   8246   7868   -881    904   -751       O  
ATOM   1497  N   SER A 220       9.242  -6.285  29.331  1.00 78.27           N  
ANISOU 1497  N   SER A 220    13355   7286   9098    -20   1464   -983       N  
ATOM   1498  CA  SER A 220      10.467  -6.894  28.824  1.00 80.16           C  
ANISOU 1498  CA  SER A 220    13665   7392   9398    280   1717  -1076       C  
ATOM   1499  C   SER A 220      10.171  -7.873  27.700  1.00 80.06           C  
ANISOU 1499  C   SER A 220    14061   7125   9233    149   1918  -1328       C  
ATOM   1500  O   SER A 220      11.033  -8.113  26.848  1.00 81.42           O  
ANISOU 1500  O   SER A 220    14301   7262   9372    316   2155  -1463       O  
ATOM   1501  CB  SER A 220      11.218  -7.601  29.951  1.00 79.15           C  
ANISOU 1501  CB  SER A 220    13513   7074   9485    645   1758   -935       C  
ATOM   1502  OG  SER A 220      10.500  -8.730  30.417  1.00 78.08           O  
ANISOU 1502  OG  SER A 220    13727   6581   9360    581   1781   -941       O  
ATOM   1503  N   ARG A 221       8.959  -8.426  27.680  1.00 82.81           N  
ANISOU 1503  N   ARG A 221    14678   7307   9480   -167   1835  -1404       N  
ATOM   1504  CA  ARG A 221       8.517  -9.275  26.583  1.00 82.82           C  
ANISOU 1504  CA  ARG A 221    15083   7090   9295   -388   1979  -1675       C  
ATOM   1505  C   ARG A 221       8.235  -8.458  25.330  1.00 82.86           C  
ANISOU 1505  C   ARG A 221    15041   7403   9041   -631   1927  -1801       C  
ATOM   1506  O   ARG A 221       8.289  -9.001  24.221  1.00 83.43           O  
ANISOU 1506  O   ARG A 221    15421   7360   8920   -730   2094  -2045       O  
ATOM   1507  CB  ARG A 221       7.264 -10.042  27.009  1.00 86.07           C  
ANISOU 1507  CB  ARG A 221    15747   7267   9689   -708   1876  -1706       C  
ATOM   1508  CG  ARG A 221       6.811 -11.143  26.081  1.00 86.32           C  
ANISOU 1508  CG  ARG A 221    16254   6985   9560   -957   2026  -2002       C  
ATOM   1509  CD  ARG A 221       7.750 -12.329  26.170  1.00 87.37           C  
ANISOU 1509  CD  ARG A 221    16714   6660   9823   -617   2342  -2087       C  
ATOM   1510  NE  ARG A 221       7.286 -13.450  25.364  1.00 87.64           N  
ANISOU 1510  NE  ARG A 221    17249   6338   9713   -872   2498  -2382       N  
ATOM   1511  CZ  ARG A 221       7.560 -13.595  24.074  1.00 88.57           C  
ANISOU 1511  CZ  ARG A 221    17499   6528   9625   -927   2625  -2610       C  
ATOM   1512  NH1 ARG A 221       8.297 -12.687  23.451  1.00 88.94           N  
ANISOU 1512  NH1 ARG A 221    17392   6839   9562   -760   2698  -2655       N  
ATOM   1513  NH2 ARG A 221       7.099 -14.645  23.409  1.00 92.15           N  
ANISOU 1513  NH2 ARG A 221    18247   6792   9973  -1159   2689  -2789       N  
ATOM   1514  N   VAL A 222       7.948  -7.163  25.487  1.00 79.89           N  
ANISOU 1514  N   VAL A 222    14313   7400   8642   -719   1708  -1635       N  
ATOM   1515  CA  VAL A 222       7.697  -6.296  24.339  1.00 80.09           C  
ANISOU 1515  CA  VAL A 222    14290   7724   8416   -917   1646  -1699       C  
ATOM   1516  C   VAL A 222       9.001  -5.927  23.645  1.00 81.58           C  
ANISOU 1516  C   VAL A 222    14408   8010   8580   -667   1884  -1735       C  
ATOM   1517  O   VAL A 222       9.131  -6.073  22.423  1.00 82.17           O  
ANISOU 1517  O   VAL A 222    14703   8110   8409   -759   2030  -1920       O  
ATOM   1518  CB  VAL A 222       6.917  -5.039  24.772  1.00 77.32           C  
ANISOU 1518  CB  VAL A 222    13613   7696   8068  -1068   1351  -1491       C  
ATOM   1519  CG1 VAL A 222       6.768  -4.072  23.608  1.00 77.80           C  
ANISOU 1519  CG1 VAL A 222    13626   8057   7876  -1214   1293  -1506       C  
ATOM   1520  CG2 VAL A 222       5.558  -5.424  25.330  1.00 76.08           C  
ANISOU 1520  CG2 VAL A 222    13507   7480   7920  -1338   1148  -1471       C  
ATOM   1521  N   PHE A 223       9.978  -5.425  24.409  1.00 79.61           N  
ANISOU 1521  N   PHE A 223    13841   7838   8568   -367   1926  -1561       N  
ATOM   1522  CA  PHE A 223      11.292  -5.131  23.842  1.00 81.37           C  
ANISOU 1522  CA  PHE A 223    13940   8162   8815   -125   2178  -1585       C  
ATOM   1523  C   PHE A 223      11.884  -6.334  23.123  1.00 82.23           C  
ANISOU 1523  C   PHE A 223    14378   7999   8867     31   2509  -1819       C  
ATOM   1524  O   PHE A 223      12.609  -6.174  22.134  1.00 83.32           O  
ANISOU 1524  O   PHE A 223    14547   8232   8879    103   2754  -1926       O  
ATOM   1525  CB  PHE A 223      12.264  -4.659  24.929  1.00 77.42           C  
ANISOU 1525  CB  PHE A 223    13045   7754   8617    172   2158  -1382       C  
ATOM   1526  CG  PHE A 223      12.075  -3.228  25.348  1.00 77.26           C  
ANISOU 1526  CG  PHE A 223    12690   8035   8629     50   1929  -1189       C  
ATOM   1527  CD1 PHE A 223      11.310  -2.359  24.587  1.00 76.39           C  
ANISOU 1527  CD1 PHE A 223    12616   8112   8296   -234   1816  -1184       C  
ATOM   1528  CD2 PHE A 223      12.691  -2.745  26.491  1.00 78.22           C  
ANISOU 1528  CD2 PHE A 223    12477   8247   8995    231   1827  -1015       C  
ATOM   1529  CE1 PHE A 223      11.149  -1.039  24.970  1.00 76.29           C  
ANISOU 1529  CE1 PHE A 223    12334   8326   8328   -319   1634  -1004       C  
ATOM   1530  CE2 PHE A 223      12.534  -1.428  26.878  1.00 78.24           C  
ANISOU 1530  CE2 PHE A 223    12217   8485   9025    108   1639   -866       C  
ATOM   1531  CZ  PHE A 223      11.762  -0.574  26.117  1.00 77.18           C  
ANISOU 1531  CZ  PHE A 223    12143   8490   8690   -158   1557   -860       C  
ATOM   1532  N   GLN A 224      11.591  -7.542  23.602  1.00 86.64           N  
ANISOU 1532  N   GLN A 224    15207   8202   9512     88   2548  -1899       N  
ATOM   1533  CA  GLN A 224      12.123  -8.744  22.978  1.00 87.49           C  
ANISOU 1533  CA  GLN A 224    15678   7981   9581    258   2883  -2132       C  
ATOM   1534  C   GLN A 224      11.398  -9.094  21.684  1.00 87.02           C  
ANISOU 1534  C   GLN A 224    16039   7863   9160    -83   2947  -2414       C  
ATOM   1535  O   GLN A 224      11.978  -9.768  20.825  1.00 87.94           O  
ANISOU 1535  O   GLN A 224    16447   7806   9162     38   3272  -2643       O  
ATOM   1536  CB  GLN A 224      12.056  -9.913  23.966  1.00 89.38           C  
ANISOU 1536  CB  GLN A 224    16104   7814  10043    438   2910  -2103       C  
ATOM   1537  CG  GLN A 224      12.770 -11.173  23.509  1.00 90.47           C  
ANISOU 1537  CG  GLN A 224    16605   7554  10216    719   3289  -2308       C  
ATOM   1538  CD  GLN A 224      12.794 -12.249  24.578  1.00 90.44           C  
ANISOU 1538  CD  GLN A 224    16772   7134  10457    952   3316  -2215       C  
ATOM   1539  OE1 GLN A 224      12.243 -12.074  25.666  1.00 89.52           O  
ANISOU 1539  OE1 GLN A 224    16512   7040  10461    875   3050  -2001       O  
ATOM   1540  NE2 GLN A 224      13.440 -13.369  24.274  1.00 91.63           N  
ANISOU 1540  NE2 GLN A 224    17252   6890  10675   1254   3658  -2368       N  
ATOM   1541  N   GLU A 225      10.156  -8.639  21.516  1.00 88.43           N  
ANISOU 1541  N   GLU A 225    16249   8204   9148   -496   2645  -2406       N  
ATOM   1542  CA  GLU A 225       9.453  -8.871  20.259  1.00 88.28           C  
ANISOU 1542  CA  GLU A 225    16591   8204   8747   -845   2648  -2663       C  
ATOM   1543  C   GLU A 225       9.803  -7.815  19.219  1.00 88.87           C  
ANISOU 1543  C   GLU A 225    16544   8655   8566   -889   2686  -2650       C  
ATOM   1544  O   GLU A 225       9.910  -8.129  18.029  1.00 89.45           O  
ANISOU 1544  O   GLU A 225    16946   8715   8325   -990   2870  -2890       O  
ATOM   1545  CB  GLU A 225       7.944  -8.909  20.494  1.00 92.13           C  
ANISOU 1545  CB  GLU A 225    17140   8726   9139  -1271   2297  -2657       C  
ATOM   1546  CG  GLU A 225       7.487 -10.111  21.290  1.00 91.65           C  
ANISOU 1546  CG  GLU A 225    17315   8248   9259  -1320   2309  -2721       C  
ATOM   1547  CD  GLU A 225       7.732 -11.414  20.554  1.00 92.48           C  
ANISOU 1547  CD  GLU A 225    17894   7985   9260  -1327   2583  -3016       C  
ATOM   1548  OE1 GLU A 225       7.678 -11.411  19.306  1.00 93.72           O  
ANISOU 1548  OE1 GLU A 225    18188   8294   9127  -1486   2621  -3183       O  
ATOM   1549  OE2 GLU A 225       7.983 -12.440  21.220  1.00 93.01           O  
ANISOU 1549  OE2 GLU A 225    18088   7682   9571  -1145   2718  -2994       O  
ATOM   1550  N   ALA A 226       9.978  -6.562  19.646  1.00 86.00           N  
ANISOU 1550  N   ALA A 226    15746   8612   8317   -827   2526  -2375       N  
ATOM   1551  CA  ALA A 226      10.402  -5.519  18.718  1.00 86.64           C  
ANISOU 1551  CA  ALA A 226    15716   9019   8183   -851   2595  -2323       C  
ATOM   1552  C   ALA A 226      11.747  -5.860  18.089  1.00 88.06           C  
ANISOU 1552  C   ALA A 226    15975   9129   8356   -566   3035  -2453       C  
ATOM   1553  O   ALA A 226      11.955  -5.643  16.889  1.00 88.58           O  
ANISOU 1553  O   ALA A 226    16230   9329   8095   -654   3208  -2575       O  
ATOM   1554  CB  ALA A 226      10.470  -4.173  19.438  1.00 81.67           C  
ANISOU 1554  CB  ALA A 226    14623   8667   7743   -806   2387  -2005       C  
ATOM   1555  N   LYS A 227      12.671  -6.406  18.883  1.00 87.80           N  
ANISOU 1555  N   LYS A 227    15795   8899   8667   -207   3227  -2420       N  
ATOM   1556  CA  LYS A 227      13.978  -6.778  18.353  1.00 89.34           C  
ANISOU 1556  CA  LYS A 227    16007   9035   8902    112   3667  -2534       C  
ATOM   1557  C   LYS A 227      13.893  -8.038  17.502  1.00 89.53           C  
ANISOU 1557  C   LYS A 227    16577   8740   8699    102   3941  -2879       C  
ATOM   1558  O   LYS A 227      14.563  -8.140  16.467  1.00 90.86           O  
ANISOU 1558  O   LYS A 227    16912   8948   8664    188   4293  -3048       O  
ATOM   1559  CB  LYS A 227      14.969  -6.967  19.500  1.00 92.01           C  
ANISOU 1559  CB  LYS A 227    15979   9292   9688    522   3749  -2371       C  
ATOM   1560  CG  LYS A 227      16.390  -7.263  19.057  1.00 93.83           C  
ANISOU 1560  CG  LYS A 227    16107   9518  10024    899   4199  -2447       C  
ATOM   1561  CD  LYS A 227      17.325  -7.335  20.251  1.00 95.03           C  
ANISOU 1561  CD  LYS A 227    15820   9667  10621   1294   4201  -2245       C  
ATOM   1562  CE  LYS A 227      18.749  -7.637  19.823  1.00 96.97           C  
ANISOU 1562  CE  LYS A 227    15894   9947  11005   1695   4650  -2307       C  
ATOM   1563  NZ  LYS A 227      19.668  -7.692  20.993  1.00 98.39           N  
ANISOU 1563  NZ  LYS A 227    15597  10175  11612   2085   4606  -2094       N  
ATOM   1564  N   ARG A 228      13.080  -9.013  17.921  1.00 89.72           N  
ANISOU 1564  N   ARG A 228    16907   8433   8750    -15   3809  -2997       N  
ATOM   1565  CA  ARG A 228      12.940 -10.235  17.137  1.00 92.59           C  
ANISOU 1565  CA  ARG A 228    17713   8509   8959    -73   3978  -3267       C  
ATOM   1566  C   ARG A 228      12.211  -9.964  15.828  1.00 94.31           C  
ANISOU 1566  C   ARG A 228    18147   8952   8733   -478   3853  -3401       C  
ATOM   1567  O   ARG A 228      12.529 -10.566  14.796  1.00 98.89           O  
ANISOU 1567  O   ARG A 228    18963   9473   9137   -469   4060  -3583       O  
ATOM   1568  CB  ARG A 228      12.184 -11.302  17.931  1.00 96.00           C  
ANISOU 1568  CB  ARG A 228    18336   8571   9569   -160   3807  -3287       C  
ATOM   1569  CG  ARG A 228      12.214 -12.678  17.274  1.00101.37           C  
ANISOU 1569  CG  ARG A 228    19385   8932  10198   -162   3983  -3501       C  
ATOM   1570  CD  ARG A 228      11.221 -13.641  17.904  1.00101.92           C  
ANISOU 1570  CD  ARG A 228    19673   8682  10369   -384   3783  -3520       C  
ATOM   1571  NE  ARG A 228       9.852 -13.245  17.587  1.00100.43           N  
ANISOU 1571  NE  ARG A 228    19541   8695   9923   -914   3424  -3559       N  
ATOM   1572  CZ  ARG A 228       9.249 -13.519  16.432  1.00103.71           C  
ANISOU 1572  CZ  ARG A 228    20201   9193  10011  -1252   3362  -3760       C  
ATOM   1573  NH1 ARG A 228       8.003 -13.118  16.218  1.00102.50           N  
ANISOU 1573  NH1 ARG A 228    20030   9265   9651  -1706   3005  -3764       N  
ATOM   1574  NH2 ARG A 228       9.894 -14.190  15.485  1.00108.59           N  
ANISOU 1574  NH2 ARG A 228    21071   9682  10508  -1128   3651  -3957       N  
ATOM   1575  N   GLN A 229      11.228  -9.069  15.854  1.00 92.25           N  
ANISOU 1575  N   GLN A 229    17809   8957   8285   -818   3505  -3306       N  
ATOM   1576  CA  GLN A 229      10.401  -8.774  14.686  1.00 93.90           C  
ANISOU 1576  CA  GLN A 229    18190   9413   8073  -1202   3307  -3389       C  
ATOM   1577  C   GLN A 229      10.949  -7.568  13.926  1.00 93.45           C  
ANISOU 1577  C   GLN A 229    17991   9733   7781  -1166   3410  -3283       C  
ATOM   1578  O   GLN A 229      10.298  -6.532  13.780  1.00 91.33           O  
ANISOU 1578  O   GLN A 229    17614   9774   7314  -1391   3140  -3136       O  
ATOM   1579  CB  GLN A 229       8.954  -8.549  15.113  1.00 91.66           C  
ANISOU 1579  CB  GLN A 229    17879   9222   7726  -1583   2850  -3323       C  
ATOM   1580  CG  GLN A 229       8.290  -9.782  15.694  1.00 92.96           C  
ANISOU 1580  CG  GLN A 229    18212   9034   8076  -1702   2754  -3429       C  
ATOM   1581  CD  GLN A 229       6.881  -9.513  16.176  1.00 90.72           C  
ANISOU 1581  CD  GLN A 229    17827   8877   7764  -2077   2324  -3345       C  
ATOM   1582  OE1 GLN A 229       6.410  -8.378  16.148  1.00 88.24           O  
ANISOU 1582  OE1 GLN A 229    17308   8911   7310  -2212   2081  -3195       O  
ATOM   1583  NE2 GLN A 229       6.200 -10.561  16.626  1.00 92.25           N  
ANISOU 1583  NE2 GLN A 229    18157   8793   8100  -2244   2240  -3426       N  
ATOM   1584  N   LEU A 230      12.179  -7.715  13.444  1.00 94.99           N  
ANISOU 1584  N   LEU A 230    18178   9901   8014   -869   3820  -3338       N  
ATOM   1585  CA  LEU A 230      12.801  -6.748  12.546  1.00 95.91           C  
ANISOU 1585  CA  LEU A 230    18202  10344   7894   -844   3996  -3256       C  
ATOM   1586  C   LEU A 230      13.054  -7.440  11.216  1.00101.66           C  
ANISOU 1586  C   LEU A 230    19246  11039   8343   -875   4206  -3476       C  
ATOM   1587  O   LEU A 230      13.926  -8.310  11.118  1.00104.95           O  
ANISOU 1587  O   LEU A 230    19734  11225   8918   -597   4552  -3619       O  
ATOM   1588  CB  LEU A 230      14.088  -6.176  13.137  1.00 94.37           C  
ANISOU 1588  CB  LEU A 230    17651  10209   7996   -482   4322  -3107       C  
ATOM   1589  CG  LEU A 230      13.858  -5.153  14.249  1.00 88.96           C  
ANISOU 1589  CG  LEU A 230    16556   9681   7566   -496   4042  -2810       C  
ATOM   1590  CD1 LEU A 230      15.158  -4.749  14.898  1.00 88.12           C  
ANISOU 1590  CD1 LEU A 230    15978   9640   7866   -143   4274  -2629       C  
ATOM   1591  CD2 LEU A 230      13.178  -3.935  13.663  1.00 87.46           C  
ANISOU 1591  CD2 LEU A 230    16328   9836   7068   -801   3780  -2635       C  
ATOM   2861  N   LYS A 263      18.848  -1.065  17.008  1.00 90.64           N  
ANISOU 2861  N   LYS A 263    14242  10808   9388    359   4498  -1702       N  
ATOM   2862  CA  LYS A 263      18.089  -0.942  18.247  1.00 89.81           C  
ANISOU 2862  CA  LYS A 263    14014  10619   9491    310   4044  -1575       C  
ATOM   2863  C   LYS A 263      17.516   0.459  18.393  1.00 88.90           C  
ANISOU 2863  C   LYS A 263    13770  10691   9318     18   3755  -1354       C  
ATOM   2864  O   LYS A 263      18.249   1.451  18.337  1.00 89.63           O  
ANISOU 2864  O   LYS A 263    13560  10982   9512    -30   3862  -1209       O  
ATOM   2865  CB  LYS A 263      18.963  -1.269  19.458  1.00 96.50           C  
ANISOU 2865  CB  LYS A 263    14440  11436  10788    620   4032  -1499       C  
ATOM   2866  CG  LYS A 263      19.237  -2.742  19.690  1.00 97.02           C  
ANISOU 2866  CG  LYS A 263    14661  11232  10970    950   4192  -1667       C  
ATOM   2867  CD  LYS A 263      19.968  -2.928  21.013  1.00 98.41           C  
ANISOU 2867  CD  LYS A 263    14402  11415  11572   1249   4080  -1528       C  
ATOM   2868  CE  LYS A 263      20.191  -4.393  21.335  1.00 98.78           C  
ANISOU 2868  CE  LYS A 263    14628  11154  11751   1612   4217  -1651       C  
ATOM   2869  NZ  LYS A 263      20.888  -4.572  22.639  1.00100.20           N  
ANISOU 2869  NZ  LYS A 263    14390  11365  12317   1925   4072  -1481       N  
ATOM   2870  N   PHE A 264      16.199   0.528  18.582  1.00 85.04           N  
ANISOU 2870  N   PHE A 264    13507  10126   8676   -177   3402  -1330       N  
ATOM   2871  CA  PHE A 264      15.501   1.771  18.902  1.00 84.00           C  
ANISOU 2871  CA  PHE A 264    13265  10121   8528   -400   3091  -1116       C  
ATOM   2872  C   PHE A 264      15.743   2.843  17.845  1.00 83.89           C  
ANISOU 2872  C   PHE A 264    13294  10303   8277   -573   3251  -1010       C  
ATOM   2873  O   PHE A 264      15.756   4.038  18.146  1.00 83.55           O  
ANISOU 2873  O   PHE A 264    13052  10366   8328   -688   3132   -804       O  
ATOM   2874  CB  PHE A 264      15.907   2.279  20.287  1.00 82.60           C  
ANISOU 2874  CB  PHE A 264    12669   9965   8749   -306   2916   -961       C  
ATOM   2875  CG  PHE A 264      15.692   1.274  21.375  1.00 82.76           C  
ANISOU 2875  CG  PHE A 264    12660   9802   8983   -127   2759  -1024       C  
ATOM   2876  CD1 PHE A 264      14.422   1.015  21.856  1.00 81.19           C  
ANISOU 2876  CD1 PHE A 264    12646   9485   8718   -236   2452  -1020       C  
ATOM   2877  CD2 PHE A 264      16.764   0.584  21.915  1.00 84.47           C  
ANISOU 2877  CD2 PHE A 264    12656   9972   9465    161   2928  -1070       C  
ATOM   2878  CE1 PHE A 264      14.224   0.087  22.858  1.00 81.13           C  
ANISOU 2878  CE1 PHE A 264    12639   9293   8892    -88   2335  -1058       C  
ATOM   2879  CE2 PHE A 264      16.574  -0.344  22.917  1.00 84.53           C  
ANISOU 2879  CE2 PHE A 264    12672   9795   9651    344   2788  -1095       C  
ATOM   2880  CZ  PHE A 264      15.302  -0.593  23.390  1.00 82.76           C  
ANISOU 2880  CZ  PHE A 264    12670   9431   9345    207   2501  -1088       C  
ATOM   2881  N   CYS A 265      15.953   2.418  16.602  1.00 85.52           N  
ANISOU 2881  N   CYS A 265    13791  10539   8164   -594   3540  -1151       N  
ATOM   2882  CA  CYS A 265      16.118   3.346  15.494  1.00 85.45           C  
ANISOU 2882  CA  CYS A 265    13899  10709   7859   -764   3712  -1044       C  
ATOM   2883  C   CYS A 265      14.813   3.629  14.766  1.00 84.13           C  
ANISOU 2883  C   CYS A 265    14106  10586   7273   -989   3451  -1005       C  
ATOM   2884  O   CYS A 265      14.698   4.671  14.109  1.00 83.83           O  
ANISOU 2884  O   CYS A 265    14140  10692   7020  -1141   3459   -819       O  
ATOM   2885  CB  CYS A 265      17.147   2.802  14.499  1.00 85.07           C  
ANISOU 2885  CB  CYS A 265    13960  10707   7657   -657   4212  -1208       C  
ATOM   2886  SG  CYS A 265      18.843   2.702  15.115  1.00 87.02           S  
ANISOU 2886  SG  CYS A 265    13682  11002   8377   -391   4578  -1205       S  
ATOM   2887  N   LEU A 266      13.835   2.734  14.865  1.00 81.44           N  
ANISOU 2887  N   LEU A 266    13998  10132   6814  -1019   3216  -1161       N  
ATOM   2888  CA  LEU A 266      12.543   2.949  14.234  1.00 80.46           C  
ANISOU 2888  CA  LEU A 266    14170  10090   6310  -1238   2917  -1126       C  
ATOM   2889  C   LEU A 266      11.671   3.824  15.127  1.00 79.35           C  
ANISOU 2889  C   LEU A 266    13809   9980   6363  -1303   2512   -887       C  
ATOM   2890  O   LEU A 266      11.755   3.757  16.356  1.00 79.14           O  
ANISOU 2890  O   LEU A 266    13501   9842   6728  -1195   2399   -853       O  
ATOM   2891  CB  LEU A 266      11.858   1.611  13.957  1.00 80.86           C  
ANISOU 2891  CB  LEU A 266    14545  10015   6162  -1289   2840  -1414       C  
ATOM   2892  CG  LEU A 266      10.556   1.644  13.158  1.00 80.28           C  
ANISOU 2892  CG  LEU A 266    14787  10069   5647  -1543   2535  -1432       C  
ATOM   2893  CD1 LEU A 266      10.792   2.205  11.762  1.00 82.24           C  
ANISOU 2893  CD1 LEU A 266    15303  10523   5423  -1645   2712  -1387       C  
ATOM   2894  CD2 LEU A 266       9.951   0.255  13.083  1.00 80.19           C  
ANISOU 2894  CD2 LEU A 266    15055   9893   5521  -1626   2461  -1744       C  
ATOM   2895  N   LYS A 267      10.841   4.658  14.492  1.00 79.88           N  
ANISOU 2895  N   LYS A 267    14014  10200   6135  -1459   2304   -714       N  
ATOM   2896  CA  LYS A 267      10.011   5.611  15.227  1.00 78.88           C  
ANISOU 2896  CA  LYS A 267    13694  10105   6173  -1491   1959   -468       C  
ATOM   2897  C   LYS A 267       9.151   4.922  16.279  1.00 78.23           C  
ANISOU 2897  C   LYS A 267    13495   9914   6314  -1474   1668   -556       C  
ATOM   2898  O   LYS A 267       9.027   5.410  17.409  1.00 77.64           O  
ANISOU 2898  O   LYS A 267    13148   9775   6575  -1402   1526   -429       O  
ATOM   2899  CB  LYS A 267       9.134   6.396  14.248  1.00 82.48           C  
ANISOU 2899  CB  LYS A 267    14365  10746   6228  -1627   1766   -284       C  
ATOM   2900  CG  LYS A 267       8.202   7.412  14.900  1.00 81.62           C  
ANISOU 2900  CG  LYS A 267    14077  10666   6267  -1621   1425    -18       C  
ATOM   2901  CD  LYS A 267       6.774   6.879  14.987  1.00 81.33           C  
ANISOU 2901  CD  LYS A 267    14085  10709   6110  -1700   1041    -73       C  
ATOM   2902  CE  LYS A 267       5.836   7.884  15.639  1.00 80.74           C  
ANISOU 2902  CE  LYS A 267    13807  10673   6197  -1651    734    193       C  
ATOM   2903  NZ  LYS A 267       5.682   9.120  14.825  1.00 81.11           N  
ANISOU 2903  NZ  LYS A 267    13970  10844   6005  -1645    700    486       N  
ATOM   2904  N   GLU A 268       8.550   3.786  15.927  1.00 77.47           N  
ANISOU 2904  N   GLU A 268    13622   9788   6025  -1559   1590   -781       N  
ATOM   2905  CA  GLU A 268       7.665   3.093  16.854  1.00 76.86           C  
ANISOU 2905  CA  GLU A 268    13461   9607   6137  -1587   1333   -858       C  
ATOM   2906  C   GLU A 268       8.430   2.376  17.960  1.00 77.00           C  
ANISOU 2906  C   GLU A 268    13313   9398   6543  -1412   1490   -963       C  
ATOM   2907  O   GLU A 268       7.862   2.132  19.030  1.00 76.41           O  
ANISOU 2907  O   GLU A 268    13089   9233   6711  -1394   1297   -937       O  
ATOM   2908  CB  GLU A 268       6.788   2.104  16.089  1.00 81.02           C  
ANISOU 2908  CB  GLU A 268    14294  10161   6328  -1785   1205  -1075       C  
ATOM   2909  CG  GLU A 268       5.793   2.754  15.135  1.00 81.13           C  
ANISOU 2909  CG  GLU A 268    14431  10443   5952  -1964    938   -952       C  
ATOM   2910  CD  GLU A 268       6.409   3.094  13.791  1.00 81.89           C  
ANISOU 2910  CD  GLU A 268    14795  10671   5646  -1993   1153   -954       C  
ATOM   2911  OE1 GLU A 268       7.593   2.762  13.578  1.00 82.34           O  
ANISOU 2911  OE1 GLU A 268    14935  10613   5739  -1884   1535  -1079       O  
ATOM   2912  OE2 GLU A 268       5.712   3.694  12.945  1.00 82.17           O  
ANISOU 2912  OE2 GLU A 268    14954  10941   5325  -2112    946   -820       O  
ATOM   2913  N   HIS A 269       9.697   2.027  17.726  1.00 75.61           N  
ANISOU 2913  N   HIS A 269    13156   9146   6427  -1269   1840  -1068       N  
ATOM   2914  CA  HIS A 269      10.528   1.474  18.790  1.00 76.13           C  
ANISOU 2914  CA  HIS A 269    13017   9035   6873  -1055   1974  -1117       C  
ATOM   2915  C   HIS A 269      10.985   2.549  19.761  1.00 76.22           C  
ANISOU 2915  C   HIS A 269    12658   9104   7197   -962   1909   -891       C  
ATOM   2916  O   HIS A 269      11.140   2.278  20.957  1.00 76.35           O  
ANISOU 2916  O   HIS A 269    12478   9013   7520   -837   1831   -871       O  
ATOM   2917  CB  HIS A 269      11.740   0.758  18.196  1.00 78.86           C  
ANISOU 2917  CB  HIS A 269    13465   9306   7193   -901   2376  -1296       C  
ATOM   2918  CG  HIS A 269      11.394  -0.507  17.479  1.00 78.82           C  
ANISOU 2918  CG  HIS A 269    13852   9157   6939   -958   2473  -1571       C  
ATOM   2919  ND1 HIS A 269      12.301  -1.200  16.709  1.00 79.85           N  
ANISOU 2919  ND1 HIS A 269    14172   9211   6955   -835   2857  -1771       N  
ATOM   2920  CD2 HIS A 269      10.237  -1.207  17.421  1.00 77.94           C  
ANISOU 2920  CD2 HIS A 269    13985   8956   6674  -1142   2246  -1696       C  
ATOM   2921  CE1 HIS A 269      11.717  -2.272  16.203  1.00 79.55           C  
ANISOU 2921  CE1 HIS A 269    14521   9015   6691   -941   2863  -2020       C  
ATOM   2922  NE2 HIS A 269      10.463  -2.298  16.619  1.00 78.42           N  
ANISOU 2922  NE2 HIS A 269    14410   8866   6521  -1149   2484  -1980       N  
ATOM   2923  N   LYS A 270      11.212   3.765  19.262  1.00 76.03           N  
ANISOU 2923  N   LYS A 270    12565   9237   7084  -1031   1944   -722       N  
ATOM   2924  CA  LYS A 270      11.515   4.885  20.142  1.00 75.86           C  
ANISOU 2924  CA  LYS A 270    12240   9250   7334   -999   1860   -521       C  
ATOM   2925  C   LYS A 270      10.320   5.224  21.020  1.00 74.52           C  
ANISOU 2925  C   LYS A 270    12009   9054   7253  -1048   1510   -415       C  
ATOM   2926  O   LYS A 270      10.492   5.634  22.173  1.00 74.41           O  
ANISOU 2926  O   LYS A 270    11760   8992   7520   -977   1416   -334       O  
ATOM   2927  CB  LYS A 270      11.933   6.094  19.311  1.00 78.44           C  
ANISOU 2927  CB  LYS A 270    12575   9707   7520  -1093   1996   -361       C  
ATOM   2928  CG  LYS A 270      13.165   5.847  18.454  1.00 79.81           C  
ANISOU 2928  CG  LYS A 270    12777   9934   7614  -1053   2390   -450       C  
ATOM   2929  CD  LYS A 270      13.561   7.086  17.670  1.00 79.74           C  
ANISOU 2929  CD  LYS A 270    12788  10042   7467  -1176   2543   -264       C  
ATOM   2930  CE  LYS A 270      14.673   6.773  16.681  1.00 81.06           C  
ANISOU 2930  CE  LYS A 270    13017  10287   7497  -1155   2971   -360       C  
ATOM   2931  NZ  LYS A 270      15.949   6.400  17.352  1.00 82.55           N  
ANISOU 2931  NZ  LYS A 270    12859  10459   8047  -1001   3198   -445       N  
ATOM   2932  N   ALA A 271       9.106   5.061  20.493  1.00 71.74           N  
ANISOU 2932  N   ALA A 271    11853   8751   6654  -1171   1315   -418       N  
ATOM   2933  CA  ALA A 271       7.913   5.276  21.304  1.00 70.66           C  
ANISOU 2933  CA  ALA A 271    11630   8610   6609  -1207   1008   -328       C  
ATOM   2934  C   ALA A 271       7.808   4.236  22.412  1.00 70.71           C  
ANISOU 2934  C   ALA A 271    11564   8465   6840  -1135    959   -449       C  
ATOM   2935  O   ALA A 271       7.385   4.553  23.530  1.00 70.05           O  
ANISOU 2935  O   ALA A 271    11309   8345   6962  -1093    804   -358       O  
ATOM   2936  CB  ALA A 271       6.665   5.251  20.425  1.00 70.70           C  
ANISOU 2936  CB  ALA A 271    11816   8747   6298  -1362    806   -309       C  
ATOM   2937  N   LEU A 272       8.185   2.990  22.121  1.00 72.15           N  
ANISOU 2937  N   LEU A 272    11903   8538   6973  -1111   1108   -651       N  
ATOM   2938  CA  LEU A 272       8.173   1.957  23.153  1.00 71.97           C  
ANISOU 2938  CA  LEU A 272    11853   8333   7161  -1022   1092   -743       C  
ATOM   2939  C   LEU A 272       9.253   2.213  24.196  1.00 72.78           C  
ANISOU 2939  C   LEU A 272    11705   8383   7566   -816   1180   -672       C  
ATOM   2940  O   LEU A 272       9.006   2.093  25.402  1.00 72.21           O  
ANISOU 2940  O   LEU A 272    11511   8238   7689   -752   1050   -615       O  
ATOM   2941  CB  LEU A 272       8.349   0.575  22.524  1.00 73.87           C  
ANISOU 2941  CB  LEU A 272    12370   8425   7275  -1032   1257   -977       C  
ATOM   2942  CG  LEU A 272       7.193   0.065  21.664  1.00 73.28           C  
ANISOU 2942  CG  LEU A 272    12560   8380   6903  -1280   1128  -1097       C  
ATOM   2943  CD1 LEU A 272       7.567  -1.247  20.996  1.00 73.72           C  
ANISOU 2943  CD1 LEU A 272    12934   8248   6827  -1287   1346  -1361       C  
ATOM   2944  CD2 LEU A 272       5.940  -0.100  22.507  1.00 72.17           C  
ANISOU 2944  CD2 LEU A 272    12343   8222   6857  -1406    857  -1038       C  
ATOM   2945  N   LYS A 273      10.463   2.560  23.747  1.00 71.49           N  
ANISOU 2945  N   LYS A 273    11455   8276   7432   -723   1401   -674       N  
ATOM   2946  CA  LYS A 273      11.534   2.897  24.681  1.00 72.92           C  
ANISOU 2946  CA  LYS A 273    11349   8463   7894   -558   1457   -604       C  
ATOM   2947  C   LYS A 273      11.138   4.054  25.589  1.00 72.27           C  
ANISOU 2947  C   LYS A 273    11078   8445   7935   -617   1240   -438       C  
ATOM   2948  O   LYS A 273      11.550   4.098  26.753  1.00 73.17           O  
ANISOU 2948  O   LYS A 273    11002   8532   8267   -510   1167   -398       O  
ATOM   2949  CB  LYS A 273      12.811   3.231  23.908  1.00 75.37           C  
ANISOU 2949  CB  LYS A 273    11561   8873   8204   -503   1736   -622       C  
ATOM   2950  CG  LYS A 273      14.034   3.496  24.773  1.00 77.42           C  
ANISOU 2950  CG  LYS A 273    11476   9181   8757   -349   1799   -570       C  
ATOM   2951  CD  LYS A 273      15.269   3.729  23.912  1.00 78.80           C  
ANISOU 2951  CD  LYS A 273    11529   9475   8936   -313   2114   -598       C  
ATOM   2952  CE  LYS A 273      16.477   4.101  24.756  1.00 80.98           C  
ANISOU 2952  CE  LYS A 273    11399   9855   9515   -201   2145   -538       C  
ATOM   2953  NZ  LYS A 273      17.671   4.391  23.912  1.00 82.16           N  
ANISOU 2953  NZ  LYS A 273    11377  10152   9689   -194   2473   -554       N  
ATOM   2954  N   THR A 274      10.335   4.991  25.081  1.00 71.83           N  
ANISOU 2954  N   THR A 274    11091   8470   7730   -771   1135   -339       N  
ATOM   2955  CA  THR A 274       9.819   6.061  25.928  1.00 70.51           C  
ANISOU 2955  CA  THR A 274    10795   8324   7672   -808    947   -195       C  
ATOM   2956  C   THR A 274       8.937   5.492  27.033  1.00 69.69           C  
ANISOU 2956  C   THR A 274    10684   8139   7656   -771    759   -206       C  
ATOM   2957  O   THR A 274       9.090   5.838  28.211  1.00 69.51           O  
ANISOU 2957  O   THR A 274    10514   8088   7808   -707    674   -156       O  
ATOM   2958  CB  THR A 274       9.044   7.071  25.080  1.00 70.27           C  
ANISOU 2958  CB  THR A 274    10869   8376   7455   -935    880    -72       C  
ATOM   2959  OG1 THR A 274       9.888   7.560  24.031  1.00 71.01           O  
ANISOU 2959  OG1 THR A 274    11003   8535   7442   -981   1085    -47       O  
ATOM   2960  CG2 THR A 274       8.590   8.248  25.932  1.00 68.55           C  
ANISOU 2960  CG2 THR A 274    10537   8140   7368   -939    732     73       C  
ATOM   2961  N   LEU A 275       8.015   4.598  26.668  1.00 70.96           N  
ANISOU 2961  N   LEU A 275    11014   8266   7680   -832    702   -277       N  
ATOM   2962  CA  LEU A 275       7.157   3.950  27.652  1.00 69.74           C  
ANISOU 2962  CA  LEU A 275    10865   8030   7602   -829    563   -286       C  
ATOM   2963  C   LEU A 275       7.935   3.031  28.582  1.00 69.79           C  
ANISOU 2963  C   LEU A 275    10839   7903   7776   -675    634   -346       C  
ATOM   2964  O   LEU A 275       7.479   2.769  29.699  1.00 68.15           O  
ANISOU 2964  O   LEU A 275    10597   7631   7666   -640    531   -305       O  
ATOM   2965  CB  LEU A 275       6.053   3.167  26.945  1.00 69.81           C  
ANISOU 2965  CB  LEU A 275    11056   8038   7429   -981    498   -363       C  
ATOM   2966  CG  LEU A 275       5.070   4.009  26.137  1.00 69.79           C  
ANISOU 2966  CG  LEU A 275    11062   8206   7250  -1116    361   -274       C  
ATOM   2967  CD1 LEU A 275       4.108   3.116  25.371  1.00 69.91           C  
ANISOU 2967  CD1 LEU A 275    11243   8255   7067  -1297    281   -382       C  
ATOM   2968  CD2 LEU A 275       4.312   4.974  27.039  1.00 68.94           C  
ANISOU 2968  CD2 LEU A 275    10777   8154   7263  -1085    208   -114       C  
ATOM   2969  N   GLY A 276       9.092   2.528  28.148  1.00 69.61           N  
ANISOU 2969  N   GLY A 276    10826   7843   7781   -564    816   -429       N  
ATOM   2970  CA  GLY A 276       9.942   1.757  29.036  1.00 70.52           C  
ANISOU 2970  CA  GLY A 276    10872   7853   8069   -363    872   -450       C  
ATOM   2971  C   GLY A 276      10.708   2.592  30.035  1.00 71.97           C  
ANISOU 2971  C   GLY A 276    10793   8130   8424   -266    801   -349       C  
ATOM   2972  O   GLY A 276      11.201   2.050  31.029  1.00 72.77           O  
ANISOU 2972  O   GLY A 276    10819   8175   8654   -103    766   -328       O  
ATOM   2973  N   ILE A 277      10.827   3.895  29.791  1.00 71.20           N  
ANISOU 2973  N   ILE A 277    10571   8165   8319   -371    773   -286       N  
ATOM   2974  CA  ILE A 277      11.542   4.771  30.713  1.00 72.86           C  
ANISOU 2974  CA  ILE A 277    10548   8456   8680   -336    698   -219       C  
ATOM   2975  C   ILE A 277      10.628   5.277  31.820  1.00 69.26           C  
ANISOU 2975  C   ILE A 277    10104   7976   8236   -381    501   -150       C  
ATOM   2976  O   ILE A 277      11.047   5.377  32.976  1.00 70.15           O  
ANISOU 2976  O   ILE A 277    10100   8105   8449   -305    403   -127       O  
ATOM   2977  CB  ILE A 277      12.201   5.929  29.939  1.00 69.75           C  
ANISOU 2977  CB  ILE A 277    10041   8174   8287   -447    799   -192       C  
ATOM   2978  CG1 ILE A 277      13.308   5.382  29.042  1.00 71.85           C  
ANISOU 2978  CG1 ILE A 277    10245   8489   8567   -370   1032   -263       C  
ATOM   2979  CG2 ILE A 277      12.755   6.975  30.889  1.00 69.70           C  
ANISOU 2979  CG2 ILE A 277     9827   8232   8423   -487    698   -141       C  
ATOM   2980  CD1 ILE A 277      13.848   6.384  28.080  1.00 71.35           C  
ANISOU 2980  CD1 ILE A 277    10120   8527   8465   -507   1184   -230       C  
ATOM   2981  N   ILE A 278       9.371   5.591  31.498  1.00 72.44           N  
ANISOU 2981  N   ILE A 278    10640   8359   8527   -496    441   -116       N  
ATOM   2982  CA  ILE A 278       8.428   5.977  32.543  1.00 69.46           C  
ANISOU 2982  CA  ILE A 278    10271   7958   8163   -514    295    -57       C  
ATOM   2983  C   ILE A 278       8.176   4.811  33.489  1.00 69.07           C  
ANISOU 2983  C   ILE A 278    10281   7824   8137   -422    252    -72       C  
ATOM   2984  O   ILE A 278       7.877   5.012  34.672  1.00 68.07           O  
ANISOU 2984  O   ILE A 278    10132   7689   8042   -388    159    -28       O  
ATOM   2985  CB  ILE A 278       7.111   6.502  31.933  1.00 69.78           C  
ANISOU 2985  CB  ILE A 278    10396   8023   8094   -626    249     -3       C  
ATOM   2986  CG1 ILE A 278       6.414   5.415  31.115  1.00 70.24           C  
ANISOU 2986  CG1 ILE A 278    10590   8064   8035   -687    270    -55       C  
ATOM   2987  CG2 ILE A 278       7.365   7.726  31.074  1.00 70.10           C  
ANISOU 2987  CG2 ILE A 278    10413   8120   8102   -693    291     52       C  
ATOM   2988  CD1 ILE A 278       5.009   5.786  30.685  1.00 69.64           C  
ANISOU 2988  CD1 ILE A 278    10545   8058   7857   -793    173      6       C  
ATOM   2989  N   MET A 279       8.300   3.578  32.991  1.00 68.72           N  
ANISOU 2989  N   MET A 279    10346   7698   8066   -381    338   -132       N  
ATOM   2990  CA  MET A 279       8.137   2.402  33.836  1.00 68.42           C  
ANISOU 2990  CA  MET A 279    10407   7533   8056   -288    325   -129       C  
ATOM   2991  C   MET A 279       9.386   2.145  34.670  1.00 71.27           C  
ANISOU 2991  C   MET A 279    10657   7897   8525    -86    315   -104       C  
ATOM   2992  O   MET A 279       9.297   1.911  35.880  1.00 71.14           O  
ANISOU 2992  O   MET A 279    10652   7852   8528     -6    223    -38       O  
ATOM   2993  CB  MET A 279       7.811   1.182  32.975  1.00 70.91           C  
ANISOU 2993  CB  MET A 279    10922   7714   8306   -328    433   -215       C  
ATOM   2994  CG  MET A 279       6.472   1.265  32.270  1.00 69.19           C  
ANISOU 2994  CG  MET A 279    10802   7522   7967   -549    395   -239       C  
ATOM   2995  SD  MET A 279       6.165  -0.171  31.228  1.00 69.72           S  
ANISOU 2995  SD  MET A 279    11133   7425   7932   -650    511   -387       S  
ATOM   2996  CE  MET A 279       4.627   0.311  30.451  1.00 69.01           C  
ANISOU 2996  CE  MET A 279    11050   7482   7688   -934    385   -391       C  
ATOM   2997  N   GLY A 280      10.560   2.181  34.034  1.00 65.93           N  
ANISOU 2997  N   GLY A 280     9863   7278   7911      1    410   -149       N  
ATOM   2998  CA  GLY A 280      11.799   1.997  34.769  1.00 69.79           C  
ANISOU 2998  CA  GLY A 280    10175   7825   8518    201    379   -117       C  
ATOM   2999  C   GLY A 280      12.047   3.088  35.791  1.00 71.27           C  
ANISOU 2999  C   GLY A 280    10187   8156   8736    159    208    -64       C  
ATOM   3000  O   GLY A 280      12.654   2.839  36.837  1.00 73.79           O  
ANISOU 3000  O   GLY A 280    10413   8523   9101    303     96    -13       O  
ATOM   3001  N   THR A 281      11.584   4.307  35.508  1.00 71.82           N  
ANISOU 3001  N   THR A 281    10230   8289   8769    -34    183    -75       N  
ATOM   3002  CA  THR A 281      11.681   5.381  36.490  1.00 72.44           C  
ANISOU 3002  CA  THR A 281    10208   8455   8861   -101     37    -53       C  
ATOM   3003  C   THR A 281      10.707   5.153  37.640  1.00 69.46           C  
ANISOU 3003  C   THR A 281     9982   8012   8399    -80    -72     -6       C  
ATOM   3004  O   THR A 281      11.062   5.327  38.812  1.00 71.63           O  
ANISOU 3004  O   THR A 281    10210   8347   8661    -27   -205     14       O  
ATOM   3005  CB  THR A 281      11.422   6.732  35.823  1.00 70.18           C  
ANISOU 3005  CB  THR A 281     9900   8198   8566   -292     75    -69       C  
ATOM   3006  OG1 THR A 281      12.400   6.955  34.800  1.00 73.20           O  
ANISOU 3006  OG1 THR A 281    10145   8651   9015   -327    202    -99       O  
ATOM   3007  CG2 THR A 281      11.499   7.855  36.844  1.00 69.91           C  
ANISOU 3007  CG2 THR A 281     9814   8205   8545   -375    -54    -76       C  
ATOM   3008  N   PHE A 282       9.468   4.765  37.318  1.00 70.29           N  
ANISOU 3008  N   PHE A 282    10263   8013   8432   -136    -17     11       N  
ATOM   3009  CA  PHE A 282       8.489   4.458  38.356  1.00 68.14           C  
ANISOU 3009  CA  PHE A 282    10123   7682   8085   -127    -73     64       C  
ATOM   3010  C   PHE A 282       9.008   3.382  39.298  1.00 70.20           C  
ANISOU 3010  C   PHE A 282    10435   7901   8338     42   -120    117       C  
ATOM   3011  O   PHE A 282       8.745   3.420  40.506  1.00 70.17           O  
ANISOU 3011  O   PHE A 282    10493   7910   8260     77   -205    170       O  
ATOM   3012  CB  PHE A 282       7.171   4.012  37.723  1.00 69.27           C  
ANISOU 3012  CB  PHE A 282    10398   7744   8179   -229      5     72       C  
ATOM   3013  CG  PHE A 282       6.063   3.795  38.716  1.00 67.72           C  
ANISOU 3013  CG  PHE A 282    10302   7509   7919   -254    -14    131       C  
ATOM   3014  CD1 PHE A 282       5.314   4.862  39.183  1.00 66.71           C  
ANISOU 3014  CD1 PHE A 282    10141   7443   7761   -312    -40    146       C  
ATOM   3015  CD2 PHE A 282       5.785   2.528  39.198  1.00 67.73           C  
ANISOU 3015  CD2 PHE A 282    10445   7396   7895   -213     23    176       C  
ATOM   3016  CE1 PHE A 282       4.297   4.666  40.098  1.00 66.15           C  
ANISOU 3016  CE1 PHE A 282    10146   7356   7631   -327    -18    199       C  
ATOM   3017  CE2 PHE A 282       4.775   2.328  40.117  1.00 66.84           C  
ANISOU 3017  CE2 PHE A 282    10421   7256   7719   -256     39    242       C  
ATOM   3018  CZ  PHE A 282       4.029   3.397  40.566  1.00 66.23           C  
ANISOU 3018  CZ  PHE A 282    10279   7276   7608   -312     23    250       C  
ATOM   3019  N   THR A 283       9.745   2.411  38.760  1.00 67.84           N  
ANISOU 3019  N   THR A 283    10131   7544   8101    166    -54    112       N  
ATOM   3020  CA  THR A 283      10.300   1.354  39.594  1.00 69.49           C  
ANISOU 3020  CA  THR A 283    10398   7692   8314    376    -95    192       C  
ATOM   3021  C   THR A 283      11.387   1.900  40.512  1.00 73.10           C  
ANISOU 3021  C   THR A 283    10661   8331   8784    486   -264    223       C  
ATOM   3022  O   THR A 283      11.353   1.682  41.727  1.00 72.98           O  
ANISOU 3022  O   THR A 283    10717   8335   8678    572   -385    308       O  
ATOM   3023  CB  THR A 283      10.850   0.229  38.717  1.00 70.29           C  
ANISOU 3023  CB  THR A 283    10547   7664   8495    514     45    169       C  
ATOM   3024  OG1 THR A 283       9.800  -0.287  37.888  1.00 67.22           O  
ANISOU 3024  OG1 THR A 283    10362   7112   8065    365    177    115       O  
ATOM   3025  CG2 THR A 283      11.406  -0.893  39.581  1.00 71.50           C  
ANISOU 3025  CG2 THR A 283    10785   7719   8664    777     11    282       C  
ATOM   3026  N   LEU A 284      12.344   2.643  39.954  1.00 69.51           N  
ANISOU 3026  N   LEU A 284     9960   8025   8424    458   -277    154       N  
ATOM   3027  CA  LEU A 284      13.453   3.143  40.756  1.00 73.19           C  
ANISOU 3027  CA  LEU A 284    10197   8694   8917    524   -455    166       C  
ATOM   3028  C   LEU A 284      13.017   4.182  41.782  1.00 72.30           C  
ANISOU 3028  C   LEU A 284    10125   8661   8683    372   -609    144       C  
ATOM   3029  O   LEU A 284      13.751   4.424  42.744  1.00 73.56           O  
ANISOU 3029  O   LEU A 284    10168   8980   8802    420   -800    158       O  
ATOM   3030  CB  LEU A 284      14.535   3.732  39.850  1.00 69.78           C  
ANISOU 3030  CB  LEU A 284     9475   8406   8633    477   -400     90       C  
ATOM   3031  CG  LEU A 284      15.247   2.726  38.940  1.00 71.01           C  
ANISOU 3031  CG  LEU A 284     9547   8523   8909    675   -237     99       C  
ATOM   3032  CD1 LEU A 284      16.231   3.424  38.013  1.00 74.34           C  
ANISOU 3032  CD1 LEU A 284     9678   9105   9464    591   -139     24       C  
ATOM   3033  CD2 LEU A 284      15.944   1.655  39.765  1.00 71.27           C  
ANISOU 3033  CD2 LEU A 284     9530   8578   8970    988   -337    209       C  
ATOM   3034  N   CYS A 285      11.848   4.803  41.609  1.00 74.36           N  
ANISOU 3034  N   CYS A 285    10547   8825   8880    199   -533    105       N  
ATOM   3035  CA  CYS A 285      11.394   5.787  42.586  1.00 73.10           C  
ANISOU 3035  CA  CYS A 285    10460   8711   8606     82   -636     69       C  
ATOM   3036  C   CYS A 285      10.628   5.147  43.737  1.00 70.68           C  
ANISOU 3036  C   CYS A 285    10374   8348   8134    169   -675    153       C  
ATOM   3037  O   CYS A 285      10.702   5.639  44.870  1.00 70.67           O  
ANISOU 3037  O   CYS A 285    10423   8432   7997    151   -806    136       O  
ATOM   3038  CB  CYS A 285      10.521   6.851  41.913  1.00 69.66           C  
ANISOU 3038  CB  CYS A 285    10079   8200   8190   -104   -523      3       C  
ATOM   3039  SG  CYS A 285      11.389   7.941  40.756  1.00 69.91           S  
ANISOU 3039  SG  CYS A 285     9904   8288   8370   -255   -473    -81       S  
ATOM   3040  N   TRP A 286       9.895   4.064  43.478  1.00 74.89           N  
ANISOU 3040  N   TRP A 286    11058   8735   8661    240   -553    236       N  
ATOM   3041  CA  TRP A 286       9.057   3.443  44.495  1.00 72.80           C  
ANISOU 3041  CA  TRP A 286    11019   8397   8245    287   -540    332       C  
ATOM   3042  C   TRP A 286       9.603   2.134  45.039  1.00 73.57           C  
ANISOU 3042  C   TRP A 286    11204   8446   8304    499   -589    468       C  
ATOM   3043  O   TRP A 286       9.313   1.796  46.187  1.00 73.07           O  
ANISOU 3043  O   TRP A 286    11311   8379   8073    561   -640    566       O  
ATOM   3044  CB  TRP A 286       7.647   3.198  43.946  1.00 72.74           C  
ANISOU 3044  CB  TRP A 286    11138   8248   8251    169   -357    341       C  
ATOM   3045  CG  TRP A 286       6.881   4.455  43.693  1.00 71.58           C  
ANISOU 3045  CG  TRP A 286    10945   8144   8109     14   -312    256       C  
ATOM   3046  CD1 TRP A 286       6.688   5.071  42.493  1.00 70.55           C  
ANISOU 3046  CD1 TRP A 286    10706   8010   8089    -86   -251    190       C  
ATOM   3047  CD2 TRP A 286       6.224   5.268  44.672  1.00 71.45           C  
ANISOU 3047  CD2 TRP A 286    11008   8169   7969    -30   -313    236       C  
ATOM   3048  NE1 TRP A 286       5.938   6.210  42.660  1.00 69.73           N  
ANISOU 3048  NE1 TRP A 286    10605   7930   7960   -170   -222    149       N  
ATOM   3049  CE2 TRP A 286       5.641   6.354  43.990  1.00 70.62           C  
ANISOU 3049  CE2 TRP A 286    10831   8064   7938   -135   -246    163       C  
ATOM   3050  CE3 TRP A 286       6.067   5.180  46.058  1.00 72.00           C  
ANISOU 3050  CE3 TRP A 286    11227   8273   7858     22   -351    277       C  
ATOM   3051  CZ2 TRP A 286       4.912   7.342  44.646  1.00 70.85           C  
ANISOU 3051  CZ2 TRP A 286    10923   8103   7893   -168   -199    121       C  
ATOM   3052  CZ3 TRP A 286       5.346   6.163  46.708  1.00 72.01           C  
ANISOU 3052  CZ3 TRP A 286    11299   8301   7762    -36   -298    216       C  
ATOM   3053  CH2 TRP A 286       4.780   7.232  46.003  1.00 71.67           C  
ANISOU 3053  CH2 TRP A 286    11173   8235   7823   -120   -215    134       C  
ATOM   3054  N   LEU A 287      10.374   1.387  44.249  1.00 74.30           N  
ANISOU 3054  N   LEU A 287    11204   8488   8537    628   -556    486       N  
ATOM   3055  CA  LEU A 287      10.909   0.122  44.743  1.00 75.08           C  
ANISOU 3055  CA  LEU A 287    11404   8505   8619    878   -588    634       C  
ATOM   3056  C   LEU A 287      11.765   0.282  45.997  1.00 77.02           C  
ANISOU 3056  C   LEU A 287    11584   8943   8736   1032   -830    720       C  
ATOM   3057  O   LEU A 287      11.624  -0.552  46.908  1.00 76.52           O  
ANISOU 3057  O   LEU A 287    11730   8805   8538   1184   -867    884       O  
ATOM   3058  CB  LEU A 287      11.689  -0.585  43.627  1.00 74.00           C  
ANISOU 3058  CB  LEU A 287    11159   8287   8671   1020   -491    612       C  
ATOM   3059  CG  LEU A 287      12.196  -2.002  43.882  1.00 74.63           C  
ANISOU 3059  CG  LEU A 287    11372   8205   8781   1318   -463    763       C  
ATOM   3060  CD1 LEU A 287      11.038  -2.966  44.101  1.00 71.93           C  
ANISOU 3060  CD1 LEU A 287    11398   7571   8361   1265   -311    848       C  
ATOM   3061  CD2 LEU A 287      13.072  -2.461  42.730  1.00 76.41           C  
ANISOU 3061  CD2 LEU A 287    11448   8384   9201   1468   -346    700       C  
ATOM   3062  N   PRO A 288      12.640   1.291  46.127  1.00 78.22           N  
ANISOU 3062  N   PRO A 288    11472   9344   8906    985  -1005    627       N  
ATOM   3063  CA  PRO A 288      13.317   1.478  47.424  1.00 79.49           C  
ANISOU 3063  CA  PRO A 288    11592   9716   8893   1084  -1271    695       C  
ATOM   3064  C   PRO A 288      12.352   1.676  48.579  1.00 77.53           C  
ANISOU 3064  C   PRO A 288    11639   9442   8376    997  -1293    734       C  
ATOM   3065  O   PRO A 288      12.551   1.099  49.655  1.00 77.81           O  
ANISOU 3065  O   PRO A 288    11818   9530   8218   1161  -1430    887       O  
ATOM   3066  CB  PRO A 288      14.186   2.721  47.190  1.00 76.69           C  
ANISOU 3066  CB  PRO A 288    10914   9606   8619    929  -1415    531       C  
ATOM   3067  CG  PRO A 288      14.420   2.743  45.734  1.00 77.70           C  
ANISOU 3067  CG  PRO A 288    10862   9659   9000    890  -1229    453       C  
ATOM   3068  CD  PRO A 288      13.155   2.232  45.114  1.00 75.05           C  
ANISOU 3068  CD  PRO A 288    10796   9047   8674    838   -978    467       C  
ATOM   3069  N   PHE A 289      11.312   2.488  48.384  1.00 81.58           N  
ANISOU 3069  N   PHE A 289    12249   9885   8865    760  -1152    611       N  
ATOM   3070  CA  PHE A 289      10.309   2.681  49.427  1.00 79.93           C  
ANISOU 3070  CA  PHE A 289    12313   9646   8411    685  -1111    638       C  
ATOM   3071  C   PHE A 289       9.633   1.364  49.794  1.00 78.63           C  
ANISOU 3071  C   PHE A 289    12416   9296   8165    810   -977    838       C  
ATOM   3072  O   PHE A 289       9.497   1.031  50.976  1.00 78.71           O  
ANISOU 3072  O   PHE A 289    12639   9341   7926    889  -1042    962       O  
ATOM   3073  CB  PHE A 289       9.279   3.715  48.968  1.00 80.41           C  
ANISOU 3073  CB  PHE A 289    12389   9644   8518    454   -941    484       C  
ATOM   3074  CG  PHE A 289       8.159   3.937  49.944  1.00 79.04           C  
ANISOU 3074  CG  PHE A 289    12470   9439   8124    389   -837    500       C  
ATOM   3075  CD1 PHE A 289       8.364   4.653  51.113  1.00 79.85           C  
ANISOU 3075  CD1 PHE A 289    12676   9685   7979    363   -973    436       C  
ATOM   3076  CD2 PHE A 289       6.895   3.437  49.685  1.00 77.15           C  
ANISOU 3076  CD2 PHE A 289    12359   9039   7917    339   -595    566       C  
ATOM   3077  CE1 PHE A 289       7.326   4.856  52.007  1.00 79.00           C  
ANISOU 3077  CE1 PHE A 289    12816   9549   7653    317   -834    442       C  
ATOM   3078  CE2 PHE A 289       5.856   3.639  50.571  1.00 76.47           C  
ANISOU 3078  CE2 PHE A 289    12470   8944   7641    283   -462    586       C  
ATOM   3079  CZ  PHE A 289       6.071   4.348  51.734  1.00 77.47           C  
ANISOU 3079  CZ  PHE A 289    12718   9202   7515    287   -565    525       C  
ATOM   3080  N   PHE A 290       9.210   0.595  48.789  1.00 80.15           N  
ANISOU 3080  N   PHE A 290    12624   9281   8548    810   -785    870       N  
ATOM   3081  CA  PHE A 290       8.469  -0.633  49.058  1.00 78.85           C  
ANISOU 3081  CA  PHE A 290    12736   8893   8330    866   -623   1041       C  
ATOM   3082  C   PHE A 290       9.360  -1.770  49.549  1.00 80.30           C  
ANISOU 3082  C   PHE A 290    13021   9019   8469   1155   -730   1242       C  
ATOM   3083  O   PHE A 290       8.884  -2.635  50.293  1.00 79.78           O  
ANISOU 3083  O   PHE A 290    13247   8808   8259   1223   -653   1426       O  
ATOM   3084  CB  PHE A 290       7.686  -1.056  47.814  1.00 75.22           C  
ANISOU 3084  CB  PHE A 290    12278   8228   8075    727   -396    980       C  
ATOM   3085  CG  PHE A 290       6.435  -0.252  47.588  1.00 73.43           C  
ANISOU 3085  CG  PHE A 290    12033   8024   7845    474   -260    871       C  
ATOM   3086  CD1 PHE A 290       5.256  -0.598  48.228  1.00 72.32           C  
ANISOU 3086  CD1 PHE A 290    12091   7800   7587    369   -102    957       C  
ATOM   3087  CD2 PHE A 290       6.442   0.859  46.765  1.00 73.21           C  
ANISOU 3087  CD2 PHE A 290    11781   8105   7931    355   -280    700       C  
ATOM   3088  CE1 PHE A 290       4.104   0.136  48.033  1.00 71.21           C  
ANISOU 3088  CE1 PHE A 290    11886   7707   7462    172     28    868       C  
ATOM   3089  CE2 PHE A 290       5.293   1.600  46.569  1.00 71.77           C  
ANISOU 3089  CE2 PHE A 290    11573   7945   7752    174   -162    626       C  
ATOM   3090  CZ  PHE A 290       4.122   1.237  47.205  1.00 70.89           C  
ANISOU 3090  CZ  PHE A 290    11620   7774   7541     94    -12    707       C  
ATOM   3091  N   ILE A 291      10.636  -1.802  49.155  1.00 79.61           N  
ANISOU 3091  N   ILE A 291    12698   9042   8509   1339   -890   1227       N  
ATOM   3092  CA  ILE A 291      11.528  -2.809  49.725  1.00 81.20           C  
ANISOU 3092  CA  ILE A 291    12966   9222   8663   1669  -1018   1442       C  
ATOM   3093  C   ILE A 291      11.793  -2.513  51.194  1.00 82.06           C  
ANISOU 3093  C   ILE A 291    13164   9552   8462   1746  -1258   1557       C  
ATOM   3094  O   ILE A 291      11.966  -3.432  52.002  1.00 82.54           O  
ANISOU 3094  O   ILE A 291    13450   9542   8370   1977  -1316   1799       O  
ATOM   3095  CB  ILE A 291      12.843  -2.908  48.926  1.00 77.84           C  
ANISOU 3095  CB  ILE A 291    12211   8895   8470   1871  -1115   1401       C  
ATOM   3096  CG1 ILE A 291      12.590  -3.462  47.527  1.00 77.10           C  
ANISOU 3096  CG1 ILE A 291    12122   8543   8632   1839   -850   1312       C  
ATOM   3097  CG2 ILE A 291      13.856  -3.793  49.639  1.00 79.71           C  
ANISOU 3097  CG2 ILE A 291    12455   9179   8653   2261  -1297   1637       C  
ATOM   3098  CD1 ILE A 291      13.824  -3.438  46.655  1.00 79.48           C  
ANISOU 3098  CD1 ILE A 291    12085   8955   9158   2012   -887   1242       C  
ATOM   3099  N   VAL A 292      11.814  -1.236  51.575  1.00 83.22           N  
ANISOU 3099  N   VAL A 292    13175   9954   8491   1554  -1398   1389       N  
ATOM   3100  CA  VAL A 292      12.047  -0.906  52.975  1.00 84.04           C  
ANISOU 3100  CA  VAL A 292    13395  10280   8257   1595  -1632   1462       C  
ATOM   3101  C   VAL A 292      10.816  -1.208  53.820  1.00 82.36           C  
ANISOU 3101  C   VAL A 292    13589   9921   7785   1510  -1451   1569       C  
ATOM   3102  O   VAL A 292      10.942  -1.618  54.980  1.00 83.03           O  
ANISOU 3102  O   VAL A 292    13904  10078   7567   1649  -1576   1755       O  
ATOM   3103  CB  VAL A 292      12.503   0.558  53.091  1.00 78.89           C  
ANISOU 3103  CB  VAL A 292    12496   9915   7562   1392  -1826   1217       C  
ATOM   3104  CG1 VAL A 292      12.517   1.007  54.532  1.00 79.39           C  
ANISOU 3104  CG1 VAL A 292    12747  10188   7229   1363  -2034   1235       C  
ATOM   3105  CG2 VAL A 292      13.897   0.689  52.510  1.00 81.14           C  
ANISOU 3105  CG2 VAL A 292    12373  10395   8063   1505  -2039   1172       C  
ATOM   3106  N   ASN A 293       9.614  -1.040  53.262  1.00 87.10           N  
ANISOU 3106  N   ASN A 293    14274  10330   8489   1287  -1153   1471       N  
ATOM   3107  CA  ASN A 293       8.410  -1.465  53.971  1.00 85.77           C  
ANISOU 3107  CA  ASN A 293    14453  10016   8122   1203   -930   1591       C  
ATOM   3108  C   ASN A 293       8.423  -2.966  54.226  1.00 85.89           C  
ANISOU 3108  C   ASN A 293    14731   9797   8107   1404   -850   1881       C  
ATOM   3109  O   ASN A 293       8.086  -3.421  55.325  1.00 86.10           O  
ANISOU 3109  O   ASN A 293    15071   9801   7842   1461   -822   2077       O  
ATOM   3110  CB  ASN A 293       7.161  -1.082  53.179  1.00 83.76           C  
ANISOU 3110  CB  ASN A 293    14161   9623   8041    940   -636   1442       C  
ATOM   3111  CG  ASN A 293       6.899   0.402  53.190  1.00 83.62           C  
ANISOU 3111  CG  ASN A 293    13992   9789   7992    761   -662   1200       C  
ATOM   3112  OD1 ASN A 293       7.086   1.065  54.207  1.00 84.47           O  
ANISOU 3112  OD1 ASN A 293    14189  10075   7832    760   -789   1159       O  
ATOM   3113  ND2 ASN A 293       6.446   0.932  52.061  1.00 82.60           N  
ANISOU 3113  ND2 ASN A 293    13661   9602   8120    609   -538   1040       N  
ATOM   3114  N   ILE A 294       8.813  -3.750  53.220  1.00 87.50           N  
ANISOU 3114  N   ILE A 294    14843   9804   8599   1516   -793   1915       N  
ATOM   3115  CA  ILE A 294       8.723  -5.200  53.333  1.00 87.51           C  
ANISOU 3115  CA  ILE A 294    15138   9497   8614   1688   -661   2172       C  
ATOM   3116  C   ILE A 294       9.802  -5.737  54.269  1.00 89.48           C  
ANISOU 3116  C   ILE A 294    15482   9845   8670   2048   -922   2421       C  
ATOM   3117  O   ILE A 294       9.636  -6.807  54.866  1.00 89.68           O  
ANISOU 3117  O   ILE A 294    15855   9650   8570   2205   -838   2698       O  
ATOM   3118  CB  ILE A 294       8.795  -5.840  51.931  1.00 86.96           C  
ANISOU 3118  CB  ILE A 294    14972   9166   8902   1692   -502   2093       C  
ATOM   3119  CG1 ILE A 294       8.208  -7.251  51.943  1.00 86.38           C  
ANISOU 3119  CG1 ILE A 294    15279   8683   8860   1723   -253   2296       C  
ATOM   3120  CG2 ILE A 294      10.220  -5.879  51.412  1.00 88.77           C  
ANISOU 3120  CG2 ILE A 294    14924   9506   9298   1977   -710   2071       C  
ATOM   3121  CD1 ILE A 294       6.714  -7.272  52.127  1.00 84.76           C  
ANISOU 3121  CD1 ILE A 294    15272   8351   8582   1376     14   2281       C  
ATOM   3122  N   VAL A 295      10.907  -5.012  54.428  1.00 90.88           N  
ANISOU 3122  N   VAL A 295    15357  10357   8815   2177  -1245   2342       N  
ATOM   3123  CA  VAL A 295      11.958  -5.427  55.354  1.00 92.93           C  
ANISOU 3123  CA  VAL A 295    15648  10789   8872   2520  -1550   2579       C  
ATOM   3124  C   VAL A 295      11.670  -4.937  56.767  1.00 93.19           C  
ANISOU 3124  C   VAL A 295    15904  11050   8454   2450  -1697   2651       C  
ATOM   3125  O   VAL A 295      11.891  -5.664  57.739  1.00 94.13           O  
ANISOU 3125  O   VAL A 295    16301  11163   8301   2685  -1805   2947       O  
ATOM   3126  CB  VAL A 295      13.331  -4.937  54.853  1.00 88.48           C  
ANISOU 3126  CB  VAL A 295    14609  10513   8496   2680  -1842   2464       C  
ATOM   3127  CG1 VAL A 295      14.410  -5.222  55.886  1.00 90.73           C  
ANISOU 3127  CG1 VAL A 295    14861  11066   8547   3017  -2216   2700       C  
ATOM   3128  CG2 VAL A 295      13.677  -5.612  53.537  1.00 88.55           C  
ANISOU 3128  CG2 VAL A 295    14459  10277   8909   2815  -1664   2434       C  
ATOM   3129  N   HIS A 296      11.187  -3.699  56.892  1.00 97.10           N  
ANISOU 3129  N   HIS A 296    16305  11738   8851   2140  -1694   2386       N  
ATOM   3130  CA  HIS A 296      10.660  -3.166  58.144  1.00 97.06           C  
ANISOU 3130  CA  HIS A 296    16565  11899   8414   2015  -1734   2395       C  
ATOM   3131  C   HIS A 296       9.767  -4.158  58.879  1.00 96.41           C  
ANISOU 3131  C   HIS A 296    16958  11572   8101   2058  -1487   2679       C  
ATOM   3132  O   HIS A 296       9.869  -4.307  60.101  1.00 97.39           O  
ANISOU 3132  O   HIS A 296    17361  11833   7808   2162  -1620   2863       O  
ATOM   3133  CB  HIS A 296       9.889  -1.876  57.863  1.00102.35           C  
ANISOU 3133  CB  HIS A 296    17125  12641   9120   1663  -1589   2061       C  
ATOM   3134  CG  HIS A 296       8.993  -1.452  58.981  1.00101.94           C  
ANISOU 3134  CG  HIS A 296    17404  12654   8674   1514  -1469   2053       C  
ATOM   3135  ND1 HIS A 296       9.466  -0.968  60.181  1.00103.31           N  
ANISOU 3135  ND1 HIS A 296    17716  13116   8420   1552  -1736   2055       N  
ATOM   3136  CD2 HIS A 296       7.642  -1.433  59.074  1.00100.51           C  
ANISOU 3136  CD2 HIS A 296    17433  12303   8454   1323  -1097   2035       C  
ATOM   3137  CE1 HIS A 296       8.444  -0.678  60.968  1.00102.70           C  
ANISOU 3137  CE1 HIS A 296    17955  13022   8044   1403  -1507   2034       C  
ATOM   3138  NE2 HIS A 296       7.327  -0.949  60.319  1.00101.08           N  
ANISOU 3138  NE2 HIS A 296    17776  12546   8082   1270  -1111   2028       N  
ATOM   3139  N   VAL A 297       8.891  -4.841  58.142  1.00 96.34           N  
ANISOU 3139  N   VAL A 297    17052  11206   8345   1956  -1128   2716       N  
ATOM   3140  CA  VAL A 297       7.976  -5.791  58.766  1.00 95.82           C  
ANISOU 3140  CA  VAL A 297    17429  10877   8100   1936   -847   2979       C  
ATOM   3141  C   VAL A 297       8.719  -7.055  59.180  1.00 97.13           C  
ANISOU 3141  C   VAL A 297    17819  10890   8195   2296   -963   3340       C  
ATOM   3142  O   VAL A 297       8.543  -7.562  60.294  1.00 98.87           O  
ANISOU 3142  O   VAL A 297    18253  11137   8175   2326   -931   3529       O  
ATOM   3143  CB  VAL A 297       6.809  -6.106  57.815  1.00 93.28           C  
ANISOU 3143  CB  VAL A 297    17112  10240   8090   1666   -445   2883       C  
ATOM   3144  CG1 VAL A 297       5.914  -7.180  58.409  1.00 93.04           C  
ANISOU 3144  CG1 VAL A 297    17524   9914   7912   1614   -138   3165       C  
ATOM   3145  CG2 VAL A 297       6.015  -4.844  57.524  1.00 92.18           C  
ANISOU 3145  CG2 VAL A 297    16753  10273   7997   1352   -332   2566       C  
ATOM   3146  N   ILE A 298       9.561  -7.583  58.290  1.00 97.07           N  
ANISOU 3146  N   ILE A 298    17616  10756   8509   2525  -1062   3365       N  
ATOM   3147  CA  ILE A 298      10.252  -8.838  58.572  1.00 98.84           C  
ANISOU 3147  CA  ILE A 298    17942  10815   8796   2855  -1118   3653       C  
ATOM   3148  C   ILE A 298      11.282  -8.648  59.679  1.00102.62           C  
ANISOU 3148  C   ILE A 298    18326  11679   8987   3102  -1518   3792       C  
ATOM   3149  O   ILE A 298      11.415  -9.493  60.573  1.00107.04           O  
ANISOU 3149  O   ILE A 298    19077  12190   9402   3247  -1530   4055       O  
ATOM   3150  CB  ILE A 298      10.893  -9.392  57.287  1.00 98.59           C  
ANISOU 3150  CB  ILE A 298    17740  10546   9175   3066  -1093   3626       C  
ATOM   3151  CG1 ILE A 298       9.817  -9.698  56.244  1.00 96.60           C  
ANISOU 3151  CG1 ILE A 298    17618   9900   9185   2779   -694   3491       C  
ATOM   3152  CG2 ILE A 298      11.703 -10.644  57.586  1.00102.54           C  
ANISOU 3152  CG2 ILE A 298    18296  10895   9771   3435  -1153   3898       C  
ATOM   3153  CD1 ILE A 298      10.371 -10.000  54.872  1.00 96.59           C  
ANISOU 3153  CD1 ILE A 298    17362   9733   9606   2879   -644   3335       C  
ATOM   3154  N   GLN A 299      12.019  -7.536  59.645  1.00103.09           N  
ANISOU 3154  N   GLN A 299    18085  12132   8951   3129  -1861   3615       N  
ATOM   3155  CA  GLN A 299      13.047  -7.294  60.650  1.00106.92           C  
ANISOU 3155  CA  GLN A 299    18426  13030   9170   3318  -2282   3715       C  
ATOM   3156  C   GLN A 299      12.445  -6.971  62.014  1.00109.10           C  
ANISOU 3156  C   GLN A 299    18973  13483   8997   3121  -2277   3752       C  
ATOM   3157  O   GLN A 299      13.148  -7.066  63.027  1.00113.65           O  
ANISOU 3157  O   GLN A 299    19531  14342   9309   3268  -2574   3905       O  
ATOM   3158  CB  GLN A 299      13.967  -6.162  60.179  1.00106.40           C  
ANISOU 3158  CB  GLN A 299    17938  13340   9149   3337  -2645   3472       C  
ATOM   3159  CG  GLN A 299      15.260  -5.996  60.969  1.00110.39           C  
ANISOU 3159  CG  GLN A 299    18166  14293   9483   3548  -3125   3563       C  
ATOM   3160  CD  GLN A 299      16.195  -7.186  60.819  1.00114.24           C  
ANISOU 3160  CD  GLN A 299    18508  14689  10210   3972  -3213   3858       C  
ATOM   3161  OE1 GLN A 299      16.328  -8.005  61.728  1.00118.91           O  
ANISOU 3161  OE1 GLN A 299    19287  15254  10638   4130  -3255   4144       O  
ATOM   3162  NE2 GLN A 299      16.849  -7.283  59.665  1.00112.78           N  
ANISOU 3162  NE2 GLN A 299    17989  14448  10415   4167  -3229   3789       N  
ATOM   3163  N   ASP A 300      11.163  -6.602  62.060  1.00108.79           N  
ANISOU 3163  N   ASP A 300    19170  13296   8867   2797  -1937   3618       N  
ATOM   3164  CA  ASP A 300      10.372  -6.317  63.258  1.00110.61           C  
ANISOU 3164  CA  ASP A 300    19682  13641   8703   2591  -1816   3628       C  
ATOM   3165  C   ASP A 300      10.826  -5.073  64.015  1.00111.53           C  
ANISOU 3165  C   ASP A 300    19693  14216   8466   2492  -2142   3423       C  
ATOM   3166  O   ASP A 300      10.248  -4.768  65.066  1.00113.58           O  
ANISOU 3166  O   ASP A 300    20188  14599   8367   2336  -2052   3409       O  
ATOM   3167  CB  ASP A 300      10.336  -7.497  64.243  1.00114.14           C  
ANISOU 3167  CB  ASP A 300    20405  13979   8984   2742  -1752   3984       C  
ATOM   3168  CG  ASP A 300       9.459  -8.640  63.761  1.00113.69           C  
ANISOU 3168  CG  ASP A 300    20571  13434   9192   2697  -1321   4139       C  
ATOM   3169  OD1 ASP A 300       8.500  -8.378  63.005  1.00109.55           O  
ANISOU 3169  OD1 ASP A 300    20058  12708   8858   2443  -1005   3957       O  
ATOM   3170  OD2 ASP A 300       9.718  -9.799  64.153  1.00117.86           O  
ANISOU 3170  OD2 ASP A 300    21263  13782   9735   2899  -1301   4440       O  
ATOM   3171  N   ASN A 301      11.828  -4.345  63.531  1.00112.78           N  
ANISOU 3171  N   ASN A 301    19508  14629   8712   2558  -2504   3249       N  
ATOM   3172  CA  ASN A 301      12.194  -3.069  64.129  1.00113.46           C  
ANISOU 3172  CA  ASN A 301    19491  15120   8499   2385  -2793   2984       C  
ATOM   3173  C   ASN A 301      11.434  -1.933  63.451  1.00108.88           C  
ANISOU 3173  C   ASN A 301    18900  14470   8000   2086  -2598   2625       C  
ATOM   3174  O   ASN A 301      11.292  -1.906  62.224  1.00107.56           O  
ANISOU 3174  O   ASN A 301    18528  14098   8244   2052  -2450   2522       O  
ATOM   3175  CB  ASN A 301      13.709  -2.843  64.059  1.00115.54           C  
ANISOU 3175  CB  ASN A 301    19358  15734   8807   2568  -3309   2974       C  
ATOM   3176  CG  ASN A 301      14.273  -2.984  62.651  1.00112.60           C  
ANISOU 3176  CG  ASN A 301    18647  15237   8899   2724  -3358   2932       C  
ATOM   3177  OD1 ASN A 301      13.541  -3.192  61.684  1.00110.27           O  
ANISOU 3177  OD1 ASN A 301    18405  14591   8901   2661  -3007   2882       O  
ATOM   3178  ND2 ASN A 301      15.592  -2.874  62.536  1.00114.82           N  
ANISOU 3178  ND2 ASN A 301    18525  15828   9273   2903  -3775   2941       N  
ATOM   3179  N   LEU A 302      10.913  -1.013  64.263  1.00109.86           N  
ANISOU 3179  N   LEU A 302    19192  14756   7793   1843  -2546   2415       N  
ATOM   3180  CA  LEU A 302      10.112   0.080  63.729  1.00107.76           C  
ANISOU 3180  CA  LEU A 302    18948  14405   7589   1569  -2323   2083       C  
ATOM   3181  C   LEU A 302      10.946   0.964  62.810  1.00108.08           C  
ANISOU 3181  C   LEU A 302    18502  14575   7990   1466  -2553   1787       C  
ATOM   3182  O   LEU A 302      12.160   1.109  62.978  1.00109.87           O  
ANISOU 3182  O   LEU A 302    18502  15080   8163   1560  -2983   1780       O  
ATOM   3183  CB  LEU A 302       9.497   0.909  64.857  1.00110.01           C  
ANISOU 3183  CB  LEU A 302    19476  14842   7479   1357  -2209   1894       C  
ATOM   3184  CG  LEU A 302       8.334   0.231  65.583  1.00111.32           C  
ANISOU 3184  CG  LEU A 302    19974  14839   7485   1339  -1789   2088       C  
ATOM   3185  CD1 LEU A 302       7.876   1.046  66.783  1.00114.10           C  
ANISOU 3185  CD1 LEU A 302    20552  15381   7418   1173  -1706   1903       C  
ATOM   3186  CD2 LEU A 302       7.182   0.011  64.611  1.00107.40           C  
ANISOU 3186  CD2 LEU A 302    19499  13996   7312   1248  -1339   2089       C  
ATOM   3187  N   ILE A 303      10.277   1.556  61.829  1.00102.04           N  
ANISOU 3187  N   ILE A 303    17562  13615   7592   1265  -2259   1556       N  
ATOM   3188  CA  ILE A 303      10.969   2.218  60.734  1.00102.18           C  
ANISOU 3188  CA  ILE A 303    17127  13676   8021   1175  -2390   1330       C  
ATOM   3189  C   ILE A 303      11.363   3.628  61.149  1.00103.03           C  
ANISOU 3189  C   ILE A 303    17171  14022   7952    942  -2600    995       C  
ATOM   3190  O   ILE A 303      10.681   4.289  61.941  1.00102.73           O  
ANISOU 3190  O   ILE A 303    17438  14004   7590    793  -2480    849       O  
ATOM   3191  CB  ILE A 303      10.100   2.214  59.460  1.00 98.48           C  
ANISOU 3191  CB  ILE A 303    16520  12898   8002   1071  -2003   1253       C  
ATOM   3192  CG1 ILE A 303      10.968   2.510  58.238  1.00 98.90           C  
ANISOU 3192  CG1 ILE A 303    16120  12974   8484   1057  -2137   1126       C  
ATOM   3193  CG2 ILE A 303       8.948   3.203  59.577  1.00 97.25           C  
ANISOU 3193  CG2 ILE A 303    16514  12658   7779    829  -1707   1021       C  
ATOM   3194  CD1 ILE A 303      12.009   1.445  57.993  1.00100.20           C  
ANISOU 3194  CD1 ILE A 303    16108  13186   8775   1340  -2352   1365       C  
ATOM   3195  N   ARG A 304      12.492   4.083  60.616  1.00 98.10           N  
ANISOU 3195  N   ARG A 304    16155  13573   7545    902  -2900    865       N  
ATOM   3196  CA  ARG A 304      13.031   5.401  60.928  1.00 99.08           C  
ANISOU 3196  CA  ARG A 304    16186  13914   7545    644  -3132    537       C  
ATOM   3197  C   ARG A 304      12.162   6.455  60.253  1.00 97.44           C  
ANISOU 3197  C   ARG A 304    15992  13469   7561    393  -2792    253       C  
ATOM   3198  O   ARG A 304      12.100   6.518  59.021  1.00 96.60           O  
ANISOU 3198  O   ARG A 304    15612  13194   7899    366  -2629    221       O  
ATOM   3199  CB  ARG A 304      14.479   5.487  60.455  1.00101.65           C  
ANISOU 3199  CB  ARG A 304    16039  14489   8095    662  -3517    510       C  
ATOM   3200  CG  ARG A 304      15.495   4.754  61.334  1.00103.86           C  
ANISOU 3200  CG  ARG A 304    16272  15105   8085    892  -3956    740       C  
ATOM   3201  CD  ARG A 304      15.425   3.244  61.114  1.00103.64           C  
ANISOU 3201  CD  ARG A 304    16276  14933   8169   1280  -3858   1142       C  
ATOM   3202  NE  ARG A 304      15.642   2.876  59.717  1.00103.18           N  
ANISOU 3202  NE  ARG A 304    15859  14687   8658   1366  -3682   1173       N  
ATOM   3203  CZ  ARG A 304      15.331   1.691  59.199  1.00102.36           C  
ANISOU 3203  CZ  ARG A 304    15813  14326   8755   1632  -3460   1439       C  
ATOM   3204  NH1 ARG A 304      14.786   0.751  59.961  1.00101.87           N  
ANISOU 3204  NH1 ARG A 304    16146  14146   8414   1831  -3377   1718       N  
ATOM   3205  NH2 ARG A 304      15.558   1.445  57.916  1.00102.12           N  
ANISOU 3205  NH2 ARG A 304    15473  14139   9190   1682  -3302   1421       N  
ATOM   3206  N   LYS A 305      11.484   7.280  61.059  1.00 96.78           N  
ANISOU 3206  N   LYS A 305    16246  13370   7156    228  -2676     53       N  
ATOM   3207  CA  LYS A 305      10.462   8.174  60.522  1.00 95.22           C  
ANISOU 3207  CA  LYS A 305    16119  12913   7146     64  -2298   -164       C  
ATOM   3208  C   LYS A 305      11.017   9.112  59.456  1.00 95.21           C  
ANISOU 3208  C   LYS A 305    15775  12861   7539   -121  -2354   -390       C  
ATOM   3209  O   LYS A 305      10.308   9.445  58.500  1.00 93.81           O  
ANISOU 3209  O   LYS A 305    15513  12442   7688   -162  -2050   -441       O  
ATOM   3210  CB  LYS A 305       9.812   8.974  61.654  1.00 98.80           C  
ANISOU 3210  CB  LYS A 305    16994  13379   7165    -59  -2186   -368       C  
ATOM   3211  CG  LYS A 305       8.690   9.894  61.195  1.00 97.42           C  
ANISOU 3211  CG  LYS A 305    16911  12933   7172   -170  -1771   -572       C  
ATOM   3212  CD  LYS A 305       7.975  10.539  62.370  1.00 97.69           C  
ANISOU 3212  CD  LYS A 305    17394  12964   6760   -234  -1598   -751       C  
ATOM   3213  CE  LYS A 305       6.992  11.595  61.895  1.00 96.72           C  
ANISOU 3213  CE  LYS A 305    17326  12574   6848   -316  -1211   -976       C  
ATOM   3214  NZ  LYS A 305       5.898  11.001  61.079  1.00 95.36           N  
ANISOU 3214  NZ  LYS A 305    17012  12214   7008   -173   -840   -767       N  
ATOM   3215  N   GLU A 306      12.274   9.543  59.585  1.00 96.44           N  
ANISOU 3215  N   GLU A 306    15720  13253   7668   -243  -2738   -513       N  
ATOM   3216  CA  GLU A 306      12.857  10.355  58.522  1.00 96.53           C  
ANISOU 3216  CA  GLU A 306    15391  13213   8073   -434  -2768   -694       C  
ATOM   3217  C   GLU A 306      13.366   9.508  57.365  1.00 96.66           C  
ANISOU 3217  C   GLU A 306    15008  13222   8497   -273  -2775   -481       C  
ATOM   3218  O   GLU A 306      13.304   9.948  56.213  1.00 95.97           O  
ANISOU 3218  O   GLU A 306    14713  12972   8780   -366  -2603   -557       O  
ATOM   3219  CB  GLU A 306      13.984  11.238  59.061  1.00105.35           C  
ANISOU 3219  CB  GLU A 306    16413  14582   9033   -691  -3149   -940       C  
ATOM   3220  CG  GLU A 306      13.505  12.399  59.915  1.00105.14           C  
ANISOU 3220  CG  GLU A 306    16783  14481   8686   -930  -3088  -1254       C  
ATOM   3221  CD  GLU A 306      14.637  13.314  60.336  1.00106.91           C  
ANISOU 3221  CD  GLU A 306    16904  14928   8788  -1251  -3465  -1533       C  
ATOM   3222  OE1 GLU A 306      15.809  12.977  60.064  1.00108.46           O  
ANISOU 3222  OE1 GLU A 306    16688  15396   9127  -1269  -3801  -1453       O  
ATOM   3223  OE2 GLU A 306      14.355  14.375  60.930  1.00106.86           O  
ANISOU 3223  OE2 GLU A 306    17224  14823   8553  -1491  -3416  -1841       O  
ATOM   3224  N   VAL A 307      13.868   8.301  57.638  1.00 93.15           N  
ANISOU 3224  N   VAL A 307    14474  12938   7980    -20  -2956   -213       N  
ATOM   3225  CA  VAL A 307      14.282   7.424  56.547  1.00 93.34           C  
ANISOU 3225  CA  VAL A 307    14168  12914   8382    168  -2910    -18       C  
ATOM   3226  C   VAL A 307      13.062   6.886  55.808  1.00 91.21           C  
ANISOU 3226  C   VAL A 307    14043  12313   8298    267  -2496     98       C  
ATOM   3227  O   VAL A 307      13.101   6.688  54.587  1.00 90.85           O  
ANISOU 3227  O   VAL A 307    13765  12135   8617    290  -2345    124       O  
ATOM   3228  CB  VAL A 307      15.178   6.291  57.084  1.00 94.98           C  
ANISOU 3228  CB  VAL A 307    14262  13363   8464    449  -3215    244       C  
ATOM   3229  CG1 VAL A 307      15.552   5.318  55.974  1.00 95.24           C  
ANISOU 3229  CG1 VAL A 307    14003  13301   8883    681  -3117    439       C  
ATOM   3230  CG2 VAL A 307      16.429   6.871  57.734  1.00 97.32           C  
ANISOU 3230  CG2 VAL A 307    14335  14043   8599    327  -3665    121       C  
ATOM   3231  N   TYR A 308      11.958   6.661  56.524  1.00 90.62           N  
ANISOU 3231  N   TYR A 308    14347  12117   7968    305  -2302    159       N  
ATOM   3232  CA  TYR A 308      10.715   6.246  55.882  1.00 88.65           C  
ANISOU 3232  CA  TYR A 308    14212  11584   7888    346  -1914    244       C  
ATOM   3233  C   TYR A 308      10.175   7.339  54.966  1.00 87.62           C  
ANISOU 3233  C   TYR A 308    13982  11297   8012    148  -1702     26       C  
ATOM   3234  O   TYR A 308       9.981   7.122  53.764  1.00 86.91           O  
ANISOU 3234  O   TYR A 308    13704  11066   8250    159  -1548     63       O  
ATOM   3235  CB  TYR A 308       9.676   5.878  56.943  1.00 90.36           C  
ANISOU 3235  CB  TYR A 308    14828  11744   7763    398  -1743    345       C  
ATOM   3236  CG  TYR A 308       8.334   5.482  56.372  1.00 88.54           C  
ANISOU 3236  CG  TYR A 308    14686  11258   7698    402  -1347    426       C  
ATOM   3237  CD1 TYR A 308       8.123   4.213  55.851  1.00 87.87           C  
ANISOU 3237  CD1 TYR A 308    14574  11037   7775    542  -1237    662       C  
ATOM   3238  CD2 TYR A 308       7.280   6.387  56.339  1.00 87.64           C  
ANISOU 3238  CD2 TYR A 308    14672  11040   7588    263  -1085    259       C  
ATOM   3239  CE1 TYR A 308       6.897   3.854  55.327  1.00 86.30           C  
ANISOU 3239  CE1 TYR A 308    14434  10632   7726    497   -900    719       C  
ATOM   3240  CE2 TYR A 308       6.052   6.037  55.813  1.00 86.30           C  
ANISOU 3240  CE2 TYR A 308    14522  10687   7580    260   -749    338       C  
ATOM   3241  CZ  TYR A 308       5.866   4.769  55.309  1.00 85.60           C  
ANISOU 3241  CZ  TYR A 308    14390  10493   7640    354   -670    562       C  
ATOM   3242  OH  TYR A 308       4.644   4.416  54.786  1.00 84.36           O  
ANISOU 3242  OH  TYR A 308    14234  10179   7641    304   -359    625       O  
ATOM   3243  N   ILE A 309       9.911   8.524  55.526  1.00 87.25           N  
ANISOU 3243  N   ILE A 309    14092  11260   7798    -26  -1687   -201       N  
ATOM   3244  CA  ILE A 309       9.317   9.610  54.748  1.00 86.24           C  
ANISOU 3244  CA  ILE A 309    13925  10951   7892   -179  -1467   -385       C  
ATOM   3245  C   ILE A 309      10.231  10.025  53.603  1.00 86.72           C  
ANISOU 3245  C   ILE A 309    13644  11021   8285   -279  -1575   -457       C  
ATOM   3246  O   ILE A 309       9.756  10.431  52.534  1.00 85.72           O  
ANISOU 3246  O   ILE A 309    13418  10723   8429   -329  -1371   -488       O  
ATOM   3247  CB  ILE A 309       8.974  10.798  55.671  1.00 87.95           C  
ANISOU 3247  CB  ILE A 309    14418  11153   7847   -325  -1432   -627       C  
ATOM   3248  CG1 ILE A 309       7.890  10.392  56.672  1.00 87.55           C  
ANISOU 3248  CG1 ILE A 309    14704  11073   7486   -215  -1230   -548       C  
ATOM   3249  CG2 ILE A 309       8.522  12.008  54.866  1.00 87.10           C  
ANISOU 3249  CG2 ILE A 309    14275  10836   7984   -461  -1231   -812       C  
ATOM   3250  CD1 ILE A 309       7.671  11.396  57.786  1.00 88.09           C  
ANISOU 3250  CD1 ILE A 309    15098  11160   7211   -326  -1210   -786       C  
ATOM   3251  N   LEU A 310      11.549   9.925  53.797  1.00 83.69           N  
ANISOU 3251  N   LEU A 310    13062  10855   7880   -308  -1892   -471       N  
ATOM   3252  CA  LEU A 310      12.494  10.192  52.716  1.00 84.54           C  
ANISOU 3252  CA  LEU A 310    12809  11004   8308   -397  -1972   -513       C  
ATOM   3253  C   LEU A 310      12.156   9.379  51.474  1.00 83.86           C  
ANISOU 3253  C   LEU A 310    12571  10779   8515   -252  -1765   -344       C  
ATOM   3254  O   LEU A 310      11.851   9.932  50.413  1.00 83.03           O  
ANISOU 3254  O   LEU A 310    12380  10522   8646   -349  -1582   -406       O  
ATOM   3255  CB  LEU A 310      13.920   9.884  53.175  1.00 83.38           C  
ANISOU 3255  CB  LEU A 310    12420  11165   8098   -385  -2342   -492       C  
ATOM   3256  CG  LEU A 310      15.011  10.042  52.112  1.00 84.80           C  
ANISOU 3256  CG  LEU A 310    12173  11438   8612   -461  -2416   -515       C  
ATOM   3257  CD1 LEU A 310      15.104  11.482  51.637  1.00 84.36           C  
ANISOU 3257  CD1 LEU A 310    12083  11281   8690   -787  -2343   -759       C  
ATOM   3258  CD2 LEU A 310      16.359   9.547  52.627  1.00 87.35           C  
ANISOU 3258  CD2 LEU A 310    12204  12107   8877   -385  -2782   -449       C  
ATOM   3259  N   LEU A 311      12.188   8.051  51.603  1.00 81.46           N  
ANISOU 3259  N   LEU A 311    12265  10510   8176    -18  -1790   -129       N  
ATOM   3260  CA  LEU A 311      11.977   7.174  50.458  1.00 81.11           C  
ANISOU 3260  CA  LEU A 311    12099  10331   8387    111  -1613     10       C  
ATOM   3261  C   LEU A 311      10.581   7.317  49.868  1.00 78.93           C  
ANISOU 3261  C   LEU A 311    11984   9819   8185     59  -1305      5       C  
ATOM   3262  O   LEU A 311      10.375   6.966  48.702  1.00 78.56           O  
ANISOU 3262  O   LEU A 311    11824   9661   8365     78  -1156     49       O  
ATOM   3263  CB  LEU A 311      12.239   5.730  50.873  1.00 78.20           C  
ANISOU 3263  CB  LEU A 311    11772  10000   7939    373  -1689    237       C  
ATOM   3264  CG  LEU A 311      13.669   5.525  51.376  1.00 80.62           C  
ANISOU 3264  CG  LEU A 311    11857  10577   8198    476  -2017    277       C  
ATOM   3265  CD1 LEU A 311      13.867   4.117  51.883  1.00 81.07           C  
ANISOU 3265  CD1 LEU A 311    12006  10643   8155    781  -2089    533       C  
ATOM   3266  CD2 LEU A 311      14.686   5.863  50.297  1.00 82.34           C  
ANISOU 3266  CD2 LEU A 311    11681  10884   8720    419  -2055    196       C  
ATOM   3267  N   ASN A 312       9.620   7.823  50.645  1.00 79.21           N  
ANISOU 3267  N   ASN A 312    12272   9797   8028      0  -1206    -51       N  
ATOM   3268  CA  ASN A 312       8.305   8.121  50.089  1.00 77.53           C  
ANISOU 3268  CA  ASN A 312    12148   9402   7907    -48   -928    -64       C  
ATOM   3269  C   ASN A 312       8.347   9.366  49.212  1.00 77.25           C  
ANISOU 3269  C   ASN A 312    11993   9299   8060   -198   -869   -218       C  
ATOM   3270  O   ASN A 312       7.524   9.509  48.300  1.00 76.19           O  
ANISOU 3270  O   ASN A 312    11826   9037   8084   -211   -679   -195       O  
ATOM   3271  CB  ASN A 312       7.287   8.294  51.218  1.00 77.55           C  
ANISOU 3271  CB  ASN A 312    12433   9379   7655    -38   -808    -72       C  
ATOM   3272  CG  ASN A 312       5.855   8.053  50.765  1.00 76.26           C  
ANISOU 3272  CG  ASN A 312    12319   9074   7582    -22   -520      2       C  
ATOM   3273  OD1 ASN A 312       4.960   7.865  51.588  1.00 75.97           O  
ANISOU 3273  OD1 ASN A 312    12474   9024   7368      9   -375     47       O  
ATOM   3274  ND2 ASN A 312       5.635   8.050  49.455  1.00 75.69           N  
ANISOU 3274  ND2 ASN A 312    12064   8919   7774    -53   -436     17       N  
ATOM   3275  N   TRP A 313       9.292  10.273  49.471  1.00 77.21           N  
ANISOU 3275  N   TRP A 313    11927   9376   8033   -324  -1036   -368       N  
ATOM   3276  CA  TRP A 313       9.438  11.471  48.650  1.00 76.69           C  
ANISOU 3276  CA  TRP A 313    11777   9214   8149   -485   -973   -501       C  
ATOM   3277  C   TRP A 313      10.211  11.217  47.364  1.00 77.21           C  
ANISOU 3277  C   TRP A 313    11564   9305   8468   -507   -988   -447       C  
ATOM   3278  O   TRP A 313       9.993  11.925  46.375  1.00 76.10           O  
ANISOU 3278  O   TRP A 313    11377   9044   8495   -596   -856   -479       O  
ATOM   3279  CB  TRP A 313      10.092  12.584  49.465  1.00 82.70           C  
ANISOU 3279  CB  TRP A 313    12618  10021   8783   -663  -1121   -704       C  
ATOM   3280  CG  TRP A 313       9.095  13.370  50.236  1.00 81.86           C  
ANISOU 3280  CG  TRP A 313    12817   9779   8506   -681   -979   -817       C  
ATOM   3281  CD1 TRP A 313       8.579  13.071  51.459  1.00 82.13           C  
ANISOU 3281  CD1 TRP A 313    13089   9865   8253   -600   -978   -822       C  
ATOM   3282  CD2 TRP A 313       8.522  14.623  49.851  1.00 80.88           C  
ANISOU 3282  CD2 TRP A 313    12813   9436   8482   -771   -796   -940       C  
ATOM   3283  NE1 TRP A 313       7.691  14.044  51.846  1.00 81.58           N  
ANISOU 3283  NE1 TRP A 313    13265   9628   8104   -627   -783   -956       N  
ATOM   3284  CE2 TRP A 313       7.645  15.014  50.879  1.00 80.86           C  
ANISOU 3284  CE2 TRP A 313    13106   9358   8258   -719   -675  -1028       C  
ATOM   3285  CE3 TRP A 313       8.659  15.449  48.730  1.00 80.09           C  
ANISOU 3285  CE3 TRP A 313    12616   9184   8631   -875   -705   -968       C  
ATOM   3286  CZ2 TRP A 313       6.908  16.196  50.822  1.00 80.33           C  
ANISOU 3286  CZ2 TRP A 313    13229   9058   8233   -740   -464  -1152       C  
ATOM   3287  CZ3 TRP A 313       7.928  16.619  48.675  1.00 79.34           C  
ANISOU 3287  CZ3 TRP A 313    12726   8851   8570   -902   -515  -1069       C  
ATOM   3288  CH2 TRP A 313       7.063  16.982  49.714  1.00 79.58           C  
ANISOU 3288  CH2 TRP A 313    13039   8800   8400   -822   -395  -1163       C  
ATOM   3289  N   ILE A 314      11.116  10.235  47.349  1.00 75.02           N  
ANISOU 3289  N   ILE A 314    11111   9179   8213   -411  -1132   -358       N  
ATOM   3290  CA  ILE A 314      11.635   9.763  46.069  1.00 75.92           C  
ANISOU 3290  CA  ILE A 314    10994   9297   8557   -377  -1071   -289       C  
ATOM   3291  C   ILE A 314      10.491   9.251  45.204  1.00 74.27           C  
ANISOU 3291  C   ILE A 314    10877   8923   8418   -302   -848   -195       C  
ATOM   3292  O   ILE A 314      10.505   9.397  43.975  1.00 73.87           O  
ANISOU 3292  O   ILE A 314    10723   8814   8529   -347   -733   -188       O  
ATOM   3293  CB  ILE A 314      12.724   8.693  46.277  1.00 73.85           C  
ANISOU 3293  CB  ILE A 314    10541   9211   8307   -223  -1237   -198       C  
ATOM   3294  CG1 ILE A 314      13.996   9.315  46.861  1.00 75.68           C  
ANISOU 3294  CG1 ILE A 314    10574   9661   8519   -338  -1482   -300       C  
ATOM   3295  CG2 ILE A 314      13.057   7.996  44.971  1.00 75.24           C  
ANISOU 3295  CG2 ILE A 314    10539   9353   8695   -136  -1109   -122       C  
ATOM   3296  CD1 ILE A 314      14.082   9.292  48.360  1.00 75.76           C  
ANISOU 3296  CD1 ILE A 314    10726   9802   8258   -314  -1704   -319       C  
ATOM   3297  N   GLY A 315       9.473   8.661  45.832  1.00 74.73           N  
ANISOU 3297  N   GLY A 315    11132   8920   8342   -207   -784   -121       N  
ATOM   3298  CA  GLY A 315       8.275   8.301  45.095  1.00 73.05           C  
ANISOU 3298  CA  GLY A 315    10990   8576   8191   -186   -589    -51       C  
ATOM   3299  C   GLY A 315       7.442   9.506  44.699  1.00 71.16           C  
ANISOU 3299  C   GLY A 315    10797   8246   7995   -288   -468   -120       C  
ATOM   3300  O   GLY A 315       6.810   9.510  43.640  1.00 69.55           O  
ANISOU 3300  O   GLY A 315    10551   7976   7900   -304   -350    -77       O  
ATOM   3301  N   TYR A 316       7.424  10.543  45.542  1.00 74.97           N  
ANISOU 3301  N   TYR A 316    11383   8720   8382   -348   -499   -226       N  
ATOM   3302  CA  TYR A 316       6.636  11.735  45.244  1.00 73.56           C  
ANISOU 3302  CA  TYR A 316    11280   8418   8252   -403   -366   -285       C  
ATOM   3303  C   TYR A 316       7.169  12.475  44.023  1.00 72.56           C  
ANISOU 3303  C   TYR A 316    11032   8235   8303   -503   -349   -307       C  
ATOM   3304  O   TYR A 316       6.387  13.019  43.233  1.00 71.10           O  
ANISOU 3304  O   TYR A 316    10864   7948   8203   -494   -220   -265       O  
ATOM   3305  CB  TYR A 316       6.595  12.655  46.468  1.00 75.58           C  
ANISOU 3305  CB  TYR A 316    11722   8643   8353   -444   -387   -422       C  
ATOM   3306  CG  TYR A 316       5.611  12.235  47.543  1.00 76.07           C  
ANISOU 3306  CG  TYR A 316    11957   8718   8228   -337   -300   -392       C  
ATOM   3307  CD1 TYR A 316       4.606  11.317  47.269  1.00 75.97           C  
ANISOU 3307  CD1 TYR A 316    11913   8712   8241   -240   -173   -247       C  
ATOM   3308  CD2 TYR A 316       5.675  12.770  48.827  1.00 76.74           C  
ANISOU 3308  CD2 TYR A 316    12245   8813   8099   -359   -331   -518       C  
ATOM   3309  CE1 TYR A 316       3.695  10.936  48.240  1.00 76.51           C  
ANISOU 3309  CE1 TYR A 316    12125   8799   8148   -167    -58   -207       C  
ATOM   3310  CE2 TYR A 316       4.765  12.392  49.807  1.00 77.14           C  
ANISOU 3310  CE2 TYR A 316    12468   8884   7957   -262   -213   -485       C  
ATOM   3311  CZ  TYR A 316       3.779  11.474  49.505  1.00 77.02           C  
ANISOU 3311  CZ  TYR A 316    12394   8877   7992   -166    -66   -319       C  
ATOM   3312  OH  TYR A 316       2.870  11.090  50.467  1.00 77.40           O  
ANISOU 3312  OH  TYR A 316    12597   8952   7859    -93     85   -273       O  
ATOM   3313  N   VAL A 317       8.488  12.505  43.845  1.00 72.60           N  
ANISOU 3313  N   VAL A 317    10902   8319   8362   -595   -472   -357       N  
ATOM   3314  CA  VAL A 317       9.087  13.284  42.766  1.00 72.10           C  
ANISOU 3314  CA  VAL A 317    10735   8205   8454   -723   -429   -379       C  
ATOM   3315  C   VAL A 317       8.922  12.542  41.444  1.00 71.19           C  
ANISOU 3315  C   VAL A 317    10506   8106   8435   -663   -341   -259       C  
ATOM   3316  O   VAL A 317       9.297  13.046  40.379  1.00 70.70           O  
ANISOU 3316  O   VAL A 317    10374   8009   8478   -750   -272   -243       O  
ATOM   3317  CB  VAL A 317      10.567  13.597  43.058  1.00 69.24           C  
ANISOU 3317  CB  VAL A 317    10228   7954   8127   -872   -576   -481       C  
ATOM   3318  CG1 VAL A 317      10.676  14.440  44.305  1.00 69.72           C  
ANISOU 3318  CG1 VAL A 317    10439   7989   8064   -976   -673   -631       C  
ATOM   3319  CG2 VAL A 317      11.383  12.323  43.188  1.00 71.64           C  
ANISOU 3319  CG2 VAL A 317    10340   8452   8426   -768   -699   -423       C  
ATOM   3320  N   ASN A 318       8.346  11.340  41.502  1.00 74.49           N  
ANISOU 3320  N   ASN A 318    10935   8567   8802   -530   -331   -177       N  
ATOM   3321  CA  ASN A 318       8.014  10.636  40.273  1.00 73.18           C  
ANISOU 3321  CA  ASN A 318    10715   8396   8695   -494   -243    -92       C  
ATOM   3322  C   ASN A 318       6.946  11.369  39.471  1.00 70.78           C  
ANISOU 3322  C   ASN A 318    10475   8004   8412   -518   -137    -42       C  
ATOM   3323  O   ASN A 318       6.941  11.295  38.237  1.00 69.93           O  
ANISOU 3323  O   ASN A 318    10322   7900   8346   -546    -79      7       O  
ATOM   3324  CB  ASN A 318       7.537   9.223  40.585  1.00 70.88           C  
ANISOU 3324  CB  ASN A 318    10461   8128   8342   -382   -248    -30       C  
ATOM   3325  CG  ASN A 318       7.602   8.324  39.383  1.00 70.13           C  
ANISOU 3325  CG  ASN A 318    10316   8032   8298   -367   -182     12       C  
ATOM   3326  OD1 ASN A 318       7.457   7.116  39.501  1.00 70.30           O  
ANISOU 3326  OD1 ASN A 318    10380   8038   8294   -295   -174     47       O  
ATOM   3327  ND2 ASN A 318       7.845   8.906  38.216  1.00 69.47           N  
ANISOU 3327  ND2 ASN A 318    10174   7948   8274   -442   -121      4       N  
ATOM   3328  N   SER A 319       6.040  12.074  40.147  1.00 71.56           N  
ANISOU 3328  N   SER A 319    10684   8036   8472   -488   -106    -48       N  
ATOM   3329  CA  SER A 319       4.939  12.735  39.459  1.00 70.52           C  
ANISOU 3329  CA  SER A 319    10588   7837   8368   -455    -15     26       C  
ATOM   3330  C   SER A 319       5.404  13.882  38.571  1.00 70.29           C  
ANISOU 3330  C   SER A 319    10573   7718   8414   -530     25     38       C  
ATOM   3331  O   SER A 319       4.633  14.344  37.723  1.00 69.89           O  
ANISOU 3331  O   SER A 319    10543   7629   8384   -487     83    139       O  
ATOM   3332  CB  SER A 319       3.920  13.235  40.480  1.00 68.98           C  
ANISOU 3332  CB  SER A 319    10493   7589   8128   -368     39     13       C  
ATOM   3333  OG  SER A 319       3.337  12.148  41.174  1.00 69.45           O  
ANISOU 3333  OG  SER A 319    10545   7732   8112   -313     38     35       O  
ATOM   3334  N   GLY A 320       6.635  14.351  38.743  1.00 69.94           N  
ANISOU 3334  N   GLY A 320    10515   7649   8410   -648     -7    -48       N  
ATOM   3335  CA  GLY A 320       7.205  15.365  37.885  1.00 69.96           C  
ANISOU 3335  CA  GLY A 320    10536   7556   8489   -761     56    -29       C  
ATOM   3336  C   GLY A 320       8.129  14.849  36.808  1.00 70.29           C  
ANISOU 3336  C   GLY A 320    10444   7697   8565   -842     75      4       C  
ATOM   3337  O   GLY A 320       8.621  15.645  36.003  1.00 70.51           O  
ANISOU 3337  O   GLY A 320    10489   7655   8646   -953    155     39       O  
ATOM   3338  N   PHE A 321       8.378  13.540  36.761  1.00 70.19           N  
ANISOU 3338  N   PHE A 321    10319   7827   8522   -785     29     -4       N  
ATOM   3339  CA  PHE A 321       9.309  12.969  35.794  1.00 71.33           C  
ANISOU 3339  CA  PHE A 321    10340   8066   8698   -831     78      6       C  
ATOM   3340  C   PHE A 321       8.655  12.609  34.467  1.00 70.25           C  
ANISOU 3340  C   PHE A 321    10255   7940   8495   -799    159    101       C  
ATOM   3341  O   PHE A 321       9.332  12.624  33.432  1.00 71.19           O  
ANISOU 3341  O   PHE A 321    10334   8098   8618   -865    253    121       O  
ATOM   3342  CB  PHE A 321       9.981  11.722  36.377  1.00 67.72           C  
ANISOU 3342  CB  PHE A 321     9758   7729   8245   -754      5    -51       C  
ATOM   3343  CG  PHE A 321      10.979  12.018  37.460  1.00 70.19           C  
ANISOU 3343  CG  PHE A 321     9963   8098   8607   -806   -102   -140       C  
ATOM   3344  CD1 PHE A 321      11.473  13.300  37.637  1.00 70.32           C  
ANISOU 3344  CD1 PHE A 321     9976   8062   8681   -975   -102   -194       C  
ATOM   3345  CD2 PHE A 321      11.425  11.012  38.300  1.00 72.70           C  
ANISOU 3345  CD2 PHE A 321    10197   8520   8905   -694   -212   -164       C  
ATOM   3346  CE1 PHE A 321      12.394  13.572  38.632  1.00 72.57           C  
ANISOU 3346  CE1 PHE A 321    10151   8427   8994  -1063   -231   -296       C  
ATOM   3347  CE2 PHE A 321      12.345  11.276  39.295  1.00 75.31           C  
ANISOU 3347  CE2 PHE A 321    10413   8948   9254   -741   -351   -237       C  
ATOM   3348  CZ  PHE A 321      12.829  12.558  39.462  1.00 75.02           C  
ANISOU 3348  CZ  PHE A 321    10350   8888   9266   -941   -371   -316       C  
ATOM   3349  N   ASN A 322       7.364  12.280  34.471  1.00 71.52           N  
ANISOU 3349  N   ASN A 322    10497   8092   8584   -711    126    156       N  
ATOM   3350  CA  ASN A 322       6.702  11.883  33.231  1.00 71.18           C  
ANISOU 3350  CA  ASN A 322    10495   8097   8451   -704    159    233       C  
ATOM   3351  C   ASN A 322       6.697  12.966  32.155  1.00 71.41           C  
ANISOU 3351  C   ASN A 322    10595   8086   8452   -760    229    336       C  
ATOM   3352  O   ASN A 322       6.928  12.622  30.983  1.00 72.06           O  
ANISOU 3352  O   ASN A 322    10699   8236   8446   -803    287    367       O  
ATOM   3353  CB  ASN A 322       5.272  11.417  33.532  1.00 72.44           C  
ANISOU 3353  CB  ASN A 322    10682   8283   8557   -629     91    274       C  
ATOM   3354  CG  ASN A 322       5.234  10.075  34.229  1.00 72.26           C  
ANISOU 3354  CG  ASN A 322    10633   8294   8528   -599     56    202       C  
ATOM   3355  OD1 ASN A 322       5.980   9.160  33.880  1.00 72.92           O  
ANISOU 3355  OD1 ASN A 322    10703   8400   8602   -612     84    145       O  
ATOM   3356  ND2 ASN A 322       4.361   9.948  35.220  1.00 71.81           N  
ANISOU 3356  ND2 ASN A 322    10582   8228   8476   -547     17    212       N  
ATOM   3357  N   PRO A 323       6.434  14.246  32.448  1.00 70.99           N  
ANISOU 3357  N   PRO A 323    10613   7910   8451   -757    243    395       N  
ATOM   3358  CA  PRO A 323       6.434  15.243  31.362  1.00 71.42           C  
ANISOU 3358  CA  PRO A 323    10772   7897   8468   -798    322    528       C  
ATOM   3359  C   PRO A 323       7.778  15.409  30.672  1.00 72.21           C  
ANISOU 3359  C   PRO A 323    10850   8002   8582   -948    444    508       C  
ATOM   3360  O   PRO A 323       7.808  15.722  29.476  1.00 72.68           O  
ANISOU 3360  O   PRO A 323    10997   8073   8545   -987    525    624       O  
ATOM   3361  CB  PRO A 323       6.001  16.533  32.073  1.00 72.15           C  
ANISOU 3361  CB  PRO A 323    10966   7799   8648   -750    333    568       C  
ATOM   3362  CG  PRO A 323       5.239  16.069  33.256  1.00 71.77           C  
ANISOU 3362  CG  PRO A 323    10868   7778   8624   -639    248    492       C  
ATOM   3363  CD  PRO A 323       5.931  14.825  33.708  1.00 71.47           C  
ANISOU 3363  CD  PRO A 323    10706   7870   8579   -692    201    360       C  
ATOM   3364  N   LEU A 324       8.893  15.216  31.380  1.00 70.57           N  
ANISOU 3364  N   LEU A 324    10518   7810   8485  -1034    460    376       N  
ATOM   3365  CA  LEU A 324      10.196  15.327  30.729  1.00 72.02           C  
ANISOU 3365  CA  LEU A 324    10620   8037   8707  -1180    594    357       C  
ATOM   3366  C   LEU A 324      10.466  14.135  29.819  1.00 72.98           C  
ANISOU 3366  C   LEU A 324    10683   8320   8728  -1138    656    339       C  
ATOM   3367  O   LEU A 324      11.055  14.290  28.743  1.00 73.95           O  
ANISOU 3367  O   LEU A 324    10823   8481   8793  -1223    812    388       O  
ATOM   3368  CB  LEU A 324      11.307  15.469  31.769  1.00 74.42           C  
ANISOU 3368  CB  LEU A 324    10756   8355   9167  -1282    567    222       C  
ATOM   3369  CG  LEU A 324      11.597  16.879  32.290  1.00 74.33           C  
ANISOU 3369  CG  LEU A 324    10817   8167   9257  -1443    587    210       C  
ATOM   3370  CD1 LEU A 324      10.500  17.383  33.217  1.00 72.91           C  
ANISOU 3370  CD1 LEU A 324    10801   7836   9064  -1339    481    203       C  
ATOM   3371  CD2 LEU A 324      12.953  16.910  32.980  1.00 76.35           C  
ANISOU 3371  CD2 LEU A 324    10851   8512   9648  -1608    563     72       C  
ATOM   3372  N   ILE A 325      10.047  12.937  30.235  1.00 71.97           N  
ANISOU 3372  N   ILE A 325    10511   8267   8567  -1015    559    265       N  
ATOM   3373  CA  ILE A 325      10.192  11.762  29.386  1.00 73.16           C  
ANISOU 3373  CA  ILE A 325    10663   8521   8613   -971    627    226       C  
ATOM   3374  C   ILE A 325       9.302  11.876  28.156  1.00 72.43           C  
ANISOU 3374  C   ILE A 325    10749   8448   8321   -985    647    327       C  
ATOM   3375  O   ILE A 325       9.575  11.249  27.125  1.00 73.61           O  
ANISOU 3375  O   ILE A 325    10954   8675   8339  -1003    753    301       O  
ATOM   3376  CB  ILE A 325       9.880  10.489  30.196  1.00 69.28           C  
ANISOU 3376  CB  ILE A 325    10129   8053   8143   -850    522    132       C  
ATOM   3377  CG1 ILE A 325      10.779  10.418  31.432  1.00 70.71           C  
ANISOU 3377  CG1 ILE A 325    10140   8242   8487   -818    470     59       C  
ATOM   3378  CG2 ILE A 325      10.100   9.242  29.354  1.00 71.12           C  
ANISOU 3378  CG2 ILE A 325    10401   8340   8281   -806    616     64       C  
ATOM   3379  CD1 ILE A 325      10.369   9.357  32.427  1.00 70.65           C  
ANISOU 3379  CD1 ILE A 325    10131   8224   8488   -690    353     11       C  
ATOM   3380  N   TYR A 326       8.244  12.684  28.236  1.00 72.55           N  
ANISOU 3380  N   TYR A 326    10861   8404   8302   -966    547    443       N  
ATOM   3381  CA  TYR A 326       7.385  12.924  27.085  1.00 72.61           C  
ANISOU 3381  CA  TYR A 326    11016   8460   8111   -965    527    573       C  
ATOM   3382  C   TYR A 326       7.980  13.970  26.153  1.00 73.15           C  
ANISOU 3382  C   TYR A 326    11188   8487   8119  -1052    675    701       C  
ATOM   3383  O   TYR A 326       7.751  13.914  24.941  1.00 73.80           O  
ANISOU 3383  O   TYR A 326    11404   8653   7986  -1076    713    786       O  
ATOM   3384  CB  TYR A 326       5.995  13.341  27.562  1.00 73.43           C  
ANISOU 3384  CB  TYR A 326    11141   8539   8220   -868    361    667       C  
ATOM   3385  CG  TYR A 326       5.281  12.242  28.316  1.00 73.07           C  
ANISOU 3385  CG  TYR A 326    11009   8554   8201   -815    241    563       C  
ATOM   3386  CD1 TYR A 326       5.662  10.912  28.168  1.00 73.60           C  
ANISOU 3386  CD1 TYR A 326    11058   8683   8222   -852    265    424       C  
ATOM   3387  CD2 TYR A 326       4.260  12.533  29.208  1.00 72.56           C  
ANISOU 3387  CD2 TYR A 326    10894   8462   8215   -725    135    604       C  
ATOM   3388  CE1 TYR A 326       5.025   9.905  28.863  1.00 73.38           C  
ANISOU 3388  CE1 TYR A 326    10985   8672   8223   -825    177    343       C  
ATOM   3389  CE2 TYR A 326       3.620  11.533  29.912  1.00 72.38           C  
ANISOU 3389  CE2 TYR A 326    10796   8491   8215   -703     56    522       C  
ATOM   3390  CZ  TYR A 326       4.005  10.220  29.734  1.00 72.63           C  
ANISOU 3390  CZ  TYR A 326    10832   8567   8199   -765     73    398       C  
ATOM   3391  OH  TYR A 326       3.370   9.217  30.430  1.00 72.54           O  
ANISOU 3391  OH  TYR A 326    10780   8571   8213   -764     14    332       O  
ATOM   3392  N   CYS A 327       8.757  14.915  26.691  1.00 73.68           N  
ANISOU 3392  N   CYS A 327    11214   8426   8355  -1122    762    713       N  
ATOM   3393  CA  CYS A 327       9.562  15.792  25.847  1.00 74.42           C  
ANISOU 3393  CA  CYS A 327    11392   8466   8418  -1253    954    817       C  
ATOM   3394  C   CYS A 327      10.632  15.030  25.084  1.00 75.79           C  
ANISOU 3394  C   CYS A 327    11494   8778   8525  -1334   1135    732       C  
ATOM   3395  O   CYS A 327      11.339  15.629  24.267  1.00 76.55           O  
ANISOU 3395  O   CYS A 327    11652   8863   8569  -1458   1334    818       O  
ATOM   3396  CB  CYS A 327      10.220  16.890  26.683  1.00 75.59           C  
ANISOU 3396  CB  CYS A 327    11497   8438   8786  -1362   1010    810       C  
ATOM   3397  SG  CYS A 327       9.074  18.098  27.370  1.00 74.51           S  
ANISOU 3397  SG  CYS A 327    11525   8069   8715  -1262    890    930       S  
ATOM   3398  N   ARG A 328      10.784  13.740  25.347  1.00 73.10           N  
ANISOU 3398  N   ARG A 328    11034   8551   8190  -1261   1097    569       N  
ATOM   3399  CA  ARG A 328      11.644  12.880  24.556  1.00 74.78           C  
ANISOU 3399  CA  ARG A 328    11208   8887   8320  -1280   1283    478       C  
ATOM   3400  C   ARG A 328      10.925  12.302  23.339  1.00 74.81           C  
ANISOU 3400  C   ARG A 328    11431   8978   8017  -1254   1290    505       C  
ATOM   3401  O   ARG A 328      11.584  11.786  22.429  1.00 76.07           O  
ANISOU 3401  O   ARG A 328    11637   9225   8043  -1284   1491    446       O  
ATOM   3402  CB  ARG A 328      12.229  11.796  25.477  1.00 71.93           C  
ANISOU 3402  CB  ARG A 328    10632   8568   8131  -1187   1252    296       C  
ATOM   3403  CG  ARG A 328      12.962  10.674  24.807  1.00 74.00           C  
ANISOU 3403  CG  ARG A 328    10859   8930   8327  -1131   1434    177       C  
ATOM   3404  CD  ARG A 328      12.160   9.403  24.943  1.00 73.98           C  
ANISOU 3404  CD  ARG A 328    10958   8916   8234  -1008   1309     73       C  
ATOM   3405  NE  ARG A 328      12.706   8.341  24.113  1.00 75.73           N  
ANISOU 3405  NE  ARG A 328    11239   9190   8346   -950   1506    -50       N  
ATOM   3406  CZ  ARG A 328      13.804   7.654  24.399  1.00 77.98           C  
ANISOU 3406  CZ  ARG A 328    11342   9498   8787   -840   1655   -155       C  
ATOM   3407  NH1 ARG A 328      14.510   7.940  25.484  1.00 79.14           N  
ANISOU 3407  NH1 ARG A 328    11215   9658   9196   -798   1597   -144       N  
ATOM   3408  NH2 ARG A 328      14.217   6.706  23.574  1.00 79.12           N  
ANISOU 3408  NH2 ARG A 328    11581   9663   8817   -764   1864   -273       N  
ATOM   3409  N   SER A 329       9.597  12.433  23.271  1.00 75.77           N  
ANISOU 3409  N   SER A 329    11685   9093   8012  -1207   1080    592       N  
ATOM   3410  CA  SER A 329       8.799  12.147  22.083  1.00 76.03           C  
ANISOU 3410  CA  SER A 329    11930   9234   7724  -1216   1030    651       C  
ATOM   3411  C   SER A 329       8.747  13.372  21.171  1.00 76.10           C  
ANISOU 3411  C   SER A 329    12110   9231   7572  -1272   1102    883       C  
ATOM   3412  O   SER A 329       8.655  14.504  21.657  1.00 75.47           O  
ANISOU 3412  O   SER A 329    12014   9019   7641  -1264   1077   1028       O  
ATOM   3413  CB  SER A 329       7.380  11.741  22.470  1.00 75.16           C  
ANISOU 3413  CB  SER A 329    11824   9160   7572  -1147    751    653       C  
ATOM   3414  OG  SER A 329       6.566  11.559  21.324  1.00 75.75           O  
ANISOU 3414  OG  SER A 329    12080   9375   7328  -1179    656    718       O  
ATOM   3415  N   PRO A 330       8.818  13.180  19.850  1.00 77.50           N  
ANISOU 3415  N   PRO A 330    12486   9529   7433  -1329   1205    924       N  
ATOM   3416  CA  PRO A 330       8.731  14.337  18.943  1.00 77.80           C  
ANISOU 3416  CA  PRO A 330    12727   9552   7280  -1371   1273   1183       C  
ATOM   3417  C   PRO A 330       7.348  14.961  18.892  1.00 77.59           C  
ANISOU 3417  C   PRO A 330    12792   9533   7154  -1268    992   1389       C  
ATOM   3418  O   PRO A 330       7.237  16.178  18.699  1.00 77.69           O  
ANISOU 3418  O   PRO A 330    12918   9433   7166  -1244   1018   1634       O  
ATOM   3419  CB  PRO A 330       9.126  13.748  17.581  1.00 75.67           C  
ANISOU 3419  CB  PRO A 330    12658   9443   6649  -1449   1447   1139       C  
ATOM   3420  CG  PRO A 330       9.886  12.505  17.905  1.00 76.03           C  
ANISOU 3420  CG  PRO A 330    12560   9521   6808  -1454   1583    846       C  
ATOM   3421  CD  PRO A 330       9.236  11.960  19.142  1.00 75.24           C  
ANISOU 3421  CD  PRO A 330    12268   9362   6957  -1362   1332    729       C  
ATOM   3422  N   ASP A 331       6.288  14.166  19.052  1.00 80.38           N  
ANISOU 3422  N   ASP A 331    13094  10013   7435  -1203    733   1306       N  
ATOM   3423  CA  ASP A 331       4.938  14.712  18.965  1.00 80.75           C  
ANISOU 3423  CA  ASP A 331    13167  10121   7394  -1087    458   1508       C  
ATOM   3424  C   ASP A 331       4.582  15.545  20.190  1.00 80.00           C  
ANISOU 3424  C   ASP A 331    12920   9837   7638   -962    391   1591       C  
ATOM   3425  O   ASP A 331       3.851  16.535  20.070  1.00 80.58           O  
ANISOU 3425  O   ASP A 331    13057   9865   7693   -834    286   1837       O  
ATOM   3426  CB  ASP A 331       3.926  13.582  18.771  1.00 80.83           C  
ANISOU 3426  CB  ASP A 331    13128  10348   7238  -1099    210   1378       C  
ATOM   3427  CG  ASP A 331       3.980  12.981  17.376  1.00 81.83           C  
ANISOU 3427  CG  ASP A 331    13480  10673   6939  -1216    221   1338       C  
ATOM   3428  OD1 ASP A 331       4.316  13.716  16.423  1.00 82.44           O  
ANISOU 3428  OD1 ASP A 331    13768  10774   6781  -1227    327   1528       O  
ATOM   3429  OD2 ASP A 331       3.683  11.777  17.232  1.00 82.05           O  
ANISOU 3429  OD2 ASP A 331    13503  10821   6853  -1306    133   1114       O  
ATOM   3430  N   PHE A 332       5.080  15.171  21.371  1.00 78.09           N  
ANISOU 3430  N   PHE A 332    12496   9482   7693   -979    453   1395       N  
ATOM   3431  CA  PHE A 332       4.799  15.970  22.560  1.00 77.35           C  
ANISOU 3431  CA  PHE A 332    12297   9204   7889   -876    411   1445       C  
ATOM   3432  C   PHE A 332       5.564  17.288  22.542  1.00 77.21           C  
ANISOU 3432  C   PHE A 332    12401   8960   7976   -910    600   1588       C  
ATOM   3433  O   PHE A 332       5.035  18.317  22.977  1.00 77.23           O  
ANISOU 3433  O   PHE A 332    12452   8797   8097   -795    559   1738       O  
ATOM   3434  CB  PHE A 332       5.115  15.178  23.827  1.00 74.94           C  
ANISOU 3434  CB  PHE A 332    11790   8861   7822   -893    407   1201       C  
ATOM   3435  CG  PHE A 332       4.093  14.126  24.157  1.00 75.09           C  
ANISOU 3435  CG  PHE A 332    11695   9027   7808   -844    211   1102       C  
ATOM   3436  CD1 PHE A 332       2.921  14.467  24.814  1.00 75.28           C  
ANISOU 3436  CD1 PHE A 332    11625   9053   7925   -712     50   1185       C  
ATOM   3437  CD2 PHE A 332       4.300  12.801  23.814  1.00 75.37           C  
ANISOU 3437  CD2 PHE A 332    11721   9185   7730   -935    213    923       C  
ATOM   3438  CE1 PHE A 332       1.975  13.507  25.122  1.00 75.75           C  
ANISOU 3438  CE1 PHE A 332    11556   9259   7967   -703   -110   1100       C  
ATOM   3439  CE2 PHE A 332       3.357  11.836  24.118  1.00 75.69           C  
ANISOU 3439  CE2 PHE A 332    11676   9332   7749   -934     47    830       C  
ATOM   3440  CZ  PHE A 332       2.193  12.190  24.773  1.00 75.87           C  
ANISOU 3440  CZ  PHE A 332    11578   9381   7870   -834   -116    923       C  
ATOM   3441  N   ARG A 333       6.810  17.281  22.057  1.00 77.17           N  
ANISOU 3441  N   ARG A 333    12447   8932   7941  -1074    830   1539       N  
ATOM   3442  CA  ARG A 333       7.558  18.530  21.932  1.00 77.29           C  
ANISOU 3442  CA  ARG A 333    12588   8732   8045  -1164   1031   1682       C  
ATOM   3443  C   ARG A 333       6.812  19.534  21.066  1.00 78.13           C  
ANISOU 3443  C   ARG A 333    12951   8771   7965  -1064    996   1999       C  
ATOM   3444  O   ARG A 333       6.656  20.701  21.441  1.00 78.13           O  
ANISOU 3444  O   ARG A 333    13059   8517   8110  -1011   1032   2151       O  
ATOM   3445  CB  ARG A 333       8.953  18.268  21.361  1.00 75.85           C  
ANISOU 3445  CB  ARG A 333    12393   8599   7828  -1367   1300   1597       C  
ATOM   3446  CG  ARG A 333       9.923  17.677  22.355  1.00 75.50           C  
ANISOU 3446  CG  ARG A 333    12082   8561   8045  -1454   1367   1338       C  
ATOM   3447  CD  ARG A 333      11.295  17.466  21.739  1.00 76.55           C  
ANISOU 3447  CD  ARG A 333    12154   8771   8161  -1629   1652   1275       C  
ATOM   3448  NE  ARG A 333      11.316  16.352  20.798  1.00 77.30           N  
ANISOU 3448  NE  ARG A 333    12289   9081   7999  -1593   1705   1201       N  
ATOM   3449  CZ  ARG A 333      12.363  16.034  20.045  1.00 78.44           C  
ANISOU 3449  CZ  ARG A 333    12413   9328   8063  -1700   1981   1151       C  
ATOM   3450  NH1 ARG A 333      13.476  16.752  20.119  1.00 79.03           N  
ANISOU 3450  NH1 ARG A 333    12386   9332   8308  -1869   2220   1184       N  
ATOM   3451  NH2 ARG A 333      12.299  15.000  19.218  1.00 79.12           N  
ANISOU 3451  NH2 ARG A 333    12580   9586   7897  -1652   2032   1057       N  
ATOM   3452  N   ILE A 334       6.337  19.094  19.899  1.00 80.24           N  
ANISOU 3452  N   ILE A 334    13338   9253   7895  -1030    922   2104       N  
ATOM   3453  CA  ILE A 334       5.565  19.977  19.033  1.00 81.38           C  
ANISOU 3453  CA  ILE A 334    13721   9378   7821   -900    844   2436       C  
ATOM   3454  C   ILE A 334       4.268  20.395  19.713  1.00 81.65           C  
ANISOU 3454  C   ILE A 334    13676   9363   7986   -650    595   2544       C  
ATOM   3455  O   ILE A 334       3.790  21.520  19.524  1.00 82.47           O  
ANISOU 3455  O   ILE A 334    13948   9296   8091   -495    583   2824       O  
ATOM   3456  CB  ILE A 334       5.317  19.287  17.678  1.00 83.01           C  
ANISOU 3456  CB  ILE A 334    14061   9882   7597   -931    777   2492       C  
ATOM   3457  CG1 ILE A 334       6.650  19.025  16.973  1.00 82.99           C  
ANISOU 3457  CG1 ILE A 334    14165   9902   7466  -1155   1094   2406       C  
ATOM   3458  CG2 ILE A 334       4.410  20.126  16.794  1.00 84.49           C  
ANISOU 3458  CG2 ILE A 334    14477  10102   7522   -764    632   2858       C  
ATOM   3459  CD1 ILE A 334       6.532  18.158  15.742  1.00 83.90           C  
ANISOU 3459  CD1 ILE A 334    14421  10309   7147  -1209   1065   2372       C  
ATOM   3460  N   ALA A 335       3.691  19.514  20.533  1.00 81.06           N  
ANISOU 3460  N   ALA A 335    13346   9418   8034   -596    418   2334       N  
ATOM   3461  CA  ALA A 335       2.464  19.854  21.243  1.00 81.61           C  
ANISOU 3461  CA  ALA A 335    13295   9466   8245   -359    217   2419       C  
ATOM   3462  C   ALA A 335       2.729  20.793  22.413  1.00 80.74           C  
ANISOU 3462  C   ALA A 335    13190   9017   8472   -301    349   2397       C  
ATOM   3463  O   ALA A 335       1.968  21.742  22.634  1.00 81.57           O  
ANISOU 3463  O   ALA A 335    13362   8967   8663    -78    304   2594       O  
ATOM   3464  CB  ALA A 335       1.771  18.585  21.732  1.00 77.62           C  
ANISOU 3464  CB  ALA A 335    12527   9212   7754   -357     19   2204       C  
ATOM   3465  N   PHE A 336       3.796  20.542  23.177  1.00 79.89           N  
ANISOU 3465  N   PHE A 336    13014   8792   8549   -491    507   2154       N  
ATOM   3466  CA  PHE A 336       4.103  21.394  24.321  1.00 79.13           C  
ANISOU 3466  CA  PHE A 336    12937   8386   8742   -483    616   2091       C  
ATOM   3467  C   PHE A 336       4.450  22.810  23.881  1.00 79.64           C  
ANISOU 3467  C   PHE A 336    13290   8139   8830   -490    789   2320       C  
ATOM   3468  O   PHE A 336       4.060  23.785  24.535  1.00 79.77           O  
ANISOU 3468  O   PHE A 336    13412   7875   9020   -355    822   2389       O  
ATOM   3469  CB  PHE A 336       5.254  20.798  25.132  1.00 73.59           C  
ANISOU 3469  CB  PHE A 336    12088   7675   8196   -706    716   1795       C  
ATOM   3470  CG  PHE A 336       4.895  19.540  25.870  1.00 72.95           C  
ANISOU 3470  CG  PHE A 336    11764   7805   8149   -671    566   1577       C  
ATOM   3471  CD1 PHE A 336       3.572  19.172  26.046  1.00 73.52           C  
ANISOU 3471  CD1 PHE A 336    11744   8010   8179   -475    378   1624       C  
ATOM   3472  CD2 PHE A 336       5.884  18.728  26.394  1.00 72.10           C  
ANISOU 3472  CD2 PHE A 336    11509   7762   8122   -832    620   1340       C  
ATOM   3473  CE1 PHE A 336       3.245  18.015  26.729  1.00 73.03           C  
ANISOU 3473  CE1 PHE A 336    11481   8116   8151   -475    268   1436       C  
ATOM   3474  CE2 PHE A 336       5.565  17.570  27.078  1.00 71.55           C  
ANISOU 3474  CE2 PHE A 336    11258   7849   8080   -791    498   1166       C  
ATOM   3475  CZ  PHE A 336       4.243  17.214  27.246  1.00 71.88           C  
ANISOU 3475  CZ  PHE A 336    11244   7994   8074   -629    332   1213       C  
ATOM   3476  N   GLN A 337       5.187  22.944  22.775  1.00 83.21           N  
ANISOU 3476  N   GLN A 337    13897   8613   9104   -649    927   2439       N  
ATOM   3477  CA  GLN A 337       5.623  24.263  22.327  1.00 83.75           C  
ANISOU 3477  CA  GLN A 337    14267   8360   9193   -704   1130   2668       C  
ATOM   3478  C   GLN A 337       4.440  25.128  21.906  1.00 84.99           C  
ANISOU 3478  C   GLN A 337    14627   8398   9268   -387   1028   3001       C  
ATOM   3479  O   GLN A 337       4.446  26.345  22.129  1.00 85.28           O  
ANISOU 3479  O   GLN A 337    14902   8054   9446   -326   1160   3153       O  
ATOM   3480  CB  GLN A 337       6.630  24.116  21.187  1.00 87.97           C  
ANISOU 3480  CB  GLN A 337    14913   8988   9524   -945   1321   2735       C  
ATOM   3481  CG  GLN A 337       7.951  23.487  21.618  1.00 87.17           C  
ANISOU 3481  CG  GLN A 337    14604   8957   9558  -1243   1477   2437       C  
ATOM   3482  CD  GLN A 337       8.909  23.276  20.460  1.00 87.82           C  
ANISOU 3482  CD  GLN A 337    14764   9167   9435  -1455   1700   2497       C  
ATOM   3483  OE1 GLN A 337       8.587  23.573  19.310  1.00 88.72           O  
ANISOU 3483  OE1 GLN A 337    15122   9320   9267  -1397   1735   2760       O  
ATOM   3484  NE2 GLN A 337      10.090  22.742  20.758  1.00 87.60           N  
ANISOU 3484  NE2 GLN A 337    14522   9225   9535  -1688   1854   2260       N  
ATOM   3485  N   GLU A 338       3.419  24.523  21.294  1.00 86.39           N  
ANISOU 3485  N   GLU A 338    14713   8891   9220   -182    789   3119       N  
ATOM   3486  CA  GLU A 338       2.196  25.262  20.988  1.00 87.89           C  
ANISOU 3486  CA  GLU A 338    15013   9030   9353    170    644   3438       C  
ATOM   3487  C   GLU A 338       1.510  25.752  22.257  1.00 87.69           C  
ANISOU 3487  C   GLU A 338    14891   8789   9639    395    614   3367       C  
ATOM   3488  O   GLU A 338       1.125  26.923  22.355  1.00 88.35           O  
ANISOU 3488  O   GLU A 338    15192   8545   9830    614    692   3590       O  
ATOM   3489  CB  GLU A 338       1.243  24.397  20.163  1.00 95.97           C  
ANISOU 3489  CB  GLU A 338    15884  10502  10078    304    352   3534       C  
ATOM   3490  CG  GLU A 338       1.556  24.361  18.682  1.00 96.88           C  
ANISOU 3490  CG  GLU A 338    16225  10777   9808    210    364   3748       C  
ATOM   3491  CD  GLU A 338       1.222  25.682  18.009  1.00 98.24           C  
ANISOU 3491  CD  GLU A 338    16728  10712   9886    432    409   4182       C  
ATOM   3492  OE1 GLU A 338       0.272  26.353  18.469  1.00 99.06           O  
ANISOU 3492  OE1 GLU A 338    16803  10684  10150    762    300   4351       O  
ATOM   3493  OE2 GLU A 338       1.901  26.050  17.027  1.00 98.53           O  
ANISOU 3493  OE2 GLU A 338    17060  10687   9689    293    571   4365       O  
ATOM   3494  N   LEU A 339       1.339  24.864  23.239  1.00 83.39           N  
ANISOU 3494  N   LEU A 339    14046   8408   9231    355    522   3063       N  
ATOM   3495  CA  LEU A 339       0.677  25.262  24.477  1.00 83.29           C  
ANISOU 3495  CA  LEU A 339    13944   8219   9482    563    517   2976       C  
ATOM   3496  C   LEU A 339       1.480  26.326  25.212  1.00 82.36           C  
ANISOU 3496  C   LEU A 339    14075   7626   9592    457    771   2897       C  
ATOM   3497  O   LEU A 339       0.909  27.262  25.782  1.00 82.84           O  
ANISOU 3497  O   LEU A 339    14268   7389   9818    698    838   2979       O  
ATOM   3498  CB  LEU A 339       0.453  24.043  25.368  1.00 78.53           C  
ANISOU 3498  CB  LEU A 339    13003   7886   8948    495    396   2668       C  
ATOM   3499  CG  LEU A 339      -0.508  22.995  24.805  1.00 79.82           C  
ANISOU 3499  CG  LEU A 339    12909   8492   8925    586    138   2715       C  
ATOM   3500  CD1 LEU A 339      -0.569  21.785  25.720  1.00 79.06           C  
ANISOU 3500  CD1 LEU A 339    12533   8596   8910    466     69   2405       C  
ATOM   3501  CD2 LEU A 339      -1.894  23.587  24.591  1.00 81.81           C  
ANISOU 3501  CD2 LEU A 339    13104   8804   9178    966     -3   2995       C  
ATOM   3502  N   LEU A 340       2.807  26.203  25.206  1.00 82.90           N  
ANISOU 3502  N   LEU A 340    14205   7616   9676     94    922   2729       N  
ATOM   3503  CA  LEU A 340       3.657  27.205  25.833  1.00 82.36           C  
ANISOU 3503  CA  LEU A 340    14365   7117   9812    -84   1150   2639       C  
ATOM   3504  C   LEU A 340       3.854  28.437  24.961  1.00 83.29           C  
ANISOU 3504  C   LEU A 340    14866   6891   9890    -70   1326   2954       C  
ATOM   3505  O   LEU A 340       4.421  29.426  25.440  1.00 83.19           O  
ANISOU 3505  O   LEU A 340    15099   6454  10057   -208   1528   2909       O  
ATOM   3506  CB  LEU A 340       5.017  26.598  26.181  1.00 82.18           C  
ANISOU 3506  CB  LEU A 340    14204   7182   9838   -489   1231   2346       C  
ATOM   3507  CG  LEU A 340       4.999  25.490  27.234  1.00 81.19           C  
ANISOU 3507  CG  LEU A 340    13755   7310   9782   -520   1089   2028       C  
ATOM   3508  CD1 LEU A 340       6.390  24.909  27.410  1.00 80.40           C  
ANISOU 3508  CD1 LEU A 340    13510   7320   9719   -879   1160   1795       C  
ATOM   3509  CD2 LEU A 340       4.451  26.005  28.555  1.00 81.08           C  
ANISOU 3509  CD2 LEU A 340    13779   7070   9957   -373   1085   1892       C  
ATOM   3510  N   CYS A 341       3.398  28.398  23.711  1.00 86.10           N  
ANISOU 3510  N   CYS A 341    15299   7413  10001     78   1253   3269       N  
ATOM   3511  CA  CYS A 341       3.498  29.516  22.775  1.00 87.15           C  
ANISOU 3511  CA  CYS A 341    15823   7243  10047    128   1408   3629       C  
ATOM   3512  C   CYS A 341       4.943  30.007  22.672  1.00 86.64           C  
ANISOU 3512  C   CYS A 341    15942   6918  10059   -308   1692   3541       C  
ATOM   3513  O   CYS A 341       5.267  31.163  22.952  1.00 88.04           O  
ANISOU 3513  O   CYS A 341    16290   6724  10437   -373   1846   3534       O  
ATOM   3514  CB  CYS A 341       2.547  30.646  23.176  1.00 91.99           C  
ANISOU 3514  CB  CYS A 341    16619   7508  10827    505   1417   3808       C  
ATOM   3515  SG  CYS A 341       2.434  31.999  21.982  1.00 97.06           S  
ANISOU 3515  SG  CYS A 341    17532   7946  11402    630   1488   4183       S  
ATOM   3516  N   LEU A 342       5.816  29.092  22.266  1.00 89.47           N  
ANISOU 3516  N   LEU A 342    16118   7586  10290   -611   1716   3394       N  
ATOM   3517  CA  LEU A 342       7.243  29.376  22.196  1.00 89.19           C  
ANISOU 3517  CA  LEU A 342    16154   7394  10338  -1049   1984   3284       C  
ATOM   3518  C   LEU A 342       7.659  29.755  20.777  1.00 91.05           C  
ANISOU 3518  C   LEU A 342    16531   7702  10361  -1136   2109   3543       C  
ATOM   3519  O   LEU A 342       7.588  28.937  19.859  1.00 90.88           O  
ANISOU 3519  O   LEU A 342    16461   8026  10043  -1116   2051   3639       O  
ATOM   3520  CB  LEU A 342       8.049  28.168  22.683  1.00 85.48           C  
ANISOU 3520  CB  LEU A 342    15286   7276   9915  -1299   1935   2914       C  
ATOM   3521  CG  LEU A 342       7.849  27.780  24.152  1.00 84.49           C  
ANISOU 3521  CG  LEU A 342    14915   7165  10021  -1255   1786   2583       C  
ATOM   3522  CD1 LEU A 342       8.590  26.491  24.491  1.00 83.69           C  
ANISOU 3522  CD1 LEU A 342    14434   7439   9926  -1444   1718   2279       C  
ATOM   3523  CD2 LEU A 342       8.278  28.909  25.078  1.00 84.50           C  
ANISOU 3523  CD2 LEU A 342    15105   6709  10291  -1415   1936   2479       C  
TER    3524      LEU A 342                                                       
HETATM 3581  C1  JTZ A1203       0.374   8.005  53.099  1.00 76.39           C  
ANISOU 3581  C1  JTZ A1203    12862   8978   7184     48    575    163       C  
HETATM 3582  N1  JTZ A1203       2.550   6.923  52.508  1.00 75.90           N  
ANISOU 3582  N1  JTZ A1203    12719   8940   7181     54     99    245       N  
HETATM 3583  O1  JTZ A1203       2.874   7.493  49.346  1.00 74.46           O  
ANISOU 3583  O1  JTZ A1203    12001   8638   7653    -46     26    164       O  
HETATM 3584  C2  JTZ A1203       1.832   7.736  53.483  1.00 76.35           C  
ANISOU 3584  C2  JTZ A1203    12954   9024   7032     57    266    148       C  
HETATM 3585  O2  JTZ A1203       2.113   4.019  50.050  1.00 72.58           O  
ANISOU 3585  O2  JTZ A1203    12008   8292   7278     -2    191    582       O  
HETATM 3586  C3  JTZ A1203       2.608   9.029  53.711  1.00 76.71           C  
ANISOU 3586  C3  JTZ A1203    13044   9091   7010     26    111    -75       C  
HETATM 3587  C4  JTZ A1203       1.761   6.618  51.325  1.00 74.70           C  
ANISOU 3587  C4  JTZ A1203    12367   8708   7308      9    243    303       C  
HETATM 3588  C5  JTZ A1203       2.681   6.315  50.142  1.00 74.16           C  
ANISOU 3588  C5  JTZ A1203    12112   8609   7458     -3     64    305       C  
HETATM 3589  C6  JTZ A1203       2.087   5.194  49.293  1.00 72.75           C  
ANISOU 3589  C6  JTZ A1203    11850   8349   7442    -42    168    434       C  
HETATM 3590  C7  JTZ A1203       1.458   2.939  49.447  1.00 71.54           C  
ANISOU 3590  C7  JTZ A1203    11860   8052   7271    -74    319    691       C  
HETATM 3591  C8  JTZ A1203       0.694   3.123  48.303  1.00 70.78           C  
ANISOU 3591  C8  JTZ A1203    11568   7940   7384   -188    408    642       C  
HETATM 3592  C9  JTZ A1203       0.051   2.041  47.719  1.00 70.07           C  
ANISOU 3592  C9  JTZ A1203    11472   7751   7401   -304    515    724       C  
HETATM 3593  C10 JTZ A1203       0.164   0.775  48.274  1.00 70.08           C  
ANISOU 3593  C10 JTZ A1203    11686   7623   7319   -300    566    863       C  
HETATM 3594  C11 JTZ A1203       0.924   0.598  49.417  1.00 70.77           C  
ANISOU 3594  C11 JTZ A1203    11978   7712   7200   -149    489    943       C  
HETATM 3595  C12 JTZ A1203       1.569   1.677  50.003  1.00 71.52           C  
ANISOU 3595  C12 JTZ A1203    12054   7952   7169    -39    351    853       C  
HETATM 3596  C13 JTZ A1203       2.405   1.465  51.264  1.00 72.59           C  
ANISOU 3596  C13 JTZ A1203    12408   8132   7041    111    223    939       C  
HETATM 3597  C14 JTZ A1203       1.635   0.709  52.344  1.00 72.77           C  
ANISOU 3597  C14 JTZ A1203    12693   8101   6854     90    410   1112       C  
HETATM 3598  C15 JTZ A1203       2.532  -0.240  53.135  1.00 73.60           C  
ANISOU 3598  C15 JTZ A1203    13042   8153   6770    257    277   1295       C  
HETATM 3599  C10 M3J A1204      -2.465  -7.805  33.650  0.79 70.43           C  
ANISOU 3599  C10 M3J A1204    12323   6380   8058  -2673    657   -558       C  
HETATM 3600  N12 M3J A1204      -3.870  -7.049  37.562  0.79 70.38           N  
ANISOU 3600  N12 M3J A1204    11936   6557   8249  -2531    816     41       N  
HETATM 3601  C13 M3J A1204      -3.808  -7.632  38.789  0.79 70.30           C  
ANISOU 3601  C13 M3J A1204    12113   6335   8262  -2463    971    200       C  
HETATM 3602  C15 M3J A1204      -4.097  -9.582  40.217  0.79 70.89           C  
ANISOU 3602  C15 M3J A1204    12724   5835   8375  -2637   1304    394       C  
HETATM 3603  C02 M3J A1204      -3.057  -5.524  39.638  0.79 69.38           C  
ANISOU 3603  C02 M3J A1204    11627   6643   8094  -1947    816    342       C  
HETATM 3604  C04 M3J A1204      -3.541  -5.778  37.390  0.79 70.01           C  
ANISOU 3604  C04 M3J A1204    11629   6797   8174  -2305    682     58       C  
HETATM 3605  C06 M3J A1204      -3.503  -6.018  34.873  0.79 70.57           C  
ANISOU 3605  C06 M3J A1204    11743   6929   8142  -2580    514   -274       C  
HETATM 3606  C07 M3J A1204      -4.349  -5.779  33.804  0.79 71.68           C  
ANISOU 3606  C07 M3J A1204    11713   7307   8216  -2858    371   -387       C  
HETATM 3607  C08 M3J A1204      -4.254  -6.550  32.658  0.79 71.98           C  
ANISOU 3607  C08 M3J A1204    11975   7215   8159  -3074    353   -596       C  
HETATM 3608  C09 M3J A1204      -3.313  -7.563  32.582  0.79 71.31           C  
ANISOU 3608  C09 M3J A1204    12290   6732   8074  -2987    511   -695       C  
HETATM 3609  C11 M3J A1204      -2.561  -7.032  34.795  0.79 70.01           C  
ANISOU 3609  C11 M3J A1204    12041   6488   8073  -2482    642   -347       C  
HETATM 3610  C14 M3J A1204      -4.164  -9.003  38.958  0.79 70.82           C  
ANISOU 3610  C14 M3J A1204    12495   6048   8363  -2718   1138    198       C  
HETATM 3611  C16 M3J A1204      -3.682  -8.819  41.311  0.79 70.47           C  
ANISOU 3611  C16 M3J A1204    12574   5935   8266  -2311   1288    572       C  
HETATM 3612  C18 M3J A1204      -3.335  -7.483  41.149  0.79 69.93           C  
ANISOU 3612  C18 M3J A1204    12196   6208   8166  -2084   1119    541       C  
HETATM 3613  C19 M3J A1204      -3.402  -6.889  39.858  0.79 69.83           C  
ANISOU 3613  C19 M3J A1204    11965   6392   8176  -2162    969    361       C  
HETATM 3614  N01 M3J A1204      -2.619  -4.689  40.742  0.79 68.96           N  
ANISOU 3614  N01 M3J A1204    11499   6707   7996  -1662    803    474       N  
HETATM 3615  N03 M3J A1204      -3.139  -5.024  38.412  0.79 69.47           N  
ANISOU 3615  N03 M3J A1204    11473   6819   8104  -2024    688    201       N  
HETATM 3616  N05 M3J A1204      -3.618  -5.195  36.065  0.79 70.32           N  
ANISOU 3616  N05 M3J A1204    11509   7045   8165  -2378    527    -81       N  
HETATM 3617 BR1  M3J A1204      -3.587  -9.629  43.068  0.79 70.81          BR  
ANISOU 3617 BR1  M3J A1204    12966   5697   8243  -2191   1505    867      BR      
END                                                                             



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