CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 191008165942126541

Job options:

ID        	=	 191008165942126541
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


ATOM      1  N   SER A   7      23.183 -12.243   7.340  1.00 44.49      A    N  
ANISOU    1  N   SER A   7     8216   3592   5095   1023   1280    164  A    N  
ATOM      2  CA  SER A   7      21.716 -12.220   7.558  1.00 43.59      A    C  
ANISOU    2  CA  SER A   7     8036   3596   4931    834   1225     87  A    C  
ATOM      3  C   SER A   7      21.163 -10.798   7.556  1.00 42.26      A    C  
ANISOU    3  C   SER A   7     7731   3589   4738    820    900   -142  A    C  
ATOM      4  O   SER A   7      20.211 -10.492   6.830  1.00 41.39      A    O  
ANISOU    4  O   SER A   7     7764   3474   4487    658    806   -126  A    O  
ATOM      5  CB  SER A   7      21.378 -12.924   8.872  1.00 44.08      A    C  
ANISOU    5  CB  SER A   7     8223   3643   4881    833   1322     81  A    C  
ATOM      6  OG  SER A   7      21.891 -14.249   8.855  1.00 44.41      A    O  
ANISOU    6  OG  SER A   7     7896   3876   5102    678   1747    337  A    O  
ATOM      7  N   LEU A   8      21.763  -9.925   8.369  1.00 42.33      A    N  
ANISOU    7  N   LEU A   8     7350   3720   5012    759    406   -263  A    N  
ATOM      8  CA  LEU A   8      21.334  -8.523   8.461  1.00 41.98      A    C  
ANISOU    8  CA  LEU A   8     6830   3948   5173    513    240   -274  A    C  
ATOM      9  C   LEU A   8      21.441  -7.823   7.107  1.00 39.42      A    C  
ANISOU    9  C   LEU A   8     5795   3722   5461     59    181     -5  A    C  
ATOM     10  O   LEU A   8      20.696  -6.897   6.781  1.00 38.54      A    O  
ANISOU   10  O   LEU A   8     5314   3657   5673   -135    164    153  A    O  
ATOM     11  CB  LEU A   8      22.160  -7.770   9.514  1.00 44.48      A    C  
ANISOU   11  CB  LEU A   8     7426   4363   5113    635    125   -485  A    C  
ATOM     12  CG  LEU A   8      21.858  -8.020  10.999  1.00 50.00      A    C  
ANISOU   12  CG  LEU A   8     8524   5324   5149    551      6   -427  A    C  
ATOM     13  CD1 LEU A   8      22.859  -7.267  11.891  1.00 54.59      A    C  
ANISOU   13  CD1 LEU A   8     9429   6126   5188    560   -313   -527  A    C  
ATOM     14  CD2 LEU A   8      20.410  -7.636  11.363  1.00 53.72      A    C  
ANISOU   14  CD2 LEU A   8     9136   5931   5345    395     93   -153  A    C  
ATOM     15  N   TYR A   9      22.388  -8.300   6.305  1.00 37.60      A    N  
ANISOU   15  N   TYR A   9     4841   3722   5722   -395    273    436  A    N  
ATOM     16  CA  TYR A   9      22.604  -7.778   4.968  1.00 36.44      A    C  
ANISOU   16  CA  TYR A   9     4217   3923   5705   -489    399    785  A    C  
ATOM     17  C   TYR A   9      21.475  -8.159   3.995  1.00 34.46      A    C  
ANISOU   17  C   TYR A   9     3806   3657   5630   -487    679    891  A    C  
ATOM     18  O   TYR A   9      20.937  -7.287   3.301  1.00 34.03      A    O  
ANISOU   18  O   TYR A   9     3440   3614   5874   -467    876   1000  A    O  
ATOM     19  CB  TYR A   9      23.987  -8.247   4.515  1.00 37.35      A    C  
ANISOU   19  CB  TYR A   9     4318   4250   5625   -478    186    957  A    C  
ATOM     20  CG  TYR A   9      24.576  -7.492   3.353  1.00 37.20      A    C  
ANISOU   20  CG  TYR A   9     4244   4611   5278   -421   -137   1150  A    C  
ATOM     21  CD1 TYR A   9      24.371  -6.124   3.190  1.00 37.62      A    C  
ANISOU   21  CD1 TYR A   9     4332   4863   5098   -496   -450   1194  A    C  
ATOM     22  CD2 TYR A   9      25.360  -8.165   2.425  1.00 36.76      A    C  
ANISOU   22  CD2 TYR A   9     4153   4863   4949   -467   -390   1333  A    C  
ATOM     23  CE1 TYR A   9      24.921  -5.445   2.108  1.00 37.68      A    C  
ANISOU   23  CE1 TYR A   9     4419   4971   4924   -744   -702   1314  A    C  
ATOM     24  CE2 TYR A   9      25.913  -7.500   1.347  1.00 37.22      A    C  
ANISOU   24  CE2 TYR A   9     4499   5036   4607   -658   -661   1412  A    C  
ATOM     25  CZ  TYR A   9      25.691  -6.147   1.197  1.00 37.60      A    C  
ANISOU   25  CZ  TYR A   9     4544   5052   4690   -912   -772   1342  A    C  
ATOM     26  OH  TYR A   9      26.249  -5.509   0.122  1.00 39.04      A    O  
ANISOU   26  OH  TYR A   9     4874   5281   4679  -1133   -732   1421  A    O  
ATOM     27  N   LYS A  10      21.090  -9.440   3.972  1.00 30.45      A    N  
ANISOU   27  N   LYS A  10     3280   3388   4902   -186   1049    601  A    N  
ATOM     28  CA  LYS A  10      19.977  -9.930   3.157  1.00 27.79      A    C  
ANISOU   28  CA  LYS A  10     3384   3183   3991     31    991    153  A    C  
ATOM     29  C   LYS A  10      18.679  -9.227   3.576  1.00 24.44      A    C  
ANISOU   29  C   LYS A  10     2779   3140   3366    -93   1054    -27  A    C  
ATOM     30  O   LYS A  10      17.820  -8.854   2.764  1.00 24.09      A    O  
ANISOU   30  O   LYS A  10     2867   3145   3143    -49   1093   -173  A    O  
ATOM     31  CB  LYS A  10      19.820 -11.439   3.344  1.00 28.79      A    C  
ANISOU   31  CB  LYS A  10     3743   3167   4029    137    829    120  A    C  
ATOM     32  CG  LYS A  10      19.274 -12.183   2.133  1.00 33.33      A    C  
ANISOU   32  CG  LYS A  10     4706   3370   4589    285     74   -104  A    C  
ATOM     33  CD  LYS A  10      18.705 -13.550   2.516  1.00 38.32      A    C  
ANISOU   33  CD  LYS A  10     5404   3574   5580    357   -723   -285  A    C  
ATOM     34  CE  LYS A  10      19.780 -14.482   3.067  1.00 40.07      A    C  
ANISOU   34  CE  LYS A  10     5457   3634   6132    395   -873   -208  A    C  
ATOM     35  NZ  LYS A  10      19.278 -15.893   3.007  1.00 41.44      A    N1+
ANISOU   35  NZ  LYS A  10     5435   3720   6589    315  -1045   -153  A    N1+
ATOM     36  N   TYR A  11      18.542  -9.040   4.879  1.00 22.01      A    N  
ANISOU   36  N   TYR A  11     2266   3070   3027   -346    794   -263  A    N  
ATOM     37  CA  TYR A  11      17.431  -8.298   5.473  1.00 20.62      A    C  
ANISOU   37  CA  TYR A  11     1912   3201   2723   -496    496   -339  A    C  
ATOM     38  C   TYR A  11      17.342  -6.888   4.890  1.00 20.56      A    C  
ANISOU   38  C   TYR A  11     1852   3127   2831   -461    249   -340  A    C  
ATOM     39  O   TYR A  11      16.295  -6.441   4.426  1.00 21.05      A    O  
ANISOU   39  O   TYR A  11     1817   3364   2815   -432    217   -419  A    O  
ATOM     40  CB  TYR A  11      17.612  -8.268   6.997  1.00 21.04      A    C  
ANISOU   40  CB  TYR A  11     1946   3316   2734   -489    342   -445  A    C  
ATOM     41  CG  TYR A  11      16.783  -7.222   7.718  1.00 21.17      A    C  
ANISOU   41  CG  TYR A  11     2008   3431   2606   -540    417   -522  A    C  
ATOM     42  CD1 TYR A  11      15.425  -7.417   7.966  1.00 22.32      A    C  
ANISOU   42  CD1 TYR A  11     2313   3424   2741   -766    684   -718  A    C  
ATOM     43  CD2 TYR A  11      17.361  -6.043   8.183  1.00 22.45      A    C  
ANISOU   43  CD2 TYR A  11     2213   3592   2725   -529     93   -640  A    C  
ATOM     44  CE1 TYR A  11      14.674  -6.447   8.644  1.00 23.41      A    C  
ANISOU   44  CE1 TYR A  11     2655   3289   2949   -775    891   -785  A    C  
ATOM     45  CE2 TYR A  11      16.626  -5.070   8.849  1.00 23.11      A    C  
ANISOU   45  CE2 TYR A  11     2426   3388   2967   -715    392   -644  A    C  
ATOM     46  CZ  TYR A  11      15.276  -5.275   9.082  1.00 23.60      A    C  
ANISOU   46  CZ  TYR A  11     2572   3228   3167   -744    692   -776  A    C  
ATOM     47  OH  TYR A  11      14.553  -4.304   9.753  1.00 25.16      A    O  
ANISOU   47  OH  TYR A  11     3032   3334   3194   -709    869   -662  A    O  
ATOM     48  N   LEU A  12      18.464  -6.178   4.897  1.00 20.33      A    N  
ANISOU   48  N   LEU A  12     1800   3034   2890   -599     43    -87  A    N  
ATOM     49  CA  LEU A  12      18.478  -4.801   4.399  1.00 21.01      A    C  
ANISOU   49  CA  LEU A  12     1658   3136   3188   -485    -82    107  A    C  
ATOM     50  C   LEU A  12      18.076  -4.684   2.934  1.00 20.09      A    C  
ANISOU   50  C   LEU A  12     1641   2908   3084   -438    153     17  A    C  
ATOM     51  O   LEU A  12      17.345  -3.764   2.549  1.00 19.44      A    O  
ANISOU   51  O   LEU A  12     1448   3059   2879   -375    -20   -109  A    O  
ATOM     52  CB  LEU A  12      19.873  -4.173   4.578  1.00 22.64      A    C  
ANISOU   52  CB  LEU A  12     1886   3160   3555   -597   -284    274  A    C  
ATOM     53  CG  LEU A  12      20.184  -3.318   5.801  1.00 27.44      A    C  
ANISOU   53  CG  LEU A  12     2307   4129   3991   -688   -780    368  A    C  
ATOM     54  CD1 LEU A  12      19.322  -3.659   6.999  1.00 30.89      A    C  
ANISOU   54  CD1 LEU A  12     3131   4598   4007   -939  -1062    485  A    C  
ATOM     55  CD2 LEU A  12      21.682  -3.373   6.124  1.00 28.98      A    C  
ANISOU   55  CD2 LEU A  12     2318   4038   4654   -662  -1368    465  A    C  
ATOM     56  N   LEU A  13      18.561  -5.620   2.120  1.00 20.25      A    N  
ANISOU   56  N   LEU A  13     1430   2964   3300   -434    394   -164  A    N  
ATOM     57  CA  LEU A  13      18.340  -5.547   0.673  1.00 19.43      A    C  
ANISOU   57  CA  LEU A  13     1221   2836   3327   -434    631   -296  A    C  
ATOM     58  C   LEU A  13      16.918  -5.903   0.275  1.00 18.78      A    C  
ANISOU   58  C   LEU A  13     1269   2745   3120   -412    653   -225  A    C  
ATOM     59  O   LEU A  13      16.395  -5.315  -0.681  1.00 18.98      A    O  
ANISOU   59  O   LEU A  13     1171   2971   3070   -344    675    -91  A    O  
ATOM     60  CB  LEU A  13      19.375  -6.396  -0.075  1.00 20.50      A    C  
ANISOU   60  CB  LEU A  13     1141   2933   3716   -386    666   -388  A    C  
ATOM     61  CG  LEU A  13      20.809  -5.863   0.013  1.00 22.36      A    C  
ANISOU   61  CG  LEU A  13     1208   3314   3973   -509    710   -573  A    C  
ATOM     62  CD1 LEU A  13      21.757  -6.870  -0.607  1.00 25.73      A    C  
ANISOU   62  CD1 LEU A  13     1194   3819   4765   -421    754   -952  A    C  
ATOM     63  CD2 LEU A  13      20.918  -4.517  -0.676  1.00 23.69      A    C  
ANISOU   63  CD2 LEU A  13     1316   3718   3968   -675    570   -463  A    C  
ATOM     64  N   LEU A  14      16.304  -6.830   1.022  1.00 18.27      A    N  
ANISOU   64  N   LEU A  14     1307   2933   2702   -630    693   -348  A    N  
ATOM     65  CA  LEU A  14      14.889  -7.151   0.792  1.00 18.82      A    C  
ANISOU   65  CA  LEU A  14     1499   2975   2678   -678    631   -505  A    C  
ATOM     66  C   LEU A  14      14.012  -5.994   1.233  1.00 18.60      A    C  
ANISOU   66  C   LEU A  14     1488   3088   2493   -631    395   -688  A    C  
ATOM     67  O   LEU A  14      13.097  -5.589   0.511  1.00 19.82      A    O  
ANISOU   67  O   LEU A  14     1445   3440   2644   -537    226   -736  A    O  
ATOM     68  CB  LEU A  14      14.473  -8.446   1.490  1.00 19.45      A    C  
ANISOU   68  CB  LEU A  14     1703   2973   2716   -724    728   -524  A    C  
ATOM     69  CG  LEU A  14      15.042  -9.718   0.855  1.00 20.59      A    C  
ANISOU   69  CG  LEU A  14     1852   3086   2885   -586    715   -496  A    C  
ATOM     70  CD1 LEU A  14      14.845 -10.925   1.761  1.00 23.30      A    C  
ANISOU   70  CD1 LEU A  14     2630   3127   3097   -684    702   -450  A    C  
ATOM     71  CD2 LEU A  14      14.391  -9.961  -0.499  1.00 21.37      A    C  
ANISOU   71  CD2 LEU A  14     1562   3574   2985   -741    666   -617  A    C  
ATOM     72  N   ARG A  15      14.295  -5.441   2.414  1.00 18.33      A    N  
ANISOU   72  N   ARG A  15     1439   3199   2328   -595    405   -746  A    N  
ATOM     73  CA  ARG A  15      13.552  -4.267   2.876  1.00 19.23      A    C  
ANISOU   73  CA  ARG A  15     1518   3366   2423   -395    364   -851  A    C  
ATOM     74  C   ARG A  15      13.692  -3.112   1.887  1.00 19.25      A    C  
ANISOU   74  C   ARG A  15     1509   3330   2477   -208    219   -878  A    C  
ATOM     75  O   ARG A  15      12.766  -2.317   1.713  1.00 20.80      A    O  
ANISOU   75  O   ARG A  15     1365   3637   2901    -93     74   -907  A    O  
ATOM     76  CB  ARG A  15      14.033  -3.804   4.254  1.00 19.86      A    C  
ANISOU   76  CB  ARG A  15     1623   3546   2377   -333    483   -829  A    C  
ATOM     77  CG  ARG A  15      13.618  -4.681   5.409  1.00 19.49      A    C  
ANISOU   77  CG  ARG A  15     1315   3382   2707   -230    496   -586  A    C  
ATOM     78  CD  ARG A  15      12.189  -4.338   5.822  1.00 21.63      A    C  
ANISOU   78  CD  ARG A  15     1474   3531   3215   -140    746   -293  A    C  
ATOM     79  NE  ARG A  15      11.763  -5.069   7.013  1.00 24.10      A    N  
ANISOU   79  NE  ARG A  15     1974   3650   3533   -240    590   -175  A    N  
ATOM     80  CZ  ARG A  15      11.262  -6.306   6.998  1.00 25.97      A    C  
ANISOU   80  CZ  ARG A  15     2433   3679   3756   -163    829   -228  A    C  
ATOM     81  NH1 ARG A  15      11.123  -6.966   5.849  1.00 26.45      A    N1+
ANISOU   81  NH1 ARG A  15     2220   3882   3946    -54    560   -491  A    N1+
ATOM     82  NH2 ARG A  15      10.915  -6.890   8.139  1.00 28.74      A    N  
ANISOU   82  NH2 ARG A  15     2836   3989   4095   -333    816      5  A    N  
ATOM     83  N   SER A  16      14.861  -3.017   1.259  1.00 18.28      A    N  
ANISOU   83  N   SER A  16     1412   3192   2338   -208     52   -772  A    N  
ATOM     84  CA  SER A  16      15.174  -1.901   0.381  1.00 18.14      A    C  
ANISOU   84  CA  SER A  16     1474   3041   2378   -229   -153   -714  A    C  
ATOM     85  C   SER A  16      14.520  -2.030  -0.993  1.00 18.62      A    C  
ANISOU   85  C   SER A  16     1612   3129   2333   -240    -98   -693  A    C  
ATOM     86  O   SER A  16      14.470  -1.063  -1.759  1.00 20.16      A    O  
ANISOU   86  O   SER A  16     2044   3194   2421   -219   -229   -627  A    O  
ATOM     87  CB  SER A  16      16.690  -1.765   0.229  1.00 18.16      A    C  
ANISOU   87  CB  SER A  16     1474   3064   2363   -259    -73   -649  A    C  
ATOM     88  OG  SER A  16      17.258  -1.282   1.429  1.00 19.88      A    O  
ANISOU   88  OG  SER A  16     1473   3255   2824   -333   -518   -548  A    O  
ATOM     89  N   THR A  17      14.017  -3.222  -1.304  1.00 18.90      A    N  
ANISOU   89  N   THR A  17     1479   3294   2407   -205   -252   -772  A    N  
ATOM     90  CA  THR A  17      13.371  -3.432  -2.604  1.00 19.63      A    C  
ANISOU   90  CA  THR A  17     1250   3639   2569    -37   -186   -798  A    C  
ATOM     91  C   THR A  17      11.878  -3.734  -2.488  1.00 22.21      A    C  
ANISOU   91  C   THR A  17     1280   4275   2883    126    -34   -886  A    C  
ATOM     92  O   THR A  17      11.291  -4.458  -3.310  1.00 22.54      A    O  
ANISOU   92  O   THR A  17     1132   4429   3003    -93    -46   -900  A    O  
ATOM     93  CB  THR A  17      14.118  -4.494  -3.420  1.00 19.24      A    C  
ANISOU   93  CB  THR A  17     1191   3569   2549     27   -230   -697  A    C  
ATOM     94  CG2 THR A  17      15.484  -3.953  -3.845  1.00 19.98      A    C  
ANISOU   94  CG2 THR A  17      982   3973   2637    -54   -194   -614  A    C  
ATOM     95  OG1 THR A  17      14.310  -5.664  -2.631  1.00 20.92      A    O  
ANISOU   95  OG1 THR A  17     1852   3447   2648     57   -318   -627  A    O  
ATOM     96  N   GLY A  18      11.267  -3.160  -1.460  1.00 25.57      A    N  
ANISOU   96  N   GLY A  18     1349   4981   3384    450    109   -895  A    N  
ATOM     97  CA  GLY A  18       9.812  -3.133  -1.365  1.00 29.05      A    C  
ANISOU   97  CA  GLY A  18     1509   5475   4052    617    186   -749  A    C  
ATOM     98  C   GLY A  18       9.203  -4.108  -0.388  1.00 30.47      A    C  
ANISOU   98  C   GLY A  18     1703   5519   4356    489    -31   -741  A    C  
ATOM     99  O   GLY A  18       7.992  -4.157  -0.233  1.00 31.07      A    O  
ANISOU   99  O   GLY A  18     1683   5792   4329    549     35   -627  A    O  
ATOM    100  N   ASP A  19      10.049  -4.871   0.291  1.00 30.58      A    N  
ANISOU  100  N   ASP A  19     1834   5177   4609    366   -302   -891  A    N  
ATOM    101  CA  ASP A  19       9.591  -5.824   1.293  1.00 31.86      A    C  
ANISOU  101  CA  ASP A  19     2125   5120   4859    208   -513   -882  A    C  
ATOM    102  C   ASP A  19       9.420  -5.129   2.645  1.00 32.65      A    C  
ANISOU  102  C   ASP A  19     2298   5309   4798    -41   -284   -898  A    C  
ATOM    103  O   ASP A  19      10.106  -5.462   3.617  1.00 33.37      A    O  
ANISOU  103  O   ASP A  19     2475   5364   4838    -81   -403   -776  A    O  
ATOM    104  CB  ASP A  19      10.589  -6.977   1.399  1.00 32.67      A    C  
ANISOU  104  CB  ASP A  19     2266   5044   5102    353   -754   -847  A    C  
ATOM    105  CG  ASP A  19       9.922  -8.315   1.620  1.00 35.72      A    C  
ANISOU  105  CG  ASP A  19     2606   5149   5817    408   -935   -520  A    C  
ATOM    106  OD1 ASP A  19       8.675  -8.381   1.625  1.00 40.17      A    O  
ANISOU  106  OD1 ASP A  19     2883   5475   6904    359   -930     52  A    O  
ATOM    107  OD2 ASP A  19      10.655  -9.309   1.788  1.00 37.19      A    O1-
ANISOU  107  OD2 ASP A  19     2639   5320   6172    533   -472   -293  A    O1-
ATOM    108  N   MET A  20       8.515  -4.150   2.686  1.00 33.80      A    N  
ANISOU  108  N   MET A  20     2196   5766   4881   -379    324  -1062  A    N  
ATOM    109  CA  MET A  20       8.201  -3.408   3.907  1.00 36.03      A    C  
ANISOU  109  CA  MET A  20     2398   6219   5073   -662    900  -1193  A    C  
ATOM    110  C   MET A  20       6.725  -3.584   4.233  1.00 35.57      A    C  
ANISOU  110  C   MET A  20     2257   6348   4910   -538    842  -1436  A    C  
ATOM    111  O   MET A  20       5.913  -3.787   3.331  1.00 36.84      A    O  
ANISOU  111  O   MET A  20     2451   6736   4809   -241    828  -1500  A    O  
ATOM    112  CB  MET A  20       8.497  -1.915   3.724  1.00 36.98      A    C  
ANISOU  112  CB  MET A  20     2511   6190   5349   -807    944  -1181  A    C  
ATOM    113  CG  MET A  20       9.956  -1.574   3.451  1.00 39.78      A    C  
ANISOU  113  CG  MET A  20     2730   6657   5727  -1058   1102   -560  A    C  
ATOM    114  SD  MET A  20      10.187   0.131   2.896  1.00 37.05      A    S  
ANISOU  114  SD  MET A  20     2205   6790   5083   -966    445   -394  A    S  
ATOM    115  CE  MET A  20       9.710   1.045   4.359  1.00 38.64      A    C  
ANISOU  115  CE  MET A  20     2572   7181   4928   -581    680   -186  A    C  
ATOM    116  N   HIS A  21       6.377  -3.495   5.514  1.00 34.13      A    N  
ANISOU  116  N   HIS A  21     1897   6115   4956   -767    781  -1594  A    N  
ATOM    117  CA  HIS A  21       4.967  -3.519   5.914  1.00 33.82      A    C  
ANISOU  117  CA  HIS A  21     1606   5917   5328   -960    579  -1536  A    C  
ATOM    118  C   HIS A  21       4.347  -2.137   5.753  1.00 33.67      A    C  
ANISOU  118  C   HIS A  21     1473   5957   5363  -1036    214  -1712  A    C  
ATOM    119  O   HIS A  21       5.060  -1.133   5.768  1.00 34.06      A    O  
ANISOU  119  O   HIS A  21     1474   5896   5572  -1141    331  -1773  A    O  
ATOM    120  CB  HIS A  21       4.812  -3.980   7.368  1.00 33.83      A    C  
ANISOU  120  CB  HIS A  21     1615   5806   5432  -1061    649  -1500  A    C  
ATOM    121  CG  HIS A  21       5.461  -3.073   8.371  1.00 35.75      A    C  
ANISOU  121  CG  HIS A  21     1923   5565   6097   -732    397  -1674  A    C  
ATOM    122  CD2 HIS A  21       6.728  -3.039   8.850  1.00 36.72      A    C  
ANISOU  122  CD2 HIS A  21     2071   5188   6692   -636    131  -1921  A    C  
ATOM    123  ND1 HIS A  21       4.796  -2.045   9.006  1.00 38.16      A    N  
ANISOU  123  ND1 HIS A  21     2213   5400   6887   -537    219  -1852  A    N  
ATOM    124  CE1 HIS A  21       5.617  -1.420   9.830  1.00 39.04      A    C  
ANISOU  124  CE1 HIS A  21     2560   5070   7203   -410    104  -1993  A    C  
ATOM    125  NE2 HIS A  21       6.802  -2.003   9.752  1.00 38.17      A    N  
ANISOU  125  NE2 HIS A  21     2383   5004   7116   -463    109  -2020  A    N  
ATOM    126  N   LYS A  22       3.023  -2.075   5.607  1.00 34.26      A    N  
ANISOU  126  N   LYS A  22     1483   6291   5245   -864   -270  -1817  A    N  
ATOM    127  CA  LYS A  22       2.320  -0.795   5.610  1.00 35.95      A    C  
ANISOU  127  CA  LYS A  22     1867   6751   5040   -485   -732  -1791  A    C  
ATOM    128  C   LYS A  22       2.526  -0.107   6.958  1.00 33.73      A    C  
ANISOU  128  C   LYS A  22     1903   6377   4535   -562   -560  -1665  A    C  
ATOM    129  O   LYS A  22       2.576  -0.773   7.994  1.00 34.00      A    O  
ANISOU  129  O   LYS A  22     2072   6352   4496   -671   -252  -1615  A    O  
ATOM    130  CB  LYS A  22       0.820  -0.983   5.369  1.00 38.34      A    C  
ANISOU  130  CB  LYS A  22     1941   7225   5400   -322  -1084  -1744  A    C  
ATOM    131  CG  LYS A  22       0.027   0.324   5.298  1.00 44.81      A    C  
ANISOU  131  CG  LYS A  22     2319   8553   6154    401  -1289  -1263  A    C  
ATOM    132  CD  LYS A  22      -1.190   0.306   6.219  1.00 52.86      A    C  
ANISOU  132  CD  LYS A  22     2624  10339   7120   1162  -1418   -544  A    C  
ATOM    133  CE  LYS A  22      -2.291  -0.594   5.668  1.00 54.96      A    C  
ANISOU  133  CE  LYS A  22     2361  11181   7342   1571  -1410   -333  A    C  
ATOM    134  NZ  LYS A  22      -2.980   0.029   4.467  1.00 57.76      A    N1+
ANISOU  134  NZ  LYS A  22     2858  11706   7383   1764  -1289   -259  A    N1+
ATOM    135  N   ALA A  23       2.655   1.215   6.943  1.00 31.62      A    N  
ANISOU  135  N   ALA A  23     1808   6129   4077   -610   -348  -1453  A    N  
ATOM    136  CA  ALA A  23       2.866   1.979   8.169  1.00 29.59      A    C  
ANISOU  136  CA  ALA A  23     1474   5921   3849   -793    -98  -1263  A    C  
ATOM    137  C   ALA A  23       1.743   1.778   9.181  1.00 28.94      A    C  
ANISOU  137  C   ALA A  23     1233   5787   3977   -908    -20  -1162  A    C  
ATOM    138  O   ALA A  23       0.552   1.746   8.820  1.00 29.53      A    O  
ANISOU  138  O   ALA A  23     1146   5981   4092   -913   -148  -1079  A    O  
ATOM    139  CB  ALA A  23       3.046   3.459   7.856  1.00 29.89      A    C  
ANISOU  139  CB  ALA A  23     1747   5956   3652   -856     24  -1177  A    C  
ATOM    140  N   LYS A  24       2.140   1.618  10.441  1.00 28.48      A    N  
ANISOU  140  N   LYS A  24     1054   5655   4113   -842    175  -1307  A    N  
ATOM    141  CA  LYS A  24       1.193   1.603  11.551  1.00 29.17      A    C  
ANISOU  141  CA  LYS A  24     1189   5521   4372   -763    313  -1342  A    C  
ATOM    142  C   LYS A  24       1.667   2.519  12.684  1.00 27.80      A    C  
ANISOU  142  C   LYS A  24      961   5350   4253   -612    394  -1421  A    C  
ATOM    143  O   LYS A  24       2.868   2.626  12.959  1.00 27.14      A    O  
ANISOU  143  O   LYS A  24      724   5170   4417   -727    498  -1483  A    O  
ATOM    144  CB  LYS A  24       0.877   0.178  12.026  1.00 30.86      A    C  
ANISOU  144  CB  LYS A  24     1527   5687   4510   -790    230  -1216  A    C  
ATOM    145  CG  LYS A  24       1.951  -0.563  12.789  1.00 37.50      A    C  
ANISOU  145  CG  LYS A  24     2867   6258   5123   -772   -379   -815  A    C  
ATOM    146  CD  LYS A  24       1.691  -0.548  14.304  1.00 44.81      A    C  
ANISOU  146  CD  LYS A  24     4266   6941   5820   -674   -926   -226  A    C  
ATOM    147  CE  LYS A  24       2.874  -1.170  15.046  1.00 46.58      A    C  
ANISOU  147  CE  LYS A  24     4541   7045   6111   -573  -1155    -31  A    C  
ATOM    148  NZ  LYS A  24       3.055  -0.630  16.423  1.00 46.50      A    N1+
ANISOU  148  NZ  LYS A  24     4343   7031   6294   -434  -1137    -62  A    N1+
ATOM    149  N   SER A  25       0.722   3.211  13.310  1.00 27.12      A    N  
ANISOU  149  N   SER A  25     1017   4992   4293   -474    478  -1342  A    N  
ATOM    150  CA  SER A  25       1.045   4.230  14.309  1.00 27.36      A    C  
ANISOU  150  CA  SER A  25     1298   4809   4287   -542    571   -988  A    C  
ATOM    151  C   SER A  25       1.682   3.638  15.557  1.00 25.25      A    C  
ANISOU  151  C   SER A  25     1263   4499   3831   -766    736   -886  A    C  
ATOM    152  O   SER A  25       1.158   2.679  16.134  1.00 27.10      A    O  
ANISOU  152  O   SER A  25     1559   4702   4034  -1027    700   -793  A    O  
ATOM    153  CB  SER A  25      -0.231   4.973  14.714  1.00 28.47      A    C  
ANISOU  153  CB  SER A  25     1474   4798   4544   -317    619  -1022  A    C  
ATOM    154  OG  SER A  25      -0.814   5.648  13.606  1.00 33.15      A    O  
ANISOU  154  OG  SER A  25     2011   5174   5411   -197    507   -493  A    O  
ATOM    155  N   PRO A  26       2.805   4.205  16.000  1.00 24.05      A    N  
ANISOU  155  N   PRO A  26     1393   4379   3366   -929    785   -640  A    N  
ATOM    156  CA  PRO A  26       3.391   3.754  17.253  1.00 24.50      A    C  
ANISOU  156  CA  PRO A  26     1728   4345   3235   -948    878   -559  A    C  
ATOM    157  C   PRO A  26       2.484   4.093  18.435  1.00 25.82      A    C  
ANISOU  157  C   PRO A  26     2157   4347   3307  -1171   1032   -553  A    C  
ATOM    158  O   PRO A  26       1.745   5.076  18.404  1.00 27.09      A    O  
ANISOU  158  O   PRO A  26     2301   4616   3375  -1001   1096   -553  A    O  
ATOM    159  CB  PRO A  26       4.703   4.546  17.342  1.00 23.89      A    C  
ANISOU  159  CB  PRO A  26     1492   4460   3127   -930    772   -551  A    C  
ATOM    160  CG  PRO A  26       4.945   5.078  15.983  1.00 23.76      A    C  
ANISOU  160  CG  PRO A  26     1315   4372   3339   -798    652   -403  A    C  
ATOM    161  CD  PRO A  26       3.614   5.245  15.344  1.00 22.80      A    C  
ANISOU  161  CD  PRO A  26     1132   4282   3249   -833    776   -582  A    C  
ATOM    162  N   THR A  27       2.570   3.296  19.486  1.00 28.48      A    N  
ANISOU  162  N   THR A  27     2856   4415   3551  -1456   1150   -406  A    N  
ATOM    163  CA  THR A  27       1.749   3.516  20.668  1.00 31.11      A    C  
ANISOU  163  CA  THR A  27     3355   4541   3925  -1650   1132   -307  A    C  
ATOM    164  C   THR A  27       2.619   3.709  21.898  1.00 30.14      A    C  
ANISOU  164  C   THR A  27     3436   4230   3785  -1404   1186   -351  A    C  
ATOM    165  O   THR A  27       2.490   4.698  22.630  1.00 31.69      A    O  
ANISOU  165  O   THR A  27     3740   4244   4056  -1229    876   -531  A    O  
ATOM    166  CB  THR A  27       0.766   2.328  20.904  1.00 32.58      A    C  
ANISOU  166  CB  THR A  27     3479   4731   4169  -1833   1096   -197  A    C  
ATOM    167  CG2 THR A  27      -0.269   2.256  19.794  1.00 34.64      A    C  
ANISOU  167  CG2 THR A  27     3528   5169   4465  -2010   1049   -274  A    C  
ATOM    168  OG1 THR A  27       1.489   1.091  20.919  1.00 36.29      A    O  
ANISOU  168  OG1 THR A  27     4320   4763   4706  -1914    820    -87  A    O  
ATOM    169  N   ILE A  28       3.504   2.744  22.127  1.00 29.61      A    N  
ANISOU  169  N   ILE A  28     3463   4086   3702  -1272   1333   -260  A    N  
ATOM    170  CA  ILE A  28       4.366   2.773  23.294  1.00 29.34      A    C  
ANISOU  170  CA  ILE A  28     3497   3914   3736  -1172   1447     59  A    C  
ATOM    171  C   ILE A  28       5.685   3.471  22.992  1.00 27.43      A    C  
ANISOU  171  C   ILE A  28     3384   3855   3185  -1075   1324    -15  A    C  
ATOM    172  O   ILE A  28       6.198   3.447  21.872  1.00 27.83      A    O  
ANISOU  172  O   ILE A  28     3422   4117   3034  -1127   1412    -41  A    O  
ATOM    173  CB  ILE A  28       4.623   1.359  23.883  1.00 30.74      A    C  
ANISOU  173  CB  ILE A  28     3643   3932   4104  -1158   1465    131  A    C  
ATOM    174  CG1 ILE A  28       5.357   0.456  22.886  1.00 33.34      A    C  
ANISOU  174  CG1 ILE A  28     3867   4151   4650   -842   1393    326  A    C  
ATOM    175  CG2 ILE A  28       3.308   0.737  24.355  1.00 32.45      A    C  
ANISOU  175  CG2 ILE A  28     3772   3995   4564  -1163   1562    472  A    C  
ATOM    176  CD1 ILE A  28       5.969  -0.795  23.507  1.00 35.77      A    C  
ANISOU  176  CD1 ILE A  28     3946   4587   5059   -383   1220    553  A    C  
ATOM    177  N   MET A  29       6.197   4.136  24.020  1.00 25.83      A    N  
ANISOU  177  N   MET A  29     3185   3662   2969   -636    925     46  A    N  
ATOM    178  CA  MET A  29       7.531   4.715  24.016  1.00 24.73      A    C  
ANISOU  178  CA  MET A  29     3120   3386   2890   -292    599     76  A    C  
ATOM    179  C   MET A  29       8.556   3.657  23.634  1.00 23.67      A    C  
ANISOU  179  C   MET A  29     2921   3217   2856    -93    412    193  A    C  
ATOM    180  O   MET A  29       8.382   2.480  23.942  1.00 24.72      A    O  
ANISOU  180  O   MET A  29     2890   3208   3294    -74    496    322  A    O  
ATOM    181  CB  MET A  29       7.834   5.225  25.421  1.00 26.43      A    C  
ANISOU  181  CB  MET A  29     3388   3610   3046   -251    412   -126  A    C  
ATOM    182  CG  MET A  29       8.792   6.386  25.489  1.00 27.62      A    C  
ANISOU  182  CG  MET A  29     3680   3819   2996   -263    472   -151  A    C  
ATOM    183  SD  MET A  29       8.811   7.070  27.157  1.00 24.41      A    S  
ANISOU  183  SD  MET A  29     2524   4205   2545     51    476   -164  A    S  
ATOM    184  CE  MET A  29       8.728   5.599  28.178  1.00 27.97      A    C  
ANISOU  184  CE  MET A  29     3824   3871   2933    -82    342   -346  A    C  
ATOM    185  N   THR A  30       9.627   4.077  22.969  1.00 22.04      A    N  
ANISOU  185  N   THR A  30     2903   2962   2511     87    285     98  A    N  
ATOM    186  CA  THR A  30      10.718   3.164  22.660  1.00 22.32      A    C  
ANISOU  186  CA  THR A  30     3181   2937   2362    285    172    -20  A    C  
ATOM    187  C   THR A  30      12.021   3.691  23.253  1.00 21.34      A    C  
ANISOU  187  C   THR A  30     3057   2872   2178    405    208     98  A    C  
ATOM    188  O   THR A  30      12.376   4.852  23.035  1.00 21.73      A    O  
ANISOU  188  O   THR A  30     3097   2870   2289    329    186    151  A    O  
ATOM    189  CB  THR A  30      10.868   3.013  21.130  1.00 22.88      A    C  
ANISOU  189  CB  THR A  30     3364   2955   2372    285    173   -172  A    C  
ATOM    190  CG2 THR A  30      12.076   2.156  20.777  1.00 24.61      A    C  
ANISOU  190  CG2 THR A  30     3689   3170   2492    476    252    -98  A    C  
ATOM    191  OG1 THR A  30       9.693   2.409  20.575  1.00 24.99      A    O  
ANISOU  191  OG1 THR A  30     3808   3129   2558    120    -30   -114  A    O  
ATOM    192  N   ARG A  31      12.725   2.841  23.995  1.00 22.39      A    N  
ANISOU  192  N   ARG A  31     3253   3086   2169    601    115    173  A    N  
ATOM    193  CA  ARG A  31      14.070   3.151  24.456  1.00 23.26      A    C  
ANISOU  193  CA  ARG A  31     3425   3262   2149    750     97    228  A    C  
ATOM    194  C   ARG A  31      15.027   2.913  23.294  1.00 23.42      A    C  
ANISOU  194  C   ARG A  31     3474   3176   2249    696    219    148  A    C  
ATOM    195  O   ARG A  31      15.159   1.796  22.799  1.00 24.53      A    O  
ANISOU  195  O   ARG A  31     3533   3224   2563    693    270     87  A    O  
ATOM    196  CB  ARG A  31      14.467   2.278  25.643  1.00 23.78      A    C  
ANISOU  196  CB  ARG A  31     3560   3359   2117    908     41    285  A    C  
ATOM    197  CG  ARG A  31      15.796   2.664  26.277  1.00 25.82      A    C  
ANISOU  197  CG  ARG A  31     4065   3607   2140   1018   -230    357  A    C  
ATOM    198  CD  ARG A  31      16.122   1.771  27.464  1.00 28.55      A    C  
ANISOU  198  CD  ARG A  31     4659   4029   2158   1544   -263    509  A    C  
ATOM    199  NE  ARG A  31      17.212   2.303  28.276  1.00 30.12      A    N  
ANISOU  199  NE  ARG A  31     4778   4629   2037   1902   -208    518  A    N  
ATOM    200  CZ  ARG A  31      17.817   1.627  29.259  1.00 31.37      A    C  
ANISOU  200  CZ  ARG A  31     4938   4863   2117   2178   -142    639  A    C  
ATOM    201  NH1 ARG A  31      17.452   0.383  29.555  1.00 33.10      A    N1+
ANISOU  201  NH1 ARG A  31     5260   4902   2416   2274    -49    640  A    N1+
ATOM    202  NH2 ARG A  31      18.796   2.192  29.957  1.00 32.35      A    N  
ANISOU  202  NH2 ARG A  31     4946   5156   2187   2318   -320    595  A    N  
ATOM    203  N   VAL A  32      15.695   3.970  22.848  1.00 23.60      A    N  
ANISOU  203  N   VAL A  32     3517   3237   2213    732    377    230  A    N  
ATOM    204  CA  VAL A  32      16.581   3.864  21.695  1.00 25.03      A    C  
ANISOU  204  CA  VAL A  32     3722   3420   2368    872    533    296  A    C  
ATOM    205  C   VAL A  32      18.026   3.629  22.123  1.00 24.78      A    C  
ANISOU  205  C   VAL A  32     3777   3407   2230   1115    467    228  A    C  
ATOM    206  O   VAL A  32      18.724   2.792  21.554  1.00 25.88      A    O  
ANISOU  206  O   VAL A  32     3989   3537   2308   1238    230     92  A    O  
ATOM    207  CB  VAL A  32      16.502   5.112  20.797  1.00 25.43      A    C  
ANISOU  207  CB  VAL A  32     3655   3522   2486    860    640    447  A    C  
ATOM    208  CG1 VAL A  32      15.056   5.414  20.435  1.00 25.75      A    C  
ANISOU  208  CG1 VAL A  32     3666   3571   2545    794    584    386  A    C  
ATOM    209  CG2 VAL A  32      17.148   6.303  21.485  1.00 26.23      A    C  
ANISOU  209  CG2 VAL A  32     3623   3736   2606    776    850    485  A    C  
ATOM    210  N   THR A  33      18.463   4.373  23.132  1.00 24.78      A    N  
ANISOU  210  N   THR A  33     3675   3578   2161   1400    406    261  A    N  
ATOM    211  CA  THR A  33      19.783   4.176  23.732  1.00 24.79      A    C  
ANISOU  211  CA  THR A  33     3512   3799   2108   1544    458    373  A    C  
ATOM    212  C   THR A  33      19.611   4.058  25.247  1.00 24.89      A    C  
ANISOU  212  C   THR A  33     3264   4070   2124   1597    443    329  A    C  
ATOM    213  O   THR A  33      18.477   3.965  25.743  1.00 25.48      A    O  
ANISOU  213  O   THR A  33     3194   4334   2152   1649    491    392  A    O  
ATOM    214  CB  THR A  33      20.755   5.333  23.401  1.00 24.72      A    C  
ANISOU  214  CB  THR A  33     3564   3747   2081   1532    472    331  A    C  
ATOM    215  CG2 THR A  33      20.879   5.541  21.883  1.00 25.07      A    C  
ANISOU  215  CG2 THR A  33     3542   3883   2099   1524    643    388  A    C  
ATOM    216  OG1 THR A  33      20.293   6.536  24.029  1.00 24.91      A    O  
ANISOU  216  OG1 THR A  33     3370   3901   2194   1562    427    170  A    O  
ATOM    217  N   ASN A  34      20.712   4.067  25.993  1.00 25.29      A    N  
ANISOU  217  N   ASN A  34     3079   4284   2247   1699    355    215  A    N  
ATOM    218  CA  ASN A  34      20.618   3.994  27.448  1.00 25.21      A    C  
ANISOU  218  CA  ASN A  34     2951   4323   2304   1676    161    137  A    C  
ATOM    219  C   ASN A  34      19.669   5.052  28.017  1.00 25.21      A    C  
ANISOU  219  C   ASN A  34     3032   4440   2107   1817    208    164  A    C  
ATOM    220  O   ASN A  34      18.836   4.745  28.875  1.00 25.96      A    O  
ANISOU  220  O   ASN A  34     3088   4571   2205   1875    315    219  A    O  
ATOM    221  CB  ASN A  34      21.984   4.106  28.120  1.00 25.64      A    C  
ANISOU  221  CB  ASN A  34     2854   4356   2531   1544     73    137  A    C  
ATOM    222  CG  ASN A  34      22.691   2.771  28.236  1.00 27.43      A    C  
ANISOU  222  CG  ASN A  34     2996   4313   3113   1221   -381    -10  A    C  
ATOM    223  ND2 ASN A  34      23.714   2.724  29.077  1.00 29.63      A    N  
ANISOU  223  ND2 ASN A  34     2912   4584   3763    939   -670     76  A    N  
ATOM    224  OD1 ASN A  34      22.328   1.788  27.591  1.00 28.98      A    O  
ANISOU  224  OD1 ASN A  34     2736   4383   3892    878   -461    -82  A    O  
ATOM    225  N   ASN A  35      19.790   6.287  27.531  1.00 24.07      A    N  
ANISOU  225  N   ASN A  35     2840   4383   1923   1858     -3     62  A    N  
ATOM    226  CA  ASN A  35      19.006   7.393  28.098  1.00 23.48      A    C  
ANISOU  226  CA  ASN A  35     2705   4408   1808   1771   -185    -35  A    C  
ATOM    227  C   ASN A  35      18.076   8.130  27.142  1.00 21.79      A    C  
ANISOU  227  C   ASN A  35     2462   4086   1729   1518   -203    -62  A    C  
ATOM    228  O   ASN A  35      17.318   9.001  27.590  1.00 22.34      A    O  
ANISOU  228  O   ASN A  35     2508   4189   1791   1562   -153    -76  A    O  
ATOM    229  CB  ASN A  35      19.922   8.419  28.761  1.00 24.36      A    C  
ANISOU  229  CB  ASN A  35     2752   4634   1869   1861   -307    -93  A    C  
ATOM    230  CG  ASN A  35      20.632   7.841  29.956  1.00 26.85      A    C  
ANISOU  230  CG  ASN A  35     2924   5213   2064   1973   -417    109  A    C  
ATOM    231  ND2 ASN A  35      21.854   7.378  29.733  1.00 29.77      A    N  
ANISOU  231  ND2 ASN A  35     3023   5651   2639   2073   -443     82  A    N  
ATOM    232  OD1 ASN A  35      20.079   7.797  31.046  1.00 29.45      A    O  
ANISOU  232  OD1 ASN A  35     3355   5658   2176   1976   -333    219  A    O  
ATOM    233  N   VAL A  36      18.146   7.795  25.858  1.00 19.70      A    N  
ANISOU  233  N   VAL A  36     2060   3756   1668   1216    -54     87  A    N  
ATOM    234  CA  VAL A  36      17.313   8.479  24.867  1.00 17.87      A    C  
ANISOU  234  CA  VAL A  36     1693   3416   1682    882    -17    159  A    C  
ATOM    235  C   VAL A  36      16.114   7.628  24.451  1.00 18.05      A    C  
ANISOU  235  C   VAL A  36     1764   3197   1897    803    136    152  A    C  
ATOM    236  O   VAL A  36      16.246   6.470  24.046  1.00 18.78      A    O  
ANISOU  236  O   VAL A  36     1932   3219   1985    877    137    148  A    O  
ATOM    237  CB  VAL A  36      18.128   8.923  23.629  1.00 17.75      A    C  
ANISOU  237  CB  VAL A  36     1579   3461   1703    772    -20    186  A    C  
ATOM    238  CG1 VAL A  36      17.259   9.671  22.633  1.00 17.13      A    C  
ANISOU  238  CG1 VAL A  36     1588   3323   1597    649   -193    197  A    C  
ATOM    239  CG2 VAL A  36      19.300   9.803  24.049  1.00 17.65      A    C  
ANISOU  239  CG2 VAL A  36     1172   3596   1939    758    -92    -31  A    C  
ATOM    240  N   TYR A  37      14.932   8.245  24.558  1.00 17.40      A    N  
ANISOU  240  N   TYR A  37     1588   3192   1832    736    120     68  A    N  
ATOM    241  CA  TYR A  37      13.660   7.583  24.264  1.00 17.61      A    C  
ANISOU  241  CA  TYR A  37     1747   3125   1817    522    186      6  A    C  
ATOM    242  C   TYR A  37      12.937   8.320  23.134  1.00 15.89      A    C  
ANISOU  242  C   TYR A  37     1488   2842   1708    408    175   -137  A    C  
ATOM    243  O   TYR A  37      13.147   9.522  22.934  1.00 15.68      A    O  
ANISOU  243  O   TYR A  37     1154   2854   1949    252    120   -109  A    O  
ATOM    244  CB  TYR A  37      12.766   7.535  25.518  1.00 18.45      A    C  
ANISOU  244  CB  TYR A  37     1939   3321   1752    524    229     76  A    C  
ATOM    245  CG  TYR A  37      13.310   6.665  26.635  1.00 20.62      A    C  
ANISOU  245  CG  TYR A  37     2468   3517   1851    680    401    197  A    C  
ATOM    246  CD1 TYR A  37      12.720   5.447  26.961  1.00 22.65      A    C  
ANISOU  246  CD1 TYR A  37     2946   3684   1975    706    489    337  A    C  
ATOM    247  CD2 TYR A  37      14.425   7.060  27.375  1.00 21.91      A    C  
ANISOU  247  CD2 TYR A  37     2655   3759   1912    847    344    241  A    C  
ATOM    248  CE1 TYR A  37      13.225   4.643  27.987  1.00 24.00      A    C  
ANISOU  248  CE1 TYR A  37     3248   3939   1932    847    471    417  A    C  
ATOM    249  CE2 TYR A  37      14.944   6.269  28.395  1.00 23.67      A    C  
ANISOU  249  CE2 TYR A  37     3129   3941   1923    957    535    476  A    C  
ATOM    250  CZ  TYR A  37      14.335   5.057  28.708  1.00 24.23      A    C  
ANISOU  250  CZ  TYR A  37     3336   3939   1932    970    482    480  A    C  
ATOM    251  OH  TYR A  37      14.843   4.257  29.721  1.00 26.78      A    O  
ANISOU  251  OH  TYR A  37     3729   4147   2298   1018    502    644  A    O  
ATOM    252  N   LEU A  38      12.106   7.575  22.398  1.00 15.76      A    N  
ANISOU  252  N   LEU A  38     1464   2698   1826    197    164    -98  A    N  
ATOM    253  CA  LEU A  38      11.323   8.114  21.275  1.00 15.83      A    C  
ANISOU  253  CA  LEU A  38     1333   2741   1941    164    172    -82  A    C  
ATOM    254  C   LEU A  38       9.834   7.890  21.541  1.00 15.88      A    C  
ANISOU  254  C   LEU A  38     1386   2583   2064     57    241   -108  A    C  
ATOM    255  O   LEU A  38       9.450   6.782  21.916  1.00 17.25      A    O  
ANISOU  255  O   LEU A  38     1630   2669   2257     98    388    -17  A    O  
ATOM    256  CB  LEU A  38      11.727   7.420  19.966  1.00 15.99      A    C  
ANISOU  256  CB  LEU A  38     1324   2777   1976    295     74    -82  A    C  
ATOM    257  CG  LEU A  38      10.886   7.673  18.702  1.00 14.71      A    C  
ANISOU  257  CG  LEU A  38      891   2791   1905     81    175    -71  A    C  
ATOM    258  CD1 LEU A  38      10.781   9.143  18.343  1.00 15.69      A    C  
ANISOU  258  CD1 LEU A  38     1080   2851   2029    195    395     49  A    C  
ATOM    259  CD2 LEU A  38      11.474   6.877  17.540  1.00 15.78      A    C  
ANISOU  259  CD2 LEU A  38     1221   2748   2027    175    436   -131  A    C  
ATOM    260  N   GLY A  39       9.018   8.924  21.343  1.00 15.65      A    N  
ANISOU  260  N   GLY A  39     1158   2671   2116    -31    331    -73  A    N  
ATOM    261  CA  GLY A  39       7.616   8.850  21.725  1.00 16.64      A    C  
ANISOU  261  CA  GLY A  39     1208   2867   2247   -115    461    -68  A    C  
ATOM    262  C   GLY A  39       6.701   9.784  20.963  1.00 15.71      A    C  
ANISOU  262  C   GLY A  39     1009   2842   2117   -296    505   -175  A    C  
ATOM    263  O   GLY A  39       7.149  10.631  20.186  1.00 15.60      A    O  
ANISOU  263  O   GLY A  39      956   2973   2000   -175    529   -162  A    O  
ATOM    264  N   ASN A  40       5.401   9.613  21.201  1.00 16.29      A    N  
ANISOU  264  N   ASN A  40      895   3111   2185   -355    612   -388  A    N  
ATOM    265  CA  ASN A  40       4.389  10.498  20.658  1.00 16.59      A    C  
ANISOU  265  CA  ASN A  40      781   3312   2212   -472    706   -458  A    C  
ATOM    266  C   ASN A  40       3.883  11.458  21.745  1.00 16.94      A    C  
ANISOU  266  C   ASN A  40      787   3429   2222   -307    723   -408  A    C  
ATOM    267  O   ASN A  40       4.439  11.541  22.852  1.00 17.08      A    O  
ANISOU  267  O   ASN A  40      876   3470   2143   -359    710   -458  A    O  
ATOM    268  CB  ASN A  40       3.257   9.672  20.040  1.00 17.02      A    C  
ANISOU  268  CB  ASN A  40      856   3422   2187   -599    709   -419  A    C  
ATOM    269  CG  ASN A  40       2.533   8.825  21.069  1.00 18.37      A    C  
ANISOU  269  CG  ASN A  40     1061   3679   2240   -788    863   -375  A    C  
ATOM    270  ND2 ASN A  40       1.724   7.897  20.571  1.00 21.96      A    N  
ANISOU  270  ND2 ASN A  40     1622   3964   2759  -1168    710   -203  A    N  
ATOM    271  OD1 ASN A  40       2.685   9.005  22.284  1.00 20.29      A    O  
ANISOU  271  OD1 ASN A  40     1365   4065   2280   -710    798   -193  A    O  
ATOM    272  N   TYR A  41       2.829  12.203  21.432  1.00 17.21      A    N  
ANISOU  272  N   TYR A  41      619   3558   2362   -237    842   -274  A    N  
ATOM    273  CA ATYR A  41       2.318  13.197  22.369  0.50 18.26      A    C  
ANISOU  273  CA ATYR A  41      867   3698   2372    -60    812   -186  A    C  
ATOM    274  CA BTYR A  41       2.309  13.199  22.361  0.50 18.24      A    C  
ANISOU  274  CA BTYR A  41      900   3677   2354    -62    790   -197  A    C  
ATOM    275  C   TYR A  41       1.783  12.576  23.659  1.00 18.55      A    C  
ANISOU  275  C   TYR A  41      996   3698   2354   -241    834   -208  A    C  
ATOM    276  O   TYR A  41       2.062  13.069  24.758  1.00 18.17      A    O  
ANISOU  276  O   TYR A  41      725   3799   2380   -285    834   -258  A    O  
ATOM    277  CB ATYR A  41       1.249  14.085  21.720  0.50 19.19      A    C  
ANISOU  277  CB ATYR A  41      970   3873   2449     91    768   -174  A    C  
ATOM    278  CB BTYR A  41       1.225  14.032  21.676  0.50 19.14      A    C  
ANISOU  278  CB BTYR A  41     1014   3817   2442     97    715   -215  A    C  
ATOM    279  CG ATYR A  41       1.065  15.382  22.469  0.50 20.88      A    C  
ANISOU  279  CG ATYR A  41     1217   4124   2594    421    516   -241  A    C  
ATOM    280  CG BTYR A  41       0.408  14.879  22.612  0.50 20.72      A    C  
ANISOU  280  CG BTYR A  41     1243   4174   2453    460    597   -296  A    C  
ATOM    281  CD1ATYR A  41       2.043  16.372  22.427  0.50 24.43      A    C  
ANISOU  281  CD1ATYR A  41     1956   4415   2910    252    524   -381  A    C  
ATOM    282  CD2ATYR A  41      -0.070  15.613  23.237  0.50 23.74      A    C  
ANISOU  282  CD2ATYR A  41     1720   4458   2842    533    544   -421  A    C  
ATOM    283  CD1BTYR A  41       0.869  16.118  23.045  0.50 23.02      A    C  
ANISOU  283  CD1BTYR A  41     1588   4359   2799    649    644   -428  A    C  
ATOM    284  CD2BTYR A  41      -0.841  14.448  23.051  0.50 22.46      A    C  
ANISOU  284  CD2BTYR A  41     1377   4487   2671    595    737   -386  A    C  
ATOM    285  CE1ATYR A  41       1.887  17.558  23.122  0.50 26.41      A    C  
ANISOU  285  CE1ATYR A  41     2152   4620   3264    182    671   -597  A    C  
ATOM    286  CE2ATYR A  41      -0.234  16.800  23.934  0.50 25.83      A    C  
ANISOU  286  CE2ATYR A  41     1941   4566   3307    450    608   -601  A    C  
ATOM    287  CE1BTYR A  41       0.110  16.906  23.902  0.50 24.32      A    C  
ANISOU  287  CE1BTYR A  41     1641   4386   3212    816    929   -467  A    C  
ATOM    288  CE2BTYR A  41      -1.601  15.225  23.912  0.50 23.59      A    C  
ANISOU  288  CE2BTYR A  41     1492   4426   3046    864    983   -403  A    C  
ATOM    289  CZ ATYR A  41       0.748  17.770  23.870  0.50 27.41      A    C  
ANISOU  289  CZ ATYR A  41     2202   4706   3508    280    723   -684  A    C  
ATOM    290  CZ BTYR A  41      -1.127  16.453  24.334  0.50 25.09      A    C  
ANISOU  290  CZ BTYR A  41     1791   4347   3395    900   1093   -381  A    C  
ATOM    291  OH ATYR A  41       0.591  18.944  24.564  0.50 29.19      A    O  
ANISOU  291  OH ATYR A  41     2313   4813   3962    118    728   -829  A    O  
ATOM    292  OH BTYR A  41      -1.887  17.223  25.190  0.50 25.88      A    O  
ANISOU  292  OH BTYR A  41     1993   4142   3698    988   1421   -318  A    O  
ATOM    293  N   LYS A  42       1.020  11.495  23.541  1.00 19.06      A    N  
ANISOU  293  N   LYS A  42     1042   3758   2442   -489    806   -247  A    N  
ATOM    294  CA  LYS A  42       0.528  10.800  24.734  1.00 20.22      A    C  
ANISOU  294  CA  LYS A  42     1386   3831   2467   -790    891   -386  A    C  
ATOM    295  C   LYS A  42       1.678  10.362  25.634  1.00 19.20      A    C  
ANISOU  295  C   LYS A  42     1500   3607   2187   -652    926   -364  A    C  
ATOM    296  O   LYS A  42       1.616  10.499  26.857  1.00 20.16      A    O  
ANISOU  296  O   LYS A  42     1404   4027   2228   -740    961   -392  A    O  
ATOM    297  CB  LYS A  42      -0.330   9.591  24.334  1.00 21.89      A    C  
ANISOU  297  CB  LYS A  42     1571   3894   2854   -929    850   -401  A    C  
ATOM    298  CG  LYS A  42      -0.797   8.743  25.523  1.00 26.76      A    C  
ANISOU  298  CG  LYS A  42     2311   4259   3596  -1500   1032   -427  A    C  
ATOM    299  CD  LYS A  42      -2.112   8.040  25.246  1.00 34.34      A    C  
ANISOU  299  CD  LYS A  42     3316   5109   4623  -2166   1190   -491  A    C  
ATOM    300  CE  LYS A  42      -2.525   7.166  26.421  1.00 36.89      A    C  
ANISOU  300  CE  LYS A  42     3702   5353   4960  -2483   1238   -489  A    C  
ATOM    301  NZ  LYS A  42      -2.532   7.883  27.734  1.00 37.59      A    N1+
ANISOU  301  NZ  LYS A  42     3603   5648   5030  -2469   1360   -511  A    N1+
ATOM    302  N   ASN A  43       2.755   9.855  25.023  1.00 18.59      A    N  
ANISOU  302  N   ASN A  43     1623   3425   2017   -467    930   -230  A    N  
ATOM    303  CA  ASN A  43       3.910   9.452  25.807  1.00 18.14      A    C  
ANISOU  303  CA  ASN A  43     1788   3095   2010   -348    873   -219  A    C  
ATOM    304  C   ASN A  43       4.485  10.651  26.576  1.00 17.43      A    C  
ANISOU  304  C   ASN A  43     1743   3000   1879   -320    860   -164  A    C  
ATOM    305  O   ASN A  43       4.966  10.500  27.711  1.00 18.63      A    O  
ANISOU  305  O   ASN A  43     1851   3233   1993   -353    715    -63  A    O  
ATOM    306  CB  ASN A  43       5.006   8.845  24.918  1.00 18.46      A    C  
ANISOU  306  CB  ASN A  43     1949   3088   1976   -320    921   -263  A    C  
ATOM    307  CG  ASN A  43       4.577   7.588  24.166  1.00 19.82      A    C  
ANISOU  307  CG  ASN A  43     2132   3059   2338   -471   1076   -241  A    C  
ATOM    308  ND2 ASN A  43       5.230   7.357  23.043  1.00 21.05      A    N  
ANISOU  308  ND2 ASN A  43     2806   3032   2161   -509   1216   -317  A    N  
ATOM    309  OD1 ASN A  43       3.698   6.814  24.590  1.00 23.49      A    O  
ANISOU  309  OD1 ASN A  43     2721   3422   2782   -834   1289   -175  A    O  
ATOM    310  N   ALA A  44       4.440  11.841  25.959  1.00 16.59      A    N  
ANISOU  310  N   ALA A  44     1263   2978   2064   -206    854   -203  A    N  
ATOM    311  CA  ALA A  44       4.961  13.040  26.648  1.00 16.89      A    C  
ANISOU  311  CA  ALA A  44     1262   2996   2161   -161    876   -274  A    C  
ATOM    312  C   ALA A  44       4.076  13.386  27.849  1.00 17.61      A    C  
ANISOU  312  C   ALA A  44     1084   3368   2240   -274    886   -467  A    C  
ATOM    313  O   ALA A  44       4.560  13.723  28.939  1.00 18.47      A    O  
ANISOU  313  O   ALA A  44     1168   3576   2273   -322    820   -469  A    O  
ATOM    314  CB  ALA A  44       5.056  14.211  25.693  1.00 16.99      A    C  
ANISOU  314  CB  ALA A  44     1206   2935   2316    -35    693   -184  A    C  
ATOM    315  N   MET A  45       2.765  13.301  27.647  1.00 18.92      A    N  
ANISOU  315  N   MET A  45     1124   3740   2325   -372   1032   -568  A    N  
ATOM    316  CA  MET A  45       1.820  13.582  28.734  1.00 20.47      A    C  
ANISOU  316  CA  MET A  45     1253   4149   2374   -366   1039   -610  A    C  
ATOM    317  C   MET A  45       1.975  12.598  29.893  1.00 21.18      A    C  
ANISOU  317  C   MET A  45     1553   4129   2365   -493   1128   -577  A    C  
ATOM    318  O   MET A  45       1.778  12.966  31.048  1.00 22.17      A    O  
ANISOU  318  O   MET A  45     1712   4262   2450   -564   1212   -630  A    O  
ATOM    319  CB  MET A  45       0.385  13.598  28.201  1.00 21.53      A    C  
ANISOU  319  CB  MET A  45     1289   4415   2477   -348    951   -666  A    C  
ATOM    320  CG  MET A  45       0.104  14.683  27.167  1.00 21.67      A    C  
ANISOU  320  CG  MET A  45      775   4620   2838   -388    693   -612  A    C  
ATOM    321  SD  MET A  45       0.587  16.361  27.598  1.00 26.38      A    S  
ANISOU  321  SD  MET A  45     1492   4747   3783    282    597   -934  A    S  
ATOM    322  CE  MET A  45       2.169  16.532  26.750  1.00 25.37      A    C  
ANISOU  322  CE  MET A  45     1133   4424   4083   -140    432   -671  A    C  
ATOM    323  N   ASP A  46       2.352  11.361  29.570  1.00 21.77      A    N  
ANISOU  323  N   ASP A  46     1897   3968   2406   -749   1186   -452  A    N  
ATOM    324  CA  ASP A  46       2.556  10.312  30.567  1.00 22.83      A    C  
ANISOU  324  CA  ASP A  46     2150   4054   2469   -869   1199   -274  A    C  
ATOM    325  C   ASP A  46       3.967  10.279  31.139  1.00 23.32      A    C  
ANISOU  325  C   ASP A  46     2293   3973   2592   -842   1067   -182  A    C  
ATOM    326  O   ASP A  46       4.257   9.492  32.050  1.00 24.36      A    O  
ANISOU  326  O   ASP A  46     2329   4241   2685   -903   1023   -113  A    O  
ATOM    327  CB  ASP A  46       2.222   8.940  29.969  1.00 23.87      A    C  
ANISOU  327  CB  ASP A  46     2398   4072   2599   -948   1186   -197  A    C  
ATOM    328  CG  ASP A  46       0.752   8.796  29.631  1.00 25.17      A    C  
ANISOU  328  CG  ASP A  46     2381   4645   2538  -1164   1412   -342  A    C  
ATOM    329  OD1 ASP A  46      -0.068   9.513  30.247  1.00 29.86      A    O  
ANISOU  329  OD1 ASP A  46     2763   5508   3075  -1127   1576   -505  A    O  
ATOM    330  OD2 ASP A  46       0.415   7.978  28.743  1.00 26.57      A    O1-
ANISOU  330  OD2 ASP A  46     2529   4702   2865  -1286   1324   -355  A    O1-
ATOM    331  N   ALA A  47       4.831  11.146  30.622  1.00 22.61      A    N  
ANISOU  331  N   ALA A  47     2221   3984   2386   -781    986   -197  A    N  
ATOM    332  CA  ALA A  47       6.226  11.200  31.042  1.00 22.15      A    C  
ANISOU  332  CA  ALA A  47     2310   3885   2222   -595    913   -109  A    C  
ATOM    333  C   ALA A  47       6.403  11.304  32.559  1.00 23.00      A    C  
ANISOU  333  C   ALA A  47     2698   3880   2161   -502    850   -118  A    C  
ATOM    334  O   ALA A  47       7.154  10.526  33.142  1.00 23.48      A    O  
ANISOU  334  O   ALA A  47     2718   4002   2203   -392    878    -82  A    O  
ATOM    335  CB  ALA A  47       6.971  12.326  30.330  1.00 22.10      A    C  
ANISOU  335  CB  ALA A  47     2230   3901   2266   -615    776     10  A    C  
ATOM    336  N   PRO A  48       5.718  12.257  33.207  1.00 24.16      A    N  
ANISOU  336  N   PRO A  48     2971   4065   2143   -375    860   -227  A    N  
ATOM    337  CA  PRO A  48       5.928  12.421  34.655  1.00 25.88      A    C  
ANISOU  337  CA  PRO A  48     3431   4237   2167   -163    882   -230  A    C  
ATOM    338  C   PRO A  48       5.686  11.160  35.496  1.00 27.51      A    C  
ANISOU  338  C   PRO A  48     3795   4402   2257    120    996    -38  A    C  
ATOM    339  O   PRO A  48       6.316  10.990  36.547  1.00 28.55      A    O  
ANISOU  339  O   PRO A  48     3943   4666   2240    204    974    -35  A    O  
ATOM    340  CB  PRO A  48       4.924  13.524  35.024  1.00 25.82      A    C  
ANISOU  340  CB  PRO A  48     3433   4203   2175   -197    895   -274  A    C  
ATOM    341  CG  PRO A  48       4.807  14.326  33.746  1.00 25.01      A    C  
ANISOU  341  CG  PRO A  48     3249   4144   2108   -351    763   -359  A    C  
ATOM    342  CD  PRO A  48       4.773  13.264  32.685  1.00 24.06      A    C  
ANISOU  342  CD  PRO A  48     3009   3930   2201   -436    776   -285  A    C  
ATOM    343  N   SER A  49       4.813  10.266  35.034  1.00 27.83      A    N  
ANISOU  343  N   SER A  49     3759   4327   2489    263   1190    216  A    N  
ATOM    344  CA ASER A  49       4.483   9.049  35.777  0.50 28.62      A    C  
ANISOU  344  CA ASER A  49     3957   4347   2572    285   1305    320  A    C  
ATOM    345  CA BSER A  49       4.461   9.048  35.763  0.50 28.79      A    C  
ANISOU  345  CA BSER A  49     3905   4347   2685    305   1208    438  A    C  
ATOM    346  C   SER A  49       5.167   7.794  35.242  1.00 28.90      A    C  
ANISOU  346  C   SER A  49     4117   4298   2567    302   1342    436  A    C  
ATOM    347  O   SER A  49       4.951   6.686  35.759  1.00 28.92      A    O  
ANISOU  347  O   SER A  49     4052   4287   2651    261   1404    449  A    O  
ATOM    348  CB ASER A  49       2.971   8.824  35.803  0.50 28.69      A    C  
ANISOU  348  CB ASER A  49     3901   4314   2687    263   1324    361  A    C  
ATOM    349  CB BSER A  49       2.945   8.853  35.708  0.50 29.08      A    C  
ANISOU  349  CB BSER A  49     3822   4379   2849    274   1208    511  A    C  
ATOM    350  OG ASER A  49       2.346   9.783  36.633  0.50 29.61      A    O  
ANISOU  350  OG ASER A  49     3853   4623   2773    219   1366    205  A    O  
ATOM    351  OG BSER A  49       2.565   7.633  36.313  0.50 30.66      A    O  
ANISOU  351  OG BSER A  49     3919   4474   3257    247    917    700  A    O  
ATOM    352  N   SER A  50       5.994   7.983  34.215  1.00 29.64      A    N  
ANISOU  352  N   SER A  50     4462   4329   2469    206   1491    368  A    N  
ATOM    353  CA  SER A  50       6.733   6.889  33.599  1.00 30.90      A    C  
ANISOU  353  CA  SER A  50     4708   4462   2569    208   1289    386  A    C  
ATOM    354  C   SER A  50       7.679   6.160  34.547  1.00 32.23      A    C  
ANISOU  354  C   SER A  50     4942   4535   2768     54   1171    592  A    C  
ATOM    355  O   SER A  50       8.201   6.747  35.494  1.00 32.55      A    O  
ANISOU  355  O   SER A  50     4787   4738   2842     73   1168    568  A    O  
ATOM    356  CB  SER A  50       7.592   7.432  32.447  1.00 29.90      A    C  
ANISOU  356  CB  SER A  50     4625   4417   2319    296   1365    313  A    C  
ATOM    357  OG  SER A  50       8.520   6.459  32.001  1.00 31.06      A    O  
ANISOU  357  OG  SER A  50     4539   4674   2590    434   1111    370  A    O  
ATOM    358  N   GLU A  51       7.907   4.878  34.262  1.00 34.10      A    N  
ANISOU  358  N   GLU A  51     5278   4375   3303   -171    744    882  A    N  
ATOM    359  CA  GLU A  51       8.893   4.072  34.983  1.00 35.15      A    C  
ANISOU  359  CA  GLU A  51     5605   4329   3420   -241    548   1096  A    C  
ATOM    360  C   GLU A  51      10.280   4.721  34.903  1.00 33.70      A    C  
ANISOU  360  C   GLU A  51     5375   4401   3030    -65    509   1146  A    C  
ATOM    361  O   GLU A  51      11.125   4.517  35.782  1.00 34.43      A    O  
ANISOU  361  O   GLU A  51     5493   4638   2949    -93    423   1199  A    O  
ATOM    362  CB  GLU A  51       8.938   2.649  34.423  1.00 36.14      A    C  
ANISOU  362  CB  GLU A  51     5849   4223   3659   -353    540   1168  A    C  
ATOM    363  CG  GLU A  51       7.623   1.888  34.559  1.00 39.64      A    C  
ANISOU  363  CG  GLU A  51     6452   4426   4185   -555    623   1031  A    C  
ATOM    364  CD  GLU A  51       7.346   1.498  35.995  1.00 43.57      A    C  
ANISOU  364  CD  GLU A  51     7099   4767   4690   -754   1014    979  A    C  
ATOM    365  OE1 GLU A  51       6.515   2.162  36.653  1.00 45.67      A    O  
ANISOU  365  OE1 GLU A  51     7257   5077   5019   -768   1074    803  A    O  
ATOM    366  OE2 GLU A  51       7.977   0.524  36.468  1.00 45.62      A    O1-
ANISOU  366  OE2 GLU A  51     7529   5041   4765   -619   1092   1053  A    O1-
ATOM    367  N   VAL A  52      10.486   5.496  33.846  1.00 31.35      A    N  
ANISOU  367  N   VAL A  52     4924   4345   2642    337    653    925  A    N  
ATOM    368  CA  VAL A  52      11.722   6.227  33.593  1.00 30.26      A    C  
ANISOU  368  CA  VAL A  52     4706   4305   2486    529    610    767  A    C  
ATOM    369  C   VAL A  52      11.668   7.595  34.259  1.00 31.01      A    C  
ANISOU  369  C   VAL A  52     4881   4541   2361    494    384    666  A    C  
ATOM    370  O   VAL A  52      10.680   8.317  34.106  1.00 31.45      A    O  
ANISOU  370  O   VAL A  52     4913   4553   2484    540    399    571  A    O  
ATOM    371  CB  VAL A  52      11.942   6.416  32.071  1.00 29.32      A    C  
ANISOU  371  CB  VAL A  52     4474   4277   2390    606    759    662  A    C  
ATOM    372  CG1 VAL A  52      13.241   7.160  31.777  1.00 28.96      A    C  
ANISOU  372  CG1 VAL A  52     4248   4239   2515    644    825    696  A    C  
ATOM    373  CG2 VAL A  52      11.917   5.070  31.360  1.00 30.35      A    C  
ANISOU  373  CG2 VAL A  52     4596   4239   2696    662    623    584  A    C  
ATOM    374  N   LYS A  53      12.720   7.952  34.991  1.00 32.74      A    N  
ANISOU  374  N   LYS A  53     5141   4845   2453    350    -54    772  A    N  
ATOM    375  CA  LYS A  53      12.800   9.283  35.610  1.00 33.63      A    C  
ANISOU  375  CA  LYS A  53     5138   5134   2504    261   -450    758  A    C  
ATOM    376  C   LYS A  53      13.408  10.310  34.651  1.00 29.46      A    C  
ANISOU  376  C   LYS A  53     4250   4758   2187    423   -230    505  A    C  
ATOM    377  O   LYS A  53      14.600  10.606  34.707  1.00 29.49      A    O  
ANISOU  377  O   LYS A  53     4099   4917   2187    573   -274    425  A    O  
ATOM    378  CB  LYS A  53      13.576   9.244  36.940  1.00 36.36      A    C  
ANISOU  378  CB  LYS A  53     5647   5483   2685    186   -658    908  A    C  
ATOM    379  CG  LYS A  53      14.676   8.177  37.070  1.00 42.95      A    C  
ANISOU  379  CG  LYS A  53     6121   6704   3495    227  -1058    895  A    C  
ATOM    380  CD  LYS A  53      15.928   8.465  36.240  1.00 49.58      A    C  
ANISOU  380  CD  LYS A  53     6603   8191   4045    428  -1154    732  A    C  
ATOM    381  CE  LYS A  53      17.036   7.462  36.528  1.00 51.67      A    C  
ANISOU  381  CE  LYS A  53     6664   8790   4178    516  -1181    544  A    C  
ATOM    382  NZ  LYS A  53      18.236   7.688  35.670  1.00 52.59      A    N1+
ANISOU  382  NZ  LYS A  53     6751   9114   4117    507  -1212    509  A    N1+
ATOM    383  N   PHE A  54      12.587  10.870  33.768  1.00 24.67      A    N  
ANISOU  383  N   PHE A  54     3258   4237   1878    379    -10    137  A    N  
ATOM    384  CA  PHE A  54      13.109  11.819  32.777  1.00 21.19      A    C  
ANISOU  384  CA  PHE A  54     2381   3941   1728    328     76   -120  A    C  
ATOM    385  C   PHE A  54      13.603  13.106  33.417  1.00 20.72      A    C  
ANISOU  385  C   PHE A  54     2034   4041   1797    340    107   -304  A    C  
ATOM    386  O   PHE A  54      12.924  13.681  34.286  1.00 21.90      A    O  
ANISOU  386  O   PHE A  54     2117   4131   2073    406    153   -410  A    O  
ATOM    387  CB  PHE A  54      12.036  12.167  31.737  1.00 19.93      A    C  
ANISOU  387  CB  PHE A  54     2148   3740   1684    346    153   -141  A    C  
ATOM    388  CG  PHE A  54      11.725  11.013  30.836  1.00 19.62      A    C  
ANISOU  388  CG  PHE A  54     2184   3537   1735    285    153    -87  A    C  
ATOM    389  CD1 PHE A  54      12.622  10.648  29.841  1.00 19.09      A    C  
ANISOU  389  CD1 PHE A  54     2336   3269   1648    482    305     40  A    C  
ATOM    390  CD2 PHE A  54      10.553  10.285  30.979  1.00 20.12      A    C  
ANISOU  390  CD2 PHE A  54     2380   3404   1861    207    419    -31  A    C  
ATOM    391  CE1 PHE A  54      12.347   9.570  29.006  1.00 20.27      A    C  
ANISOU  391  CE1 PHE A  54     2354   3400   1949    399    366    -62  A    C  
ATOM    392  CE2 PHE A  54      10.263   9.212  30.150  1.00 20.71      A    C  
ANISOU  392  CE2 PHE A  54     2511   3366   1993     63    507    -37  A    C  
ATOM    393  CZ  PHE A  54      11.164   8.850  29.150  1.00 21.72      A    C  
ANISOU  393  CZ  PHE A  54     2842   3355   2055    137    562      0  A    C  
ATOM    394  N   LYS A  55      14.773  13.557  32.970  1.00 20.09      A    N  
ANISOU  394  N   LYS A  55     1738   4126   1770    370    -70   -282  A    N  
ATOM    395  CA  LYS A  55      15.242  14.898  33.297  1.00 19.99      A    C  
ANISOU  395  CA  LYS A  55     1500   4235   1861    272   -252   -296  A    C  
ATOM    396  C   LYS A  55      14.719  15.891  32.261  1.00 18.40      A    C  
ANISOU  396  C   LYS A  55     1189   4038   1764    293   -197   -333  A    C  
ATOM    397  O   LYS A  55      14.354  17.030  32.598  1.00 18.95      A    O  
ANISOU  397  O   LYS A  55     1164   4104   1932    241    -31   -438  A    O  
ATOM    398  CB  LYS A  55      16.772  14.965  33.378  1.00 20.97      A    C  
ANISOU  398  CB  LYS A  55     1527   4336   2106    315   -326   -285  A    C  
ATOM    399  CG  LYS A  55      17.284  16.355  33.729  1.00 23.84      A    C  
ANISOU  399  CG  LYS A  55     1737   4717   2606    109   -582   -417  A    C  
ATOM    400  CD  LYS A  55      18.752  16.374  34.121  1.00 27.22      A    C  
ANISOU  400  CD  LYS A  55     1773   5044   3524     31   -678   -662  A    C  
ATOM    401  CE  LYS A  55      19.153  17.785  34.533  1.00 29.92      A    C  
ANISOU  401  CE  LYS A  55     1817   5292   4259   -285   -684   -794  A    C  
ATOM    402  NZ  LYS A  55      20.544  17.822  35.076  1.00 33.20      A    N1+
ANISOU  402  NZ  LYS A  55     2319   5572   4722   -197   -750   -974  A    N1+
ATOM    403  N   TYR A  56      14.669  15.444  31.008  1.00 17.19      A    N  
ANISOU  403  N   TYR A  56      981   3874   1676    148   -141   -230  A    N  
ATOM    404  CA  TYR A  56      14.303  16.300  29.890  1.00 16.24      A    C  
ANISOU  404  CA  TYR A  56      770   3664   1738    131    -71   -262  A    C  
ATOM    405  C   TYR A  56      13.226  15.666  29.028  1.00 15.16      A    C  
ANISOU  405  C   TYR A  56      664   3334   1761    219    -98   -259  A    C  
ATOM    406  O   TYR A  56      13.153  14.442  28.909  1.00 16.05      A    O  
ANISOU  406  O   TYR A  56      847   3258   1993    263   -125   -175  A    O  
ATOM    407  CB  TYR A  56      15.520  16.540  28.995  1.00 16.38      A    C  
ANISOU  407  CB  TYR A  56      585   3869   1770     92      6   -285  A    C  
ATOM    408  CG  TYR A  56      16.623  17.357  29.625  1.00 17.51      A    C  
ANISOU  408  CG  TYR A  56      675   4110   1867     70     -6   -511  A    C  
ATOM    409  CD1 TYR A  56      16.473  18.727  29.822  1.00 18.87      A    C  
ANISOU  409  CD1 TYR A  56      833   4320   2017     97     57   -820  A    C  
ATOM    410  CD2 TYR A  56      17.820  16.767  29.998  1.00 19.48      A    C  
ANISOU  410  CD2 TYR A  56     1084   4316   2002    195   -207   -544  A    C  
ATOM    411  CE1 TYR A  56      17.471  19.485  30.395  1.00 20.50      A    C  
ANISOU  411  CE1 TYR A  56     1075   4435   2280    109    -65   -750  A    C  
ATOM    412  CE2 TYR A  56      18.826  17.516  30.564  1.00 20.02      A    C  
ANISOU  412  CE2 TYR A  56      971   4528   2108    -35   -131   -820  A    C  
ATOM    413  CZ  TYR A  56      18.653  18.874  30.753  1.00 20.72      A    C  
ANISOU  413  CZ  TYR A  56      863   4623   2386    107   -141   -825  A    C  
ATOM    414  OH  TYR A  56      19.667  19.617  31.315  1.00 23.83      A    O  
ANISOU  414  OH  TYR A  56     1324   4949   2779   -252   -307   -746  A    O  
ATOM    415  N   VAL A  57      12.400  16.517  28.422  1.00 15.04      A    N  
ANISOU  415  N   VAL A  57      604   3269   1843    263    -93   -344  A    N  
ATOM    416  CA  VAL A  57      11.561  16.144  27.281  1.00 14.89      A    C  
ANISOU  416  CA  VAL A  57      623   3264   1771    109     -5   -302  A    C  
ATOM    417  C   VAL A  57      11.859  17.145  26.157  1.00 14.16      A    C  
ANISOU  417  C   VAL A  57      482   3125   1773    -23     43   -370  A    C  
ATOM    418  O   VAL A  57      11.823  18.373  26.398  1.00 15.59      A    O  
ANISOU  418  O   VAL A  57      759   3190   1976    -87     35   -395  A    O  
ATOM    419  CB  VAL A  57      10.062  16.165  27.662  1.00 15.50      A    C  
ANISOU  419  CB  VAL A  57      705   3336   1849     -3     31   -274  A    C  
ATOM    420  CG1 VAL A  57       9.175  16.008  26.421  1.00 16.66      A    C  
ANISOU  420  CG1 VAL A  57      498   3804   2029    313     49   -392  A    C  
ATOM    421  CG2 VAL A  57       9.749  15.047  28.638  1.00 16.87      A    C  
ANISOU  421  CG2 VAL A  57     1123   3289   1999    -70    219   -205  A    C  
ATOM    422  N   LEU A  58      12.158  16.612  24.966  1.00 13.51      A    N  
ANISOU  422  N   LEU A  58      426   2969   1738    -15      6   -280  A    N  
ATOM    423  CA  LEU A  58      12.355  17.447  23.801  1.00 13.34      A    C  
ANISOU  423  CA  LEU A  58      260   2998   1808     88     65   -230  A    C  
ATOM    424  C   LEU A  58      11.042  17.431  22.993  1.00 12.88      A    C  
ANISOU  424  C   LEU A  58      263   2883   1747     52    112   -210  A    C  
ATOM    425  O   LEU A  58      10.702  16.444  22.356  1.00 13.17      A    O  
ANISOU  425  O   LEU A  58      269   2880   1853      0    160   -240  A    O  
ATOM    426  CB  LEU A  58      13.550  16.932  22.981  1.00 14.47      A    C  
ANISOU  426  CB  LEU A  58      306   3172   2020    113    162   -283  A    C  
ATOM    427  CG  LEU A  58      13.865  17.721  21.731  1.00 16.30      A    C  
ANISOU  427  CG  LEU A  58      307   3503   2381    194    295    -60  A    C  
ATOM    428  CD1 LEU A  58      14.176  19.165  22.074  1.00 20.08      A    C  
ANISOU  428  CD1 LEU A  58     1246   3709   2673    252    599    -97  A    C  
ATOM    429  CD2 LEU A  58      15.092  17.060  21.074  1.00 19.02      A    C  
ANISOU  429  CD2 LEU A  58      421   4025   2779    296    606     38  A    C  
ATOM    430  N   ASN A  59      10.344  18.555  23.078  1.00 13.42      A    N  
ANISOU  430  N   ASN A  59      269   2935   1896     74    148    -54  A    N  
ATOM    431  CA  ASN A  59       9.053  18.750  22.429  1.00 13.06      A    C  
ANISOU  431  CA  ASN A  59      281   2944   1738     92    186   -118  A    C  
ATOM    432  C   ASN A  59       9.293  19.376  21.052  1.00 12.83      A    C  
ANISOU  432  C   ASN A  59      286   2754   1835    105    210    -74  A    C  
ATOM    433  O   ASN A  59       9.641  20.548  20.957  1.00 13.51      A    O  
ANISOU  433  O   ASN A  59      306   2795   2034     93    294    -43  A    O  
ATOM    434  CB  ASN A  59       8.207  19.687  23.289  1.00 13.61      A    C  
ANISOU  434  CB  ASN A  59      281   3025   1863    172    148   -215  A    C  
ATOM    435  CG  ASN A  59       6.924  20.139  22.593  1.00 13.59      A    C  
ANISOU  435  CG  ASN A  59      346   3124   1692    252    306   -125  A    C  
ATOM    436  ND2 ASN A  59       6.388  21.267  23.040  1.00 15.20      A    N  
ANISOU  436  ND2 ASN A  59      410   3055   2310     76    555   -204  A    N  
ATOM    437  OD1 ASN A  59       6.456  19.491  21.650  1.00 14.91      A    O  
ANISOU  437  OD1 ASN A  59      377   3402   1888    217    401   -249  A    O  
ATOM    438  N   LEU A  60       9.076  18.578  20.012  1.00 13.22      A    N  
ANISOU  438  N   LEU A  60      276   2991   1755     57    175   -126  A    N  
ATOM    439  CA  LEU A  60       9.279  19.005  18.636  1.00 14.22      A    C  
ANISOU  439  CA  LEU A  60      284   3124   1995    283     48   -206  A    C  
ATOM    440  C   LEU A  60       7.978  19.475  17.990  1.00 14.55      A    C  
ANISOU  440  C   LEU A  60      302   3269   1958    353     98    -92  A    C  
ATOM    441  O   LEU A  60       7.965  19.838  16.815  1.00 14.86      A    O  
ANISOU  441  O   LEU A  60      289   3346   2011    285    109   -118  A    O  
ATOM    442  CB  LEU A  60       9.864  17.858  17.807  1.00 14.16      A    C  
ANISOU  442  CB  LEU A  60      298   3025   2055    349     26   -170  A    C  
ATOM    443  CG  LEU A  60      11.384  17.697  17.741  1.00 20.88      A    C  
ANISOU  443  CG  LEU A  60      593   3483   3858    417    -31   -715  A    C  
ATOM    444  CD1 LEU A  60      12.085  18.546  18.787  1.00 19.64      A    C  
ANISOU  444  CD1 LEU A  60      483   3379   3600    571   -206   -586  A    C  
ATOM    445  CD2 LEU A  60      11.767  16.233  17.879  1.00 19.00      A    C  
ANISOU  445  CD2 LEU A  60      408   3424   3388    623    -54   -803  A    C  
ATOM    446  N   THR A  61       6.882  19.463  18.745  1.00 15.20      A    N  
ANISOU  446  N   THR A  61      344   3194   2238    423    219   -142  A    N  
ATOM    447  CA  THR A  61       5.604  19.940  18.191  1.00 16.25      A    C  
ANISOU  447  CA  THR A  61      357   3416   2401    502    226      0  A    C  
ATOM    448  C   THR A  61       5.564  21.461  18.216  1.00 16.50      A    C  
ANISOU  448  C   THR A  61      386   3418   2465    582    238     15  A    C  
ATOM    449  O   THR A  61       6.392  22.110  18.869  1.00 17.13      A    O  
ANISOU  449  O   THR A  61      337   3452   2720    493    148     68  A    O  
ATOM    450  CB  THR A  61       4.365  19.400  18.955  1.00 16.31      A    C  
ANISOU  450  CB  THR A  61      313   3459   2423    393    149    -63  A    C  
ATOM    451  CG2 THR A  61       4.439  17.899  19.121  1.00 16.82      A    C  
ANISOU  451  CG2 THR A  61      315   3479   2596    446     23    -11  A    C  
ATOM    452  OG1 THR A  61       4.255  20.051  20.229  1.00 17.05      A    O  
ANISOU  452  OG1 THR A  61      296   3612   2569    266    216   -119  A    O  
ATOM    453  N   MET A  62       4.550  22.048  17.572  1.00 17.17      A    N  
ANISOU  453  N   MET A  62      456   3503   2565    762    263    109  A    N  
ATOM    454  CA  MET A  62       4.501  23.505  17.496  1.00 18.33      A    C  
ANISOU  454  CA  MET A  62      611   3671   2682    854    284     68  A    C  
ATOM    455  C   MET A  62       4.006  24.157  18.790  1.00 19.51      A    C  
ANISOU  455  C   MET A  62      886   3731   2795    917    377     31  A    C  
ATOM    456  O   MET A  62       4.286  25.331  19.035  1.00 21.58      A    O  
ANISOU  456  O   MET A  62     1360   3770   3070    816    524    -65  A    O  
ATOM    457  CB  MET A  62       3.626  23.964  16.318  1.00 18.54      A    C  
ANISOU  457  CB  MET A  62      531   3797   2718    974    186    126  A    C  
ATOM    458  CG  MET A  62       4.263  23.666  14.975  1.00 19.83      A    C  
ANISOU  458  CG  MET A  62      746   3955   2833    833    119     37  A    C  
ATOM    459  SD  MET A  62       5.766  24.624  14.686  1.00 21.54      A    S  
ANISOU  459  SD  MET A  62      741   4246   3197    680    153    260  A    S  
ATOM    460  CE  MET A  62       5.055  26.247  14.367  1.00 24.35      A    C  
ANISOU  460  CE  MET A  62      855   4336   4059    675    417    163  A    C  
ATOM    461  N  AASP A  63       3.285  23.403  19.620  0.50 19.66      A    N  
ANISOU  461  N  AASP A  63      759   3975   2736    834    472     38  A    N  
ATOM    462  N  BASP A  63       3.327  23.402  19.639  0.50 19.66      A    N  
ANISOU  462  N  BASP A  63      758   3975   2736    834    472     38  A    N  
ATOM    463  CA AASP A  63       2.675  23.958  20.839  0.50 20.18      A    C  
ANISOU  463  CA AASP A  63      921   3982   2763    737    586      6  A    C  
ATOM    464  CA BASP A  63       2.711  24.021  20.802  0.50 20.17      A    C  
ANISOU  464  CA BASP A  63      919   3982   2763    737    586      6  A    C  
ATOM    465  C  AASP A  63       3.593  23.854  22.058  0.50 19.32      A    C  
ANISOU  465  C  AASP A  63      876   3743   2723    706    749      6  A    C  
ATOM    466  C  BASP A  63       3.489  23.844  22.108  0.50 19.33      A    C  
ANISOU  466  C  BASP A  63      878   3745   2723    706    746      6  A    C  
ATOM    467  O  AASP A  63       4.143  22.787  22.343  0.50 19.24      A    O  
ANISOU  467  O  AASP A  63      816   3720   2773    706    789    -17  A    O  
ATOM    468  O  BASP A  63       3.861  22.731  22.482  0.50 19.36      A    O  
ANISOU  468  O  BASP A  63      847   3727   2781    706    771    -19  A    O  
ATOM    469  CB AASP A  63       1.322  23.286  21.135  0.50 20.71      A    C  
ANISOU  469  CB AASP A  63      974   4151   2745    680    579     31  A    C  
ATOM    470  CB BASP A  63       1.241  23.622  20.908  0.50 20.69      A    C  
ANISOU  470  CB BASP A  63      962   4156   2743    680    575     31  A    C  
ATOM    471  CG AASP A  63       0.621  23.877  22.360  0.50 20.44      A    C  
ANISOU  471  CG AASP A  63      988   4038   2739    324    502     96  A    C  
ATOM    472  CG BASP A  63       0.425  24.144  19.737  0.50 20.97      A    C  
ANISOU  472  CG BASP A  63     1067   4088   2811    351    496     54  A    C  
ATOM    473  OD1AASP A  63       0.327  25.092  22.362  0.50 21.35      A    O  
ANISOU  473  OD1AASP A  63      991   4201   2921    296    423    230  A    O  
ATOM    474  OD2AASP A  63       0.346  23.121  23.319  0.50 22.12      A    O1-
ANISOU  474  OD2AASP A  63     1333   4162   2908     87    425    109  A    O1-
ATOM    475  OD1BASP A  63      -0.007  25.316  19.798  0.50 21.49      A    O  
ANISOU  475  OD1BASP A  63     1115   4111   2939    513    181    228  A    O  
ATOM    476  OD2BASP A  63       0.238  23.397  18.749  0.50 21.25      A    O1-
ANISOU  476  OD2BASP A  63      935   4158   2980    205    366     65  A    O1-
ATOM    477  N   LYS A  64       3.742  24.967  22.776  1.00 19.06      A    N  
ANISOU  477  N   LYS A  64      943   3521   2777    449    917     71  A    N  
ATOM    478  CA  LYS A  64       4.563  25.007  23.985  1.00 20.33      A    C  
ANISOU  478  CA  LYS A  64     1429   3393   2903     31    987    147  A    C  
ATOM    479  C   LYS A  64       3.780  24.632  25.242  1.00 20.33      A    C  
ANISOU  479  C   LYS A  64     1630   3192   2901     20   1120    175  A    C  
ATOM    480  O   LYS A  64       3.382  25.498  26.032  1.00 22.68      A    O  
ANISOU  480  O   LYS A  64     2185   3298   3136     52   1251    124  A    O  
ATOM    481  CB  LYS A  64       5.193  26.403  24.141  1.00 21.33      A    C  
ANISOU  481  CB  LYS A  64     1479   3470   3156   -126    992     87  A    C  
ATOM    482  CG  LYS A  64       6.323  26.480  25.168  1.00 24.80      A    C  
ANISOU  482  CG  LYS A  64     1967   3826   3630   -186    803   -186  A    C  
ATOM    483  CD  LYS A  64       6.808  27.906  25.352  1.00 28.42      A    C  
ANISOU  483  CD  LYS A  64     2335   4097   4368   -350    736   -307  A    C  
ATOM    484  CE  LYS A  64       7.377  28.511  24.061  1.00 31.73      A    C  
ANISOU  484  CE  LYS A  64     2847   4338   4870   -272    798   -284  A    C  
ATOM    485  NZ  LYS A  64       8.621  27.833  23.592  1.00 32.14      A    N1+
ANISOU  485  NZ  LYS A  64     2784   4314   5113   -339    768   -498  A    N1+
ATOM    486  N   TYR A  65       3.587  23.344  25.450  1.00 18.35      A    N  
ANISOU  486  N   TYR A  65     1061   3082   2829    -15   1000    247  A    N  
ATOM    487  CA  TYR A  65       2.849  22.870  26.617  1.00 17.78      A    C  
ANISOU  487  CA  TYR A  65     1034   3039   2682     68    939    192  A    C  
ATOM    488  C   TYR A  65       3.729  22.921  27.867  1.00 18.03      A    C  
ANISOU  488  C   TYR A  65     1042   3115   2694     12    988    137  A    C  
ATOM    489  O   TYR A  65       4.970  23.048  27.780  1.00 18.69      A    O  
ANISOU  489  O   TYR A  65      972   3282   2847    -40    872     82  A    O  
ATOM    490  CB  TYR A  65       2.283  21.452  26.367  1.00 17.17      A    C  
ANISOU  490  CB  TYR A  65      681   3027   2815     87    803    228  A    C  
ATOM    491  CG  TYR A  65       3.354  20.395  26.276  1.00 16.69      A    C  
ANISOU  491  CG  TYR A  65      723   3104   2515    181    627    175  A    C  
ATOM    492  CD1 TYR A  65       3.901  19.788  27.413  1.00 16.44      A    C  
ANISOU  492  CD1 TYR A  65      462   3395   2388    317    625    131  A    C  
ATOM    493  CD2 TYR A  65       3.848  20.001  25.039  1.00 15.81      A    C  
ANISOU  493  CD2 TYR A  65      377   3294   2337    186    493    194  A    C  
ATOM    494  CE1 TYR A  65       4.900  18.831  27.323  1.00 16.82      A    C  
ANISOU  494  CE1 TYR A  65      482   3583   2327    296    577     63  A    C  
ATOM    495  CE2 TYR A  65       4.845  19.041  24.940  1.00 15.58      A    C  
ANISOU  495  CE2 TYR A  65      308   3292   2318     96    333    131  A    C  
ATOM    496  CZ  TYR A  65       5.355  18.457  26.073  1.00 16.68      A    C  
ANISOU  496  CZ  TYR A  65      620   3443   2275    247    599    173  A    C  
ATOM    497  OH  TYR A  65       6.364  17.524  25.985  1.00 15.76      A    O  
ANISOU  497  OH  TYR A  65      329   3420   2240    229    236     17  A    O  
ATOM    498  N   THR A  66       3.095  22.781  29.025  1.00 18.93      A    N  
ANISOU  498  N   THR A  66     1421   3167   2606     68   1062    118  A    N  
ATOM    499  CA  THR A  66       3.788  22.629  30.289  1.00 19.73      A    C  
ANISOU  499  CA  THR A  66     1527   3282   2687    141   1180     82  A    C  
ATOM    500  C   THR A  66       3.369  21.325  30.965  1.00 18.67      A    C  
ANISOU  500  C   THR A  66     1322   3303   2469      5   1005    103  A    C  
ATOM    501  O   THR A  66       2.313  20.746  30.639  1.00 19.44      A    O  
ANISOU  501  O   THR A  66     1384   3434   2569   -102    952     57  A    O  
ATOM    502  CB  THR A  66       3.508  23.811  31.243  1.00 20.54      A    C  
ANISOU  502  CB  THR A  66     1720   3346   2739    109   1185     37  A    C  
ATOM    503  CG2 THR A  66       3.923  25.135  30.622  1.00 22.66      A    C  
ANISOU  503  CG2 THR A  66     2099   3373   3138    153   1456     35  A    C  
ATOM    504  OG1 THR A  66       2.105  23.854  31.531  1.00 23.21      A    O  
ANISOU  504  OG1 THR A  66     2017   3585   3215    377   1420     31  A    O  
ATOM    505  N   LEU A  67       4.212  20.864  31.881  1.00 18.09      A    N  
ANISOU  505  N   LEU A  67     1351   3240   2284     81    850    -13  A    N  
ATOM    506  CA  LEU A  67       3.894  19.777  32.794  1.00 17.24      A    C  
ANISOU  506  CA  LEU A  67     1098   3188   2266     65    631   -197  A    C  
ATOM    507  C   LEU A  67       4.128  20.305  34.208  1.00 17.92      A    C  
ANISOU  507  C   LEU A  67     1305   3237   2266     63    658   -197  A    C  
ATOM    508  O   LEU A  67       5.129  19.968  34.852  1.00 19.03      A    O  
ANISOU  508  O   LEU A  67     1263   3630   2336    -43    590   -258  A    O  
ATOM    509  CB  LEU A  67       4.787  18.558  32.509  1.00 17.21      A    C  
ANISOU  509  CB  LEU A  67     1150   3203   2187    120    584   -252  A    C  
ATOM    510  CG  LEU A  67       4.658  17.945  31.111  1.00 17.52      A    C  
ANISOU  510  CG  LEU A  67      935   3348   2374     35    438   -294  A    C  
ATOM    511  CD1 LEU A  67       5.829  17.004  30.836  1.00 19.69      A    C  
ANISOU  511  CD1 LEU A  67     1342   3463   2675    357    438   -388  A    C  
ATOM    512  CD2 LEU A  67       3.318  17.227  30.924  1.00 20.43      A    C  
ANISOU  512  CD2 LEU A  67     1331   3495   2937   -109    186   -318  A    C  
ATOM    513  N   PRO A  68       3.201  21.148  34.688  1.00 18.93      A    N  
ANISOU  513  N   PRO A  68     1342   3357   2495     49    838   -271  A    N  
ATOM    514  CA  PRO A  68       3.458  21.994  35.860  1.00 19.50      A    C  
ANISOU  514  CA  PRO A  68     1418   3294   2698   -103    934   -296  A    C  
ATOM    515  C   PRO A  68       3.580  21.232  37.172  1.00 19.79      A    C  
ANISOU  515  C   PRO A  68     1392   3499   2628   -230    942   -315  A    C  
ATOM    516  O   PRO A  68       4.112  21.788  38.147  1.00 21.01      A    O  
ANISOU  516  O   PRO A  68     1428   3716   2840   -342    776   -333  A    O  
ATOM    517  CB  PRO A  68       2.237  22.924  35.907  1.00 20.58      A    C  
ANISOU  517  CB  PRO A  68     1523   3388   2908    -30   1018   -401  A    C  
ATOM    518  CG  PRO A  68       1.151  22.127  35.259  1.00 20.13      A    C  
ANISOU  518  CG  PRO A  68     1525   3495   2628     -6    926   -313  A    C  
ATOM    519  CD  PRO A  68       1.834  21.345  34.167  1.00 19.31      A    C  
ANISOU  519  CD  PRO A  68     1287   3474   2576     70    895   -219  A    C  
ATOM    520  N   ASN A  69       3.110  19.987  37.194  1.00 18.75      A    N  
ANISOU  520  N   ASN A  69     1052   3481   2592   -197    876    -63  A    N  
ATOM    521  CA  ASN A  69       3.225  19.168  38.403  1.00 19.53      A    C  
ANISOU  521  CA  ASN A  69     1186   3655   2581   -183    741     76  A    C  
ATOM    522  C   ASN A  69       4.465  18.281  38.421  1.00 19.72      A    C  
ANISOU  522  C   ASN A  69     1272   3621   2599   -185    634    104  A    C  
ATOM    523  O   ASN A  69       4.653  17.484  39.327  1.00 21.60      A    O  
ANISOU  523  O   ASN A  69     1659   3865   2682   -140    619    219  A    O  
ATOM    524  CB  ASN A  69       1.940  18.360  38.556  1.00 19.24      A    C  
ANISOU  524  CB  ASN A  69     1076   3562   2671   -120    842    153  A    C  
ATOM    525  CG  ASN A  69       0.724  19.271  38.472  1.00 19.35      A    C  
ANISOU  525  CG  ASN A  69     1115   3601   2635    -62    793     68  A    C  
ATOM    526  ND2 ASN A  69      -0.148  19.023  37.496  1.00 20.12      A    N  
ANISOU  526  ND2 ASN A  69      734   3711   3201    -71    652   -218  A    N  
ATOM    527  OD1 ASN A  69       0.606  20.199  39.262  1.00 20.67      A    O  
ANISOU  527  OD1 ASN A  69     1168   4077   2610     35    665   -119  A    O  
ATOM    528  N   SER A  70       5.340  18.456  37.431  1.00 19.56      A    N  
ANISOU  528  N   SER A  70     1106   3734   2592   -230    403   -160  A    N  
ATOM    529  CA  SER A  70       6.534  17.640  37.251  1.00 19.89      A    C  
ANISOU  529  CA  SER A  70     1036   3840   2682   -274    237   -410  A    C  
ATOM    530  C   SER A  70       7.772  18.520  37.305  1.00 20.04      A    C  
ANISOU  530  C   SER A  70     1036   3986   2594   -263      6   -467  A    C  
ATOM    531  O   SER A  70       7.683  19.712  37.021  1.00 21.05      A    O  
ANISOU  531  O   SER A  70     1069   3858   3070   -386    219   -463  A    O  
ATOM    532  CB  SER A  70       6.454  17.000  35.874  1.00 20.59      A    C  
ANISOU  532  CB  SER A  70     1186   3810   2829   -130     -6   -595  A    C  
ATOM    533  OG  SER A  70       7.605  16.285  35.544  1.00 23.24      A    O  
ANISOU  533  OG  SER A  70     1421   4413   2996   -252    307   -675  A    O  
ATOM    534  N   ASN A  71       8.918  17.931  37.632  1.00 19.97      A    N  
ANISOU  534  N   ASN A  71      921   4453   2213   -170    -51   -560  A    N  
ATOM    535  CA  ASN A  71      10.172  18.683  37.614  1.00 20.71      A    C  
ANISOU  535  CA  ASN A  71     1054   4805   2011     -3   -120   -579  A    C  
ATOM    536  C   ASN A  71      10.912  18.495  36.294  1.00 19.30      A    C  
ANISOU  536  C   ASN A  71     1097   4352   1884    -38      0   -582  A    C  
ATOM    537  O   ASN A  71      12.077  18.860  36.186  1.00 19.63      A    O  
ANISOU  537  O   ASN A  71      945   4557   1958    -57    -20   -634  A    O  
ATOM    538  CB  ASN A  71      11.065  18.313  38.808  1.00 23.16      A    C  
ANISOU  538  CB  ASN A  71     1368   5307   2124    -10   -170   -386  A    C  
ATOM    539  CG  ASN A  71      11.522  16.853  38.787  1.00 28.00      A    C  
ANISOU  539  CG  ASN A  71     2020   6211   2407    658   -392   -185  A    C  
ATOM    540  ND2 ASN A  71      12.188  16.439  39.861  1.00 34.74      A    N  
ANISOU  540  ND2 ASN A  71     3160   7171   2870   1027   -652     80  A    N  
ATOM    541  OD1 ASN A  71      11.282  16.106  37.835  1.00 31.09      A    O  
ANISOU  541  OD1 ASN A  71     2533   6521   2757    903   -581    -26  A    O  
ATOM    542  N   ILE A  72      10.237  17.948  35.287  1.00 18.58      A    N  
ANISOU  542  N   ILE A  72     1162   4117   1779   -109    208   -631  A    N  
ATOM    543  CA  ILE A  72      10.858  17.738  33.971  1.00 18.45      A    C  
ANISOU  543  CA  ILE A  72     1186   3986   1840   -208    263   -604  A    C  
ATOM    544  C   ILE A  72      11.157  19.082  33.313  1.00 18.09      A    C  
ANISOU  544  C   ILE A  72     1000   3984   1888   -173    370   -640  A    C  
ATOM    545  O   ILE A  72      10.345  20.009  33.408  1.00 18.64      A    O  
ANISOU  545  O   ILE A  72      918   3925   2239   -250    412   -627  A    O  
ATOM    546  CB  ILE A  72       9.946  16.887  33.045  1.00 18.39      A    C  
ANISOU  546  CB  ILE A  72     1221   3887   1878   -153    216   -590  A    C  
ATOM    547  CG1 ILE A  72       9.886  15.440  33.545  1.00 19.83      A    C  
ANISOU  547  CG1 ILE A  72     1474   3921   2140   -252    241   -474  A    C  
ATOM    548  CG2 ILE A  72      10.395  16.977  31.586  1.00 19.49      A    C  
ANISOU  548  CG2 ILE A  72     1315   4266   1826   -370    250   -553  A    C  
ATOM    549  CD1 ILE A  72       8.786  14.599  32.902  1.00 20.79      A    C  
ANISOU  549  CD1 ILE A  72     1588   3790   2520   -229     27   -335  A    C  
ATOM    550  N   ASN A  73      12.334  19.197  32.684  1.00 18.03      A    N  
ANISOU  550  N   ASN A  73      798   4140   1914   -184    285   -606  A    N  
ATOM    551  CA  ASN A  73      12.642  20.377  31.885  1.00 18.87      A    C  
ANISOU  551  CA  ASN A  73      961   4047   2161   -230    250   -595  A    C  
ATOM    552  C   ASN A  73      12.234  20.088  30.456  1.00 17.25      A    C  
ANISOU  552  C   ASN A  73     1080   3395   2081    -93    238   -516  A    C  
ATOM    553  O   ASN A  73      12.747  19.141  29.855  1.00 16.70      A    O  
ANISOU  553  O   ASN A  73      890   3341   2116    -38    119   -533  A    O  
ATOM    554  CB  ASN A  73      14.135  20.705  31.938  1.00 20.97      A    C  
ANISOU  554  CB  ASN A  73     1025   4481   2460   -487    241   -648  A    C  
ATOM    555  CG  ASN A  73      14.515  22.007  31.235  1.00 27.48      A    C  
ANISOU  555  CG  ASN A  73     1764   5284   3395   -991      0   -362  A    C  
ATOM    556  ND2 ASN A  73      15.531  22.680  31.771  1.00 34.28      A    N  
ANISOU  556  ND2 ASN A  73     2603   5866   4557  -1357   -197   -282  A    N  
ATOM    557  OD1 ASN A  73      13.932  22.404  30.227  1.00 33.59      A    O  
ANISOU  557  OD1 ASN A  73     2476   6118   4169  -1377    -10    -62  A    O  
ATOM    558  N   ILE A  74      11.289  20.891  29.946  1.00 16.39      A    N  
ANISOU  558  N   ILE A  74      986   3176   2064     52    381   -390  A    N  
ATOM    559  CA  ILE A  74      10.748  20.698  28.598  1.00 16.22      A    C  
ANISOU  559  CA  ILE A  74      830   3097   2237     48    460   -359  A    C  
ATOM    560  C   ILE A  74      11.443  21.684  27.647  1.00 15.84      A    C  
ANISOU  560  C   ILE A  74      938   2980   2099     -5    439   -445  A    C  
ATOM    561  O   ILE A  74      11.278  22.905  27.773  1.00 17.92      A    O  
ANISOU  561  O   ILE A  74     1288   3018   2504    -24    644   -458  A    O  
ATOM    562  CB  ILE A  74       9.212  20.889  28.528  1.00 16.35      A    C  
ANISOU  562  CB  ILE A  74      761   3106   2345    103    518   -403  A    C  
ATOM    563  CG1 ILE A  74       8.504  20.010  29.556  1.00 19.34      A    C  
ANISOU  563  CG1 ILE A  74     1102   3515   2732    107    520   -252  A    C  
ATOM    564  CG2 ILE A  74       8.705  20.596  27.116  1.00 17.44      A    C  
ANISOU  564  CG2 ILE A  74      786   3231   2608    -41    296   -296  A    C  
ATOM    565  CD1 ILE A  74       7.134  20.499  29.937  1.00 20.62      A    C  
ANISOU  565  CD1 ILE A  74      805   3980   3048     65    571   -489  A    C  
ATOM    566  N   ILE A  75      12.226  21.138  26.724  1.00 15.47      A    N  
ANISOU  566  N   ILE A  75      761   3088   2029   -120    307   -419  A    N  
ATOM    567  CA  ILE A  75      12.890  21.944  25.714  1.00 16.32      A    C  
ANISOU  567  CA  ILE A  75      636   3404   2161   -225    208   -284  A    C  
ATOM    568  C   ILE A  75      12.022  21.974  24.468  1.00 15.17      A    C  
ANISOU  568  C   ILE A  75      474   3106   2184   -195    272   -208  A    C  
ATOM    569  O   ILE A  75      11.664  20.929  23.926  1.00 15.96      A    O  
ANISOU  569  O   ILE A  75      505   3199   2361   -147     98   -252  A    O  
ATOM    570  CB  ILE A  75      14.263  21.359  25.362  1.00 17.27      A    C  
ANISOU  570  CB  ILE A  75      588   3688   2284   -227    217   -216  A    C  
ATOM    571  CG1 ILE A  75      15.135  21.280  26.617  1.00 21.44      A    C  
ANISOU  571  CG1 ILE A  75     1316   4140   2689   -432   -130   -248  A    C  
ATOM    572  CG2 ILE A  75      14.939  22.197  24.279  1.00 18.95      A    C  
ANISOU  572  CG2 ILE A  75      780   4023   2398   -366    326   -164  A    C  
ATOM    573  CD1 ILE A  75      16.016  20.067  26.649  1.00 28.66      A    C  
ANISOU  573  CD1 ILE A  75     2682   4753   3454   -719   -307   -230  A    C  
ATOM    574  N   HIS A  76      11.676  23.178  24.029  1.00 15.63      A    N  
ANISOU  574  N   HIS A  76      514   3106   2319   -159    318   -120  A    N  
ATOM    575  CA  HIS A  76      10.763  23.335  22.910  1.00 15.70      A    C  
ANISOU  575  CA  HIS A  76      549   3046   2370     17    474    -68  A    C  
ATOM    576  C   HIS A  76      11.518  23.741  21.653  1.00 15.26      A    C  
ANISOU  576  C   HIS A  76      443   2921   2435     10    474    -98  A    C  
ATOM    577  O   HIS A  76      12.110  24.825  21.595  1.00 16.59      A    O  
ANISOU  577  O   HIS A  76      691   2926   2685   -193    500    -46  A    O  
ATOM    578  CB  HIS A  76       9.696  24.374  23.237  1.00 15.76      A    C  
ANISOU  578  CB  HIS A  76      357   3138   2492      3    480   -173  A    C  
ATOM    579  CG  HIS A  76       8.581  24.421  22.242  1.00 16.39      A    C  
ANISOU  579  CG  HIS A  76      500   3222   2506     74    476    -81  A    C  
ATOM    580  CD2 HIS A  76       8.119  23.487  21.377  1.00 16.39      A    C  
ANISOU  580  CD2 HIS A  76      406   3291   2529     85    397    -13  A    C  
ATOM    581  ND1 HIS A  76       7.802  25.542  22.048  1.00 17.73      A    N  
ANISOU  581  ND1 HIS A  76      741   3321   2675    151    588     -3  A    N  
ATOM    582  CE1 HIS A  76       6.896  25.292  21.119  1.00 17.83      A    C  
ANISOU  582  CE1 HIS A  76      744   3413   2617    474    408     31  A    C  
ATOM    583  NE2 HIS A  76       7.059  24.049  20.703  1.00 17.25      A    N  
ANISOU  583  NE2 HIS A  76      535   3312   2707    346    392     82  A    N  
ATOM    584  N   ILE A  77      11.493  22.863  20.655  1.00 14.82      A    N  
ANISOU  584  N   ILE A  77      359   2980   2293     49    460    -81  A    N  
ATOM    585  CA  ILE A  77      11.993  23.202  19.323  1.00 16.72      A    C  
ANISOU  585  CA  ILE A  77      802   3091   2458    183    570   -118  A    C  
ATOM    586  C   ILE A  77      10.830  23.020  18.348  1.00 15.59      A    C  
ANISOU  586  C   ILE A  77      834   2754   2335    152    597    -43  A    C  
ATOM    587  O   ILE A  77      10.599  21.919  17.855  1.00 15.56      A    O  
ANISOU  587  O   ILE A  77      697   2732   2484    114    603     24  A    O  
ATOM    588  CB  ILE A  77      13.187  22.317  18.901  1.00 18.44      A    C  
ANISOU  588  CB  ILE A  77     1005   3370   2632    239    538   -125  A    C  
ATOM    589  CG1 ILE A  77      14.331  22.416  19.921  1.00 21.16      A    C  
ANISOU  589  CG1 ILE A  77      878   4097   3064    627    546   -324  A    C  
ATOM    590  CG2 ILE A  77      13.669  22.724  17.520  1.00 20.81      A    C  
ANISOU  590  CG2 ILE A  77     1226   3828   2851    204    776   -263  A    C  
ATOM    591  CD1 ILE A  77      15.527  21.532  19.603  1.00 24.35      A    C  
ANISOU  591  CD1 ILE A  77     1103   4535   3614    798    630   -317  A    C  
ATOM    592  N   PRO A  78      10.082  24.097  18.092  1.00 16.61      A    N  
ANISOU  592  N   PRO A  78      846   2809   2655    197    498   -129  A    N  
ATOM    593  CA  PRO A  78       8.858  23.954  17.294  1.00 17.29      A    C  
ANISOU  593  CA  PRO A  78      980   2969   2619    241    412   -230  A    C  
ATOM    594  C   PRO A  78       9.158  23.680  15.827  1.00 17.59      A    C  
ANISOU  594  C   PRO A  78     1018   3068   2599    252    454   -208  A    C  
ATOM    595  O   PRO A  78       9.865  24.470  15.185  1.00 19.28      A    O  
ANISOU  595  O   PRO A  78     1412   3188   2725     49    494    -76  A    O  
ATOM    596  CB  PRO A  78       8.152  25.297  17.468  1.00 17.97      A    C  
ANISOU  596  CB  PRO A  78     1084   2991   2754    252    392   -247  A    C  
ATOM    597  CG  PRO A  78       9.180  26.247  17.960  1.00 17.19      A    C  
ANISOU  597  CG  PRO A  78      842   2860   2831    270    405   -181  A    C  
ATOM    598  CD  PRO A  78      10.226  25.437  18.670  1.00 17.06      A    C  
ANISOU  598  CD  PRO A  78      922   2791   2768    175    458    -93  A    C  
ATOM    599  N   LEU A  79       8.650  22.554  15.332  1.00 15.63      A    N  
ANISOU  599  N   LEU A  79      368   3242   2328    329    348   -205  A    N  
ATOM    600  CA  LEU A  79       8.786  22.173  13.933  1.00 16.17      A    C  
ANISOU  600  CA  LEU A  79      359   3440   2345    452    208   -152  A    C  
ATOM    601  C   LEU A  79       7.425  21.774  13.397  1.00 15.33      A    C  
ANISOU  601  C   LEU A  79      370   3398   2056    472    266   -114  A    C  
ATOM    602  O   LEU A  79       6.560  21.348  14.157  1.00 16.02      A    O  
ANISOU  602  O   LEU A  79      326   3720   2039    432    195     97  A    O  
ATOM    603  CB  LEU A  79       9.734  20.984  13.794  1.00 16.49      A    C  
ANISOU  603  CB  LEU A  79      355   3384   2527    410    131   -160  A    C  
ATOM    604  CG  LEU A  79      11.161  21.187  14.290  1.00 18.33      A    C  
ANISOU  604  CG  LEU A  79      322   3797   2845    419    228     57  A    C  
ATOM    605  CD1 LEU A  79      11.847  19.837  14.402  1.00 19.45      A    C  
ANISOU  605  CD1 LEU A  79      293   3851   3246    320    207    296  A    C  
ATOM    606  CD2 LEU A  79      11.901  22.100  13.329  1.00 21.85      A    C  
ANISOU  606  CD2 LEU A  79      893   3914   3495    230    348    249  A    C  
ATOM    607  N   VAL A  80       7.263  21.904  12.085  1.00 15.82      A    N  
ANISOU  607  N   VAL A  80      395   3596   2018    383    219    -63  A    N  
ATOM    608  CA  VAL A  80       6.085  21.383  11.388  1.00 16.27      A    C  
ANISOU  608  CA  VAL A  80      518   3574   2090    511    109    -38  A    C  
ATOM    609  C   VAL A  80       6.434  20.090  10.640  1.00 15.97      A    C  
ANISOU  609  C   VAL A  80      392   3560   2116    535     74    -12  A    C  
ATOM    610  O   VAL A  80       7.499  19.969  10.028  1.00 17.00      A    O  
ANISOU  610  O   VAL A  80      436   3759   2265    573    196    -63  A    O  
ATOM    611  CB  VAL A  80       5.481  22.418  10.409  1.00 17.46      A    C  
ANISOU  611  CB  VAL A  80      821   3564   2249    524     31     -3  A    C  
ATOM    612  CG1 VAL A  80       4.240  21.846   9.737  1.00 19.03      A    C  
ANISOU  612  CG1 VAL A  80      766   3907   2558    584   -120      5  A    C  
ATOM    613  CG2 VAL A  80       5.111  23.710  11.135  1.00 19.43      A    C  
ANISOU  613  CG2 VAL A  80     1280   3583   2520    581    186     12  A    C  
ATOM    614  N   ASP A  81       5.539  19.107  10.674  1.00 15.65      A    N  
ANISOU  614  N   ASP A  81      331   3630   1985    509     31     -5  A    N  
ATOM    615  CA  ASP A  81       5.693  17.888   9.883  1.00 15.85      A    C  
ANISOU  615  CA  ASP A  81      443   3763   1817    571     54     43  A    C  
ATOM    616  C   ASP A  81       5.130  18.142   8.492  1.00 17.12      A    C  
ANISOU  616  C   ASP A  81      571   4142   1791    798     73     65  A    C  
ATOM    617  O   ASP A  81       3.948  17.885   8.230  1.00 18.48      A    O  
ANISOU  617  O   ASP A  81      434   4481   2108    863    -68     98  A    O  
ATOM    618  CB  ASP A  81       5.002  16.702  10.554  1.00 15.96      A    C  
ANISOU  618  CB  ASP A  81      331   3689   2043    516     24     41  A    C  
ATOM    619  CG  ASP A  81       5.144  15.409   9.770  1.00 15.78      A    C  
ANISOU  619  CG  ASP A  81      309   3765   1921    443    -24     41  A    C  
ATOM    620  OD1 ASP A  81       6.001  15.325   8.835  1.00 17.87      A    O  
ANISOU  620  OD1 ASP A  81      557   4205   2027    551    274    -31  A    O  
ATOM    621  OD2 ASP A  81       4.441  14.435  10.120  1.00 17.70      A    O1-
ANISOU  621  OD2 ASP A  81      308   3772   2646    421    105      0  A    O1-
ATOM    622  N   ASP A  82       5.949  18.697   7.611  1.00 18.82      A    N  
ANISOU  622  N   ASP A  82      930   4431   1788   1164    129    159  A    N  
ATOM    623  CA  ASP A  82       5.527  18.915   6.236  1.00 22.20      A    C  
ANISOU  623  CA  ASP A  82     1356   5156   1923   1824    241    373  A    C  
ATOM    624  C   ASP A  82       6.715  18.741   5.312  1.00 23.91      A    C  
ANISOU  624  C   ASP A  82     1570   5697   1817   2011    252    487  A    C  
ATOM    625  O   ASP A  82       7.840  18.548   5.771  1.00 22.05      A    O  
ANISOU  625  O   ASP A  82     1212   5281   1885   1629     91    368  A    O  
ATOM    626  CB  ASP A  82       4.906  20.304   6.064  1.00 24.70      A    C  
ANISOU  626  CB  ASP A  82     1914   5144   2328   1905    285    469  A    C  
ATOM    627  CG  ASP A  82       5.907  21.423   6.272  1.00 28.61      A    C  
ANISOU  627  CG  ASP A  82     2433   5120   3316   2046    529    612  A    C  
ATOM    628  OD1 ASP A  82       7.116  21.187   6.077  1.00 32.19      A    O  
ANISOU  628  OD1 ASP A  82     2772   5008   4449   1985    930    815  A    O  
ATOM    629  OD2 ASP A  82       5.484  22.542   6.630  1.00 32.66      A    O1-
ANISOU  629  OD2 ASP A  82     2813   5310   4286   2081    842    724  A    O1-
ATOM    630  N   THR A  83       6.470  18.787   4.010  1.00 28.33      A    N  
ANISOU  630  N   THR A  83     1967   7041   1756   2388    252    540  A    N  
ATOM    631  CA  THR A  83       7.529  18.440   3.066  1.00 32.64      A    C  
ANISOU  631  CA  THR A  83     2610   7911   1879   2691    417    617  A    C  
ATOM    632  C   THR A  83       8.364  19.672   2.674  1.00 33.91      A    C  
ANISOU  632  C   THR A  83     2694   8093   2097   2930    520    908  A    C  
ATOM    633  O   THR A  83       9.265  19.568   1.836  1.00 34.76      A    O  
ANISOU  633  O   THR A  83     2554   8403   2249   3064    617    986  A    O  
ATOM    634  CB  THR A  83       6.991  17.650   1.846  1.00 33.50      A    C  
ANISOU  634  CB  THR A  83     2775   8011   1941   2709    296    502  A    C  
ATOM    635  CG2 THR A  83       6.532  16.253   2.278  1.00 35.03      A    C  
ANISOU  635  CG2 THR A  83     3152   8008   2149   2748    337    386  A    C  
ATOM    636  OG1 THR A  83       5.870  18.328   1.284  1.00 34.07      A    O  
ANISOU  636  OG1 THR A  83     2894   7997   2055   2608    285    456  A    O  
ATOM    637  N   THR A  84       8.108  20.804   3.339  1.00 36.15      A    N  
ANISOU  637  N   THR A  84     3251   7713   2772   3237    850   1280  A    N  
ATOM    638  CA  THR A  84       8.807  22.071   3.073  1.00 38.29      A    C  
ANISOU  638  CA  THR A  84     3943   7135   3472   3337   1168   1551  A    C  
ATOM    639  C   THR A  84       9.799  22.536   4.169  1.00 36.95      A    C  
ANISOU  639  C   THR A  84     3847   6420   3772   3000   1448   1578  A    C  
ATOM    640  O   THR A  84      10.773  23.229   3.871  1.00 38.69      A    O  
ANISOU  640  O   THR A  84     4122   6402   4176   2937   1553   1805  A    O  
ATOM    641  CB  THR A  84       7.802  23.206   2.702  1.00 39.78      A    C  
ANISOU  641  CB  THR A  84     4194   7322   3598   3452   1133   1597  A    C  
ATOM    642  CG2 THR A  84       7.408  24.039   3.927  1.00 39.99      A    C  
ANISOU  642  CG2 THR A  84     4259   7206   3731   3646    930   1518  A    C  
ATOM    643  OG1 THR A  84       8.376  24.055   1.699  1.00 41.75      A    O  
ANISOU  643  OG1 THR A  84     4629   7336   3898   3330   1023   1624  A    O  
ATOM    644  N   THR A  85       9.582  22.110   5.411  1.00 33.95      A    N  
ANISOU  644  N   THR A  85     3583   5618   3700   2583   1462   1230  A    N  
ATOM    645  CA  THR A  85      10.409  22.547   6.541  1.00 30.96      A    C  
ANISOU  645  CA  THR A  85     3253   4884   3625   1967   1456    811  A    C  
ATOM    646  C   THR A  85      11.836  21.992   6.512  1.00 27.45      A    C  
ANISOU  646  C   THR A  85     3097   4004   3330   1553   1401    570  A    C  
ATOM    647  O   THR A  85      12.042  20.815   6.228  1.00 26.52      A    O  
ANISOU  647  O   THR A  85     2989   3819   3269   1473   1368    586  A    O  
ATOM    648  CB  THR A  85       9.769  22.156   7.889  1.00 32.57      A    C  
ANISOU  648  CB  THR A  85     3337   5464   3576   2108   1490    780  A    C  
ATOM    649  CG2 THR A  85      10.799  22.206   9.009  1.00 33.37      A    C  
ANISOU  649  CG2 THR A  85     3307   5539   3833   1958   1532    789  A    C  
ATOM    650  OG1 THR A  85       8.697  23.056   8.191  1.00 34.81      A    O  
ANISOU  650  OG1 THR A  85     3576   5727   3925   2117   1395    701  A    O  
ATOM    651  N  AASP A  86      12.783  22.838   6.500  0.50 26.21      A    N  
ANISOU  651  N  AASP A  86     3125   3614   3219   1324   1230    526  A    N  
ATOM    652  N  BASP A  86      12.812  22.844   6.827  0.50 26.36      A    N  
ANISOU  652  N  BASP A  86     3140   3580   3294   1254   1411    485  A    N  
ATOM    653  CA AASP A  86      14.099  22.434   6.969  0.50 24.01      A    C  
ANISOU  653  CA AASP A  86     2858   3264   3000   1026   1168    474  A    C  
ATOM    654  CA BASP A  86      14.211  22.424   6.927  0.50 24.42      A    C  
ANISOU  654  CA BASP A  86     3034   3143   3102    864   1303    460  A    C  
ATOM    655  C  AASP A  86      14.021  21.979   8.419  0.50 21.54      A    C  
ANISOU  655  C  AASP A  86     2405   3082   2696    719    838    274  A    C  
ATOM    656  C  BASP A  86      14.615  22.031   8.345  0.50 22.57      A    C  
ANISOU  656  C  BASP A  86     2694   3041   2842    476   1026    241  A    C  
ATOM    657  O  AASP A  86      13.553  22.715   9.288  0.50 19.63      A    O  
ANISOU  657  O  AASP A  86     1693   3023   2743    700    785    296  A    O  
ATOM    658  O  BASP A  86      15.071  22.866   9.127  0.50 22.27      A    O  
ANISOU  658  O  BASP A  86     2560   2975   2926    153   1062    230  A    O  
ATOM    659  CB AASP A  86      15.106  23.575   6.822  0.50 25.56      A    C  
ANISOU  659  CB AASP A  86     3161   3366   3185   1076   1386    489  A    C  
ATOM    660  CB BASP A  86      15.152  23.521   6.427  0.50 25.52      A    C  
ANISOU  660  CB BASP A  86     3264   3143   3289    952   1500    540  A    C  
ATOM    661  CG AASP A  86      16.498  23.182   7.267  0.50 27.04      A    C  
ANISOU  661  CG AASP A  86     3316   3528   3429    939   1518    597  A    C  
ATOM    662  CG BASP A  86      16.612  23.218   6.730  0.50 25.97      A    C  
ANISOU  662  CG BASP A  86     3472   2842   3555    847   1430    768  A    C  
ATOM    663  OD1AASP A  86      17.026  23.821   8.198  0.50 29.52      A    O  
ANISOU  663  OD1AASP A  86     3576   4056   3585    829   1676    579  A    O  
ATOM    664  OD2AASP A  86      17.061  22.229   6.691  0.50 29.27      A    O1-
ANISOU  664  OD2AASP A  86     3431   3984   3707   1098   1553    533  A    O1-
ATOM    665  OD1BASP A  86      16.981  22.027   6.745  0.50 27.24      A    O  
ANISOU  665  OD1BASP A  86     3576   2888   3885    762   1656    847  A    O  
ATOM    666  OD2BASP A  86      17.392  24.168   6.950  0.50 26.62      A    O1-
ANISOU  666  OD2BASP A  86     3562   2833   3720    684   1518    855  A    O1-
ATOM    667  N   ILE A  87      14.467  20.754   8.667  1.00 18.79      A    N  
ANISOU  667  N   ILE A  87     1720   3000   2421    373    533    153  A    N  
ATOM    668  CA  ILE A  87      14.739  20.281  10.026  1.00 17.74      A    C  
ANISOU  668  CA  ILE A  87     1166   3228   2347    -12    131     43  A    C  
ATOM    669  C   ILE A  87      16.247  20.152  10.237  1.00 16.48      A    C  
ANISOU  669  C   ILE A  87      900   3176   2187    -35    192   -147  A    C  
ATOM    670  O   ILE A  87      16.716  20.108  11.374  1.00 16.21      A    O  
ANISOU  670  O   ILE A  87      719   3226   2213   -208     80   -184  A    O  
ATOM    671  CB  ILE A  87      14.003  18.962  10.338  1.00 18.11      A    C  
ANISOU  671  CB  ILE A  87     1150   3361   2370   -135   -142    175  A    C  
ATOM    672  CG1 ILE A  87      14.447  17.827   9.405  1.00 18.88      A    C  
ANISOU  672  CG1 ILE A  87     1230   3289   2655   -269   -522    318  A    C  
ATOM    673  CG2 ILE A  87      12.491  19.197  10.325  1.00 20.90      A    C  
ANISOU  673  CG2 ILE A  87     1321   3786   2833   -196   -164    148  A    C  
ATOM    674  CD1 ILE A  87      14.136  16.452   9.960  1.00 22.96      A    C  
ANISOU  674  CD1 ILE A  87     1967   3598   3160   -482   -785    553  A    C  
ATOM    675  N   SER A  88      17.000  20.104   9.135  1.00 17.09      A    N  
ANISOU  675  N   SER A  88      891   3251   2352    -76    318   -294  A    N  
ATOM    676  CA  SER A  88      18.441  19.878   9.226  1.00 18.12      A    C  
ANISOU  676  CA  SER A  88      973   3388   2524   -102    478   -388  A    C  
ATOM    677  C   SER A  88      19.154  21.004   9.972  1.00 17.58      A    C  
ANISOU  677  C   SER A  88      988   3192   2500   -142    414   -252  A    C  
ATOM    678  O   SER A  88      20.217  20.756  10.538  1.00 17.77      A    O  
ANISOU  678  O   SER A  88      833   3409   2511    -80    441   -270  A    O  
ATOM    679  CB  SER A  88      19.043  19.685   7.830  1.00 18.83      A    C  
ANISOU  679  CB  SER A  88      986   3535   2633    -20    494   -408  A    C  
ATOM    680  OG  SER A  88      19.201  20.918   7.159  1.00 23.03      A    O  
ANISOU  680  OG  SER A  88     1824   3939   2987     17    899   -329  A    O  
ATOM    681  N   LYS A  89      18.577  22.211  10.002  1.00 17.93      A    N  
ANISOU  681  N   LYS A  89     1104   3055   2655   -136    357   -147  A    N  
ATOM    682  CA  LYS A  89      19.216  23.331  10.719  1.00 19.03      A    C  
ANISOU  682  CA  LYS A  89     1518   2978   2736   -164    263    -46  A    C  
ATOM    683  C   LYS A  89      19.460  23.020  12.200  1.00 17.34      A    C  
ANISOU  683  C   LYS A  89     1092   2867   2628   -260    344    -87  A    C  
ATOM    684  O   LYS A  89      20.329  23.640  12.827  1.00 18.54      A    O  
ANISOU  684  O   LYS A  89     1194   3097   2752   -522    417    -97  A    O  
ATOM    685  CB  LYS A  89      18.421  24.643  10.570  1.00 20.47      A    C  
ANISOU  685  CB  LYS A  89     1850   3084   2845      6    124    -74  A    C  
ATOM    686  CG  LYS A  89      17.061  24.659  11.240  1.00 25.29      A    C  
ANISOU  686  CG  LYS A  89     2542   3919   3147    447    -13   -285  A    C  
ATOM    687  CD  LYS A  89      16.360  26.017  11.138  1.00 32.49      A    C  
ANISOU  687  CD  LYS A  89     3542   5194   3607   1357   -152   -241  A    C  
ATOM    688  CE  LYS A  89      15.317  26.050  10.037  1.00 36.94      A    C  
ANISOU  688  CE  LYS A  89     4210   6003   3824   1720   -125   -326  A    C  
ATOM    689  NZ  LYS A  89      15.813  26.660   8.765  1.00 38.74      A    N1+
ANISOU  689  NZ  LYS A  89     4350   6621   3747   1964     76   -285  A    N1+
ATOM    690  N   TYR A  90      18.706  22.074  12.759  1.00 16.07      A    N  
ANISOU  690  N   TYR A  90      629   2949   2529   -322    324   -104  A    N  
ATOM    691  CA  TYR A  90      18.829  21.728  14.176  1.00 15.20      A    C  
ANISOU  691  CA  TYR A  90      346   2951   2477   -328    372   -263  A    C  
ATOM    692  C   TYR A  90      19.570  20.429  14.448  1.00 14.36      A    C  
ANISOU  692  C   TYR A  90      318   2928   2210   -344    239   -329  A    C  
ATOM    693  O   TYR A  90      19.777  20.088  15.608  1.00 15.13      A    O  
ANISOU  693  O   TYR A  90      350   3203   2196   -240    206   -271  A    O  
ATOM    694  CB  TYR A  90      17.428  21.612  14.808  1.00 16.74      A    C  
ANISOU  694  CB  TYR A  90      410   3176   2773   -342    526   -285  A    C  
ATOM    695  CG  TYR A  90      16.603  22.867  14.683  1.00 20.77      A    C  
ANISOU  695  CG  TYR A  90      858   3400   3634   -142    832   -186  A    C  
ATOM    696  CD1 TYR A  90      16.870  23.985  15.465  1.00 26.44      A    C  
ANISOU  696  CD1 TYR A  90     2117   3750   4178    386    930   -361  A    C  
ATOM    697  CD2 TYR A  90      15.531  22.934  13.783  1.00 24.91      A    C  
ANISOU  697  CD2 TYR A  90     1149   3734   4582    175    922     76  A    C  
ATOM    698  CE1 TYR A  90      16.095  25.148  15.356  1.00 29.65      A    C  
ANISOU  698  CE1 TYR A  90     2484   3966   4816    612   1203   -272  A    C  
ATOM    699  CE2 TYR A  90      14.758  24.087  13.666  1.00 27.88      A    C  
ANISOU  699  CE2 TYR A  90     1392   3905   5296    185   1115    282  A    C  
ATOM    700  CZ  TYR A  90      15.038  25.184  14.458  1.00 29.45      A    C  
ANISOU  700  CZ  TYR A  90     1835   4029   5324    560   1500    -12  A    C  
ATOM    701  OH  TYR A  90      14.291  26.325  14.330  1.00 33.81      A    O  
ANISOU  701  OH  TYR A  90     2356   4329   6161    588   1465     38  A    O  
ATOM    702  N   PHE A  91      19.977  19.687  13.409  1.00 14.51      A    N  
ANISOU  702  N   PHE A  91      306   2969   2238   -186    252   -324  A    N  
ATOM    703  CA  PHE A  91      20.632  18.396  13.637  1.00 15.09      A    C  
ANISOU  703  CA  PHE A  91      421   2994   2319    -98    142   -397  A    C  
ATOM    704  C   PHE A  91      21.870  18.495  14.548  1.00 16.11      A    C  
ANISOU  704  C   PHE A  91      509   3156   2457   -114    136   -436  A    C  
ATOM    705  O   PHE A  91      22.010  17.716  15.488  1.00 16.38      A    O  
ANISOU  705  O   PHE A  91      375   3393   2457   -146     87   -383  A    O  
ATOM    706  CB  PHE A  91      21.050  17.745  12.320  1.00 15.88      A    C  
ANISOU  706  CB  PHE A  91      487   3088   2458   -109    120   -460  A    C  
ATOM    707  CG  PHE A  91      19.915  17.161  11.496  1.00 15.26      A    C  
ANISOU  707  CG  PHE A  91      388   2910   2500    120   -164   -456  A    C  
ATOM    708  CD1 PHE A  91      18.665  16.863  12.038  1.00 16.77      A    C  
ANISOU  708  CD1 PHE A  91      377   2896   3097     98   -307   -269  A    C  
ATOM    709  CD2 PHE A  91      20.139  16.892  10.139  1.00 18.25      A    C  
ANISOU  709  CD2 PHE A  91      649   3558   2727    417   -197   -736  A    C  
ATOM    710  CE1 PHE A  91      17.653  16.300  11.234  1.00 16.67      A    C  
ANISOU  710  CE1 PHE A  91      294   2966   3073    131   -324   -366  A    C  
ATOM    711  CE2 PHE A  91      19.148  16.342   9.331  1.00 19.29      A    C  
ANISOU  711  CE2 PHE A  91      995   3546   2788    509   -482   -630  A    C  
ATOM    712  CZ  PHE A  91      17.894  16.049   9.883  1.00 19.54      A    C  
ANISOU  712  CZ  PHE A  91      865   3321   3237    184   -344   -535  A    C  
ATOM    713  N   ASP A  92      22.770  19.437  14.269  1.00 17.24      A    N  
ANISOU  713  N   ASP A  92      491   3467   2594   -152    184   -454  A    N  
ATOM    714  CA  ASP A  92      23.997  19.491  15.066  1.00 18.86      A    C  
ANISOU  714  CA  ASP A  92      593   3903   2669   -285    197   -518  A    C  
ATOM    715  C   ASP A  92      23.732  19.721  16.553  1.00 18.20      A    C  
ANISOU  715  C   ASP A  92      571   3725   2619   -293    273   -465  A    C  
ATOM    716  O   ASP A  92      24.244  18.996  17.418  1.00 18.52      A    O  
ANISOU  716  O   ASP A  92      412   3869   2754   -293    357   -456  A    O  
ATOM    717  CB  ASP A  92      24.938  20.556  14.514  1.00 19.74      A    C  
ANISOU  717  CB  ASP A  92      634   4120   2748   -384    197   -494  A    C  
ATOM    718  CG  ASP A  92      25.602  20.148  13.215  1.00 23.75      A    C  
ANISOU  718  CG  ASP A  92      763   5188   3072   -549    381   -670  A    C  
ATOM    719  OD1 ASP A  92      25.514  18.966  12.822  1.00 28.53      A    O  
ANISOU  719  OD1 ASP A  92     1278   5924   3637   -241    520   -996  A    O  
ATOM    720  OD2 ASP A  92      26.223  21.021  12.571  1.00 29.05      A    O1-
ANISOU  720  OD2 ASP A  92     1148   6503   3388  -1133    653   -702  A    O1-
ATOM    721  N   ASP A  93      22.912  20.717  16.879  1.00 17.96      A    N  
ANISOU  721  N   ASP A  93      480   3704   2639   -307    357   -423  A    N  
ATOM    722  CA  ASP A  93      22.655  21.023  18.285  1.00 18.55      A    C  
ANISOU  722  CA  ASP A  93      794   3495   2759   -357    241   -447  A    C  
ATOM    723  C   ASP A  93      21.803  19.958  18.970  1.00 16.11      A    C  
ANISOU  723  C   ASP A  93      295   3467   2360   -219    160   -408  A    C  
ATOM    724  O   ASP A  93      21.999  19.655  20.143  1.00 16.72      A    O  
ANISOU  724  O   ASP A  93      350   3639   2362   -346     26   -368  A    O  
ATOM    725  CB  ASP A  93      22.037  22.413  18.442  1.00 21.11      A    C  
ANISOU  725  CB  ASP A  93     1272   3501   3249   -377    410   -527  A    C  
ATOM    726  CG  ASP A  93      23.070  23.530  18.276  1.00 26.65      A    C  
ANISOU  726  CG  ASP A  93     2099   3564   4462   -614    428   -571  A    C  
ATOM    727  OD1 ASP A  93      24.271  23.243  18.064  1.00 30.59      A    O  
ANISOU  727  OD1 ASP A  93     2453   3878   5289   -921    388   -768  A    O  
ATOM    728  OD2 ASP A  93      22.672  24.707  18.364  1.00 32.41      A    O1-
ANISOU  728  OD2 ASP A  93     3075   3713   5526   -706    732   -507  A    O1-
ATOM    729  N   VAL A  94      20.841  19.377  18.252  1.00 15.26      A    N  
ANISOU  729  N   VAL A  94      276   3300   2221   -140      0   -366  A    N  
ATOM    730  CA  VAL A  94      20.019  18.331  18.869  1.00 15.15      A    C  
ANISOU  730  CA  VAL A  94      253   3368   2133     -7      0   -274  A    C  
ATOM    731  C   VAL A  94      20.870  17.093  19.164  1.00 14.88      A    C  
ANISOU  731  C   VAL A  94      253   3433   1967    -31     17   -406  A    C  
ATOM    732  O   VAL A  94      20.816  16.544  20.260  1.00 15.72      A    O  
ANISOU  732  O   VAL A  94      265   3806   1903    194     28   -287  A    O  
ATOM    733  CB  VAL A  94      18.769  17.970  18.036  1.00 15.00      A    C  
ANISOU  733  CB  VAL A  94      258   3197   2243      6    -97   -213  A    C  
ATOM    734  CG1 VAL A  94      18.101  16.693  18.567  1.00 15.18      A    C  
ANISOU  734  CG1 VAL A  94      263   3167   2338     80   -126    -86  A    C  
ATOM    735  CG2 VAL A  94      17.785  19.140  18.053  1.00 15.64      A    C  
ANISOU  735  CG2 VAL A  94      285   3181   2474    295     61   -155  A    C  
ATOM    736  N   THR A  95      21.669  16.659  18.189  1.00 15.56      A    N  
ANISOU  736  N   THR A  95      253   3638   2020     26      0   -562  A    N  
ATOM    737  CA  THR A  95      22.445  15.446  18.403  1.00 16.87      A    C  
ANISOU  737  CA  THR A  95      255   3817   2335     77    -19   -644  A    C  
ATOM    738  C   THR A  95      23.516  15.664  19.492  1.00 17.67      A    C  
ANISOU  738  C   THR A  95      258   3977   2477    131    -35   -719  A    C  
ATOM    739  O   THR A  95      23.776  14.753  20.276  1.00 18.54      A    O  
ANISOU  739  O   THR A  95      271   4158   2617    219   -142   -658  A    O  
ATOM    740  CB  THR A  95      23.109  14.920  17.100  1.00 16.88      A    C  
ANISOU  740  CB  THR A  95      263   3822   2328    103     17   -610  A    C  
ATOM    741  CG2 THR A  95      22.027  14.618  16.059  1.00 17.33      A    C  
ANISOU  741  CG2 THR A  95      258   3982   2345    132    -56   -665  A    C  
ATOM    742  OG1 THR A  95      24.003  15.902  16.564  1.00 18.21      A    O  
ANISOU  742  OG1 THR A  95      263   4144   2511     18    146   -615  A    O  
ATOM    743  N   ALA A  96      24.074  16.866  19.593  1.00 18.34      A    N  
ANISOU  743  N   ALA A  96      256   4235   2476     27    -82   -697  A    N  
ATOM    744  CA  ALA A  96      25.042  17.155  20.665  1.00 19.03      A    C  
ANISOU  744  CA  ALA A  96      291   4426   2515   -109   -172   -640  A    C  
ATOM    745  C   ALA A  96      24.346  17.106  22.029  1.00 19.09      A    C  
ANISOU  745  C   ALA A  96      282   4469   2502     76   -184   -577  A    C  
ATOM    746  O   ALA A  96      24.883  16.601  23.013  1.00 20.48      A    O  
ANISOU  746  O   ALA A  96      527   4724   2529     82   -238   -573  A    O  
ATOM    747  CB  ALA A  96      25.683  18.506  20.441  1.00 19.92      A    C  
ANISOU  747  CB  ALA A  96      304   4575   2691   -263   -252   -538  A    C  
ATOM    748  N   PHE A  97      23.109  17.603  22.086  1.00 18.08      A    N  
ANISOU  748  N   PHE A  97      263   4198   2410    102   -136   -635  A    N  
ATOM    749  CA  PHE A  97      22.359  17.580  23.330  1.00 17.92      A    C  
ANISOU  749  CA  PHE A  97      373   4061   2372    285    -93   -586  A    C  
ATOM    750  C   PHE A  97      21.999  16.149  23.740  1.00 17.23      A    C  
ANISOU  750  C   PHE A  97      355   3977   2213    425   -159   -538  A    C  
ATOM    751  O   PHE A  97      22.147  15.763  24.910  1.00 17.79      A    O  
ANISOU  751  O   PHE A  97      339   4226   2195    489   -285   -555  A    O  
ATOM    752  CB  PHE A  97      21.102  18.451  23.205  1.00 17.87      A    C  
ANISOU  752  CB  PHE A  97      282   4056   2450    252    125   -496  A    C  
ATOM    753  CG  PHE A  97      20.082  18.217  24.299  1.00 20.56      A    C  
ANISOU  753  CG  PHE A  97      754   4399   2657    353    520   -397  A    C  
ATOM    754  CD1 PHE A  97      20.363  18.555  25.618  1.00 25.57      A    C  
ANISOU  754  CD1 PHE A  97     1729   5062   2924    557    819   -269  A    C  
ATOM    755  CD2 PHE A  97      18.835  17.662  23.984  1.00 22.53      A    C  
ANISOU  755  CD2 PHE A  97      749   4666   3147    342    988   -120  A    C  
ATOM    756  CE1 PHE A  97      19.405  18.341  26.623  1.00 27.35      A    C  
ANISOU  756  CE1 PHE A  97     2063   5296   3034    995    948     12  A    C  
ATOM    757  CE2 PHE A  97      17.888  17.435  24.986  1.00 26.57      A    C  
ANISOU  757  CE2 PHE A  97     1692   5012   3393    763   1216     60  A    C  
ATOM    758  CZ  PHE A  97      18.181  17.768  26.304  1.00 27.36      A    C  
ANISOU  758  CZ  PHE A  97     2046   5249   3102    868   1429    120  A    C  
ATOM    759  N   LEU A  98      21.533  15.359  22.776  1.00 16.50      A    N  
ANISOU  759  N   LEU A  98      366   3777   2125    610   -186   -461  A    N  
ATOM    760  CA  LEU A  98      21.228  13.955  23.080  1.00 16.83      A    C  
ANISOU  760  CA  LEU A  98      388   3889   2117    666   -217   -368  A    C  
ATOM    761  C   LEU A  98      22.488  13.177  23.527  1.00 18.22      A    C  
ANISOU  761  C   LEU A  98      416   4250   2257    768   -241   -388  A    C  
ATOM    762  O   LEU A  98      22.408  12.380  24.456  1.00 19.00      A    O  
ANISOU  762  O   LEU A  98      483   4420   2318    872   -361   -241  A    O  
ATOM    763  CB  LEU A  98      20.547  13.305  21.889  1.00 16.18      A    C  
ANISOU  763  CB  LEU A  98      386   3679   2081    658   -173   -368  A    C  
ATOM    764  CG  LEU A  98      19.162  13.897  21.579  1.00 15.12      A    C  
ANISOU  764  CG  LEU A  98      307   3531   1906    422    -21   -192  A    C  
ATOM    765  CD1 LEU A  98      18.617  13.198  20.353  1.00 15.30      A    C  
ANISOU  765  CD1 LEU A  98      340   3472   2000    513     47   -260  A    C  
ATOM    766  CD2 LEU A  98      18.193  13.795  22.779  1.00 15.28      A    C  
ANISOU  766  CD2 LEU A  98      280   3513   2011    287    -52   -154  A    C  
ATOM    767  N  ASER A  99      23.627  13.424  22.880  0.50 19.83      A    N  
ANISOU  767  N  ASER A  99      405   4708   2422    741   -313   -425  A    N  
ATOM    768  N  BSER A  99      23.621  13.422  22.870  0.50 19.58      A    N  
ANISOU  768  N  BSER A  99      408   4668   2362    754   -305   -447  A    N  
ATOM    769  CA ASER A  99      24.885  12.804  23.277  0.50 21.42      A    C  
ANISOU  769  CA ASER A  99      406   5148   2585    688   -344   -487  A    C  
ATOM    770  CA BSER A  99      24.877  12.809  23.267  0.50 20.62      A    C  
ANISOU  770  CA BSER A  99      405   4953   2477    749   -315   -520  A    C  
ATOM    771  C  ASER A  99      25.260  13.144  24.714  0.50 21.63      A    C  
ANISOU  771  C  ASER A  99      444   5152   2623    674   -430   -507  A    C  
ATOM    772  C  BSER A  99      25.208  13.129  24.723  0.50 21.26      A    C  
ANISOU  772  C  BSER A  99      439   5119   2518    687   -390   -502  A    C  
ATOM    773  O  ASER A  99      25.777  12.300  25.446  0.50 22.48      A    O  
ANISOU  773  O  ASER A  99      726   5141   2675    649   -505   -522  A    O  
ATOM    774  O  BSER A  99      25.634  12.256  25.479  0.50 22.31      A    O  
ANISOU  774  O  BSER A  99      728   5145   2603    675   -467   -496  A    O  
ATOM    775  CB ASER A  99      25.970  13.256  22.315  0.50 21.97      A    C  
ANISOU  775  CB ASER A  99      372   5296   2680    697   -287   -463  A    C  
ATOM    776  CB BSER A  99      25.975  13.310  22.341  0.50 20.68      A    C  
ANISOU  776  CB BSER A  99      388   4992   2476    722   -313   -549  A    C  
ATOM    777  OG ASER A  99      25.861  12.537  21.101  0.50 24.89      A    O  
ANISOU  777  OG ASER A  99      592   6014   2851    658   -274   -493  A    O  
ATOM    778  OG BSER A  99      27.217  12.741  22.718  0.50 20.67      A    O  
ANISOU  778  OG BSER A  99      421   4834   2599    842   -274   -579  A    O  
ATOM    779  N   LYS A 100      24.994  14.382  25.117  1.00 21.75      A    N  
ANISOU  779  N   LYS A 100      531   5223   2509    723   -485   -509  A    N  
ATOM    780  CA  LYS A 100      25.268  14.835  26.479  1.00 23.27      A    C  
ANISOU  780  CA  LYS A 100      841   5457   2545    807   -498   -568  A    C  
ATOM    781  C   LYS A 100      24.335  14.143  27.474  1.00 22.89      A    C  
ANISOU  781  C   LYS A 100      802   5483   2413    988   -500   -520  A    C  
ATOM    782  O   LYS A 100      24.761  13.751  28.564  1.00 24.04      A    O  
ANISOU  782  O   LYS A 100      986   5702   2444    851   -542   -480  A    O  
ATOM    783  CB  LYS A 100      25.190  16.361  26.550  1.00 24.45      A    C  
ANISOU  783  CB  LYS A 100     1087   5522   2680    781   -546   -693  A    C  
ATOM    784  CG  LYS A 100      25.571  16.991  27.882  1.00 29.27      A    C  
ANISOU  784  CG  LYS A 100     1958   5946   3219    487   -515   -878  A    C  
ATOM    785  CD  LYS A 100      25.968  18.456  27.705  1.00 36.42      A    C  
ANISOU  785  CD  LYS A 100     3023   6560   4255    142   -562   -763  A    C  
ATOM    786  CE  LYS A 100      24.790  19.421  27.798  1.00 40.63      A    C  
ANISOU  786  CE  LYS A 100     3616   7031   4791     -6   -680   -315  A    C  
ATOM    787  NZ  LYS A 100      23.813  19.245  26.686  1.00 44.34      A    N1+
ANISOU  787  NZ  LYS A 100     3847   7562   5440   -197   -856    -19  A    N1+
ATOM    788  N   CYS A 101      23.062  13.965  27.101  1.00 22.32      A    N  
ANISOU  788  N   CYS A 101      886   5256   2337   1040   -476   -531  A    N  
ATOM    789  CA  CYS A 101      22.146  13.223  27.965  1.00 21.76      A    C  
ANISOU  789  CA  CYS A 101     1085   4924   2257   1186   -522   -612  A    C  
ATOM    790  C   CYS A 101      22.649  11.795  28.202  1.00 23.32      A    C  
ANISOU  790  C   CYS A 101     1562   5088   2211   1553   -535   -670  A    C  
ATOM    791  O   CYS A 101      22.616  11.296  29.331  1.00 24.32      A    O  
ANISOU  791  O   CYS A 101     1736   5278   2228   1595   -627   -597  A    O  
ATOM    792  CB  CYS A 101      20.750  13.209  27.368  1.00 21.30      A    C  
ANISOU  792  CB  CYS A 101      917   4841   2334   1023   -527   -529  A    C  
ATOM    793  SG  CYS A 101      19.951  14.828  27.403  1.00 20.73      A    S  
ANISOU  793  SG  CYS A 101      797   4596   2484    688   -296   -463  A    S  
ATOM    794  N   ASP A 102      23.143  11.152  27.146  1.00 25.12      A    N  
ANISOU  794  N   ASP A 102     2026   5289   2231   1888   -737   -869  A    N  
ATOM    795  CA  ASP A 102      23.702   9.807  27.299  1.00 26.89      A    C  
ANISOU  795  CA  ASP A 102     2249   5594   2372   2152   -973   -986  A    C  
ATOM    796  C   ASP A 102      24.986   9.774  28.138  1.00 28.63      A    C  
ANISOU  796  C   ASP A 102     2345   5942   2590   2248  -1208  -1022  A    C  
ATOM    797  O   ASP A 102      25.195   8.847  28.919  1.00 29.89      A    O  
ANISOU  797  O   ASP A 102     2368   6140   2847   2275  -1181   -930  A    O  
ATOM    798  CB  ASP A 102      23.899   9.138  25.926  1.00 26.74      A    C  
ANISOU  798  CB  ASP A 102     2333   5493   2334   2150   -961   -996  A    C  
ATOM    799  CG  ASP A 102      22.729   8.239  25.535  1.00 27.50      A    C  
ANISOU  799  CG  ASP A 102     2487   5615   2345   2073   -767  -1049  A    C  
ATOM    800  OD1 ASP A 102      22.398   8.148  24.330  1.00 26.64      A    O  
ANISOU  800  OD1 ASP A 102     2222   5442   2459   1985   -979   -913  A    O  
ATOM    801  OD2 ASP A 102      22.150   7.594  26.442  1.00 28.08      A    O1-
ANISOU  801  OD2 ASP A 102     2347   5895   2426   1985   -780   -860  A    O1-
ATOM    802  N   GLN A 103      25.827  10.795  27.992  1.00 29.62      A    N  
ANISOU  802  N   GLN A 103     2203   6248   2802   2328  -1404  -1080  A    N  
ATOM    803  CA  GLN A 103      27.069  10.883  28.771  1.00 32.70      A    C  
ANISOU  803  CA  GLN A 103     2585   6657   3183   2213  -1597  -1089  A    C  
ATOM    804  C   GLN A 103      26.765  11.063  30.259  1.00 32.82      A    C  
ANISOU  804  C   GLN A 103     2542   6998   2930   2291  -1597  -1133  A    C  
ATOM    805  O   GLN A 103      27.431  10.483  31.115  1.00 33.98      A    O  
ANISOU  805  O   GLN A 103     2711   7185   3016   2372  -1497  -1052  A    O  
ATOM    806  CB  GLN A 103      27.926  12.054  28.285  1.00 33.30      A    C  
ANISOU  806  CB  GLN A 103     2495   6664   3494   2099  -1718  -1080  A    C  
ATOM    807  CG  GLN A 103      28.528  11.886  26.902  1.00 40.41      A    C  
ANISOU  807  CG  GLN A 103     3542   6674   5138   1779  -2055   -964  A    C  
ATOM    808  CD  GLN A 103      29.079  13.191  26.346  1.00 46.96      A    C  
ANISOU  808  CD  GLN A 103     4304   6765   6772   1492  -2414   -790  A    C  
ATOM    809  NE2 GLN A 103      28.442  13.705  25.297  1.00 49.86      A    N  
ANISOU  809  NE2 GLN A 103     4343   7024   7577   1535  -2460   -661  A    N  
ATOM    810  OE1 GLN A 103      30.064  13.729  26.855  1.00 49.68      A    O  
ANISOU  810  OE1 GLN A 103     4745   6966   7164   1445  -2186  -1075  A    O  
ATOM    811  N   ARG A 104      25.754  11.877  30.547  1.00 33.01      A    N  
ANISOU  811  N   ARG A 104     2707   7092   2745   2283  -1541   -986  A    N  
ATOM    812  CA  ARG A 104      25.420  12.254  31.916  1.00 32.86      A    C  
ANISOU  812  CA  ARG A 104     2842   6987   2657   2117  -1497   -913  A    C  
ATOM    813  C   ARG A 104      24.373  11.354  32.577  1.00 32.77      A    C  
ANISOU  813  C   ARG A 104     3230   6638   2585   2301  -1324   -728  A    C  
ATOM    814  O   ARG A 104      24.023  11.562  33.745  1.00 33.11      A    O  
ANISOU  814  O   ARG A 104     3296   6771   2515   2292  -1358   -781  A    O  
ATOM    815  CB  ARG A 104      24.952  13.718  31.964  1.00 32.85      A    C  
ANISOU  815  CB  ARG A 104     2766   6998   2716   1923  -1483   -935  A    C  
ATOM    816  CG  ARG A 104      25.995  14.730  31.517  1.00 34.68      A    C  
ANISOU  816  CG  ARG A 104     2851   7415   2910   1348  -1368   -895  A    C  
ATOM    817  CD  ARG A 104      25.432  16.142  31.417  1.00 36.46      A    C  
ANISOU  817  CD  ARG A 104     3027   7710   3115    571  -1014  -1014  A    C  
ATOM    818  NE  ARG A 104      24.868  16.630  32.674  1.00 40.66      A    N  
ANISOU  818  NE  ARG A 104     3671   8177   3601    175   -719  -1289  A    N  
ATOM    819  CZ  ARG A 104      25.492  17.416  33.547  1.00 43.53      A    C  
ANISOU  819  CZ  ARG A 104     4282   8467   3790     76   -640  -1465  A    C  
ATOM    820  NH1 ARG A 104      26.736  17.827  33.321  1.00 45.80      A    N1+
ANISOU  820  NH1 ARG A 104     4557   8827   4018   -370   -732  -1489  A    N1+
ATOM    821  NH2 ARG A 104      24.880  17.802  34.664  1.00 45.42      A    N  
ANISOU  821  NH2 ARG A 104     4785   8564   3907    421   -555  -1500  A    N  
ATOM    822  N   ASN A 105      23.879  10.349  31.851  1.00 32.21      A    N  
ANISOU  822  N   ASN A 105     3452   6291   2495   2431  -1145   -430  A    N  
ATOM    823  CA  ASN A 105      22.814   9.469  32.359  1.00 32.57      A    C  
ANISOU  823  CA  ASN A 105     3761   6147   2467   2441   -957   -124  A    C  
ATOM    824  C   ASN A 105      21.582  10.270  32.782  1.00 30.66      A    C  
ANISOU  824  C   ASN A 105     3508   5867   2275   2090   -850   -216  A    C  
ATOM    825  O   ASN A 105      21.035  10.076  33.876  1.00 31.30      A    O  
ANISOU  825  O   ASN A 105     3689   5964   2238   2061   -877   -185  A    O  
ATOM    826  CB  ASN A 105      23.284   8.559  33.503  1.00 34.23      A    C  
ANISOU  826  CB  ASN A 105     4065   6438   2502   2662   -851    -15  A    C  
ATOM    827  CG  ASN A 105      23.890   7.257  33.004  1.00 36.90      A    C  
ANISOU  827  CG  ASN A 105     4526   6832   2662   3079   -754    262  A    C  
ATOM    828  ND2 ASN A 105      24.821   6.720  33.784  1.00 40.39      A    N  
ANISOU  828  ND2 ASN A 105     4798   7368   3181   3402   -727    270  A    N  
ATOM    829  OD1 ASN A 105      23.533   6.733  31.941  1.00 39.10      A    O  
ANISOU  829  OD1 ASN A 105     4498   7368   2989   3497   -727    252  A    O  
ATOM    830  N   GLU A 106      21.161  11.166  31.893  1.00 27.37      A    N  
ANISOU  830  N   GLU A 106     2818   5422   2159   1685   -724   -331  A    N  
ATOM    831  CA  GLU A 106      19.993  11.999  32.128  1.00 24.21      A    C  
ANISOU  831  CA  GLU A 106     2132   4949   2117   1119   -584   -405  A    C  
ATOM    832  C   GLU A 106      18.941  11.619  31.100  1.00 22.55      A    C  
ANISOU  832  C   GLU A 106     2098   4539   1932    917   -434   -142  A    C  
ATOM    833  O   GLU A 106      19.070  11.999  29.942  1.00 22.81      A    O  
ANISOU  833  O   GLU A 106     2035   4690   1941    820   -320   -131  A    O  
ATOM    834  CB  GLU A 106      20.357  13.483  32.037  1.00 23.59      A    C  
ANISOU  834  CB  GLU A 106     1870   4978   2113   1014   -592   -480  A    C  
ATOM    835  CG  GLU A 106      21.342  13.892  33.127  1.00 24.78      A    C  
ANISOU  835  CG  GLU A 106     1587   5440   2387    671   -626   -631  A    C  
ATOM    836  CD  GLU A 106      21.872  15.308  33.009  1.00 26.12      A    C  
ANISOU  836  CD  GLU A 106     1553   5655   2714    529   -604   -697  A    C  
ATOM    837  OE1 GLU A 106      21.783  15.901  31.906  1.00 26.04      A    O  
ANISOU  837  OE1 GLU A 106     1448   5619   2827    590   -627   -737  A    O  
ATOM    838  OE2 GLU A 106      22.401  15.807  34.035  1.00 27.49      A    O1-
ANISOU  838  OE2 GLU A 106     1605   5989   2851    518   -898   -688  A    O1-
ATOM    839  N   PRO A 107      17.948  10.816  31.508  1.00 22.19      A    N  
ANISOU  839  N   PRO A 107     2125   4347   1958    856   -335    135  A    N  
ATOM    840  CA  PRO A 107      16.952  10.343  30.544  1.00 20.80      A    C  
ANISOU  840  CA  PRO A 107     2046   4034   1823    790   -241    164  A    C  
ATOM    841  C   PRO A 107      16.202  11.481  29.858  1.00 18.92      A    C  
ANISOU  841  C   PRO A 107     1676   3837   1676    772   -135    -35  A    C  
ATOM    842  O   PRO A 107      15.828  12.472  30.500  1.00 18.98      A    O  
ANISOU  842  O   PRO A 107     1711   3774   1726    697    -98   -118  A    O  
ATOM    843  CB  PRO A 107      16.010   9.484  31.386  1.00 21.48      A    C  
ANISOU  843  CB  PRO A 107     1982   4169   2011    825   -164    218  A    C  
ATOM    844  CG  PRO A 107      16.834   9.062  32.554  1.00 23.65      A    C  
ANISOU  844  CG  PRO A 107     2441   4489   2055    790   -241    421  A    C  
ATOM    845  CD  PRO A 107      17.716  10.250  32.849  1.00 23.00      A    C  
ANISOU  845  CD  PRO A 107     2275   4462   2002    850   -388    294  A    C  
ATOM    846  N   VAL A 108      16.008  11.330  28.552  1.00 17.43      A    N  
ANISOU  846  N   VAL A 108     1472   3555   1597    631   -131    -54  A    N  
ATOM    847  CA  VAL A 108      15.337  12.347  27.748  1.00 16.24      A    C  
ANISOU  847  CA  VAL A 108     1118   3388   1664    540    -93   -120  A    C  
ATOM    848  C   VAL A 108      14.373  11.663  26.789  1.00 15.32      A    C  
ANISOU  848  C   VAL A 108     1080   3197   1544    469     20   -131  A    C  
ATOM    849  O   VAL A 108      14.706  10.665  26.149  1.00 16.43      A    O  
ANISOU  849  O   VAL A 108     1286   3262   1693    498     19   -137  A    O  
ATOM    850  CB  VAL A 108      16.349  13.217  26.953  1.00 15.93      A    C  
ANISOU  850  CB  VAL A 108     1023   3294   1737    504    -24   -120  A    C  
ATOM    851  CG1 VAL A 108      17.301  12.348  26.147  1.00 17.57      A    C  
ANISOU  851  CG1 VAL A 108      885   3932   1860    678    -49   -285  A    C  
ATOM    852  CG2 VAL A 108      15.656  14.220  26.015  1.00 16.51      A    C  
ANISOU  852  CG2 VAL A 108      865   3488   1921    386   -215    -54  A    C  
ATOM    853  N   LEU A 109      13.157  12.205  26.729  1.00 15.12      A    N  
ANISOU  853  N   LEU A 109      913   3068   1763    329     57    -73  A    N  
ATOM    854  CA  LEU A 109      12.159  11.726  25.778  1.00 14.14      A    C  
ANISOU  854  CA  LEU A 109      925   2912   1536    164    230   -115  A    C  
ATOM    855  C   LEU A 109      12.076  12.694  24.598  1.00 13.40      A    C  
ANISOU  855  C   LEU A 109      733   2822   1536    146    285   -115  A    C  
ATOM    856  O   LEU A 109      11.778  13.877  24.815  1.00 14.04      A    O  
ANISOU  856  O   LEU A 109      753   2739   1841    120    307   -137  A    O  
ATOM    857  CB  LEU A 109      10.783  11.608  26.455  1.00 15.12      A    C  
ANISOU  857  CB  LEU A 109      979   2930   1835     15    274    -87  A    C  
ATOM    858  CG  LEU A 109       9.603  11.315  25.508  1.00 15.87      A    C  
ANISOU  858  CG  LEU A 109      957   3169   1902    -17    383   -283  A    C  
ATOM    859  CD1 LEU A 109       9.735   9.965  24.822  1.00 17.43      A    C  
ANISOU  859  CD1 LEU A 109     1482   3235   1905    -74    331   -203  A    C  
ATOM    860  CD2 LEU A 109       8.278  11.381  26.259  1.00 16.99      A    C  
ANISOU  860  CD2 LEU A 109      913   3425   2117     -6    522   -208  A    C  
ATOM    861  N   VAL A 110      12.361  12.194  23.388  1.00 12.93      A    N  
ANISOU  861  N   VAL A 110      509   2973   1430    148    252    -59  A    N  
ATOM    862  CA  VAL A 110      12.215  12.977  22.169  1.00 13.05      A    C  
ANISOU  862  CA  VAL A 110      287   3142   1528    171    172    -28  A    C  
ATOM    863  C   VAL A 110      10.844  12.649  21.576  1.00 12.29      A    C  
ANISOU  863  C   VAL A 110      299   2739   1632    161    217    -83  A    C  
ATOM    864  O   VAL A 110      10.566  11.487  21.287  1.00 13.30      A    O  
ANISOU  864  O   VAL A 110      289   2759   2004    153    199   -170  A    O  
ATOM    865  CB  VAL A 110      13.339  12.629  21.147  1.00 13.55      A    C  
ANISOU  865  CB  VAL A 110      293   3415   1439    225    164    -24  A    C  
ATOM    866  CG1 VAL A 110      13.184  13.504  19.903  1.00 14.43      A    C  
ANISOU  866  CG1 VAL A 110      282   3614   1585     31    195    153  A    C  
ATOM    867  CG2 VAL A 110      14.718  12.835  21.794  1.00 15.29      A    C  
ANISOU  867  CG2 VAL A 110      255   3621   1932     89      8     59  A    C  
ATOM    868  N   HIS A 111       9.994  13.654  21.409  1.00 12.41      A    N  
ANISOU  868  N   HIS A 111      271   2716   1729     85    142    -86  A    N  
ATOM    869  CA  HIS A 111       8.645  13.364  20.929  1.00 12.61      A    C  
ANISOU  869  CA  HIS A 111      282   2806   1703    -54    200    -15  A    C  
ATOM    870  C   HIS A 111       8.125  14.365  19.923  1.00 11.93      A    C  
ANISOU  870  C   HIS A 111      299   2620   1614     40    244   -118  A    C  
ATOM    871  O   HIS A 111       8.560  15.512  19.864  1.00 12.80      A    O  
ANISOU  871  O   HIS A 111      269   2635   1958    115    128    -39  A    O  
ATOM    872  CB  HIS A 111       7.643  13.211  22.091  1.00 12.84      A    C  
ANISOU  872  CB  HIS A 111      337   2840   1703    -38    346    -74  A    C  
ATOM    873  CG  HIS A 111       7.092  14.511  22.588  1.00 13.20      A    C  
ANISOU  873  CG  HIS A 111      339   2903   1773     27    357   -124  A    C  
ATOM    874  CD2 HIS A 111       7.543  15.360  23.540  1.00 13.83      A    C  
ANISOU  874  CD2 HIS A 111      370   2930   1955      0    439   -304  A    C  
ATOM    875  ND1 HIS A 111       5.947  15.084  22.072  1.00 13.68      A    N  
ANISOU  875  ND1 HIS A 111      390   3000   1808    -49    460    -54  A    N  
ATOM    876  CE1 HIS A 111       5.720  16.230  22.686  1.00 14.00      A    C  
ANISOU  876  CE1 HIS A 111      340   3199   1781     10    359   -175  A    C  
ATOM    877  NE2 HIS A 111       6.665  16.417  23.590  1.00 13.86      A    N  
ANISOU  877  NE2 HIS A 111      368   3055   1844      0    425   -185  A    N  
ATOM    878  N   CYS A 112       7.156  13.908  19.154  1.00  0.00      A    N  
ATOM    879  CA  CYS A 112       6.321  14.766  18.318  1.00  0.00      A    C  
ATOM    880  C   CYS A 112       4.855  14.526  18.591  1.00  0.00      A    C  
ATOM    881  O   CYS A 112       4.536  14.112  19.708  1.00  0.00      A    O  
ATOM    882  CB  CYS A 112       6.692  14.523  16.842  1.00  0.00      A    C  
ATOM    883  SG  CYS A 112       6.386  12.803  16.380  1.00  0.00      A    S  
ATOM    884  N   ALA A 113       4.004  14.721  17.617  1.00 16.37      A    N  
ANISOU  884  N   ALA A 113      302   3907   2011    -97    286   -238  A    N  
ATOM    885  CA  ALA A 113       2.583  14.404  17.811  1.00 17.29      A    C  
ANISOU  885  CA  ALA A 113      294   3923   2352    -74    291   -335  A    C  
ATOM    886  C   ALA A 113       2.363  12.903  17.637  1.00 17.43      A    C  
ANISOU  886  C   ALA A 113      286   3998   2339   -135    252   -368  A    C  
ATOM    887  O   ALA A 113       1.832  12.227  18.530  1.00 17.63      A    O  
ANISOU  887  O   ALA A 113      329   4007   2363    -92    399   -373  A    O  
ATOM    888  CB  ALA A 113       1.735  15.193  16.839  1.00 17.76      A    C  
ANISOU  888  CB  ALA A 113      285   4101   2363   -108    252   -320  A    C  
ATOM    889  N   ALA A 114       2.778  12.383  16.484  1.00 16.78      A    N  
ANISOU  889  N   ALA A 114      311   3819   2247   -209    320   -394  A    N  
ATOM    890  CA  ALA A 114       2.620  10.971  16.175  1.00 16.95      A    C  
ANISOU  890  CA  ALA A 114      329   3810   2300   -305    349   -417  A    C  
ATOM    891  C   ALA A 114       3.785  10.090  16.616  1.00 16.02      A    C  
ANISOU  891  C   ALA A 114      337   3564   2187   -384    322   -450  A    C  
ATOM    892  O   ALA A 114       3.663   8.862  16.613  1.00 16.87      A    O  
ANISOU  892  O   ALA A 114      435   3540   2433   -520    531   -467  A    O  
ATOM    893  CB  ALA A 114       2.353  10.781  14.689  1.00 16.95      A    C  
ANISOU  893  CB  ALA A 114      340   3804   2297   -406    320   -306  A    C  
ATOM    894  N   GLY A 115       4.918  10.695  16.971  1.00 15.16      A    N  
ANISOU  894  N   GLY A 115      324   3355   2081   -296    310   -379  A    N  
ATOM    895  CA  GLY A 115       6.106   9.918  17.296  1.00 14.90      A    C  
ANISOU  895  CA  GLY A 115      306   3379   1976    -86    296   -351  A    C  
ATOM    896  C   GLY A 115       6.717   9.197  16.100  1.00 13.89      A    C  
ANISOU  896  C   GLY A 115      328   3025   1923   -207    329   -225  A    C  
ATOM    897  O   GLY A 115       7.319   8.128  16.245  1.00 14.66      A    O  
ANISOU  897  O   GLY A 115      447   3052   2072   -208    348   -160  A    O  
ATOM    898  N   VAL A 116       6.560   9.793  14.919  1.00 14.05      A    N  
ANISOU  898  N   VAL A 116      284   3253   1800   -161    195   -216  A    N  
ATOM    899  CA  VAL A 116       6.996   9.176  13.670  1.00 14.16      A    C  
ANISOU  899  CA  VAL A 116      428   3093   1861   -250    175   -186  A    C  
ATOM    900  C   VAL A 116       8.018  10.032  12.913  1.00 13.47      A    C  
ANISOU  900  C   VAL A 116      291   2967   1860    -49    225   -120  A    C  
ATOM    901  O   VAL A 116       9.107   9.550  12.555  1.00 13.92      A    O  
ANISOU  901  O   VAL A 116      284   3055   1949     87    217    -23  A    O  
ATOM    902  CB  VAL A 116       5.776   8.881  12.752  1.00 14.06      A    C  
ANISOU  902  CB  VAL A 116      320   3100   1923   -274    175   -270  A    C  
ATOM    903  CG1 VAL A 116       6.225   8.426  11.376  1.00 14.88      A    C  
ANISOU  903  CG1 VAL A 116      397   3264   1993   -313    285   -307  A    C  
ATOM    904  CG2 VAL A 116       4.884   7.828  13.383  1.00 16.56      A    C  
ANISOU  904  CG2 VAL A 116      577   3537   2178   -460    295   -219  A    C  
ATOM    905  N   ASN A 117       7.660  11.289  12.656  1.00 13.24      A    N  
ANISOU  905  N   ASN A 117      364   2991   1676      6     76      3  A    N  
ATOM    906  CA  ASN A 117       8.381  12.093  11.674  1.00 12.59      A    C  
ANISOU  906  CA  ASN A 117      263   2882   1638    162     -6   -106  A    C  
ATOM    907  C   ASN A 117       9.349  13.081  12.278  1.00 12.84      A    C  
ANISOU  907  C   ASN A 117      259   2910   1709    120    -20   -227  A    C  
ATOM    908  O   ASN A 117      10.562  12.911  12.112  1.00 13.12      A    O  
ANISOU  908  O   ASN A 117      281   2982   1721    272     10   -120  A    O  
ATOM    909  CB  ASN A 117       7.435  12.787  10.698  1.00 13.08      A    C  
ANISOU  909  CB  ASN A 117      262   3089   1615    156     -5    -60  A    C  
ATOM    910  CG  ASN A 117       6.878  11.841   9.664  1.00 13.98      A    C  
ANISOU  910  CG  ASN A 117      315   3181   1817    375     70   -342  A    C  
ATOM    911  ND2 ASN A 117       5.628  12.089   9.253  1.00 16.78      A    N  
ANISOU  911  ND2 ASN A 117      299   3840   2237    305   -225   -276  A    N  
ATOM    912  OD1 ASN A 117       7.531  10.896   9.243  1.00 14.87      A    O  
ANISOU  912  OD1 ASN A 117      271   3364   2014    227     23   -254  A    O  
ATOM    913  N   ARG A 118       8.889  14.107  12.980  1.00 12.34      A    N  
ANISOU  913  N   ARG A 118      259   2799   1632    107     31   -186  A    N  
ATOM    914  CA  ARG A 118       9.831  15.103  13.527  1.00 11.82      A    C  
ANISOU  914  CA  ARG A 118      267   2594   1629    103    109    -38  A    C  
ATOM    915  C   ARG A 118      10.729  14.424  14.542  1.00 11.50      A    C  
ANISOU  915  C   ARG A 118      273   2554   1544     98     85     19  A    C  
ATOM    916  O   ARG A 118      11.985  14.620  14.525  1.00 12.70      A    O  
ANISOU  916  O   ARG A 118      260   2824   1743     56     92     61  A    O  
ATOM    917  CB  ARG A 118       9.085  16.270  14.170  1.00 12.41      A    C  
ANISOU  917  CB  ARG A 118      291   2671   1755    226    152    -49  A    C  
ATOM    918  CG  ARG A 118       8.391  17.142  13.130  1.00 13.79      A    C  
ANISOU  918  CG  ARG A 118      318   3057   1862    408     94     37  A    C  
ATOM    919  CD  ARG A 118       7.344  18.039  13.758  1.00 14.75      A    C  
ANISOU  919  CD  ARG A 118      335   2939   2329    230    364     71  A    C  
ATOM    920  NE  ARG A 118       6.150  17.256  14.113  1.00 14.64      A    N  
ANISOU  920  NE  ARG A 118      289   3224   2047    309     71     10  A    N  
ATOM    921  CZ  ARG A 118       5.031  17.806  14.599  1.00 15.22      A    C  
ANISOU  921  CZ  ARG A 118      322   3240   2222    443     74    125  A    C  
ATOM    922  NH1 ARG A 118       4.963  19.116  14.800  1.00 15.41      A    N1+
ANISOU  922  NH1 ARG A 118      291   3323   2241    328    -77      0  A    N1+
ATOM    923  NH2 ARG A 118       4.005  17.005  14.898  1.00 15.72      A    N  
ANISOU  923  NH2 ARG A 118      282   3528   2161    231    151     20  A    N  
ATOM    924  N   SER A 119      10.156  13.633  15.434  1.00 11.45      A    N  
ANISOU  924  N   SER A 119      265   2585   1499    145     71    125  A    N  
ATOM    925  CA  SER A 119      10.934  12.938  16.469  1.00 11.91      A    C  
ANISOU  925  CA  SER A 119      395   2560   1571     85    219     87  A    C  
ATOM    926  C   SER A 119      11.746  11.812  15.867  1.00 11.82      A    C  
ANISOU  926  C   SER A 119      267   2563   1660    131     93     -6  A    C  
ATOM    927  O   SER A 119      12.937  11.641  16.210  1.00 12.43      A    O  
ANISOU  927  O   SER A 119      267   2777   1676    164     57     -6  A    O  
ATOM    928  CB  SER A 119       9.971  12.429  17.552  1.00 12.27      A    C  
ANISOU  928  CB  SER A 119      412   2590   1659    -20    260     43  A    C  
ATOM    929  OG  SER A 119       8.938  11.641  16.963  1.00 13.78      A    O  
ANISOU  929  OG  SER A 119      342   2858   2037   -193    366    -38  A    O  
ATOM    930  N   GLY A 120      11.152  11.004  14.989  1.00 11.82      A    N  
ANISOU  930  N   GLY A 120      260   2603   1626     40     92    -39  A    N  
ATOM    931  CA  GLY A 120      11.886   9.920  14.345  1.00 11.99      A    C  
ANISOU  931  CA  GLY A 120      465   2442   1648   -113    263     52  A    C  
ATOM    932  C   GLY A 120      13.092  10.479  13.621  1.00 11.38      A    C  
ANISOU  932  C   GLY A 120      276   2493   1553    -74    163     81  A    C  
ATOM    933  O   GLY A 120      14.188   9.884  13.680  1.00 12.31      A    O  
ANISOU  933  O   GLY A 120      264   2655   1756    108     99     44  A    O  
ATOM    934  N   ALA A 121      12.954  11.606  12.950  1.00 11.12      A    N  
ANISOU  934  N   ALA A 121      295   2474   1456   -104    197    164  A    N  
ATOM    935  CA  ALA A 121      14.095  12.179  12.199  1.00 11.08      A    C  
ANISOU  935  CA  ALA A 121      274   2477   1460   -151    103    135  A    C  
ATOM    936  C   ALA A 121      15.212  12.605  13.140  1.00 11.54      A    C  
ANISOU  936  C   ALA A 121      253   2526   1604     15     14    -52  A    C  
ATOM    937  O   ALA A 121      16.399  12.400  12.813  1.00 12.42      A    O  
ANISOU  937  O   ALA A 121      287   2703   1729    276     64    -20  A    O  
ATOM    938  CB  ALA A 121      13.644  13.347  11.355  1.00 11.84      A    C  
ANISOU  938  CB  ALA A 121      289   2732   1476     -8    204    311  A    C  
ATOM    939  N   MET A 122      14.917  13.200  14.285  1.00 11.24      A    N  
ANISOU  939  N   MET A 122      260   2472   1536    121    -40   -153  A    N  
ATOM    940  CA  MET A 122      15.965  13.604  15.234  1.00 11.44      A    C  
ANISOU  940  CA  MET A 122      256   2486   1605    -50     58    -99  A    C  
ATOM    941  C   MET A 122      16.610  12.395  15.832  1.00 11.75      A    C  
ANISOU  941  C   MET A 122      258   2538   1668     30     76    -20  A    C  
ATOM    942  O   MET A 122      17.847  12.420  16.058  1.00 13.24      A    O  
ANISOU  942  O   MET A 122      260   2964   1807    123     41   -117  A    O  
ATOM    943  CB  MET A 122      15.404  14.526  16.324  1.00 12.27      A    C  
ANISOU  943  CB  MET A 122      263   2612   1787    -40     74   -186  A    C  
ATOM    944  CG  MET A 122      14.919  15.862  15.774  1.00 13.75      A    C  
ANISOU  944  CG  MET A 122      273   2624   2329   -100    182    -93  A    C  
ATOM    945  SD  MET A 122      16.263  16.729  14.907  1.00 15.59      A    S  
ANISOU  945  SD  MET A 122      255   3012   2654     38     65     95  A    S  
ATOM    946  CE  MET A 122      15.391  18.232  14.405  1.00 20.03      A    C  
ANISOU  946  CE  MET A 122      522   3023   4065     15   -208    463  A    C  
ATOM    947  N   ILE A 123      15.878  11.314  16.068  1.00 11.60      A    N  
ANISOU  947  N   ILE A 123      273   2476   1659    164    104    108  A    N  
ATOM    948  CA  ILE A 123      16.482  10.081  16.570  1.00 11.88      A    C  
ANISOU  948  CA  ILE A 123      430   2486   1597     93    142    -13  A    C  
ATOM    949  C   ILE A 123      17.366   9.450  15.505  1.00 11.83      A    C  
ANISOU  949  C   ILE A 123      265   2651   1580    145     59    -79  A    C  
ATOM    950  O   ILE A 123      18.488   8.978  15.797  1.00 12.75      A    O  
ANISOU  950  O   ILE A 123      275   2794   1775    235      0      0  A    O  
ATOM    951  CB  ILE A 123      15.387   9.069  17.012  1.00 12.79      A    C  
ANISOU  951  CB  ILE A 123      544   2517   1800     74    263     93  A    C  
ATOM    952  CG1 ILE A 123      14.682   9.552  18.287  1.00 15.14      A    C  
ANISOU  952  CG1 ILE A 123      934   3079   1738    175    240    -34  A    C  
ATOM    953  CG2 ILE A 123      15.937   7.664  17.147  1.00 14.38      A    C  
ANISOU  953  CG2 ILE A 123      780   2592   2090    192    263    131  A    C  
ATOM    954  CD1 ILE A 123      15.587   9.710  19.505  1.00 15.91      A    C  
ANISOU  954  CD1 ILE A 123     1001   3212   1831    372      6    172  A    C  
ATOM    955  N   LEU A 124      16.929   9.438  14.254  1.00 11.85      A    N  
ANISOU  955  N   LEU A 124      273   2707   1521    201     48   -174  A    N  
ATOM    956  CA  LEU A 124      17.764   8.899  13.172  1.00 12.19      A    C  
ANISOU  956  CA  LEU A 124      412   2666   1553    130     43   -151  A    C  
ATOM    957  C   LEU A 124      19.036   9.725  13.049  1.00 12.01      A    C  
ANISOU  957  C   LEU A 124      276   2547   1738    227     18    -97  A    C  
ATOM    958  O   LEU A 124      20.155   9.163  12.895  1.00 13.29      A    O  
ANISOU  958  O   LEU A 124      348   2790   1911    461    115    -87  A    O  
ATOM    959  CB  LEU A 124      16.971   8.891  11.865  1.00 11.72      A    C  
ANISOU  959  CB  LEU A 124      260   2725   1468    134     -5   -158  A    C  
ATOM    960  CG  LEU A 124      17.572   8.208  10.652  1.00 15.17      A    C  
ANISOU  960  CG  LEU A 124      579   3508   1676    562   -186   -322  A    C  
ATOM    961  CD1 LEU A 124      18.275   6.891  10.947  1.00 18.57      A    C  
ANISOU  961  CD1 LEU A 124     1288   3528   2240    612   -230   -216  A    C  
ATOM    962  CD2 LEU A 124      16.574   8.036   9.516  1.00 14.35      A    C  
ANISOU  962  CD2 LEU A 124      265   3607   1580    196    -57   -434  A    C  
ATOM    963  N   ALA A 125      18.926  11.044  13.103  1.00 12.04      A    N  
ANISOU  963  N   ALA A 125      260   2514   1800    123      8    -65  A    N  
ATOM    964  CA  ALA A 125      20.114  11.918  13.069  1.00 12.17      A    C  
ANISOU  964  CA  ALA A 125      256   2657   1710     93      3     20  A    C  
ATOM    965  C   ALA A 125      21.047  11.590  14.229  1.00 12.85      A    C  
ANISOU  965  C   ALA A 125      276   2946   1659    247     -5     -7  A    C  
ATOM    966  O   ALA A 125      22.278  11.475  14.042  1.00 14.23      A    O  
ANISOU  966  O   ALA A 125      311   3140   1957    388     91    -27  A    O  
ATOM    967  CB  ALA A 125      19.714  13.372  13.172  1.00 12.67      A    C  
ANISOU  967  CB  ALA A 125      254   2576   1982     43    -21    -38  A    C  
ATOM    968  N   TYR A 126      20.511  11.391  15.416  1.00 12.97      A    N  
ANISOU  968  N   TYR A 126      311   3084   1532    401     -6    107  A    N  
ATOM    969  CA  TYR A 126      21.338  11.075  16.584  1.00 13.85      A    C  
ANISOU  969  CA  TYR A 126      434   3215   1615    553     -5      0  A    C  
ATOM    970  C   TYR A 126      22.086   9.791  16.323  1.00 14.71      A    C  
ANISOU  970  C   TYR A 126      434   3305   1852    636    -31   -137  A    C  
ATOM    971  O   TYR A 126      23.318   9.728  16.511  1.00 16.15      A    O  
ANISOU  971  O   TYR A 126      408   3718   2011    727   -119   -304  A    O  
ATOM    972  CB  TYR A 126      20.478  10.957  17.838  1.00 14.61      A    C  
ANISOU  972  CB  TYR A 126      663   3395   1492    697      6     46  A    C  
ATOM    973  CG  TYR A 126      21.262  10.603  19.091  1.00 14.93      A    C  
ANISOU  973  CG  TYR A 126      692   3339   1640    916   -197     19  A    C  
ATOM    974  CD1 TYR A 126      22.457  11.257  19.403  1.00 17.35      A    C  
ANISOU  974  CD1 TYR A 126      944   3734   1914    856   -362   -186  A    C  
ATOM    975  CD2 TYR A 126      20.819   9.622  19.967  1.00 16.21      A    C  
ANISOU  975  CD2 TYR A 126      974   3501   1685   1115   -109    120  A    C  
ATOM    976  CE1 TYR A 126      23.173  10.933  20.555  1.00 18.35      A    C  
ANISOU  976  CE1 TYR A 126     1316   4007   1650   1067   -394    -82  A    C  
ATOM    977  CE2 TYR A 126      21.529   9.294  21.124  1.00 18.23      A    C  
ANISOU  977  CE2 TYR A 126     1360   3783   1782   1120   -115    115  A    C  
ATOM    978  CZ  TYR A 126      22.709   9.953  21.421  1.00 18.75      A    C  
ANISOU  978  CZ  TYR A 126     1421   4011   1692   1111   -292   -142  A    C  
ATOM    979  OH  TYR A 126      23.425   9.622  22.559  1.00 22.28      A    O  
ANISOU  979  OH  TYR A 126     1624   4874   1967   1216   -337      6  A    O  
ATOM    980  N   LEU A 127      21.388   8.746  15.890  1.00 14.44      A    N  
ANISOU  980  N   LEU A 127      419   3224   1844    701    -41   -129  A    N  
ATOM    981  CA  LEU A 127      22.063   7.468  15.662  1.00 15.89      A    C  
ANISOU  981  CA  LEU A 127      832   3185   2020    706     31    -93  A    C  
ATOM    982  C   LEU A 127      23.111   7.561  14.560  1.00 14.84      A    C  
ANISOU  982  C   LEU A 127      518   3046   2073    744    -48   -153  A    C  
ATOM    983  O   LEU A 127      24.214   6.999  14.710  1.00 16.30      A    O  
ANISOU  983  O   LEU A 127      553   3287   2354    922   -219    -74  A    O  
ATOM    984  CB  LEU A 127      21.048   6.365  15.381  1.00 16.30      A    C  
ANISOU  984  CB  LEU A 127      848   3192   2152    700     91    -34  A    C  
ATOM    985  CG  LEU A 127      20.119   6.037  16.561  1.00 19.19      A    C  
ANISOU  985  CG  LEU A 127     1324   3650   2317    731    348     98  A    C  
ATOM    986  CD1 LEU A 127      19.009   5.105  16.128  1.00 22.03      A    C  
ANISOU  986  CD1 LEU A 127     1659   3670   3041    627    553      6  A    C  
ATOM    987  CD2 LEU A 127      20.897   5.437  17.738  1.00 23.27      A    C  
ANISOU  987  CD2 LEU A 127     1993   4192   2657    832    485    390  A    C  
ATOM    988  N   MET A 128      22.831   8.288  13.484  1.00 14.87      A    N  
ANISOU  988  N   MET A 128      394   3255   2000    649    -46   -227  A    N  
ATOM    989  CA  MET A 128      23.828   8.464  12.435  1.00 15.33      A    C  
ANISOU  989  CA  MET A 128      497   3300   2029    465    -49   -373  A    C  
ATOM    990  C   MET A 128      25.027   9.207  13.017  1.00 15.53      A    C  
ANISOU  990  C   MET A 128      342   3418   2140    527    -51   -516  A    C  
ATOM    991  O   MET A 128      26.198   8.886  12.671  1.00 17.14      A    O  
ANISOU  991  O   MET A 128      390   3842   2280    684    -26   -684  A    O  
ATOM    992  CB  MET A 128      23.271   9.259  11.254  1.00 14.71      A    C  
ANISOU  992  CB  MET A 128      311   3258   2020    417    -35   -285  A    C  
ATOM    993  CG  MET A 128      22.174   8.552  10.453  1.00 15.33      A    C  
ANISOU  993  CG  MET A 128      260   3425   2140    116    -77   -254  A    C  
ATOM    994  SD  MET A 128      22.579   6.918   9.816  1.00 15.80      A    S  
ANISOU  994  SD  MET A 128      304   3413   2286    263     43   -215  A    S  
ATOM    995  CE  MET A 128      23.885   7.300   8.613  1.00 17.51      A    C  
ANISOU  995  CE  MET A 128      399   3573   2682    148    274   -162  A    C  
ATOM    996  N   SER A 129      24.796  10.180  13.884  1.00 16.25      A    N  
ANISOU  996  N   SER A 129      348   3594   2231    555   -164   -658  A    N  
ATOM    997  CA  SER A 129      25.874  11.029  14.410  1.00 18.04      A    C  
ANISOU  997  CA  SER A 129      456   3968   2430    604   -285   -797  A    C  
ATOM    998  C   SER A 129      26.783  10.204  15.299  1.00 19.20      A    C  
ANISOU  998  C   SER A 129      427   4280   2587    798   -324   -744  A    C  
ATOM    999  O   SER A 129      27.987  10.494  15.396  1.00 21.59      A    O  
ANISOU  999  O   SER A 129      375   4781   3048    666   -366   -794  A    O  
ATOM   1000  CB  SER A 129      25.347  12.239  15.192  1.00 17.67      A    C  
ANISOU 1000  CB  SER A 129      359   3925   2428    563   -326   -864  A    C  
ATOM   1001  OG  SER A 129      24.861  11.875  16.477  1.00 20.04      A    O  
ANISOU 1001  OG  SER A 129      353   4695   2567    656   -195   -807  A    O  
ATOM   1002  N   LYS A 130      26.229   9.181  15.942  1.00 20.20      A    N  
ANISOU 1002  N   LYS A 130      568   4514   2592   1110   -395   -606  A    N  
ATOM   1003  CA  LYS A 130      26.978   8.364  16.895  1.00 22.76      A    C  
ANISOU 1003  CA  LYS A 130     1168   4820   2657   1421   -386   -640  A    C  
ATOM   1004  C   LYS A 130      27.735   7.264  16.173  1.00 22.13      A    C  
ANISOU 1004  C   LYS A 130      864   4760   2786   1359   -315   -653  A    C  
ATOM   1005  O   LYS A 130      28.651   6.665  16.747  1.00 22.88      A    O  
ANISOU 1005  O   LYS A 130      752   4935   3007   1492   -414   -557  A    O  
ATOM   1006  CB  LYS A 130      26.025   7.767  17.935  1.00 24.04      A    C  
ANISOU 1006  CB  LYS A 130     1544   5095   2495   1544   -361   -568  A    C  
ATOM   1007  CG  LYS A 130      25.729   8.687  19.102  1.00 29.75      A    C  
ANISOU 1007  CG  LYS A 130     2416   6050   2836   2002   -487   -913  A    C  
ATOM   1008  CD  LYS A 130      26.651   8.383  20.288  1.00 38.03      A    C  
ANISOU 1008  CD  LYS A 130     3700   7458   3291   2257   -631  -1482  A    C  
ATOM   1009  CE  LYS A 130      26.523   9.404  21.408  1.00 41.31      A    C  
ANISOU 1009  CE  LYS A 130     4099   7746   3851   2404   -608  -1826  A    C  
ATOM   1010  NZ  LYS A 130      27.609  10.435  21.343  1.00 44.20      A    N1+
ANISOU 1010  NZ  LYS A 130     4663   7846   4284   2345   -326  -2016  A    N1+
ATOM   1011  N   ASN A 131      27.379   6.998  14.920  1.00 21.56      A    N  
ANISOU 1011  N   ASN A 131      640   4726   2827   1315   -229   -750  A    N  
ATOM   1012  CA  ASN A 131      28.062   5.957  14.152  1.00 21.38      A    C  
ANISOU 1012  CA  ASN A 131      661   4650   2811   1132   -153   -719  A    C  
ATOM   1013  C   ASN A 131      29.427   6.410  13.661  1.00 20.85      A    C  
ANISOU 1013  C   ASN A 131      601   4508   2813   1115   -274   -590  A    C  
ATOM   1014  O   ASN A 131      29.512   7.325  12.842  1.00 21.40      A    O  
ANISOU 1014  O   ASN A 131      562   4591   2976   1055   -472   -403  A    O  
ATOM   1015  CB  ASN A 131      27.216   5.516  12.954  1.00 20.91      A    C  
ANISOU 1015  CB  ASN A 131      544   4627   2775   1111    -54   -762  A    C  
ATOM   1016  CG  ASN A 131      28.009   4.668  11.969  1.00 20.44      A    C  
ANISOU 1016  CG  ASN A 131      493   4318   2953    955     25   -736  A    C  
ATOM   1017  ND2 ASN A 131      27.997   5.062  10.700  1.00 20.89      A    N  
ANISOU 1017  ND2 ASN A 131      368   4672   2899    649    120   -671  A    N  
ATOM   1018  OD1 ASN A 131      28.637   3.679  12.354  1.00 22.84      A    O  
ANISOU 1018  OD1 ASN A 131     1129   4140   3409    715     38   -825  A    O  
ATOM   1019  N   LYS A 132      30.484   5.754  14.159  1.00 20.37      A    N  
ANISOU 1019  N   LYS A 132      500   4329   2910    983   -272   -483  A    N  
ATOM   1020  CA  LYS A 132      31.873   6.003  13.735  1.00 20.99      A    C  
ANISOU 1020  CA  LYS A 132      527   4286   3163    908   -274   -604  A    C  
ATOM   1021  C   LYS A 132      32.470   4.767  13.052  1.00 20.29      A    C  
ANISOU 1021  C   LYS A 132      518   4158   3034   1000   -262   -439  A    C  
ATOM   1022  O   LYS A 132      33.600   4.807  12.531  1.00 22.30      A    O  
ANISOU 1022  O   LYS A 132      848   4350   3276    974    -19   -377  A    O  
ATOM   1023  CB  LYS A 132      32.731   6.401  14.940  1.00 22.10      A    C  
ANISOU 1023  CB  LYS A 132      706   4370   3321    832   -322   -662  A    C  
ATOM   1024  CG  LYS A 132      32.185   7.560  15.761  1.00 26.75      A    C  
ANISOU 1024  CG  LYS A 132     1412   4798   3953    498   -450  -1212  A    C  
ATOM   1025  CD  LYS A 132      33.124   7.939  16.890  1.00 34.43      A    C  
ANISOU 1025  CD  LYS A 132     2791   5482   4809    153   -441  -1534  A    C  
ATOM   1026  CE  LYS A 132      33.815   9.268  16.603  1.00 38.65      A    C  
ANISOU 1026  CE  LYS A 132     3495   5881   5310     23   -208  -1586  A    C  
ATOM   1027  NZ  LYS A 132      34.854   9.568  17.634  1.00 41.36      A    N1+
ANISOU 1027  NZ  LYS A 132     3948   6168   5598     31    -52  -1430  A    N1+
ATOM   1028  N   GLU A 133      31.713   3.670  13.068  1.00 21.01      A    N  
ANISOU 1028  N   GLU A 133      743   4214   3025   1067   -337   -571  A    N  
ATOM   1029  CA  GLU A 133      32.227   2.344  12.714  1.00 21.55      A    C  
ANISOU 1029  CA  GLU A 133      864   4280   3043   1180   -505   -627  A    C  
ATOM   1030  C   GLU A 133      31.814   1.881  11.319  1.00 21.18      A    C  
ANISOU 1030  C   GLU A 133      719   4311   3018   1312   -456   -675  A    C  
ATOM   1031  O   GLU A 133      32.641   1.338  10.570  1.00 22.64      A    O  
ANISOU 1031  O   GLU A 133      898   4487   3219   1303   -373   -768  A    O  
ATOM   1032  CB  GLU A 133      31.763   1.299  13.737  1.00 22.57      A    C  
ANISOU 1032  CB  GLU A 133     1112   4435   3030   1221   -493   -549  A    C  
ATOM   1033  CG  GLU A 133      32.320   1.477  15.141  1.00 23.21      A    C  
ANISOU 1033  CG  GLU A 133      903   4758   3156   1348   -603   -640  A    C  
ATOM   1034  CD  GLU A 133      33.593   0.682  15.369  1.00 23.54      A    C  
ANISOU 1034  CD  GLU A 133      798   5120   3027   1316   -230   -913  A    C  
ATOM   1035  OE1 GLU A 133      33.731  -0.408  14.781  1.00 26.77      A    O  
ANISOU 1035  OE1 GLU A 133     1225   5303   3643   1588   -542   -970  A    O  
ATOM   1036  OE2 GLU A 133      34.435   1.145  16.159  1.00 22.31      A    O1-
ANISOU 1036  OE2 GLU A 133      439   4586   3452    831   -393   -568  A    O1-
ATOM   1037  N   SER A 134      30.537   2.075  10.986  1.00 20.85      A    N  
ANISOU 1037  N   SER A 134      588   4257   3077   1054   -390   -688  A    N  
ATOM   1038  CA  SER A 134      29.943   1.431   9.817  1.00 21.39      A    C  
ANISOU 1038  CA  SER A 134      621   4508   3000    864   -164   -630  A    C  
ATOM   1039  C   SER A 134      29.787   2.371   8.627  1.00 20.53      A    C  
ANISOU 1039  C   SER A 134      427   4494   2881    841    -10   -709  A    C  
ATOM   1040  O   SER A 134      29.643   3.576   8.810  1.00 20.50      A    O  
ANISOU 1040  O   SER A 134      428   4582   2779    858    -28   -696  A    O  
ATOM   1041  CB  SER A 134      28.569   0.864  10.215  1.00 21.71      A    C  
ANISOU 1041  CB  SER A 134      688   4539   3021    702   -204   -535  A    C  
ATOM   1042  OG  SER A 134      28.680  -0.130  11.229  1.00 26.07      A    O  
ANISOU 1042  OG  SER A 134     1191   5216   3497    640    -87   -197  A    O  
ATOM   1043  N   LEU A 135      29.814   1.826   7.412  1.00 20.77      A    N  
ANISOU 1043  N   LEU A 135      456   4519   2915    784     49   -749  A    N  
ATOM   1044  CA  LEU A 135      29.584   2.638   6.214  1.00 20.53      A    C  
ANISOU 1044  CA  LEU A 135      456   4503   2842    680    219   -719  A    C  
ATOM   1045  C   LEU A 135      28.234   3.331   6.363  1.00 18.80      A    C  
ANISOU 1045  C   LEU A 135      306   4106   2730    386    135   -487  A    C  
ATOM   1046  O   LEU A 135      27.245   2.658   6.610  1.00 18.79      A    O  
ANISOU 1046  O   LEU A 135      480   3937   2721    274    108   -361  A    O  
ATOM   1047  CB  LEU A 135      29.598   1.776   4.943  1.00 22.63      A    C  
ANISOU 1047  CB  LEU A 135      776   4798   3025    658    193   -872  A    C  
ATOM   1048  CG  LEU A 135      30.868   0.957   4.693  1.00 27.13      A    C  
ANISOU 1048  CG  LEU A 135     1298   5403   3607    702    384  -1230  A    C  
ATOM   1049  CD1 LEU A 135      30.627  -0.114   3.643  1.00 30.37      A    C  
ANISOU 1049  CD1 LEU A 135     1949   5752   3837    803    293  -1419  A    C  
ATOM   1050  CD2 LEU A 135      32.035   1.858   4.284  1.00 31.32      A    C  
ANISOU 1050  CD2 LEU A 135     1527   6165   4208    496    397  -1474  A    C  
ATOM   1051  N   PRO A 136      28.205   4.660   6.233  1.00 17.99      A    N  
ANISOU 1051  N   PRO A 136      285   3935   2614    217    189   -310  A    N  
ATOM   1052  CA  PRO A 136      26.963   5.409   6.468  1.00 17.65      A    C  
ANISOU 1052  CA  PRO A 136      264   3844   2597    180     57   -245  A    C  
ATOM   1053  C   PRO A 136      25.777   4.871   5.677  1.00 17.43      A    C  
ANISOU 1053  C   PRO A 136      284   3896   2441     98      0   -164  A    C  
ATOM   1054  O   PRO A 136      24.676   4.794   6.234  1.00 17.20      A    O  
ANISOU 1054  O   PRO A 136      264   3727   2545    161     80   -208  A    O  
ATOM   1055  CB  PRO A 136      27.326   6.823   6.026  1.00 18.11      A    C  
ANISOU 1055  CB  PRO A 136      259   3856   2766    136    -41   -186  A    C  
ATOM   1056  CG  PRO A 136      28.777   6.924   6.339  1.00 18.68      A    C  
ANISOU 1056  CG  PRO A 136      260   3932   2906      0    138   -170  A    C  
ATOM   1057  CD  PRO A 136      29.357   5.561   6.024  1.00 18.65      A    C  
ANISOU 1057  CD  PRO A 136      276   4029   2781     90    220   -331  A    C  
ATOM   1058  N   MET A 137      25.964   4.503   4.413  1.00 17.90      A    N  
ANISOU 1058  N   MET A 137      331   4077   2395    -15    -43   -170  A    N  
ATOM   1059  CA  MET A 137      24.809   4.032   3.613  1.00 19.83      A    C  
ANISOU 1059  CA  MET A 137      734   4419   2381   -142    -57   -153  A    C  
ATOM   1060  C   MET A 137      24.192   2.783   4.245  1.00 18.70      A    C  
ANISOU 1060  C   MET A 137      579   4018   2509     57    148   -296  A    C  
ATOM   1061  O   MET A 137      22.962   2.652   4.356  1.00 18.80      A    O  
ANISOU 1061  O   MET A 137      460   3971   2712    109    208   -384  A    O  
ATOM   1062  CB  MET A 137      25.214   3.765   2.159  1.00 22.36      A    C  
ANISOU 1062  CB  MET A 137     1307   4888   2301   -340   -174   -120  A    C  
ATOM   1063  CG  MET A 137      24.155   2.988   1.399  1.00 27.32      A    C  
ANISOU 1063  CG  MET A 137     2117   5799   2465   -706   -230   -153  A    C  
ATOM   1064  SD  MET A 137      24.675   2.420  -0.217  0.50 31.00      A    S  
ANISOU 1064  SD  MET A 137     3253   5971   2554   -856   -107   -315  A    S  
ATOM   1065  CE  MET A 137      26.432   2.167   0.041  1.00 34.11      A    C  
ANISOU 1065  CE  MET A 137     3634   6610   2718   -837   -142   -401  A    C  
ATOM   1066  N   LEU A 138      25.037   1.857   4.686  1.00 19.23      A    N  
ANISOU 1066  N   LEU A 138      708   3822   2775    195    225   -359  A    N  
ATOM   1067  CA  LEU A 138      24.575   0.610   5.278  1.00 19.86      A    C  
ANISOU 1067  CA  LEU A 138      939   3625   2982    410    357   -467  A    C  
ATOM   1068  C   LEU A 138      23.963   0.875   6.640  1.00 18.00      A    C  
ANISOU 1068  C   LEU A 138      601   3395   2845    410    271   -364  A    C  
ATOM   1069  O   LEU A 138      22.923   0.316   6.982  1.00 18.87      A    O  
ANISOU 1069  O   LEU A 138      697   3476   2996    263    324   -322  A    O  
ATOM   1070  CB  LEU A 138      25.727  -0.387   5.430  1.00 22.00      A    C  
ANISOU 1070  CB  LEU A 138     1254   3704   3400    540    518   -627  A    C  
ATOM   1071  CG  LEU A 138      26.264  -1.026   4.151  1.00 27.00      A    C  
ANISOU 1071  CG  LEU A 138     2184   4079   3995    688    925   -860  A    C  
ATOM   1072  CD1 LEU A 138      27.491  -1.871   4.474  1.00 31.02      A    C  
ANISOU 1072  CD1 LEU A 138     2657   4307   4823    961   1347  -1080  A    C  
ATOM   1073  CD2 LEU A 138      25.191  -1.887   3.498  1.00 31.25      A    C  
ANISOU 1073  CD2 LEU A 138     2985   4438   4449    649    952  -1132  A    C  
ATOM   1074  N   TYR A 139      24.602   1.735   7.432  1.00 17.45      A    N  
ANISOU 1074  N   TYR A 139      627   3343   2660    471     87   -219  A    N  
ATOM   1075  CA  TYR A 139      24.096   2.031   8.770  1.00 17.16      A    C  
ANISOU 1075  CA  TYR A 139      557   3433   2529    557    -63    -65  A    C  
ATOM   1076  C   TYR A 139      22.729   2.725   8.683  1.00 16.16      A    C  
ANISOU 1076  C   TYR A 139      460   3233   2448    434    -93      0  A    C  
ATOM   1077  O   TYR A 139      21.816   2.433   9.483  1.00 17.41      A    O  
ANISOU 1077  O   TYR A 139      571   3370   2675    386    -38     98  A    O  
ATOM   1078  CB  TYR A 139      25.103   2.868   9.579  1.00 18.01      A    C  
ANISOU 1078  CB  TYR A 139      719   3713   2412    584   -152     19  A    C  
ATOM   1079  CG  TYR A 139      24.776   2.836  11.054  1.00 18.44      A    C  
ANISOU 1079  CG  TYR A 139      597   4065   2345    610   -175    109  A    C  
ATOM   1080  CD1 TYR A 139      24.939   1.656  11.787  1.00 20.16      A    C  
ANISOU 1080  CD1 TYR A 139      864   4352   2442    538   -174    322  A    C  
ATOM   1081  CD2 TYR A 139      24.296   3.959  11.716  1.00 18.37      A    C  
ANISOU 1081  CD2 TYR A 139      329   4244   2406    511   -150      0  A    C  
ATOM   1082  CE1 TYR A 139      24.621   1.608  13.133  1.00 22.71      A    C  
ANISOU 1082  CE1 TYR A 139     1747   4415   2465    531   -219    197  A    C  
ATOM   1083  CE2 TYR A 139      23.987   3.925  13.078  1.00 20.44      A    C  
ANISOU 1083  CE2 TYR A 139      900   4345   2522    522    -59    -15  A    C  
ATOM   1084  CZ  TYR A 139      24.141   2.743  13.775  1.00 21.59      A    C  
ANISOU 1084  CZ  TYR A 139     1421   4377   2407    384   -241     40  A    C  
ATOM   1085  OH  TYR A 139      23.835   2.684  15.109  1.00 24.93      A    O  
ANISOU 1085  OH  TYR A 139     2108   4634   2730    269    -82     43  A    O  
ATOM   1086  N   PHE A 140      22.583   3.646   7.737  1.00 15.12      A    N  
ANISOU 1086  N   PHE A 140      291   2996   2458    252   -126     31  A    N  
ATOM   1087  CA  PHE A 140      21.316   4.355   7.511  1.00 13.71      A    C  
ANISOU 1087  CA  PHE A 140      285   2739   2187     76   -153     10  A    C  
ATOM   1088  C   PHE A 140      20.213   3.358   7.200  1.00 13.51      A    C  
ANISOU 1088  C   PHE A 140      346   2750   2037      0    -76    -26  A    C  
ATOM   1089  O   PHE A 140      19.125   3.416   7.789  1.00 14.09      A    O  
ANISOU 1089  O   PHE A 140      262   2949   2142     96     98      6  A    O  
ATOM   1090  CB  PHE A 140      21.468   5.343   6.349  1.00 14.06      A    C  
ANISOU 1090  CB  PHE A 140      269   2829   2242     27   -173     99  A    C  
ATOM   1091  CG  PHE A 140      20.162   5.931   5.859  1.00 13.37      A    C  
ANISOU 1091  CG  PHE A 140      256   2838   1987     14    -71    -17  A    C  
ATOM   1092  CD1 PHE A 140      19.494   6.919   6.589  1.00 13.62      A    C  
ANISOU 1092  CD1 PHE A 140      260   2842   2071     14   -110    -89  A    C  
ATOM   1093  CD2 PHE A 140      19.632   5.489   4.648  1.00 14.76      A    C  
ANISOU 1093  CD2 PHE A 140      408   3165   2037    -74    -96   -130  A    C  
ATOM   1094  CE1 PHE A 140      18.279   7.465   6.105  1.00 14.25      A    C  
ANISOU 1094  CE1 PHE A 140      322   3106   1985     65     82     24  A    C  
ATOM   1095  CE2 PHE A 140      18.435   6.006   4.173  1.00 16.06      A    C  
ANISOU 1095  CE2 PHE A 140      900   3041   2161     46   -259    -35  A    C  
ATOM   1096  CZ  PHE A 140      17.766   6.991   4.909  1.00 15.32      A    C  
ANISOU 1096  CZ  PHE A 140      719   2985   2117    -27     65     20  A    C  
ATOM   1097  N   LEU A 141      20.451   2.436   6.279  1.00 13.80      A    N  
ANISOU 1097  N   LEU A 141      460   2621   2161    -49    -43    -62  A    N  
ATOM   1098  CA  LEU A 141      19.422   1.449   5.940  1.00 14.71      A    C  
ANISOU 1098  CA  LEU A 141      597   2569   2425    -60     20    -65  A    C  
ATOM   1099  C   LEU A 141      19.090   0.554   7.131  1.00 15.68      A    C  
ANISOU 1099  C   LEU A 141      577   2736   2644      0     86     86  A    C  
ATOM   1100  O   LEU A 141      17.926   0.233   7.387  1.00 16.70      A    O  
ANISOU 1100  O   LEU A 141      483   2858   3005   -114    219      5  A    O  
ATOM   1101  CB  LEU A 141      19.823   0.601   4.731  1.00 15.68      A    C  
ANISOU 1101  CB  LEU A 141      776   2648   2533   -137    104   -175  A    C  
ATOM   1102  CG  LEU A 141      19.924   1.383   3.411  1.00 17.12      A    C  
ANISOU 1102  CG  LEU A 141      912   2912   2680    109    175   -175  A    C  
ATOM   1103  CD1 LEU A 141      20.446   0.468   2.325  1.00 19.02      A    C  
ANISOU 1103  CD1 LEU A 141      926   3370   2930     35    461   -467  A    C  
ATOM   1104  CD2 LEU A 141      18.568   1.985   3.011  1.00 19.10      A    C  
ANISOU 1104  CD2 LEU A 141      802   3179   3276    -38     31   -109  A    C  
ATOM   1105  N   TYR A 142      20.119   0.141   7.871  1.00 16.82      A    N  
ANISOU 1105  N   TYR A 142      716   2890   2786    225     86    284  A    N  
ATOM   1106  CA  TYR A 142      19.924  -0.708   9.033  1.00 18.61      A    C  
ANISOU 1106  CA  TYR A 142     1035   3115   2921    410    175    397  A    C  
ATOM   1107  C   TYR A 142      19.088  -0.011  10.102  1.00 18.24      A    C  
ANISOU 1107  C   TYR A 142     1057   3037   2836    313    164    320  A    C  
ATOM   1108  O   TYR A 142      18.099  -0.594  10.595  1.00 19.04      A    O  
ANISOU 1108  O   TYR A 142      986   3059   3188    173    322    296  A    O  
ATOM   1109  CB  TYR A 142      21.268  -1.174   9.631  1.00 20.94      A    C  
ANISOU 1109  CB  TYR A 142     1366   3431   3158    688    186    644  A    C  
ATOM   1110  CG  TYR A 142      21.042  -1.905  10.940  1.00 25.78      A    C  
ANISOU 1110  CG  TYR A 142     2002   4178   3616   1194    450   1118  A    C  
ATOM   1111  CD1 TYR A 142      20.528  -3.201  10.929  1.00 31.30      A    C  
ANISOU 1111  CD1 TYR A 142     3003   4584   4307   1439    847   1571  A    C  
ATOM   1112  CD2 TYR A 142      21.289  -1.307  12.173  1.00 31.06      A    C  
ANISOU 1112  CD2 TYR A 142     2973   4989   3840   1606    595   1473  A    C  
ATOM   1113  CE1 TYR A 142      20.287  -3.890  12.110  1.00 35.87      A    C  
ANISOU 1113  CE1 TYR A 142     3901   5113   4616   1500   1124   1825  A    C  
ATOM   1114  CE2 TYR A 142      21.049  -1.990  13.365  1.00 35.28      A    C  
ANISOU 1114  CE2 TYR A 142     3828   5414   4162   1694   1000   1720  A    C  
ATOM   1115  CZ  TYR A 142      20.550  -3.282  13.323  1.00 37.19      A    C  
ANISOU 1115  CZ  TYR A 142     4147   5478   4505   1648   1313   1869  A    C  
ATOM   1116  OH  TYR A 142      20.309  -3.976  14.488  1.00 40.20      A    O  
ANISOU 1116  OH  TYR A 142     4623   5849   4802   1756   1553   1897  A    O  
ATOM   1117  N   VAL A 143      19.474   1.204  10.472  1.00 17.65      A    N  
ANISOU 1117  N   VAL A 143      794   3113   2800    270    164    120  A    N  
ATOM   1118  CA  VAL A 143      18.756   1.932  11.523  1.00 17.14      A    C  
ANISOU 1118  CA  VAL A 143      684   3359   2469    153     71     43  A    C  
ATOM   1119  C   VAL A 143      17.327   2.216  11.051  1.00 15.15      A    C  
ANISOU 1119  C   VAL A 143      522   3021   2213      6    142     74  A    C  
ATOM   1120  O   VAL A 143      16.380   2.042  11.824  1.00 15.53      A    O  
ANISOU 1120  O   VAL A 143      666   3086   2150      6    185     31  A    O  
ATOM   1121  CB  VAL A 143      19.453   3.249  11.969  1.00 18.19      A    C  
ANISOU 1121  CB  VAL A 143      689   3625   2596    193    -31   -173  A    C  
ATOM   1122  CG1 VAL A 143      18.501   4.073  12.869  1.00 19.56      A    C  
ANISOU 1122  CG1 VAL A 143      850   3935   2646    196     17   -252  A    C  
ATOM   1123  CG2 VAL A 143      20.772   2.943  12.678  1.00 21.82      A    C  
ANISOU 1123  CG2 VAL A 143      948   4528   2813    241   -109   -109  A    C  
ATOM   1124  N   TYR A 144      17.185   2.656   9.796  1.00 14.00      A    N  
ANISOU 1124  N   TYR A 144      406   2845   2069     59     91     49  A    N  
ATOM   1125  CA  TYR A 144      15.871   2.990   9.271  1.00 13.74      A    C  
ANISOU 1125  CA  TYR A 144      479   2651   2090    -24    148    -74  A    C  
ATOM   1126  C   TYR A 144      14.945   1.790   9.412  1.00 13.79      A    C  
ANISOU 1126  C   TYR A 144      666   2624   1949    -71    340   -164  A    C  
ATOM   1127  O   TYR A 144      13.857   1.878  10.008  1.00 14.34      A    O  
ANISOU 1127  O   TYR A 144      392   2879   2178    -71    386   -237  A    O  
ATOM   1128  CB  TYR A 144      15.936   3.480   7.800  1.00 13.42      A    C  
ANISOU 1128  CB  TYR A 144      269   2770   2060     -1    171    -18  A    C  
ATOM   1129  CG  TYR A 144      14.523   3.844   7.396  1.00 13.58      A    C  
ANISOU 1129  CG  TYR A 144      269   2969   1920     45    156   -174  A    C  
ATOM   1130  CD1 TYR A 144      14.017   5.083   7.783  1.00 13.87      A    C  
ANISOU 1130  CD1 TYR A 144      333   2944   1992    250     82   -129  A    C  
ATOM   1131  CD2 TYR A 144      13.695   2.960   6.714  1.00 15.46      A    C  
ANISOU 1131  CD2 TYR A 144      300   3373   2201    375      0   -496  A    C  
ATOM   1132  CE1 TYR A 144      12.713   5.435   7.488  1.00 15.53      A    C  
ANISOU 1132  CE1 TYR A 144      593   3359   1949    450    -68   -241  A    C  
ATOM   1133  CE2 TYR A 144      12.370   3.310   6.411  1.00 16.21      A    C  
ANISOU 1133  CE2 TYR A 144      291   3607   2258    355    -63   -688  A    C  
ATOM   1134  CZ  TYR A 144      11.901   4.549   6.804  1.00 14.83      A    C  
ANISOU 1134  CZ  TYR A 144      405   3328   1903    296    -93   -335  A    C  
ATOM   1135  OH  TYR A 144      10.597   4.909   6.522  1.00 18.25      A    O  
ANISOU 1135  OH  TYR A 144      304   4056   2574    362   -241   -564  A    O  
ATOM   1136  N   HIS A 145      15.340   0.671   8.824  1.00 14.69      A    N  
ANISOU 1136  N   HIS A 145      917   2502   2161   -175    480   -228  A    N  
ATOM   1137  CA  HIS A 145      14.439  -0.485   8.772  1.00 16.21      A    C  
ANISOU 1137  CA  HIS A 145     1254   2517   2389   -184    653   -230  A    C  
ATOM   1138  C   HIS A 145      14.230  -1.155  10.117  1.00 17.03      A    C  
ANISOU 1138  C   HIS A 145     1316   2687   2469   -184    772   -151  A    C  
ATOM   1139  O   HIS A 145      13.114  -1.596  10.417  1.00 18.52      A    O  
ANISOU 1139  O   HIS A 145     1360   2908   2768   -362    913   -219  A    O  
ATOM   1140  CB  HIS A 145      14.882  -1.466   7.688  1.00 16.78      A    C  
ANISOU 1140  CB  HIS A 145     1392   2560   2422   -305    631   -335  A    C  
ATOM   1141  CG  HIS A 145      14.593  -0.951   6.318  1.00 18.16      A    C  
ANISOU 1141  CG  HIS A 145     1509   2869   2522   -318    489   -377  A    C  
ATOM   1142  CD2 HIS A 145      15.420  -0.580   5.306  1.00 18.79      A    C  
ANISOU 1142  CD2 HIS A 145     1576   3088   2477   -511    355   -296  A    C  
ATOM   1143  ND1 HIS A 145      13.314  -0.734   5.858  1.00 19.58      A    N  
ANISOU 1143  ND1 HIS A 145     1420   3217   2804   -405    386   -549  A    N  
ATOM   1144  CE1 HIS A 145      13.362  -0.258   4.621  1.00 20.03      A    C  
ANISOU 1144  CE1 HIS A 145     1594   3298   2718   -390    294   -548  A    C  
ATOM   1145  NE2 HIS A 145      14.632  -0.158   4.260  1.00 19.34      A    N  
ANISOU 1145  NE2 HIS A 145     1527   3402   2417   -463    229   -465  A    N  
ATOM   1146  N   SER A 146      15.269  -1.220  10.941  1.00 17.75      A    N  
ANISOU 1146  N   SER A 146     1473   2768   2504     73    776    -54  A    N  
ATOM   1147  CA  SER A 146      15.132  -1.851  12.246  1.00 18.58      A    C  
ANISOU 1147  CA  SER A 146     1615   2763   2680    296    829     60  A    C  
ATOM   1148  C   SER A 146      14.224  -1.016  13.157  1.00 17.62      A    C  
ANISOU 1148  C   SER A 146     1532   2644   2520    102    939      0  A    C  
ATOM   1149  O   SER A 146      13.400  -1.583  13.884  1.00 18.70      A    O  
ANISOU 1149  O   SER A 146     1597   2815   2694    -48   1089     46  A    O  
ATOM   1150  CB  SER A 146      16.487  -2.131  12.901  1.00 20.01      A    C  
ANISOU 1150  CB  SER A 146     1835   2964   2802    428    715     87  A    C  
ATOM   1151  OG  SER A 146      17.208  -0.939  13.151  1.00 22.64      A    O  
ANISOU 1151  OG  SER A 146     1851   3357   3393    511    478     98  A    O  
ATOM   1152  N   MET A 147      14.351   0.311  13.104  1.00 16.66      A    N  
ANISOU 1152  N   MET A 147     1177   2612   2540     74    763   -164  A    N  
ATOM   1153  CA  MET A 147      13.469   1.186  13.884  1.00 16.08      A    C  
ANISOU 1153  CA  MET A 147      873   2725   2513    -26    564   -252  A    C  
ATOM   1154  C   MET A 147      12.029   1.120  13.385  1.00 16.41      A    C  
ANISOU 1154  C   MET A 147      840   2933   2460   -153    599   -307  A    C  
ATOM   1155  O   MET A 147      11.078   1.118  14.172  1.00 17.64      A    O  
ANISOU 1155  O   MET A 147      891   3271   2542   -197    619   -357  A    O  
ATOM   1156  CB  MET A 147      13.964   2.638  13.845  1.00 16.00      A    C  
ANISOU 1156  CB  MET A 147      812   2716   2551      0    447   -237  A    C  
ATOM   1157  CG  MET A 147      15.200   2.944  14.702  1.00 18.11      A    C  
ANISOU 1157  CG  MET A 147      969   3260   2651    104    162   -184  A    C  
ATOM   1158  SD  MET A 147      14.935   2.658  16.481  1.00 24.07      A    S  
ANISOU 1158  SD  MET A 147     2442   4047   2655     31    119    -31  A    S  
ATOM   1159  CE  MET A 147      13.679   3.863  16.862  1.00 25.03      A    C  
ANISOU 1159  CE  MET A 147     1360   5788   2363    781    357   -293  A    C  
ATOM   1160  N   ARG A 148      11.863   1.082  12.074  1.00 16.68      A    N  
ANISOU 1160  N   ARG A 148      867   2975   2496   -219    568   -390  A    N  
ATOM   1161  CA  ARG A 148      10.523   1.031  11.499  1.00 17.53      A    C  
ANISOU 1161  CA  ARG A 148     1044   2978   2639   -271    560   -320  A    C  
ATOM   1162  C   ARG A 148       9.817  -0.274  11.854  1.00 18.40      A    C  
ANISOU 1162  C   ARG A 148     1224   2933   2833   -443    846   -480  A    C  
ATOM   1163  O   ARG A 148       8.603  -0.291  12.147  1.00 19.26      A    O  
ANISOU 1163  O   ARG A 148     1025   3296   2998   -489    979   -482  A    O  
ATOM   1164  CB  ARG A 148      10.582   1.214   9.982  1.00 17.34      A    C  
ANISOU 1164  CB  ARG A 148      943   3084   2560   -109    516   -322  A    C  
ATOM   1165  CG  ARG A 148       9.200   1.483   9.396  1.00 19.17      A    C  
ANISOU 1165  CG  ARG A 148     1000   3391   2894    -98    130   -241  A    C  
ATOM   1166  CD  ARG A 148       9.312   1.750   7.923  1.00 20.36      A    C  
ANISOU 1166  CD  ARG A 148     1071   3731   2935     76    -81   -428  A    C  
ATOM   1167  NE  ARG A 148       8.051   2.218   7.363  1.00 21.34      A    N  
ANISOU 1167  NE  ARG A 148      991   3973   3143   -153   -296   -500  A    N  
ATOM   1168  CZ  ARG A 148       7.118   1.429   6.852  1.00 23.26      A    C  
ANISOU 1168  CZ  ARG A 148     1604   4138   3095   -606    -63   -416  A    C  
ATOM   1169  NH1 ARG A 148       7.275   0.112   6.809  1.00 25.20      A    N1+
ANISOU 1169  NH1 ARG A 148     1976   4135   3463   -723    241   -340  A    N1+
ATOM   1170  NH2 ARG A 148       6.018   1.971   6.366  1.00 23.35      A    N  
ANISOU 1170  NH2 ARG A 148     1000   4888   2984   -588    -30   -353  A    N  
ATOM   1171  N   ASP A 149      10.565  -1.377  11.829  1.00 20.64      A    N  
ANISOU 1171  N   ASP A 149     1756   2851   3237   -606   1049   -568  A    N  
ATOM   1172  CA  ASP A 149      10.003  -2.677  12.192  1.00 23.37      A    C  
ANISOU 1172  CA  ASP A 149     2425   2930   3526   -653   1092   -540  A    C  
ATOM   1173  C   ASP A 149       9.552  -2.697  13.654  1.00 24.16      A    C  
ANISOU 1173  C   ASP A 149     2635   3109   3436   -656   1067   -294  A    C  
ATOM   1174  O   ASP A 149       8.533  -3.300  14.000  1.00 24.97      A    O  
ANISOU 1174  O   ASP A 149     2536   3458   3494   -696   1067   -186  A    O  
ATOM   1175  CB  ASP A 149      11.026  -3.788  11.927  1.00 24.80      A    C  
ANISOU 1175  CB  ASP A 149     2660   2874   3887   -706   1119   -627  A    C  
ATOM   1176  CG  ASP A 149      11.193  -4.102  10.447  1.00 27.73      A    C  
ANISOU 1176  CG  ASP A 149     2960   3143   4433   -702   1251   -900  A    C  
ATOM   1177  OD1 ASP A 149      10.468  -3.520   9.603  1.00 31.16      A    O  
ANISOU 1177  OD1 ASP A 149     3576   3734   4528   -741   1392   -806  A    O  
ATOM   1178  OD2 ASP A 149      12.064  -4.932  10.111  1.00 31.22      A    O1-
ANISOU 1178  OD2 ASP A 149     3100   3411   5353   -675   1579  -1225  A    O1-
ATOM   1179  N   LEU A 150      10.318  -2.014  14.500  1.00 23.53      A    N  
ANISOU 1179  N   LEU A 150     2533   3172   3237   -379   1000   -108  A    N  
ATOM   1180  CA  LEU A 150      10.049  -1.943  15.934  1.00 24.05      A    C  
ANISOU 1180  CA  LEU A 150     2691   3249   3197   -170    904     82  A    C  
ATOM   1181  C   LEU A 150       8.884  -1.018  16.269  1.00 23.69      A    C  
ANISOU 1181  C   LEU A 150     2508   3203   3289   -142   1058     24  A    C  
ATOM   1182  O   LEU A 150       8.024  -1.367  17.097  1.00 24.94      A    O  
ANISOU 1182  O   LEU A 150     2606   3486   3384   -114   1238    208  A    O  
ATOM   1183  CB  LEU A 150      11.308  -1.481  16.685  1.00 24.92      A    C  
ANISOU 1183  CB  LEU A 150     2942   3321   3206   -131    776     15  A    C  
ATOM   1184  CG  LEU A 150      11.201  -1.342  18.209  1.00 28.06      A    C  
ANISOU 1184  CG  LEU A 150     3790   3659   3212    -87    467    142  A    C  
ATOM   1185  CD1 LEU A 150      10.763  -2.651  18.860  1.00 30.46      A    C  
ANISOU 1185  CD1 LEU A 150     4370   3937   3267    -34    280    197  A    C  
ATOM   1186  CD2 LEU A 150      12.525  -0.851  18.774  1.00 30.45      A    C  
ANISOU 1186  CD2 LEU A 150     4359   3952   3257    -31    -10    204  A    C  
ATOM   1187  N   ARG A 151       8.844   0.146  15.629  1.00 21.55      A    N  
ANISOU 1187  N   ARG A 151     1949   3122   3118   -208    820   -259  A    N  
ATOM   1188  CA  ARG A 151       7.869   1.193  15.929  1.00 20.98      A    C  
ANISOU 1188  CA  ARG A 151     1641   3312   3018   -208    684   -571  A    C  
ATOM   1189  C   ARG A 151       6.575   1.066  15.132  1.00 20.63      A    C  
ANISOU 1189  C   ARG A 151     1351   3504   2985   -401    798   -688  A    C  
ATOM   1190  O   ARG A 151       5.533   1.491  15.625  1.00 22.41      A    O  
ANISOU 1190  O   ARG A 151     1339   3968   3206   -230    886   -851  A    O  
ATOM   1191  CB  ARG A 151       8.468   2.577  15.647  1.00 20.95      A    C  
ANISOU 1191  CB  ARG A 151     1483   3185   3291   -195    469   -643  A    C  
ATOM   1192  CG  ARG A 151       9.780   2.900  16.356  1.00 22.57      A    C  
ANISOU 1192  CG  ARG A 151     1606   3576   3395     51    324   -714  A    C  
ATOM   1193  CD  ARG A 151       9.551   3.568  17.691  1.00 21.03      A    C  
ANISOU 1193  CD  ARG A 151     1439   3677   2876    388    313   -390  A    C  
ATOM   1194  NE  ARG A 151       8.734   4.787  17.638  1.00 17.77      A    N  
ANISOU 1194  NE  ARG A 151     1050   3355   2347    208    472   -195  A    N  
ATOM   1195  CZ  ARG A 151       7.951   5.172  18.651  1.00 18.11      A    C  
ANISOU 1195  CZ  ARG A 151     1430   2991   2460   -208    571   -160  A    C  
ATOM   1196  NH1 ARG A 151       7.881   4.417  19.755  1.00 20.47      A    N1+
ANISOU 1196  NH1 ARG A 151     2178   3244   2356   -109    573   -120  A    N1+
ATOM   1197  NH2 ARG A 151       7.238   6.293  18.554  1.00 16.43      A    N  
ANISOU 1197  NH2 ARG A 151     1008   2980   2255   -175    573   -329  A    N  
ATOM   1198  N   GLY A 152       6.648   0.516  13.924  1.00 19.38      A    N  
ANISOU 1198  N   GLY A 152      992   3553   2818   -498    828   -635  A    N  
ATOM   1199  CA  GLY A 152       5.479   0.429  13.031  1.00 19.57      A    C  
ANISOU 1199  CA  GLY A 152      894   3698   2842   -636    675   -568  A    C  
ATOM   1200  C   GLY A 152       5.498   1.486  11.935  1.00 18.31      A    C  
ANISOU 1200  C   GLY A 152      612   3625   2720   -546    557   -621  A    C  
ATOM   1201  O   GLY A 152       5.059   1.234  10.807  1.00 19.75      A    O  
ANISOU 1201  O   GLY A 152      663   3984   2858   -679    460   -652  A    O  
ATOM   1202  N   ALA A 153       6.002   2.667  12.280  1.00 18.39      A    N  
ANISOU 1202  N   ALA A 153      571   3684   2732   -582    377   -498  A    N  
ATOM   1203  CA  ALA A 153       6.195   3.756  11.334  1.00 17.22      A    C  
ANISOU 1203  CA  ALA A 153      379   3562   2603   -445    208   -460  A    C  
ATOM   1204  C   ALA A 153       7.353   4.613  11.840  1.00 16.22      A    C  
ANISOU 1204  C   ALA A 153      439   3357   2365   -416    164   -430  A    C  
ATOM   1205  O   ALA A 153       7.494   4.820  13.042  1.00 17.23      A    O  
ANISOU 1205  O   ALA A 153      693   3553   2299   -505    262   -390  A    O  
ATOM   1206  CB  ALA A 153       4.921   4.591  11.201  1.00 18.59      A    C  
ANISOU 1206  CB  ALA A 153      421   3844   2797   -359    103   -483  A    C  
ATOM   1207  N   PHE A 154       8.178   5.104  10.921  1.00 15.01      A    N  
ANISOU 1207  N   PHE A 154      289   3177   2236   -315     90   -329  A    N  
ATOM   1208  CA  PHE A 154       9.435   5.761  11.289  1.00 13.87      A    C  
ANISOU 1208  CA  PHE A 154      267   2863   2140   -186     44   -205  A    C  
ATOM   1209  C   PHE A 154       9.854   6.618  10.107  1.00 13.36      A    C  
ANISOU 1209  C   PHE A 154      262   2828   1985   -150      8   -283  A    C  
ATOM   1210  O   PHE A 154      10.002   6.113   8.997  1.00 14.14      A    O  
ANISOU 1210  O   PHE A 154      263   2974   2134     -5    137   -345  A    O  
ATOM   1211  CB  PHE A 154      10.494   4.718  11.675  1.00 14.09      A    C  
ANISOU 1211  CB  PHE A 154      284   2949   2122   -153     96   -120  A    C  
ATOM   1212  CG  PHE A 154      11.793   5.307  12.167  1.00 13.49      A    C  
ANISOU 1212  CG  PHE A 154      465   2587   2073   -140    228   -135  A    C  
ATOM   1213  CD1 PHE A 154      11.868   5.965  13.390  1.00 12.71      A    C  
ANISOU 1213  CD1 PHE A 154      263   2453   2113   -136     55   -115  A    C  
ATOM   1214  CD2 PHE A 154      12.943   5.184  11.408  1.00 13.30      A    C  
ANISOU 1214  CD2 PHE A 154      320   2714   2019    -87    296    -71  A    C  
ATOM   1215  CE1 PHE A 154      13.064   6.499  13.844  1.00 13.66      A    C  
ANISOU 1215  CE1 PHE A 154      518   2565   2108     19    329   -160  A    C  
ATOM   1216  CE2 PHE A 154      14.143   5.715  11.859  1.00 13.17      A    C  
ANISOU 1216  CE2 PHE A 154      306   2648   2048    -65    305   -153  A    C  
ATOM   1217  CZ  PHE A 154      14.201   6.369  13.076  1.00 13.14      A    C  
ANISOU 1217  CZ  PHE A 154      333   2498   2159     -1    390    -57  A    C  
ATOM   1218  N   VAL A 155      10.039   7.909  10.358  1.00 13.22      A    N  
ANISOU 1218  N   VAL A 155      262   2851   1908   -146     43   -217  A    N  
ATOM   1219  CA  VAL A 155      10.333   8.875   9.307  1.00 13.67      A    C  
ANISOU 1219  CA  VAL A 155      264   3066   1862   -170     44    -87  A    C  
ATOM   1220  C   VAL A 155       9.734   8.571   7.940  1.00 14.04      A    C  
ANISOU 1220  C   VAL A 155      359   3131   1844   -181    131   -186  A    C  
ATOM   1221  O   VAL A 155      10.446   8.458   6.946  1.00 14.77      A    O  
ANISOU 1221  O   VAL A 155      259   3310   2044     -6    103   -190  A    O  
ATOM   1222  CB  VAL A 155      11.855   9.070   9.163  1.00 13.68      A    C  
ANISOU 1222  CB  VAL A 155      264   3177   1755   -164     59     17  A    C  
ATOM   1223  CG1 VAL A 155      12.149  10.387   8.469  1.00 15.32      A    C  
ANISOU 1223  CG1 VAL A 155      513   3300   2008    -98    142    163  A    C  
ATOM   1224  CG2 VAL A 155      12.524   9.024  10.530  1.00 14.09      A    C  
ANISOU 1224  CG2 VAL A 155      335   3174   1844   -131    120    -12  A    C  
ATOM   1225  N   GLU A 156       8.412   8.444   7.902  1.00 14.46      A    N  
ANISOU 1225  N   GLU A 156      258   3321   1914   -115    -17   -153  A    N  
ATOM   1226  CA  GLU A 156       7.692   8.304   6.643  1.00 15.42      A    C  
ANISOU 1226  CA  GLU A 156      265   3690   1903   -202      0   -258  A    C  
ATOM   1227  C   GLU A 156       7.804   9.525   5.733  1.00 15.40      A    C  
ANISOU 1227  C   GLU A 156      254   3779   1819    -57     -8   -201  A    C  
ATOM   1228  O   GLU A 156       7.679   9.413   4.516  1.00 17.35      A    O  
ANISOU 1228  O   GLU A 156      754   3901   1938    -93    -74   -195  A    O  
ATOM   1229  CB  GLU A 156       6.222   7.961   6.906  1.00 16.18      A    C  
ANISOU 1229  CB  GLU A 156      280   3822   2046   -307     35   -297  A    C  
ATOM   1230  CG  GLU A 156       6.019   6.853   7.929  1.00 17.90      A    C  
ANISOU 1230  CG  GLU A 156      472   3862   2467   -353     17   -346  A    C  
ATOM   1231  CD  GLU A 156       6.546   5.512   7.455  1.00 20.00      A    C  
ANISOU 1231  CD  GLU A 156      795   4032   2772   -439   -120   -526  A    C  
ATOM   1232  OE1 GLU A 156       6.276   5.140   6.296  1.00 22.40      A    O  
ANISOU 1232  OE1 GLU A 156      872   4598   3041   -388   -241   -763  A    O  
ATOM   1233  OE2 GLU A 156       7.228   4.824   8.244  1.00 19.97      A    O1-
ANISOU 1233  OE2 GLU A 156      752   4041   2793   -494    170   -461  A    O1-
ATOM   1234  N   ASN A 157       8.046  10.686   6.332  1.00 15.50      A    N  
ANISOU 1234  N   ASN A 157      254   3781   1853     45     27   -147  A    N  
ATOM   1235  CA  ASN A 157       8.144  11.946   5.589  1.00 15.38      A    C  
ANISOU 1235  CA  ASN A 157      263   3824   1758    118     88   -126  A    C  
ATOM   1236  C   ASN A 157       9.379  11.894   4.674  1.00 15.20      A    C  
ANISOU 1236  C   ASN A 157      295   3785   1694    175     38   -208  A    C  
ATOM   1237  O   ASN A 157      10.500  11.840   5.169  1.00 15.75      A    O  
ANISOU 1237  O   ASN A 157      262   4005   1717    182     -6   -131  A    O  
ATOM   1238  CB  ASN A 157       8.210  13.106   6.593  1.00 15.21      A    C  
ANISOU 1238  CB  ASN A 157      326   3761   1694    297    252    -63  A    C  
ATOM   1239  CG  ASN A 157       8.334  14.472   5.937  1.00 15.78      A    C  
ANISOU 1239  CG  ASN A 157      453   3785   1756    544    203    -17  A    C  
ATOM   1240  ND2 ASN A 157       7.773  15.479   6.606  1.00 15.67      A    N  
ANISOU 1240  ND2 ASN A 157      350   3813   1791    575     52   -136  A    N  
ATOM   1241  OD1 ASN A 157       8.961  14.633   4.883  1.00 18.14      A    O  
ANISOU 1241  OD1 ASN A 157     1005   3878   2008    535    537    103  A    O  
ATOM   1242  N   PRO A 158       9.185  11.852   3.349  1.00 16.48      A    N  
ANISOU 1242  N   PRO A 158      496   4142   1622    131      0   -115  A    N  
ATOM   1243  CA  PRO A 158      10.350  11.688   2.468  1.00 17.26      A    C  
ANISOU 1243  CA  PRO A 158      819   4088   1650    263    126    -76  A    C  
ATOM   1244  C   PRO A 158      11.292  12.887   2.459  1.00 16.34      A    C  
ANISOU 1244  C   PRO A 158      652   3855   1703    487    237    115  A    C  
ATOM   1245  O   PRO A 158      12.476  12.711   2.157  1.00 16.53      A    O  
ANISOU 1245  O   PRO A 158      427   3973   1879    588    151      5  A    O  
ATOM   1246  CB  PRO A 158       9.725  11.476   1.085  1.00 18.60      A    C  
ANISOU 1246  CB  PRO A 158     1007   4386   1676    226     87    -98  A    C  
ATOM   1247  CG  PRO A 158       8.367  12.086   1.179  1.00 19.58      A    C  
ANISOU 1247  CG  PRO A 158     1106   4623   1712    104   -153   -197  A    C  
ATOM   1248  CD  PRO A 158       7.910  11.913   2.595  1.00 16.77      A    C  
ANISOU 1248  CD  PRO A 158      577   4117   1676    115   -120    -20  A    C  
ATOM   1249  N   SER A 159      10.799  14.088   2.764  1.00 15.77      A    N  
ANISOU 1249  N   SER A 159      597   3709   1684    606    152    230  A    N  
ATOM   1250  CA ASER A 159      11.662  15.274   2.850  0.50 15.49      A    C  
ANISOU 1250  CA ASER A 159      636   3528   1720    634    216    364  A    C  
ATOM   1251  CA BSER A 159      11.675  15.252   2.822  0.50 15.30      A    C  
ANISOU 1251  CA BSER A 159      575   3560   1676    593    197    364  A    C  
ATOM   1252  C   SER A 159      12.608  15.170   4.038  1.00 14.66      A    C  
ANISOU 1252  C   SER A 159      544   3413   1612    621    219    218  A    C  
ATOM   1253  O   SER A 159      13.788  15.554   3.963  1.00 14.86      A    O  
ANISOU 1253  O   SER A 159      553   3303   1790    454    261    197  A    O  
ATOM   1254  CB ASER A 159      10.868  16.576   2.968  0.50 16.22      A    C  
ANISOU 1254  CB ASER A 159      708   3567   1886    640    219    452  A    C  
ATOM   1255  CB BSER A 159      10.847  16.538   2.793  0.50 15.89      A    C  
ANISOU 1255  CB BSER A 159      597   3625   1817    586    175    414  A    C  
ATOM   1256  OG ASER A 159      11.745  17.666   3.258  0.50 17.47      A    O  
ANISOU 1256  OG ASER A 159      750   3621   2266    820    342    469  A    O  
ATOM   1257  OG BSER A 159      10.100  16.606   1.579  0.50 15.63      A    O  
ANISOU 1257  OG BSER A 159      353   3655   1932    535    249    593  A    O  
ATOM   1258  N   PHE A 160      12.117  14.651   5.150  1.00 14.35      A    N  
ANISOU 1258  N   PHE A 160      500   3420   1534    540    205    175  A    N  
ATOM   1259  CA  PHE A 160      12.967  14.476   6.326  1.00 13.11      A    C  
ANISOU 1259  CA  PHE A 160      388   3127   1465    489    252     30  A    C  
ATOM   1260  C   PHE A 160      14.016  13.402   6.032  1.00 12.99      A    C  
ANISOU 1260  C   PHE A 160      318   2976   1641    335    171    -60  A    C  
ATOM   1261  O   PHE A 160      15.194  13.562   6.378  1.00 13.24      A    O  
ANISOU 1261  O   PHE A 160      287   3084   1659    290     79     68  A    O  
ATOM   1262  CB  PHE A 160      12.118  14.077   7.537  1.00 13.31      A    C  
ANISOU 1262  CB  PHE A 160      379   3185   1492    518    209     46  A    C  
ATOM   1263  CG  PHE A 160      11.265  15.195   8.104  1.00 13.56      A    C  
ANISOU 1263  CG  PHE A 160      337   3179   1634    469    115     80  A    C  
ATOM   1264  CD1 PHE A 160      11.256  16.472   7.546  1.00 14.65      A    C  
ANISOU 1264  CD1 PHE A 160      434   3183   1948    678    226    113  A    C  
ATOM   1265  CD2 PHE A 160      10.486  14.958   9.210  1.00 14.06      A    C  
ANISOU 1265  CD2 PHE A 160      366   3476   1500    474      6    -52  A    C  
ATOM   1266  CE1 PHE A 160      10.455  17.484   8.094  1.00 14.87      A    C  
ANISOU 1266  CE1 PHE A 160      560   3210   1879    634    137    196  A    C  
ATOM   1267  CE2 PHE A 160       9.680  15.952   9.758  1.00 13.77      A    C  
ANISOU 1267  CE2 PHE A 160      328   3416   1489    461     98     34  A    C  
ATOM   1268  CZ  PHE A 160       9.680  17.211   9.215  1.00 14.71      A    C  
ANISOU 1268  CZ  PHE A 160      372   3517   1699    617     92    219  A    C  
ATOM   1269  N   LYS A 161      13.616  12.306   5.389  1.00 12.88      A    N  
ANISOU 1269  N   LYS A 161      403   2752   1738    291    313    -76  A    N  
ATOM   1270  CA  LYS A 161      14.591  11.267   5.002  1.00 13.43      A    C  
ANISOU 1270  CA  LYS A 161      693   2594   1815    173    403     65  A    C  
ATOM   1271  C   LYS A 161      15.644  11.847   4.082  1.00 12.49      A    C  
ANISOU 1271  C   LYS A 161      579   2544   1624    241    285    151  A    C  
ATOM   1272  O   LYS A 161      16.840  11.547   4.243  1.00 12.93      A    O  
ANISOU 1272  O   LYS A 161      326   2689   1897    366    186    115  A    O  
ATOM   1273  CB  LYS A 161      13.931  10.072   4.319  1.00 14.32      A    C  
ANISOU 1273  CB  LYS A 161      805   2680   1956     24    518    -68  A    C  
ATOM   1274  CG  LYS A 161      13.158   9.217   5.300  1.00 18.69      A    C  
ANISOU 1274  CG  LYS A 161     1524   3095   2483   -364    656    -68  A    C  
ATOM   1275  CD  LYS A 161      12.722   7.915   4.699  1.00 21.76      A    C  
ANISOU 1275  CD  LYS A 161     1753   3445   3070   -653    575   -296  A    C  
ATOM   1276  CE  LYS A 161      11.544   8.133   3.784  1.00 24.97      A    C  
ANISOU 1276  CE  LYS A 161     1949   3822   3716   -759    259   -445  A    C  
ATOM   1277  NZ  LYS A 161      10.552   7.040   3.999  1.00 25.44      A    N1+
ANISOU 1277  NZ  LYS A 161     1500   3921   4246   -820    303   -666  A    N1+
ATOM   1278  N   ARG A 162      15.228  12.667   3.131  1.00 12.06      A    N  
ANISOU 1278  N   ARG A 162      438   2599   1544    153    226    274  A    N  
ATOM   1279  CA  ARG A 162      16.176  13.289   2.188  1.00 12.25      A    C  
ANISOU 1279  CA  ARG A 162      710   2524   1421     52    207    219  A    C  
ATOM   1280  C   ARG A 162      17.216  14.101   2.959  1.00 11.93      A    C  
ANISOU 1280  C   ARG A 162      540   2457   1536    194    263     24  A    C  
ATOM   1281  O   ARG A 162      18.417  14.040   2.656  1.00 12.93      A    O  
ANISOU 1281  O   ARG A 162      340   2829   1744    252    307     35  A    O  
ATOM   1282  CB  ARG A 162      15.455  14.215   1.215  1.00 12.87      A    C  
ANISOU 1282  CB  ARG A 162      864   2599   1427     86    218    320  A    C  
ATOM   1283  CG  ARG A 162      16.381  14.864   0.168  1.00 14.02      A    C  
ANISOU 1283  CG  ARG A 162     1086   2689   1553     98    263    438  A    C  
ATOM   1284  CD  ARG A 162      15.773  16.115  -0.432  1.00 16.03      A    C  
ANISOU 1284  CD  ARG A 162     1351   2621   2117    115    377    480  A    C  
ATOM   1285  NE  ARG A 162      15.878  17.258   0.484  1.00 16.82      A    N  
ANISOU 1285  NE  ARG A 162     1404   2685   2301    280    205    342  A    N  
ATOM   1286  CZ  ARG A 162      14.853  17.965   0.947  1.00 15.46      A    C  
ANISOU 1286  CZ  ARG A 162     1023   2781   2071     41     13    291  A    C  
ATOM   1287  NH1 ARG A 162      13.592  17.641   0.624  1.00 18.03      A    N1+
ANISOU 1287  NH1 ARG A 162      864   3379   2608    -65   -147    527  A    N1+
ATOM   1288  NH2 ARG A 162      15.065  18.987   1.752  1.00 17.65      A    N  
ANISOU 1288  NH2 ARG A 162     1676   3021   2008     15     17    164  A    N  
ATOM   1289  N   GLN A 163      16.770  14.861   3.951  1.00 12.32      A    N  
ANISOU 1289  N   GLN A 163      603   2417   1659    241    208   -113  A    N  
ATOM   1290  CA  GLN A 163      17.668  15.710   4.753  1.00 12.31      A    C  
ANISOU 1290  CA  GLN A 163      675   2290   1712    239    164    -38  A    C  
ATOM   1291  C   GLN A 163      18.657  14.885   5.565  1.00 12.52      A    C  
ANISOU 1291  C   GLN A 163      522   2356   1879    219    148     46  A    C  
ATOM   1292  O   GLN A 163      19.836  15.263   5.690  1.00 13.84      A    O  
ANISOU 1292  O   GLN A 163      439   2745   2073    -74    205     43  A    O  
ATOM   1293  CB  GLN A 163      16.868  16.659   5.638  1.00 12.54      A    C  
ANISOU 1293  CB  GLN A 163      665   2442   1657    284     65    -87  A    C  
ATOM   1294  CG  GLN A 163      16.171  17.712   4.786  1.00 13.50      A    C  
ANISOU 1294  CG  GLN A 163      675   2596   1859    438    126      0  A    C  
ATOM   1295  CD  GLN A 163      15.263  18.590   5.618  1.00 14.05      A    C  
ANISOU 1295  CD  GLN A 163      849   2714   1773    666    -59   -115  A    C  
ATOM   1296  NE2 GLN A 163      13.970  18.657   5.244  1.00 15.99      A    N  
ANISOU 1296  NE2 GLN A 163      777   3260   2037    715     92     93  A    N  
ATOM   1297  OE1 GLN A 163      15.714  19.227   6.580  1.00 16.73      A    O  
ANISOU 1297  OE1 GLN A 163     1402   2989   1967    522   -109   -296  A    O  
ATOM   1298  N   ILE A 164      18.229  13.758   6.111  1.00 12.06      A    N  
ANISOU 1298  N   ILE A 164      410   2381   1791    285    173    163  A    N  
ATOM   1299  CA  ILE A 164      19.122  12.845   6.808  1.00 12.76      A    C  
ANISOU 1299  CA  ILE A 164      439   2504   1905    351    159    135  A    C  
ATOM   1300  C   ILE A 164      20.155  12.293   5.828  1.00 13.08      A    C  
ANISOU 1300  C   ILE A 164      392   2630   1946    247    186     -3  A    C  
ATOM   1301  O   ILE A 164      21.360  12.235   6.152  1.00 13.75      A    O  
ANISOU 1301  O   ILE A 164      285   2966   1972    140    211     57  A    O  
ATOM   1302  CB  ILE A 164      18.360  11.675   7.463  1.00 13.19      A    C  
ANISOU 1302  CB  ILE A 164      497   2617   1897    417    153    208  A    C  
ATOM   1303  CG1 ILE A 164      17.485  12.214   8.607  1.00 14.54      A    C  
ANISOU 1303  CG1 ILE A 164      509   3145   1870    388    208     87  A    C  
ATOM   1304  CG2 ILE A 164      19.328  10.586   7.945  1.00 14.43      A    C  
ANISOU 1304  CG2 ILE A 164      364   2861   2256    500    241    397  A    C  
ATOM   1305  CD1 ILE A 164      18.270  12.566   9.848  1.00 17.86      A    C  
ANISOU 1305  CD1 ILE A 164     1097   3643   2046    423      3    -54  A    C  
ATOM   1306  N   ILE A 165      19.716  11.869   4.651  1.00 12.68      A    N  
ANISOU 1306  N   ILE A 165      340   2671   1808     93    280     26  A    N  
ATOM   1307  CA  ILE A 165      20.642  11.315   3.662  1.00 13.20      A    C  
ANISOU 1307  CA  ILE A 165      504   2642   1870    124    248     57  A    C  
ATOM   1308  C   ILE A 165      21.676  12.353   3.253  1.00 13.49      A    C  
ANISOU 1308  C   ILE A 165      348   2669   2109    142    403     96  A    C  
ATOM   1309  O   ILE A 165      22.887  12.043   3.126  1.00 14.94      A    O  
ANISOU 1309  O   ILE A 165      372   3152   2152    307    414    115  A    O  
ATOM   1310  CB  ILE A 165      19.871  10.786   2.422  1.00 12.96      A    C  
ANISOU 1310  CB  ILE A 165      285   2795   1842     92    212     -8  A    C  
ATOM   1311  CG1 ILE A 165      19.092   9.519   2.808  1.00 13.98      A    C  
ANISOU 1311  CG1 ILE A 165      447   2829   2037     15     87   -104  A    C  
ATOM   1312  CG2 ILE A 165      20.813  10.508   1.251  1.00 15.49      A    C  
ANISOU 1312  CG2 ILE A 165      744   3125   2016    208    384   -148  A    C  
ATOM   1313  CD1 ILE A 165      17.922   9.222   1.872  1.00 15.36      A    C  
ANISOU 1313  CD1 ILE A 165      362   2982   2492    140   -194   -295  A    C  
ATOM   1314  N   GLU A 166      21.242  13.581   3.006  1.00 14.05      A    N  
ANISOU 1314  N   GLU A 166      491   2655   2194     10    491    230  A    N  
ATOM   1315  CA  GLU A 166      22.167  14.666   2.625  1.00 15.72      A    C  
ANISOU 1315  CA  GLU A 166      810   2894   2266    -87    500    136  A    C  
ATOM   1316  C   GLU A 166      23.228  14.922   3.701  1.00 16.32      A    C  
ANISOU 1316  C   GLU A 166      662   3142   2395   -137    500    -15  A    C  
ATOM   1317  O   GLU A 166      24.429  15.048   3.403  1.00 18.77      A    O  
ANISOU 1317  O   GLU A 166      614   3833   2685   -130    621   -142  A    O  
ATOM   1318  CB  GLU A 166      21.384  15.947   2.337  1.00 16.51      A    C  
ANISOU 1318  CB  GLU A 166     1001   2799   2474   -197    520    315  A    C  
ATOM   1319  CG  GLU A 166      20.546  15.850   1.079  1.00 17.77      A    C  
ANISOU 1319  CG  GLU A 166      891   3282   2578     93    571    537  A    C  
ATOM   1320  CD  GLU A 166      19.459  16.915   0.990  1.00 21.46      A    C  
ANISOU 1320  CD  GLU A 166     1676   3364   3115    164    368    754  A    C  
ATOM   1321  OE1 GLU A 166      19.162  17.598   1.999  1.00 23.81      A    O  
ANISOU 1321  OE1 GLU A 166     1727   3797   3524    617    599    653  A    O  
ATOM   1322  OE2 GLU A 166      18.897  17.074  -0.113  1.00 23.76      A    O1-
ANISOU 1322  OE2 GLU A 166     1949   3546   3531    -74    -86   1013  A    O1-
ATOM   1323  N   LYS A 167      22.798  14.994   4.961  1.00 16.60      A    N  
ANISOU 1323  N   LYS A 167      814   3194   2301    -41    388    -65  A    N  
ATOM   1324  CA  LYS A 167      23.703  15.331   6.059  1.00 16.87      A    C  
ANISOU 1324  CA  LYS A 167      867   3109   2433   -102    335   -126  A    C  
ATOM   1325  C   LYS A 167      24.689  14.210   6.403  1.00 16.31      A    C  
ANISOU 1325  C   LYS A 167      541   3203   2451    -35    333   -104  A    C  
ATOM   1326  O   LYS A 167      25.896  14.451   6.572  1.00 17.98      A    O  
ANISOU 1326  O   LYS A 167      357   3619   2854   -186    322   -104  A    O  
ATOM   1327  CB  LYS A 167      22.878  15.682   7.305  1.00 17.64      A    C  
ANISOU 1327  CB  LYS A 167     1130   3212   2360     57    285   -228  A    C  
ATOM   1328  CG  LYS A 167      23.685  15.898   8.577  1.00 21.59      A    C  
ANISOU 1328  CG  LYS A 167     1747   3781   2675   -219     49   -454  A    C  
ATOM   1329  CD  LYS A 167      24.322  17.271   8.631  1.00 26.41      A    C  
ANISOU 1329  CD  LYS A 167     2492   4359   3183   -496      5   -715  A    C  
ATOM   1330  CE  LYS A 167      24.840  17.568  10.036  1.00 26.97      A    C  
ANISOU 1330  CE  LYS A 167     2416   4514   3318   -644      0   -886  A    C  
ATOM   1331  NZ  LYS A 167      25.630  18.831  10.084  1.00 29.39      A    N1+
ANISOU 1331  NZ  LYS A 167     2734   4877   3553   -687    241   -841  A    N1+
ATOM   1332  N   TYR A 168      24.192  12.983   6.495  1.00 15.80      A    N  
ANISOU 1332  N   TYR A 168      410   3134   2460    120    368    -63  A    N  
ATOM   1333  CA  TYR A 168      24.966  11.898   7.090  1.00 16.26      A    C  
ANISOU 1333  CA  TYR A 168      527   3298   2353    261    274   -147  A    C  
ATOM   1334  C   TYR A 168      25.478  10.857   6.103  1.00 16.33      A    C  
ANISOU 1334  C   TYR A 168      395   3528   2283    443    285   -185  A    C  
ATOM   1335  O   TYR A 168      26.368  10.078   6.467  1.00 18.30      A    O  
ANISOU 1335  O   TYR A 168      562   3860   2531    688     65   -307  A    O  
ATOM   1336  CB  TYR A 168      24.142  11.210   8.193  1.00 15.89      A    C  
ANISOU 1336  CB  TYR A 168      593   3296   2148    274    274   -120  A    C  
ATOM   1337  CG  TYR A 168      23.803  12.153   9.321  1.00 15.31      A    C  
ANISOU 1337  CG  TYR A 168      289   3228   2299    197    197   -197  A    C  
ATOM   1338  CD1 TYR A 168      24.767  12.525  10.253  1.00 16.07      A    C  
ANISOU 1338  CD1 TYR A 168      362   3384   2361    197      3   -292  A    C  
ATOM   1339  CD2 TYR A 168      22.505  12.676   9.459  1.00 15.27      A    C  
ANISOU 1339  CD2 TYR A 168      311   3330   2161    241    262    -93  A    C  
ATOM   1340  CE1 TYR A 168      24.495  13.396  11.278  1.00 15.94      A    C  
ANISOU 1340  CE1 TYR A 168      285   3362   2409     83    243   -289  A    C  
ATOM   1341  CE2 TYR A 168      22.226  13.542  10.479  1.00 15.06      A    C  
ANISOU 1341  CE2 TYR A 168      478   3093   2152   -102    131   -115  A    C  
ATOM   1342  CZ  TYR A 168      23.200  13.902  11.400  1.00 15.10      A    C  
ANISOU 1342  CZ  TYR A 168      262   3111   2363     87     98   -296  A    C  
ATOM   1343  OH  TYR A 168      22.901  14.782  12.419  1.00 16.98      A    O  
ANISOU 1343  OH  TYR A 168      256   3535   2659    -52     77   -610  A    O  
ATOM   1344  N   VAL A 169      24.945  10.833   4.884  1.00 16.94      A    N  
ANISOU 1344  N   VAL A 169      342   3785   2308    328    324   -214  A    N  
ATOM   1345  CA  VAL A 169      25.348   9.824   3.904  1.00 19.42      A    C  
ANISOU 1345  CA  VAL A 169      645   4219   2515    537    388   -164  A    C  
ATOM   1346  C   VAL A 169      26.101  10.414   2.709  1.00 22.34      A    C  
ANISOU 1346  C   VAL A 169      804   4820   2863    494    894     27  A    C  
ATOM   1347  O   VAL A 169      27.180   9.937   2.362  1.00 23.60      A    O  
ANISOU 1347  O   VAL A 169      646   5317   3003    798    850    -31  A    O  
ATOM   1348  CB  VAL A 169      24.158   8.967   3.410  1.00 18.33      A    C  
ANISOU 1348  CB  VAL A 169      638   3844   2480    573    194   -263  A    C  
ATOM   1349  CG1 VAL A 169      24.650   7.899   2.431  1.00 20.33      A    C  
ANISOU 1349  CG1 VAL A 169      895   4162   2666    724     31   -410  A    C  
ATOM   1350  CG2 VAL A 169      23.450   8.323   4.584  1.00 19.34      A    C  
ANISOU 1350  CG2 VAL A 169     1053   3671   2623    507     97   -196  A    C  
ATOM   1351  N  AILE A 170      25.536  11.445   2.090  0.50 25.94      A    N  
ANISOU 1351  N  AILE A 170     1238   5400   3219    381   1167    408  A    N  
ATOM   1352  N  BILE A 170      25.537  11.439   2.079  0.50 25.94      A    N  
ANISOU 1352  N  BILE A 170     1237   5400   3219    383   1167    408  A    N  
ATOM   1353  CA AILE A 170      26.162  12.092   0.940  0.50 32.66      A    C  
ANISOU 1353  CA AILE A 170     2319   6280   3810    -57   1448    728  A    C  
ATOM   1354  CA BILE A 170      26.180  12.076   0.932  0.50 32.66      A    C  
ANISOU 1354  CA BILE A 170     2319   6280   3810    -57   1448    728  A    C  
ATOM   1355  C  AILE A 170      27.315  12.971   1.403  0.50 36.82      A    C  
ANISOU 1355  C  AILE A 170     2773   6977   4239   -584   1456    697  A    C  
ATOM   1356  C  BILE A 170      27.270  13.027   1.419  0.50 36.81      A    C  
ANISOU 1356  C  BILE A 170     2773   6977   4237   -584   1456    697  A    C  
ATOM   1357  O  AILE A 170      27.122  13.890   2.196  0.50 40.85      A    O  
ANISOU 1357  O  AILE A 170     3231   7713   4578  -1010   1526    513  A    O  
ATOM   1358  O  BILE A 170      27.016  13.900   2.250  0.50 40.85      A    O  
ANISOU 1358  O  BILE A 170     3231   7713   4578  -1010   1526    515  A    O  
ATOM   1359  CB AILE A 170      25.158  12.967   0.147  0.50 32.66      A    C  
ANISOU 1359  CB AILE A 170     2469   6171   3768    -17   1410    929  A    C  
ATOM   1360  CB BILE A 170      25.170  12.863   0.065  0.50 32.66      A    C  
ANISOU 1360  CB BILE A 170     2469   6171   3767    -17   1411    929  A    C  
ATOM   1361  CG1AILE A 170      23.922  12.148  -0.273  0.50 33.07      A    C  
ANISOU 1361  CG1AILE A 170     2574   6165   3826    197   1360    820  A    C  
ATOM   1362  CG2AILE A 170      25.846  13.613  -1.066  0.50 34.05      A    C  
ANISOU 1362  CG2AILE A 170     2576   6557   3806    120   1571   1014  A    C  
ATOM   1363  CG1BILE A 170      24.114  11.919  -0.515  0.50 33.06      A    C  
ANISOU 1363  CG1BILE A 170     2569   6165   3826    197   1360    820  A    C  
ATOM   1364  CG2BILE A 170      25.898  13.617  -1.052  0.50 34.05      A    C  
ANISOU 1364  CG2BILE A 170     2574   6557   3806    120   1571   1014  A    C  
ATOM   1365  CD1AILE A 170      24.248  10.789  -0.885  0.50 32.94      A    C  
ANISOU 1365  CD1AILE A 170     2585   6082   3849    362   1149    807  A    C  
ATOM   1366  CD1BILE A 170      22.939  12.636  -1.178  0.50 33.14      A    C  
ANISOU 1366  CD1BILE A 170     2594   6093   3903    384   1106    807  A    C  
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.