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***  npa3_DAO_2  ***

elNémo ID: 210603093732118321

Job options:

ID        	=	 210603093732118321
JOBID     	=	 npa3_DAO_2
USERID    	=	 juliomluna2
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER npa3_DAO_2

ATOM      1  N   SER A   2      30.117  12.846  29.235  1.00141.91           N  
ANISOU    1  N   SER A   2    18616  17883  17420   2257   1877   1491       N  
ATOM      2  CA  SER A   2      31.351  13.616  29.141  1.00146.73           C  
ANISOU    2  CA  SER A   2    19425  18487  17838   2165   1693   1271       C  
ATOM      3  C   SER A   2      32.168  13.239  27.900  1.00137.42           C  
ANISOU    3  C   SER A   2    18095  17308  16812   1900   1520   1119       C  
ATOM      4  O   SER A   2      33.380  13.431  27.863  1.00140.74           O  
ANISOU    4  O   SER A   2    18612  17727  17138   1805   1368    969       O  
ATOM      5  CB  SER A   2      32.191  13.422  30.403  1.00154.89           C  
ANISOU    5  CB  SER A   2    20649  19530  18673   2280   1673   1260       C  
ATOM      6  OG  SER A   2      33.301  14.301  30.410  1.00159.89           O  
ANISOU    6  OG  SER A   2    21491  20144  19116   2208   1488   1069       O  
ATOM      7  N   LEU A   3      31.486  12.701  26.892  1.00131.35           N  
ANISOU    7  N   LEU A   3    17093  16534  16283   1788   1543   1169       N  
ATOM      8  CA  LEU A   3      32.077  12.366  25.590  1.00120.90           C  
ANISOU    8  CA  LEU A   3    15634  15200  15103   1552   1400   1034       C  
ATOM      9  C   LEU A   3      31.949  13.525  24.603  1.00126.49           C  
ANISOU    9  C   LEU A   3    16394  15896  15770   1460   1320    921       C  
ATOM     10  O   LEU A   3      30.984  14.292  24.673  1.00126.67           O  
ANISOU   10  O   LEU A   3    16459  15912  15756   1558   1403    996       O  
ATOM     11  CB  LEU A   3      31.390  11.119  25.020  1.00118.16           C  
ANISOU   11  CB  LEU A   3    15027  14839  15029   1479   1451   1146       C  
ATOM     12  CG  LEU A   3      31.369  10.755  23.526  1.00117.46           C  
ANISOU   12  CG  LEU A   3    14779  14723  15127   1266   1348   1063       C  
ATOM     13  CD1 LEU A   3      31.096   9.270  23.395  1.00110.81           C  
ANISOU   13  CD1 LEU A   3    13732  13855  14517   1217   1379   1162       C  
ATOM     14  CD2 LEU A   3      30.329  11.515  22.714  1.00106.87           C  
ANISOU   14  CD2 LEU A   3    13397  13368  13842   1238   1354   1092       C  
ATOM     15  N   SER A   4      32.888  13.635  23.662  1.00110.98           N  
ANISOU   15  N   SER A   4    14417  13927  13823   1279   1171    756       N  
ATOM     16  CA  SER A   4      32.816  14.684  22.628  1.00115.58           C  
ANISOU   16  CA  SER A   4    15035  14501  14381   1180   1091    651       C  
ATOM     17  C   SER A   4      32.839  14.085  21.215  1.00116.80           C  
ANISOU   17  C   SER A   4    15012  14644  14723    989   1020    594       C  
ATOM     18  O   SER A   4      33.392  13.008  21.015  1.00116.94           O  
ANISOU   18  O   SER A   4    14929  14656  14846    909    992    575       O  
ATOM     19  CB  SER A   4      33.960  15.692  22.798  1.00 99.83           C  
ANISOU   19  CB  SER A   4    13235  12503  12193   1155    969    501       C  
ATOM     20  OG  SER A   4      35.223  15.072  22.639  1.00101.79           O  
ANISOU   20  OG  SER A   4    13452  12755  12470   1043    868    412       O  
ATOM     21  N   THR A   5      32.250  14.780  20.237  1.00108.00           N  
ANISOU   21  N   THR A   5    13872  13521  13642    920    990    566       N  
ATOM     22  CA  THR A   5      32.096  14.199  18.896  1.00 94.34           C  
ANISOU   22  CA  THR A   5    11992  11773  12081    754    926    525       C  
ATOM     23  C   THR A   5      32.855  14.932  17.798  1.00110.25           C  
ANISOU   23  C   THR A   5    14063  13789  14037    617    805    361       C  
ATOM     24  O   THR A   5      32.802  16.161  17.698  1.00100.55           O  
ANISOU   24  O   THR A   5    12942  12570  12693    638    782    319       O  
ATOM     25  CB  THR A   5      30.616  14.139  18.480  1.00 99.25           C  
ANISOU   25  CB  THR A   5    12490  12377  12844    768    983    661       C  
ATOM     26  CG2 THR A   5      30.478  13.592  17.062  1.00 96.37           C  
ANISOU   26  CG2 THR A   5    12003  11982  12631    589    886    605       C  
ATOM     27  OG1 THR A   5      29.897  13.287  19.381  1.00105.53           O  
ANISOU   27  OG1 THR A   5    13193  13165  13738    883   1099    836       O  
ATOM     28  N   ILE A   6      33.559  14.164  16.970  1.00102.89           N  
ANISOU   28  N   ILE A   6    13062  12843  13188    484    736    276       N  
ATOM     29  CA  ILE A   6      34.299  14.719  15.842  1.00 96.50           C  
ANISOU   29  CA  ILE A   6    12291  12034  12339    358    638    136       C  
ATOM     30  C   ILE A   6      33.752  14.181  14.526  1.00100.76           C  
ANISOU   30  C   ILE A   6    12728  12546  13012    239    599    120       C  
ATOM     31  O   ILE A   6      33.670  12.970  14.331  1.00 94.93           O  
ANISOU   31  O   ILE A   6    11894  11775  12399    198    606    144       O  
ATOM     32  CB  ILE A   6      35.785  14.389  15.943  1.00 96.66           C  
ANISOU   32  CB  ILE A   6    12349  12058  12319    313    590     44       C  
ATOM     33  CG1 ILE A   6      36.336  14.867  17.285  1.00 91.38           C  
ANISOU   33  CG1 ILE A   6    11794  11408  11520    424    600     64       C  
ATOM     34  CG2 ILE A   6      36.544  15.004  14.780  1.00 93.69           C  
ANISOU   34  CG2 ILE A   6    12008  11682  11909    198    506    -78       C  
ATOM     35  CD1 ILE A   6      37.671  14.170  17.646  1.00101.16           C  
ANISOU   35  CD1 ILE A   6    13028  12645  12765    395    565     27       C  
ATOM     36  N   ILE A   7      33.398  15.085  13.622  1.00 93.74           N  
ANISOU   36  N   ILE A   7    11866  11661  12090    183    550     77       N  
ATOM     37  CA  ILE A   7      32.714  14.716  12.385  1.00 92.98           C  
ANISOU   37  CA  ILE A   7    11693  11534  12103     76    499     71       C  
ATOM     38  C   ILE A   7      33.615  15.052  11.229  1.00106.09           C  
ANISOU   38  C   ILE A   7    13412  13196  13703    -32    421    -71       C  
ATOM     39  O   ILE A   7      33.925  16.229  10.990  1.00101.91           O  
ANISOU   39  O   ILE A   7    12961  12696  13065    -35    395   -124       O  
ATOM     40  CB  ILE A   7      31.356  15.465  12.216  1.00 97.46           C  
ANISOU   40  CB  ILE A   7    12228  12104  12699    104    509    169       C  
ATOM     41  CG1 ILE A   7      30.579  15.429  13.527  1.00 95.36           C  
ANISOU   41  CG1 ILE A   7    11930  11845  12456    252    617    324       C  
ATOM     42  CG2 ILE A   7      30.543  14.879  11.066  1.00 95.08           C  
ANISOU   42  CG2 ILE A   7    11832  11758  12535     -7    437    191       C  
ATOM     43  CD1 ILE A   7      29.123  15.927  13.430  1.00 98.91           C  
ANISOU   43  CD1 ILE A   7    12312  12288  12983    293    651    466       C  
ATOM     44  N   CYS A   8      34.039  14.027  10.505  1.00 88.76           N  
ANISOU   44  N   CYS A   8    11184  10964  11577   -114    390   -129       N  
ATOM     45  CA  CYS A   8      35.005  14.223   9.437  1.00 92.59           C  
ANISOU   45  CA  CYS A   8    11730  11447  12002   -198    341   -254       C  
ATOM     46  C   CYS A   8      34.298  14.475   8.120  1.00 99.18           C  
ANISOU   46  C   CYS A   8    12572  12262  12851   -284    272   -285       C  
ATOM     47  O   CYS A   8      33.444  13.691   7.690  1.00 96.76           O  
ANISOU   47  O   CYS A   8    12210  11906  12649   -328    236   -247       O  
ATOM     48  CB  CYS A   8      35.953  13.024   9.330  1.00 95.48           C  
ANISOU   48  CB  CYS A   8    12083  11779  12416   -224    359   -304       C  
ATOM     49  SG  CYS A   8      36.812  12.740  10.876  1.00 95.07           S  
ANISOU   49  SG  CYS A   8    12020  11753  12349   -129    426   -258       S  
ATOM     50  N   ILE A   9      34.648  15.609   7.514  1.00 91.75           N  
ANISOU   50  N   ILE A   9    11700  11355  11807   -308    243   -344       N  
ATOM     51  CA  ILE A   9      34.068  16.049   6.258  1.00 93.84           C  
ANISOU   51  CA  ILE A   9    11987  11611  12057   -384    174   -374       C  
ATOM     52  C   ILE A   9      35.184  16.502   5.332  1.00 99.41           C  
ANISOU   52  C   ILE A   9    12775  12332  12666   -429    159   -482       C  
ATOM     53  O   ILE A   9      36.165  17.085   5.797  1.00 94.87           O  
ANISOU   53  O   ILE A   9    12231  11790  12027   -392    193   -505       O  
ATOM     54  CB  ILE A   9      33.060  17.198   6.491  1.00 98.04           C  
ANISOU   54  CB  ILE A   9    12506  12175  12571   -351    166   -296       C  
ATOM     55  CG1 ILE A   9      31.887  16.726   7.355  1.00 88.66           C  
ANISOU   55  CG1 ILE A   9    11224  10968  11494   -294    199   -161       C  
ATOM     56  CG2 ILE A   9      32.548  17.769   5.175  1.00 96.09           C  
ANISOU   56  CG2 ILE A   9    12283  11925  12300   -431     88   -324       C  
ATOM     57  CD1 ILE A   9      30.906  17.862   7.699  1.00 93.27           C  
ANISOU   57  CD1 ILE A   9    11795  11580  12064   -236    219    -65       C  
ATOM     58  N   GLY A  10      35.063  16.211   4.038  1.00 93.20           N  
ANISOU   58  N   GLY A  10    12028  11515  11871   -504    106   -540       N  
ATOM     59  CA  GLY A  10      36.037  16.691   3.068  1.00108.78           C  
ANISOU   59  CA  GLY A  10    14082  13503  13748   -534    107   -626       C  
ATOM     60  C   GLY A  10      35.751  16.165   1.676  1.00108.24           C  
ANISOU   60  C   GLY A  10    14077  13387  13662   -604     49   -686       C  
ATOM     61  O   GLY A  10      35.071  15.160   1.541  1.00 98.73           O  
ANISOU   61  O   GLY A  10    12857  12122  12532   -635      5   -678       O  
ATOM     62  N   MET A  11      36.251  16.832   0.637  1.00104.88           N  
ANISOU   62  N   MET A  11    13730  12982  13137   -628     41   -743       N  
ATOM     63  CA  MET A  11      35.964  16.381  -0.723  1.00 98.65           C  
ANISOU   63  CA  MET A  11    13034  12145  12304   -685    -20   -804       C  
ATOM     64  C   MET A  11      36.568  15.015  -0.963  1.00104.06           C  
ANISOU   64  C   MET A  11    13771  12759  13009   -681     14   -864       C  
ATOM     65  O   MET A  11      37.463  14.588  -0.225  1.00106.77           O  
ANISOU   65  O   MET A  11    14076  13105  13385   -631    102   -861       O  
ATOM     66  CB  MET A  11      36.487  17.373  -1.770  1.00 96.18           C  
ANISOU   66  CB  MET A  11    12804  11873  11869   -694    -14   -845       C  
ATOM     67  CG  MET A  11      35.707  18.711  -1.898  1.00 87.98           C  
ANISOU   67  CG  MET A  11    11737  10889  10803   -714    -70   -794       C  
ATOM     68  SD  MET A  11      36.832  19.990  -2.537  1.00115.44           S  
ANISOU   68  SD  MET A  11    15266  14429  14168   -691    -11   -817       S  
ATOM     69  CE  MET A  11      36.985  19.543  -4.266  1.00117.87           C  
ANISOU   69  CE  MET A  11    15721  14701  14365   -723    -35   -894       C  
ATOM     70  N   ALA A  12      36.070  14.335  -1.993  1.00 99.39           N  
ANISOU   70  N   ALA A  12    13273  12096  12395   -732    -63   -918       N  
ATOM     71  CA  ALA A  12      36.632  13.056  -2.419  1.00108.26           C  
ANISOU   71  CA  ALA A  12    14484  13134  13516   -725    -34   -990       C  
ATOM     72  C   ALA A  12      38.140  13.155  -2.555  1.00116.86           C  
ANISOU   72  C   ALA A  12    15616  14249  14534   -657    104  -1027       C  
ATOM     73  O   ALA A  12      38.649  14.091  -3.171  1.00106.76           O  
ANISOU   73  O   ALA A  12    14384  13024  13157   -641    138  -1037       O  
ATOM     74  CB  ALA A  12      36.021  12.620  -3.731  1.00116.39           C  
ANISOU   74  CB  ALA A  12    15659  14084  14480   -784   -147  -1059       C  
ATOM     75  N   GLY A  13      38.851  12.212  -1.946  1.00121.33           N  
ANISOU   75  N   GLY A  13    16153  14781  15167   -614    187  -1028       N  
ATOM     76  CA  GLY A  13      40.297  12.155  -2.067  1.00130.20           C  
ANISOU   76  CA  GLY A  13    17302  15916  16250   -548    322  -1043       C  
ATOM     77  C   GLY A  13      41.097  12.994  -1.083  1.00118.84           C  
ANISOU   77  C   GLY A  13    15741  14564  14847   -509    391   -969       C  
ATOM     78  O   GLY A  13      42.323  12.983  -1.113  1.00139.56           O  
ANISOU   78  O   GLY A  13    18362  17199  17466   -459    495   -956       O  
ATOM     79  N   SER A  14      40.414  13.716  -0.204  1.00110.66           N  
ANISOU   79  N   SER A  14    14611  13583  13852   -529    329   -913       N  
ATOM     80  CA  SER A  14      41.100  14.523   0.799  1.00113.71           C  
ANISOU   80  CA  SER A  14    14906  14037  14263   -495    367   -849       C  
ATOM     81  C   SER A  14      41.781  13.648   1.842  1.00107.74           C  
ANISOU   81  C   SER A  14    14078  13263  13598   -454    429   -815       C  
ATOM     82  O   SER A  14      42.637  14.115   2.591  1.00 98.88           O  
ANISOU   82  O   SER A  14    12895  12180  12496   -424    462   -766       O  
ATOM     83  CB  SER A  14      40.124  15.474   1.482  1.00115.81           C  
ANISOU   83  CB  SER A  14    15117  14352  14534   -511    291   -803       C  
ATOM     84  OG  SER A  14      39.039  14.748   2.031  1.00101.40           O  
ANISOU   84  OG  SER A  14    13252  12495  12782   -523    247   -780       O  
ATOM     85  N   GLY A  15      41.389  12.376   1.885  1.00111.27           N  
ANISOU   85  N   GLY A  15    14532  13643  14103   -457    432   -836       N  
ATOM     86  CA  GLY A  15      41.979  11.410   2.797  1.00 95.31           C  
ANISOU   86  CA  GLY A  15    12444  11596  12173   -419    493   -802       C  
ATOM     87  C   GLY A  15      41.293  11.320   4.153  1.00103.80           C  
ANISOU   87  C   GLY A  15    13422  12694  13321   -408    457   -735       C  
ATOM     88  O   GLY A  15      41.948  11.091   5.174  1.00103.39           O  
ANISOU   88  O   GLY A  15    13304  12661  13320   -367    500   -683       O  
ATOM     89  N   LYS A  16      39.974  11.477   4.177  1.00 94.20           N  
ANISOU   89  N   LYS A  16    12200  11475  12116   -438    382   -723       N  
ATOM     90  CA  LYS A  16      39.279  11.538   5.452  1.00102.34           C  
ANISOU   90  CA  LYS A  16    13145  12534  13207   -409    366   -641       C  
ATOM     91  C   LYS A  16      39.192  10.157   6.120  1.00 99.61           C  
ANISOU   91  C   LYS A  16    12739  12135  12974   -388    399   -607       C  
ATOM     92  O   LYS A  16      39.291  10.049   7.348  1.00106.08           O  
ANISOU   92  O   LYS A  16    13490  12983  13834   -335    431   -536       O  
ATOM     93  CB  LYS A  16      37.889  12.166   5.276  1.00 95.85           C  
ANISOU   93  CB  LYS A  16    12317  11724  12378   -438    291   -613       C  
ATOM     94  CG  LYS A  16      36.804  11.238   4.813  1.00114.22           C  
ANISOU   94  CG  LYS A  16    14632  13978  14789   -485    233   -606       C  
ATOM     95  CD  LYS A  16      35.482  11.979   4.746  1.00125.02           C  
ANISOU   95  CD  LYS A  16    15970  15365  16167   -508    162   -547       C  
ATOM     96  CE  LYS A  16      35.493  12.961   3.602  1.00121.92           C  
ANISOU   96  CE  LYS A  16    15661  14996  15666   -554    112   -609       C  
ATOM     97  NZ  LYS A  16      35.566  12.265   2.276  1.00109.16           N1+
ANISOU   97  NZ  LYS A  16    14138  13308  14028   -619     59   -697       N1+
ATOM     98  N   THR A  17      39.043   9.097   5.332  1.00 95.68           N  
ANISOU   98  N   THR A  17    12278  11554  12522   -424    390   -656       N  
ATOM     99  CA  THR A  17      39.000   7.762   5.939  1.00 99.02           C  
ANISOU   99  CA  THR A  17    12643  11917  13065   -405    421   -621       C  
ATOM    100  C   THR A  17      40.382   7.374   6.513  1.00105.89           C  
ANISOU  100  C   THR A  17    13487  12801  13945   -351    519   -612       C  
ATOM    101  O   THR A  17      40.463   6.815   7.613  1.00100.52           O  
ANISOU  101  O   THR A  17    12724  12127  13344   -309    554   -541       O  
ATOM    102  CB  THR A  17      38.490   6.697   4.943  1.00100.93           C  
ANISOU  102  CB  THR A  17    12946  12046  13357   -461    371   -680       C  
ATOM    103  CG2 THR A  17      38.520   5.290   5.583  1.00 94.07           C  
ANISOU  103  CG2 THR A  17    12013  11105  12625   -441    407   -642       C  
ATOM    104  OG1 THR A  17      37.128   7.009   4.571  1.00107.44           O  
ANISOU  104  OG1 THR A  17    13767  12854  14202   -518    261   -659       O  
ATOM    105  N   THR A  18      41.459   7.707   5.802  1.00 91.12           N  
ANISOU  105  N   THR A  18    11681  10939  12002   -347    563   -667       N  
ATOM    106  CA  THR A  18      42.817   7.463   6.313  1.00 96.57           C  
ANISOU  106  CA  THR A  18    12332  11645  12715   -299    650   -636       C  
ATOM    107  C   THR A  18      43.081   8.311   7.561  1.00103.03           C  
ANISOU  107  C   THR A  18    13078  12549  13521   -266    635   -558       C  
ATOM    108  O   THR A  18      43.697   7.847   8.523  1.00 92.20           O  
ANISOU  108  O   THR A  18    11639  11185  12207   -226    673   -498       O  
ATOM    109  CB  THR A  18      43.878   7.770   5.254  1.00106.31           C  
ANISOU  109  CB  THR A  18    13639  12872  13883   -295    707   -686       C  
ATOM    110  CG2 THR A  18      45.270   7.326   5.721  1.00 95.03           C  
ANISOU  110  CG2 THR A  18    12152  11443  12513   -245    803   -633       C  
ATOM    111  OG1 THR A  18      43.540   7.091   4.039  1.00111.43           O  
ANISOU  111  OG1 THR A  18    14394  13436  14508   -317    711   -770       O  
ATOM    112  N   PHE A  19      42.592   9.551   7.532  1.00 97.48           N  
ANISOU  112  N   PHE A  19    12399  11901  12736   -282    574   -561       N  
ATOM    113  CA  PHE A  19      42.654  10.469   8.670  1.00 87.03           C  
ANISOU  113  CA  PHE A  19    11044  10644  11378   -249    542   -501       C  
ATOM    114  C   PHE A  19      41.954   9.905   9.910  1.00 92.28           C  
ANISOU  114  C   PHE A  19    11652  11312  12100   -203    544   -430       C  
ATOM    115  O   PHE A  19      42.435  10.043  11.036  1.00 96.03           O  
ANISOU  115  O   PHE A  19    12098  11818  12569   -156    548   -372       O  
ATOM    116  CB  PHE A  19      42.017  11.817   8.299  1.00 93.98           C  
ANISOU  116  CB  PHE A  19    11976  11567  12167   -272    479   -523       C  
ATOM    117  CG  PHE A  19      41.859  12.756   9.469  1.00 97.70           C  
ANISOU  117  CG  PHE A  19    12443  12088  12590   -229    441   -469       C  
ATOM    118  CD1 PHE A  19      42.895  13.598   9.833  1.00 90.49           C  
ANISOU  118  CD1 PHE A  19    11547  11204  11631   -221    415   -459       C  
ATOM    119  CD2 PHE A  19      40.678  12.795  10.207  1.00 94.71           C  
ANISOU  119  CD2 PHE A  19    12052  11719  12214   -191    430   -421       C  
ATOM    120  CE1 PHE A  19      42.762  14.469  10.911  1.00 96.15           C  
ANISOU  120  CE1 PHE A  19    12293  11952  12288   -179    366   -420       C  
ATOM    121  CE2 PHE A  19      40.537  13.663  11.282  1.00 99.69           C  
ANISOU  121  CE2 PHE A  19    12711  12388  12780   -133    407   -375       C  
ATOM    122  CZ  PHE A  19      41.578  14.500  11.635  1.00101.31           C  
ANISOU  122  CZ  PHE A  19    12957  12615  12922   -128    368   -385       C  
ATOM    123  N   MET A  20      40.782   9.317   9.705  1.00 90.02           N  
ANISOU  123  N   MET A  20    11348  10988  11865   -217    535   -424       N  
ATOM    124  CA  MET A  20      40.032   8.742  10.811  1.00101.60           C  
ANISOU  124  CA  MET A  20    12749  12454  13402   -168    550   -337       C  
ATOM    125  C   MET A  20      40.684   7.473  11.372  1.00 88.17           C  
ANISOU  125  C   MET A  20    10987  10717  11794   -139    609   -302       C  
ATOM    126  O   MET A  20      40.750   7.280  12.588  1.00103.21           O  
ANISOU  126  O   MET A  20    12847  12650  13718    -76    635   -222       O  
ATOM    127  CB  MET A  20      38.619   8.440  10.366  1.00112.09           C  
ANISOU  127  CB  MET A  20    14056  13743  14791   -198    517   -319       C  
ATOM    128  CG  MET A  20      37.894   7.484  11.286  1.00151.25           C  
ANISOU  128  CG  MET A  20    18924  18676  19867   -155    548   -218       C  
ATOM    129  SD  MET A  20      36.159   7.657  10.955  1.00182.45           S  
ANISOU  129  SD  MET A  20    22836  22602  23884   -182    493   -155       S  
ATOM    130  CE  MET A  20      36.218   9.384  10.512  1.00 89.31           C  
ANISOU  130  CE  MET A  20    11130  10878  11926   -190    455   -210       C  
ATOM    131  N   GLN A  21      41.141   6.600  10.490  1.00 86.36           N  
ANISOU  131  N   GLN A  21    10769  10424  11620   -179    633   -359       N  
ATOM    132  CA  GLN A  21      42.016   5.500  10.918  1.00 91.19           C  
ANISOU  132  CA  GLN A  21    11332  11002  12315   -151    699   -332       C  
ATOM    133  C   GLN A  21      43.177   5.967  11.807  1.00101.99           C  
ANISOU  133  C   GLN A  21    12677  12431  13643   -106    720   -285       C  
ATOM    134  O   GLN A  21      43.416   5.417  12.881  1.00100.88           O  
ANISOU  134  O   GLN A  21    12475  12301  13554    -57    748   -209       O  
ATOM    135  CB  GLN A  21      42.609   4.790   9.720  1.00 85.64           C  
ANISOU  135  CB  GLN A  21    10678  10223  11639   -187    735   -413       C  
ATOM    136  CG  GLN A  21      43.552   3.659  10.149  1.00102.80           C  
ANISOU  136  CG  GLN A  21    12797  12356  13905   -150    816   -376       C  
ATOM    137  CD  GLN A  21      43.919   2.749   9.015  1.00116.49           C  
ANISOU  137  CD  GLN A  21    14593  13992  15676   -169    864   -451       C  
ATOM    138  NE2 GLN A  21      44.880   1.860   9.253  1.00143.68           N  
ANISOU  138  NE2 GLN A  21    17998  17397  19195   -131    951   -421       N  
ATOM    139  OE1 GLN A  21      43.345   2.834   7.933  1.00113.82           O  
ANISOU  139  OE1 GLN A  21    14346  13606  15294   -214    824   -534       O  
ATOM    140  N   ARG A  22      43.893   6.989  11.346  1.00102.77           N  
ANISOU  140  N   ARG A  22    12826  12566  13657   -126    697   -324       N  
ATOM    141  CA  ARG A  22      45.036   7.509  12.091  1.00 87.06           C  
ANISOU  141  CA  ARG A  22    10816  10621  11641   -100    687   -275       C  
ATOM    142  C   ARG A  22      44.589   8.187  13.392  1.00 96.62           C  
ANISOU  142  C   ARG A  22    12033  11888  12791    -54    632   -216       C  
ATOM    143  O   ARG A  22      45.270   8.114  14.401  1.00 99.09           O  
ANISOU  143  O   ARG A  22    12320  12221  13109    -17    620   -152       O  
ATOM    144  CB  ARG A  22      45.835   8.471  11.224  1.00100.06           C  
ANISOU  144  CB  ARG A  22    12506  12283  13228   -137    669   -318       C  
ATOM    145  CG  ARG A  22      47.014   9.111  11.941  1.00115.68           C  
ANISOU  145  CG  ARG A  22    14458  14298  15198   -126    631   -256       C  
ATOM    146  CD  ARG A  22      47.822   8.119  12.751  1.00 98.63           C  
ANISOU  146  CD  ARG A  22    12220  12123  13133    -92    671   -178       C  
ATOM    147  NE  ARG A  22      48.708   7.354  11.905  1.00 98.51           N  
ANISOU  147  NE  ARG A  22    12166  12061  13203    -99    762   -178       N  
ATOM    148  CZ  ARG A  22      49.636   6.538  12.373  1.00111.35           C  
ANISOU  148  CZ  ARG A  22    13714  13667  14928    -74    812   -102       C  
ATOM    149  NH1 ARG A  22      49.782   6.386  13.686  1.00109.51           N1+
ANISOU  149  NH1 ARG A  22    13435  13460  14714    -46    765    -25       N1+
ATOM    150  NH2 ARG A  22      50.412   5.884  11.528  1.00118.13           N  
ANISOU  150  NH2 ARG A  22    14548  14477  15861    -68    913    -99       N  
ATOM    151  N   LEU A  23      43.421   8.813  13.386  1.00 92.52           N  
ANISOU  151  N   LEU A  23    11555  11387  12212    -49    599   -230       N  
ATOM    152  CA  LEU A  23      42.880   9.404  14.612  1.00 90.96           C  
ANISOU  152  CA  LEU A  23    11383  11232  11946     17    568   -170       C  
ATOM    153  C   LEU A  23      42.542   8.308  15.625  1.00100.41           C  
ANISOU  153  C   LEU A  23    12517  12419  13215     80    621    -85       C  
ATOM    154  O   LEU A  23      42.776   8.430  16.834  1.00 95.62           O  
ANISOU  154  O   LEU A  23    11924  11842  12564    148    612    -21       O  
ATOM    155  CB  LEU A  23      41.635  10.235  14.297  1.00 86.78           C  
ANISOU  155  CB  LEU A  23    10900  10716  11355     17    545   -189       C  
ATOM    156  CG  LEU A  23      40.997  10.979  15.471  1.00 89.06           C  
ANISOU  156  CG  LEU A  23    11240  11042  11555    103    531   -128       C  
ATOM    157  CD1 LEU A  23      42.006  11.933  16.091  1.00 94.25           C  
ANISOU  157  CD1 LEU A  23    11977  11726  12108    120    464   -139       C  
ATOM    158  CD2 LEU A  23      39.769  11.732  15.013  1.00 89.63           C  
ANISOU  158  CD2 LEU A  23    11343  11121  11590    102    524   -135       C  
ATOM    159  N   ASN A  24      41.967   7.239  15.102  1.00 97.93           N  
ANISOU  159  N   ASN A  24    12141  12057  13012     58    670    -85       N  
ATOM    160  CA  ASN A  24      41.556   6.104  15.904  1.00104.92           C  
ANISOU  160  CA  ASN A  24    12948  12921  13994    110    725      1       C  
ATOM    161  C   ASN A  24      42.798   5.519  16.542  1.00105.01           C  
ANISOU  161  C   ASN A  24    12927  12937  14037    133    748     36       C  
ATOM    162  O   ASN A  24      42.914   5.409  17.768  1.00 97.92           O  
ANISOU  162  O   ASN A  24    12017  12070  13117    206    756    119       O  
ATOM    163  CB  ASN A  24      40.847   5.081  15.023  1.00 97.43           C  
ANISOU  163  CB  ASN A  24    11947  11899  13173     59    750    -18       C  
ATOM    164  CG  ASN A  24      39.993   4.124  15.806  1.00103.20           C  
ANISOU  164  CG  ASN A  24    12591  12606  14014    111    795     89       C  
ATOM    165  ND2 ASN A  24      39.028   3.532  15.134  1.00 92.48           N  
ANISOU  165  ND2 ASN A  24    11194  11184  12762     65    784     89       N  
ATOM    166  OD1 ASN A  24      40.188   3.921  17.001  1.00101.12           O  
ANISOU  166  OD1 ASN A  24    12298  12377  13745    190    832    177       O  
ATOM    167  N   SER A  25      43.751   5.194  15.681  1.00 90.33           N  
ANISOU  167  N   SER A  25    11057  11044  12221     76    759    -22       N  
ATOM    168  CA  SER A  25      44.996   4.586  16.109  1.00104.34           C  
ANISOU  168  CA  SER A  25    12782  12812  14050     90    786     21       C  
ATOM    169  C   SER A  25      45.704   5.495  17.111  1.00103.71           C  
ANISOU  169  C   SER A  25    12737  12793  13875    123    719     67       C  
ATOM    170  O   SER A  25      46.197   5.033  18.141  1.00 93.65           O  
ANISOU  170  O   SER A  25    11425  11533  12624    170    722    148       O  
ATOM    171  CB  SER A  25      45.884   4.296  14.900  1.00100.90           C  
ANISOU  171  CB  SER A  25    12344  12330  13664     34    821    -44       C  
ATOM    172  OG  SER A  25      47.220   4.676  15.153  1.00124.36           O  
ANISOU  172  OG  SER A  25    15299  15326  16626     34    804     -9       O  
ATOM    173  N   HIS A  26      45.716   6.794  16.825  1.00110.16           N  
ANISOU  173  N   HIS A  26    13634  13641  14582     98    648     17       N  
ATOM    174  CA  HIS A  26      46.354   7.763  17.706  1.00101.18           C  
ANISOU  174  CA  HIS A  26    12553  12544  13347    120    557     49       C  
ATOM    175  C   HIS A  26      45.660   7.816  19.064  1.00111.23           C  
ANISOU  175  C   HIS A  26    13870  13846  14545    210    544    114       C  
ATOM    176  O   HIS A  26      46.312   7.979  20.095  1.00121.50           O  
ANISOU  176  O   HIS A  26    15201  15165  15798    248    486    170       O  
ATOM    177  CB  HIS A  26      46.356   9.152  17.060  1.00101.10           C  
ANISOU  177  CB  HIS A  26    12624  12548  13241     75    484    -20       C  
ATOM    178  CG  HIS A  26      46.848  10.237  17.963  1.00102.07           C  
ANISOU  178  CG  HIS A  26    12830  12696  13257     95    370      3       C  
ATOM    179  CD2 HIS A  26      48.080  10.773  18.125  1.00118.39           C  
ANISOU  179  CD2 HIS A  26    14900  14758  15325     57    278     26       C  
ATOM    180  ND1 HIS A  26      46.023  10.903  18.842  1.00121.72           N  
ANISOU  180  ND1 HIS A  26    15421  15206  15621    163    331     11       N  
ATOM    181  CE1 HIS A  26      46.725  11.812  19.504  1.00110.71           C  
ANISOU  181  CE1 HIS A  26    14110  13814  14140    165    212     21       C  
ATOM    182  NE2 HIS A  26      47.973  11.752  19.083  1.00116.04           N  
ANISOU  182  NE2 HIS A  26    14719  14473  14898     94    168     34       N  
ATOM    183  N   LEU A  27      44.336   7.694  19.058  1.00110.03           N  
ANISOU  183  N   LEU A  27    13727  13696  14383    248    597    116       N  
ATOM    184  CA  LEU A  27      43.563   7.708  20.294  1.00110.41           C  
ANISOU  184  CA  LEU A  27    13816  13770  14364    354    616    194       C  
ATOM    185  C   LEU A  27      43.690   6.400  21.049  1.00103.83           C  
ANISOU  185  C   LEU A  27    12894  12929  13626    405    682    287       C  
ATOM    186  O   LEU A  27      43.691   6.382  22.280  1.00102.81           O  
ANISOU  186  O   LEU A  27    12808  12828  13429    495    679    364       O  
ATOM    187  CB  LEU A  27      42.095   7.980  20.008  1.00104.01           C  
ANISOU  187  CB  LEU A  27    13019  12961  13540    383    662    194       C  
ATOM    188  CG  LEU A  27      41.772   9.404  19.602  1.00103.22           C  
ANISOU  188  CG  LEU A  27    13024  12877  13319    367    602    128       C  
ATOM    189  CD1 LEU A  27      40.347   9.439  19.138  1.00 89.63           C  
ANISOU  189  CD1 LEU A  27    11276  11147  11632    380    657    144       C  
ATOM    190  CD2 LEU A  27      42.001  10.363  20.770  1.00107.32           C  
ANISOU  190  CD2 LEU A  27    13679  13423  13674    452    544    152       C  
ATOM    191  N   ARG A  28      43.770   5.304  20.302  1.00102.94           N  
ANISOU  191  N   ARG A  28    12671  12774  13667    352    743    278       N  
ATOM    192  CA  ARG A  28      44.026   3.993  20.898  1.00111.53           C  
ANISOU  192  CA  ARG A  28    13663  13844  14870    387    807    363       C  
ATOM    193  C   ARG A  28      45.365   3.975  21.610  1.00115.89           C  
ANISOU  193  C   ARG A  28    14219  14417  15398    397    759    403       C  
ATOM    194  O   ARG A  28      45.489   3.409  22.693  1.00110.49           O  
ANISOU  194  O   ARG A  28    13511  13750  14721    468    778    498       O  
ATOM    195  CB  ARG A  28      43.987   2.897  19.840  1.00103.00           C  
ANISOU  195  CB  ARG A  28    12487  12697  13953    321    869    329       C  
ATOM    196  CG  ARG A  28      42.588   2.680  19.303  1.00 98.16           C  
ANISOU  196  CG  ARG A  28    11853  12051  13393    311    901    319       C  
ATOM    197  CD  ARG A  28      42.490   1.423  18.476  1.00113.03           C  
ANISOU  197  CD  ARG A  28    13655  13850  15442    257    948    298       C  
ATOM    198  NE  ARG A  28      41.117   1.216  18.039  1.00109.62           N  
ANISOU  198  NE  ARG A  28    13198  13377  15074    241    950    307       N  
ATOM    199  CZ  ARG A  28      40.551   0.025  17.931  1.00117.96           C  
ANISOU  199  CZ  ARG A  28    14168  14361  16290    231    987    354       C  
ATOM    200  NH1 ARG A  28      41.243  -1.064  18.241  1.00 97.93           N1+
ANISOU  200  NH1 ARG A  28    11567  11787  13854    245   1037    390       N1+
ATOM    201  NH2 ARG A  28      39.298  -0.070  17.521  1.00109.25           N  
ANISOU  201  NH2 ARG A  28    13038  13217  15256    206    967    374       N  
ATOM    202  N   ALA A  29      46.358   4.616  21.000  1.00105.13           N  
ANISOU  202  N   ALA A  29    12881  13051  14012    326    691    342       N  
ATOM    203  CA  ALA A  29      47.688   4.706  21.584  1.00109.47           C  
ANISOU  203  CA  ALA A  29    13423  13612  14558    318    622    391       C  
ATOM    204  C   ALA A  29      47.631   5.389  22.943  1.00109.81           C  
ANISOU  204  C   ALA A  29    13573  13698  14453    393    535    444       C  
ATOM    205  O   ALA A  29      48.353   5.026  23.863  1.00124.42           O  
ANISOU  205  O   ALA A  29    15409  15558  16307    424    495    525       O  
ATOM    206  CB  ALA A  29      48.629   5.454  20.651  1.00104.42           C  
ANISOU  206  CB  ALA A  29    12792  12961  13924    231    561    331       C  
ATOM    207  N   GLU A  30      46.757   6.377  23.072  1.00105.81           N  
ANISOU  207  N   GLU A  30    13184  13211  13809    428    504    400       N  
ATOM    208  CA  GLU A  30      46.596   7.079  24.338  1.00115.35           C  
ANISOU  208  CA  GLU A  30    14532  14447  14849    517    430    439       C  
ATOM    209  C   GLU A  30      45.664   6.286  25.251  1.00115.48           C  
ANISOU  209  C   GLU A  30    14538  14483  14858    635    535    529       C  
ATOM    210  O   GLU A  30      45.190   6.803  26.264  1.00130.74           O  
ANISOU  210  O   GLU A  30    16601  16438  16637    740    517    566       O  
ATOM    211  CB  GLU A  30      46.051   8.496  24.113  1.00124.80           C  
ANISOU  211  CB  GLU A  30    15872  15650  15899    519    367    360       C  
ATOM    212  CG  GLU A  30      46.820   9.309  23.090  1.00125.42           C  
ANISOU  212  CG  GLU A  30    15948  15708  15997    403    279    277       C  
ATOM    213  CD  GLU A  30      48.201   9.674  23.571  1.00149.12           C  
ANISOU  213  CD  GLU A  30    18976  18698  18984    361    134    305       C  
ATOM    214  OE1 GLU A  30      49.179   9.071  23.078  1.00149.57           O  
ANISOU  214  OE1 GLU A  30    18906  18741  19184    290    138    333       O  
ATOM    215  OE2 GLU A  30      48.304  10.564  24.443  1.00161.52           O1-
ANISOU  215  OE2 GLU A  30    20700  20267  20404    402     14    306       O1-
ATOM    216  N   LYS A  31      45.404   5.036  24.871  1.00109.90           N  
ANISOU  216  N   LYS A  31    13680  13758  14318    623    647    568       N  
ATOM    217  CA  LYS A  31      44.508   4.135  25.603  1.00114.98           C  
ANISOU  217  CA  LYS A  31    14274  14410  15003    724    759    671       C  
ATOM    218  C   LYS A  31      43.095   4.730  25.809  1.00132.06           C  
ANISOU  218  C   LYS A  31    16513  16590  17075    810    815    685       C  
ATOM    219  O   LYS A  31      42.389   4.401  26.771  1.00128.16           O  
ANISOU  219  O   LYS A  31    16034  16116  16546    934    891    792       O  
ATOM    220  CB  LYS A  31      45.142   3.745  26.945  1.00129.48           C  
ANISOU  220  CB  LYS A  31    16139  16273  16784    806    733    773       C  
ATOM    221  CG  LYS A  31      46.548   3.137  26.810  1.00134.55           C  
ANISOU  221  CG  LYS A  31    16690  16899  17535    726    680    786       C  
ATOM    222  CD  LYS A  31      46.763   1.984  27.782  1.00140.70           C  
ANISOU  222  CD  LYS A  31    17392  17688  18381    798    737    915       C  
ATOM    223  CE  LYS A  31      47.027   0.676  27.048  1.00141.97           C  
ANISOU  223  CE  LYS A  31    17366  17804  18771    736    832    934       C  
ATOM    224  NZ  LYS A  31      46.956  -0.490  27.974  1.00147.65           N1+
ANISOU  224  NZ  LYS A  31    18001  18532  19569    817    911   1068       N1+
ATOM    225  N   THR A  32      42.682   5.591  24.882  1.00108.99           N  
ANISOU  225  N   THR A  32    13632  13658  14122    751    787    591       N  
ATOM    226  CA  THR A  32      41.330   6.127  24.880  1.00110.87           C  
ANISOU  226  CA  THR A  32    13915  13904  14307    818    846    610       C  
ATOM    227  C   THR A  32      40.629   5.828  23.559  1.00108.01           C  
ANISOU  227  C   THR A  32    13443  13506  14091    725    884    564       C  
ATOM    228  O   THR A  32      40.414   6.732  22.757  1.00123.23           O  
ANISOU  228  O   THR A  32    15423  15430  15970    667    838    477       O  
ATOM    229  CB  THR A  32      41.334   7.656  25.119  1.00124.18           C  
ANISOU  229  CB  THR A  32    15786  15608  15788    851    764    548       C  
ATOM    230  CG2 THR A  32      41.932   7.980  26.475  1.00128.90           C  
ANISOU  230  CG2 THR A  32    16527  16228  16222    951    708    592       C  
ATOM    231  OG1 THR A  32      42.114   8.305  24.103  1.00122.43           O  
ANISOU  231  OG1 THR A  32    15577  15372  15570    720    662    426       O  
ATOM    232  N   PRO A  33      40.281   4.555  23.315  1.00108.18           N  
ANISOU  232  N   PRO A  33    13317  13493  14292    706    958    622       N  
ATOM    233  CA  PRO A  33      39.628   4.248  22.041  1.00103.58           C  
ANISOU  233  CA  PRO A  33    12651  12862  13843    610    968    572       C  
ATOM    234  C   PRO A  33      38.337   5.017  21.853  1.00108.28           C  
ANISOU  234  C   PRO A  33    13277  13464  14400    643    986    595       C  
ATOM    235  O   PRO A  33      37.644   5.324  22.832  1.00110.26           O  
ANISOU  235  O   PRO A  33    13564  13747  14582    769   1044    700       O  
ATOM    236  CB  PRO A  33      39.355   2.734  22.128  1.00116.40           C  
ANISOU  236  CB  PRO A  33    14129  14438  15660    611   1040    658       C  
ATOM    237  CG  PRO A  33      39.562   2.366  23.557  1.00108.97           C  
ANISOU  237  CG  PRO A  33    13189  13536  14679    733   1093    779       C  
ATOM    238  CD  PRO A  33      40.584   3.333  24.078  1.00109.31           C  
ANISOU  238  CD  PRO A  33    13370  13630  14531    754   1017    723       C  
ATOM    239  N   PRO A  34      38.029   5.361  20.599  1.00107.26           N  
ANISOU  239  N   PRO A  34    13140  13306  14309    539    939    505       N  
ATOM    240  CA  PRO A  34      36.799   6.089  20.283  1.00104.74           C  
ANISOU  240  CA  PRO A  34    12833  12989  13974    556    948    531       C  
ATOM    241  C   PRO A  34      35.653   5.184  19.875  1.00108.07           C  
ANISOU  241  C   PRO A  34    13117  13357  14589    532    986    620       C  
ATOM    242  O   PRO A  34      35.876   4.060  19.424  1.00 93.00           O  
ANISOU  242  O   PRO A  34    11119  11392  12826    463    979    609       O  
ATOM    243  CB  PRO A  34      37.214   6.961  19.108  1.00101.59           C  
ANISOU  243  CB  PRO A  34    12503  12587  13509    447    859    385       C  
ATOM    244  CG  PRO A  34      38.248   6.096  18.387  1.00106.49           C  
ANISOU  244  CG  PRO A  34    13079  13169  14213    347    829    302       C  
ATOM    245  CD  PRO A  34      38.985   5.363  19.478  1.00 89.63           C  
ANISOU  245  CD  PRO A  34    10917  11047  12090    414    871    368       C  
ATOM    246  N   TYR A  35      34.434   5.699  20.051  1.00 98.26           N  
ANISOU  246  N   TYR A  35    11859  12123  13353    593   1024    715       N  
ATOM    247  CA  TYR A  35      33.239   5.140  19.458  1.00103.36           C  
ANISOU  247  CA  TYR A  35    12376  12711  14186    548   1027    800       C  
ATOM    248  C   TYR A  35      33.229   5.599  18.016  1.00105.77           C  
ANISOU  248  C   TYR A  35    12712  12985  14490    407    920    663       C  
ATOM    249  O   TYR A  35      33.436   6.777  17.737  1.00106.56           O  
ANISOU  249  O   TYR A  35    12920  13127  14441    401    886    581       O  
ATOM    250  CB  TYR A  35      31.989   5.617  20.202  1.00102.08           C  
ANISOU  250  CB  TYR A  35    12182  12573  14031    677   1116    972       C  
ATOM    251  CG  TYR A  35      30.731   4.788  19.993  1.00107.92           C  
ANISOU  251  CG  TYR A  35    12746  13250  15010    661   1140   1132       C  
ATOM    252  CD1 TYR A  35      30.534   3.585  20.679  1.00119.97           C  
ANISOU  252  CD1 TYR A  35    14148  14745  16690    712   1209   1270       C  
ATOM    253  CD2 TYR A  35      29.720   5.230  19.147  1.00101.15           C  
ANISOU  253  CD2 TYR A  35    11839  12361  14234    597   1089   1162       C  
ATOM    254  CE1 TYR A  35      29.379   2.843  20.505  1.00102.55           C  
ANISOU  254  CE1 TYR A  35    11769  12471  14724    694   1220   1434       C  
ATOM    255  CE2 TYR A  35      28.570   4.502  18.969  1.00112.55           C  
ANISOU  255  CE2 TYR A  35    13113  13739  15913    576   1091   1325       C  
ATOM    256  CZ  TYR A  35      28.400   3.309  19.645  1.00114.42           C  
ANISOU  256  CZ  TYR A  35    13224  13939  16312    622   1154   1462       C  
ATOM    257  OH  TYR A  35      27.237   2.600  19.447  1.00118.73           O  
ANISOU  257  OH  TYR A  35    13589  14408  17116    591   1142   1639       O  
ATOM    258  N   VAL A  36      33.001   4.677  17.095  1.00 99.01           N  
ANISOU  258  N   VAL A  36    11774  12049  13794    295    863    638       N  
ATOM    259  CA  VAL A  36      33.110   5.002  15.682  1.00 95.83           C  
ANISOU  259  CA  VAL A  36    11425  11612  13375    163    757    497       C  
ATOM    260  C   VAL A  36      31.799   4.841  14.925  1.00110.02           C  
ANISOU  260  C   VAL A  36    13140  13345  15317     94    693    563       C  
ATOM    261  O   VAL A  36      31.104   3.821  15.041  1.00 99.97           O  
ANISOU  261  O   VAL A  36    11746  12003  14235     81    692    674       O  
ATOM    262  CB  VAL A  36      34.176   4.136  15.012  1.00104.18           C  
ANISOU  262  CB  VAL A  36    12508  12618  14460     77    720    370       C  
ATOM    263  CG1 VAL A  36      34.231   4.429  13.519  1.00 93.46           C  
ANISOU  263  CG1 VAL A  36    11220  11216  13073    -45    620    232       C  
ATOM    264  CG2 VAL A  36      35.526   4.376  15.680  1.00 99.57           C  
ANISOU  264  CG2 VAL A  36    11993  12096  13745    133    768    315       C  
ATOM    265  N   ILE A  37      31.474   5.862  14.139  1.00102.95           N  
ANISOU  265  N   ILE A  37    12308  12469  14342     45    631    502       N  
ATOM    266  CA  ILE A  37      30.301   5.839  13.281  1.00 97.99           C  
ANISOU  266  CA  ILE A  37    11614  11779  13836    -38    543    554       C  
ATOM    267  C   ILE A  37      30.640   6.107  11.804  1.00117.11           C  
ANISOU  267  C   ILE A  37    14134  14167  16195   -171    420    384       C  
ATOM    268  O   ILE A  37      31.244   7.131  11.479  1.00109.15           O  
ANISOU  268  O   ILE A  37    13235  13220  15016   -172    417    277       O  
ATOM    269  CB  ILE A  37      29.287   6.865  13.755  1.00100.44           C  
ANISOU  269  CB  ILE A  37    11890  12142  14129     44    590    688       C  
ATOM    270  CG1 ILE A  37      28.935   6.616  15.223  1.00100.98           C  
ANISOU  270  CG1 ILE A  37    11881  12244  14242    198    729    865       C  
ATOM    271  CG2 ILE A  37      28.063   6.851  12.858  1.00 98.83           C  
ANISOU  271  CG2 ILE A  37    11603  11875  14072    -49    487    761       C  
ATOM    272  CD1 ILE A  37      27.968   7.638  15.784  1.00100.34           C  
ANISOU  272  CD1 ILE A  37    11783  12212  14130    309    806   1008       C  
ATOM    273  N   ASN A  38      30.271   5.181  10.915  1.00113.63           N  
ANISOU  273  N   ASN A  38    13665  13622  15889   -281    316    361       N  
ATOM    274  CA  ASN A  38      30.463   5.380   9.470  1.00104.46           C  
ANISOU  274  CA  ASN A  38    12613  12416  14662   -399    195    209       C  
ATOM    275  C   ASN A  38      29.176   5.654   8.694  1.00113.05           C  
ANISOU  275  C   ASN A  38    13658  13455  15842   -482     69    276       C  
ATOM    276  O   ASN A  38      28.264   4.830   8.672  1.00116.76           O  
ANISOU  276  O   ASN A  38    14021  13836  16508   -527      1    388       O  
ATOM    277  CB  ASN A  38      31.154   4.170   8.840  1.00106.39           C  
ANISOU  277  CB  ASN A  38    12913  12562  14949   -468    150     96       C  
ATOM    278  CG  ASN A  38      31.005   4.152   7.328  1.00123.34           C  
ANISOU  278  CG  ASN A  38    15170  14631  17061   -588      8    -27       C  
ATOM    279  ND2 ASN A  38      30.303   3.144   6.809  1.00108.89           N  
ANISOU  279  ND2 ASN A  38    13313  12672  15390   -673   -110     -2       N  
ATOM    280  OD1 ASN A  38      31.489   5.053   6.635  1.00120.18           O  
ANISOU  280  OD1 ASN A  38    14885  14282  16495   -604     -4   -137       O  
ATOM    281  N   LEU A  39      29.126   6.806   8.033  1.00114.59           N  
ANISOU  281  N   LEU A  39    13932  13702  15905   -507     30    213       N  
ATOM    282  CA  LEU A  39      27.948   7.213   7.278  1.00104.85           C  
ANISOU  282  CA  LEU A  39    12661  12433  14744   -585    -92    279       C  
ATOM    283  C   LEU A  39      28.164   7.157   5.767  1.00113.16           C  
ANISOU  283  C   LEU A  39    13848  13423  15724   -710   -239    122       C  
ATOM    284  O   LEU A  39      27.328   7.629   5.007  1.00115.79           O  
ANISOU  284  O   LEU A  39    14180  13735  16081   -783   -356    153       O  
ATOM    285  CB  LEU A  39      27.513   8.617   7.688  1.00103.01           C  
ANISOU  285  CB  LEU A  39    12407  12302  14430   -511    -27    357       C  
ATOM    286  CG  LEU A  39      27.104   8.724   9.153  1.00103.32           C  
ANISOU  286  CG  LEU A  39    12332  12392  14533   -372    118    531       C  
ATOM    287  CD1 LEU A  39      26.573  10.094   9.447  1.00 87.45           C  
ANISOU  287  CD1 LEU A  39    10320  10461  12445   -299    175    607       C  
ATOM    288  CD2 LEU A  39      26.044   7.686   9.467  1.00107.55           C  
ANISOU  288  CD2 LEU A  39    12701  12844  15321   -388     86    713       C  
ATOM    289  N   ASP A  40      29.275   6.577   5.322  1.00115.76           N  
ANISOU  289  N   ASP A  40    14300  13721  15964   -730   -230    -38       N  
ATOM    290  CA  ASP A  40      29.445   6.350   3.891  1.00124.46           C  
ANISOU  290  CA  ASP A  40    15548  14744  16996   -834   -363   -181       C  
ATOM    291  C   ASP A  40      28.912   4.970   3.565  1.00120.71           C  
ANISOU  291  C   ASP A  40    15054  14119  16693   -914   -484   -161       C  
ATOM    292  O   ASP A  40      29.461   3.968   4.017  1.00132.00           O  
ANISOU  292  O   ASP A  40    16473  15499  18182   -886   -425   -181       O  
ATOM    293  CB  ASP A  40      30.906   6.468   3.463  1.00136.05           C  
ANISOU  293  CB  ASP A  40    17172  16245  18276   -805   -283   -355       C  
ATOM    294  CG  ASP A  40      31.085   6.445   1.945  1.00145.70           C  
ANISOU  294  CG  ASP A  40    18570  17400  19387   -888   -397   -499       C  
ATOM    295  OD1 ASP A  40      30.147   6.036   1.222  1.00135.35           O  
ANISOU  295  OD1 ASP A  40    17280  15992  18156   -982   -562   -483       O  
ATOM    296  OD2 ASP A  40      32.181   6.832   1.475  1.00148.04           O1-
ANISOU  296  OD2 ASP A  40    18991  17740  19516   -856   -325   -620       O1-
ATOM    297  N   PRO A  41      27.830   4.912   2.782  1.00113.87           N  
ANISOU  297  N   PRO A  41    14180  13171  15916  -1019   -665   -116       N  
ATOM    298  CA  PRO A  41      27.242   3.626   2.401  1.00121.27           C  
ANISOU  298  CA  PRO A  41    15106  13942  17029  -1113   -820    -94       C  
ATOM    299  C   PRO A  41      28.139   2.858   1.434  1.00135.94           C  
ANISOU  299  C   PRO A  41    17181  15700  18769  -1154   -870   -299       C  
ATOM    300  O   PRO A  41      28.186   1.624   1.455  1.00142.27           O  
ANISOU  300  O   PRO A  41    17995  16374  19687  -1184   -918   -316       O  
ATOM    301  CB  PRO A  41      25.929   4.032   1.724  1.00113.69           C  
ANISOU  301  CB  PRO A  41    14099  12934  16162  -1217  -1014      3       C  
ATOM    302  CG  PRO A  41      25.658   5.404   2.223  1.00116.46           C  
ANISOU  302  CG  PRO A  41    14360  13438  16452  -1145   -908     98       C  
ATOM    303  CD  PRO A  41      26.999   6.040   2.346  1.00108.90           C  
ANISOU  303  CD  PRO A  41    13526  12594  15258  -1054   -741    -53       C  
ATOM    304  N   ALA A  42      28.867   3.606   0.611  1.00146.36           N  
ANISOU  304  N   ALA A  42    18673  17077  19861  -1144   -847   -448       N  
ATOM    305  CA  ALA A  42      29.579   3.044  -0.528  1.00145.89           C  
ANISOU  305  CA  ALA A  42    18849  16918  19664  -1179   -904   -636       C  
ATOM    306  C   ALA A  42      30.922   2.386  -0.187  1.00152.92           C  
ANISOU  306  C   ALA A  42    19807  17807  20489  -1090   -732   -734       C  
ATOM    307  O   ALA A  42      31.498   1.692  -1.025  1.00150.08           O  
ANISOU  307  O   ALA A  42    19638  17342  20045  -1103   -760   -874       O  
ATOM    308  CB  ALA A  42      29.788   4.135  -1.577  1.00135.93           C  
ANISOU  308  CB  ALA A  42    17739  15720  18187  -1194   -937   -734       C  
ATOM    309  N   VAL A  43      31.424   2.592   1.028  1.00153.97           N  
ANISOU  309  N   VAL A  43    19795  18049  20658   -996   -556   -656       N  
ATOM    310  CA  VAL A  43      32.770   2.122   1.355  1.00148.47           C  
ANISOU  310  CA  VAL A  43    19150  17368  19894   -910   -390   -734       C  
ATOM    311  C   VAL A  43      32.893   0.613   1.377  1.00151.67           C  
ANISOU  311  C   VAL A  43    19584  17622  20422   -926   -414   -761       C  
ATOM    312  O   VAL A  43      31.923  -0.110   1.601  1.00155.95           O  
ANISOU  312  O   VAL A  43    20038  18067  21150   -988   -532   -675       O  
ATOM    313  CB  VAL A  43      33.263   2.630   2.723  1.00144.62           C  
ANISOU  313  CB  VAL A  43    18503  17023  19424   -811   -219   -637       C  
ATOM    314  CG1 VAL A  43      33.405   4.121   2.711  1.00151.78           C  
ANISOU  314  CG1 VAL A  43    19410  18070  20189   -782   -176   -633       C  
ATOM    315  CG2 VAL A  43      32.339   2.176   3.836  1.00141.31           C  
ANISOU  315  CG2 VAL A  43    17886  16592  19212   -807   -231   -468       C  
ATOM    316  N   LEU A  44      34.114   0.156   1.143  1.00156.32           N  
ANISOU  316  N   LEU A  44    20292  18188  20915   -865   -296   -871       N  
ATOM    317  CA  LEU A  44      34.455  -1.248   1.267  1.00154.80           C  
ANISOU  317  CA  LEU A  44    20129  17861  20827   -856   -276   -900       C  
ATOM    318  C   LEU A  44      34.626  -1.582   2.744  1.00149.04           C  
ANISOU  318  C   LEU A  44    19186  17197  20246   -792   -153   -765       C  
ATOM    319  O   LEU A  44      33.771  -2.219   3.355  1.00134.09           O  
ANISOU  319  O   LEU A  44    17157  15245  18545   -826   -220   -653       O  
ATOM    320  CB  LEU A  44      35.732  -1.572   0.471  1.00160.08           C  
ANISOU  320  CB  LEU A  44    21004  18484  21335   -797   -172  -1053       C  
ATOM    321  CG  LEU A  44      36.948  -0.625   0.504  1.00162.88           C  
ANISOU  321  CG  LEU A  44    21381  18984  21521   -705      6  -1084       C  
ATOM    322  CD1 LEU A  44      38.241  -1.386   0.211  1.00164.82           C  
ANISOU  322  CD1 LEU A  44    21746  19166  21711   -623    153  -1167       C  
ATOM    323  CD2 LEU A  44      36.797   0.553  -0.459  1.00161.88           C  
ANISOU  323  CD2 LEU A  44    21369  18921  21217   -731    -51  -1145       C  
ATOM    324  N   ARG A  45      35.724  -1.112   3.321  1.00158.04           N  
ANISOU  324  N   ARG A  45    20294  18459  21296   -698     21   -765       N  
ATOM    325  CA  ARG A  45      36.050  -1.404   4.702  1.00158.16           C  
ANISOU  325  CA  ARG A  45    20135  18540  21419   -627    142   -648       C  
ATOM    326  C   ARG A  45      35.768  -0.193   5.584  1.00144.37           C  
ANISOU  326  C   ARG A  45    18258  16956  19638   -590    181   -543       C  
ATOM    327  O   ARG A  45      35.548   0.919   5.099  1.00143.87           O  
ANISOU  327  O   ARG A  45    18245  16964  19457   -611    140   -573       O  
ATOM    328  CB  ARG A  45      37.524  -1.831   4.820  1.00164.37           C  
ANISOU  328  CB  ARG A  45    20973  19333  22147   -547    299   -707       C  
ATOM    329  CG  ARG A  45      37.881  -2.552   6.119  1.00170.83           C  
ANISOU  329  CG  ARG A  45    21636  20171  23102   -485    403   -598       C  
ATOM    330  CD  ARG A  45      39.271  -3.181   6.084  1.00179.48           C  
ANISOU  330  CD  ARG A  45    22786  21239  24171   -418    541   -651       C  
ATOM    331  NE  ARG A  45      39.523  -3.990   7.278  1.00197.18           N  
ANISOU  331  NE  ARG A  45    24878  23483  26557   -367    622   -541       N  
ATOM    332  CZ  ARG A  45      40.420  -4.972   7.355  1.00202.37           C  
ANISOU  332  CZ  ARG A  45    25552  24071  27270   -320    720   -557       C  
ATOM    333  NH1 ARG A  45      41.163  -5.284   6.301  1.00200.64           N1+
ANISOU  333  NH1 ARG A  45    25497  23768  26969   -310    762   -677       N1+
ATOM    334  NH2 ARG A  45      40.571  -5.648   8.487  1.00199.99           N  
ANISOU  334  NH2 ARG A  45    25104  23781  27102   -276    786   -443       N  
ATOM    335  N   VAL A  46      35.726  -0.436   6.884  1.00126.43           N  
ANISOU  335  N   VAL A  46    15830  14736  17471   -531    258   -416       N  
ATOM    336  CA  VAL A  46      35.839   0.619   7.867  1.00119.20           C  
ANISOU  336  CA  VAL A  46    14828  13973  16492   -462    334   -333       C  
ATOM    337  C   VAL A  46      37.018   0.250   8.740  1.00126.13           C  
ANISOU  337  C   VAL A  46    15666  14895  17362   -380    468   -314       C  
ATOM    338  O   VAL A  46      36.994  -0.796   9.395  1.00116.28           O  
ANISOU  338  O   VAL A  46    14335  13595  16252   -355    505   -245       O  
ATOM    339  CB  VAL A  46      34.594   0.776   8.717  1.00114.79           C  
ANISOU  339  CB  VAL A  46    14124  13441  16051   -451    304   -174       C  
ATOM    340  CG1 VAL A  46      34.921   1.612   9.936  1.00100.06           C  
ANISOU  340  CG1 VAL A  46    12192  11715  14113   -351    410    -91       C  
ATOM    341  CG2 VAL A  46      33.470   1.394   7.905  1.00112.30           C  
ANISOU  341  CG2 VAL A  46    13831  13103  15733   -529    173   -172       C  
ATOM    342  N   PRO A  47      38.047   1.112   8.741  1.00115.81           N  
ANISOU  342  N   PRO A  47    14415  13681  15908   -341    533   -366       N  
ATOM    343  CA  PRO A  47      39.384   0.921   9.297  1.00126.94           C  
ANISOU  343  CA  PRO A  47    15812  15130  17289   -276    643   -366       C  
ATOM    344  C   PRO A  47      39.435  -0.065  10.453  1.00137.58           C  
ANISOU  344  C   PRO A  47    17040  16462  18772   -224    703   -259       C  
ATOM    345  O   PRO A  47      39.950  -1.167  10.283  1.00162.41           O  
ANISOU  345  O   PRO A  47    20189  19522  21998   -222    745   -280       O  
ATOM    346  CB  PRO A  47      39.755   2.330   9.747  1.00132.15           C  
ANISOU  346  CB  PRO A  47    16474  15921  17816   -242    658   -349       C  
ATOM    347  CG  PRO A  47      39.135   3.195   8.691  1.00124.79           C  
ANISOU  347  CG  PRO A  47    15628  14991  16796   -302    575   -420       C  
ATOM    348  CD  PRO A  47      37.896   2.468   8.192  1.00111.16           C  
ANISOU  348  CD  PRO A  47    13894  13166  15177   -363    489   -413       C  
ATOM    349  N   TYR A  48      38.886   0.298  11.601  1.00120.92           N  
ANISOU  349  N   TYR A  48    14834  14427  16684   -176    713   -141       N  
ATOM    350  CA  TYR A  48      38.963  -0.599  12.741  1.00114.76           C  
ANISOU  350  CA  TYR A  48    13943  13641  16019   -115    778    -29       C  
ATOM    351  C   TYR A  48      37.681  -1.407  12.889  1.00111.99           C  
ANISOU  351  C   TYR A  48    13504  13211  15835   -137    737     59       C  
ATOM    352  O   TYR A  48      37.695  -2.592  13.256  1.00112.04           O  
ANISOU  352  O   TYR A  48    13439  13147  15986   -125    770    116       O  
ATOM    353  CB  TYR A  48      39.257   0.200  14.006  1.00107.06           C  
ANISOU  353  CB  TYR A  48    12929  12790  14959    -30    825     58       C  
ATOM    354  CG  TYR A  48      40.710   0.570  14.103  1.00108.18           C  
ANISOU  354  CG  TYR A  48    13118  12982  15002     -8    864      8       C  
ATOM    355  CD1 TYR A  48      41.180   1.768  13.579  1.00108.71           C  
ANISOU  355  CD1 TYR A  48    13272  13106  14927    -30    831    -70       C  
ATOM    356  CD2 TYR A  48      41.625  -0.295  14.688  1.00115.88           C  
ANISOU  356  CD2 TYR A  48    14040  13944  16045     31    932     51       C  
ATOM    357  CE1 TYR A  48      42.528   2.104  13.659  1.00105.15           C  
ANISOU  357  CE1 TYR A  48    12847  12694  14413    -15    860    -94       C  
ATOM    358  CE2 TYR A  48      42.961   0.026  14.767  1.00113.05           C  
ANISOU  358  CE2 TYR A  48    13707  13626  15621     47    961     28       C  
ATOM    359  CZ  TYR A  48      43.405   1.230  14.257  1.00111.17           C  
ANISOU  359  CZ  TYR A  48    13548  13441  15251     22    922    -41       C  
ATOM    360  OH  TYR A  48      44.732   1.551  14.341  1.00114.45           O  
ANISOU  360  OH  TYR A  48    13970  13889  15625     33    942    -42       O  
ATOM    361  N   GLY A  49      36.580  -0.750  12.557  1.00 97.00           N  
ANISOU  361  N   GLY A  49    11607  11321  13928   -173    662     79       N  
ATOM    362  CA  GLY A  49      35.258  -1.252  12.827  1.00105.24           C  
ANISOU  362  CA  GLY A  49    12543  12310  15136   -186    619    203       C  
ATOM    363  C   GLY A  49      34.407  -0.098  13.304  1.00106.38           C  
ANISOU  363  C   GLY A  49    12653  12547  15219   -144    617    292       C  
ATOM    364  O   GLY A  49      34.811   0.683  14.181  1.00102.41           O  
ANISOU  364  O   GLY A  49    12160  12154  14596    -55    691    328       O  
ATOM    365  N   ALA A  50      33.225   0.019  12.707  1.00 98.95           N  
ANISOU  365  N   ALA A  50    11682  11553  14361   -208    524    331       N  
ATOM    366  CA  ALA A  50      32.264   1.024  13.102  1.00106.88           C  
ANISOU  366  CA  ALA A  50    12640  12629  15341   -167    527    438       C  
ATOM    367  C   ALA A  50      31.291   0.421  14.104  1.00112.67           C  
ANISOU  367  C   ALA A  50    13209  13345  16257   -101    578    651       C  
ATOM    368  O   ALA A  50      30.724  -0.650  13.869  1.00115.32           O  
ANISOU  368  O   ALA A  50    13455  13568  16792   -159    522    714       O  
ATOM    369  CB  ALA A  50      31.526   1.563  11.896  1.00120.15           C  
ANISOU  369  CB  ALA A  50    14368  14268  17016   -270    399    383       C  
ATOM    370  N   ASN A  51      31.118   1.108  15.228  1.00109.24           N  
ANISOU  370  N   ASN A  51    12743  13012  15751     26    686    765       N  
ATOM    371  CA  ASN A  51      30.192   0.681  16.268  1.00 99.14           C  
ANISOU  371  CA  ASN A  51    11314  11732  14623    120    766    988       C  
ATOM    372  C   ASN A  51      28.770   0.860  15.819  1.00106.50           C  
ANISOU  372  C   ASN A  51    12147  12614  15705     75    699   1114       C  
ATOM    373  O   ASN A  51      27.883   0.071  16.162  1.00109.56           O  
ANISOU  373  O   ASN A  51    12377  12936  16314     85    706   1294       O  
ATOM    374  CB  ASN A  51      30.445   1.457  17.551  1.00 99.10           C  
ANISOU  374  CB  ASN A  51    11344  11848  14462    282    903   1062       C  
ATOM    375  CG  ASN A  51      31.827   1.206  18.099  1.00110.93           C  
ANISOU  375  CG  ASN A  51    12921  13390  15837    324    955    968       C  
ATOM    376  ND2 ASN A  51      31.957   0.174  18.930  1.00108.25           N  
ANISOU  376  ND2 ASN A  51    12492  13032  15608    385   1027   1074       N  
ATOM    377  OD1 ASN A  51      32.778   1.907  17.756  1.00112.03           O  
ANISOU  377  OD1 ASN A  51    13191  13576  15800    298    925    811       O  
ATOM    378  N   ILE A  52      28.553   1.923  15.057  1.00108.38           N  
ANISOU  378  N   ILE A  52    12467  12881  15831     26    632   1032       N  
ATOM    379  CA  ILE A  52      27.315   2.088  14.319  1.00105.81           C  
ANISOU  379  CA  ILE A  52    12063  12494  15647    -55    526   1118       C  
ATOM    380  C   ILE A  52      27.664   2.349  12.861  1.00115.22           C  
ANISOU  380  C   ILE A  52    13382  13640  16755   -204    372    914       C  
ATOM    381  O   ILE A  52      28.274   3.369  12.516  1.00111.17           O  
ANISOU  381  O   ILE A  52    13003  13204  16034   -200    378    778       O  
ATOM    382  CB  ILE A  52      26.445   3.212  14.870  1.00 99.29           C  
ANISOU  382  CB  ILE A  52    11195  11747  14783     49    607   1267       C  
ATOM    383  CG1 ILE A  52      26.380   3.152  16.399  1.00110.28           C  
ANISOU  383  CG1 ILE A  52    12527  13206  16170    233    792   1435       C  
ATOM    384  CG2 ILE A  52      25.041   3.109  14.293  1.00105.38           C  
ANISOU  384  CG2 ILE A  52    11826  12439  15774    -27    507   1424       C  
ATOM    385  CD1 ILE A  52      25.381   4.141  17.008  1.00120.31           C  
ANISOU  385  CD1 ILE A  52    13750  14536  17425    360    895   1616       C  
ATOM    386  N   ASP A  53      27.308   1.389  12.017  1.00113.99           N  
ANISOU  386  N   ASP A  53    13194  13354  16764   -331    233    895       N  
ATOM    387  CA  ASP A  53      27.612   1.450  10.601  1.00102.16           C  
ANISOU  387  CA  ASP A  53    11833  11793  15190   -467     81    705       C  
ATOM    388  C   ASP A  53      26.306   1.523   9.825  1.00120.63           C  
ANISOU  388  C   ASP A  53    14102  14050  17682   -572    -81    798       C  
ATOM    389  O   ASP A  53      25.361   0.779  10.094  1.00131.85           O  
ANISOU  389  O   ASP A  53    15365  15385  19346   -596   -130    975       O  
ATOM    390  CB  ASP A  53      28.458   0.245  10.191  1.00103.82           C  
ANISOU  390  CB  ASP A  53    12115  11904  15428   -525     43    573       C  
ATOM    391  CG  ASP A  53      28.958   0.325   8.758  1.00114.40           C  
ANISOU  391  CG  ASP A  53    13639  13185  16645   -636    -83    360       C  
ATOM    392  OD1 ASP A  53      28.280   0.961   7.925  1.00108.88           O  
ANISOU  392  OD1 ASP A  53    12975  12472  15924   -711   -203    346       O  
ATOM    393  OD2 ASP A  53      30.027  -0.269   8.460  1.00105.94           O1-
ANISOU  393  OD2 ASP A  53    12677  12076  15500   -642    -56    214       O1-
ATOM    394  N   ILE A  54      26.268   2.428   8.856  1.00118.04           N  
ANISOU  394  N   ILE A  54    13886  13745  17219   -637   -170    689       N  
ATOM    395  CA  ILE A  54      25.027   2.767   8.179  1.00119.78           C  
ANISOU  395  CA  ILE A  54    14041  13914  17558   -726   -318    791       C  
ATOM    396  C   ILE A  54      24.557   1.640   7.272  1.00133.77           C  
ANISOU  396  C   ILE A  54    15812  15510  19505   -876   -527    774       C  
ATOM    397  O   ILE A  54      23.356   1.406   7.149  1.00150.56           O  
ANISOU  397  O   ILE A  54    17797  17557  21850   -941   -646    947       O  
ATOM    398  CB  ILE A  54      25.173   4.088   7.356  1.00115.44           C  
ANISOU  398  CB  ILE A  54    13622  13441  16800   -754   -358    673       C  
ATOM    399  CG1 ILE A  54      23.826   4.534   6.791  1.00111.86           C  
ANISOU  399  CG1 ILE A  54    13077  12947  16479   -832   -498    812       C  
ATOM    400  CG2 ILE A  54      26.221   3.957   6.245  1.00123.30           C  
ANISOU  400  CG2 ILE A  54    14831  14403  17614   -831   -433    417       C  
ATOM    401  CD1 ILE A  54      23.861   5.874   6.108  1.00104.39           C  
ANISOU  401  CD1 ILE A  54    12234  12083  15347   -846   -521    730       C  
ATOM    402  N   ARG A  55      25.489   0.913   6.665  1.00142.39           N  
ANISOU  402  N   ARG A  55    17059  16531  20511   -928   -573    576       N  
ATOM    403  CA  ARG A  55      25.098  -0.007   5.606  1.00167.41           C  
ANISOU  403  CA  ARG A  55    20292  19522  23794  -1076   -796    518       C  
ATOM    404  C   ARG A  55      24.468  -1.307   6.120  1.00179.75           C  
ANISOU  404  C   ARG A  55    21694  20951  25650  -1107   -852    674       C  
ATOM    405  O   ARG A  55      23.574  -1.842   5.466  1.00191.77           O  
ANISOU  405  O   ARG A  55    23184  22328  27352  -1235  -1066    735       O  
ATOM    406  CB  ARG A  55      26.286  -0.316   4.683  1.00168.49           C  
ANISOU  406  CB  ARG A  55    20678  19615  23726  -1110   -821    251       C  
ATOM    407  CG  ARG A  55      27.661   0.008   5.226  1.00164.76           C  
ANISOU  407  CG  ARG A  55    20281  19267  23053   -988   -605    137       C  
ATOM    408  CD  ARG A  55      28.376  -1.276   5.594  1.00175.02           C  
ANISOU  408  CD  ARG A  55    21592  20482  24424   -964   -546     93       C  
ATOM    409  NE  ARG A  55      29.738  -1.096   6.097  1.00160.34           N  
ANISOU  409  NE  ARG A  55    19797  18727  22398   -856   -354     -4       N  
ATOM    410  CZ  ARG A  55      30.788  -0.817   5.335  1.00145.62           C  
ANISOU  410  CZ  ARG A  55    18121  16880  20327   -852   -324   -192       C  
ATOM    411  NH1 ARG A  55      31.989  -0.703   5.882  1.00156.77           N1+
ANISOU  411  NH1 ARG A  55    19558  18380  21628   -757   -155   -245       N1+
ATOM    412  NH2 ARG A  55      30.634  -0.640   4.031  1.00140.74           N  
ANISOU  412  NH2 ARG A  55    17665  16192  19619   -939   -464   -314       N  
ATOM    413  N   ASP A  56      24.886  -1.816   7.279  1.00184.43           N  
ANISOU  413  N   ASP A  56    22184  21587  26304   -998   -676    753       N  
ATOM    414  CA  ASP A  56      24.233  -3.024   7.787  1.00192.95           C  
ANISOU  414  CA  ASP A  56    23093  22541  27680  -1024   -725    924       C  
ATOM    415  C   ASP A  56      22.924  -2.640   8.486  1.00200.43           C  
ANISOU  415  C   ASP A  56    23795  23521  28839   -990   -708   1218       C  
ATOM    416  O   ASP A  56      22.197  -3.493   9.002  1.00210.39           O  
ANISOU  416  O   ASP A  56    24869  24690  30379  -1001   -737   1419       O  
ATOM    417  CB  ASP A  56      25.164  -3.850   8.704  1.00177.91           C  
ANISOU  417  CB  ASP A  56    21168  20651  25777   -925   -553    905       C  
ATOM    418  CG  ASP A  56      25.679  -3.082   9.913  1.00145.25           C  
ANISOU  418  CG  ASP A  56    16977  16706  21506   -754   -304    966       C  
ATOM    419  OD1 ASP A  56      25.112  -2.032  10.269  1.00128.53           O  
ANISOU  419  OD1 ASP A  56    14791  14698  19348   -695   -246   1078       O  
ATOM    420  OD2 ASP A  56      26.653  -3.568  10.529  1.00135.24           O1-
ANISOU  420  OD2 ASP A  56    15738  15471  20177   -675   -170    908       O1-
ATOM    421  N   SER A  57      22.630  -1.344   8.465  1.00187.13           N  
ANISOU  421  N   SER A  57    22112  21962  27028   -946   -659   1249       N  
ATOM    422  CA  SER A  57      21.344  -0.819   8.901  1.00187.29           C  
ANISOU  422  CA  SER A  57    21925  22009  27229   -919   -653   1519       C  
ATOM    423  C   SER A  57      20.445  -0.555   7.686  1.00181.80           C  
ANISOU  423  C   SER A  57    21242  21217  26618  -1081   -908   1531       C  
ATOM    424  O   SER A  57      19.219  -0.666   7.765  1.00177.06           O  
ANISOU  424  O   SER A  57    20443  20551  26280  -1124   -999   1776       O  
ATOM    425  CB  SER A  57      21.548   0.461   9.720  1.00185.57           C  
ANISOU  425  CB  SER A  57    21704  21982  26823   -753   -427   1562       C  
ATOM    426  OG  SER A  57      20.313   1.039  10.106  1.00188.62           O  
ANISOU  426  OG  SER A  57    21904  22394  27369   -710   -401   1825       O  
ATOM    427  N   ILE A  58      21.073  -0.213   6.563  1.00182.34           N  
ANISOU  427  N   ILE A  58    21542  21276  26465  -1166  -1021   1277       N  
ATOM    428  CA  ILE A  58      20.369   0.142   5.330  1.00181.07           C  
ANISOU  428  CA  ILE A  58    21439  21037  26323  -1316  -1267   1252       C  
ATOM    429  C   ILE A  58      21.085  -0.395   4.085  1.00185.87           C  
ANISOU  429  C   ILE A  58    22308  21533  26783  -1437  -1444    975       C  
ATOM    430  O   ILE A  58      22.207   0.014   3.785  1.00168.16           O  
ANISOU  430  O   ILE A  58    20264  19369  24259  -1389  -1347    750       O  
ATOM    431  CB  ILE A  58      20.226   1.676   5.180  1.00174.46           C  
ANISOU  431  CB  ILE A  58    20629  20351  25307  -1264  -1195   1254       C  
ATOM    432  CG1 ILE A  58      19.317   2.256   6.267  1.00165.61           C  
ANISOU  432  CG1 ILE A  58    19264  19318  24344  -1147  -1042   1546       C  
ATOM    433  CG2 ILE A  58      19.696   2.035   3.801  1.00178.30           C  
ANISOU  433  CG2 ILE A  58    21216  20762  25769  -1420  -1452   1188       C  
ATOM    434  CD1 ILE A  58      20.064   2.855   7.437  1.00143.93           C  
ANISOU  434  CD1 ILE A  58    16527  16737  21425   -952   -747   1535       C  
ATOM    435  N   LYS A  59      20.434  -1.295   3.354  1.00197.54           N  
ANISOU  435  N   LYS A  59    23790  22818  28448  -1590  -1705    999       N  
ATOM    436  CA  LYS A  59      21.027  -1.864   2.144  1.00205.02           C  
ANISOU  436  CA  LYS A  59    25012  23635  29254  -1698  -1885    742       C  
ATOM    437  C   LYS A  59      20.205  -1.489   0.906  1.00220.59           C  
ANISOU  437  C   LYS A  59    27066  25517  31231  -1852  -2172    731       C  
ATOM    438  O   LYS A  59      18.975  -1.489   0.959  1.00225.05           O  
ANISOU  438  O   LYS A  59    27437  26020  32054  -1932  -2323    961       O  
ATOM    439  CB  LYS A  59      21.141  -3.388   2.267  1.00197.72           C  
ANISOU  439  CB  LYS A  59    24087  22528  28509  -1749  -1968    731       C  
ATOM    440  CG  LYS A  59      21.187  -3.905   3.705  1.00190.36           C  
ANISOU  440  CG  LYS A  59    22925  21645  27758  -1631  -1756    909       C  
ATOM    441  CD  LYS A  59      19.795  -4.280   4.214  1.00190.55           C  
ANISOU  441  CD  LYS A  59    22657  21586  28157  -1685  -1863   1228       C  
ATOM    442  CE  LYS A  59      19.774  -4.419   5.728  1.00189.41           C  
ANISOU  442  CE  LYS A  59    22273  21546  28149  -1529  -1600   1438       C  
ATOM    443  NZ  LYS A  59      20.854  -5.316   6.229  1.00189.44           N1+
ANISOU  443  NZ  LYS A  59    22353  21534  28093  -1458  -1461   1311       N1+
ATOM    444  N   TYR A  60      20.879  -1.160  -0.197  1.00222.46           N  
ANISOU  444  N   TYR A  60    27587  25749  31189  -1890  -2244    481       N  
ATOM    445  CA  TYR A  60      20.178  -0.837  -1.443  1.00220.30           C  
ANISOU  445  CA  TYR A  60    27429  25386  30889  -2035  -2529    449       C  
ATOM    446  C   TYR A  60      20.436  -1.889  -2.531  1.00216.58           C  
ANISOU  446  C   TYR A  60    27227  24700  30365  -2153  -2770    251       C  
ATOM    447  O   TYR A  60      21.597  -2.153  -2.849  1.00204.47           O  
ANISOU  447  O   TYR A  60    25928  23167  28594  -2090  -2663     17       O  
ATOM    448  CB  TYR A  60      20.558   0.555  -1.953  1.00216.32           C  
ANISOU  448  CB  TYR A  60    27044  25048  30100  -1987  -2444    345       C  
ATOM    449  CG  TYR A  60      22.030   0.767  -2.203  1.00215.75           C  
ANISOU  449  CG  TYR A  60    27213  25061  29701  -1886  -2257     82       C  
ATOM    450  CD1 TYR A  60      22.886   1.096  -1.160  1.00215.84           C  
ANISOU  450  CD1 TYR A  60    27147  25229  29633  -1730  -1953     78       C  
ATOM    451  CD2 TYR A  60      22.563   0.664  -3.482  1.00214.36           C  
ANISOU  451  CD2 TYR A  60    27345  24807  29296  -1942  -2385   -149       C  
ATOM    452  CE1 TYR A  60      24.233   1.303  -1.375  1.00211.61           C  
ANISOU  452  CE1 TYR A  60    26808  24768  28826  -1642  -1788   -135       C  
ATOM    453  CE2 TYR A  60      23.913   0.869  -3.709  1.00214.32           C  
ANISOU  453  CE2 TYR A  60    27542  24879  29009  -1839  -2197   -362       C  
ATOM    454  CZ  TYR A  60      24.744   1.190  -2.647  1.00206.93           C  
ANISOU  454  CZ  TYR A  60    26499  24098  28026  -1694  -1902   -347       C  
ATOM    455  OH  TYR A  60      26.090   1.402  -2.846  1.00187.41           O  
ANISOU  455  OH  TYR A  60    24204  21701  25303  -1596  -1719   -533       O  
ATOM    456  N   LYS A  61      19.395  -2.494  -3.125  1.00221.62           N  
ANISOU  456  N   LYS A  61    27847  25144  31216  -2318  -3096    343       N  
ATOM    457  CA  LYS A  61      17.955  -2.186  -2.973  1.00226.44           C  
ANISOU  457  CA  LYS A  61    28192  25726  32119  -2416  -3271    630       C  
ATOM    458  C   LYS A  61      17.658  -0.732  -3.364  1.00221.81           C  
ANISOU  458  C   LYS A  61    27596  25299  31382  -2402  -3249    663       C  
ATOM    459  O   LYS A  61      16.771  -0.084  -2.810  1.00229.88           O  
ANISOU  459  O   LYS A  61    28350  26404  32590  -2390  -3214    917       O  
ATOM    460  CB  LYS A  61      17.451  -2.504  -1.545  1.00225.52           C  
ANISOU  460  CB  LYS A  61    27719  25652  32318  -2342  -3106    912       C  
ATOM    461  CG  LYS A  61      15.935  -2.534  -1.349  1.00221.44           C  
ANISOU  461  CG  LYS A  61    26906  25054  32176  -2448  -3299   1243       C  
ATOM    462  CD  LYS A  61      15.570  -2.396   0.129  1.00209.31           C  
ANISOU  462  CD  LYS A  61    25028  23639  30862  -2311  -3032   1523       C  
ATOM    463  CE  LYS A  61      15.877  -1.000   0.667  1.00192.75           C  
ANISOU  463  CE  LYS A  61    22883  21795  28560  -2149  -2738   1541       C  
ATOM    464  NZ  LYS A  61      15.005   0.036   0.053  1.00182.32           N1+
ANISOU  464  NZ  LYS A  61    21508  20512  27252  -2217  -2872   1654       N1+
ATOM    465  N   LYS A  62      18.419  -0.225  -4.328  1.00206.09           N  
ANISOU  465  N   LYS A  62    25902  23349  29053  -2395  -3258    410       N  
ATOM    466  CA  LYS A  62      18.174   1.112  -4.852  1.00190.03           C  
ANISOU  466  CA  LYS A  62    23891  21449  26864  -2395  -3264    421       C  
ATOM    467  C   LYS A  62      17.210   1.038  -6.036  1.00192.74           C  
ANISOU  467  C   LYS A  62    24324  21636  27274  -2582  -3651    451       C  
ATOM    468  O   LYS A  62      17.256   0.094  -6.830  1.00196.14           O  
ANISOU  468  O   LYS A  62    24970  21868  27685  -2691  -3894    316       O  
ATOM    469  CB  LYS A  62      19.483   1.785  -5.259  1.00169.24           C  
ANISOU  469  CB  LYS A  62    21511  18951  23840  -2283  -3062    159       C  
ATOM    470  CG  LYS A  62      20.261   1.031  -6.307  1.00160.42           C  
ANISOU  470  CG  LYS A  62    20748  17695  22508  -2324  -3183   -115       C  
ATOM    471  CD  LYS A  62      21.464   1.823  -6.736  1.00157.91           C  
ANISOU  471  CD  LYS A  62    20649  17521  21828  -2209  -2977   -329       C  
ATOM    472  CE  LYS A  62      22.124   1.191  -7.937  1.00158.31           C  
ANISOU  472  CE  LYS A  62    21073  17431  21646  -2242  -3105   -584       C  
ATOM    473  NZ  LYS A  62      23.333   1.964  -8.321  1.00151.85           N1+
ANISOU  473  NZ  LYS A  62    20446  16757  20492  -2116  -2879   -766       N1+
ATOM    474  N   VAL A  63      16.325   2.027  -6.135  1.00181.31           N  
ANISOU  474  N   VAL A  63    22714  20268  25906  -2619  -3714    633       N  
ATOM    475  CA  VAL A  63      15.286   2.037  -7.161  1.00174.76           C  
ANISOU  475  CA  VAL A  63    21922  19300  25179  -2803  -4092    712       C  
ATOM    476  C   VAL A  63      15.063   3.446  -7.713  1.00159.40           C  
ANISOU  476  C   VAL A  63    19995  17502  23068  -2794  -4082    731       C  
ATOM    477  O   VAL A  63      16.016   4.170  -8.021  1.00159.29           O  
ANISOU  477  O   VAL A  63    20173  17625  22726  -2694  -3901    529       O  
ATOM    478  CB  VAL A  63      13.940   1.477  -6.612  1.00161.21           C  
ANISOU  478  CB  VAL A  63    19875  17460  23917  -2910  -4274   1044       C  
ATOM    479  CG1 VAL A  63      12.780   1.797  -7.562  1.00153.01           C  
ANISOU  479  CG1 VAL A  63    18813  16320  23004  -3091  -4642   1181       C  
ATOM    480  CG2 VAL A  63      14.045  -0.037  -6.335  1.00157.57           C  
ANISOU  480  CG2 VAL A  63    19431  16801  23635  -2962  -4376   1017       C  
ATOM    481  N   GLY A  70      20.759   8.076  -9.085  1.00226.28           N  
ANISOU  481  N   GLY A  70    29380  26805  29791  -2167  -2916   -258       N  
ATOM    482  CA  GLY A  70      21.583   7.106  -9.786  1.00234.13           C  
ANISOU  482  CA  GLY A  70    30667  27678  30614  -2173  -2970   -484       C  
ATOM    483  C   GLY A  70      22.618   6.458  -8.885  1.00236.34           C  
ANISOU  483  C   GLY A  70    30930  27980  30888  -2054  -2719   -563       C  
ATOM    484  O   GLY A  70      22.308   5.499  -8.175  1.00242.57           O  
ANISOU  484  O   GLY A  70    31591  28677  31897  -2078  -2745   -484       O  
ATOM    485  N   PRO A  71      23.868   6.952  -8.943  1.00225.24           N  
ANISOU  485  N   PRO A  71    29653  26690  29237  -1929  -2481   -712       N  
ATOM    486  CA  PRO A  71      24.937   6.594  -8.006  1.00210.26           C  
ANISOU  486  CA  PRO A  71    27710  24851  27326  -1803  -2212   -765       C  
ATOM    487  C   PRO A  71      25.130   7.650  -6.918  1.00197.87           C  
ANISOU  487  C   PRO A  71    25914  23474  25792  -1701  -1974   -650       C  
ATOM    488  O   PRO A  71      25.820   7.398  -5.930  1.00186.86           O  
ANISOU  488  O   PRO A  71    24430  22133  24434  -1605  -1770   -648       O  
ATOM    489  CB  PRO A  71      26.165   6.518  -8.907  1.00206.55           C  
ANISOU  489  CB  PRO A  71    27543  24374  26564  -1737  -2127   -989       C  
ATOM    490  CG  PRO A  71      25.911   7.582  -9.923  1.00208.30           C  
ANISOU  490  CG  PRO A  71    27875  24655  26613  -1769  -2219  -1012       C  
ATOM    491  CD  PRO A  71      24.406   7.643 -10.130  1.00218.76           C  
ANISOU  491  CD  PRO A  71    29084  25910  28125  -1913  -2495   -860       C  
ATOM    492  N   ASN A  72      24.530   8.822  -7.115  1.00194.03           N  
ANISOU  492  N   ASN A  72    25350  23084  25290  -1721  -2008   -557       N  
ATOM    493  CA  ASN A  72      24.600   9.911  -6.147  1.00179.67           C  
ANISOU  493  CA  ASN A  72    23337  21433  23498  -1627  -1805   -446       C  
ATOM    494  C   ASN A  72      23.315  10.055  -5.356  1.00166.39           C  
ANISOU  494  C   ASN A  72    21390  19751  22079  -1661  -1861   -210       C  
ATOM    495  O   ASN A  72      23.345  10.315  -4.156  1.00152.43           O  
ANISOU  495  O   ASN A  72    19443  18066  20406  -1569  -1682   -103       O  
ATOM    496  CB  ASN A  72      24.922  11.225  -6.846  1.00180.30           C  
ANISOU  496  CB  ASN A  72    23510  21626  23371  -1602  -1763   -501       C  
ATOM    497  CG  ASN A  72      26.392  11.369  -7.138  1.00185.32           C  
ANISOU  497  CG  ASN A  72    24326  22317  23771  -1510  -1592   -682       C  
ATOM    498  ND2 ASN A  72      26.864  10.671  -8.166  1.00185.48           N  
ANISOU  498  ND2 ASN A  72    24585  22239  23651  -1539  -1677   -836       N  
ATOM    499  OD1 ASN A  72      27.104  12.086  -6.437  1.00183.73           O  
ANISOU  499  OD1 ASN A  72    24053  22238  23517  -1410  -1386   -676       O  
ATOM    500  N   GLY A  73      22.186   9.892  -6.036  1.00172.92           N  
ANISOU  500  N   GLY A  73    22196  20483  23025  -1788  -2112   -119       N  
ATOM    501  CA  GLY A  73      20.908   9.807  -5.358  1.00176.60           C  
ANISOU  501  CA  GLY A  73    22402  20918  23781  -1830  -2187    129       C  
ATOM    502  C   GLY A  73      20.893   8.588  -4.453  1.00170.64           C  
ANISOU  502  C   GLY A  73    21537  20078  23220  -1814  -2148    185       C  
ATOM    503  O   GLY A  73      20.307   8.619  -3.371  1.00156.93           O  
ANISOU  503  O   GLY A  73    19562  18375  21688  -1763  -2051    383       O  
ATOM    504  N   ALA A  74      21.559   7.522  -4.900  1.00180.13           N  
ANISOU  504  N   ALA A  74    22923  21169  24349  -1846  -2211     14       N  
ATOM    505  CA  ALA A  74      21.649   6.264  -4.153  1.00184.52           C  
ANISOU  505  CA  ALA A  74    23404  21629  25077  -1837  -2184     43       C  
ATOM    506  C   ALA A  74      22.419   6.436  -2.850  1.00171.08           C  
ANISOU  506  C   ALA A  74    21589  20054  23360  -1680  -1880     63       C  
ATOM    507  O   ALA A  74      22.201   5.706  -1.885  1.00156.11           O  
ANISOU  507  O   ALA A  74    19533  18123  21658  -1648  -1817    179       O  
ATOM    508  CB  ALA A  74      22.301   5.179  -5.009  1.00191.33           C  
ANISOU  508  CB  ALA A  74    24526  22344  25828  -1892  -2305   -168       C  
ATOM    509  N   ILE A  75      23.334   7.396  -2.834  1.00172.05           N  
ANISOU  509  N   ILE A  75    21799  20320  23252  -1584  -1699    -47       N  
ATOM    510  CA  ILE A  75      24.023   7.762  -1.608  1.00156.41           C  
ANISOU  510  CA  ILE A  75    19718  18467  21243  -1440  -1432    -19       C  
ATOM    511  C   ILE A  75      23.130   8.713  -0.799  1.00147.23           C  
ANISOU  511  C   ILE A  75    18340  17402  20200  -1389  -1359    195       C  
ATOM    512  O   ILE A  75      22.997   8.569   0.417  1.00132.37           O  
ANISOU  512  O   ILE A  75    16296  15559  18441  -1300  -1215    324       O  
ATOM    513  CB  ILE A  75      25.401   8.401  -1.906  1.00146.72           C  
ANISOU  513  CB  ILE A  75    18670  17341  19738  -1362  -1281   -213       C  
ATOM    514  CG1 ILE A  75      26.331   7.373  -2.564  1.00144.06           C  
ANISOU  514  CG1 ILE A  75    18535  16905  19296  -1382  -1309   -403       C  
ATOM    515  CG2 ILE A  75      26.034   8.949  -0.640  1.00131.92           C  
ANISOU  515  CG2 ILE A  75    16690  15598  17835  -1224  -1037   -170       C  
ATOM    516  CD1 ILE A  75      27.750   7.854  -2.758  1.00149.57           C  
ANISOU  516  CD1 ILE A  75    19381  17692  19757  -1293  -1138   -564       C  
ATOM    517  N   VAL A  76      22.494   9.661  -1.485  1.00143.79           N  
ANISOU  517  N   VAL A  76    17907  16999  19728  -1440  -1457    240       N  
ATOM    518  CA  VAL A  76      21.585  10.603  -0.835  1.00155.56           C  
ANISOU  518  CA  VAL A  76    19205  18570  21332  -1390  -1391    450       C  
ATOM    519  C   VAL A  76      20.535   9.894   0.009  1.00161.71           C  
ANISOU  519  C   VAL A  76    19753  19280  22409  -1391  -1412    686       C  
ATOM    520  O   VAL A  76      20.444  10.119   1.216  1.00164.41           O  
ANISOU  520  O   VAL A  76    19954  19693  22821  -1267  -1220    815       O  
ATOM    521  CB  VAL A  76      20.850  11.496  -1.860  1.00170.31           C  
ANISOU  521  CB  VAL A  76    21096  20445  23168  -1476  -1548    489       C  
ATOM    522  CG1 VAL A  76      19.714  12.254  -1.182  1.00168.96           C  
ANISOU  522  CG1 VAL A  76    20699  20325  23175  -1431  -1497    746       C  
ATOM    523  CG2 VAL A  76      21.813  12.462  -2.529  1.00176.53           C  
ANISOU  523  CG2 VAL A  76    22074  21328  23670  -1446  -1484    300       C  
ATOM    524  N   THR A  77      19.759   9.028  -0.637  1.00150.72           N  
ANISOU  524  N   THR A  77    18332  17744  21191  -1529  -1649    745       N  
ATOM    525  CA  THR A  77      18.642   8.356   0.010  1.00164.38           C  
ANISOU  525  CA  THR A  77    19825  19392  23242  -1552  -1704    999       C  
ATOM    526  C   THR A  77      19.050   7.611   1.275  1.00159.29           C  
ANISOU  526  C   THR A  77    19084  18756  22682  -1440  -1513   1047       C  
ATOM    527  O   THR A  77      18.315   7.605   2.264  1.00156.29           O  
ANISOU  527  O   THR A  77    18484  18395  22505  -1365  -1411   1284       O  
ATOM    528  CB  THR A  77      17.956   7.358  -0.944  1.00170.53           C  
ANISOU  528  CB  THR A  77    20624  19986  24183  -1735  -2020   1017       C  
ATOM    529  CG2 THR A  77      18.980   6.487  -1.644  1.00176.90           C  
ANISOU  529  CG2 THR A  77    21685  20708  24820  -1789  -2100    745       C  
ATOM    530  OG1 THR A  77      17.079   6.513  -0.193  1.00174.95           O  
ANISOU  530  OG1 THR A  77    20950  20456  25069  -1749  -2053   1255       O  
ATOM    531  N   SER A  78      20.222   6.985   1.238  1.00147.73           N  
ANISOU  531  N   SER A  78    17785  17281  21066  -1421  -1458    832       N  
ATOM    532  CA  SER A  78      20.702   6.205   2.370  1.00142.65           C  
ANISOU  532  CA  SER A  78    17067  16641  20492  -1323  -1291    861       C  
ATOM    533  C   SER A  78      20.767   7.096   3.604  1.00142.10           C  
ANISOU  533  C   SER A  78    16885  16722  20383  -1151  -1032    977       C  
ATOM    534  O   SER A  78      20.323   6.715   4.689  1.00123.11           O  
ANISOU  534  O   SER A  78    14305  14320  18153  -1068   -920   1165       O  
ATOM    535  CB  SER A  78      22.076   5.596   2.071  1.00151.30           C  
ANISOU  535  CB  SER A  78    18375  17719  21394  -1317  -1252    601       C  
ATOM    536  OG  SER A  78      22.113   4.975   0.795  1.00157.41           O  
ANISOU  536  OG  SER A  78    19313  18359  22135  -1458  -1480    458       O  
ATOM    537  N   LEU A  79      21.311   8.293   3.416  1.00143.47           N  
ANISOU  537  N   LEU A  79    17171  17015  20325  -1096   -942    868       N  
ATOM    538  CA  LEU A  79      21.389   9.271   4.485  1.00143.57           C  
ANISOU  538  CA  LEU A  79    17119  17160  20270   -937   -719    956       C  
ATOM    539  C   LEU A  79      20.006   9.539   5.048  1.00141.74           C  
ANISOU  539  C   LEU A  79    16666  16923  20266   -898   -698   1247       C  
ATOM    540  O   LEU A  79      19.804   9.531   6.263  1.00140.76           O  
ANISOU  540  O   LEU A  79    16424  16841  20216   -760   -518   1399       O  
ATOM    541  CB  LEU A  79      22.011  10.568   3.979  1.00156.23           C  
ANISOU  541  CB  LEU A  79    18874  18867  21619   -915   -678    808       C  
ATOM    542  CG  LEU A  79      22.594  11.456   5.078  1.00161.11           C  
ANISOU  542  CG  LEU A  79    19507  19611  22098   -749   -447    809       C  
ATOM    543  CD1 LEU A  79      23.844  10.805   5.660  1.00143.68           C  
ANISOU  543  CD1 LEU A  79    17385  17418  19788   -692   -343    670       C  
ATOM    544  CD2 LEU A  79      22.882  12.869   4.569  1.00158.51           C  
ANISOU  544  CD2 LEU A  79    19286  19369  21573   -736   -429    720       C  
ATOM    545  N   ASN A  80      19.057   9.763   4.145  1.00147.89           N  
ANISOU  545  N   ASN A  80    17392  17644  21157  -1015   -883   1334       N  
ATOM    546  CA  ASN A  80      17.683  10.036   4.532  1.00145.08           C  
ANISOU  546  CA  ASN A  80    16810  17271  21042   -991   -881   1633       C  
ATOM    547  C   ASN A  80      17.144   8.981   5.476  1.00133.24           C  
ANISOU  547  C   ASN A  80    15118  15705  19803   -945   -827   1840       C  
ATOM    548  O   ASN A  80      16.696   9.305   6.578  1.00133.37           O  
ANISOU  548  O   ASN A  80    14995  15779  19901   -792   -628   2041       O  
ATOM    549  CB  ASN A  80      16.794  10.136   3.298  1.00145.88           C  
ANISOU  549  CB  ASN A  80    16881  17289  21256  -1161  -1144   1690       C  
ATOM    550  CG  ASN A  80      17.190  11.277   2.397  1.00153.47           C  
ANISOU  550  CG  ASN A  80    18010  18324  21975  -1193  -1185   1525       C  
ATOM    551  ND2 ASN A  80      16.614  12.450   2.640  1.00161.33           N  
ANISOU  551  ND2 ASN A  80    18925  19402  22971  -1115  -1087   1664       N  
ATOM    552  OD1 ASN A  80      18.011  11.113   1.497  1.00148.44           O  
ANISOU  552  OD1 ASN A  80    17576  17669  21154  -1278  -1292   1281       O  
ATOM    553  N   LEU A  81      17.208   7.723   5.042  1.00140.71           N  
ANISOU  553  N   LEU A  81    16069  16525  20871  -1070   -997   1790       N  
ATOM    554  CA  LEU A  81      16.749   6.599   5.849  1.00148.12           C  
ANISOU  554  CA  LEU A  81    16825  17382  22071  -1045   -968   1978       C  
ATOM    555  C   LEU A  81      17.388   6.624   7.225  1.00149.71           C  
ANISOU  555  C   LEU A  81    17013  17685  22184   -847   -679   1994       C  
ATOM    556  O   LEU A  81      16.725   6.411   8.236  1.00151.14           O  
ANISOU  556  O   LEU A  81    17003  17871  22554   -737   -544   2245       O  
ATOM    557  CB  LEU A  81      17.058   5.263   5.163  1.00169.90           C  
ANISOU  557  CB  LEU A  81    19656  19990  24906  -1199  -1180   1847       C  
ATOM    558  CG  LEU A  81      16.025   4.676   4.195  1.00182.20           C  
ANISOU  558  CG  LEU A  81    21132  21383  26711  -1393  -1492   1956       C  
ATOM    559  CD1 LEU A  81      16.145   3.153   4.123  1.00177.94           C  
ANISOU  559  CD1 LEU A  81    20588  20683  26338  -1486  -1630   1927       C  
ATOM    560  CD2 LEU A  81      14.613   5.087   4.582  1.00185.46           C  
ANISOU  560  CD2 LEU A  81    21271  21791  27405  -1372  -1493   2308       C  
ATOM    561  N   PHE A  82      18.684   6.898   7.259  1.00151.51           N  
ANISOU  561  N   PHE A  82    17450  17994  22125   -799   -585   1735       N  
ATOM    562  CA  PHE A  82      19.408   6.915   8.514  1.00132.07           C  
ANISOU  562  CA  PHE A  82    15004  15622  19553   -624   -339   1725       C  
ATOM    563  C   PHE A  82      18.887   8.034   9.407  1.00125.25           C  
ANISOU  563  C   PHE A  82    14067  14866  18657   -455   -140   1899       C  
ATOM    564  O   PHE A  82      18.535   7.816  10.565  1.00122.59           O  
ANISOU  564  O   PHE A  82    13606  14550  18421   -312     31   2091       O  
ATOM    565  CB  PHE A  82      20.907   7.084   8.265  1.00135.41           C  
ANISOU  565  CB  PHE A  82    15662  16105  19682   -621   -303   1420       C  
ATOM    566  CG  PHE A  82      21.744   6.832   9.476  1.00126.64           C  
ANISOU  566  CG  PHE A  82    14574  15061  18481   -474   -100   1397       C  
ATOM    567  CD1 PHE A  82      22.309   5.589   9.691  1.00131.48           C  
ANISOU  567  CD1 PHE A  82    15187  15610  19159   -499   -110   1341       C  
ATOM    568  CD2 PHE A  82      21.945   7.825  10.416  1.00121.11           C  
ANISOU  568  CD2 PHE A  82    13902  14481  17634   -309     95   1437       C  
ATOM    569  CE1 PHE A  82      23.072   5.347  10.811  1.00127.14           C  
ANISOU  569  CE1 PHE A  82    14654  15122  18530   -366     68   1331       C  
ATOM    570  CE2 PHE A  82      22.710   7.589  11.542  1.00121.02           C  
ANISOU  570  CE2 PHE A  82    13925  14526  17532   -176    263   1418       C  
ATOM    571  CZ  PHE A  82      23.272   6.351  11.739  1.00117.89           C  
ANISOU  571  CZ  PHE A  82    13516  14072  17204   -206    249   1370       C  
ATOM    572  N   SER A  83      18.821   9.233   8.847  1.00124.06           N  
ANISOU  572  N   SER A  83    13999  14776  18362   -464   -159   1837       N  
ATOM    573  CA  SER A  83      18.479  10.424   9.611  1.00133.24           C  
ANISOU  573  CA  SER A  83    15143  16038  19445   -298     32   1958       C  
ATOM    574  C   SER A  83      17.153  10.331  10.363  1.00138.98           C  
ANISOU  574  C   SER A  83    15635  16739  20433   -200    130   2304       C  
ATOM    575  O   SER A  83      16.868  11.165  11.212  1.00146.92           O  
ANISOU  575  O   SER A  83    16626  17818  21379    -24    330   2428       O  
ATOM    576  CB  SER A  83      18.449  11.635   8.682  1.00146.36           C  
ANISOU  576  CB  SER A  83    16906  17742  20962   -357    -46   1858       C  
ATOM    577  OG  SER A  83      17.757  11.322   7.490  1.00154.18           O  
ANISOU  577  OG  SER A  83    17832  18644  22106   -539   -283   1890       O  
ATOM    578  N   THR A  84      16.342   9.325  10.061  1.00133.96           N  
ANISOU  578  N   THR A  84    14819  15992  20090   -306     -9   2469       N  
ATOM    579  CA  THR A  84      15.051   9.194  10.728  1.00149.45           C  
ANISOU  579  CA  THR A  84    16529  17920  22336   -218     80   2830       C  
ATOM    580  C   THR A  84      15.161   8.484  12.081  1.00158.28           C  
ANISOU  580  C   THR A  84    17566  19051  23521    -52    288   2965       C  
ATOM    581  O   THR A  84      14.546   8.909  13.063  1.00140.81           O  
ANISOU  581  O   THR A  84    15252  16885  21366    137    505   3201       O  
ATOM    582  CB  THR A  84      14.038   8.452   9.838  1.00148.00           C  
ANISOU  582  CB  THR A  84    16161  17599  22474   -409   -176   2988       C  
ATOM    583  CG2 THR A  84      13.092   9.448   9.180  1.00136.30           C  
ANISOU  583  CG2 THR A  84    14603  16121  21063   -452   -252   3125       C  
ATOM    584  OG1 THR A  84      14.736   7.732   8.816  1.00156.19           O  
ANISOU  584  OG1 THR A  84    17336  18561  23447   -605   -414   2728       O  
ATOM    585  N   LYS A  85      15.950   7.413  12.142  1.00164.55           N  
ANISOU  585  N   LYS A  85    18415  19805  24302   -112    233   2819       N  
ATOM    586  CA  LYS A  85      16.185   6.714  13.407  1.00161.29           C  
ANISOU  586  CA  LYS A  85    17944  19410  23929     41    425   2923       C  
ATOM    587  C   LYS A  85      17.219   7.466  14.251  1.00140.54           C  
ANISOU  587  C   LYS A  85    15522  16912  20966    215    635   2760       C  
ATOM    588  O   LYS A  85      17.776   6.911  15.197  1.00124.72           O  
ANISOU  588  O   LYS A  85    13541  14934  18912    325    769   2757       O  
ATOM    589  CB  LYS A  85      16.649   5.262  13.162  1.00167.95           C  
ANISOU  589  CB  LYS A  85    18766  20154  24894    -88    287   2834       C  
ATOM    590  CG  LYS A  85      15.534   4.196  13.110  1.00173.58           C  
ANISOU  590  CG  LYS A  85    19213  20731  26007   -168    178   3114       C  
ATOM    591  CD  LYS A  85      16.111   2.786  12.888  1.00176.34           C  
ANISOU  591  CD  LYS A  85    19575  20976  26449   -289     45   2995       C  
ATOM    592  CE  LYS A  85      15.033   1.701  12.862  1.00173.80           C  
ANISOU  592  CE  LYS A  85    18991  20506  26540   -374    -77   3275       C  
ATOM    593  NZ  LYS A  85      15.585   0.326  12.626  1.00171.94           N1+
ANISOU  593  NZ  LYS A  85    18780  20152  26397   -493   -213   3154       N1+
ATOM    594  N   ILE A  86      17.453   8.734  13.916  1.00147.44           N  
ANISOU  594  N   ILE A  86    16542  17860  21618    238    653   2634       N  
ATOM    595  CA  ILE A  86      18.517   9.519  14.536  1.00144.72           C  
ANISOU  595  CA  ILE A  86    16418  17622  20947    367    798   2446       C  
ATOM    596  C   ILE A  86      18.401   9.609  16.062  1.00148.55           C  
ANISOU  596  C   ILE A  86    16889  18162  21390    614   1059   2615       C  
ATOM    597  O   ILE A  86      19.403   9.489  16.768  1.00145.07           O  
ANISOU  597  O   ILE A  86    16589  17772  20758    696   1146   2479       O  
ATOM    598  CB  ILE A  86      18.570  10.950  13.943  1.00146.33           C  
ANISOU  598  CB  ILE A  86    16754  17883  20963    359    776   2334       C  
ATOM    599  CG1 ILE A  86      19.790  11.705  14.475  1.00137.87           C  
ANISOU  599  CG1 ILE A  86    15921  16903  19562    460    880   2114       C  
ATOM    600  CG2 ILE A  86      17.283  11.721  14.233  1.00142.82           C  
ANISOU  600  CG2 ILE A  86    16179  17444  20641    472    885   2608       C  
ATOM    601  CD1 ILE A  86      21.097  10.948  14.322  1.00126.04           C  
ANISOU  601  CD1 ILE A  86    14536  15402  17952    373    803   1874       C  
ATOM    602  N   ASP A  87      17.188   9.795  16.573  1.00146.83           N  
ANISOU  602  N   ASP A  87    16505  17932  21354    735   1184   2921       N  
ATOM    603  CA  ASP A  87      16.995   9.940  18.007  1.00143.39           C  
ANISOU  603  CA  ASP A  87    16072  17546  20865    993   1451   3100       C  
ATOM    604  C   ASP A  87      17.384   8.655  18.725  1.00131.49           C  
ANISOU  604  C   ASP A  87    14502  16016  19441   1024   1495   3141       C  
ATOM    605  O   ASP A  87      17.853   8.686  19.862  1.00127.12           O  
ANISOU  605  O   ASP A  87    14051  15520  18729   1208   1677   3149       O  
ATOM    606  CB  ASP A  87      15.547  10.327  18.321  1.00152.34           C  
ANISOU  606  CB  ASP A  87    17014  18659  22209   1119   1584   3451       C  
ATOM    607  CG  ASP A  87      15.361  11.826  18.436  1.00162.53           C  
ANISOU  607  CG  ASP A  87    18443  20011  23300   1247   1700   3439       C  
ATOM    608  OD1 ASP A  87      16.224  12.480  19.058  1.00167.38           O  
ANISOU  608  OD1 ASP A  87    19297  20694  23606   1371   1806   3264       O  
ATOM    609  OD2 ASP A  87      14.363  12.353  17.902  1.00168.46           O1-
ANISOU  609  OD2 ASP A  87    19066  20735  24207   1222   1677   3607       O1-
ATOM    610  N   GLN A  88      17.206   7.526  18.048  1.00126.35           N  
ANISOU  610  N   GLN A  88    13697  15276  19035    841   1319   3161       N  
ATOM    611  CA  GLN A  88      17.577   6.236  18.614  1.00141.98           C  
ANISOU  611  CA  GLN A  88    15605  17220  21119    847   1341   3194       C  
ATOM    612  C   GLN A  88      19.097   6.140  18.683  1.00148.64           C  
ANISOU  612  C   GLN A  88    16677  18114  21684    818   1310   2874       C  
ATOM    613  O   GLN A  88      19.658   5.690  19.684  1.00141.66           O  
ANISOU  613  O   GLN A  88    15837  17266  20720    942   1441   2882       O  
ATOM    614  CB  GLN A  88      16.990   5.091  17.783  1.00155.28           C  
ANISOU  614  CB  GLN A  88    17082  18776  23140    646   1136   3285       C  
ATOM    615  CG  GLN A  88      17.032   3.726  18.461  1.00180.28           C  
ANISOU  615  CG  GLN A  88    20113  21888  26496    673   1181   3412       C  
ATOM    616  CD  GLN A  88      16.161   2.693  17.759  1.00190.61           C  
ANISOU  616  CD  GLN A  88    21185  23052  28187    498    990   3577       C  
ATOM    617  NE2 GLN A  88      16.121   1.481  18.307  1.00191.70           N  
ANISOU  617  NE2 GLN A  88    21186  23128  28523    513   1018   3706       N  
ATOM    618  OE1 GLN A  88      15.531   2.982  16.741  1.00190.31           O  
ANISOU  618  OE1 GLN A  88    21090  22953  28267    349    809   3591       O  
ATOM    619  N   VAL A  89      19.751   6.586  17.612  1.00146.65           N  
ANISOU  619  N   VAL A  89    16565  17864  21290    657   1140   2607       N  
ATOM    620  CA  VAL A  89      21.211   6.592  17.523  1.00123.99           C  
ANISOU  620  CA  VAL A  89    13904  15038  18168    615   1098   2307       C  
ATOM    621  C   VAL A  89      21.811   7.383  18.667  1.00112.12           C  
ANISOU  621  C   VAL A  89    12564  13638  16400    817   1286   2274       C  
ATOM    622  O   VAL A  89      22.694   6.903  19.369  1.00128.11           O  
ANISOU  622  O   VAL A  89    14665  15691  18321    876   1344   2199       O  
ATOM    623  CB  VAL A  89      21.691   7.182  16.184  1.00111.78           C  
ANISOU  623  CB  VAL A  89    12482  13485  16503    438    913   2061       C  
ATOM    624  CG1 VAL A  89      23.180   7.508  16.240  1.00112.78           C  
ANISOU  624  CG1 VAL A  89    12827  13675  16347    438    915   1788       C  
ATOM    625  CG2 VAL A  89      21.409   6.207  15.047  1.00108.73           C  
ANISOU  625  CG2 VAL A  89    11994  12986  16332    228    702   2033       C  
ATOM    626  N   ILE A  90      21.309   8.595  18.852  1.00115.92           N  
ANISOU  626  N   ILE A  90    13103  14165  16774    924   1373   2336       N  
ATOM    627  CA  ILE A  90      21.725   9.452  19.946  1.00109.36           C  
ANISOU  627  CA  ILE A  90    12448  13415  15688   1129   1545   2320       C  
ATOM    628  C   ILE A  90      21.521   8.801  21.315  1.00119.60           C  
ANISOU  628  C   ILE A  90    13692  14726  17025   1324   1735   2518       C  
ATOM    629  O   ILE A  90      22.371   8.931  22.195  1.00118.11           O  
ANISOU  629  O   ILE A  90    13668  14589  16620   1439   1816   2430       O  
ATOM    630  CB  ILE A  90      20.973  10.784  19.898  1.00111.32           C  
ANISOU  630  CB  ILE A  90    12742  13689  15864   1221   1619   2400       C  
ATOM    631  CG1 ILE A  90      21.162  11.444  18.524  1.00108.35           C  
ANISOU  631  CG1 ILE A  90    12414  13303  15449   1030   1431   2213       C  
ATOM    632  CG2 ILE A  90      21.443  11.697  21.020  1.00121.04           C  
ANISOU  632  CG2 ILE A  90    14193  14987  16809   1435   1782   2362       C  
ATOM    633  CD1 ILE A  90      22.616  11.716  18.162  1.00116.67           C  
ANISOU  633  CD1 ILE A  90    13671  14392  16266    936   1324   1900       C  
ATOM    634  N   ARG A  91      20.404   8.099  21.497  1.00121.31           N  
ANISOU  634  N   ARG A  91    13679  14892  17522   1360   1799   2795       N  
ATOM    635  CA  ARG A  91      20.181   7.366  22.744  1.00129.85           C  
ANISOU  635  CA  ARG A  91    14687  15982  18669   1541   1981   3004       C  
ATOM    636  C   ARG A  91      21.308   6.365  22.973  1.00130.79           C  
ANISOU  636  C   ARG A  91    14850  16100  18742   1476   1920   2851       C  
ATOM    637  O   ARG A  91      21.841   6.242  24.080  1.00122.41           O  
ANISOU  637  O   ARG A  91    13892  15089  17528   1635   2052   2863       O  
ATOM    638  CB  ARG A  91      18.833   6.642  22.731  1.00123.82           C  
ANISOU  638  CB  ARG A  91    13630  15148  18266   1552   2028   3333       C  
ATOM    639  CG  ARG A  91      17.726   7.388  23.470  1.00145.51           C  
ANISOU  639  CG  ARG A  91    16329  17919  21039   1783   2252   3618       C  
ATOM    640  CD  ARG A  91      16.409   6.610  23.476  1.00141.95           C  
ANISOU  640  CD  ARG A  91    15560  17394  20982   1792   2298   3976       C  
ATOM    641  NE  ARG A  91      15.746   6.648  22.176  1.00147.56           N  
ANISOU  641  NE  ARG A  91    16115  18032  21921   1573   2091   3993       N  
ATOM    642  CZ  ARG A  91      14.900   7.603  21.795  1.00157.07           C  
ANISOU  642  CZ  ARG A  91    17278  19236  23166   1601   2116   4108       C  
ATOM    643  NH1 ARG A  91      14.607   8.606  22.617  1.00152.50           N1+
ANISOU  643  NH1 ARG A  91    16808  18721  22414   1845   2351   4215       N1+
ATOM    644  NH2 ARG A  91      14.347   7.557  20.589  1.00159.55           N  
ANISOU  644  NH2 ARG A  91    17453  19480  23688   1386   1902   4118       N  
ATOM    645  N   LEU A  92      21.675   5.665  21.906  1.00120.79           N  
ANISOU  645  N   LEU A  92    13517  14774  17602   1245   1717   2706       N  
ATOM    646  CA  LEU A  92      22.704   4.640  21.962  1.00119.51           C  
ANISOU  646  CA  LEU A  92    13378  14597  17434   1165   1649   2567       C  
ATOM    647  C   LEU A  92      24.048   5.241  22.385  1.00122.41           C  
ANISOU  647  C   LEU A  92    13994  15044  17471   1215   1665   2332       C  
ATOM    648  O   LEU A  92      24.675   4.758  23.330  1.00122.91           O  
ANISOU  648  O   LEU A  92    14106  15140  17455   1316   1751   2342       O  
ATOM    649  CB  LEU A  92      22.800   3.943  20.602  1.00123.22           C  
ANISOU  649  CB  LEU A  92    13766  14977  18077    913   1426   2440       C  
ATOM    650  CG  LEU A  92      23.665   2.705  20.387  1.00127.34           C  
ANISOU  650  CG  LEU A  92    14271  15446  18666    798   1335   2318       C  
ATOM    651  CD1 LEU A  92      23.773   1.877  21.654  1.00133.59           C  
ANISOU  651  CD1 LEU A  92    14992  16254  19512    947   1489   2476       C  
ATOM    652  CD2 LEU A  92      23.061   1.880  19.247  1.00124.69           C  
ANISOU  652  CD2 LEU A  92    13785  14985  18606    600   1152   2339       C  
ATOM    653  N   VAL A  93      24.468   6.307  21.703  1.00127.34           N  
ANISOU  653  N   VAL A  93    14772  15698  17914   1146   1577   2137       N  
ATOM    654  CA  VAL A  93      25.731   6.987  22.013  1.00125.86           C  
ANISOU  654  CA  VAL A  93    14815  15576  17430   1176   1566   1920       C  
ATOM    655  C   VAL A  93      25.708   7.628  23.399  1.00124.83           C  
ANISOU  655  C   VAL A  93    14816  15509  17105   1415   1742   2017       C  
ATOM    656  O   VAL A  93      26.731   7.676  24.089  1.00117.24           O  
ANISOU  656  O   VAL A  93    14006  14589  15953   1474   1755   1910       O  
ATOM    657  CB  VAL A  93      26.067   8.075  20.964  1.00104.12           C  
ANISOU  657  CB  VAL A  93    12183  12834  14543   1056   1440   1719       C  
ATOM    658  CG1 VAL A  93      27.325   8.864  21.356  1.00105.92           C  
ANISOU  658  CG1 VAL A  93    12640  13122  14482   1096   1427   1523       C  
ATOM    659  CG2 VAL A  93      26.249   7.463  19.592  1.00104.06           C  
ANISOU  659  CG2 VAL A  93    12094  12765  14679    830   1264   1596       C  
ATOM    660  N   GLU A  94      24.541   8.117  23.811  1.00125.06           N  
ANISOU  660  N   GLU A  94    14795  15541  17183   1559   1876   2226       N  
ATOM    661  CA  GLU A  94      24.432   8.762  25.113  1.00128.49           C  
ANISOU  661  CA  GLU A  94    15380  16025  17417   1808   2058   2325       C  
ATOM    662  C   GLU A  94      24.621   7.732  26.223  1.00137.12           C  
ANISOU  662  C   GLU A  94    16429  17128  18541   1933   2172   2455       C  
ATOM    663  O   GLU A  94      25.240   8.018  27.247  1.00131.57           O  
ANISOU  663  O   GLU A  94    15915  16470  17605   2082   2248   2419       O  
ATOM    664  CB  GLU A  94      23.090   9.481  25.259  1.00137.52           C  
ANISOU  664  CB  GLU A  94    16468  17160  18622   1946   2198   2540       C  
ATOM    665  CG  GLU A  94      23.156  10.736  26.128  1.00144.35           C  
ANISOU  665  CG  GLU A  94    17587  18068  19191   2160   2327   2526       C  
ATOM    666  CD  GLU A  94      22.370  11.891  25.540  1.00153.71           C  
ANISOU  666  CD  GLU A  94    18789  19242  20370   2169   2341   2555       C  
ATOM    667  OE1 GLU A  94      21.492  11.638  24.686  1.00153.09           O  
ANISOU  667  OE1 GLU A  94    18491  19127  20550   2059   2299   2671       O  
ATOM    668  OE2 GLU A  94      22.635  13.052  25.925  1.00159.16           O1-
ANISOU  668  OE2 GLU A  94    19717  19955  20803   2282   2384   2462       O1-
ATOM    669  N   GLN A  95      24.106   6.526  26.007  1.00142.05           N  
ANISOU  669  N   GLN A  95    16812  17705  19455   1865   2171   2603       N  
ATOM    670  CA  GLN A  95      24.283   5.443  26.971  1.00144.16           C  
ANISOU  670  CA  GLN A  95    17011  17978  19786   1965   2271   2734       C  
ATOM    671  C   GLN A  95      25.764   5.086  27.126  1.00125.13           C  
ANISOU  671  C   GLN A  95    14735  15593  17214   1892   2170   2508       C  
ATOM    672  O   GLN A  95      26.215   4.608  28.174  1.00123.90           O  
ANISOU  672  O   GLN A  95    14631  15469  16975   2018   2259   2565       O  
ATOM    673  CB  GLN A  95      23.483   4.215  26.544  1.00139.23           C  
ANISOU  673  CB  GLN A  95    16092  17280  19530   1872   2253   2920       C  
ATOM    674  CG  GLN A  95      22.833   3.489  27.693  1.00156.40           C  
ANISOU  674  CG  GLN A  95    18141  19456  21827   2069   2453   3216       C  
ATOM    675  CD  GLN A  95      22.184   2.206  27.245  1.00183.39           C  
ANISOU  675  CD  GLN A  95    21267  22789  25625   1952   2405   3384       C  
ATOM    676  NE2 GLN A  95      21.351   1.624  28.104  1.00195.99           N  
ANISOU  676  NE2 GLN A  95    22702  24374  27391   2116   2583   3695       N  
ATOM    677  OE1 GLN A  95      22.425   1.741  26.132  1.00189.14           O  
ANISOU  677  OE1 GLN A  95    21920  23453  26492   1718   2207   3240       O  
ATOM    678  N   LYS A  96      26.531   5.343  26.079  1.00101.57           N  
ANISOU  678  N   LYS A  96    11810  12597  14185   1693   1986   2262       N  
ATOM    679  CA  LYS A  96      27.928   4.984  26.102  1.00113.31           C  
ANISOU  679  CA  LYS A  96    13396  14101  15556   1609   1887   2065       C  
ATOM    680  C   LYS A  96      28.809   6.231  26.246  1.00128.75           C  
ANISOU  680  C   LYS A  96    15608  16108  17203   1634   1833   1870       C  
ATOM    681  O   LYS A  96      29.993   6.201  25.911  1.00135.63           O  
ANISOU  681  O   LYS A  96    16561  16987  17986   1520   1710   1677       O  
ATOM    682  CB  LYS A  96      28.264   4.176  24.835  1.00125.62           C  
ANISOU  682  CB  LYS A  96    14825  15597  17308   1371   1727   1941       C  
ATOM    683  CG  LYS A  96      27.524   2.810  24.753  1.00120.34           C  
ANISOU  683  CG  LYS A  96    13913  14858  16953   1335   1754   2124       C  
ATOM    684  CD  LYS A  96      27.675   2.119  23.386  1.00121.81           C  
ANISOU  684  CD  LYS A  96    13999  14960  17324   1102   1584   1999       C  
ATOM    685  CE  LYS A  96      27.214   0.648  23.405  1.00122.91           C  
ANISOU  685  CE  LYS A  96    13925  15015  17758   1059   1588   2151       C  
ATOM    686  NZ  LYS A  96      27.024   0.085  22.022  1.00109.19           N1+
ANISOU  686  NZ  LYS A  96    12101  13174  16213    845   1417   2059       N1+
ATOM    687  N   LYS A  97      28.242   7.312  26.788  1.00126.36           N  
ANISOU  687  N   LYS A  97    15434  15834  16742   1792   1929   1935       N  
ATOM    688  CA  LYS A  97      28.917   8.618  26.786  1.00123.66           C  
ANISOU  688  CA  LYS A  97    15335  15522  16130   1802   1859   1754       C  
ATOM    689  C   LYS A  97      29.986   8.813  27.865  1.00136.64           C  
ANISOU  689  C   LYS A  97    17190  17202  17525   1905   1854   1678       C  
ATOM    690  O   LYS A  97      30.709   9.812  27.854  1.00136.05           O  
ANISOU  690  O   LYS A  97    17316  17139  17239   1889   1762   1516       O  
ATOM    691  CB  LYS A  97      27.889   9.741  26.907  1.00116.75           C  
ANISOU  691  CB  LYS A  97    14532  14649  15180   1932   1959   1846       C  
ATOM    692  CG  LYS A  97      27.433  10.081  28.324  1.00131.31           C  
ANISOU  692  CG  LYS A  97    16513  16516  16861   2208   2149   2008       C  
ATOM    693  CD  LYS A  97      26.383  11.207  28.279  1.00132.93           C  
ANISOU  693  CD  LYS A  97    16780  16713  17016   2328   2253   2098       C  
ATOM    694  CE  LYS A  97      25.597  11.337  29.578  1.00135.59           C  
ANISOU  694  CE  LYS A  97    17196  17061  17262   2621   2490   2326       C  
ATOM    695  NZ  LYS A  97      24.261  11.975  29.355  1.00127.59           N1+
ANISOU  695  NZ  LYS A  97    16110  16026  16341   2722   2627   2503       N1+
ATOM    696  N   ASP A  98      30.097   7.873  28.794  1.00129.77           N  
ANISOU  696  N   ASP A  98    16277  16345  16685   2006   1940   1800       N  
ATOM    697  CA  ASP A  98      31.111   7.993  29.829  1.00133.82           C  
ANISOU  697  CA  ASP A  98    16988  16889  16967   2098   1918   1738       C  
ATOM    698  C   ASP A  98      32.113   6.854  29.720  1.00144.56           C  
ANISOU  698  C   ASP A  98    18242  18249  18434   1971   1829   1681       C  
ATOM    699  O   ASP A  98      33.087   6.802  30.468  1.00150.66           O  
ANISOU  699  O   ASP A  98    19148  19045  19053   2010   1781   1627       O  
ATOM    700  CB  ASP A  98      30.468   8.025  31.217  1.00141.95           C  
ANISOU  700  CB  ASP A  98    18118  17941  17876   2368   2107   1935       C  
ATOM    701  CG  ASP A  98      29.825   9.367  31.533  1.00152.59           C  
ANISOU  701  CG  ASP A  98    19665  19287  19024   2523   2184   1950       C  
ATOM    702  OD1 ASP A  98      30.519  10.402  31.408  1.00155.28           O  
ANISOU  702  OD1 ASP A  98    20217  19623  19157   2483   2060   1765       O  
ATOM    703  OD2 ASP A  98      28.627   9.388  31.899  1.00145.19           O1-
ANISOU  703  OD2 ASP A  98    18670  18347  18148   2688   2372   2157       O1-
ATOM    704  N   LYS A  99      31.867   5.945  28.779  1.00147.84           N  
ANISOU  704  N   LYS A  99    18426  18629  19116   1819   1802   1695       N  
ATOM    705  CA  LYS A  99      32.788   4.846  28.503  1.00145.74           C  
ANISOU  705  CA  LYS A  99    18052  18349  18974   1687   1722   1633       C  
ATOM    706  C   LYS A  99      33.864   5.298  27.522  1.00136.91           C  
ANISOU  706  C   LYS A  99    16996  17221  17802   1502   1549   1401       C  
ATOM    707  O   LYS A  99      35.041   4.997  27.698  1.00133.85           O  
ANISOU  707  O   LYS A  99    16650  16843  17363   1450   1471   1315       O  
ATOM    708  CB  LYS A  99      32.038   3.623  27.950  1.00149.66           C  
ANISOU  708  CB  LYS A  99    18290  18795  19780   1615   1767   1753       C  
ATOM    709  CG  LYS A  99      31.670   2.570  28.999  1.00163.15           C  
ANISOU  709  CG  LYS A  99    19892  20508  21589   1753   1905   1966       C  
ATOM    710  CD  LYS A  99      30.637   1.559  28.478  1.00175.04           C  
ANISOU  710  CD  LYS A  99    21142  21951  23415   1698   1953   2120       C  
ATOM    711  CE  LYS A  99      31.229   0.563  27.479  1.00174.92           C  
ANISOU  711  CE  LYS A  99    20998  21871  23592   1490   1830   2005       C  
ATOM    712  NZ  LYS A  99      30.186  -0.362  26.933  1.00177.46           N1+
ANISOU  712  NZ  LYS A  99    21090  22111  24225   1425   1846   2147       N1+
ATOM    713  N   PHE A 100      33.451   6.031  26.492  1.00122.55           N  
ANISOU  713  N   PHE A 100    15176  15383  16003   1408   1493   1317       N  
ATOM    714  CA  PHE A 100      34.377   6.506  25.467  1.00118.97           C  
ANISOU  714  CA  PHE A 100    14774  14921  15510   1239   1344   1112       C  
ATOM    715  C   PHE A 100      34.627   8.000  25.575  1.00124.13           C  
ANISOU  715  C   PHE A 100    15632  15600  15932   1275   1289   1013       C  
ATOM    716  O   PHE A 100      33.704   8.789  25.823  1.00122.32           O  
ANISOU  716  O   PHE A 100    15468  15378  15630   1379   1357   1078       O  
ATOM    717  CB  PHE A 100      33.843   6.177  24.073  1.00115.72           C  
ANISOU  717  CB  PHE A 100    14216  14461  15293   1084   1300   1072       C  
ATOM    718  CG  PHE A 100      33.619   4.720  23.851  1.00123.32           C  
ANISOU  718  CG  PHE A 100    14990  15376  16490   1030   1328   1152       C  
ATOM    719  CD1 PHE A 100      32.382   4.150  24.112  1.00127.59           C  
ANISOU  719  CD1 PHE A 100    15393  15890  17194   1098   1425   1338       C  
ATOM    720  CD2 PHE A 100      34.647   3.914  23.400  1.00118.31           C  
ANISOU  720  CD2 PHE A 100    14314  14714  15923    917   1262   1054       C  
ATOM    721  CE1 PHE A 100      32.170   2.808  23.916  1.00127.49           C  
ANISOU  721  CE1 PHE A 100    15209  15821  17411   1042   1437   1415       C  
ATOM    722  CE2 PHE A 100      34.446   2.567  23.201  1.00123.25           C  
ANISOU  722  CE2 PHE A 100    14782  15283  16765    870   1286   1122       C  
ATOM    723  CZ  PHE A 100      33.206   2.010  23.461  1.00140.35           C  
ANISOU  723  CZ  PHE A 100    16814  17418  19094    928   1365   1298       C  
ATOM    724  N   GLN A 101      35.881   8.383  25.373  1.00113.91           N  
ANISOU  724  N   GLN A 101    14432  14312  14536   1188   1165    865       N  
ATOM    725  CA  GLN A 101      36.278   9.782  25.427  1.00109.35           C  
ANISOU  725  CA  GLN A 101    14048  13746  13754   1199   1083    759       C  
ATOM    726  C   GLN A 101      35.771  10.557  24.215  1.00114.19           C  
ANISOU  726  C   GLN A 101    14641  14344  14404   1102   1044    681       C  
ATOM    727  O   GLN A 101      35.375  11.721  24.326  1.00125.15           O  
ANISOU  727  O   GLN A 101    16160  15735  15657   1162   1042    661       O  
ATOM    728  CB  GLN A 101      37.801   9.899  25.514  1.00118.88           C  
ANISOU  728  CB  GLN A 101    15332  14956  14881   1120    948    645       C  
ATOM    729  CG  GLN A 101      38.311  11.334  25.513  1.00121.70           C  
ANISOU  729  CG  GLN A 101    15881  15310  15050   1110    835    534       C  
ATOM    730  CD  GLN A 101      39.823  11.409  25.447  1.00125.97           C  
ANISOU  730  CD  GLN A 101    16457  15844  15560   1006    688    441       C  
ATOM    731  NE2 GLN A 101      40.352  11.685  24.259  1.00116.55           N  
ANISOU  731  NE2 GLN A 101    15204  14638  14443    855    611    338       N  
ATOM    732  OE1 GLN A 101      40.509  11.213  26.452  1.00126.68           O  
ANISOU  732  OE1 GLN A 101    16628  15940  15566   1065    646    472       O  
ATOM    733  N   ASN A 102      35.800   9.907  23.056  1.00109.72           N  
ANISOU  733  N   ASN A 102    13922  13755  14013    954   1012    635       N  
ATOM    734  CA  ASN A 102      35.404  10.538  21.803  1.00 98.61           C  
ANISOU  734  CA  ASN A 102    12492  12332  12645    846    961    556       C  
ATOM    735  C   ASN A 102      34.519   9.658  20.938  1.00104.94           C  
ANISOU  735  C   ASN A 102    13115  13098  13657    772    993    611       C  
ATOM    736  O   ASN A 102      34.620   8.433  20.955  1.00102.58           O  
ANISOU  736  O   ASN A 102    12701  12776  13500    743   1016    655       O  
ATOM    737  CB  ASN A 102      36.633  10.931  20.984  1.00101.44           C  
ANISOU  737  CB  ASN A 102    12896  12687  12961    710    838    395       C  
ATOM    738  CG  ASN A 102      37.566  11.841  21.737  1.00103.72           C  
ANISOU  738  CG  ASN A 102    13352  12994  13062    757    769    340       C  
ATOM    739  ND2 ASN A 102      37.239  13.127  21.760  1.00105.34           N  
ANISOU  739  ND2 ASN A 102    13685  13203  13135    795    743    306       N  
ATOM    740  OD1 ASN A 102      38.571  11.399  22.290  1.00 99.08           O  
ANISOU  740  OD1 ASN A 102    12780  12411  12454    756    732    331       O  
ATOM    741  N   CYS A 103      33.652  10.301  20.171  1.00 99.38           N  
ANISOU  741  N   CYS A 103    12397  12385  12979    736    982    609       N  
ATOM    742  CA  CYS A 103      32.920   9.615  19.126  1.00 98.07           C  
ANISOU  742  CA  CYS A 103    12084  12174  13004    630    962    633       C  
ATOM    743  C   CYS A 103      33.401  10.184  17.808  1.00100.60           C  
ANISOU  743  C   CYS A 103    12447  12485  13291    487    851    474       C  
ATOM    744  O   CYS A 103      33.458  11.406  17.627  1.00 93.88           O  
ANISOU  744  O   CYS A 103    11700  11661  12310    494    821    415       O  
ATOM    745  CB  CYS A 103      31.407   9.792  19.291  1.00 96.94           C  
ANISOU  745  CB  CYS A 103    11864  12021  12947    706   1037    795       C  
ATOM    746  SG  CYS A 103      30.462   9.264  17.860  1.00103.64           S  
ANISOU  746  SG  CYS A 103    12559  12806  14014    553    960    813       S  
ATOM    747  N   ILE A 104      33.782   9.305  16.896  1.00 92.32           N  
ANISOU  747  N   ILE A 104    11331  11394  12353    365    796    405       N  
ATOM    748  CA  ILE A 104      34.323   9.753  15.621  1.00108.87           C  
ANISOU  748  CA  ILE A 104    13476  13479  14409    240    704    257       C  
ATOM    749  C   ILE A 104      33.390   9.399  14.474  1.00109.31           C  
ANISOU  749  C   ILE A 104    13457  13482  14594    142    652    263       C  
ATOM    750  O   ILE A 104      32.996   8.241  14.335  1.00110.44           O  
ANISOU  750  O   ILE A 104    13503  13567  14891    109    651    315       O  
ATOM    751  CB  ILE A 104      35.683   9.128  15.340  1.00114.61           C  
ANISOU  751  CB  ILE A 104    14222  14194  15132    179    677    154       C  
ATOM    752  CG1 ILE A 104      36.710   9.558  16.379  1.00132.24           C  
ANISOU  752  CG1 ILE A 104    16532  16474  17239    254    695    145       C  
ATOM    753  CG2 ILE A 104      36.168   9.531  13.970  1.00115.53           C  
ANISOU  753  CG2 ILE A 104    14387  14294  15213     65    603     21       C  
ATOM    754  CD1 ILE A 104      38.035   8.845  16.191  1.00137.84           C  
ANISOU  754  CD1 ILE A 104    17230  17167  17974    202    680     79       C  
ATOM    755  N   ILE A 105      33.055  10.382  13.641  1.00 98.11           N  
ANISOU  755  N   ILE A 105    12088  12075  13115     91    595    210       N  
ATOM    756  CA  ILE A 105      32.125  10.146  12.542  1.00 98.77           C  
ANISOU  756  CA  ILE A 105    12113  12106  13308     -5    525    220       C  
ATOM    757  C   ILE A 105      32.722  10.354  11.145  1.00113.83           C  
ANISOU  757  C   ILE A 105    14095  13995  15160   -125    433     65       C  
ATOM    758  O   ILE A 105      33.246  11.423  10.827  1.00107.81           O  
ANISOU  758  O   ILE A 105    13423  13279  14263   -132    417    -15       O  
ATOM    759  CB  ILE A 105      30.904  11.040  12.711  1.00103.37           C  
ANISOU  759  CB  ILE A 105    12667  12711  13899     45    540    333       C  
ATOM    760  CG1 ILE A 105      30.364  10.868  14.130  1.00 99.30           C  
ANISOU  760  CG1 ILE A 105    12095  12216  13420    191    657    496       C  
ATOM    761  CG2 ILE A 105      29.849  10.728  11.659  1.00 89.77           C  
ANISOU  761  CG2 ILE A 105    10864  10928  12316    -57    451    374       C  
ATOM    762  CD1 ILE A 105      29.043  11.495  14.361  1.00 94.87           C  
ANISOU  762  CD1 ILE A 105    11476  11660  12908    258    700    648       C  
ATOM    763  N   ASP A 106      32.647   9.316  10.314  1.00 98.10           N  
ANISOU  763  N   ASP A 106    12074  11927  13271   -216    374     26       N  
ATOM    764  CA  ASP A 106      33.065   9.427   8.918  1.00 91.12           C  
ANISOU  764  CA  ASP A 106    11276  11014  12332   -319    291   -111       C  
ATOM    765  C   ASP A 106      31.870   9.739   8.047  1.00116.22           C  
ANISOU  765  C   ASP A 106    14437  14160  15563   -391    194    -78       C  
ATOM    766  O   ASP A 106      30.758   9.291   8.313  1.00121.72           O  
ANISOU  766  O   ASP A 106    15029  14816  16403   -393    171     47       O  
ATOM    767  CB  ASP A 106      33.747   8.150   8.437  1.00 88.70           C  
ANISOU  767  CB  ASP A 106    10989  10632  12082   -369    279   -188       C  
ATOM    768  CG  ASP A 106      34.628   8.371   7.216  1.00109.69           C  
ANISOU  768  CG  ASP A 106    13770  13278  14630   -431    244   -339       C  
ATOM    769  OD1 ASP A 106      34.490   9.425   6.558  1.00108.75           O  
ANISOU  769  OD1 ASP A 106    13710  13198  14414   -459    203   -378       O  
ATOM    770  OD2 ASP A 106      35.462   7.476   6.912  1.00101.37           O1-
ANISOU  770  OD2 ASP A 106    12755  12173  13590   -444    268   -409       O1-
ATOM    771  N   THR A 107      32.097  10.526   7.008  1.00123.41           N  
ANISOU  771  N   THR A 107    15440  15087  16364   -449    136   -176       N  
ATOM    772  CA  THR A 107      31.019  10.943   6.134  1.00104.65           C  
ANISOU  772  CA  THR A 107    13055  12686  14019   -520     33   -146       C  
ATOM    773  C   THR A 107      31.352  10.509   4.712  1.00107.85           C  
ANISOU  773  C   THR A 107    13566  13027  14385   -623    -66   -277       C  
ATOM    774  O   THR A 107      32.486  10.152   4.427  1.00112.27           O  
ANISOU  774  O   THR A 107    14210  13580  14868   -621    -28   -389       O  
ATOM    775  CB  THR A 107      30.797  12.451   6.230  1.00 97.43           C  
ANISOU  775  CB  THR A 107    12163  11855  13003   -481     55   -122       C  
ATOM    776  CG2 THR A 107      30.338  12.809   7.634  1.00101.31           C  
ANISOU  776  CG2 THR A 107    12573  12391  13528   -365    155     14       C  
ATOM    777  OG1 THR A 107      32.025  13.145   5.937  1.00109.65           O  
ANISOU  777  OG1 THR A 107    13819  13453  14390   -472     87   -246       O  
ATOM    778  N   PRO A 108      30.357  10.489   3.821  1.00120.22           N  
ANISOU  778  N   PRO A 108    15132  14540  16006   -709   -194   -255       N  
ATOM    779  CA  PRO A 108      30.678  10.044   2.463  1.00112.54           C  
ANISOU  779  CA  PRO A 108    14291  13496  14971   -798   -294   -387       C  
ATOM    780  C   PRO A 108      31.457  11.086   1.669  1.00119.74           C  
ANISOU  780  C   PRO A 108    15329  14474  15693   -797   -275   -498       C  
ATOM    781  O   PRO A 108      31.351  12.281   1.945  1.00109.98           O  
ANISOU  781  O   PRO A 108    14066  13325  14398   -761   -237   -457       O  
ATOM    782  CB  PRO A 108      29.307   9.829   1.845  1.00105.66           C  
ANISOU  782  CB  PRO A 108    13377  12550  14217   -890   -456   -310       C  
ATOM    783  CG  PRO A 108      28.454  10.850   2.541  1.00121.42           C  
ANISOU  783  CG  PRO A 108    15248  14624  16261   -845   -421   -162       C  
ATOM    784  CD  PRO A 108      28.940  10.868   3.953  1.00112.23           C  
ANISOU  784  CD  PRO A 108    14009  13523  15110   -727   -258   -105       C  
ATOM    785  N   GLY A 109      32.210  10.623   0.678  1.00128.95           N  
ANISOU  785  N   GLY A 109    16636  15590  16768   -830   -297   -629       N  
ATOM    786  CA  GLY A 109      32.997  11.490  -0.177  1.00117.20           C  
ANISOU  786  CA  GLY A 109    15269  14154  15106   -824   -270   -726       C  
ATOM    787  C   GLY A 109      32.189  12.528  -0.926  1.00124.69           C  
ANISOU  787  C   GLY A 109    16239  15134  16002   -875   -366   -703       C  
ATOM    788  O   GLY A 109      32.561  13.702  -0.961  1.00145.95           O  
ANISOU  788  O   GLY A 109    18941  17915  18597   -843   -314   -706       O  
ATOM    789  N   GLN A 110      31.102  12.092  -1.551  1.00122.83           N  
ANISOU  789  N   GLN A 110    16012  14822  15836   -959   -518   -676       N  
ATOM    790  CA  GLN A 110      30.133  13.013  -2.129  1.00120.51           C  
ANISOU  790  CA  GLN A 110    15705  14554  15531  -1013   -624   -620       C  
ATOM    791  C   GLN A 110      29.754  14.013  -1.057  1.00117.34           C  
ANISOU  791  C   GLN A 110    15156  14247  15180   -951   -540   -497       C  
ATOM    792  O   GLN A 110      28.887  13.765  -0.229  1.00115.82           O  
ANISOU  792  O   GLN A 110    14826  14040  15139   -940   -547   -368       O  
ATOM    793  CB  GLN A 110      28.894  12.270  -2.637  1.00121.68           C  
ANISOU  793  CB  GLN A 110    15834  14594  15805  -1114   -812   -564       C  
ATOM    794  CG  GLN A 110      29.192  11.066  -3.510  1.00148.68           C  
ANISOU  794  CG  GLN A 110    19409  17889  19192  -1170   -906   -684       C  
ATOM    795  CD  GLN A 110      29.614  11.444  -4.916  1.00162.15           C  
ANISOU  795  CD  GLN A 110    21323  19586  20701  -1200   -966   -812       C  
ATOM    796  NE2 GLN A 110      29.274  10.589  -5.878  1.00166.78           N  
ANISOU  796  NE2 GLN A 110    22053  20045  21271  -1278  -1128   -882       N  
ATOM    797  OE1 GLN A 110      30.232  12.490  -5.142  1.00158.96           O  
ANISOU  797  OE1 GLN A 110    20957  19282  20157  -1151   -872   -845       O  
ATOM    798  N   ILE A 111      30.424  15.150  -1.061  1.00118.32           N  
ANISOU  798  N   ILE A 111    15316  14462  15178   -902   -456   -531       N  
ATOM    799  CA  ILE A 111      30.342  16.035   0.076  1.00106.68           C  
ANISOU  799  CA  ILE A 111    13739  13066  13726   -822   -356   -442       C  
ATOM    800  C   ILE A 111      29.025  16.805   0.108  1.00 98.98           C  
ANISOU  800  C   ILE A 111    12676  12109  12823   -839   -416   -313       C  
ATOM    801  O   ILE A 111      28.487  17.074   1.187  1.00108.42           O  
ANISOU  801  O   ILE A 111    13762  13329  14102   -773   -350   -196       O  
ATOM    802  CB  ILE A 111      31.553  16.997   0.079  1.00112.10           C  
ANISOU  802  CB  ILE A 111    14497  13829  14267   -770   -260   -519       C  
ATOM    803  CG1 ILE A 111      31.556  17.884   1.322  1.00 98.74           C  
ANISOU  803  CG1 ILE A 111    12731  12201  12584   -683   -168   -442       C  
ATOM    804  CG2 ILE A 111      31.603  17.811  -1.200  1.00118.07           C  
ANISOU  804  CG2 ILE A 111    15345  14606  14909   -820   -321   -574       C  
ATOM    805  CD1 ILE A 111      32.906  18.539   1.578  1.00 91.95           C  
ANISOU  805  CD1 ILE A 111    11929  11392  11615   -634    -84   -513       C  
ATOM    806  N   GLU A 112      28.495  17.146  -1.066  1.00106.42           N  
ANISOU  806  N   GLU A 112    13668  13035  13731   -920   -536   -326       N  
ATOM    807  CA  GLU A 112      27.297  17.986  -1.129  1.00116.36           C  
ANISOU  807  CA  GLU A 112    14840  14314  15056   -937   -592   -195       C  
ATOM    808  C   GLU A 112      26.167  17.261  -0.427  1.00119.12           C  
ANISOU  808  C   GLU A 112    15042  14610  15609   -941   -625    -42       C  
ATOM    809  O   GLU A 112      25.366  17.868   0.285  1.00126.63           O  
ANISOU  809  O   GLU A 112    15875  15591  16647   -887   -575    105       O  
ATOM    810  CB  GLU A 112      26.913  18.320  -2.579  1.00112.20           C  
ANISOU  810  CB  GLU A 112    14395  13769  14465  -1035   -739   -232       C  
ATOM    811  CG  GLU A 112      27.691  19.486  -3.178  1.00104.56           C  
ANISOU  811  CG  GLU A 112    13528  12877  13322  -1014   -690   -316       C  
ATOM    812  CD  GLU A 112      27.337  19.772  -4.637  1.00123.74           C  
ANISOU  812  CD  GLU A 112    16053  15292  15673  -1104   -833   -351       C  
ATOM    813  OE1 GLU A 112      28.260  20.150  -5.396  1.00121.07           O  
ANISOU  813  OE1 GLU A 112    15844  14984  15174  -1098   -804   -463       O  
ATOM    814  OE2 GLU A 112      26.149  19.639  -5.023  1.00113.40           O1-
ANISOU  814  OE2 GLU A 112    14686  13937  14462  -1177   -973   -255       O1-
ATOM    815  N   CYS A 113      26.159  15.943  -0.598  1.00123.34           N  
ANISOU  815  N   CYS A 113    15586  15058  16221   -995   -698    -72       N  
ATOM    816  CA  CYS A 113      25.117  15.065  -0.077  1.00122.64           C  
ANISOU  816  CA  CYS A 113    15355  14897  16346  -1018   -754     76       C  
ATOM    817  C   CYS A 113      24.984  15.147   1.440  1.00128.40           C  
ANISOU  817  C   CYS A 113    15953  15669  17162   -895   -590    199       C  
ATOM    818  O   CYS A 113      24.005  14.681   2.007  1.00139.01           O  
ANISOU  818  O   CYS A 113    17150  16972  18694   -887   -602    367       O  
ATOM    819  CB  CYS A 113      25.395  13.617  -0.510  1.00 92.62           C  
ANISOU  819  CB  CYS A 113    11615  10987  12588  -1091   -850    -11       C  
ATOM    820  SG  CYS A 113      25.270  13.380  -2.317  1.00159.37           S  
ANISOU  820  SG  CYS A 113    20243  19359  20951  -1234  -1075   -133       S  
ATOM    821  N   PHE A 114      25.953  15.760   2.100  1.00131.91           N  
ANISOU  821  N   PHE A 114    16454  16193  17471   -796   -440    128       N  
ATOM    822  CA  PHE A 114      25.909  15.814   3.546  1.00135.86           C  
ANISOU  822  CA  PHE A 114    16867  16730  18023   -671   -289    229       C  
ATOM    823  C   PHE A 114      25.829  17.230   4.074  1.00137.30           C  
ANISOU  823  C   PHE A 114    17056  16993  18119   -576   -188    277       C  
ATOM    824  O   PHE A 114      25.119  17.494   5.041  1.00154.88           O  
ANISOU  824  O   PHE A 114    19189  19234  20425   -480    -97    429       O  
ATOM    825  CB  PHE A 114      27.131  15.122   4.145  1.00144.47           C  
ANISOU  825  CB  PHE A 114    18019  17826  19049   -624   -203    119       C  
ATOM    826  CG  PHE A 114      27.057  14.985   5.628  1.00128.76           C  
ANISOU  826  CG  PHE A 114    15950  15861  17113   -499    -66    226       C  
ATOM    827  CD1 PHE A 114      26.482  13.860   6.198  1.00129.66           C  
ANISOU  827  CD1 PHE A 114    15950  15918  17398   -489    -60    339       C  
ATOM    828  CD2 PHE A 114      27.521  15.995   6.455  1.00102.55           C  
ANISOU  828  CD2 PHE A 114    12676  12615  13673   -389     52    222       C  
ATOM    829  CE1 PHE A 114      26.382  13.734   7.567  1.00116.12           C  
ANISOU  829  CE1 PHE A 114    14168  14229  15724   -361     76    450       C  
ATOM    830  CE2 PHE A 114      27.428  15.880   7.823  1.00100.31           C  
ANISOU  830  CE2 PHE A 114    12346  12350  13417   -263    175    320       C  
ATOM    831  CZ  PHE A 114      26.860  14.750   8.383  1.00125.02           C  
ANISOU  831  CZ  PHE A 114    15361  15432  16708   -244    195    437       C  
ATOM    832  N   VAL A 115      26.570  18.136   3.450  1.00133.60           N  
ANISOU  832  N   VAL A 115    16703  16572  17488   -594   -196    152       N  
ATOM    833  CA  VAL A 115      26.680  19.499   3.958  1.00127.21           C  
ANISOU  833  CA  VAL A 115    15924  15829  16582   -505   -105    172       C  
ATOM    834  C   VAL A 115      25.472  20.392   3.630  1.00152.48           C  
ANISOU  834  C   VAL A 115    19057  19038  19842   -509   -135    304       C  
ATOM    835  O   VAL A 115      25.051  21.203   4.457  1.00167.17           O  
ANISOU  835  O   VAL A 115    20889  20927  21702   -401    -33    403       O  
ATOM    836  CB  VAL A 115      27.954  20.159   3.427  1.00125.70           C  
ANISOU  836  CB  VAL A 115    15867  15679  16215   -524   -104      5       C  
ATOM    837  CG1 VAL A 115      29.163  19.430   3.964  1.00126.28           C  
ANISOU  837  CG1 VAL A 115    15991  15750  16240   -496    -48    -94       C  
ATOM    838  CG2 VAL A 115      27.971  20.152   1.909  1.00136.20           C  
ANISOU  838  CG2 VAL A 115    17250  16993  17507   -644   -228    -73       C  
ATOM    839  N   TRP A 116      24.912  20.242   2.435  1.00154.24           N  
ANISOU  839  N   TRP A 116    19262  19230  20113   -627   -276    309       N  
ATOM    840  CA  TRP A 116      23.793  21.078   2.022  1.00152.61           C  
ANISOU  840  CA  TRP A 116    18984  19029  19970   -644   -321    441       C  
ATOM    841  C   TRP A 116      22.464  20.409   2.309  1.00145.35           C  
ANISOU  841  C   TRP A 116    17899  18055  19274   -654   -359    642       C  
ATOM    842  O   TRP A 116      21.470  21.081   2.575  1.00155.26           O  
ANISOU  842  O   TRP A 116    19055  19319  20620   -605   -321    813       O  
ATOM    843  CB  TRP A 116      23.897  21.410   0.539  1.00149.61           C  
ANISOU  843  CB  TRP A 116    18682  18650  19514   -766   -465    350       C  
ATOM    844  CG  TRP A 116      24.959  22.398   0.251  1.00147.25           C  
ANISOU  844  CG  TRP A 116    18510  18412  19025   -741   -413    210       C  
ATOM    845  CD1 TRP A 116      25.597  23.201   1.152  1.00146.60           C  
ANISOU  845  CD1 TRP A 116    18467  18378  18857   -632   -276    185       C  
ATOM    846  CD2 TRP A 116      25.524  22.698  -1.031  1.00146.70           C  
ANISOU  846  CD2 TRP A 116    18551  18356  18831   -827   -503     86       C  
ATOM    847  CE2 TRP A 116      26.502  23.698  -0.826  1.00134.06           C  
ANISOU  847  CE2 TRP A 116    17031  16815  17092   -765   -407      2       C  
ATOM    848  CE3 TRP A 116      25.300  22.225  -2.325  1.00146.22           C  
ANISOU  848  CE3 TRP A 116    18540  18259  18760   -945   -658     41       C  
ATOM    849  NE1 TRP A 116      26.524  23.987   0.509  1.00135.43           N  
ANISOU  849  NE1 TRP A 116    17163  17003  17293   -653   -283     59       N  
ATOM    850  CZ2 TRP A 116      27.253  24.226  -1.876  1.00124.02           C  
ANISOU  850  CZ2 TRP A 116    15865  15571  15686   -813   -446   -110       C  
ATOM    851  CZ3 TRP A 116      26.048  22.753  -3.363  1.00139.01           C  
ANISOU  851  CZ3 TRP A 116    17754  17376  17688   -983   -690    -80       C  
ATOM    852  CH2 TRP A 116      27.013  23.742  -3.131  1.00127.39           C  
ANISOU  852  CH2 TRP A 116    16339  15970  16095   -915   -576   -147       C  
ATOM    853  N   SER A 117      22.458  19.082   2.257  1.00142.22           N  
ANISOU  853  N   SER A 117    17469  17594  18975   -715   -430    633       N  
ATOM    854  CA  SER A 117      21.242  18.301   2.458  1.00142.25           C  
ANISOU  854  CA  SER A 117    17304  17528  19216   -744   -491    830       C  
ATOM    855  C   SER A 117      20.627  18.555   3.825  1.00140.45           C  
ANISOU  855  C   SER A 117    16951  17323  19090   -590   -314   1023       C  
ATOM    856  O   SER A 117      21.303  19.025   4.742  1.00126.40           O  
ANISOU  856  O   SER A 117    15241  15599  17185   -461   -151    971       O  
ATOM    857  CB  SER A 117      21.533  16.812   2.302  1.00148.48           C  
ANISOU  857  CB  SER A 117    18098  18238  20079   -822   -581    766       C  
ATOM    858  OG  SER A 117      22.154  16.302   3.468  1.00152.05           O  
ANISOU  858  OG  SER A 117    18546  18708  20520   -715   -429    750       O  
ATOM    859  N   ALA A 118      19.344  18.231   3.958  1.00137.81           N  
ANISOU  859  N   ALA A 118    16437  16938  18986   -599   -349   1254       N  
ATOM    860  CA  ALA A 118      18.623  18.499   5.195  1.00139.88           C  
ANISOU  860  CA  ALA A 118    16574  17217  19358   -438   -167   1472       C  
ATOM    861  C   ALA A 118      18.719  17.325   6.163  1.00136.15           C  
ANISOU  861  C   ALA A 118    16033  16710  18990   -378    -90   1532       C  
ATOM    862  O   ALA A 118      18.781  17.511   7.375  1.00143.45           O  
ANISOU  862  O   ALA A 118    16947  17670  19887   -211    105   1608       O  
ATOM    863  CB  ALA A 118      17.174  18.826   4.900  1.00145.26           C  
ANISOU  863  CB  ALA A 118    17075  17864  20252   -461   -219   1727       C  
ATOM    864  N   SER A 119      18.732  16.112   5.630  1.00124.87           N  
ANISOU  864  N   SER A 119    14567  15205  17675   -510   -245   1498       N  
ATOM    865  CA  SER A 119      18.930  14.941   6.471  1.00135.75           C  
ANISOU  865  CA  SER A 119    15886  16546  19148   -465   -182   1536       C  
ATOM    866  C   SER A 119      20.371  14.934   6.984  1.00139.18           C  
ANISOU  866  C   SER A 119    16495  17038  19350   -395    -74   1314       C  
ATOM    867  O   SER A 119      20.669  14.381   8.045  1.00124.19           O  
ANISOU  867  O   SER A 119    14574  15147  17468   -291     55   1351       O  
ATOM    868  CB  SER A 119      18.608  13.656   5.706  1.00139.33           C  
ANISOU  868  CB  SER A 119    16272  16887  19781   -632   -392   1543       C  
ATOM    869  OG  SER A 119      19.368  13.564   4.516  1.00149.26           O  
ANISOU  869  OG  SER A 119    17698  18126  20889   -771   -554   1302       O  
ATOM    870  N   GLY A 120      21.262  15.566   6.230  1.00131.98           N  
ANISOU  870  N   GLY A 120    15750  16167  18230   -452   -127   1098       N  
ATOM    871  CA  GLY A 120      22.622  15.744   6.688  1.00123.91           C  
ANISOU  871  CA  GLY A 120    14882  15202  16997   -386    -28    909       C  
ATOM    872  C   GLY A 120      22.663  16.696   7.864  1.00120.96           C  
ANISOU  872  C   GLY A 120    14531  14897  16530   -209    161    977       C  
ATOM    873  O   GLY A 120      23.348  16.442   8.859  1.00118.22           O  
ANISOU  873  O   GLY A 120    14232  14575  16110   -108    277    942       O  
ATOM    874  N   ALA A 121      21.921  17.794   7.747  1.00120.77           N  
ANISOU  874  N   ALA A 121    14482  14899  16505   -169    189   1077       N  
ATOM    875  CA  ALA A 121      21.959  18.860   8.743  1.00123.92           C  
ANISOU  875  CA  ALA A 121    14941  15353  16788      2    360   1123       C  
ATOM    876  C   ALA A 121      21.291  18.411  10.031  1.00122.39           C  
ANISOU  876  C   ALA A 121    14646  15147  16709    156    516   1327       C  
ATOM    877  O   ALA A 121      21.618  18.890  11.118  1.00125.87           O  
ANISOU  877  O   ALA A 121    15175  15623  17028    317    670   1333       O  
ATOM    878  CB  ALA A 121      21.294  20.113   8.207  1.00127.93           C  
ANISOU  878  CB  ALA A 121    15448  15881  17280      4    350   1184       C  
ATOM    879  N   ILE A 122      20.350  17.487   9.895  1.00132.02           N  
ANISOU  879  N   ILE A 122    15685  16310  18166    107    468   1500       N  
ATOM    880  CA  ILE A 122      19.627  16.944  11.034  1.00130.02           C  
ANISOU  880  CA  ILE A 122    15304  16038  18059    248    615   1727       C  
ATOM    881  C   ILE A 122      20.545  16.081  11.901  1.00133.85           C  
ANISOU  881  C   ILE A 122    15852  16532  18475    306    684   1640       C  
ATOM    882  O   ILE A 122      20.630  16.262  13.119  1.00138.76           O  
ANISOU  882  O   ILE A 122    16515  17184  19024    486    861   1711       O  
ATOM    883  CB  ILE A 122      18.425  16.118  10.567  1.00120.95           C  
ANISOU  883  CB  ILE A 122    13929  14814  17211    156    517   1942       C  
ATOM    884  CG1 ILE A 122      17.352  17.038   9.997  1.00128.97           C  
ANISOU  884  CG1 ILE A 122    14857  15827  18320    142    488   2096       C  
ATOM    885  CG2 ILE A 122      17.857  15.301  11.714  1.00119.28           C  
ANISOU  885  CG2 ILE A 122    13576  14578  17169    287    660   2166       C  
ATOM    886  CD1 ILE A 122      16.250  16.295   9.283  1.00132.11           C  
ANISOU  886  CD1 ILE A 122    15042  16141  19014      5    329   2284       C  
ATOM    887  N   ILE A 123      21.228  15.142  11.256  1.00119.80           N  
ANISOU  887  N   ILE A 123    14087  14720  16712    158    544   1489       N  
ATOM    888  CA  ILE A 123      22.216  14.295  11.918  1.00121.26           C  
ANISOU  888  CA  ILE A 123    14331  14909  16831    190    589   1387       C  
ATOM    889  C   ILE A 123      23.249  15.123  12.686  1.00117.23           C  
ANISOU  889  C   ILE A 123    14006  14471  16064    310    701   1253       C  
ATOM    890  O   ILE A 123      23.502  14.893  13.871  1.00107.80           O  
ANISOU  890  O   ILE A 123    12839  13297  14823    451    834   1304       O  
ATOM    891  CB  ILE A 123      22.927  13.416  10.896  1.00116.91           C  
ANISOU  891  CB  ILE A 123    13812  14314  16296      9    417   1208       C  
ATOM    892  CG1 ILE A 123      21.952  12.378  10.351  1.00116.84           C  
ANISOU  892  CG1 ILE A 123    13629  14212  16551   -101    298   1346       C  
ATOM    893  CG2 ILE A 123      24.136  12.735  11.519  1.00120.69           C  
ANISOU  893  CG2 ILE A 123    14376  14808  16675     44    470   1078       C  
ATOM    894  CD1 ILE A 123      22.418  11.744   9.069  1.00114.01           C  
ANISOU  894  CD1 ILE A 123    13330  13794  16197   -289    101   1171       C  
ATOM    895  N   THR A 124      23.828  16.098  11.999  1.00105.08           N  
ANISOU  895  N   THR A 124    12597  12964  14363    254    636   1089       N  
ATOM    896  CA  THR A 124      24.757  17.025  12.617  1.00114.80           C  
ANISOU  896  CA  THR A 124    14005  14250  15364    350    711    967       C  
ATOM    897  C   THR A 124      24.149  17.743  13.833  1.00123.42           C  
ANISOU  897  C   THR A 124    15125  15362  16407    555    883   1120       C  
ATOM    898  O   THR A 124      24.720  17.720  14.927  1.00109.99           O  
ANISOU  898  O   THR A 124    13522  13681  14588    680    980   1101       O  
ATOM    899  CB  THR A 124      25.232  18.060  11.593  1.00114.46           C  
ANISOU  899  CB  THR A 124    14066  14229  15195    254    612    811       C  
ATOM    900  CG2 THR A 124      26.239  19.005  12.220  1.00104.13           C  
ANISOU  900  CG2 THR A 124    12935  12962  13666    340    666    688       C  
ATOM    901  OG1 THR A 124      25.838  17.378  10.486  1.00111.06           O  
ANISOU  901  OG1 THR A 124    13632  13777  14789     86    471    671       O  
ATOM    902  N   GLU A 125      22.987  18.366  13.652  1.00119.55           N  
ANISOU  902  N   GLU A 125    14557  14863  16003    596    924   1278       N  
ATOM    903  CA  GLU A 125      22.352  19.082  14.752  1.00109.73           C  
ANISOU  903  CA  GLU A 125    13351  13631  14710    807   1106   1434       C  
ATOM    904  C   GLU A 125      21.983  18.153  15.908  1.00113.67           C  
ANISOU  904  C   GLU A 125    13772  14118  15298    945   1245   1603       C  
ATOM    905  O   GLU A 125      22.166  18.512  17.075  1.00118.53           O  
ANISOU  905  O   GLU A 125    14511  14751  15772   1131   1391   1634       O  
ATOM    906  CB  GLU A 125      21.114  19.830  14.263  1.00127.09           C  
ANISOU  906  CB  GLU A 125    15452  15816  17022    822   1130   1599       C  
ATOM    907  CG  GLU A 125      21.421  21.208  13.696  1.00143.79           C  
ANISOU  907  CG  GLU A 125    17704  17953  18977    798   1086   1469       C  
ATOM    908  CD  GLU A 125      21.594  22.266  14.773  1.00142.23           C  
ANISOU  908  CD  GLU A 125    17690  17768  18583   1002   1241   1468       C  
ATOM    909  OE1 GLU A 125      21.482  21.931  15.978  1.00119.56           O  
ANISOU  909  OE1 GLU A 125    14852  14893  15682   1172   1389   1566       O  
ATOM    910  OE2 GLU A 125      21.833  23.440  14.404  1.00151.65           O1-
ANISOU  910  OE2 GLU A 125    19002  18969  19648    995   1213   1371       O1-
ATOM    911  N   SER A 126      21.482  16.959  15.590  1.00104.31           N  
ANISOU  911  N   SER A 126    12396  12897  14342    857   1192   1712       N  
ATOM    912  CA  SER A 126      21.099  16.002  16.623  1.00117.75           C  
ANISOU  912  CA  SER A 126    13998  14584  16158    979   1320   1891       C  
ATOM    913  C   SER A 126      22.301  15.632  17.482  1.00106.93           C  
ANISOU  913  C   SER A 126    12777  13243  14609   1042   1359   1748       C  
ATOM    914  O   SER A 126      22.167  15.382  18.680  1.00118.01           O  
ANISOU  914  O   SER A 126    14199  14656  15983   1219   1517   1870       O  
ATOM    915  CB  SER A 126      20.493  14.748  16.003  1.00114.35           C  
ANISOU  915  CB  SER A 126    13341  14096  16011    838   1216   2004       C  
ATOM    916  OG  SER A 126      19.542  15.087  15.014  1.00133.63           O  
ANISOU  916  OG  SER A 126    15659  16505  18609    735   1121   2099       O  
ATOM    917  N   PHE A 127      23.476  15.602  16.867  1.00109.60           N  
ANISOU  917  N   PHE A 127    13220  13593  14829    902   1219   1501       N  
ATOM    918  CA  PHE A 127      24.697  15.369  17.628  1.00107.01           C  
ANISOU  918  CA  PHE A 127    13037  13293  14330    951   1239   1364       C  
ATOM    919  C   PHE A 127      25.112  16.630  18.360  1.00107.54           C  
ANISOU  919  C   PHE A 127    13319  13394  14149   1092   1314   1298       C  
ATOM    920  O   PHE A 127      25.495  16.578  19.531  1.00108.77           O  
ANISOU  920  O   PHE A 127    13584  13564  14180   1240   1412   1316       O  
ATOM    921  CB  PHE A 127      25.819  14.885  16.723  1.00103.19           C  
ANISOU  921  CB  PHE A 127    12579  12804  13823    761   1074   1146       C  
ATOM    922  CG  PHE A 127      25.888  13.406  16.620  1.00102.77           C  
ANISOU  922  CG  PHE A 127    12391  12715  13942    684   1037   1179       C  
ATOM    923  CD1 PHE A 127      26.500  12.667  17.617  1.00 98.30           C  
ANISOU  923  CD1 PHE A 127    11848  12160  13343    766   1108   1189       C  
ATOM    924  CD2 PHE A 127      25.314  12.745  15.546  1.00105.56           C  
ANISOU  924  CD2 PHE A 127    12600  13015  14492    532    926   1207       C  
ATOM    925  CE1 PHE A 127      26.560  11.291  17.540  1.00104.33           C  
ANISOU  925  CE1 PHE A 127    12484  12884  14274    699   1079   1225       C  
ATOM    926  CE2 PHE A 127      25.360  11.370  15.464  1.00121.93           C  
ANISOU  926  CE2 PHE A 127    14560  15039  16729    463    885   1237       C  
ATOM    927  CZ  PHE A 127      25.994  10.638  16.457  1.00117.80           C  
ANISOU  927  CZ  PHE A 127    14052  14528  16178    547    968   1245       C  
ATOM    928  N   ALA A 128      25.025  17.762  17.670  1.00103.69           N  
ANISOU  928  N   ALA A 128    12900  12910  13586   1047   1260   1224       N  
ATOM    929  CA  ALA A 128      25.379  19.038  18.266  1.00102.77           C  
ANISOU  929  CA  ALA A 128    12997  12809  13243   1170   1312   1156       C  
ATOM    930  C   ALA A 128      24.573  19.288  19.543  1.00115.68           C  
ANISOU  930  C   ALA A 128    14680  14438  14834   1415   1513   1346       C  
ATOM    931  O   ALA A 128      25.112  19.773  20.542  1.00117.82           O  
ANISOU  931  O   ALA A 128    15153  14713  14899   1555   1574   1295       O  
ATOM    932  CB  ALA A 128      25.170  20.153  17.266  1.00117.98           C  
ANISOU  932  CB  ALA A 128    14951  14734  15143   1086   1237   1089       C  
ATOM    933  N   SER A 129      23.293  18.922  19.518  1.00110.36           N  
ANISOU  933  N   SER A 129    13824  13749  14357   1469   1613   1575       N  
ATOM    934  CA  SER A 129      22.398  19.208  20.632  1.00115.58           C  
ANISOU  934  CA  SER A 129    14516  14403  14998   1716   1829   1789       C  
ATOM    935  C   SER A 129      22.547  18.247  21.796  1.00118.58           C  
ANISOU  935  C   SER A 129    14896  14788  15369   1850   1942   1883       C  
ATOM    936  O   SER A 129      21.909  18.437  22.827  1.00122.45           O  
ANISOU  936  O   SER A 129    15438  15274  15814   2079   2139   2059       O  
ATOM    937  CB  SER A 129      20.946  19.200  20.160  1.00123.80           C  
ANISOU  937  CB  SER A 129    15338  15421  16278   1729   1900   2031       C  
ATOM    938  OG  SER A 129      20.691  20.307  19.315  1.00137.03           O  
ANISOU  938  OG  SER A 129    17047  17093  17927   1664   1838   1975       O  
ATOM    939  N   SER A 130      23.384  17.221  21.653  1.00111.77           N  
ANISOU  939  N   SER A 130    13984  13935  14547   1720   1832   1776       N  
ATOM    940  CA  SER A 130      23.544  16.264  22.743  1.00109.03           C  
ANISOU  940  CA  SER A 130    13627  13596  14202   1840   1935   1871       C  
ATOM    941  C   SER A 130      24.981  16.156  23.249  1.00118.61           C  
ANISOU  941  C   SER A 130    15030  14832  15206   1823   1854   1664       C  
ATOM    942  O   SER A 130      25.200  15.825  24.412  1.00120.79           O  
ANISOU  942  O   SER A 130    15396  15118  15380   1981   1958   1724       O  
ATOM    943  CB  SER A 130      23.032  14.892  22.313  1.00118.03           C  
ANISOU  943  CB  SER A 130    14492  14717  15638   1732   1909   2005       C  
ATOM    944  OG  SER A 130      21.662  14.972  21.936  1.00140.41           O  
ANISOU  944  OG  SER A 130    17140  17523  18686   1755   1977   2228       O  
ATOM    945  N   PHE A 131      25.954  16.438  22.384  1.00108.60           N  
ANISOU  945  N   PHE A 131    13817  13568  13877   1636   1670   1435       N  
ATOM    946  CA  PHE A 131      27.368  16.423  22.777  1.00103.73           C  
ANISOU  946  CA  PHE A 131    13367  12967  13080   1603   1576   1247       C  
ATOM    947  C   PHE A 131      28.104  17.636  22.232  1.00105.31           C  
ANISOU  947  C   PHE A 131    13732  13164  13115   1522   1449   1049       C  
ATOM    948  O   PHE A 131      27.698  18.210  21.231  1.00114.30           O  
ANISOU  948  O   PHE A 131    14815  14296  14318   1426   1398   1021       O  
ATOM    949  CB  PHE A 131      28.072  15.145  22.283  1.00100.25           C  
ANISOU  949  CB  PHE A 131    12782  12528  12779   1436   1471   1180       C  
ATOM    950  CG  PHE A 131      27.239  13.908  22.424  1.00110.45           C  
ANISOU  950  CG  PHE A 131    13859  13807  14301   1457   1558   1371       C  
ATOM    951  CD1 PHE A 131      27.180  13.232  23.630  1.00108.25           C  
ANISOU  951  CD1 PHE A 131    13585  13538  14008   1613   1683   1500       C  
ATOM    952  CD2 PHE A 131      26.493  13.439  21.356  1.00114.83           C  
ANISOU  952  CD2 PHE A 131    14210  14333  15088   1321   1507   1430       C  
ATOM    953  CE1 PHE A 131      26.392  12.109  23.769  1.00118.32           C  
ANISOU  953  CE1 PHE A 131    14649  14796  15512   1634   1765   1693       C  
ATOM    954  CE2 PHE A 131      25.709  12.322  21.486  1.00102.35           C  
ANISOU  954  CE2 PHE A 131    12427  12725  13735   1333   1569   1616       C  
ATOM    955  CZ  PHE A 131      25.653  11.656  22.696  1.00106.77           C  
ANISOU  955  CZ  PHE A 131    12977  13296  14295   1490   1703   1752       C  
ATOM    956  N   PRO A 132      29.194  18.038  22.897  1.00113.64           N  
ANISOU  956  N   PRO A 132    14992  14222  13965   1558   1391    919       N  
ATOM    957  CA  PRO A 132      30.076  18.997  22.230  1.00111.91           C  
ANISOU  957  CA  PRO A 132    14890  13995  13637   1436   1237    726       C  
ATOM    958  C   PRO A 132      30.561  18.373  20.933  1.00110.78           C  
ANISOU  958  C   PRO A 132    14576  13862  13652   1209   1112    633       C  
ATOM    959  O   PRO A 132      31.165  17.306  21.010  1.00122.38           O  
ANISOU  959  O   PRO A 132    15967  15341  15191   1149   1081    616       O  
ATOM    960  CB  PRO A 132      31.233  19.174  23.222  1.00107.51           C  
ANISOU  960  CB  PRO A 132    14537  13430  12880   1495   1175    629       C  
ATOM    961  CG  PRO A 132      30.702  18.705  24.542  1.00104.70           C  
ANISOU  961  CG  PRO A 132    14239  13078  12466   1705   1330    780       C  
ATOM    962  CD  PRO A 132      29.695  17.638  24.224  1.00103.40           C  
ANISOU  962  CD  PRO A 132    13821  12929  12535   1700   1444    947       C  
ATOM    963  N   THR A 133      30.281  18.961  19.773  1.00110.22           N  
ANISOU  963  N   THR A 133    14452  13788  13639   1094   1049    582       N  
ATOM    964  CA  THR A 133      30.839  18.372  18.559  1.00106.68           C  
ANISOU  964  CA  THR A 133    13880  13345  13310    893    931    482       C  
ATOM    965  C   THR A 133      31.575  19.394  17.676  1.00111.05           C  
ANISOU  965  C   THR A 133    14516  13898  13779    778    809    326       C  
ATOM    966  O   THR A 133      31.155  20.551  17.518  1.00112.16           O  
ANISOU  966  O   THR A 133    14737  14031  13846    814    813    322       O  
ATOM    967  CB  THR A 133      29.749  17.608  17.729  1.00108.92           C  
ANISOU  967  CB  THR A 133    13955  13619  13810    823    957    590       C  
ATOM    968  CG2 THR A 133      28.445  17.522  18.474  1.00 93.34           C  
ANISOU  968  CG2 THR A 133    11924  11640  11902    979   1104    794       C  
ATOM    969  OG1 THR A 133      29.533  18.228  16.461  1.00105.32           O  
ANISOU  969  OG1 THR A 133    13467  13160  13388    699    873    526       O  
ATOM    970  N   VAL A 134      32.706  18.934  17.143  1.00 98.14           N  
ANISOU  970  N   VAL A 134    12859  12267  12161    650    709    208       N  
ATOM    971  CA  VAL A 134      33.609  19.709  16.303  1.00 87.84           C  
ANISOU  971  CA  VAL A 134    11614  10964  10798    535    594     70       C  
ATOM    972  C   VAL A 134      33.616  19.128  14.896  1.00 96.16           C  
ANISOU  972  C   VAL A 134    12535  12020  11980    381    544     26       C  
ATOM    973  O   VAL A 134      33.637  17.906  14.738  1.00 91.68           O  
ANISOU  973  O   VAL A 134    11862  11447  11523    339    557     48       O  
ATOM    974  CB  VAL A 134      35.046  19.696  16.874  1.00 98.75           C  
ANISOU  974  CB  VAL A 134    13090  12343  12090    523    522    -16       C  
ATOM    975  CG1 VAL A 134      36.059  20.210  15.856  1.00106.64           C  
ANISOU  975  CG1 VAL A 134    14096  13341  13081    386    410   -135       C  
ATOM    976  CG2 VAL A 134      35.108  20.491  18.156  1.00 99.95           C  
ANISOU  976  CG2 VAL A 134    13418  12478  12080    664    536      2       C  
ATOM    977  N   ILE A 135      33.577  19.991  13.881  1.00 98.71           N  
ANISOU  977  N   ILE A 135    12875  12347  12285    302    485    -34       N  
ATOM    978  CA  ILE A 135      33.739  19.556  12.493  1.00 94.58           C  
ANISOU  978  CA  ILE A 135    12266  11823  11846    160    426    -94       C  
ATOM    979  C   ILE A 135      35.219  19.451  12.127  1.00105.43           C  
ANISOU  979  C   ILE A 135    13675  13200  13184     82    362   -207       C  
ATOM    980  O   ILE A 135      35.946  20.423  12.257  1.00 95.43           O  
ANISOU  980  O   ILE A 135    12499  11937  11823     85    317   -261       O  
ATOM    981  CB  ILE A 135      33.106  20.516  11.477  1.00 97.36           C  
ANISOU  981  CB  ILE A 135    12621  12181  12192    108    390   -105       C  
ATOM    982  CG1 ILE A 135      31.638  20.811  11.806  1.00 87.99           C  
ANISOU  982  CG1 ILE A 135    11393  10989  11048    189    455     26       C  
ATOM    983  CG2 ILE A 135      33.255  19.920  10.084  1.00 98.82           C  
ANISOU  983  CG2 ILE A 135    12737  12361  12450    -27    328   -164       C  
ATOM    984  CD1 ILE A 135      30.781  19.564  11.754  1.00 85.78           C  
ANISOU  984  CD1 ILE A 135    10977  10692  10922    178    487    126       C  
ATOM    985  N   ALA A 136      35.672  18.294  11.653  1.00 92.87           N  
ANISOU  985  N   ALA A 136    12012  11599  11676     15    357   -235       N  
ATOM    986  CA  ALA A 136      37.043  18.206  11.134  1.00 85.81           C  
ANISOU  986  CA  ALA A 136    11138  10705  10763    -56    312   -325       C  
ATOM    987  C   ALA A 136      36.980  18.314   9.622  1.00 97.31           C  
ANISOU  987  C   ALA A 136    12575  12158  12241   -156    277   -383       C  
ATOM    988  O   ALA A 136      36.485  17.407   8.958  1.00 95.95           O  
ANISOU  988  O   ALA A 136    12347  11964  12147   -202    282   -382       O  
ATOM    989  CB  ALA A 136      37.701  16.911  11.561  1.00 99.11           C  
ANISOU  989  CB  ALA A 136    12771  12375  12513    -53    342   -319       C  
ATOM    990  N   TYR A 137      37.446  19.426   9.065  1.00 91.91           N  
ANISOU  990  N   TYR A 137    11946  11489  11486   -189    234   -431       N  
ATOM    991  CA  TYR A 137      37.317  19.609   7.622  1.00 90.04           C  
ANISOU  991  CA  TYR A 137    11705  11253  11253   -272    205   -479       C  
ATOM    992  C   TYR A 137      38.629  19.253   6.939  1.00 89.24           C  
ANISOU  992  C   TYR A 137    11608  11146  11152   -323    205   -541       C  
ATOM    993  O   TYR A 137      39.584  20.046   6.915  1.00 89.11           O  
ANISOU  993  O   TYR A 137    11624  11142  11093   -330    184   -561       O  
ATOM    994  CB  TYR A 137      36.884  21.041   7.261  1.00 90.56           C  
ANISOU  994  CB  TYR A 137    11816  11339  11253   -276    170   -478       C  
ATOM    995  CG  TYR A 137      36.549  21.170   5.792  1.00 87.09           C  
ANISOU  995  CG  TYR A 137    11372  10903  10814   -355    140   -512       C  
ATOM    996  CD1 TYR A 137      35.296  20.815   5.317  1.00 96.16           C  
ANISOU  996  CD1 TYR A 137    12482  12041  12011   -378    125   -475       C  
ATOM    997  CD2 TYR A 137      37.488  21.620   4.875  1.00 92.03           C  
ANISOU  997  CD2 TYR A 137    12031  11539  11398   -405    121   -569       C  
ATOM    998  CE1 TYR A 137      34.987  20.907   3.970  1.00 87.79           C  
ANISOU  998  CE1 TYR A 137    11434  10979  10941   -453     79   -507       C  
ATOM    999  CE2 TYR A 137      37.186  21.718   3.518  1.00 85.67           C  
ANISOU  999  CE2 TYR A 137    11239  10737  10575   -467     97   -600       C  
ATOM   1000  CZ  TYR A 137      35.932  21.359   3.077  1.00 87.68           C  
ANISOU 1000  CZ  TYR A 137    11472  10979  10861   -493     68   -575       C  
ATOM   1001  OH  TYR A 137      35.609  21.444   1.740  1.00 90.70           O  
ANISOU 1001  OH  TYR A 137    11884  11360  11216   -556     25   -605       O  
ATOM   1002  N   ILE A 138      38.665  18.049   6.375  1.00 89.48           N  
ANISOU 1002  N   ILE A 138    11608  11149  11240   -356    229   -563       N  
ATOM   1003  CA  ILE A 138      39.879  17.502   5.799  1.00 88.70           C  
ANISOU 1003  CA  ILE A 138    11515  11037  11152   -382    257   -609       C  
ATOM   1004  C   ILE A 138      40.125  18.087   4.424  1.00100.65           C  
ANISOU 1004  C   ILE A 138    13075  12557  12612   -432    243   -657       C  
ATOM   1005  O   ILE A 138      39.251  18.059   3.561  1.00 90.41           O  
ANISOU 1005  O   ILE A 138    11803  11251  11299   -468    215   -678       O  
ATOM   1006  CB  ILE A 138      39.820  15.973   5.698  1.00 92.58           C  
ANISOU 1006  CB  ILE A 138    11976  11484  11718   -387    294   -618       C  
ATOM   1007  CG1 ILE A 138      39.081  15.392   6.902  1.00 86.54           C  
ANISOU 1007  CG1 ILE A 138    11157  10711  11013   -341    304   -555       C  
ATOM   1008  CG2 ILE A 138      41.224  15.407   5.605  1.00 90.30           C  
ANISOU 1008  CG2 ILE A 138    11681  11179  11449   -381    347   -636       C  
ATOM   1009  CD1 ILE A 138      39.693  15.761   8.243  1.00 90.05           C  
ANISOU 1009  CD1 ILE A 138    11593  11183  11440   -278    317   -510       C  
ATOM   1010  N   VAL A 139      41.322  18.625   4.226  1.00 96.66           N  
ANISOU 1010  N   VAL A 139    12577  12065  12084   -433    259   -662       N  
ATOM   1011  CA  VAL A 139      41.661  19.245   2.967  1.00 93.98           C  
ANISOU 1011  CA  VAL A 139    12279  11736  11694   -466    262   -691       C  
ATOM   1012  C   VAL A 139      42.765  18.469   2.264  1.00101.32           C  
ANISOU 1012  C   VAL A 139    13215  12641  12640   -462    336   -708       C  
ATOM   1013  O   VAL A 139      43.739  18.054   2.888  1.00 88.73           O  
ANISOU 1013  O   VAL A 139    11574  11036  11101   -436    374   -676       O  
ATOM   1014  CB  VAL A 139      42.104  20.703   3.183  1.00 94.03           C  
ANISOU 1014  CB  VAL A 139    12286  11774  11668   -467    223   -662       C  
ATOM   1015  CG1 VAL A 139      42.784  21.247   1.942  1.00 90.85           C  
ANISOU 1015  CG1 VAL A 139    11906  11381  11231   -491    247   -671       C  
ATOM   1016  CG2 VAL A 139      40.897  21.560   3.569  1.00 95.72           C  
ANISOU 1016  CG2 VAL A 139    12518  12006  11846   -463    164   -650       C  
ATOM   1017  N   ASP A 140      42.589  18.258   0.964  1.00 97.89           N  
ANISOU 1017  N   ASP A 140    12845  12192  12155   -481    357   -754       N  
ATOM   1018  CA  ASP A 140      43.606  17.647   0.130  1.00 88.67           C  
ANISOU 1018  CA  ASP A 140    11711  10998  10981   -460    447   -768       C  
ATOM   1019  C   ASP A 140      44.803  18.574  -0.156  1.00106.68           C  
ANISOU 1019  C   ASP A 140    13964  13308  13261   -444    490   -714       C  
ATOM   1020  O   ASP A 140      44.983  19.040  -1.285  1.00 99.41           O  
ANISOU 1020  O   ASP A 140    13099  12397  12277   -443    521   -723       O  
ATOM   1021  CB  ASP A 140      42.992  17.201  -1.195  1.00 99.09           C  
ANISOU 1021  CB  ASP A 140    13141  12287  12223   -476    448   -836       C  
ATOM   1022  CG  ASP A 140      43.822  16.118  -1.875  1.00112.64           C  
ANISOU 1022  CG  ASP A 140    14918  13948  13931   -435    552   -864       C  
ATOM   1023  OD1 ASP A 140      44.959  15.890  -1.428  1.00109.41           O  
ANISOU 1023  OD1 ASP A 140    14448  13538  13586   -393    635   -814       O  
ATOM   1024  OD2 ASP A 140      43.346  15.489  -2.841  1.00123.95           O1-
ANISOU 1024  OD2 ASP A 140    16465  15332  15296   -441    548   -932       O1-
ATOM   1025  N   THR A 141      45.648  18.789   0.848  1.00 93.85           N  
ANISOU 1025  N   THR A 141    12253  11691  11713   -430    489   -650       N  
ATOM   1026  CA  THR A 141      46.712  19.781   0.760  1.00100.61           C  
ANISOU 1026  CA  THR A 141    13062  12568  12600   -429    496   -579       C  
ATOM   1027  C   THR A 141      47.622  19.730  -0.470  1.00 91.53           C  
ANISOU 1027  C   THR A 141    11928  11409  11439   -399    606   -549       C  
ATOM   1028  O   THR A 141      47.959  20.790  -0.997  1.00 99.62           O  
ANISOU 1028  O   THR A 141    12943  12458  12450   -408    599   -506       O  
ATOM   1029  CB  THR A 141      47.622  19.729   1.983  1.00 91.54           C  
ANISOU 1029  CB  THR A 141    11822  11410  11551   -420    473   -507       C  
ATOM   1030  CG2 THR A 141      48.392  21.027   2.081  1.00 90.08           C  
ANISOU 1030  CG2 THR A 141    11588  11237  11401   -441    419   -433       C  
ATOM   1031  OG1 THR A 141      46.827  19.550   3.166  1.00 92.92           O  
ANISOU 1031  OG1 THR A 141    11997  11586  11723   -425    397   -532       O  
ATOM   1032  N   PRO A 142      48.017  18.531  -0.945  1.00 98.11           N  
ANISOU 1032  N   PRO A 142    12793  12205  12278   -355    714   -564       N  
ATOM   1033  CA  PRO A 142      48.955  18.630  -2.073  1.00103.48           C  
ANISOU 1033  CA  PRO A 142    13495  12879  12944   -307    836   -516       C  
ATOM   1034  C   PRO A 142      48.307  19.114  -3.373  1.00109.77           C  
ANISOU 1034  C   PRO A 142    14409  13691  13608   -308    842   -571       C  
ATOM   1035  O   PRO A 142      48.976  19.137  -4.401  1.00117.12           O  
ANISOU 1035  O   PRO A 142    15384  14615  14501   -254    956   -536       O  
ATOM   1036  CB  PRO A 142      49.466  17.192  -2.249  1.00100.19           C  
ANISOU 1036  CB  PRO A 142    13107  12408  12554   -247    958   -525       C  
ATOM   1037  CG  PRO A 142      48.952  16.408  -1.073  1.00 93.64           C  
ANISOU 1037  CG  PRO A 142    12239  11561  11780   -274    890   -562       C  
ATOM   1038  CD  PRO A 142      47.748  17.121  -0.578  1.00 91.02           C  
ANISOU 1038  CD  PRO A 142    11916  11264  11403   -337    746   -612       C  
ATOM   1039  N   ARG A 143      47.026  19.460  -3.343  1.00111.23           N  
ANISOU 1039  N   ARG A 143    14646  13894  13724   -362    729   -646       N  
ATOM   1040  CA  ARG A 143      46.388  20.044  -4.516  1.00109.63           C  
ANISOU 1040  CA  ARG A 143    14544  13710  13400   -372    713   -686       C  
ATOM   1041  C   ARG A 143      45.447  21.170  -4.109  1.00114.46           C  
ANISOU 1041  C   ARG A 143    15123  14365  14000   -435    581   -690       C  
ATOM   1042  O   ARG A 143      44.610  21.601  -4.899  1.00119.51           O  
ANISOU 1042  O   ARG A 143    15839  15022  14549   -459    535   -729       O  
ATOM   1043  CB  ARG A 143      45.637  18.981  -5.312  1.00119.20           C  
ANISOU 1043  CB  ARG A 143    15900  14876  14514   -364    720   -786       C  
ATOM   1044  CG  ARG A 143      44.490  18.337  -4.556  1.00145.42           C  
ANISOU 1044  CG  ARG A 143    19217  18173  17862   -415    613   -848       C  
ATOM   1045  CD  ARG A 143      43.175  18.417  -5.336  1.00163.16           C  
ANISOU 1045  CD  ARG A 143    21570  20412  20011   -463    512   -918       C  
ATOM   1046  NE  ARG A 143      42.860  17.185  -6.060  1.00174.90           N  
ANISOU 1046  NE  ARG A 143    23193  21824  21438   -453    520   -998       N  
ATOM   1047  CZ  ARG A 143      41.705  16.952  -6.683  1.00186.36           C  
ANISOU 1047  CZ  ARG A 143    24744  23243  22821   -503    409  -1061       C  
ATOM   1048  NH1 ARG A 143      40.741  17.867  -6.674  1.00188.92           N1+
ANISOU 1048  NH1 ARG A 143    25034  23614  23135   -563    297  -1043       N1+
ATOM   1049  NH2 ARG A 143      41.511  15.799  -7.315  1.00187.04           N  
ANISOU 1049  NH2 ARG A 143    24969  23244  22856   -494    404  -1138       N  
ATOM   1050  N   ASN A 144      45.608  21.655  -2.879  1.00108.52           N  
ANISOU 1050  N   ASN A 144    14269  13627  13338   -456    521   -646       N  
ATOM   1051  CA  ASN A 144      44.769  22.722  -2.340  1.00110.11           C  
ANISOU 1051  CA  ASN A 144    14447  13857  13531   -500    409   -645       C  
ATOM   1052  C   ASN A 144      44.712  23.967  -3.224  1.00118.75           C  
ANISOU 1052  C   ASN A 144    15562  14986  14573   -515    394   -619       C  
ATOM   1053  O   ASN A 144      43.705  24.678  -3.230  1.00128.51           O  
ANISOU 1053  O   ASN A 144    16817  16242  15768   -547    315   -638       O  
ATOM   1054  CB  ASN A 144      45.257  23.133  -0.946  1.00113.77           C  
ANISOU 1054  CB  ASN A 144    14822  14319  14087   -504    358   -595       C  
ATOM   1055  CG  ASN A 144      46.430  24.093  -1.001  1.00111.28           C  
ANISOU 1055  CG  ASN A 144    14444  14008  13828   -504    364   -509       C  
ATOM   1056  ND2 ASN A 144      46.254  25.284  -0.424  1.00109.13           N  
ANISOU 1056  ND2 ASN A 144    14151  13743  13570   -532    268   -485       N  
ATOM   1057  OD1 ASN A 144      47.477  23.780  -1.577  1.00122.53           O  
ANISOU 1057  OD1 ASN A 144    15841  15424  15291   -476    456   -458       O  
ATOM   1058  N   SER A 145      45.790  24.223  -3.965  1.00118.65           N  
ANISOU 1058  N   SER A 145    15536  14977  14568   -485    479   -561       N  
ATOM   1059  CA  SER A 145      45.922  25.458  -4.741  1.00108.07           C  
ANISOU 1059  CA  SER A 145    14195  13668  13198   -493    475   -512       C  
ATOM   1060  C   SER A 145      45.285  25.353  -6.123  1.00 95.20           C  
ANISOU 1060  C   SER A 145    12680  12055  11437   -482    507   -559       C  
ATOM   1061  O   SER A 145      45.118  26.359  -6.800  1.00111.06           O  
ANISOU 1061  O   SER A 145    14701  14095  13403   -492    492   -528       O  
ATOM   1062  CB  SER A 145      47.390  25.837  -4.897  1.00114.11           C  
ANISOU 1062  CB  SER A 145    14878  14428  14050   -461    554   -402       C  
ATOM   1063  OG  SER A 145      47.982  25.047  -5.911  1.00124.18           O  
ANISOU 1063  OG  SER A 145    16208  15694  15282   -397    695   -389       O  
ATOM   1064  N   SER A 146      44.946  24.138  -6.553  1.00 98.64           N  
ANISOU 1064  N   SER A 146    13210  12463  11808   -462    544   -632       N  
ATOM   1065  CA  SER A 146      44.180  23.987  -7.792  1.00113.51           C  
ANISOU 1065  CA  SER A 146    15228  14349  13553   -462    536   -690       C  
ATOM   1066  C   SER A 146      42.846  24.741  -7.670  1.00126.69           C  
ANISOU 1066  C   SER A 146    16896  16046  15196   -530    400   -714       C  
ATOM   1067  O   SER A 146      42.139  24.603  -6.669  1.00130.36           O  
ANISOU 1067  O   SER A 146    17307  16502  15721   -567    320   -733       O  
ATOM   1068  CB  SER A 146      43.931  22.516  -8.115  1.00124.63           C  
ANISOU 1068  CB  SER A 146    16747  15702  14904   -441    563   -774       C  
ATOM   1069  OG  SER A 146      42.883  22.397  -9.064  1.00140.06           O  
ANISOU 1069  OG  SER A 146    18834  17648  16734   -469    490   -841       O  
ATOM   1070  N   PRO A 147      42.499  25.536  -8.694  1.00126.25           N  
ANISOU 1070  N   PRO A 147    16896  16022  15051   -537    383   -700       N  
ATOM   1071  CA  PRO A 147      41.436  26.542  -8.573  1.00119.80           C  
ANISOU 1071  CA  PRO A 147    16049  15237  14232   -594    271   -688       C  
ATOM   1072  C   PRO A 147      40.054  25.960  -8.218  1.00126.61           C  
ANISOU 1072  C   PRO A 147    16934  16079  15093   -644    161   -744       C  
ATOM   1073  O   PRO A 147      39.375  26.506  -7.346  1.00123.26           O  
ANISOU 1073  O   PRO A 147    16430  15665  14737   -674     93   -719       O  
ATOM   1074  CB  PRO A 147      41.427  27.201  -9.958  1.00104.85           C  
ANISOU 1074  CB  PRO A 147    14236  13377  12227   -581    292   -666       C  
ATOM   1075  CG  PRO A 147      41.993  26.173 -10.870  1.00124.15           C  
ANISOU 1075  CG  PRO A 147    16805  15790  14574   -525    384   -706       C  
ATOM   1076  CD  PRO A 147      43.019  25.440 -10.068  1.00129.80           C  
ANISOU 1076  CD  PRO A 147    17458  16475  15385   -484    474   -696       C  
ATOM   1077  N   THR A 148      39.654  24.867  -8.861  1.00116.90           N  
ANISOU 1077  N   THR A 148    15812  14810  13794   -649    144   -809       N  
ATOM   1078  CA  THR A 148      38.383  24.229  -8.538  1.00104.92           C  
ANISOU 1078  CA  THR A 148    14301  13261  12303   -703     31   -844       C  
ATOM   1079  C   THR A 148      38.390  23.705  -7.111  1.00109.25           C  
ANISOU 1079  C   THR A 148    14747  13789  12975   -699     38   -837       C  
ATOM   1080  O   THR A 148      37.401  23.817  -6.397  1.00112.83           O  
ANISOU 1080  O   THR A 148    15134  14241  13493   -731    -37   -813       O  
ATOM   1081  CB  THR A 148      38.077  23.080  -9.495  1.00124.60           C  
ANISOU 1081  CB  THR A 148    16942  15696  14704   -712     -2   -919       C  
ATOM   1082  CG2 THR A 148      36.726  22.439  -9.161  1.00126.21           C  
ANISOU 1082  CG2 THR A 148    17134  15856  14964   -780   -139   -935       C  
ATOM   1083  OG1 THR A 148      38.050  23.586 -10.833  1.00141.15           O  
ANISOU 1083  OG1 THR A 148    19156  17811  16664   -708    -12   -925       O  
ATOM   1084  N   THR A 149      39.525  23.157  -6.693  1.00105.93           N  
ANISOU 1084  N   THR A 149    14309  13352  12587   -652    135   -845       N  
ATOM   1085  CA  THR A 149      39.647  22.599  -5.356  1.00100.76           C  
ANISOU 1085  CA  THR A 149    13566  12678  12039   -641    146   -836       C  
ATOM   1086  C   THR A 149      39.634  23.690  -4.303  1.00101.96           C  
ANISOU 1086  C   THR A 149    13615  12867  12256   -640    126   -776       C  
ATOM   1087  O   THR A 149      38.947  23.568  -3.286  1.00106.35           O  
ANISOU 1087  O   THR A 149    14116  13417  12875   -645     84   -761       O  
ATOM   1088  CB  THR A 149      40.930  21.763  -5.218  1.00104.54           C  
ANISOU 1088  CB  THR A 149    14050  13129  12541   -591    255   -847       C  
ATOM   1089  CG2 THR A 149      40.962  21.052  -3.876  1.00103.48           C  
ANISOU 1089  CG2 THR A 149    13834  12972  12511   -583    256   -840       C  
ATOM   1090  OG1 THR A 149      40.962  20.783  -6.260  1.00111.00           O  
ANISOU 1090  OG1 THR A 149    14993  13901  13281   -578    283   -909       O  
ATOM   1091  N   PHE A 150      40.395  24.753  -4.548  1.00 96.68           N  
ANISOU 1091  N   PHE A 150    12929  12232  11574   -626    158   -737       N  
ATOM   1092  CA  PHE A 150      40.392  25.907  -3.667  1.00 89.72           C  
ANISOU 1092  CA  PHE A 150    11976  11371  10741   -627    123   -687       C  
ATOM   1093  C   PHE A 150      38.985  26.511  -3.542  1.00103.85           C  
ANISOU 1093  C   PHE A 150    13764  13175  12520   -654     43   -676       C  
ATOM   1094  O   PHE A 150      38.497  26.751  -2.434  1.00108.68           O  
ANISOU 1094  O   PHE A 150    14333  13779  13180   -641     14   -654       O  
ATOM   1095  CB  PHE A 150      41.363  26.965  -4.177  1.00 84.33           C  
ANISOU 1095  CB  PHE A 150    11279  10712  10051   -619    156   -640       C  
ATOM   1096  CG  PHE A 150      41.479  28.154  -3.282  1.00 93.19           C  
ANISOU 1096  CG  PHE A 150    12346  11837  11227   -622    108   -595       C  
ATOM   1097  CD1 PHE A 150      42.268  28.100  -2.144  1.00 97.84           C  
ANISOU 1097  CD1 PHE A 150    12886  12400  11889   -605    104   -574       C  
ATOM   1098  CD2 PHE A 150      40.811  29.337  -3.578  1.00 96.03           C  
ANISOU 1098  CD2 PHE A 150    12711  12217  11560   -640     58   -571       C  
ATOM   1099  CE1 PHE A 150      42.390  29.195  -1.318  1.00105.01           C  
ANISOU 1099  CE1 PHE A 150    13771  13295  12834   -607     41   -541       C  
ATOM   1100  CE2 PHE A 150      40.934  30.432  -2.753  1.00 92.23           C  
ANISOU 1100  CE2 PHE A 150    12199  11723  11122   -638     10   -536       C  
ATOM   1101  CZ  PHE A 150      41.723  30.361  -1.622  1.00104.40           C  
ANISOU 1101  CZ  PHE A 150    13711  13230  12726   -621     -3   -526       C  
ATOM   1102  N   MET A 151      38.337  26.755  -4.679  1.00 93.94           N  
ANISOU 1102  N   MET A 151    12558  11936  11199   -684     11   -682       N  
ATOM   1103  CA  MET A 151      36.997  27.333  -4.668  1.00 96.84           C  
ANISOU 1103  CA  MET A 151    12911  12316  11569   -711    -64   -652       C  
ATOM   1104  C   MET A 151      36.016  26.393  -3.968  1.00 90.26           C  
ANISOU 1104  C   MET A 151    12051  11452  10793   -718   -101   -653       C  
ATOM   1105  O   MET A 151      35.259  26.826  -3.099  1.00 88.35           O  
ANISOU 1105  O   MET A 151    11755  11210  10603   -703   -122   -605       O  
ATOM   1106  CB  MET A 151      36.513  27.645  -6.089  1.00 98.73           C  
ANISOU 1106  CB  MET A 151    13211  12575  11726   -748   -104   -653       C  
ATOM   1107  CG  MET A 151      35.034  28.077  -6.155  1.00104.45           C  
ANISOU 1107  CG  MET A 151    13911  13307  12469   -784   -192   -608       C  
ATOM   1108  SD  MET A 151      34.354  28.380  -7.809  1.00114.60           S  
ANISOU 1108  SD  MET A 151    15272  14612  13658   -837   -269   -602       S  
ATOM   1109  CE  MET A 151      35.276  29.843  -8.273  1.00126.94           C  
ANISOU 1109  CE  MET A 151    16834  16225  15174   -809   -206   -569       C  
ATOM   1110  N   SER A 152      36.050  25.105  -4.316  1.00 86.22           N  
ANISOU 1110  N   SER A 152    11578  10907  10276   -733   -102   -700       N  
ATOM   1111  CA  SER A 152      35.148  24.128  -3.694  1.00 90.59           C  
ANISOU 1111  CA  SER A 152    12095  11421  10902   -744   -142   -691       C  
ATOM   1112  C   SER A 152      35.359  24.081  -2.181  1.00100.93           C  
ANISOU 1112  C   SER A 152    13332  12729  12287   -692    -94   -660       C  
ATOM   1113  O   SER A 152      34.407  23.995  -1.409  1.00 98.26           O  
ANISOU 1113  O   SER A 152    12938  12382  12016   -680   -115   -606       O  
ATOM   1114  CB  SER A 152      35.359  22.725  -4.282  1.00 96.31           C  
ANISOU 1114  CB  SER A 152    12887  12096  11612   -764   -148   -756       C  
ATOM   1115  OG  SER A 152      35.091  22.688  -5.672  1.00 98.09           O  
ANISOU 1115  OG  SER A 152    13209  12311  11748   -806   -205   -791       O  
ATOM   1116  N   ASN A 153      36.616  24.132  -1.763  1.00 89.28           N  
ANISOU 1116  N   ASN A 153    11859  11260  10803   -657    -28   -683       N  
ATOM   1117  CA  ASN A 153      36.944  24.031  -0.350  1.00 95.33           C  
ANISOU 1117  CA  ASN A 153    12577  12019  11625   -608      5   -660       C  
ATOM   1118  C   ASN A 153      36.557  25.282   0.412  1.00 95.09           C  
ANISOU 1118  C   ASN A 153    12528  12008  11595   -576    -10   -610       C  
ATOM   1119  O   ASN A 153      36.051  25.191   1.524  1.00 96.95           O  
ANISOU 1119  O   ASN A 153    12737  12233  11868   -532     -3   -574       O  
ATOM   1120  CB  ASN A 153      38.441  23.744  -0.154  1.00 86.29           C  
ANISOU 1120  CB  ASN A 153    11436  10869  10480   -587     62   -687       C  
ATOM   1121  CG  ASN A 153      38.724  22.264  -0.066  1.00 92.48           C  
ANISOU 1121  CG  ASN A 153    12219  11619  11301   -582     98   -719       C  
ATOM   1122  ND2 ASN A 153      39.879  21.857  -0.554  1.00 85.65           N  
ANISOU 1122  ND2 ASN A 153    11375  10744  10423   -575    154   -745       N  
ATOM   1123  OD1 ASN A 153      37.903  21.493   0.428  1.00 91.90           O  
ANISOU 1123  OD1 ASN A 153    12122  11523  11275   -580     80   -709       O  
ATOM   1124  N   MET A 154      36.799  26.449  -0.173  1.00 91.02           N  
ANISOU 1124  N   MET A 154    12033  11515  11034   -591    -26   -605       N  
ATOM   1125  CA  MET A 154      36.362  27.693   0.454  1.00 82.78           C  
ANISOU 1125  CA  MET A 154    10989  10478   9987   -560    -44   -561       C  
ATOM   1126  C   MET A 154      34.830  27.712   0.570  1.00 90.69           C  
ANISOU 1126  C   MET A 154    11964  11479  11014   -551    -63   -507       C  
ATOM   1127  O   MET A 154      34.276  27.970   1.640  1.00 91.81           O  
ANISOU 1127  O   MET A 154    12096  11607  11179   -492    -45   -462       O  
ATOM   1128  CB  MET A 154      36.882  28.903  -0.335  1.00 86.20           C  
ANISOU 1128  CB  MET A 154    11442  10929  10379   -584    -61   -559       C  
ATOM   1129  CG  MET A 154      38.373  29.154  -0.187  1.00 91.61           C  
ANISOU 1129  CG  MET A 154    12131  11606  11069   -582    -45   -575       C  
ATOM   1130  SD  MET A 154      38.800  29.688   1.489  1.00106.59           S  
ANISOU 1130  SD  MET A 154    14042  13464  12992   -528    -70   -561       S  
ATOM   1131  CE  MET A 154      37.696  31.083   1.628  1.00131.05           C  
ANISOU 1131  CE  MET A 154    17173  16559  16063   -505   -102   -525       C  
ATOM   1132  N   LEU A 155      34.149  27.388  -0.519  1.00 93.08           N  
ANISOU 1132  N   LEU A 155    12260  11791  11315   -606    -99   -503       N  
ATOM   1133  CA  LEU A 155      32.685  27.395  -0.536  1.00 92.09           C  
ANISOU 1133  CA  LEU A 155    12091  11661  11238   -611   -132   -431       C  
ATOM   1134  C   LEU A 155      32.053  26.358   0.408  1.00 97.73           C  
ANISOU 1134  C   LEU A 155    12754  12346  12033   -578   -112   -390       C  
ATOM   1135  O   LEU A 155      31.131  26.673   1.150  1.00100.59           O  
ANISOU 1135  O   LEU A 155    13073  12703  12445   -527    -91   -304       O  
ATOM   1136  CB  LEU A 155      32.205  27.147  -1.954  1.00 98.89           C  
ANISOU 1136  CB  LEU A 155    12966  12528  12079   -690   -201   -439       C  
ATOM   1137  CG  LEU A 155      30.760  27.494  -2.245  1.00 99.16           C  
ANISOU 1137  CG  LEU A 155    12949  12563  12165   -713   -258   -347       C  
ATOM   1138  CD1 LEU A 155      30.541  28.941  -1.916  1.00104.20           C  
ANISOU 1138  CD1 LEU A 155    13576  13224  12790   -668   -229   -292       C  
ATOM   1139  CD2 LEU A 155      30.511  27.244  -3.701  1.00112.42           C  
ANISOU 1139  CD2 LEU A 155    14669  14244  13802   -797   -347   -372       C  
ATOM   1140  N   TYR A 156      32.547  25.118   0.390  1.00101.66           N  
ANISOU 1140  N   TYR A 156    13255  12823  12548   -598   -109   -440       N  
ATOM   1141  CA  TYR A 156      31.999  24.092   1.281  1.00 90.68           C  
ANISOU 1141  CA  TYR A 156    11808  11401  11244   -567    -88   -394       C  
ATOM   1142  C   TYR A 156      32.270  24.397   2.761  1.00 92.09           C  
ANISOU 1142  C   TYR A 156    11982  11584  11425   -470    -14   -363       C  
ATOM   1143  O   TYR A 156      31.380  24.277   3.612  1.00 98.88           O  
ANISOU 1143  O   TYR A 156    12793  12432  12345   -411     19   -274       O  
ATOM   1144  CB  TYR A 156      32.551  22.705   0.928  1.00 97.90           C  
ANISOU 1144  CB  TYR A 156    12737  12285  12177   -607    -99   -460       C  
ATOM   1145  CG  TYR A 156      32.016  22.123  -0.366  1.00 90.28           C  
ANISOU 1145  CG  TYR A 156    11793  11291  11217   -693   -186   -483       C  
ATOM   1146  CD1 TYR A 156      30.657  22.160  -0.669  1.00108.50           C  
ANISOU 1146  CD1 TYR A 156    14048  13583  13594   -731   -261   -399       C  
ATOM   1147  CD2 TYR A 156      32.872  21.529  -1.284  1.00102.52           C  
ANISOU 1147  CD2 TYR A 156    13425  12825  12703   -732   -196   -580       C  
ATOM   1148  CE1 TYR A 156      30.175  21.626  -1.853  1.00105.92           C  
ANISOU 1148  CE1 TYR A 156    13757  13220  13269   -818   -369   -421       C  
ATOM   1149  CE2 TYR A 156      32.404  21.005  -2.472  1.00104.67           C  
ANISOU 1149  CE2 TYR A 156    13753  13061  12957   -804   -286   -611       C  
ATOM   1150  CZ  TYR A 156      31.055  21.048  -2.750  1.00107.85           C  
ANISOU 1150  CZ  TYR A 156    14110  13444  13425   -853   -385   -536       C  
ATOM   1151  OH  TYR A 156      30.598  20.512  -3.933  1.00110.56           O  
ANISOU 1151  OH  TYR A 156    14524  13740  13745   -932   -501   -569       O  
ATOM   1152  N   ALA A 157      33.507  24.770   3.062  1.00 86.01           N  
ANISOU 1152  N   ALA A 157    11266  10824  10591   -450     10   -427       N  
ATOM   1153  CA  ALA A 157      33.916  25.077   4.424  1.00 90.09           C  
ANISOU 1153  CA  ALA A 157    11806  11334  11088   -365     55   -413       C  
ATOM   1154  C   ALA A 157      33.094  26.215   5.014  1.00 92.74           C  
ANISOU 1154  C   ALA A 157    12162  11671  11404   -296     73   -345       C  
ATOM   1155  O   ALA A 157      32.560  26.102   6.117  1.00 89.94           O  
ANISOU 1155  O   ALA A 157    11806  11301  11064   -208    124   -284       O  
ATOM   1156  CB  ALA A 157      35.416  25.428   4.457  1.00 84.52           C  
ANISOU 1156  CB  ALA A 157    11152  10632  10329   -377     46   -484       C  
ATOM   1157  N   CYS A 158      33.001  27.324   4.289  1.00 90.71           N  
ANISOU 1157  N   CYS A 158    11930  11427  11109   -325     42   -351       N  
ATOM   1158  CA  CYS A 158      32.218  28.449   4.782  1.00 89.99           C  
ANISOU 1158  CA  CYS A 158    11865  11328  10999   -255     66   -286       C  
ATOM   1159  C   CYS A 158      30.729  28.096   4.935  1.00 98.50           C  
ANISOU 1159  C   CYS A 158    12868  12402  12156   -219    102   -172       C  
ATOM   1160  O   CYS A 158      30.066  28.581   5.856  1.00 92.56           O  
ANISOU 1160  O   CYS A 158    12134  11633  11402   -116    165    -96       O  
ATOM   1161  CB  CYS A 158      32.412  29.654   3.863  1.00 87.03           C  
ANISOU 1161  CB  CYS A 158    11518  10966  10582   -303     23   -308       C  
ATOM   1162  SG  CYS A 158      34.097  30.363   3.969  1.00 94.95           S  
ANISOU 1162  SG  CYS A 158    12601  11958  11517   -321    -14   -400       S  
ATOM   1163  N   SER A 159      30.223  27.223   4.063  1.00107.88           N  
ANISOU 1163  N   SER A 159    13977  13597  13415   -299     61   -154       N  
ATOM   1164  CA  SER A 159      28.819  26.796   4.113  1.00100.44           C  
ANISOU 1164  CA  SER A 159    12939  12642  12580   -285     72    -28       C  
ATOM   1165  C   SER A 159      28.517  26.007   5.377  1.00107.79           C  
ANISOU 1165  C   SER A 159    13838  13552  13565   -193    150     40       C  
ATOM   1166  O   SER A 159      27.457  26.159   5.986  1.00108.05           O  
ANISOU 1166  O   SER A 159    13818  13573  13663   -111    213    172       O  
ATOM   1167  CB  SER A 159      28.471  25.950   2.887  1.00 95.62           C  
ANISOU 1167  CB  SER A 159    12270  12028  12033   -405    -21    -36       C  
ATOM   1168  OG  SER A 159      28.637  26.710   1.702  1.00115.04           O  
ANISOU 1168  OG  SER A 159    14766  14510  14434   -479    -87    -82       O  
ATOM   1169  N   ILE A 160      29.458  25.149   5.747  1.00104.61           N  
ANISOU 1169  N   ILE A 160    13461  13144  13141   -200    153    -40       N  
ATOM   1170  CA  ILE A 160      29.382  24.367   6.973  1.00 96.81           C  
ANISOU 1170  CA  ILE A 160    12454  12140  12189   -112    227     12       C  
ATOM   1171  C   ILE A 160      29.402  25.240   8.222  1.00 94.29           C  
ANISOU 1171  C   ILE A 160    12219  11818  11790     28    312     46       C  
ATOM   1172  O   ILE A 160      28.543  25.099   9.091  1.00 94.94           O  
ANISOU 1172  O   ILE A 160    12270  11888  11916    134    397    166       O  
ATOM   1173  CB  ILE A 160      30.553  23.375   7.062  1.00 96.63           C  
ANISOU 1173  CB  ILE A 160    12452  12115  12149   -152    208    -90       C  
ATOM   1174  CG1 ILE A 160      30.390  22.264   6.026  1.00 88.08           C  
ANISOU 1174  CG1 ILE A 160    11300  11015  11151   -263    142   -111       C  
ATOM   1175  CG2 ILE A 160      30.648  22.813   8.465  1.00 95.17           C  
ANISOU 1175  CG2 ILE A 160    12272  11919  11970    -45    288    -43       C  
ATOM   1176  CD1 ILE A 160      31.681  21.585   5.706  1.00100.92           C  
ANISOU 1176  CD1 ILE A 160    12968  12638  12737   -316    120   -231       C  
ATOM   1177  N   LEU A 161      30.409  26.113   8.313  1.00 88.94           N  
ANISOU 1177  N   LEU A 161    11654  11145  10996     31    286    -53       N  
ATOM   1178  CA  LEU A 161      30.512  27.093   9.397  1.00 90.63           C  
ANISOU 1178  CA  LEU A 161    11985  11338  11110    154    337    -43       C  
ATOM   1179  C   LEU A 161      29.200  27.851   9.577  1.00104.46           C  
ANISOU 1179  C   LEU A 161    13726  13079  12884    243    409     79       C  
ATOM   1180  O   LEU A 161      28.708  28.025  10.696  1.00105.37           O  
ANISOU 1180  O   LEU A 161    13896  13173  12969    386    505    157       O  
ATOM   1181  CB  LEU A 161      31.643  28.083   9.116  1.00 93.34           C  
ANISOU 1181  CB  LEU A 161    12432  11677  11356    109    263   -157       C  
ATOM   1182  CG  LEU A 161      33.016  27.588   9.556  1.00104.75           C  
ANISOU 1182  CG  LEU A 161    13925  13116  12759     84    219   -247       C  
ATOM   1183  CD1 LEU A 161      34.084  28.633   9.281  1.00 97.20           C  
ANISOU 1183  CD1 LEU A 161    13054  12145  11733     38    139   -332       C  
ATOM   1184  CD2 LEU A 161      32.961  27.261  11.032  1.00114.55           C  
ANISOU 1184  CD2 LEU A 161    15236  14333  13955    211    279   -210       C  
ATOM   1185  N   TYR A 162      28.628  28.271   8.458  1.00102.96           N  
ANISOU 1185  N   TYR A 162    13466  12904  12749    163    367    105       N  
ATOM   1186  CA  TYR A 162      27.376  29.028   8.465  1.00105.80           C  
ANISOU 1186  CA  TYR A 162    13795  13254  13150    234    430    235       C  
ATOM   1187  C   TYR A 162      26.155  28.198   8.864  1.00109.68           C  
ANISOU 1187  C   TYR A 162    14161  13739  13773    295    509    402       C  
ATOM   1188  O   TYR A 162      25.441  28.561   9.795  1.00107.26           O  
ANISOU 1188  O   TYR A 162    13879  13411  13464    445    627    517       O  
ATOM   1189  CB  TYR A 162      27.161  29.641   7.089  1.00103.00           C  
ANISOU 1189  CB  TYR A 162    13391  12920  12824    119    347    221       C  
ATOM   1190  CG  TYR A 162      25.858  30.373   6.897  1.00113.27           C  
ANISOU 1190  CG  TYR A 162    14632  14213  14192    168    396    366       C  
ATOM   1191  CD1 TYR A 162      25.743  31.724   7.208  1.00102.02           C  
ANISOU 1191  CD1 TYR A 162    13304  12768  12692    256    446    378       C  
ATOM   1192  CD2 TYR A 162      24.750  29.721   6.368  1.00116.53           C  
ANISOU 1192  CD2 TYR A 162    14890  14632  14753    123    383    498       C  
ATOM   1193  CE1 TYR A 162      24.544  32.401   7.013  1.00100.17           C  
ANISOU 1193  CE1 TYR A 162    13007  12525  12528    307    502    524       C  
ATOM   1194  CE2 TYR A 162      23.556  30.380   6.171  1.00113.61           C  
ANISOU 1194  CE2 TYR A 162    14447  14255  14465    165    424    652       C  
ATOM   1195  CZ  TYR A 162      23.455  31.721   6.492  1.00115.11           C  
ANISOU 1195  CZ  TYR A 162    14729  14431  14577    261    493    667       C  
ATOM   1196  OH  TYR A 162      22.263  32.370   6.289  1.00104.32           O  
ANISOU 1196  OH  TYR A 162    13282  13054  13300    309    545    832       O  
ATOM   1197  N   LYS A 163      25.920  27.087   8.169  1.00 96.81           N  
ANISOU 1197  N   LYS A 163    12404  12120  12260    186    445    421       N  
ATOM   1198  CA  LYS A 163      24.700  26.326   8.373  1.00 94.43           C  
ANISOU 1198  CA  LYS A 163    11957  11803  12119    218    493    598       C  
ATOM   1199  C   LYS A 163      24.750  25.481   9.636  1.00108.34           C  
ANISOU 1199  C   LYS A 163    13719  13552  13895    331    593    651       C  
ATOM   1200  O   LYS A 163      23.722  25.223  10.254  1.00111.92           O  
ANISOU 1200  O   LYS A 163    14086  13989  14452    432    692    830       O  
ATOM   1201  CB  LYS A 163      24.401  25.428   7.169  1.00105.39           C  
ANISOU 1201  CB  LYS A 163    13222  13190  13633     54    364    600       C  
ATOM   1202  CG  LYS A 163      22.944  24.978   7.137  1.00142.82           C  
ANISOU 1202  CG  LYS A 163    17794  17905  18567     65    381    813       C  
ATOM   1203  CD  LYS A 163      22.660  23.854   6.150  1.00158.91           C  
ANISOU 1203  CD  LYS A 163    19722  19918  20737    -93    237    818       C  
ATOM   1204  CE  LYS A 163      21.186  23.453   6.246  1.00162.43           C  
ANISOU 1204  CE  LYS A 163    19986  20328  21400    -77    246   1058       C  
ATOM   1205  NZ  LYS A 163      20.754  22.477   5.207  1.00165.48           N1+
ANISOU 1205  NZ  LYS A 163    20272  20673  21931   -243     72   1079       N1+
ATOM   1206  N   THR A 164      25.933  25.025  10.022  1.00105.63           N  
ANISOU 1206  N   THR A 164    13462  13214  13457    318    571    513       N  
ATOM   1207  CA  THR A 164      26.020  24.179  11.204  1.00 99.30           C  
ANISOU 1207  CA  THR A 164    12662  12403  12665    422    659    564       C  
ATOM   1208  C   THR A 164      26.186  25.012  12.456  1.00 95.87           C  
ANISOU 1208  C   THR A 164    12379  11959  12086    598    770    575       C  
ATOM   1209  O   THR A 164      25.704  24.633  13.524  1.00104.06           O  
ANISOU 1209  O   THR A 164    13413  12985  13139    740    890    693       O  
ATOM   1210  CB  THR A 164      27.193  23.182  11.132  1.00114.34           C  
ANISOU 1210  CB  THR A 164    14582  14313  14547    335    589    429       C  
ATOM   1211  CG2 THR A 164      27.091  22.327   9.873  1.00103.38           C  
ANISOU 1211  CG2 THR A 164    13079  12921  13279    169    477    400       C  
ATOM   1212  OG1 THR A 164      28.438  23.902  11.146  1.00107.58           O  
ANISOU 1212  OG1 THR A 164    13872  13469  13534    317    541    270       O  
ATOM   1213  N   LYS A 165      26.877  26.140  12.318  1.00 96.82           N  
ANISOU 1213  N   LYS A 165    12643  12079  12067    592    726    456       N  
ATOM   1214  CA  LYS A 165      27.211  26.969  13.466  1.00 99.75           C  
ANISOU 1214  CA  LYS A 165    13200  12425  12277    745    796    433       C  
ATOM   1215  C   LYS A 165      27.927  26.116  14.510  1.00109.18           C  
ANISOU 1215  C   LYS A 165    14452  13616  13414    804    818    400       C  
ATOM   1216  O   LYS A 165      27.605  26.161  15.695  1.00110.47           O  
ANISOU 1216  O   LYS A 165    14704  13759  13510    974    931    477       O  
ATOM   1217  CB  LYS A 165      25.948  27.618  14.054  1.00113.53           C  
ANISOU 1217  CB  LYS A 165    14958  14145  14032    914    943    600       C  
ATOM   1218  CG  LYS A 165      25.312  28.681  13.160  1.00108.22           C  
ANISOU 1218  CG  LYS A 165    14256  13470  13394    876    925    633       C  
ATOM   1219  CD  LYS A 165      24.083  29.310  13.820  1.00125.56           C  
ANISOU 1219  CD  LYS A 165    16466  15636  15604   1064   1092    815       C  
ATOM   1220  CE  LYS A 165      23.693  30.638  13.157  1.00134.79           C  
ANISOU 1220  CE  LYS A 165    17669  16790  16756   1054   1081    820       C  
ATOM   1221  NZ  LYS A 165      23.254  30.511  11.731  1.00136.19           N1+
ANISOU 1221  NZ  LYS A 165    17660  17001  17086    879    979    850       N1+
ATOM   1222  N   LEU A 166      28.882  25.313  14.045  1.00109.42           N  
ANISOU 1222  N   LEU A 166    14435  13666  13472    670    717    293       N  
ATOM   1223  CA  LEU A 166      29.690  24.472  14.920  1.00104.10           C  
ANISOU 1223  CA  LEU A 166    13805  12993  12756    704    720    255       C  
ATOM   1224  C   LEU A 166      31.156  24.851  14.794  1.00100.62           C  
ANISOU 1224  C   LEU A 166    13474  12548  12210    622    600     90       C  
ATOM   1225  O   LEU A 166      31.561  25.372  13.763  1.00108.76           O  
ANISOU 1225  O   LEU A 166    14489  13585  13248    503    512      9       O  
ATOM   1226  CB  LEU A 166      29.487  22.996  14.574  1.00 95.91           C  
ANISOU 1226  CB  LEU A 166    12593  11972  11877    628    722    305       C  
ATOM   1227  CG  LEU A 166      28.257  22.346  15.200  1.00108.25           C  
ANISOU 1227  CG  LEU A 166    14054  13528  13547    742    849    492       C  
ATOM   1228  CD1 LEU A 166      28.024  20.967  14.624  1.00105.73           C  
ANISOU 1228  CD1 LEU A 166    13553  13211  13408    635    817    533       C  
ATOM   1229  CD2 LEU A 166      28.426  22.276  16.708  1.00109.61           C  
ANISOU 1229  CD2 LEU A 166    14345  13692  13609    919    952    538       C  
ATOM   1230  N   PRO A 167      31.957  24.594  15.844  1.00108.99           N  
ANISOU 1230  N   PRO A 167    14639  13596  13178    687    594     54       N  
ATOM   1231  CA  PRO A 167      33.407  24.843  15.793  1.00104.60           C  
ANISOU 1231  CA  PRO A 167    14165  13030  12550    604    469    -79       C  
ATOM   1232  C   PRO A 167      34.064  24.010  14.706  1.00 97.62           C  
ANISOU 1232  C   PRO A 167    13138  12174  11779    441    402   -137       C  
ATOM   1233  O   PRO A 167      33.654  22.884  14.499  1.00 93.09           O  
ANISOU 1233  O   PRO A 167    12438  11619  11314    418    449    -85       O  
ATOM   1234  CB  PRO A 167      33.908  24.395  17.172  1.00105.52           C  
ANISOU 1234  CB  PRO A 167    14386  13130  12578    710    486    -68       C  
ATOM   1235  CG  PRO A 167      32.696  24.247  18.018  1.00114.26           C  
ANISOU 1235  CG  PRO A 167    15513  14233  13669    878    633     63       C  
ATOM   1236  CD  PRO A 167      31.548  23.954  17.105  1.00114.83           C  
ANISOU 1236  CD  PRO A 167    15409  14329  13892    838    702    152       C  
ATOM   1237  N   MET A 168      35.070  24.539  14.028  1.00 98.70           N  
ANISOU 1237  N   MET A 168    13300  12308  11895    335    299   -236       N  
ATOM   1238  CA  MET A 168      35.663  23.799  12.922  1.00 92.57           C  
ANISOU 1238  CA  MET A 168    12403  11554  11214    198    257   -284       C  
ATOM   1239  C   MET A 168      37.169  23.800  12.982  1.00 96.33           C  
ANISOU 1239  C   MET A 168    12914  12021  11667    137    171   -359       C  
ATOM   1240  O   MET A 168      37.777  24.831  13.226  1.00106.44           O  
ANISOU 1240  O   MET A 168    14295  13276  12871    140     99   -398       O  
ATOM   1241  CB  MET A 168      35.205  24.387  11.591  1.00 96.25           C  
ANISOU 1241  CB  MET A 168    12820  12034  11717    114    235   -302       C  
ATOM   1242  CG  MET A 168      36.066  24.023  10.397  1.00 89.07           C  
ANISOU 1242  CG  MET A 168    11845  11139  10858    -16    179   -373       C  
ATOM   1243  SD  MET A 168      35.054  24.162   8.929  1.00105.87           S  
ANISOU 1243  SD  MET A 168    13897  13286  13043    -92    179   -359       S  
ATOM   1244  CE  MET A 168      36.201  24.705   7.716  1.00 89.66           C  
ANISOU 1244  CE  MET A 168    11856  11243  10967   -199    110   -447       C  
ATOM   1245  N   ILE A 169      37.767  22.633  12.764  1.00 95.27           N  
ANISOU 1245  N   ILE A 169    12690  11898  11609     84    177   -369       N  
ATOM   1246  CA  ILE A 169      39.211  22.536  12.602  1.00 90.94           C  
ANISOU 1246  CA  ILE A 169    12138  11343  11073     14    108   -419       C  
ATOM   1247  C   ILE A 169      39.507  22.233  11.150  1.00 95.75           C  
ANISOU 1247  C   ILE A 169    12656  11968  11755    -93    108   -457       C  
ATOM   1248  O   ILE A 169      39.101  21.195  10.643  1.00 96.11           O  
ANISOU 1248  O   ILE A 169    12622  12023  11871   -117    161   -449       O  
ATOM   1249  CB  ILE A 169      39.808  21.439  13.491  1.00 90.88           C  
ANISOU 1249  CB  ILE A 169    12106  11332  11092     46    123   -395       C  
ATOM   1250  CG1 ILE A 169      39.521  21.757  14.955  1.00 93.78           C  
ANISOU 1250  CG1 ILE A 169    12587  11681  11362    166    122   -356       C  
ATOM   1251  CG2 ILE A 169      41.321  21.265  13.239  1.00 87.80           C  
ANISOU 1251  CG2 ILE A 169    11684  10932  10742    -30     57   -425       C  
ATOM   1252  CD1 ILE A 169      39.699  20.543  15.845  1.00101.10           C  
ANISOU 1252  CD1 ILE A 169    13478  12614  12320    217    166   -309       C  
ATOM   1253  N   VAL A 170      40.191  23.143  10.468  1.00 92.83           N  
ANISOU 1253  N   VAL A 170    12309  11595  11368   -152     49   -494       N  
ATOM   1254  CA  VAL A 170      40.599  22.862   9.099  1.00 90.00           C  
ANISOU 1254  CA  VAL A 170    11881  11250  11063   -239     60   -525       C  
ATOM   1255  C   VAL A 170      41.851  21.995   9.134  1.00 90.77           C  
ANISOU 1255  C   VAL A 170    11927  11340  11220   -266     66   -526       C  
ATOM   1256  O   VAL A 170      42.870  22.368   9.707  1.00 99.73           O  
ANISOU 1256  O   VAL A 170    13080  12458  12355   -268      9   -514       O  
ATOM   1257  CB  VAL A 170      40.847  24.142   8.296  1.00 92.86           C  
ANISOU 1257  CB  VAL A 170    12273  11615  11393   -284     11   -546       C  
ATOM   1258  CG1 VAL A 170      41.350  23.783   6.906  1.00 96.00           C  
ANISOU 1258  CG1 VAL A 170    12613  12028  11834   -356     38   -570       C  
ATOM   1259  CG2 VAL A 170      39.539  24.970   8.213  1.00 93.25           C  
ANISOU 1259  CG2 VAL A 170    12367  11671  11393   -254     15   -536       C  
ATOM   1260  N   VAL A 171      41.753  20.808   8.554  1.00 94.21           N  
ANISOU 1260  N   VAL A 171    12301  11780  11714   -287    130   -535       N  
ATOM   1261  CA  VAL A 171      42.852  19.875   8.619  1.00 83.85           C  
ANISOU 1261  CA  VAL A 171    10937  10455  10466   -299    156   -527       C  
ATOM   1262  C   VAL A 171      43.540  19.812   7.273  1.00 87.69           C  
ANISOU 1262  C   VAL A 171    11397  10942  10980   -355    187   -551       C  
ATOM   1263  O   VAL A 171      43.044  19.161   6.353  1.00 90.55           O  
ANISOU 1263  O   VAL A 171    11754  11301  11350   -374    236   -583       O  
ATOM   1264  CB  VAL A 171      42.369  18.490   9.021  1.00 86.97           C  
ANISOU 1264  CB  VAL A 171    11291  10841  10912   -270    216   -514       C  
ATOM   1265  CG1 VAL A 171      43.557  17.547   9.152  1.00 97.78           C  
ANISOU 1265  CG1 VAL A 171    12607  12194  12352   -275    249   -498       C  
ATOM   1266  CG2 VAL A 171      41.579  18.568  10.328  1.00 85.54           C  
ANISOU 1266  CG2 VAL A 171    11138  10664  10699   -198    206   -473       C  
ATOM   1267  N   PHE A 172      44.666  20.517   7.136  1.00 84.33           N  
ANISOU 1267  N   PHE A 172    10961  10512  10567   -377    153   -529       N  
ATOM   1268  CA  PHE A 172      45.496  20.345   5.948  1.00 85.34           C  
ANISOU 1268  CA  PHE A 172    11056  10638  10731   -409    208   -528       C  
ATOM   1269  C   PHE A 172      46.177  18.992   6.037  1.00 86.82           C  
ANISOU 1269  C   PHE A 172    11191  10805  10991   -391    283   -510       C  
ATOM   1270  O   PHE A 172      47.192  18.848   6.696  1.00 94.75           O  
ANISOU 1270  O   PHE A 172    12146  11797  12058   -384    270   -453       O  
ATOM   1271  CB  PHE A 172      46.513  21.475   5.802  1.00 90.62           C  
ANISOU 1271  CB  PHE A 172    11708  11304  11419   -435    156   -482       C  
ATOM   1272  CG  PHE A 172      45.888  22.759   5.385  1.00 96.08           C  
ANISOU 1272  CG  PHE A 172    12451  12010  12045   -455    102   -503       C  
ATOM   1273  CD1 PHE A 172      45.297  22.868   4.138  1.00 87.31           C  
ANISOU 1273  CD1 PHE A 172    11363  10920  10890   -471    150   -539       C  
ATOM   1274  CD2 PHE A 172      45.835  23.840   6.252  1.00 96.81           C  
ANISOU 1274  CD2 PHE A 172    12582  12090  12113   -454     -2   -489       C  
ATOM   1275  CE1 PHE A 172      44.684  24.047   3.748  1.00 92.58           C  
ANISOU 1275  CE1 PHE A 172    12071  11603  11503   -489    103   -551       C  
ATOM   1276  CE2 PHE A 172      45.237  25.028   5.869  1.00 97.41           C  
ANISOU 1276  CE2 PHE A 172    12706  12172  12133   -468    -45   -506       C  
ATOM   1277  CZ  PHE A 172      44.657  25.133   4.614  1.00 96.85           C  
ANISOU 1277  CZ  PHE A 172    12638  12130  12031   -487     11   -533       C  
ATOM   1278  N   ASN A 173      45.578  17.997   5.385  1.00 90.83           N  
ANISOU 1278  N   ASN A 173    11714  11302  11495   -387    352   -555       N  
ATOM   1279  CA  ASN A 173      46.054  16.620   5.432  1.00 86.18           C  
ANISOU 1279  CA  ASN A 173    11089  10682  10972   -365    430   -547       C  
ATOM   1280  C   ASN A 173      47.245  16.316   4.510  1.00100.46           C  
ANISOU 1280  C   ASN A 173    12878  12472  12820   -358    518   -524       C  
ATOM   1281  O   ASN A 173      47.555  17.096   3.620  1.00104.25           O  
ANISOU 1281  O   ASN A 173    13379  12965  13266   -372    529   -521       O  
ATOM   1282  CB  ASN A 173      44.890  15.693   5.080  1.00 95.04           C  
ANISOU 1282  CB  ASN A 173    12249  11784  12080   -365    454   -605       C  
ATOM   1283  CG  ASN A 173      45.173  14.235   5.405  1.00106.68           C  
ANISOU 1283  CG  ASN A 173    13688  13216  13630   -339    519   -598       C  
ATOM   1284  ND2 ASN A 173      44.426  13.336   4.762  1.00100.84           N  
ANISOU 1284  ND2 ASN A 173    12989  12436  12890   -348    543   -651       N  
ATOM   1285  OD1 ASN A 173      46.042  13.916   6.224  1.00104.25           O  
ANISOU 1285  OD1 ASN A 173    13320  12907  13384   -314    537   -542       O  
ATOM   1286  N   LYS A 174      47.886  15.164   4.719  1.00 95.31           N  
ANISOU 1286  N   LYS A 174    12184  11787  12241   -329    593   -498       N  
ATOM   1287  CA  LYS A 174      49.034  14.698   3.922  1.00 95.89           C  
ANISOU 1287  CA  LYS A 174    12236  11833  12364   -301    706   -460       C  
ATOM   1288  C   LYS A 174      50.251  15.650   3.935  1.00100.89           C  
ANISOU 1288  C   LYS A 174    12799  12485  13052   -306    697   -361       C  
ATOM   1289  O   LYS A 174      50.855  15.881   2.880  1.00 96.57           O  
ANISOU 1289  O   LYS A 174    12259  11931  12501   -289    779   -334       O  
ATOM   1290  CB  LYS A 174      48.630  14.455   2.453  1.00 92.50           C  
ANISOU 1290  CB  LYS A 174    11909  11383  11855   -292    779   -533       C  
ATOM   1291  CG  LYS A 174      47.204  14.001   2.227  1.00100.29           C  
ANISOU 1291  CG  LYS A 174    12978  12353  12773   -314    732   -631       C  
ATOM   1292  CD  LYS A 174      46.901  13.784   0.738  1.00102.00           C  
ANISOU 1292  CD  LYS A 174    13316  12538  12901   -309    783   -703       C  
ATOM   1293  CE  LYS A 174      45.494  13.208   0.540  1.00101.09           C  
ANISOU 1293  CE  LYS A 174    13275  12391  12744   -343    712   -789       C  
ATOM   1294  NZ  LYS A 174      45.121  13.057  -0.901  1.00 99.26           N1+
ANISOU 1294  NZ  LYS A 174    13184  12121  12408   -346    726   -865       N1+
ATOM   1295  N   THR A 175      50.624  16.182   5.104  1.00 97.36           N  
ANISOU 1295  N   THR A 175    12286  12051  12655   -327    596   -299       N  
ATOM   1296  CA  THR A 175      51.763  17.100   5.177  1.00 98.22           C  
ANISOU 1296  CA  THR A 175    12320  12163  12837   -346    555   -194       C  
ATOM   1297  C   THR A 175      53.078  16.379   4.923  1.00 97.83           C  
ANISOU 1297  C   THR A 175    12176  12084  12911   -311    667    -87       C  
ATOM   1298  O   THR A 175      54.091  17.017   4.677  1.00 99.16           O  
ANISOU 1298  O   THR A 175    12268  12247  13162   -320    667     20       O  
ATOM   1299  CB  THR A 175      51.855  17.846   6.547  1.00 93.38           C  
ANISOU 1299  CB  THR A 175    11683  11556  12242   -380    391   -156       C  
ATOM   1300  CG2 THR A 175      50.686  18.810   6.714  1.00 93.62           C  
ANISOU 1300  CG2 THR A 175    11809  11610  12154   -402    294   -240       C  
ATOM   1301  OG1 THR A 175      51.849  16.903   7.628  1.00 99.13           O  
ANISOU 1301  OG1 THR A 175    12388  12274  13005   -359    379   -145       O  
ATOM   1302  N   ASP A 176      53.058  15.049   4.950  1.00 98.78           N  
ANISOU 1302  N   ASP A 176    12297  12179  13056   -268    767   -107       N  
ATOM   1303  CA  ASP A 176      54.269  14.285   4.668  1.00103.85           C  
ANISOU 1303  CA  ASP A 176    12854  12786  13817   -221    897     -1       C  
ATOM   1304  C   ASP A 176      54.785  14.514   3.241  1.00106.34           C  
ANISOU 1304  C   ASP A 176    13191  13092  14122   -180   1034     30       C  
ATOM   1305  O   ASP A 176      55.971  14.294   2.973  1.00119.38           O  
ANISOU 1305  O   ASP A 176    14750  14719  15889   -137   1138    160       O  
ATOM   1306  CB  ASP A 176      54.030  12.795   4.901  1.00 99.66           C  
ANISOU 1306  CB  ASP A 176    12340  12222  13304   -177    985    -42       C  
ATOM   1307  CG  ASP A 176      52.861  12.265   4.100  1.00113.06           C  
ANISOU 1307  CG  ASP A 176    14174  13904  14878   -163   1035   -188       C  
ATOM   1308  OD1 ASP A 176      51.715  12.330   4.603  1.00113.71           O  
ANISOU 1308  OD1 ASP A 176    14308  14005  14891   -199    936   -274       O  
ATOM   1309  OD2 ASP A 176      53.089  11.799   2.959  1.00107.05           O1-
ANISOU 1309  OD2 ASP A 176    13476  13108  14090   -114   1170   -208       O1-
ATOM   1310  N   VAL A 177      53.914  14.952   2.327  1.00 99.64           N  
ANISOU 1310  N   VAL A 177    12461  12260  13139   -185   1040    -75       N  
ATOM   1311  CA  VAL A 177      54.378  15.322   0.985  1.00 89.97           C  
ANISOU 1311  CA  VAL A 177    11270  11031  11884   -140   1161    -40       C  
ATOM   1312  C   VAL A 177      54.161  16.802   0.669  1.00 96.73           C  
ANISOU 1312  C   VAL A 177    12130  11929  12694   -190   1066    -32       C  
ATOM   1313  O   VAL A 177      54.186  17.207  -0.495  1.00107.92           O  
ANISOU 1313  O   VAL A 177    13606  13354  14045   -159   1147    -33       O  
ATOM   1314  CB  VAL A 177      53.699  14.491  -0.120  1.00 95.22           C  
ANISOU 1314  CB  VAL A 177    12093  11666  12421    -87   1277   -160       C  
ATOM   1315  CG1 VAL A 177      54.035  12.995   0.028  1.00103.41           C  
ANISOU 1315  CG1 VAL A 177    13137  12644  13511    -26   1394   -162       C  
ATOM   1316  CG2 VAL A 177      52.188  14.721  -0.113  1.00 97.93           C  
ANISOU 1316  CG2 VAL A 177    12547  12030  12631   -145   1152   -310       C  
ATOM   1317  N   CYS A 178      53.958  17.619   1.692  1.00 92.61           N  
ANISOU 1317  N   CYS A 178    11556  11430  12202   -260    896    -21       N  
ATOM   1318  CA  CYS A 178      53.775  19.045   1.438  1.00 91.78           C  
ANISOU 1318  CA  CYS A 178    11456  11354  12063   -307    801    -10       C  
ATOM   1319  C   CYS A 178      54.826  19.900   2.107  1.00105.48           C  
ANISOU 1319  C   CYS A 178    13058  13079  13941   -347    705    134       C  
ATOM   1320  O   CYS A 178      55.594  19.416   2.933  1.00110.97           O  
ANISOU 1320  O   CYS A 178    13660  13749  14754   -348    683    219       O  
ATOM   1321  CB  CYS A 178      52.391  19.512   1.897  1.00 87.24           C  
ANISOU 1321  CB  CYS A 178    10972  10805  11369   -355    668   -139       C  
ATOM   1322  SG  CYS A 178      51.052  18.705   1.045  1.00105.25           S  
ANISOU 1322  SG  CYS A 178    13399  13091  13499   -331    737   -292       S  
ATOM   1323  N   LYS A 179      54.826  21.181   1.737  1.00104.47           N  
ANISOU 1323  N   LYS A 179    12926  12965  13804   -384    635    163       N  
ATOM   1324  CA  LYS A 179      55.709  22.178   2.317  1.00110.11           C  
ANISOU 1324  CA  LYS A 179    13528  13655  14651   -437    508    293       C  
ATOM   1325  C   LYS A 179      55.700  22.063   3.831  1.00112.11           C  
ANISOU 1325  C   LYS A 179    13767  13887  14942   -482    345    283       C  
ATOM   1326  O   LYS A 179      54.639  22.046   4.445  1.00106.41           O  
ANISOU 1326  O   LYS A 179    13148  13181  14103   -495    266    156       O  
ATOM   1327  CB  LYS A 179      55.282  23.586   1.879  1.00107.66           C  
ANISOU 1327  CB  LYS A 179    13257  13360  14289   -480    421    274       C  
ATOM   1328  CG  LYS A 179      55.876  24.710   2.706  1.00112.87           C  
ANISOU 1328  CG  LYS A 179    13843  13981  15061   -553    230    366       C  
ATOM   1329  CD  LYS A 179      55.516  26.103   2.156  1.00111.80           C  
ANISOU 1329  CD  LYS A 179    13740  13852  14887   -590    162    359       C  
ATOM   1330  CE  LYS A 179      54.047  26.461   2.361  1.00106.01           C  
ANISOU 1330  CE  LYS A 179    13158  13146  13974   -601     95    186       C  
ATOM   1331  NZ  LYS A 179      53.825  27.888   2.040  1.00102.77           N1+
ANISOU 1331  NZ  LYS A 179    12767  12729  13554   -643      4    197       N1+
ATOM   1332  N   ALA A 180      56.885  21.943   4.421  1.00106.22           N  
ANISOU 1332  N   ALA A 180    12893  13104  14363   -499    300    429       N  
ATOM   1333  CA  ALA A 180      57.027  21.965   5.875  1.00110.65           C  
ANISOU 1333  CA  ALA A 180    13443  13637  14962   -545    119    440       C  
ATOM   1334  C   ALA A 180      56.353  23.210   6.468  1.00117.02           C  
ANISOU 1334  C   ALA A 180    14346  14434  15680   -603    -77    364       C  
ATOM   1335  O   ALA A 180      56.332  24.270   5.830  1.00102.43           O  
ANISOU 1335  O   ALA A 180    12504  12584  13833   -630   -107    380       O  
ATOM   1336  CB  ALA A 180      58.513  21.922   6.270  1.00107.65           C  
ANISOU 1336  CB  ALA A 180    12896  13210  14797   -571     70    639       C  
ATOM   1337  N   ASP A 181      55.801  23.063   7.674  1.00 93.70           N  
ANISOU 1337  N   ASP A 181    11478  11474  12651   -611   -198    287       N  
ATOM   1338  CA  ASP A 181      55.167  24.155   8.396  1.00106.82           C  
ANISOU 1338  CA  ASP A 181    13255  13114  14217   -647   -378    215       C  
ATOM   1339  C   ASP A 181      53.971  24.703   7.629  1.00 99.01           C  
ANISOU 1339  C   ASP A 181    12369  12164  13087   -629   -316     95       C  
ATOM   1340  O   ASP A 181      53.671  25.878   7.743  1.00 95.50           O  
ANISOU 1340  O   ASP A 181    11988  11696  12600   -661   -433     70       O  
ATOM   1341  CB  ASP A 181      56.175  25.288   8.650  1.00103.98           C  
ANISOU 1341  CB  ASP A 181    12835  12688  13985   -720   -556    334       C  
ATOM   1342  CG  ASP A 181      56.087  25.848  10.049  1.00123.78           C  
ANISOU 1342  CG  ASP A 181    15447  15140  16444   -754   -787    304       C  
ATOM   1343  OD1 ASP A 181      55.602  25.118  10.941  1.00128.80           O  
ANISOU 1343  OD1 ASP A 181    16160  15790  16989   -714   -793    237       O  
ATOM   1344  OD2 ASP A 181      56.519  27.009  10.254  1.00141.56           O1-
ANISOU 1344  OD2 ASP A 181    17711  17328  18749   -816   -963    352       O1-
ATOM   1345  N   PHE A 182      53.320  23.873   6.821  1.00 96.24           N  
ANISOU 1345  N   PHE A 182    12032  11863  12670   -581   -142     29       N  
ATOM   1346  CA  PHE A 182      52.246  24.361   5.943  1.00102.45           C  
ANISOU 1346  CA  PHE A 182    12901  12687  13340   -571    -86    -66       C  
ATOM   1347  C   PHE A 182      51.128  25.086   6.701  1.00 96.81           C  
ANISOU 1347  C   PHE A 182    12311  11970  12503   -573   -199   -160       C  
ATOM   1348  O   PHE A 182      50.674  26.146   6.276  1.00 93.49           O  
ANISOU 1348  O   PHE A 182    11937  11550  12033   -592   -240   -186       O  
ATOM   1349  CB  PHE A 182      51.634  23.211   5.128  1.00 91.20           C  
ANISOU 1349  CB  PHE A 182    11495  11301  11855   -523     87   -132       C  
ATOM   1350  CG  PHE A 182      50.682  23.670   4.044  1.00 98.35           C  
ANISOU 1350  CG  PHE A 182    12472  12241  12657   -519    142   -207       C  
ATOM   1351  CD1 PHE A 182      49.377  24.027   4.350  1.00 91.16           C  
ANISOU 1351  CD1 PHE A 182    11656  11347  11633   -520     87   -302       C  
ATOM   1352  CD2 PHE A 182      51.093  23.733   2.722  1.00 98.31           C  
ANISOU 1352  CD2 PHE A 182    12439  12249  12666   -508    252   -170       C  
ATOM   1353  CE1 PHE A 182      48.495  24.465   3.361  1.00 94.80           C  
ANISOU 1353  CE1 PHE A 182    12173  11837  12008   -522    124   -357       C  
ATOM   1354  CE2 PHE A 182      50.226  24.151   1.725  1.00105.66           C  
ANISOU 1354  CE2 PHE A 182    13443  13211  13494   -506    289   -235       C  
ATOM   1355  CZ  PHE A 182      48.920  24.529   2.043  1.00 95.76           C  
ANISOU 1355  CZ  PHE A 182    12273  11973  12137   -520    217   -329       C  
ATOM   1356  N   ALA A 183      50.686  24.522   7.817  1.00109.80           N  
ANISOU 1356  N   ALA A 183    14010  13610  14098   -545   -239   -202       N  
ATOM   1357  CA  ALA A 183      49.503  25.041   8.499  1.00103.53           C  
ANISOU 1357  CA  ALA A 183    13341  12817  13177   -520   -302   -286       C  
ATOM   1358  C   ALA A 183      49.774  26.407   9.097  1.00 99.84           C  
ANISOU 1358  C   ALA A 183    12939  12298  12699   -550   -469   -270       C  
ATOM   1359  O   ALA A 183      48.929  27.292   9.016  1.00104.96           O  
ANISOU 1359  O   ALA A 183    13677  12944  13261   -541   -499   -324       O  
ATOM   1360  CB  ALA A 183      49.042  24.082   9.568  1.00 95.41           C  
ANISOU 1360  CB  ALA A 183    12352  11795  12105   -469   -291   -315       C  
ATOM   1361  N   LYS A 184      50.958  26.575   9.682  1.00 93.63           N  
ANISOU 1361  N   LYS A 184    12107  11460  12008   -588   -585   -189       N  
ATOM   1362  CA  LYS A 184      51.363  27.845  10.266  1.00100.04           C  
ANISOU 1362  CA  LYS A 184    12985  12200  12828   -629   -774   -167       C  
ATOM   1363  C   LYS A 184      51.559  28.916   9.200  1.00104.40           C  
ANISOU 1363  C   LYS A 184    13493  12742  13431   -677   -781   -136       C  
ATOM   1364  O   LYS A 184      51.246  30.093   9.423  1.00102.80           O  
ANISOU 1364  O   LYS A 184    13387  12493  13181   -692   -895   -166       O  
ATOM   1365  CB  LYS A 184      52.656  27.696  11.066  1.00114.97           C  
ANISOU 1365  CB  LYS A 184    14819  14031  14834   -672   -913    -69       C  
ATOM   1366  CG  LYS A 184      52.563  26.822  12.302  1.00132.93           C  
ANISOU 1366  CG  LYS A 184    17152  16302  17052   -628   -947    -88       C  
ATOM   1367  CD  LYS A 184      53.867  26.920  13.082  1.00150.47           C  
ANISOU 1367  CD  LYS A 184    19329  18452  19391   -685  -1128     17       C  
ATOM   1368  CE  LYS A 184      54.022  25.798  14.097  1.00158.10           C  
ANISOU 1368  CE  LYS A 184    20302  19428  20339   -646  -1130     31       C  
ATOM   1369  NZ  LYS A 184      55.386  25.810  14.713  1.00149.74           N1+
ANISOU 1369  NZ  LYS A 184    19169  18303  19422   -713  -1305    157       N1+
ATOM   1370  N   GLU A 185      52.090  28.515   8.048  1.00 98.07           N  
ANISOU 1370  N   GLU A 185    12557  11979  12726   -693   -655    -73       N  
ATOM   1371  CA  GLU A 185      52.365  29.491   6.992  1.00 93.44           C  
ANISOU 1371  CA  GLU A 185    11918  11387  12198   -732   -649    -23       C  
ATOM   1372  C   GLU A 185      51.063  29.899   6.337  1.00 97.89           C  
ANISOU 1372  C   GLU A 185    12568  11997  12627   -702   -570   -124       C  
ATOM   1373  O   GLU A 185      50.933  31.022   5.850  1.00102.87           O  
ANISOU 1373  O   GLU A 185    13215  12610  13258   -728   -616   -115       O  
ATOM   1374  CB  GLU A 185      53.342  28.942   5.944  1.00 97.54           C  
ANISOU 1374  CB  GLU A 185    12278  11932  12851   -739   -519     89       C  
ATOM   1375  CG  GLU A 185      54.703  28.564   6.527  1.00104.44           C  
ANISOU 1375  CG  GLU A 185    13035  12756  13890   -771   -591    222       C  
ATOM   1376  CD  GLU A 185      55.824  28.642   5.520  1.00108.23           C  
ANISOU 1376  CD  GLU A 185    13351  13233  14539   -786   -507    378       C  
ATOM   1377  OE1 GLU A 185      55.548  28.966   4.338  1.00113.94           O  
ANISOU 1377  OE1 GLU A 185    14063  13995  15233   -766   -385    376       O  
ATOM   1378  OE2 GLU A 185      56.987  28.391   5.930  1.00111.62           O1-
ANISOU 1378  OE2 GLU A 185    13660  13617  15132   -815   -565    515       O1-
ATOM   1379  N   TRP A 186      50.102  28.977   6.324  1.00 92.99           N  
ANISOU 1379  N   TRP A 186    11996  11432  11905   -649   -459   -208       N  
ATOM   1380  CA  TRP A 186      48.757  29.274   5.826  1.00 92.76           C  
ANISOU 1380  CA  TRP A 186    12046  11443  11754   -621   -399   -295       C  
ATOM   1381  C   TRP A 186      48.076  30.328   6.699  1.00 88.34           C  
ANISOU 1381  C   TRP A 186    11611  10841  11115   -610   -522   -342       C  
ATOM   1382  O   TRP A 186      47.565  31.318   6.189  1.00 97.91           O  
ANISOU 1382  O   TRP A 186    12859  12050  12291   -620   -536   -358       O  
ATOM   1383  CB  TRP A 186      47.899  28.002   5.774  1.00 91.66           C  
ANISOU 1383  CB  TRP A 186    11924  11356  11547   -573   -278   -359       C  
ATOM   1384  CG  TRP A 186      46.718  28.135   4.869  1.00 95.29           C  
ANISOU 1384  CG  TRP A 186    12421  11861  11922   -560   -202   -416       C  
ATOM   1385  CD1 TRP A 186      46.640  27.759   3.559  1.00103.55           C  
ANISOU 1385  CD1 TRP A 186    13431  12948  12967   -567    -96   -418       C  
ATOM   1386  CD2 TRP A 186      45.449  28.694   5.202  1.00 91.86           C  
ANISOU 1386  CD2 TRP A 186    12076  11432  11396   -535   -229   -470       C  
ATOM   1387  CE2 TRP A 186      44.645  28.629   4.043  1.00 96.90           C  
ANISOU 1387  CE2 TRP A 186    12709  12115  11993   -540   -150   -496       C  
ATOM   1388  CE3 TRP A 186      44.907  29.252   6.368  1.00 84.88           C  
ANISOU 1388  CE3 TRP A 186    11284  10513  10455   -499   -309   -493       C  
ATOM   1389  NE1 TRP A 186      45.397  28.046   3.053  1.00104.11           N  
ANISOU 1389  NE1 TRP A 186    13557  13048  12952   -560    -75   -471       N  
ATOM   1390  CZ2 TRP A 186      43.337  29.095   4.013  1.00 96.56           C  
ANISOU 1390  CZ2 TRP A 186    12725  12086  11877   -520   -152   -530       C  
ATOM   1391  CZ3 TRP A 186      43.605  29.719   6.338  1.00 95.28           C  
ANISOU 1391  CZ3 TRP A 186    12666  11843  11692   -465   -290   -527       C  
ATOM   1392  CH2 TRP A 186      42.834  29.635   5.169  1.00 93.93           C  
ANISOU 1392  CH2 TRP A 186    12464  11721  11505   -480   -214   -539       C  
ATOM   1393  N   MET A 187      48.063  30.109   8.011  1.00 92.69           N  
ANISOU 1393  N   MET A 187    12235  11353  11630   -582   -603   -363       N  
ATOM   1394  CA  MET A 187      47.485  31.071   8.939  1.00 87.37           C  
ANISOU 1394  CA  MET A 187    11708  10623  10864   -554   -715   -407       C  
ATOM   1395  C   MET A 187      48.199  32.423   8.852  1.00107.52           C  
ANISOU 1395  C   MET A 187    14276  13102  13476   -613   -860   -368       C  
ATOM   1396  O   MET A 187      47.555  33.470   8.848  1.00109.55           O  
ANISOU 1396  O   MET A 187    14628  13327  13669   -600   -902   -404       O  
ATOM   1397  CB  MET A 187      47.538  30.542  10.375  1.00 92.89           C  
ANISOU 1397  CB  MET A 187    12494  11289  11511   -507   -782   -425       C  
ATOM   1398  CG  MET A 187      46.468  29.516  10.696  1.00 92.30           C  
ANISOU 1398  CG  MET A 187    12446  11271  11352   -428   -653   -469       C  
ATOM   1399  SD  MET A 187      46.637  28.870  12.364  1.00105.85           S  
ANISOU 1399  SD  MET A 187    14258  12952  13009   -365   -721   -472       S  
ATOM   1400  CE  MET A 187      48.060  27.804  12.173  1.00114.53           C  
ANISOU 1400  CE  MET A 187    15195  14064  14258   -430   -724   -397       C  
ATOM   1401  N   THR A 188      49.524  32.400   8.769  1.00102.07           N  
ANISOU 1401  N   THR A 188    13484  12376  12921   -678   -936   -282       N  
ATOM   1402  CA  THR A 188      50.297  33.639   8.656  1.00 90.46           C  
ANISOU 1402  CA  THR A 188    12004  10824  11542   -746  -1087   -221       C  
ATOM   1403  C   THR A 188      49.908  34.443   7.423  1.00 92.75           C  
ANISOU 1403  C   THR A 188    12253  11144  11845   -763  -1015   -213       C  
ATOM   1404  O   THR A 188      49.664  35.645   7.519  1.00101.83           O  
ANISOU 1404  O   THR A 188    13484  12233  12974   -777  -1115   -229       O  
ATOM   1405  CB  THR A 188      51.795  33.334   8.638  1.00 93.26           C  
ANISOU 1405  CB  THR A 188    12216  11146  12074   -813  -1157    -98       C  
ATOM   1406  CG2 THR A 188      52.614  34.616   8.419  1.00 94.12           C  
ANISOU 1406  CG2 THR A 188    12286  11164  12309   -892  -1316    -12       C  
ATOM   1407  OG1 THR A 188      52.143  32.778   9.905  1.00 97.40           O  
ANISOU 1407  OG1 THR A 188    12799  11628  12581   -803  -1263   -104       O  
ATOM   1408  N   ASP A 189      49.803  33.786   6.269  1.00 95.30           N  
ANISOU 1408  N   ASP A 189    12465  11556  12189   -755   -843   -192       N  
ATOM   1409  CA  ASP A 189      49.362  34.496   5.070  1.00 99.68           C  
ANISOU 1409  CA  ASP A 189    12992  12147  12736   -764   -769   -185       C  
ATOM   1410  C   ASP A 189      47.901  34.914   5.142  1.00101.00           C  
ANISOU 1410  C   ASP A 189    13283  12335  12757   -716   -739   -284       C  
ATOM   1411  O   ASP A 189      47.531  35.895   4.516  1.00103.80           O  
ANISOU 1411  O   ASP A 189    13650  12685  13103   -729   -744   -278       O  
ATOM   1412  CB  ASP A 189      49.543  33.661   3.812  1.00 88.12           C  
ANISOU 1412  CB  ASP A 189    11413  10767  11302   -755   -593   -147       C  
ATOM   1413  CG  ASP A 189      50.977  33.241   3.597  1.00100.83           C  
ANISOU 1413  CG  ASP A 189    12885  12360  13066   -786   -584    -26       C  
ATOM   1414  OD1 ASP A 189      51.870  34.008   4.000  1.00 97.40           O  
ANISOU 1414  OD1 ASP A 189    12408  11849  12749   -838   -724     58       O  
ATOM   1415  OD2 ASP A 189      51.192  32.134   3.044  1.00 97.96           O1-
ANISOU 1415  OD2 ASP A 189    12458  12051  12710   -756   -441    -11       O1-
ATOM   1416  N   PHE A 190      47.063  34.165   5.855  1.00 95.99           N  
ANISOU 1416  N   PHE A 190    12729  11725  12020   -658   -697   -358       N  
ATOM   1417  CA  PHE A 190      45.655  34.562   5.938  1.00 94.80           C  
ANISOU 1417  CA  PHE A 190    12680  11591  11750   -604   -659   -427       C  
ATOM   1418  C   PHE A 190      45.530  35.797   6.819  1.00 98.24           C  
ANISOU 1418  C   PHE A 190    13248  11933  12148   -591   -796   -447       C  
ATOM   1419  O   PHE A 190      44.851  36.749   6.462  1.00 98.90           O  
ANISOU 1419  O   PHE A 190    13379  12004  12194   -581   -795   -459       O  
ATOM   1420  CB  PHE A 190      44.754  33.456   6.484  1.00 91.42           C  
ANISOU 1420  CB  PHE A 190    12291  11207  11237   -539   -572   -479       C  
ATOM   1421  CG  PHE A 190      43.288  33.843   6.519  1.00103.13           C  
ANISOU 1421  CG  PHE A 190    13854  12707  12622   -480   -520   -520       C  
ATOM   1422  CD1 PHE A 190      42.762  34.553   7.590  1.00 89.65           C  
ANISOU 1422  CD1 PHE A 190    12286  10937  10838   -419   -582   -546       C  
ATOM   1423  CD2 PHE A 190      42.451  33.527   5.465  1.00100.87           C  
ANISOU 1423  CD2 PHE A 190    13511  12493  12323   -483   -414   -522       C  
ATOM   1424  CE1 PHE A 190      41.418  34.919   7.616  1.00 94.48           C  
ANISOU 1424  CE1 PHE A 190    12962  11563  11375   -354   -517   -562       C  
ATOM   1425  CE2 PHE A 190      41.098  33.894   5.483  1.00100.85           C  
ANISOU 1425  CE2 PHE A 190    13562  12503  12253   -434   -371   -536       C  
ATOM   1426  CZ  PHE A 190      40.588  34.591   6.561  1.00 88.41           C  
ANISOU 1426  CZ  PHE A 190    12108  10869  10615   -365   -413   -549       C  
ATOM   1427  N   GLU A 191      46.174  35.755   7.980  1.00 94.88           N  
ANISOU 1427  N   GLU A 191    12892  11434  11725   -588   -918   -450       N  
ATOM   1428  CA  GLU A 191      46.112  36.850   8.937  1.00 91.56           C  
ANISOU 1428  CA  GLU A 191    12634  10905  11251   -568  -1067   -480       C  
ATOM   1429  C   GLU A 191      46.780  38.125   8.414  1.00105.34           C  
ANISOU 1429  C   GLU A 191    14355  12578  13091   -644  -1184   -433       C  
ATOM   1430  O   GLU A 191      46.243  39.230   8.596  1.00106.27           O  
ANISOU 1430  O   GLU A 191    14593  12631  13154   -620  -1240   -466       O  
ATOM   1431  CB  GLU A 191      46.744  36.416  10.260  1.00104.35           C  
ANISOU 1431  CB  GLU A 191    14340  12461  12849   -554  -1186   -490       C  
ATOM   1432  CG  GLU A 191      46.042  35.216  10.893  1.00107.91           C  
ANISOU 1432  CG  GLU A 191    14824  12973  13202   -469  -1073   -529       C  
ATOM   1433  CD  GLU A 191      46.777  34.688  12.108  1.00114.61           C  
ANISOU 1433  CD  GLU A 191    15738  13771  14039   -460  -1186   -526       C  
ATOM   1434  OE1 GLU A 191      47.824  35.271  12.469  1.00118.87           O  
ANISOU 1434  OE1 GLU A 191    16300  14219  14645   -526  -1368   -494       O  
ATOM   1435  OE2 GLU A 191      46.308  33.695  12.700  1.00122.12           O1-
ANISOU 1435  OE2 GLU A 191    16713  14767  14920   -390  -1101   -546       O1-
ATOM   1436  N   SER A 192      47.932  37.975   7.758  1.00 98.44           N  
ANISOU 1436  N   SER A 192    13323  11712  12368   -727  -1211   -346       N  
ATOM   1437  CA  SER A 192      48.609  39.123   7.154  1.00117.62           C  
ANISOU 1437  CA  SER A 192    15695  14079  14917   -801  -1308   -275       C  
ATOM   1438  C   SER A 192      47.767  39.651   5.994  1.00122.40           C  
ANISOU 1438  C   SER A 192    16264  14749  15493   -787  -1181   -279       C  
ATOM   1439  O   SER A 192      47.877  40.810   5.605  1.00111.76           O  
ANISOU 1439  O   SER A 192    14919  13345  14198   -823  -1250   -246       O  
ATOM   1440  CB  SER A 192      50.011  38.756   6.671  1.00112.04           C  
ANISOU 1440  CB  SER A 192    14806  13374  14392   -880  -1336   -153       C  
ATOM   1441  OG  SER A 192      49.979  38.399   5.302  1.00129.21           O  
ANISOU 1441  OG  SER A 192    16833  15651  16609   -882  -1159   -102       O  
ATOM   1442  N   PHE A 193      46.915  38.791   5.446  1.00105.03           N  
ANISOU 1442  N   PHE A 193    14031  12661  13213   -738  -1005   -316       N  
ATOM   1443  CA  PHE A 193      45.967  39.234   4.437  1.00105.30           C  
ANISOU 1443  CA  PHE A 193    14051  12757  13202   -720   -897   -325       C  
ATOM   1444  C   PHE A 193      44.840  40.064   5.052  1.00 97.60           C  
ANISOU 1444  C   PHE A 193    13233  11734  12117   -661   -927   -392       C  
ATOM   1445  O   PHE A 193      44.479  41.123   4.511  1.00102.85           O  
ANISOU 1445  O   PHE A 193    13909  12378  12790   -670   -937   -375       O  
ATOM   1446  CB  PHE A 193      45.388  38.052   3.678  1.00105.74           C  
ANISOU 1446  CB  PHE A 193    14035  12932  13208   -693   -727   -342       C  
ATOM   1447  CG  PHE A 193      44.290  38.432   2.738  1.00110.76           C  
ANISOU 1447  CG  PHE A 193    14672  13628  13783   -675   -635   -354       C  
ATOM   1448  CD1 PHE A 193      44.541  39.279   1.678  1.00102.89           C  
ANISOU 1448  CD1 PHE A 193    13611  12641  12842   -715   -629   -294       C  
ATOM   1449  CD2 PHE A 193      43.006  37.941   2.907  1.00106.87           C  
ANISOU 1449  CD2 PHE A 193    14235  13182  13189   -617   -557   -410       C  
ATOM   1450  CE1 PHE A 193      43.533  39.631   0.799  1.00113.99           C  
ANISOU 1450  CE1 PHE A 193    15017  14103  14191   -700   -553   -299       C  
ATOM   1451  CE2 PHE A 193      41.996  38.290   2.032  1.00109.79           C  
ANISOU 1451  CE2 PHE A 193    14595  13603  13516   -608   -488   -406       C  
ATOM   1452  CZ  PHE A 193      42.258  39.142   0.981  1.00108.34           C  
ANISOU 1452  CZ  PHE A 193    14357  13430  13377   -650   -490   -355       C  
ATOM   1453  N   GLN A 194      44.298  39.610   6.186  1.00 98.36           N  
ANISOU 1453  N   GLN A 194    13451  11808  12114   -592   -934   -456       N  
ATOM   1454  CA  GLN A 194      43.233  40.365   6.870  1.00 88.60           C  
ANISOU 1454  CA  GLN A 194    12380  10518  10767   -512   -943   -508       C  
ATOM   1455  C   GLN A 194      43.687  41.781   7.180  1.00113.78           C  
ANISOU 1455  C   GLN A 194    15665  13579  13986   -538  -1098   -504       C  
ATOM   1456  O   GLN A 194      42.900  42.724   7.120  1.00116.97           O  
ANISOU 1456  O   GLN A 194    16155  13946  14341   -496  -1086   -520       O  
ATOM   1457  CB  GLN A 194      42.818  39.713   8.186  1.00 92.58           C  
ANISOU 1457  CB  GLN A 194    13014  10998  11163   -424   -940   -563       C  
ATOM   1458  CG  GLN A 194      42.102  38.390   8.088  1.00103.53           C  
ANISOU 1458  CG  GLN A 194    14334  12492  12510   -378   -789   -569       C  
ATOM   1459  CD  GLN A 194      41.825  37.821   9.468  1.00116.15           C  
ANISOU 1459  CD  GLN A 194    16063  14058  14012   -288   -794   -606       C  
ATOM   1460  NE2 GLN A 194      40.549  37.790   9.849  1.00101.61           N  
ANISOU 1460  NE2 GLN A 194    14299  12231  12077   -183   -690   -617       N  
ATOM   1461  OE1 GLN A 194      42.752  37.432  10.197  1.00 98.57           O  
ANISOU 1461  OE1 GLN A 194    13864  11791  11798   -307   -889   -613       O  
ATOM   1462  N   ALA A 195      44.962  41.902   7.539  1.00106.00           N  
ANISOU 1462  N   ALA A 195    14665  12520  13092   -608  -1250   -476       N  
ATOM   1463  CA  ALA A 195      45.529  43.155   8.007  1.00109.20           C  
ANISOU 1463  CA  ALA A 195    15175  12778  13538   -644  -1440   -473       C  
ATOM   1464  C   ALA A 195      45.701  44.131   6.856  1.00117.26           C  
ANISOU 1464  C   ALA A 195    16089  13796  14669   -709  -1441   -406       C  
ATOM   1465  O   ALA A 195      45.426  45.332   6.985  1.00125.00           O  
ANISOU 1465  O   ALA A 195    17176  14679  15639   -701  -1520   -421       O  
ATOM   1466  CB  ALA A 195      46.855  42.905   8.691  1.00113.86           C  
ANISOU 1466  CB  ALA A 195    15757  13290  14214   -713  -1615   -442       C  
ATOM   1467  N   ALA A 196      46.158  43.603   5.727  1.00 96.23           N  
ANISOU 1467  N   ALA A 196    13221  11235  12106   -766  -1347   -330       N  
ATOM   1468  CA  ALA A 196      46.359  44.405   4.534  1.00111.27           C  
ANISOU 1468  CA  ALA A 196    15006  13155  14115   -820  -1324   -251       C  
ATOM   1469  C   ALA A 196      45.049  45.032   4.109  1.00127.15           C  
ANISOU 1469  C   ALA A 196    17083  15199  16031   -761  -1227   -289       C  
ATOM   1470  O   ALA A 196      45.005  46.157   3.614  1.00129.95           O  
ANISOU 1470  O   ALA A 196    17431  15505  16440   -786  -1266   -251       O  
ATOM   1471  CB  ALA A 196      46.922  43.565   3.429  1.00106.88           C  
ANISOU 1471  CB  ALA A 196    14252  12716  13641   -859  -1202   -171       C  
ATOM   1472  N   ILE A 197      43.986  44.272   4.331  1.00123.52           N  
ANISOU 1472  N   ILE A 197    16676  14816  15441   -683  -1102   -354       N  
ATOM   1473  CA  ILE A 197      42.628  44.671   4.016  1.00129.41           C  
ANISOU 1473  CA  ILE A 197    17473  15600  16098   -617   -997   -378       C  
ATOM   1474  C   ILE A 197      42.181  45.905   4.807  1.00126.89           C  
ANISOU 1474  C   ILE A 197    17332  15149  15731   -567  -1086   -415       C  
ATOM   1475  O   ILE A 197      41.401  46.716   4.308  1.00133.06           O  
ANISOU 1475  O   ILE A 197    18127  15931  16499   -541  -1036   -399       O  
ATOM   1476  CB  ILE A 197      41.659  43.480   4.283  1.00124.78           C  
ANISOU 1476  CB  ILE A 197    16901  15106  15403   -544   -864   -424       C  
ATOM   1477  CG1 ILE A 197      41.854  42.419   3.214  1.00131.33           C  
ANISOU 1477  CG1 ILE A 197    17566  16064  16270   -589   -760   -389       C  
ATOM   1478  CG2 ILE A 197      40.211  43.907   4.287  1.00134.26           C  
ANISOU 1478  CG2 ILE A 197    18174  16322  16519   -462   -773   -437       C  
ATOM   1479  CD1 ILE A 197      41.820  42.992   1.831  1.00126.34           C  
ANISOU 1479  CD1 ILE A 197    16828  15483  15692   -637   -715   -326       C  
ATOM   1480  N   LYS A 198      42.694  46.051   6.026  1.00117.35           N  
ANISOU 1480  N   LYS A 198    16269  13823  14494   -551  -1223   -463       N  
ATOM   1481  CA  LYS A 198      42.151  47.020   6.976  1.00118.17           C  
ANISOU 1481  CA  LYS A 198    16597  13795  14508   -472  -1293   -521       C  
ATOM   1482  C   LYS A 198      42.845  48.394   6.930  1.00131.43           C  
ANISOU 1482  C   LYS A 198    18329  15329  16281   -536  -1466   -500       C  
ATOM   1483  O   LYS A 198      42.631  49.231   7.812  1.00142.36           O  
ANISOU 1483  O   LYS A 198    19927  16571  17594   -479  -1564   -556       O  
ATOM   1484  CB  LYS A 198      42.212  46.435   8.400  1.00107.96           C  
ANISOU 1484  CB  LYS A 198    15478  12442  13102   -400  -1349   -594       C  
ATOM   1485  CG  LYS A 198      41.253  45.265   8.625  1.00102.48           C  
ANISOU 1485  CG  LYS A 198    14770  11865  12303   -308  -1170   -613       C  
ATOM   1486  CD  LYS A 198      41.533  44.454   9.894  1.00119.75           C  
ANISOU 1486  CD  LYS A 198    17080  14018  14400   -254  -1218   -664       C  
ATOM   1487  CE  LYS A 198      40.688  43.162   9.885  1.00142.79           C  
ANISOU 1487  CE  LYS A 198    19923  17071  17261   -186  -1032   -658       C  
ATOM   1488  NZ  LYS A 198      40.979  42.186  10.982  1.00149.13           N1+
ANISOU 1488  NZ  LYS A 198    20802  17868  17992   -139  -1054   -691       N1+
ATOM   1489  N   GLU A 199      43.630  48.641   5.883  1.00121.09           N  
ANISOU 1489  N   GLU A 199    16831  14051  15127   -645  -1496   -414       N  
ATOM   1490  CA  GLU A 199      44.460  49.847   5.814  1.00143.13           C  
ANISOU 1490  CA  GLU A 199    19637  16702  18045   -723  -1676   -371       C  
ATOM   1491  C   GLU A 199      43.736  51.107   5.302  1.00150.01           C  
ANISOU 1491  C   GLU A 199    20550  17526  18922   -698  -1648   -357       C  
ATOM   1492  O   GLU A 199      42.822  51.024   4.476  1.00138.70           O  
ANISOU 1492  O   GLU A 199    19035  16211  17454   -659  -1474   -334       O  
ATOM   1493  CB  GLU A 199      45.682  49.583   4.931  1.00137.92           C  
ANISOU 1493  CB  GLU A 199    18743  16089  17569   -843  -1713   -258       C  
ATOM   1494  CG  GLU A 199      46.514  48.376   5.329  1.00141.93           C  
ANISOU 1494  CG  GLU A 199    19182  16641  18103   -875  -1738   -248       C  
ATOM   1495  CD  GLU A 199      47.432  48.634   6.510  1.00153.58           C  
ANISOU 1495  CD  GLU A 199    20780  17953  19618   -918  -1979   -267       C  
ATOM   1496  OE1 GLU A 199      48.064  47.666   6.985  1.00158.77           O  
ANISOU 1496  OE1 GLU A 199    21401  18636  20288   -937  -2011   -262       O  
ATOM   1497  OE2 GLU A 199      47.533  49.797   6.957  1.00162.77           O1-
ANISOU 1497  OE2 GLU A 199    22081  18958  20804   -934  -2145   -285       O1-
ATOM   1498  N   ASP A 200      44.179  52.266   5.797  1.00152.47           N  
ANISOU 1498  N   ASP A 200    20989  17657  19287   -726  -1834   -366       N  
ATOM   1499  CA  ASP A 200      43.667  53.575   5.389  1.00161.58           C  
ANISOU 1499  CA  ASP A 200    22191  18733  20469   -711  -1839   -347       C  
ATOM   1500  C   ASP A 200      44.221  54.010   4.030  1.00155.11           C  
ANISOU 1500  C   ASP A 200    21130  17970  19833   -814  -1822   -218       C  
ATOM   1501  O   ASP A 200      44.708  55.136   3.879  1.00152.67           O  
ANISOU 1501  O   ASP A 200    20827  17532  19647   -872  -1958   -170       O  
ATOM   1502  CB  ASP A 200      44.008  54.640   6.446  1.00180.86           C  
ANISOU 1502  CB  ASP A 200    24876  20939  22904   -707  -2063   -408       C  
ATOM   1503  CG  ASP A 200      42.781  55.404   6.940  1.00190.46           C  
ANISOU 1503  CG  ASP A 200    26320  22075  23970   -572  -1993   -486       C  
ATOM   1504  OD1 ASP A 200      41.749  54.763   7.239  1.00209.02           O  
ANISOU 1504  OD1 ASP A 200    28736  24518  26164   -453  -1817   -535       O  
ATOM   1505  OD2 ASP A 200      42.850  56.648   7.038  1.00179.43           O1-
ANISOU 1505  OD2 ASP A 200    25036  20517  22621   -582  -2112   -489       O1-
ATOM   1506  N   GLN A 201      44.148  53.116   3.049  1.00150.09           N  
ANISOU 1506  N   GLN A 201    20292  17521  19213   -830  -1657   -159       N  
ATOM   1507  CA  GLN A 201      44.513  53.454   1.680  1.00165.59           C  
ANISOU 1507  CA  GLN A 201    22041  19561  21315   -899  -1598    -34       C  
ATOM   1508  C   GLN A 201      43.301  53.343   0.777  1.00181.78           C  
ANISOU 1508  C   GLN A 201    24037  21755  23275   -837  -1393    -26       C  
ATOM   1509  O   GLN A 201      42.300  52.721   1.135  1.00175.51           O  
ANISOU 1509  O   GLN A 201    23326  21027  22334   -754  -1286   -102       O  
ATOM   1510  CB  GLN A 201      45.626  52.551   1.161  1.00168.32           C  
ANISOU 1510  CB  GLN A 201    22194  19992  21767   -973  -1587     50       C  
ATOM   1511  CG  GLN A 201      46.894  52.596   1.983  1.00176.69           C  
ANISOU 1511  CG  GLN A 201    23272  20917  22946  -1046  -1797     71       C  
ATOM   1512  CD  GLN A 201      47.307  51.218   2.461  1.00179.94           C  
ANISOU 1512  CD  GLN A 201    23660  21400  23310  -1041  -1770     39       C  
ATOM   1513  NE2 GLN A 201      48.323  51.165   3.322  1.00171.04           N  
ANISOU 1513  NE2 GLN A 201    22565  20154  22268  -1099  -1962     50       N  
ATOM   1514  OE1 GLN A 201      46.711  50.210   2.067  1.00179.37           O  
ANISOU 1514  OE1 GLN A 201    23541  21480  23131   -989  -1589      8       O  
ATOM   1515  N   ASP A 202      43.397  53.951  -0.398  1.00200.31           N  
ANISOU 1515  N   ASP A 202    26240  24148  25719   -879  -1346     79       N  
ATOM   1516  CA  ASP A 202      42.290  53.960  -1.340  1.00206.67           C  
ANISOU 1516  CA  ASP A 202    26991  25081  26452   -832  -1177    102       C  
ATOM   1517  C   ASP A 202      42.087  52.569  -1.936  1.00198.29           C  
ANISOU 1517  C   ASP A 202    25830  24198  25313   -822  -1033     99       C  
ATOM   1518  O   ASP A 202      43.015  51.974  -2.488  1.00197.26           O  
ANISOU 1518  O   ASP A 202    25572  24128  25251   -874  -1019    158       O  
ATOM   1519  CB  ASP A 202      42.533  54.995  -2.442  1.00213.86           C  
ANISOU 1519  CB  ASP A 202    27779  25991  27488   -880  -1174    223       C  
ATOM   1520  CG  ASP A 202      42.902  56.366  -1.890  1.00215.78           C  
ANISOU 1520  CG  ASP A 202    28110  26040  27838   -906  -1338    235       C  
ATOM   1521  OD1 ASP A 202      42.707  56.603  -0.677  1.00216.65           O  
ANISOU 1521  OD1 ASP A 202    28411  26018  27889   -867  -1438    134       O  
ATOM   1522  OD2 ASP A 202      43.383  57.210  -2.674  1.00212.74           O1-
ANISOU 1522  OD2 ASP A 202    27611  25629  27593   -960  -1367    348       O1-
ATOM   1523  N   GLY A 212      40.869  52.053  -1.808  1.00189.00           N  
ANISOU 1523  N   GLY A 212    24715  23096  24000   -750   -926     38       N  
ATOM   1524  CA  GLY A 212      40.536  50.731  -2.307  1.00175.67           C  
ANISOU 1524  CA  GLY A 212    22955  21558  22233   -739   -805     25       C  
ATOM   1525  C   GLY A 212      39.989  49.832  -1.213  1.00157.37           C  
ANISOU 1525  C   GLY A 212    20748  19238  19808   -677   -788    -74       C  
ATOM   1526  O   GLY A 212      39.442  48.766  -1.491  1.00151.10           O  
ANISOU 1526  O   GLY A 212    19917  18555  18941   -657   -690    -93       O  
ATOM   1527  N   TYR A 213      40.130  50.285   0.032  1.00155.08           N  
ANISOU 1527  N   TYR A 213    20604  18813  19506   -644   -888   -133       N  
ATOM   1528  CA  TYR A 213      39.784  49.497   1.215  1.00143.28           C  
ANISOU 1528  CA  TYR A 213    19231  17298  17911   -578   -883   -221       C  
ATOM   1529  C   TYR A 213      38.818  50.217   2.145  1.00136.54           C  
ANISOU 1529  C   TYR A 213    18558  16346  16976   -477   -882   -267       C  
ATOM   1530  O   TYR A 213      38.345  49.648   3.133  1.00127.51           O  
ANISOU 1530  O   TYR A 213    17529  15186  15734   -397   -853   -328       O  
ATOM   1531  CB  TYR A 213      41.047  49.141   2.005  1.00151.35           C  
ANISOU 1531  CB  TYR A 213    20285  18244  18977   -622  -1013   -252       C  
ATOM   1532  CG  TYR A 213      41.984  48.207   1.283  1.00163.46           C  
ANISOU 1532  CG  TYR A 213    21652  19873  20581   -697   -989   -205       C  
ATOM   1533  CD1 TYR A 213      41.491  47.233   0.425  1.00162.31           C  
ANISOU 1533  CD1 TYR A 213    21403  19877  20392   -690   -845   -190       C  
ATOM   1534  CD2 TYR A 213      43.361  48.298   1.457  1.00172.67           C  
ANISOU 1534  CD2 TYR A 213    22771  20972  21864   -770  -1113   -166       C  
ATOM   1535  CE1 TYR A 213      42.334  46.377  -0.236  1.00160.27           C  
ANISOU 1535  CE1 TYR A 213    21016  19695  20184   -741   -810   -150       C  
ATOM   1536  CE2 TYR A 213      44.217  47.443   0.795  1.00173.12           C  
ANISOU 1536  CE2 TYR A 213    22675  21113  21991   -823  -1069   -108       C  
ATOM   1537  CZ  TYR A 213      43.694  46.487  -0.051  1.00170.42           C  
ANISOU 1537  CZ  TYR A 213    22250  20917  21585   -801   -909   -106       C  
ATOM   1538  OH  TYR A 213      44.532  45.629  -0.720  1.00169.80           O  
ANISOU 1538  OH  TYR A 213    22042  20913  21562   -837   -851    -51       O  
ATOM   1539  N   MET A 214      38.542  51.477   1.839  1.00139.78           N  
ANISOU 1539  N   MET A 214    18998  16687  17426   -472   -905   -232       N  
ATOM   1540  CA  MET A 214      37.772  52.306   2.744  1.00136.36           C  
ANISOU 1540  CA  MET A 214    18756  16132  16922   -368   -909   -272       C  
ATOM   1541  C   MET A 214      36.278  52.077   2.578  1.00124.74           C  
ANISOU 1541  C   MET A 214    17278  14743  15374   -272   -740   -246       C  
ATOM   1542  O   MET A 214      35.495  52.360   3.482  1.00133.76           O  
ANISOU 1542  O   MET A 214    18580  15809  16432   -154   -696   -277       O  
ATOM   1543  CB  MET A 214      38.137  53.770   2.525  1.00134.50           C  
ANISOU 1543  CB  MET A 214    18561  15770  16774   -402  -1011   -242       C  
ATOM   1544  CG  MET A 214      39.594  54.063   2.846  1.00122.48           C  
ANISOU 1544  CG  MET A 214    17055  14137  15346   -496  -1204   -256       C  
ATOM   1545  SD  MET A 214      39.888  54.354   4.605  1.00177.48           S  
ANISOU 1545  SD  MET A 214    24315  20899  22219   -428  -1361   -372       S  
ATOM   1546  CE  MET A 214      40.127  52.702   5.258  1.00128.61           C  
ANISOU 1546  CE  MET A 214    18116  14808  15941   -413  -1325   -425       C  
ATOM   1547  N   SER A 215      35.898  51.517   1.435  1.00111.57           N  
ANISOU 1547  N   SER A 215    15429  13226  13737   -319   -647   -182       N  
ATOM   1548  CA  SER A 215      34.493  51.345   1.083  1.00101.43           C  
ANISOU 1548  CA  SER A 215    14103  12023  12413   -252   -508   -129       C  
ATOM   1549  C   SER A 215      33.731  50.460   2.064  1.00113.23           C  
ANISOU 1549  C   SER A 215    15677  13529  13816   -150   -427   -163       C  
ATOM   1550  O   SER A 215      34.316  49.648   2.790  1.00109.18           O  
ANISOU 1550  O   SER A 215    15214  13007  13263   -149   -465   -229       O  
ATOM   1551  CB  SER A 215      34.374  50.765  -0.324  1.00102.31           C  
ANISOU 1551  CB  SER A 215    14018  12289  12565   -337   -457    -64       C  
ATOM   1552  OG  SER A 215      34.931  49.456  -0.379  1.00114.16           O  
ANISOU 1552  OG  SER A 215    15459  13869  14046   -383   -460   -102       O  
ATOM   1553  N   SER A 216      32.412  50.619   2.063  1.00100.40           N  
ANISOU 1553  N   SER A 216    14053  11925  12169    -62   -310   -102       N  
ATOM   1554  CA  SER A 216      31.564  49.894   2.976  1.00102.06           C  
ANISOU 1554  CA  SER A 216    14328  12140  12309     52   -213   -102       C  
ATOM   1555  C   SER A 216      31.608  48.405   2.611  1.00 94.37           C  
ANISOU 1555  C   SER A 216    13221  11296  11340     -9   -190   -103       C  
ATOM   1556  O   SER A 216      31.541  47.542   3.481  1.00 96.50           O  
ANISOU 1556  O   SER A 216    13544  11564  11556     47   -160   -138       O  
ATOM   1557  CB  SER A 216      30.137  50.447   2.928  1.00102.92           C  
ANISOU 1557  CB  SER A 216    14436  12244  12425    157    -87     -3       C  
ATOM   1558  OG  SER A 216      29.360  49.925   3.989  1.00124.62           O  
ANISOU 1558  OG  SER A 216    17273  14969  15109    294     17     10       O  
ATOM   1559  N   LEU A 217      31.774  48.131   1.319  1.00 89.25           N  
ANISOU 1559  N   LEU A 217    12411  10751  10749   -122   -208    -66       N  
ATOM   1560  CA  LEU A 217      31.912  46.774   0.807  1.00 86.69           C  
ANISOU 1560  CA  LEU A 217    11971  10538  10428   -191   -199    -74       C  
ATOM   1561  C   LEU A 217      33.123  46.057   1.358  1.00104.26           C  
ANISOU 1561  C   LEU A 217    14236  12747  12631   -226   -266   -164       C  
ATOM   1562  O   LEU A 217      33.009  44.985   1.957  1.00112.66           O  
ANISOU 1562  O   LEU A 217    15309  13836  13663   -197   -235   -191       O  
ATOM   1563  CB  LEU A 217      32.009  46.789  -0.715  1.00 87.02           C  
ANISOU 1563  CB  LEU A 217    11873  10675  10516   -297   -218    -27       C  
ATOM   1564  CG  LEU A 217      32.164  45.420  -1.378  1.00 88.35           C  
ANISOU 1564  CG  LEU A 217    11944  10948  10677   -368   -214    -41       C  
ATOM   1565  CD1 LEU A 217      31.028  44.464  -0.991  1.00 91.68           C  
ANISOU 1565  CD1 LEU A 217    12340  11406  11088   -317   -149     -9       C  
ATOM   1566  CD2 LEU A 217      32.174  45.611  -2.879  1.00 97.65           C  
ANISOU 1566  CD2 LEU A 217    13020  12205  11876   -452   -230     10       C  
ATOM   1567  N   VAL A 218      34.292  46.640   1.130  1.00100.24           N  
ANISOU 1567  N   VAL A 218    13738  12195  12154   -293   -358   -195       N  
ATOM   1568  CA  VAL A 218      35.528  46.043   1.608  1.00 95.88           C  
ANISOU 1568  CA  VAL A 218    13207  11619  11603   -335   -433   -260       C  
ATOM   1569  C   VAL A 218      35.475  45.941   3.130  1.00101.03           C  
ANISOU 1569  C   VAL A 218    14019  12179  12188   -242   -449   -318       C  
ATOM   1570  O   VAL A 218      35.986  44.989   3.714  1.00106.87           O  
ANISOU 1570  O   VAL A 218    14772  12930  12905   -244   -466   -362       O  
ATOM   1571  CB  VAL A 218      36.749  46.850   1.136  1.00 96.43           C  
ANISOU 1571  CB  VAL A 218    13253  11642  11745   -418   -535   -255       C  
ATOM   1572  CG1 VAL A 218      37.999  46.438   1.883  1.00 97.64           C  
ANISOU 1572  CG1 VAL A 218    13447  11739  11915   -450   -631   -307       C  
ATOM   1573  CG2 VAL A 218      36.927  46.669  -0.369  1.00 87.26           C  
ANISOU 1573  CG2 VAL A 218    11935  10588  10632   -501   -501   -196       C  
ATOM   1574  N   ASN A 219      34.812  46.889   3.782  1.00 99.96           N  
ANISOU 1574  N   ASN A 219    14014  11954  12014   -148   -433   -313       N  
ATOM   1575  CA  ASN A 219      34.638  46.732   5.217  1.00 96.68           C  
ANISOU 1575  CA  ASN A 219    13771  11453  11508    -36   -428   -364       C  
ATOM   1576  C   ASN A 219      33.724  45.539   5.554  1.00 99.16           C  
ANISOU 1576  C   ASN A 219    14045  11850  11782     34   -304   -338       C  
ATOM   1577  O   ASN A 219      33.940  44.865   6.556  1.00 92.52           O  
ANISOU 1577  O   ASN A 219    13290  10984  10881     89   -306   -382       O  
ATOM   1578  CB  ASN A 219      34.089  48.003   5.856  1.00100.11           C  
ANISOU 1578  CB  ASN A 219    14379  11762  11895     70   -422   -363       C  
ATOM   1579  CG  ASN A 219      34.179  47.955   7.365  1.00115.93           C  
ANISOU 1579  CG  ASN A 219    16605  13656  13787    186   -444   -430       C  
ATOM   1580  ND2 ASN A 219      35.358  48.259   7.897  1.00135.54           N  
ANISOU 1580  ND2 ASN A 219    19198  16042  16261    138   -605   -504       N  
ATOM   1581  OD1 ASN A 219      33.213  47.613   8.045  1.00114.53           O  
ANISOU 1581  OD1 ASN A 219    16499  13482  13535    318   -320   -406       O  
ATOM   1582  N   SER A 220      32.715  45.280   4.724  1.00106.70           N  
ANISOU 1582  N   SER A 220    14868  12897  12777     30   -205   -260       N  
ATOM   1583  CA  SER A 220      31.783  44.173   4.978  1.00 89.78           C  
ANISOU 1583  CA  SER A 220    12666  10822  10623     88    -98   -214       C  
ATOM   1584  C   SER A 220      32.495  42.830   4.789  1.00103.16           C  
ANISOU 1584  C   SER A 220    14271  12592  12334      4   -132   -257       C  
ATOM   1585  O   SER A 220      32.281  41.882   5.542  1.00109.88           O  
ANISOU 1585  O   SER A 220    15139  13454  13155     60    -86   -263       O  
ATOM   1586  CB  SER A 220      30.562  44.255   4.056  1.00 94.25           C  
ANISOU 1586  CB  SER A 220    13102  11460  11250     84    -15   -107       C  
ATOM   1587  OG  SER A 220      29.771  45.415   4.296  1.00101.80           O  
ANISOU 1587  OG  SER A 220    14133  12348  12199    180     42    -49       O  
ATOM   1588  N   MET A 221      33.338  42.759   3.765  1.00 90.92           N  
ANISOU 1588  N   MET A 221    12625  11088  10832   -121   -202   -279       N  
ATOM   1589  CA  MET A 221      34.184  41.599   3.525  1.00 97.54           C  
ANISOU 1589  CA  MET A 221    13391  11983  11687   -198   -233   -321       C  
ATOM   1590  C   MET A 221      35.109  41.312   4.691  1.00107.87           C  
ANISOU 1590  C   MET A 221    14803  13227  12958   -170   -290   -387       C  
ATOM   1591  O   MET A 221      35.219  40.181   5.145  1.00 97.49           O  
ANISOU 1591  O   MET A 221    13470  11941  11629   -159   -266   -406       O  
ATOM   1592  CB  MET A 221      35.041  41.810   2.293  1.00 99.95           C  
ANISOU 1592  CB  MET A 221    13604  12330  12043   -314   -288   -322       C  
ATOM   1593  CG  MET A 221      34.310  42.404   1.145  1.00114.99           C  
ANISOU 1593  CG  MET A 221    15435  14282  13974   -344   -260   -259       C  
ATOM   1594  SD  MET A 221      34.545  41.383  -0.288  1.00127.07           S  
ANISOU 1594  SD  MET A 221    16831  15924  15524   -445   -248   -250       S  
ATOM   1595  CE  MET A 221      33.935  39.836   0.373  1.00100.36           C  
ANISOU 1595  CE  MET A 221    13437  12572  12122   -407   -197   -268       C  
ATOM   1596  N   SER A 222      35.810  42.345   5.142  1.00 94.05           N  
ANISOU 1596  N   SER A 222    13158  11381  11196   -167   -380   -419       N  
ATOM   1597  CA  SER A 222      36.749  42.207   6.246  1.00 95.35           C  
ANISOU 1597  CA  SER A 222    13435  11468  11325   -151   -468   -479       C  
ATOM   1598  C   SER A 222      36.044  41.597   7.459  1.00 99.44           C  
ANISOU 1598  C   SER A 222    14060  11968  11756    -27   -399   -490       C  
ATOM   1599  O   SER A 222      36.541  40.657   8.073  1.00110.37           O  
ANISOU 1599  O   SER A 222    15451  13363  13121    -24   -415   -519       O  
ATOM   1600  CB  SER A 222      37.368  43.576   6.580  1.00 93.71           C  
ANISOU 1600  CB  SER A 222    13351  11137  11118   -157   -589   -503       C  
ATOM   1601  OG  SER A 222      38.159  43.523   7.755  1.00106.67           O  
ANISOU 1601  OG  SER A 222    15131  12685  12713   -134   -696   -559       O  
ATOM   1602  N   LEU A 223      34.863  42.114   7.776  1.00100.52           N  
ANISOU 1602  N   LEU A 223    14268  12080  11845     82   -309   -453       N  
ATOM   1603  CA  LEU A 223      34.049  41.577   8.867  1.00100.27           C  
ANISOU 1603  CA  LEU A 223    14328  12035  11735    221   -210   -436       C  
ATOM   1604  C   LEU A 223      33.659  40.121   8.638  1.00105.31           C  
ANISOU 1604  C   LEU A 223    14818  12780  12414    203   -128   -399       C  
ATOM   1605  O   LEU A 223      33.733  39.302   9.558  1.00 97.66           O  
ANISOU 1605  O   LEU A 223    13898  11807  11400    265   -103   -412       O  
ATOM   1606  CB  LEU A 223      32.778  42.399   9.048  1.00 95.74           C  
ANISOU 1606  CB  LEU A 223    13824  11425  11128    345   -102   -373       C  
ATOM   1607  CG  LEU A 223      32.810  43.571  10.020  1.00116.27           C  
ANISOU 1607  CG  LEU A 223    16665  13885  13627    458   -133   -411       C  
ATOM   1608  CD1 LEU A 223      33.948  44.519   9.703  1.00143.00           C  
ANISOU 1608  CD1 LEU A 223    20104  17196  17035    354   -302   -480       C  
ATOM   1609  CD2 LEU A 223      31.482  44.300   9.959  1.00117.63           C  
ANISOU 1609  CD2 LEU A 223    16865  14038  13791    576      4   -325       C  
ATOM   1610  N   MET A 224      33.215  39.820   7.419  1.00103.80           N  
ANISOU 1610  N   MET A 224    14455  12676  12307    122    -92   -351       N  
ATOM   1611  CA  MET A 224      32.816  38.468   7.061  1.00 98.85           C  
ANISOU 1611  CA  MET A 224    13690  12138  11730     90    -33   -317       C  
ATOM   1612  C   MET A 224      34.002  37.518   7.203  1.00103.90           C  
ANISOU 1612  C   MET A 224    14305  12796  12375     20    -97   -384       C  
ATOM   1613  O   MET A 224      33.877  36.418   7.743  1.00104.29           O  
ANISOU 1613  O   MET A 224    14332  12870  12424     52    -54   -378       O  
ATOM   1614  CB  MET A 224      32.265  38.424   5.637  1.00 99.97           C  
ANISOU 1614  CB  MET A 224    13681  12355  11949      1    -19   -266       C  
ATOM   1615  CG  MET A 224      31.710  37.042   5.257  1.00 91.82           C  
ANISOU 1615  CG  MET A 224    12521  11396  10971    -31     27   -228       C  
ATOM   1616  SD  MET A 224      31.273  36.920   3.515  1.00 96.34           S  
ANISOU 1616  SD  MET A 224    12947  12045  11611   -154      1   -189       S  
ATOM   1617  CE  MET A 224      32.808  37.394   2.728  1.00 97.78           C  
ANISOU 1617  CE  MET A 224    13145  12232  11775   -258    -89   -276       C  
ATOM   1618  N   LEU A 225      35.162  37.959   6.737  1.00103.00           N  
ANISOU 1618  N   LEU A 225    14190  12666  12279    -71   -197   -435       N  
ATOM   1619  CA  LEU A 225      36.381  37.178   6.897  1.00102.46           C  
ANISOU 1619  CA  LEU A 225    14097  12605  12230   -132   -259   -483       C  
ATOM   1620  C   LEU A 225      36.671  36.881   8.358  1.00109.22           C  
ANISOU 1620  C   LEU A 225    15077  13402  13020    -49   -280   -512       C  
ATOM   1621  O   LEU A 225      36.985  35.749   8.719  1.00114.84           O  
ANISOU 1621  O   LEU A 225    15750  14144  13741    -52   -264   -521       O  
ATOM   1622  CB  LEU A 225      37.578  37.901   6.294  1.00 98.88           C  
ANISOU 1622  CB  LEU A 225    13627  12125  11819   -227   -362   -506       C  
ATOM   1623  CG  LEU A 225      38.099  37.343   4.979  1.00104.36           C  
ANISOU 1623  CG  LEU A 225    14174  12895  12582   -331   -351   -494       C  
ATOM   1624  CD1 LEU A 225      36.935  37.058   4.055  1.00 98.70           C  
ANISOU 1624  CD1 LEU A 225    13380  12250  11870   -334   -266   -458       C  
ATOM   1625  CD2 LEU A 225      39.038  38.371   4.364  1.00114.28           C  
ANISOU 1625  CD2 LEU A 225    15416  14119  13887   -401   -433   -486       C  
ATOM   1626  N   GLU A 226      36.575  37.899   9.201  1.00 97.96           N  
ANISOU 1626  N   GLU A 226    13813  11886  11520     29   -318   -528       N  
ATOM   1627  CA  GLU A 226      36.930  37.707  10.595  1.00 96.94           C  
ANISOU 1627  CA  GLU A 226    13835  11691  11307    111   -357   -561       C  
ATOM   1628  C   GLU A 226      35.930  36.791  11.301  1.00 98.92           C  
ANISOU 1628  C   GLU A 226    14093  11977  11513    227   -225   -520       C  
ATOM   1629  O   GLU A 226      36.302  36.052  12.206  1.00 91.30           O  
ANISOU 1629  O   GLU A 226    13181  11003  10507    269   -235   -536       O  
ATOM   1630  CB  GLU A 226      37.028  39.050  11.319  1.00 98.19           C  
ANISOU 1630  CB  GLU A 226    14199  11729  11382    177   -437   -595       C  
ATOM   1631  CG  GLU A 226      37.402  38.939  12.800  1.00122.74           C  
ANISOU 1631  CG  GLU A 226    17505  14753  14375    270   -497   -637       C  
ATOM   1632  CD  GLU A 226      38.698  38.168  13.042  1.00140.81           C  
ANISOU 1632  CD  GLU A 226    19748  17048  16704    179   -613   -666       C  
ATOM   1633  OE1 GLU A 226      39.651  38.315  12.247  1.00149.05           O  
ANISOU 1633  OE1 GLU A 226    20678  18101  17853     45   -709   -670       O  
ATOM   1634  OE2 GLU A 226      38.764  37.415  14.038  1.00144.37           O1-
ANISOU 1634  OE2 GLU A 226    20273  17494  17087    250   -602   -674       O1-
ATOM   1635  N   GLU A 227      34.663  36.842  10.896  1.00 96.69           N  
ANISOU 1635  N   GLU A 227    13753  11735  11251    279   -103   -453       N  
ATOM   1636  CA  GLU A 227      33.631  36.045  11.559  1.00 98.59           C  
ANISOU 1636  CA  GLU A 227    13985  12002  11472    396     30   -385       C  
ATOM   1637  C   GLU A 227      33.833  34.554  11.287  1.00100.98           C  
ANISOU 1637  C   GLU A 227    14135  12383  11851    329     51   -374       C  
ATOM   1638  O   GLU A 227      33.682  33.724  12.188  1.00107.78           O  
ANISOU 1638  O   GLU A 227    15022  13247  12683    408    105   -352       O  
ATOM   1639  CB  GLU A 227      32.230  36.488  11.117  1.00 95.13           C  
ANISOU 1639  CB  GLU A 227    13495  11582  11067    457    146   -292       C  
ATOM   1640  CG  GLU A 227      31.110  35.510  11.504  1.00117.79           C  
ANISOU 1640  CG  GLU A 227    16286  14496  13975    549    285   -187       C  
ATOM   1641  CD  GLU A 227      30.779  35.501  12.992  1.00136.20           C  
ANISOU 1641  CD  GLU A 227    18784  16770  16197    732    371   -157       C  
ATOM   1642  OE1 GLU A 227      31.396  36.266  13.765  1.00140.00           O  
ANISOU 1642  OE1 GLU A 227    19467  17170  16556    792    311   -230       O  
ATOM   1643  OE2 GLU A 227      29.886  34.722  13.388  1.00145.13           O1-
ANISOU 1643  OE2 GLU A 227    19848  17931  17366    820    495    -54       O1-
ATOM   1644  N   PHE A 228      34.175  34.225  10.042  1.00 92.54           N  
ANISOU 1644  N   PHE A 228    12917  11372  10872    191     12   -389       N  
ATOM   1645  CA  PHE A 228      34.491  32.852   9.656  1.00 95.33           C  
ANISOU 1645  CA  PHE A 228    13140  11787  11296    119     20   -392       C  
ATOM   1646  C   PHE A 228      35.774  32.367  10.308  1.00100.05           C  
ANISOU 1646  C   PHE A 228    13782  12362  11869     97    -52   -452       C  
ATOM   1647  O   PHE A 228      35.789  31.330  10.958  1.00102.47           O  
ANISOU 1647  O   PHE A 228    14072  12682  12179    134    -14   -439       O  
ATOM   1648  CB  PHE A 228      34.606  32.735   8.139  1.00 95.96           C  
ANISOU 1648  CB  PHE A 228    13088  11919  11452    -10     -6   -400       C  
ATOM   1649  CG  PHE A 228      33.279  32.667   7.446  1.00108.82           C  
ANISOU 1649  CG  PHE A 228    14630  13585  13131     -7     60   -326       C  
ATOM   1650  CD1 PHE A 228      32.224  31.970   8.019  1.00108.16           C  
ANISOU 1650  CD1 PHE A 228    14512  13509  13076     73    146   -248       C  
ATOM   1651  CD2 PHE A 228      33.073  33.308   6.237  1.00100.27           C  
ANISOU 1651  CD2 PHE A 228    13495  12526  12075    -82     31   -320       C  
ATOM   1652  CE1 PHE A 228      31.003  31.902   7.394  1.00102.93           C  
ANISOU 1652  CE1 PHE A 228    13754  12872  12482     68    190   -160       C  
ATOM   1653  CE2 PHE A 228      31.844  33.251   5.612  1.00102.44           C  
ANISOU 1653  CE2 PHE A 228    13690  12831  12403    -86     72   -241       C  
ATOM   1654  CZ  PHE A 228      30.811  32.538   6.187  1.00107.17           C  
ANISOU 1654  CZ  PHE A 228    14244  13432  13044    -15    146   -159       C  
ATOM   1655  N   TYR A 229      36.840  33.138  10.149  1.00 93.86           N  
ANISOU 1655  N   TYR A 229    13049  11540  11073     35   -159   -505       N  
ATOM   1656  CA  TYR A 229      38.143  32.733  10.642  1.00 95.54           C  
ANISOU 1656  CA  TYR A 229    13282  11729  11289     -5   -247   -545       C  
ATOM   1657  C   TYR A 229      38.139  32.472  12.147  1.00103.66           C  
ANISOU 1657  C   TYR A 229    14445  12712  12231    105   -250   -547       C  
ATOM   1658  O   TYR A 229      38.782  31.537  12.625  1.00105.49           O  
ANISOU 1658  O   TYR A 229    14649  12954  12477     94   -267   -552       O  
ATOM   1659  CB  TYR A 229      39.171  33.798  10.290  1.00102.09           C  
ANISOU 1659  CB  TYR A 229    14147  12509  12134    -81   -371   -577       C  
ATOM   1660  CG  TYR A 229      40.596  33.372  10.521  1.00103.82           C  
ANISOU 1660  CG  TYR A 229    14339  12709  12398   -149   -469   -593       C  
ATOM   1661  CD1 TYR A 229      41.102  32.215   9.946  1.00 99.47           C  
ANISOU 1661  CD1 TYR A 229    13646  12219  11928   -212   -427   -580       C  
ATOM   1662  CD2 TYR A 229      41.443  34.136  11.302  1.00109.95           C  
ANISOU 1662  CD2 TYR A 229    15234  13396  13144   -152   -609   -613       C  
ATOM   1663  CE1 TYR A 229      42.416  31.828  10.156  1.00 95.31           C  
ANISOU 1663  CE1 TYR A 229    13082  11673  11458   -268   -506   -576       C  
ATOM   1664  CE2 TYR A 229      42.769  33.758  11.515  1.00109.20           C  
ANISOU 1664  CE2 TYR A 229    15098  13279  13114   -222   -711   -607       C  
ATOM   1665  CZ  TYR A 229      43.246  32.604  10.939  1.00 98.83           C  
ANISOU 1665  CZ  TYR A 229    13627  12036  11889   -276   -650   -582       C  
ATOM   1666  OH  TYR A 229      44.560  32.245  11.158  1.00 96.88           O  
ANISOU 1666  OH  TYR A 229    13328  11764  11718   -338   -741   -556       O  
ATOM   1667  N   SER A 230      37.388  33.280  12.887  1.00 98.02           N  
ANISOU 1667  N   SER A 230    13879  11945  11420    219   -224   -538       N  
ATOM   1668  CA  SER A 230      37.409  33.207  14.347  1.00112.65           C  
ANISOU 1668  CA  SER A 230    15901  13741  13158    341   -232   -544       C  
ATOM   1669  C   SER A 230      36.725  31.966  14.914  1.00104.06           C  
ANISOU 1669  C   SER A 230    14763  12705  12071    427   -105   -487       C  
ATOM   1670  O   SER A 230      36.963  31.600  16.068  1.00112.51           O  
ANISOU 1670  O   SER A 230    15945  13745  13058    512   -113   -488       O  
ATOM   1671  CB  SER A 230      36.754  34.447  14.949  1.00123.23           C  
ANISOU 1671  CB  SER A 230    17438  15001  14382    460   -222   -547       C  
ATOM   1672  OG  SER A 230      35.356  34.411  14.746  1.00129.07           O  
ANISOU 1672  OG  SER A 230    18133  15779  15130    549    -61   -474       O  
ATOM   1673  N   GLN A 231      35.864  31.337  14.114  1.00101.43           N  
ANISOU 1673  N   GLN A 231    14265  12443  11831    404      5   -431       N  
ATOM   1674  CA  GLN A 231      35.196  30.093  14.509  1.00108.47           C  
ANISOU 1674  CA  GLN A 231    15074  13381  12760    466    119   -362       C  
ATOM   1675  C   GLN A 231      36.098  28.883  14.344  1.00121.96           C  
ANISOU 1675  C   GLN A 231    16671  15126  14541    374     80   -387       C  
ATOM   1676  O   GLN A 231      35.855  27.825  14.931  1.00117.43           O  
ANISOU 1676  O   GLN A 231    16057  14575  13987    427    148   -342       O  
ATOM   1677  CB  GLN A 231      33.929  29.857  13.680  1.00114.30           C  
ANISOU 1677  CB  GLN A 231    15671  14167  13590    462    226   -283       C  
ATOM   1678  CG  GLN A 231      32.826  30.884  13.855  1.00127.87           C  
ANISOU 1678  CG  GLN A 231    17467  15855  15261    571    302   -223       C  
ATOM   1679  CD  GLN A 231      31.635  30.584  12.966  1.00144.94           C  
ANISOU 1679  CD  GLN A 231    19464  18065  17542    546    385   -129       C  
ATOM   1680  NE2 GLN A 231      31.029  31.634  12.406  1.00137.15           N  
ANISOU 1680  NE2 GLN A 231    18487  17065  16557    550    396   -104       N  
ATOM   1681  OE1 GLN A 231      31.269  29.418  12.774  1.00155.32           O  
ANISOU 1681  OE1 GLN A 231    20640  19420  18953    517    427    -76       O  
ATOM   1682  N   LEU A 232      37.125  29.025  13.517  1.00107.95           N  
ANISOU 1682  N   LEU A 232    14840  13358  12818    242    -19   -447       N  
ATOM   1683  CA  LEU A 232      37.875  27.852  13.118  1.00111.92           C  
ANISOU 1683  CA  LEU A 232    15216  13899  13410    155    -30   -458       C  
ATOM   1684  C   LEU A 232      39.284  27.844  13.676  1.00106.99           C  
ANISOU 1684  C   LEU A 232    14644  13240  12767    120   -141   -497       C  
ATOM   1685  O   LEU A 232      39.771  28.860  14.171  1.00101.29           O  
ANISOU 1685  O   LEU A 232    14052  12461  11974    134   -239   -526       O  
ATOM   1686  CB  LEU A 232      37.902  27.733  11.586  1.00106.50           C  
ANISOU 1686  CB  LEU A 232    14394  13253  12816     36    -27   -473       C  
ATOM   1687  CG  LEU A 232      38.764  28.659  10.727  1.00 94.19           C  
ANISOU 1687  CG  LEU A 232    12836  11683  11270    -58   -115   -517       C  
ATOM   1688  CD1 LEU A 232      40.137  28.095  10.549  1.00106.54           C  
ANISOU 1688  CD1 LEU A 232    14343  13248  12890   -134   -170   -539       C  
ATOM   1689  CD2 LEU A 232      38.132  28.818   9.376  1.00100.98           C  
ANISOU 1689  CD2 LEU A 232    13611  12582  12176   -119    -77   -511       C  
ATOM   1690  N   ASP A 233      39.911  26.670  13.611  1.00101.97           N  
ANISOU 1690  N   ASP A 233    13907  12634  12205     74   -131   -491       N  
ATOM   1691  CA  ASP A 233      41.334  26.498  13.898  1.00 95.94           C  
ANISOU 1691  CA  ASP A 233    13140  11845  11466     17   -232   -507       C  
ATOM   1692  C   ASP A 233      41.990  25.767  12.720  1.00103.64           C  
ANISOU 1692  C   ASP A 233    13955  12859  12563    -91   -209   -510       C  
ATOM   1693  O   ASP A 233      41.319  25.089  11.947  1.00108.06           O  
ANISOU 1693  O   ASP A 233    14426  13461  13172   -106   -115   -505       O  
ATOM   1694  CB  ASP A 233      41.553  25.722  15.200  1.00101.82           C  
ANISOU 1694  CB  ASP A 233    13938  12579  12172     92   -234   -482       C  
ATOM   1695  CG  ASP A 233      41.209  26.528  16.442  1.00128.27           C  
ANISOU 1695  CG  ASP A 233    17486  15875  15376    205   -278   -485       C  
ATOM   1696  OD1 ASP A 233      41.483  27.748  16.477  1.00152.66           O  
ANISOU 1696  OD1 ASP A 233    20689  18909  18407    193   -380   -520       O  
ATOM   1697  OD2 ASP A 233      40.670  25.931  17.396  1.00135.40           O1-
ANISOU 1697  OD2 ASP A 233    18442  16784  16220    313   -210   -449       O1-
ATOM   1698  N   VAL A 234      43.301  25.909  12.574  1.00 97.56           N  
ANISOU 1698  N   VAL A 234    13155  12067  11845   -161   -296   -510       N  
ATOM   1699  CA  VAL A 234      44.002  25.290  11.450  1.00103.35           C  
ANISOU 1699  CA  VAL A 234    13752  12830  12687   -245   -258   -502       C  
ATOM   1700  C   VAL A 234      45.139  24.390  11.891  1.00 98.01           C  
ANISOU 1700  C   VAL A 234    13012  12145  12083   -264   -278   -467       C  
ATOM   1701  O   VAL A 234      46.042  24.831  12.605  1.00106.53           O  
ANISOU 1701  O   VAL A 234    14130  13181  13165   -277   -394   -444       O  
ATOM   1702  CB  VAL A 234      44.595  26.341  10.502  1.00106.78           C  
ANISOU 1702  CB  VAL A 234    14166  13251  13153   -318   -315   -505       C  
ATOM   1703  CG1 VAL A 234      45.391  25.665   9.385  1.00106.34           C  
ANISOU 1703  CG1 VAL A 234    13983  13222  13199   -383   -255   -484       C  
ATOM   1704  CG2 VAL A 234      43.508  27.216   9.932  1.00 91.95           C  
ANISOU 1704  CG2 VAL A 234    12336  11384  11216   -306   -290   -532       C  
ATOM   1705  N   VAL A 235      45.102  23.131  11.461  1.00 92.32           N  
ANISOU 1705  N   VAL A 235    12196  11457  11425   -269   -176   -459       N  
ATOM   1706  CA  VAL A 235      46.246  22.254  11.664  1.00 91.56           C  
ANISOU 1706  CA  VAL A 235    12019  11352  11417   -292   -176   -417       C  
ATOM   1707  C   VAL A 235      46.606  21.495  10.407  1.00 97.22           C  
ANISOU 1707  C   VAL A 235    12630  12091  12220   -335    -76   -415       C  
ATOM   1708  O   VAL A 235      45.757  21.220   9.553  1.00104.17           O  
ANISOU 1708  O   VAL A 235    13504  12994  13082   -336      4   -455       O  
ATOM   1709  CB  VAL A 235      46.007  21.236  12.786  1.00100.58           C  
ANISOU 1709  CB  VAL A 235    13170  12497  12548   -228   -150   -397       C  
ATOM   1710  CG1 VAL A 235      45.836  21.937  14.119  1.00105.60           C  
ANISOU 1710  CG1 VAL A 235    13935  13105  13083   -171   -250   -393       C  
ATOM   1711  CG2 VAL A 235      44.790  20.354  12.463  1.00 97.14           C  
ANISOU 1711  CG2 VAL A 235    12708  12092  12107   -191    -27   -419       C  
ATOM   1712  N   GLY A 236      47.890  21.164  10.313  1.00 91.79           N  
ANISOU 1712  N   GLY A 236    11864  11386  11625   -367    -85   -361       N  
ATOM   1713  CA  GLY A 236      48.412  20.319   9.262  1.00 87.49           C  
ANISOU 1713  CA  GLY A 236    11230  10851  11162   -386     26   -346       C  
ATOM   1714  C   GLY A 236      48.741  18.959   9.862  1.00 99.50           C  
ANISOU 1714  C   GLY A 236    12697  12365  12744   -355     81   -316       C  
ATOM   1715  O   GLY A 236      49.242  18.870  10.983  1.00 98.37           O  
ANISOU 1715  O   GLY A 236    12548  12207  12621   -343      8   -269       O  
ATOM   1716  N   VAL A 237      48.404  17.886   9.156  1.00 93.78           N  
ANISOU 1716  N   VAL A 237    11943  11646  12042   -342    201   -345       N  
ATOM   1717  CA  VAL A 237      48.694  16.563   9.662  1.00 92.60           C  
ANISOU 1717  CA  VAL A 237    11740  11484  11959   -312    262   -316       C  
ATOM   1718  C   VAL A 237      49.080  15.657   8.532  1.00 87.13           C  
ANISOU 1718  C   VAL A 237    11004  10775  11326   -312    388   -322       C  
ATOM   1719  O   VAL A 237      48.751  15.914   7.377  1.00101.41           O  
ANISOU 1719  O   VAL A 237    12850  12586  13095   -327    432   -371       O  
ATOM   1720  CB  VAL A 237      47.497  15.917  10.388  1.00 97.23           C  
ANISOU 1720  CB  VAL A 237    12363  12078  12501   -271    274   -350       C  
ATOM   1721  CG1 VAL A 237      46.942  16.823  11.460  1.00 87.24           C  
ANISOU 1721  CG1 VAL A 237    11170  10826  11151   -246    174   -348       C  
ATOM   1722  CG2 VAL A 237      46.425  15.518   9.402  1.00 93.13           C  
ANISOU 1722  CG2 VAL A 237    11870  11559  11955   -277    344   -418       C  
ATOM   1723  N   SER A 238      49.779  14.586   8.878  1.00 84.54           N  
ANISOU 1723  N   SER A 238    10610  10426  11087   -289    447   -272       N  
ATOM   1724  CA  SER A 238      49.977  13.495   7.956  1.00 95.11           C  
ANISOU 1724  CA  SER A 238    11931  11734  12471   -269    580   -289       C  
ATOM   1725  C   SER A 238      49.276  12.258   8.517  1.00106.26           C  
ANISOU 1725  C   SER A 238    13344  13128  13903   -240    616   -315       C  
ATOM   1726  O   SER A 238      49.619  11.783   9.603  1.00101.13           O  
ANISOU 1726  O   SER A 238    12640  12478  13308   -220    596   -256       O  
ATOM   1727  CB  SER A 238      51.460  13.225   7.734  1.00 94.39           C  
ANISOU 1727  CB  SER A 238    11754  11622  12490   -257    645   -191       C  
ATOM   1728  OG  SER A 238      51.658  11.940   7.163  1.00 91.55           O  
ANISOU 1728  OG  SER A 238    11385  11220  12179   -217    783   -200       O  
ATOM   1729  N   SER A 239      48.291  11.747   7.785  1.00 99.11           N  
ANISOU 1729  N   SER A 239    12497  12202  12956   -242    659   -396       N  
ATOM   1730  CA  SER A 239      47.558  10.558   8.239  1.00 92.77           C  
ANISOU 1730  CA  SER A 239    11687  11371  12190   -221    687   -414       C  
ATOM   1731  C   SER A 239      48.403   9.288   8.176  1.00 99.67           C  
ANISOU 1731  C   SER A 239    12511  12195  13165   -190    789   -380       C  
ATOM   1732  O   SER A 239      48.160   8.334   8.904  1.00101.86           O  
ANISOU 1732  O   SER A 239    12749  12452  13502   -167    807   -357       O  
ATOM   1733  CB  SER A 239      46.295  10.376   7.415  1.00 92.08           C  
ANISOU 1733  CB  SER A 239    11674  11262  12051   -243    682   -499       C  
ATOM   1734  OG  SER A 239      45.428  11.471   7.616  1.00 99.20           O  
ANISOU 1734  OG  SER A 239    12607  12208  12875   -264    596   -514       O  
ATOM   1735  N   PHE A 240      49.386   9.287   7.289  1.00 98.40           N  
ANISOU 1735  N   PHE A 240    12351  12013  13024   -180    867   -366       N  
ATOM   1736  CA  PHE A 240      50.357   8.210   7.210  1.00104.92           C  
ANISOU 1736  CA  PHE A 240    13125  12789  13949   -138    981   -315       C  
ATOM   1737  C   PHE A 240      51.231   8.110   8.463  1.00112.67           C  
ANISOU 1737  C   PHE A 240    13991  13794  15026   -125    954   -199       C  
ATOM   1738  O   PHE A 240      51.335   7.043   9.081  1.00108.90           O  
ANISOU 1738  O   PHE A 240    13464  13288  14626    -97    995   -165       O  
ATOM   1739  CB  PHE A 240      51.251   8.398   5.985  1.00106.38           C  
ANISOU 1739  CB  PHE A 240    13339  12952  14130   -115   1083   -305       C  
ATOM   1740  CG  PHE A 240      50.582   8.062   4.687  1.00102.84           C  
ANISOU 1740  CG  PHE A 240    13024  12456  13596   -108   1138   -416       C  
ATOM   1741  CD1 PHE A 240      49.299   7.547   4.664  1.00114.82           C  
ANISOU 1741  CD1 PHE A 240    14611  13945  15070   -134   1083   -509       C  
ATOM   1742  CD2 PHE A 240      51.249   8.249   3.490  1.00110.05           C  
ANISOU 1742  CD2 PHE A 240    13995  13347  14473    -72   1241   -416       C  
ATOM   1743  CE1 PHE A 240      48.691   7.226   3.471  1.00116.32           C  
ANISOU 1743  CE1 PHE A 240    14935  14080  15181   -136   1106   -610       C  
ATOM   1744  CE2 PHE A 240      50.647   7.935   2.298  1.00112.11           C  
ANISOU 1744  CE2 PHE A 240    14405  13558  14635    -60   1281   -522       C  
ATOM   1745  CZ  PHE A 240      49.363   7.421   2.288  1.00116.81           C  
ANISOU 1745  CZ  PHE A 240    15078  14120  15185    -98   1201   -625       C  
ATOM   1746  N   THR A 241      51.857   9.222   8.838  1.00101.16           N  
ANISOU 1746  N   THR A 241    12493  12380  13564   -149    874   -135       N  
ATOM   1747  CA  THR A 241      52.860   9.196   9.900  1.00 97.57           C  
ANISOU 1747  CA  THR A 241    11934  11936  13203   -144    831    -14       C  
ATOM   1748  C   THR A 241      52.294   9.434  11.305  1.00 98.99           C  
ANISOU 1748  C   THR A 241    12118  12150  13342   -152    702     -5       C  
ATOM   1749  O   THR A 241      52.903   9.033  12.298  1.00117.08           O  
ANISOU 1749  O   THR A 241    14339  14442  15704   -139    671     83       O  
ATOM   1750  CB  THR A 241      53.941  10.236   9.634  1.00106.13           C  
ANISOU 1750  CB  THR A 241    12967  13033  14326   -170    791     71       C  
ATOM   1751  CG2 THR A 241      54.489  10.044   8.244  1.00107.62           C  
ANISOU 1751  CG2 THR A 241    13158  13190  14543   -143    938     77       C  
ATOM   1752  OG1 THR A 241      53.359  11.542   9.728  1.00102.49           O  
ANISOU 1752  OG1 THR A 241    12571  12609  13760   -213    664     22       O  
ATOM   1753  N   GLY A 242      51.141  10.090  11.392  1.00 94.15           N  
ANISOU 1753  N   GLY A 242    11592  11565  12615   -167    633    -87       N  
ATOM   1754  CA  GLY A 242      50.604  10.487  12.684  1.00100.48           C  
ANISOU 1754  CA  GLY A 242    12423  12399  13357   -157    522    -75       C  
ATOM   1755  C   GLY A 242      51.156  11.834  13.126  1.00 99.97           C  
ANISOU 1755  C   GLY A 242    12380  12355  13249   -187    387    -39       C  
ATOM   1756  O   GLY A 242      50.858  12.322  14.225  1.00106.68           O  
ANISOU 1756  O   GLY A 242    13281  13222  14031   -173    281    -27       O  
ATOM   1757  N   ASP A 243      51.986  12.428  12.270  1.00 97.89           N  
ANISOU 1757  N   ASP A 243    12085  12081  13026   -224    391    -15       N  
ATOM   1758  CA  ASP A 243      52.485  13.785  12.489  1.00102.48           C  
ANISOU 1758  CA  ASP A 243    12687  12669  13582   -266    255     17       C  
ATOM   1759  C   ASP A 243      51.321  14.778  12.518  1.00102.20           C  
ANISOU 1759  C   ASP A 243    12770  12656  13405   -270    186    -76       C  
ATOM   1760  O   ASP A 243      50.539  14.876  11.568  1.00105.73           O  
ANISOU 1760  O   ASP A 243    13257  13114  13803   -272    255   -153       O  
ATOM   1761  CB  ASP A 243      53.510  14.151  11.400  1.00117.19           C  
ANISOU 1761  CB  ASP A 243    14478  14515  15533   -297    302     73       C  
ATOM   1762  CG  ASP A 243      54.064  15.564  11.545  1.00130.68           C  
ANISOU 1762  CG  ASP A 243    16191  16218  17242   -349    154    118       C  
ATOM   1763  OD1 ASP A 243      54.171  16.060  12.692  1.00122.71           O  
ANISOU 1763  OD1 ASP A 243    15216  15203  16206   -365     -1    144       O  
ATOM   1764  OD2 ASP A 243      54.400  16.175  10.499  1.00116.04           O1-
ANISOU 1764  OD2 ASP A 243    14316  14361  15413   -372    191    131       O1-
ATOM   1765  N   GLY A 244      51.189  15.487  13.634  1.00103.07           N  
ANISOU 1765  N   GLY A 244    12947  12769  13447   -265     50    -66       N  
ATOM   1766  CA  GLY A 244      50.212  16.557  13.737  1.00 98.05           C  
ANISOU 1766  CA  GLY A 244    12428  12146  12681   -260    -17   -138       C  
ATOM   1767  C   GLY A 244      48.975  16.209  14.537  1.00103.91           C  
ANISOU 1767  C   GLY A 244    13248  12906  13328   -194      5   -179       C  
ATOM   1768  O   GLY A 244      48.130  17.076  14.806  1.00103.98           O  
ANISOU 1768  O   GLY A 244    13359  12921  13226   -171    -43   -223       O  
ATOM   1769  N   PHE A 245      48.860  14.948  14.939  1.00 95.87           N  
ANISOU 1769  N   PHE A 245    12176  11892  12359   -155     84   -152       N  
ATOM   1770  CA  PHE A 245      47.614  14.492  15.545  1.00 99.40           C  
ANISOU 1770  CA  PHE A 245    12670  12355  12741    -88    133   -172       C  
ATOM   1771  C   PHE A 245      47.490  14.900  17.007  1.00109.71           C  
ANISOU 1771  C   PHE A 245    14071  13663  13950    -26     43   -139       C  
ATOM   1772  O   PHE A 245      46.381  15.140  17.504  1.00 94.52           O  
ANISOU 1772  O   PHE A 245    12228  11752  11931     39     62   -156       O  
ATOM   1773  CB  PHE A 245      47.474  12.986  15.357  1.00 94.81           C  
ANISOU 1773  CB  PHE A 245    11996  11769  12258    -71    253   -153       C  
ATOM   1774  CG  PHE A 245      46.848  12.631  14.040  1.00 96.29           C  
ANISOU 1774  CG  PHE A 245    12159  11949  12479   -103    344   -215       C  
ATOM   1775  CD1 PHE A 245      47.575  12.733  12.866  1.00 93.15           C  
ANISOU 1775  CD1 PHE A 245    11727  11536  12128   -156    372   -238       C  
ATOM   1776  CD2 PHE A 245      45.521  12.249  13.969  1.00 90.58           C  
ANISOU 1776  CD2 PHE A 245    11452  11229  11737    -75    393   -241       C  
ATOM   1777  CE1 PHE A 245      46.999  12.449  11.644  1.00 91.43           C  
ANISOU 1777  CE1 PHE A 245    11517  11306  11917   -180    442   -302       C  
ATOM   1778  CE2 PHE A 245      44.930  11.961  12.742  1.00 91.34           C  
ANISOU 1778  CE2 PHE A 245    11539  11308  11860   -114    446   -299       C  
ATOM   1779  CZ  PHE A 245      45.674  12.068  11.576  1.00 91.03           C  
ANISOU 1779  CZ  PHE A 245    11491  11253  11844   -165    467   -337       C  
ATOM   1780  N   ASP A 246      48.629  15.016  17.676  1.00105.35           N  
ANISOU 1780  N   ASP A 246    13514  13094  13420    -43    -58    -84       N  
ATOM   1781  CA  ASP A 246      48.681  15.641  18.991  1.00114.63           C  
ANISOU 1781  CA  ASP A 246    14817  14257  14480      6   -183    -63       C  
ATOM   1782  C   ASP A 246      48.051  17.025  18.932  1.00111.81           C  
ANISOU 1782  C   ASP A 246    14599  13889  13994     15   -252   -126       C  
ATOM   1783  O   ASP A 246      47.129  17.334  19.692  1.00115.47           O  
ANISOU 1783  O   ASP A 246    15187  14356  14330    102   -246   -142       O  
ATOM   1784  CB  ASP A 246      50.127  15.753  19.487  1.00135.61           C  
ANISOU 1784  CB  ASP A 246    17446  16884  17197    -44   -320      6       C  
ATOM   1785  CG  ASP A 246      50.797  14.405  19.651  1.00147.95           C  
ANISOU 1785  CG  ASP A 246    18872  18455  18890    -45   -253     84       C  
ATOM   1786  OD1 ASP A 246      51.174  13.794  18.624  1.00152.61           O  
ANISOU 1786  OD1 ASP A 246    19328  19047  19610    -89   -149     94       O  
ATOM   1787  OD2 ASP A 246      50.955  13.967  20.811  1.00151.29           O1-
ANISOU 1787  OD2 ASP A 246    19329  18877  19276      5   -300    138       O1-
ATOM   1788  N   GLU A 247      48.564  17.851  18.022  1.00110.52           N  
ANISOU 1788  N   GLU A 247    14413  13709  13871    -67   -307   -152       N  
ATOM   1789  CA  GLU A 247      48.079  19.214  17.846  1.00113.11           C  
ANISOU 1789  CA  GLU A 247    14860  14019  14097    -70   -377   -210       C  
ATOM   1790  C   GLU A 247      46.594  19.213  17.518  1.00109.16           C  
ANISOU 1790  C   GLU A 247    14397  13551  13529    -10   -254   -259       C  
ATOM   1791  O   GLU A 247      45.862  20.080  17.987  1.00 98.60           O  
ANISOU 1791  O   GLU A 247    13196  12201  12067     48   -287   -287       O  
ATOM   1792  CB  GLU A 247      48.849  19.943  16.737  1.00103.06           C  
ANISOU 1792  CB  GLU A 247    13521  12730  12908   -170   -426   -215       C  
ATOM   1793  CG  GLU A 247      50.301  20.296  17.066  1.00127.37           C  
ANISOU 1793  CG  GLU A 247    16568  15762  16063   -237   -581   -148       C  
ATOM   1794  CD  GLU A 247      51.267  19.135  16.864  1.00125.01           C  
ANISOU 1794  CD  GLU A 247    16105  15473  15918   -268   -524    -68       C  
ATOM   1795  OE1 GLU A 247      50.813  17.974  16.857  1.00130.90           O  
ANISOU 1795  OE1 GLU A 247    16798  16255  16684   -222   -386    -69       O  
ATOM   1796  OE2 GLU A 247      52.483  19.384  16.706  1.00126.74           O1-
ANISOU 1796  OE2 GLU A 247    16244  15660  16250   -337   -614      8       O1-
ATOM   1797  N   PHE A 248      46.162  18.245  16.710  1.00113.16           N  
ANISOU 1797  N   PHE A 248    14786  14089  14121    -22   -118   -261       N  
ATOM   1798  CA  PHE A 248      44.757  18.162  16.318  1.00101.83           C  
ANISOU 1798  CA  PHE A 248    13361  12677  12651     19    -15   -290       C  
ATOM   1799  C   PHE A 248      43.902  17.989  17.563  1.00100.29           C  
ANISOU 1799  C   PHE A 248    13252  12487  12366    134     14   -255       C  
ATOM   1800  O   PHE A 248      42.943  18.738  17.774  1.00103.97           O  
ANISOU 1800  O   PHE A 248    13813  12953  12739    194     27   -267       O  
ATOM   1801  CB  PHE A 248      44.511  17.022  15.318  1.00104.27           C  
ANISOU 1801  CB  PHE A 248    13540  13003  13075    -19    100   -295       C  
ATOM   1802  CG  PHE A 248      43.051  16.813  14.978  1.00 98.44           C  
ANISOU 1802  CG  PHE A 248    12798  12279  12326     15    185   -305       C  
ATOM   1803  CD1 PHE A 248      42.383  17.691  14.136  1.00 98.39           C  
ANISOU 1803  CD1 PHE A 248    12823  12279  12283    -13    179   -347       C  
ATOM   1804  CD2 PHE A 248      42.352  15.748  15.512  1.00 93.97           C  
ANISOU 1804  CD2 PHE A 248    12188  11718  11800     73    264   -259       C  
ATOM   1805  CE1 PHE A 248      41.042  17.508  13.830  1.00 97.36           C  
ANISOU 1805  CE1 PHE A 248    12677  12158  12160     11    243   -338       C  
ATOM   1806  CE2 PHE A 248      41.008  15.554  15.213  1.00 99.34           C  
ANISOU 1806  CE2 PHE A 248    12847  12403  12496     98    330   -245       C  
ATOM   1807  CZ  PHE A 248      40.349  16.442  14.375  1.00 95.64           C  
ANISOU 1807  CZ  PHE A 248    12406  11938  11993     65    315   -283       C  
ATOM   1808  N   MET A 249      44.275  17.036  18.409  1.00103.10           N  
ANISOU 1808  N   MET A 249    13579  12846  12749    174     29   -203       N  
ATOM   1809  CA  MET A 249      43.496  16.776  19.611  1.00110.99           C  
ANISOU 1809  CA  MET A 249    14657  13853  13663    298     74   -154       C  
ATOM   1810  C   MET A 249      43.518  17.959  20.568  1.00111.10           C  
ANISOU 1810  C   MET A 249    14864  13839  13509    366    -27   -166       C  
ATOM   1811  O   MET A 249      42.560  18.183  21.315  1.00108.59           O  
ANISOU 1811  O   MET A 249    14653  13523  13085    486     30   -140       O  
ATOM   1812  CB  MET A 249      43.991  15.519  20.318  1.00100.24           C  
ANISOU 1812  CB  MET A 249    13223  12498  12363    325    105    -89       C  
ATOM   1813  CG  MET A 249      43.540  14.239  19.646  1.00105.54           C  
ANISOU 1813  CG  MET A 249    13736  13185  13178    302    233    -66       C  
ATOM   1814  SD  MET A 249      41.823  14.276  19.080  1.00108.86           S  
ANISOU 1814  SD  MET A 249    14137  13617  13609    339    344    -65       S  
ATOM   1815  CE  MET A 249      40.914  14.414  20.618  1.00 88.56           C  
ANISOU 1815  CE  MET A 249    11676  11056  10916    508    395     21       C  
ATOM   1816  N   GLN A 250      44.608  18.717  20.541  1.00112.84           N  
ANISOU 1816  N   GLN A 250    15137  14026  13711    296   -175   -199       N  
ATOM   1817  CA  GLN A 250      44.690  19.927  21.342  1.00101.95           C  
ANISOU 1817  CA  GLN A 250    13962  12601  12175    345   -300   -225       C  
ATOM   1818  C   GLN A 250      43.611  20.898  20.910  1.00105.58           C  
ANISOU 1818  C   GLN A 250    14501  13056  12559    384   -250   -268       C  
ATOM   1819  O   GLN A 250      42.884  21.439  21.745  1.00113.83           O  
ANISOU 1819  O   GLN A 250    15712  14080  13457    505   -234   -265       O  
ATOM   1820  CB  GLN A 250      46.056  20.586  21.208  1.00122.15           C  
ANISOU 1820  CB  GLN A 250    16534  15113  14765    238   -484   -243       C  
ATOM   1821  CG  GLN A 250      47.202  19.820  21.820  1.00129.79           C  
ANISOU 1821  CG  GLN A 250    17447  16073  15796    206   -566   -184       C  
ATOM   1822  CD  GLN A 250      48.484  20.638  21.823  1.00139.72           C  
ANISOU 1822  CD  GLN A 250    18732  17269  17085    106   -774   -182       C  
ATOM   1823  NE2 GLN A 250      49.602  19.981  22.099  1.00133.75           N  
ANISOU 1823  NE2 GLN A 250    17881  16506  16432     51   -847   -113       N  
ATOM   1824  OE1 GLN A 250      48.466  21.849  21.578  1.00145.73           O  
ANISOU 1824  OE1 GLN A 250    19592  17986  17791     77   -870   -230       O  
ATOM   1825  N   CYS A 251      43.518  21.118  19.600  1.00 94.60           N  
ANISOU 1825  N   CYS A 251    12997  11682  11265    290   -220   -302       N  
ATOM   1826  CA  CYS A 251      42.481  21.980  19.036  1.00104.20           C  
ANISOU 1826  CA  CYS A 251    14258  12900  12435    314   -168   -333       C  
ATOM   1827  C   CYS A 251      41.100  21.504  19.414  1.00114.38           C  
ANISOU 1827  C   CYS A 251    15551  14216  13691    431    -16   -284       C  
ATOM   1828  O   CYS A 251      40.251  22.304  19.810  1.00116.49           O  
ANISOU 1828  O   CYS A 251    15944  14466  13850    527     14   -279       O  
ATOM   1829  CB  CYS A 251      42.579  22.036  17.516  1.00115.64           C  
ANISOU 1829  CB  CYS A 251    15565  14371  14002    194   -145   -365       C  
ATOM   1830  SG  CYS A 251      43.939  23.010  16.902  1.00132.45           S  
ANISOU 1830  SG  CYS A 251    17697  16462  16167     72   -303   -404       S  
ATOM   1831  N   VAL A 252      40.877  20.197  19.263  1.00103.17           N  
ANISOU 1831  N   VAL A 252    13986  12834  12379    426     81   -237       N  
ATOM   1832  CA  VAL A 252      39.594  19.614  19.596  1.00 97.92           C  
ANISOU 1832  CA  VAL A 252    13291  12192  11723    529    223   -165       C  
ATOM   1833  C   VAL A 252      39.264  19.916  21.045  1.00 97.95           C  
ANISOU 1833  C   VAL A 252    13464  12177  11574    688    242   -118       C  
ATOM   1834  O   VAL A 252      38.207  20.467  21.347  1.00103.57           O  
ANISOU 1834  O   VAL A 252    14258  12883  12212    797    321    -81       O  
ATOM   1835  CB  VAL A 252      39.578  18.107  19.395  1.00 97.02           C  
ANISOU 1835  CB  VAL A 252    13009  12105  11751    499    301   -117       C  
ATOM   1836  CG1 VAL A 252      38.281  17.549  19.929  1.00 93.47           C  
ANISOU 1836  CG1 VAL A 252    12530  11669  11317    616    436    -19       C  
ATOM   1837  CG2 VAL A 252      39.740  17.768  17.928  1.00 98.09           C  
ANISOU 1837  CG2 VAL A 252    13003  12249  12018    363    299   -165       C  
ATOM   1838  N   ASP A 253      40.185  19.559  21.934  1.00100.91           N  
ANISOU 1838  N   ASP A 253    13900  12540  11901    707    171   -113       N  
ATOM   1839  CA  ASP A 253      40.032  19.859  23.350  1.00104.15           C  
ANISOU 1839  CA  ASP A 253    14507  12926  12139    860    167    -78       C  
ATOM   1840  C   ASP A 253      39.800  21.368  23.580  1.00119.77           C  
ANISOU 1840  C   ASP A 253    16700  14852  13955    917    102   -133       C  
ATOM   1841  O   ASP A 253      38.967  21.738  24.406  1.00123.63           O  
ANISOU 1841  O   ASP A 253    17341  15325  14309   1079    184    -91       O  
ATOM   1842  CB  ASP A 253      41.257  19.360  24.132  1.00103.53           C  
ANISOU 1842  CB  ASP A 253    14465  12835  12036    839     53    -76       C  
ATOM   1843  CG  ASP A 253      41.335  17.837  24.188  1.00119.60           C  
ANISOU 1843  CG  ASP A 253    16319  14915  14208    829    144     -3       C  
ATOM   1844  OD1 ASP A 253      40.312  17.176  23.895  1.00114.39           O  
ANISOU 1844  OD1 ASP A 253    15542  14287  13633    870    297     56       O  
ATOM   1845  OD2 ASP A 253      42.409  17.299  24.535  1.00122.36           O1-
ANISOU 1845  OD2 ASP A 253    16640  15262  14590    779     57      4       O1-
ATOM   1846  N   LYS A 254      40.512  22.226  22.843  1.00117.32           N  
ANISOU 1846  N   LYS A 254    16401  14513  13663    792    -34   -217       N  
ATOM   1847  CA  LYS A 254      40.327  23.684  22.949  1.00124.57           C  
ANISOU 1847  CA  LYS A 254    17513  15371  14446    830   -106   -274       C  
ATOM   1848  C   LYS A 254      38.893  24.068  22.606  1.00126.89           C  
ANISOU 1848  C   LYS A 254    17803  15680  14728    919     53   -239       C  
ATOM   1849  O   LYS A 254      38.232  24.780  23.359  1.00130.76           O  
ANISOU 1849  O   LYS A 254    18485  16131  15066   1066     98   -225       O  
ATOM   1850  CB  LYS A 254      41.311  24.436  22.034  1.00119.20           C  
ANISOU 1850  CB  LYS A 254    16795  14662  13834    664   -266   -352       C  
ATOM   1851  CG  LYS A 254      41.231  25.968  22.076  1.00128.19           C  
ANISOU 1851  CG  LYS A 254    18124  15726  14854    683   -362   -415       C  
ATOM   1852  CD  LYS A 254      40.632  26.521  20.779  1.00149.71           C  
ANISOU 1852  CD  LYS A 254    20737  18476  17669    615   -299   -434       C  
ATOM   1853  CE  LYS A 254      40.585  28.049  20.760  1.00159.95           C  
ANISOU 1853  CE  LYS A 254    22212  19697  18866    627   -394   -492       C  
ATOM   1854  NZ  LYS A 254      39.830  28.585  19.585  1.00159.28           N1+
ANISOU 1854  NZ  LYS A 254    22025  19640  18854    584   -312   -495       N1+
ATOM   1855  N   LYS A 255      38.401  23.572  21.477  1.00127.24           N  
ANISOU 1855  N   LYS A 255    17634  15778  14934    835    139   -217       N  
ATOM   1856  CA  LYS A 255      37.045  23.892  21.063  1.00114.60           C  
ANISOU 1856  CA  LYS A 255    15999  14191  13351    901    275   -167       C  
ATOM   1857  C   LYS A 255      36.018  23.252  21.997  1.00107.82           C  
ANISOU 1857  C   LYS A 255    15158  13350  12460   1074    440    -49       C  
ATOM   1858  O   LYS A 255      34.873  23.700  22.068  1.00103.43           O  
ANISOU 1858  O   LYS A 255    14633  12788  11877   1183    559     18       O  
ATOM   1859  CB  LYS A 255      36.812  23.465  19.606  1.00107.02           C  
ANISOU 1859  CB  LYS A 255    14814  13277  12572    757    301   -171       C  
ATOM   1860  CG  LYS A 255      37.515  24.370  18.562  1.00111.80           C  
ANISOU 1860  CG  LYS A 255    15413  13867  13198    617    177   -266       C  
ATOM   1861  CD  LYS A 255      37.150  25.846  18.765  1.00127.56           C  
ANISOU 1861  CD  LYS A 255    17584  15813  15070    683    147   -294       C  
ATOM   1862  CE  LYS A 255      37.660  26.769  17.653  1.00109.50           C  
ANISOU 1862  CE  LYS A 255    15271  13513  12822    550     44   -367       C  
ATOM   1863  NZ  LYS A 255      37.134  28.156  17.858  1.00116.85           N1+
ANISOU 1863  NZ  LYS A 255    16366  14390  13642    626     34   -383       N1+
ATOM   1864  N   VAL A 256      36.419  22.230  22.745  1.00112.99           N  
ANISOU 1864  N   VAL A 256    15790  14021  13118   1109    455     -9       N  
ATOM   1865  CA  VAL A 256      35.442  21.525  23.575  1.00112.86           C  
ANISOU 1865  CA  VAL A 256    15763  14025  13095   1273    624    122       C  
ATOM   1866  C   VAL A 256      34.997  22.303  24.818  1.00122.78           C  
ANISOU 1866  C   VAL A 256    17279  15237  14135   1483    682    158       C  
ATOM   1867  O   VAL A 256      33.802  22.467  25.023  1.00137.98           O  
ANISOU 1867  O   VAL A 256    19210  17164  16051   1621    843    262       O  
ATOM   1868  CB  VAL A 256      35.946  20.148  24.027  1.00112.21           C  
ANISOU 1868  CB  VAL A 256    15574  13974  13087   1259    637    168       C  
ATOM   1869  CG1 VAL A 256      35.133  19.669  25.212  1.00 98.42           C  
ANISOU 1869  CG1 VAL A 256    13888  12235  11273   1463    793    303       C  
ATOM   1870  CG2 VAL A 256      35.832  19.150  22.888  1.00115.06           C  
ANISOU 1870  CG2 VAL A 256    15669  14374  13675   1113    661    183       C  
ATOM   1871  N   ASP A 257      35.914  22.772  25.662  1.00126.87           N  
ANISOU 1871  N   ASP A 257    18017  15710  14480   1518    555     84       N  
ATOM   1872  CA  ASP A 257      35.455  23.477  26.867  1.00133.65           C  
ANISOU 1872  CA  ASP A 257    19156  16516  15110   1736    615    114       C  
ATOM   1873  C   ASP A 257      34.860  24.832  26.507  1.00122.80           C  
ANISOU 1873  C   ASP A 257    17909  15091  13660   1778    629     75       C  
ATOM   1874  O   ASP A 257      34.050  25.376  27.254  1.00116.65           O  
ANISOU 1874  O   ASP A 257    17314  14274  12733   1980    753    134       O  
ATOM   1875  CB  ASP A 257      36.577  23.652  27.886  1.00142.23           C  
ANISOU 1875  CB  ASP A 257    20473  17552  16017   1761    450     42       C  
ATOM   1876  CG  ASP A 257      37.898  23.945  27.241  1.00155.80           C  
ANISOU 1876  CG  ASP A 257    22152  19249  17796   1546    214    -83       C  
ATOM   1877  OD1 ASP A 257      37.897  24.322  26.051  1.00156.93           O  
ANISOU 1877  OD1 ASP A 257    22152  19404  18072   1405    184   -129       O  
ATOM   1878  OD2 ASP A 257      38.934  23.796  27.924  1.00160.77           O1-
ANISOU 1878  OD2 ASP A 257    22889  19849  18348   1521     61   -121       O1-
ATOM   1879  N   GLU A 258      35.254  25.358  25.350  1.00124.28           N  
ANISOU 1879  N   GLU A 258    17994  15276  13951   1597    515    -14       N  
ATOM   1880  CA  GLU A 258      34.687  26.597  24.836  1.00133.13           C  
ANISOU 1880  CA  GLU A 258    19193  16356  15035   1613    528    -45       C  
ATOM   1881  C   GLU A 258      33.224  26.384  24.445  1.00135.89           C  
ANISOU 1881  C   GLU A 258    19394  16747  15490   1699    745     89       C  
ATOM   1882  O   GLU A 258      32.430  27.327  24.437  1.00132.42           O  
ANISOU 1882  O   GLU A 258    19057  16270  14986   1803    826    116       O  
ATOM   1883  CB  GLU A 258      35.500  27.112  23.632  1.00139.81           C  
ANISOU 1883  CB  GLU A 258    19939  17199  15985   1391    357   -158       C  
ATOM   1884  CG  GLU A 258      36.870  27.711  23.987  1.00144.07           C  
ANISOU 1884  CG  GLU A 258    20648  17669  16422   1313    126   -278       C  
ATOM   1885  CD  GLU A 258      37.576  28.358  22.796  1.00142.88           C  
ANISOU 1885  CD  GLU A 258    20399  17508  16379   1115    -20   -365       C  
ATOM   1886  OE1 GLU A 258      37.122  28.158  21.644  1.00139.56           O  
ANISOU 1886  OE1 GLU A 258    19767  17147  16114   1024     52   -342       O  
ATOM   1887  OE2 GLU A 258      38.586  29.068  23.020  1.00135.56           O1-
ANISOU 1887  OE2 GLU A 258    19612  16511  15385   1052   -212   -448       O1-
ATOM   1888  N   TYR A 259      32.877  25.134  24.143  1.00125.56           N  
ANISOU 1888  N   TYR A 259    17844  15509  14353   1657    833    181       N  
ATOM   1889  CA  TYR A 259      31.556  24.789  23.613  1.00117.08           C  
ANISOU 1889  CA  TYR A 259    16578  14473  13432   1695   1005    321       C  
ATOM   1890  C   TYR A 259      30.413  25.255  24.513  1.00132.03           C  
ANISOU 1890  C   TYR A 259    18610  16337  15219   1945   1198    453       C  
ATOM   1891  O   TYR A 259      29.371  25.686  24.024  1.00103.47           O  
ANISOU 1891  O   TYR A 259    14915  12720  11679   1985   1307    543       O  
ATOM   1892  CB  TYR A 259      31.453  23.276  23.402  1.00110.46           C  
ANISOU 1892  CB  TYR A 259    15495  13695  12779   1628   1053    403       C  
ATOM   1893  CG  TYR A 259      30.321  22.816  22.513  1.00107.47           C  
ANISOU 1893  CG  TYR A 259    14870  13350  12613   1584   1154    523       C  
ATOM   1894  CD1 TYR A 259      30.439  22.852  21.126  1.00 95.61           C  
ANISOU 1894  CD1 TYR A 259    13211  11867  11251   1385   1056    454       C  
ATOM   1895  CD2 TYR A 259      29.137  22.330  23.058  1.00104.61           C  
ANISOU 1895  CD2 TYR A 259    14432  12996  12317   1741   1343    715       C  
ATOM   1896  CE1 TYR A 259      29.403  22.426  20.302  1.00 95.82           C  
ANISOU 1896  CE1 TYR A 259    13024  11913  11469   1335   1121    563       C  
ATOM   1897  CE2 TYR A 259      28.095  21.903  22.246  1.00107.08           C  
ANISOU 1897  CE2 TYR A 259    14510  13329  12846   1688   1412    839       C  
ATOM   1898  CZ  TYR A 259      28.233  21.947  20.869  1.00106.01           C  
ANISOU 1898  CZ  TYR A 259    14234  13207  12840   1480   1289    757       C  
ATOM   1899  OH  TYR A 259      27.200  21.512  20.061  1.00110.39           O  
ANISOU 1899  OH  TYR A 259    14567  13771  13604   1419   1331    880       O  
ATOM   1900  N   ASP A 260      30.609  25.154  25.823  1.00151.10           N  
ANISOU 1900  N   ASP A 260    21231  18725  17456   2118   1245    476       N  
ATOM   1901  CA  ASP A 260      29.584  25.558  26.775  1.00148.78           C  
ANISOU 1901  CA  ASP A 260    21097  18397  17035   2385   1449    610       C  
ATOM   1902  C   ASP A 260      29.254  27.031  26.594  1.00151.84           C  
ANISOU 1902  C   ASP A 260    21669  18718  17307   2446   1449    557       C  
ATOM   1903  O   ASP A 260      28.087  27.427  26.523  1.00143.58           O  
ANISOU 1903  O   ASP A 260    20593  17662  16297   2576   1627    689       O  
ATOM   1904  CB  ASP A 260      30.047  25.289  28.206  1.00156.61           C  
ANISOU 1904  CB  ASP A 260    22330  19363  17813   2555   1467    612       C  
ATOM   1905  CG  ASP A 260      29.020  24.527  29.012  1.00162.62           C  
ANISOU 1905  CG  ASP A 260    23039  20152  18595   2773   1717    828       C  
ATOM   1906  OD1 ASP A 260      28.321  23.672  28.426  1.00148.47           O  
ANISOU 1906  OD1 ASP A 260    20946  18419  17048   2716   1817    963       O  
ATOM   1907  OD2 ASP A 260      28.910  24.790  30.228  1.00179.36           O1-
ANISOU 1907  OD2 ASP A 260    25429  22231  20490   3005   1811    867       O1-
ATOM   1908  N   GLN A 261      30.304  27.832  26.492  1.00152.38           N  
ANISOU 1908  N   GLN A 261    21914  18733  17250   2345   1242    372       N  
ATOM   1909  CA  GLN A 261      30.163  29.272  26.396  1.00153.51           C  
ANISOU 1909  CA  GLN A 261    22265  18796  17267   2397   1212    299       C  
ATOM   1910  C   GLN A 261      29.559  29.730  25.071  1.00159.26           C  
ANISOU 1910  C   GLN A 261    22781  19550  18179   2272   1229    321       C  
ATOM   1911  O   GLN A 261      28.563  30.455  25.053  1.00166.25           O  
ANISOU 1911  O   GLN A 261    23715  20404  19047   2405   1374    408       O  
ATOM   1912  CB  GLN A 261      31.523  29.943  26.601  1.00145.27           C  
ANISOU 1912  CB  GLN A 261    21442  17683  16072   2296    956    103       C  
ATOM   1913  CG  GLN A 261      31.512  31.435  26.341  1.00151.46           C  
ANISOU 1913  CG  GLN A 261    22418  18374  16755   2306    885     12       C  
ATOM   1914  CD  GLN A 261      32.737  32.135  26.890  1.00153.54           C  
ANISOU 1914  CD  GLN A 261    22963  18539  16837   2264    644   -155       C  
ATOM   1915  NE2 GLN A 261      32.738  33.462  26.808  1.00165.59           N  
ANISOU 1915  NE2 GLN A 261    24693  19964  18258   2290    576   -236       N  
ATOM   1916  OE1 GLN A 261      33.663  31.499  27.399  1.00133.88           O  
ANISOU 1916  OE1 GLN A 261    20508  16056  14305   2209    514   -203       O  
ATOM   1917  N   TYR A 262      30.156  29.300  23.966  1.00143.92           N  
ANISOU 1917  N   TYR A 262    20611  17663  16410   2026   1088    251       N  
ATOM   1918  CA  TYR A 262      29.889  29.925  22.674  1.00133.11           C  
ANISOU 1918  CA  TYR A 262    19098  16306  15172   1884   1044    226       C  
ATOM   1919  C   TYR A 262      28.813  29.245  21.835  1.00138.34           C  
ANISOU 1919  C   TYR A 262    19463  17040  16060   1841   1171    373       C  
ATOM   1920  O   TYR A 262      27.962  29.915  21.242  1.00147.95           O  
ANISOU 1920  O   TYR A 262    20623  18250  17341   1857   1240    438       O  
ATOM   1921  CB  TYR A 262      31.182  29.993  21.864  1.00126.05           C  
ANISOU 1921  CB  TYR A 262    18149  15421  14324   1645    813     64       C  
ATOM   1922  CG  TYR A 262      32.265  30.829  22.509  1.00134.99           C  
ANISOU 1922  CG  TYR A 262    19554  16467  15268   1652    647    -77       C  
ATOM   1923  CD1 TYR A 262      32.373  32.189  22.242  1.00136.73           C  
ANISOU 1923  CD1 TYR A 262    19925  16614  15413   1643    568   -155       C  
ATOM   1924  CD2 TYR A 262      33.183  30.259  23.381  1.00144.09           C  
ANISOU 1924  CD2 TYR A 262    20812  17607  16328   1662    555   -126       C  
ATOM   1925  CE1 TYR A 262      33.367  32.959  22.827  1.00136.68           C  
ANISOU 1925  CE1 TYR A 262    20170  16513  15248   1638    392   -280       C  
ATOM   1926  CE2 TYR A 262      34.179  31.021  23.973  1.00147.99           C  
ANISOU 1926  CE2 TYR A 262    21557  18013  16661   1656    374   -247       C  
ATOM   1927  CZ  TYR A 262      34.267  32.371  23.692  1.00143.40           C  
ANISOU 1927  CZ  TYR A 262    21125  17350  16012   1642    288   -325       C  
ATOM   1928  OH  TYR A 262      35.257  33.133  24.278  1.00136.46           O  
ANISOU 1928  OH  TYR A 262    20496  16366  14985   1626     85   -441       O  
ATOM   1929  N   TYR A 263      28.847  27.919  21.786  1.00137.15           N  
ANISOU 1929  N   TYR A 263    19122  16950  16037   1782   1190    431       N  
ATOM   1930  CA  TYR A 263      28.077  27.193  20.783  1.00123.71           C  
ANISOU 1930  CA  TYR A 263    17126  15306  14571   1676   1238    536       C  
ATOM   1931  C   TYR A 263      26.806  26.518  21.309  1.00128.84           C  
ANISOU 1931  C   TYR A 263    17662  15972  15319   1835   1445    758       C  
ATOM   1932  O   TYR A 263      25.934  26.146  20.518  1.00115.09           O  
ANISOU 1932  O   TYR A 263    15693  14258  13777   1771   1490    875       O  
ATOM   1933  CB  TYR A 263      28.976  26.146  20.109  1.00120.39           C  
ANISOU 1933  CB  TYR A 263    16544  14933  14266   1469   1099    448       C  
ATOM   1934  CG  TYR A 263      29.979  26.728  19.127  1.00114.75           C  
ANISOU 1934  CG  TYR A 263    15841  14217  13543   1278    914    277       C  
ATOM   1935  CD1 TYR A 263      31.261  27.090  19.533  1.00119.95           C  
ANISOU 1935  CD1 TYR A 263    16665  14846  14066   1243    780    135       C  
ATOM   1936  CD2 TYR A 263      29.639  26.917  17.789  1.00114.60           C  
ANISOU 1936  CD2 TYR A 263    15665  14223  13656   1136    871    272       C  
ATOM   1937  CE1 TYR A 263      32.181  27.624  18.627  1.00115.83           C  
ANISOU 1937  CE1 TYR A 263    16135  14320  13556   1073    621      4       C  
ATOM   1938  CE2 TYR A 263      30.547  27.456  16.879  1.00111.30           C  
ANISOU 1938  CE2 TYR A 263    15255  13805  13229    975    719    131       C  
ATOM   1939  CZ  TYR A 263      31.813  27.803  17.305  1.00121.92           C  
ANISOU 1939  CZ  TYR A 263    16749  15121  14453    947    602      5       C  
ATOM   1940  OH  TYR A 263      32.709  28.327  16.402  1.00137.80           O  
ANISOU 1940  OH  TYR A 263    18751  17131  16477    794    463   -110       O  
ATOM   1941  N   LYS A 264      26.683  26.354  22.625  1.00123.55           N  
ANISOU 1941  N   LYS A 264    17146  15280  14518   2042   1568    829       N  
ATOM   1942  CA  LYS A 264      25.547  25.602  23.152  1.00128.98           C  
ANISOU 1942  CA  LYS A 264    17705  15985  15317   2196   1773   1059       C  
ATOM   1943  C   LYS A 264      24.264  26.398  22.991  1.00146.08           C  
ANISOU 1943  C   LYS A 264    19843  18126  17533   2323   1931   1218       C  
ATOM   1944  O   LYS A 264      23.170  25.825  22.973  1.00141.72           O  
ANISOU 1944  O   LYS A 264    19095  17593  17161   2391   2078   1435       O  
ATOM   1945  CB  LYS A 264      25.742  25.221  24.621  1.00126.45           C  
ANISOU 1945  CB  LYS A 264    17566  15650  14830   2404   1880   1107       C  
ATOM   1946  CG  LYS A 264      24.833  24.065  25.032  1.00118.61           C  
ANISOU 1946  CG  LYS A 264    16372  14690  14003   2505   2057   1339       C  
ATOM   1947  CD  LYS A 264      24.849  23.784  26.524  1.00135.61           C  
ANISOU 1947  CD  LYS A 264    18715  16829  15982   2750   2202   1420       C  
ATOM   1948  CE  LYS A 264      24.551  22.310  26.785  1.00144.55           C  
ANISOU 1948  CE  LYS A 264    19619  18007  17296   2754   2283   1578       C  
ATOM   1949  NZ  LYS A 264      23.596  21.748  25.778  1.00148.19           N1+
ANISOU 1949  NZ  LYS A 264    19742  18492  18073   2635   2313   1730       N1+
ATOM   1950  N   LYS A 265      24.416  27.718  22.875  1.00157.27           N  
ANISOU 1950  N   LYS A 265    21453  19497  18806   2353   1895   1118       N  
ATOM   1951  CA  LYS A 265      23.305  28.631  22.614  1.00153.93           C  
ANISOU 1951  CA  LYS A 265    21017  19043  18425   2458   2028   1248       C  
ATOM   1952  C   LYS A 265      22.505  28.186  21.393  1.00149.59           C  
ANISOU 1952  C   LYS A 265    20135  18541  18163   2300   2012   1368       C  
ATOM   1953  O   LYS A 265      21.277  28.209  21.401  1.00144.58           O  
ANISOU 1953  O   LYS A 265    19371  17902  17662   2412   2178   1591       O  
ATOM   1954  CB  LYS A 265      23.823  30.060  22.398  1.00151.30           C  
ANISOU 1954  CB  LYS A 265    20914  18654  17921   2442   1930   1078       C  
ATOM   1955  CG  LYS A 265      24.820  30.552  23.446  1.00158.21           C  
ANISOU 1955  CG  LYS A 265    22133  19468  18513   2544   1868    916       C  
ATOM   1956  CD  LYS A 265      25.418  31.908  23.064  1.00150.97           C  
ANISOU 1956  CD  LYS A 265    21409  18486  17467   2480   1726    740       C  
ATOM   1957  CE  LYS A 265      26.288  32.469  24.181  1.00147.24           C  
ANISOU 1957  CE  LYS A 265    21301  17930  16713   2597   1658    598       C  
ATOM   1958  NZ  LYS A 265      26.814  33.825  23.860  1.00152.56           N1+
ANISOU 1958  NZ  LYS A 265    22169  18524  17274   2543   1518    441       N1+
ATOM   1959  N   HIS A 266      23.220  27.758  20.355  1.00150.83           N  
ANISOU 1959  N   HIS A 266    20161  18736  18413   2043   1808   1227       N  
ATOM   1960  CA  HIS A 266      22.620  27.469  19.056  1.00148.79           C  
ANISOU 1960  CA  HIS A 266    19633  18511  18391   1865   1743   1295       C  
ATOM   1961  C   HIS A 266      22.192  26.008  18.863  1.00139.49           C  
ANISOU 1961  C   HIS A 266    18199  17368  17434   1792   1751   1424       C  
ATOM   1962  O   HIS A 266      21.907  25.601  17.735  1.00136.78           O  
ANISOU 1962  O   HIS A 266    17650  17044  17274   1610   1645   1442       O  
ATOM   1963  CB  HIS A 266      23.597  27.857  17.935  1.00149.47           C  
ANISOU 1963  CB  HIS A 266    19730  18612  18450   1632   1521   1074       C  
ATOM   1964  CG  HIS A 266      24.035  29.292  17.978  1.00151.84           C  
ANISOU 1964  CG  HIS A 266    20253  18870  18567   1673   1486    948       C  
ATOM   1965  CD2 HIS A 266      24.877  29.939  18.821  1.00150.68           C  
ANISOU 1965  CD2 HIS A 266    20376  18679  18196   1764   1463    816       C  
ATOM   1966  ND1 HIS A 266      23.596  30.230  17.074  1.00154.07           N  
ANISOU 1966  ND1 HIS A 266    20496  19145  18899   1612   1456    956       N  
ATOM   1967  CE1 HIS A 266      24.145  31.402  17.357  1.00155.74           C  
ANISOU 1967  CE1 HIS A 266    20938  19308  18928   1666   1425    833       C  
ATOM   1968  NE2 HIS A 266      24.924  31.251  18.410  1.00154.35           N  
ANISOU 1968  NE2 HIS A 266    20956  19104  18585   1755   1421    745       N  
ATOM   1969  N   HIS A 267      22.143  25.221  19.940  1.00130.68           N  
ANISOU 1969  N   HIS A 267    17102  16252  16298   1932   1867   1516       N  
ATOM   1970  CA  HIS A 267      21.787  23.799  19.822  1.00145.52           C  
ANISOU 1970  CA  HIS A 267    18743  18155  18393   1864   1870   1640       C  
ATOM   1971  C   HIS A 267      21.028  23.224  21.024  1.00170.34           C  
ANISOU 1971  C   HIS A 267    21856  21290  21576   2092   2089   1871       C  
ATOM   1972  O   HIS A 267      21.640  22.821  22.020  1.00168.38           O  
ANISOU 1972  O   HIS A 267    21743  21046  21189   2196   2136   1829       O  
ATOM   1973  CB  HIS A 267      23.044  22.960  19.589  1.00116.90           C  
ANISOU 1973  CB  HIS A 267    15126  14554  14736   1694   1702   1443       C  
ATOM   1974  CG  HIS A 267      23.875  23.422  18.434  1.00117.29           C  
ANISOU 1974  CG  HIS A 267    15202  14614  14750   1481   1501   1227       C  
ATOM   1975  CD2 HIS A 267      24.999  24.181  18.384  1.00117.07           C  
ANISOU 1975  CD2 HIS A 267    15368  14584  14530   1434   1395   1016       C  
ATOM   1976  ND1 HIS A 267      23.569  23.113  17.126  1.00110.17           N  
ANISOU 1976  ND1 HIS A 267    14111  13722  14025   1288   1385   1226       N  
ATOM   1977  CE1 HIS A 267      24.470  23.651  16.320  1.00111.62           C  
ANISOU 1977  CE1 HIS A 267    14376  13916  14120   1143   1235   1025       C  
ATOM   1978  NE2 HIS A 267      25.351  24.308  17.068  1.00109.67           N  
ANISOU 1978  NE2 HIS A 267    14349  13661  13660   1226   1239    901       N  
ATOM   1979  N   HIS A 268      19.701  23.163  20.907  1.00179.88           N  
ANISOU 1979  N   HIS A 268    22877  22485  22983   2168   2219   2129       N  
ATOM   1980  CA  HIS A 268      18.841  22.593  21.944  1.00184.36           C  
ANISOU 1980  CA  HIS A 268    23371  23043  23633   2387   2445   2396       C  
ATOM   1981  C   HIS A 268      17.948  21.479  21.387  1.00185.37           C  
ANISOU 1981  C   HIS A 268    23156  23170  24105   2282   2430   2612       C  
ATOM   1982  O   HIS A 268      17.988  21.180  20.192  1.00181.59           O  
ANISOU 1982  O   HIS A 268    22521  22694  23781   2041   2237   2542       O  
ATOM   1983  CB  HIS A 268      17.977  23.686  22.582  1.00188.91           C  
ANISOU 1983  CB  HIS A 268    24067  23588  24123   2645   2670   2559       C  
ATOM   1984  CG  HIS A 268      18.720  24.582  23.522  1.00189.50           C  
ANISOU 1984  CG  HIS A 268    24505  23643  23854   2818   2730   2399       C  
ATOM   1985  CD2 HIS A 268      18.551  25.888  23.836  1.00189.75           C  
ANISOU 1985  CD2 HIS A 268    24763  23634  23699   2976   2825   2375       C  
ATOM   1986  ND1 HIS A 268      19.791  24.148  24.281  1.00185.24           N  
ANISOU 1986  ND1 HIS A 268    24147  23115  23123   2840   2679   2239       N  
ATOM   1987  CE1 HIS A 268      20.242  25.145  25.015  1.00184.83           C  
ANISOU 1987  CE1 HIS A 268    24420  23027  22781   2997   2725   2123       C  
ATOM   1988  NE2 HIS A 268      19.508  26.216  24.764  1.00188.13           N  
ANISOU 1988  NE2 HIS A 268    24879  23409  23193   3085   2816   2197       N  
ATOM   1989  N   HIS A 269      17.139  20.878  22.258  1.00188.13           N  
ANISOU 1989  N   HIS A 269    23399  23510  24573   2468   2632   2882       N  
ATOM   1990  CA  HIS A 269      16.221  19.806  21.871  1.00180.42           C  
ANISOU 1990  CA  HIS A 269    22089  22518  23945   2388   2627   3125       C  
ATOM   1991  C   HIS A 269      15.218  19.506  22.988  1.00178.93           C  
ANISOU 1991  C   HIS A 269    21815  22314  23858   2661   2910   3464       C  
ATOM   1992  O   HIS A 269      14.314  18.680  22.832  1.00176.38           O  
ANISOU 1992  O   HIS A 269    21203  21968  23844   2636   2942   3725       O  
ATOM   1993  CB  HIS A 269      16.995  18.538  21.508  1.00175.95           C  
ANISOU 1993  CB  HIS A 269    21430  21961  23461   2181   2441   2989       C  
ATOM   1994  CG  HIS A 269      17.771  17.960  22.647  1.00183.11           C  
ANISOU 1994  CG  HIS A 269    22480  22889  24204   2307   2525   2929       C  
ATOM   1995  CD2 HIS A 269      18.196  16.696  22.888  1.00186.61           C  
ANISOU 1995  CD2 HIS A 269    22830  23336  24736   2243   2478   2924       C  
ATOM   1996  ND1 HIS A 269      18.195  18.713  23.724  1.00183.35           N  
ANISOU 1996  ND1 HIS A 269    22793  22934  23939   2530   2671   2869       N  
ATOM   1997  CE1 HIS A 269      18.846  17.943  24.570  1.00182.71           C  
ANISOU 1997  CE1 HIS A 269    22783  22870  23768   2594   2704   2833       C  
ATOM   1998  NE2 HIS A 269      18.862  16.710  24.089  1.00184.58           N  
ANISOU 1998  NE2 HIS A 269    22788  23103  24239   2425   2596   2868       N  
TER   
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.