CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 22010510434787365

Job options:

ID        	=	 22010510434787365
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   ASN A  -5      33.571 -22.068  22.387  1.00 31.80      A    N  
ANISOU    1  N   ASN A  -5     3720   3760   4600    -47   -113     27  A    N  
ATOM      2  CA  ASN A  -5      33.382 -22.804  21.083  1.00 31.59      A    C  
ANISOU    2  CA  ASN A  -5     3652   3915   4433    -76    -39   -100  A    C  
ATOM      3  C   ASN A  -5      33.887 -24.266  21.253  1.00 32.05      A    C  
ANISOU    3  C   ASN A  -5     3702   4005   4469   -168   -101    -25  A    C  
ATOM      4  O   ASN A  -5      34.043 -24.731  22.368  1.00 32.55      A    O  
ANISOU    4  O   ASN A  -5     3768   4055   4545   -227   -144   -146  A    O  
ATOM      5  CB  ASN A  -5      34.052 -22.037  19.920  1.00 32.56      A    C  
ANISOU    5  CB  ASN A  -5     3811   3997   4563     36   -283      0  A    C  
ATOM      6  CG  ASN A  -5      35.591 -21.821  20.111  1.00 34.07      A    C  
ANISOU    6  CG  ASN A  -5     3957   4214   4771   -241     -4   -171  A    C  
ATOM      7  ND2 ASN A  -5      36.091 -20.682  19.568  1.00 34.32      A    N  
ANISOU    7  ND2 ASN A  -5     4614   3992   4434    148   -355    -63  A    N  
ATOM      8  OD1 ASN A  -5      36.314 -22.659  20.708  1.00 34.95      A    O  
ANISOU    8  OD1 ASN A  -5     3683   4647   4946     87    318   -422  A    O  
ATOM      9  N   LEU A  -4      34.121 -25.016  20.182  1.00 32.86      A    N  
ANISOU    9  N   LEU A  -4     3821   4123   4540    -45      5    -38  A    N  
ATOM     10  CA  LEU A  -4      34.612 -26.401  20.358  1.00 34.20      A    C  
ANISOU   10  CA  LEU A  -4     4099   4230   4664     49    -30     52  A    C  
ATOM     11  C   LEU A  -4      35.949 -26.515  21.052  1.00 33.75      A    C  
ANISOU   11  C   LEU A  -4     4031   4234   4556     85     58    -38  A    C  
ATOM     12  O   LEU A  -4      36.291 -27.603  21.550  1.00 34.22      A    O  
ANISOU   12  O   LEU A  -4     4028   4294   4677    145    -31    346  A    O  
ATOM     13  CB  LEU A  -4      34.693 -27.149  19.043  1.00 35.50      A    C  
ANISOU   13  CB  LEU A  -4     4289   4458   4740     34   -123    -64  A    C  
ATOM     14  CG  LEU A  -4      33.340 -27.688  18.472  1.00 39.97      A    C  
ANISOU   14  CG  LEU A  -4     4755   5087   5342   -101   -187    -32  A    C  
ATOM     15  CD1 LEU A  -4      33.398 -27.993  16.942  1.00 44.61      A    C  
ANISOU   15  CD1 LEU A  -4     5425   5964   5558    362   -153   -458  A    C  
ATOM     16  CD2 LEU A  -4      32.780 -28.890  19.236  1.00 43.07      A    C  
ANISOU   16  CD2 LEU A  -4     5459   5281   5622   -563   -167   -163  A    C  
ATOM     17  N   TYR A  -3      36.704 -25.420  21.103  1.00 33.50      A    N  
ANISOU   17  N   TYR A  -3     4002   4276   4450    101     65   -175  A    N  
ATOM     18  CA  TYR A  -3      38.131 -25.476  21.496  1.00 33.11      A    C  
ANISOU   18  CA  TYR A  -3     4101   4268   4210      3      2   -341  A    C  
ATOM     19  C   TYR A  -3      38.490 -24.659  22.729  1.00 32.68      A    C  
ANISOU   19  C   TYR A  -3     4023   4323   4068     41    122   -302  A    C  
ATOM     20  O   TYR A  -3      39.400 -25.042  23.463  1.00 32.33      A    O  
ANISOU   20  O   TYR A  -3     4279   4161   3841    224    272   -228  A    O  
ATOM     21  CB  TYR A  -3      39.014 -25.024  20.329  1.00 33.20      A    C  
ANISOU   21  CB  TYR A  -3     4090   4316   4207   -101    -57   -276  A    C  
ATOM     22  CG  TYR A  -3      38.777 -25.850  19.086  1.00 34.19      A    C  
ANISOU   22  CG  TYR A  -3     4404   4289   4295   -288   -189   -271  A    C  
ATOM     23  CD1 TYR A  -3      39.281 -27.158  18.971  1.00 34.00      A    C  
ANISOU   23  CD1 TYR A  -3     4131   4252   4532   -490   -193   -351  A    C  
ATOM     24  CD2 TYR A  -3      38.015 -25.342  18.021  1.00 37.03      A    C  
ANISOU   24  CD2 TYR A  -3     5026   4557   4486   -267   -225   -102  A    C  
ATOM     25  CE1 TYR A  -3      38.997 -27.948  17.808  1.00 33.18      A    C  
ANISOU   25  CE1 TYR A  -3     4138   4117   4350   -731    158   -395  A    C  
ATOM     26  CE2 TYR A  -3      37.744 -26.107  16.900  1.00 37.15      A    C  
ANISOU   26  CE2 TYR A  -3     5216   4619   4280   -442    106     -3  A    C  
ATOM     27  CZ  TYR A  -3      38.243 -27.391  16.795  1.00 36.91      A    C  
ANISOU   27  CZ  TYR A  -3     5114   4751   4158   -503    273   -226  A    C  
ATOM     28  OH  TYR A  -3      37.910 -28.102  15.664  1.00 42.34      A    O  
ANISOU   28  OH  TYR A  -3     5577   5393   5116   -989   -208   -382  A    O  
ATOM     29  N   PHE A  -2      37.844 -23.503  22.894  1.00 33.05      A    N  
ANISOU   29  N   PHE A  -2     4033   4397   4127    -72    332   -422  A    N  
ATOM     30  CA  PHE A  -2      38.077 -22.668  24.064  1.00 33.26      A    C  
ANISOU   30  CA  PHE A  -2     4027   4378   4232     -2    443   -336  A    C  
ATOM     31  C   PHE A  -2      36.744 -22.509  24.807  1.00 33.31      A    C  
ANISOU   31  C   PHE A  -2     3965   4302   4387    -40    403   -260  A    C  
ATOM     32  O   PHE A  -2      35.755 -22.201  24.155  1.00 33.93      A    O  
ANISOU   32  O   PHE A  -2     3908   4601   4382    -51    551   -159  A    O  
ATOM     33  CB  PHE A  -2      38.579 -21.301  23.636  1.00 33.83      A    C  
ANISOU   33  CB  PHE A  -2     3924   4551   4377    -88    466   -410  A    C  
ATOM     34  CG  PHE A  -2      38.617 -20.296  24.756  1.00 33.11      A    C  
ANISOU   34  CG  PHE A  -2     3867   4640   4072     20    519   -404  A    C  
ATOM     35  CD1 PHE A  -2      39.598 -20.378  25.750  1.00 34.52      A    C  
ANISOU   35  CD1 PHE A  -2     3489   5412   4212    456    917   -358  A    C  
ATOM     36  CD2 PHE A  -2      37.644 -19.289  24.847  1.00 32.94      A    C  
ANISOU   36  CD2 PHE A  -2     3598   4764   4153    -20    143      1  A    C  
ATOM     37  CE1 PHE A  -2      39.637 -19.452  26.836  1.00 35.90      A    C  
ANISOU   37  CE1 PHE A  -2     4280   4856   4502    172    197   -264  A    C  
ATOM     38  CE2 PHE A  -2      37.684 -18.351  25.897  1.00 34.29      A    C  
ANISOU   38  CE2 PHE A  -2     3847   4577   4604   -122    417    -42  A    C  
ATOM     39  CZ  PHE A  -2      38.677 -18.464  26.922  1.00 33.33      A    C  
ANISOU   39  CZ  PHE A  -2     4053   4530   4080      2    522   -230  A    C  
ATOM     40  N   GLN A  -1      36.747 -22.690  26.141  1.00 33.34      A    N  
ANISOU   40  N   GLN A  -1     4099   4228   4339    -53    447   -187  A    N  
ATOM     41  CA  GLN A  -1      35.630 -22.299  27.049  1.00 34.23      A    C  
ANISOU   41  CA  GLN A  -1     4343   4246   4416    -89    322   -161  A    C  
ATOM     42  C   GLN A  -1      36.212 -21.526  28.241  1.00 34.98      A    C  
ANISOU   42  C   GLN A  -1     4483   4429   4376    -66    249   -131  A    C  
ATOM     43  O   GLN A  -1      37.362 -21.773  28.645  1.00 35.77      A    O  
ANISOU   43  O   GLN A  -1     4867   4680   4044    -26     28    -15  A    O  
ATOM     44  CB  GLN A  -1      34.818 -23.516  27.559  1.00 34.90      A    C  
ANISOU   44  CB  GLN A  -1     4365   4297   4596   -168    287   -200  A    C  
ATOM     45  CG  GLN A  -1      34.410 -24.444  26.407  1.00 36.09      A    C  
ANISOU   45  CG  GLN A  -1     4148   4402   5161   -261    420   -450  A    C  
ATOM     46  CD  GLN A  -1      35.528 -25.347  25.895  1.00 38.98      A    C  
ANISOU   46  CD  GLN A  -1     4735   4771   5303    224     34   -732  A    C  
ATOM     47  NE2 GLN A  -1      35.498 -25.644  24.618  1.00 36.82      A    N  
ANISOU   47  NE2 GLN A  -1     4653   4432   4904    171    317  -1029  A    N  
ATOM     48  OE1 GLN A  -1      36.406 -25.776  26.655  1.00 41.09      A    O  
ANISOU   48  OE1 GLN A  -1     4451   5124   6035    312   -238  -1212  A    O  
ATOM     49  N   GLY A   0      35.417 -20.610  28.790  1.00 34.27      A    N  
ANISOU   49  N   GLY A   0     4664   4085   4270    -62    176   -161  A    N  
ATOM     50  CA  GLY A   0      35.794 -19.814  29.986  1.00 33.95      A    C  
ANISOU   50  CA  GLY A   0     4471   4112   4316    -29    188    -33  A    C  
ATOM     51  C   GLY A   0      35.563 -18.336  29.755  1.00 32.99      A    C  
ANISOU   51  C   GLY A   0     4243   4030   4260     95    223   -115  A    C  
ATOM     52  O   GLY A   0      34.903 -17.959  28.815  1.00 30.67      A    O  
ANISOU   52  O   GLY A   0     3803   3811   4036    119    433    -64  A    O  
ATOM     53  N   MET A   1      36.142 -17.533  30.634  1.00 33.99      A    N  
ANISOU   53  N   MET A   1     4196   4180   4536     50    110   -129  A    N  
ATOM     54  CA  MET A   1      36.048 -16.098  30.723  1.00 35.93      A    C  
ANISOU   54  CA  MET A   1     4535   4200   4914     95    -67    -66  A    C  
ATOM     55  C   MET A   1      37.090 -15.375  29.861  1.00 35.86      A    C  
ANISOU   55  C   MET A   1     4477   4066   5081    120    -89   -114  A    C  
ATOM     56  O   MET A   1      38.258 -15.826  29.726  1.00 36.41      A    O  
ANISOU   56  O   MET A   1     4537   3803   5493    191   -116    -18  A    O  
ATOM     57  CB  MET A   1      36.456 -15.777  32.161  1.00 38.84      A    C  
ANISOU   57  CB  MET A   1     5024   4537   5194     93    109   -181  A    C  
ATOM     58  CG  MET A   1      35.439 -15.404  33.088  1.00 46.92      A    C  
ANISOU   58  CG  MET A   1     5889   5928   6008    126     88    -98  A    C  
ATOM     59  SD  MET A   1      36.391 -14.304  34.194  1.00 63.76      A    S  
ANISOU   59  SD  MET A   1     8501   8492   7231   -618   -853   -474  A    S  
ATOM     60  CE  MET A   1      37.241 -13.183  33.003  1.00 58.90      A    C  
ANISOU   60  CE  MET A   1     7201   8490   6686   -458   -782   -554  A    C  
ATOM     61  N   ALA A   2      36.736 -14.202  29.350  1.00 34.01      A    N  
ANISOU   61  N   ALA A   2     4178   3794   4951     43   -110    -51  A    N  
ATOM     62  CA  ALA A   2      37.761 -13.279  28.824  1.00 34.61      A    C  
ANISOU   62  CA  ALA A   2     4281   3926   4943    102    -55   -100  A    C  
ATOM     63  C   ALA A   2      37.247 -11.863  29.005  1.00 34.01      A    C  
ANISOU   63  C   ALA A   2     4139   3906   4878    206    -39     13  A    C  
ATOM     64  O   ALA A   2      36.037 -11.612  28.977  1.00 34.13      A    O  
ANISOU   64  O   ALA A   2     3911   4047   5009    394    -87    189  A    O  
ATOM     65  CB  ALA A   2      38.088 -13.530  27.356  1.00 34.44      A    C  
ANISOU   65  CB  ALA A   2     4337   3839   4909     34      8    -37  A    C  
ATOM     66  N   THR A   3      38.180 -10.956  29.214  1.00 33.87      A    N  
ANISOU   66  N   THR A   3     4001   4078   4789    275    -23   -155  A    N  
ATOM     67  CA  THR A   3      37.871  -9.532  29.281  1.00 33.98      A    C  
ANISOU   67  CA  THR A   3     4006   4162   4741    348    -84   -210  A    C  
ATOM     68  C   THR A   3      37.900  -9.000  27.865  1.00 34.42      A    C  
ANISOU   68  C   THR A   3     4035   4295   4748    335     81   -212  A    C  
ATOM     69  O   THR A   3      38.866  -9.210  27.131  1.00 35.09      A    O  
ANISOU   69  O   THR A   3     4083   4402   4848    442    132   -255  A    O  
ATOM     70  CB  THR A   3      38.896  -8.829  30.140  1.00 34.00      A    C  
ANISOU   70  CB  THR A   3     4120   4192   4603    336     15   -253  A    C  
ATOM     71  CG2 THR A   3      38.679  -7.304  30.178  1.00 36.28      A    C  
ANISOU   71  CG2 THR A   3     4546   4404   4833    366    206   -700  A    C  
ATOM     72  OG1 THR A   3      38.730  -9.359  31.420  1.00 34.06      A    O  
ANISOU   72  OG1 THR A   3     3921   4769   4249    408   -904   -521  A    O  
ATOM     73  N   ILE A   4      36.862  -8.262  27.502  1.00 32.90      A    N  
ANISOU   73  N   ILE A   4     3852   4048   4598    322     69    -10  A    N  
ATOM     74  CA  ILE A   4      36.742  -7.756  26.156  1.00 33.33      A    C  
ANISOU   74  CA  ILE A   4     4112   4033   4517    253    268    -66  A    C  
ATOM     75  C   ILE A   4      36.552  -6.253  26.233  1.00 32.64      A    C  
ANISOU   75  C   ILE A   4     4092   3906   4402    185    257     18  A    C  
ATOM     76  O   ILE A   4      36.003  -5.720  27.232  1.00 33.75      A    O  
ANISOU   76  O   ILE A   4     4243   3826   4752     33    290    -20  A    O  
ATOM     77  CB  ILE A   4      35.620  -8.455  25.354  1.00 33.04      A    C  
ANISOU   77  CB  ILE A   4     4040   3940   4573    151    369   -255  A    C  
ATOM     78  CG1 ILE A   4      34.289  -8.370  26.059  1.00 33.79      A    C  
ANISOU   78  CG1 ILE A   4     4133   4305   4398    314   -103     64  A    C  
ATOM     79  CG2 ILE A   4      35.975  -9.990  25.092  1.00 35.33      A    C  
ANISOU   79  CG2 ILE A   4     4636   3803   4983     79    151    252  A    C  
ATOM     80  CD1 ILE A   4      33.119  -9.070  25.324  1.00 38.71      A    C  
ANISOU   80  CD1 ILE A   4     5089   3953   5664   -406   -135    234  A    C  
ATOM     81  N   THR A   5      36.994  -5.544  25.205  1.00 33.15      A    N  
ANISOU   81  N   THR A   5     4107   4091   4396    279    263      3  A    N  
ATOM     82  CA  THR A   5      36.818  -4.078  25.224  1.00 33.21      A    C  
ANISOU   82  CA  THR A   5     4318   4216   4084    118    175    224  A    C  
ATOM     83  C   THR A   5      36.240  -3.702  23.873  1.00 32.90      A    C  
ANISOU   83  C   THR A   5     4377   4106   4016    311    242    167  A    C  
ATOM     84  O   THR A   5      36.608  -4.280  22.831  1.00 32.89      A    O  
ANISOU   84  O   THR A   5     4406   4106   3982    723    651    148  A    O  
ATOM     85  CB  THR A   5      38.125  -3.328  25.484  1.00 34.71      A    C  
ANISOU   85  CB  THR A   5     4474   4655   4057    167    157    305  A    C  
ATOM     86  CG2 THR A   5      38.821  -3.755  26.774  1.00 30.11      A    C  
ANISOU   86  CG2 THR A   5     4390   3746   3302   -425    -74    488  A    C  
ATOM     87  OG1 THR A   5      38.972  -3.636  24.405  1.00 38.87      A    O  
ANISOU   87  OG1 THR A   5     4650   5380   4735     -3    391    152  A    O  
ATOM     88  N   LEU A   6      35.303  -2.773  23.891  1.00 30.78      A    N  
ANISOU   88  N   LEU A   6     4089   3774   3830    325    218    115  A    N  
ATOM     89  CA  LEU A   6      34.722  -2.248  22.673  1.00 31.36      A    C  
ANISOU   89  CA  LEU A   6     4086   3824   4005    193     24     84  A    C  
ATOM     90  C   LEU A   6      34.808  -0.713  22.732  1.00 30.77      A    C  
ANISOU   90  C   LEU A   6     3936   3715   4038    169     89    123  A    C  
ATOM     91  O   LEU A   6      35.156  -0.153  23.769  1.00 31.99      A    O  
ANISOU   91  O   LEU A   6     4310   3628   4216    215    -53     70  A    O  
ATOM     92  CB  LEU A   6      33.246  -2.689  22.536  1.00 30.28      A    C  
ANISOU   92  CB  LEU A   6     3930   3613   3961    153     29    201  A    C  
ATOM     93  CG  LEU A   6      32.951  -4.180  22.372  1.00 31.79      A    C  
ANISOU   93  CG  LEU A   6     3851   3980   4244     91     38    157  A    C  
ATOM     94  CD1 LEU A   6      31.473  -4.406  22.355  1.00 28.49      A    C  
ANISOU   94  CD1 LEU A   6     3125   3833   3867    195    362    868  A    C  
ATOM     95  CD2 LEU A   6      33.535  -4.669  21.062  1.00 32.94      A    C  
ANISOU   95  CD2 LEU A   6     4665   4052   3797    390   -594   -358  A    C  
ATOM     96  N   GLU A   7      34.464  -0.041  21.652  1.00 30.94      A    N  
ANISOU   96  N   GLU A   7     3800   3951   4002    153    159    150  A    N  
ATOM     97  CA  GLU A   7      34.560   1.402  21.572  1.00 31.34      A    C  
ANISOU   97  CA  GLU A   7     3787   3899   4221     87    233    108  A    C  
ATOM     98  C   GLU A   7      33.211   1.890  21.126  1.00 31.16      A    C  
ANISOU   98  C   GLU A   7     3831   3891   4117     -4    137    180  A    C  
ATOM     99  O   GLU A   7      32.545   1.265  20.276  1.00 32.88      A    O  
ANISOU   99  O   GLU A   7     3989   4141   4362    186     36    139  A    O  
ATOM    100  CB  GLU A   7      35.618   1.818  20.549  1.00 32.96      A    C  
ANISOU  100  CB  GLU A   7     4287   3922   4312     26    411    256  A    C  
ATOM    101  CG  GLU A   7      35.823   3.372  20.509  1.00 41.41      A    C  
ANISOU  101  CG  GLU A   7     5206   4830   5695     32    653     54  A    C  
ATOM    102  CD  GLU A   7      37.287   3.825  20.345  1.00 50.31      A    C  
ANISOU  102  CD  GLU A   7     5894   5931   7291   -251    819    238  A    C  
ATOM    103  OE1 GLU A   7      38.222   2.992  20.275  1.00 55.97      A    O  
ANISOU  103  OE1 GLU A   7     6358   7205   7702    186   1068    177  A    O  
ATOM    104  OE2 GLU A   7      37.515   5.038  20.295  1.00 53.19      A    O1-
ANISOU  104  OE2 GLU A   7     6532   6324   7352   -712    849    236  A    O1-
ATOM    105  N   ARG A   8      32.737   2.931  21.760  1.00 29.84      A    N  
ANISOU  105  N   ARG A   8     3368   3811   4155   -152    101    249  A    N  
ATOM    106  CA  ARG A   8      31.535   3.607  21.300  1.00 29.36      A    C  
ANISOU  106  CA  ARG A   8     3200   3985   3968   -101    203    134  A    C  
ATOM    107  C   ARG A   8      31.815   5.114  21.371  1.00 29.39      A    C  
ANISOU  107  C   ARG A   8     3010   3982   4174   -256    145    144  A    C  
ATOM    108  O   ARG A   8      32.094   5.616  22.449  1.00 28.43      A    O  
ANISOU  108  O   ARG A   8     2868   4017   3914   -287    -22     18  A    O  
ATOM    109  CB  ARG A   8      30.309   3.169  22.166  1.00 28.20      A    C  
ANISOU  109  CB  ARG A   8     3086   3784   3842   -335    225    247  A    C  
ATOM    110  CG  ARG A   8      28.942   3.596  21.612  1.00 26.88      A    C  
ANISOU  110  CG  ARG A   8     3365   3947   2898   -117    447    -67  A    C  
ATOM    111  CD  ARG A   8      28.567   5.078  21.949  1.00 25.27      A    C  
ANISOU  111  CD  ARG A   8     3117   3602   2880   -209   -413    -25  A    C  
ATOM    112  NE  ARG A   8      28.423   5.213  23.392  1.00 26.72      A    N  
ANISOU  112  NE  ARG A   8     3616   3539   2996   -113   -425     81  A    N  
ATOM    113  CZ  ARG A   8      28.358   6.376  24.034  1.00 29.09      A    C  
ANISOU  113  CZ  ARG A   8     3704   3913   3434   -326   -169    137  A    C  
ATOM    114  NH1 ARG A   8      28.425   7.517  23.347  1.00 30.38      A    N1+
ANISOU  114  NH1 ARG A   8     4436   4066   3040    119   -840    504  A    N1+
ATOM    115  NH2 ARG A   8      28.292   6.406  25.362  1.00 27.70      A    N  
ANISOU  115  NH2 ARG A   8     2888   4464   3171   -316   -192    226  A    N  
ATOM    116  N   ASP A   9      31.750   5.839  20.236  1.00 30.48      A    N  
ANISOU  116  N   ASP A   9     3204   4061   4314   -118     43     80  A    N  
ATOM    117  CA  ASP A   9      32.025   7.326  20.261  1.00 32.95      A    C  
ANISOU  117  CA  ASP A   9     3719   4307   4492   -224    -65    232  A    C  
ATOM    118  C   ASP A   9      33.304   7.770  21.060  1.00 33.73      A    C  
ANISOU  118  C   ASP A   9     3814   4496   4506   -221    -58    429  A    C  
ATOM    119  O   ASP A   9      33.342   8.770  21.887  1.00 33.98      A    O  
ANISOU  119  O   ASP A   9     4012   4747   4152   -496   -132    717  A    O  
ATOM    120  CB  ASP A   9      30.818   8.098  20.820  1.00 32.99      A    C  
ANISOU  120  CB  ASP A   9     3709   4253   4572    -70      7     62  A    C  
ATOM    121  CG  ASP A   9      29.568   7.913  19.999  1.00 33.40      A    C  
ANISOU  121  CG  ASP A   9     4011   4114   4563    -79   -163    133  A    C  
ATOM    122  OD1 ASP A   9      29.679   7.501  18.806  1.00 30.90      A    O  
ANISOU  122  OD1 ASP A   9     3544   4143   4052      6    677    499  A    O  
ATOM    123  OD2 ASP A   9      28.475   8.159  20.555  1.00 35.01      A    O1-
ANISOU  123  OD2 ASP A   9     3663   4079   5557     95   -468    248  A    O1-
ATOM    124  N   GLY A  10      34.352   7.032  20.863  1.00 33.25      A    N  
ANISOU  124  N   GLY A  10     3730   4669   4233   -314     81    653  A    N  
ATOM    125  CA  GLY A  10      35.595   7.463  21.522  1.00 32.90      A    C  
ANISOU  125  CA  GLY A  10     4097   4535   3866   -336   -179    537  A    C  
ATOM    126  C   GLY A  10      35.721   7.048  22.977  1.00 31.68      A    C  
ANISOU  126  C   GLY A  10     3914   4346   3776   -278    -39    514  A    C  
ATOM    127  O   GLY A  10      36.717   7.418  23.605  1.00 31.36      A    O  
ANISOU  127  O   GLY A  10     3794   4607   3512   -556    -78    743  A    O  
ATOM    128  N   LEU A  11      34.739   6.293  23.498  1.00 29.16      A    N  
ANISOU  128  N   LEU A  11     3645   3931   3502    -71    159    396  A    N  
ATOM    129  CA  LEU A  11      34.821   5.755  24.850  1.00 29.26      A    C  
ANISOU  129  CA  LEU A  11     3588   3878   3649     39    113    197  A    C  
ATOM    130  C   LEU A  11      35.107   4.264  24.788  1.00 28.53      A    C  
ANISOU  130  C   LEU A  11     3622   3643   3574    -47    173    274  A    C  
ATOM    131  O   LEU A  11      34.480   3.549  23.964  1.00 30.72      A    O  
ANISOU  131  O   LEU A  11     3901   3810   3959    106    -86    232  A    O  
ATOM    132  CB  LEU A  11      33.499   5.948  25.599  1.00 28.85      A    C  
ANISOU  132  CB  LEU A  11     3499   3926   3536    113    264    249  A    C  
ATOM    133  CG  LEU A  11      32.974   7.369  25.705  1.00 26.89      A    C  
ANISOU  133  CG  LEU A  11     3369   3724   3124    -45    469   -179  A    C  
ATOM    134  CD1 LEU A  11      31.524   7.285  26.299  1.00 31.48      A    C  
ANISOU  134  CD1 LEU A  11     3959   3982   4018   -146   1132    374  A    C  
ATOM    135  CD2 LEU A  11      33.862   8.256  26.523  1.00 23.83      A    C  
ANISOU  135  CD2 LEU A  11     2405   3753   2895   -351   1056   -201  A    C  
ATOM    136  N   GLN A  12      36.023   3.781  25.633  1.00 27.45      A    N  
ANISOU  136  N   GLN A  12     3280   3593   3555      0    327    147  A    N  
ATOM    137  CA AGLN A  12      36.204   2.346  25.798  0.50 27.45      A    C  
ANISOU  137  CA AGLN A  12     3374   3631   3425    -59    342    240  A    C  
ATOM    138  CA BGLN A  12      36.176   2.325  25.767  0.50 27.56      A    C  
ANISOU  138  CA BGLN A  12     3330   3697   3443    -76    338    333  A    C  
ATOM    139  C   GLN A  12      35.145   1.777  26.732  1.00 27.70      A    C  
ANISOU  139  C   GLN A  12     3408   3674   3442     10    336    253  A    C  
ATOM    140  O   GLN A  12      34.863   2.408  27.780  1.00 28.27      A    O  
ANISOU  140  O   GLN A  12     3648   3869   3222   -229    562    293  A    O  
ATOM    141  CB AGLN A  12      37.579   2.032  26.334  0.50 27.33      A    C  
ANISOU  141  CB AGLN A  12     3309   3613   3460     57    282    265  A    C  
ATOM    142  CB BGLN A  12      37.602   1.890  26.102  0.50 27.49      A    C  
ANISOU  142  CB BGLN A  12     3258   3761   3426     31    287    400  A    C  
ATOM    143  CG AGLN A  12      37.769   0.573  26.481  0.50 27.33      A    C  
ANISOU  143  CG AGLN A  12     3420   3359   3602    -31    495    132  A    C  
ATOM    144  CG BGLN A  12      38.576   2.467  25.091  0.50 27.88      A    C  
ANISOU  144  CG BGLN A  12     3052   3832   3706   -149    425    799  A    C  
ATOM    145  CD AGLN A  12      39.153   0.184  26.951  0.50 29.10      A    C  
ANISOU  145  CD AGLN A  12     3627   3185   4244    169    395     73  A    C  
ATOM    146  CD BGLN A  12      39.963   1.804  25.017  0.50 33.15      A    C  
ANISOU  146  CD BGLN A  12     3797   4469   4326    168    270   1186  A    C  
ATOM    147  NE2AGLN A  12      39.913  -0.399  26.038  0.50 29.98      A    N  
ANISOU  147  NE2AGLN A  12     4010   3206   4175    120    589    111  A    N  
ATOM    148  NE2BGLN A  12      40.750   2.232  24.013  0.50 33.65      A    N  
ANISOU  148  NE2BGLN A  12     3657   5058   4068     68    393   1021  A    N  
ATOM    149  OE1AGLN A  12      39.518   0.340  28.129  0.50 29.24      A    O  
ANISOU  149  OE1AGLN A  12     3476   3447   4186    532    331   -136  A    O  
ATOM    150  OE1BGLN A  12      40.330   0.947  25.830  0.50 34.45      A    O  
ANISOU  150  OE1BGLN A  12     3883   4322   4883    163    -42   1285  A    O  
ATOM    151  N   LEU A  13      34.532   0.666  26.325  1.00 25.85      A    N  
ANISOU  151  N   LEU A  13     3038   3585   3197     36    274    206  A    N  
ATOM    152  CA  LEU A  13      33.588  -0.095  27.154  1.00 27.82      A    C  
ANISOU  152  CA  LEU A  13     3353   3657   3559    152     34    273  A    C  
ATOM    153  C   LEU A  13      34.284  -1.413  27.484  1.00 27.83      A    C  
ANISOU  153  C   LEU A  13     3423   3694   3455    272     72    183  A    C  
ATOM    154  O   LEU A  13      34.707  -2.138  26.566  1.00 26.82      A    O  
ANISOU  154  O   LEU A  13     3320   3827   3042    272    257    131  A    O  
ATOM    155  CB  LEU A  13      32.267  -0.352  26.400  1.00 27.21      A    C  
ANISOU  155  CB  LEU A  13     2892   3611   3833    235     82    174  A    C  
ATOM    156  CG  LEU A  13      31.492   0.907  25.904  1.00 29.22      A    C  
ANISOU  156  CG  LEU A  13     3411   3677   4012    299     91    280  A    C  
ATOM    157  CD1 LEU A  13      30.244   0.579  25.130  1.00 29.96      A    C  
ANISOU  157  CD1 LEU A  13     3564   4043   3776    335     76   -180  A    C  
ATOM    158  CD2 LEU A  13      31.148   1.827  27.053  1.00 28.12      A    C  
ANISOU  158  CD2 LEU A  13     2678   4162   3843   1103   -294   -377  A    C  
ATOM    159  N   VAL A  14      34.370  -1.721  28.779  1.00 26.92      A    N  
ANISOU  159  N   VAL A  14     3393   3600   3232    289     -6    363  A    N  
ATOM    160  CA  VAL A  14      35.006  -2.947  29.291  1.00 28.49      A    C  
ANISOU  160  CA  VAL A  14     3676   3610   3537     96     22    376  A    C  
ATOM    161  C   VAL A  14      33.941  -3.946  29.663  1.00 28.65      A    C  
ANISOU  161  C   VAL A  14     3593   3663   3627    131    -52    330  A    C  
ATOM    162  O   VAL A  14      32.981  -3.596  30.365  1.00 29.53      A    O  
ANISOU  162  O   VAL A  14     4019   3676   3523    108    116    175  A    O  
ATOM    163  CB  VAL A  14      35.912  -2.628  30.532  1.00 27.90      A    C  
ANISOU  163  CB  VAL A  14     3382   3622   3595     37   -102    674  A    C  
ATOM    164  CG1 VAL A  14      36.642  -3.866  31.004  1.00 29.43      A    C  
ANISOU  164  CG1 VAL A  14     3489   3493   4198    131    231    594  A    C  
ATOM    165  CG2 VAL A  14      36.899  -1.515  30.136  1.00 30.61      A    C  
ANISOU  165  CG2 VAL A  14     4249   3772   3607   -242   -144   1007  A    C  
ATOM    166  N   GLY A  15      34.100  -5.186  29.204  1.00 28.71      A    N  
ANISOU  166  N   GLY A  15     3598   3632   3675    105    130    241  A    N  
ATOM    167  CA  GLY A  15      33.106  -6.238  29.435  1.00 29.43      A    C  
ANISOU  167  CA  GLY A  15     3701   3526   3954    117     40    175  A    C  
ATOM    168  C   GLY A  15      33.751  -7.597  29.742  1.00 29.60      A    C  
ANISOU  168  C   GLY A  15     3723   3665   3857     94    -48    195  A    C  
ATOM    169  O   GLY A  15      34.998  -7.758  29.607  1.00 29.48      A    O  
ANISOU  169  O   GLY A  15     3735   3606   3856    268    113    152  A    O  
ATOM    170  N   THR A  16      32.910  -8.558  30.121  1.00 29.48      A    N  
ANISOU  170  N   THR A  16     3814   3574   3811     -3     23    283  A    N  
ATOM    171  CA  THR A  16      33.329  -9.940  30.357  1.00 29.86      A    C  
ANISOU  171  CA  THR A  16     3715   3714   3914   -149    111    260  A    C  
ATOM    172  C   THR A  16      32.480 -10.880  29.482  1.00 28.89      A    C  
ANISOU  172  C   THR A  16     3639   3573   3763   -183     42    266  A    C  
ATOM    173  O   THR A  16      31.260 -10.842  29.525  1.00 29.49      A    O  
ANISOU  173  O   THR A  16     3565   3835   3805   -128     37     68  A    O  
ATOM    174  CB  THR A  16      33.133 -10.306  31.833  1.00 30.40      A    C  
ANISOU  174  CB  THR A  16     3823   3699   4029   -152    119    410  A    C  
ATOM    175  CG2 THR A  16      33.599 -11.769  32.115  1.00 30.96      A    C  
ANISOU  175  CG2 THR A  16     3719   3671   4371   -130    389    776  A    C  
ATOM    176  OG1 THR A  16      33.798  -9.331  32.665  1.00 30.34      A    O  
ANISOU  176  OG1 THR A  16     3529   4041   3958   -290    509    281  A    O  
ATOM    177  N   ARG A  17      33.142 -11.766  28.768  1.00 27.82      A    N  
ANISOU  177  N   ARG A  17     3472   3532   3565   -333    103    177  A    N  
ATOM    178  CA  ARG A  17      32.472 -12.744  27.917  1.00 29.24      A    C  
ANISOU  178  CA  ARG A  17     3870   3512   3726   -171    216    166  A    C  
ATOM    179  C   ARG A  17      32.624 -14.114  28.618  1.00 29.71      A    C  
ANISOU  179  C   ARG A  17     3825   3558   3904   -100    225    317  A    C  
ATOM    180  O   ARG A  17      33.690 -14.430  29.131  1.00 29.50      A    O  
ANISOU  180  O   ARG A  17     3830   3677   3701   -177    524    219  A    O  
ATOM    181  CB  ARG A  17      33.090 -12.740  26.533  1.00 28.06      A    C  
ANISOU  181  CB  ARG A  17     3666   3441   3554   -196    125     90  A    C  
ATOM    182  CG  ARG A  17      32.488 -13.822  25.619  1.00 27.71      A    C  
ANISOU  182  CG  ARG A  17     4141   3350   3035   -271    230   -108  A    C  
ATOM    183  CD  ARG A  17      33.050 -13.676  24.208  1.00 29.13      A    C  
ANISOU  183  CD  ARG A  17     3845   3739   3482     25    108   -122  A    C  
ATOM    184  NE  ARG A  17      32.554 -14.771  23.378  1.00 33.18      A    N  
ANISOU  184  NE  ARG A  17     4727   3803   4075   -157    -88    -36  A    N  
ATOM    185  CZ  ARG A  17      32.089 -14.609  22.152  1.00 37.25      A    C  
ANISOU  185  CZ  ARG A  17     5192   4296   4666   -169     22     39  A    C  
ATOM    186  NH1 ARG A  17      32.007 -13.393  21.626  1.00 37.65      A    N1+
ANISOU  186  NH1 ARG A  17     5347   4337   4621   -131    546    305  A    N1+
ATOM    187  NH2 ARG A  17      31.660 -15.651  21.466  1.00 37.54      A    N  
ANISOU  187  NH2 ARG A  17     5053   3795   5414   -494    251     88  A    N  
ATOM    188  N   GLU A  18      31.519 -14.869  28.704  1.00 31.66      A    N  
ANISOU  188  N   GLU A  18     4070   3672   4288     21     99    302  A    N  
ATOM    189  CA  GLU A  18      31.543 -16.263  29.115  1.00 32.56      A    C  
ANISOU  189  CA  GLU A  18     4224   3772   4375      5    204    334  A    C  
ATOM    190  C   GLU A  18      31.321 -17.097  27.860  1.00 33.25      A    C  
ANISOU  190  C   GLU A  18     4161   3858   4615    113    221    210  A    C  
ATOM    191  O   GLU A  18      30.335 -16.907  27.125  1.00 33.72      A    O  
ANISOU  191  O   GLU A  18     3996   4072   4741    142    293    -54  A    O  
ATOM    192  CB  GLU A  18      30.472 -16.510  30.164  1.00 34.41      A    C  
ANISOU  192  CB  GLU A  18     4382   3955   4736     71    324    171  A    C  
ATOM    193  CG  GLU A  18      30.511 -15.539  31.304  1.00 35.69      A    C  
ANISOU  193  CG  GLU A  18     4678   4201   4681    234    198    247  A    C  
ATOM    194  CD  GLU A  18      31.514 -15.887  32.403  1.00 41.94      A    C  
ANISOU  194  CD  GLU A  18     5649   4683   5599    631    -27    381  A    C  
ATOM    195  OE1 GLU A  18      32.122 -17.016  32.377  1.00 43.87      A    O  
ANISOU  195  OE1 GLU A  18     6439   4266   5960    676    401    447  A    O  
ATOM    196  OE2 GLU A  18      31.671 -15.000  33.296  1.00 44.04      A    O1-
ANISOU  196  OE2 GLU A  18     5929   4489   6315    464   -505    114  A    O1-
ATOM    197  N   GLU A  19      32.314 -17.919  27.530  1.00 33.11      A    N  
ANISOU  197  N   GLU A  19     4170   3874   4533    139    264    248  A    N  
ATOM    198  CA  GLU A  19      32.322 -18.699  26.320  1.00 33.02      A    C  
ANISOU  198  CA  GLU A  19     4070   3918   4554    162    254    184  A    C  
ATOM    199  C   GLU A  19      31.981 -20.141  26.695  1.00 32.64      A    C  
ANISOU  199  C   GLU A  19     4043   3846   4513    129    246     70  A    C  
ATOM    200  O   GLU A  19      32.715 -20.759  27.456  1.00 31.86      A    O  
ANISOU  200  O   GLU A  19     4096   3739   4269    170    197    107  A    O  
ATOM    201  CB  GLU A  19      33.734 -18.610  25.649  1.00 32.85      A    C  
ANISOU  201  CB  GLU A  19     4155   3772   4551    163    387    210  A    C  
ATOM    202  CG  GLU A  19      33.889 -19.392  24.320  1.00 31.98      A    C  
ANISOU  202  CG  GLU A  19     3966   4088   4095    317    109     97  A    C  
ATOM    203  CD  GLU A  19      33.047 -18.850  23.145  1.00 36.16      A    C  
ANISOU  203  CD  GLU A  19     4573   4839   4324    135    -46    -13  A    C  
ATOM    204  OE1 GLU A  19      32.416 -17.743  23.267  1.00 35.89      A    O  
ANISOU  204  OE1 GLU A  19     4442   5049   4146    130    237    114  A    O  
ATOM    205  OE2 GLU A  19      33.072 -19.531  22.078  1.00 35.51      A    O1-
ANISOU  205  OE2 GLU A  19     4115   4838   4538   -429    109   -264  A    O1-
ATOM    206  N   PRO A  20      30.845 -20.666  26.183  1.00 32.99      A    N  
ANISOU  206  N   PRO A  20     3959   3900   4672    110    245     66  A    N  
ATOM    207  CA  PRO A  20      30.478 -22.075  26.478  1.00 34.70      A    C  
ANISOU  207  CA  PRO A  20     4038   4077   5068     84    173     88  A    C  
ATOM    208  C   PRO A  20      31.074 -23.073  25.465  1.00 35.32      A    C  
ANISOU  208  C   PRO A  20     4183   4204   5032     54    171      7  A    C  
ATOM    209  O   PRO A  20      31.814 -22.675  24.538  1.00 35.48      A    O  
ANISOU  209  O   PRO A  20     4157   3898   5424     30    163    127  A    O  
ATOM    210  CB  PRO A  20      28.977 -22.050  26.297  1.00 34.63      A    C  
ANISOU  210  CB  PRO A  20     3869   4246   5044    118    179    155  A    C  
ATOM    211  CG  PRO A  20      28.848 -21.138  25.020  1.00 33.67      A    C  
ANISOU  211  CG  PRO A  20     4005   4031   4755      8    226     30  A    C  
ATOM    212  CD  PRO A  20      29.913 -20.057  25.201  1.00 32.45      A    C  
ANISOU  212  CD  PRO A  20     3734   4002   4591    111    253    -35  A    C  
ATOM    213  N   PHE A  21      30.777 -24.372  25.661  1.00 36.29      A    N  
ANISOU  213  N   PHE A  21     4319   4305   5162     83    254    -36  A    N  
ATOM    214  CA APHE A  21      31.113 -25.438  24.712  0.50 36.65      A    C  
ANISOU  214  CA APHE A  21     4268   4473   5182    103    232    -67  A    C  
ATOM    215  CA BPHE A  21      31.188 -25.371  24.686  0.50 37.14      A    C  
ANISOU  215  CA BPHE A  21     4400   4582   5128    144    291   -105  A    C  
ATOM    216  C   PHE A  21      30.261 -25.342  23.460  1.00 37.20      A    C  
ANISOU  216  C   PHE A  21     4289   4656   5190    175    239   -107  A    C  
ATOM    217  O   PHE A  21      29.140 -24.840  23.502  1.00 38.83      A    O  
ANISOU  217  O   PHE A  21     4477   4973   5304    257    455   -165  A    O  
ATOM    218  CB APHE A  21      30.808 -26.794  25.342  0.50 36.02      A    C  
ANISOU  218  CB APHE A  21     4203   4279   5204    137    131    -12  A    C  
ATOM    219  CB BPHE A  21      31.237 -26.767  25.315  0.50 37.07      A    C  
ANISOU  219  CB BPHE A  21     4451   4538   5096    181    287    -71  A    C  
ATOM    220  CG APHE A  21      31.734 -27.164  26.429  0.50 35.79      A    C  
ANISOU  220  CG APHE A  21     3988   4284   5326    -45     15     99  A    C  
ATOM    221  CG BPHE A  21      31.383 -27.874  24.308  0.50 38.57      A    C  
ANISOU  221  CG BPHE A  21     4829   4809   5015    225    430   -117  A    C  
ATOM    222  CD1APHE A  21      32.919 -27.824  26.139  0.50 34.74      A    C  
ANISOU  222  CD1APHE A  21     3859   4051   5289    -17    -79    293  A    C  
ATOM    223  CD1BPHE A  21      32.512 -27.950  23.509  0.50 38.17      A    C  
ANISOU  223  CD1BPHE A  21     5037   4739   4725    426    570    -19  A    C  
ATOM    224  CD2APHE A  21      31.436 -26.854  27.742  0.50 34.45      A    C  
ANISOU  224  CD2APHE A  21     3766   4194   5127     46   -190    259  A    C  
ATOM    225  CD2BPHE A  21      30.378 -28.824  24.140  0.50 40.13      A    C  
ANISOU  225  CD2BPHE A  21     5248   4929   5070    278    498   -314  A    C  
ATOM    226  CE1APHE A  21      33.803 -28.147  27.163  0.50 35.42      A    C  
ANISOU  226  CE1APHE A  21     3922   4344   5189     10   -117    338  A    C  
ATOM    227  CE1BPHE A  21      32.634 -28.934  22.582  0.50 38.86      A    C  
ANISOU  227  CE1BPHE A  21     5454   4837   4473    218    583   -180  A    C  
ATOM    228  CE2APHE A  21      32.304 -27.185  28.758  0.50 37.44      A    C  
ANISOU  228  CE2APHE A  21     4100   4453   5670    470   -306    384  A    C  
ATOM    229  CE2BPHE A  21      30.508 -29.820  23.201  0.50 41.77      A    C  
ANISOU  229  CE2BPHE A  21     5474   5156   5240    290    569   -385  A    C  
ATOM    230  CZ APHE A  21      33.497 -27.824  28.457  0.50 35.00      A    C  
ANISOU  230  CZ APHE A  21     3581   4530   5185    108    -27    297  A    C  
ATOM    231  CZ BPHE A  21      31.638 -29.870  22.429  0.50 40.43      A    C  
ANISOU  231  CZ BPHE A  21     5462   5194   4706    312    695   -390  A    C  
ATOM    232  N   GLY A  22      30.755 -25.870  22.353  1.00 37.37      A    N  
ANISOU  232  N   GLY A  22     4191   4663   5343    135    190   -156  A    N  
ATOM    233  CA  GLY A  22      29.982 -26.030  21.146  1.00 38.31      A    C  
ANISOU  233  CA  GLY A  22     4329   4742   5486    265    -16   -158  A    C  
ATOM    234  C   GLY A  22      30.299 -25.060  20.037  1.00 38.88      A    C  
ANISOU  234  C   GLY A  22     4390   4813   5567    350    -54   -255  A    C  
ATOM    235  O   GLY A  22      30.659 -23.885  20.263  1.00 38.11      A    O  
ANISOU  235  O   GLY A  22     4428   4463   5589    474   -149   -192  A    O  
ATOM    236  N   GLU A  23      30.128 -25.525  18.822  1.00 39.72      A    N  
ANISOU  236  N   GLU A  23     4558   4900   5634    439    -64   -363  A    N  
ATOM    237  CA  GLU A  23      30.419 -24.702  17.661  1.00 41.34      A    C  
ANISOU  237  CA  GLU A  23     4858   5026   5821    577    -23   -304  A    C  
ATOM    238  C   GLU A  23      29.353 -23.541  17.515  1.00 41.22      A    C  
ANISOU  238  C   GLU A  23     4869   4931   5858    512    -58   -312  A    C  
ATOM    239  O   GLU A  23      29.662 -22.422  17.088  1.00 41.23      A    O  
ANISOU  239  O   GLU A  23     4968   4632   6065    713     -8   -163  A    O  
ATOM    240  CB  GLU A  23      30.475 -25.619  16.426  1.00 42.06      A    C  
ANISOU  240  CB  GLU A  23     4832   5282   5866    577    137   -377  A    C  
ATOM    241  CG  GLU A  23      30.677 -24.900  15.184  1.00 46.62      A    C  
ANISOU  241  CG  GLU A  23     5457   6144   6110    762    309   -232  A    C  
ATOM    242  CD  GLU A  23      30.946 -25.839  14.055  1.00 53.78      A    C  
ANISOU  242  CD  GLU A  23     6958   7023   6451    635    703   -300  A    C  
ATOM    243  OE1 GLU A  23      30.864 -27.078  14.252  1.00 56.53      A    O  
ANISOU  243  OE1 GLU A  23     7400   7111   6966    569    715   -386  A    O  
ATOM    244  OE2 GLU A  23      31.229 -25.325  12.962  1.00 57.92      A    O1-
ANISOU  244  OE2 GLU A  23     6849   7861   7295    410   1651     99  A    O1-
ATOM    245  N   ILE A  24      28.135 -23.806  17.938  1.00 39.29      A    N  
ANISOU  245  N   ILE A  24     4627   4740   5559    417   -169   -350  A    N  
ATOM    246  CA  ILE A  24      27.052 -22.858  17.786  1.00 39.53      A    C  
ANISOU  246  CA  ILE A  24     4694   4939   5384    424   -258   -350  A    C  
ATOM    247  C   ILE A  24      26.300 -22.828  19.094  1.00 38.67      A    C  
ANISOU  247  C   ILE A  24     4704   4646   5340    338   -188   -250  A    C  
ATOM    248  O   ILE A  24      26.140 -23.856  19.734  1.00 38.36      A    O  
ANISOU  248  O   ILE A  24     4648   4270   5655    324   -161   -221  A    O  
ATOM    249  CB  ILE A  24      26.084 -23.268  16.612  1.00 40.52      A    C  
ANISOU  249  CB  ILE A  24     4738   5336   5319    538   -402   -367  A    C  
ATOM    250  CG1 ILE A  24      26.773 -23.058  15.270  1.00 41.51      A    C  
ANISOU  250  CG1 ILE A  24     4662   5852   5255    401   -420   -385  A    C  
ATOM    251  CG2 ILE A  24      24.837 -22.441  16.627  1.00 41.68      A    C  
ANISOU  251  CG2 ILE A  24     4847   5431   5558    722   -251   -342  A    C  
ATOM    252  CD1 ILE A  24      26.252 -23.974  14.179  1.00 45.58      A    C  
ANISOU  252  CD1 ILE A  24     5921   5930   5465    330   -657   -353  A    C  
ATOM    253  N   TYR A  25      25.912 -21.623  19.526  1.00 36.75      A    N  
ANISOU  253  N   TYR A  25     4435   4277   5248    402   -167    -97  A    N  
ATOM    254  CA  TYR A  25      25.238 -21.446  20.803  1.00 35.62      A    C  
ANISOU  254  CA  TYR A  25     4236   4216   5080    253   -148    -94  A    C  
ATOM    255  C   TYR A  25      24.455 -20.151  20.783  1.00 34.71      A    C  
ANISOU  255  C   TYR A  25     4133   4009   5043    294    -65    -90  A    C  
ATOM    256  O   TYR A  25      24.724 -19.256  19.970  1.00 35.15      A    O  
ANISOU  256  O   TYR A  25     4194   3962   5198    252      5   -176  A    O  
ATOM    257  CB  TYR A  25      26.208 -21.386  22.013  1.00 35.07      A    C  
ANISOU  257  CB  TYR A  25     4064   4350   4908    258   -314     14  A    C  
ATOM    258  CG  TYR A  25      27.483 -20.610  21.710  1.00 35.47      A    C  
ANISOU  258  CG  TYR A  25     4087   4302   5087     43   -357    106  A    C  
ATOM    259  CD1 TYR A  25      27.504 -19.218  21.739  1.00 34.00      A    C  
ANISOU  259  CD1 TYR A  25     3658   4322   4936    -36   -844    168  A    C  
ATOM    260  CD2 TYR A  25      28.670 -21.280  21.396  1.00 34.20      A    C  
ANISOU  260  CD2 TYR A  25     3864   4281   4849   -465   -119    294  A    C  
ATOM    261  CE1 TYR A  25      28.644 -18.496  21.446  1.00 34.49      A    C  
ANISOU  261  CE1 TYR A  25     3874   4145   5084    -42   -349   -172  A    C  
ATOM    262  CE2 TYR A  25      29.822 -20.562  21.140  1.00 34.85      A    C  
ANISOU  262  CE2 TYR A  25     3995   4479   4766   -490   -154    -29  A    C  
ATOM    263  CZ  TYR A  25      29.787 -19.167  21.131  1.00 34.77      A    C  
ANISOU  263  CZ  TYR A  25     4011   4207   4991   -139   -454    -32  A    C  
ATOM    264  OH  TYR A  25      30.920 -18.459  20.838  1.00 36.60      A    O  
ANISOU  264  OH  TYR A  25     4598   3750   5556   -292   -474     71  A    O  
ATOM    265  N   ASP A  26      23.527 -20.034  21.722  1.00 34.59      A    N  
ANISOU  265  N   ASP A  26     4069   3915   5157    190     35   -129  A    N  
ATOM    266  CA  ASP A  26      22.864 -18.751  21.924  1.00 35.04      A    C  
ANISOU  266  CA  ASP A  26     4067   3962   5282    157    122   -191  A    C  
ATOM    267  C   ASP A  26      23.712 -17.844  22.800  1.00 34.93      A    C  
ANISOU  267  C   ASP A  26     4200   3946   5125    140    102   -112  A    C  
ATOM    268  O   ASP A  26      24.617 -18.317  23.510  1.00 35.16      A    O  
ANISOU  268  O   ASP A  26     4120   3773   5465    194    109    -84  A    O  
ATOM    269  CB  ASP A  26      21.470 -19.019  22.536  1.00 34.49      A    C  
ANISOU  269  CB  ASP A  26     3853   4001   5251     18    118    -24  A    C  
ATOM    270  CG  ASP A  26      20.734 -20.021  21.706  1.00 37.33      A    C  
ANISOU  270  CG  ASP A  26     4370   4312   5501     16    201   -138  A    C  
ATOM    271  OD1 ASP A  26      20.788 -19.835  20.475  1.00 36.96      A    O  
ANISOU  271  OD1 ASP A  26     4097   4395   5548    247    229    209  A    O  
ATOM    272  OD2 ASP A  26      20.200 -21.032  22.230  1.00 41.04      A    O1-
ANISOU  272  OD2 ASP A  26     4844   4392   6355   -430    -24   -283  A    O1-
ATOM    273  N   MET A  27      23.417 -16.536  22.758  1.00 33.81      A    N  
ANISOU  273  N   MET A  27     4287   3802   4755    111    212   -105  A    N  
ATOM    274  CA  MET A  27      24.173 -15.603  23.561  1.00 32.97      A    C  
ANISOU  274  CA  MET A  27     4168   3782   4575    109    364   -103  A    C  
ATOM    275  C   MET A  27      23.264 -14.544  24.165  1.00 31.99      A    C  
ANISOU  275  C   MET A  27     3992   3748   4412    219    354    -80  A    C  
ATOM    276  O   MET A  27      22.493 -13.937  23.428  1.00 31.68      A    O  
ANISOU  276  O   MET A  27     3910   3474   4650    392    324     48  A    O  
ATOM    277  CB  MET A  27      25.272 -14.915  22.744  1.00 33.71      A    C  
ANISOU  277  CB  MET A  27     4167   4112   4529    -43    602   -168  A    C  
ATOM    278  CG  MET A  27      26.145 -13.978  23.673  1.00 39.02      A    C  
ANISOU  278  CG  MET A  27     5186   4468   5170   -223    734   -448  A    C  
ATOM    279  SD  MET A  27      27.556 -13.330  22.866  1.00 48.42      A    S  
ANISOU  279  SD  MET A  27     6244   5414   6737   -737    -76     -1  A    S  
ATOM    280  CE  MET A  27      28.635 -14.715  22.652  1.00 47.18      A    C  
ANISOU  280  CE  MET A  27     5575   6049   6299   -721   1040   -316  A    C  
ATOM    281  N   ALA A  28      23.418 -14.301  25.464  1.00 30.11      A    N  
ANISOU  281  N   ALA A  28     3750   3569   4120    221    392   -131  A    N  
ATOM    282  CA  ALA A  28      22.746 -13.196  26.172  1.00 29.70      A    C  
ANISOU  282  CA  ALA A  28     3620   3661   4003    109    426   -209  A    C  
ATOM    283  C   ALA A  28      23.662 -12.004  26.369  1.00 29.55      A    C  
ANISOU  283  C   ALA A  28     3553   3753   3920    131    432   -169  A    C  
ATOM    284  O   ALA A  28      24.806 -12.180  26.806  1.00 32.06      A    O  
ANISOU  284  O   ALA A  28     3879   3948   4354     47    339   -395  A    O  
ATOM    285  CB  ALA A  28      22.321 -13.681  27.526  1.00 28.68      A    C  
ANISOU  285  CB  ALA A  28     3283   3794   3817    -64    632      3  A    C  
ATOM    286  N   ILE A  29      23.157 -10.790  26.117  1.00 28.44      A    N  
ANISOU  286  N   ILE A  29     3387   3688   3728      8    559   -209  A    N  
ATOM    287  CA  ILE A  29      23.817  -9.576  26.540  1.00 28.80      A    C  
ANISOU  287  CA  ILE A  29     3567   3628   3746     35    296    -69  A    C  
ATOM    288  C   ILE A  29      23.168  -9.148  27.838  1.00 29.71      A    C  
ANISOU  288  C   ILE A  29     3731   3707   3847     30    196     85  A    C  
ATOM    289  O   ILE A  29      21.926  -9.078  27.902  1.00 31.34      A    O  
ANISOU  289  O   ILE A  29     3887   3863   4156    -32    117    271  A    O  
ATOM    290  CB  ILE A  29      23.691  -8.462  25.485  1.00 28.34      A    C  
ANISOU  290  CB  ILE A  29     3733   3538   3496    -25    408   -220  A    C  
ATOM    291  CG1 ILE A  29      24.120  -8.976  24.088  1.00 27.59      A    C  
ANISOU  291  CG1 ILE A  29     3097   4059   3326    -44    315    -35  A    C  
ATOM    292  CG2 ILE A  29      24.421  -7.259  26.001  1.00 24.83      A    C  
ANISOU  292  CG2 ILE A  29     2918   3515   2998   -330    456    257  A    C  
ATOM    293  CD1 ILE A  29      23.816  -8.016  22.925  1.00 31.14      A    C  
ANISOU  293  CD1 ILE A  29     3580   4427   3822    382     32    129  A    C  
ATOM    294  N   ILE A  30      23.964  -8.925  28.910  1.00 29.86      A    N  
ANISOU  294  N   ILE A  30     3793   3689   3864     15    124     58  A    N  
ATOM    295  CA  ILE A  30      23.397  -8.700  30.236  1.00 30.34      A    C  
ANISOU  295  CA  ILE A  30     4014   3565   3947    113     59    224  A    C  
ATOM    296  C   ILE A  30      23.756  -7.260  30.653  1.00 28.43      A    C  
ANISOU  296  C   ILE A  30     3665   3465   3670     79     14    229  A    C  
ATOM    297  O   ILE A  30      24.927  -6.847  30.596  1.00 29.30      A    O  
ANISOU  297  O   ILE A  30     3621   3631   3880    -82    451    366  A    O  
ATOM    298  CB  ILE A  30      24.004  -9.663  31.276  1.00 28.26      A    C  
ANISOU  298  CB  ILE A  30     3955   3195   3584    170     61    260  A    C  
ATOM    299  CG1 ILE A  30      23.841 -11.127  30.795  1.00 31.70      A    C  
ANISOU  299  CG1 ILE A  30     3775   3703   4565    137    147    300  A    C  
ATOM    300  CG2 ILE A  30      23.320  -9.430  32.665  1.00 33.32      A    C  
ANISOU  300  CG2 ILE A  30     4611   3680   4367    230    201    367  A    C  
ATOM    301  CD1 ILE A  30      24.739 -12.147  31.529  1.00 34.58      A    C  
ANISOU  301  CD1 ILE A  30     3888   4055   5194    111   -591    544  A    C  
ATOM    302  N   PHE A  31      22.745  -6.498  31.060  1.00 28.34      A    N  
ANISOU  302  N   PHE A  31     3578   3563   3625    -22    273    239  A    N  
ATOM    303  CA  PHE A  31      22.931  -5.062  31.295  1.00 28.41      A    C  
ANISOU  303  CA  PHE A  31     3461   3601   3732    -63    326    341  A    C  
ATOM    304  C   PHE A  31      22.700  -4.725  32.745  1.00 27.88      A    C  
ANISOU  304  C   PHE A  31     3422   3602   3568    -40    255    335  A    C  
ATOM    305  O   PHE A  31      21.577  -4.935  33.273  1.00 26.92      A    O  
ANISOU  305  O   PHE A  31     3305   3555   3368   -223    767    531  A    O  
ATOM    306  CB  PHE A  31      21.934  -4.217  30.473  1.00 28.74      A    C  
ANISOU  306  CB  PHE A  31     3285   3786   3846     98    399    397  A    C  
ATOM    307  CG  PHE A  31      22.044  -4.373  28.975  1.00 29.79      A    C  
ANISOU  307  CG  PHE A  31     3582   3805   3932     33    165     79  A    C  
ATOM    308  CD1 PHE A  31      23.164  -3.918  28.296  1.00 28.69      A    C  
ANISOU  308  CD1 PHE A  31     3943   3551   3407    -48    527     78  A    C  
ATOM    309  CD2 PHE A  31      20.970  -4.977  28.225  1.00 30.48      A    C  
ANISOU  309  CD2 PHE A  31     4103   3544   3932   -313     47    -75  A    C  
ATOM    310  CE1 PHE A  31      23.222  -4.061  26.874  1.00 28.82      A    C  
ANISOU  310  CE1 PHE A  31     3696   4060   3192     70    468    -51  A    C  
ATOM    311  CE2 PHE A  31      21.032  -5.136  26.866  1.00 28.92      A    C  
ANISOU  311  CE2 PHE A  31     3709   3497   3780   -320    558    710  A    C  
ATOM    312  CZ  PHE A  31      22.169  -4.691  26.169  1.00 27.29      A    C  
ANISOU  312  CZ  PHE A  31     3190   3314   3861    -94    941    454  A    C  
ATOM    313  N   HIS A  32      23.698  -4.118  33.361  1.00 28.52      A    N  
ANISOU  313  N   HIS A  32     3625   3565   3646    -70    280    252  A    N  
ATOM    314  CA  HIS A  32      23.572  -3.699  34.784  1.00 29.46      A    C  
ANISOU  314  CA  HIS A  32     3816   3704   3674    -11    164    180  A    C  
ATOM    315  C   HIS A  32      22.696  -2.400  34.945  1.00 30.10      A    C  
ANISOU  315  C   HIS A  32     3934   3787   3714   -123    348     85  A    C  
ATOM    316  O   HIS A  32      22.419  -1.675  33.965  1.00 30.39      A    O  
ANISOU  316  O   HIS A  32     4156   3935   3455    -19    248    148  A    O  
ATOM    317  CB  HIS A  32      25.006  -3.507  35.422  1.00 28.45      A    C  
ANISOU  317  CB  HIS A  32     3529   3707   3571    -43    202    156  A    C  
ATOM    318  CG  HIS A  32      25.753  -2.318  34.921  1.00 28.69      A    C  
ANISOU  318  CG  HIS A  32     3506   3693   3699   -186    141    441  A    C  
ATOM    319  CD2 HIS A  32      26.813  -2.212  34.071  1.00 26.80      A    C  
ANISOU  319  CD2 HIS A  32     3282   3862   3039    -16    312    548  A    C  
ATOM    320  ND1 HIS A  32      25.444  -1.038  35.311  1.00 26.96      A    N  
ANISOU  320  ND1 HIS A  32     3293   3631   3320    -45    -30    383  A    N  
ATOM    321  CE1 HIS A  32      26.263  -0.185  34.702  1.00 28.81      A    C  
ANISOU  321  CE1 HIS A  32     3603   3951   3393   -166    389    619  A    C  
ATOM    322  NE2 HIS A  32      27.109  -0.871  33.961  1.00 27.12      A    N  
ANISOU  322  NE2 HIS A  32     3354   3342   3607   -327    145    589  A    N  
ATOM    323  N   GLY A  33      22.394  -2.050  36.180  1.00 29.56      A    N  
ANISOU  323  N   GLY A  33     3815   3809   3608   -330    652    114  A    N  
ATOM    324  CA  GLY A  33      21.580  -0.856  36.469  1.00 29.02      A    C  
ANISOU  324  CA  GLY A  33     3760   3650   3615   -225    642    -27  A    C  
ATOM    325  C   GLY A  33      22.349   0.404  36.883  1.00 29.19      A    C  
ANISOU  325  C   GLY A  33     3789   3839   3460   -194    484     25  A    C  
ATOM    326  O   GLY A  33      23.586   0.479  36.830  1.00 30.33      A    O  
ANISOU  326  O   GLY A  33     3944   4082   3496   -135    292    139  A    O  
ATOM    327  N   PHE A  34      21.583   1.427  37.234  1.00 29.27      A    N  
ANISOU  327  N   PHE A  34     3894   3721   3507   -129    445      5  A    N  
ATOM    328  CA  PHE A  34      22.056   2.803  37.595  1.00 30.06      A    C  
ANISOU  328  CA  PHE A  34     3809   3893   3719   -163    260   -112  A    C  
ATOM    329  C   PHE A  34      23.041   2.726  38.790  1.00 31.44      A    C  
ANISOU  329  C   PHE A  34     4032   4094   3817   -151    267     33  A    C  
ATOM    330  O   PHE A  34      22.686   2.216  39.873  1.00 31.92      A    O  
ANISOU  330  O   PHE A  34     4088   4295   3742   -263    395    105  A    O  
ATOM    331  CB  PHE A  34      20.761   3.538  37.961  1.00 30.90      A    C  
ANISOU  331  CB  PHE A  34     3973   3809   3956    -79    349   -207  A    C  
ATOM    332  CG  PHE A  34      20.874   5.005  38.238  1.00 31.99      A    C  
ANISOU  332  CG  PHE A  34     3942   4074   4138   -145    408   -251  A    C  
ATOM    333  CD1 PHE A  34      21.516   5.879  37.370  1.00 33.22      A    C  
ANISOU  333  CD1 PHE A  34     4265   4098   4257   -214     16    -93  A    C  
ATOM    334  CD2 PHE A  34      20.209   5.530  39.318  1.00 37.02      A    C  
ANISOU  334  CD2 PHE A  34     4709   4636   4721    152    797   -440  A    C  
ATOM    335  CE1 PHE A  34      21.538   7.279  37.624  1.00 31.79      A    C  
ANISOU  335  CE1 PHE A  34     4397   4283   3397   -152    320   -318  A    C  
ATOM    336  CE2 PHE A  34      20.212   6.934  39.576  1.00 35.76      A    C  
ANISOU  336  CE2 PHE A  34     4791   4376   4420   -307    756   -584  A    C  
ATOM    337  CZ  PHE A  34      20.890   7.799  38.741  1.00 34.01      A    C  
ANISOU  337  CZ  PHE A  34     4472   4290   4159    204    599   -346  A    C  
ATOM    338  N   THR A  35      24.272   3.213  38.584  1.00 30.15      A    N  
ANISOU  338  N   THR A  35     3820   3947   3688   -151    249    101  A    N  
ATOM    339  CA  THR A  35      25.342   3.250  39.621  1.00 31.49      A    C  
ANISOU  339  CA  THR A  35     3968   4114   3881    -60    220    241  A    C  
ATOM    340  C   THR A  35      25.941   1.864  39.900  1.00 31.54      A    C  
ANISOU  340  C   THR A  35     3824   4193   3966    -46    338    193  A    C  
ATOM    341  O   THR A  35      26.822   1.745  40.768  1.00 32.24      A    O  
ANISOU  341  O   THR A  35     4056   4383   3809    105    367    298  A    O  
ATOM    342  CB  THR A  35      24.904   3.932  40.997  1.00 31.74      A    C  
ANISOU  342  CB  THR A  35     3890   4006   4162   -150    256    202  A    C  
ATOM    343  CG2 THR A  35      24.082   5.230  40.786  1.00 30.76      A    C  
ANISOU  343  CG2 THR A  35     3745   4195   3747    251     83    230  A    C  
ATOM    344  OG1 THR A  35      24.176   3.017  41.815  1.00 32.10      A    O  
ANISOU  344  OG1 THR A  35     4802   4020   3373    304    122    451  A    O  
ATOM    345  N   ALA A  36      25.480   0.815  39.193  1.00 31.82      A    N  
ANISOU  345  N   ALA A  36     4034   4146   3908    -92    478    306  A    N  
ATOM    346  CA  ALA A  36      26.007  -0.527  39.439  1.00 30.76      A    C  
ANISOU  346  CA  ALA A  36     3804   3948   3933     12    450    289  A    C  
ATOM    347  C   ALA A  36      27.137  -0.786  38.467  1.00 31.73      A    C  
ANISOU  347  C   ALA A  36     4134   4018   3902    134    241    411  A    C  
ATOM    348  O   ALA A  36      27.713   0.168  37.925  1.00 31.25      A    O  
ANISOU  348  O   ALA A  36     3978   4045   3848    151    416    603  A    O  
ATOM    349  CB  ALA A  36      24.878  -1.601  39.311  1.00 32.82      A    C  
ANISOU  349  CB  ALA A  36     4104   3964   4401     -3    409    466  A    C  
ATOM    350  N   ASN A  37      27.458  -2.062  38.248  1.00 31.34      A    N  
ANISOU  350  N   ASN A  37     3985   4116   3804    350    267    258  A    N  
ATOM    351  CA  ASN A  37      28.540  -2.449  37.323  1.00 30.39      A    C  
ANISOU  351  CA  ASN A  37     4046   3903   3596    299    242    347  A    C  
ATOM    352  C   ASN A  37      28.276  -3.884  36.827  1.00 29.89      A    C  
ANISOU  352  C   ASN A  37     3903   3725   3727    390    229    483  A    C  
ATOM    353  O   ASN A  37      27.294  -4.549  37.219  1.00 30.59      A    O  
ANISOU  353  O   ASN A  37     4026   3695   3898    372    198    549  A    O  
ATOM    354  CB  ASN A  37      29.939  -2.291  37.969  1.00 29.12      A    C  
ANISOU  354  CB  ASN A  37     3678   3915   3471    351    425    441  A    C  
ATOM    355  CG  ASN A  37      30.175  -3.287  39.140  1.00 34.59      A    C  
ANISOU  355  CG  ASN A  37     4925   4213   4003    489    147    419  A    C  
ATOM    356  ND2 ASN A  37      30.089  -2.803  40.377  1.00 39.36      A    N  
ANISOU  356  ND2 ASN A  37     5708   5258   3989    311    336    680  A    N  
ATOM    357  OD1 ASN A  37      30.394  -4.452  38.923  1.00 37.72      A    O  
ANISOU  357  OD1 ASN A  37     5503   4362   4467    557    259    205  A    O  
ATOM    358  N   ARG A  38      29.149  -4.347  35.966  1.00 28.32      A    N  
ANISOU  358  N   ARG A  38     4041   3625   3093    358    336    487  A    N  
ATOM    359  CA  ARG A  38      28.924  -5.600  35.248  1.00 29.74      A    C  
ANISOU  359  CA  ARG A  38     4058   3789   3451    146    446    545  A    C  
ATOM    360  C   ARG A  38      29.122  -6.826  36.147  1.00 29.53      A    C  
ANISOU  360  C   ARG A  38     3986   3806   3426    137    454    503  A    C  
ATOM    361  O   ARG A  38      28.695  -7.913  35.800  1.00 30.50      A    O  
ANISOU  361  O   ARG A  38     4455   3622   3511    225    404    449  A    O  
ATOM    362  CB  ARG A  38      29.902  -5.676  34.067  1.00 30.38      A    C  
ANISOU  362  CB  ARG A  38     4206   3963   3371    218    435    441  A    C  
ATOM    363  CG  ARG A  38      31.328  -6.050  34.396  1.00 28.85      A    C  
ANISOU  363  CG  ARG A  38     4326   3949   2684   -109    293    612  A    C  
ATOM    364  CD  ARG A  38      32.149  -5.865  33.114  1.00 28.31      A    C  
ANISOU  364  CD  ARG A  38     3501   3875   3378   -170    836     16  A    C  
ATOM    365  NE  ARG A  38      33.449  -6.518  33.170  1.00 29.93      A    N  
ANISOU  365  NE  ARG A  38     3660   4123   3587     72    480     29  A    N  
ATOM    366  CZ  ARG A  38      34.562  -5.934  33.619  1.00 30.96      A    C  
ANISOU  366  CZ  ARG A  38     3726   4384   3651    125    714   -215  A    C  
ATOM    367  NH1 ARG A  38      34.514  -4.645  34.008  1.00 28.84      A    N1+
ANISOU  367  NH1 ARG A  38     4013   3884   3058   -170    260    262  A    N1+
ATOM    368  NH2 ARG A  38      35.736  -6.638  33.665  1.00 33.29      A    N  
ANISOU  368  NH2 ARG A  38     4189   4422   4038    494    546    129  A    N  
ATOM    369  N   ASN A  39      29.768  -6.649  37.293  1.00 29.91      A    N  
ANISOU  369  N   ASN A  39     3783   4026   3553    149    521    530  A    N  
ATOM    370  CA  ASN A  39      30.175  -7.774  38.123  1.00 31.00      A    C  
ANISOU  370  CA  ASN A  39     3983   4117   3675     93    446    719  A    C  
ATOM    371  C   ASN A  39      29.439  -7.784  39.479  1.00 33.08      A    C  
ANISOU  371  C   ASN A  39     4352   4399   3817    210    379    703  A    C  
ATOM    372  O   ASN A  39      29.950  -8.355  40.443  1.00 34.15      A    O  
ANISOU  372  O   ASN A  39     4621   4250   4105    238    252    962  A    O  
ATOM    373  CB  ASN A  39      31.671  -7.751  38.354  1.00 32.33      A    C  
ANISOU  373  CB  ASN A  39     4124   4314   3844    260    466    739  A    C  
ATOM    374  CG  ASN A  39      32.454  -8.297  37.201  1.00 32.95      A    C  
ANISOU  374  CG  ASN A  39     4013   4571   3935    -18    431    702  A    C  
ATOM    375  ND2 ASN A  39      31.963  -9.323  36.556  1.00 36.79      A    N  
ANISOU  375  ND2 ASN A  39     4749   4763   4467     58    555    653  A    N  
ATOM    376  OD1 ASN A  39      33.519  -7.775  36.882  1.00 38.92      A    O  
ANISOU  376  OD1 ASN A  39     4366   5995   4426      0    948    398  A    O  
ATOM    377  N   THR A  40      28.244  -7.186  39.570  1.00 34.30      A    N  
ANISOU  377  N   THR A  40     4655   4340   4037    217    431    796  A    N  
ATOM    378  CA  THR A  40      27.419  -7.475  40.748  1.00 34.82      A    C  
ANISOU  378  CA  THR A  40     4518   4593   4118    217    690    798  A    C  
ATOM    379  C   THR A  40      27.199  -9.008  40.925  1.00 34.05      A    C  
ANISOU  379  C   THR A  40     4417   4518   4001    253    772    745  A    C  
ATOM    380  O   THR A  40      27.262  -9.819  39.977  1.00 32.88      A    O  
ANISOU  380  O   THR A  40     3924   4752   3814     93    952   1014  A    O  
ATOM    381  CB  THR A  40      26.037  -6.835  40.710  1.00 35.70      A    C  
ANISOU  381  CB  THR A  40     4790   4524   4249    218    506    858  A    C  
ATOM    382  CG2 THR A  40      26.056  -5.314  40.655  1.00 37.03      A    C  
ANISOU  382  CG2 THR A  40     4792   4802   4474    622    640    813  A    C  
ATOM    383  OG1 THR A  40      25.307  -7.408  39.633  1.00 37.37      A    O  
ANISOU  383  OG1 THR A  40     5198   5117   3883    570    282   1298  A    O  
ATOM    384  N   SER A  41      26.866  -9.424  42.149  1.00 35.01      A    N  
ANISOU  384  N   SER A  41     4637   4472   4193    311    623    789  A    N  
ATOM    385  CA  SER A  41      26.583 -10.823  42.395  1.00 34.11      A    C  
ANISOU  385  CA  SER A  41     4377   4442   4141    134    697    646  A    C  
ATOM    386  C   SER A  41      25.465 -11.380  41.524  1.00 34.64      A    C  
ANISOU  386  C   SER A  41     4368   4436   4356    254    623    632  A    C  
ATOM    387  O   SER A  41      25.598 -12.475  40.983  1.00 32.34      A    O  
ANISOU  387  O   SER A  41     3904   4198   4186    310    663    621  A    O  
ATOM    388  CB  SER A  41      26.301 -11.059  43.862  1.00 35.26      A    C  
ANISOU  388  CB  SER A  41     4657   4460   4279    112    691    852  A    C  
ATOM    389  OG  SER A  41      26.153 -12.439  44.013  1.00 37.52      A    O  
ANISOU  389  OG  SER A  41     4870   4822   4564   -244   1037    864  A    O  
ATOM    390  N   LEU A  42      24.367 -10.631  41.377  1.00 35.14      A    N  
ANISOU  390  N   LEU A  42     4283   4586   4483    309    518    594  A    N  
ATOM    391  CA  LEU A  42      23.255 -11.045  40.504  1.00 35.20      A    C  
ANISOU  391  CA  LEU A  42     4378   4551   4445    259    425    508  A    C  
ATOM    392  C   LEU A  42      23.743 -11.301  39.071  1.00 35.43      A    C  
ANISOU  392  C   LEU A  42     4451   4487   4523    198    346    560  A    C  
ATOM    393  O   LEU A  42      23.466 -12.352  38.469  1.00 36.42      A    O  
ANISOU  393  O   LEU A  42     4537   4473   4827    269    168    513  A    O  
ATOM    394  CB  LEU A  42      22.102  -9.989  40.531  1.00 34.44      A    C  
ANISOU  394  CB  LEU A  42     4215   4430   4438    310    458    421  A    C  
ATOM    395  CG  LEU A  42      20.954 -10.159  39.545  1.00 36.62      A    C  
ANISOU  395  CG  LEU A  42     4655   4543   4716    417    450    683  A    C  
ATOM    396  CD1 LEU A  42      20.195 -11.480  39.752  1.00 40.73      A    C  
ANISOU  396  CD1 LEU A  42     5241   4903   5329     70    524    508  A    C  
ATOM    397  CD2 LEU A  42      19.934  -8.915  39.585  1.00 39.01      A    C  
ANISOU  397  CD2 LEU A  42     4829   4852   5141    704    453    466  A    C  
ATOM    398  N   LEU A  43      24.476 -10.350  38.504  1.00 35.11      A    N  
ANISOU  398  N   LEU A  43     4399   4494   4446    198    382    625  A    N  
ATOM    399  CA  LEU A  43      24.830 -10.538  37.104  1.00 33.09      A    C  
ANISOU  399  CA  LEU A  43     4455   4199   3917     77    390    707  A    C  
ATOM    400  C   LEU A  43      25.877 -11.638  36.922  1.00 33.53      A    C  
ANISOU  400  C   LEU A  43     4549   4232   3956    -24    405    697  A    C  
ATOM    401  O   LEU A  43      25.815 -12.387  35.917  1.00 33.67      A    O  
ANISOU  401  O   LEU A  43     4715   4049   4027    -62    580    914  A    O  
ATOM    402  CB  LEU A  43      25.285  -9.212  36.469  1.00 33.26      A    C  
ANISOU  402  CB  LEU A  43     4412   3963   4262   -110    491    644  A    C  
ATOM    403  CG  LEU A  43      24.264  -8.063  36.625  1.00 32.93      A    C  
ANISOU  403  CG  LEU A  43     4295   3873   4344   -147    383    920  A    C  
ATOM    404  CD1 LEU A  43      24.827  -6.839  35.918  1.00 36.72      A    C  
ANISOU  404  CD1 LEU A  43     5009   3724   5219      0     76   1278  A    C  
ATOM    405  CD2 LEU A  43      22.865  -8.383  36.062  1.00 33.37      A    C  
ANISOU  405  CD2 LEU A  43     4062   3789   4825    246    792    866  A    C  
ATOM    406  N   ARG A  44      26.825 -11.750  37.863  1.00 32.79      A    N  
ANISOU  406  N   ARG A  44     4366   4347   3744     17    412    710  A    N  
ATOM    407  CA  ARG A  44      27.877 -12.790  37.770  1.00 33.79      A    C  
ANISOU  407  CA  ARG A  44     4375   4471   3993    -33    249    605  A    C  
ATOM    408  C   ARG A  44      27.154 -14.147  37.794  1.00 35.00      A    C  
ANISOU  408  C   ARG A  44     4441   4596   4258     72    283    665  A    C  
ATOM    409  O   ARG A  44      27.538 -15.118  37.072  1.00 34.61      A    O  
ANISOU  409  O   ARG A  44     4467   4562   4120    -12    470    598  A    O  
ATOM    410  CB  ARG A  44      28.906 -12.688  38.933  1.00 33.80      A    C  
ANISOU  410  CB  ARG A  44     4284   4669   3886    -39    411    508  A    C  
ATOM    411  CG  ARG A  44      29.987 -11.635  38.776  1.00 36.74      A    C  
ANISOU  411  CG  ARG A  44     4675   4808   4474   -243   -177     97  A    C  
ATOM    412  CD  ARG A  44      30.829 -11.600  40.063  1.00 40.26      A    C  
ANISOU  412  CD  ARG A  44     5007   5103   5185     65   -334    462  A    C  
ATOM    413  NE  ARG A  44      31.851 -10.538  39.993  1.00 44.44      A    N  
ANISOU  413  NE  ARG A  44     4995   5566   6322    111    204    116  A    N  
ATOM    414  CZ  ARG A  44      33.120 -10.657  39.551  1.00 42.18      A    C  
ANISOU  414  CZ  ARG A  44     4742   5371   5911    543    282    250  A    C  
ATOM    415  NH1 ARG A  44      33.592 -11.813  39.083  1.00 41.51      A    N1+
ANISOU  415  NH1 ARG A  44     3597   6233   5941   1210    834    142  A    N1+
ATOM    416  NH2 ARG A  44      33.905  -9.597  39.548  1.00 41.71      A    N  
ANISOU  416  NH2 ARG A  44     4555   5358   5935    228    786    503  A    N  
ATOM    417  N   GLU A  45      26.123 -14.225  38.628  1.00 35.69      A    N  
ANISOU  417  N   GLU A  45     4215   4702   4643    147    279    758  A    N  
ATOM    418  CA  GLU A  45      25.398 -15.476  38.772  1.00 36.33      A    C  
ANISOU  418  CA  GLU A  45     4304   4657   4840    105    213    802  A    C  
ATOM    419  C   GLU A  45      24.471 -15.807  37.627  1.00 35.70      A    C  
ANISOU  419  C   GLU A  45     4278   4532   4753    111    305    800  A    C  
ATOM    420  O   GLU A  45      24.300 -16.975  37.316  1.00 36.45      A    O  
ANISOU  420  O   GLU A  45     4328   4595   4924     59    154    828  A    O  
ATOM    421  CB  GLU A  45      24.617 -15.508  40.089  1.00 37.84      A    C  
ANISOU  421  CB  GLU A  45     4402   4959   5013    269    310    777  A    C  
ATOM    422  CG  GLU A  45      25.431 -16.060  41.268  1.00 44.57      A    C  
ANISOU  422  CG  GLU A  45     5198   5752   5982    300    105    851  A    C  
ATOM    423  CD  GLU A  45      26.450 -17.144  40.826  1.00 50.83      A    C  
ANISOU  423  CD  GLU A  45     5842   6207   7263    898    149   1027  A    C  
ATOM    424  OE1 GLU A  45      26.037 -18.231  40.298  1.00 53.77      A    O  
ANISOU  424  OE1 GLU A  45     6777   6148   7503    793    735   1238  A    O  
ATOM    425  OE2 GLU A  45      27.668 -16.863  40.968  1.00 53.35      A    O1-
ANISOU  425  OE2 GLU A  45     6267   6654   7349    837   -241   1389  A    O1-
ATOM    426  N   ILE A  46      23.868 -14.798  36.993  1.00 34.82      A    N  
ANISOU  426  N   ILE A  46     3957   4504   4767    132    262    846  A    N  
ATOM    427  CA  ILE A  46      23.139 -15.016  35.747  1.00 33.66      A    C  
ANISOU  427  CA  ILE A  46     3992   4293   4502    226    228    682  A    C  
ATOM    428  C   ILE A  46      24.093 -15.550  34.679  1.00 34.50      A    C  
ANISOU  428  C   ILE A  46     4150   4273   4684    175    119    679  A    C  
ATOM    429  O   ILE A  46      23.820 -16.569  34.042  1.00 34.44      A    O  
ANISOU  429  O   ILE A  46     4184   4413   4487    245    155    458  A    O  
ATOM    430  CB  ILE A  46      22.449 -13.696  35.263  1.00 33.96      A    C  
ANISOU  430  CB  ILE A  46     4032   4430   4441    267    259    666  A    C  
ATOM    431  CG1 ILE A  46      21.248 -13.360  36.186  1.00 35.94      A    C  
ANISOU  431  CG1 ILE A  46     4127   4817   4709    571    266    639  A    C  
ATOM    432  CG2 ILE A  46      21.893 -13.879  33.904  1.00 32.80      A    C  
ANISOU  432  CG2 ILE A  46     3930   4060   4472      8   -116    818  A    C  
ATOM    433  CD1 ILE A  46      20.528 -12.000  35.824  1.00 37.99      A    C  
ANISOU  433  CD1 ILE A  46     4660   4908   4864    901    933    809  A    C  
ATOM    434  N   ALA A  47      25.247 -14.903  34.533  1.00 33.73      A    N  
ANISOU  434  N   ALA A  47     3919   4178   4717    225    190    737  A    N  
ATOM    435  CA  ALA A  47      26.212 -15.332  33.533  1.00 34.65      A    C  
ANISOU  435  CA  ALA A  47     4008   4223   4934     14    219    616  A    C  
ATOM    436  C   ALA A  47      26.652 -16.793  33.796  1.00 35.37      A    C  
ANISOU  436  C   ALA A  47     4027   4295   5114    -88    224    532  A    C  
ATOM    437  O   ALA A  47      26.640 -17.617  32.872  1.00 35.17      A    O  
ANISOU  437  O   ALA A  47     3778   4294   5289    -59    356    442  A    O  
ATOM    438  CB  ALA A  47      27.425 -14.356  33.510  1.00 35.06      A    C  
ANISOU  438  CB  ALA A  47     4160   4165   4996   -122    211    740  A    C  
ATOM    439  N   ASN A  48      26.966 -17.097  35.063  1.00 36.69      A    N  
ANISOU  439  N   ASN A  48     4257   4417   5264    -30     83    500  A    N  
ATOM    440  CA  ASN A  48      27.377 -18.433  35.449  1.00 38.16      A    C  
ANISOU  440  CA  ASN A  48     4471   4603   5421    -43     69    497  A    C  
ATOM    441  C   ASN A  48      26.310 -19.453  35.174  1.00 37.57      A    C  
ANISOU  441  C   ASN A  48     4448   4466   5361      9     63    571  A    C  
ATOM    442  O   ASN A  48      26.593 -20.453  34.524  1.00 38.59      A    O  
ANISOU  442  O   ASN A  48     4498   4424   5740     12    156    702  A    O  
ATOM    443  CB  ASN A  48      27.841 -18.525  36.896  1.00 39.72      A    C  
ANISOU  443  CB  ASN A  48     4630   4916   5543   -136   -103    373  A    C  
ATOM    444  CG  ASN A  48      29.211 -17.929  37.095  1.00 44.93      A    C  
ANISOU  444  CG  ASN A  48     5172   5840   6057   -332   -197    425  A    C  
ATOM    445  ND2 ASN A  48      29.555 -17.677  38.346  1.00 49.18      A    N  
ANISOU  445  ND2 ASN A  48     5683   6693   6310   -802   -744    288  A    N  
ATOM    446  OD1 ASN A  48      29.953 -17.677  36.129  1.00 49.69      A    O  
ANISOU  446  OD1 ASN A  48     5505   6643   6731   -622   -123    764  A    O  
ATOM    447  N   SER A  49      25.081 -19.162  35.577  1.00 36.32      A    N  
ANISOU  447  N   SER A  49     4176   4243   5379     33    184    642  A    N  
ATOM    448  CA  SER A  49      23.977 -20.081  35.338  1.00 37.03      A    C  
ANISOU  448  CA  SER A  49     4356   4012   5701     43    257    596  A    C  
ATOM    449  C   SER A  49      23.705 -20.338  33.822  1.00 36.38      A    C  
ANISOU  449  C   SER A  49     4217   3901   5703    119    270    567  A    C  
ATOM    450  O   SER A  49      23.408 -21.459  33.421  1.00 34.18      A    O  
ANISOU  450  O   SER A  49     3801   3609   5574    311    392    453  A    O  
ATOM    451  CB  SER A  49      22.742 -19.595  36.128  1.00 37.66      A    C  
ANISOU  451  CB  SER A  49     4177   4133   5995      0    315    589  A    C  
ATOM    452  OG  SER A  49      21.605 -20.442  35.977  1.00 39.74      A    O  
ANISOU  452  OG  SER A  49     4644   3845   6607   -208    311    865  A    O  
ATOM    453  N   LEU A  50      23.847 -19.313  32.971  1.00 35.71      A    N  
ANISOU  453  N   LEU A  50     4224   3749   5594     96    380    726  A    N  
ATOM    454  CA  LEU A  50      23.583 -19.458  31.551  1.00 37.08      A    C  
ANISOU  454  CA  LEU A  50     4378   3956   5753     62    133    497  A    C  
ATOM    455  C   LEU A  50      24.708 -20.280  30.932  1.00 38.55      A    C  
ANISOU  455  C   LEU A  50     4590   4194   5861    108    185    463  A    C  
ATOM    456  O   LEU A  50      24.467 -21.156  30.087  1.00 37.58      A    O  
ANISOU  456  O   LEU A  50     4339   4199   5740    130    170    487  A    O  
ATOM    457  CB  LEU A  50      23.484 -18.077  30.842  1.00 36.90      A    C  
ANISOU  457  CB  LEU A  50     4369   4006   5644     19     67    651  A    C  
ATOM    458  CG  LEU A  50      22.204 -17.247  31.150  1.00 36.35      A    C  
ANISOU  458  CG  LEU A  50     4606   3494   5710    -67   -277    552  A    C  
ATOM    459  CD1 LEU A  50      22.343 -15.819  30.631  1.00 35.78      A    C  
ANISOU  459  CD1 LEU A  50     4898   3282   5413    -44   -219    796  A    C  
ATOM    460  CD2 LEU A  50      20.953 -17.960  30.532  1.00 36.09      A    C  
ANISOU  460  CD2 LEU A  50     4027   3478   6208   -432     80    671  A    C  
ATOM    461  N   ARG A  51      25.934 -20.004  31.359  1.00 39.71      A    N  
ANISOU  461  N   ARG A  51     4730   4316   6043     96    109    460  A    N  
ATOM    462  CA  ARG A  51      27.080 -20.740  30.839  1.00 41.00      A    C  
ANISOU  462  CA  ARG A  51     5005   4427   6143    141    224    420  A    C  
ATOM    463  C   ARG A  51      26.931 -22.226  31.209  1.00 42.27      A    C  
ANISOU  463  C   ARG A  51     5180   4592   6289    135    205    365  A    C  
ATOM    464  O   ARG A  51      27.310 -23.053  30.420  1.00 41.17      A    O  
ANISOU  464  O   ARG A  51     4948   4211   6483    210    280    490  A    O  
ATOM    465  CB  ARG A  51      28.381 -20.171  31.400  1.00 42.54      A    C  
ANISOU  465  CB  ARG A  51     5162   4666   6334    117    147    424  A    C  
ATOM    466  CG  ARG A  51      29.674 -20.791  30.829  1.00 45.80      A    C  
ANISOU  466  CG  ARG A  51     5777   5357   6266    325    208    315  A    C  
ATOM    467  CD  ARG A  51      30.351 -21.648  31.892  1.00 56.86      A    C  
ANISOU  467  CD  ARG A  51     7579   6782   7240    380   -479    341  A    C  
ATOM    468  NE  ARG A  51      30.748 -20.902  33.101  1.00 61.83      A    N  
ANISOU  468  NE  ARG A  51     8194   7583   7716     59   -337   -166  A    N  
ATOM    469  CZ  ARG A  51      30.311 -21.127  34.354  1.00 63.36      A    C  
ANISOU  469  CZ  ARG A  51     8340   7851   7882     45   -140   -242  A    C  
ATOM    470  NH1 ARG A  51      30.766 -20.392  35.359  1.00 63.95      A    N1+
ANISOU  470  NH1 ARG A  51     8535   7767   7994    326   -204   -432  A    N1+
ATOM    471  NH2 ARG A  51      29.431 -22.080  34.622  1.00 64.88      A    N  
ANISOU  471  NH2 ARG A  51     8644   8062   7943    -85    -13   -115  A    N  
ATOM    472  N   ASP A  52      26.334 -22.531  32.376  1.00 43.84      A    N  
ANISOU  472  N   ASP A  52     5501   4794   6360    130    195    470  A    N  
ATOM    473  CA  ASP A  52      26.073 -23.921  32.812  1.00 44.89      A    C  
ANISOU  473  CA  ASP A  52     5645   4969   6440    150    168    425  A    C  
ATOM    474  C   ASP A  52      25.146 -24.645  31.873  1.00 44.33      A    C  
ANISOU  474  C   ASP A  52     5548   4896   6398    191    193    379  A    C  
ATOM    475  O   ASP A  52      25.101 -25.870  31.890  1.00 44.90      A    O  
ANISOU  475  O   ASP A  52     5552   4869   6638    322    172    444  A    O  
ATOM    476  CB  ASP A  52      25.433 -23.968  34.201  1.00 46.01      A    C  
ANISOU  476  CB  ASP A  52     5918   5100   6461    118     89    456  A    C  
ATOM    477  CG  ASP A  52      26.434 -23.765  35.329  1.00 49.09      A    C  
ANISOU  477  CG  ASP A  52     6339   5546   6765    326     19    641  A    C  
ATOM    478  OD1 ASP A  52      27.647 -23.886  35.085  1.00 50.68      A    O  
ANISOU  478  OD1 ASP A  52     6448   5093   7714   1355   -109    943  A    O  
ATOM    479  OD2 ASP A  52      25.986 -23.448  36.459  1.00 53.51      A    O1-
ANISOU  479  OD2 ASP A  52     7576   6177   6579    411    -78    413  A    O1-
ATOM    480  N   GLU A  53      24.379 -23.891  31.089  1.00 43.74      A    N  
ANISOU  480  N   GLU A  53     5360   4760   6498    301    110    305  A    N  
ATOM    481  CA  GLU A  53      23.430 -24.429  30.083  1.00 43.57      A    C  
ANISOU  481  CA  GLU A  53     5431   4677   6445    246     93    202  A    C  
ATOM    482  C   GLU A  53      23.915 -24.208  28.676  1.00 42.50      A    C  
ANISOU  482  C   GLU A  53     5297   4518   6334    230      3    101  A    C  
ATOM    483  O   GLU A  53      23.104 -24.230  27.750  1.00 43.47      A    O  
ANISOU  483  O   GLU A  53     5445   4621   6447     27   -127     24  A    O  
ATOM    484  CB  GLU A  53      22.038 -23.743  30.182  1.00 43.73      A    C  
ANISOU  484  CB  GLU A  53     5357   4777   6481    273     64    182  A    C  
ATOM    485  CG  GLU A  53      21.362 -23.894  31.490  1.00 46.35      A    C  
ANISOU  485  CG  GLU A  53     5792   5036   6779     99    233    561  A    C  
ATOM    486  CD  GLU A  53      21.047 -25.332  31.861  1.00 49.10      A    C  
ANISOU  486  CD  GLU A  53     6626   5127   6901    -41    239    530  A    C  
ATOM    487  OE1 GLU A  53      20.600 -26.102  30.988  1.00 50.07      A    O  
ANISOU  487  OE1 GLU A  53     6726   5063   7233   -680     86    763  A    O  
ATOM    488  OE2 GLU A  53      21.239 -25.684  33.050  1.00 49.53      A    O1-
ANISOU  488  OE2 GLU A  53     6716   4995   7106    -50    412   1301  A    O1-
ATOM    489  N   ASN A  54      25.223 -23.955  28.514  1.00 41.60      A    N  
ANISOU  489  N   ASN A  54     5234   4343   6226    149     14     66  A    N  
ATOM    490  CA  ASN A  54      25.812 -23.650  27.211  1.00 40.48      A    C  
ANISOU  490  CA  ASN A  54     4957   4334   6089    152     44    -18  A    C  
ATOM    491  C   ASN A  54      25.276 -22.412  26.473  1.00 38.27      A    C  
ANISOU  491  C   ASN A  54     4570   4231   5739    141     38    109  A    C  
ATOM    492  O   ASN A  54      25.256 -22.381  25.273  1.00 39.73      A    O  
ANISOU  492  O   ASN A  54     4737   4276   6081    305    -90    100  A    O  
ATOM    493  CB  ASN A  54      25.830 -24.890  26.290  1.00 42.44      A    C  
ANISOU  493  CB  ASN A  54     5299   4539   6287     90    -16    -28  A    C  
ATOM    494  CG  ASN A  54      26.961 -25.827  26.622  1.00 44.03      A    C  
ANISOU  494  CG  ASN A  54     5238   4566   6923    -33    249   -279  A    C  
ATOM    495  ND2 ASN A  54      28.144 -25.267  26.940  1.00 39.71      A    N  
ANISOU  495  ND2 ASN A  54     4686   4252   6149   -149   1202    -98  A    N  
ATOM    496  OD1 ASN A  54      26.776 -27.052  26.622  1.00 51.08      A    O  
ANISOU  496  OD1 ASN A  54     6573   4885   7949   -362    496    -61  A    O  
ATOM    497  N   ILE A  55      24.878 -21.404  27.215  1.00 35.93      A    N  
ANISOU  497  N   ILE A  55     3999   3908   5743     40     77    220  A    N  
ATOM    498  CA  ILE A  55      24.441 -20.156  26.627  1.00 34.97      A    C  
ANISOU  498  CA  ILE A  55     3952   3898   5436     27    124    247  A    C  
ATOM    499  C   ILE A  55      25.536 -19.141  26.953  1.00 34.17      A    C  
ANISOU  499  C   ILE A  55     3921   3847   5214    137    128    178  A    C  
ATOM    500  O   ILE A  55      25.912 -18.959  28.127  1.00 33.92      A    O  
ANISOU  500  O   ILE A  55     4231   3583   5074     28    298    143  A    O  
ATOM    501  CB  ILE A  55      23.058 -19.687  27.157  1.00 34.51      A    C  
ANISOU  501  CB  ILE A  55     3733   3821   5556     65     75    268  A    C  
ATOM    502  CG1 ILE A  55      21.987 -20.719  26.784  1.00 37.08      A    C  
ANISOU  502  CG1 ILE A  55     4127   4258   5704    -79     87    150  A    C  
ATOM    503  CG2 ILE A  55      22.681 -18.269  26.568  1.00 35.95      A    C  
ANISOU  503  CG2 ILE A  55     3830   3938   5891   -104    164    407  A    C  
ATOM    504  CD1 ILE A  55      20.767 -20.763  27.682  1.00 38.79      A    C  
ANISOU  504  CD1 ILE A  55     3765   5143   5827      0     45    245  A    C  
ATOM    505  N   ALA A  56      26.100 -18.549  25.905  1.00 33.34      A    N  
ANISOU  505  N   ALA A  56     3858   3804   5003    252    189    152  A    N  
ATOM    506  CA  ALA A  56      27.195 -17.611  26.066  1.00 32.00      A    C  
ANISOU  506  CA  ALA A  56     3701   3698   4759    252    128     -5  A    C  
ATOM    507  C   ALA A  56      26.615 -16.344  26.660  1.00 32.74      A    C  
ANISOU  507  C   ALA A  56     3838   3704   4895    229    -20     -7  A    C  
ATOM    508  O   ALA A  56      25.394 -16.191  26.737  1.00 34.07      A    O  
ANISOU  508  O   ALA A  56     3767   3836   5342    -57     56   -138  A    O  
ATOM    509  CB  ALA A  56      27.866 -17.330  24.698  1.00 30.21      A    C  
ANISOU  509  CB  ALA A  56     3427   3698   4352    366    215   -103  A    C  
ATOM    510  N   SER A  57      27.469 -15.473  27.173  1.00 31.79      A    N  
ANISOU  510  N   SER A  57     3779   3464   4834    119    -51    144  A    N  
ATOM    511  CA  SER A  57      27.000 -14.135  27.565  1.00 32.61      A    C  
ANISOU  511  CA  SER A  57     3970   3698   4720    121     27    -22  A    C  
ATOM    512  C   SER A  57      28.143 -13.130  27.481  1.00 32.30      A    C  
ANISOU  512  C   SER A  57     3922   3605   4743     89    -78     -8  A    C  
ATOM    513  O   SER A  57      29.341 -13.495  27.493  1.00 31.91      A    O  
ANISOU  513  O   SER A  57     3954   3510   4660     62   -181   -107  A    O  
ATOM    514  CB  SER A  57      26.365 -14.093  28.969  1.00 32.33      A    C  
ANISOU  514  CB  SER A  57     3818   3864   4601    296    110    119  A    C  
ATOM    515  OG  SER A  57      27.292 -14.504  29.995  1.00 33.08      A    O  
ANISOU  515  OG  SER A  57     3702   4441   4423    229    422    -41  A    O  
ATOM    516  N   VAL A  58      27.731 -11.870  27.326  1.00 31.20      A    N  
ANISOU  516  N   VAL A  58     3854   3429   4572     54    -83    -43  A    N  
ATOM    517  CA  VAL A  58      28.611 -10.739  27.555  1.00 30.52      A    C  
ANISOU  517  CA  VAL A  58     3764   3459   4372     71     -1    -88  A    C  
ATOM    518  C   VAL A  58      27.887  -9.779  28.456  1.00 29.73      A    C  
ANISOU  518  C   VAL A  58     3677   3530   4089     66    127    -31  A    C  
ATOM    519  O   VAL A  58      26.654  -9.684  28.391  1.00 30.48      A    O  
ANISOU  519  O   VAL A  58     3867   3772   3941     67     13   -226  A    O  
ATOM    520  CB  VAL A  58      29.076 -10.039  26.284  1.00 29.49      A    C  
ANISOU  520  CB  VAL A  58     3547   3387   4269     77     89    -74  A    C  
ATOM    521  CG1 VAL A  58      29.994 -10.945  25.474  1.00 29.97      A    C  
ANISOU  521  CG1 VAL A  58     3757   3450   4178    135     20   -620  A    C  
ATOM    522  CG2 VAL A  58      27.897  -9.518  25.404  1.00 31.02      A    C  
ANISOU  522  CG2 VAL A  58     3904   3306   4574    122   -157    158  A    C  
ATOM    523  N   ARG A  59      28.668  -9.072  29.273  1.00 29.56      A    N  
ANISOU  523  N   ARG A  59     3653   3720   3858    160    234    130  A    N  
ATOM    524  CA  ARG A  59      28.177  -8.118  30.255  1.00 30.37      A    C  
ANISOU  524  CA  ARG A  59     3977   3591   3970    -11     28    114  A    C  
ATOM    525  C   ARG A  59      29.226  -7.011  30.343  1.00 30.29      A    C  
ANISOU  525  C   ARG A  59     3796   3734   3979     18     18    148  A    C  
ATOM    526  O   ARG A  59      30.392  -7.281  30.603  1.00 30.61      A    O  
ANISOU  526  O   ARG A  59     3891   3686   4052     56    -75    -20  A    O  
ATOM    527  CB  ARG A  59      27.883  -8.814  31.599  1.00 29.55      A    C  
ANISOU  527  CB  ARG A  59     3705   3608   3915    101    267    150  A    C  
ATOM    528  CG  ARG A  59      29.103  -9.321  32.395  1.00 31.83      A    C  
ANISOU  528  CG  ARG A  59     4047   3897   4149    -13     23    211  A    C  
ATOM    529  CD  ARG A  59      28.661 -10.179  33.547  1.00 30.32      A    C  
ANISOU  529  CD  ARG A  59     3172   3823   4525    233   1003    231  A    C  
ATOM    530  NE  ARG A  59      29.750 -10.504  34.490  1.00 33.03      A    N  
ANISOU  530  NE  ARG A  59     3885   3808   4856    470    521    355  A    N  
ATOM    531  CZ  ARG A  59      30.554 -11.561  34.403  1.00 35.03      A    C  
ANISOU  531  CZ  ARG A  59     4262   4489   4557    492    376    668  A    C  
ATOM    532  NH1 ARG A  59      30.383 -12.476  33.472  1.00 33.12      A    N1+
ANISOU  532  NH1 ARG A  59     3434   4585   4562    229     66    615  A    N1+
ATOM    533  NH2 ARG A  59      31.524 -11.726  35.290  1.00 37.40      A    N  
ANISOU  533  NH2 ARG A  59     4558   4801   4850    468    302    763  A    N  
ATOM    534  N   PHE A  60      28.808  -5.772  30.067  1.00 28.80      A    N  
ANISOU  534  N   PHE A  60     3785   3504   3651    -18    101    195  A    N  
ATOM    535  CA  PHE A  60      29.728  -4.631  29.985  1.00 28.80      A    C  
ANISOU  535  CA  PHE A  60     3797   3511   3632    -71    113    177  A    C  
ATOM    536  C   PHE A  60      29.402  -3.632  31.035  1.00 28.44      A    C  
ANISOU  536  C   PHE A  60     3841   3576   3387   -103     94    230  A    C  
ATOM    537  O   PHE A  60      28.224  -3.454  31.411  1.00 29.14      A    O  
ANISOU  537  O   PHE A  60     3682   3522   3868   -137    217     55  A    O  
ATOM    538  CB  PHE A  60      29.610  -3.878  28.609  1.00 27.88      A    C  
ANISOU  538  CB  PHE A  60     3746   3609   3237   -102    280    111  A    C  
ATOM    539  CG  PHE A  60      30.364  -4.589  27.486  1.00 28.81      A    C  
ANISOU  539  CG  PHE A  60     3939   3608   3399     55    189     19  A    C  
ATOM    540  CD1 PHE A  60      31.624  -4.167  27.105  1.00 29.42      A    C  
ANISOU  540  CD1 PHE A  60     4366   3436   3376    -35    -71    241  A    C  
ATOM    541  CD2 PHE A  60      29.831  -5.746  26.906  1.00 27.13      A    C  
ANISOU  541  CD2 PHE A  60     4159   3658   2488    271    -80    498  A    C  
ATOM    542  CE1 PHE A  60      32.363  -4.813  26.118  1.00 25.49      A    C  
ANISOU  542  CE1 PHE A  60     3285   3200   3198   -151    379    479  A    C  
ATOM    543  CE2 PHE A  60      30.540  -6.411  25.900  1.00 27.97      A    C  
ANISOU  543  CE2 PHE A  60     3409   3556   3660   -108    489    129  A    C  
ATOM    544  CZ  PHE A  60      31.842  -5.959  25.528  1.00 27.97      A    C  
ANISOU  544  CZ  PHE A  60     3340   3607   3678   -562      8    391  A    C  
ATOM    545  N   ASP A  61      30.415  -2.877  31.424  1.00 27.99      A    N  
ANISOU  545  N   ASP A  61     3696   3518   3421    -65    -30    284  A    N  
ATOM    546  CA  ASP A  61      30.123  -1.690  32.215  1.00 27.88      A    C  
ANISOU  546  CA  ASP A  61     3619   3632   3343     84    -43    255  A    C  
ATOM    547  C   ASP A  61      29.638  -0.602  31.246  1.00 27.48      A    C  
ANISOU  547  C   ASP A  61     3464   3571   3404     76     49    204  A    C  
ATOM    548  O   ASP A  61      30.268  -0.367  30.213  1.00 26.80      A    O  
ANISOU  548  O   ASP A  61     3320   3762   3101    135    416     88  A    O  
ATOM    549  CB  ASP A  61      31.385  -1.237  32.946  1.00 28.82      A    C  
ANISOU  549  CB  ASP A  61     3823   3767   3360    105   -184    390  A    C  
ATOM    550  CG  ASP A  61      31.700  -2.146  34.150  1.00 30.88      A    C  
ANISOU  550  CG  ASP A  61     3984   3845   3901    272   -138    519  A    C  
ATOM    551  OD1 ASP A  61      30.736  -2.573  34.827  1.00 33.75      A    O  
ANISOU  551  OD1 ASP A  61     3955   4503   4364    -49    -43    703  A    O  
ATOM    552  OD2 ASP A  61      32.891  -2.413  34.386  1.00 31.80      A    O1-
ANISOU  552  OD2 ASP A  61     3585   4262   4235    -20   -193    230  A    O1-
ATOM    553  N   PHE A  62      28.488   0.021  31.544  1.00 26.38      A    N  
ANISOU  553  N   PHE A  62     3276   3433   3312    232     76    144  A    N  
ATOM    554  CA  PHE A  62      28.037   1.212  30.788  1.00 26.59      A    C  
ANISOU  554  CA  PHE A  62     3153   3453   3497     86    315    201  A    C  
ATOM    555  C   PHE A  62      29.006   2.368  30.961  1.00 26.90      A    C  
ANISOU  555  C   PHE A  62     3314   3474   3432     57    288    232  A    C  
ATOM    556  O   PHE A  62      29.819   2.385  31.924  1.00 24.85      A    O  
ANISOU  556  O   PHE A  62     3036   3478   2927    164    670    244  A    O  
ATOM    557  CB  PHE A  62      26.651   1.653  31.284  1.00 27.80      A    C  
ANISOU  557  CB  PHE A  62     3099   3602   3861    297    118    229  A    C  
ATOM    558  CG  PHE A  62      25.535   0.807  30.755  1.00 26.24      A    C  
ANISOU  558  CG  PHE A  62     2948   3505   3514    202   -103    128  A    C  
ATOM    559  CD1 PHE A  62      25.239   0.800  29.382  1.00 27.14      A    C  
ANISOU  559  CD1 PHE A  62     3117   3838   3355    112   -201    -50  A    C  
ATOM    560  CD2 PHE A  62      24.741   0.060  31.631  1.00 27.16      A    C  
ANISOU  560  CD2 PHE A  62     3499   3341   3477   -162   -529    212  A    C  
ATOM    561  CE1 PHE A  62      24.153   0.022  28.874  1.00 27.38      A    C  
ANISOU  561  CE1 PHE A  62     3158   3466   3777   -428    537     70  A    C  
ATOM    562  CE2 PHE A  62      23.648  -0.701  31.160  1.00 28.14      A    C  
ANISOU  562  CE2 PHE A  62     3789   3352   3547   -361   -207      5  A    C  
ATOM    563  CZ  PHE A  62      23.368  -0.759  29.772  1.00 25.99      A    C  
ANISOU  563  CZ  PHE A  62     3778   3513   2584   -138    283    573  A    C  
ATOM    564  N   ASN A  63      28.948   3.320  30.015  1.00 26.60      A    N  
ANISOU  564  N   ASN A  63     3209   3439   3456    -79    344    413  A    N  
ATOM    565  CA  ASN A  63      29.758   4.559  30.184  1.00 26.47      A    C  
ANISOU  565  CA  ASN A  63     3280   3441   3335    -68    281    270  A    C  
ATOM    566  C   ASN A  63      29.476   5.138  31.572  1.00 26.79      A    C  
ANISOU  566  C   ASN A  63     3425   3581   3171    -92    152    275  A    C  
ATOM    567  O   ASN A  63      28.338   5.074  32.076  1.00 26.28      A    O  
ANISOU  567  O   ASN A  63     3244   3468   3270    -64    -10    394  A    O  
ATOM    568  CB  ASN A  63      29.527   5.587  29.049  1.00 25.08      A    C  
ANISOU  568  CB  ASN A  63     2902   3431   3196   -159    347    392  A    C  
ATOM    569  CG  ASN A  63      28.143   6.264  29.109  1.00 25.12      A    C  
ANISOU  569  CG  ASN A  63     3256   3179   3107    -70    105    367  A    C  
ATOM    570  ND2 ASN A  63      28.125   7.396  29.709  1.00 23.25      A    N  
ANISOU  570  ND2 ASN A  63     2997   3257   2579     81    408    456  A    N  
ATOM    571  OD1 ASN A  63      27.086   5.724  28.620  1.00 29.87      A    O  
ANISOU  571  OD1 ASN A  63     3697   4542   3107   -274    216   -107  A    O  
ATOM    572  N   GLY A  64      30.486   5.719  32.187  1.00 27.10      A    N  
ANISOU  572  N   GLY A  64     3337   3750   3209    -53    239    266  A    N  
ATOM    573  CA  GLY A  64      30.251   6.376  33.482  1.00 27.42      A    C  
ANISOU  573  CA  GLY A  64     3824   3694   2897     70    156    231  A    C  
ATOM    574  C   GLY A  64      30.145   5.398  34.651  1.00 27.80      A    C  
ANISOU  574  C   GLY A  64     3763   3697   3103    127    246    264  A    C  
ATOM    575  O   GLY A  64      29.808   5.830  35.744  1.00 28.37      A    O  
ANISOU  575  O   GLY A  64     4286   3655   2837    252      7    204  A    O  
ATOM    576  N   HIS A  65      30.385   4.105  34.406  1.00 26.95      A    N  
ANISOU  576  N   HIS A  65     3447   3736   3056     95    230    148  A    N  
ATOM    577  CA  HIS A  65      30.284   3.002  35.403  1.00 28.39      A    C  
ANISOU  577  CA  HIS A  65     3395   3761   3628    195    -25    183  A    C  
ATOM    578  C   HIS A  65      31.488   2.020  35.335  1.00 28.99      A    C  
ANISOU  578  C   HIS A  65     3499   3922   3594    206   -113    230  A    C  
ATOM    579  O   HIS A  65      32.072   1.846  34.293  1.00 28.28      A    O  
ANISOU  579  O   HIS A  65     3481   4034   3230     88   -444    525  A    O  
ATOM    580  CB  HIS A  65      28.991   2.206  35.192  1.00 28.71      A    C  
ANISOU  580  CB  HIS A  65     3610   3445   3852     52    165    118  A    C  
ATOM    581  CG  HIS A  65      27.737   2.985  35.439  1.00 27.92      A    C  
ANISOU  581  CG  HIS A  65     3494   3464   3650    269    309    -16  A    C  
ATOM    582  CD2 HIS A  65      26.818   2.905  36.449  1.00 28.74      A    C  
ANISOU  582  CD2 HIS A  65     3488   3695   3737   -185    459    250  A    C  
ATOM    583  ND1 HIS A  65      27.304   4.007  34.596  1.00 25.69      A    N  
ANISOU  583  ND1 HIS A  65     3355   3419   2986    492     40    -43  A    N  
ATOM    584  CE1 HIS A  65      26.165   4.512  35.080  1.00 25.13      A    C  
ANISOU  584  CE1 HIS A  65     3244   3880   2423    -89    676     80  A    C  
ATOM    585  NE2 HIS A  65      25.862   3.869  36.205  1.00 29.75      A    N  
ANISOU  585  NE2 HIS A  65     4023   3995   3282   -140    308   -106  A    N  
ATOM    586  N   GLY A  66      31.840   1.408  36.479  1.00 30.68      A    N  
ANISOU  586  N   GLY A  66     3637   4197   3822    263     -7    369  A    N  
ATOM    587  CA  GLY A  66      32.826   0.319  36.557  1.00 30.61      A    C  
ANISOU  587  CA  GLY A  66     3550   4267   3811    203   -153    391  A    C  
ATOM    588  C   GLY A  66      34.135   0.713  35.869  1.00 31.35      A    C  
ANISOU  588  C   GLY A  66     3737   4210   3962     30   -249    357  A    C  
ATOM    589  O   GLY A  66      34.679   1.811  36.148  1.00 32.56      A    O  
ANISOU  589  O   GLY A  66     3958   4326   4084   -107   -525    259  A    O  
ATOM    590  N   ASP A  67      34.637  -0.171  34.994  1.00 28.74      A    N  
ANISOU  590  N   ASP A  67     3335   4070   3514     38    -95    270  A    N  
ATOM    591  CA  ASP A  67      35.918   0.008  34.309  1.00 29.78      A    C  
ANISOU  591  CA  ASP A  67     3538   4086   3689     -5     26    204  A    C  
ATOM    592  C   ASP A  67      35.782   0.783  33.010  1.00 29.78      A    C  
ANISOU  592  C   ASP A  67     3542   4088   3685    -65    136    196  A    C  
ATOM    593  O   ASP A  67      36.817   1.046  32.274  1.00 30.30      A    O  
ANISOU  593  O   ASP A  67     3348   4147   4017     70    212     12  A    O  
ATOM    594  CB  ASP A  67      36.496  -1.380  34.029  1.00 29.59      A    C  
ANISOU  594  CB  ASP A  67     3301   4193   3748     66    282    215  A    C  
ATOM    595  CG  ASP A  67      36.875  -2.101  35.285  1.00 31.54      A    C  
ANISOU  595  CG  ASP A  67     3828   4212   3942     21   -129     61  A    C  
ATOM    596  OD1 ASP A  67      37.276  -1.418  36.288  1.00 32.22      A    O  
ANISOU  596  OD1 ASP A  67     3916   4654   3671    330     39    125  A    O  
ATOM    597  OD2 ASP A  67      36.765  -3.365  35.296  1.00 32.34      A    O1-
ANISOU  597  OD2 ASP A  67     3885   4083   4319    396   -342    189  A    O1-
ATOM    598  N   SER A  68      34.540   1.128  32.655  1.00 29.27      A    N  
ANISOU  598  N   SER A  68     3565   4027   3528     19    368    177  A    N  
ATOM    599  CA  SER A  68      34.361   1.835  31.365  1.00 29.55      A    C  
ANISOU  599  CA  SER A  68     3513   3988   3727   -126    267    426  A    C  
ATOM    600  C   SER A  68      34.701   3.312  31.426  1.00 28.77      A    C  
ANISOU  600  C   SER A  68     3473   3923   3534    -78    293    251  A    C  
ATOM    601  O   SER A  68      34.764   3.905  32.499  1.00 29.67      A    O  
ANISOU  601  O   SER A  68     3117   4123   4033   -191    305    211  A    O  
ATOM    602  CB  SER A  68      32.987   1.614  30.733  1.00 29.94      A    C  
ANISOU  602  CB  SER A  68     3586   4019   3772   -187    233    162  A    C  
ATOM    603  OG  SER A  68      32.874   0.274  30.258  1.00 26.86      A    O  
ANISOU  603  OG  SER A  68     3324   3610   3270     -3    797    380  A    O  
ATOM    604  N   ASP A  69      34.946   3.891  30.237  1.00 27.19      A    N  
ANISOU  604  N   ASP A  69     3110   3731   3490   -205    413    599  A    N  
ATOM    605  CA  ASP A  69      35.264   5.312  30.146  1.00 28.26      A    C  
ANISOU  605  CA  ASP A  69     3531   3756   3450   -144    389    397  A    C  
ATOM    606  C   ASP A  69      34.087   6.216  30.391  1.00 26.93      A    C  
ANISOU  606  C   ASP A  69     3447   3680   3104   -146    511    201  A    C  
ATOM    607  O   ASP A  69      32.913   5.767  30.362  1.00 26.84      A    O  
ANISOU  607  O   ASP A  69     3362   3559   3277    102     70   -124  A    O  
ATOM    608  CB  ASP A  69      35.822   5.651  28.726  1.00 28.12      A    C  
ANISOU  608  CB  ASP A  69     3588   3928   3168   -100    341    702  A    C  
ATOM    609  CG  ASP A  69      37.245   5.155  28.496  1.00 30.93      A    C  
ANISOU  609  CG  ASP A  69     3954   4044   3754   -115    314    474  A    C  
ATOM    610  OD1 ASP A  69      37.950   4.722  29.471  1.00 28.19      A    O  
ANISOU  610  OD1 ASP A  69     3514   3595   3601   -126    142     24  A    O  
ATOM    611  OD2 ASP A  69      37.692   5.197  27.306  1.00 28.99      A    O1-
ANISOU  611  OD2 ASP A  69     3013   4138   3864    -29    398    348  A    O1-
ATOM    612  N   GLY A  70      34.387   7.496  30.633  1.00 27.44      A    N  
ANISOU  612  N   GLY A  70     3553   3689   3182   -175    635    233  A    N  
ATOM    613  CA  GLY A  70      33.354   8.548  30.710  1.00 27.02      A    C  
ANISOU  613  CA  GLY A  70     3372   3687   3207   -155    437     61  A    C  
ATOM    614  C   GLY A  70      32.976   8.831  32.178  1.00 28.14      A    C  
ANISOU  614  C   GLY A  70     3510   3813   3366   -245    420     42  A    C  
ATOM    615  O   GLY A  70      33.045   7.942  33.038  1.00 27.81      A    O  
ANISOU  615  O   GLY A  70     3694   3829   3042   -182    148    108  A    O  
ATOM    616  N   LYS A  71      32.612  10.077  32.459  1.00 28.03      A    N  
ANISOU  616  N   LYS A  71     3479   3870   3299   -314    468   -208  A    N  
ATOM    617  CA  LYS A  71      32.164  10.516  33.803  1.00 29.52      A    C  
ANISOU  617  CA  LYS A  71     3577   3962   3677   -316    500   -180  A    C  
ATOM    618  C   LYS A  71      30.737  10.017  34.028  1.00 28.45      A    C  
ANISOU  618  C   LYS A  71     3551   3876   3382   -396    266    -74  A    C  
ATOM    619  O   LYS A  71      29.954   9.994  33.099  1.00 30.42      A    O  
ANISOU  619  O   LYS A  71     3562   4390   3606   -295    205     35  A    O  
ATOM    620  CB  LYS A  71      32.184  12.058  33.812  1.00 30.04      A    C  
ANISOU  620  CB  LYS A  71     3636   3797   3979   -545    511   -358  A    C  
ATOM    621  CG  LYS A  71      33.591  12.636  33.973  1.00 32.39      A    C  
ANISOU  621  CG  LYS A  71     3703   4023   4580   -594    497   -454  A    C  
ATOM    622  CD  LYS A  71      33.551  14.106  34.176  1.00 39.26      A    C  
ANISOU  622  CD  LYS A  71     4692   4072   6151  -1081    314   -367  A    C  
ATOM    623  CE  LYS A  71      34.960  14.665  34.001  1.00 46.78      A    C  
ANISOU  623  CE  LYS A  71     5574   4870   7329  -1482    422    -74  A    C  
ATOM    624  NZ  LYS A  71      34.946  16.113  33.567  1.00 50.53      A    N1+
ANISOU  624  NZ  LYS A  71     6433   4807   7956  -1500    264   -156  A    N1+
ATOM    625  N   PHE A  72      30.389   9.656  35.253  1.00 27.18      A    N  
ANISOU  625  N   PHE A  72     3390   3787   3149   -336    398    -50  A    N  
ATOM    626  CA  PHE A  72      29.031   9.328  35.609  1.00 27.99      A    C  
ANISOU  626  CA  PHE A  72     3609   3877   3149   -157    238     98  A    C  
ATOM    627  C   PHE A  72      28.043  10.492  35.316  1.00 28.20      A    C  
ANISOU  627  C   PHE A  72     3648   3802   3265   -100    181     79  A    C  
ATOM    628  O   PHE A  72      26.943  10.272  34.870  1.00 27.19      A    O  
ANISOU  628  O   PHE A  72     3472   3588   3268   -183    406    140  A    O  
ATOM    629  CB  PHE A  72      28.964   8.975  37.093  1.00 27.04      A    C  
ANISOU  629  CB  PHE A  72     3429   3862   2981   -227    656    241  A    C  
ATOM    630  CG  PHE A  72      27.547   8.649  37.566  1.00 25.50      A    C  
ANISOU  630  CG  PHE A  72     3374   3885   2427   -314    329    369  A    C  
ATOM    631  CD1 PHE A  72      26.992   7.384  37.330  1.00 26.84      A    C  
ANISOU  631  CD1 PHE A  72     3727   4217   2253   -661    388    359  A    C  
ATOM    632  CD2 PHE A  72      26.771   9.632  38.112  1.00 26.29      A    C  
ANISOU  632  CD2 PHE A  72     3408   4324   2257    237    339    520  A    C  
ATOM    633  CE1 PHE A  72      25.688   7.050  37.769  1.00 28.93      A    C  
ANISOU  633  CE1 PHE A  72     3365   4745   2879    -42    277    -52  A    C  
ATOM    634  CE2 PHE A  72      25.448   9.335  38.586  1.00 30.29      A    C  
ANISOU  634  CE2 PHE A  72     3991   4795   2720   -392   -125    344  A    C  
ATOM    635  CZ  PHE A  72      24.896   8.034  38.403  1.00 30.07      A    C  
ANISOU  635  CZ  PHE A  72     4144   4139   3142    -67    323    331  A    C  
ATOM    636  N   GLU A  73      28.493  11.712  35.544  1.00 28.21      A    N  
ANISOU  636  N   GLU A  73     3828   3719   3169    -48     93   -101  A    N  
ATOM    637  CA  GLU A  73      27.716  12.925  35.285  1.00 29.88      A    C  
ANISOU  637  CA  GLU A  73     4029   3934   3390   -120    -82   -114  A    C  
ATOM    638  C   GLU A  73      27.297  13.025  33.816  1.00 28.75      A    C  
ANISOU  638  C   GLU A  73     3819   3878   3225   -162     16    -58  A    C  
ATOM    639  O   GLU A  73      26.301  13.693  33.515  1.00 28.26      A    O  
ANISOU  639  O   GLU A  73     3672   3999   3064   -129     37   -121  A    O  
ATOM    640  CB  GLU A  73      28.523  14.161  35.727  1.00 30.30      A    C  
ANISOU  640  CB  GLU A  73     4369   3709   3433     -2   -101   -210  A    C  
ATOM    641  CG  GLU A  73      27.759  15.421  35.652  1.00 36.40      A    C  
ANISOU  641  CG  GLU A  73     4883   4636   4308    -38    -11   -348  A    C  
ATOM    642  CD  GLU A  73      28.663  16.669  35.798  1.00 42.85      A    C  
ANISOU  642  CD  GLU A  73     5558   5112   5609   -472    -71   -413  A    C  
ATOM    643  OE1 GLU A  73      29.846  16.508  36.248  1.00 46.00      A    O  
ANISOU  643  OE1 GLU A  73     5823   5406   6248   -783   -777   -715  A    O  
ATOM    644  OE2 GLU A  73      28.189  17.793  35.451  1.00 44.90      A    O1-
ANISOU  644  OE2 GLU A  73     6042   5361   5657    114    399   -579  A    O1-
ATOM    645  N   ASN A  74      28.090  12.416  32.923  1.00 27.92      A    N  
ANISOU  645  N   ASN A  74     3777   3617   3211   -269   -108   -132  A    N  
ATOM    646  CA  ASN A  74      27.780  12.460  31.496  1.00 27.09      A    C  
ANISOU  646  CA  ASN A  74     3436   3663   3193   -336     83     41  A    C  
ATOM    647  C   ASN A  74      26.951  11.300  30.939  1.00 26.46      A    C  
ANISOU  647  C   ASN A  74     3455   3372   3225   -118    184    -21  A    C  
ATOM    648  O   ASN A  74      26.563  11.310  29.739  1.00 26.57      A    O  
ANISOU  648  O   ASN A  74     3316   3506   3274   -223     64   -187  A    O  
ATOM    649  CB  ASN A  74      29.052  12.745  30.648  1.00 26.72      A    C  
ANISOU  649  CB  ASN A  74     3323   3745   3082   -395     37    -26  A    C  
ATOM    650  CG  ASN A  74      29.655  14.132  31.001  1.00 29.63      A    C  
ANISOU  650  CG  ASN A  74     3725   3608   3925   -238     90    -82  A    C  
ATOM    651  ND2 ASN A  74      30.992  14.226  31.044  1.00 30.56      A    N  
ANISOU  651  ND2 ASN A  74     3762   3816   4032   -567    638   -342  A    N  
ATOM    652  OD1 ASN A  74      28.899  15.122  31.221  1.00 32.04      A    O  
ANISOU  652  OD1 ASN A  74     4611   3407   4155   -282    400     62  A    O  
ATOM    653  N   MET A  75      26.598  10.352  31.816  1.00 26.99      A    N  
ANISOU  653  N   MET A  75     3550   3366   3337   -265    266     20  A    N  
ATOM    654  CA  MET A  75      25.814   9.189  31.405  1.00 25.87      A    C  
ANISOU  654  CA  MET A  75     3356   3153   3317   -136    256     33  A    C  
ATOM    655  C   MET A  75      24.336   9.564  31.301  1.00 26.23      A    C  
ANISOU  655  C   MET A  75     3423   3209   3333   -181    200    178  A    C  
ATOM    656  O   MET A  75      23.856  10.357  32.132  1.00 25.23      A    O  
ANISOU  656  O   MET A  75     3087   3013   3484     49    521    134  A    O  
ATOM    657  CB  MET A  75      26.007   8.050  32.426  1.00 25.38      A    C  
ANISOU  657  CB  MET A  75     3390   3236   3015   -236    286    273  A    C  
ATOM    658  CG  MET A  75      25.048   6.862  32.204  1.00 23.34      A    C  
ANISOU  658  CG  MET A  75     3008   3061   2799   -295    437    177  A    C  
ATOM    659  SD  MET A  75      23.421   7.025  33.030  1.00 27.41      A    S  
ANISOU  659  SD  MET A  75     3181   3745   3488   -141    429    237  A    S  
ATOM    660  CE  MET A  75      23.971   7.539  34.658  1.00 27.62      A    C  
ANISOU  660  CE  MET A  75     2932   4280   3281      9   -199     63  A    C  
ATOM    661  N   THR A  76      23.637   9.068  30.265  1.00 25.43      A    N  
ANISOU  661  N   THR A  76     3343   3194   3123   -102     20    221  A    N  
ATOM    662  CA  THR A  76      22.172   9.237  30.247  1.00 26.18      A    C  
ANISOU  662  CA  THR A  76     3481   3321   3146   -151    100    162  A    C  
ATOM    663  C   THR A  76      21.597   7.873  29.883  1.00 25.76      A    C  
ANISOU  663  C   THR A  76     3431   3348   3006    -38     67    139  A    C  
ATOM    664  O   THR A  76      22.340   7.001  29.428  1.00 24.07      A    O  
ANISOU  664  O   THR A  76     3538   3021   2584    114     26    -37  A    O  
ATOM    665  CB  THR A  76      21.673  10.313  29.199  1.00 26.35      A    C  
ANISOU  665  CB  THR A  76     3442   3525   3044   -262     33     68  A    C  
ATOM    666  CG2 THR A  76      22.362  11.634  29.311  1.00 25.34      A    C  
ANISOU  666  CG2 THR A  76     3717   3064   2847   -291    454   -112  A    C  
ATOM    667  OG1 THR A  76      21.845   9.781  27.919  1.00 26.04      A    O  
ANISOU  667  OG1 THR A  76     3618   3495   2779   -286    302     30  A    O  
ATOM    668  N   VAL A  77      20.296   7.663  30.036  1.00 24.06      A    N  
ANISOU  668  N   VAL A  77     3004   3311   2827   -103    331     68  A    N  
ATOM    669  CA  VAL A  77      19.792   6.409  29.488  1.00 25.51      A    C  
ANISOU  669  CA  VAL A  77     3190   3495   3005    -70    358    -20  A    C  
ATOM    670  C   VAL A  77      20.014   6.314  27.928  1.00 26.17      A    C  
ANISOU  670  C   VAL A  77     3190   3609   3144     23    370     47  A    C  
ATOM    671  O   VAL A  77      20.189   5.219  27.400  1.00 26.02      A    O  
ANISOU  671  O   VAL A  77     3299   3572   3013     61    422    129  A    O  
ATOM    672  CB  VAL A  77      18.339   6.197  29.760  1.00 25.16      A    C  
ANISOU  672  CB  VAL A  77     2967   3531   3061   -222    253    -23  A    C  
ATOM    673  CG1 VAL A  77      17.845   4.941  29.054  1.00 25.35      A    C  
ANISOU  673  CG1 VAL A  77     3043   3078   3510   -312    794     97  A    C  
ATOM    674  CG2 VAL A  77      18.149   6.108  31.212  1.00 26.14      A    C  
ANISOU  674  CG2 VAL A  77     3058   3781   3091   -308    517   -144  A    C  
ATOM    675  N   LEU A  78      19.932   7.434  27.217  1.00 25.70      A    N  
ANISOU  675  N   LEU A  78     3208   3702   2854     63    244    177  A    N  
ATOM    676  CA  LEU A  78      20.162   7.442  25.772  1.00 27.15      A    C  
ANISOU  676  CA  LEU A  78     3341   3777   3195    281    242    104  A    C  
ATOM    677  C   LEU A  78      21.570   6.973  25.408  1.00 26.07      A    C  
ANISOU  677  C   LEU A  78     3224   3561   3117    232    152    130  A    C  
ATOM    678  O   LEU A  78      21.708   6.118  24.539  1.00 24.61      A    O  
ANISOU  678  O   LEU A  78     2702   3636   3012    652    432     -6  A    O  
ATOM    679  CB  LEU A  78      19.911   8.851  25.207  1.00 28.24      A    C  
ANISOU  679  CB  LEU A  78     3636   3881   3212    178     68    222  A    C  
ATOM    680  CG  LEU A  78      20.345   9.080  23.744  1.00 29.07      A    C  
ANISOU  680  CG  LEU A  78     3883   3873   3288    247     56     33  A    C  
ATOM    681  CD1 LEU A  78      19.630   8.095  22.806  1.00 32.46      A    C  
ANISOU  681  CD1 LEU A  78     4402   4428   3503   -286    -86     32  A    C  
ATOM    682  CD2 LEU A  78      20.159  10.511  23.338  1.00 32.41      A    C  
ANISOU  682  CD2 LEU A  78     4876   3508   3930    316    124     54  A    C  
ATOM    683  N   ASN A  79      22.598   7.468  26.070  1.00 24.39      A    N  
ANISOU  683  N   ASN A  79     2877   3387   3003    150    106    177  A    N  
ATOM    684  CA  ASN A  79      23.927   7.032  25.663  1.00 25.34      A    C  
ANISOU  684  CA  ASN A  79     3205   3279   3142   -103    152    121  A    C  
ATOM    685  C   ASN A  79      24.253   5.617  26.171  1.00 24.97      A    C  
ANISOU  685  C   ASN A  79     3105   3267   3115   -126    111    111  A    C  
ATOM    686  O   ASN A  79      25.054   4.928  25.582  1.00 24.75      A    O  
ANISOU  686  O   ASN A  79     3067   3047   3287    -20    172    220  A    O  
ATOM    687  CB  ASN A  79      25.015   8.110  25.870  1.00 26.02      A    C  
ANISOU  687  CB  ASN A  79     3248   3378   3257   -253    168    230  A    C  
ATOM    688  CG  ASN A  79      25.169   8.551  27.300  1.00 25.86      A    C  
ANISOU  688  CG  ASN A  79     3336   3243   3245    -62    430    224  A    C  
ATOM    689  ND2 ASN A  79      25.418   9.859  27.480  1.00 27.11      A    N  
ANISOU  689  ND2 ASN A  79     3362   3556   3381   -127    328    786  A    N  
ATOM    690  OD1 ASN A  79      25.073   7.752  28.245  1.00 25.71      A    O  
ANISOU  690  OD1 ASN A  79     3621   2942   3206   -303    272    300  A    O  
ATOM    691  N   GLU A  80      23.494   5.139  27.158  1.00 25.54      A    N  
ANISOU  691  N   GLU A  80     3189   3310   3205   -341    117    167  A    N  
ATOM    692  CA  GLU A  80      23.557   3.722  27.519  1.00 26.57      A    C  
ANISOU  692  CA  GLU A  80     3337   3441   3314   -204     -8    115  A    C  
ATOM    693  C   GLU A  80      22.908   2.845  26.441  1.00 26.30      A    C  
ANISOU  693  C   GLU A  80     3319   3525   3148    -19     -8     30  A    C  
ATOM    694  O   GLU A  80      23.413   1.747  26.154  1.00 27.77      A    O  
ANISOU  694  O   GLU A  80     3372   3540   3638    -41    -23    105  A    O  
ATOM    695  CB  GLU A  80      22.863   3.467  28.863  1.00 25.74      A    C  
ANISOU  695  CB  GLU A  80     3376   3481   2923   -390   -125    232  A    C  
ATOM    696  CG  GLU A  80      23.697   4.068  30.080  1.00 27.26      A    C  
ANISOU  696  CG  GLU A  80     3616   3595   3145   -471   -390    340  A    C  
ATOM    697  CD  GLU A  80      23.422   3.433  31.428  1.00 26.69      A    C  
ANISOU  697  CD  GLU A  80     3257   3285   3598     17   -303    627  A    C  
ATOM    698  OE1 GLU A  80      22.323   2.863  31.643  1.00 28.17      A    O  
ANISOU  698  OE1 GLU A  80     3370   3748   3583   -322    101    -40  A    O  
ATOM    699  OE2 GLU A  80      24.315   3.614  32.311  1.00 25.07      A    O1-
ANISOU  699  OE2 GLU A  80     2853   3601   3070    164    252    361  A    O1-
ATOM    700  N   ILE A  81      21.816   3.297  25.839  1.00 25.59      A    N  
ANISOU  700  N   ILE A  81     3143   3466   3112     21    264     54  A    N  
ATOM    701  CA  ILE A  81      21.256   2.620  24.653  1.00 25.46      A    C  
ANISOU  701  CA  ILE A  81     2981   3663   3030     12    122    -10  A    C  
ATOM    702  C   ILE A  81      22.276   2.573  23.522  1.00 25.23      A    C  
ANISOU  702  C   ILE A  81     3169   3443   2973     51     89     86  A    C  
ATOM    703  O   ILE A  81      22.423   1.548  22.842  1.00 26.93      A    O  
ANISOU  703  O   ILE A  81     3561   3560   3112    146    112     85  A    O  
ATOM    704  CB  ILE A  81      19.918   3.253  24.166  1.00 25.78      A    C  
ANISOU  704  CB  ILE A  81     3125   3719   2950     30     67    -56  A    C  
ATOM    705  CG1 ILE A  81      18.853   3.021  25.270  1.00 24.26      A    C  
ANISOU  705  CG1 ILE A  81     2891   3724   2603    -36    229    -72  A    C  
ATOM    706  CG2 ILE A  81      19.442   2.574  22.831  1.00 27.15      A    C  
ANISOU  706  CG2 ILE A  81     3053   4235   3025    -97     63   -341  A    C  
ATOM    707  CD1 ILE A  81      17.552   3.777  25.068  1.00 29.70      A    C  
ANISOU  707  CD1 ILE A  81     3494   3965   3825    383    171    197  A    C  
ATOM    708  N   GLU A  82      22.989   3.664  23.334  1.00 25.05      A    N  
ANISOU  708  N   GLU A  82     3028   3485   3002     -7   -133     99  A    N  
ATOM    709  CA  GLU A  82      24.085   3.673  22.360  1.00 25.60      A    C  
ANISOU  709  CA  GLU A  82     3251   3243   3231    -83     25     95  A    C  
ATOM    710  C   GLU A  82      25.204   2.692  22.705  1.00 27.13      A    C  
ANISOU  710  C   GLU A  82     3386   3489   3430   -121   -124    124  A    C  
ATOM    711  O   GLU A  82      25.707   1.956  21.803  1.00 27.01      A    O  
ANISOU  711  O   GLU A  82     3204   3428   3626   -200    -40    -32  A    O  
ATOM    712  CB  GLU A  82      24.611   5.105  22.161  1.00 25.98      A    C  
ANISOU  712  CB  GLU A  82     3440   3086   3343   -137     -1    225  A    C  
ATOM    713  CG  GLU A  82      23.446   5.967  21.592  1.00 24.36      A    C  
ANISOU  713  CG  GLU A  82     3242   3244   2766      7     27    120  A    C  
ATOM    714  CD  GLU A  82      23.790   7.449  21.507  1.00 30.01      A    C  
ANISOU  714  CD  GLU A  82     4130   3477   3794      7   -225    103  A    C  
ATOM    715  OE1 GLU A  82      24.721   7.933  22.225  1.00 27.70      A    O  
ANISOU  715  OE1 GLU A  82     3594   3691   3240    171    526   -479  A    O  
ATOM    716  OE2 GLU A  82      23.130   8.142  20.703  1.00 32.60      A    O1-
ANISOU  716  OE2 GLU A  82     4631   3777   3978     36    -17    133  A    O1-
ATOM    717  N   ASP A  83      25.577   2.623  23.997  1.00 26.40      A    N  
ANISOU  717  N   ASP A  83     3226   3452   3350   -103   -254    136  A    N  
ATOM    718  CA  ASP A  83      26.533   1.580  24.398  1.00 27.13      A    C  
ANISOU  718  CA  ASP A  83     3518   3444   3344     32   -205    144  A    C  
ATOM    719  C   ASP A  83      26.003   0.177  24.047  1.00 27.32      A    C  
ANISOU  719  C   ASP A  83     3413   3585   3380     75   -150    111  A    C  
ATOM    720  O   ASP A  83      26.757  -0.692  23.555  1.00 26.63      A    O  
ANISOU  720  O   ASP A  83     3342   3420   3356    270    -93     85  A    O  
ATOM    721  CB  ASP A  83      26.676   1.604  25.900  1.00 27.78      A    C  
ANISOU  721  CB  ASP A  83     3653   3537   3365    -55   -451    166  A    C  
ATOM    722  CG  ASP A  83      27.468   2.830  26.418  1.00 28.10      A    C  
ANISOU  722  CG  ASP A  83     3811   3529   3334    -65   -179    -29  A    C  
ATOM    723  OD1 ASP A  83      28.176   3.577  25.636  1.00 28.33      A    O  
ANISOU  723  OD1 ASP A  83     3848   3656   3258     41   -293    498  A    O  
ATOM    724  OD2 ASP A  83      27.365   3.013  27.612  1.00 29.69      A    O1-
ANISOU  724  OD2 ASP A  83     3878   4113   3289      6   -299     75  A    O1-
ATOM    725  N   ALA A  84      24.727  -0.067  24.392  1.00 26.23      A    N  
ANISOU  725  N   ALA A  84     3146   3551   3269    140     77    285  A    N  
ATOM    726  CA  ALA A  84      24.056  -1.358  24.105  1.00 26.94      A    C  
ANISOU  726  CA  ALA A  84     3175   3695   3363     37    227    129  A    C  
ATOM    727  C   ALA A  84      24.083  -1.734  22.622  1.00 28.43      A    C  
ANISOU  727  C   ALA A  84     3456   3700   3644      0    -72     53  A    C  
ATOM    728  O   ALA A  84      24.337  -2.884  22.297  1.00 29.40      A    O  
ANISOU  728  O   ALA A  84     3507   3687   3976    194     71     77  A    O  
ATOM    729  CB  ALA A  84      22.580  -1.408  24.712  1.00 26.85      A    C  
ANISOU  729  CB  ALA A  84     3146   3869   3185   -100    372    299  A    C  
ATOM    730  N   ASN A  85      23.892  -0.770  21.731  1.00 27.24      A    N  
ANISOU  730  N   ASN A  85     3400   3535   3412     16     93    103  A    N  
ATOM    731  CA  ASN A  85      23.878  -1.041  20.319  1.00 27.08      A    C  
ANISOU  731  CA  ASN A  85     3271   3611   3405    -36     57    114  A    C  
ATOM    732  C   ASN A  85      25.318  -1.409  19.854  1.00 26.97      A    C  
ANISOU  732  C   ASN A  85     3493   3531   3221     -2    166    111  A    C  
ATOM    733  O   ASN A  85      25.487  -2.266  18.986  1.00 27.60      A    O  
ANISOU  733  O   ASN A  85     3353   3522   3609    250    211     64  A    O  
ATOM    734  CB  ASN A  85      23.420   0.211  19.609  1.00 24.76      A    C  
ANISOU  734  CB  ASN A  85     2969   3462   2976    -38     88      6  A    C  
ATOM    735  CG  ASN A  85      23.417   0.023  18.130  1.00 28.14      A    C  
ANISOU  735  CG  ASN A  85     3186   3933   3571   -169    195     91  A    C  
ATOM    736  ND2 ASN A  85      24.334   0.708  17.440  1.00 25.64      A    N  
ANISOU  736  ND2 ASN A  85     2968   3684   3090     58    629    339  A    N  
ATOM    737  OD1 ASN A  85      22.662  -0.789  17.611  1.00 28.18      A    O  
ANISOU  737  OD1 ASN A  85     3323   3636   3746   -143     43    -53  A    O  
ATOM    738  N   ALA A  86      26.336  -0.722  20.390  1.00 26.55      A    N  
ANISOU  738  N   ALA A  86     3296   3544   3248   -138    178     51  A    N  
ATOM    739  CA  ALA A  86      27.771  -1.061  20.153  1.00 28.07      A    C  
ANISOU  739  CA  ALA A  86     3613   3596   3457    -82    196    -34  A    C  
ATOM    740  C   ALA A  86      28.090  -2.515  20.555  1.00 27.70      A    C  
ANISOU  740  C   ALA A  86     3588   3517   3420      7    123     -3  A    C  
ATOM    741  O   ALA A  86      28.768  -3.227  19.860  1.00 28.32      A    O  
ANISOU  741  O   ALA A  86     3756   3561   3441    228     50     56  A    O  
ATOM    742  CB  ALA A  86      28.727  -0.103  20.899  1.00 27.04      A    C  
ANISOU  742  CB  ALA A  86     3210   3438   3624   -389    375    -12  A    C  
ATOM    743  N   ILE A  87      27.496  -2.946  21.667  1.00 27.68      A    N  
ANISOU  743  N   ILE A  87     3878   3416   3220     60    -46    -18  A    N  
ATOM    744  CA  ILE A  87      27.701  -4.288  22.189  1.00 28.45      A    C  
ANISOU  744  CA  ILE A  87     3848   3558   3401     41    162    -94  A    C  
ATOM    745  C   ILE A  87      26.953  -5.273  21.274  1.00 28.47      A    C  
ANISOU  745  C   ILE A  87     3883   3629   3304     39      0    -52  A    C  
ATOM    746  O   ILE A  87      27.521  -6.301  20.866  1.00 28.18      A    O  
ANISOU  746  O   ILE A  87     4117   3536   3052    -91    115    -25  A    O  
ATOM    747  CB  ILE A  87      27.294  -4.392  23.676  1.00 27.46      A    C  
ANISOU  747  CB  ILE A  87     3759   3512   3159    124    177   -130  A    C  
ATOM    748  CG1 ILE A  87      28.157  -3.454  24.572  1.00 25.60      A    C  
ANISOU  748  CG1 ILE A  87     3165   3595   2967    112    754   -265  A    C  
ATOM    749  CG2 ILE A  87      27.337  -5.889  24.221  1.00 25.26      A    C  
ANISOU  749  CG2 ILE A  87     3476   3160   2960     89    389   -144  A    C  
ATOM    750  CD1 ILE A  87      27.439  -3.122  25.910  1.00 23.49      A    C  
ANISOU  750  CD1 ILE A  87     3309   3415   2199     31   1282    310  A    C  
ATOM    751  N   LEU A  88      25.709  -4.926  20.932  1.00 29.28      A    N  
ANISOU  751  N   LEU A  88     3745   3848   3532    -42    134   -142  A    N  
ATOM    752  CA  LEU A  88      24.964  -5.685  19.918  1.00 30.58      A    C  
ANISOU  752  CA  LEU A  88     3848   3871   3899     90   -126   -169  A    C  
ATOM    753  C   LEU A  88      25.739  -5.856  18.608  1.00 31.70      A    C  
ANISOU  753  C   LEU A  88     3918   3995   4130    156     21   -304  A    C  
ATOM    754  O   LEU A  88      25.697  -6.923  18.032  1.00 33.71      A    O  
ANISOU  754  O   LEU A  88     4039   4194   4573    213   -221   -288  A    O  
ATOM    755  CB  LEU A  88      23.564  -5.107  19.647  1.00 29.97      A    C  
ANISOU  755  CB  LEU A  88     3778   3880   3728     64   -107   -247  A    C  
ATOM    756  CG  LEU A  88      22.631  -5.962  18.803  1.00 27.09      A    C  
ANISOU  756  CG  LEU A  88     3725   3242   3324    -84   -419    333  A    C  
ATOM    757  CD1 LEU A  88      22.427  -7.344  19.407  1.00 29.10      A    C  
ANISOU  757  CD1 LEU A  88     3866   3189   4001    105   -535    272  A    C  
ATOM    758  CD2 LEU A  88      21.282  -5.251  18.716  1.00 29.29      A    C  
ANISOU  758  CD2 LEU A  88     3314   4316   3499     39    -26    423  A    C  
ATOM    759  N   ASN A  89      26.402  -4.791  18.116  1.00 33.31      A    N  
ANISOU  759  N   ASN A  89     4067   4235   4353    219     92   -280  A    N  
ATOM    760  CA  ASN A  89      27.233  -4.863  16.895  1.00 32.78      A    C  
ANISOU  760  CA  ASN A  89     4212   4274   3968    222     57   -487  A    C  
ATOM    761  C   ASN A  89      28.277  -5.975  16.991  1.00 32.94      A    C  
ANISOU  761  C   ASN A  89     4104   4359   4052    285    -36   -434  A    C  
ATOM    762  O   ASN A  89      28.494  -6.730  16.023  1.00 33.21      A    O  
ANISOU  762  O   ASN A  89     4073   4356   4187    541    203   -757  A    O  
ATOM    763  CB  ASN A  89      27.970  -3.546  16.648  1.00 33.59      A    C  
ANISOU  763  CB  ASN A  89     4370   4334   4055    219    -23   -308  A    C  
ATOM    764  CG  ASN A  89      27.048  -2.444  16.113  1.00 35.05      A    C  
ANISOU  764  CG  ASN A  89     4458   4564   4295    130    -97   -438  A    C  
ATOM    765  ND2 ASN A  89      27.533  -1.207  16.148  1.00 36.01      A    N  
ANISOU  765  ND2 ASN A  89     4927   4488   4267     50    488   -138  A    N  
ATOM    766  OD1 ASN A  89      25.929  -2.714  15.639  1.00 36.63      A    O  
ANISOU  766  OD1 ASN A  89     4471   5032   4414   -299   -439   -685  A    O  
ATOM    767  N   TYR A  90      28.983  -6.011  18.119  1.00 33.25      A    N  
ANISOU  767  N   TYR A  90     4159   4411   4062    305     30   -312  A    N  
ATOM    768  CA  TYR A  90      29.969  -7.068  18.425  1.00 33.52      A    C  
ANISOU  768  CA  TYR A  90     4160   4475   4097    176   -134   -247  A    C  
ATOM    769  C   TYR A  90      29.318  -8.480  18.422  1.00 33.06      A    C  
ANISOU  769  C   TYR A  90     4119   4350   4092    181   -157   -317  A    C  
ATOM    770  O   TYR A  90      29.847  -9.409  17.808  1.00 33.52      A    O  
ANISOU  770  O   TYR A  90     4388   4168   4178    121   -220   -476  A    O  
ATOM    771  CB  TYR A  90      30.658  -6.742  19.803  1.00 32.30      A    C  
ANISOU  771  CB  TYR A  90     3797   4463   4011    144   -257   -282  A    C  
ATOM    772  CG  TYR A  90      31.400  -7.917  20.439  1.00 33.62      A    C  
ANISOU  772  CG  TYR A  90     3806   4687   4280    262     95   -202  A    C  
ATOM    773  CD1 TYR A  90      32.656  -8.298  19.971  1.00 32.56      A    C  
ANISOU  773  CD1 TYR A  90     3063   4438   4869    219   -204   -288  A    C  
ATOM    774  CD2 TYR A  90      30.836  -8.661  21.474  1.00 35.91      A    C  
ANISOU  774  CD2 TYR A  90     4033   5060   4548    301   -148      4  A    C  
ATOM    775  CE1 TYR A  90      33.355  -9.327  20.569  1.00 33.41      A    C  
ANISOU  775  CE1 TYR A  90     3512   4726   4455    519    285   -347  A    C  
ATOM    776  CE2 TYR A  90      31.513  -9.728  22.057  1.00 33.07      A    C  
ANISOU  776  CE2 TYR A  90     3610   4646   4309    381   -271   -579  A    C  
ATOM    777  CZ  TYR A  90      32.770 -10.050  21.578  1.00 33.92      A    C  
ANISOU  777  CZ  TYR A  90     3970   4664   4251    323   -170   -356  A    C  
ATOM    778  OH  TYR A  90      33.460 -11.076  22.136  1.00 37.48      A    O  
ANISOU  778  OH  TYR A  90     4568   4718   4955    378     24   -459  A    O  
ATOM    779  N   VAL A  91      28.161  -8.616  19.087  1.00 32.70      A    N  
ANISOU  779  N   VAL A  91     4098   4253   4070    152   -206   -199  A    N  
ATOM    780  CA  VAL A  91      27.481  -9.912  19.270  1.00 32.39      A    C  
ANISOU  780  CA  VAL A  91     3960   4154   4191    202    -25   -158  A    C  
ATOM    781  C   VAL A  91      26.917 -10.430  17.943  1.00 32.54      A    C  
ANISOU  781  C   VAL A  91     4215   4037   4112    195     30   -145  A    C  
ATOM    782  O   VAL A  91      27.120 -11.599  17.622  1.00 33.05      A    O  
ANISOU  782  O   VAL A  91     4381   4008   4167    269    190   -213  A    O  
ATOM    783  CB  VAL A  91      26.346  -9.877  20.378  1.00 31.32      A    C  
ANISOU  783  CB  VAL A  91     3962   3952   3986    150      8   -124  A    C  
ATOM    784  CG1 VAL A  91      25.611 -11.200  20.437  1.00 32.99      A    C  
ANISOU  784  CG1 VAL A  91     3662   4242   4627     60    578   -284  A    C  
ATOM    785  CG2 VAL A  91      26.876  -9.462  21.811  1.00 33.83      A    C  
ANISOU  785  CG2 VAL A  91     3937   4528   4389    301    -66    153  A    C  
ATOM    786  N   LYS A  92      26.274  -9.558  17.157  1.00 33.46      A    N  
ANISOU  786  N   LYS A  92     4383   4083   4246    296    -54   -238  A    N  
ATOM    787  CA  LYS A  92      25.555  -9.994  15.946  1.00 34.37      A    C  
ANISOU  787  CA  LYS A  92     4664   4180   4214    243   -171    -63  A    C  
ATOM    788  C   LYS A  92      26.513 -10.365  14.815  1.00 36.38      A    C  
ANISOU  788  C   LYS A  92     4985   4482   4353    232   -164   -114  A    C  
ATOM    789  O   LYS A  92      26.105 -10.946  13.847  1.00 37.98      A    O  
ANISOU  789  O   LYS A  92     5287   4701   4443    171   -149   -385  A    O  
ATOM    790  CB  LYS A  92      24.544  -8.951  15.461  1.00 34.37      A    C  
ANISOU  790  CB  LYS A  92     4685   4021   4352    171   -161   -118  A    C  
ATOM    791  CG  LYS A  92      25.181  -7.720  14.814  1.00 31.84      A    C  
ANISOU  791  CG  LYS A  92     4746   3916   3435    207   -223    108  A    C  
ATOM    792  CD  LYS A  92      24.083  -6.687  14.488  1.00 35.47      A    C  
ANISOU  792  CD  LYS A  92     5113   3972   4393      4   -776    253  A    C  
ATOM    793  CE  LYS A  92      24.652  -5.433  13.866  1.00 35.35      A    C  
ANISOU  793  CE  LYS A  92     5414   3978   4038   -241  -1105    176  A    C  
ATOM    794  NZ  LYS A  92      23.577  -4.392  13.869  1.00 38.63      A    N1+
ANISOU  794  NZ  LYS A  92     5227   4392   5059   -150  -1053   -180  A    N1+
ATOM    795  N   THR A  93      27.781 -10.021  14.919  1.00 36.67      A    N  
ANISOU  795  N   THR A  93     4875   4645   4411    272    -24     27  A    N  
ATOM    796  CA  THR A  93      28.743 -10.413  13.869  1.00 38.70      A    C  
ANISOU  796  CA  THR A  93     5245   4971   4486    339     42    -21  A    C  
ATOM    797  C   THR A  93      29.566 -11.611  14.351  1.00 38.44      A    C  
ANISOU  797  C   THR A  93     5089   4924   4592    348      3     -3  A    C  
ATOM    798  O   THR A  93      30.528 -11.996  13.707  1.00 40.30      A    O  
ANISOU  798  O   THR A  93     5541   5184   4585    399     84     87  A    O  
ATOM    799  CB  THR A  93      29.720  -9.281  13.492  1.00 38.71      A    C  
ANISOU  799  CB  THR A  93     4957   5221   4528    320     14    -54  A    C  
ATOM    800  CG2 THR A  93      29.028  -8.125  12.753  1.00 39.76      A    C  
ANISOU  800  CG2 THR A  93     5477   5219   4410    287    313     93  A    C  
ATOM    801  OG1 THR A  93      30.306  -8.767  14.684  1.00 42.19      A    O  
ANISOU  801  OG1 THR A  93     5443   6129   4457    227    366   -187  A    O  
ATOM    802  N   ASP A  94      29.252 -12.161  15.527  1.00 37.55      A    N  
ANISOU  802  N   ASP A  94     4925   4574   4767    225     38    -66  A    N  
ATOM    803  CA  ASP A  94      29.992 -13.339  15.960  1.00 36.24      A    C  
ANISOU  803  CA  ASP A  94     4673   4396   4700    232    -91    -36  A    C  
ATOM    804  C   ASP A  94      29.478 -14.588  15.236  1.00 35.62      A    C  
ANISOU  804  C   ASP A  94     4477   4242   4814    285     58    -84  A    C  
ATOM    805  O   ASP A  94      28.320 -14.919  15.357  1.00 34.52      A    O  
ANISOU  805  O   ASP A  94     4196   4004   4916    734   -229   -102  A    O  
ATOM    806  CB  ASP A  94      29.860 -13.534  17.440  1.00 36.02      A    C  
ANISOU  806  CB  ASP A  94     4711   4278   4697    162     13    -41  A    C  
ATOM    807  CG  ASP A  94      30.771 -14.610  17.931  1.00 35.83      A    C  
ANISOU  807  CG  ASP A  94     4595   4235   4781    211    -11   -145  A    C  
ATOM    808  OD1 ASP A  94      31.698 -14.305  18.723  1.00 37.41      A    O  
ANISOU  808  OD1 ASP A  94     5391   4314   4507    196    -53   -299  A    O  
ATOM    809  OD2 ASP A  94      30.597 -15.756  17.484  1.00 35.82      A    O1-
ANISOU  809  OD2 ASP A  94     4855   4113   4641    286   -306     46  A    O1-
ATOM    810  N   PRO A  95      30.351 -15.311  14.499  1.00 37.09      A    N  
ANISOU  810  N   PRO A  95     4404   4569   5119    134    104   -206  A    N  
ATOM    811  CA  PRO A  95      29.831 -16.397  13.665  1.00 37.15      A    C  
ANISOU  811  CA  PRO A  95     4445   4649   5022    104    146   -334  A    C  
ATOM    812  C   PRO A  95      29.272 -17.604  14.439  1.00 37.00      A    C  
ANISOU  812  C   PRO A  95     4342   4727   4989    -35     72   -380  A    C  
ATOM    813  O   PRO A  95      28.638 -18.446  13.835  1.00 36.53      A    O  
ANISOU  813  O   PRO A  95     4094   4834   4950   -164   -112   -621  A    O  
ATOM    814  CB  PRO A  95      31.091 -16.852  12.866  1.00 37.81      A    C  
ANISOU  814  CB  PRO A  95     4306   4864   5195    -28    207   -340  A    C  
ATOM    815  CG  PRO A  95      32.243 -16.346  13.657  1.00 37.18      A    C  
ANISOU  815  CG  PRO A  95     4310   4824   4992     53    164   -417  A    C  
ATOM    816  CD  PRO A  95      31.750 -15.002  14.131  1.00 37.14      A    C  
ANISOU  816  CD  PRO A  95     4248   4660   5203    171    250   -199  A    C  
ATOM    817  N   HIS A  96      29.573 -17.724  15.736  1.00 35.95      A    N  
ANISOU  817  N   HIS A  96     4284   4674   4698    146     73   -296  A    N  
ATOM    818  CA  HIS A  96      29.061 -18.847  16.568  1.00 35.55      A    C  
ANISOU  818  CA  HIS A  96     4012   4665   4830    154    103   -211  A    C  
ATOM    819  C   HIS A  96      27.660 -18.609  17.128  1.00 35.40      A    C  
ANISOU  819  C   HIS A  96     4069   4544   4836    204     24   -184  A    C  
ATOM    820  O   HIS A  96      27.036 -19.544  17.662  1.00 35.23      A    O  
ANISOU  820  O   HIS A  96     4263   4231   4891    243    -79     15  A    O  
ATOM    821  CB  HIS A  96      30.009 -19.160  17.766  1.00 35.21      A    C  
ANISOU  821  CB  HIS A  96     3817   4970   4589     32    202   -161  A    C  
ATOM    822  CG  HIS A  96      31.433 -19.429  17.359  1.00 36.77      A    C  
ANISOU  822  CG  HIS A  96     3798   4836   5335    180    211   -422  A    C  
ATOM    823  CD2 HIS A  96      32.491 -18.587  17.183  1.00 38.35      A    C  
ANISOU  823  CD2 HIS A  96     3436   5218   5916     -7    365   -644  A    C  
ATOM    824  ND1 HIS A  96      31.897 -20.693  17.055  1.00 36.15      A    N  
ANISOU  824  ND1 HIS A  96     3359   4768   5605    336    333   -263  A    N  
ATOM    825  CE1 HIS A  96      33.173 -20.622  16.703  1.00 37.72      A    C  
ANISOU  825  CE1 HIS A  96     3621   4784   5927   -129    337   -513  A    C  
ATOM    826  NE2 HIS A  96      33.556 -19.360  16.773  1.00 38.49      A    N  
ANISOU  826  NE2 HIS A  96     3466   4998   6158   -196    318   -285  A    N  
ATOM    827  N   VAL A  97      27.173 -17.361  17.079  1.00 33.66      A    N  
ANISOU  827  N   VAL A  97     3878   4299   4612    386     35   -201  A    N  
ATOM    828  CA  VAL A  97      25.966 -17.061  17.809  1.00 33.91      A    C  
ANISOU  828  CA  VAL A  97     3750   4328   4805    423    176   -376  A    C  
ATOM    829  C   VAL A  97      24.752 -17.407  16.957  1.00 35.62      A    C  
ANISOU  829  C   VAL A  97     4144   4469   4920    377    109   -313  A    C  
ATOM    830  O   VAL A  97      24.665 -17.039  15.778  1.00 35.63      A    O  
ANISOU  830  O   VAL A  97     4167   4411   4960    425     97   -218  A    O  
ATOM    831  CB  VAL A  97      25.955 -15.559  18.232  1.00 34.64      A    C  
ANISOU  831  CB  VAL A  97     3787   4569   4803    406    243   -519  A    C  
ATOM    832  CG1 VAL A  97      24.588 -15.138  18.725  1.00 33.79      A    C  
ANISOU  832  CG1 VAL A  97     3609   4390   4836    805    529   -758  A    C  
ATOM    833  CG2 VAL A  97      27.018 -15.327  19.280  1.00 30.04      A    C  
ANISOU  833  CG2 VAL A  97     3396   4142   3875    260    407   -760  A    C  
ATOM    834  N   ARG A  98      23.820 -18.133  17.575  1.00 36.54      A    N  
ANISOU  834  N   ARG A  98     4106   4579   5198    391     57   -247  A    N  
ATOM    835  CA  ARG A  98      22.574 -18.479  16.952  1.00 37.55      A    C  
ANISOU  835  CA  ARG A  98     4342   4594   5330    346     -1   -316  A    C  
ATOM    836  C   ARG A  98      21.477 -17.447  17.356  1.00 37.97      A    C  
ANISOU  836  C   ARG A  98     4319   4775   5331    413   -102   -339  A    C  
ATOM    837  O   ARG A  98      21.149 -16.562  16.547  1.00 39.17      A    O  
ANISOU  837  O   ARG A  98     4426   4730   5724    694      7   -335  A    O  
ATOM    838  CB  ARG A  98      22.221 -19.899  17.326  1.00 37.54      A    C  
ANISOU  838  CB  ARG A  98     4529   4360   5372    362     -5   -249  A    C  
ATOM    839  CG  ARG A  98      20.849 -20.352  16.836  1.00 39.52      A    C  
ANISOU  839  CG  ARG A  98     4653   4610   5750    345   -118   -122  A    C  
ATOM    840  CD  ARG A  98      20.641 -21.820  17.113  1.00 43.05      A    C  
ANISOU  840  CD  ARG A  98     5886   4508   5960   -416    318   -122  A    C  
ATOM    841  NE  ARG A  98      20.622 -22.098  18.549  1.00 47.41      A    N  
ANISOU  841  NE  ARG A  98     6833   4932   6245   -455    -76   -495  A    N  
ATOM    842  CZ  ARG A  98      21.112 -23.205  19.128  1.00 49.24      A    C  
ANISOU  842  CZ  ARG A  98     7352   5425   5931   -133    236   -504  A    C  
ATOM    843  NH1 ARG A  98      21.697 -24.165  18.406  1.00 47.67      A    N1+
ANISOU  843  NH1 ARG A  98     7375   5032   5703   -231    355   -742  A    N1+
ATOM    844  NH2 ARG A  98      21.032 -23.346  20.455  1.00 49.11      A    N  
ANISOU  844  NH2 ARG A  98     7524   5567   5568   -130    807   -885  A    N  
ATOM    845  N   ASN A  99      20.908 -17.558  18.563  1.00 36.32      A    N  
ANISOU  845  N   ASN A  99     4120   4510   5166    223    -50   -505  A    N  
ATOM    846  CA  ASN A  99      19.904 -16.582  18.994  1.00 35.95      A    C  
ANISOU  846  CA  ASN A  99     4182   4248   5227      2   -119   -451  A    C  
ATOM    847  C   ASN A  99      20.533 -15.580  19.914  1.00 35.78      A    C  
ANISOU  847  C   ASN A  99     4290   4112   5190     10   -136   -390  A    C  
ATOM    848  O   ASN A  99      21.379 -15.942  20.747  1.00 36.36      A    O  
ANISOU  848  O   ASN A  99     4607   3968   5240      5   -399   -209  A    O  
ATOM    849  CB  ASN A  99      18.767 -17.261  19.753  1.00 34.64      A    C  
ANISOU  849  CB  ASN A  99     3825   4312   5023     31     -5   -481  A    C  
ATOM    850  CG  ASN A  99      18.003 -18.231  18.871  1.00 37.85      A    C  
ANISOU  850  CG  ASN A  99     4197   4698   5485    -42    -21   -223  A    C  
ATOM    851  ND2 ASN A  99      17.716 -19.415  19.409  1.00 43.50      A    N  
ANISOU  851  ND2 ASN A  99     4375   5302   6849   -748   -525     -2  A    N  
ATOM    852  OD1 ASN A  99      17.664 -17.922  17.726  1.00 38.68      A    O  
ANISOU  852  OD1 ASN A  99     4150   5425   5122    358    389    174  A    O  
ATOM    853  N   ILE A 100      20.059 -14.346  19.824  1.00 34.43      A    N  
ANISOU  853  N   ILE A 100     4256   3746   5079    -35   -152   -275  A    N  
ATOM    854  CA  ILE A 100      20.554 -13.297  20.734  1.00 32.71      A    C  
ANISOU  854  CA  ILE A 100     4075   3629   4721    -50     82   -269  A    C  
ATOM    855  C   ILE A 100      19.483 -12.952  21.762  1.00 31.74      A    C  
ANISOU  855  C   ILE A 100     3829   3480   4748   -108    195   -159  A    C  
ATOM    856  O   ILE A 100      18.310 -12.650  21.398  1.00 33.99      A    O  
ANISOU  856  O   ILE A 100     4165   3576   5171     60    113   -148  A    O  
ATOM    857  CB  ILE A 100      20.962 -12.046  19.960  1.00 30.94      A    C  
ANISOU  857  CB  ILE A 100     3690   3445   4619    -89     48   -193  A    C  
ATOM    858  CG1 ILE A 100      22.140 -12.351  19.039  1.00 33.07      A    C  
ANISOU  858  CG1 ILE A 100     4631   3702   4229    -42    276   -237  A    C  
ATOM    859  CG2 ILE A 100      21.440 -10.931  20.930  1.00 30.45      A    C  
ANISOU  859  CG2 ILE A 100     3977   3502   4090     14     56   -388  A    C  
ATOM    860  CD1 ILE A 100      22.405 -11.220  18.044  1.00 34.26      A    C  
ANISOU  860  CD1 ILE A 100     4198   4070   4747    146   1020    -70  A    C  
ATOM    861  N   TYR A 101      19.861 -13.001  23.028  1.00 31.03      A    N  
ANISOU  861  N   TYR A 101     3667   3490   4632    -62    345   -150  A    N  
ATOM    862  CA  TYR A 101      18.899 -12.666  24.112  1.00 30.20      A    C  
ANISOU  862  CA  TYR A 101     3492   3524   4456    -74    374   -236  A    C  
ATOM    863  C   TYR A 101      19.366 -11.377  24.789  1.00 31.10      A    C  
ANISOU  863  C   TYR A 101     3591   3677   4548   -175    379   -209  A    C  
ATOM    864  O   TYR A 101      20.573 -11.113  24.825  1.00 30.56      A    O  
ANISOU  864  O   TYR A 101     3502   3798   4311   -246    462   -116  A    O  
ATOM    865  CB  TYR A 101      18.815 -13.765  25.150  1.00 30.90      A    C  
ANISOU  865  CB  TYR A 101     3502   3457   4780     22    499   -231  A    C  
ATOM    866  CG  TYR A 101      18.550 -15.151  24.583  1.00 32.38      A    C  
ANISOU  866  CG  TYR A 101     3675   3663   4965      1    549   -297  A    C  
ATOM    867  CD1 TYR A 101      17.567 -15.364  23.604  1.00 33.14      A    C  
ANISOU  867  CD1 TYR A 101     3311   3688   5593    -78    551   -395  A    C  
ATOM    868  CD2 TYR A 101      19.299 -16.259  25.017  1.00 35.53      A    C  
ANISOU  868  CD2 TYR A 101     4519   3225   5754    -46    649    117  A    C  
ATOM    869  CE1 TYR A 101      17.308 -16.650  23.081  1.00 34.17      A    C  
ANISOU  869  CE1 TYR A 101     4077   3506   5399    114    424   -910  A    C  
ATOM    870  CE2 TYR A 101      19.032 -17.544  24.490  1.00 36.86      A    C  
ANISOU  870  CE2 TYR A 101     4798   3731   5474     71    580   -353  A    C  
ATOM    871  CZ  TYR A 101      18.059 -17.717  23.526  1.00 36.79      A    C  
ANISOU  871  CZ  TYR A 101     4414   3587   5977    -64    311   -574  A    C  
ATOM    872  OH  TYR A 101      17.827 -18.966  22.984  1.00 40.16      A    O  
ANISOU  872  OH  TYR A 101     4283   3559   7416   -395    558   -387  A    O  
ATOM    873  N   LEU A 102      18.435 -10.575  25.304  1.00 30.86      A    N  
ANISOU  873  N   LEU A 102     3402   3666   4656   -276    347   -108  A    N  
ATOM    874  CA  LEU A 102      18.797  -9.448  26.154  1.00 30.38      A    C  
ANISOU  874  CA  LEU A 102     3480   3616   4446    -92    362    -39  A    C  
ATOM    875  C   LEU A 102      18.294  -9.659  27.590  1.00 31.04      A    C  
ANISOU  875  C   LEU A 102     3717   3495   4582   -168    300    155  A    C  
ATOM    876  O   LEU A 102      17.185 -10.092  27.747  1.00 31.13      A    O  
ANISOU  876  O   LEU A 102     3820   3449   4558   -245    507    207  A    O  
ATOM    877  CB  LEU A 102      18.260  -8.124  25.575  1.00 31.06      A    C  
ANISOU  877  CB  LEU A 102     3583   3846   4369   -160    248    110  A    C  
ATOM    878  CG  LEU A 102      18.618  -7.780  24.140  1.00 29.53      A    C  
ANISOU  878  CG  LEU A 102     3078   3867   4275    151    301   -146  A    C  
ATOM    879  CD1 LEU A 102      17.924  -6.458  23.813  1.00 33.47      A    C  
ANISOU  879  CD1 LEU A 102     3646   3875   5194    204    466   -163  A    C  
ATOM    880  CD2 LEU A 102      20.193  -7.752  23.838  1.00 28.15      A    C  
ANISOU  880  CD2 LEU A 102     2810   4089   3793    137    205   -704  A    C  
ATOM    881  N   VAL A 103      19.089  -9.312  28.603  1.00 30.28      A    N  
ANISOU  881  N   VAL A 103     3822   3202   4481   -148    293    276  A    N  
ATOM    882  CA  VAL A 103      18.726  -9.482  29.970  1.00 30.19      A    C  
ANISOU  882  CA  VAL A 103     3863   3176   4431    -12    242     97  A    C  
ATOM    883  C   VAL A 103      19.103  -8.193  30.644  1.00 30.67      A    C  
ANISOU  883  C   VAL A 103     3898   3285   4470    -49    209    196  A    C  
ATOM    884  O   VAL A 103      20.249  -7.788  30.596  1.00 30.69      A    O  
ANISOU  884  O   VAL A 103     4152   3213   4292    -11    621    276  A    O  
ATOM    885  CB  VAL A 103      19.500 -10.673  30.689  1.00 30.48      A    C  
ANISOU  885  CB  VAL A 103     3763   3260   4558    -40    194    102  A    C  
ATOM    886  CG1 VAL A 103      19.246 -10.653  32.220  1.00 30.23      A    C  
ANISOU  886  CG1 VAL A 103     3878   3225   4380     24    116    355  A    C  
ATOM    887  CG2 VAL A 103      19.166 -12.071  30.047  1.00 29.01      A    C  
ANISOU  887  CG2 VAL A 103     3271   3523   4225   -128    751    -59  A    C  
ATOM    888  N   GLY A 104      18.157  -7.555  31.291  1.00 29.77      A    N  
ANISOU  888  N   GLY A 104     3970   3238   4101    -13    247     88  A    N  
ATOM    889  CA  GLY A 104      18.476  -6.291  31.959  1.00 30.39      A    C  
ANISOU  889  CA  GLY A 104     3948   3429   4167     36    196    153  A    C  
ATOM    890  C   GLY A 104      17.923  -6.110  33.358  1.00 30.78      A    C  
ANISOU  890  C   GLY A 104     3982   3600   4111    128    178    277  A    C  
ATOM    891  O   GLY A 104      16.730  -6.354  33.586  1.00 30.81      A    O  
ANISOU  891  O   GLY A 104     3978   3682   4046    108    313    360  A    O  
ATOM    892  N   HIS A 105      18.766  -5.629  34.273  1.00 29.56      A    N  
ANISOU  892  N   HIS A 105     3825   3745   3660    153    162    287  A    N  
ATOM    893  CA  HIS A 105      18.312  -5.292  35.612  1.00 30.36      A    C  
ANISOU  893  CA  HIS A 105     3899   3869   3765    -25    332    480  A    C  
ATOM    894  C   HIS A 105      18.108  -3.795  35.736  1.00 30.22      A    C  
ANISOU  894  C   HIS A 105     3919   3878   3682   -151    321    453  A    C  
ATOM    895  O   HIS A 105      19.040  -3.012  35.537  1.00 28.60      A    O  
ANISOU  895  O   HIS A 105     3761   3561   3542   -212    372    625  A    O  
ATOM    896  CB  HIS A 105      19.299  -5.790  36.680  1.00 29.33      A    C  
ANISOU  896  CB  HIS A 105     3768   4013   3360   -234    480    613  A    C  
ATOM    897  CG  HIS A 105      18.984  -5.339  38.090  1.00 32.32      A    C  
ANISOU  897  CG  HIS A 105     4479   4042   3758   -141    392    905  A    C  
ATOM    898  CD2 HIS A 105      19.633  -4.485  38.908  1.00 29.20      A    C  
ANISOU  898  CD2 HIS A 105     4357   4164   2573   -272    369   1389  A    C  
ATOM    899  ND1 HIS A 105      17.890  -5.798  38.813  1.00 32.93      A    N  
ANISOU  899  ND1 HIS A 105     4367   4269   3876    337    862    804  A    N  
ATOM    900  CE1 HIS A 105      17.897  -5.261  40.017  1.00 29.63      A    C  
ANISOU  900  CE1 HIS A 105     3972   4114   3170   -343    811   1106  A    C  
ATOM    901  NE2 HIS A 105      18.965  -4.494  40.118  1.00 34.09      A    N  
ANISOU  901  NE2 HIS A 105     4632   4523   3798   -304    856   1006  A    N  
ATOM    902  N   ALA A 106      16.884  -3.421  36.143  1.00 29.22      A    N  
ANISOU  902  N   ALA A 106     3813   3818   3471   -208    383    373  A    N  
ATOM    903  CA  ALA A 106      16.574  -2.064  36.572  1.00 29.46      A    C  
ANISOU  903  CA  ALA A 106     3929   3745   3518   -203    365    445  A    C  
ATOM    904  C   ALA A 106      16.799  -1.075  35.426  1.00 28.07      A    C  
ANISOU  904  C   ALA A 106     3870   3495   3298   -144    290    351  A    C  
ATOM    905  O   ALA A 106      16.183  -1.247  34.417  1.00 29.22      A    O  
ANISOU  905  O   ALA A 106     4156   3411   3532   -218    165    360  A    O  
ATOM    906  CB  ALA A 106      17.379  -1.708  37.852  1.00 28.17      A    C  
ANISOU  906  CB  ALA A 106     3840   3727   3136   -352    417    338  A    C  
ATOM    907  N   GLN A 107      17.667  -0.071  35.550  1.00 27.83      A    N  
ANISOU  907  N   GLN A 107     3750   3636   3188   -143    361    407  A    N  
ATOM    908  CA  GLN A 107      17.819   0.862  34.424  1.00 27.56      A    C  
ANISOU  908  CA  GLN A 107     3648   3504   3320   -189    448    266  A    C  
ATOM    909  C   GLN A 107      18.331   0.034  33.231  1.00 27.67      A    C  
ANISOU  909  C   GLN A 107     3693   3525   3293   -237    290    157  A    C  
ATOM    910  O   GLN A 107      18.101   0.357  32.073  1.00 28.11      A    O  
ANISOU  910  O   GLN A 107     3747   3547   3386   -348    313    339  A    O  
ATOM    911  CB  GLN A 107      18.814   1.966  34.750  1.00 26.53      A    C  
ANISOU  911  CB  GLN A 107     3473   3389   3219   -227    300    252  A    C  
ATOM    912  CG  GLN A 107      19.004   3.005  33.568  1.00 24.42      A    C  
ANISOU  912  CG  GLN A 107     3166   3491   2619    -13    414    295  A    C  
ATOM    913  CD  GLN A 107      19.703   4.248  34.086  1.00 26.79      A    C  
ANISOU  913  CD  GLN A 107     3403   3369   3406    -23    679    583  A    C  
ATOM    914  NE2 GLN A 107      20.964   4.469  33.673  1.00 26.18      A    N  
ANISOU  914  NE2 GLN A 107     2887   4058   2999     53   1047    416  A    N  
ATOM    915  OE1 GLN A 107      19.151   4.957  34.916  1.00 28.32      A    O  
ANISOU  915  OE1 GLN A 107     3763   3918   3078   -383    342    400  A    O  
ATOM    916  N   GLY A 108      19.034  -1.033  33.526  1.00 27.57      A    N  
ANISOU  916  N   GLY A 108     3625   3506   3342    -47    467     86  A    N  
ATOM    917  CA  GLY A 108      19.547  -1.931  32.460  1.00 28.06      A    C  
ANISOU  917  CA  GLY A 108     3529   3677   3453   -123    509     69  A    C  
ATOM    918  C   GLY A 108      18.404  -2.641  31.772  1.00 28.26      A    C  
ANISOU  918  C   GLY A 108     3614   3657   3467   -117    466    187  A    C  
ATOM    919  O   GLY A 108      18.507  -2.998  30.600  1.00 27.91      A    O  
ANISOU  919  O   GLY A 108     3520   3622   3460   -205    566    235  A    O  
ATOM    920  N   GLY A 109      17.298  -2.852  32.494  1.00 27.32      A    N  
ANISOU  920  N   GLY A 109     3364   3553   3462    119    424    429  A    N  
ATOM    921  CA  GLY A 109      16.090  -3.359  31.867  1.00 27.93      A    C  
ANISOU  921  CA  GLY A 109     3588   3627   3394   -107    311    399  A    C  
ATOM    922  C   GLY A 109      15.412  -2.350  30.920  1.00 28.02      A    C  
ANISOU  922  C   GLY A 109     3515   3792   3336    -82    334    353  A    C  
ATOM    923  O   GLY A 109      14.826  -2.770  29.907  1.00 29.43      A    O  
ANISOU  923  O   GLY A 109     3427   4203   3551   -148    300    441  A    O  
ATOM    924  N   VAL A 110      15.483  -1.044  31.219  1.00 27.16      A    N  
ANISOU  924  N   VAL A 110     3390   3766   3162    -44    588    477  A    N  
ATOM    925  CA  VAL A 110      14.997  -0.029  30.301  1.00 26.32      A    C  
ANISOU  925  CA  VAL A 110     3301   3625   3072     61    563    362  A    C  
ATOM    926  C   VAL A 110      15.886  -0.018  29.068  1.00 26.14      A    C  
ANISOU  926  C   VAL A 110     3354   3468   3108      5    496    241  A    C  
ATOM    927  O   VAL A 110      15.374   0.034  27.932  1.00 26.55      A    O  
ANISOU  927  O   VAL A 110     3290   3674   3123     19    390    225  A    O  
ATOM    928  CB  VAL A 110      14.972   1.380  30.937  1.00 26.90      A    C  
ANISOU  928  CB  VAL A 110     3347   3761   3111     -8    463    495  A    C  
ATOM    929  CG1 VAL A 110      14.626   2.481  29.877  1.00 25.56      A    C  
ANISOU  929  CG1 VAL A 110     3152   3760   2798   -207    452    662  A    C  
ATOM    930  CG2 VAL A 110      13.952   1.362  32.016  1.00 26.00      A    C  
ANISOU  930  CG2 VAL A 110     3178   3997   2702     95    854    556  A    C  
ATOM    931  N   VAL A 111      17.194  -0.101  29.264  1.00 25.37      A    N  
ANISOU  931  N   VAL A 111     3265   3366   3006   -291    711      7  A    N  
ATOM    932  CA  VAL A 111      18.100  -0.236  28.078  1.00 25.76      A    C  
ANISOU  932  CA  VAL A 111     3256   3435   3096   -189    661   -123  A    C  
ATOM    933  C   VAL A 111      17.702  -1.453  27.211  1.00 27.35      A    C  
ANISOU  933  C   VAL A 111     3326   3609   3455   -291    519    -47  A    C  
ATOM    934  O   VAL A 111      17.609  -1.355  25.962  1.00 27.35      A    O  
ANISOU  934  O   VAL A 111     3040   3751   3600   -370    732    -53  A    O  
ATOM    935  CB  VAL A 111      19.582  -0.200  28.484  1.00 25.57      A    C  
ANISOU  935  CB  VAL A 111     3416   3242   3055   -191    832   -113  A    C  
ATOM    936  CG1 VAL A 111      20.543  -0.479  27.222  1.00 24.82      A    C  
ANISOU  936  CG1 VAL A 111     3229   3243   2958    -90    553   -436  A    C  
ATOM    937  CG2 VAL A 111      19.911   1.178  29.134  1.00 23.66      A    C  
ANISOU  937  CG2 VAL A 111     3064   3396   2527   -435    551    -34  A    C  
ATOM    938  N   ALA A 112      17.516  -2.602  27.854  1.00 25.95      A    N  
ANISOU  938  N   ALA A 112     2983   3290   3585   -210    409    -44  A    N  
ATOM    939  CA  ALA A 112      17.216  -3.831  27.102  1.00 28.31      A    C  
ANISOU  939  CA  ALA A 112     3350   3564   3840   -169    329     68  A    C  
ATOM    940  C   ALA A 112      15.891  -3.710  26.343  1.00 27.26      A    C  
ANISOU  940  C   ALA A 112     3338   3370   3647   -149    398     66  A    C  
ATOM    941  O   ALA A 112      15.774  -4.112  25.218  1.00 26.94      A    O  
ANISOU  941  O   ALA A 112     3506   3264   3463   -189    442    166  A    O  
ATOM    942  CB  ALA A 112      17.173  -5.050  28.093  1.00 28.37      A    C  
ANISOU  942  CB  ALA A 112     3390   3429   3960   -362    413     78  A    C  
ATOM    943  N   SER A 113      14.865  -3.184  27.026  1.00 26.56      A    N  
ANISOU  943  N   SER A 113     3148   3211   3732    -46    534     53  A    N  
ATOM    944  CA  SER A 113      13.502  -3.153  26.456  1.00 26.45      A    C  
ANISOU  944  CA  SER A 113     3062   3382   3605    136    575    112  A    C  
ATOM    945  C   SER A 113      13.476  -2.215  25.233  1.00 26.66      A    C  
ANISOU  945  C   SER A 113     3163   3420   3544     26    547     29  A    C  
ATOM    946  O   SER A 113      12.913  -2.549  24.183  1.00 26.38      A    O  
ANISOU  946  O   SER A 113     2947   3534   3543     61    484    247  A    O  
ATOM    947  CB  SER A 113      12.461  -2.828  27.585  1.00 27.51      A    C  
ANISOU  947  CB  SER A 113     3288   3506   3657    149    580      3  A    C  
ATOM    948  OG  SER A 113      12.400  -1.459  27.867  1.00 29.87      A    O  
ANISOU  948  OG  SER A 113     3463   3996   3888    330    587   -306  A    O  
ATOM    949  N   MET A 114      14.115  -1.051  25.373  1.00 26.14      A    N  
ANISOU  949  N   MET A 114     3088   3329   3514   -203    596    201  A    N  
ATOM    950  CA  MET A 114      14.172  -0.111  24.247  1.00 26.81      A    C  
ANISOU  950  CA  MET A 114     3468   3140   3577   -156    280    187  A    C  
ATOM    951  C   MET A 114      15.045  -0.662  23.141  1.00 26.56      A    C  
ANISOU  951  C   MET A 114     3312   3171   3605   -207    278    275  A    C  
ATOM    952  O   MET A 114      14.696  -0.547  21.917  1.00 26.95      A    O  
ANISOU  952  O   MET A 114     3158   3626   3457    -79    291   -116  A    O  
ATOM    953  CB  MET A 114      14.679   1.271  24.719  1.00 26.90      A    C  
ANISOU  953  CB  MET A 114     3438   3077   3705    -58    166    -29  A    C  
ATOM    954  CG  MET A 114      13.697   1.851  25.801  1.00 27.09      A    C  
ANISOU  954  CG  MET A 114     3875   3157   3257   -282    307    325  A    C  
ATOM    955  SD  MET A 114      13.916   3.561  26.182  1.00 27.51      A    S  
ANISOU  955  SD  MET A 114     3151   3734   3569   -249    146    -70  A    S  
ATOM    956  CE  MET A 114      13.541   4.410  24.602  1.00 32.30      A    C  
ANISOU  956  CE  MET A 114     3984   4178   4110    127   -477   -245  A    C  
ATOM    957  N   LEU A 115      16.174  -1.285  23.493  1.00 27.24      A    N  
ANISOU  957  N   LEU A 115     3362   3443   3545   -113    179    301  A    N  
ATOM    958  CA  LEU A 115      16.999  -1.849  22.412  1.00 27.79      A    C  
ANISOU  958  CA  LEU A 115     3439   3566   3555   -139     86    -32  A    C  
ATOM    959  C   LEU A 115      16.233  -2.986  21.670  1.00 29.11      A    C  
ANISOU  959  C   LEU A 115     3514   3737   3808   -248     48    -16  A    C  
ATOM    960  O   LEU A 115      16.287  -3.069  20.451  1.00 28.74      A    O  
ANISOU  960  O   LEU A 115     3409   3691   3817    -91    167   -128  A    O  
ATOM    961  CB  LEU A 115      18.365  -2.382  22.859  1.00 27.01      A    C  
ANISOU  961  CB  LEU A 115     3280   3560   3420    -31    164    -62  A    C  
ATOM    962  CG  LEU A 115      19.333  -2.847  21.767  1.00 26.54      A    C  
ANISOU  962  CG  LEU A 115     3124   3480   3480    -22    -60   -154  A    C  
ATOM    963  CD1 LEU A 115      19.803  -1.644  20.964  1.00 28.27      A    C  
ANISOU  963  CD1 LEU A 115     3798   3223   3718     14    667   -557  A    C  
ATOM    964  CD2 LEU A 115      20.506  -3.582  22.476  1.00 28.00      A    C  
ANISOU  964  CD2 LEU A 115     3500   3765   3373    258   -205   -730  A    C  
ATOM    965  N   ALA A 116      15.511  -3.824  22.405  1.00 27.33      A    N  
ANISOU  965  N   ALA A 116     3229   3452   3702   -336     83    123  A    N  
ATOM    966  CA  ALA A 116      14.723  -4.868  21.745  1.00 28.38      A    C  
ANISOU  966  CA  ALA A 116     3651   3541   3589   -413    -77     25  A    C  
ATOM    967  C   ALA A 116      13.607  -4.296  20.860  1.00 27.76      A    C  
ANISOU  967  C   ALA A 116     3378   3562   3606   -455      6    -75  A    C  
ATOM    968  O   ALA A 116      13.326  -4.862  19.807  1.00 28.30      A    O  
ANISOU  968  O   ALA A 116     3734   3455   3562   -387   -231   -205  A    O  
ATOM    969  CB  ALA A 116      14.132  -5.841  22.761  1.00 27.52      A    C  
ANISOU  969  CB  ALA A 116     3245   3496   3715   -609    197     33  A    C  
ATOM    970  N   GLY A 117      13.045  -3.148  21.209  1.00 27.82      A    N  
ANISOU  970  N   GLY A 117     3469   3466   3632   -475     81    -16  A    N  
ATOM    971  CA  GLY A 117      12.018  -2.511  20.373  1.00 29.22      A    C  
ANISOU  971  CA  GLY A 117     3694   3660   3747   -458     61   -106  A    C  
ATOM    972  C   GLY A 117      12.592  -1.843  19.140  1.00 29.11      A    C  
ANISOU  972  C   GLY A 117     3730   3463   3866   -377     55   -169  A    C  
ATOM    973  O   GLY A 117      11.859  -1.568  18.178  1.00 30.71      A    O  
ANISOU  973  O   GLY A 117     3910   3788   3969   -379    197   -114  A    O  
ATOM    974  N   LEU A 118      13.898  -1.584  19.176  1.00 30.28      A    N  
ANISOU  974  N   LEU A 118     4018   3435   4052   -268    -17   -319  A    N  
ATOM    975  CA  LEU A 118      14.659  -1.062  18.011  1.00 30.50      A    C  
ANISOU  975  CA  LEU A 118     3820   3585   4182   -326     -7   -458  A    C  
ATOM    976  C   LEU A 118      15.175  -2.207  17.119  1.00 30.53      A    C  
ANISOU  976  C   LEU A 118     3851   3583   4166   -303    -52   -447  A    C  
ATOM    977  O   LEU A 118      15.408  -2.004  15.933  1.00 31.37      A    O  
ANISOU  977  O   LEU A 118     4057   3667   4195   -203   -194   -688  A    O  
ATOM    978  CB  LEU A 118      15.832  -0.203  18.473  1.00 30.72      A    C  
ANISOU  978  CB  LEU A 118     3831   3557   4282   -371   -150   -447  A    C  
ATOM    979  CG  LEU A 118      15.408   1.142  19.041  1.00 29.04      A    C  
ANISOU  979  CG  LEU A 118     3734   3651   3648   -287      7   -488  A    C  
ATOM    980  CD1 LEU A 118      16.534   1.850  19.910  1.00 25.16      A    C  
ANISOU  980  CD1 LEU A 118     3417   3343   2800   -846    407   -130  A    C  
ATOM    981  CD2 LEU A 118      14.817   2.123  17.942  1.00 29.58      A    C  
ANISOU  981  CD2 LEU A 118     4202   3743   3293   -336   -255   -279  A    C  
ATOM    982  N   TYR A 119      15.394  -3.379  17.708  1.00 29.74      A    N  
ANISOU  982  N   TYR A 119     3724   3377   4197   -341    -69   -405  A    N  
ATOM    983  CA  TYR A 119      15.827  -4.530  16.966  1.00 29.88      A    C  
ANISOU  983  CA  TYR A 119     3590   3431   4330   -230      0   -255  A    C  
ATOM    984  C   TYR A 119      14.845  -5.730  17.123  1.00 30.60      A    C  
ANISOU  984  C   TYR A 119     3519   3618   4489   -211    -48   -254  A    C  
ATOM    985  O   TYR A 119      15.248  -6.818  17.544  1.00 30.69      A    O  
ANISOU  985  O   TYR A 119     3086   3467   5105   -172    -75   -175  A    O  
ATOM    986  CB  TYR A 119      17.211  -4.914  17.445  1.00 28.66      A    C  
ANISOU  986  CB  TYR A 119     3653   3219   4018   -463   -126   -418  A    C  
ATOM    987  CG  TYR A 119      18.309  -4.053  16.886  1.00 28.32      A    C  
ANISOU  987  CG  TYR A 119     3766   3436   3557   -161     85   -140  A    C  
ATOM    988  CD1 TYR A 119      18.887  -4.329  15.635  1.00 27.03      A    C  
ANISOU  988  CD1 TYR A 119     3362   3726   3180    487     52    299  A    C  
ATOM    989  CD2 TYR A 119      18.744  -2.926  17.583  1.00 28.92      A    C  
ANISOU  989  CD2 TYR A 119     3818   3676   3493   -355    -62    -60  A    C  
ATOM    990  CE1 TYR A 119      19.929  -3.516  15.157  1.00 29.93      A    C  
ANISOU  990  CE1 TYR A 119     4528   3649   3193   -167   -195    244  A    C  
ATOM    991  CE2 TYR A 119      19.778  -2.111  17.098  1.00 26.96      A    C  
ANISOU  991  CE2 TYR A 119     3837   3379   3024   -351   -308   -223  A    C  
ATOM    992  CZ  TYR A 119      20.352  -2.391  15.904  1.00 27.86      A    C  
ANISOU  992  CZ  TYR A 119     3993   3343   3248   -294     42    363  A    C  
ATOM    993  OH  TYR A 119      21.394  -1.591  15.473  1.00 28.92      A    O  
ANISOU  993  OH  TYR A 119     4236   3744   3007   -395    776    447  A    O  
ATOM    994  N   PRO A 120      13.538  -5.514  16.831  1.00 31.33      A    N  
ANISOU  994  N   PRO A 120     3710   3793   4399   -138     -7   -299  A    N  
ATOM    995  CA  PRO A 120      12.548  -6.572  17.089  1.00 32.27      A    C  
ANISOU  995  CA  PRO A 120     3834   3899   4525   -140     81   -256  A    C  
ATOM    996  C   PRO A 120      12.693  -7.804  16.169  1.00 34.54      A    C  
ANISOU  996  C   PRO A 120     4283   4171   4669   -170    105   -239  A    C  
ATOM    997  O   PRO A 120      12.235  -8.922  16.541  1.00 35.83      A    O  
ANISOU  997  O   PRO A 120     4459   4257   4896   -127    102   -122  A    O  
ATOM    998  CB  PRO A 120      11.216  -5.841  16.882  1.00 32.70      A    C  
ANISOU  998  CB  PRO A 120     4035   3808   4581   -113     92   -367  A    C  
ATOM    999  CG  PRO A 120      11.516  -4.835  15.740  1.00 31.70      A    C  
ANISOU  999  CG  PRO A 120     3686   3595   4762   -338     67   -271  A    C  
ATOM   1000  CD  PRO A 120      12.949  -4.348  16.123  1.00 29.69      A    C  
ANISOU 1000  CD  PRO A 120     3314   3753   4211    -84    -47   -231  A    C  
ATOM   1001  N   ASP A 121      13.358  -7.593  14.999  1.00 36.24      A    N  
ANISOU 1001  N   ASP A 121     4586   4390   4791    -45    211   -369  A    N  
ATOM   1002  CA  ASP A 121      13.723  -8.646  14.025  1.00 37.37      A    C  
ANISOU 1002  CA  ASP A 121     4883   4441   4875   -146    143   -481  A    C  
ATOM   1003  C   ASP A 121      14.950  -9.459  14.436  1.00 38.20      A    C  
ANISOU 1003  C   ASP A 121     4862   4412   5237   -112     77   -648  A    C  
ATOM   1004  O   ASP A 121      15.145 -10.614  13.959  1.00 39.47      A    O  
ANISOU 1004  O   ASP A 121     5145   4361   5489   -208    -97   -929  A    O  
ATOM   1005  CB  ASP A 121      14.046  -8.022  12.644  1.00 36.44      A    C  
ANISOU 1005  CB  ASP A 121     4890   4266   4688   -283    300   -506  A    C  
ATOM   1006  CG  ASP A 121      14.969  -6.796  12.730  1.00 36.04      A    C  
ANISOU 1006  CG  ASP A 121     4845   4481   4367   -467    576   -459  A    C  
ATOM   1007  OD1 ASP A 121      15.612  -6.477  11.724  1.00 37.04      A    O  
ANISOU 1007  OD1 ASP A 121     4878   4419   4774   -957    464   -263  A    O  
ATOM   1008  OD2 ASP A 121      15.071  -6.117  13.762  1.00 36.42      A    O1-
ANISOU 1008  OD2 ASP A 121     5499   4027   4311  -1336   1082   -350  A    O1-
ATOM   1009  N   LEU A 122      15.783  -8.892  15.311  1.00 36.67      A    N  
ANISOU 1009  N   LEU A 122     4568   4160   5203   -134     15   -682  A    N  
ATOM   1010  CA  LEU A 122      17.079  -9.519  15.596  1.00 37.26      A    C  
ANISOU 1010  CA  LEU A 122     4601   4338   5215   -218     37   -489  A    C  
ATOM   1011  C   LEU A 122      17.092 -10.214  16.973  1.00 36.94      A    C  
ANISOU 1011  C   LEU A 122     4534   4315   5185   -131     59   -374  A    C  
ATOM   1012  O   LEU A 122      17.555 -11.347  17.098  1.00 39.08      A    O  
ANISOU 1012  O   LEU A 122     5082   4372   5394    -70    124   -187  A    O  
ATOM   1013  CB  LEU A 122      18.277  -8.537  15.348  1.00 36.22      A    C  
ANISOU 1013  CB  LEU A 122     4162   4356   5242   -226    172   -617  A    C  
ATOM   1014  CG  LEU A 122      19.670  -9.139  15.631  1.00 37.94      A    C  
ANISOU 1014  CG  LEU A 122     4430   4643   5340   -310    123   -638  A    C  
ATOM   1015  CD1 LEU A 122      20.111 -10.259  14.642  1.00 41.17      A    C  
ANISOU 1015  CD1 LEU A 122     4357   5336   5948     22    487   -498  A    C  
ATOM   1016  CD2 LEU A 122      20.652  -8.025  15.634  1.00 38.28      A    C  
ANISOU 1016  CD2 LEU A 122     3664   4899   5980   -237    666   -795  A    C  
ATOM   1017  N   ILE A 123      16.523  -9.573  17.971  1.00 35.44      A    N  
ANISOU 1017  N   ILE A 123     4341   4170   4951   -201     20   -368  A    N  
ATOM   1018  CA  ILE A 123      16.434 -10.163  19.310  1.00 34.98      A    C  
ANISOU 1018  CA  ILE A 123     4185   4130   4973   -199     49   -225  A    C  
ATOM   1019  C   ILE A 123      15.366 -11.236  19.347  1.00 35.39      A    C  
ANISOU 1019  C   ILE A 123     4230   4144   5072   -242     48   -142  A    C  
ATOM   1020  O   ILE A 123      14.259 -11.063  18.836  1.00 35.27      A    O  
ANISOU 1020  O   ILE A 123     4152   4329   4918   -379    193    -86  A    O  
ATOM   1021  CB  ILE A 123      16.193  -9.070  20.427  1.00 34.59      A    C  
ANISOU 1021  CB  ILE A 123     4246   4153   4743   -303    -35   -168  A    C  
ATOM   1022  CG1 ILE A 123      17.235  -7.935  20.246  1.00 34.13      A    C  
ANISOU 1022  CG1 ILE A 123     4247   4039   4680   -289     24     93  A    C  
ATOM   1023  CG2 ILE A 123      16.160  -9.710  21.884  1.00 33.36      A    C  
ANISOU 1023  CG2 ILE A 123     3917   4267   4491   -202    175   -289  A    C  
ATOM   1024  CD1 ILE A 123      18.733  -8.446  20.199  1.00 28.07      A    C  
ANISOU 1024  CD1 ILE A 123     3604   3281   3778   -458      0    451  A    C  
ATOM   1025  N   LYS A 124      15.735 -12.357  19.944  1.00 37.25      A    N  
ANISOU 1025  N   LYS A 124     4342   4211   5600   -173     -8   -222  A    N  
ATOM   1026  CA  LYS A 124      14.870 -13.544  20.029  1.00 37.40      A    C  
ANISOU 1026  CA  LYS A 124     4272   4071   5865   -119    -59   -257  A    C  
ATOM   1027  C   LYS A 124      14.004 -13.621  21.353  1.00 36.52      A    C  
ANISOU 1027  C   LYS A 124     4176   3937   5762     69    -85   -363  A    C  
ATOM   1028  O   LYS A 124      12.844 -14.007  21.293  1.00 35.05      A    O  
ANISOU 1028  O   LYS A 124     3619   3827   5868     93    -69   -470  A    O  
ATOM   1029  CB  LYS A 124      15.751 -14.787  19.828  1.00 38.45      A    C  
ANISOU 1029  CB  LYS A 124     4460   3978   6169   -183   -119   -490  A    C  
ATOM   1030  CG  LYS A 124      14.983 -16.114  19.848  1.00 43.75      A    C  
ANISOU 1030  CG  LYS A 124     5178   4822   6620   -278   -410   -520  A    C  
ATOM   1031  CD  LYS A 124      14.411 -16.449  18.460  1.00 44.88      A    C  
ANISOU 1031  CD  LYS A 124     5630   5067   6354   -138   -344  -1212  A    C  
ATOM   1032  CE  LYS A 124      14.000 -17.917  18.406  1.00 48.19      A    C  
ANISOU 1032  CE  LYS A 124     6386   5156   6767   -370   -757  -1156  A    C  
ATOM   1033  NZ  LYS A 124      13.452 -18.238  17.074  1.00 48.88      A    N1+
ANISOU 1033  NZ  LYS A 124     6880   5216   6476   -182   -544  -1597  A    N1+
ATOM   1034  N   LYS A 125      14.580 -13.286  22.515  1.00 35.11      A    N  
ANISOU 1034  N   LYS A 125     4111   3789   5438    111   -101   -258  A    N  
ATOM   1035  CA  LYS A 125      13.881 -13.252  23.821  1.00 35.15      A    C  
ANISOU 1035  CA  LYS A 125     4241   3787   5324     25    -97   -191  A    C  
ATOM   1036  C   LYS A 125      14.521 -12.150  24.684  1.00 33.70      A    C  
ANISOU 1036  C   LYS A 125     4019   3674   5111     52    -35   -174  A    C  
ATOM   1037  O   LYS A 125      15.694 -11.831  24.484  1.00 31.79      A    O  
ANISOU 1037  O   LYS A 125     3541   3640   4896    183    180   -274  A    O  
ATOM   1038  CB  LYS A 125      14.025 -14.586  24.630  1.00 35.10      A    C  
ANISOU 1038  CB  LYS A 125     4404   3634   5298    -42    -63   -142  A    C  
ATOM   1039  CG  LYS A 125      13.397 -15.832  23.997  1.00 36.61      A    C  
ANISOU 1039  CG  LYS A 125     4430   3746   5732   -503   -291    105  A    C  
ATOM   1040  CD  LYS A 125      13.759 -17.054  24.758  1.00 39.07      A    C  
ANISOU 1040  CD  LYS A 125     5118   3589   6135   -618   -111    303  A    C  
ATOM   1041  CE  LYS A 125      13.036 -18.214  24.115  1.00 43.35      A    C  
ANISOU 1041  CE  LYS A 125     5815   4232   6424   -569   -497    207  A    C  
ATOM   1042  NZ  LYS A 125      13.523 -19.438  24.729  1.00 48.90      A    N1+
ANISOU 1042  NZ  LYS A 125     6913   4583   7083   -459   -491    396  A    N1+
ATOM   1043  N   VAL A 126      13.757 -11.626  25.655  1.00 33.15      A    N  
ANISOU 1043  N   VAL A 126     3975   3829   4790    -17    -16   -131  A    N  
ATOM   1044  CA  VAL A 126      14.224 -10.585  26.553  1.00 33.08      A    C  
ANISOU 1044  CA  VAL A 126     4023   3783   4762    -19    121    -58  A    C  
ATOM   1045  C   VAL A 126      13.807 -10.956  27.964  1.00 33.84      A    C  
ANISOU 1045  C   VAL A 126     4022   3945   4889     40     91     17  A    C  
ATOM   1046  O   VAL A 126      12.640 -11.346  28.202  1.00 35.76      A    O  
ANISOU 1046  O   VAL A 126     4154   3974   5456     66    181      4  A    O  
ATOM   1047  CB  VAL A 126      13.540  -9.240  26.270  1.00 32.36      A    C  
ANISOU 1047  CB  VAL A 126     3967   3733   4593     17     45    -21  A    C  
ATOM   1048  CG1 VAL A 126      13.772  -8.245  27.441  1.00 28.99      A    C  
ANISOU 1048  CG1 VAL A 126     3861   2640   4514   -380    277    -36  A    C  
ATOM   1049  CG2 VAL A 126      13.911  -8.674  24.902  1.00 33.15      A    C  
ANISOU 1049  CG2 VAL A 126     3925   3669   4999   -280    277    -28  A    C  
ATOM   1050  N   VAL A 127      14.733 -10.807  28.913  1.00 32.39      A    N  
ANISOU 1050  N   VAL A 127     3996   3857   4453     42     81    -77  A    N  
ATOM   1051  CA  VAL A 127      14.377 -10.909  30.330  1.00 31.35      A    C  
ANISOU 1051  CA  VAL A 127     3716   3769   4424     44    392    122  A    C  
ATOM   1052  C   VAL A 127      14.590  -9.558  30.996  1.00 30.40      A    C  
ANISOU 1052  C   VAL A 127     3643   3806   4102   -137    418    184  A    C  
ATOM   1053  O   VAL A 127      15.698  -8.986  30.979  1.00 28.94      A    O  
ANISOU 1053  O   VAL A 127     3579   3807   3607   -293    666    355  A    O  
ATOM   1054  CB  VAL A 127      15.235 -11.928  31.070  1.00 30.77      A    C  
ANISOU 1054  CB  VAL A 127     3523   3912   4254    -76    269     85  A    C  
ATOM   1055  CG1 VAL A 127      14.796 -12.012  32.558  1.00 32.94      A    C  
ANISOU 1055  CG1 VAL A 127     3860   4182   4474    444    132     22  A    C  
ATOM   1056  CG2 VAL A 127      15.200 -13.274  30.307  1.00 33.60      A    C  
ANISOU 1056  CG2 VAL A 127     3750   3911   5104     49    458    -69  A    C  
ATOM   1057  N   LEU A 128      13.531  -9.046  31.611  1.00 29.05      A    N  
ANISOU 1057  N   LEU A 128     3429   3531   4076   -107    591    423  A    N  
ATOM   1058  CA  LEU A 128      13.658  -7.789  32.370  1.00 29.47      A    C  
ANISOU 1058  CA  LEU A 128     3456   3744   3997   -249    373    379  A    C  
ATOM   1059  C   LEU A 128      13.536  -8.074  33.852  1.00 30.97      A    C  
ANISOU 1059  C   LEU A 128     3719   3827   4220   -158    313    463  A    C  
ATOM   1060  O   LEU A 128      12.561  -8.635  34.297  1.00 31.84      A    O  
ANISOU 1060  O   LEU A 128     3932   3795   4371   -434    390    597  A    O  
ATOM   1061  CB  LEU A 128      12.579  -6.784  31.951  1.00 28.71      A    C  
ANISOU 1061  CB  LEU A 128     3468   3548   3892   -168    278    572  A    C  
ATOM   1062  CG  LEU A 128      12.515  -6.479  30.444  1.00 27.87      A    C  
ANISOU 1062  CG  LEU A 128     2672   3841   4075   -242    186    412  A    C  
ATOM   1063  CD1 LEU A 128      11.393  -5.395  30.282  1.00 30.56      A    C  
ANISOU 1063  CD1 LEU A 128     3326   3779   4505     21    682   -237  A    C  
ATOM   1064  CD2 LEU A 128      13.803  -5.923  29.925  1.00 27.75      A    C  
ANISOU 1064  CD2 LEU A 128     2716   3550   4277   -136    740   -101  A    C  
ATOM   1065  N   LEU A 129      14.557  -7.686  34.589  1.00 31.57      A    N  
ANISOU 1065  N   LEU A 129     3967   3833   4192   -129    213    343  A    N  
ATOM   1066  CA  LEU A 129      14.531  -7.806  36.071  1.00 31.32      A    C  
ANISOU 1066  CA  LEU A 129     3781   3927   4193    -26    656    409  A    C  
ATOM   1067  C   LEU A 129      14.336  -6.436  36.766  1.00 31.64      A    C  
ANISOU 1067  C   LEU A 129     3667   3975   4377    -13    594    335  A    C  
ATOM   1068  O   LEU A 129      15.231  -5.559  36.718  1.00 31.56      A    O  
ANISOU 1068  O   LEU A 129     3296   4053   4640    175    788    197  A    O  
ATOM   1069  CB  LEU A 129      15.779  -8.526  36.606  1.00 30.18      A    C  
ANISOU 1069  CB  LEU A 129     3716   3796   3955    -92    775    502  A    C  
ATOM   1070  CG  LEU A 129      15.903  -9.975  36.122  1.00 29.40      A    C  
ANISOU 1070  CG  LEU A 129     3649   3784   3737    -89    685    587  A    C  
ATOM   1071  CD1 LEU A 129      17.063  -9.953  35.157  1.00 29.77      A    C  
ANISOU 1071  CD1 LEU A 129     4350   3600   3361    273   1203    344  A    C  
ATOM   1072  CD2 LEU A 129      16.179 -10.935  37.244  1.00 33.66      A    C  
ANISOU 1072  CD2 LEU A 129     4320   3690   4778    -64    466    810  A    C  
ATOM   1073  N   ALA A 130      13.159  -6.231  37.390  1.00 30.51      A    N  
ANISOU 1073  N   ALA A 130     3269   3938   4383     26    675    402  A    N  
ATOM   1074  CA  ALA A 130      12.838  -4.936  38.001  1.00 31.77      A    C  
ANISOU 1074  CA  ALA A 130     3628   3973   4469    -99    528    387  A    C  
ATOM   1075  C   ALA A 130      13.100  -3.703  37.076  1.00 31.05      A    C  
ANISOU 1075  C   ALA A 130     3553   3951   4293    -81    538    392  A    C  
ATOM   1076  O   ALA A 130      13.732  -2.716  37.545  1.00 31.56      A    O  
ANISOU 1076  O   ALA A 130     3685   3741   4563   -187    821    641  A    O  
ATOM   1077  CB  ALA A 130      13.595  -4.760  39.331  1.00 31.38      A    C  
ANISOU 1077  CB  ALA A 130     3354   4193   4376    -81    461    595  A    C  
ATOM   1078  N   PRO A 131      12.614  -3.741  35.804  1.00 31.64      A    N  
ANISOU 1078  N   PRO A 131     3635   3899   4488    -84    435    334  A    N  
ATOM   1079  CA  PRO A 131      13.049  -2.726  34.802  1.00 30.95      A    C  
ANISOU 1079  CA  PRO A 131     3627   3904   4228    -68    328    393  A    C  
ATOM   1080  C   PRO A 131      12.575  -1.333  35.286  1.00 31.56      A    C  
ANISOU 1080  C   PRO A 131     3871   3937   4183   -169    261    326  A    C  
ATOM   1081  O   PRO A 131      11.379  -1.163  35.669  1.00 32.62      A    O  
ANISOU 1081  O   PRO A 131     3754   4270   4371    -88    316    265  A    O  
ATOM   1082  CB  PRO A 131      12.330  -3.152  33.494  1.00 30.13      A    C  
ANISOU 1082  CB  PRO A 131     3577   3577   4291   -143    524    298  A    C  
ATOM   1083  CG  PRO A 131      11.114  -4.027  34.012  1.00 29.32      A    C  
ANISOU 1083  CG  PRO A 131     2961   3743   4436     65    384    421  A    C  
ATOM   1084  CD  PRO A 131      11.666  -4.731  35.231  1.00 31.02      A    C  
ANISOU 1084  CD  PRO A 131     3555   3898   4331   -156    288    345  A    C  
ATOM   1085  N   ALA A 132      13.494  -0.365  35.316  1.00 29.79      A    N  
ANISOU 1085  N   ALA A 132     3802   3784   3732   -239    308    505  A    N  
ATOM   1086  CA  ALA A 132      13.215   0.893  36.049  1.00 28.59      A    C  
ANISOU 1086  CA  ALA A 132     3706   3672   3481   -137    492    427  A    C  
ATOM   1087  C   ALA A 132      12.495   1.907  35.152  1.00 28.83      A    C  
ANISOU 1087  C   ALA A 132     3685   3783   3486    -19    508    254  A    C  
ATOM   1088  O   ALA A 132      12.996   3.050  34.975  1.00 27.76      A    O  
ANISOU 1088  O   ALA A 132     3703   3618   3224   -139    589    494  A    O  
ATOM   1089  CB  ALA A 132      14.528   1.494  36.555  1.00 28.57      A    C  
ANISOU 1089  CB  ALA A 132     3768   3699   3387    -77    393    419  A    C  
ATOM   1090  N   ALA A 133      11.398   1.494  34.506  1.00 28.52      A    N  
ANISOU 1090  N   ALA A 133     3466   3845   3524     30    623    284  A    N  
ATOM   1091  CA  ALA A 133      10.670   2.404  33.595  1.00 29.78      A    C  
ANISOU 1091  CA  ALA A 133     3519   4114   3681    117    451    144  A    C  
ATOM   1092  C   ALA A 133      10.122   3.617  34.396  1.00 30.81      A    C  
ANISOU 1092  C   ALA A 133     3652   4053   3998    127    388    243  A    C  
ATOM   1093  O   ALA A 133       9.749   4.633  33.810  1.00 31.09      A    O  
ANISOU 1093  O   ALA A 133     3643   4071   4097    215    491    293  A    O  
ATOM   1094  CB  ALA A 133       9.563   1.648  32.877  1.00 30.18      A    C  
ANISOU 1094  CB  ALA A 133     3628   4221   3619     45    366    222  A    C  
ATOM   1095  N   THR A 134      10.068   3.481  35.729  1.00 30.48      A    N  
ANISOU 1095  N   THR A 134     3675   4111   3795     73    397    188  A    N  
ATOM   1096  CA  THR A 134       9.587   4.550  36.605  1.00 30.69      A    C  
ANISOU 1096  CA  THR A 134     3689   4095   3873    194    412    253  A    C  
ATOM   1097  C   THR A 134      10.570   5.715  36.639  1.00 29.85      A    C  
ANISOU 1097  C   THR A 134     3574   3969   3796    199    343    189  A    C  
ATOM   1098  O   THR A 134      10.293   6.792  37.170  1.00 30.56      A    O  
ANISOU 1098  O   THR A 134     3801   3977   3832     15    434     44  A    O  
ATOM   1099  CB  THR A 134       9.369   4.031  38.021  1.00 32.10      A    C  
ANISOU 1099  CB  THR A 134     3786   4436   3974    308    340    312  A    C  
ATOM   1100  CG2 THR A 134       8.151   3.168  38.066  1.00 30.06      A    C  
ANISOU 1100  CG2 THR A 134     3336   3994   4088    404    864   -115  A    C  
ATOM   1101  OG1 THR A 134      10.506   3.224  38.364  1.00 35.15      A    O  
ANISOU 1101  OG1 THR A 134     4469   4637   4246    432    423    300  A    O  
ATOM   1102  N   LEU A 135      11.741   5.528  36.054  1.00 29.38      A    N  
ANISOU 1102  N   LEU A 135     3690   3776   3696    143    348    263  A    N  
ATOM   1103  CA  LEU A 135      12.679   6.639  36.053  1.00 28.90      A    C  
ANISOU 1103  CA  LEU A 135     3411   3852   3717    167    449     98  A    C  
ATOM   1104  C   LEU A 135      12.095   7.857  35.308  1.00 27.44      A    C  
ANISOU 1104  C   LEU A 135     3144   3703   3579    194    534     28  A    C  
ATOM   1105  O   LEU A 135      12.435   9.004  35.619  1.00 28.68      A    O  
ANISOU 1105  O   LEU A 135     3320   3979   3597    395    627   -116  A    O  
ATOM   1106  CB  LEU A 135      14.089   6.225  35.522  1.00 28.39      A    C  
ANISOU 1106  CB  LEU A 135     3340   3676   3768    341    449     37  A    C  
ATOM   1107  CG  LEU A 135      14.290   5.764  34.066  1.00 26.78      A    C  
ANISOU 1107  CG  LEU A 135     3471   3297   3407    284    483    573  A    C  
ATOM   1108  CD1 LEU A 135      14.426   6.991  33.123  1.00 25.46      A    C  
ANISOU 1108  CD1 LEU A 135     3296   3337   3038     42    641    623  A    C  
ATOM   1109  CD2 LEU A 135      15.535   4.949  34.006  1.00 26.25      A    C  
ANISOU 1109  CD2 LEU A 135     3025   3419   3529    199    839    765  A    C  
ATOM   1110  N   LYS A 136      11.239   7.613  34.328  1.00 27.17      A    N  
ANISOU 1110  N   LYS A 136     3019   4037   3265    358    671    122  A    N  
ATOM   1111  CA  LYS A 136      10.627   8.691  33.551  1.00 28.52      A    C  
ANISOU 1111  CA  LYS A 136     3346   3968   3522    123    555    117  A    C  
ATOM   1112  C   LYS A 136       9.671   9.477  34.421  1.00 29.94      A    C  
ANISOU 1112  C   LYS A 136     3464   4262   3648     30    598    193  A    C  
ATOM   1113  O   LYS A 136       9.789  10.711  34.543  1.00 29.51      A    O  
ANISOU 1113  O   LYS A 136     3484   4145   3582    107    739    368  A    O  
ATOM   1114  CB  LYS A 136       9.869   8.129  32.339  1.00 28.03      A    C  
ANISOU 1114  CB  LYS A 136     3224   4219   3208    326    541    183  A    C  
ATOM   1115  CG  LYS A 136       9.130   9.175  31.494  1.00 27.99      A    C  
ANISOU 1115  CG  LYS A 136     3478   3820   3336     80    315    226  A    C  
ATOM   1116  CD  LYS A 136       8.578   8.475  30.245  1.00 28.21      A    C  
ANISOU 1116  CD  LYS A 136     3782   4063   2872    163    373    154  A    C  
ATOM   1117  CE  LYS A 136       7.762   9.414  29.453  1.00 29.17      A    C  
ANISOU 1117  CE  LYS A 136     3584   4428   3072    184   -149   -313  A    C  
ATOM   1118  NZ  LYS A 136       7.239   8.685  28.318  1.00 32.00      A    N1+
ANISOU 1118  NZ  LYS A 136     4443   4889   2826   -162   -297   -122  A    N1+
ATOM   1119  N   GLY A 137       8.699   8.766  35.013  1.00 30.28      A    N  
ANISOU 1119  N   GLY A 137     3557   4300   3647   -191    540    423  A    N  
ATOM   1120  CA  GLY A 137       7.757   9.431  35.932  1.00 31.14      A    C  
ANISOU 1120  CA  GLY A 137     3791   4282   3755    -78    416     55  A    C  
ATOM   1121  C   GLY A 137       8.446  10.150  37.096  1.00 31.76      A    C  
ANISOU 1121  C   GLY A 137     3837   4365   3864   -108    417    118  A    C  
ATOM   1122  O   GLY A 137       7.983  11.242  37.564  1.00 29.81      A    O  
ANISOU 1122  O   GLY A 137     3466   4135   3725    -70    734    232  A    O  
ATOM   1123  N   ASP A 138       9.514   9.528  37.608  1.00 30.96      A    N  
ANISOU 1123  N   ASP A 138     3795   4230   3736   -118    335    119  A    N  
ATOM   1124  CA  ASP A 138      10.252  10.137  38.754  1.00 31.11      A    C  
ANISOU 1124  CA  ASP A 138     3888   4269   3662    -88    397     -5  A    C  
ATOM   1125  C   ASP A 138      10.838  11.495  38.319  1.00 31.03      A    C  
ANISOU 1125  C   ASP A 138     3939   4166   3682    -25    482     36  A    C  
ATOM   1126  O   ASP A 138      10.788  12.478  39.061  1.00 30.15      A    O  
ANISOU 1126  O   ASP A 138     3883   3921   3648   -129    563    -28  A    O  
ATOM   1127  CB  ASP A 138      11.430   9.270  39.179  1.00 30.02      A    C  
ANISOU 1127  CB  ASP A 138     3987   4115   3304    -51    462     86  A    C  
ATOM   1128  CG  ASP A 138      11.021   8.035  39.908  1.00 31.82      A    C  
ANISOU 1128  CG  ASP A 138     3923   4250   3916    -76    658    -76  A    C  
ATOM   1129  OD1 ASP A 138       9.841   7.877  40.287  1.00 31.17      A    O  
ANISOU 1129  OD1 ASP A 138     3849   4467   3525    -50   1300   -221  A    O  
ATOM   1130  OD2 ASP A 138      11.930   7.245  40.150  1.00 33.00      A    O1-
ANISOU 1130  OD2 ASP A 138     4335   4176   4028    117    798    478  A    O1-
ATOM   1131  N   ALA A 139      11.424  11.519  37.104  1.00 31.43      A    N  
ANISOU 1131  N   ALA A 139     4011   4262   3668     47    470    -22  A    N  
ATOM   1132  CA  ALA A 139      12.018  12.747  36.558  1.00 30.09      A    C  
ANISOU 1132  CA  ALA A 139     3655   4067   3709    -63    528    -64  A    C  
ATOM   1133  C   ALA A 139      10.974  13.819  36.256  1.00 30.84      A    C  
ANISOU 1133  C   ALA A 139     3717   4162   3838    -58    450   -111  A    C  
ATOM   1134  O   ALA A 139      11.249  15.024  36.411  1.00 30.58      A    O  
ANISOU 1134  O   ALA A 139     3528   4114   3974     42    452   -307  A    O  
ATOM   1135  CB  ALA A 139      12.915  12.459  35.266  1.00 29.41      A    C  
ANISOU 1135  CB  ALA A 139     3671   4059   3443   -175    700    -48  A    C  
ATOM   1136  N   LEU A 140       9.781  13.386  35.836  1.00 30.69      A    N  
ANISOU 1136  N   LEU A 140     3638   4150   3872     32    248    -40  A    N  
ATOM   1137  CA  LEU A 140       8.658  14.304  35.575  1.00 31.57      A    C  
ANISOU 1137  CA  LEU A 140     3757   4274   3962     79    318    -95  A    C  
ATOM   1138  C   LEU A 140       8.148  14.864  36.906  1.00 31.73      A    C  
ANISOU 1138  C   LEU A 140     3592   4424   4038    147    538   -188  A    C  
ATOM   1139  O   LEU A 140       7.723  16.025  36.975  1.00 31.37      A    O  
ANISOU 1139  O   LEU A 140     3479   4417   4023     68    590   -357  A    O  
ATOM   1140  CB  LEU A 140       7.533  13.625  34.763  1.00 30.73      A    C  
ANISOU 1140  CB  LEU A 140     3688   4243   3745    -33    177     55  A    C  
ATOM   1141  CG  LEU A 140       7.854  13.339  33.273  1.00 29.67      A    C  
ANISOU 1141  CG  LEU A 140     3754   4054   3465     11    209    400  A    C  
ATOM   1142  CD1 LEU A 140       6.762  12.434  32.732  1.00 32.05      A    C  
ANISOU 1142  CD1 LEU A 140     3821   4040   4313    -44    507     74  A    C  
ATOM   1143  CD2 LEU A 140       7.899  14.662  32.440  1.00 30.27      A    C  
ANISOU 1143  CD2 LEU A 140     4061   3719   3720    379    480    674  A    C  
ATOM   1144  N   GLU A 141       8.303  14.089  37.965  1.00 33.29      A    N  
ANISOU 1144  N   GLU A 141     3855   4621   4170    173    781   -185  A    N  
ATOM   1145  CA  GLU A 141       7.816  14.559  39.265  1.00 35.69      A    C  
ANISOU 1145  CA  GLU A 141     4335   4725   4499     65    610   -448  A    C  
ATOM   1146  C   GLU A 141       8.836  15.387  40.073  1.00 35.54      A    C  
ANISOU 1146  C   GLU A 141     4198   4720   4583     91    616   -466  A    C  
ATOM   1147  O   GLU A 141       8.446  16.064  41.039  1.00 36.29      A    O  
ANISOU 1147  O   GLU A 141     4267   4889   4629     35    568   -861  A    O  
ATOM   1148  CB  GLU A 141       7.290  13.379  40.067  1.00 37.74      A    C  
ANISOU 1148  CB  GLU A 141     4535   5000   4804     83    790   -395  A    C  
ATOM   1149  CG  GLU A 141       7.540  13.440  41.545  1.00 43.32      A    C  
ANISOU 1149  CG  GLU A 141     5712   5704   5044    -24    987   -495  A    C  
ATOM   1150  CD  GLU A 141       6.917  12.271  42.260  1.00 53.70      A    C  
ANISOU 1150  CD  GLU A 141     7192   6712   6499   -329   1489   -487  A    C  
ATOM   1151  OE1 GLU A 141       7.009  11.117  41.767  1.00 56.74      A    O  
ANISOU 1151  OE1 GLU A 141     7843   6777   6936   -247   1576   -737  A    O  
ATOM   1152  OE2 GLU A 141       6.306  12.518  43.331  1.00 60.21      A    O1-
ANISOU 1152  OE2 GLU A 141     8304   7870   6703   -238   1584   -475  A    O1-
ATOM   1153  N   GLY A 142      10.121  15.349  39.679  1.00 34.91      A    N  
ANISOU 1153  N   GLY A 142     4126   4569   4567     51    580   -393  A    N  
ATOM   1154  CA  GLY A 142      11.149  16.113  40.363  1.00 32.71      A    C  
ANISOU 1154  CA  GLY A 142     3748   4362   4315      6    533   -230  A    C  
ATOM   1155  C   GLY A 142      11.660  15.375  41.584  1.00 33.89      A    C  
ANISOU 1155  C   GLY A 142     4115   4348   4411    -11    402   -188  A    C  
ATOM   1156  O   GLY A 142      12.020  16.014  42.594  1.00 33.51      A    O  
ANISOU 1156  O   GLY A 142     4156   4212   4363   -256    198   -165  A    O  
ATOM   1157  N   ASN A 143      11.738  14.037  41.501  1.00 32.86      A    N  
ANISOU 1157  N   ASN A 143     4245   4100   4140    -76    328     57  A    N  
ATOM   1158  CA  ASN A 143      12.153  13.271  42.673  1.00 33.40      A    C  
ANISOU 1158  CA  ASN A 143     4254   4262   4174    100    612    100  A    C  
ATOM   1159  C   ASN A 143      12.749  11.967  42.184  1.00 32.62      A    C  
ANISOU 1159  C   ASN A 143     4285   4162   3947      5    526    172  A    C  
ATOM   1160  O   ASN A 143      12.036  11.053  41.830  1.00 32.18      A    O  
ANISOU 1160  O   ASN A 143     4166   4017   4043    -55    661    213  A    O  
ATOM   1161  CB  ASN A 143      10.984  13.057  43.668  1.00 33.61      A    C  
ANISOU 1161  CB  ASN A 143     4369   4281   4119    -41    753    124  A    C  
ATOM   1162  CG  ASN A 143      11.430  12.400  44.981  1.00 34.75      A    C  
ANISOU 1162  CG  ASN A 143     4359   4904   3939    427   1068      3  A    C  
ATOM   1163  ND2 ASN A 143      10.727  12.721  46.098  1.00 37.45      A    N  
ANISOU 1163  ND2 ASN A 143     5254   5402   3572    513   1670    234  A    N  
ATOM   1164  OD1 ASN A 143      12.351  11.589  44.999  1.00 36.75      A    O  
ANISOU 1164  OD1 ASN A 143     4220   5536   4207    432    841    411  A    O  
ATOM   1165  N   THR A 144      14.071  11.919  42.146  1.00 31.76      A    N  
ANISOU 1165  N   THR A 144     4188   4199   3679     91    680    312  A    N  
ATOM   1166  CA  THR A 144      14.806  10.731  41.735  1.00 32.77      A    C  
ANISOU 1166  CA  THR A 144     4211   4413   3826    136    654    258  A    C  
ATOM   1167  C   THR A 144      15.500  10.123  42.954  1.00 33.93      A    C  
ANISOU 1167  C   THR A 144     4431   4545   3914     27    614    244  A    C  
ATOM   1168  O   THR A 144      16.396  10.741  43.515  1.00 34.98      A    O  
ANISOU 1168  O   THR A 144     4430   4962   3896   -110    630    395  A    O  
ATOM   1169  CB  THR A 144      15.858  11.127  40.664  1.00 31.80      A    C  
ANISOU 1169  CB  THR A 144     4107   4309   3663    126    586    340  A    C  
ATOM   1170  CG2 THR A 144      16.689   9.866  40.269  1.00 32.27      A    C  
ANISOU 1170  CG2 THR A 144     3781   4678   3802    272    876    334  A    C  
ATOM   1171  OG1 THR A 144      15.166  11.650  39.507  1.00 33.25      A    O  
ANISOU 1171  OG1 THR A 144     3935   4369   4329    390    597    357  A    O  
ATOM   1172  N   GLN A 145      15.013   8.968  43.435  1.00 35.31      A    N  
ANISOU 1172  N   GLN A 145     4699   4536   4178    174    648    106  A    N  
ATOM   1173  CA  GLN A 145      15.636   8.259  44.547  1.00 35.76      A    C  
ANISOU 1173  CA  GLN A 145     4735   4731   4117    161    488     42  A    C  
ATOM   1174  C   GLN A 145      15.751   9.173  45.752  1.00 37.53      A    C  
ANISOU 1174  C   GLN A 145     5016   4829   4415    140    365     22  A    C  
ATOM   1175  O   GLN A 145      16.731   9.152  46.537  1.00 37.45      A    O  
ANISOU 1175  O   GLN A 145     4829   4963   4436    151    374    -32  A    O  
ATOM   1176  CB  GLN A 145      16.937   7.576  44.159  1.00 36.03      A    C  
ANISOU 1176  CB  GLN A 145     4776   4559   4355    122    388     86  A    C  
ATOM   1177  CG  GLN A 145      16.715   6.545  43.006  1.00 36.05      A    C  
ANISOU 1177  CG  GLN A 145     4628   4843   4224    393    538   -196  A    C  
ATOM   1178  CD  GLN A 145      17.888   5.597  42.732  1.00 36.94      A    C  
ANISOU 1178  CD  GLN A 145     4350   4932   4752     43    749    -34  A    C  
ATOM   1179  NE2 GLN A 145      18.984   5.758  43.463  1.00 38.69      A    N  
ANISOU 1179  NE2 GLN A 145     4477   4518   5703    305    446   -142  A    N  
ATOM   1180  OE1 GLN A 145      17.781   4.697  41.880  1.00 39.71      A    O  
ANISOU 1180  OE1 GLN A 145     4456   4867   5762   -354    792   -177  A    O  
ATOM   1181  N   GLY A 146      14.715   9.990  45.908  1.00 38.72      A    N  
ANISOU 1181  N   GLY A 146     5240   5039   4431    148    355     21  A    N  
ATOM   1182  CA  GLY A 146      14.639  10.837  47.109  1.00 39.07      A    C  
ANISOU 1182  CA  GLY A 146     5457   5075   4310     42    298     16  A    C  
ATOM   1183  C   GLY A 146      15.335  12.181  46.935  1.00 39.36      A    C  
ANISOU 1183  C   GLY A 146     5421   5135   4396     17    203     78  A    C  
ATOM   1184  O   GLY A 146      15.198  13.044  47.806  1.00 40.60      A    O  
ANISOU 1184  O   GLY A 146     5962   5317   4148    -92    236    274  A    O  
ATOM   1185  N   VAL A 147      16.036  12.407  45.814  1.00 38.23      A    N  
ANISOU 1185  N   VAL A 147     5082   5138   4305     99     62     89  A    N  
ATOM   1186  CA  VAL A 147      16.735  13.668  45.564  1.00 37.32      A    C  
ANISOU 1186  CA  VAL A 147     4648   5057   4473    103     83    156  A    C  
ATOM   1187  C   VAL A 147      15.830  14.551  44.678  1.00 37.18      A    C  
ANISOU 1187  C   VAL A 147     4714   4962   4451     48    168     83  A    C  
ATOM   1188  O   VAL A 147      15.428  14.166  43.563  1.00 36.75      A    O  
ANISOU 1188  O   VAL A 147     4662   5045   4255     11    123    115  A    O  
ATOM   1189  CB  VAL A 147      18.154  13.446  44.868  1.00 37.56      A    C  
ANISOU 1189  CB  VAL A 147     4530   5097   4644     86    -36    244  A    C  
ATOM   1190  CG1 VAL A 147      18.840  14.724  44.664  1.00 37.93      A    C  
ANISOU 1190  CG1 VAL A 147     4688   5155   4566     -8   -270    388  A    C  
ATOM   1191  CG2 VAL A 147      19.018  12.518  45.721  1.00 37.31      A    C  
ANISOU 1191  CG2 VAL A 147     3932   5433   4809     89   -109    469  A    C  
ATOM   1192  N   THR A 148      15.488  15.724  45.198  1.00 37.04      A    N  
ANISOU 1192  N   THR A 148     4649   4983   4441    -28    251    -14  A    N  
ATOM   1193  CA  THR A 148      14.479  16.585  44.561  1.00 36.40      A    C  
ANISOU 1193  CA  THR A 148     4703   4903   4224      8    356    -30  A    C  
ATOM   1194  C   THR A 148      15.038  17.805  43.827  1.00 35.72      A    C  
ANISOU 1194  C   THR A 148     4668   4817   4087     39    313    -87  A    C  
ATOM   1195  O   THR A 148      16.168  18.263  44.072  1.00 35.75      A    O  
ANISOU 1195  O   THR A 148     4854   5057   3670      0    160    -44  A    O  
ATOM   1196  CB  THR A 148      13.428  17.060  45.575  1.00 36.84      A    C  
ANISOU 1196  CB  THR A 148     4678   4992   4326    -62    428    -12  A    C  
ATOM   1197  CG2 THR A 148      12.700  15.861  46.218  1.00 38.99      A    C  
ANISOU 1197  CG2 THR A 148     5096   5277   4441     30    523    291  A    C  
ATOM   1198  OG1 THR A 148      14.092  17.840  46.556  1.00 37.01      A    O  
ANISOU 1198  OG1 THR A 148     4710   5263   4087   -143    760   -216  A    O  
ATOM   1199  N   TYR A 149      14.240  18.291  42.878  1.00 35.39      A    N  
ANISOU 1199  N   TYR A 149     4543   4665   4236     36    279   -151  A    N  
ATOM   1200  CA  TYR A 149      14.646  19.367  41.956  1.00 34.07      A    C  
ANISOU 1200  CA  TYR A 149     4319   4537   4087    127    317   -185  A    C  
ATOM   1201  C   TYR A 149      13.347  19.752  41.266  1.00 34.46      A    C  
ANISOU 1201  C   TYR A 149     4406   4437   4249    144    247   -303  A    C  
ATOM   1202  O   TYR A 149      12.397  18.977  41.230  1.00 35.45      A    O  
ANISOU 1202  O   TYR A 149     4333   4529   4607     97    244   -315  A    O  
ATOM   1203  CB  TYR A 149      15.729  18.904  40.919  1.00 33.91      A    C  
ANISOU 1203  CB  TYR A 149     4208   4487   4189    144    320   -314  A    C  
ATOM   1204  CG  TYR A 149      15.343  17.617  40.249  1.00 31.29      A    C  
ANISOU 1204  CG  TYR A 149     3689   4399   3800    271    848   -161  A    C  
ATOM   1205  CD1 TYR A 149      14.625  17.602  39.048  1.00 28.41      A    C  
ANISOU 1205  CD1 TYR A 149     3051   4018   3723    209   1073   -325  A    C  
ATOM   1206  CD2 TYR A 149      15.627  16.399  40.862  1.00 31.13      A    C  
ANISOU 1206  CD2 TYR A 149     3996   4128   3703    140    821    -22  A    C  
ATOM   1207  CE1 TYR A 149      14.211  16.406  38.509  1.00 30.03      A    C  
ANISOU 1207  CE1 TYR A 149     3782   3857   3769    166    617   -131  A    C  
ATOM   1208  CE2 TYR A 149      15.253  15.210  40.313  1.00 30.03      A    C  
ANISOU 1208  CE2 TYR A 149     3674   4225   3510     14    746   -166  A    C  
ATOM   1209  CZ  TYR A 149      14.537  15.216  39.169  1.00 30.53      A    C  
ANISOU 1209  CZ  TYR A 149     4106   3916   3576     99    637   -156  A    C  
ATOM   1210  OH  TYR A 149      14.161  14.029  38.662  1.00 31.88      A    O  
ANISOU 1210  OH  TYR A 149     4075   3755   4282    360    451    -75  A    O  
ATOM   1211  N   ASN A 150      13.303  20.970  40.758  1.00 34.50      A    N  
ANISOU 1211  N   ASN A 150     4497   4315   4294    308      3   -312  A    N  
ATOM   1212  CA  ASN A 150      12.223  21.438  39.913  1.00 34.21      A    C  
ANISOU 1212  CA  ASN A 150     4720   4171   4107    318   -193   -484  A    C  
ATOM   1213  C   ASN A 150      12.210  20.716  38.543  1.00 33.64      A    C  
ANISOU 1213  C   ASN A 150     4576   4129   4076    298   -125   -497  A    C  
ATOM   1214  O   ASN A 150      13.093  20.972  37.716  1.00 33.14      A    O  
ANISOU 1214  O   ASN A 150     4918   3990   3682    316   -193   -505  A    O  
ATOM   1215  CB  ASN A 150      12.367  22.969  39.752  1.00 35.18      A    C  
ANISOU 1215  CB  ASN A 150     4842   4291   4232    480   -401   -387  A    C  
ATOM   1216  CG  ASN A 150      11.155  23.597  39.130  1.00 37.03      A    C  
ANISOU 1216  CG  ASN A 150     4987   4123   4958    764   -567   -548  A    C  
ATOM   1217  ND2 ASN A 150      11.023  24.909  39.302  1.00 37.36      A    N  
ANISOU 1217  ND2 ASN A 150     5530   3787   4878   1080  -1022   -351  A    N  
ATOM   1218  OD1 ASN A 150      10.340  22.900  38.461  1.00 39.09      A    O  
ANISOU 1218  OD1 ASN A 150     5090   4238   5524    801  -1030   -406  A    O  
ATOM   1219  N   PRO A 151      11.196  19.874  38.292  1.00 32.65      A    N  
ANISOU 1219  N   PRO A 151     4436   3960   4009    134     -2   -595  A    N  
ATOM   1220  CA  PRO A 151      11.236  19.131  37.006  1.00 32.71      A    C  
ANISOU 1220  CA  PRO A 151     4285   4089   4054     40    -66   -526  A    C  
ATOM   1221  C   PRO A 151      11.086  20.058  35.786  1.00 33.83      A    C  
ANISOU 1221  C   PRO A 151     4400   4223   4229    -19     -4   -511  A    C  
ATOM   1222  O   PRO A 151      11.359  19.628  34.683  1.00 33.05      A    O  
ANISOU 1222  O   PRO A 151     4527   4028   4001    -19    100   -479  A    O  
ATOM   1223  CB  PRO A 151      10.071  18.156  37.112  1.00 32.99      A    C  
ANISOU 1223  CB  PRO A 151     4323   3944   4265    128    102   -588  A    C  
ATOM   1224  CG  PRO A 151       9.033  18.926  37.910  1.00 32.22      A    C  
ANISOU 1224  CG  PRO A 151     4507   4068   3664    151     55   -888  A    C  
ATOM   1225  CD  PRO A 151       9.888  19.706  38.975  1.00 32.77      A    C  
ANISOU 1225  CD  PRO A 151     4371   3902   4179      0   -143   -643  A    C  
ATOM   1226  N   ASP A 152      10.689  21.323  35.997  1.00 33.73      A    N  
ANISOU 1226  N   ASP A 152     4193   4305   4315    -56    -91   -518  A    N  
ATOM   1227  CA  ASP A 152      10.619  22.305  34.906  1.00 34.99      A    C  
ANISOU 1227  CA  ASP A 152     4413   4522   4357    -32      7   -528  A    C  
ATOM   1228  C   ASP A 152      11.808  23.233  34.799  1.00 34.22      A    C  
ANISOU 1228  C   ASP A 152     4287   4465   4248     55     67   -573  A    C  
ATOM   1229  O   ASP A 152      11.861  24.056  33.897  1.00 34.98      A    O  
ANISOU 1229  O   ASP A 152     4354   4655   4280    -80     87   -548  A    O  
ATOM   1230  CB  ASP A 152       9.362  23.148  35.022  1.00 35.55      A    C  
ANISOU 1230  CB  ASP A 152     4338   4755   4412     45   -151   -534  A    C  
ATOM   1231  CG  ASP A 152       8.131  22.307  34.963  1.00 38.32      A    C  
ANISOU 1231  CG  ASP A 152     4824   5003   4729   -235     69   -437  A    C  
ATOM   1232  OD1 ASP A 152       7.869  21.722  33.901  1.00 37.41      A    O  
ANISOU 1232  OD1 ASP A 152     4261   5251   4699   -351    104   -588  A    O  
ATOM   1233  OD2 ASP A 152       7.458  22.163  35.999  1.00 42.20      A    O1-
ANISOU 1233  OD2 ASP A 152     5342   5461   5229    275    262   -877  A    O1-
ATOM   1234  N   HIS A 153      12.729  23.150  35.731  1.00 33.22      A    N  
ANISOU 1234  N   HIS A 153     4264   4354   4002    173    125   -749  A    N  
ATOM   1235  CA  HIS A 153      13.952  23.984  35.679  1.00 33.54      A    C  
ANISOU 1235  CA  HIS A 153     4524   4116   4104    110    109   -595  A    C  
ATOM   1236  C   HIS A 153      15.072  23.096  36.197  1.00 32.42      A    C  
ANISOU 1236  C   HIS A 153     4237   4081   3998    113    175   -566  A    C  
ATOM   1237  O   HIS A 153      15.615  23.312  37.278  1.00 33.96      A    O  
ANISOU 1237  O   HIS A 153     4433   4238   4230    294    -16   -488  A    O  
ATOM   1238  CB  HIS A 153      13.749  25.289  36.489  1.00 35.02      A    C  
ANISOU 1238  CB  HIS A 153     4765   4278   4262    266     29   -654  A    C  
ATOM   1239  CG  HIS A 153      12.689  26.165  35.888  1.00 41.49      A    C  
ANISOU 1239  CG  HIS A 153     5454   5034   5274    187   -130   -555  A    C  
ATOM   1240  CD2 HIS A 153      11.349  26.237  36.108  1.00 43.90      A    C  
ANISOU 1240  CD2 HIS A 153     5428   5276   5976    170    -76   -600  A    C  
ATOM   1241  ND1 HIS A 153      12.938  26.987  34.806  1.00 46.16      A    N  
ANISOU 1241  ND1 HIS A 153     6207   5283   6048   -136    -60   -152  A    N  
ATOM   1242  CE1 HIS A 153      11.814  27.584  34.432  1.00 45.80      A    C  
ANISOU 1242  CE1 HIS A 153     5672   5747   5983    262     66   -416  A    C  
ATOM   1243  NE2 HIS A 153      10.834  27.134  35.196  1.00 45.36      A    N  
ANISOU 1243  NE2 HIS A 153     5798   5392   6044     76   -197   -345  A    N  
ATOM   1244  N   ILE A 154      15.297  21.996  35.478  1.00 31.29      A    N  
ANISOU 1244  N   ILE A 154     4180   3936   3772    275    289   -365  A    N  
ATOM   1245  CA  ILE A 154      16.292  21.001  35.853  1.00 30.89      A    C  
ANISOU 1245  CA  ILE A 154     4221   3825   3690    264     90   -322  A    C  
ATOM   1246  C   ILE A 154      17.669  21.683  35.951  1.00 29.25      A    C  
ANISOU 1246  C   ILE A 154     4050   3591   3471    314    140   -125  A    C  
ATOM   1247  O   ILE A 154      18.034  22.428  35.049  1.00 30.10      A    O  
ANISOU 1247  O   ILE A 154     4390   3707   3340    311    202    -91  A    O  
ATOM   1248  CB  ILE A 154      16.239  19.763  34.877  1.00 31.07      A    C  
ANISOU 1248  CB  ILE A 154     4208   3716   3881    297     90   -280  A    C  
ATOM   1249  CG1 ILE A 154      14.920  18.972  35.185  1.00 31.72      A    C  
ANISOU 1249  CG1 ILE A 154     4021   3815   4214     17    -77   -617  A    C  
ATOM   1250  CG2 ILE A 154      17.512  18.897  35.013  1.00 30.73      A    C  
ANISOU 1250  CG2 ILE A 154     4110   3947   3619    486    118   -376  A    C  
ATOM   1251  CD1 ILE A 154      14.573  17.809  34.189  1.00 33.08      A    C  
ANISOU 1251  CD1 ILE A 154     4137   4359   4071    102   -448   -742  A    C  
ATOM   1252  N   PRO A 155      18.397  21.528  37.083  1.00 29.64      A    N  
ANISOU 1252  N   PRO A 155     4011   3812   3437    286     41    174  A    N  
ATOM   1253  CA  PRO A 155      19.681  22.245  37.103  1.00 29.40      A    C  
ANISOU 1253  CA  PRO A 155     3899   3935   3334    232    -78    247  A    C  
ATOM   1254  C   PRO A 155      20.709  21.643  36.125  1.00 28.98      A    C  
ANISOU 1254  C   PRO A 155     3780   3963   3265    165    -48    275  A    C  
ATOM   1255  O   PRO A 155      20.490  20.492  35.600  1.00 27.28      A    O  
ANISOU 1255  O   PRO A 155     3369   3986   3010    170    -34    247  A    O  
ATOM   1256  CB  PRO A 155      20.195  22.039  38.522  1.00 31.42      A    C  
ANISOU 1256  CB  PRO A 155     4114   4202   3620    278    -35    110  A    C  
ATOM   1257  CG  PRO A 155      19.604  20.699  38.937  1.00 32.39      A    C  
ANISOU 1257  CG  PRO A 155     4180   4347   3779     17   -182    339  A    C  
ATOM   1258  CD  PRO A 155      18.205  20.635  38.248  1.00 29.32      A    C  
ANISOU 1258  CD  PRO A 155     3772   3942   3423    359     44    205  A    C  
ATOM   1259  N   ASP A 156      21.830  22.354  35.904  1.00 29.27      A    N  
ANISOU 1259  N   ASP A 156     3890   4016   3212     48   -197    257  A    N  
ATOM   1260  CA  ASP A 156      22.915  21.790  35.062  1.00 30.30      A    C  
ANISOU 1260  CA  ASP A 156     3903   4136   3471     72     16    250  A    C  
ATOM   1261  C   ASP A 156      23.447  20.454  35.566  1.00 31.02      A    C  
ANISOU 1261  C   ASP A 156     4072   4116   3596    -17    187     66  A    C  
ATOM   1262  O   ASP A 156      23.673  19.572  34.795  1.00 30.27      A    O  
ANISOU 1262  O   ASP A 156     3781   4352   3366    -22    447   -183  A    O  
ATOM   1263  CB  ASP A 156      24.111  22.767  34.870  1.00 31.81      A    C  
ANISOU 1263  CB  ASP A 156     4031   4188   3866    -29   -133    367  A    C  
ATOM   1264  CG  ASP A 156      23.701  24.115  34.156  1.00 36.63      A    C  
ANISOU 1264  CG  ASP A 156     4853   4813   4251      4    -29    381  A    C  
ATOM   1265  OD1 ASP A 156      22.548  24.266  33.654  1.00 40.51      A    O  
ANISOU 1265  OD1 ASP A 156     5298   6196   3896     58    159    -93  A    O  
ATOM   1266  OD2 ASP A 156      24.545  25.041  34.091  1.00 42.17      A    O1-
ANISOU 1266  OD2 ASP A 156     5397   5504   5120   -402    148    227  A    O1-
ATOM   1267  N   ARG A 157      23.619  20.305  36.876  1.00 30.51      A    N  
ANISOU 1267  N   ARG A 157     3999   4187   3405    192      9     26  A    N  
ATOM   1268  CA  ARG A 157      24.056  19.060  37.482  1.00 33.55      A    C  
ANISOU 1268  CA  ARG A 157     4462   4375   3910     83    122    140  A    C  
ATOM   1269  C   ARG A 157      23.413  18.971  38.868  1.00 32.80      A    C  
ANISOU 1269  C   ARG A 157     4485   4269   3707    211     75     81  A    C  
ATOM   1270  O   ARG A 157      23.038  20.006  39.441  1.00 33.76      A    O  
ANISOU 1270  O   ARG A 157     4758   4336   3733    119    108    101  A    O  
ATOM   1271  CB  ARG A 157      25.560  19.018  37.578  1.00 34.88      A    C  
ANISOU 1271  CB  ARG A 157     4530   4545   4176    417    -86    223  A    C  
ATOM   1272  CG  ARG A 157      26.164  20.098  38.529  1.00 39.53      A    C  
ANISOU 1272  CG  ARG A 157     5122   5234   4663    -40    -31    300  A    C  
ATOM   1273  CD  ARG A 157      27.711  20.257  38.352  1.00 45.16      A    C  
ANISOU 1273  CD  ARG A 157     5488   6438   5231   -461    359    899  A    C  
ATOM   1274  NE  ARG A 157      28.013  20.291  36.934  1.00 50.64      A    N  
ANISOU 1274  NE  ARG A 157     6346   7226   5667   -477    480    633  A    N  
ATOM   1275  CZ  ARG A 157      27.958  21.389  36.147  1.00 52.32      A    C  
ANISOU 1275  CZ  ARG A 157     6597   7242   6039   -593    296    499  A    C  
ATOM   1276  NH1 ARG A 157      27.604  22.591  36.611  1.00 48.73      A    N1+
ANISOU 1276  NH1 ARG A 157     5927   6944   5645   -662    226    165  A    N1+
ATOM   1277  NH2 ARG A 157      28.258  21.273  34.851  1.00 53.99      A    N  
ANISOU 1277  NH2 ARG A 157     7013   7685   5813  -1039     73    877  A    N  
ATOM   1278  N   LEU A 158      23.226  17.749  39.374  1.00 32.11      A    N  
ANISOU 1278  N   LEU A 158     4353   4205   3641    228     83     34  A    N  
ATOM   1279  CA  LEU A 158      22.444  17.549  40.575  1.00 32.03      A    C  
ANISOU 1279  CA  LEU A 158     4463   4299   3407    135    -10      2  A    C  
ATOM   1280  C   LEU A 158      23.332  16.726  41.498  1.00 33.23      A    C  
ANISOU 1280  C   LEU A 158     4546   4529   3548    112    -80    -29  A    C  
ATOM   1281  O   LEU A 158      23.615  15.552  41.194  1.00 31.98      A    O  
ANISOU 1281  O   LEU A 158     4493   4462   3193    156   -213     22  A    O  
ATOM   1282  CB  LEU A 158      21.124  16.764  40.272  1.00 31.85      A    C  
ANISOU 1282  CB  LEU A 158     4471   4366   3262    156     82    -61  A    C  
ATOM   1283  CG  LEU A 158      20.156  16.418  41.433  1.00 34.39      A    C  
ANISOU 1283  CG  LEU A 158     4580   4562   3922   -143    118   -113  A    C  
ATOM   1284  CD1 LEU A 158      19.433  17.669  41.965  1.00 34.32      A    C  
ANISOU 1284  CD1 LEU A 158     4872   4682   3484    132    202   -240  A    C  
ATOM   1285  CD2 LEU A 158      19.098  15.346  41.148  1.00 33.58      A    C  
ANISOU 1285  CD2 LEU A 158     4193   5054   3509     32    171   -617  A    C  
ATOM   1286  N   PRO A 159      23.748  17.301  42.651  1.00 34.81      A    N  
ANISOU 1286  N   PRO A 159     4669   4612   3945     -1   -223    -77  A    N  
ATOM   1287  CA  PRO A 159      24.388  16.423  43.656  1.00 34.77      A    C  
ANISOU 1287  CA  PRO A 159     4632   4764   3813    -62   -109    -59  A    C  
ATOM   1288  C   PRO A 159      23.479  15.270  44.003  1.00 33.78      A    C  
ANISOU 1288  C   PRO A 159     4522   4725   3587    -48    -72   -106  A    C  
ATOM   1289  O   PRO A 159      22.280  15.487  44.279  1.00 33.44      A    O  
ANISOU 1289  O   PRO A 159     4043   4935   3725   -319    106   -106  A    O  
ATOM   1290  CB  PRO A 159      24.600  17.354  44.864  1.00 36.41      A    C  
ANISOU 1290  CB  PRO A 159     4950   4750   4132    -86    -56    -99  A    C  
ATOM   1291  CG  PRO A 159      24.476  18.734  44.299  1.00 37.32      A    C  
ANISOU 1291  CG  PRO A 159     5269   4957   3952    -80   -189    205  A    C  
ATOM   1292  CD  PRO A 159      23.534  18.663  43.174  1.00 36.11      A    C  
ANISOU 1292  CD  PRO A 159     4814   4764   4141    -53   -269   -159  A    C  
ATOM   1293  N   PHE A 160      24.021  14.058  43.940  1.00 32.67      A    N  
ANISOU 1293  N   PHE A 160     4368   4740   3304     52    -47     74  A    N  
ATOM   1294  CA  PHE A 160      23.180  12.861  43.894  1.00 33.04      A    C  
ANISOU 1294  CA  PHE A 160     4450   4738   3366    139    -15    280  A    C  
ATOM   1295  C   PHE A 160      23.825  11.779  44.739  1.00 35.02      A    C  
ANISOU 1295  C   PHE A 160     4645   4831   3828    251    -44    346  A    C  
ATOM   1296  O   PHE A 160      24.667  11.018  44.256  1.00 34.82      A    O  
ANISOU 1296  O   PHE A 160     4968   4465   3793    229    100    627  A    O  
ATOM   1297  CB  PHE A 160      22.866  12.326  42.465  1.00 32.83      A    C  
ANISOU 1297  CB  PHE A 160     4269   4817   3386    236    -53    178  A    C  
ATOM   1298  CG  PHE A 160      21.938  11.119  42.461  1.00 33.29      A    C  
ANISOU 1298  CG  PHE A 160     4465   4990   3191    244   -116    -51  A    C  
ATOM   1299  CD1 PHE A 160      20.569  11.273  42.671  1.00 34.48      A    C  
ANISOU 1299  CD1 PHE A 160     4266   5285   3550    402    -59   -158  A    C  
ATOM   1300  CD2 PHE A 160      22.437   9.800  42.298  1.00 39.67      A    C  
ANISOU 1300  CD2 PHE A 160     4781   5436   4853    469     52   -134  A    C  
ATOM   1301  CE1 PHE A 160      19.694  10.138  42.682  1.00 38.55      A    C  
ANISOU 1301  CE1 PHE A 160     4410   5546   4690    321    257     18  A    C  
ATOM   1302  CE2 PHE A 160      21.566   8.653  42.330  1.00 40.12      A    C  
ANISOU 1302  CE2 PHE A 160     4727   5709   4806    494    178   -128  A    C  
ATOM   1303  CZ  PHE A 160      20.175   8.833  42.543  1.00 37.22      A    C  
ANISOU 1303  CZ  PHE A 160     4399   5742   4000    515    384   -316  A    C  
ATOM   1304  N   LYS A 161      23.437  11.790  46.022  1.00 36.08      A    N  
ANISOU 1304  N   LYS A 161     4680   4998   4030    201    -14    494  A    N  
ATOM   1305  CA  LYS A 161      24.047  10.975  47.075  1.00 36.91      A    C  
ANISOU 1305  CA  LYS A 161     4573   5157   4294     71   -122    400  A    C  
ATOM   1306  C   LYS A 161      25.549  11.333  47.063  1.00 36.09      A    C  
ANISOU 1306  C   LYS A 161     4650   4927   4133     -6   -251    309  A    C  
ATOM   1307  O   LYS A 161      25.898  12.492  47.301  1.00 37.87      A    O  
ANISOU 1307  O   LYS A 161     4885   5205   4298   -113   -113    402  A    O  
ATOM   1308  CB  LYS A 161      23.801   9.495  46.807  1.00 38.48      A    C  
ANISOU 1308  CB  LYS A 161     4670   5248   4700    -20   -184    392  A    C  
ATOM   1309  CG  LYS A 161      22.447   9.009  47.254  1.00 43.97      A    C  
ANISOU 1309  CG  LYS A 161     5337   6194   5172   -457   -222    464  A    C  
ATOM   1310  CD  LYS A 161      21.611   8.534  46.115  1.00 44.18      A    C  
ANISOU 1310  CD  LYS A 161     5265   6285   5233   -177   -604    427  A    C  
ATOM   1311  CE  LYS A 161      20.215   8.141  46.588  1.00 47.54      A    C  
ANISOU 1311  CE  LYS A 161     5978   6602   5482   -874   -413    483  A    C  
ATOM   1312  NZ  LYS A 161      19.883   6.822  45.996  1.00 51.43      A    N1+
ANISOU 1312  NZ  LYS A 161     6595   7215   5727   -702   -562    131  A    N1+
ATOM   1313  N   ASP A 162      26.416  10.378  46.738  1.00 33.32      A    N  
ANISOU 1313  N   ASP A 162     4278   4781   3601     44   -204    258  A    N  
ATOM   1314  CA  ASP A 162      27.824  10.656  46.674  1.00 32.40      A    C  
ANISOU 1314  CA  ASP A 162     4229   4398   3683   -101   -346    121  A    C  
ATOM   1315  C   ASP A 162      28.338  11.043  45.287  1.00 31.53      A    C  
ANISOU 1315  C   ASP A 162     4093   4256   3628   -152   -350    214  A    C  
ATOM   1316  O   ASP A 162      29.527  11.351  45.146  1.00 32.91      A    O  
ANISOU 1316  O   ASP A 162     4384   4420   3700   -238   -318    105  A    O  
ATOM   1317  CB  ASP A 162      28.622   9.436  47.190  1.00 32.29      A    C  
ANISOU 1317  CB  ASP A 162     4345   4259   3663   -155   -435    243  A    C  
ATOM   1318  CG  ASP A 162      28.416   9.179  48.683  1.00 32.41      A    C  
ANISOU 1318  CG  ASP A 162     4090   4345   3878   -209    -72     34  A    C  
ATOM   1319  OD1 ASP A 162      28.433  10.136  49.481  1.00 29.69      A    O  
ANISOU 1319  OD1 ASP A 162     3882   4267   3132    -69    422    -82  A    O  
ATOM   1320  OD2 ASP A 162      28.303   7.990  49.062  1.00 36.34      A    O1-
ANISOU 1320  OD2 ASP A 162     4665   4567   4574   -238   -214    329  A    O1-
ATOM   1321  N   LEU A 163      27.447  10.974  44.278  1.00 31.24      A    N  
ANISOU 1321  N   LEU A 163     4163   4048   3655   -125   -239    209  A    N  
ATOM   1322  CA  LEU A 163      27.741  11.273  42.894  1.00 29.87      A    C  
ANISOU 1322  CA  LEU A 163     4006   3738   3604    -22   -248     99  A    C  
ATOM   1323  C   LEU A 163      27.160  12.626  42.436  1.00 30.37      A    C  
ANISOU 1323  C   LEU A 163     4144   3834   3560    -22   -205    212  A    C  
ATOM   1324  O   LEU A 163      26.593  13.418  43.237  1.00 30.11      A    O  
ANISOU 1324  O   LEU A 163     4417   3645   3378      2   -231    238  A    O  
ATOM   1325  CB  LEU A 163      27.205  10.120  41.996  1.00 29.98      A    C  
ANISOU 1325  CB  LEU A 163     3850   3851   3689   -104    -89     82  A    C  
ATOM   1326  CG  LEU A 163      27.652   8.704  42.440  1.00 29.56      A    C  
ANISOU 1326  CG  LEU A 163     3702   3571   3957   -256   -550     56  A    C  
ATOM   1327  CD1 LEU A 163      26.636   7.674  41.833  1.00 30.09      A    C  
ANISOU 1327  CD1 LEU A 163     3756   3630   4044   -419   -967    153  A    C  
ATOM   1328  CD2 LEU A 163      29.094   8.422  41.972  1.00 31.39      A    C  
ANISOU 1328  CD2 LEU A 163     4375   3876   3674    159   -493    486  A    C  
ATOM   1329  N   THR A 164      27.336  12.895  41.146  1.00 30.97      A    N  
ANISOU 1329  N   THR A 164     4339   3900   3529    -33   -357    157  A    N  
ATOM   1330  CA  THR A 164      26.767  14.079  40.510  1.00 30.36      A    C  
ANISOU 1330  CA  THR A 164     4033   4021   3479    -11   -359    212  A    C  
ATOM   1331  C   THR A 164      26.023  13.545  39.284  1.00 30.26      A    C  
ANISOU 1331  C   THR A 164     3980   4095   3422     -8   -305    109  A    C  
ATOM   1332  O   THR A 164      26.646  13.061  38.351  1.00 29.67      A    O  
ANISOU 1332  O   THR A 164     4059   4080   3133     62   -251    139  A    O  
ATOM   1333  CB  THR A 164      27.857  15.015  40.030  1.00 30.00      A    C  
ANISOU 1333  CB  THR A 164     4144   3983   3269   -104   -337    368  A    C  
ATOM   1334  CG2 THR A 164      27.230  16.251  39.322  1.00 34.02      A    C  
ANISOU 1334  CG2 THR A 164     4252   4186   4488    374   -344    446  A    C  
ATOM   1335  OG1 THR A 164      28.614  15.496  41.131  1.00 29.99      A    O  
ANISOU 1335  OG1 THR A 164     3759   3936   3699   -360    133    173  A    O  
ATOM   1336  N   LEU A 165      24.692  13.666  39.301  1.00 29.26      A    N  
ANISOU 1336  N   LEU A 165     3838   3930   3347   -143   -211    173  A    N  
ATOM   1337  CA  LEU A 165      23.865  13.222  38.225  1.00 27.18      A    C  
ANISOU 1337  CA  LEU A 165     3578   3653   3093   -218   -307    145  A    C  
ATOM   1338  C   LEU A 165      23.737  14.418  37.206  1.00 29.10      A    C  
ANISOU 1338  C   LEU A 165     4014   3745   3294    -47   -304    140  A    C  
ATOM   1339  O   LEU A 165      23.475  15.587  37.592  1.00 29.57      A    O  
ANISOU 1339  O   LEU A 165     4298   3771   3165     36   -237   -100  A    O  
ATOM   1340  CB  LEU A 165      22.483  12.850  38.777  1.00 26.93      A    C  
ANISOU 1340  CB  LEU A 165     3713   3595   2924   -273   -175     -4  A    C  
ATOM   1341  CG  LEU A 165      21.518  12.211  37.757  1.00 24.81      A    C  
ANISOU 1341  CG  LEU A 165     2551   3568   3304   -406    -78   -213  A    C  
ATOM   1342  CD1 LEU A 165      21.997  10.841  37.239  1.00 27.33      A    C  
ANISOU 1342  CD1 LEU A 165     3057   3413   3914    -95    488   -146  A    C  
ATOM   1343  CD2 LEU A 165      20.170  12.009  38.493  1.00 28.63      A    C  
ANISOU 1343  CD2 LEU A 165     2693   4339   3843   -523    319     78  A    C  
ATOM   1344  N   GLY A 166      23.933  14.143  35.930  1.00 28.69      A    N  
ANISOU 1344  N   GLY A 166     3959   3680   3262     42   -255    154  A    N  
ATOM   1345  CA  GLY A 166      23.784  15.208  34.910  1.00 27.54      A    C  
ANISOU 1345  CA  GLY A 166     3692   3805   2965      5   -312    298  A    C  
ATOM   1346  C   GLY A 166      22.333  15.701  34.757  1.00 26.34      A    C  
ANISOU 1346  C   GLY A 166     3518   3635   2853     77    124    214  A    C  
ATOM   1347  O   GLY A 166      21.382  14.891  34.694  1.00 27.03      A    O  
ANISOU 1347  O   GLY A 166     3695   3707   2868    149   -315    213  A    O  
ATOM   1348  N   GLY A 167      22.165  17.024  34.621  1.00 24.59      A    N  
ANISOU 1348  N   GLY A 167     3332   3489   2520     -4    184     85  A    N  
ATOM   1349  CA  GLY A 167      20.887  17.597  34.199  1.00 24.00      A    C  
ANISOU 1349  CA  GLY A 167     3215   3501   2399     12    367    -34  A    C  
ATOM   1350  C   GLY A 167      20.336  16.922  32.943  1.00 25.45      A    C  
ANISOU 1350  C   GLY A 167     3313   3516   2839    -70     83    133  A    C  
ATOM   1351  O   GLY A 167      19.169  16.719  32.811  1.00 25.68      A    O  
ANISOU 1351  O   GLY A 167     3386   3565   2803    -93    -33     98  A    O  
ATOM   1352  N   PHE A 168      21.215  16.577  32.012  1.00 24.83      A    N  
ANISOU 1352  N   PHE A 168     3511   3376   2544    -40    179    116  A    N  
ATOM   1353  CA  PHE A 168      20.767  16.020  30.742  1.00 26.60      A    C  
ANISOU 1353  CA  PHE A 168     3623   3509   2974   -164     72    266  A    C  
ATOM   1354  C   PHE A 168      20.236  14.609  30.895  1.00 26.88      A    C  
ANISOU 1354  C   PHE A 168     3657   3509   3045    -88    104    171  A    C  
ATOM   1355  O   PHE A 168      19.235  14.253  30.261  1.00 26.33      A    O  
ANISOU 1355  O   PHE A 168     3559   3504   2940   -133    368    259  A    O  
ATOM   1356  CB  PHE A 168      21.848  16.135  29.663  1.00 27.27      A    C  
ANISOU 1356  CB  PHE A 168     3771   3788   2799   -261    286    144  A    C  
ATOM   1357  CG  PHE A 168      21.312  15.984  28.226  1.00 28.35      A    C  
ANISOU 1357  CG  PHE A 168     3690   3978   3103   -392    329    249  A    C  
ATOM   1358  CD1 PHE A 168      20.260  16.753  27.761  1.00 27.33      A    C  
ANISOU 1358  CD1 PHE A 168     3596   3753   3033   -380    836    279  A    C  
ATOM   1359  CD2 PHE A 168      21.937  15.080  27.335  1.00 29.75      A    C  
ANISOU 1359  CD2 PHE A 168     4511   3954   2837   -729    602    153  A    C  
ATOM   1360  CE1 PHE A 168      19.781  16.646  26.449  1.00 31.28      A    C  
ANISOU 1360  CE1 PHE A 168     4312   4154   3418     -6     27    -51  A    C  
ATOM   1361  CE2 PHE A 168      21.498  14.966  25.985  1.00 31.04      A    C  
ANISOU 1361  CE2 PHE A 168     3914   4383   3494   -350   -214    -82  A    C  
ATOM   1362  CZ  PHE A 168      20.398  15.743  25.532  1.00 30.10      A    C  
ANISOU 1362  CZ  PHE A 168     4219   3571   3644   -116    510    588  A    C  
ATOM   1363  N   TYR A 169      20.825  13.850  31.816  1.00 25.68      A    N  
ANISOU 1363  N   TYR A 169     3347   3249   3160    115     54    245  A    N  
ATOM   1364  CA  TYR A 169      20.184  12.585  32.220  1.00 25.79      A    C  
ANISOU 1364  CA  TYR A 169     3187   3500   3111    140    244    199  A    C  
ATOM   1365  C   TYR A 169      18.673  12.813  32.534  1.00 25.31      A    C  
ANISOU 1365  C   TYR A 169     3000   3641   2974    114    189     39  A    C  
ATOM   1366  O   TYR A 169      17.799  12.092  32.043  1.00 25.35      A    O  
ANISOU 1366  O   TYR A 169     2968   4042   2622    150    546   -296  A    O  
ATOM   1367  CB  TYR A 169      20.930  11.984  33.444  1.00 26.14      A    C  
ANISOU 1367  CB  TYR A 169     3157   3494   3280    163    -49    299  A    C  
ATOM   1368  CG  TYR A 169      20.238  10.736  34.040  1.00 25.76      A    C  
ANISOU 1368  CG  TYR A 169     3093   3573   3121    100    264    275  A    C  
ATOM   1369  CD1 TYR A 169      20.741   9.432  33.769  1.00 26.54      A    C  
ANISOU 1369  CD1 TYR A 169     3586   3391   3104     10    156    458  A    C  
ATOM   1370  CD2 TYR A 169      19.058  10.837  34.787  1.00 27.37      A    C  
ANISOU 1370  CD2 TYR A 169     3162   3971   3265   -340    337     72  A    C  
ATOM   1371  CE1 TYR A 169      20.120   8.295  34.239  1.00 27.08      A    C  
ANISOU 1371  CE1 TYR A 169     3599   3355   3334    -98    434     57  A    C  
ATOM   1372  CE2 TYR A 169      18.443   9.702  35.288  1.00 29.16      A    C  
ANISOU 1372  CE2 TYR A 169     4058   3894   3128   -240    275    309  A    C  
ATOM   1373  CZ  TYR A 169      18.955   8.436  35.013  1.00 26.47      A    C  
ANISOU 1373  CZ  TYR A 169     3612   3814   2631   -143    437    338  A    C  
ATOM   1374  OH  TYR A 169      18.336   7.282  35.502  1.00 27.29      A    O  
ANISOU 1374  OH  TYR A 169     3409   3850   3106    -91    744    244  A    O  
ATOM   1375  N   LEU A 170      18.371  13.834  33.343  1.00 25.62      A    N  
ANISOU 1375  N   LEU A 170     2878   3811   3044    186    139    215  A    N  
ATOM   1376  CA  LEU A 170      16.972  14.007  33.889  1.00 24.68      A    C  
ANISOU 1376  CA  LEU A 170     3091   3544   2741    193    106    145  A    C  
ATOM   1377  C   LEU A 170      16.063  14.552  32.778  1.00 25.87      A    C  
ANISOU 1377  C   LEU A 170     3115   3660   3055     33    -42     72  A    C  
ATOM   1378  O   LEU A 170      14.914  14.141  32.644  1.00 26.93      A    O  
ANISOU 1378  O   LEU A 170     3362   3920   2948     -7   -101   -209  A    O  
ATOM   1379  CB  LEU A 170      17.007  14.962  35.080  1.00 25.05      A    C  
ANISOU 1379  CB  LEU A 170     3120   3464   2934     80    156     60  A    C  
ATOM   1380  CG  LEU A 170      17.737  14.437  36.286  1.00 25.10      A    C  
ANISOU 1380  CG  LEU A 170     3076   3574   2884    -51    193    -52  A    C  
ATOM   1381  CD1 LEU A 170      17.967  15.571  37.291  1.00 30.39      A    C  
ANISOU 1381  CD1 LEU A 170     3925   3909   3714    -15     76   -710  A    C  
ATOM   1382  CD2 LEU A 170      16.870  13.367  36.889  1.00 28.20      A    C  
ANISOU 1382  CD2 LEU A 170     3920   3787   3005   -155     81    177  A    C  
ATOM   1383  N   ARG A 171      16.615  15.428  31.935  1.00 25.67      A    N  
ANISOU 1383  N   ARG A 171     3308   3461   2982    -50    -44    145  A    N  
ATOM   1384  CA  ARG A 171      15.811  15.995  30.799  1.00 25.69      A    C  
ANISOU 1384  CA  ARG A 171     3346   3403   3011   -335    -82    173  A    C  
ATOM   1385  C   ARG A 171      15.468  14.896  29.770  1.00 26.61      A    C  
ANISOU 1385  C   ARG A 171     3342   3476   3290   -263     -2    131  A    C  
ATOM   1386  O   ARG A 171      14.333  14.833  29.292  1.00 27.05      A    O  
ANISOU 1386  O   ARG A 171     3302   3648   3325   -168   -174    238  A    O  
ATOM   1387  CB  ARG A 171      16.580  17.161  30.132  1.00 24.23      A    C  
ANISOU 1387  CB  ARG A 171     3142   3352   2710   -542    301     50  A    C  
ATOM   1388  CG  ARG A 171      16.660  18.379  31.080  1.00 25.19      A    C  
ANISOU 1388  CG  ARG A 171     2917   3044   3609   -356    -70    141  A    C  
ATOM   1389  CD  ARG A 171      17.497  19.477  30.431  1.00 24.20      A    C  
ANISOU 1389  CD  ARG A 171     3201   3238   2753    -77   1160   -326  A    C  
ATOM   1390  NE  ARG A 171      17.577  20.596  31.367  1.00 26.62      A    N  
ANISOU 1390  NE  ARG A 171     4239   2781   3095    338    105   -442  A    N  
ATOM   1391  CZ  ARG A 171      16.741  21.655  31.375  1.00 29.03      A    C  
ANISOU 1391  CZ  ARG A 171     4222   3405   3401    385    157   -572  A    C  
ATOM   1392  NH1 ARG A 171      15.741  21.792  30.461  1.00 24.82      A    N1+
ANISOU 1392  NH1 ARG A 171     3641   2982   2806   -279    490   -209  A    N1+
ATOM   1393  NH2 ARG A 171      16.949  22.609  32.305  1.00 30.59      A    N  
ANISOU 1393  NH2 ARG A 171     4828   3762   3030     40     16   -258  A    N  
ATOM   1394  N   ILE A 172      16.446  14.034  29.465  1.00 25.60      A    N  
ANISOU 1394  N   ILE A 172     3237   3419   3071   -214    342    132  A    N  
ATOM   1395  CA  ILE A 172      16.209  12.844  28.640  1.00 26.03      A    C  
ANISOU 1395  CA  ILE A 172     3436   3378   3076   -290    204    146  A    C  
ATOM   1396  C   ILE A 172      15.211  11.949  29.272  1.00 26.08      A    C  
ANISOU 1396  C   ILE A 172     3494   3376   3039   -228    173    114  A    C  
ATOM   1397  O   ILE A 172      14.299  11.490  28.597  1.00 26.29      A    O  
ANISOU 1397  O   ILE A 172     3442   3494   3051   -222    187    168  A    O  
ATOM   1398  CB  ILE A 172      17.529  12.033  28.350  1.00 26.82      A    C  
ANISOU 1398  CB  ILE A 172     3646   3351   3193   -302    379    -26  A    C  
ATOM   1399  CG1 ILE A 172      18.472  12.854  27.470  1.00 28.56      A    C  
ANISOU 1399  CG1 ILE A 172     4567   3517   2764   -529    178    345  A    C  
ATOM   1400  CG2 ILE A 172      17.246  10.698  27.732  1.00 26.37      A    C  
ANISOU 1400  CG2 ILE A 172     3784   3628   2604   -522    242   -139  A    C  
ATOM   1401  CD1 ILE A 172      17.995  12.821  26.035  1.00 30.09      A    C  
ANISOU 1401  CD1 ILE A 172     4105   4050   3277   -204    290    380  A    C  
ATOM   1402  N   ALA A 173      15.342  11.703  30.587  1.00 26.23      A    N  
ANISOU 1402  N   ALA A 173     3560   3352   3053   -352     67    258  A    N  
ATOM   1403  CA  ALA A 173      14.513  10.695  31.246  1.00 26.36      A    C  
ANISOU 1403  CA  ALA A 173     3417   3376   3222   -145    165    282  A    C  
ATOM   1404  C   ALA A 173      13.015  11.086  31.166  1.00 26.84      A    C  
ANISOU 1404  C   ALA A 173     3471   3410   3315   -190    143    145  A    C  
ATOM   1405  O   ALA A 173      12.175  10.268  30.910  1.00 26.75      A    O  
ANISOU 1405  O   ALA A 173     3498   3268   3395   -188    374     89  A    O  
ATOM   1406  CB  ALA A 173      14.950  10.610  32.693  1.00 24.86      A    C  
ANISOU 1406  CB  ALA A 173     3441   3257   2746   -244     71    338  A    C  
ATOM   1407  N   GLN A 174      12.713  12.379  31.327  1.00 26.84      A    N  
ANISOU 1407  N   GLN A 174     3523   3435   3236    -10    159      9  A    N  
ATOM   1408  CA  GLN A 174      11.329  12.902  31.279  1.00 27.45      A    C  
ANISOU 1408  CA  GLN A 174     3501   3415   3511    -27    180    -37  A    C  
ATOM   1409  C   GLN A 174      10.630  12.596  29.971  1.00 27.77      A    C  
ANISOU 1409  C   GLN A 174     3536   3501   3512    -26    117    -11  A    C  
ATOM   1410  O   GLN A 174       9.397  12.406  29.963  1.00 30.02      A    O  
ANISOU 1410  O   GLN A 174     3708   3769   3928    177   -148    149  A    O  
ATOM   1411  CB  GLN A 174      11.363  14.429  31.395  1.00 27.15      A    C  
ANISOU 1411  CB  GLN A 174     3483   3441   3392   -165    392   -171  A    C  
ATOM   1412  CG  GLN A 174      11.801  14.927  32.762  1.00 28.06      A    C  
ANISOU 1412  CG  GLN A 174     4089   3215   3357   -211    307   -375  A    C  
ATOM   1413  CD  GLN A 174      11.542  16.377  32.871  1.00 27.87      A    C  
ANISOU 1413  CD  GLN A 174     3903   3298   3388    215    351   -301  A    C  
ATOM   1414  NE2 GLN A 174      11.159  16.826  34.068  1.00 30.87      A    N  
ANISOU 1414  NE2 GLN A 174     3897   4024   3807   -127    684   -811  A    N  
ATOM   1415  OE1 GLN A 174      11.635  17.116  31.860  1.00 32.43      A    O  
ANISOU 1415  OE1 GLN A 174     5268   3266   3785    249    537     64  A    O  
ATOM   1416  N   GLN A 175      11.390  12.509  28.860  1.00 29.42      A    N  
ANISOU 1416  N   GLN A 175     3955   3580   3640    -33     -9     65  A    N  
ATOM   1417  CA  GLN A 175      10.752  12.376  27.532  1.00 28.56      A    C  
ANISOU 1417  CA  GLN A 175     4053   3363   3435    154    -48    121  A    C  
ATOM   1418  C   GLN A 175      11.127  11.108  26.780  1.00 28.75      A    C  
ANISOU 1418  C   GLN A 175     4011   3458   3452     77    -66    116  A    C  
ATOM   1419  O   GLN A 175      10.876  10.986  25.602  1.00 27.77      A    O  
ANISOU 1419  O   GLN A 175     4032   3271   3248     87    188   -237  A    O  
ATOM   1420  CB  GLN A 175      11.009  13.642  26.671  1.00 29.14      A    C  
ANISOU 1420  CB  GLN A 175     4082   3451   3537     80    156    108  A    C  
ATOM   1421  CG  GLN A 175      10.292  14.889  27.290  1.00 30.02      A    C  
ANISOU 1421  CG  GLN A 175     4294   3209   3900    297     79    279  A    C  
ATOM   1422  CD  GLN A 175      10.325  16.110  26.409  1.00 29.75      A    C  
ANISOU 1422  CD  GLN A 175     4302   3345   3657    294     -5     66  A    C  
ATOM   1423  NE2 GLN A 175       9.633  16.029  25.255  1.00 28.38      A    N  
ANISOU 1423  NE2 GLN A 175     4330   3126   3326    728   -159   -544  A    N  
ATOM   1424  OE1 GLN A 175      11.005  17.134  26.752  1.00 32.62      A    O  
ANISOU 1424  OE1 GLN A 175     4745   3746   3901     95     79    -51  A    O  
ATOM   1425  N   LEU A 176      11.702  10.151  27.509  1.00 28.47      A    N  
ANISOU 1425  N   LEU A 176     3755   3519   3540     81   -157     -1  A    N  
ATOM   1426  CA  LEU A 176      12.138   8.884  26.948  1.00 28.93      A    C  
ANISOU 1426  CA  LEU A 176     3749   3688   3555     59   -126    301  A    C  
ATOM   1427  C   LEU A 176      10.874   8.075  26.544  1.00 26.92      A    C  
ANISOU 1427  C   LEU A 176     3649   3410   3167     20   -117     64  A    C  
ATOM   1428  O   LEU A 176       9.987   7.852  27.402  1.00 28.49      A    O  
ANISOU 1428  O   LEU A 176     3633   3651   3538    -22    -71   -349  A    O  
ATOM   1429  CB  LEU A 176      12.917   8.193  28.086  1.00 30.07      A    C  
ANISOU 1429  CB  LEU A 176     3876   3972   3576    131   -115    541  A    C  
ATOM   1430  CG  LEU A 176      13.842   7.084  27.729  1.00 33.30      A    C  
ANISOU 1430  CG  LEU A 176     4298   4312   4042    177   -113   1222  A    C  
ATOM   1431  CD1 LEU A 176      14.974   7.462  26.751  1.00 34.77      A    C  
ANISOU 1431  CD1 LEU A 176     4700   4270   4240   -120     91   2007  A    C  
ATOM   1432  CD2 LEU A 176      14.389   6.628  29.083  1.00 31.93      A    C  
ANISOU 1432  CD2 LEU A 176     3710   5189   3231    491    -61   1785  A    C  
ATOM   1433  N   PRO A 177      10.751   7.653  25.259  1.00 27.22      A    N  
ANISOU 1433  N   PRO A 177     3570   3482   3288    110    214    -73  A    N  
ATOM   1434  CA  PRO A 177       9.564   6.903  24.896  0.50 25.43      A    C  
ANISOU 1434  CA  PRO A 177     3134   3430   3098     44    112    -41  A    C  
ATOM   1435  C   PRO A 177       9.740   5.424  25.272  1.00 27.03      A    C  
ANISOU 1435  C   PRO A 177     3237   3736   3297    -12    171    -61  A    C  
ATOM   1436  O   PRO A 177       9.844   4.546  24.390  1.00 27.96      A    O  
ANISOU 1436  O   PRO A 177     3269   3527   3828   -385   -118    180  A    O  
ATOM   1437  CB  PRO A 177       9.454   7.151  23.388  1.00 25.60      A    C  
ANISOU 1437  CB  PRO A 177     2886   3573   3265    439    351   -210  A    C  
ATOM   1438  CG  PRO A 177      10.895   7.281  22.909  1.00 25.94      A    C  
ANISOU 1438  CG  PRO A 177     3193   3743   2920    -99    277   -234  A    C  
ATOM   1439  CD  PRO A 177      11.616   7.983  24.090  1.00 26.50      A    C  
ANISOU 1439  CD  PRO A 177     3550   3556   2963     65     78   -129  A    C  
ATOM   1440  N   ILE A 178       9.796   5.141  26.598  1.00 27.87      A    N  
ANISOU 1440  N   ILE A 178     3560   3532   3497   -283    -22    129  A    N  
ATOM   1441  CA  ILE A 178      10.189   3.787  27.066  1.00 27.63      A    C  
ANISOU 1441  CA  ILE A 178     3435   3552   3508   -200    173    -58  A    C  
ATOM   1442  C   ILE A 178       9.208   2.696  26.526  1.00 29.26      A    C  
ANISOU 1442  C   ILE A 178     3599   3703   3815   -169    255   -143  A    C  
ATOM   1443  O   ILE A 178       9.607   1.759  25.828  1.00 29.56      A    O  
ANISOU 1443  O   ILE A 178     3488   3689   4053     80    461   -210  A    O  
ATOM   1444  CB  ILE A 178      10.227   3.752  28.575  1.00 26.49      A    C  
ANISOU 1444  CB  ILE A 178     3357   3364   3342   -277    158   -129  A    C  
ATOM   1445  CG1 ILE A 178      11.364   4.591  29.078  1.00 24.93      A    C  
ANISOU 1445  CG1 ILE A 178     3276   3445   2750   -404    179   -528  A    C  
ATOM   1446  CG2 ILE A 178      10.362   2.259  29.147  1.00 26.88      A    C  
ANISOU 1446  CG2 ILE A 178     3282   3596   3335     93    479    192  A    C  
ATOM   1447  CD1 ILE A 178      11.399   4.747  30.641  1.00 27.70      A    C  
ANISOU 1447  CD1 ILE A 178     3732   4540   2252   -122     35   -619  A    C  
ATOM   1448  N   TYR A 179       7.913   2.847  26.802  1.00 30.13      A    N  
ANISOU 1448  N   TYR A 179     3612   3843   3992   -263    237    -42  A    N  
ATOM   1449  CA  TYR A 179       6.980   1.826  26.435  1.00 29.49      A    C  
ANISOU 1449  CA  TYR A 179     3475   4045   3683   -145    253      9  A    C  
ATOM   1450  C   TYR A 179       6.674   1.883  24.914  1.00 29.21      A    C  
ANISOU 1450  C   TYR A 179     3419   3975   3702    -92    304     18  A    C  
ATOM   1451  O   TYR A 179       6.417   0.831  24.313  1.00 27.21      A    O  
ANISOU 1451  O   TYR A 179     3120   3760   3459    -71    346      0  A    O  
ATOM   1452  CB  TYR A 179       5.712   2.068  27.233  1.00 29.14      A    C  
ANISOU 1452  CB  TYR A 179     3504   4061   3505    -68    444    331  A    C  
ATOM   1453  CG  TYR A 179       5.897   1.810  28.732  1.00 31.01      A    C  
ANISOU 1453  CG  TYR A 179     3736   4432   3611    131    371     40  A    C  
ATOM   1454  CD1 TYR A 179       6.336   0.556  29.176  1.00 31.71      A    C  
ANISOU 1454  CD1 TYR A 179     4038   4328   3679     40    365    352  A    C  
ATOM   1455  CD2 TYR A 179       5.601   2.799  29.698  1.00 31.69      A    C  
ANISOU 1455  CD2 TYR A 179     4630   4255   3156     95    550    277  A    C  
ATOM   1456  CE1 TYR A 179       6.515   0.284  30.548  1.00 35.35      A    C  
ANISOU 1456  CE1 TYR A 179     4542   5134   3755    570    687     73  A    C  
ATOM   1457  CE2 TYR A 179       5.797   2.530  31.067  1.00 33.76      A    C  
ANISOU 1457  CE2 TYR A 179     4958   4610   3259    596    990    -66  A    C  
ATOM   1458  CZ  TYR A 179       6.230   1.281  31.470  1.00 34.56      A    C  
ANISOU 1458  CZ  TYR A 179     4290   5194   3645    597    552    145  A    C  
ATOM   1459  OH  TYR A 179       6.383   1.013  32.800  1.00 35.71      A    O  
ANISOU 1459  OH  TYR A 179     4010   5511   4046    367    333    644  A    O  
ATOM   1460  N   GLU A 180       6.688   3.090  24.318  1.00 27.95      A    N  
ANISOU 1460  N   GLU A 180     3208   3695   3713    -50    202    -73  A    N  
ATOM   1461  CA  GLU A 180       6.397   3.271  22.884  1.00 28.32      A    C  
ANISOU 1461  CA  GLU A 180     3367   3593   3799    174    419    -41  A    C  
ATOM   1462  C   GLU A 180       7.405   2.413  22.078  1.00 28.38      A    C  
ANISOU 1462  C   GLU A 180     3329   3486   3965    106    274    -87  A    C  
ATOM   1463  O   GLU A 180       7.029   1.580  21.220  1.00 29.94      A    O  
ANISOU 1463  O   GLU A 180     3485   3861   4029     62    293    -97  A    O  
ATOM   1464  CB  GLU A 180       6.543   4.750  22.474  1.00 26.94      A    C  
ANISOU 1464  CB  GLU A 180     3283   3353   3598     80    372    -53  A    C  
ATOM   1465  CG  GLU A 180       5.433   5.697  22.961  1.00 31.80      A    C  
ANISOU 1465  CG  GLU A 180     4161   3725   4195    553    168   -105  A    C  
ATOM   1466  CD  GLU A 180       5.583   6.132  24.442  1.00 35.47      A    C  
ANISOU 1466  CD  GLU A 180     4293   4332   4849    650    208   -442  A    C  
ATOM   1467  OE1 GLU A 180       6.570   5.716  25.132  1.00 34.78      A    O  
ANISOU 1467  OE1 GLU A 180     3308   4441   5465   -252    285    -66  A    O  
ATOM   1468  OE2 GLU A 180       4.704   6.908  24.938  1.00 35.58      A    O1-
ANISOU 1468  OE2 GLU A 180     4628   4110   4780    741    390   -807  A    O1-
ATOM   1469  N   VAL A 181       8.675   2.547  22.406  1.00 27.67      A    N  
ANISOU 1469  N   VAL A 181     3158   3232   4123    -14    320     38  A    N  
ATOM   1470  CA  VAL A 181       9.690   1.781  21.646  1.00 26.09      A    C  
ANISOU 1470  CA  VAL A 181     3068   3101   3741    -41    154     -7  A    C  
ATOM   1471  C   VAL A 181       9.667   0.304  22.110  1.00 28.18      A    C  
ANISOU 1471  C   VAL A 181     3199   3488   4019   -207    106   -144  A    C  
ATOM   1472  O   VAL A 181       9.706  -0.609  21.289  1.00 28.11      A    O  
ANISOU 1472  O   VAL A 181     3115   3253   4310   -402    -41   -344  A    O  
ATOM   1473  CB  VAL A 181      11.043   2.398  21.866  1.00 25.19      A    C  
ANISOU 1473  CB  VAL A 181     2889   2944   3737    -68    363     63  A    C  
ATOM   1474  CG1 VAL A 181      12.145   1.533  21.279  1.00 26.11      A    C  
ANISOU 1474  CG1 VAL A 181     3157   3010   3751    292    442   -226  A    C  
ATOM   1475  CG2 VAL A 181      11.087   3.820  21.208  1.00 25.87      A    C  
ANISOU 1475  CG2 VAL A 181     3376   3069   3383     95   -183     59  A    C  
ATOM   1476  N   SER A 182       9.613   0.068  23.423  1.00 28.88      A    N  
ANISOU 1476  N   SER A 182     3377   3646   3949   -242      2     33  A    N  
ATOM   1477  CA  SER A 182       9.715  -1.301  23.908  1.00 28.88      A    C  
ANISOU 1477  CA  SER A 182     3283   3662   4025   -240     29    -41  A    C  
ATOM   1478  C   SER A 182       8.610  -2.192  23.330  1.00 29.14      A    C  
ANISOU 1478  C   SER A 182     3455   3720   3894   -230     80   -103  A    C  
ATOM   1479  O   SER A 182       8.840  -3.382  23.077  1.00 29.96      A    O  
ANISOU 1479  O   SER A 182     3548   3852   3983   -300    263   -119  A    O  
ATOM   1480  CB  SER A 182       9.682  -1.366  25.445  1.00 28.70      A    C  
ANISOU 1480  CB  SER A 182     3223   3766   3914   -220    183    -96  A    C  
ATOM   1481  OG  SER A 182      10.738  -0.631  26.095  1.00 29.46      A    O  
ANISOU 1481  OG  SER A 182     3474   3882   3836   -422    374    173  A    O  
ATOM   1482  N   ALA A 183       7.412  -1.623  23.191  1.00 29.14      A    N  
ANISOU 1482  N   ALA A 183     3522   3692   3856   -278   -110     62  A    N  
ATOM   1483  CA  ALA A 183       6.242  -2.389  22.733  1.00 28.93      A    C  
ANISOU 1483  CA  ALA A 183     3295   3710   3985   -156     40     22  A    C  
ATOM   1484  C   ALA A 183       6.370  -2.929  21.339  1.00 29.44      A    C  
ANISOU 1484  C   ALA A 183     3477   3480   4229   -219    -58      3  A    C  
ATOM   1485  O   ALA A 183       5.573  -3.766  20.951  1.00 31.00      A    O  
ANISOU 1485  O   ALA A 183     3398   3664   4713   -202     69     42  A    O  
ATOM   1486  CB  ALA A 183       4.940  -1.537  22.865  1.00 30.16      A    C  
ANISOU 1486  CB  ALA A 183     3769   3477   4214     95   -180     -4  A    C  
ATOM   1487  N   GLN A 184       7.371  -2.485  20.570  1.00 28.31      A    N  
ANISOU 1487  N   GLN A 184     3393   3452   3908   -291    122    -39  A    N  
ATOM   1488  CA  GLN A 184       7.478  -3.008  19.213  1.00 29.61      A    C  
ANISOU 1488  CA  GLN A 184     3628   3463   4156   -388     18   -108  A    C  
ATOM   1489  C   GLN A 184       8.117  -4.420  19.239  1.00 30.15      A    C  
ANISOU 1489  C   GLN A 184     3658   3546   4249   -158    -19   -207  A    C  
ATOM   1490  O   GLN A 184       8.144  -5.096  18.191  1.00 30.50      A    O  
ANISOU 1490  O   GLN A 184     3633   3805   4150   -332    192   -276  A    O  
ATOM   1491  CB  GLN A 184       8.294  -2.124  18.319  1.00 28.93      A    C  
ANISOU 1491  CB  GLN A 184     3542   3628   3820   -322    -83    105  A    C  
ATOM   1492  CG  GLN A 184       7.845  -0.642  18.379  1.00 29.04      A    C  
ANISOU 1492  CG  GLN A 184     3496   3411   4125   -478    283   -187  A    C  
ATOM   1493  CD  GLN A 184       6.333  -0.497  18.256  1.00 30.83      A    C  
ANISOU 1493  CD  GLN A 184     3952   3893   3866   -386   -369   -476  A    C  
ATOM   1494  NE2 GLN A 184       5.770   0.217  19.167  1.00 30.17      A    N  
ANISOU 1494  NE2 GLN A 184     3963   3987   3512   -679     17    -14  A    N  
ATOM   1495  OE1 GLN A 184       5.679  -1.050  17.339  1.00 31.20      A    O  
ANISOU 1495  OE1 GLN A 184     4439   3582   3830   -379   -668   -274  A    O  
ATOM   1496  N   PHE A 185       8.631  -4.852  20.389  1.00 29.04      A    N  
ANISOU 1496  N   PHE A 185     3438   3323   4270   -193    -18    -19  A    N  
ATOM   1497  CA  PHE A 185       9.171  -6.207  20.501  1.00 31.25      A    C  
ANISOU 1497  CA  PHE A 185     3646   3478   4747   -167   -154     42  A    C  
ATOM   1498  C   PHE A 185       8.010  -7.183  20.839  1.00 31.37      A    C  
ANISOU 1498  C   PHE A 185     3728   3415   4775    -43    -67    227  A    C  
ATOM   1499  O   PHE A 185       7.396  -7.080  21.898  1.00 32.30      A    O  
ANISOU 1499  O   PHE A 185     3676   3364   5231    -28    150     92  A    O  
ATOM   1500  CB  PHE A 185      10.295  -6.279  21.535  1.00 31.98      A    C  
ANISOU 1500  CB  PHE A 185     3799   3607   4744    131   -160    244  A    C  
ATOM   1501  CG  PHE A 185      10.923  -7.635  21.615  1.00 34.19      A    C  
ANISOU 1501  CG  PHE A 185     4007   3635   5349    -27   -172   -139  A    C  
ATOM   1502  CD1 PHE A 185      11.851  -8.018  20.678  1.00 32.16      A    C  
ANISOU 1502  CD1 PHE A 185     3770   3814   4632    154   -381   -406  A    C  
ATOM   1503  CD2 PHE A 185      10.588  -8.532  22.651  1.00 34.52      A    C  
ANISOU 1503  CD2 PHE A 185     4091   3622   5403    234   -529    111  A    C  
ATOM   1504  CE1 PHE A 185      12.407  -9.317  20.720  1.00 35.67      A    C  
ANISOU 1504  CE1 PHE A 185     4202   3624   5724    -27   -472    197  A    C  
ATOM   1505  CE2 PHE A 185      11.162  -9.835  22.707  1.00 35.85      A    C  
ANISOU 1505  CE2 PHE A 185     4194   3657   5770    349   -277   -231  A    C  
ATOM   1506  CZ  PHE A 185      12.082 -10.193  21.758  1.00 35.03      A    C  
ANISOU 1506  CZ  PHE A 185     4319   3477   5515     22   -186   -188  A    C  
ATOM   1507  N   THR A 186       7.685  -8.066  19.902  1.00 33.05      A    N  
ANISOU 1507  N   THR A 186     3761   3613   5181   -139   -142    165  A    N  
ATOM   1508  CA  THR A 186       6.460  -8.908  20.033  1.00 33.50      A    C  
ANISOU 1508  CA  THR A 186     3805   3753   5169   -374     -6    220  A    C  
ATOM   1509  C   THR A 186       6.812 -10.361  20.288  1.00 35.49      A    C  
ANISOU 1509  C   THR A 186     4028   3876   5581   -183      6    169  A    C  
ATOM   1510  O   THR A 186       5.889 -11.212  20.408  1.00 35.70      A    O  
ANISOU 1510  O   THR A 186     4187   3683   5694   -241    -20    214  A    O  
ATOM   1511  CB  THR A 186       5.563  -8.873  18.787  1.00 34.01      A    C  
ANISOU 1511  CB  THR A 186     3813   4039   5068   -181     67    174  A    C  
ATOM   1512  CG2 THR A 186       5.067  -7.450  18.587  1.00 32.98      A    C  
ANISOU 1512  CG2 THR A 186     3701   3604   5224   -454   -532   -143  A    C  
ATOM   1513  OG1 THR A 186       6.363  -9.223  17.638  1.00 33.62      A    O  
ANISOU 1513  OG1 THR A 186     3792   4142   4838   -862    502   -225  A    O  
ATOM   1514  N   LYS A 187       8.113 -10.646  20.374  1.00 36.69      A    N  
ANISOU 1514  N   LYS A 187     4224   4027   5686   -140    -20    183  A    N  
ATOM   1515  CA  LYS A 187       8.599 -11.989  20.733  1.00 37.42      A    C  
ANISOU 1515  CA  LYS A 187     4239   4200   5776      7     -6    -18  A    C  
ATOM   1516  C   LYS A 187       8.577 -12.166  22.277  1.00 36.84      A    C  
ANISOU 1516  C   LYS A 187     4224   4135   5638     -8     14    -77  A    C  
ATOM   1517  O   LYS A 187       8.175 -11.237  23.016  1.00 37.71      A    O  
ANISOU 1517  O   LYS A 187     4044   4203   6079    241     89   -147  A    O  
ATOM   1518  CB  LYS A 187       9.960 -12.283  20.059  1.00 36.05      A    C  
ANISOU 1518  CB  LYS A 187     4258   4001   5438      0    119    -57  A    C  
ATOM   1519  CG  LYS A 187       9.861 -12.535  18.554  1.00 40.09      A    C  
ANISOU 1519  CG  LYS A 187     4535   4739   5955    184    238   -174  A    C  
ATOM   1520  CD  LYS A 187      11.279 -12.668  18.028  1.00 43.62      A    C  
ANISOU 1520  CD  LYS A 187     5102   5532   5937     91    472    146  A    C  
ATOM   1521  CE  LYS A 187      11.476 -11.977  16.703  1.00 44.00      A    C  
ANISOU 1521  CE  LYS A 187     5767   5388   5562     86     94     43  A    C  
ATOM   1522  NZ  LYS A 187      12.923 -11.543  16.534  1.00 40.59      A    N1+
ANISOU 1522  NZ  LYS A 187     5856   4904   4660    448   -192   -246  A    N1+
ATOM   1523  N   PRO A 188       8.990 -13.346  22.792  1.00 36.40      A    N  
ANISOU 1523  N   PRO A 188     4197   4080   5553     25     19    -80  A    N  
ATOM   1524  CA  PRO A 188       8.783 -13.586  24.225  1.00 36.10      A    C  
ANISOU 1524  CA  PRO A 188     4312   4017   5387     -5    -63    -10  A    C  
ATOM   1525  C   PRO A 188       9.606 -12.769  25.226  1.00 35.59      A    C  
ANISOU 1525  C   PRO A 188     4230   3973   5318    -10    -76    182  A    C  
ATOM   1526  O   PRO A 188      10.823 -12.586  25.075  1.00 35.61      A    O  
ANISOU 1526  O   PRO A 188     4335   3807   5388   -218   -333    159  A    O  
ATOM   1527  CB  PRO A 188       9.038 -15.091  24.380  1.00 36.96      A    C  
ANISOU 1527  CB  PRO A 188     4512   4157   5374    104      0      3  A    C  
ATOM   1528  CG  PRO A 188       8.777 -15.664  22.985  1.00 37.97      A    C  
ANISOU 1528  CG  PRO A 188     4743   4324   5358     35     73    -74  A    C  
ATOM   1529  CD  PRO A 188       9.293 -14.601  22.067  1.00 37.13      A    C  
ANISOU 1529  CD  PRO A 188     4425   4091   5590     14     66    -96  A    C  
ATOM   1530  N   VAL A 189       8.901 -12.209  26.191  1.00 34.51      A    N  
ANISOU 1530  N   VAL A 189     4167   3854   5088   -237    -66    292  A    N  
ATOM   1531  CA  VAL A 189       9.492 -11.442  27.258  1.00 33.97      A    C  
ANISOU 1531  CA  VAL A 189     3983   3852   5071    -98     58    272  A    C  
ATOM   1532  C   VAL A 189       9.183 -12.090  28.599  1.00 34.45      A    C  
ANISOU 1532  C   VAL A 189     3957   3924   5205   -111     15    395  A    C  
ATOM   1533  O   VAL A 189       8.020 -12.509  28.869  1.00 35.08      A    O  
ANISOU 1533  O   VAL A 189     3880   3916   5532   -307   -138    256  A    O  
ATOM   1534  CB  VAL A 189       8.964  -9.983  27.261  1.00 33.40      A    C  
ANISOU 1534  CB  VAL A 189     4063   3714   4911   -147     78    340  A    C  
ATOM   1535  CG1 VAL A 189       9.675  -9.206  28.401  1.00 32.66      A    C  
ANISOU 1535  CG1 VAL A 189     4058   3374   4976   -217    297    323  A    C  
ATOM   1536  CG2 VAL A 189       9.176  -9.334  25.899  1.00 32.07      A    C  
ANISOU 1536  CG2 VAL A 189     3414   3600   5168   -167    -13    323  A    C  
ATOM   1537  N   CYS A 190      10.200 -12.116  29.456  1.00 33.61      A    N  
ANISOU 1537  N   CYS A 190     3657   4048   5064    -44     76    335  A    N  
ATOM   1538  CA  CYS A 190      10.079 -12.571  30.850  1.00 35.31      A    C  
ANISOU 1538  CA  CYS A 190     3956   4189   5267    -54    100    447  A    C  
ATOM   1539  C   CYS A 190      10.333 -11.388  31.754  1.00 34.58      A    C  
ANISOU 1539  C   CYS A 190     3817   4183   5136     36     96    447  A    C  
ATOM   1540  O   CYS A 190      11.349 -10.739  31.642  1.00 34.17      A    O  
ANISOU 1540  O   CYS A 190     3561   4063   5356     95    294    327  A    O  
ATOM   1541  CB  CYS A 190      11.099 -13.670  31.140  1.00 34.67      A    C  
ANISOU 1541  CB  CYS A 190     3950   4110   5112    -19     93    341  A    C  
ATOM   1542  SG  CYS A 190      11.001 -14.395  32.778  1.00 39.03      A    S  
ANISOU 1542  SG  CYS A 190     4402   4596   5830     23    622   1029  A    S  
ATOM   1543  N   LEU A 191       9.362 -11.081  32.592  1.00 34.67      A    N  
ANISOU 1543  N   LEU A 191     3662   4343   5167   -133    238    550  A    N  
ATOM   1544  CA  LEU A 191       9.395  -9.956  33.529  1.00 35.13      A    C  
ANISOU 1544  CA  LEU A 191     3691   4452   5205   -178    287    587  A    C  
ATOM   1545  C   LEU A 191       9.448 -10.517  34.946  1.00 35.78      A    C  
ANISOU 1545  C   LEU A 191     3785   4626   5184   -232    382    621  A    C  
ATOM   1546  O   LEU A 191       8.602 -11.351  35.297  1.00 38.27      A    O  
ANISOU 1546  O   LEU A 191     4033   4882   5624   -315    358    755  A    O  
ATOM   1547  CB  LEU A 191       8.119  -9.141  33.376  1.00 34.92      A    C  
ANISOU 1547  CB  LEU A 191     3505   4386   5378   -252    499    558  A    C  
ATOM   1548  CG  LEU A 191       7.830  -8.587  31.987  1.00 35.56      A    C  
ANISOU 1548  CG  LEU A 191     3464   4430   5614   -605    695    726  A    C  
ATOM   1549  CD1 LEU A 191       6.397  -8.088  31.794  1.00 37.67      A    C  
ANISOU 1549  CD1 LEU A 191     3475   4853   5981   -460    764    452  A    C  
ATOM   1550  CD2 LEU A 191       8.877  -7.504  31.506  1.00 36.36      A    C  
ANISOU 1550  CD2 LEU A 191     3287   3879   6648  -1195    637    305  A    C  
ATOM   1551  N   ILE A 192      10.405 -10.049  35.755  1.00 33.53      A    N  
ANISOU 1551  N   ILE A 192     3581   4514   4643   -130    364    686  A    N  
ATOM   1552  CA  ILE A 192      10.675 -10.602  37.090  1.00 32.50      A    C  
ANISOU 1552  CA  ILE A 192     3567   4507   4274   -235    668    640  A    C  
ATOM   1553  C   ILE A 192      10.773  -9.362  37.977  1.00 33.39      A    C  
ANISOU 1553  C   ILE A 192     3716   4491   4479   -417    615    708  A    C  
ATOM   1554  O   ILE A 192      11.558  -8.470  37.698  1.00 34.60      A    O  
ANISOU 1554  O   ILE A 192     3938   4799   4407   -619    987    926  A    O  
ATOM   1555  CB  ILE A 192      12.008 -11.387  37.140  1.00 30.19      A    C  
ANISOU 1555  CB  ILE A 192     3210   4437   3823   -293    787    736  A    C  
ATOM   1556  CG1 ILE A 192      11.918 -12.665  36.320  1.00 30.41      A    C  
ANISOU 1556  CG1 ILE A 192     2852   4422   4278   -482   1056    680  A    C  
ATOM   1557  CG2 ILE A 192      12.339 -11.816  38.579  1.00 30.78      A    C  
ANISOU 1557  CG2 ILE A 192     3555   4611   3527      2    624    414  A    C  
ATOM   1558  CD1 ILE A 192      13.314 -13.272  35.730  1.00 30.15      A    C  
ANISOU 1558  CD1 ILE A 192     2297   4456   4702   -380    375    522  A    C  
ATOM   1559  N   HIS A 193       9.991  -9.271  39.033  1.00 32.05      A    N  
ANISOU 1559  N   HIS A 193     3543   4214   4419   -491    863    841  A    N  
ATOM   1560  CA  HIS A 193      10.007  -8.070  39.850  1.00 34.32      A    C  
ANISOU 1560  CA  HIS A 193     3831   4529   4680   -336    690    762  A    C  
ATOM   1561  C   HIS A 193       9.692  -8.460  41.271  1.00 35.08      A    C  
ANISOU 1561  C   HIS A 193     3987   4486   4853   -270    646    834  A    C  
ATOM   1562  O   HIS A 193       8.747  -9.225  41.464  1.00 38.55      A    O  
ANISOU 1562  O   HIS A 193     4202   4901   5543   -189    392    715  A    O  
ATOM   1563  CB  HIS A 193       8.919  -7.115  39.382  1.00 32.98      A    C  
ANISOU 1563  CB  HIS A 193     3777   4258   4495   -368    836    920  A    C  
ATOM   1564  CG  HIS A 193       9.276  -5.663  39.532  1.00 33.96      A    C  
ANISOU 1564  CG  HIS A 193     3515   4570   4816   -355   1008    624  A    C  
ATOM   1565  CD2 HIS A 193       9.315  -4.674  38.616  1.00 31.23      A    C  
ANISOU 1565  CD2 HIS A 193     3124   4624   4116   -101   1694    738  A    C  
ATOM   1566  ND1 HIS A 193       9.586  -5.074  40.742  1.00 35.60      A    N  
ANISOU 1566  ND1 HIS A 193     3623   5015   4888   -315   1002    722  A    N  
ATOM   1567  CE1 HIS A 193       9.805  -3.780  40.568  1.00 32.74      A    C  
ANISOU 1567  CE1 HIS A 193     3122   4827   4489   -364   1129   1027  A    C  
ATOM   1568  NE2 HIS A 193       9.685  -3.518  39.275  1.00 33.23      A    N  
ANISOU 1568  NE2 HIS A 193     3217   5017   4392   -101   1200    323  A    N  
ATOM   1569  N   GLY A 194      10.477  -7.977  42.237  1.00 35.82      A    N  
ANISOU 1569  N   GLY A 194     4227   4610   4771   -189    610    722  A    N  
ATOM   1570  CA  GLY A 194      10.264  -8.268  43.684  1.00 36.38      A    C  
ANISOU 1570  CA  GLY A 194     4286   4706   4831   -319    615    734  A    C  
ATOM   1571  C   GLY A 194       9.100  -7.435  44.169  1.00 36.66      A    C  
ANISOU 1571  C   GLY A 194     4332   4877   4720   -373    734    727  A    C  
ATOM   1572  O   GLY A 194       9.050  -6.265  43.853  1.00 35.84      A    O  
ANISOU 1572  O   GLY A 194     4008   4825   4782   -221    732    777  A    O  
ATOM   1573  N   THR A 195       8.143  -8.035  44.899  1.00 38.11      A    N  
ANISOU 1573  N   THR A 195     4589   5111   4779   -547    640    865  A    N  
ATOM   1574  CA  THR A 195       7.004  -7.270  45.487  1.00 39.13      A    C  
ANISOU 1574  CA  THR A 195     4800   5165   4903   -608    874    933  A    C  
ATOM   1575  C   THR A 195       7.438  -6.231  46.521  1.00 39.23      A    C  
ANISOU 1575  C   THR A 195     4864   5306   4736   -449    835    986  A    C  
ATOM   1576  O   THR A 195       6.713  -5.269  46.768  1.00 40.81      A    O  
ANISOU 1576  O   THR A 195     5185   5439   4880   -448   1058   1102  A    O  
ATOM   1577  CB  THR A 195       5.923  -8.161  46.213  1.00 39.76      A    C  
ANISOU 1577  CB  THR A 195     4816   5371   4919   -649    969    842  A    C  
ATOM   1578  CG2 THR A 195       5.430  -9.280  45.349  1.00 39.53      A    C  
ANISOU 1578  CG2 THR A 195     4701   5175   5140   -889   1067    882  A    C  
ATOM   1579  OG1 THR A 195       6.482  -8.703  47.406  1.00 43.07      A    O  
ANISOU 1579  OG1 THR A 195     5124   5723   5515   -654    781   1076  A    O  
ATOM   1580  N   ASP A 196       8.576  -6.427  47.160  1.00 38.30      A    N  
ANISOU 1580  N   ASP A 196     4622   5396   4534   -475    765   1037  A    N  
ATOM   1581  CA AASP A 196       9.072  -5.461  48.138  0.50 38.94      A    C  
ANISOU 1581  CA AASP A 196     4748   5436   4610   -275    673    997  A    C  
ATOM   1582  CA BASP A 196       9.058  -5.446  48.131  0.50 39.89      A    C  
ANISOU 1582  CA BASP A 196     4846   5523   4785   -270    552    937  A    C  
ATOM   1583  C   ASP A 196      10.165  -4.551  47.537  1.00 39.10      A    C  
ANISOU 1583  C   ASP A 196     4771   5430   4655   -284    497    950  A    C  
ATOM   1584  O   ASP A 196      11.057  -4.061  48.243  1.00 41.07      A    O  
ANISOU 1584  O   ASP A 196     4987   5608   5009    -22    179   1053  A    O  
ATOM   1585  CB AASP A 196       9.574  -6.179  49.414  0.50 37.97      A    C  
ANISOU 1585  CB AASP A 196     4573   5467   4385   -313    839   1056  A    C  
ATOM   1586  CB BASP A 196       9.515  -6.155  49.420  0.50 40.16      A    C  
ANISOU 1586  CB BASP A 196     4804   5668   4785   -251    546    974  A    C  
ATOM   1587  CG AASP A 196       8.448  -6.734  50.257  0.50 37.83      A    C  
ANISOU 1587  CG AASP A 196     4627   5444   4302   -251   1066   1233  A    C  
ATOM   1588  CG BASP A 196       9.517  -5.238  50.626  0.50 43.25      A    C  
ANISOU 1588  CG BASP A 196     5240   5981   5210   -185    355    853  A    C  
ATOM   1589  OD1AASP A 196       7.293  -6.325  50.035  0.50 36.62      A    O  
ANISOU 1589  OD1AASP A 196     4149   5826   3937   -833   1632   1621  A    O  
ATOM   1590  OD1BASP A 196       9.802  -4.028  50.499  0.50 48.09      A    O  
ANISOU 1590  OD1BASP A 196     5813   6416   6044   -354     70   1101  A    O  
ATOM   1591  OD2AASP A 196       8.723  -7.561  51.164  0.50 34.54      A    O1-
ANISOU 1591  OD2AASP A 196     4300   5221   3602   -358   2513   1356  A    O1-
ATOM   1592  OD2BASP A 196       9.241  -5.744  51.729  0.50 45.21      A    O1-
ANISOU 1592  OD2BASP A 196     4950   6734   5491   -145    905    755  A    O1-
ATOM   1593  N   ASP A 197      10.105  -4.300  46.232  1.00 38.38      A    N  
ANISOU 1593  N   ASP A 197     4628   5360   4592   -231    488    890  A    N  
ATOM   1594  CA  ASP A 197      11.052  -3.361  45.605  1.00 36.40      A    C  
ANISOU 1594  CA  ASP A 197     4559   5201   4071   -100    710    963  A    C  
ATOM   1595  C   ASP A 197      10.649  -1.930  45.993  1.00 36.59      A    C  
ANISOU 1595  C   ASP A 197     4571   5245   4087   -240    810   1110  A    C  
ATOM   1596  O   ASP A 197       9.573  -1.500  45.595  1.00 37.45      A    O  
ANISOU 1596  O   ASP A 197     4695   5514   4020   -122   1036   1285  A    O  
ATOM   1597  CB  ASP A 197      11.105  -3.608  44.072  1.00 36.35      A    C  
ANISOU 1597  CB  ASP A 197     4610   5089   4110   -167    615    991  A    C  
ATOM   1598  CG  ASP A 197      12.233  -2.902  43.427  1.00 34.64      A    C  
ANISOU 1598  CG  ASP A 197     4265   5077   3816    213    721    671  A    C  
ATOM   1599  OD1 ASP A 197      12.728  -1.884  43.984  1.00 35.37      A    O  
ANISOU 1599  OD1 ASP A 197     3974   5926   3538   -327    664    753  A    O  
ATOM   1600  OD2 ASP A 197      12.625  -3.332  42.334  1.00 33.92      A    O1-
ANISOU 1600  OD2 ASP A 197     4382   4881   3622    148    945    758  A    O1-
ATOM   1601  N   THR A 198      11.449  -1.211  46.796  1.00 36.37      A    N  
ANISOU 1601  N   THR A 198     4507   5298   4012   -209    888   1031  A    N  
ATOM   1602  CA  THR A 198      11.151   0.194  47.128  0.60 37.01      A    C  
ANISOU 1602  CA  THR A 198     4566   5245   4251   -241    881    843  A    C  
ATOM   1603  C   THR A 198      11.844   1.191  46.246  1.00 36.44      A    C  
ANISOU 1603  C   THR A 198     4450   5160   4236   -209    768    645  A    C  
ATOM   1604  O   THR A 198      11.692   2.412  46.453  1.00 36.00      A    O  
ANISOU 1604  O   THR A 198     4436   5282   3960   -220   1152    553  A    O  
ATOM   1605  CB  THR A 198      11.540   0.569  48.553  1.00 37.96      A    C  
ANISOU 1605  CB  THR A 198     4586   5341   4495   -328    825    819  A    C  
ATOM   1606  CG2 THR A 198      10.853  -0.390  49.578  1.00 40.48      A    C  
ANISOU 1606  CG2 THR A 198     5105   5544   4730   -289   1126    972  A    C  
ATOM   1607  OG1 THR A 198      12.957   0.512  48.705  1.00 40.24      A    O  
ANISOU 1607  OG1 THR A 198     5185   5401   4704      0    479    936  A    O  
ATOM   1608  N   VAL A 199      12.596   0.694  45.264  1.00 35.80      A    N  
ANISOU 1608  N   VAL A 199     4244   5135   4221   -216    743    646  A    N  
ATOM   1609  CA  VAL A 199      13.407   1.558  44.376  1.00 34.37      A    C  
ANISOU 1609  CA  VAL A 199     4194   4929   3934    -72    673    590  A    C  
ATOM   1610  C   VAL A 199      12.624   1.726  43.061  1.00 34.01      A    C  
ANISOU 1610  C   VAL A 199     4136   4788   3997      9    719    520  A    C  
ATOM   1611  O   VAL A 199      12.486   2.843  42.577  1.00 34.78      A    O  
ANISOU 1611  O   VAL A 199     4425   5008   3780     28    828    797  A    O  
ATOM   1612  CB  VAL A 199      14.845   0.988  44.143  1.00 33.58      A    C  
ANISOU 1612  CB  VAL A 199     4128   4729   3900   -247    529    504  A    C  
ATOM   1613  CG1 VAL A 199      15.594   1.826  43.097  1.00 31.81      A    C  
ANISOU 1613  CG1 VAL A 199     3516   4967   3601     84    747    434  A    C  
ATOM   1614  CG2 VAL A 199      15.651   0.977  45.417  1.00 36.68      A    C  
ANISOU 1614  CG2 VAL A 199     4622   5096   4216     66    396    669  A    C  
ATOM   1615  N   VAL A 200      12.098   0.638  42.491  1.00 33.12      A    N  
ANISOU 1615  N   VAL A 200     3839   4979   3765    -12    719    476  A    N  
ATOM   1616  CA  VAL A 200      11.216   0.700  41.322  1.00 32.39      A    C  
ANISOU 1616  CA  VAL A 200     3733   4882   3692   -109    832    304  A    C  
ATOM   1617  C   VAL A 200       9.939  -0.039  41.753  1.00 33.39      A    C  
ANISOU 1617  C   VAL A 200     3898   4819   3969   -127    727    422  A    C  
ATOM   1618  O   VAL A 200       9.974  -1.246  42.104  1.00 33.11      A    O  
ANISOU 1618  O   VAL A 200     3809   4857   3913   -172    910    709  A    O  
ATOM   1619  CB  VAL A 200      11.899   0.004  40.113  1.00 31.69      A    C  
ANISOU 1619  CB  VAL A 200     3780   4857   3401    -15    654    264  A    C  
ATOM   1620  CG1 VAL A 200      10.970  -0.144  38.895  1.00 29.91      A    C  
ANISOU 1620  CG1 VAL A 200     3348   4758   3257   -116    818    221  A    C  
ATOM   1621  CG2 VAL A 200      13.186   0.697  39.795  1.00 32.06      A    C  
ANISOU 1621  CG2 VAL A 200     4214   4734   3232   -356    310    275  A    C  
ATOM   1622  N   SER A 201       8.817   0.674  41.688  1.00 30.97      A    N  
ANISOU 1622  N   SER A 201     3320   4814   3632    -60   1230    392  A    N  
ATOM   1623  CA  SER A 201       7.549   0.030  41.947  1.00 33.91      A    C  
ANISOU 1623  CA  SER A 201     3866   4727   4289   -119    776    455  A    C  
ATOM   1624  C   SER A 201       7.271  -1.159  41.023  1.00 34.60      A    C  
ANISOU 1624  C   SER A 201     4154   4684   4309    -39    743    556  A    C  
ATOM   1625  O   SER A 201       7.531  -1.100  39.829  1.00 32.39      A    O  
ANISOU 1625  O   SER A 201     3965   4448   3894    173   1130    397  A    O  
ATOM   1626  CB  SER A 201       6.436   1.044  41.870  1.00 33.10      A    C  
ANISOU 1626  CB  SER A 201     3432   4714   4428    -45    956    380  A    C  
ATOM   1627  OG  SER A 201       5.241   0.298  41.772  1.00 35.51      A    O  
ANISOU 1627  OG  SER A 201     3927   5377   4189   -219   1244    806  A    O  
ATOM   1628  N   PRO A 202       6.766  -2.280  41.597  1.00 35.57      A    N  
ANISOU 1628  N   PRO A 202     4319   4702   4493   -209    684    664  A    N  
ATOM   1629  CA  PRO A 202       6.402  -3.450  40.821  1.00 35.50      A    C  
ANISOU 1629  CA  PRO A 202     4382   4582   4522   -275    495    718  A    C  
ATOM   1630  C   PRO A 202       5.373  -3.080  39.728  1.00 35.95      A    C  
ANISOU 1630  C   PRO A 202     4509   4574   4577   -256    557    737  A    C  
ATOM   1631  O   PRO A 202       5.188  -3.832  38.776  1.00 35.17      A    O  
ANISOU 1631  O   PRO A 202     4473   4559   4330   -224    599    892  A    O  
ATOM   1632  CB  PRO A 202       5.760  -4.379  41.887  1.00 36.13      A    C  
ANISOU 1632  CB  PRO A 202     4675   4617   4434   -306    362    811  A    C  
ATOM   1633  CG  PRO A 202       6.394  -4.004  43.116  1.00 37.75      A    C  
ANISOU 1633  CG  PRO A 202     4788   4813   4740   -341    566    787  A    C  
ATOM   1634  CD  PRO A 202       6.670  -2.524  43.053  1.00 36.75      A    C  
ANISOU 1634  CD  PRO A 202     4680   4752   4532   -168    480    665  A    C  
ATOM   1635  N   ASN A 203       4.679  -1.946  39.877  1.00 37.40      A    N  
ANISOU 1635  N   ASN A 203     4651   4660   4896   -180    482    695  A    N  
ATOM   1636  CA  ASN A 203       3.763  -1.461  38.820  1.00 37.22      A    C  
ANISOU 1636  CA  ASN A 203     4621   4809   4711     -1    543    617  A    C  
ATOM   1637  C   ASN A 203       4.457  -1.284  37.469  1.00 36.75      A    C  
ANISOU 1637  C   ASN A 203     4516   4765   4682     49    488    641  A    C  
ATOM   1638  O   ASN A 203       3.801  -1.375  36.443  1.00 37.52      A    O  
ANISOU 1638  O   ASN A 203     4479   4988   4786    153    601    691  A    O  
ATOM   1639  CB  ASN A 203       3.097  -0.131  39.214  1.00 39.71      A    C  
ANISOU 1639  CB  ASN A 203     4851   5211   5025     12    621    535  A    C  
ATOM   1640  CG  ASN A 203       2.254  -0.253  40.442  1.00 40.65      A    C  
ANISOU 1640  CG  ASN A 203     4929   5465   5049     82    720    249  A    C  
ATOM   1641  ND2 ASN A 203       2.145   0.811  41.174  1.00 44.93      A    N  
ANISOU 1641  ND2 ASN A 203     5382   6137   5551    135    546   -293  A    N  
ATOM   1642  OD1 ASN A 203       1.709  -1.298  40.723  1.00 43.02      A    O  
ANISOU 1642  OD1 ASN A 203     4841   5828   5675    201   1023    319  A    O  
ATOM   1643  N   ALA A 204       5.772  -1.112  37.461  1.00 34.05      A    N  
ANISOU 1643  N   ALA A 204     4109   4473   4355      8    626    712  A    N  
ATOM   1644  CA  ALA A 204       6.498  -0.946  36.164  1.00 32.40      A    C  
ANISOU 1644  CA  ALA A 204     3904   4330   4074     92    506    582  A    C  
ATOM   1645  C   ALA A 204       6.443  -2.232  35.374  1.00 32.06      A    C  
ANISOU 1645  C   ALA A 204     3589   4459   4134    -35    500    558  A    C  
ATOM   1646  O   ALA A 204       6.110  -2.201  34.190  1.00 32.62      A    O  
ANISOU 1646  O   ALA A 204     3558   4634   4201   -152    692    389  A    O  
ATOM   1647  CB  ALA A 204       7.901  -0.501  36.365  1.00 31.36      A    C  
ANISOU 1647  CB  ALA A 204     3889   4304   3720     54    501    604  A    C  
ATOM   1648  N   SER A 205       6.700  -3.356  36.050  1.00 31.24      A    N  
ANISOU 1648  N   SER A 205     3395   4072   4402      7    442    513  A    N  
ATOM   1649  CA  SER A 205       6.565  -4.674  35.446  1.00 31.73      A    C  
ANISOU 1649  CA  SER A 205     3372   4186   4498    -74    417    595  A    C  
ATOM   1650  C   SER A 205       5.094  -5.014  35.096  1.00 31.88      A    C  
ANISOU 1650  C   SER A 205     3464   4140   4506   -127    341    628  A    C  
ATOM   1651  O   SER A 205       4.862  -5.621  34.079  1.00 31.15      A    O  
ANISOU 1651  O   SER A 205     3129   3884   4821   -287    411    646  A    O  
ATOM   1652  CB  SER A 205       7.228  -5.748  36.334  1.00 31.51      A    C  
ANISOU 1652  CB  SER A 205     3218   4082   4673    154    332    486  A    C  
ATOM   1653  OG  SER A 205       8.631  -5.659  36.182  1.00 31.68      A    O  
ANISOU 1653  OG  SER A 205     3225   4138   4672    371    397    179  A    O  
ATOM   1654  N   LYS A 206       4.123  -4.642  35.950  1.00 33.11      A    N  
ANISOU 1654  N   LYS A 206     3548   4304   4726   -191    468    570  A    N  
ATOM   1655  CA  LYS A 206       2.702  -4.859  35.615  1.00 33.82      A    C  
ANISOU 1655  CA  LYS A 206     3787   4515   4548   -257    374    554  A    C  
ATOM   1656  C   LYS A 206       2.330  -4.058  34.362  1.00 34.75      A    C  
ANISOU 1656  C   LYS A 206     3929   4527   4747   -157    344    476  A    C  
ATOM   1657  O   LYS A 206       1.602  -4.546  33.485  1.00 34.99      A    O  
ANISOU 1657  O   LYS A 206     3808   4795   4692   -360    497    404  A    O  
ATOM   1658  CB  LYS A 206       1.774  -4.540  36.785  1.00 34.73      A    C  
ANISOU 1658  CB  LYS A 206     3789   4587   4816   -155    366    537  A    C  
ATOM   1659  CG  LYS A 206       2.072  -5.331  38.034  1.00 34.46      A    C  
ANISOU 1659  CG  LYS A 206     3585   4745   4763   -720    613    820  A    C  
ATOM   1660  CD  LYS A 206       1.037  -5.004  39.176  1.00 38.48      A    C  
ANISOU 1660  CD  LYS A 206     4587   5063   4967   -571    890   1028  A    C  
ATOM   1661  CE  LYS A 206       1.279  -5.961  40.300  1.00 42.37      A    C  
ANISOU 1661  CE  LYS A 206     5265   5981   4851   -413    816   1195  A    C  
ATOM   1662  NZ  LYS A 206       0.926  -5.378  41.595  1.00 48.54      A    N1+
ANISOU 1662  NZ  LYS A 206     5964   6602   5876   -170    601    484  A    N1+
ATOM   1663  N   LYS A 207       2.905  -2.862  34.225  1.00 33.81      A    N  
ANISOU 1663  N   LYS A 207     3882   4396   4565   -195    489    559  A    N  
ATOM   1664  CA  LYS A 207       2.677  -2.133  32.984  1.00 34.46      A    C  
ANISOU 1664  CA  LYS A 207     4200   4427   4465    -70    391    532  A    C  
ATOM   1665  C   LYS A 207       3.355  -2.753  31.739  1.00 33.40      A    C  
ANISOU 1665  C   LYS A 207     3970   4286   4431   -162    406    486  A    C  
ATOM   1666  O   LYS A 207       2.732  -2.865  30.667  1.00 34.51      A    O  
ANISOU 1666  O   LYS A 207     4007   4416   4688   -227    538    401  A    O  
ATOM   1667  CB  LYS A 207       3.000  -0.655  33.113  1.00 35.02      A    C  
ANISOU 1667  CB  LYS A 207     4358   4560   4385   -176    339    650  A    C  
ATOM   1668  CG  LYS A 207       2.622   0.132  31.815  1.00 37.75      A    C  
ANISOU 1668  CG  LYS A 207     5435   4419   4489     43    295   1019  A    C  
ATOM   1669  CD  LYS A 207       2.571   1.578  32.127  1.00 44.66      A    C  
ANISOU 1669  CD  LYS A 207     6647   4987   5335    275    198   1108  A    C  
ATOM   1670  CE  LYS A 207       2.108   2.331  30.916  1.00 46.06      A    C  
ANISOU 1670  CE  LYS A 207     7425   4813   5260     88    461   1606  A    C  
ATOM   1671  NZ  LYS A 207       1.823   3.713  31.346  1.00 50.48      A    N1+
ANISOU 1671  NZ  LYS A 207     7946   5477   5754    767    308    997  A    N1+
ATOM   1672  N   TYR A 208       4.619  -3.134  31.841  1.00 32.90      A    N  
ANISOU 1672  N   TYR A 208     3928   4204   4365   -124    375    330  A    N  
ATOM   1673  CA  TYR A 208       5.242  -3.776  30.688  1.00 32.07      A    C  
ANISOU 1673  CA  TYR A 208     3750   4084   4348   -231    271    302  A    C  
ATOM   1674  C   TYR A 208       4.404  -5.025  30.321  1.00 33.33      A    C  
ANISOU 1674  C   TYR A 208     3896   4185   4580   -210    142    254  A    C  
ATOM   1675  O   TYR A 208       4.164  -5.313  29.167  1.00 31.50      A    O  
ANISOU 1675  O   TYR A 208     3660   3735   4574   -335    116    195  A    O  
ATOM   1676  CB  TYR A 208       6.628  -4.250  31.069  1.00 30.68      A    C  
ANISOU 1676  CB  TYR A 208     3298   4165   4190   -270    398    246  A    C  
ATOM   1677  CG  TYR A 208       7.768  -3.284  30.870  1.00 31.47      A    C  
ANISOU 1677  CG  TYR A 208     3977   4036   3941   -264    193    179  A    C  
ATOM   1678  CD1 TYR A 208       8.239  -2.998  29.592  1.00 30.77      A    C  
ANISOU 1678  CD1 TYR A 208     3562   3702   4425    104    443     70  A    C  
ATOM   1679  CD2 TYR A 208       8.449  -2.751  31.983  1.00 28.90      A    C  
ANISOU 1679  CD2 TYR A 208     3550   3408   4021   -300     36    126  A    C  
ATOM   1680  CE1 TYR A 208       9.367  -2.171  29.397  1.00 28.76      A    C  
ANISOU 1680  CE1 TYR A 208     3674   3135   4118   -375   -198    271  A    C  
ATOM   1681  CE2 TYR A 208       9.541  -1.909  31.841  1.00 27.73      A    C  
ANISOU 1681  CE2 TYR A 208     3473   3268   3792   -311    329    516  A    C  
ATOM   1682  CZ  TYR A 208      10.011  -1.625  30.525  1.00 29.90      A    C  
ANISOU 1682  CZ  TYR A 208     3945   3657   3757   -526     52    263  A    C  
ATOM   1683  OH  TYR A 208      11.137  -0.832  30.354  1.00 28.90      A    O  
ANISOU 1683  OH  TYR A 208     3580   3388   4010   -354    -74    521  A    O  
ATOM   1684  N   ASP A 209       3.938  -5.740  31.334  1.00 34.29      A    N  
ANISOU 1684  N   ASP A 209     3805   4265   4957   -155    222    318  A    N  
ATOM   1685  CA  ASP A 209       3.153  -6.956  31.059  1.00 36.35      A    C  
ANISOU 1685  CA  ASP A 209     4076   4701   5031   -156    179    238  A    C  
ATOM   1686  C   ASP A 209       1.856  -6.608  30.266  1.00 36.99      A    C  
ANISOU 1686  C   ASP A 209     4101   4862   5091   -106    151    119  A    C  
ATOM   1687  O   ASP A 209       1.434  -7.349  29.427  1.00 36.46      A    O  
ANISOU 1687  O   ASP A 209     3926   5041   4885    -64    290    109  A    O  
ATOM   1688  CB  ASP A 209       2.908  -7.763  32.344  1.00 36.97      A    C  
ANISOU 1688  CB  ASP A 209     4252   4542   5251   -211    170    392  A    C  
ATOM   1689  CG  ASP A 209       2.204  -9.078  32.074  1.00 38.72      A    C  
ANISOU 1689  CG  ASP A 209     4382   4796   5533   -379    393    561  A    C  
ATOM   1690  OD1 ASP A 209       2.656  -9.852  31.193  1.00 36.73      A    O  
ANISOU 1690  OD1 ASP A 209     3909   4463   5584   -337    207    173  A    O  
ATOM   1691  OD2 ASP A 209       1.168  -9.316  32.735  1.00 39.29      A    O1-
ANISOU 1691  OD2 ASP A 209     4178   4675   6075   -954    602   1525  A    O1-
ATOM   1692  N   GLN A 210       1.293  -5.430  30.499  1.00 39.02      A    N  
ANISOU 1692  N   GLN A 210     4339   5187   5299      4    103     67  A    N  
ATOM   1693  CA  GLN A 210       0.106  -4.974  29.768  1.00 40.70      A    C  
ANISOU 1693  CA  GLN A 210     4616   5463   5383     56     -6     33  A    C  
ATOM   1694  C   GLN A 210       0.472  -4.656  28.340  1.00 39.38      A    C  
ANISOU 1694  C   GLN A 210     4450   5268   5242    147    128   -102  A    C  
ATOM   1695  O   GLN A 210      -0.223  -5.054  27.438  1.00 40.87      A    O  
ANISOU 1695  O   GLN A 210     4443   5706   5379    196    207   -103  A    O  
ATOM   1696  CB  GLN A 210      -0.521  -3.730  30.428  1.00 41.10      A    C  
ANISOU 1696  CB  GLN A 210     4627   5768   5221     42     71   -127  A    C  
ATOM   1697  CG  GLN A 210      -1.189  -4.004  31.766  1.00 49.48      A    C  
ANISOU 1697  CG  GLN A 210     5752   7080   5966   -193    -60    236  A    C  
ATOM   1698  CD  GLN A 210      -2.182  -5.120  31.671  1.00 55.13      A    C  
ANISOU 1698  CD  GLN A 210     6198   8087   6661   -413   -273    379  A    C  
ATOM   1699  NE2 GLN A 210      -2.121  -6.077  32.626  1.00 56.27      A    N  
ANISOU 1699  NE2 GLN A 210     6350   8649   6380   -100   -534    624  A    N  
ATOM   1700  OE1 GLN A 210      -2.995  -5.152  30.719  1.00 58.93      A    O  
ANISOU 1700  OE1 GLN A 210     6682   9100   6606    -39   -343    172  A    O  
ATOM   1701  N   ILE A 211       1.589  -3.961  28.137  1.00 39.21      A    N  
ANISOU 1701  N   ILE A 211     4537   5128   5231    218    185     87  A    N  
ATOM   1702  CA  ILE A 211       1.948  -3.443  26.800  1.00 38.46      A    C  
ANISOU 1702  CA  ILE A 211     4583   4858   5172    102    120    109  A    C  
ATOM   1703  C   ILE A 211       2.517  -4.512  25.823  1.00 36.14      A    C  
ANISOU 1703  C   ILE A 211     4177   4615   4939     29    183    101  A    C  
ATOM   1704  O   ILE A 211       2.258  -4.448  24.624  1.00 37.00      A    O  
ANISOU 1704  O   ILE A 211     4249   4452   5355    145    104   -310  A    O  
ATOM   1705  CB  ILE A 211       2.816  -2.163  26.936  1.00 39.54      A    C  
ANISOU 1705  CB  ILE A 211     4694   4977   5350    167     44    297  A    C  
ATOM   1706  CG1 ILE A 211       4.221  -2.466  27.475  1.00 41.48      A    C  
ANISOU 1706  CG1 ILE A 211     4955   5554   5251     35     52    347  A    C  
ATOM   1707  CG2 ILE A 211       2.102  -1.171  27.868  1.00 37.86      A    C  
ANISOU 1707  CG2 ILE A 211     4878   4776   4730    -44    383    365  A    C  
ATOM   1708  CD1 ILE A 211       5.319  -2.573  26.425  1.00 42.10      A    C  
ANISOU 1708  CD1 ILE A 211     5015   6024   4954    692     -7    367  A    C  
ATOM   1709  N   TYR A 212       3.249  -5.494  26.349  1.00 34.60      A    N  
ANISOU 1709  N   TYR A 212     3942   4272   4931   -124    219     -4  A    N  
ATOM   1710  CA  TYR A 212       3.829  -6.574  25.571  1.00 34.71      A    C  
ANISOU 1710  CA  TYR A 212     3929   4223   5037    -50    156    202  A    C  
ATOM   1711  C   TYR A 212       2.826  -7.564  24.974  1.00 35.82      A    C  
ANISOU 1711  C   TYR A 212     4049   4249   5311    -41    284    254  A    C  
ATOM   1712  O   TYR A 212       1.928  -8.037  25.671  1.00 35.12      A    O  
ANISOU 1712  O   TYR A 212     4032   3815   5496   -100    475    599  A    O  
ATOM   1713  CB  TYR A 212       4.819  -7.330  26.429  1.00 34.46      A    C  
ANISOU 1713  CB  TYR A 212     3891   4192   5009    -62    108    113  A    C  
ATOM   1714  CG  TYR A 212       6.175  -6.687  26.477  1.00 32.24      A    C  
ANISOU 1714  CG  TYR A 212     3579   3959   4709     25    300     61  A    C  
ATOM   1715  CD1 TYR A 212       6.827  -6.292  25.295  1.00 30.39      A    C  
ANISOU 1715  CD1 TYR A 212     3470   3747   4330    168    244    -68  A    C  
ATOM   1716  CD2 TYR A 212       6.827  -6.496  27.689  1.00 31.63      A    C  
ANISOU 1716  CD2 TYR A 212     2979   4439   4599    -54    145    108  A    C  
ATOM   1717  CE1 TYR A 212       8.099  -5.685  25.339  1.00 28.73      A    C  
ANISOU 1717  CE1 TYR A 212     3154   3457   4303    115    238   -104  A    C  
ATOM   1718  CE2 TYR A 212       8.114  -5.917  27.748  1.00 30.02      A    C  
ANISOU 1718  CE2 TYR A 212     3278   3598   4530   -145    447    313  A    C  
ATOM   1719  CZ  TYR A 212       8.734  -5.536  26.571  1.00 30.97      A    C  
ANISOU 1719  CZ  TYR A 212     3596   3722   4446   -130    282     21  A    C  
ATOM   1720  OH  TYR A 212       9.995  -4.985  26.637  1.00 33.87      A    O  
ANISOU 1720  OH  TYR A 212     4191   3686   4989   -174   -110     65  A    O  
ATOM   1721  N   GLN A 213       2.990  -7.884  23.682  1.00 36.63      A    N  
ANISOU 1721  N   GLN A 213     4015   4381   5520    -24    295    147  A    N  
ATOM   1722  CA  GLN A 213       2.116  -8.874  23.027  1.00 37.33      A    C  
ANISOU 1722  CA  GLN A 213     3994   4451   5736   -190    345    157  A    C  
ATOM   1723  C   GLN A 213       2.333 -10.309  23.512  1.00 38.01      A    C  
ANISOU 1723  C   GLN A 213     4082   4458   5902   -227    336     51  A    C  
ATOM   1724  O   GLN A 213       1.417 -11.086  23.502  1.00 38.15      A    O  
ANISOU 1724  O   GLN A 213     3830   4481   6184   -384    437    -95  A    O  
ATOM   1725  CB  GLN A 213       2.235  -8.795  21.494  1.00 36.88      A    C  
ANISOU 1725  CB  GLN A 213     3832   4388   5792   -277    494    201  A    C  
ATOM   1726  CG  GLN A 213       1.911  -7.406  20.984  1.00 36.80      A    C  
ANISOU 1726  CG  GLN A 213     3473   4736   5771    271    735    490  A    C  
ATOM   1727  CD  GLN A 213       0.613  -6.929  21.595  1.00 39.80      A    C  
ANISOU 1727  CD  GLN A 213     3765   5453   5905     -7    808    324  A    C  
ATOM   1728  NE2 GLN A 213      -0.452  -7.582  21.188  1.00 37.76      A    N  
ANISOU 1728  NE2 GLN A 213     3500   5349   5496   -406   1220    375  A    N  
ATOM   1729  OE1 GLN A 213       0.561  -6.016  22.476  1.00 38.26      A    O  
ANISOU 1729  OE1 GLN A 213     3807   5406   5323    192    981    683  A    O  
ATOM   1730  N   ASN A 214       3.533 -10.651  23.949  1.00 39.24      A    N  
ANISOU 1730  N   ASN A 214     4259   4660   5987   -335    162    106  A    N  
ATOM   1731  CA  ASN A 214       3.856 -12.051  24.318  1.00 39.76      A    C  
ANISOU 1731  CA  ASN A 214     4468   4736   5902   -315    135      8  A    C  
ATOM   1732  C   ASN A 214       4.758 -11.980  25.540  1.00 39.04      A    C  
ANISOU 1732  C   ASN A 214     4318   4601   5915   -355    151     48  A    C  
ATOM   1733  O   ASN A 214       5.952 -12.054  25.391  1.00 41.63      A    O  
ANISOU 1733  O   ASN A 214     4684   5007   6126   -317     13    -42  A    O  
ATOM   1734  CB  ASN A 214       4.574 -12.781  23.157  1.00 39.20      A    C  
ANISOU 1734  CB  ASN A 214     4170   4885   5838   -445    206    -58  A    C  
ATOM   1735  CG  ASN A 214       3.603 -13.297  22.048  1.00 42.46      A    C  
ANISOU 1735  CG  ASN A 214     5140   5199   5794   -538    439   -243  A    C  
ATOM   1736  ND2 ASN A 214       3.877 -12.901  20.775  1.00 42.87      A    N  
ANISOU 1736  ND2 ASN A 214     4754   5708   5825   -722   1878   -995  A    N  
ATOM   1737  OD1 ASN A 214       2.624 -14.028  22.324  1.00 43.32      A    O  
ANISOU 1737  OD1 ASN A 214     5194   5428   5835  -1097    213   -773  A    O  
ATOM   1738  N   SER A 215       4.214 -11.758  26.727  1.00 38.35      A    N  
ANISOU 1738  N   SER A 215     4169   4556   5846   -444    360    244  A    N  
ATOM   1739  CA  SER A 215       5.011 -11.627  27.966  1.00 37.95      A    C  
ANISOU 1739  CA  SER A 215     3951   4503   5964   -373    363    298  A    C  
ATOM   1740  C   SER A 215       4.485 -12.529  29.119  1.00 38.64      A    C  
ANISOU 1740  C   SER A 215     4096   4612   5970   -320    422    358  A    C  
ATOM   1741  O   SER A 215       3.344 -13.021  29.032  1.00 38.57      A    O  
ANISOU 1741  O   SER A 215     3825   4744   6084   -315    573    424  A    O  
ATOM   1742  CB  SER A 215       5.123 -10.175  28.451  1.00 38.63      A    C  
ANISOU 1742  CB  SER A 215     3990   4674   6011   -216    398    177  A    C  
ATOM   1743  OG  SER A 215       3.889  -9.690  28.992  1.00 38.29      A    O  
ANISOU 1743  OG  SER A 215     3717   4379   6451   -866    757    -56  A    O  
ATOM   1744  N   THR A 216       5.317 -12.724  30.154  1.00 37.66      A    N  
ANISOU 1744  N   THR A 216     4167   4334   5807   -351    416    476  A    N  
ATOM   1745  CA  THR A 216       5.066 -13.569  31.329  1.00 38.72      A    C  
ANISOU 1745  CA  THR A 216     4387   4581   5741   -206    474    403  A    C  
ATOM   1746  C   THR A 216       5.631 -12.802  32.481  1.00 38.10      A    C  
ANISOU 1746  C   THR A 216     4270   4488   5719   -184    489    450  A    C  
ATOM   1747  O   THR A 216       6.808 -12.415  32.483  1.00 37.95      A    O  
ANISOU 1747  O   THR A 216     4163   4281   5974   -111    811    541  A    O  
ATOM   1748  CB  THR A 216       5.807 -14.967  31.288  1.00 39.39      A    C  
ANISOU 1748  CB  THR A 216     4682   4550   5734   -395    407    495  A    C  
ATOM   1749  CG2 THR A 216       5.503 -15.827  32.560  1.00 39.95      A    C  
ANISOU 1749  CG2 THR A 216     4589   4777   5810   -482    393    768  A    C  
ATOM   1750  OG1 THR A 216       5.393 -15.685  30.133  1.00 38.31      A    O  
ANISOU 1750  OG1 THR A 216     4616   4182   5759   -495    463    238  A    O  
ATOM   1751  N   LEU A 217       4.789 -12.606  33.473  1.00 37.12      A    N  
ANISOU 1751  N   LEU A 217     4159   4498   5447    -90    591    574  A    N  
ATOM   1752  CA  LEU A 217       5.087 -11.819  34.637  1.00 37.38      A    C  
ANISOU 1752  CA  LEU A 217     4188   4613   5401   -166    577    588  A    C  
ATOM   1753  C   LEU A 217       5.307 -12.708  35.845  1.00 38.12      A    C  
ANISOU 1753  C   LEU A 217     4335   4651   5498   -150    618    603  A    C  
ATOM   1754  O   LEU A 217       4.433 -13.524  36.193  1.00 39.27      A    O  
ANISOU 1754  O   LEU A 217     4321   4839   5760   -348    741    790  A    O  
ATOM   1755  CB  LEU A 217       3.917 -10.886  34.931  1.00 36.77      A    C  
ANISOU 1755  CB  LEU A 217     4328   4657   4982     77    729    585  A    C  
ATOM   1756  CG  LEU A 217       4.063 -10.022  36.172  1.00 38.30      A    C  
ANISOU 1756  CG  LEU A 217     4480   4706   5364    106    847    628  A    C  
ATOM   1757  CD1 LEU A 217       5.289  -9.171  36.109  1.00 35.90      A    C  
ANISOU 1757  CD1 LEU A 217     4203   4748   4687    311   1964     51  A    C  
ATOM   1758  CD2 LEU A 217       2.774  -9.182  36.431  1.00 39.50      A    C  
ANISOU 1758  CD2 LEU A 217     5265   4568   5175    491   1694    404  A    C  
ATOM   1759  N   HIS A 218       6.439 -12.539  36.502  1.00 37.85      A    N  
ANISOU 1759  N   HIS A 218     4282   4627   5473    -60    601    668  A    N  
ATOM   1760  CA  HIS A 218       6.766 -13.267  37.714  1.00 39.67      A    C  
ANISOU 1760  CA  HIS A 218     4671   4832   5568      6    573    696  A    C  
ATOM   1761  C   HIS A 218       6.931 -12.255  38.811  1.00 40.26      A    C  
ANISOU 1761  C   HIS A 218     4699   5010   5587     18    553    709  A    C  
ATOM   1762  O   HIS A 218       7.950 -11.538  38.889  1.00 40.48      A    O  
ANISOU 1762  O   HIS A 218     4632   5220   5525     31    788    812  A    O  
ATOM   1763  CB  HIS A 218       8.063 -14.119  37.552  1.00 38.48      A    C  
ANISOU 1763  CB  HIS A 218     4367   4704   5546      6    493    753  A    C  
ATOM   1764  CG  HIS A 218       7.988 -15.114  36.435  1.00 41.31      A    C  
ANISOU 1764  CG  HIS A 218     4962   4931   5802     84    415    553  A    C  
ATOM   1765  CD2 HIS A 218       8.439 -15.069  35.153  1.00 43.33      A    C  
ANISOU 1765  CD2 HIS A 218     4851   5318   6293     56    568    -41  A    C  
ATOM   1766  ND1 HIS A 218       7.345 -16.329  36.571  1.00 42.65      A    N  
ANISOU 1766  ND1 HIS A 218     4996   5132   6077   -238    601     10  A    N  
ATOM   1767  CE1 HIS A 218       7.391 -16.979  35.421  1.00 45.35      A    C  
ANISOU 1767  CE1 HIS A 218     5578   5258   6394    -11    634   -142  A    C  
ATOM   1768  NE2 HIS A 218       8.069 -16.249  34.552  1.00 45.40      A    N  
ANISOU 1768  NE2 HIS A 218     5543   5395   6309    -44    385     88  A    N  
ATOM   1769  N   LEU A 219       5.908 -12.136  39.649  1.00 40.34      A    N  
ANISOU 1769  N   LEU A 219     4653   5022   5649   -114    638    956  A    N  
ATOM   1770  CA  LEU A 219       6.083 -11.321  40.846  1.00 41.19      A    C  
ANISOU 1770  CA  LEU A 219     4712   5236   5701    -55    529    918  A    C  
ATOM   1771  C   LEU A 219       6.676 -12.179  41.958  1.00 42.00      A    C  
ANISOU 1771  C   LEU A 219     4754   5290   5915    -63    434    972  A    C  
ATOM   1772  O   LEU A 219       6.018 -13.151  42.386  1.00 43.24      A    O  
ANISOU 1772  O   LEU A 219     4946   5346   6136   -158    339   1111  A    O  
ATOM   1773  CB  LEU A 219       4.764 -10.653  41.300  1.00 41.08      A    C  
ANISOU 1773  CB  LEU A 219     4605   5340   5660     58    507    910  A    C  
ATOM   1774  CG  LEU A 219       4.054  -9.718  40.316  1.00 41.10      A    C  
ANISOU 1774  CG  LEU A 219     4690   5326   5599    172    640    832  A    C  
ATOM   1775  CD1 LEU A 219       2.661  -9.303  40.853  1.00 43.89      A    C  
ANISOU 1775  CD1 LEU A 219     4838   5621   6218    637    409    531  A    C  
ATOM   1776  CD2 LEU A 219       4.925  -8.480  39.919  1.00 42.01      A    C  
ANISOU 1776  CD2 LEU A 219     4903   5428   5630    197    669    377  A    C  
ATOM   1777  N   ILE A 220       7.855 -11.799  42.469  1.00 42.06      A    N  
ANISOU 1777  N   ILE A 220     4639   5389   5949   -177    467   1031  A    N  
ATOM   1778  CA  ILE A 220       8.538 -12.550  43.534  1.00 42.39      A    C  
ANISOU 1778  CA  ILE A 220     4732   5469   5902   -176    518   1093  A    C  
ATOM   1779  C   ILE A 220       8.229 -12.029  44.946  1.00 43.23      A    C  
ANISOU 1779  C   ILE A 220     4882   5549   5994   -338    579   1016  A    C  
ATOM   1780  O   ILE A 220       8.724 -10.975  45.377  1.00 41.94      A    O  
ANISOU 1780  O   ILE A 220     4577   5333   6024   -420    633   1208  A    O  
ATOM   1781  CB  ILE A 220      10.114 -12.531  43.413  1.00 43.25      A    C  
ANISOU 1781  CB  ILE A 220     4890   5530   6011    -85    372   1176  A    C  
ATOM   1782  CG1 ILE A 220      10.602 -12.791  41.994  1.00 45.29      A    C  
ANISOU 1782  CG1 ILE A 220     5405   5436   6366   -125    414   1090  A    C  
ATOM   1783  CG2 ILE A 220      10.740 -13.480  44.487  1.00 41.70      A    C  
ANISOU 1783  CG2 ILE A 220     4478   5418   5948    199    343   1369  A    C  
ATOM   1784  CD1 ILE A 220      10.131 -14.015  41.335  1.00 48.48      A    C  
ANISOU 1784  CD1 ILE A 220     5929   5767   6722   -182    286    648  A    C  
ATOM   1785  N   GLU A 221       7.407 -12.790  45.676  1.00 44.16      A    N  
ANISOU 1785  N   GLU A 221     5182   5607   5987   -547    847    970  A    N  
ATOM   1786  CA  GLU A 221       6.988 -12.395  47.005  1.00 44.97      A    C  
ANISOU 1786  CA  GLU A 221     5274   5818   5993   -543   1078   1040  A    C  
ATOM   1787  C   GLU A 221       8.169 -12.039  47.905  1.00 44.33      A    C  
ANISOU 1787  C   GLU A 221     5181   5770   5891   -572   1196   1158  A    C  
ATOM   1788  O   GLU A 221       9.089 -12.841  48.088  1.00 45.62      A    O  
ANISOU 1788  O   GLU A 221     5250   6057   6024   -582   1361   1387  A    O  
ATOM   1789  CB  GLU A 221       6.084 -13.499  47.639  1.00 46.50      A    C  
ANISOU 1789  CB  GLU A 221     5424   5980   6262   -597   1091    977  A    C  
ATOM   1790  CG  GLU A 221       5.326 -13.052  48.900  1.00 49.72      A    C  
ANISOU 1790  CG  GLU A 221     5791   6385   6715   -322   1065    514  A    C  
ATOM   1791  CD  GLU A 221       4.506 -11.810  48.640  1.00 52.45      A    C  
ANISOU 1791  CD  GLU A 221     5754   7072   7100    -19   1000    228  A    C  
ATOM   1792  OE1 GLU A 221       3.806 -11.793  47.586  1.00 51.24      A    O  
ANISOU 1792  OE1 GLU A 221     5081   7298   7089    -55    890    393  A    O  
ATOM   1793  OE2 GLU A 221       4.606 -10.856  49.471  1.00 53.89      A    O1-
ANISOU 1793  OE2 GLU A 221     5839   7570   7064    -97   1906   -122  A    O1-
ATOM   1794  N   GLY A 222       8.143 -10.828  48.448  1.00 43.82      A    N  
ANISOU 1794  N   GLY A 222     5135   5726   5787   -575   1186   1208  A    N  
ATOM   1795  CA  GLY A 222       9.109 -10.358  49.444  1.00 42.39      A    C  
ANISOU 1795  CA  GLY A 222     4785   5596   5723   -525   1049   1180  A    C  
ATOM   1796  C   GLY A 222      10.471  -9.914  48.893  1.00 42.40      A    C  
ANISOU 1796  C   GLY A 222     4870   5539   5700   -422    888   1032  A    C  
ATOM   1797  O   GLY A 222      11.277  -9.357  49.639  1.00 42.25      A    O  
ANISOU 1797  O   GLY A 222     4762   5401   5891   -435   1004    987  A    O  
ATOM   1798  N   ALA A 223      10.730 -10.139  47.597  1.00 41.72      A    N  
ANISOU 1798  N   ALA A 223     4769   5407   5674   -319    887   1143  A    N  
ATOM   1799  CA  ALA A 223      12.040  -9.827  47.044  1.00 40.83      A    C  
ANISOU 1799  CA  ALA A 223     4828   5327   5359   -327    790   1156  A    C  
ATOM   1800  C   ALA A 223      12.228  -8.325  46.985  1.00 40.40      A    C  
ANISOU 1800  C   ALA A 223     4878   5338   5133   -266    743   1231  A    C  
ATOM   1801  O   ALA A 223      11.260  -7.573  46.847  1.00 38.84      A    O  
ANISOU 1801  O   ALA A 223     4560   5321   4876   -366    896   1482  A    O  
ATOM   1802  CB  ALA A 223      12.249 -10.473  45.685  1.00 40.16      A    C  
ANISOU 1802  CB  ALA A 223     4772   5232   5254    -95    747   1183  A    C  
ATOM   1803  N   ASP A 224      13.491  -7.930  47.183  1.00 39.90      A    N  
ANISOU 1803  N   ASP A 224     4979   5291   4887   -388    618   1173  A    N  
ATOM   1804  CA  ASP A 224      13.973  -6.557  47.092  1.00 38.97      A    C  
ANISOU 1804  CA  ASP A 224     4972   5191   4644   -233    578    990  A    C  
ATOM   1805  C   ASP A 224      14.485  -6.187  45.638  1.00 37.10      A    C  
ANISOU 1805  C   ASP A 224     4836   4860   4397   -161    540   1041  A    C  
ATOM   1806  O   ASP A 224      14.371  -6.981  44.706  1.00 36.21      A    O  
ANISOU 1806  O   ASP A 224     4574   4825   4358     13    728   1240  A    O  
ATOM   1807  CB  ASP A 224      15.063  -6.401  48.126  1.00 39.63      A    C  
ANISOU 1807  CB  ASP A 224     5039   5405   4611   -223    489    890  A    C  
ATOM   1808  CG  ASP A 224      16.351  -7.117  47.746  1.00 43.19      A    C  
ANISOU 1808  CG  ASP A 224     5222   5878   5311   -226    406   1007  A    C  
ATOM   1809  OD1 ASP A 224      16.385  -8.274  47.204  1.00 43.97      A    O  
ANISOU 1809  OD1 ASP A 224     5332   6501   4873   -276    865    988  A    O  
ATOM   1810  OD2 ASP A 224      17.368  -6.488  48.032  1.00 49.17      A    O1-
ANISOU 1810  OD2 ASP A 224     5573   6228   6879   -531    445   1225  A    O1-
ATOM   1811  N   HIS A 225      15.007  -4.975  45.471  1.00 35.69      A    N  
ANISOU 1811  N   HIS A 225     4566   4757   4234   -197    687    963  A    N  
ATOM   1812  CA  HIS A 225      15.271  -4.418  44.123  1.00 34.69      A    C  
ANISOU 1812  CA  HIS A 225     4560   4421   4200    -66    516    934  A    C  
ATOM   1813  C   HIS A 225      16.414  -5.179  43.471  1.00 35.15      A    C  
ANISOU 1813  C   HIS A 225     4533   4515   4307    -90    532    773  A    C  
ATOM   1814  O   HIS A 225      16.458  -5.367  42.238  1.00 34.50      A    O  
ANISOU 1814  O   HIS A 225     4373   4335   4400     83    770    770  A    O  
ATOM   1815  CB  HIS A 225      15.648  -2.919  44.276  1.00 35.18      A    C  
ANISOU 1815  CB  HIS A 225     4615   4491   4258   -145    552    909  A    C  
ATOM   1816  CG  HIS A 225      15.941  -2.239  42.973  1.00 32.84      A    C  
ANISOU 1816  CG  HIS A 225     4927   3893   3656     77    481   1077  A    C  
ATOM   1817  CD2 HIS A 225      17.052  -1.604  42.519  1.00 34.19      A    C  
ANISOU 1817  CD2 HIS A 225     4581   4790   3617    459    856    691  A    C  
ATOM   1818  ND1 HIS A 225      15.061  -2.272  41.911  1.00 35.94      A    N  
ANISOU 1818  ND1 HIS A 225     4924   4594   4137    175    250    987  A    N  
ATOM   1819  CE1 HIS A 225      15.591  -1.633  40.864  1.00 31.26      A    C  
ANISOU 1819  CE1 HIS A 225     4536   5053   2286    378    389    401  A    C  
ATOM   1820  NE2 HIS A 225      16.799  -1.210  41.204  1.00 32.53      A    N  
ANISOU 1820  NE2 HIS A 225     4304   5299   2754    605    531    693  A    N  
ATOM   1821  N   CYS A 226      17.340  -5.622  44.322  1.00 35.41      A    N  
ANISOU 1821  N   CYS A 226     4704   4375   4374   -102    613    946  A    N  
ATOM   1822  CA  CYS A 226      18.591  -6.252  43.881  1.00 37.85      A    C  
ANISOU 1822  CA  CYS A 226     4832   4786   4761   -173    534    749  A    C  
ATOM   1823  C   CYS A 226      18.494  -7.802  43.845  1.00 38.12      A    C  
ANISOU 1823  C   CYS A 226     4747   4955   4779   -141    447    859  A    C  
ATOM   1824  O   CYS A 226      19.392  -8.479  43.375  1.00 38.06      A    O  
ANISOU 1824  O   CYS A 226     4778   5249   4433   -183    404    798  A    O  
ATOM   1825  CB  CYS A 226      19.751  -5.756  44.742  1.00 37.68      A    C  
ANISOU 1825  CB  CYS A 226     4759   4880   4677   -265    816    714  A    C  
ATOM   1826  SG  CYS A 226      20.318  -4.090  44.274  1.00 45.10      A    S  
ANISOU 1826  SG  CYS A 226     6307   4425   6401   -397    517    678  A    S  
ATOM   1827  N   PHE A 227      17.364  -8.372  44.280  1.00 38.42      A    N  
ANISOU 1827  N   PHE A 227     4730   4999   4867   -238    487    945  A    N  
ATOM   1828  CA  PHE A 227      17.200  -9.852  44.344  1.00 40.17      A    C  
ANISOU 1828  CA  PHE A 227     4706   5169   5385   -154    434   1016  A    C  
ATOM   1829  C   PHE A 227      18.329 -10.441  45.125  1.00 41.52      A    C  
ANISOU 1829  C   PHE A 227     4859   5238   5679   -162    449   1066  A    C  
ATOM   1830  O   PHE A 227      19.070 -11.332  44.644  1.00 42.19      A    O  
ANISOU 1830  O   PHE A 227     4944   5192   5892   -109    370   1196  A    O  
ATOM   1831  CB  PHE A 227      17.052 -10.525  42.978  1.00 39.30      A    C  
ANISOU 1831  CB  PHE A 227     4575   5074   5280   -201    431   1132  A    C  
ATOM   1832  CG  PHE A 227      15.890  -9.993  42.175  1.00 39.21      A    C  
ANISOU 1832  CG  PHE A 227     4299   5341   5258   -228    418   1115  A    C  
ATOM   1833  CD1 PHE A 227      14.587 -10.493  42.386  1.00 36.42      A    C  
ANISOU 1833  CD1 PHE A 227     3951   5257   4629     -8   1027    981  A    C  
ATOM   1834  CD2 PHE A 227      16.090  -8.968  41.244  1.00 38.20      A    C  
ANISOU 1834  CD2 PHE A 227     4307   5245   4962   -208    693   1016  A    C  
ATOM   1835  CE1 PHE A 227      13.510 -10.000  41.644  1.00 36.84      A    C  
ANISOU 1835  CE1 PHE A 227     4279   5123   4594   -213    623    802  A    C  
ATOM   1836  CE2 PHE A 227      15.027  -8.464  40.484  1.00 37.83      A    C  
ANISOU 1836  CE2 PHE A 227     4301   5200   4870   -172    631    926  A    C  
ATOM   1837  CZ  PHE A 227      13.729  -8.973  40.685  1.00 37.48      A    C  
ANISOU 1837  CZ  PHE A 227     4265   5124   4852   -181    453    966  A    C  
ATOM   1838  N   SER A 228      18.509  -9.887  46.299  1.00 42.36      A    N  
ANISOU 1838  N   SER A 228     4961   5399   5734   -140    462   1019  A    N  
ATOM   1839  CA  SER A 228      19.671 -10.213  47.014  1.00 45.72      A    C  
ANISOU 1839  CA  SER A 228     5356   5816   6197     82    276    976  A    C  
ATOM   1840  C   SER A 228      19.488 -11.356  47.981  1.00 47.63      A    C  
ANISOU 1840  C   SER A 228     5716   6098   6283    115    312   1011  A    C  
ATOM   1841  O   SER A 228      18.396 -11.591  48.527  1.00 48.27      A    O  
ANISOU 1841  O   SER A 228     5836   6109   6396    171    420   1142  A    O  
ATOM   1842  CB  SER A 228      20.322  -8.998  47.644  1.00 46.02      A    C  
ANISOU 1842  CB  SER A 228     5389   5933   6160     60    229    749  A    C  
ATOM   1843  OG  SER A 228      19.388  -8.081  48.114  1.00 48.18      A    O  
ANISOU 1843  OG  SER A 228     4730   6575   7000    513   -101    628  A    O  
ATOM   1844  N   ASP A 229      20.591 -12.091  48.092  1.00 48.94      A    N  
ANISOU 1844  N   ASP A 229     5964   6254   6377    231    173   1084  A    N  
ATOM   1845  CA  ASP A 229      20.767 -13.174  49.035  1.00 50.38      A    C  
ANISOU 1845  CA  ASP A 229     6258   6481   6402    267     49    959  A    C  
ATOM   1846  C   ASP A 229      19.824 -14.291  48.798  1.00 50.07      A    C  
ANISOU 1846  C   ASP A 229     6211   6421   6390    264     13    938  A    C  
ATOM   1847  O   ASP A 229      19.816 -14.965  47.732  1.00 49.49      A    O  
ANISOU 1847  O   ASP A 229     6013   6541   6250    290    220    971  A    O  
ATOM   1848  CB  ASP A 229      20.597 -12.629  50.455  1.00 51.02      A    C  
ANISOU 1848  CB  ASP A 229     6547   6541   6296    335     27    981  A    C  
ATOM   1849  CG  ASP A 229      21.729 -11.730  50.837  1.00 54.20      A    C  
ANISOU 1849  CG  ASP A 229     7008   7091   6493    415   -124    700  A    C  
ATOM   1850  OD1 ASP A 229      22.843 -11.962  50.290  1.00 55.59      A    O  
ANISOU 1850  OD1 ASP A 229     7569   7523   6027    871    -49    430  A    O  
ATOM   1851  OD2 ASP A 229      21.513 -10.784  51.646  1.00 59.52      A    O1-
ANISOU 1851  OD2 ASP A 229     7932   7826   6854    791     17    204  A    O1-
ATOM   1852  N   SER A 230      18.994 -14.462  49.823  1.00 50.05      A    N  
ANISOU 1852  N   SER A 230     6280   6396   6338    170     21    804  A    N  
ATOM   1853  CA  SER A 230      18.039 -15.528  49.841  1.00 50.49      A    C  
ANISOU 1853  CA  SER A 230     6382   6334   6465    -14    -75    598  A    C  
ATOM   1854  C   SER A 230      17.020 -15.472  48.663  1.00 49.70      A    C  
ANISOU 1854  C   SER A 230     6411   6075   6395    -44   -153    647  A    C  
ATOM   1855  O   SER A 230      16.240 -16.416  48.524  1.00 49.23      A    O  
ANISOU 1855  O   SER A 230     6590   5677   6435   -103   -329    593  A    O  
ATOM   1856  CB  SER A 230      17.364 -15.615  51.262  1.00 50.50      A    C  
ANISOU 1856  CB  SER A 230     6518   6314   6354    -81    -40    526  A    C  
ATOM   1857  OG  SER A 230      16.680 -14.408  51.584  1.00 50.53      A    O  
ANISOU 1857  OG  SER A 230     6324   6688   6186    -46    -30    166  A    O  
ATOM   1858  N   TYR A 231      17.019 -14.372  47.863  1.00 48.34      A    N  
ANISOU 1858  N   TYR A 231     6052   5902   6413    -14     21    637  A    N  
ATOM   1859  CA  TYR A 231      16.146 -14.180  46.686  1.00 47.20      A    C  
ANISOU 1859  CA  TYR A 231     5864   5729   6341    126    121    676  A    C  
ATOM   1860  C   TYR A 231      16.848 -14.315  45.351  1.00 46.92      A    C  
ANISOU 1860  C   TYR A 231     5788   5675   6361    146    182    677  A    C  
ATOM   1861  O   TYR A 231      16.203 -14.477  44.314  1.00 47.15      A    O  
ANISOU 1861  O   TYR A 231     5732   5594   6588    138     35    723  A    O  
ATOM   1862  CB  TYR A 231      15.469 -12.779  46.664  1.00 46.59      A    C  
ANISOU 1862  CB  TYR A 231     5684   5714   6301    200    146    698  A    C  
ATOM   1863  CG  TYR A 231      14.505 -12.629  47.750  1.00 46.77      A    C  
ANISOU 1863  CG  TYR A 231     5606   5763   6402    688     57    785  A    C  
ATOM   1864  CD1 TYR A 231      13.264 -13.319  47.699  1.00 48.54      A    C  
ANISOU 1864  CD1 TYR A 231     5894   5868   6680    771    326    619  A    C  
ATOM   1865  CD2 TYR A 231      14.829 -11.889  48.879  1.00 46.45      A    C  
ANISOU 1865  CD2 TYR A 231     5462   5573   6615    901    287    637  A    C  
ATOM   1866  CE1 TYR A 231      12.360 -13.233  48.729  1.00 49.13      A    C  
ANISOU 1866  CE1 TYR A 231     5994   6080   6592    731    334   1147  A    C  
ATOM   1867  CE2 TYR A 231      13.937 -11.806  49.932  1.00 50.41      A    C  
ANISOU 1867  CE2 TYR A 231     5762   6485   6906    916    461    848  A    C  
ATOM   1868  CZ  TYR A 231      12.707 -12.474  49.831  1.00 49.50      A    C  
ANISOU 1868  CZ  TYR A 231     5922   6310   6576    914    787    990  A    C  
ATOM   1869  OH  TYR A 231      11.842 -12.400  50.838  1.00 49.90      A    O  
ANISOU 1869  OH  TYR A 231     5051   7066   6841   1204   1277   1410  A    O  
ATOM   1870  N   GLN A 232      18.168 -14.194  45.363  1.00 46.21      A    N  
ANISOU 1870  N   GLN A 232     5682   5675   6202    189    353    848  A    N  
ATOM   1871  CA  GLN A 232      18.929 -14.241  44.105  1.00 45.06      A    C  
ANISOU 1871  CA  GLN A 232     5726   5546   5849    160    446   1186  A    C  
ATOM   1872  C   GLN A 232      18.754 -15.486  43.234  1.00 44.51      A    C  
ANISOU 1872  C   GLN A 232     5746   5413   5752    184    529   1169  A    C  
ATOM   1873  O   GLN A 232      18.570 -15.369  42.053  1.00 43.03      A    O  
ANISOU 1873  O   GLN A 232     5577   5191   5579    156    826   1277  A    O  
ATOM   1874  CB  GLN A 232      20.404 -13.969  44.390  1.00 45.29      A    C  
ANISOU 1874  CB  GLN A 232     5685   5731   5790    127    444   1256  A    C  
ATOM   1875  CG  GLN A 232      21.242 -13.828  43.152  1.00 47.95      A    C  
ANISOU 1875  CG  GLN A 232     5480   6450   6288    182    437   1468  A    C  
ATOM   1876  CD  GLN A 232      22.692 -13.708  43.516  1.00 49.60      A    C  
ANISOU 1876  CD  GLN A 232     5568   7029   6246    347     44   1573  A    C  
ATOM   1877  NE2 GLN A 232      23.408 -14.802  43.362  1.00 50.86      A    N  
ANISOU 1877  NE2 GLN A 232     5481   7710   6133    754    278   1616  A    N  
ATOM   1878  OE1 GLN A 232      23.159 -12.659  43.971  1.00 49.23      A    O  
ANISOU 1878  OE1 GLN A 232     5294   7437   5971   -116    176   1815  A    O  
ATOM   1879  N   LYS A 233      18.771 -16.691  43.817  1.00 44.80      A    N  
ANISOU 1879  N   LYS A 233     6036   5203   5781    248    577   1141  A    N  
ATOM   1880  CA  LYS A 233      18.601 -17.927  43.051  1.00 45.24      A    C  
ANISOU 1880  CA  LYS A 233     6105   5205   5877    320    606   1015  A    C  
ATOM   1881  C   LYS A 233      17.311 -18.026  42.245  1.00 44.86      A    C  
ANISOU 1881  C   LYS A 233     6062   5086   5894    268    666    993  A    C  
ATOM   1882  O   LYS A 233      17.276 -18.604  41.164  1.00 43.32      A    O  
ANISOU 1882  O   LYS A 233     5817   4820   5821    397    702   1054  A    O  
ATOM   1883  CB  LYS A 233      18.671 -19.146  43.991  1.00 46.77      A    C  
ANISOU 1883  CB  LYS A 233     6541   5168   6058    346    526   1008  A    C  
ATOM   1884  CG  LYS A 233      18.874 -20.452  43.219  1.00 51.00      A    C  
ANISOU 1884  CG  LYS A 233     7234   5617   6526    609    706    782  A    C  
ATOM   1885  CD  LYS A 233      19.536 -21.556  44.051  1.00 56.24      A    C  
ANISOU 1885  CD  LYS A 233     8360   6089   6919    917    674    802  A    C  
ATOM   1886  CE  LYS A 233      20.496 -22.354  43.182  1.00 57.59      A    C  
ANISOU 1886  CE  LYS A 233     8515   6335   7032   1023    934    623  A    C  
ATOM   1887  NZ  LYS A 233      20.366 -23.849  43.391  1.00 59.54      A    N1+
ANISOU 1887  NZ  LYS A 233     8989   6535   7096    558   1343    572  A    N1+
ATOM   1888  N   ASN A 234      16.218 -17.525  42.807  1.00 44.59      A    N  
ANISOU 1888  N   ASN A 234     5821   5124   5994    268    702    948  A    N  
ATOM   1889  CA  ASN A 234      14.949 -17.654  42.106  1.00 45.11      A    C  
ANISOU 1889  CA  ASN A 234     5877   5263   5997    163    738    835  A    C  
ATOM   1890  C   ASN A 234      14.981 -16.778  40.851  1.00 43.25      A    C  
ANISOU 1890  C   ASN A 234     5587   5130   5716     55    787    749  A    C  
ATOM   1891  O   ASN A 234      14.492 -17.214  39.835  1.00 42.10      A    O  
ANISOU 1891  O   ASN A 234     5376   4933   5686     27    786    750  A    O  
ATOM   1892  CB  ASN A 234      13.786 -17.265  43.033  1.00 46.09      A    C  
ANISOU 1892  CB  ASN A 234     5928   5463   6119    106    977    764  A    C  
ATOM   1893  CG  ASN A 234      12.379 -17.410  42.377  1.00 47.78      A    C  
ANISOU 1893  CG  ASN A 234     6242   5639   6273    284    896    867  A    C  
ATOM   1894  ND2 ASN A 234      11.365 -16.990  43.118  1.00 50.24      A    N  
ANISOU 1894  ND2 ASN A 234     7051   5110   6927    884   1340    968  A    N  
ATOM   1895  OD1 ASN A 234      12.207 -17.919  41.252  1.00 50.23      A    O  
ANISOU 1895  OD1 ASN A 234     6364   6014   6706    201   1089    833  A    O  
ATOM   1896  N   ALA A 235      15.527 -15.544  40.966  1.00 42.19      A    N  
ANISOU 1896  N   ALA A 235     5325   4975   5730    130    791    798  A    N  
ATOM   1897  CA  ALA A 235      15.659 -14.610  39.824  1.00 41.05      A    C  
ANISOU 1897  CA  ALA A 235     5120   4739   5737     58    667    763  A    C  
ATOM   1898  C   ALA A 235      16.522 -15.249  38.723  1.00 40.49      A    C  
ANISOU 1898  C   ALA A 235     4931   4802   5650     31    694    850  A    C  
ATOM   1899  O   ALA A 235      16.150 -15.258  37.518  1.00 39.09      A    O  
ANISOU 1899  O   ALA A 235     4499   4551   5802     49    709    964  A    O  
ATOM   1900  CB  ALA A 235      16.255 -13.243  40.305  1.00 40.76      A    C  
ANISOU 1900  CB  ALA A 235     4956   4755   5775     73    537    793  A    C  
ATOM   1901  N   VAL A 236      17.645 -15.857  39.142  1.00 40.99      A    N  
ANISOU 1901  N   VAL A 236     5021   4864   5688     40    774    816  A    N  
ATOM   1902  CA  VAL A 236      18.606 -16.504  38.207  1.00 40.97      A    C  
ANISOU 1902  CA  VAL A 236     5007   4935   5621     87    749    729  A    C  
ATOM   1903  C   VAL A 236      17.957 -17.722  37.566  1.00 40.78      A    C  
ANISOU 1903  C   VAL A 236     4989   4800   5706     68    745    793  A    C  
ATOM   1904  O   VAL A 236      18.005 -17.900  36.327  1.00 40.86      A    O  
ANISOU 1904  O   VAL A 236     4901   4687   5937    133    573    828  A    O  
ATOM   1905  CB  VAL A 236      19.968 -16.833  38.898  1.00 41.28      A    C  
ANISOU 1905  CB  VAL A 236     5090   4992   5602    110    833    661  A    C  
ATOM   1906  CG1 VAL A 236      20.855 -17.709  37.994  1.00 42.82      A    C  
ANISOU 1906  CG1 VAL A 236     5095   5347   5828    404    705    596  A    C  
ATOM   1907  CG2 VAL A 236      20.717 -15.498  39.325  1.00 41.09      A    C  
ANISOU 1907  CG2 VAL A 236     4919   4961   5731   -121    825    634  A    C  
ATOM   1908  N   ASN A 237      17.302 -18.544  38.399  1.00 41.36      A    N  
ANISOU 1908  N   ASN A 237     5081   4679   5954     62    723    834  A    N  
ATOM   1909  CA  ASN A 237      16.535 -19.668  37.868  1.00 41.60      A    C  
ANISOU 1909  CA  ASN A 237     5097   4728   5981    -90    748    932  A    C  
ATOM   1910  C   ASN A 237      15.461 -19.349  36.822  1.00 41.36      A    C  
ANISOU 1910  C   ASN A 237     5176   4624   5913   -214    754    841  A    C  
ATOM   1911  O   ASN A 237      15.413 -19.991  35.791  1.00 41.44      A    O  
ANISOU 1911  O   ASN A 237     5458   4362   5925   -340    903    799  A    O  
ATOM   1912  CB  ASN A 237      15.994 -20.560  39.016  1.00 42.91      A    C  
ANISOU 1912  CB  ASN A 237     5243   4850   6207    -36    702   1073  A    C  
ATOM   1913  CG  ASN A 237      17.113 -21.352  39.714  1.00 45.65      A    C  
ANISOU 1913  CG  ASN A 237     5560   5210   6573    229    806   1333  A    C  
ATOM   1914  ND2 ASN A 237      16.832 -21.845  40.942  1.00 48.83      A    N  
ANISOU 1914  ND2 ASN A 237     6127   5229   7194    165   1168   1660  A    N  
ATOM   1915  OD1 ASN A 237      18.225 -21.495  39.166  1.00 47.59      A    O  
ANISOU 1915  OD1 ASN A 237     5285   5419   7376    819   1017   1578  A    O  
ATOM   1916  N   LEU A 238      14.605 -18.362  37.079  1.00 40.76      A    N  
ANISOU 1916  N   LEU A 238     4850   4613   6023   -193    623    742  A    N  
ATOM   1917  CA  LEU A 238      13.563 -17.998  36.112  1.00 40.97      A    C  
ANISOU 1917  CA  LEU A 238     4699   4766   6101   -151    407    529  A    C  
ATOM   1918  C   LEU A 238      14.174 -17.495  34.810  1.00 40.38      A    C  
ANISOU 1918  C   LEU A 238     4514   4783   6044    -49    294    493  A    C  
ATOM   1919  O   LEU A 238      13.776 -17.884  33.694  1.00 40.68      A    O  
ANISOU 1919  O   LEU A 238     4263   4784   6407    -39    178    621  A    O  
ATOM   1920  CB  LEU A 238      12.628 -16.940  36.717  1.00 41.45      A    C  
ANISOU 1920  CB  LEU A 238     4684   4946   6119    -85    528    428  A    C  
ATOM   1921  CG  LEU A 238      11.531 -17.369  37.722  1.00 43.40      A    C  
ANISOU 1921  CG  LEU A 238     4698   5233   6559   -162    530    134  A    C  
ATOM   1922  CD1 LEU A 238      11.032 -16.159  38.528  1.00 42.44      A    C  
ANISOU 1922  CD1 LEU A 238     3886   5339   6899    136   1173    131  A    C  
ATOM   1923  CD2 LEU A 238      10.383 -18.094  37.029  1.00 41.91      A    C  
ANISOU 1923  CD2 LEU A 238     4229   5235   6460   -208    518     78  A    C  
ATOM   1924  N   THR A 239      15.197 -16.652  34.950  1.00 39.49      A    N  
ANISOU 1924  N   THR A 239     4422   4638   5942    -27    300    627  A    N  
ATOM   1925  CA  THR A 239      15.942 -16.166  33.779  1.00 37.93      A    C  
ANISOU 1925  CA  THR A 239     4343   4555   5512    110    106    717  A    C  
ATOM   1926  C   THR A 239      16.491 -17.311  32.893  1.00 37.75      A    C  
ANISOU 1926  C   THR A 239     4417   4472   5453     89     33    636  A    C  
ATOM   1927  O   THR A 239      16.292 -17.315  31.682  1.00 36.14      A    O  
ANISOU 1927  O   THR A 239     4129   4184   5417     30    -55    696  A    O  
ATOM   1928  CB  THR A 239      17.078 -15.194  34.245  1.00 38.21      A    C  
ANISOU 1928  CB  THR A 239     4398   4539   5579    -24    211    701  A    C  
ATOM   1929  CG2 THR A 239      17.848 -14.641  33.085  1.00 35.19      A    C  
ANISOU 1929  CG2 THR A 239     4089   4263   5016    156    185   1055  A    C  
ATOM   1930  OG1 THR A 239      16.513 -14.109  34.986  1.00 36.12      A    O  
ANISOU 1930  OG1 THR A 239     4019   4726   4979    283    422   1130  A    O  
ATOM   1931  N   THR A 240      17.166 -18.287  33.521  1.00 38.01      A    N  
ANISOU 1931  N   THR A 240     4545   4400   5496    158     52    624  A    N  
ATOM   1932  CA  THR A 240      17.868 -19.345  32.785  1.00 38.22      A    C  
ANISOU 1932  CA  THR A 240     4733   4358   5430    232     67    654  A    C  
ATOM   1933  C   THR A 240      16.851 -20.236  32.067  1.00 38.98      A    C  
ANISOU 1933  C   THR A 240     4801   4505   5503    121    133    640  A    C  
ATOM   1934  O   THR A 240      17.032 -20.595  30.895  1.00 40.06      A    O  
ANISOU 1934  O   THR A 240     4730   4550   5938    -66    448    671  A    O  
ATOM   1935  CB  THR A 240      18.794 -20.132  33.768  1.00 38.48      A    C  
ANISOU 1935  CB  THR A 240     4771   4426   5422    334   -131    437  A    C  
ATOM   1936  CG2 THR A 240      19.424 -21.348  33.118  1.00 37.95      A    C  
ANISOU 1936  CG2 THR A 240     4688   4857   4872    857    396    294  A    C  
ATOM   1937  OG1 THR A 240      19.848 -19.273  34.159  1.00 39.45      A    O  
ANISOU 1937  OG1 THR A 240     4924   4282   5783    120   -262    744  A    O  
ATOM   1938  N   ASP A 241      15.749 -20.535  32.758  1.00 39.83      A    N  
ANISOU 1938  N   ASP A 241     4839   4520   5773     74    271    685  A    N  
ATOM   1939  CA  ASP A 241      14.687 -21.438  32.261  1.00 41.38      A    C  
ANISOU 1939  CA  ASP A 241     5056   4795   5870      3    346    543  A    C  
ATOM   1940  C   ASP A 241      13.964 -20.845  31.093  1.00 40.75      A    C  
ANISOU 1940  C   ASP A 241     4755   4706   6019     16    321    380  A    C  
ATOM   1941  O   ASP A 241      13.685 -21.509  30.067  1.00 41.61      A    O  
ANISOU 1941  O   ASP A 241     4818   4579   6412    -69    289    293  A    O  
ATOM   1942  CB  ASP A 241      13.711 -21.749  33.412  1.00 42.62      A    C  
ANISOU 1942  CB  ASP A 241     5158   5000   6033     42    445    607  A    C  
ATOM   1943  CG  ASP A 241      14.273 -22.775  34.367  1.00 47.03      A    C  
ANISOU 1943  CG  ASP A 241     6232   5412   6224   -110    515    804  A    C  
ATOM   1944  OD1 ASP A 241      15.279 -23.448  33.996  1.00 50.56      A    O  
ANISOU 1944  OD1 ASP A 241     7645   4844   6722    181    537    872  A    O  
ATOM   1945  OD2 ASP A 241      13.758 -22.877  35.521  1.00 53.61      A    O1-
ANISOU 1945  OD2 ASP A 241     7172   6005   7191   -541    797   1221  A    O1-
ATOM   1946  N   PHE A 242      13.725 -19.539  31.217  1.00 40.48      A    N  
ANISOU 1946  N   PHE A 242     4686   4617   6077   -123    320    368  A    N  
ATOM   1947  CA  PHE A 242      13.068 -18.836  30.176  1.00 39.36      A    C  
ANISOU 1947  CA  PHE A 242     4613   4433   5907   -109    261    351  A    C  
ATOM   1948  C   PHE A 242      13.938 -18.891  28.930  1.00 39.97      A    C  
ANISOU 1948  C   PHE A 242     4814   4455   5918   -114    149    227  A    C  
ATOM   1949  O   PHE A 242      13.459 -19.161  27.826  1.00 39.51      A    O  
ANISOU 1949  O   PHE A 242     4583   4251   6176   -162    139    211  A    O  
ATOM   1950  CB  PHE A 242      12.868 -17.397  30.610  1.00 39.08      A    C  
ANISOU 1950  CB  PHE A 242     4624   4491   5733   -130    339    423  A    C  
ATOM   1951  CG  PHE A 242      12.151 -16.600  29.604  1.00 41.72      A    C  
ANISOU 1951  CG  PHE A 242     4899   4590   6359     68     14    507  A    C  
ATOM   1952  CD1 PHE A 242      10.787 -16.811  29.390  1.00 41.99      A    C  
ANISOU 1952  CD1 PHE A 242     5029   4222   6701     33   -204    650  A    C  
ATOM   1953  CD2 PHE A 242      12.837 -15.672  28.825  1.00 39.74      A    C  
ANISOU 1953  CD2 PHE A 242     4753   4364   5983    232    -35    556  A    C  
ATOM   1954  CE1 PHE A 242      10.109 -16.103  28.438  1.00 44.42      A    C  
ANISOU 1954  CE1 PHE A 242     5510   4745   6623     37   -493    760  A    C  
ATOM   1955  CE2 PHE A 242      12.182 -14.965  27.861  1.00 42.61      A    C  
ANISOU 1955  CE2 PHE A 242     5270   4351   6567    522   -274    543  A    C  
ATOM   1956  CZ  PHE A 242      10.801 -15.171  27.668  1.00 43.42      A    C  
ANISOU 1956  CZ  PHE A 242     5274   4683   6538    226   -286    674  A    C  
ATOM   1957  N   LEU A 243      15.228 -18.609  29.115  1.00 40.93      A    N  
ANISOU 1957  N   LEU A 243     4983   4470   6097    -83    108    202  A    N  
ATOM   1958  CA  LEU A 243      16.168 -18.591  28.006  1.00 42.00      A    C  
ANISOU 1958  CA  LEU A 243     5219   4682   6056   -136     23     78  A    C  
ATOM   1959  C   LEU A 243      16.532 -19.972  27.463  1.00 45.34      A    C  
ANISOU 1959  C   LEU A 243     5693   5141   6392   -110    -41    -49  A    C  
ATOM   1960  O   LEU A 243      16.873 -20.081  26.286  1.00 45.03      A    O  
ANISOU 1960  O   LEU A 243     5710   5043   6353   -137     68   -152  A    O  
ATOM   1961  CB  LEU A 243      17.444 -17.759  28.351  1.00 40.36      A    C  
ANISOU 1961  CB  LEU A 243     5013   4390   5931   -159    -97    149  A    C  
ATOM   1962  CG  LEU A 243      17.116 -16.271  28.653  1.00 38.44      A    C  
ANISOU 1962  CG  LEU A 243     4578   4057   5968   -460   -133    177  A    C  
ATOM   1963  CD1 LEU A 243      18.349 -15.510  29.055  1.00 35.64      A    C  
ANISOU 1963  CD1 LEU A 243     4690   2745   6107   -612   -323    385  A    C  
ATOM   1964  CD2 LEU A 243      16.459 -15.644  27.434  1.00 36.44      A    C  
ANISOU 1964  CD2 LEU A 243     4118   3574   6152    -32     39     65  A    C  
ATOM   1965  N   GLN A 244      16.485 -21.017  28.281  1.00 49.38      A    N  
ANISOU 1965  N   GLN A 244     6268   5691   6801   -167    -17     -3  A    N  
ATOM   1966  CA  GLN A 244      16.939 -22.335  27.764  1.00 54.46      A    C  
ANISOU 1966  CA  GLN A 244     7042   6300   7351    -29    -63    -32  A    C  
ATOM   1967  C   GLN A 244      15.885 -23.029  26.879  1.00 56.38      A    C  
ANISOU 1967  C   GLN A 244     7305   6557   7556    -86    -55    -26  A    C  
ATOM   1968  O   GLN A 244      16.231 -23.880  26.064  1.00 57.70      A    O  
ANISOU 1968  O   GLN A 244     7622   6536   7763      8   -133    -52  A    O  
ATOM   1969  CB  GLN A 244      17.429 -23.237  28.870  1.00 55.22      A    C  
ANISOU 1969  CB  GLN A 244     7126   6332   7523    -45    -74     11  A    C  
ATOM   1970  CG  GLN A 244      16.356 -24.150  29.355  1.00 60.68      A    C  
ANISOU 1970  CG  GLN A 244     7596   7099   8357   -229   -165     91  A    C  
ATOM   1971  CD  GLN A 244      16.831 -24.996  30.468  1.00 65.05      A    C  
ANISOU 1971  CD  GLN A 244     8085   7449   9181   -224   -535    320  A    C  
ATOM   1972  NE2 GLN A 244      16.327 -26.230  30.528  1.00 67.85      A    N  
ANISOU 1972  NE2 GLN A 244     8320   7701   9759   -469   -383   -216  A    N  
ATOM   1973  OE1 GLN A 244      17.642 -24.550  31.296  1.00 64.96      A    O  
ANISOU 1973  OE1 GLN A 244     7567   7291   9824   -509   -644    418  A    O  
ATOM   1974  N   ASN A 245      14.634 -22.588  26.974  1.00 59.00      A    N  
ANISOU 1974  N   ASN A 245     7538   7087   7792    -51     -7     36  A    N  
ATOM   1975  CA  ASN A 245      13.515 -23.161  26.221  1.00 61.33      A    C  
ANISOU 1975  CA  ASN A 245     7765   7610   7926    -72    -13    182  A    C  
ATOM   1976  C   ASN A 245      13.716 -23.270  24.690  1.00 62.24      A    C  
ANISOU 1976  C   ASN A 245     7899   7795   7954    -68    -44    252  A    C  
ATOM   1977  O   ASN A 245      13.077 -22.548  23.904  1.00 62.84      A    O  
ANISOU 1977  O   ASN A 245     8001   8037   7836   -160    -93    433  A    O  
ATOM   1978  CB  ASN A 245      12.239 -22.379  26.539  1.00 62.39      A    C  
ANISOU 1978  CB  ASN A 245     7867   7685   8153    -18      5    160  A    C  
ATOM   1979  CG  ASN A 245      11.123 -23.279  27.082  1.00 64.97      A    C  
ANISOU 1979  CG  ASN A 245     8076   8122   8486    147    189    462  A    C  
ATOM   1980  ND2 ASN A 245       9.885 -23.004  26.663  1.00 67.31      A    N  
ANISOU 1980  ND2 ASN A 245     8359   8342   8874    491      3    565  A    N  
ATOM   1981  OD1 ASN A 245      11.373 -24.206  27.872  1.00 66.27      A    O  
ANISOU 1981  OD1 ASN A 245     8383   7907   8887    772    319    444  A    O  
TER   
END



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