CNRS Nantes University US2B US2B
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***  receptor  ***

elNémo ID: 2303081325574163

Job options:

ID        	=	 2303081325574163
JOBID     	=	 receptor
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER receptor

REMARK    File generated by Swiss-PdbViewer  4.00b0
REMARK    http://www.expasy.org/spdbv/
REMARK    File generated by Swiss-PdbViewer  4.00b0
REMARK    http://www.expasy.org/spdbv/
HEADER                                            01-JUN-22                     
TITLE     ALPHAFOLD MONOMER V2.0 PREDICTION FOR SODIUM-DEPENDENT DOPAMINE       
TITLE    2 TRANSPORTER (Q01959)                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SODIUM-DEPENDENT DOPAMINE TRANSPORTER;                     
COMPND   3 CHAIN: A                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606                                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   JOHN JUMPER, RICHARD EVANS, ALEXANDER PRITZEL, TIM GREEN,    
REMARK   1  AUTH 2 MICHAEL FIGURNOV, OLAF RONNEBERGER, KATHRYN TUNYASUVUNAKOOL, 
REMARK   1  AUTH 3 RUSS BATES, AUGUSTIN ZIDEK, ANNA POTAPENKO, ALEX BRIDGLAND,  
REMARK   1  AUTH 4 CLEMENS MEYER, SIMON A A KOHL, ANDREW J BALLARD,             
REMARK   1  AUTH 5 ANDREW COWIE, BERNARDINO ROMERA-PAREDES, STANISLAV NIKOLOV,  
REMARK   1  AUTH 6 RISHUB JAIN, JONAS ADLER, TREVOR BACK, STIG PETERSEN,        
REMARK   1  AUTH 7 DAVID REIMAN, ELLEN CLANCY, MICHAL ZIELINSKI,                
REMARK   1  AUTH 8 MARTIN STEINEGGER, MICHALINA PACHOLSKA, TAMAS BERGHAMMER,    
REMARK   1  AUTH 9 DAVID SILVER, ORIOL VINYALS, ANDREW W SENIOR,                
REMARK   1  AUTH10 KORAY KAVUKCUOGLU, PUSHMEET KOHLI, DEMIS HASSABIS            
REMARK   1  TITL   HIGHLY ACCURATE PROTEIN STRUCTURE PREDICTION WITH ALPHAFOLD  
REMARK   1  REF    NATURE                        V. 596   583 2021              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   34265844                                                     
REMARK   1  DOI    10.1038/s41586-021-03819-2                                   
REMARK   1                                                                      
REMARK   1 DISCLAIMERS                                                          
REMARK   1 ALPHAFOLD DATA, COPYRIGHT (2021) DEEPMIND TECHNOLOGIES LIMITED. THE  
REMARK   1 INFORMATION PROVIDED IS THEORETICAL MODELLING ONLY AND CAUTION SHOULD
REMARK   1 BE EXERCISED IN ITS USE. IT IS PROVIDED "AS-IS" WITHOUT ANY WARRANTY 
REMARK   1 OF ANY KIND, WHETHER EXPRESSED OR IMPLIED. NO WARRANTY IS GIVEN THAT 
REMARK   1 USE OF THE INFORMATION SHALL NOT INFRINGE THE RIGHTS OF ANY THIRD    
REMARK   1 PARTY. THE INFORMATION IS NOT INTENDED TO BE A SUBSTITUTE FOR        
REMARK   1 PROFESSIONAL MEDICAL ADVICE, DIAGNOSIS, OR TREATMENT, AND DOES NOT   
REMARK   1 CONSTITUTE MEDICAL OR OTHER PROFESSIONAL ADVICE. IT IS AVAILABLE FOR 
REMARK   1 ACADEMIC AND COMMERCIAL PURPOSES, UNDER CC-BY 4.0 LICENCE.           
DBREF  XXXX A    1   620  UNP    Q01959   SC6A3_HUMAN      1    620             
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1   
ATOM      1  N   LYS A   1      -2.907 -23.271   5.550  1.00 94.12
ATOM      2  CA  LYS A   1      -2.365 -22.214   6.434  1.00 94.12
ATOM      3  C   LYS A   1      -1.232 -21.415   5.779  1.00 94.12
ATOM      4  O   LYS A   1      -1.074 -20.237   6.062  1.00 94.12
ATOM      5  CB  LYS A   1      -1.841 -22.811   7.750  1.00 94.12
ATOM      6  CG  LYS A   1      -2.936 -23.416   8.637  1.00 94.12
ATOM      7  CD  LYS A   1      -2.337 -23.843   9.985  1.00 94.12
ATOM      8  CE  LYS A   1      -3.430 -24.382  10.912  1.00 94.12
ATOM      9  NZ  LYS A   1      -2.900 -24.680  12.267  1.00 94.12
ATOM     10  N   ILE A   2      -0.435 -22.074   4.935  1.00 95.55
ATOM     11  CA  ILE A   2       0.663 -21.428   4.213  1.00 95.55
ATOM     12  C   ILE A   2       0.156 -20.506   3.101  1.00 95.55
ATOM     13  O   ILE A   2       0.821 -19.522   2.825  1.00 95.55
ATOM     14  CB  ILE A   2       1.665 -22.483   3.694  1.00 95.55
ATOM     15  CG1 ILE A   2       2.992 -21.890   3.174  1.00 95.55
ATOM     16  CG2 ILE A   2       1.044 -23.361   2.595  1.00 95.55
ATOM     17  CD1 ILE A   2       3.787 -21.123   4.237  1.00 95.55
ATOM     18  N   ASP A   3      -1.023 -20.773   2.522  1.00 96.19
ATOM     19  CA  ASP A   3      -1.607 -19.892   1.503  1.00 96.19
ATOM     20  C   ASP A   3      -1.915 -18.523   2.133  1.00 96.19
ATOM     21  O   ASP A   3      -1.495 -17.505   1.604  1.00 96.19
ATOM     22  CB  ASP A   3      -2.876 -20.505   0.876  1.00 96.19
ATOM     23  CG  ASP A   3      -2.722 -21.906   0.260  1.00 96.19
ATOM     24  OD1 ASP A   3      -1.595 -22.331  -0.094  1.00 96.19
ATOM     25  OD2 ASP A   3      -3.755 -22.621   0.227  1.00 96.19
ATOM     26  N   PHE A   4      -2.530 -18.511   3.326  1.00 97.07
ATOM     27  CA  PHE A   4      -2.726 -17.290   4.119  1.00 97.07
ATOM     28  C   PHE A   4      -1.402 -16.588   4.442  1.00 97.07
ATOM     29  O   PHE A   4      -1.265 -15.393   4.197  1.00 97.07
ATOM     30  CB  PHE A   4      -3.452 -17.633   5.428  1.00 97.07
ATOM     31  CG  PHE A   4      -3.421 -16.524   6.466  1.00 97.07
ATOM     32  CD1 PHE A   4      -2.596 -16.647   7.601  1.00 97.07
ATOM     33  CD2 PHE A   4      -4.173 -15.348   6.278  1.00 97.07
ATOM     34  CE1 PHE A   4      -2.527 -15.604   8.536  1.00 97.07
ATOM     35  CE2 PHE A   4      -4.119 -14.316   7.231  1.00 97.07
ATOM     36  CZ  PHE A   4      -3.287 -14.443   8.353  1.00 97.07
ATOM     37  N   LEU A   5      -0.427 -17.322   4.995  1.00 97.73
ATOM     38  CA  LEU A   5       0.848 -16.730   5.403  1.00 97.73
ATOM     39  C   LEU A   5       1.595 -16.124   4.205  1.00 97.73
ATOM     40  O   LEU A   5       2.115 -15.021   4.322  1.00 97.73
ATOM     41  CB  LEU A   5       1.688 -17.787   6.142  1.00 97.73
ATOM     42  CG  LEU A   5       3.050 -17.271   6.647  1.00 97.73
ATOM     43  CD1 LEU A   5       2.908 -16.151   7.679  1.00 97.73
ATOM     44  CD2 LEU A   5       3.821 -18.418   7.306  1.00 97.73
ATOM     45  N   LEU A   6       1.608 -16.805   3.055  1.00 97.39
ATOM     46  CA  LEU A   6       2.186 -16.278   1.819  1.00 97.39
ATOM     47  C   LEU A   6       1.415 -15.065   1.299  1.00 97.39
ATOM     48  O   LEU A   6       2.057 -14.114   0.881  1.00 97.39
ATOM     49  CB  LEU A   6       2.242 -17.368   0.735  1.00 97.39
ATOM     50  CG  LEU A   6       3.337 -18.427   0.941  1.00 97.39
ATOM     51  CD1 LEU A   6       3.183 -19.521  -0.118  1.00 97.39
ATOM     52  CD2 LEU A   6       4.749 -17.845   0.819  1.00 97.39
ATOM     53  N   SER A   7       0.079 -15.049   1.362  1.00 97.78
ATOM     54  CA  SER A   7      -0.711 -13.871   0.975  1.00 97.78
ATOM     55  C   SER A   7      -0.416 -12.657   1.851  1.00 97.78
ATOM     56  O   SER A   7      -0.281 -11.550   1.344  1.00 97.78
ATOM     57  CB  SER A   7      -2.214 -14.166   1.044  1.00 97.78
ATOM     58  OG  SER A   7      -2.599 -15.123   0.077  1.00 97.78
ATOM     59  N   VAL A   8      -0.283 -12.855   3.163  1.00 97.82
ATOM     60  CA  VAL A   8       0.049 -11.776   4.099  1.00 97.82
ATOM     61  C   VAL A   8       1.495 -11.297   3.904  1.00 97.82
ATOM     62  O   VAL A   8       1.738 -10.095   3.953  1.00 97.82
ATOM     63  CB  VAL A   8      -0.226 -12.242   5.536  1.00 97.82
ATOM     64  CG1 VAL A   8       0.185 -11.203   6.562  1.00 97.82
ATOM     65  CG2 VAL A   8      -1.713 -12.484   5.803  1.00 97.82
ATOM     66  N   ILE A   9       2.442 -12.203   3.628  1.00 97.72
ATOM     67  CA  ILE A   9       3.826 -11.842   3.276  1.00 97.72
ATOM     68  C   ILE A   9       3.876 -11.102   1.941  1.00 97.72
ATOM     69  O   ILE A   9       4.520 -10.068   1.887  1.00 97.72
ATOM     70  CB  ILE A   9       4.757 -13.077   3.275  1.00 97.72
ATOM     71  CG1 ILE A   9       4.980 -13.577   4.720  1.00 97.72
ATOM     72  CG2 ILE A   9       6.124 -12.762   2.628  1.00 97.72
ATOM     73  CD1 ILE A   9       5.574 -14.990   4.783  1.00 97.72
ATOM     74  N   GLY A  10       3.205 -11.587   0.895  1.00 96.80
ATOM     75  CA  GLY A  10       3.180 -10.937  -0.419  1.00 96.80
ATOM     76  C   GLY A  10       2.529  -9.556  -0.377  1.00 96.80
ATOM     77  O   GLY A  10       2.982  -8.645  -1.052  1.00 96.80
ATOM     78  N   PHE A  11       1.510  -9.363   0.465  1.00 96.96
ATOM     79  CA  PHE A  11       0.932  -8.038   0.691  1.00 96.96
ATOM     80  C   PHE A  11       1.894  -7.099   1.429  1.00 96.96
ATOM     81  O   PHE A  11       2.037  -5.947   1.029  1.00 96.96
ATOM     82  CB  PHE A  11      -0.387  -8.184   1.459  1.00 96.96
ATOM     83  CG  PHE A  11      -0.940  -6.863   1.954  1.00 96.96
ATOM     84  CD1 PHE A  11      -0.877  -6.534   3.319  1.00 96.96
ATOM     85  CD2 PHE A  11      -1.474  -5.940   1.038  1.00 96.96
ATOM     86  CE1 PHE A  11      -1.361  -5.295   3.764  1.00 96.96
ATOM     87  CE2 PHE A  11      -1.903  -4.676   1.471  1.00 96.96
ATOM     88  CZ  PHE A  11      -1.855  -4.355   2.838  1.00 96.96
ATOM     89  N   ALA A  12       2.529  -7.585   2.502  1.00 96.76
ATOM     90  CA  ALA A  12       3.429  -6.778   3.320  1.00 96.76
ATOM     91  C   ALA A  12       4.781  -6.532   2.637  1.00 96.76
ATOM     92  O   ALA A  12       5.435  -5.544   2.909  1.00 96.76
ATOM     93  CB  ALA A  12       3.612  -7.472   4.678  1.00 96.76
ATOM     94  N   VAL A  13       5.275  -7.445   1.810  1.00 96.29
ATOM     95  CA  VAL A  13       6.523  -7.268   1.064  1.00 96.29
ATOM     96  C   VAL A  13       6.156  -6.727  -0.298  1.00 96.29
ATOM     97  O   VAL A  13       5.859  -7.482  -1.218  1.00 96.29
ATOM     98  CB  VAL A  13       7.340  -8.560   1.004  1.00 96.29
ATOM     99  CG1 VAL A  13       8.599  -8.394   0.146  1.00 96.29
ATOM    100  CG2 VAL A  13       7.788  -8.916   2.430  1.00 96.29
ATOM    101  N   ASP A  14       6.164  -5.409  -0.400  1.00 93.57
ATOM    102  CA  ASP A  14       5.658  -4.688  -1.548  1.00 93.57
ATOM    103  C   ASP A  14       6.752  -3.871  -2.239  1.00 93.57
ATOM    104  O   ASP A  14       7.953  -3.969  -1.951  1.00 93.57
ATOM    105  CB  ASP A  14       4.451  -3.844  -1.100  1.00 93.57
ATOM    106  CG  ASP A  14       4.773  -2.550  -0.357  1.00 93.57
ATOM    107  OD1 ASP A  14       5.936  -2.344   0.049  1.00 93.57
ATOM    108  OD2 ASP A  14       3.903  -1.654  -0.388  1.00 93.57
ATOM    109  N   LEU A  15       6.321  -3.031  -3.180  1.00 91.65
ATOM    110  CA  LEU A  15       7.202  -2.069  -3.817  1.00 91.65
ATOM    111  C   LEU A  15       7.947  -1.237  -2.770  1.00 91.65
ATOM    112  O   LEU A  15       9.166  -1.151  -2.888  1.00 91.65
ATOM    113  CB  LEU A  15       6.399  -1.196  -4.796  1.00 91.65
ATOM    114  CG  LEU A  15       5.860  -1.975  -6.012  1.00 91.65
ATOM    115  CD1 LEU A  15       4.994  -1.050  -6.861  1.00 91.65
ATOM    116  CD2 LEU A  15       6.990  -2.483  -6.907  1.00 91.65
ATOM    117  N   ALA A  16       7.277  -0.698  -1.736  1.00 89.71
ATOM    118  CA  ALA A  16       7.844   0.176  -0.700  1.00 89.71
ATOM    119  C   ALA A  16       9.049  -0.427   0.034  1.00 89.71
ATOM    120  O   ALA A  16       9.971   0.325   0.366  1.00 89.71
ATOM    121  CB  ALA A  16       6.750   0.627   0.280  1.00 89.71
ATOM    122  N   ASN A  17       9.107  -1.746   0.229  1.00 93.53
ATOM    123  CA  ASN A  17      10.296  -2.417   0.770  1.00 93.53
ATOM    124  C   ASN A  17      11.525  -2.279  -0.139  1.00 93.53
ATOM    125  O   ASN A  17      12.641  -2.134   0.358  1.00 93.53
ATOM    126  CB  ASN A  17       9.996  -3.908   0.964  1.00 93.53
ATOM    127  CG  ASN A  17       8.901  -4.143   1.971  1.00 93.53
ATOM    128  OD1 ASN A  17       7.741  -4.188   1.653  1.00 93.53
ATOM    129  ND2 ASN A  17       9.218  -4.318   3.221  1.00 93.53
ATOM    130  N   VAL A  18      11.328  -2.330  -1.458  1.00 90.59
ATOM    131  CA  VAL A  18      12.414  -2.383  -2.446  1.00 90.59
ATOM    132  C   VAL A  18      12.992  -1.003  -2.751  1.00 90.59
ATOM    133  O   VAL A  18      14.204  -0.864  -2.869  1.00 90.59
ATOM    134  CB  VAL A  18      11.963  -3.116  -3.725  1.00 90.59
ATOM    135  CG1 VAL A  18      13.081  -3.193  -4.775  1.00 90.59
ATOM    136  CG2 VAL A  18      11.550  -4.554  -3.386  1.00 90.59
ATOM    137  N   TRP A  19      12.151   0.025  -2.863  1.00 80.87
ATOM    138  CA  TRP A  19      12.561   1.373  -3.307  1.00 80.87
ATOM    139  C   TRP A  19      12.503   2.458  -2.222  1.00 80.87
ATOM    140  O   TRP A  19      13.470   3.189  -2.016  1.00 80.87
ATOM    141  CB  TRP A  19      11.728   1.764  -4.535  1.00 80.87
ATOM    142  CG  TRP A  19      10.270   2.063  -4.329  1.00 80.87
ATOM    143  CD1 TRP A  19       9.483   1.538  -3.374  1.00 80.87
ATOM    144  CD2 TRP A  19       9.396   3.011  -5.002  1.00 80.87
ATOM    145  NE1 TRP A  19       8.187   1.955  -3.490  1.00 80.87
ATOM    146  CE2 TRP A  19       8.078   2.906  -4.447  1.00 80.87
ATOM    147  CE3 TRP A  19       9.577   4.003  -5.968  1.00 80.87
ATOM    148  CZ2 TRP A  19       6.984   3.678  -4.830  1.00 80.87
ATOM    149  CZ3 TRP A  19       8.474   4.791  -6.314  1.00 80.87
ATOM    150  CH2 TRP A  19       7.194   4.650  -5.794  1.00 80.87
ATOM    151  N   ARG A  20      11.388   2.553  -1.494  1.00 88.86
ATOM    152  CA  ARG A  20      11.078   3.642  -0.572  1.00 88.86
ATOM    153  C   ARG A  20      11.887   3.487   0.701  1.00 88.86
ATOM    154  O   ARG A  20      12.492   4.453   1.144  1.00 88.86
ATOM    155  CB  ARG A  20       9.562   3.681  -0.315  1.00 88.86
ATOM    156  CG  ARG A  20       9.132   4.894   0.520  1.00 88.86
ATOM    157  CD  ARG A  20       7.618   4.861   0.761  1.00 88.86
ATOM    158  NE  ARG A  20       7.179   5.986   1.607  1.00 88.86
ATOM    159  CZ  ARG A  20       5.929   6.307   1.895  1.00 88.86
ATOM    160  NH1 ARG A  20       4.911   5.618   1.459  1.00 88.86
ATOM    161  NH2 ARG A  20       5.674   7.349   2.634  1.00 88.86
ATOM    162  N   PHE A  21      11.962   2.278   1.256  1.00 93.52
ATOM    163  CA  PHE A  21      12.744   2.034   2.464  1.00 93.52
ATOM    164  C   PHE A  21      14.234   2.379   2.288  1.00 93.52
ATOM    165  O   PHE A  21      14.729   3.177   3.084  1.00 93.52
ATOM    166  CB  PHE A  21      12.499   0.616   2.993  1.00 93.52
ATOM    167  CG  PHE A  21      13.403   0.259   4.149  1.00 93.52
ATOM    168  CD1 PHE A  21      14.677  -0.293   3.918  1.00 93.52
ATOM    169  CD2 PHE A  21      12.962   0.470   5.467  1.00 93.52
ATOM    170  CE1 PHE A  21      15.495  -0.647   5.001  1.00 93.52
ATOM    171  CE2 PHE A  21      13.786   0.121   6.549  1.00 93.52
ATOM    172  CZ  PHE A  21      15.047  -0.449   6.317  1.00 93.52
ATOM    173  N   PRO A  22      14.959   1.879   1.263  1.00 91.73
ATOM    174  CA  PRO A  22      16.369   2.230   1.082  1.00 91.73
ATOM    175  C   PRO A  22      16.588   3.729   0.878  1.00 91.73
ATOM    176  O   PRO A  22      17.511   4.302   1.458  1.00 91.73
ATOM    177  CB  PRO A  22      16.833   1.419  -0.129  1.00 91.73
ATOM    178  CG  PRO A  22      15.953   0.175  -0.010  1.00 91.73
ATOM    179  CD  PRO A  22      14.615   0.802   0.341  1.00 91.73
ATOM    180  N   TYR A  23      15.707   4.378   0.119  1.00 87.80
ATOM    181  CA  TYR A  23      15.751   5.823  -0.052  1.00 87.80
ATOM    182  C   TYR A  23      15.555   6.573   1.278  1.00 87.80
ATOM    183  O   TYR A  23      16.341   7.459   1.612  1.00 87.80
ATOM    184  CB  TYR A  23      14.696   6.232  -1.080  1.00 87.80
ATOM    185  CG  TYR A  23      14.643   7.729  -1.197  1.00 87.80
ATOM    186  CD1 TYR A  23      13.719   8.443  -0.418  1.00 87.80
ATOM    187  CD2 TYR A  23      15.618   8.405  -1.953  1.00 87.80
ATOM    188  CE1 TYR A  23      13.789   9.841  -0.372  1.00 87.80
ATOM    189  CE2 TYR A  23      15.674   9.808  -1.924  1.00 87.80
ATOM    190  CZ  TYR A  23      14.757  10.526  -1.138  1.00 87.80
ATOM    191  OH  TYR A  23      14.776  11.881  -1.169  1.00 87.80
ATOM    192  N   LEU A  24      14.552   6.191   2.077  1.00 91.08
ATOM    193  CA  LEU A  24      14.301   6.797   3.385  1.00 91.08
ATOM    194  C   LEU A  24      15.456   6.566   4.358  1.00 91.08
ATOM    195  O   LEU A  24      15.774   7.479   5.116  1.00 91.08
ATOM    196  CB  LEU A  24      12.995   6.259   3.988  1.00 91.08
ATOM    197  CG  LEU A  24      11.708   6.765   3.316  1.00 91.08
ATOM    198  CD1 LEU A  24      10.516   6.115   4.015  1.00 91.08
ATOM    199  CD2 LEU A  24      11.555   8.284   3.394  1.00 91.08
ATOM    200  N   CYS A  25      16.118   5.405   4.312  1.00 92.24
ATOM    201  CA  CYS A  25      17.370   5.200   5.033  1.00 92.24
ATOM    202  C   CYS A  25      18.400   6.249   4.616  1.00 92.24
ATOM    203  O   CYS A  25      18.911   6.953   5.478  1.00 92.24
ATOM    204  CB  CYS A  25      17.924   3.787   4.803  1.00 92.24
ATOM    205  SG  CYS A  25      16.976   2.541   5.714  1.00 92.24
ATOM    206  N   TYR A  26      18.662   6.408   3.314  1.00 88.88
ATOM    207  CA  TYR A  26      19.639   7.381   2.819  1.00 88.88
ATOM    208  C   TYR A  26      19.344   8.806   3.300  1.00 88.88
ATOM    209  O   TYR A  26      20.169   9.436   3.966  1.00 88.88
ATOM    210  CB  TYR A  26      19.659   7.416   1.282  1.00 88.88
ATOM    211  CG  TYR A  26      20.829   8.219   0.756  1.00 88.88
ATOM    212  CD1 TYR A  26      20.562   9.356  -0.026  1.00 88.88
ATOM    213  CD2 TYR A  26      22.155   7.920   1.136  1.00 88.88
ATOM    214  CE1 TYR A  26      21.612  10.200  -0.422  1.00 88.88
ATOM    215  CE2 TYR A  26      23.211   8.754   0.725  1.00 88.88
ATOM    216  CZ  TYR A  26      22.938   9.897  -0.055  1.00 88.88
ATOM    217  OH  TYR A  26      23.953  10.724  -0.412  1.00 88.88
ATOM    218  N   LYS A  27      18.134   9.284   2.988  1.00 88.38
ATOM    219  CA  LYS A  27      17.663  10.646   3.251  1.00 88.38
ATOM    220  C   LYS A  27      17.772  11.012   4.729  1.00 88.38
ATOM    221  O   LYS A  27      18.083  12.153   5.060  1.00 88.38
ATOM    222  CB  LYS A  27      16.212  10.721   2.755  1.00 88.38
ATOM    223  CG  LYS A  27      15.554  12.085   3.005  1.00 88.38
ATOM    224  CD  LYS A  27      14.098  12.027   2.548  1.00 88.38
ATOM    225  CE  LYS A  27      13.346  13.301   2.922  1.00 88.38
ATOM    226  NZ  LYS A  27      11.893  13.100   2.709  1.00 88.38
ATOM    227  N   ASN A  28      17.547  10.038   5.609  1.00 91.40
ATOM    228  CA  ASN A  28      17.459  10.231   7.051  1.00 91.40
ATOM    229  C   ASN A  28      18.726   9.784   7.809  1.00 91.40
ATOM    230  O   ASN A  28      18.650   9.412   8.980  1.00 91.40
ATOM    231  CB  ASN A  28      16.155   9.579   7.529  1.00 91.40
ATOM    232  CG  ASN A  28      14.915  10.270   6.978  1.00 91.40
ATOM    233  OD1 ASN A  28      14.801  11.482   6.994  1.00 91.40
ATOM    234  ND2 ASN A  28      13.942   9.538   6.491  1.00 91.40
ATOM    235  N   GLY A  29      19.897   9.840   7.163  1.00 89.11
ATOM    236  CA  GLY A  29      21.192   9.605   7.819  1.00 89.11
ATOM    237  C   GLY A  29      21.682   8.158   7.773  1.00 89.11
ATOM    238  O   GLY A  29      22.353   7.711   8.706  1.00 89.11
ATOM    239  N   GLY A  30      21.311   7.423   6.723  1.00 89.74
ATOM    240  CA  GLY A  30      21.704   6.039   6.464  1.00 89.74
ATOM    241  C   GLY A  30      21.190   5.068   7.528  1.00 89.74
ATOM    242  O   GLY A  30      19.988   4.946   7.783  1.00 89.74
ATOM    243  N   GLY A  31      22.120   4.384   8.187  1.00 90.67
ATOM    244  CA  GLY A  31      21.859   3.453   9.277  1.00 90.67
ATOM    245  C   GLY A  31      21.217   4.103  10.506  1.00 90.67
ATOM    246  O   GLY A  31      20.590   3.391  11.289  1.00 90.67
ATOM    247  N   ALA A  32      21.290   5.433  10.668  1.00 93.86
ATOM    248  CA  ALA A  32      20.596   6.131  11.755  1.00 93.86
ATOM    249  C   ALA A  32      19.074   5.918  11.690  1.00 93.86
ATOM    250  O   ALA A  32      18.453   5.668  12.721  1.00 93.86
ATOM    251  CB  ALA A  32      20.955   7.621  11.718  1.00 93.86
ATOM    252  N   PHE A  33      18.486   5.900  10.487  1.00 95.24
ATOM    253  CA  PHE A  33      17.053   5.661  10.267  1.00 95.24
ATOM    254  C   PHE A  33      16.574   4.283  10.755  1.00 95.24
ATOM    255  O   PHE A  33      15.403   4.112  11.099  1.00 95.24
ATOM    256  CB  PHE A  33      16.777   5.790   8.768  1.00 95.24
ATOM    257  CG  PHE A  33      15.316   5.637   8.385  1.00 95.24
ATOM    258  CD1 PHE A  33      14.837   4.419   7.865  1.00 95.24
ATOM    259  CD2 PHE A  33      14.425   6.711   8.558  1.00 95.24
ATOM    260  CE1 PHE A  33      13.496   4.294   7.464  1.00 95.24
ATOM    261  CE2 PHE A  33      13.086   6.590   8.154  1.00 95.24
ATOM    262  CZ  PHE A  33      12.624   5.387   7.593  1.00 95.24
ATOM    263  N   LEU A  34      17.470   3.293  10.841  1.00 94.36
ATOM    264  CA  LEU A  34      17.122   1.960  11.341  1.00 94.36
ATOM    265  C   LEU A  34      16.715   1.991  12.818  1.00 94.36
ATOM    266  O   LEU A  34      15.910   1.163  13.234  1.00 94.36
ATOM    267  CB  LEU A  34      18.288   0.981  11.125  1.00 94.36
ATOM    268  CG  LEU A  34      18.704   0.791   9.656  1.00 94.36
ATOM    269  CD1 LEU A  34      19.930  -0.117   9.580  1.00 94.36
ATOM    270  CD2 LEU A  34      17.591   0.155   8.822  1.00 94.36
ATOM    271  N   VAL A  35      17.218   2.949  13.605  1.00 94.74
ATOM    272  CA  VAL A  35      16.865   3.097  15.025  1.00 94.74
ATOM    273  C   VAL A  35      15.373   3.423  15.204  1.00 94.74
ATOM    274  O   VAL A  35      14.679   2.612  15.827  1.00 94.74
ATOM    275  CB  VAL A  35      17.786   4.104  15.748  1.00 94.74
ATOM    276  CG1 VAL A  35      17.395   4.263  17.223  1.00 94.74
ATOM    277  CG2 VAL A  35      19.252   3.655  15.687  1.00 94.74
ATOM    278  N   PRO A  36      14.828   4.535  14.662  1.00 94.37
ATOM    279  CA  PRO A  36      13.402   4.822  14.768  1.00 94.37
ATOM    280  C   PRO A  36      12.543   3.794  14.021  1.00 94.37
ATOM    281  O   PRO A  36      11.480   3.438  14.526  1.00 94.37
ATOM    282  CB  PRO A  36      13.223   6.243  14.226  1.00 94.37
ATOM    283  CG  PRO A  36      14.387   6.421  13.263  1.00 94.37
ATOM    284  CD  PRO A  36      15.489   5.621  13.949  1.00 94.37
ATOM    285  N   TYR A  37      13.001   3.255  12.881  1.00 95.76
ATOM    286  CA  TYR A  37      12.276   2.208  12.149  1.00 95.76
ATOM    287  C   TYR A  37      12.081   0.940  12.991  1.00 95.76
ATOM    288  O   TYR A  37      10.952   0.480  13.154  1.00 95.76
ATOM    289  CB  TYR A  37      13.002   1.893  10.834  1.00 95.76
ATOM    290  CG  TYR A  37      12.407   0.722  10.072  1.00 95.76
ATOM    291  CD1 TYR A  37      12.934  -0.573  10.247  1.00 95.76
ATOM    292  CD2 TYR A  37      11.308   0.920   9.214  1.00 95.76
ATOM    293  CE1 TYR A  37      12.353  -1.670   9.582  1.00 95.76
ATOM    294  CE2 TYR A  37      10.724  -0.176   8.544  1.00 95.76
ATOM    295  CZ  TYR A  37      11.241  -1.477   8.737  1.00 95.76
ATOM    296  OH  TYR A  37      10.662  -2.553   8.135  1.00 95.76
ATOM    297  N   LEU A  38      13.154   0.388  13.570  1.00 96.17
ATOM    298  CA  LEU A  38      13.079  -0.819  14.400  1.00 96.17
ATOM    299  C   LEU A  38      12.316  -0.562  15.699  1.00 96.17
ATOM    300  O   LEU A  38      11.533  -1.409  16.126  1.00 96.17
ATOM    301  CB  LEU A  38      14.491  -1.338  14.720  1.00 96.17
ATOM    302  CG  LEU A  38      15.245  -1.945  13.524  1.00 96.17
ATOM    303  CD1 LEU A  38      16.677  -2.271  13.949  1.00 96.17
ATOM    304  CD2 LEU A  38      14.587  -3.231  13.017  1.00 96.17
ATOM    305  N   LEU A  39      12.501   0.610  16.313  1.00 95.10
ATOM    306  CA  LEU A  39      11.751   0.978  17.507  1.00 95.10
ATOM    307  C   LEU A  39      10.249   1.020  17.208  1.00 95.10
ATOM    308  O   LEU A  39       9.481   0.378  17.921  1.00 95.10
ATOM    309  CB  LEU A  39      12.286   2.309  18.057  1.00 95.10
ATOM    310  CG  LEU A  39      11.547   2.814  19.310  1.00 95.10
ATOM    311  CD1 LEU A  39      11.573   1.813  20.467  1.00 95.10
ATOM    312  CD2 LEU A  39      12.208   4.091  19.819  1.00 95.10
ATOM    313  N   PHE A  40       9.834   1.703  16.138  1.00 94.03
ATOM    314  CA  PHE A  40       8.429   1.783  15.748  1.00 94.03
ATOM    315  C   PHE A  40       7.866   0.427  15.300  1.00 94.03
ATOM    316  O   PHE A  40       6.732   0.090  15.642  1.00 94.03
ATOM    317  CB  PHE A  40       8.246   2.866  14.689  1.00 94.03
ATOM    318  CG  PHE A  40       6.784   3.155  14.431  1.00 94.03
ATOM    319  CD1 PHE A  40       6.153   2.571  13.332  1.00 94.03
ATOM    320  CD2 PHE A  40       6.026   3.923  15.324  1.00 94.03
ATOM    321  CE1 PHE A  40       4.805   2.837  13.039  1.00 94.03
ATOM    322  CE2 PHE A  40       4.662   4.156  15.058  1.00 94.03
ATOM    323  CZ  PHE A  40       4.062   3.656  13.896  1.00 94.03
ATOM    324  N   MET A  41       8.669  -0.396  14.621  1.00 96.64
ATOM    325  CA  MET A  41       8.318  -1.776  14.280  1.00 96.64
ATOM    326  C   MET A  41       7.974  -2.595  15.532  1.00 96.64
ATOM    327  O   MET A  41       6.966  -3.297  15.547  1.00 96.64
ATOM    328  CB  MET A  41       9.474  -2.414  13.490  1.00 96.64
ATOM    329  CG  MET A  41       9.175  -3.845  13.033  1.00 96.64
ATOM    330  SD  MET A  41       7.683  -4.011  12.023  1.00 96.64
ATOM    331  CE  MET A  41       8.235  -3.339  10.429  1.00 96.64
ATOM    332  N   VAL A  42       8.761  -2.469  16.603  1.00 96.74
ATOM    333  CA  VAL A  42       8.516  -3.166  17.873  1.00 96.74
ATOM    334  C   VAL A  42       7.311  -2.566  18.603  1.00 96.74
ATOM    335  O   VAL A  42       6.385  -3.290  18.939  1.00 96.74
ATOM    336  CB  VAL A  42       9.800  -3.182  18.729  1.00 96.74
ATOM    337  CG1 VAL A  42       9.604  -3.736  20.145  1.00 96.74
ATOM    338  CG2 VAL A  42      10.869  -4.065  18.066  1.00 96.74
ATOM    339  N   ILE A  43       7.255  -1.252  18.829  1.00 94.63
ATOM    340  CA  ILE A  43       6.238  -0.665  19.723  1.00 94.63
ATOM    341  C   ILE A  43       4.868  -0.429  19.075  1.00 94.63
ATOM    342  O   ILE A  43       3.885  -0.241  19.792  1.00 94.63
ATOM    343  CB  ILE A  43       6.744   0.631  20.384  1.00 94.63
ATOM    344  CG1 ILE A  43       6.830   1.791  19.368  1.00 94.63
ATOM    345  CG2 ILE A  43       8.052   0.360  21.149  1.00 94.63
ATOM    346  CD1 ILE A  43       7.381   3.111  19.912  1.00 94.63
ATOM    347  N   ALA A  44       4.788  -0.389  17.745  1.00 94.35
ATOM    348  CA  ALA A  44       3.562  -0.070  17.019  1.00 94.35
ATOM    349  C   ALA A  44       3.307  -1.039  15.865  1.00 94.35
ATOM    350  O   ALA A  44       2.278  -1.706  15.883  1.00 94.35
ATOM    351  CB  ALA A  44       3.616   1.389  16.561  1.00 94.35
ATOM    352  N   GLY A  45       4.240  -1.182  14.920  1.00 96.53
ATOM    353  CA  GLY A  45       4.044  -1.993  13.713  1.00 96.53
ATOM    354  C   GLY A  45       3.581  -3.418  14.014  1.00 96.53
ATOM    355  O   GLY A  45       2.457  -3.796  13.697  1.00 96.53
ATOM    356  N   MET A  46       4.418  -4.199  14.693  1.00 97.79
ATOM    357  CA  MET A  46       4.137  -5.595  15.020  1.00 97.79
ATOM    358  C   MET A  46       2.945  -5.771  15.983  1.00 97.79
ATOM    359  O   MET A  46       2.119  -6.653  15.731  1.00 97.79
ATOM    360  CB  MET A  46       5.448  -6.240  15.494  1.00 97.79
ATOM    361  CG  MET A  46       5.341  -7.718  15.870  1.00 97.79
ATOM    362  SD  MET A  46       6.803  -8.303  16.775  1.00 97.79
ATOM    363  CE  MET A  46       8.060  -8.275  15.469  1.00 97.79
ATOM    364  N   PRO A  47       2.778  -4.963  17.053  1.00 97.96
ATOM    365  CA  PRO A  47       1.573  -5.000  17.876  1.00 97.96
ATOM    366  C   PRO A  47       0.294  -4.741  17.090  1.00 97.96
ATOM    367  O   PRO A  47      -0.637  -5.537  17.196  1.00 97.96
ATOM    368  CB  PRO A  47       1.791  -3.978  18.996  1.00 97.96
ATOM    369  CG  PRO A  47       3.307  -3.982  19.156  1.00 97.96
ATOM    370  CD  PRO A  47       3.796  -4.167  17.722  1.00 97.96
ATOM    371  N   LEU A  48       0.224  -3.671  16.303  1.00 97.59
ATOM    372  CA  LEU A  48      -0.988  -3.319  15.561  1.00 97.59
ATOM    373  C   LEU A  48      -1.294  -4.346  14.470  1.00 97.59
ATOM    374  O   LEU A  48      -2.442  -4.743  14.309  1.00 97.59
ATOM    375  CB  LEU A  48      -0.826  -1.915  14.975  1.00 97.59
ATOM    376  CG  LEU A  48      -0.705  -0.815  16.042  1.00 97.59
ATOM    377  CD1 LEU A  48      -0.206   0.464  15.387  1.00 97.59
ATOM    378  CD2 LEU A  48      -2.041  -0.538  16.732  1.00 97.59
ATOM    379  N   PHE A  49      -0.262  -4.887  13.825  1.00 98.28
ATOM    380  CA  PHE A  49      -0.400  -6.010  12.906  1.00 98.28
ATOM    381  C   PHE A  49      -1.042  -7.231  13.579  1.00 98.28
ATOM    382  O   PHE A  49      -1.991  -7.820  13.063  1.00 98.28
ATOM    383  CB  PHE A  49       0.994  -6.354  12.385  1.00 98.28
ATOM    384  CG  PHE A  49       0.985  -7.251  11.181  1.00 98.28
ATOM    385  CD1 PHE A  49       0.876  -8.647  11.307  1.00 98.28
ATOM    386  CD2 PHE A  49       1.102  -6.659   9.917  1.00 98.28
ATOM    387  CE1 PHE A  49       0.923  -9.446  10.153  1.00 98.28
ATOM    388  CE2 PHE A  49       1.144  -7.453   8.768  1.00 98.28
ATOM    389  CZ  PHE A  49       1.054  -8.842   8.894  1.00 98.28
ATOM    390  N   TYR A  50      -0.557  -7.606  14.769  1.00 98.43
ATOM    391  CA  TYR A  50      -1.140  -8.708  15.533  1.00 98.43
ATOM    392  C   TYR A  50      -2.583  -8.408  15.967  1.00 98.43
ATOM    393  O   TYR A  50      -3.432  -9.299  15.924  1.00 98.43
ATOM    394  CB  TYR A  50      -0.248  -9.038  16.742  1.00 98.43
ATOM    395  CG  TYR A  50      -0.749 -10.170  17.628  1.00 98.43
ATOM    396  CD1 TYR A  50      -0.517 -10.125  19.018  1.00 98.43
ATOM    397  CD2 TYR A  50      -1.442 -11.268  17.078  1.00 98.43
ATOM    398  CE1 TYR A  50      -1.007 -11.142  19.859  1.00 98.43
ATOM    399  CE2 TYR A  50      -1.938 -12.280  17.914  1.00 98.43
ATOM    400  CZ  TYR A  50      -1.723 -12.221  19.300  1.00 98.43
ATOM    401  OH  TYR A  50      -2.162 -13.240  20.078  1.00 98.43
ATOM    402  N   MET A  51      -2.869  -7.160  16.345  1.00 98.23
ATOM    403  CA  MET A  51      -4.215  -6.708  16.690  1.00 98.23
ATOM    404  C   MET A  51      -5.176  -6.900  15.515  1.00 98.23
ATOM    405  O   MET A  51      -6.195  -7.557  15.698  1.00 98.23
ATOM    406  CB  MET A  51      -4.170  -5.242  17.133  1.00 98.23
ATOM    407  CG  MET A  51      -5.502  -4.720  17.670  1.00 98.23
ATOM    408  SD  MET A  51      -5.456  -2.950  18.064  1.00 98.23
ATOM    409  CE  MET A  51      -5.393  -2.266  16.377  1.00 98.23
ATOM    410  N   GLU A  52      -4.842  -6.425  14.314  1.00 98.24
ATOM    411  CA  GLU A  52      -5.696  -6.584  13.129  1.00 98.24
ATOM    412  C   GLU A  52      -5.932  -8.053  12.762  1.00 98.24
ATOM    413  O   GLU A  52      -7.067  -8.456  12.494  1.00 98.24
ATOM    414  CB  GLU A  52      -5.079  -5.876  11.918  1.00 98.24
ATOM    415  CG  GLU A  52      -5.418  -4.389  11.906  1.00 98.24
ATOM    416  CD  GLU A  52      -5.019  -3.696  10.597  1.00 98.24
ATOM    417  OE1 GLU A  52      -4.374  -2.631  10.662  1.00 98.24
ATOM    418  OE2 GLU A  52      -5.310  -4.250   9.506  1.00 98.24
ATOM    419  N   LEU A  53      -4.880  -8.882  12.803  1.00 98.44
ATOM    420  CA  LEU A  53      -5.010 -10.313  12.527  1.00 98.44
ATOM    421  C   LEU A  53      -5.920 -11.020  13.536  1.00 98.44
ATOM    422  O   LEU A  53      -6.738 -11.860  13.161  1.00 98.44
ATOM    423  CB  LEU A  53      -3.631 -10.994  12.538  1.00 98.44
ATOM    424  CG  LEU A  53      -2.685 -10.678  11.367  1.00 98.44
ATOM    425  CD1 LEU A  53      -1.502 -11.645  11.463  1.00 98.44
ATOM    426  CD2 LEU A  53      -3.348 -10.888  10.010  1.00 98.44
ATOM    427  N   ALA A  54      -5.774 -10.719  14.826  1.00 98.41
ATOM    428  CA  ALA A  54      -6.635 -11.284  15.858  1.00 98.41
ATOM    429  C   ALA A  54      -8.074 -10.768  15.726  1.00 98.41
ATOM    430  O   ALA A  54      -9.025 -11.536  15.879  1.00 98.41
ATOM    431  CB  ALA A  54      -6.031 -10.955  17.225  1.00 98.41
ATOM    432  N   LEU A  55      -8.230  -9.487  15.402  1.00 98.02
ATOM    433  CA  LEU A  55      -9.516  -8.830  15.275  1.00 98.02
ATOM    434  C   LEU A  55     -10.342  -9.416  14.118  1.00 98.02
ATOM    435  O   LEU A  55     -11.506  -9.774  14.326  1.00 98.02
ATOM    436  CB  LEU A  55      -9.250  -7.315  15.153  1.00 98.02
ATOM    437  CG  LEU A  55     -10.531  -6.495  15.056  1.00 98.02
ATOM    438  CD1 LEU A  55     -11.344  -6.543  16.349  1.00 98.02
ATOM    439  CD2 LEU A  55     -10.272  -5.043  14.675  1.00 98.02
ATOM    440  N   GLY A  56      -9.743  -9.581  12.936  1.00 97.87
ATOM    441  CA  GLY A  56     -10.403 -10.211  11.791  1.00 97.87
ATOM    442  C   GLY A  56     -10.671 -11.701  12.010  1.00 97.87
ATOM    443  O   GLY A  56     -11.786 -12.164  11.761  1.00 97.87
ATOM    444  N   GLN A  57      -9.709 -12.454  12.559  1.00 97.77
ATOM    445  CA  GLN A  57      -9.866 -13.896  12.798  1.00 97.77
ATOM    446  C   GLN A  57     -10.959 -14.225  13.825  1.00 97.77
ATOM    447  O   GLN A  57     -11.704 -15.188  13.629  1.00 97.77
ATOM    448  CB  GLN A  57      -8.520 -14.497  13.227  1.00 97.77
ATOM    449  CG  GLN A  57      -8.569 -16.028  13.320  1.00 97.77
ATOM    450  CD  GLN A  57      -7.195 -16.608  13.619  1.00 97.77
ATOM    451  OE1 GLN A  57      -6.273 -16.554  12.813  1.00 97.77
ATOM    452  NE2 GLN A  57      -7.017 -17.204  14.777  1.00 97.77
ATOM    453  N   PHE A  58     -11.072 -13.443  14.903  1.00 97.37
ATOM    454  CA  PHE A  58     -12.074 -13.684  15.942  1.00 97.37
ATOM    455  C   PHE A  58     -13.489 -13.424  15.432  1.00 97.37
ATOM    456  O   PHE A  58     -14.395 -14.228  15.649  1.00 97.37
ATOM    457  CB  PHE A  58     -11.793 -12.794  17.159  1.00 97.37
ATOM    458  CG  PHE A  58     -12.731 -13.075  18.314  1.00 97.37
ATOM    459  CD1 PHE A  58     -13.824 -12.226  18.566  1.00 97.37
ATOM    460  CD2 PHE A  58     -12.526 -14.206  19.126  1.00 97.37
ATOM    461  CE1 PHE A  58     -14.697 -12.499  19.633  1.00 97.37
ATOM    462  CE2 PHE A  58     -13.391 -14.473  20.200  1.00 97.37
ATOM    463  CZ  PHE A  58     -14.476 -13.619  20.456  1.00 97.37
ATOM    464  N   ASN A  59     -13.676 -12.298  14.741  1.00 96.13
ATOM    465  CA  ASN A  59     -14.995 -11.846  14.312  1.00 96.13
ATOM    466  C   ASN A  59     -15.458 -12.474  12.996  1.00 96.13
ATOM    467  O   ASN A  59     -16.664 -12.475  12.747  1.00 96.13
ATOM    468  CB  ASN A  59     -14.982 -10.319  14.228  1.00 96.13
ATOM    469  CG  ASN A  59     -14.910  -9.697  15.608  1.00 96.13
ATOM    470  OD1 ASN A  59     -15.872  -9.717  16.361  1.00 96.13
ATOM    471  ND2 ASN A  59     -13.771  -9.181  15.998  1.00 96.13
ATOM    472  N   ARG A  60     -14.520 -12.994  12.190  1.00 95.78
ATOM    473  CA  ARG A  60     -14.736 -13.551  10.844  1.00 95.78
ATOM    474  C   ARG A  60     -15.499 -12.605   9.918  1.00 95.78
ATOM    475  O   ARG A  60     -16.331 -13.041   9.125  1.00 95.78
ATOM    476  CB  ARG A  60     -15.341 -14.959  10.912  1.00 95.78
ATOM    477  CG  ARG A  60     -14.442 -15.933  11.688  1.00 95.78
ATOM    478  CD  ARG A  60     -14.854 -17.385  11.428  1.00 95.78
ATOM    479  NE  ARG A  60     -14.531 -17.788  10.044  1.00 95.78
ATOM    480  CZ  ARG A  60     -14.832 -18.930   9.456  1.00 95.78
ATOM    481  NH1 ARG A  60     -15.385 -19.909  10.114  1.00 95.78
ATOM    482  NH2 ARG A  60     -14.599 -19.095   8.184  1.00 95.78
ATOM    483  N   GLU A  61     -15.170 -11.322  10.007  1.00 95.15
ATOM    484  CA  GLU A  61     -15.758 -10.228   9.233  1.00 95.15
ATOM    485  C   GLU A  61     -14.668  -9.291   8.706  1.00 95.15
ATOM    486  O   GLU A  61     -13.567  -9.222   9.255  1.00 95.15
ATOM    487  CB  GLU A  61     -16.773  -9.464  10.091  1.00 95.15
ATOM    488  CG  GLU A  61     -18.094 -10.244  10.200  1.00 95.15
ATOM    489  CD  GLU A  61     -19.076  -9.620  11.190  1.00 95.15
ATOM    490  OE1 GLU A  61     -20.012 -10.329  11.627  1.00 95.15
ATOM    491  OE2 GLU A  61     -18.809  -8.511  11.686  1.00 95.15
ATOM    492  N   GLY A  62     -14.984  -8.575   7.632  1.00 95.71
ATOM    493  CA  GLY A  62     -14.161  -7.538   7.039  1.00 95.71
ATOM    494  C   GLY A  62     -14.124  -6.258   7.863  1.00 95.71
ATOM    495  O   GLY A  62     -14.766  -6.123   8.907  1.00 95.71
ATOM    496  N   ALA A  63     -13.392  -5.280   7.336  1.00 96.00
ATOM    497  CA  ALA A  63     -13.049  -4.054   8.045  1.00 96.00
ATOM    498  C   ALA A  63     -14.245  -3.244   8.575  1.00 96.00
ATOM    499  O   ALA A  63     -14.104  -2.596   9.604  1.00 96.00
ATOM    500  CB  ALA A  63     -12.200  -3.209   7.100  1.00 96.00
ATOM    501  N   ALA A  64     -15.414  -3.276   7.920  1.00 96.34
ATOM    502  CA  ALA A  64     -16.628  -2.614   8.414  1.00 96.34
ATOM    503  C   ALA A  64     -17.411  -3.464   9.427  1.00 96.34
ATOM    504  O   ALA A  64     -17.765  -2.962  10.495  1.00 96.34
ATOM    505  CB  ALA A  64     -17.493  -2.182   7.226  1.00 96.34
ATOM    506  N   GLY A  65     -17.663  -4.741   9.120  1.00 95.15
ATOM    507  CA  GLY A  65     -18.463  -5.631   9.974  1.00 95.15
ATOM    508  C   GLY A  65     -17.860  -5.816  11.367  1.00 95.15
ATOM    509  O   GLY A  65     -18.559  -5.726  12.379  1.00 95.15
ATOM    510  N   VAL A  66     -16.529  -5.917  11.432  1.00 97.08
ATOM    511  CA  VAL A  66     -15.773  -6.169  12.664  1.00 97.08
ATOM    512  C   VAL A  66     -16.059  -5.180  13.801  1.00 97.08
ATOM    513  O   VAL A  66     -15.939  -5.523  14.978  1.00 97.08
ATOM    514  CB  VAL A  66     -14.286  -6.203  12.296  1.00 97.08
ATOM    515  CG1 VAL A  66     -13.673  -4.821  12.056  1.00 97.08
ATOM    516  CG2 VAL A  66     -13.494  -6.926  13.357  1.00 97.08
ATOM    517  N   TRP A  67     -16.531  -3.975  13.474  1.00 97.53
ATOM    518  CA  TRP A  67     -16.942  -2.949  14.430  1.00 97.53
ATOM    519  C   TRP A  67     -18.274  -3.226  15.138  1.00 97.53
ATOM    520  O   TRP A  67     -18.722  -2.401  15.931  1.00 97.53
ATOM    521  CB  TRP A  67     -16.918  -1.586  13.753  1.00 97.53
ATOM    522  CG  TRP A  67     -15.539  -1.139  13.411  1.00 97.53
ATOM    523  CD1 TRP A  67     -14.954  -1.223  12.199  1.00 97.53
ATOM    524  CD2 TRP A  67     -14.520  -0.631  14.314  1.00 97.53
ATOM    525  NE1 TRP A  67     -13.631  -0.839  12.295  1.00 97.53
ATOM    526  CE2 TRP A  67     -13.307  -0.471  13.585  1.00 97.53
ATOM    527  CE3 TRP A  67     -14.500  -0.340  15.693  1.00 97.53
ATOM    528  CZ2 TRP A  67     -12.123  -0.050  14.202  1.00 97.53
ATOM    529  CZ3 TRP A  67     -13.321   0.101  16.319  1.00 97.53
ATOM    530  CH2 TRP A  67     -12.135   0.241  15.579  1.00 97.53
ATOM    531  N   LYS A  68     -18.872  -4.415  14.986  1.00 96.03
ATOM    532  CA  LYS A  68     -19.876  -4.932  15.937  1.00 96.03
ATOM    533  C   LYS A  68     -19.360  -4.982  17.382  1.00 96.03
ATOM    534  O   LYS A  68     -20.152  -5.027  18.320  1.00 96.03
ATOM    535  CB  LYS A  68     -20.373  -6.311  15.475  1.00 96.03
ATOM    536  CG  LYS A  68     -19.293  -7.405  15.536  1.00 96.03
ATOM    537  CD  LYS A  68     -19.837  -8.726  14.987  1.00 96.03
ATOM    538  CE  LYS A  68     -18.703  -9.749  14.874  1.00 96.03
ATOM    539  NZ  LYS A  68     -19.134 -10.938  14.101  1.00 96.03
ATOM    540  N   ILE A  69     -18.040  -4.940  17.577  1.00 96.58
ATOM    541  CA  ILE A  69     -17.408  -4.781  18.894  1.00 96.58
ATOM    542  C   ILE A  69     -17.635  -3.393  19.520  1.00 96.58
ATOM    543  O   ILE A  69     -17.548  -3.258  20.735  1.00 96.58
ATOM    544  CB  ILE A  69     -15.896  -5.079  18.808  1.00 96.58
ATOM    545  CG1 ILE A  69     -15.127  -4.000  18.010  1.00 96.58
ATOM    546  CG2 ILE A  69     -15.650  -6.517  18.312  1.00 96.58
ATOM    547  CD1 ILE A  69     -13.611  -4.159  18.070  1.00 96.58
ATOM    548  N   CYS A  70     -17.889  -2.366  18.705  1.00 96.68
ATOM    549  CA  CYS A  70     -18.124  -0.985  19.124  1.00 96.68
ATOM    550  C   CYS A  70     -18.905  -0.247  18.015  1.00 96.68
ATOM    551  O   CYS A  70     -18.300   0.403  17.155  1.00 96.68
ATOM    552  CB  CYS A  70     -16.775  -0.317  19.424  1.00 96.68
ATOM    553  SG  CYS A  70     -17.082   1.327  20.129  1.00 96.68
ATOM    554  N   PRO A  71     -20.248  -0.358  17.993  1.00 96.73
ATOM    555  CA  PRO A  71     -21.071   0.078  16.864  1.00 96.73
ATOM    556  C   PRO A  71     -20.920   1.549  16.455  1.00 96.73
ATOM    557  O   PRO A  71     -21.111   1.869  15.283  1.00 96.73
ATOM    558  CB  PRO A  71     -22.511  -0.227  17.285  1.00 96.73
ATOM    559  CG  PRO A  71     -22.359  -1.430  18.207  1.00 96.73
ATOM    560  CD  PRO A  71     -21.048  -1.143  18.926  1.00 96.73
ATOM    561  N   ILE A  72     -20.589   2.454  17.381  1.00 96.81
ATOM    562  CA  ILE A  72     -20.356   3.879  17.093  1.00 96.81
ATOM    563  C   ILE A  72     -19.113   4.106  16.224  1.00 96.81
ATOM    564  O   ILE A  72     -19.060   5.077  15.474  1.00 96.81
ATOM    565  CB  ILE A  72     -20.286   4.683  18.412  1.00 96.81
ATOM    566  CG1 ILE A  72     -20.526   6.185  18.158  1.00 96.81
ATOM    567  CG2 ILE A  72     -18.979   4.449  19.182  1.00 96.81
ATOM    568  CD1 ILE A  72     -20.706   7.019  19.434  1.00 96.81
ATOM    569  N   LEU A  73     -18.136   3.196  16.286  1.00 97.42
ATOM    570  CA  LEU A  73     -16.862   3.281  15.570  1.00 97.42
ATOM    571  C   LEU A  73     -16.866   2.540  14.230  1.00 97.42
ATOM    572  O   LEU A  73     -15.830   2.459  13.582  1.00 97.42
ATOM    573  CB  LEU A  73     -15.716   2.807  16.481  1.00 97.42
ATOM    574  CG  LEU A  73     -15.442   3.691  17.706  1.00 97.42
ATOM    575  CD1 LEU A  73     -14.247   3.130  18.470  1.00 97.42
ATOM    576  CD2 LEU A  73     -15.129   5.144  17.342  1.00 97.42
ATOM    577  N   LYS A  74     -18.018   2.065  13.741  1.00 97.18
ATOM    578  CA  LYS A  74     -18.102   1.416  12.418  1.00 97.18
ATOM    579  C   LYS A  74     -17.596   2.292  11.268  1.00 97.18
ATOM    580  O   LYS A  74     -17.114   1.773  10.265  1.00 97.18
ATOM    581  CB  LYS A  74     -19.542   0.981  12.160  1.00 97.18
ATOM    582  CG  LYS A  74     -19.635  -0.114  11.099  1.00 97.18
ATOM    583  CD  LYS A  74     -21.090  -0.508  10.863  1.00 97.18
ATOM    584  CE  LYS A  74     -21.118  -1.812  10.085  1.00 97.18
ATOM    585  NZ  LYS A  74     -22.479  -2.378   9.998  1.00 97.18
ATOM    586  N   GLY A  75     -17.649   3.615  11.436  1.00 97.41
ATOM    587  CA  GLY A  75     -17.044   4.571  10.512  1.00 97.41
ATOM    588  C   GLY A  75     -15.551   4.331  10.266  1.00 97.41
ATOM    589  O   GLY A  75     -15.100   4.572   9.156  1.00 97.41
ATOM    590  N   VAL A  76     -14.810   3.773  11.233  1.00 97.60
ATOM    591  CA  VAL A  76     -13.390   3.405  11.072  1.00 97.60
ATOM    592  C   VAL A  76     -13.222   2.347   9.986  1.00 97.60
ATOM    593  O   VAL A  76     -12.345   2.460   9.136  1.00 97.60
ATOM    594  CB  VAL A  76     -12.806   2.872  12.394  1.00 97.60
ATOM    595  CG1 VAL A  76     -11.321   2.512  12.253  1.00 97.60
ATOM    596  CG2 VAL A  76     -12.921   3.895  13.525  1.00 97.60
ATOM    597  N   GLY A  77     -14.113   1.356   9.954  1.00 97.32
ATOM    598  CA  GLY A  77     -14.132   0.346   8.904  1.00 97.32
ATOM    599  C   GLY A  77     -14.369   0.932   7.513  1.00 97.32
ATOM    600  O   GLY A  77     -13.685   0.572   6.560  1.00 97.32
ATOM    601  N   PHE A  78     -15.291   1.890   7.394  1.00 97.23
ATOM    602  CA  PHE A  78     -15.510   2.607   6.135  1.00 97.23
ATOM    603  C   PHE A  78     -14.341   3.531   5.767  1.00 97.23
ATOM    604  O   PHE A  78     -14.023   3.645   4.585  1.00 97.23
ATOM    605  CB  PHE A  78     -16.833   3.377   6.189  1.00 97.23
ATOM    606  CG  PHE A  78     -18.057   2.482   6.172  1.00 97.23
ATOM    607  CD1 PHE A  78     -18.369   1.743   5.014  1.00 97.23
ATOM    608  CD2 PHE A  78     -18.887   2.387   7.305  1.00 97.23
ATOM    609  CE1 PHE A  78     -19.507   0.917   4.987  1.00 97.23
ATOM    610  CE2 PHE A  78     -20.029   1.568   7.275  1.00 97.23
ATOM    611  CZ  PHE A  78     -20.339   0.835   6.117  1.00 97.23
ATOM    612  N   THR A  79     -13.664   4.137   6.748  1.00 96.73
ATOM    613  CA  THR A  79     -12.433   4.910   6.533  1.00 96.73
ATOM    614  C   THR A  79     -11.358   4.049   5.876  1.00 96.73
ATOM    615  O   THR A  79     -10.857   4.427   4.820  1.00 96.73
ATOM    616  CB  THR A  79     -11.904   5.511   7.849  1.00 96.73
ATOM    617  OG1 THR A  79     -12.814   6.450   8.358  1.00 96.73
ATOM    618  CG2 THR A  79     -10.575   6.248   7.702  1.00 96.73
ATOM    619  N   VAL A  80     -11.038   2.874   6.431  1.00 95.34
ATOM    620  CA  VAL A  80      -9.972   2.013   5.879  1.00 95.34
ATOM    621  C   VAL A  80     -10.346   1.396   4.525  1.00 95.34
ATOM    622  O   VAL A  80      -9.480   1.228   3.666  1.00 95.34
ATOM    623  CB  VAL A  80      -9.506   0.937   6.877  1.00 95.34
ATOM    624  CG1 VAL A  80      -9.030   1.557   8.197  1.00 95.34
ATOM    625  CG2 VAL A  80     -10.579  -0.094   7.210  1.00 95.34
ATOM    626  N   ILE A  81     -11.638   1.126   4.286  1.00 96.27
ATOM    627  CA  ILE A  81     -12.147   0.716   2.965  1.00 96.27
ATOM    628  C   ILE A  81     -11.929   1.837   1.943  1.00 96.27
ATOM    629  O   ILE A  81     -11.429   1.578   0.850  1.00 96.27
ATOM    630  CB  ILE A  81     -13.639   0.306   3.054  1.00 96.27
ATOM    631  CG1 ILE A  81     -13.779  -1.042   3.796  1.00 96.27
ATOM    632  CG2 ILE A  81     -14.298   0.194   1.665  1.00 96.27
ATOM    633  CD1 ILE A  81     -15.220  -1.357   4.222  1.00 96.27
ATOM    634  N   LEU A  82     -12.270   3.082   2.285  1.00 95.25
ATOM    635  CA  LEU A  82     -12.125   4.208   1.364  1.00 95.25
ATOM    636  C   LEU A  82     -10.653   4.529   1.078  1.00 95.25
ATOM    637  O   LEU A  82     -10.299   4.772  -0.071  1.00 95.25
ATOM    638  CB  LEU A  82     -12.889   5.424   1.916  1.00 95.25
ATOM    639  CG  LEU A  82     -13.037   6.566   0.893  1.00 95.25
ATOM    640  CD1 LEU A  82     -13.854   6.149  -0.333  1.00 95.25
ATOM    641  CD2 LEU A  82     -13.737   7.759   1.542  1.00 95.25
ATOM    642  N   ILE A  83      -9.789   4.457   2.092  1.00 93.72
ATOM    643  CA  ILE A  83      -8.335   4.595   1.931  1.00 93.72
ATOM    644  C   ILE A  83      -7.790   3.518   0.986  1.00 93.72
ATOM    645  O   ILE A  83      -7.069   3.838   0.043  1.00 93.72
ATOM    646  CB  ILE A  83      -7.653   4.529   3.313  1.00 93.72
ATOM    647  CG1 ILE A  83      -7.964   5.806   4.125  1.00 93.72
ATOM    648  CG2 ILE A  83      -6.132   4.350   3.197  1.00 93.72
ATOM    649  CD1 ILE A  83      -7.584   5.699   5.606  1.00 93.72
ATOM    650  N   SER A  84      -8.164   2.252   1.193  1.00 94.41
ATOM    651  CA  SER A  84      -7.730   1.146   0.326  1.00 94.41
ATOM    652  C   SER A  84      -8.200   1.332  -1.114  1.00 94.41
ATOM    653  O   SER A  84      -7.459   1.046  -2.053  1.00 94.41
ATOM    654  CB  SER A  84      -8.252  -0.190   0.852  1.00 94.41
ATOM    655  OG  SER A  84      -7.736  -0.407   2.143  1.00 94.41
ATOM    656  N   LEU A  85      -9.406   1.874  -1.298  1.00 94.16
ATOM    657  CA  LEU A  85      -9.937   2.218  -2.610  1.00 94.16
ATOM    658  C   LEU A  85      -9.136   3.358  -3.269  1.00 94.16
ATOM    659  O   LEU A  85      -8.769   3.236  -4.436  1.00 94.16
ATOM    660  CB  LEU A  85     -11.435   2.538  -2.447  1.00 94.16
ATOM    661  CG  LEU A  85     -12.162   2.751  -3.779  1.00 94.16
ATOM    662  CD1 LEU A  85     -12.269   1.468  -4.604  1.00 94.16
ATOM    663  CD2 LEU A  85     -13.575   3.282  -3.535  1.00 94.16
ATOM    664  N   TYR A  86      -8.806   4.420  -2.524  1.00 92.92
ATOM    665  CA  TYR A  86      -7.977   5.531  -3.009  1.00 92.92
ATOM    666  C   TYR A  86      -6.583   5.078  -3.430  1.00 92.92
ATOM    667  O   TYR A  86      -6.127   5.440  -4.514  1.00 92.92
ATOM    668  CB  TYR A  86      -7.874   6.632  -1.938  1.00 92.92
ATOM    669  CG  TYR A  86      -9.145   7.402  -1.613  1.00 92.92
ATOM    670  CD1 TYR A  86     -10.243   7.380  -2.494  1.00 92.92
ATOM    671  CD2 TYR A  86      -9.215   8.186  -0.441  1.00 92.92
ATOM    672  CE1 TYR A  86     -11.379   8.157  -2.240  1.00 92.92
ATOM    673  CE2 TYR A  86     -10.354   8.979  -0.184  1.00 92.92
ATOM    674  CZ  TYR A  86     -11.433   8.968  -1.096  1.00 92.92
ATOM    675  OH  TYR A  86     -12.551   9.710  -0.903  1.00 92.92
ATOM    676  N   VAL A  87      -5.933   4.241  -2.619  1.00 92.62
ATOM    677  CA  VAL A  87      -4.638   3.650  -2.977  1.00 92.62
ATOM    678  C   VAL A  87      -4.770   2.753  -4.202  1.00 92.62
ATOM    679  O   VAL A  87      -3.953   2.849  -5.114  1.00 92.62
ATOM    680  CB  VAL A  87      -3.989   2.955  -1.767  1.00 92.62
ATOM    681  CG1 VAL A  87      -2.694   2.229  -2.151  1.00 92.62
ATOM    682  CG2 VAL A  87      -3.647   4.028  -0.720  1.00 92.62
ATOM    683  N   GLY A  88      -5.848   1.973  -4.307  1.00 93.34
ATOM    684  CA  GLY A  88      -6.149   1.182  -5.500  1.00 93.34
ATOM    685  C   GLY A  88      -6.195   2.000  -6.799  1.00 93.34
ATOM    686  O   GLY A  88      -5.796   1.490  -7.845  1.00 93.34
ATOM    687  N   PHE A  89      -6.614   3.271  -6.760  1.00 91.32
ATOM    688  CA  PHE A  89      -6.682   4.120  -7.957  1.00 91.32
ATOM    689  C   PHE A  89      -5.309   4.427  -8.552  1.00 91.32
ATOM    690  O   PHE A  89      -5.141   4.350  -9.767  1.00 91.32
ATOM    691  CB  PHE A  89      -7.397   5.445  -7.654  1.00 91.32
ATOM    692  CG  PHE A  89      -8.811   5.352  -7.121  1.00 91.32
ATOM    693  CD1 PHE A  89      -9.618   4.224  -7.369  1.00 91.32
ATOM    694  CD2 PHE A  89      -9.339   6.441  -6.405  1.00 91.32
ATOM    695  CE1 PHE A  89     -10.932   4.175  -6.879  1.00 91.32
ATOM    696  CE2 PHE A  89     -10.653   6.392  -5.916  1.00 91.32
ATOM    697  CZ  PHE A  89     -11.445   5.255  -6.144  1.00 91.32
ATOM    698  N   PHE A  90      -4.319   4.767  -7.732  1.00 92.45
ATOM    699  CA  PHE A  90      -3.006   5.165  -8.241  1.00 92.45
ATOM    700  C   PHE A  90      -1.988   4.021  -8.203  1.00 92.45
ATOM    701  O   PHE A  90      -1.076   3.980  -9.023  1.00 92.45
ATOM    702  CB  PHE A  90      -2.544   6.418  -7.501  1.00 92.45
ATOM    703  CG  PHE A  90      -2.190   6.206  -6.047  1.00 92.45
ATOM    704  CD1 PHE A  90      -3.089   6.600  -5.042  1.00 92.45
ATOM    705  CD2 PHE A  90      -0.940   5.665  -5.696  1.00 92.45
ATOM    706  CE1 PHE A  90      -2.715   6.500  -3.691  1.00 92.45
ATOM    707  CE2 PHE A  90      -0.582   5.529  -4.346  1.00 92.45
ATOM    708  CZ  PHE A  90      -1.467   5.954  -3.345  1.00 92.45
ATOM    709  N   TYR A  91      -2.148   3.040  -7.316  1.00 93.72
ATOM    710  CA  TYR A  91      -1.207   1.928  -7.204  1.00 93.72
ATOM    711  C   TYR A  91      -1.235   1.025  -8.447  1.00 93.72
ATOM    712  O   TYR A  91      -0.185   0.644  -8.959  1.00 93.72
ATOM    713  CB  TYR A  91      -1.503   1.161  -5.916  1.00 93.72
ATOM    714  CG  TYR A  91      -0.372   0.263  -5.485  1.00 93.72
ATOM    715  CD1 TYR A  91      -0.304  -1.062  -5.945  1.00 93.72
ATOM    716  CD2 TYR A  91       0.611   0.762  -4.608  1.00 93.72
ATOM    717  CE1 TYR A  91       0.750  -1.886  -5.520  1.00 93.72
ATOM    718  CE2 TYR A  91       1.653  -0.073  -4.165  1.00 93.72
ATOM    719  CZ  TYR A  91       1.725  -1.403  -4.624  1.00 93.72
ATOM    720  OH  TYR A  91       2.712  -2.222  -4.182  1.00 93.72
ATOM    721  N   ASN A  92      -2.420   0.784  -9.026  1.00 95.40
ATOM    722  CA  ASN A  92      -2.566   0.045 -10.290  1.00 95.40
ATOM    723  C   ASN A  92      -1.827   0.708 -11.468  1.00 95.40
ATOM    724  O   ASN A  92      -1.445   0.032 -12.423  1.00 95.40
ATOM    725  CB  ASN A  92      -4.065  -0.103 -10.607  1.00 95.40
ATOM    726  CG  ASN A  92      -4.775  -1.093  -9.703  1.00 95.40
ATOM    727  OD1 ASN A  92      -4.204  -2.036  -9.187  1.00 95.40
ATOM    728  ND2 ASN A  92      -6.059  -0.929  -9.502  1.00 95.40
ATOM    729  N   VAL A  93      -1.585   2.019 -11.394  1.00 96.23
ATOM    730  CA  VAL A  93      -0.838   2.779 -12.407  1.00 96.23
ATOM    731  C   VAL A  93       0.655   2.471 -12.318  1.00 96.23
ATOM    732  O   VAL A  93       1.295   2.290 -13.349  1.00 96.23
ATOM    733  CB  VAL A  93      -1.090   4.286 -12.241  1.00 96.23
ATOM    734  CG1 VAL A  93      -0.317   5.117 -13.262  1.00 96.23
ATOM    735  CG2 VAL A  93      -2.585   4.620 -12.320  1.00 96.23
ATOM    736  N   ILE A  94       1.194   2.308 -11.105  1.00 95.11
ATOM    737  CA  ILE A  94       2.586   1.878 -10.894  1.00 95.11
ATOM    738  C   ILE A  94       2.812   0.495 -11.516  1.00 95.11
ATOM    739  O   ILE A  94       3.808   0.264 -12.202  1.00 95.11
ATOM    740  CB  ILE A  94       2.953   1.851  -9.391  1.00 95.11
ATOM    741  CG1 ILE A  94       2.596   3.173  -8.680  1.00 95.11
ATOM    742  CG2 ILE A  94       4.453   1.553  -9.242  1.00 95.11
ATOM    743  CD1 ILE A  94       2.900   3.178  -7.174  1.00 95.11
ATOM    744  N   ILE A  95       1.850  -0.412 -11.334  1.00 96.74
ATOM    745  CA  ILE A  95       1.878  -1.747 -11.943  1.00 96.74
ATOM    746  C   ILE A  95       1.802  -1.641 -13.473  1.00 96.74
ATOM    747  O   ILE A  95       2.522  -2.348 -14.176  1.00 96.74
ATOM    748  CB  ILE A  95       0.738  -2.628 -11.387  1.00 96.74
ATOM    749  CG1 ILE A  95       0.707  -2.634  -9.845  1.00 96.74
ATOM    750  CG2 ILE A  95       0.909  -4.074 -11.873  1.00 96.74
ATOM    751  CD1 ILE A  95      -0.457  -3.435  -9.255  1.00 96.74
ATOM    752  N   ALA A  96       0.980  -0.731 -14.008  1.00 98.03
ATOM    753  CA  ALA A  96       0.900  -0.479 -15.446  1.00 98.03
ATOM    754  C   ALA A  96       2.219   0.072 -16.020  1.00 98.03
ATOM    755  O   ALA A  96       2.614  -0.341 -17.110  1.00 98.03
ATOM    756  CB  ALA A  96      -0.285   0.450 -15.733  1.00 98.03
ATOM    757  N   TRP A  97       2.936   0.936 -15.291  1.00 97.66
ATOM    758  CA  TRP A  97       4.288   1.366 -15.663  1.00 97.66
ATOM    759  C   TRP A  97       5.263   0.186 -15.671  1.00 97.66
ATOM    760  O   TRP A  97       5.948  -0.022 -16.669  1.00 97.66
ATOM    761  CB  TRP A  97       4.795   2.472 -14.725  1.00 97.66
ATOM    762  CG  TRP A  97       4.028   3.759 -14.703  1.00 97.66
ATOM    763  CD1 TRP A  97       3.288   4.269 -15.712  1.00 97.66
ATOM    764  CD2 TRP A  97       3.941   4.735 -13.622  1.00 97.66
ATOM    765  NE1 TRP A  97       2.742   5.478 -15.332  1.00 97.66
ATOM    766  CE2 TRP A  97       3.114   5.815 -14.051  1.00 97.66
ATOM    767  CE3 TRP A  97       4.480   4.819 -12.322  1.00 97.66
ATOM    768  CZ2 TRP A  97       2.818   6.911 -13.229  1.00 97.66
ATOM    769  CZ3 TRP A  97       4.183   5.908 -11.481  1.00 97.66
ATOM    770  CH2 TRP A  97       3.347   6.946 -11.928  1.00 97.66
ATOM    771  N   ALA A  98       5.280  -0.640 -14.621  1.00 97.45
ATOM    772  CA  ALA A  98       6.127  -1.835 -14.569  1.00 97.45
ATOM    773  C   ALA A  98       5.846  -2.797 -15.731  1.00 97.45
ATOM    774  O   ALA A  98       6.775  -3.310 -16.352  1.00 97.45
ATOM    775  CB  ALA A  98       5.944  -2.515 -13.207  1.00 97.45
ATOM    776  N   LEU A  99       4.574  -2.987 -16.079  1.00 98.07
ATOM    777  CA  LEU A  99       4.163  -3.823 -17.201  1.00 98.07
ATOM    778  C   LEU A  99       4.569  -3.228 -18.558  1.00 98.07
ATOM    779  O   LEU A  99       5.014  -3.961 -19.439  1.00 98.07
ATOM    780  CB  LEU A  99       2.650  -4.029 -17.081  1.00 98.07
ATOM    781  CG  LEU A  99       2.065  -5.019 -18.095  1.00 98.07
ATOM    782  CD1 LEU A  99       2.692  -6.411 -18.001  1.00 98.07
ATOM    783  CD2 LEU A  99       0.576  -5.148 -17.800  1.00 98.07
ATOM    784  N   HIS A 100       4.475  -1.907 -18.721  1.00 98.30
ATOM    785  CA  HIS A 100       4.957  -1.221 -19.918  1.00 98.30
ATOM    786  C   HIS A 100       6.468  -1.416 -20.103  1.00 98.30
ATOM    787  O   HIS A 100       6.916  -1.807 -21.179  1.00 98.30
ATOM    788  CB  HIS A 100       4.590   0.266 -19.834  1.00 98.30
ATOM    789  CG  HIS A 100       5.031   1.030 -21.051  1.00 98.30
ATOM    790  ND1 HIS A 100       4.396   1.041 -22.270  1.00 98.30
ATOM    791  CD2 HIS A 100       6.173   1.772 -21.179  1.00 98.30
ATOM    792  CE1 HIS A 100       5.140   1.774 -23.115  1.00 98.30
ATOM    793  NE2 HIS A 100       6.226   2.246 -22.492  1.00 98.30
ATOM    794  N   TYR A 101       7.252  -1.226 -19.041  1.00 98.24
ATOM    795  CA  TYR A 101       8.691  -1.481 -19.071  1.00 98.24
ATOM    796  C   TYR A 101       9.029  -2.955 -19.307  1.00 98.24
ATOM    797  O   TYR A 101       9.989  -3.245 -20.019  1.00 98.24
ATOM    798  CB  TYR A 101       9.322  -1.026 -17.763  1.00 98.24
ATOM    799  CG  TYR A 101       9.761   0.420 -17.733  1.00 98.24
ATOM    800  CD1 TYR A 101      11.127   0.747 -17.856  1.00 98.24
ATOM    801  CD2 TYR A 101       8.813   1.439 -17.553  1.00 98.24
ATOM    802  CE1 TYR A 101      11.554   2.077 -17.701  1.00 98.24
ATOM    803  CE2 TYR A 101       9.226   2.774 -17.450  1.00 98.24
ATOM    804  CZ  TYR A 101      10.595   3.092 -17.500  1.00 98.24
ATOM    805  OH  TYR A 101      10.968   4.382 -17.366  1.00 98.24
ATOM    806  N   LEU A 102       8.241  -3.889 -18.763  1.00 97.97
ATOM    807  CA  LEU A 102       8.404  -5.316 -19.037  1.00 97.97
ATOM    808  C   LEU A 102       8.267  -5.602 -20.537  1.00 97.97
ATOM    809  O   LEU A 102       9.129  -6.268 -21.103  1.00 97.97
ATOM    810  CB  LEU A 102       7.392  -6.126 -18.207  1.00 97.97
ATOM    811  CG  LEU A 102       7.445  -7.643 -18.456  1.00 97.97
ATOM    812  CD1 LEU A 102       8.826  -8.235 -18.174  1.00 97.97
ATOM    813  CD2 LEU A 102       6.424  -8.349 -17.565  1.00 97.97
ATOM    814  N   PHE A 103       7.239  -5.064 -21.200  1.00 98.11
ATOM    815  CA  PHE A 103       7.087  -5.215 -22.650  1.00 98.11
ATOM    816  C   PHE A 103       8.239  -4.578 -23.426  1.00 98.11
ATOM    817  O   PHE A 103       8.790  -5.209 -24.328  1.00 98.11
ATOM    818  CB  PHE A 103       5.738  -4.656 -23.113  1.00 98.11
ATOM    819  CG  PHE A 103       4.532  -5.450 -22.651  1.00 98.11
ATOM    820  CD1 PHE A 103       4.513  -6.855 -22.768  1.00 98.11
ATOM    821  CD2 PHE A 103       3.405  -4.781 -22.136  1.00 98.11
ATOM    822  CE1 PHE A 103       3.390  -7.586 -22.348  1.00 98.11
ATOM    823  CE2 PHE A 103       2.272  -5.512 -21.739  1.00 98.11
ATOM    824  CZ  PHE A 103       2.268  -6.914 -21.837  1.00 98.11
ATOM    825  N   SER A 104       8.661  -3.382 -23.024  1.00 97.44
ATOM    826  CA  SER A 104       9.810  -2.689 -23.611  1.00 97.44
ATOM    827  C   SER A 104      11.157  -3.368 -23.341  1.00 97.44
ATOM    828  O   SER A 104      12.140  -3.025 -23.985  1.00 97.44
ATOM    829  CB  SER A 104       9.849  -1.255 -23.093  1.00 97.44
ATOM    830  OG  SER A 104       8.704  -0.557 -23.542  1.00 97.44
ATOM    831  N   SER A 105      11.219  -4.334 -22.419  1.00 97.70
ATOM    832  CA  SER A 105      12.435  -5.106 -22.131  1.00 97.70
ATOM    833  C   SER A 105      12.652  -6.265 -23.109  1.00 97.70
ATOM    834  O   SER A 105      13.749  -6.818 -23.162  1.00 97.70
ATOM    835  CB  SER A 105      12.415  -5.646 -20.700  1.00 97.70
ATOM    836  OG  SER A 105      12.294  -4.608 -19.751  1.00 97.70
ATOM    837  N   PHE A 106      11.643  -6.642 -23.905  1.00 96.76
ATOM    838  CA  PHE A 106      11.758  -7.678 -24.943  1.00 96.76
ATOM    839  C   PHE A 106      12.352  -7.129 -26.249  1.00 96.76
ATOM    840  O   PHE A 106      11.860  -7.398 -27.345  1.00 96.76
ATOM    841  CB  PHE A 106      10.420  -8.402 -25.145  1.00 96.76
ATOM    842  CG  PHE A 106       9.991  -9.238 -23.959  1.00 96.76
ATOM    843  CD1 PHE A 106      10.567 -10.502 -23.735  1.00 96.76
ATOM    844  CD2 PHE A 106       9.020  -8.748 -23.073  1.00 96.76
ATOM    845  CE1 PHE A 106      10.167 -11.273 -22.629  1.00 96.76
ATOM    846  CE2 PHE A 106       8.616  -9.517 -21.969  1.00 96.76
ATOM    847  CZ  PHE A 106       9.190 -10.780 -21.745  1.00 96.76
ATOM    848  N   THR A 107      13.432  -6.364 -26.130  1.00 94.27
ATOM    849  CA  THR A 107      14.211  -5.818 -27.241  1.00 94.27
ATOM    850  C   THR A 107      15.684  -6.191 -27.094  1.00 94.27
ATOM    851  O   THR A 107      16.155  -6.553 -26.013  1.00 94.27
ATOM    852  CB  THR A 107      14.047  -4.295 -27.348  1.00 94.27
ATOM    853  OG1 THR A 107      14.481  -3.692 -26.158  1.00 94.27
ATOM    854  CG2 THR A 107      12.596  -3.878 -27.598  1.00 94.27
ATOM    855  N   THR A 108      16.434  -6.141 -28.196  1.00 90.26
ATOM    856  CA  THR A 108      17.891  -6.354 -28.176  1.00 90.26
ATOM    857  C   THR A 108      18.621  -5.187 -27.523  1.00 90.26
ATOM    858  O   THR A 108      19.549  -5.397 -26.751  1.00 90.26
ATOM    859  CB  THR A 108      18.433  -6.544 -29.598  1.00 90.26
ATOM    860  OG1 THR A 108      17.948  -5.530 -30.454  1.00 90.26
ATOM    861  CG2 THR A 108      17.971  -7.876 -30.186  1.00 90.26
ATOM    862  N   GLU A 109      18.169  -3.971 -27.817  1.00 91.93
ATOM    863  CA  GLU A 109      18.623  -2.730 -27.203  1.00 91.93
ATOM    864  C   GLU A 109      17.460  -2.129 -26.419  1.00 91.93
ATOM    865  O   GLU A 109      16.353  -1.980 -26.943  1.00 91.93
ATOM    866  CB  GLU A 109      19.135  -1.766 -28.279  1.00 91.93
ATOM    867  CG  GLU A 109      20.487  -2.242 -28.834  1.00 91.93
ATOM    868  CD  GLU A 109      21.123  -1.263 -29.830  1.00 91.93
ATOM    869  OE1 GLU A 109      22.331  -1.450 -30.100  1.00 91.93
ATOM    870  OE2 GLU A 109      20.400  -0.389 -30.352  1.00 91.93
ATOM    871  N   LEU A 110      17.686  -1.840 -25.139  1.00 95.77
ATOM    872  CA  LEU A 110      16.662  -1.262 -24.274  1.00 95.77
ATOM    873  C   LEU A 110      16.389   0.194 -24.701  1.00 95.77
ATOM    874  O   LEU A 110      17.334   0.931 -24.966  1.00 95.77
ATOM    875  CB  LEU A 110      17.113  -1.362 -22.808  1.00 95.77
ATOM    876  CG  LEU A 110      17.207  -2.797 -22.263  1.00 95.77
ATOM    877  CD1 LEU A 110      17.883  -2.770 -20.892  1.00 95.77
ATOM    878  CD2 LEU A 110      15.821  -3.430 -22.148  1.00 95.77
ATOM    879  N   PRO A 111      15.133   0.667 -24.726  1.00 95.29
ATOM    880  CA  PRO A 111      14.805   1.987 -25.283  1.00 95.29
ATOM    881  C   PRO A 111      15.291   3.179 -24.439  1.00 95.29
ATOM    882  O   PRO A 111      15.212   4.322 -24.882  1.00 95.29
ATOM    883  CB  PRO A 111      13.285   1.978 -25.448  1.00 95.29
ATOM    884  CG  PRO A 111      12.804   0.963 -24.415  1.00 95.29
ATOM    885  CD  PRO A 111      13.932  -0.063 -24.356  1.00 95.29
ATOM    886  N   TRP A 112      15.791   2.927 -23.228  1.00 94.96
ATOM    887  CA  TRP A 112      16.306   3.931 -22.293  1.00 94.96
ATOM    888  C   TRP A 112      17.841   4.022 -22.261  1.00 94.96
ATOM    889  O   TRP A 112      18.395   4.495 -21.270  1.00 94.96
ATOM    890  CB  TRP A 112      15.712   3.657 -20.909  1.00 94.96
ATOM    891  CG  TRP A 112      15.902   2.282 -20.368  1.00 94.96
ATOM    892  CD1 TRP A 112      17.006   1.823 -19.741  1.00 94.96
ATOM    893  CD2 TRP A 112      14.949   1.187 -20.364  1.00 94.96
ATOM    894  NE1 TRP A 112      16.796   0.520 -19.336  1.00 94.96
ATOM    895  CE2 TRP A 112      15.538   0.077 -19.695  1.00 94.96
ATOM    896  CE3 TRP A 112      13.637   1.038 -20.849  1.00 94.96
ATOM    897  CZ2 TRP A 112      14.841  -1.125 -19.506  1.00 94.96
ATOM    898  CZ3 TRP A 112      12.939  -0.172 -20.694  1.00 94.96
ATOM    899  CH2 TRP A 112      13.539  -1.250 -20.022  1.00 94.96
ATOM    900  N   ILE A 113      18.539   3.545 -23.301  1.00 92.45
ATOM    901  CA  ILE A 113      20.016   3.579 -23.358  1.00 92.45
ATOM    902  C   ILE A 113      20.595   4.748 -24.153  1.00 92.45
ATOM    903  O   ILE A 113      21.749   5.088 -23.923  1.00 92.45
ATOM    904  CB  ILE A 113      20.609   2.254 -23.881  1.00 92.45
ATOM    905  CG1 ILE A 113      20.366   2.056 -25.395  1.00 92.45
ATOM    906  CG2 ILE A 113      20.099   1.100 -23.013  1.00 92.45
ATOM    907  CD1 ILE A 113      20.810   0.696 -25.937  1.00 92.45
ATOM    908  N   HIS A 114      19.833   5.319 -25.089  1.00 91.26
ATOM    909  CA  HIS A 114      20.320   6.344 -26.011  1.00 91.26
ATOM    910  C   HIS A 114      19.299   7.472 -26.217  1.00 91.26
ATOM    911  O   HIS A 114      18.089   7.254 -26.117  1.00 91.26
ATOM    912  CB  HIS A 114      20.729   5.701 -27.346  1.00 91.26
ATOM    913  CG  HIS A 114      19.628   4.947 -28.057  1.00 91.26
ATOM    914  ND1 HIS A 114      18.416   5.458 -28.471  1.00 91.26
ATOM    915  CD2 HIS A 114      19.649   3.627 -28.424  1.00 91.26
ATOM    916  CE1 HIS A 114      17.731   4.473 -29.072  1.00 91.26
ATOM    917  NE2 HIS A 114      18.436   3.336 -29.053  1.00 91.26
ATOM    918  N   CYS A 115      19.771   8.654 -26.598  1.00 91.79
ATOM    919  CA  CYS A 115      18.970   9.853 -26.844  1.00 91.79
ATOM    920  C   CYS A 115      18.434   9.954 -28.282  1.00 91.79
ATOM    921  O   CYS A 115      17.731  10.905 -28.616  1.00 91.79
ATOM    922  CB  CYS A 115      19.814  11.077 -26.483  1.00 91.79
ATOM    923  SG  CYS A 115      20.154  11.270 -24.720  1.00 91.79
ATOM    924  N   ASN A 116      18.738   8.992 -29.159  1.00 90.82
ATOM    925  CA  ASN A 116      18.296   9.006 -30.558  1.00 90.82
ATOM    926  C   ASN A 116      16.861   8.469 -30.748  1.00 90.82
ATOM    927  O   ASN A 116      16.628   7.566 -31.552  1.00 90.82
ATOM    928  CB  ASN A 116      19.342   8.293 -31.430  1.00 90.82
ATOM    929  CG  ASN A 116      19.111   8.526 -32.916  1.00 90.82
ATOM    930  OD1 ASN A 116      18.483   9.476 -33.355  1.00 90.82
ATOM    931  ND2 ASN A 116      19.652   7.674 -33.755  1.00 90.82
ATOM    932  N   ASN A 117      15.890   8.990 -29.993  1.00 92.95
ATOM    933  CA  ASN A 117      14.477   8.646 -30.158  1.00 92.95
ATOM    934  C   ASN A 117      13.603   9.878 -30.400  1.00 92.95
ATOM    935  O   ASN A 117      13.928  10.999 -30.024  1.00 92.95
ATOM    936  CB  ASN A 117      13.930   7.855 -28.964  1.00 92.95
ATOM    937  CG  ASN A 117      14.762   6.658 -28.563  1.00 92.95
ATOM    938  OD1 ASN A 117      14.627   5.588 -29.129  1.00 92.95
ATOM    939  ND2 ASN A 117      15.596   6.801 -27.562  1.00 92.95
ATOM    940  N   SER A 118      12.418   9.642 -30.967  1.00 93.39
ATOM    941  CA  SER A 118      11.441  10.698 -31.281  1.00 93.39
ATOM    942  C   SER A 118      10.939  11.504 -30.075  1.00 93.39
ATOM    943  O   SER A 118      10.488  12.634 -30.247  1.00 93.39
ATOM    944  CB  SER A 118      10.236  10.085 -31.999  1.00 93.39
ATOM    945  OG  SER A 118       9.574   9.131 -31.183  1.00 93.39
ATOM    946  N   TRP A 119      10.991  10.939 -28.865  1.00 93.51
ATOM    947  CA  TRP A 119      10.551  11.614 -27.641  1.00 93.51
ATOM    948  C   TRP A 119      11.666  12.393 -26.947  1.00 93.51
ATOM    949  O   TRP A 119      11.359  13.161 -26.032  1.00 93.51
ATOM    950  CB  TRP A 119       9.934  10.594 -26.677  1.00 93.51
ATOM    951  CG  TRP A 119      10.841   9.470 -26.278  1.00 93.51
ATOM    952  CD1 TRP A 119      11.775   9.498 -25.299  1.00 93.51
ATOM    953  CD2 TRP A 119      10.941   8.150 -26.888  1.00 93.51
ATOM    954  NE1 TRP A 119      12.443   8.289 -25.262  1.00 93.51
ATOM    955  CE2 TRP A 119      11.958   7.415 -26.211  1.00 93.51
ATOM    956  CE3 TRP A 119      10.283   7.514 -27.964  1.00 93.51
ATOM    957  CZ2 TRP A 119      12.306   6.110 -26.580  1.00 93.51
ATOM    958  CZ3 TRP A 119      10.626   6.202 -28.344  1.00 93.51
ATOM    959  CH2 TRP A 119      11.636   5.503 -27.655  1.00 93.51
ATOM    960  N   ASN A 120      12.930  12.200 -27.334  1.00 94.66
ATOM    961  CA  ASN A 120      14.048  12.809 -26.631  1.00 94.66
ATOM    962  C   ASN A 120      14.104  14.327 -26.847  1.00 94.66
ATOM    963  O   ASN A 120      13.702  14.849 -27.889  1.00 94.66
ATOM    964  CB  ASN A 120      15.364  12.103 -26.988  1.00 94.66
ATOM    965  CG  ASN A 120      15.491  10.741 -26.333  1.00 94.66
ATOM    966  OD1 ASN A 120      15.517   9.698 -26.966  1.00 94.66
ATOM    967  ND2 ASN A 120      15.562  10.699 -25.026  1.00 94.66
ATOM    968  N   SER A 121      14.553  15.053 -25.826  1.00 92.81
ATOM    969  CA  SER A 121      14.790  16.490 -25.910  1.00 92.81
ATOM    970  C   SER A 121      16.204  16.788 -26.427  1.00 92.81
ATOM    971  O   SER A 121      17.085  15.935 -26.328  1.00 92.81
ATOM    972  CB  SER A 121      14.516  17.163 -24.561  1.00 92.81
ATOM    973  OG  SER A 121      15.653  17.229 -23.737  1.00 92.81
ATOM    974  N   PRO A 122      16.468  18.011 -26.923  1.00 87.89
ATOM    975  CA  PRO A 122      17.822  18.419 -27.303  1.00 87.89
ATOM    976  C   PRO A 122      18.829  18.428 -26.141  1.00 87.89
ATOM    977  O   PRO A 122      20.025  18.452 -26.398  1.00 87.89
ATOM    978  CB  PRO A 122      17.674  19.826 -27.893  1.00 87.89
ATOM    979  CG  PRO A 122      16.212  19.894 -28.326  1.00 87.89
ATOM    980  CD  PRO A 122      15.509  19.048 -27.269  1.00 87.89
ATOM    981  N   ASN A 123      18.354  18.431 -24.888  1.00 87.62
ATOM    982  CA  ASN A 123      19.187  18.417 -23.681  1.00 87.62
ATOM    983  C   ASN A 123      19.524  16.991 -23.201  1.00 87.62
ATOM    984  O   ASN A 123      20.150  16.808 -22.156  1.00 87.62
ATOM    985  CB  ASN A 123      18.459  19.220 -22.586  1.00 87.62
ATOM    986  CG  ASN A 123      19.393  19.601 -21.451  1.00 87.62
ATOM    987  OD1 ASN A 123      20.529  19.959 -21.660  1.00 87.62
ATOM    988  ND2 ASN A 123      18.944  19.581 -20.218  1.00 87.62
ATOM    989  N   CYS A 124      19.056  15.970 -23.923  1.00 89.84
ATOM    990  CA  CYS A 124      19.366  14.586 -23.617  1.00 89.84
ATOM    991  C   CYS A 124      20.832  14.304 -23.948  1.00 89.84
ATOM    992  O   CYS A 124      21.259  14.507 -25.087  1.00 89.84
ATOM    993  CB  CYS A 124      18.427  13.687 -24.418  1.00 89.84
ATOM    994  SG  CYS A 124      18.424  11.946 -23.925  1.00 89.84
ATOM    995  N   SER A 125      21.592  13.802 -22.976  1.00 85.30
ATOM    996  CA  SER A 125      22.991  13.437 -23.173  1.00 85.30
ATOM    997  C   SER A 125      23.230  11.942 -22.950  1.00 85.30
ATOM    998  O   SER A 125      23.009  11.397 -21.871  1.00 85.30
ATOM    999  CB  SER A 125      23.905  14.330 -22.324  1.00 85.30
ATOM   1000  OG  SER A 125      23.625  14.222 -20.943  1.00 85.30
ATOM   1001  N   ASP A 126      23.759  11.281 -23.984  1.00 77.71
ATOM   1002  CA  ASP A 126      24.314   9.918 -23.893  1.00 77.71
ATOM   1003  C   ASP A 126      25.731   9.916 -23.293  1.00 77.71
ATOM   1004  O   ASP A 126      26.283   8.867 -22.941  1.00 77.71
ATOM   1005  CB  ASP A 126      24.349   9.291 -25.301  1.00 77.71
ATOM   1006  CG  ASP A 126      22.955   9.022 -25.862  1.00 77.71
ATOM   1007  OD1 ASP A 126      22.031   8.841 -25.052  1.00 77.71
ATOM   1008  OD2 ASP A 126      22.772   8.969 -27.099  1.00 77.71
ATOM   1009  N   ALA A 127      26.337  11.107 -23.227  1.00 59.58
ATOM   1010  CA  ALA A 127      27.752  11.310 -22.987  1.00 59.58
ATOM   1011  C   ALA A 127      28.199  10.660 -21.675  1.00 59.58
ATOM   1012  O   ALA A 127      27.786  11.034 -20.578  1.00 59.58
ATOM   1013  CB  ALA A 127      28.063  12.812 -23.028  1.00 59.58
ATOM   1014  N   HIS A 128      29.108   9.696 -21.803  1.00 52.84
ATOM   1015  CA  HIS A 128      29.942   9.256 -20.700  1.00 52.84
ATOM   1016  C   HIS A 128      30.825  10.448 -20.308  1.00 52.84
ATOM   1017  O   HIS A 128      31.534  10.952 -21.180  1.00 52.84
ATOM   1018  CB  HIS A 128      30.773   8.045 -21.157  1.00 52.84
ATOM   1019  CG  HIS A 128      29.938   6.823 -21.461  1.00 52.84
ATOM   1020  ND1 HIS A 128      28.563   6.742 -21.413  1.00 52.84
ATOM   1021  CD2 HIS A 128      30.397   5.598 -21.863  1.00 52.84
ATOM   1022  CE1 HIS A 128      28.207   5.502 -21.775  1.00 52.84
ATOM   1023  NE2 HIS A 128      29.291   4.747 -22.009  1.00 52.84
ATOM   1024  N   PRO A 129      30.850  10.899 -19.040  1.00 46.31
ATOM   1025  CA  PRO A 129      31.670  12.045 -18.630  1.00 46.31
ATOM   1026  C   PRO A 129      33.175  11.918 -18.955  1.00 46.31
ATOM   1027  O   PRO A 129      33.909  12.892 -18.826  1.00 46.31
ATOM   1028  CB  PRO A 129      31.425  12.193 -17.124  1.00 46.31
ATOM   1029  CG  PRO A 129      30.033  11.597 -16.918  1.00 46.31
ATOM   1030  CD  PRO A 129      29.974  10.480 -17.954  1.00 46.31
ATOM   1031  N   GLY A 130      33.647  10.735 -19.372  1.00 43.63
ATOM   1032  CA  GLY A 130      35.020  10.484 -19.815  1.00 43.63
ATOM   1033  C   GLY A 130      35.311  10.686 -21.312  1.00 43.63
ATOM   1034  O   GLY A 130      36.485  10.796 -21.650  1.00 43.63
ATOM   1035  N   ASP A 131      34.308  10.773 -22.196  1.00 44.20
ATOM   1036  CA  ASP A 131      34.527  10.862 -23.658  1.00 44.20
ATOM   1037  C   ASP A 131      34.476  12.297 -24.216  1.00 44.20
ATOM   1038  O   ASP A 131      34.575  12.500 -25.428  1.00 44.20
ATOM   1039  CB  ASP A 131      33.616   9.878 -24.422  1.00 44.20
ATOM   1040  CG  ASP A 131      34.158   8.441 -24.487  1.00 44.20
ATOM   1041  OD1 ASP A 131      35.358   8.221 -24.204  1.00 44.20
ATOM   1042  OD2 ASP A 131      33.351   7.547 -24.828  1.00 44.20
ATOM   1043  N   SER A 132      34.424  13.313 -23.346  1.00 42.72
ATOM   1044  CA  SER A 132      34.605  14.731 -23.701  1.00 42.72
ATOM   1045  C   SER A 132      36.060  15.033 -24.093  1.00 42.72
ATOM   1046  O   SER A 132      36.767  15.810 -23.450  1.00 42.72
ATOM   1047  CB  SER A 132      34.148  15.650 -22.563  1.00 42.72
ATOM   1048  OG  SER A 132      32.856  15.295 -22.118  1.00 42.72
ATOM   1049  N   SER A 133      36.532  14.398 -25.160  1.00 36.31
ATOM   1050  CA  SER A 133      37.763  14.755 -25.849  1.00 36.31
ATOM   1051  C   SER A 133      37.470  15.893 -26.834  1.00 36.31
ATOM   1052  O   SER A 133      36.944  15.674 -27.913  1.00 36.31
ATOM   1053  CB  SER A 133      38.415  13.515 -26.484  1.00 36.31
ATOM   1054  OG  SER A 133      37.551  12.750 -27.302  1.00 36.31
ATOM   1055  N   GLY A 134      37.816  17.122 -26.435  1.00 38.08
ATOM   1056  CA  GLY A 134      38.041  18.255 -27.343  1.00 38.08
ATOM   1057  C   GLY A 134      36.804  18.958 -27.911  1.00 38.08
ATOM   1058  O   GLY A 134      36.392  18.664 -29.021  1.00 38.08
ATOM   1059  N   ASP A 135      36.258  19.926 -27.169  1.00 36.04
ATOM   1060  CA  ASP A 135      36.048  21.310 -27.642  1.00 36.04
ATOM   1061  C   ASP A 135      35.252  22.099 -26.593  1.00 36.04
ATOM   1062  O   ASP A 135      34.023  22.137 -26.564  1.00 36.04
ATOM   1063  CB  ASP A 135      35.398  21.438 -29.044  1.00 36.04
ATOM   1064  CG  ASP A 135      36.425  21.553 -30.190  1.00 36.04
ATOM   1065  OD1 ASP A 135      37.626  21.777 -29.893  1.00 36.04
ATOM   1066  OD2 ASP A 135      35.991  21.547 -31.363  1.00 36.04
ATOM   1067  N   SER A 136      35.973  22.759 -25.686  1.00 34.48
ATOM   1068  CA  SER A 136      35.398  23.674 -24.702  1.00 34.48
ATOM   1069  C   SER A 136      35.011  24.996 -25.377  1.00 34.48
ATOM   1070  O   SER A 136      35.720  25.995 -25.256  1.00 34.48
ATOM   1071  CB  SER A 136      36.391  23.879 -23.552  1.00 34.48
ATOM   1072  OG  SER A 136      37.620  24.350 -24.073  1.00 34.48
ATOM   1073  N   SER A 137      33.895  25.013 -26.104  1.00 33.93
ATOM   1074  CA  SER A 137      33.243  26.252 -26.535  1.00 33.93
ATOM   1075  C   SER A 137      31.834  26.349 -25.941  1.00 33.93
ATOM   1076  O   SER A 137      30.871  25.791 -26.443  1.00 33.93
ATOM   1077  CB  SER A 137      33.332  26.464 -28.054  1.00 33.93
ATOM   1078  OG  SER A 137      32.608  25.529 -28.817  1.00 33.93
ATOM   1079  N   GLY A 138      31.749  27.061 -24.815  1.00 37.16
ATOM   1080  CA  GLY A 138      30.566  27.809 -24.389  1.00 37.16
ATOM   1081  C   GLY A 138      29.231  27.070 -24.292  1.00 37.16
ATOM   1082  O   GLY A 138      28.294  27.456 -24.979  1.00 37.16
ATOM   1083  N   LEU A 139      29.083  26.141 -23.348  1.00 37.43
ATOM   1084  CA  LEU A 139      27.772  25.849 -22.768  1.00 37.43
ATOM   1085  C   LEU A 139      27.926  25.791 -21.247  1.00 37.43
ATOM   1086  O   LEU A 139      28.594  24.914 -20.707  1.00 37.43
ATOM   1087  CB  LEU A 139      27.166  24.565 -23.370  1.00 37.43
ATOM   1088  CG  LEU A 139      26.723  24.671 -24.845  1.00 37.43
ATOM   1089  CD1 LEU A 139      26.483  23.283 -25.429  1.00 37.43
ATOM   1090  CD2 LEU A 139      25.429  25.480 -24.994  1.00 37.43
ATOM   1091  N   ASN A 140      27.297  26.742 -20.555  1.00 38.91
ATOM   1092  CA  ASN A 140      26.877  26.580 -19.162  1.00 38.91
ATOM   1093  C   ASN A 140      25.787  25.491 -19.120  1.00 38.91
ATOM   1094  O   ASN A 140      24.644  25.782 -18.770  1.00 38.91
ATOM   1095  CB  ASN A 140      26.347  27.930 -18.621  1.00 38.91
ATOM   1096  CG  ASN A 140      27.394  28.894 -18.114  1.00 38.91
ATOM   1097  OD1 ASN A 140      28.508  28.554 -17.767  1.00 38.91
ATOM   1098  ND2 ASN A 140      27.042  30.154 -17.994  1.00 38.91
ATOM   1099  N   ASP A 141      26.113  24.276 -19.569  1.00 41.37
ATOM   1100  CA  ASP A 141      25.158  23.189 -19.723  1.00 41.37
ATOM   1101  C   ASP A 141      24.848  22.625 -18.340  1.00 41.37
ATOM   1102  O   ASP A 141      25.535  21.772 -17.777  1.00 41.37
ATOM   1103  CB  ASP A 141      25.639  22.133 -20.739  1.00 41.37
ATOM   1104  CG  ASP A 141      24.487  21.479 -21.516  1.00 41.37
ATOM   1105  OD1 ASP A 141      23.407  22.107 -21.591  1.00 41.37
ATOM   1106  OD2 ASP A 141      24.738  20.391 -22.075  1.00 41.37
ATOM   1107  N   THR A 142      23.839  23.232 -17.734  1.00 47.69
ATOM   1108  CA  THR A 142      23.094  22.727 -16.594  1.00 47.69
ATOM   1109  C   THR A 142      22.711  21.272 -16.848  1.00 47.69
ATOM   1110  O   THR A 142      21.770  21.038 -17.594  1.00 47.69
ATOM   1111  CB  THR A 142      21.811  23.571 -16.441  1.00 47.69
ATOM   1112  OG1 THR A 142      21.292  23.959 -17.698  1.00 47.69
ATOM   1113  CG2 THR A 142      22.072  24.860 -15.668  1.00 47.69
ATOM   1114  N   PHE A 143      23.444  20.332 -16.237  1.00 56.40
ATOM   1115  CA  PHE A 143      23.133  18.900 -16.103  1.00 56.40
ATOM   1116  C   PHE A 143      22.168  18.358 -17.177  1.00 56.40
ATOM   1117  O   PHE A 143      20.958  18.291 -16.943  1.00 56.40
ATOM   1118  CB  PHE A 143      22.588  18.636 -14.686  1.00 56.40
ATOM   1119  CG  PHE A 143      23.586  18.832 -13.558  1.00 56.40
ATOM   1120  CD1 PHE A 143      24.430  17.771 -13.177  1.00 56.40
ATOM   1121  CD2 PHE A 143      23.652  20.056 -12.867  1.00 56.40
ATOM   1122  CE1 PHE A 143      25.330  17.931 -12.109  1.00 56.40
ATOM   1123  CE2 PHE A 143      24.556  20.219 -11.800  1.00 56.40
ATOM   1124  CZ  PHE A 143      25.392  19.155 -11.420  1.00 56.40
ATOM   1125  N   GLY A 144      22.698  17.976 -18.346  1.00 65.83
ATOM   1126  CA  GLY A 144      21.924  17.260 -19.365  1.00 65.83
ATOM   1127  C   GLY A 144      21.143  16.083 -18.762  1.00 65.83
ATOM   1128  O   GLY A 144      21.586  15.437 -17.806  1.00 65.83
ATOM   1129  N   THR A 145      19.939  15.836 -19.270  1.00 84.31
ATOM   1130  CA  THR A 145      19.044  14.784 -18.767  1.00 84.31
ATOM   1131  C   THR A 145      19.449  13.413 -19.304  1.00 84.31
ATOM   1132  O   THR A 145      19.818  13.285 -20.469  1.00 84.31
ATOM   1133  CB  THR A 145      17.574  15.098 -19.100  1.00 84.31
ATOM   1134  OG1 THR A 145      17.431  15.695 -20.369  1.00 84.31
ATOM   1135  CG2 THR A 145      17.015  16.135 -18.126  1.00 84.31
ATOM   1136  N   THR A 146      19.356  12.365 -18.475  1.00 88.79
ATOM   1137  CA  THR A 146      19.742  11.008 -18.903  1.00 88.79
ATOM   1138  C   THR A 146      18.697  10.383 -19.839  1.00 88.79
ATOM   1139  O   THR A 146      17.498  10.670 -19.700  1.00 88.79
ATOM   1140  CB  THR A 146      20.077  10.049 -17.738  1.00 88.79
ATOM   1141  OG1 THR A 146      18.955   9.634 -16.985  1.00 88.79
ATOM   1142  CG2 THR A 146      21.082  10.651 -16.759  1.00 88.79
ATOM   1143  N   PRO A 147      19.098   9.462 -20.741  1.00 92.54
ATOM   1144  CA  PRO A 147      18.169   8.754 -21.626  1.00 92.54
ATOM   1145  C   PRO A 147      17.064   8.017 -20.863  1.00 92.54
ATOM   1146  O   PRO A 147      15.917   7.977 -21.305  1.00 92.54
ATOM   1147  CB  PRO A 147      19.029   7.762 -22.415  1.00 92.54
ATOM   1148  CG  PRO A 147      20.417   8.382 -22.394  1.00 92.54
ATOM   1149  CD  PRO A 147      20.473   9.086 -21.047  1.00 92.54
ATOM   1150  N   ALA A 148      17.384   7.476 -19.684  1.00 92.80
ATOM   1151  CA  ALA A 148      16.421   6.795 -18.827  1.00 92.80
ATOM   1152  C   ALA A 148      15.414   7.744 -18.175  1.00 92.80
ATOM   1153  O   ALA A 148      14.230   7.406 -18.085  1.00 92.80
ATOM   1154  CB  ALA A 148      17.190   5.968 -17.793  1.00 92.80
ATOM   1155  N   ALA A 149      15.851   8.940 -17.770  1.00 90.96
ATOM   1156  CA  ALA A 149      14.951   9.955 -17.235  1.00 90.96
ATOM   1157  C   ALA A 149      13.954  10.403 -18.306  1.00 90.96
ATOM   1158  O   ALA A 149      12.744  10.412 -18.072  1.00 90.96
ATOM   1159  CB  ALA A 149      15.776  11.125 -16.685  1.00 90.96
ATOM   1160  N   GLU A 150      14.449  10.685 -19.511  1.00 94.50
ATOM   1161  CA  GLU A 150      13.592  11.080 -20.622  1.00 94.50
ATOM   1162  C   GLU A 150      12.717   9.944 -21.146  1.00 94.50
ATOM   1163  O   GLU A 150      11.594  10.198 -21.579  1.00 94.50
ATOM   1164  CB  GLU A 150      14.421  11.625 -21.774  1.00 94.50
ATOM   1165  CG  GLU A 150      15.077  12.969 -21.433  1.00 94.50
ATOM   1166  CD  GLU A 150      15.423  13.753 -22.697  1.00 94.50
ATOM   1167  OE1 GLU A 150      15.825  14.926 -22.579  1.00 94.50
ATOM   1168  OE2 GLU A 150      15.188  13.243 -23.813  1.00 94.50
ATOM   1169  N   TYR A 151      13.171   8.691 -21.087  1.00 96.39
ATOM   1170  CA  TYR A 151      12.310   7.562 -21.412  1.00 96.39
ATOM   1171  C   TYR A 151      11.100   7.516 -20.475  1.00 96.39
ATOM   1172  O   TYR A 151       9.977   7.466 -20.966  1.00 96.39
ATOM   1173  CB  TYR A 151      13.092   6.248 -21.396  1.00 96.39
ATOM   1174  CG  TYR A 151      12.207   5.057 -21.708  1.00 96.39
ATOM   1175  CD1 TYR A 151      11.775   4.212 -20.671  1.00 96.39
ATOM   1176  CD2 TYR A 151      11.764   4.835 -23.025  1.00 96.39
ATOM   1177  CE1 TYR A 151      10.895   3.149 -20.946  1.00 96.39
ATOM   1178  CE2 TYR A 151      10.889   3.768 -23.306  1.00 96.39
ATOM   1179  CZ  TYR A 151      10.454   2.927 -22.264  1.00 96.39
ATOM   1180  OH  TYR A 151       9.606   1.898 -22.514  1.00 96.39
ATOM   1181  N   PHE A 152      11.286   7.629 -19.155  1.00 95.92
ATOM   1182  CA  PHE A 152      10.157   7.664 -18.220  1.00 95.92
ATOM   1183  C   PHE A 152       9.270   8.897 -18.440  1.00 95.92
ATOM   1184  O   PHE A 152       8.073   8.781 -18.702  1.00 95.92
ATOM   1185  CB  PHE A 152      10.662   7.621 -16.770  1.00 95.92
ATOM   1186  CG  PHE A 152       9.546   7.530 -15.743  1.00 95.92
ATOM   1187  CD1 PHE A 152       9.354   8.565 -14.808  1.00 95.92
ATOM   1188  CD2 PHE A 152       8.679   6.421 -15.732  1.00 95.92
ATOM   1189  CE1 PHE A 152       8.323   8.477 -13.855  1.00 95.92
ATOM   1190  CE2 PHE A 152       7.642   6.334 -14.785  1.00 95.92
ATOM   1191  CZ  PHE A 152       7.466   7.361 -13.844  1.00 95.92
ATOM   1192  N   GLU A 153       9.848  10.095 -18.372  1.00 94.33
ATOM   1193  CA  GLU A 153       9.080  11.342 -18.352  1.00 94.33
ATOM   1194  C   GLU A 153       8.497  11.701 -19.721  1.00 94.33
ATOM   1195  O   GLU A 153       7.374  12.193 -19.811  1.00 94.33
ATOM   1196  CB  GLU A 153       9.965  12.486 -17.844  1.00 94.33
ATOM   1197  CG  GLU A 153      10.353  12.302 -16.368  1.00 94.33
ATOM   1198  CD  GLU A 153      11.245  13.431 -15.833  1.00 94.33
ATOM   1199  OE1 GLU A 153      11.465  13.433 -14.599  1.00 94.33
ATOM   1200  OE2 GLU A 153      11.684  14.283 -16.637  1.00 94.33
ATOM   1201  N   ARG A 154       9.225  11.458 -20.813  1.00 95.43
ATOM   1202  CA  ARG A 154       8.814  11.863 -22.165  1.00 95.43
ATOM   1203  C   ARG A 154       8.325  10.690 -23.000  1.00 95.43
ATOM   1204  O   ARG A 154       7.307  10.846 -23.665  1.00 95.43
ATOM   1205  CB  ARG A 154       9.939  12.633 -22.881  1.00 95.43
ATOM   1206  CG  ARG A 154      10.466  13.838 -22.078  1.00 95.43
ATOM   1207  CD  ARG A 154      11.612  14.554 -22.804  1.00 95.43
ATOM   1208  NE  ARG A 154      11.182  15.119 -24.095  1.00 95.43
ATOM   1209  CZ  ARG A 154      10.953  16.375 -24.413  1.00 95.43
ATOM   1210  NH1 ARG A 154      11.080  17.342 -23.546  1.00 95.43
ATOM   1211  NH2 ARG A 154      10.605  16.672 -25.631  1.00 95.43
ATOM   1212  N   GLY A 155       9.000   9.545 -22.942  1.00 95.36
ATOM   1213  CA  GLY A 155       8.618   8.343 -23.688  1.00 95.36
ATOM   1214  C   GLY A 155       7.370   7.659 -23.125  1.00 95.36
ATOM   1215  O   GLY A 155       6.425   7.385 -23.862  1.00 95.36
ATOM   1216  N   VAL A 156       7.329   7.418 -21.814  1.00 96.87
ATOM   1217  CA  VAL A 156       6.238   6.692 -21.147  1.00 96.87
ATOM   1218  C   VAL A 156       5.118   7.649 -20.741  1.00 96.87
ATOM   1219  O   VAL A 156       3.978   7.487 -21.178  1.00 96.87
ATOM   1220  CB  VAL A 156       6.769   5.858 -19.961  1.00 96.87
ATOM   1221  CG1 VAL A 156       5.645   5.079 -19.274  1.00 96.87
ATOM   1222  CG2 VAL A 156       7.818   4.842 -20.427  1.00 96.87
ATOM   1223  N   LEU A 157       5.434   8.676 -19.946  1.00 96.17
ATOM   1224  CA  LEU A 157       4.433   9.596 -19.394  1.00 96.17
ATOM   1225  C   LEU A 157       3.986  10.684 -20.377  1.00 96.17
ATOM   1226  O   LEU A 157       2.858  11.151 -20.280  1.00 96.17
ATOM   1227  CB  LEU A 157       4.976  10.234 -18.103  1.00 96.17
ATOM   1228  CG  LEU A 157       5.272   9.263 -16.945  1.00 96.17
ATOM   1229  CD1 LEU A 157       5.783  10.069 -15.750  1.00 96.17
ATOM   1230  CD2 LEU A 157       4.036   8.478 -16.510  1.00 96.17
ATOM   1231  N   HIS A 158       4.843  11.085 -21.324  1.00 95.64
ATOM   1232  CA  HIS A 158       4.632  12.281 -22.157  1.00 95.64
ATOM   1233  C   HIS A 158       4.382  13.554 -21.327  1.00 95.64
ATOM   1234  O   HIS A 158       3.632  14.442 -21.731  1.00 95.64
ATOM   1235  CB  HIS A 158       3.548  12.051 -23.219  1.00 95.64
ATOM   1236  CG  HIS A 158       3.891  11.020 -24.256  1.00 95.64
ATOM   1237  ND1 HIS A 158       4.161   9.686 -24.054  1.00 95.64
ATOM   1238  CD2 HIS A 158       3.979  11.245 -25.601  1.00 95.64
ATOM   1239  CE1 HIS A 158       4.418   9.133 -25.250  1.00 95.64
ATOM   1240  NE2 HIS A 158       4.270  10.038 -26.232  1.00 95.64
ATOM   1241  N   LEU A 159       5.053  13.665 -20.180  1.00 93.40
ATOM   1242  CA  LEU A 159       4.912  14.760 -19.224  1.00 93.40
ATOM   1243  C   LEU A 159       5.171  16.133 -19.856  1.00 93.40
ATOM   1244  O   LEU A 159       4.504  17.102 -19.528  1.00 93.40
ATOM   1245  CB  LEU A 159       5.891  14.487 -18.069  1.00 93.40
ATOM   1246  CG  LEU A 159       5.796  15.499 -16.916  1.00 93.40
ATOM   1247  CD1 LEU A 159       4.383  15.536 -16.339  1.00 93.40
ATOM   1248  CD2 LEU A 159       6.786  15.104 -15.821  1.00 93.40
ATOM   1249  N   HIS A 160       6.081  16.204 -20.831  1.00 92.35
ATOM   1250  CA  HIS A 160       6.383  17.420 -21.597  1.00 92.35
ATOM   1251  C   HIS A 160       5.192  17.986 -22.398  1.00 92.35
ATOM   1252  O   HIS A 160       5.286  19.093 -22.919  1.00 92.35
ATOM   1253  CB  HIS A 160       7.558  17.123 -22.542  1.00 92.35
ATOM   1254  CG  HIS A 160       7.227  16.118 -23.623  1.00 92.35
ATOM   1255  ND1 HIS A 160       7.285  14.747 -23.510  1.00 92.35
ATOM   1256  CD2 HIS A 160       6.782  16.393 -24.889  1.00 92.35
ATOM   1257  CE1 HIS A 160       6.890  14.209 -24.676  1.00 92.35
ATOM   1258  NE2 HIS A 160       6.571  15.177 -25.550  1.00 92.35
ATOM   1259  N   GLN A 161       4.103  17.225 -22.543  1.00 93.81
ATOM   1260  CA  GLN A 161       2.861  17.646 -23.198  1.00 93.81
ATOM   1261  C   GLN A 161       1.806  18.154 -22.204  1.00 93.81
ATOM   1262  O   GLN A 161       0.661  18.342 -22.602  1.00 93.81
ATOM   1263  CB  GLN A 161       2.274  16.479 -24.006  1.00 93.81
ATOM   1264  CG  GLN A 161       3.230  15.892 -25.041  1.00 93.81
ATOM   1265  CD  GLN A 161       2.592  14.824 -25.925  1.00 93.81
ATOM   1266  OE1 GLN A 161       1.501  14.292 -25.708  1.00 93.81
ATOM   1267  NE2 GLN A 161       3.290  14.454 -26.976  1.00 93.81
ATOM   1268  N   SER A 162       2.157  18.287 -20.924  1.00 94.51
ATOM   1269  CA  SER A 162       1.297  18.798 -19.861  1.00 94.51
ATOM   1270  C   SER A 162       1.999  19.950 -19.156  1.00 94.51
ATOM   1271  O   SER A 162       3.190  19.877 -18.849  1.00 94.51
ATOM   1272  CB  SER A 162       0.988  17.679 -18.865  1.00 94.51
ATOM   1273  OG  SER A 162       0.327  18.175 -17.720  1.00 94.51
ATOM   1274  N   HIS A 163       1.256  21.014 -18.869  1.00 92.08
ATOM   1275  CA  HIS A 163       1.763  22.145 -18.089  1.00 92.08
ATOM   1276  C   HIS A 163       1.569  21.992 -16.570  1.00 92.08
ATOM   1277  O   HIS A 163       2.029  22.843 -15.807  1.00 92.08
ATOM   1278  CB  HIS A 163       1.132  23.429 -18.635  1.00 92.08
ATOM   1279  CG  HIS A 163       1.603  23.743 -20.032  1.00 92.08
ATOM   1280  ND1 HIS A 163       2.834  24.262 -20.361  1.00 92.08
ATOM   1281  CD2 HIS A 163       0.925  23.534 -21.204  1.00 92.08
ATOM   1282  CE1 HIS A 163       2.892  24.374 -21.698  1.00 92.08
ATOM   1283  NE2 HIS A 163       1.748  23.958 -22.256  1.00 92.08
ATOM   1284  N   GLY A 164       0.886  20.940 -16.111  1.00 93.18
ATOM   1285  CA  GLY A 164       0.546  20.758 -14.702  1.00 93.18
ATOM   1286  C   GLY A 164      -0.761  20.000 -14.492  1.00 93.18
ATOM   1287  O   GLY A 164      -1.345  19.447 -15.422  1.00 93.18
ATOM   1288  N   ILE A 165      -1.260  20.017 -13.255  1.00 94.07
ATOM   1289  CA  ILE A 165      -2.515  19.341 -12.891  1.00 94.07
ATOM   1290  C   ILE A 165      -3.764  19.968 -13.546  1.00 94.07
ATOM   1291  O   ILE A 165      -4.755  19.273 -13.751  1.00 94.07
ATOM   1292  CB  ILE A 165      -2.614  19.237 -11.354  1.00 94.07
ATOM   1293  CG1 ILE A 165      -3.699  18.215 -10.954  1.00 94.07
ATOM   1294  CG2 ILE A 165      -2.840  20.601 -10.688  1.00 94.07
ATOM   1295  CD1 ILE A 165      -3.745  17.904  -9.455  1.00 94.07
ATOM   1296  N   ASP A 166      -3.700  21.246 -13.933  1.00 93.44
ATOM   1297  CA  ASP A 166      -4.748  21.941 -14.700  1.00 93.44
ATOM   1298  C   ASP A 166      -4.826  21.493 -16.176  1.00 93.44
ATOM   1299  O   ASP A 166      -5.819  21.753 -16.854  1.00 93.44
ATOM   1300  CB  ASP A 166      -4.490  23.457 -14.628  1.00 93.44
ATOM   1301  CG  ASP A 166      -4.684  24.031 -13.223  1.00 93.44
ATOM   1302  OD1 ASP A 166      -5.838  24.045 -12.755  1.00 93.44
ATOM   1303  OD2 ASP A 166      -3.690  24.465 -12.600  1.00 93.44
ATOM   1304  N   ASP A 167      -3.794  20.809 -16.682  1.00 94.55
ATOM   1305  CA  ASP A 167      -3.666  20.384 -18.078  1.00 94.55
ATOM   1306  C   ASP A 167      -3.280  18.902 -18.158  1.00 94.55
ATOM   1307  O   ASP A 167      -2.140  18.523 -18.426  1.00 94.55
ATOM   1308  CB  ASP A 167      -2.672  21.293 -18.807  1.00 94.55
ATOM   1309  CG  ASP A 167      -2.457  20.851 -20.257  1.00 94.55
ATOM   1310  OD1 ASP A 167      -3.418  20.318 -20.867  1.00 94.55
ATOM   1311  OD2 ASP A 167      -1.312  21.048 -20.720  1.00 94.55
ATOM   1312  N   LEU A 168      -4.244  18.025 -17.881  1.00 94.29
ATOM   1313  CA  LEU A 168      -3.986  16.585 -17.827  1.00 94.29
ATOM   1314  C   LEU A 168      -3.681  15.970 -19.199  1.00 94.29
ATOM   1315  O   LEU A 168      -3.016  14.936 -19.262  1.00 94.29
ATOM   1316  CB  LEU A 168      -5.177  15.882 -17.155  1.00 94.29
ATOM   1317  CG  LEU A 168      -5.390  16.257 -15.676  1.00 94.29
ATOM   1318  CD1 LEU A 168      -6.541  15.421 -15.112  1.00 94.29
ATOM   1319  CD2 LEU A 168      -4.152  16.002 -14.816  1.00 94.29
ATOM   1320  N   GLY A 169      -4.163  16.565 -20.290  1.00 94.31
ATOM   1321  CA  GLY A 169      -4.129  15.953 -21.617  1.00 94.31
ATOM   1322  C   GLY A 169      -4.909  14.623 -21.711  1.00 94.31
ATOM   1323  O   GLY A 169      -5.600  14.215 -20.773  1.00 94.31
ATOM   1324  N   PRO A 170      -4.831  13.915 -22.853  1.00 95.07
ATOM   1325  CA  PRO A 170      -5.548  12.658 -23.047  1.00 95.07
ATOM   1326  C   PRO A 170      -4.845  11.463 -22.374  1.00 95.07
ATOM   1327  O   PRO A 170      -3.606  11.420 -22.376  1.00 95.07
ATOM   1328  CB  PRO A 170      -5.658  12.452 -24.560  1.00 95.07
ATOM   1329  CG  PRO A 170      -4.751  13.505 -25.203  1.00 95.07
ATOM   1330  CD  PRO A 170      -4.131  14.313 -24.062  1.00 95.07
ATOM   1331  N   PRO A 171      -5.601  10.442 -21.911  1.00 95.84
ATOM   1332  CA  PRO A 171      -5.046   9.166 -21.455  1.00 95.84
ATOM   1333  C   PRO A 171      -4.097   8.557 -22.492  1.00 95.84
ATOM   1334  O   PRO A 171      -4.422   8.479 -23.680  1.00 95.84
ATOM   1335  CB  PRO A 171      -6.245   8.246 -21.194  1.00 95.84
ATOM   1336  CG  PRO A 171      -7.393   9.215 -20.924  1.00 95.84
ATOM   1337  CD  PRO A 171      -7.056  10.411 -21.814  1.00 95.84
ATOM   1338  N   ARG A 172      -2.911   8.117 -22.062  1.00 95.70
ATOM   1339  CA  ARG A 172      -1.945   7.447 -22.943  1.00 95.70
ATOM   1340  C   ARG A 172      -2.436   6.053 -23.280  1.00 95.70
ATOM   1341  O   ARG A 172      -2.641   5.237 -22.383  1.00 95.70
ATOM   1342  CB  ARG A 172      -0.558   7.402 -22.284  1.00 95.70
ATOM   1343  CG  ARG A 172       0.119   8.770 -22.107  1.00 95.70
ATOM   1344  CD  ARG A 172       0.400   9.477 -23.439  1.00 95.70
ATOM   1345  NE  ARG A 172      -0.785  10.187 -23.954  1.00 95.70
ATOM   1346  CZ  ARG A 172      -0.756  11.155 -24.846  1.00 95.70
ATOM   1347  NH1 ARG A 172       0.306  11.429 -25.555  1.00 95.70
ATOM   1348  NH2 ARG A 172      -1.811  11.897 -24.990  1.00 95.70
ATOM   1349  N   TRP A 173      -2.609   5.758 -24.567  1.00 96.45
ATOM   1350  CA  TRP A 173      -3.208   4.491 -24.986  1.00 96.45
ATOM   1351  C   TRP A 173      -2.340   3.281 -24.600  1.00 96.45
ATOM   1352  O   TRP A 173      -2.893   2.257 -24.209  1.00 96.45
ATOM   1353  CB  TRP A 173      -3.528   4.524 -26.485  1.00 96.45
ATOM   1354  CG  TRP A 173      -2.366   4.283 -27.394  1.00 96.45
ATOM   1355  CD1 TRP A 173      -1.594   5.228 -27.976  1.00 96.45
ATOM   1356  CD2 TRP A 173      -1.807   2.998 -27.807  1.00 96.45
ATOM   1357  NE1 TRP A 173      -0.613   4.617 -28.731  1.00 96.45
ATOM   1358  CE2 TRP A 173      -0.683   3.245 -28.647  1.00 96.45
ATOM   1359  CE3 TRP A 173      -2.123   1.650 -27.531  1.00 96.45
ATOM   1360  CZ2 TRP A 173       0.096   2.210 -29.183  1.00 96.45
ATOM   1361  CZ3 TRP A 173      -1.349   0.602 -28.064  1.00 96.45
ATOM   1362  CH2 TRP A 173      -0.242   0.879 -28.887  1.00 96.45
ATOM   1363  N   GLN A 174      -1.004   3.404 -24.619  1.00 97.41
ATOM   1364  CA  GLN A 174      -0.086   2.332 -24.210  1.00 97.41
ATOM   1365  C   GLN A 174      -0.219   2.014 -22.716  1.00 97.41
ATOM   1366  O   GLN A 174      -0.350   0.850 -22.338  1.00 97.41
ATOM   1367  CB  GLN A 174       1.383   2.689 -24.507  1.00 97.41
ATOM   1368  CG  GLN A 174       1.723   2.936 -25.984  1.00 97.41
ATOM   1369  CD  GLN A 174       1.554   4.389 -26.427  1.00 97.41
ATOM   1370  OE1 GLN A 174       0.817   5.178 -25.851  1.00 97.41
ATOM   1371  NE2 GLN A 174       2.246   4.807 -27.466  1.00 97.41
ATOM   1372  N   LEU A 175      -0.228   3.047 -21.865  1.00 97.87
ATOM   1373  CA  LEU A 175      -0.428   2.882 -20.424  1.00 97.87
ATOM   1374  C   LEU A 175      -1.840   2.411 -20.103  1.00 97.87
ATOM   1375  O   LEU A 175      -2.013   1.553 -19.247  1.00 97.87
ATOM   1376  CB  LEU A 175      -0.142   4.198 -19.684  1.00 97.87
ATOM   1377  CG  LEU A 175       1.330   4.637 -19.695  1.00 97.87
ATOM   1378  CD1 LEU A 175       1.477   5.888 -18.831  1.00 97.87
ATOM   1379  CD2 LEU A 175       2.229   3.525 -19.150  1.00 97.87
ATOM   1380  N   THR A 176      -2.839   2.908 -20.830  1.00 98.12
ATOM   1381  CA  THR A 176      -4.230   2.464 -20.702  1.00 98.12
ATOM   1382  C   THR A 176      -4.357   0.980 -21.048  1.00 98.12
ATOM   1383  O   THR A 176      -5.007   0.245 -20.315  1.00 98.12
ATOM   1384  CB  THR A 176      -5.165   3.304 -21.584  1.00 98.12
ATOM   1385  OG1 THR A 176      -5.045   4.671 -21.265  1.00 98.12
ATOM   1386  CG2 THR A 176      -6.632   2.934 -21.383  1.00 98.12
ATOM   1387  N   ALA A 177      -3.691   0.500 -22.104  1.00 98.30
ATOM   1388  CA  ALA A 177      -3.669  -0.920 -22.457  1.00 98.30
ATOM   1389  C   ALA A 177      -2.975  -1.778 -21.384  1.00 98.30
ATOM   1390  O   ALA A 177      -3.490  -2.835 -21.015  1.00 98.30
ATOM   1391  CB  ALA A 177      -2.999  -1.074 -23.828  1.00 98.30
ATOM   1392  N   CYS A 178      -1.849  -1.308 -20.834  1.00 98.43
ATOM   1393  CA  CYS A 178      -1.181  -1.974 -19.711  1.00 98.43
ATOM   1394  C   CYS A 178      -2.089  -2.016 -18.475  1.00 98.43
ATOM   1395  O   CYS A 178      -2.232  -3.061 -17.849  1.00 98.43
ATOM   1396  CB  CYS A 178       0.147  -1.270 -19.397  1.00 98.43
ATOM   1397  SG  CYS A 178       1.294  -1.445 -20.792  1.00 98.43
ATOM   1398  N   LEU A 179      -2.763  -0.909 -18.165  1.00 98.00
ATOM   1399  CA  LEU A 179      -3.709  -0.810 -17.062  1.00 98.00
ATOM   1400  C   LEU A 179      -4.899  -1.765 -17.251  1.00 98.00
ATOM   1401  O   LEU A 179      -5.270  -2.450 -16.304  1.00 98.00
ATOM   1402  CB  LEU A 179      -4.136   0.661 -16.933  1.00 98.00
ATOM   1403  CG  LEU A 179      -5.097   0.928 -15.768  1.00 98.00
ATOM   1404  CD1 LEU A 179      -4.439   0.737 -14.401  1.00 98.00
ATOM   1405  CD2 LEU A 179      -5.644   2.350 -15.874  1.00 98.00
ATOM   1406  N   VAL A 180      -5.456  -1.888 -18.462  1.00 98.33
ATOM   1407  CA  VAL A 180      -6.499  -2.887 -18.767  1.00 98.33
ATOM   1408  C   VAL A 180      -5.997  -4.298 -18.457  1.00 98.33
ATOM   1409  O   VAL A 180      -6.703  -5.061 -17.802  1.00 98.33
ATOM   1410  CB  VAL A 180      -6.978  -2.788 -20.232  1.00 98.33
ATOM   1411  CG1 VAL A 180      -7.848  -3.979 -20.662  1.00 98.33
ATOM   1412  CG2 VAL A 180      -7.827  -1.530 -20.446  1.00 98.33
ATOM   1413  N   LEU A 181      -4.776  -4.646 -18.869  1.00 98.16
ATOM   1414  CA  LEU A 181      -4.206  -5.964 -18.584  1.00 98.16
ATOM   1415  C   LEU A 181      -4.000  -6.190 -17.076  1.00 98.16
ATOM   1416  O   LEU A 181      -4.358  -7.252 -16.573  1.00 98.16
ATOM   1417  CB  LEU A 181      -2.919  -6.140 -19.407  1.00 98.16
ATOM   1418  CG  LEU A 181      -2.216  -7.499 -19.223  1.00 98.16
ATOM   1419  CD1 LEU A 181      -3.142  -8.697 -19.460  1.00 98.16
ATOM   1420  CD2 LEU A 181      -1.074  -7.630 -20.233  1.00 98.16
ATOM   1421  N   VAL A 182      -3.508  -5.191 -16.340  1.00 97.88
ATOM   1422  CA  VAL A 182      -3.382  -5.238 -14.870  1.00 97.88
ATOM   1423  C   VAL A 182      -4.735  -5.521 -14.212  1.00 97.88
ATOM   1424  O   VAL A 182      -4.863  -6.440 -13.410  1.00 97.88
ATOM   1425  CB  VAL A 182      -2.763  -3.923 -14.348  1.00 97.88
ATOM   1426  CG1 VAL A 182      -2.872  -3.753 -12.832  1.00 97.88
ATOM   1427  CG2 VAL A 182      -1.276  -3.859 -14.708  1.00 97.88
ATOM   1428  N   ILE A 183      -5.771  -4.789 -14.604  1.00 96.85
ATOM   1429  CA  ILE A 183      -7.139  -4.920 -14.089  1.00 96.85
ATOM   1430  C   ILE A 183      -7.735  -6.298 -14.419  1.00 96.85
ATOM   1431  O   ILE A 183      -8.366  -6.917 -13.563  1.00 96.85
ATOM   1432  CB  ILE A 183      -7.925  -3.716 -14.654  1.00 96.85
ATOM   1433  CG1 ILE A 183      -7.443  -2.402 -13.986  1.00 96.85
ATOM   1434  CG2 ILE A 183      -9.457  -3.787 -14.650  1.00 96.85
ATOM   1435  CD1 ILE A 183      -7.677  -2.233 -12.476  1.00 96.85
ATOM   1436  N   VAL A 184      -7.473  -6.836 -15.614  1.00 97.52
ATOM   1437  CA  VAL A 184      -7.865  -8.204 -15.994  1.00 97.52
ATOM   1438  C   VAL A 184      -7.177  -9.250 -15.111  1.00 97.52
ATOM   1439  O   VAL A 184      -7.845 -10.160 -14.615  1.00 97.52
ATOM   1440  CB  VAL A 184      -7.579  -8.447 -17.489  1.00 97.52
ATOM   1441  CG1 VAL A 184      -7.712  -9.921 -17.887  1.00 97.52
ATOM   1442  CG2 VAL A 184      -8.577  -7.672 -18.360  1.00 97.52
ATOM   1443  N   LEU A 185      -5.866  -9.120 -14.878  1.00 96.47
ATOM   1444  CA  LEU A 185      -5.123 -10.017 -13.986  1.00 96.47
ATOM   1445  C   LEU A 185      -5.695  -9.972 -12.565  1.00 96.47
ATOM   1446  O   LEU A 185      -5.955 -11.015 -11.969  1.00 96.47
ATOM   1447  CB  LEU A 185      -3.626  -9.644 -13.985  1.00 96.47
ATOM   1448  CG  LEU A 185      -2.877  -9.948 -15.295  1.00 96.47
ATOM   1449  CD1 LEU A 185      -1.461  -9.371 -15.221  1.00 96.47
ATOM   1450  CD2 LEU A 185      -2.773 -11.450 -15.564  1.00 96.47
ATOM   1451  N   LEU A 186      -5.966  -8.774 -12.049  1.00 96.73
ATOM   1452  CA  LEU A 186      -6.509  -8.578 -10.709  1.00 96.73
ATOM   1453  C   LEU A 186      -7.921  -9.157 -10.559  1.00 96.73
ATOM   1454  O   LEU A 186      -8.204  -9.831  -9.566  1.00 96.73
ATOM   1455  CB  LEU A 186      -6.480  -7.081 -10.383  1.00 96.73
ATOM   1456  CG  LEU A 186      -5.047  -6.528 -10.200  1.00 96.73
ATOM   1457  CD1 LEU A 186      -4.973  -5.002 -10.287  1.00 96.73
ATOM   1458  CD2 LEU A 186      -4.401  -7.000  -8.899  1.00 96.73
ATOM   1459  N   TYR A 187      -8.788  -8.973 -11.558  1.00 97.32
ATOM   1460  CA  TYR A 187     -10.118  -9.579 -11.574  1.00 97.32
ATOM   1461  C   TYR A 187     -10.042 -11.105 -11.447  1.00 97.32
ATOM   1462  O   TYR A 187     -10.652 -11.680 -10.545  1.00 97.32
ATOM   1463  CB  TYR A 187     -10.863  -9.177 -12.854  1.00 97.32
ATOM   1464  CG  TYR A 187     -12.172  -9.920 -13.031  1.00 97.32
ATOM   1465  CD1 TYR A 187     -12.297 -10.917 -14.020  1.00 97.32
ATOM   1466  CD2 TYR A 187     -13.243  -9.653 -12.161  1.00 97.32
ATOM   1467  CE1 TYR A 187     -13.506 -11.626 -14.158  1.00 97.32
ATOM   1468  CE2 TYR A 187     -14.439 -10.382 -12.276  1.00 97.32
ATOM   1469  CZ  TYR A 187     -14.584 -11.350 -13.288  1.00 97.32
ATOM   1470  OH  TYR A 187     -15.765 -12.006 -13.424  1.00 97.32
ATOM   1471  N   PHE A 188      -9.251 -11.772 -12.294  1.00 96.40
ATOM   1472  CA  PHE A 188      -9.136 -13.234 -12.265  1.00 96.40
ATOM   1473  C   PHE A 188      -8.436 -13.769 -11.009  1.00 96.40
ATOM   1474  O   PHE A 188      -8.714 -14.896 -10.583  1.00 96.40
ATOM   1475  CB  PHE A 188      -8.433 -13.725 -13.534  1.00 96.40
ATOM   1476  CG  PHE A 188      -9.297 -13.667 -14.778  1.00 96.40
ATOM   1477  CD1 PHE A 188     -10.494 -14.407 -14.833  1.00 96.40
ATOM   1478  CD2 PHE A 188      -8.902 -12.907 -15.893  1.00 96.40
ATOM   1479  CE1 PHE A 188     -11.295 -14.379 -15.987  1.00 96.40
ATOM   1480  CE2 PHE A 188      -9.700 -12.888 -17.051  1.00 96.40
ATOM   1481  CZ  PHE A 188     -10.899 -13.616 -17.096  1.00 96.40
ATOM   1482  N   SER A 189      -7.576 -12.970 -10.379  1.00 96.07
ATOM   1483  CA  SER A 189      -6.980 -13.307  -9.086  1.00 96.07
ATOM   1484  C   SER A 189      -7.995 -13.266  -7.935  1.00 96.07
ATOM   1485  O   SER A 189      -7.903 -14.089  -7.020  1.00 96.07
ATOM   1486  CB  SER A 189      -5.811 -12.367  -8.801  1.00 96.07
ATOM   1487  OG  SER A 189      -4.758 -12.630  -9.706  1.00 96.07
ATOM   1488  N   LEU A 190      -8.994 -12.375  -7.990  1.00 95.73
ATOM   1489  CA  LEU A 190      -9.908 -12.076  -6.872  1.00 95.73
ATOM   1490  C   LEU A 190     -11.344 -12.604  -7.023  1.00 95.73
ATOM   1491  O   LEU A 190     -12.029 -12.792  -6.020  1.00 95.73
ATOM   1492  CB  LEU A 190      -9.944 -10.552  -6.671  1.00 95.73
ATOM   1493  CG  LEU A 190      -8.615  -9.923  -6.222  1.00 95.73
ATOM   1494  CD1 LEU A 190      -8.783  -8.407  -6.171  1.00 95.73
ATOM   1495  CD2 LEU A 190      -8.185 -10.425  -4.844  1.00 95.73
ATOM   1496  N   TRP A 191     -11.827 -12.864  -8.241  1.00 94.05
ATOM   1497  CA  TRP A 191     -13.241 -13.187  -8.514  1.00 94.05
ATOM   1498  C   TRP A 191     -13.810 -14.361  -7.696  1.00 94.05
ATOM   1499  O   TRP A 191     -14.959 -14.319  -7.265  1.00 94.05
ATOM   1500  CB  TRP A 191     -13.420 -13.449 -10.018  1.00 94.05
ATOM   1501  CG  TRP A 191     -12.777 -14.680 -10.605  1.00 94.05
ATOM   1502  CD1 TRP A 191     -11.689 -15.340 -10.141  1.00 94.05
ATOM   1503  CD2 TRP A 191     -13.103 -15.339 -11.865  1.00 94.05
ATOM   1504  NE1 TRP A 191     -11.368 -16.388 -10.973  1.00 94.05
ATOM   1505  CE2 TRP A 191     -12.210 -16.435 -12.058  1.00 94.05
ATOM   1506  CE3 TRP A 191     -14.028 -15.083 -12.894  1.00 94.05
ATOM   1507  CZ2 TRP A 191     -12.237 -17.242 -13.206  1.00 94.05
ATOM   1508  CZ3 TRP A 191     -14.057 -15.871 -14.061  1.00 94.05
ATOM   1509  CH2 TRP A 191     -13.168 -16.949 -14.217  1.00 94.05
ATOM   1510  N   LYS A 192     -12.992 -15.382  -7.412  1.00 91.79
ATOM   1511  CA  LYS A 192     -13.344 -16.569  -6.611  1.00 91.79
ATOM   1512  C   LYS A 192     -12.788 -16.497  -5.184  1.00 91.79
ATOM   1513  O   LYS A 192     -12.621 -17.529  -4.532  1.00 91.79
ATOM   1514  CB  LYS A 192     -12.908 -17.842  -7.345  1.00 91.79
ATOM   1515  CG  LYS A 192     -13.698 -18.058  -8.636  1.00 91.79
ATOM   1516  CD  LYS A 192     -13.257 -19.341  -9.343  1.00 91.79
ATOM   1517  CE  LYS A 192     -14.100 -19.443 -10.614  1.00 91.79
ATOM   1518  NZ  LYS A 192     -13.843 -20.691 -11.368  1.00 91.79
ATOM   1519  N   GLY A 193     -12.465 -15.287  -4.740  1.00 91.44
ATOM   1520  CA  GLY A 193     -11.967 -14.966  -3.414  1.00 91.44
ATOM   1521  C   GLY A 193     -10.624 -15.585  -3.070  1.00 91.44
ATOM   1522  O   GLY A 193      -9.746 -15.777  -3.920  1.00 91.44
ATOM   1523  N   VAL A 194     -10.455 -15.917  -1.791  1.00 92.07
ATOM   1524  CA  VAL A 194      -9.154 -16.334  -1.244  1.00 92.07
ATOM   1525  C   VAL A 194      -8.636 -17.650  -1.831  1.00 92.07
ATOM   1526  O   VAL A 194      -7.444 -17.942  -1.760  1.00 92.07
ATOM   1527  CB  VAL A 194      -9.179 -16.385   0.291  1.00 92.07
ATOM   1528  CG1 VAL A 194      -9.393 -14.985   0.869  1.00 92.07
ATOM   1529  CG2 VAL A 194     -10.226 -17.351   0.858  1.00 92.07
ATOM   1530  N   LYS A 195      -9.499 -18.447  -2.477  1.00 90.40
ATOM   1531  CA  LYS A 195      -9.113 -19.711  -3.128  1.00 90.40
ATOM   1532  C   LYS A 195      -8.299 -19.519  -4.407  1.00 90.40
ATOM   1533  O   LYS A 195      -7.483 -20.386  -4.726  1.00 90.40
ATOM   1534  CB  LYS A 195     -10.362 -20.535  -3.454  1.00 90.40
ATOM   1535  CG  LYS A 195     -11.089 -21.018  -2.196  1.00 90.40
ATOM   1536  CD  LYS A 195     -12.315 -21.844  -2.595  1.00 90.40
ATOM   1537  CE  LYS A 195     -13.104 -22.200  -1.336  1.00 90.40
ATOM   1538  NZ  LYS A 195     -14.430 -22.773  -1.669  1.00 90.40
ATOM   1539  N   THR A 196      -8.552 -18.456  -5.174  1.00 92.10
ATOM   1540  CA  THR A 196      -7.733 -18.105  -6.347  1.00 92.10
ATOM   1541  C   THR A 196      -6.529 -17.292  -5.927  1.00 92.10
ATOM   1542  O   THR A 196      -5.418 -17.654  -6.309  1.00 92.10
ATOM   1543  CB  THR A 196      -8.521 -17.365  -7.438  1.00 92.10
ATOM   1544  OG1 THR A 196      -9.407 -16.414  -6.903  1.00 92.10
ATOM   1545  CG2 THR A 196      -9.351 -18.378  -8.225  1.00 92.10
ATOM   1546  N   SER A 197      -6.731 -16.297  -5.058  1.00 92.26
ATOM   1547  CA  SER A 197      -5.648 -15.477  -4.513  1.00 92.26
ATOM   1548  C   SER A 197      -4.549 -16.347  -3.893  1.00 92.26
ATOM   1549  O   SER A 197      -3.399 -16.286  -4.319  1.00 92.26
ATOM   1550  CB  SER A 197      -6.224 -14.483  -3.501  1.00 92.26
ATOM   1551  OG  SER A 197      -5.182 -13.757  -2.893  1.00 92.26
ATOM   1552  N   GLY A 198      -4.925 -17.300  -3.031  1.00 92.64
ATOM   1553  CA  GLY A 198      -3.997 -18.231  -2.385  1.00 92.64
ATOM   1554  C   GLY A 198      -3.191 -19.130  -3.332  1.00 92.64
ATOM   1555  O   GLY A 198      -2.206 -19.712  -2.898  1.00 92.64
ATOM   1556  N   LYS A 199      -3.568 -19.260  -4.613  1.00 94.12
ATOM   1557  CA  LYS A 199      -2.779 -19.980  -5.633  1.00 94.12
ATOM   1558  C   LYS A 199      -1.836 -19.055  -6.392  1.00 94.12
ATOM   1559  O   LYS A 199      -0.724 -19.467  -6.701  1.00 94.12
ATOM   1560  CB  LYS A 199      -3.698 -20.681  -6.636  1.00 94.12
ATOM   1561  CG  LYS A 199      -4.502 -21.814  -5.997  1.00 94.12
ATOM   1562  CD  LYS A 199      -5.480 -22.368  -7.032  1.00 94.12
ATOM   1563  CE  LYS A 199      -6.358 -23.432  -6.381  1.00 94.12
ATOM   1564  NZ  LYS A 199      -7.385 -23.909  -7.336  1.00 94.12
ATOM   1565  N   VAL A 200      -2.286 -17.840  -6.698  1.00 95.48
ATOM   1566  CA  VAL A 200      -1.493 -16.833  -7.419  1.00 95.48
ATOM   1567  C   VAL A 200      -0.270 -16.429  -6.589  1.00 95.48
ATOM   1568  O   VAL A 200       0.843 -16.451  -7.115  1.00 95.48
ATOM   1569  CB  VAL A 200      -2.379 -15.627  -7.792  1.00 95.48
ATOM   1570  CG1 VAL A 200      -1.579 -14.504  -8.456  1.00 95.48
ATOM   1571  CG2 VAL A 200      -3.486 -16.053  -8.771  1.00 95.48
ATOM   1572  N   VAL A 201      -0.453 -16.232  -5.275  1.00 96.27
ATOM   1573  CA  VAL A 201       0.610 -15.823  -4.330  1.00 96.27
ATOM   1574  C   VAL A 201       1.801 -16.777  -4.255  1.00 96.27
ATOM   1575  O   VAL A 201       2.893 -16.368  -3.880  1.00 96.27
ATOM   1576  CB  VAL A 201       0.067 -15.548  -2.919  1.00 96.27
ATOM   1577  CG1 VAL A 201      -0.935 -14.387  -2.956  1.00 96.27
ATOM   1578  CG2 VAL A 201      -0.558 -16.796  -2.288  1.00 96.27
ATOM   1579  N   TRP A 202       1.649 -18.045  -4.648  1.00 96.00
ATOM   1580  CA  TRP A 202       2.786 -18.971  -4.703  1.00 96.00
ATOM   1581  C   TRP A 202       3.836 -18.555  -5.728  1.00 96.00
ATOM   1582  O   TRP A 202       5.010 -18.863  -5.541  1.00 96.00
ATOM   1583  CB  TRP A 202       2.304 -20.387  -5.015  1.00 96.00
ATOM   1584  CG  TRP A 202       1.831 -21.137  -3.818  1.00 96.00
ATOM   1585  CD1 TRP A 202       0.578 -21.133  -3.320  1.00 96.00
ATOM   1586  CD2 TRP A 202       2.619 -21.956  -2.911  1.00 96.00
ATOM   1587  NE1 TRP A 202       0.522 -21.906  -2.174  1.00 96.00
ATOM   1588  CE2 TRP A 202       1.755 -22.458  -1.895  1.00 96.00
ATOM   1589  CE3 TRP A 202       3.983 -22.314  -2.843  1.00 96.00
ATOM   1590  CZ2 TRP A 202       2.215 -23.308  -0.881  1.00 96.00
ATOM   1591  CZ3 TRP A 202       4.459 -23.148  -1.815  1.00 96.00
ATOM   1592  CH2 TRP A 202       3.579 -23.648  -0.838  1.00 96.00
ATOM   1593  N   ILE A 203       3.423 -17.879  -6.800  1.00 95.51
ATOM   1594  CA  ILE A 203       4.329 -17.341  -7.815  1.00 95.51
ATOM   1595  C   ILE A 203       4.695 -15.906  -7.446  1.00 95.51
ATOM   1596  O   ILE A 203       5.878 -15.572  -7.405  1.00 95.51
ATOM   1597  CB  ILE A 203       3.693 -17.446  -9.220  1.00 95.51
ATOM   1598  CG1 ILE A 203       3.431 -18.929  -9.578  1.00 95.51
ATOM   1599  CG2 ILE A 203       4.605 -16.785 -10.274  1.00 95.51
ATOM   1600  CD1 ILE A 203       2.656 -19.139 -10.885  1.00 95.51
ATOM   1601  N   THR A 204       3.698 -15.069  -7.162  1.00 96.08
ATOM   1602  CA  THR A 204       3.901 -13.626  -7.000  1.00 96.08
ATOM   1603  C   THR A 204       4.655 -13.261  -5.721  1.00 96.08
ATOM   1604  O   THR A 204       5.559 -12.434  -5.798  1.00 96.08
ATOM   1605  CB  THR A 204       2.579 -12.858  -7.120  1.00 96.08
ATOM   1606  OG1 THR A 204       1.593 -13.498  -6.370  1.00 96.08
ATOM   1607  CG2 THR A 204       2.030 -12.876  -8.546  1.00 96.08
ATOM   1608  N   ALA A 205       4.436 -13.960  -4.601  1.00 95.90
ATOM   1609  CA  ALA A 205       5.131 -13.654  -3.346  1.00 95.90
ATOM   1610  C   ALA A 205       6.541 -14.270  -3.275  1.00 95.90
ATOM   1611  O   ALA A 205       7.379 -13.834  -2.488  1.00 95.90
ATOM   1612  CB  ALA A 205       4.266 -14.108  -2.162  1.00 95.90
ATOM   1613  N   THR A 206       6.826 -15.307  -4.072  1.00 95.46
ATOM   1614  CA  THR A 206       8.118 -16.020  -4.028  1.00 95.46
ATOM   1615  C   THR A 206       9.125 -15.501  -5.051  1.00 95.46
ATOM   1616  O   THR A 206      10.319 -15.441  -4.748  1.00 95.46
ATOM   1617  CB  THR A 206       7.957 -17.536  -4.185  1.00 95.46
ATOM   1618  OG1 THR A 206       7.460 -17.859  -5.460  1.00 95.46
ATOM   1619  CG2 THR A 206       7.045 -18.152  -3.123  1.00 95.46
ATOM   1620  N   MET A 207       8.668 -15.081  -6.236  1.00 94.85
ATOM   1621  CA  MET A 207       9.527 -14.541  -7.295  1.00 94.85
ATOM   1622  C   MET A 207      10.411 -13.368  -6.848  1.00 94.85
ATOM   1623  O   MET A 207      11.607 -13.403  -7.150  1.00 94.85
ATOM   1624  CB  MET A 207       8.688 -14.144  -8.525  1.00 94.85
ATOM   1625  CG  MET A 207       8.593 -15.301  -9.518  1.00 94.85
ATOM   1626  SD  MET A 207      10.191 -15.714 -10.281  1.00 94.85
ATOM   1627  CE  MET A 207       9.719 -17.188 -11.215  1.00 94.85
ATOM   1628  N   PRO A 208       9.912 -12.373  -6.087  1.00 95.30
ATOM   1629  CA  PRO A 208      10.726 -11.246  -5.648  1.00 95.30
ATOM   1630  C   PRO A 208      11.987 -11.662  -4.897  1.00 95.30
ATOM   1631  O   PRO A 208      13.044 -11.086  -5.120  1.00 95.30
ATOM   1632  CB  PRO A 208       9.808 -10.390  -4.774  1.00 95.30
ATOM   1633  CG  PRO A 208       8.428 -10.664  -5.362  1.00 95.30
ATOM   1634  CD  PRO A 208       8.518 -12.133  -5.749  1.00 95.30
ATOM   1635  N   TYR A 209      11.932 -12.716  -4.080  1.00 95.73
ATOM   1636  CA  TYR A 209      13.107 -13.212  -3.361  1.00 95.73
ATOM   1637  C   TYR A 209      14.170 -13.809  -4.282  1.00 95.73
ATOM   1638  O   TYR A 209      15.365 -13.612  -4.046  1.00 95.73
ATOM   1639  CB  TYR A 209      12.667 -14.251  -2.330  1.00 95.73
ATOM   1640  CG  TYR A 209      11.879 -13.633  -1.205  1.00 95.73
ATOM   1641  CD1 TYR A 209      12.561 -12.855  -0.252  1.00 95.73
ATOM   1642  CD2 TYR A 209      10.480 -13.777  -1.142  1.00 95.73
ATOM   1643  CE1 TYR A 209      11.843 -12.211   0.765  1.00 95.73
ATOM   1644  CE2 TYR A 209       9.759 -13.145  -0.114  1.00 95.73
ATOM   1645  CZ  TYR A 209      10.444 -12.355   0.830  1.00 95.73
ATOM   1646  OH  TYR A 209       9.768 -11.704   1.797  1.00 95.73
ATOM   1647  N   VAL A 210      13.757 -14.507  -5.343  1.00 95.59
ATOM   1648  CA  VAL A 210      14.677 -15.026  -6.366  1.00 95.59
ATOM   1649  C   VAL A 210      15.381 -13.862  -7.065  1.00 95.59
ATOM   1650  O   VAL A 210      16.607 -13.864  -7.190  1.00 95.59
ATOM   1651  CB  VAL A 210      13.935 -15.914  -7.388  1.00 95.59
ATOM   1652  CG1 VAL A 210      14.888 -16.463  -8.458  1.00 95.59
ATOM   1653  CG2 VAL A 210      13.266 -17.114  -6.703  1.00 95.59
ATOM   1654  N   VAL A 211      14.621 -12.839  -7.459  1.00 94.66
ATOM   1655  CA  VAL A 211      15.147 -11.674  -8.181  1.00 94.66
ATOM   1656  C   VAL A 211      16.026 -10.798  -7.293  1.00 94.66
ATOM   1657  O   VAL A 211      17.144 -10.480  -7.689  1.00 94.66
ATOM   1658  CB  VAL A 211      14.010 -10.859  -8.817  1.00 94.66
ATOM   1659  CG1 VAL A 211      14.582  -9.649  -9.570  1.00 94.66
ATOM   1660  CG2 VAL A 211      13.196 -11.755  -9.762  1.00 94.66
ATOM   1661  N   LEU A 212      15.585 -10.465  -6.077  1.00 94.30
ATOM   1662  CA  LEU A 212      16.370  -9.693  -5.109  1.00 94.30
ATOM   1663  C   LEU A 212      17.692 -10.385  -4.788  1.00 94.30
ATOM   1664  O   LEU A 212      18.722  -9.723  -4.721  1.00 94.30
ATOM   1665  CB  LEU A 212      15.571  -9.488  -3.808  1.00 94.30
ATOM   1666  CG  LEU A 212      14.439  -8.450  -3.900  1.00 94.30
ATOM   1667  CD1 LEU A 212      13.613  -8.472  -2.613  1.00 94.30
ATOM   1668  CD2 LEU A 212      14.978  -7.030  -4.093  1.00 94.30
ATOM   1669  N   THR A 213      17.691 -11.712  -4.647  1.00 95.56
ATOM   1670  CA  THR A 213      18.926 -12.470  -4.413  1.00 95.56
ATOM   1671  C   THR A 213      19.856 -12.400  -5.626  1.00 95.56
ATOM   1672  O   THR A 213      21.048 -12.146  -5.467  1.00 95.56
ATOM   1673  CB  THR A 213      18.624 -13.929  -4.048  1.00 95.56
ATOM   1674  OG1 THR A 213      17.791 -13.985  -2.914  1.00 95.56
ATOM   1675  CG2 THR A 213      19.891 -14.709  -3.692  1.00 95.56
ATOM   1676  N   ALA A 214      19.337 -12.569  -6.846  1.00 94.47
ATOM   1677  CA  ALA A 214      20.141 -12.468  -8.065  1.00 94.47
ATOM   1678  C   ALA A 214      20.727 -11.058  -8.262  1.00 94.47
ATOM   1679  O   ALA A 214      21.914 -10.918  -8.567  1.00 94.47
ATOM   1680  CB  ALA A 214      19.275 -12.894  -9.257  1.00 94.47
ATOM   1681  N   LEU A 215      19.921 -10.017  -8.036  1.00 93.30
ATOM   1682  CA  LEU A 215      20.352  -8.621  -8.105  1.00 93.30
ATOM   1683  C   LEU A 215      21.331  -8.270  -6.990  1.00 93.30
ATOM   1684  O   LEU A 215      22.266  -7.527  -7.250  1.00 93.30
ATOM   1685  CB  LEU A 215      19.138  -7.683  -8.041  1.00 93.30
ATOM   1686  CG  LEU A 215      18.237  -7.715  -9.283  1.00 93.30
ATOM   1687  CD1 LEU A 215      17.016  -6.837  -9.031  1.00 93.30
ATOM   1688  CD2 LEU A 215      18.948  -7.194 -10.536  1.00 93.30
ATOM   1689  N   LEU A 216      21.178  -8.827  -5.787  1.00 94.92
ATOM   1690  CA  LEU A 216      22.148  -8.657  -4.708  1.00 94.92
ATOM   1691  C   LEU A 216      23.503  -9.235  -5.115  1.00 94.92
ATOM   1692  O   LEU A 216      24.506  -8.531  -5.066  1.00 94.92
ATOM   1693  CB  LEU A 216      21.629  -9.326  -3.421  1.00 94.92
ATOM   1694  CG  LEU A 216      22.574  -9.176  -2.218  1.00 94.92
ATOM   1695  CD1 LEU A 216      22.786  -7.715  -1.820  1.00 94.92
ATOM   1696  CD2 LEU A 216      21.980  -9.916  -1.020  1.00 94.92
ATOM   1697  N   LEU A 217      23.527 -10.497  -5.556  1.00 95.94
ATOM   1698  CA  LEU A 217      24.755 -11.176  -5.974  1.00 95.94
ATOM   1699  C   LEU A 217      25.438 -10.448  -7.133  1.00 95.94
ATOM   1700  O   LEU A 217      26.660 -10.326  -7.141  1.00 95.94
ATOM   1701  CB  LEU A 217      24.438 -12.625  -6.380  1.00 95.94
ATOM   1702  CG  LEU A 217      24.037 -13.554  -5.221  1.00 95.94
ATOM   1703  CD1 LEU A 217      23.636 -14.915  -5.792  1.00 95.94
ATOM   1704  CD2 LEU A 217      25.173 -13.763  -4.219  1.00 95.94
ATOM   1705  N   ARG A 218      24.669  -9.933  -8.098  1.00 94.25
ATOM   1706  CA  ARG A 218      25.225  -9.135  -9.193  1.00 94.25
ATOM   1707  C   ARG A 218      25.696  -7.765  -8.709  1.00 94.25
ATOM   1708  O   ARG A 218      26.825  -7.384  -9.004  1.00 94.25
ATOM   1709  CB  ARG A 218      24.198  -9.035 -10.334  1.00 94.25
ATOM   1710  CG  ARG A 218      24.684  -8.194 -11.526  1.00 94.25
ATOM   1711  CD  ARG A 218      26.013  -8.710 -12.097  1.00 94.25
ATOM   1712  NE  ARG A 218      26.506  -7.853 -13.185  1.00 94.25
ATOM   1713  CZ  ARG A 218      27.710  -7.911 -13.726  1.00 94.25
ATOM   1714  NH1 ARG A 218      28.585  -8.806 -13.359  1.00 94.25
ATOM   1715  NH2 ARG A 218      28.075  -7.054 -14.640  1.00 94.25
ATOM   1716  N   GLY A 219      24.861  -7.052  -7.967  1.00 94.06
ATOM   1717  CA  GLY A 219      25.092  -5.685  -7.516  1.00 94.06
ATOM   1718  C   GLY A 219      26.355  -5.550  -6.672  1.00 94.06
ATOM   1719  O   GLY A 219      27.178  -4.683  -6.944  1.00 94.06
ATOM   1720  N   VAL A 220      26.597  -6.467  -5.726  1.00 96.24
ATOM   1721  CA  VAL A 220      27.810  -6.429  -4.879  1.00 96.24
ATOM   1722  C   VAL A 220      29.113  -6.686  -5.646  1.00 96.24
ATOM   1723  O   VAL A 220      30.186  -6.387  -5.129  1.00 96.24
ATOM   1724  CB  VAL A 220      27.718  -7.385  -3.674  1.00 96.24
ATOM   1725  CG1 VAL A 220      26.526  -7.040  -2.774  1.00 96.24
ATOM   1726  CG2 VAL A 220      27.677  -8.865  -4.080  1.00 96.24
ATOM   1727  N   THR A 221      29.043  -7.232  -6.866  1.00 95.91
ATOM   1728  CA  THR A 221      30.219  -7.467  -7.729  1.00 95.91
ATOM   1729  C   THR A 221      30.542  -6.296  -8.656  1.00 95.91
ATOM   1730  O   THR A 221      31.535  -6.350  -9.382  1.00 95.91
ATOM   1731  CB  THR A 221      30.105  -8.763  -8.552  1.00 95.91
ATOM   1732  OG1 THR A 221      29.068  -8.732  -9.514  1.00 95.91
ATOM   1733  CG2 THR A 221      29.925  -9.995  -7.666  1.00 95.91
ATOM   1734  N   LEU A 222      29.713  -5.247  -8.667  1.00 94.79
ATOM   1735  CA  LEU A 222      29.932  -4.069  -9.500  1.00 94.79
ATOM   1736  C   LEU A 222      30.991  -3.137  -8.885  1.00 94.79
ATOM   1737  O   LEU A 222      31.103  -3.045  -7.658  1.00 94.79
ATOM   1738  CB  LEU A 222      28.599  -3.337  -9.737  1.00 94.79
ATOM   1739  CG  LEU A 222      27.557  -4.142 -10.532  1.00 94.79
ATOM   1740  CD1 LEU A 222      26.241  -3.370 -10.598  1.00 94.79
ATOM   1741  CD2 LEU A 222      28.017  -4.433 -11.965  1.00 94.79
ATOM   1742  N   PRO A 223      31.769  -2.415  -9.713  1.00 95.29
ATOM   1743  CA  PRO A 223      32.702  -1.412  -9.207  1.00 95.29
ATOM   1744  C   PRO A 223      31.933  -0.310  -8.463  1.00 95.29
ATOM   1745  O   PRO A 223      30.829   0.042  -8.858  1.00 95.29
ATOM   1746  CB  PRO A 223      33.466  -0.909 -10.435  1.00 95.29
ATOM   1747  CG  PRO A 223      32.511  -1.160 -11.600  1.00 95.29
ATOM   1748  CD  PRO A 223      31.730  -2.402 -11.170  1.00 95.29
ATOM   1749  N   GLY A 224      32.464   0.183  -7.343  1.00 94.16
ATOM   1750  CA  GLY A 224      31.837   1.279  -6.584  1.00 94.16
ATOM   1751  C   GLY A 224      30.651   0.858  -5.717  1.00 94.16
ATOM   1752  O   GLY A 224      30.208   1.625  -4.863  1.00 94.16
ATOM   1753  N   ALA A 225      30.181  -0.391  -5.835  1.00 95.52
ATOM   1754  CA  ALA A 225      29.105  -0.929  -5.003  1.00 95.52
ATOM   1755  C   ALA A 225      29.397  -0.791  -3.499  1.00 95.52
ATOM   1756  O   ALA A 225      28.494  -0.527  -2.705  1.00 95.52
ATOM   1757  CB  ALA A 225      28.901  -2.399  -5.379  1.00 95.52
ATOM   1758  N   ILE A 226      30.669  -0.916  -3.102  1.00 96.23
ATOM   1759  CA  ILE A 226      31.090  -0.761  -1.707  1.00 96.23
ATOM   1760  C   ILE A 226      30.864   0.656  -1.171  1.00 96.23
ATOM   1761  O   ILE A 226      30.514   0.804  -0.002  1.00 96.23
ATOM   1762  CB  ILE A 226      32.557  -1.208  -1.529  1.00 96.23
ATOM   1763  CG1 ILE A 226      32.966  -1.354  -0.047  1.00 96.23
ATOM   1764  CG2 ILE A 226      33.555  -0.264  -2.228  1.00 96.23
ATOM   1765  CD1 ILE A 226      32.125  -2.372   0.736  1.00 96.23
ATOM   1766  N   ASP A 227      31.018   1.690  -1.999  1.00 94.27
ATOM   1767  CA  ASP A 227      30.805   3.077  -1.579  1.00 94.27
ATOM   1768  C   ASP A 227      29.314   3.355  -1.385  1.00 94.27
ATOM   1769  O   ASP A 227      28.923   3.991  -0.407  1.00 94.27
ATOM   1770  CB  ASP A 227      31.466   4.036  -2.576  1.00 94.27
ATOM   1771  CG  ASP A 227      32.987   3.837  -2.610  1.00 94.27
ATOM   1772  OD1 ASP A 227      33.580   3.592  -1.521  1.00 94.27
ATOM   1773  OD2 ASP A 227      33.547   3.871  -3.725  1.00 94.27
ATOM   1774  N   GLY A 228      28.473   2.754  -2.228  1.00 93.80
ATOM   1775  CA  GLY A 228      27.030   2.688  -2.020  1.00 93.80
ATOM   1776  C   GLY A 228      26.650   2.017  -0.700  1.00 93.80
ATOM   1777  O   GLY A 228      25.919   2.590   0.105  1.00 93.80
ATOM   1778  N   ILE A 229      27.186   0.826  -0.422  1.00 95.20
ATOM   1779  CA  ILE A 229      26.912   0.094   0.829  1.00 95.20
ATOM   1780  C   ILE A 229      27.406   0.878   2.056  1.00 95.20
ATOM   1781  O   ILE A 229      26.732   0.906   3.086  1.00 95.20
ATOM   1782  CB  ILE A 229      27.529  -1.321   0.763  1.00 95.20
ATOM   1783  CG1 ILE A 229      26.805  -2.166  -0.311  1.00 95.20
ATOM   1784  CG2 ILE A 229      27.451  -2.038   2.127  1.00 95.20
ATOM   1785  CD1 ILE A 229      27.561  -3.443  -0.697  1.00 95.20
ATOM   1786  N   ARG A 230      28.555   1.555   1.957  1.00 95.02
ATOM   1787  CA  ARG A 230      29.046   2.453   3.013  1.00 95.02
ATOM   1788  C   ARG A 230      28.105   3.630   3.233  1.00 95.02
ATOM   1789  O   ARG A 230      27.836   3.950   4.383  1.00 95.02
ATOM   1790  CB  ARG A 230      30.439   2.978   2.662  1.00 95.02
ATOM   1791  CG  ARG A 230      31.540   1.937   2.883  1.00 95.02
ATOM   1792  CD  ARG A 230      32.824   2.502   2.277  1.00 95.02
ATOM   1793  NE  ARG A 230      33.961   1.583   2.432  1.00 95.02
ATOM   1794  CZ  ARG A 230      35.059   1.628   1.699  1.00 95.02
ATOM   1795  NH1 ARG A 230      35.218   2.455   0.699  1.00 95.02
ATOM   1796  NH2 ARG A 230      36.039   0.809   1.965  1.00 95.02
ATOM   1797  N   ALA A 231      27.585   4.243   2.171  1.00 91.63
ATOM   1798  CA  ALA A 231      26.599   5.313   2.285  1.00 91.63
ATOM   1799  C   ALA A 231      25.303   4.816   2.945  1.00 91.63
ATOM   1800  O   ALA A 231      24.779   5.481   3.836  1.00 91.63
ATOM   1801  CB  ALA A 231      26.347   5.905   0.896  1.00 91.63
ATOM   1802  N   TYR A 232      24.840   3.617   2.588  1.00 93.07
ATOM   1803  CA  TYR A 232      23.662   2.996   3.192  1.00 93.07
ATOM   1804  C   TYR A 232      23.812   2.780   4.702  1.00 93.07
ATOM   1805  O   TYR A 232      22.912   3.108   5.472  1.00 93.07
ATOM   1806  CB  TYR A 232      23.399   1.647   2.510  1.00 93.07
ATOM   1807  CG  TYR A 232      22.218   0.881   3.069  1.00 93.07
ATOM   1808  CD1 TYR A 232      22.347  -0.489   3.377  1.00 93.07
ATOM   1809  CD2 TYR A 232      21.002   1.546   3.317  1.00 93.07
ATOM   1810  CE1 TYR A 232      21.270  -1.183   3.962  1.00 93.07
ATOM   1811  CE2 TYR A 232      19.927   0.857   3.897  1.00 93.07
ATOM   1812  CZ  TYR A 232      20.068  -0.500   4.238  1.00 93.07
ATOM   1813  OH  TYR A 232      19.024  -1.131   4.825  1.00 93.07
ATOM   1814  N   LEU A 233      24.958   2.241   5.125  1.00 93.67
ATOM   1815  CA  LEU A 233      25.234   1.900   6.523  1.00 93.67
ATOM   1816  C   LEU A 233      25.883   3.041   7.316  1.00 93.67
ATOM   1817  O   LEU A 233      26.137   2.875   8.509  1.00 93.67
ATOM   1818  CB  LEU A 233      26.087   0.621   6.572  1.00 93.67
ATOM   1819  CG  LEU A 233      25.422  -0.627   5.963  1.00 93.67
ATOM   1820  CD1 LEU A 233      26.399  -1.801   6.048  1.00 93.67
ATOM   1821  CD2 LEU A 233      24.132  -1.027   6.684  1.00 93.67
ATOM   1822  N   SER A 234      26.163   4.183   6.684  1.00 92.50
ATOM   1823  CA  SER A 234      26.681   5.365   7.375  1.00 92.50
ATOM   1824  C   SER A 234      25.681   5.821   8.432  1.00 92.50
ATOM   1825  O   SER A 234      24.480   5.752   8.203  1.00 92.50
ATOM   1826  CB  SER A 234      27.019   6.498   6.397  1.00 92.50
ATOM   1827  OG  SER A 234      25.880   7.064   5.781  1.00 92.50
ATOM   1828  N   VAL A 235      26.151   6.230   9.611  1.00 94.23
ATOM   1829  CA  VAL A 235      25.267   6.595  10.727  1.00 94.23
ATOM   1830  C   VAL A 235      25.495   8.052  11.087  1.00 94.23
ATOM   1831  O   VAL A 235      26.489   8.387  11.730  1.00 94.23
ATOM   1832  CB  VAL A 235      25.457   5.671  11.947  1.00 94.23
ATOM   1833  CG1 VAL A 235      24.410   5.986  13.022  1.00 94.23
ATOM   1834  CG2 VAL A 235      25.299   4.189  11.583  1.00 94.23
ATOM   1835  N   ASP A 236      24.558   8.910  10.693  1.00 91.88
ATOM   1836  CA  ASP A 236      24.516  10.302  11.134  1.00 91.88
ATOM   1837  C   ASP A 236      23.533  10.462  12.303  1.00 91.88
ATOM   1838  O   ASP A 236      22.326  10.627  12.122  1.00 91.88
ATOM   1839  CB  ASP A 236      24.199  11.228   9.953  1.00 91.88
ATOM   1840  CG  ASP A 236      24.250  12.709  10.350  1.00 91.88
ATOM   1841  OD1 ASP A 236      24.568  13.000  11.531  1.00 91.88
ATOM   1842  OD2 ASP A 236      23.938  13.539   9.469  1.00 91.88
ATOM   1843  N   PHE A 237      24.052  10.402  13.532  1.00 92.85
ATOM   1844  CA  PHE A 237      23.235  10.519  14.742  1.00 92.85
ATOM   1845  C   PHE A 237      22.559  11.888  14.896  1.00 92.85
ATOM   1846  O   PHE A 237      21.548  11.970  15.595  1.00 92.85
ATOM   1847  CB  PHE A 237      24.084  10.210  15.981  1.00 92.85
ATOM   1848  CG  PHE A 237      24.474   8.752  16.118  1.00 92.85
ATOM   1849  CD1 PHE A 237      23.526   7.814  16.568  1.00 92.85
ATOM   1850  CD2 PHE A 237      25.779   8.328  15.808  1.00 92.85
ATOM   1851  CE1 PHE A 237      23.877   6.462  16.715  1.00 92.85
ATOM   1852  CE2 PHE A 237      26.134   6.976  15.961  1.00 92.85
ATOM   1853  CZ  PHE A 237      25.186   6.044  16.419  1.00 92.85
ATOM   1854  N   TYR A 238      23.053  12.949  14.246  1.00 94.38
ATOM   1855  CA  TYR A 238      22.420  14.268  14.327  1.00 94.38
ATOM   1856  C   TYR A 238      21.037  14.277  13.671  1.00 94.38
ATOM   1857  O   TYR A 238      20.148  14.992  14.138  1.00 94.38
ATOM   1858  CB  TYR A 238      23.327  15.336  13.709  1.00 94.38
ATOM   1859  CG  TYR A 238      24.593  15.587  14.504  1.00 94.38
ATOM   1860  CD1 TYR A 238      24.527  16.334  15.695  1.00 94.38
ATOM   1861  CD2 TYR A 238      25.828  15.078  14.059  1.00 94.38
ATOM   1862  CE1 TYR A 238      25.693  16.582  16.443  1.00 94.38
ATOM   1863  CE2 TYR A 238      26.999  15.321  14.804  1.00 94.38
ATOM   1864  CZ  TYR A 238      26.933  16.075  15.994  1.00 94.38
ATOM   1865  OH  TYR A 238      28.061  16.318  16.711  1.00 94.38
ATOM   1866  N   ARG A 239      20.811  13.413  12.671  1.00 91.66
ATOM   1867  CA  ARG A 239      19.497  13.237  12.036  1.00 91.66
ATOM   1868  C   ARG A 239      18.432  12.736  13.007  1.00 91.66
ATOM   1869  O   ARG A 239      17.269  13.083  12.851  1.00 91.66
ATOM   1870  CB  ARG A 239      19.621  12.299  10.820  1.00 91.66
ATOM   1871  CG  ARG A 239      20.490  12.862   9.688  1.00 91.66
ATOM   1872  CD  ARG A 239      19.946  14.199   9.184  1.00 91.66
ATOM   1873  NE  ARG A 239      20.618  14.642   7.955  1.00 91.66
ATOM   1874  CZ  ARG A 239      20.138  15.559   7.136  1.00 91.66
ATOM   1875  NH1 ARG A 239      19.060  16.241   7.404  1.00 91.66
ATOM   1876  NH2 ARG A 239      20.756  15.815   6.016  1.00 91.66
ATOM   1877  N   LEU A 240      18.798  12.007  14.065  1.00 92.35
ATOM   1878  CA  LEU A 240      17.832  11.524  15.064  1.00 92.35
ATOM   1879  C   LEU A 240      17.157  12.650  15.864  1.00 92.35
ATOM   1880  O   LEU A 240      16.108  12.414  16.468  1.00 92.35
ATOM   1881  CB  LEU A 240      18.513  10.542  16.029  1.00 92.35
ATOM   1882  CG  LEU A 240      19.052   9.260  15.377  1.00 92.35
ATOM   1883  CD1 LEU A 240      19.702   8.390  16.452  1.00 92.35
ATOM   1884  CD2 LEU A 240      17.936   8.446  14.723  1.00 92.35
ATOM   1885  N   CYS A 241      17.733  13.856  15.868  1.00 93.40
ATOM   1886  CA  CYS A 241      17.131  15.042  16.476  1.00 93.40
ATOM   1887  C   CYS A 241      16.004  15.646  15.618  1.00 93.40
ATOM   1888  O   CYS A 241      15.222  16.454  16.120  1.00 93.40
ATOM   1889  CB  CYS A 241      18.234  16.080  16.720  1.00 93.40
ATOM   1890  SG  CYS A 241      19.452  15.457  17.918  1.00 93.40
ATOM   1891  N   GLU A 242      15.907  15.284  14.337  1.00 90.47
ATOM   1892  CA  GLU A 242      14.882  15.792  13.429  1.00 90.47
ATOM   1893  C   GLU A 242      13.596  14.961  13.533  1.00 90.47
ATOM   1894  O   GLU A 242      13.589  13.748  13.324  1.00 90.47
ATOM   1895  CB  GLU A 242      15.390  15.815  11.981  1.00 90.47
ATOM   1896  CG  GLU A 242      16.579  16.756  11.747  1.00 90.47
ATOM   1897  CD  GLU A 242      17.022  16.734  10.275  1.00 90.47
ATOM   1898  OE1 GLU A 242      18.230  16.537  10.014  1.00 90.47
ATOM   1899  OE2 GLU A 242      16.167  16.927   9.382  1.00 90.47
ATOM   1900  N   ALA A 243      12.465  15.618  13.805  1.00 86.89
ATOM   1901  CA  ALA A 243      11.170  14.942  13.919  1.00 86.89
ATOM   1902  C   ALA A 243      10.725  14.248  12.614  1.00 86.89
ATOM   1903  O   ALA A 243      10.016  13.245  12.666  1.00 86.89
ATOM   1904  CB  ALA A 243      10.130  15.968  14.386  1.00 86.89
ATOM   1905  N   SER A 244      11.162  14.744  11.452  1.00 85.53
ATOM   1906  CA  SER A 244      10.892  14.150  10.133  1.00 85.53
ATOM   1907  C   SER A 244      11.374  12.704  10.028  1.00 85.53
ATOM   1908  O   SER A 244      10.637  11.869   9.516  1.00 85.53
ATOM   1909  CB  SER A 244      11.579  14.972   9.035  1.00 85.53
ATOM   1910  OG  SER A 244      12.897  15.282   9.449  1.00 85.53
ATOM   1911  N   VAL A 245      12.548  12.378  10.581  1.00 90.42
ATOM   1912  CA  VAL A 245      13.118  11.016  10.571  1.00 90.42
ATOM   1913  C   VAL A 245      12.178  10.032  11.271  1.00 90.42
ATOM   1914  O   VAL A 245      11.945   8.923  10.792  1.00 90.42
ATOM   1915  CB  VAL A 245      14.503  11.023  11.253  1.00 90.42
ATOM   1916  CG1 VAL A 245      15.171   9.641  11.388  1.00 90.42
ATOM   1917  CG2 VAL A 245      15.451  11.954  10.491  1.00 90.42
ATOM   1918  N   TRP A 246      11.585  10.457  12.386  1.00 87.79
ATOM   1919  CA  TRP A 246      10.641   9.655  13.161  1.00 87.79
ATOM   1920  C   TRP A 246       9.293   9.480  12.451  1.00 87.79
ATOM   1921  O   TRP A 246       8.723   8.389  12.484  1.00 87.79
ATOM   1922  CB  TRP A 246      10.475  10.301  14.539  1.00 87.79
ATOM   1923  CG  TRP A 246      11.708  10.252  15.387  1.00 87.79
ATOM   1924  CD1 TRP A 246      12.709  11.161  15.422  1.00 87.79
ATOM   1925  CD2 TRP A 246      12.101   9.200  16.309  1.00 87.79
ATOM   1926  NE1 TRP A 246      13.691  10.743  16.300  1.00 87.79
ATOM   1927  CE2 TRP A 246      13.371   9.528  16.871  1.00 87.79
ATOM   1928  CE3 TRP A 246      11.500   7.993  16.711  1.00 87.79
ATOM   1929  CZ2 TRP A 246      14.018   8.685  17.788  1.00 87.79
ATOM   1930  CZ3 TRP A 246      12.132   7.148  17.634  1.00 87.79
ATOM   1931  CH2 TRP A 246      13.391   7.485  18.170  1.00 87.79
ATOM   1932  N   ILE A 247       8.797  10.525  11.780  1.00 84.66
ATOM   1933  CA  ILE A 247       7.556  10.478  10.989  1.00 84.66
ATOM   1934  C   ILE A 247       7.731   9.583   9.761  1.00 84.66
ATOM   1935  O   ILE A 247       6.871   8.743   9.495  1.00 84.66
ATOM   1936  CB  ILE A 247       7.131  11.898  10.564  1.00 84.66
ATOM   1937  CG1 ILE A 247       6.811  12.772  11.792  1.00 84.66
ATOM   1938  CG2 ILE A 247       5.912  11.883   9.619  1.00 84.66
ATOM   1939  CD1 ILE A 247       6.769  14.258  11.429  1.00 84.66
ATOM   1940  N   ASP A 248       8.844   9.721   9.040  1.00 87.96
ATOM   1941  CA  ASP A 248       9.168   8.910   7.865  1.00 87.96
ATOM   1942  C   ASP A 248       9.291   7.429   8.250  1.00 87.96
ATOM   1943  O   ASP A 248       8.746   6.566   7.561  1.00 87.96
ATOM   1944  CB  ASP A 248      10.476   9.407   7.216  1.00 87.96
ATOM   1945  CG  ASP A 248      10.338  10.642   6.308  1.00 87.96
ATOM   1946  OD1 ASP A 248       9.203  11.127   6.109  1.00 87.96
ATOM   1947  OD2 ASP A 248      11.379  11.051   5.734  1.00 87.96
ATOM   1948  N   ALA A 249       9.932   7.125   9.385  1.00 91.49
ATOM   1949  CA  ALA A 249      10.034   5.765   9.911  1.00 91.49
ATOM   1950  C   ALA A 249       8.663   5.175  10.270  1.00 91.49
ATOM   1951  O   ALA A 249       8.358   4.042   9.892  1.00 91.49
ATOM   1952  CB  ALA A 249      10.974   5.779  11.120  1.00 91.49
ATOM   1953  N   ALA A 250       7.818   5.948  10.957  1.00 87.71
ATOM   1954  CA  ALA A 250       6.475   5.521  11.336  1.00 87.71
ATOM   1955  C   ALA A 250       5.586   5.265  10.115  1.00 87.71
ATOM   1956  O   ALA A 250       4.950   4.217   9.999  1.00 87.71
ATOM   1957  CB  ALA A 250       5.877   6.591  12.247  1.00 87.71
ATOM   1958  N   THR A 251       5.606   6.205   9.170  1.00 85.85
ATOM   1959  CA  THR A 251       4.883   6.111   7.901  1.00 85.85
ATOM   1960  C   THR A 251       5.351   4.886   7.125  1.00 85.85
ATOM   1961  O   THR A 251       4.523   4.080   6.714  1.00 85.85
ATOM   1962  CB  THR A 251       5.077   7.386   7.070  1.00 85.85
ATOM   1963  OG1 THR A 251       4.693   8.508   7.827  1.00 85.85
ATOM   1964  CG2 THR A 251       4.208   7.399   5.817  1.00 85.85
ATOM   1965  N   GLN A 252       6.666   4.679   6.996  1.00 91.78
ATOM   1966  CA  GLN A 252       7.214   3.519   6.298  1.00 91.78
ATOM   1967  C   GLN A 252       6.736   2.204   6.911  1.00 91.78
ATOM   1968  O   GLN A 252       6.359   1.312   6.165  1.00 91.78
ATOM   1969  CB  GLN A 252       8.749   3.591   6.286  1.00 91.78
ATOM   1970  CG  GLN A 252       9.411   2.413   5.547  1.00 91.78
ATOM   1971  CD  GLN A 252       8.981   2.273   4.086  1.00 91.78
ATOM   1972  OE1 GLN A 252       8.716   3.239   3.392  1.00 91.78
ATOM   1973  NE2 GLN A 252       8.918   1.074   3.551  1.00 91.78
ATOM   1974  N   VAL A 253       6.721   2.059   8.237  1.00 93.21
ATOM   1975  CA  VAL A 253       6.254   0.822   8.886  1.00 93.21
ATOM   1976  C   VAL A 253       4.756   0.601   8.683  1.00 93.21
ATOM   1977  O   VAL A 253       4.374  -0.514   8.336  1.00 93.21
ATOM   1978  CB  VAL A 253       6.593   0.844  10.377  1.00 93.21
ATOM   1979  CG1 VAL A 253       5.911  -0.271  11.187  1.00 93.21
ATOM   1980  CG2 VAL A 253       8.105   0.710  10.601  1.00 93.21
ATOM   1981  N   CYS A 254       3.913   1.623   8.868  1.00 88.97
ATOM   1982  CA  CYS A 254       2.465   1.479   8.672  1.00 88.97
ATOM   1983  C   CYS A 254       2.127   1.108   7.223  1.00 88.97
ATOM   1984  O   CYS A 254       1.354   0.180   7.002  1.00 88.97
ATOM   1985  CB  CYS A 254       1.737   2.767   9.079  1.00 88.97
ATOM   1986  SG  CYS A 254       1.779   2.985  10.881  1.00 88.97
ATOM   1987  N   PHE A 255       2.749   1.783   6.251  1.00 87.35
ATOM   1988  CA  PHE A 255       2.565   1.490   4.828  1.00 87.35
ATOM   1989  C   PHE A 255       3.099   0.110   4.445  1.00 87.35
ATOM   1990  O   PHE A 255       2.367  -0.674   3.860  1.00 87.35
ATOM   1991  CB  PHE A 255       3.248   2.568   3.983  1.00 87.35
ATOM   1992  CG  PHE A 255       2.357   3.741   3.648  1.00 87.35
ATOM   1993  CD1 PHE A 255       1.692   3.748   2.411  1.00 87.35
ATOM   1994  CD2 PHE A 255       2.206   4.826   4.530  1.00 87.35
ATOM   1995  CE1 PHE A 255       0.969   4.880   2.015  1.00 87.35
ATOM   1996  CE2 PHE A 255       1.465   5.951   4.143  1.00 87.35
ATOM   1997  CZ  PHE A 255       0.889   5.993   2.867  1.00 87.35
ATOM   1998  N   SER A 256       4.341  -0.198   4.825  1.00 93.53
ATOM   1999  CA  SER A 256       5.023  -1.459   4.503  1.00 93.53
ATOM   2000  C   SER A 256       4.292  -2.668   5.081  1.00 93.53
ATOM   2001  O   SER A 256       4.166  -3.692   4.436  1.00 93.53
ATOM   2002  CB  SER A 256       6.444  -1.363   5.070  1.00 93.53
ATOM   2003  OG  SER A 256       7.259  -2.498   4.906  1.00 93.53
ATOM   2004  N   LEU A 257       3.781  -2.585   6.308  1.00 95.55
ATOM   2005  CA  LEU A 257       2.999  -3.683   6.880  1.00 95.55
ATOM   2006  C   LEU A 257       1.534  -3.693   6.421  1.00 95.55
ATOM   2007  O   LEU A 257       0.834  -4.680   6.646  1.00 95.55
ATOM   2008  CB  LEU A 257       3.082  -3.590   8.403  1.00 95.55
ATOM   2009  CG  LEU A 257       4.458  -3.870   9.018  1.00 95.55
ATOM   2010  CD1 LEU A 257       4.293  -3.754  10.533  1.00 95.55
ATOM   2011  CD2 LEU A 257       4.988  -5.266   8.682  1.00 95.55
ATOM   2012  N   GLY A 258       1.063  -2.583   5.850  1.00 92.37
ATOM   2013  CA  GLY A 258      -0.330  -2.351   5.490  1.00 92.37
ATOM   2014  C   GLY A 258      -1.300  -2.365   6.677  1.00 92.37
ATOM   2015  O   GLY A 258      -2.461  -2.753   6.530  1.00 92.37
ATOM   2016  N   VAL A 259      -0.829  -1.925   7.848  1.00 94.13
ATOM   2017  CA  VAL A 259      -1.677  -1.674   9.024  1.00 94.13
ATOM   2018  C   VAL A 259      -2.551  -0.451   8.728  1.00 94.13
ATOM   2019  O   VAL A 259      -2.048   0.580   8.281  1.00 94.13
ATOM   2020  CB  VAL A 259      -0.817  -1.471  10.288  1.00 94.13
ATOM   2021  CG1 VAL A 259      -1.630  -1.152  11.545  1.00 94.13
ATOM   2022  CG2 VAL A 259       0.011  -2.723  10.614  1.00 94.13
ATOM   2023  N   GLY A 260      -3.858  -0.558   8.957  1.00 91.49
ATOM   2024  CA  GLY A 260      -4.851   0.479   8.657  1.00 91.49
ATOM   2025  C   GLY A 260      -5.442   0.427   7.252  1.00 91.49
ATOM   2026  O   GLY A 260      -6.189   1.328   6.879  1.00 91.49
ATOM   2027  N   PHE A 261      -5.147  -0.611   6.467  1.00 93.43
ATOM   2028  CA  PHE A 261      -5.813  -0.861   5.181  1.00 93.43
ATOM   2029  C   PHE A 261      -6.974  -1.864   5.299  1.00 93.43
ATOM   2030  O   PHE A 261      -7.665  -2.165   4.326  1.00 93.43
ATOM   2031  CB  PHE A 261      -4.773  -1.325   4.161  1.00 93.43
ATOM   2032  CG  PHE A 261      -3.862  -0.234   3.654  1.00 93.43
ATOM   2033  CD1 PHE A 261      -4.186   0.412   2.450  1.00 93.43
ATOM   2034  CD2 PHE A 261      -2.681   0.105   4.337  1.00 93.43
ATOM   2035  CE1 PHE A 261      -3.304   1.348   1.899  1.00 93.43
ATOM   2036  CE2 PHE A 261      -1.788   1.033   3.777  1.00 93.43
ATOM   2037  CZ  PHE A 261      -2.091   1.640   2.545  1.00 93.43
ATOM   2038  N   GLY A 262      -7.177  -2.463   6.476  1.00 95.56
ATOM   2039  CA  GLY A 262      -8.173  -3.518   6.672  1.00 95.56
ATOM   2040  C   GLY A 262      -7.874  -4.814   5.904  1.00 95.56
ATOM   2041  O   GLY A 262      -8.689  -5.736   5.922  1.00 95.56
ATOM   2042  N   VAL A 263      -6.718  -4.912   5.238  1.00 97.21
ATOM   2043  CA  VAL A 263      -6.275  -6.104   4.497  1.00 97.21
ATOM   2044  C   VAL A 263      -5.967  -7.239   5.458  1.00 97.21
ATOM   2045  O   VAL A 263      -6.384  -8.370   5.225  1.00 97.21
ATOM   2046  CB  VAL A 263      -5.044  -5.799   3.624  1.00 97.21
ATOM   2047  CG1 VAL A 263      -4.594  -7.045   2.851  1.00 97.21
ATOM   2048  CG2 VAL A 263      -5.369  -4.696   2.615  1.00 97.21
ATOM   2049  N   LEU A 264      -5.310  -6.944   6.580  1.00 98.17
ATOM   2050  CA  LEU A 264      -4.991  -7.938   7.603  1.00 98.17
ATOM   2051  C   LEU A 264      -6.270  -8.467   8.265  1.00 98.17
ATOM   2052  O   LEU A 264      -6.408  -9.677   8.460  1.00 98.17
ATOM   2053  CB  LEU A 264      -4.051  -7.298   8.631  1.00 98.17
ATOM   2054  CG  LEU A 264      -2.782  -6.645   8.065  1.00 98.17
ATOM   2055  CD1 LEU A 264      -1.992  -6.042   9.221  1.00 98.17
ATOM   2056  CD2 LEU A 264      -1.919  -7.655   7.307  1.00 98.17
ATOM   2057  N   ILE A 265      -7.243  -7.587   8.526  1.00 98.04
ATOM   2058  CA  ILE A 265      -8.589  -7.959   8.990  1.00 98.04
ATOM   2059  C   ILE A 265      -9.271  -8.866   7.954  1.00 98.04
ATOM   2060  O   ILE A 265      -9.728  -9.960   8.288  1.00 98.04
ATOM   2061  CB  ILE A 265      -9.439  -6.699   9.293  1.00 98.04
ATOM   2062  CG1 ILE A 265      -8.756  -5.822  10.369  1.00 98.04
ATOM   2063  CG2 ILE A 265     -10.861  -7.090   9.740  1.00 98.04
ATOM   2064  CD1 ILE A 265      -9.486  -4.505  10.659  1.00 98.04
ATOM   2065  N   ALA A 266      -9.286  -8.464   6.680  1.00 97.29
ATOM   2066  CA  ALA A 266      -9.906  -9.236   5.608  1.00 97.29
ATOM   2067  C   ALA A 266      -9.242 -10.609   5.431  1.00 97.29
ATOM   2068  O   ALA A 266      -9.924 -11.626   5.495  1.00 97.29
ATOM   2069  CB  ALA A 266      -9.887  -8.412   4.319  1.00 97.29
ATOM   2070  N   PHE A 267      -7.920 -10.692   5.298  1.00 97.86
ATOM   2071  CA  PHE A 267      -7.217 -11.966   5.136  1.00 97.86
ATOM   2072  C   PHE A 267      -7.391 -12.889   6.344  1.00 97.86
ATOM   2073  O   PHE A 267      -7.636 -14.087   6.172  1.00 97.86
ATOM   2074  CB  PHE A 267      -5.730 -11.700   4.862  1.00 97.86
ATOM   2075  CG  PHE A 267      -5.355 -11.200   3.477  1.00 97.86
ATOM   2076  CD1 PHE A 267      -6.292 -11.097   2.424  1.00 97.86
ATOM   2077  CD2 PHE A 267      -4.005 -10.898   3.223  1.00 97.86
ATOM   2078  CE1 PHE A 267      -5.866 -10.740   1.134  1.00 97.86
ATOM   2079  CE2 PHE A 267      -3.582 -10.540   1.935  1.00 97.86
ATOM   2080  CZ  PHE A 267      -4.508 -10.482   0.885  1.00 97.86
ATOM   2081  N   SER A 268      -7.310 -12.355   7.563  1.00 97.91
ATOM   2082  CA  SER A 268      -7.451 -13.157   8.782  1.00 97.91
ATOM   2083  C   SER A 268      -8.884 -13.623   9.040  1.00 97.91
ATOM   2084  O   SER A 268      -9.073 -14.696   9.607  1.00 97.91
ATOM   2085  CB  SER A 268      -6.918 -12.400   9.990  1.00 97.91
ATOM   2086  OG  SER A 268      -7.683 -11.247  10.233  1.00 97.91
ATOM   2087  N   SER A 269      -9.900 -12.902   8.564  1.00 97.16
ATOM   2088  CA  SER A 269     -11.305 -13.316   8.688  1.00 97.16
ATOM   2089  C   SER A 269     -11.635 -14.630   7.955  1.00 97.16
ATOM   2090  O   SER A 269     -12.547 -15.363   8.352  1.00 97.16
ATOM   2091  CB  SER A 269     -12.201 -12.182   8.201  1.00 97.16
ATOM   2092  OG  SER A 269     -12.113 -12.089   6.803  1.00 97.16
ATOM   2093  N   TYR A 270     -10.847 -14.976   6.930  1.00 96.73
ATOM   2094  CA  TYR A 270     -10.909 -16.252   6.209  1.00 96.73
ATOM   2095  C   TYR A 270     -10.045 -17.357   6.852  1.00 96.73
ATOM   2096  O   TYR A 270      -9.983 -18.484   6.350  1.00 96.73
ATOM   2097  CB  TYR A 270     -10.519 -16.020   4.746  1.00 96.73
ATOM   2098  CG  TYR A 270     -11.401 -15.051   3.978  1.00 96.73
ATOM   2099  CD1 TYR A 270     -12.695 -15.429   3.583  1.00 96.73
ATOM   2100  CD2 TYR A 270     -10.903 -13.795   3.590  1.00 96.73
ATOM   2101  CE1 TYR A 270     -13.466 -14.589   2.761  1.00 96.73
ATOM   2102  CE2 TYR A 270     -11.668 -12.949   2.764  1.00 96.73
ATOM   2103  CZ  TYR A 270     -12.939 -13.361   2.317  1.00 96.73
ATOM   2104  OH  TYR A 270     -13.663 -12.573   1.486  1.00 96.73
ATOM   2105  N   ASN A 271      -9.358 -17.090   7.966  1.00 96.54
ATOM   2106  CA  ASN A 271      -8.660 -18.138   8.703  1.00 96.54
ATOM   2107  C   ASN A 271      -9.635 -19.046   9.451  1.00 96.54
ATOM   2108  O   ASN A 271     -10.752 -18.682   9.818  1.00 96.54
ATOM   2109  CB  ASN A 271      -7.595 -17.555   9.648  1.00 96.54
ATOM   2110  CG  ASN A 271      -6.349 -17.106   8.919  1.00 96.54
ATOM   2111  OD1 ASN A 271      -6.039 -17.590   7.846  1.00 96.54
ATOM   2112  ND2 ASN A 271      -5.558 -16.262   9.532  1.00 96.54
ATOM   2113  N   LYS A 272      -9.160 -20.257   9.747  1.00 95.15
ATOM   2114  CA  LYS A 272      -9.788 -21.084  10.779  1.00 95.15
ATOM   2115  C   LYS A 272      -9.659 -20.366  12.123  1.00 95.15
ATOM   2116  O   LYS A 272      -8.596 -19.830  12.422  1.00 95.15
ATOM   2117  CB  LYS A 272      -9.151 -22.480  10.826  1.00 95.15
ATOM   2118  CG  LYS A 272      -9.363 -23.235   9.506  1.00 95.15
ATOM   2119  CD  LYS A 272      -8.824 -24.667   9.581  1.00 95.15
ATOM   2120  CE  LYS A 272      -9.063 -25.341   8.225  1.00 95.15
ATOM   2121  NZ  LYS A 272      -8.674 -26.772   8.225  1.00 95.15
ATOM   2122  N   PHE A 273     -10.701 -20.440  12.949  1.00 95.48
ATOM   2123  CA  PHE A 273     -10.777 -19.734  14.234  1.00 95.48
ATOM   2124  C   PHE A 273      -9.558 -19.968  15.148  1.00 95.48
ATOM   2125  O   PHE A 273      -9.085 -19.046  15.803  1.00 95.48
ATOM   2126  CB  PHE A 273     -12.073 -20.179  14.924  1.00 95.48
ATOM   2127  CG  PHE A 273     -12.351 -19.449  16.219  1.00 95.48
ATOM   2128  CD1 PHE A 273     -12.076 -20.065  17.455  1.00 95.48
ATOM   2129  CD2 PHE A 273     -12.864 -18.139  16.187  1.00 95.48
ATOM   2130  CE1 PHE A 273     -12.316 -19.373  18.653  1.00 95.48
ATOM   2131  CE2 PHE A 273     -13.116 -17.453  17.387  1.00 95.48
ATOM   2132  CZ  PHE A 273     -12.841 -18.069  18.620  1.00 95.48
ATOM   2133  N   THR A 274      -8.997 -21.182  15.141  1.00 95.71
ATOM   2134  CA  THR A 274      -7.836 -21.565  15.964  1.00 95.71
ATOM   2135  C   THR A 274      -6.485 -21.420  15.248  1.00 95.71
ATOM   2136  O   THR A 274      -5.509 -22.092  15.600  1.00 95.71
ATOM   2137  CB  THR A 274      -7.998 -22.989  16.513  1.00 95.71
ATOM   2138  OG1 THR A 274      -7.946 -23.908  15.438  1.00 95.71
ATOM   2139  CG2 THR A 274      -9.308 -23.207  17.268  1.00 95.71
ATOM   2140  N   ASN A 275      -6.408 -20.639  14.165  1.00 96.24
ATOM   2141  CA  ASN A 275      -5.136 -20.389  13.493  1.00 96.24
ATOM   2142  C   ASN A 275      -4.210 -19.534  14.381  1.00 96.24
ATOM   2143  O   ASN A 275      -4.663 -18.707  15.169  1.00 96.24
ATOM   2144  CB  ASN A 275      -5.366 -19.815  12.089  1.00 96.24
ATOM   2145  CG  ASN A 275      -4.041 -19.671  11.370  1.00 96.24
ATOM   2146  OD1 ASN A 275      -3.363 -20.674  11.150  1.00 96.24
ATOM   2147  ND2 ASN A 275      -3.621 -18.456  11.124  1.00 96.24
ATOM   2148  N   ASN A 276      -2.899 -19.758  14.285  1.00 96.61
ATOM   2149  CA  ASN A 276      -1.928 -19.093  15.151  1.00 96.61
ATOM   2150  C   ASN A 276      -1.546 -17.716  14.582  1.00 96.61
ATOM   2151  O   ASN A 276      -0.451 -17.539  14.049  1.00 96.61
ATOM   2152  CB  ASN A 276      -0.737 -20.035  15.411  1.00 96.61
ATOM   2153  CG  ASN A 276       0.201 -19.496  16.481  1.00 96.61
ATOM   2154  OD1 ASN A 276       0.185 -18.341  16.859  1.00 96.61
ATOM   2155  ND2 ASN A 276       1.061 -20.325  17.024  1.00 96.61
ATOM   2156  N   CYS A 277      -2.453 -16.748  14.724  1.00 96.78
ATOM   2157  CA  CYS A 277      -2.253 -15.372  14.269  1.00 96.78
ATOM   2158  C   CYS A 277      -1.071 -14.668  14.960  1.00 96.78
ATOM   2159  O   CYS A 277      -0.453 -13.801  14.351  1.00 96.78
ATOM   2160  CB  CYS A 277      -3.566 -14.591  14.437  1.00 96.78
ATOM   2161  SG  CYS A 277      -4.199 -14.690  16.138  1.00 96.78
ATOM   2162  N   TYR A 278      -0.693 -15.081  16.178  1.00 97.01
ATOM   2163  CA  TYR A 278       0.516 -14.594  16.853  1.00 97.01
ATOM   2164  C   TYR A 278       1.781 -14.945  16.063  1.00 97.01
ATOM   2165  O   TYR A 278       2.586 -14.072  15.745  1.00 97.01
ATOM   2166  CB  TYR A 278       0.592 -15.178  18.272  1.00 97.01
ATOM   2167  CG  TYR A 278       1.925 -14.937  18.954  1.00 97.01
ATOM   2168  CD1 TYR A 278       2.926 -15.932  18.943  1.00 97.01
ATOM   2169  CD2 TYR A 278       2.181 -13.692  19.553  1.00 97.01
ATOM   2170  CE1 TYR A 278       4.184 -15.677  19.523  1.00 97.01
ATOM   2171  CE2 TYR A 278       3.431 -13.443  20.144  1.00 97.01
ATOM   2172  CZ  TYR A 278       4.441 -14.427  20.120  1.00 97.01
ATOM   2173  OH  TYR A 278       5.661 -14.174  20.661  1.00 97.01
ATOM   2174  N   ARG A 279       1.951 -16.223  15.703  1.00 97.63
ATOM   2175  CA  ARG A 279       3.099 -16.669  14.901  1.00 97.63
ATOM   2176  C   ARG A 279       3.115 -15.963  13.551  1.00 97.63
ATOM   2177  O   ARG A 279       4.173 -15.526  13.113  1.00 97.63
ATOM   2178  CB  ARG A 279       3.034 -18.187  14.719  1.00 97.63
ATOM   2179  CG  ARG A 279       4.228 -18.736  13.916  1.00 97.63
ATOM   2180  CD  ARG A 279       3.914 -20.118  13.349  1.00 97.63
ATOM   2181  NE  ARG A 279       2.861 -20.027  12.319  1.00 97.63
ATOM   2182  CZ  ARG A 279       2.363 -21.000  11.598  1.00 97.63
ATOM   2183  NH1 ARG A 279       2.745 -22.241  11.760  1.00 97.63
ATOM   2184  NH2 ARG A 279       1.475 -20.703  10.700  1.00 97.63
ATOM   2185  N   ASP A 280       1.958 -15.867  12.908  1.00 98.01
ATOM   2186  CA  ASP A 280       1.853 -15.264  11.583  1.00 98.01
ATOM   2187  C   ASP A 280       2.214 -13.763  11.631  1.00 98.01
ATOM   2188  O   ASP A 280       2.916 -13.284  10.741  1.00 98.01
ATOM   2189  CB  ASP A 280       0.461 -15.563  11.000  1.00 98.01
ATOM   2190  CG  ASP A 280       0.135 -17.072  10.892  1.00 98.01
ATOM   2191  OD1 ASP A 280       1.057 -17.933  10.821  1.00 98.01
ATOM   2192  OD2 ASP A 280      -1.069 -17.416  10.902  1.00 98.01
ATOM   2193  N   ALA A 281       1.872 -13.052  12.715  1.00 98.17
ATOM   2194  CA  ALA A 281       2.310 -11.676  12.955  1.00 98.17
ATOM   2195  C   ALA A 281       3.836 -11.550  13.099  1.00 98.17
ATOM   2196  O   ALA A 281       4.450 -10.740  12.405  1.00 98.17
ATOM   2197  CB  ALA A 281       1.595 -11.120  14.194  1.00 98.17
ATOM   2198  N   ILE A 282       4.464 -12.359  13.962  1.00 98.15
ATOM   2199  CA  ILE A 282       5.922 -12.316  14.185  1.00 98.15
ATOM   2200  C   ILE A 282       6.690 -12.650  12.906  1.00 98.15
ATOM   2201  O   ILE A 282       7.628 -11.942  12.544  1.00 98.15
ATOM   2202  CB  ILE A 282       6.344 -13.282  15.318  1.00 98.15
ATOM   2203  CG1 ILE A 282       5.715 -12.942  16.685  1.00 98.15
ATOM   2204  CG2 ILE A 282       7.878 -13.344  15.463  1.00 98.15
ATOM   2205  CD1 ILE A 282       5.998 -11.530  17.192  1.00 98.15
ATOM   2206  N   VAL A 283       6.297 -13.725  12.219  1.00 98.43
ATOM   2207  CA  VAL A 283       6.970 -14.188  11.001  1.00 98.43
ATOM   2208  C   VAL A 283       6.857 -13.143   9.895  1.00 98.43
ATOM   2209  O   VAL A 283       7.878 -12.771   9.325  1.00 98.43
ATOM   2210  CB  VAL A 283       6.418 -15.557  10.558  1.00 98.43
ATOM   2211  CG1 VAL A 283       6.928 -15.984   9.177  1.00 98.43
ATOM   2212  CG2 VAL A 283       6.836 -16.652  11.551  1.00 98.43
ATOM   2213  N   THR A 284       5.654 -12.627   9.623  1.00 98.33
ATOM   2214  CA  THR A 284       5.455 -11.673   8.520  1.00 98.33
ATOM   2215  C   THR A 284       6.201 -10.367   8.768  1.00 98.33
ATOM   2216  O   THR A 284       6.939  -9.913   7.901  1.00 98.33
ATOM   2217  CB  THR A 284       3.976 -11.347   8.278  1.00 98.33
ATOM   2218  OG1 THR A 284       3.232 -12.542   8.185  1.00 98.33
ATOM   2219  CG2 THR A 284       3.805 -10.571   6.969  1.00 98.33
ATOM   2220  N   THR A 285       6.067  -9.781   9.959  1.00 98.11
ATOM   2221  CA  THR A 285       6.725  -8.503  10.291  1.00 98.11
ATOM   2222  C   THR A 285       8.251  -8.624  10.262  1.00 98.11
ATOM   2223  O   THR A 285       8.935  -7.733   9.766  1.00 98.11
ATOM   2224  CB  THR A 285       6.270  -7.989  11.663  1.00 98.11
ATOM   2225  OG1 THR A 285       6.450  -8.975  12.650  1.00 98.11
ATOM   2226  CG2 THR A 285       4.786  -7.619  11.681  1.00 98.11
ATOM   2227  N   SER A 286       8.791  -9.765  10.700  1.00 97.95
ATOM   2228  CA  SER A 286      10.230 -10.046  10.641  1.00 97.95
ATOM   2229  C   SER A 286      10.725 -10.220   9.202  1.00 97.95
ATOM   2230  O   SER A 286      11.766  -9.672   8.842  1.00 97.95
ATOM   2231  CB  SER A 286      10.557 -11.300  11.455  1.00 97.95
ATOM   2232  OG  SER A 286      10.211 -11.123  12.814  1.00 97.95
ATOM   2233  N   ILE A 287       9.973 -10.939   8.360  1.00 98.03
ATOM   2234  CA  ILE A 287      10.272 -11.087   6.929  1.00 98.03
ATOM   2235  C   ILE A 287      10.189  -9.733   6.216  1.00 98.03
ATOM   2236  O   ILE A 287      11.081  -9.417   5.433  1.00 98.03
ATOM   2237  CB  ILE A 287       9.344 -12.147   6.291  1.00 98.03
ATOM   2238  CG1 ILE A 287       9.770 -13.555   6.765  1.00 98.03
ATOM   2239  CG2 ILE A 287       9.387 -12.081   4.757  1.00 98.03
ATOM   2240  CD1 ILE A 287       8.805 -14.671   6.349  1.00 98.03
ATOM   2241  N   ASN A 288       9.180  -8.913   6.517  1.00 97.44
ATOM   2242  CA  ASN A 288       9.038  -7.557   5.991  1.00 97.44
ATOM   2243  C   ASN A 288      10.278  -6.707   6.299  1.00 97.44
ATOM   2244  O   ASN A 288      10.922  -6.203   5.380  1.00 97.44
ATOM   2245  CB  ASN A 288       7.760  -6.935   6.576  1.00 97.44
ATOM   2246  CG  ASN A 288       7.583  -5.495   6.141  1.00 97.44
ATOM   2247  OD1 ASN A 288       7.954  -4.548   6.824  1.00 97.44
ATOM   2248  ND2 ASN A 288       7.032  -5.289   4.980  1.00 97.44
ATOM   2249  N   SER A 289      10.671  -6.611   7.573  1.00 97.25
ATOM   2250  CA  SER A 289      11.852  -5.839   7.976  1.00 97.25
ATOM   2251  C   SER A 289      13.151  -6.379   7.389  1.00 97.25
ATOM   2252  O   SER A 289      13.987  -5.592   6.945  1.00 97.25
ATOM   2253  CB  SER A 289      11.984  -5.806   9.497  1.00 97.25
ATOM   2254  OG  SER A 289      10.937  -5.051  10.054  1.00 97.25
ATOM   2255  N   LEU A 290      13.329  -7.703   7.350  1.00 96.83
ATOM   2256  CA  LEU A 290      14.511  -8.308   6.743  1.00 96.83
ATOM   2257  C   LEU A 290      14.563  -8.024   5.240  1.00 96.83
ATOM   2258  O   LEU A 290      15.619  -7.674   4.727  1.00 96.83
ATOM   2259  CB  LEU A 290      14.526  -9.816   7.042  1.00 96.83
ATOM   2260  CG  LEU A 290      15.758 -10.553   6.480  1.00 96.83
ATOM   2261  CD1 LEU A 290      17.072 -10.020   7.058  1.00 96.83
ATOM   2262  CD2 LEU A 290      15.655 -12.040   6.817  1.00 96.83
ATOM   2263  N   THR A 291      13.426  -8.109   4.547  1.00 96.72
ATOM   2264  CA  THR A 291      13.351  -7.837   3.107  1.00 96.72
ATOM   2265  C   THR A 291      13.641  -6.370   2.804  1.00 96.72
ATOM   2266  O   THR A 291      14.411  -6.090   1.888  1.00 96.72
ATOM   2267  CB  THR A 291      11.997  -8.240   2.502  1.00 96.72
ATOM   2268  OG1 THR A 291      11.672  -9.571   2.846  1.00 96.72
ATOM   2269  CG2 THR A 291      12.062  -8.155   0.979  1.00 96.72
ATOM   2270  N   SER A 292      13.111  -5.437   3.602  1.00 96.09
ATOM   2271  CA  SER A 292      13.458  -4.009   3.532  1.00 96.09
ATOM   2272  C   SER A 292      14.963  -3.785   3.675  1.00 96.09
ATOM   2273  O   SER A 292      15.593  -3.144   2.835  1.00 96.09
ATOM   2274  CB  SER A 292      12.776  -3.250   4.671  1.00 96.09
ATOM   2275  OG  SER A 292      11.384  -3.244   4.515  1.00 96.09
ATOM   2276  N   PHE A 293      15.559  -4.354   4.726  1.00 95.74
ATOM   2277  CA  PHE A 293      16.984  -4.211   5.005  1.00 95.74
ATOM   2278  C   PHE A 293      17.853  -4.812   3.891  1.00 95.74
ATOM   2279  O   PHE A 293      18.764  -4.155   3.392  1.00 95.74
ATOM   2280  CB  PHE A 293      17.275  -4.832   6.375  1.00 95.74
ATOM   2281  CG  PHE A 293      18.713  -4.674   6.822  1.00 95.74
ATOM   2282  CD1 PHE A 293      19.549  -5.800   6.941  1.00 95.74
ATOM   2283  CD2 PHE A 293      19.220  -3.394   7.113  1.00 95.74
ATOM   2284  CE1 PHE A 293      20.880  -5.646   7.368  1.00 95.74
ATOM   2285  CE2 PHE A 293      20.561  -3.237   7.502  1.00 95.74
ATOM   2286  CZ  PHE A 293      21.389  -4.363   7.638  1.00 95.74
ATOM   2287  N   SER A 294      17.536  -6.027   3.431  1.00 95.60
ATOM   2288  CA  SER A 294      18.227  -6.680   2.314  1.00 95.60
ATOM   2289  C   SER A 294      18.077  -5.913   0.998  1.00 95.60
ATOM   2290  O   SER A 294      19.051  -5.792   0.257  1.00 95.60
ATOM   2291  CB  SER A 294      17.711  -8.110   2.133  1.00 95.60
ATOM   2292  OG  SER A 294      18.067  -8.904   3.249  1.00 95.60
ATOM   2293  N   SER A 295      16.903  -5.338   0.727  1.00 94.72
ATOM   2294  CA  SER A 295      16.682  -4.490  -0.452  1.00 94.72
ATOM   2295  C   SER A 295      17.548  -3.232  -0.423  1.00 94.72
ATOM   2296  O   SER A 295      17.984  -2.772  -1.475  1.00 94.72
ATOM   2297  CB  SER A 295      15.216  -4.080  -0.573  1.00 94.72
ATOM   2298  OG  SER A 295      14.400  -5.226  -0.698  1.00 94.72
ATOM   2299  N   GLY A 296      17.889  -2.728   0.768  1.00 94.00
ATOM   2300  CA  GLY A 296      18.875  -1.662   0.947  1.00 94.00
ATOM   2301  C   GLY A 296      20.227  -1.988   0.316  1.00 94.00
ATOM   2302  O   GLY A 296      20.753  -1.188  -0.455  1.00 94.00
ATOM   2303  N   PHE A 297      20.752  -3.194   0.545  1.00 95.77
ATOM   2304  CA  PHE A 297      21.999  -3.634  -0.091  1.00 95.77
ATOM   2305  C   PHE A 297      21.874  -3.734  -1.609  1.00 95.77
ATOM   2306  O   PHE A 297      22.800  -3.340  -2.316  1.00 95.77
ATOM   2307  CB  PHE A 297      22.452  -4.985   0.466  1.00 95.77
ATOM   2308  CG  PHE A 297      22.908  -4.920   1.901  1.00 95.77
ATOM   2309  CD1 PHE A 297      24.261  -4.680   2.202  1.00 95.77
ATOM   2310  CD2 PHE A 297      21.973  -5.066   2.935  1.00 95.77
ATOM   2311  CE1 PHE A 297      24.676  -4.591   3.543  1.00 95.77
ATOM   2312  CE2 PHE A 297      22.385  -4.964   4.269  1.00 95.77
ATOM   2313  CZ  PHE A 297      23.735  -4.731   4.579  1.00 95.77
ATOM   2314  N   VAL A 298      20.734  -4.218  -2.113  1.00 93.86
ATOM   2315  CA  VAL A 298      20.474  -4.273  -3.557  1.00 93.86
ATOM   2316  C   VAL A 298      20.518  -2.860  -4.138  1.00 93.86
ATOM   2317  O   VAL A 298      21.398  -2.581  -4.947  1.00 93.86
ATOM   2318  CB  VAL A 298      19.151  -4.989  -3.895  1.00 93.86
ATOM   2319  CG1 VAL A 298      18.957  -5.086  -5.412  1.00 93.86
ATOM   2320  CG2 VAL A 298      19.144  -6.421  -3.355  1.00 93.86
ATOM   2321  N   VAL A 299      19.668  -1.942  -3.663  1.00 91.92
ATOM   2322  CA  VAL A 299      19.585  -0.558  -4.169  1.00 91.92
ATOM   2323  C   VAL A 299      20.938   0.131  -4.129  1.00 91.92
ATOM   2324  O   VAL A 299      21.401   0.653  -5.141  1.00 91.92
ATOM   2325  CB  VAL A 299      18.562   0.274  -3.365  1.00 91.92
ATOM   2326  CG1 VAL A 299      18.550   1.749  -3.786  1.00 91.92
ATOM   2327  CG2 VAL A 299      17.122  -0.212  -3.521  1.00 91.92
ATOM   2328  N   PHE A 300      21.601   0.121  -2.979  1.00 92.71
ATOM   2329  CA  PHE A 300      22.820   0.896  -2.823  1.00 92.71
ATOM   2330  C   PHE A 300      24.025   0.294  -3.529  1.00 92.71
ATOM   2331  O   PHE A 300      24.906   1.048  -3.927  1.00 92.71
ATOM   2332  CB  PHE A 300      23.095   1.126  -1.356  1.00 92.71
ATOM   2333  CG  PHE A 300      22.347   2.319  -0.823  1.00 92.71
ATOM   2334  CD1 PHE A 300      23.008   3.557  -0.731  1.00 92.71
ATOM   2335  CD2 PHE A 300      21.051   2.163  -0.304  1.00 92.71
ATOM   2336  CE1 PHE A 300      22.442   4.587   0.027  1.00 92.71
ATOM   2337  CE2 PHE A 300      20.483   3.196   0.448  1.00 92.71
ATOM   2338  CZ  PHE A 300      21.221   4.366   0.680  1.00 92.71
ATOM   2339  N   SER A 301      24.062  -1.019  -3.759  1.00 94.77
ATOM   2340  CA  SER A 301      25.103  -1.599  -4.610  1.00 94.77
ATOM   2341  C   SER A 301      25.036  -1.049  -6.044  1.00 94.77
ATOM   2342  O   SER A 301      26.067  -0.682  -6.608  1.00 94.77
ATOM   2343  CB  SER A 301      25.036  -3.125  -4.572  1.00 94.77
ATOM   2344  OG  SER A 301      23.897  -3.642  -5.231  1.00 94.77
ATOM   2345  N   PHE A 302      23.828  -0.871  -6.591  1.00 92.17
ATOM   2346  CA  PHE A 302      23.619  -0.239  -7.895  1.00 92.17
ATOM   2347  C   PHE A 302      23.815   1.284  -7.854  1.00 92.17
ATOM   2348  O   PHE A 302      24.433   1.826  -8.767  1.00 92.17
ATOM   2349  CB  PHE A 302      22.239  -0.622  -8.447  1.00 92.17
ATOM   2350  CG  PHE A 302      22.184  -2.018  -9.044  1.00 92.17
ATOM   2351  CD1 PHE A 302      22.532  -2.218 -10.390  1.00 92.17
ATOM   2352  CD2 PHE A 302      21.788  -3.123  -8.270  1.00 92.17
ATOM   2353  CE1 PHE A 302      22.459  -3.496 -10.966  1.00 92.17
ATOM   2354  CE2 PHE A 302      21.745  -4.411  -8.832  1.00 92.17
ATOM   2355  CZ  PHE A 302      22.071  -4.599 -10.186  1.00 92.17
ATOM   2356  N   LEU A 303      23.371   1.982  -6.799  1.00 90.85
ATOM   2357  CA  LEU A 303      23.608   3.429  -6.662  1.00 90.85
ATOM   2358  C   LEU A 303      25.098   3.766  -6.549  1.00 90.85
ATOM   2359  O   LEU A 303      25.549   4.712  -7.184  1.00 90.85
ATOM   2360  CB  LEU A 303      22.876   4.017  -5.442  1.00 90.85
ATOM   2361  CG  LEU A 303      21.344   4.087  -5.532  1.00 90.85
ATOM   2362  CD1 LEU A 303      20.788   4.660  -4.227  1.00 90.85
ATOM   2363  CD2 LEU A 303      20.888   4.996  -6.668  1.00 90.85
ATOM   2364  N   GLY A 304      25.870   2.993  -5.779  1.00 93.33
ATOM   2365  CA  GLY A 304      27.321   3.171  -5.668  1.00 93.33
ATOM   2366  C   GLY A 304      28.027   2.970  -7.008  1.00 93.33
ATOM   2367  O   GLY A 304      28.886   3.764  -7.387  1.00 93.33
ATOM   2368  N   TYR A 305      27.598   1.962  -7.770  1.00 92.50
ATOM   2369  CA  TYR A 305      28.073   1.745  -9.133  1.00 92.50
ATOM   2370  C   TYR A 305      27.748   2.919 -10.068  1.00 92.50
ATOM   2371  O   TYR A 305      28.631   3.401 -10.779  1.00 92.50
ATOM   2372  CB  TYR A 305      27.496   0.421  -9.647  1.00 92.50
ATOM   2373  CG  TYR A 305      27.688   0.226 -11.134  1.00 92.50
ATOM   2374  CD1 TYR A 305      26.600   0.374 -12.009  1.00 92.50
ATOM   2375  CD2 TYR A 305      28.973  -0.008 -11.647  1.00 92.50
ATOM   2376  CE1 TYR A 305      26.802   0.283 -13.395  1.00 92.50
ATOM   2377  CE2 TYR A 305      29.183  -0.127 -13.031  1.00 92.50
ATOM   2378  CZ  TYR A 305      28.091   0.019 -13.909  1.00 92.50
ATOM   2379  OH  TYR A 305      28.294  -0.080 -15.249  1.00 92.50
ATOM   2380  N   MET A 306      26.512   3.423 -10.042  1.00 89.79
ATOM   2381  CA  MET A 306      26.101   4.562 -10.870  1.00 89.79
ATOM   2382  C   MET A 306      26.817   5.859 -10.486  1.00 89.79
ATOM   2383  O   MET A 306      27.246   6.601 -11.367  1.00 89.79
ATOM   2384  CB  MET A 306      24.579   4.742 -10.789  1.00 89.79
ATOM   2385  CG  MET A 306      23.824   3.637 -11.536  1.00 89.79
ATOM   2386  SD  MET A 306      24.294   3.406 -13.274  1.00 89.79
ATOM   2387  CE  MET A 306      23.738   4.990 -13.944  1.00 89.79
ATOM   2388  N   ALA A 307      27.013   6.102  -9.190  1.00 90.05
ATOM   2389  CA  ALA A 307      27.771   7.238  -8.677  1.00 90.05
ATOM   2390  C   ALA A 307      29.220   7.221  -9.184  1.00 90.05
ATOM   2391  O   ALA A 307      29.711   8.226  -9.696  1.00 90.05
ATOM   2392  CB  ALA A 307      27.699   7.190  -7.149  1.00 90.05
ATOM   2393  N   GLN A 308      29.887   6.060  -9.136  1.00 90.75
ATOM   2394  CA  GLN A 308      31.232   5.920  -9.693  1.00 90.75
ATOM   2395  C   GLN A 308      31.245   6.097 -11.216  1.00 90.75
ATOM   2396  O   GLN A 308      32.131   6.771 -11.739  1.00 90.75
ATOM   2397  CB  GLN A 308      31.843   4.571  -9.285  1.00 90.75
ATOM   2398  CG  GLN A 308      33.310   4.509  -9.751  1.00 90.75
ATOM   2399  CD  GLN A 308      34.070   3.277  -9.292  1.00 90.75
ATOM   2400  OE1 GLN A 308      33.545   2.306  -8.792  1.00 90.75
ATOM   2401  NE2 GLN A 308      35.370   3.243  -9.476  1.00 90.75
ATOM   2402  N   LYS A 309      30.271   5.519 -11.931  1.00 85.92
ATOM   2403  CA  LYS A 309      30.181   5.623 -13.395  1.00 85.92
ATOM   2404  C   LYS A 309      30.051   7.076 -13.860  1.00 85.92
ATOM   2405  O   LYS A 309      30.718   7.466 -14.813  1.00 85.92
ATOM   2406  CB  LYS A 309      29.011   4.759 -13.898  1.00 85.92
ATOM   2407  CG  LYS A 309      28.978   4.740 -15.432  1.00 85.92
ATOM   2408  CD  LYS A 309      27.837   3.887 -15.991  1.00 85.92
ATOM   2409  CE  LYS A 309      27.901   4.010 -17.519  1.00 85.92
ATOM   2410  NZ  LYS A 309      26.753   3.365 -18.195  1.00 85.92
ATOM   2411  N   HIS A 310      29.230   7.867 -13.176  1.00 85.23
ATOM   2412  CA  HIS A 310      29.012   9.281 -13.492  1.00 85.23
ATOM   2413  C   HIS A 310      30.008  10.224 -12.809  1.00 85.23
ATOM   2414  O   HIS A 310      29.995  11.418 -13.079  1.00 85.23
ATOM   2415  CB  HIS A 310      27.555   9.629 -13.177  1.00 85.23
ATOM   2416  CG  HIS A 310      26.597   9.028 -14.166  1.00 85.23
ATOM   2417  ND1 HIS A 310      26.643   9.239 -15.543  1.00 85.23
ATOM   2418  CD2 HIS A 310      25.497   8.279 -13.867  1.00 85.23
ATOM   2419  CE1 HIS A 310      25.544   8.655 -16.042  1.00 85.23
ATOM   2420  NE2 HIS A 310      24.847   8.058 -15.063  1.00 85.23
ATOM   2421  N   SER A 311      30.895   9.707 -11.951  1.00 87.58
ATOM   2422  CA  SER A 311      31.819  10.510 -11.135  1.00 87.58
ATOM   2423  C   SER A 311      31.108  11.590 -10.304  1.00 87.58
ATOM   2424  O   SER A 311      31.640  12.680 -10.098  1.00 87.58
ATOM   2425  CB  SER A 311      32.959  11.076 -11.990  1.00 87.58
ATOM   2426  OG  SER A 311      33.670  10.014 -12.598  1.00 87.58
ATOM   2427  N   VAL A 312      29.908  11.272  -9.810  1.00 87.36
ATOM   2428  CA  VAL A 312      29.087  12.154  -8.966  1.00 87.36
ATOM   2429  C   VAL A 312      28.899  11.554  -7.570  1.00 87.36
ATOM   2430  O   VAL A 312      28.969  10.333  -7.399  1.00 87.36
ATOM   2431  CB  VAL A 312      27.716  12.489  -9.591  1.00 87.36
ATOM   2432  CG1 VAL A 312      27.868  13.266 -10.901  1.00 87.36
ATOM   2433  CG2 VAL A 312      26.858  11.243  -9.821  1.00 87.36
ATOM   2434  N   PRO A 313      28.638  12.380  -6.545  1.00 87.24
ATOM   2435  CA  PRO A 313      28.192  11.898  -5.245  1.00 87.24
ATOM   2436  C   PRO A 313      26.936  11.017  -5.346  1.00 87.24
ATOM   2437  O   PRO A 313      26.026  11.286  -6.125  1.00 87.24
ATOM   2438  CB  PRO A 313      27.919  13.159  -4.418  1.00 87.24
ATOM   2439  CG  PRO A 313      28.785  14.231  -5.079  1.00 87.24
ATOM   2440  CD  PRO A 313      28.762  13.829  -6.548  1.00 87.24
ATOM   2441  N   ILE A 314      26.836   9.999  -4.484  1.00 85.80
ATOM   2442  CA  ILE A 314      25.679   9.078  -4.433  1.00 85.80
ATOM   2443  C   ILE A 314      24.347   9.825  -4.253  1.00 85.80
ATOM   2444  O   ILE A 314      23.325   9.396  -4.788  1.00 85.80
ATOM   2445  CB  ILE A 314      25.899   8.035  -3.308  1.00 85.80
ATOM   2446  CG1 ILE A 314      27.055   7.084  -3.694  1.00 85.80
ATOM   2447  CG2 ILE A 314      24.631   7.210  -3.003  1.00 85.80
ATOM   2448  CD1 ILE A 314      27.658   6.339  -2.502  1.00 85.80
ATOM   2449  N   GLY A 315      24.360  10.948  -3.531  1.00 79.71
ATOM   2450  CA  GLY A 315      23.160  11.742  -3.272  1.00 79.71
ATOM   2451  C   GLY A 315      22.545  12.372  -4.517  1.00 79.71
ATOM   2452  O   GLY A 315      21.329  12.520  -4.560  1.00 79.71
ATOM   2453  N   ASP A 316      23.345  12.640  -5.549  1.00 78.29
ATOM   2454  CA  ASP A 316      22.859  13.233  -6.800  1.00 78.29
ATOM   2455  C   ASP A 316      22.178  12.187  -7.702  1.00 78.29
ATOM   2456  O   ASP A 316      21.380  12.521  -8.577  1.00 78.29
ATOM   2457  CB  ASP A 316      24.026  13.929  -7.520  1.00 78.29
ATOM   2458  CG  ASP A 316      24.630  15.098  -6.725  1.00 78.29
ATOM   2459  OD1 ASP A 316      23.947  15.635  -5.823  1.00 78.29
ATOM   2460  OD2 ASP A 316      25.801  15.436  -7.004  1.00 78.29
ATOM   2461  N   VAL A 317      22.452  10.901  -7.459  1.00 77.00
ATOM   2462  CA  VAL A 317      21.830   9.768  -8.164  1.00 77.00
ATOM   2463  C   VAL A 317      20.572   9.279  -7.437  1.00 77.00
ATOM   2464  O   VAL A 317      19.649   8.754  -8.063  1.00 77.00
ATOM   2465  CB  VAL A 317      22.844   8.618  -8.334  1.00 77.00
ATOM   2466  CG1 VAL A 317      22.309   7.510  -9.248  1.00 77.00
ATOM   2467  CG2 VAL A 317      24.168   9.096  -8.942  1.00 77.00
ATOM   2468  N   ALA A 318      20.506   9.440  -6.113  1.00 69.98
ATOM   2469  CA  ALA A 318      19.396   8.977  -5.285  1.00 69.98
ATOM   2470  C   ALA A 318      18.149   9.866  -5.454  1.00 69.98
ATOM   2471  O   ALA A 318      17.875  10.745  -4.640  1.00 69.98
ATOM   2472  CB  ALA A 318      19.880   8.878  -3.832  1.00 69.98
ATOM   2473  N   LYS A 319      17.370   9.624  -6.515  1.00 68.79
ATOM   2474  CA  LYS A 319      16.088  10.304  -6.741  1.00 68.79
ATOM   2475  C   LYS A 319      14.968   9.731  -5.874  1.00 68.79
ATOM   2476  O   LYS A 319      14.873   8.523  -5.668  1.00 68.79
ATOM   2477  CB  LYS A 319      15.698  10.304  -8.226  1.00 68.79
ATOM   2478  CG  LYS A 319      16.660  11.163  -9.061  1.00 68.79
ATOM   2479  CD  LYS A 319      16.143  11.340 -10.495  1.00 68.79
ATOM   2480  CE  LYS A 319      17.105  12.237 -11.283  1.00 68.79
ATOM   2481  NZ  LYS A 319      16.623  12.495 -12.666  1.00 68.79
ATOM   2482  N   ASP A 320      14.101  10.631  -5.428  1.00 66.26
ATOM   2483  CA  ASP A 320      12.888  10.330  -4.675  1.00 66.26
ATOM   2484  C   ASP A 320      11.778   9.757  -5.587  1.00 66.26
ATOM   2485  O   ASP A 320      11.724  10.045  -6.788  1.00 66.26
ATOM   2486  CB  ASP A 320      12.440  11.629  -3.959  1.00 66.26
ATOM   2487  CG  ASP A 320      12.150  11.434  -2.478  1.00 66.26
ATOM   2488  OD1 ASP A 320      11.762  10.303  -2.134  1.00 66.26
ATOM   2489  OD2 ASP A 320      12.328  12.388  -1.674  1.00 66.26
ATOM   2490  N   GLY A 321      10.859   8.971  -5.021  1.00 73.25
ATOM   2491  CA  GLY A 321       9.656   8.504  -5.726  1.00 73.25
ATOM   2492  C   GLY A 321       9.910   7.621  -6.971  1.00 73.25
ATOM   2493  O   GLY A 321      10.879   6.852  -6.998  1.00 73.25
ATOM   2494  N   PRO A 322       9.007   7.631  -7.992  1.00 82.05
ATOM   2495  CA  PRO A 322       9.003   6.653  -9.115  1.00 82.05
ATOM   2496  C   PRO A 322      10.266   6.676  -9.951  1.00 82.05
ATOM   2497  O   PRO A 322      10.619   5.657 -10.548  1.00 82.05
ATOM   2498  CB  PRO A 322       7.706   6.888  -9.893  1.00 82.05
ATOM   2499  CG  PRO A 322       7.248   8.276  -9.456  1.00 82.05
ATOM   2500  CD  PRO A 322       7.785   8.421  -8.034  1.00 82.05
ATOM   2501  N   GLY A 323      11.012   7.778  -9.893  1.00 83.66
ATOM   2502  CA  GLY A 323      12.313   7.884 -10.528  1.00 83.66
ATOM   2503  C   GLY A 323      13.303   6.811 -10.071  1.00 83.66
ATOM   2504  O   GLY A 323      14.079   6.330 -10.891  1.00 83.66
ATOM   2505  N   LEU A 324      13.269   6.346  -8.818  1.00 84.23
ATOM   2506  CA  LEU A 324      14.246   5.345  -8.378  1.00 84.23
ATOM   2507  C   LEU A 324      14.120   4.033  -9.175  1.00 84.23
ATOM   2508  O   LEU A 324      15.107   3.541  -9.718  1.00 84.23
ATOM   2509  CB  LEU A 324      14.123   5.134  -6.860  1.00 84.23
ATOM   2510  CG  LEU A 324      15.233   4.243  -6.269  1.00 84.23
ATOM   2511  CD1 LEU A 324      16.640   4.803  -6.493  1.00 84.23
ATOM   2512  CD2 LEU A 324      15.037   4.116  -4.762  1.00 84.23
ATOM   2513  N   ILE A 325      12.905   3.493  -9.299  1.00 90.10
ATOM   2514  CA  ILE A 325      12.655   2.198  -9.956  1.00 90.10
ATOM   2515  C   ILE A 325      12.453   2.290 -11.469  1.00 90.10
ATOM   2516  O   ILE A 325      12.700   1.303 -12.156  1.00 90.10
ATOM   2517  CB  ILE A 325      11.472   1.450  -9.311  1.00 90.10
ATOM   2518  CG1 ILE A 325      10.187   2.305  -9.286  1.00 90.10
ATOM   2519  CG2 ILE A 325      11.884   0.996  -7.908  1.00 90.10
ATOM   2520  CD1 ILE A 325       8.934   1.534  -8.856  1.00 90.10
ATOM   2521  N   PHE A 326      12.015   3.437 -11.996  1.00 93.46
ATOM   2522  CA  PHE A 326      11.742   3.604 -13.430  1.00 93.46
ATOM   2523  C   PHE A 326      12.803   4.423 -14.175  1.00 93.46
ATOM   2524  O   PHE A 326      12.823   4.400 -15.404  1.00 93.46
ATOM   2525  CB  PHE A 326      10.331   4.170 -13.635  1.00 93.46
ATOM   2526  CG  PHE A 326       9.223   3.256 -13.147  1.00 93.46
ATOM   2527  CD1 PHE A 326       9.015   2.012 -13.769  1.00 93.46
ATOM   2528  CD2 PHE A 326       8.408   3.636 -12.068  1.00 93.46
ATOM   2529  CE1 PHE A 326       8.023   1.142 -13.288  1.00 93.46
ATOM   2530  CE2 PHE A 326       7.424   2.760 -11.582  1.00 93.46
ATOM   2531  CZ  PHE A 326       7.227   1.510 -12.191  1.00 93.46
ATOM   2532  N   ILE A 327      13.714   5.101 -13.471  1.00 91.56
ATOM   2533  CA  ILE A 327      14.822   5.852 -14.082  1.00 91.56
ATOM   2534  C   ILE A 327      16.161   5.239 -13.673  1.00 91.56
ATOM   2535  O   ILE A 327      16.869   4.697 -14.516  1.00 91.56
ATOM   2536  CB  ILE A 327      14.729   7.370 -13.776  1.00 91.56
ATOM   2537  CG1 ILE A 327      13.380   7.949 -14.265  1.00 91.56
ATOM   2538  CG2 ILE A 327      15.941   8.095 -14.376  1.00 91.56
ATOM   2539  CD1 ILE A 327      13.134   9.401 -13.829  1.00 91.56
ATOM   2540  N   ILE A 328      16.485   5.251 -12.379  1.00 87.00
ATOM   2541  CA  ILE A 328      17.835   4.911 -11.905  1.00 87.00
ATOM   2542  C   ILE A 328      18.146   3.417 -12.052  1.00 87.00
ATOM   2543  O   ILE A 328      19.203   3.048 -12.557  1.00 87.00
ATOM   2544  CB  ILE A 328      18.018   5.387 -10.451  1.00 87.00
ATOM   2545  CG1 ILE A 328      17.748   6.899 -10.266  1.00 87.00
ATOM   2546  CG2 ILE A 328      19.416   5.029  -9.930  1.00 87.00
ATOM   2547  CD1 ILE A 328      18.662   7.829 -11.077  1.00 87.00
ATOM   2548  N   TYR A 329      17.229   2.539 -11.644  1.00 87.97
ATOM   2549  CA  TYR A 329      17.409   1.094 -11.809  1.00 87.97
ATOM   2550  C   TYR A 329      17.511   0.661 -13.275  1.00 87.97
ATOM   2551  O   TYR A 329      18.438  -0.080 -13.600  1.00 87.97
ATOM   2552  CB  TYR A 329      16.285   0.331 -11.109  1.00 87.97
ATOM   2553  CG  TYR A 329      16.678  -0.183  -9.756  1.00 87.97
ATOM   2554  CD1 TYR A 329      17.169  -1.493  -9.634  1.00 87.97
ATOM   2555  CD2 TYR A 329      16.531   0.637  -8.626  1.00 87.97
ATOM   2556  CE1 TYR A 329      17.450  -2.012  -8.363  1.00 87.97
ATOM   2557  CE2 TYR A 329      16.802   0.122  -7.350  1.00 87.97
ATOM   2558  CZ  TYR A 329      17.233  -1.219  -7.223  1.00 87.97
ATOM   2559  OH  TYR A 329      17.397  -1.806  -6.015  1.00 87.97
ATOM   2560  N   PRO A 330      16.613   1.103 -14.174  1.00 92.44
ATOM   2561  CA  PRO A 330      16.706   0.759 -15.588  1.00 92.44
ATOM   2562  C   PRO A 330      18.002   1.264 -16.218  1.00 92.44
ATOM   2563  O   PRO A 330      18.613   0.530 -16.996  1.00 92.44
ATOM   2564  CB  PRO A 330      15.456   1.359 -16.236  1.00 92.44
ATOM   2565  CG  PRO A 330      14.468   1.301 -15.080  1.00 92.44
ATOM   2566  CD  PRO A 330      15.329   1.728 -13.912  1.00 92.44
ATOM   2567  N   GLU A 331      18.464   2.454 -15.827  1.00 91.22
ATOM   2568  CA  GLU A 331      19.763   2.996 -16.234  1.00 91.22
ATOM   2569  C   GLU A 331      20.924   2.110 -15.759  1.00 91.22
ATOM   2570  O   GLU A 331      21.810   1.772 -16.542  1.00 91.22
ATOM   2571  CB  GLU A 331      19.898   4.427 -15.689  1.00 91.22
ATOM   2572  CG  GLU A 331      21.038   5.194 -16.361  1.00 91.22
ATOM   2573  CD  GLU A 331      21.189   6.624 -15.821  1.00 91.22
ATOM   2574  OE1 GLU A 331      22.359   7.043 -15.668  1.00 91.22
ATOM   2575  OE2 GLU A 331      20.163   7.311 -15.593  1.00 91.22
ATOM   2576  N   ALA A 332      20.898   1.661 -14.502  1.00 89.92
ATOM   2577  CA  ALA A 332      21.937   0.799 -13.947  1.00 89.92
ATOM   2578  C   ALA A 332      21.913  -0.622 -14.538  1.00 89.92
ATOM   2579  O   ALA A 332      22.957  -1.216 -14.791  1.00 89.92
ATOM   2580  CB  ALA A 332      21.791   0.801 -12.422  1.00 89.92
ATOM   2581  N   ILE A 333      20.727  -1.169 -14.802  1.00 92.49
ATOM   2582  CA  ILE A 333      20.542  -2.473 -15.450  1.00 92.49
ATOM   2583  C   ILE A 333      21.001  -2.429 -16.911  1.00 92.49
ATOM   2584  O   ILE A 333      21.583  -3.400 -17.398  1.00 92.49
ATOM   2585  CB  ILE A 333      19.068  -2.915 -15.313  1.00 92.49
ATOM   2586  CG1 ILE A 333      18.798  -3.350 -13.853  1.00 92.49
ATOM   2587  CG2 ILE A 333      18.740  -4.060 -16.283  1.00 92.49
ATOM   2588  CD1 ILE A 333      17.312  -3.550 -13.529  1.00 92.49
ATOM   2589  N   ALA A 334      20.792  -1.306 -17.602  1.00 93.04
ATOM   2590  CA  ALA A 334      21.210  -1.123 -18.987  1.00 93.04
ATOM   2591  C   ALA A 334      22.725  -1.266 -19.194  1.00 93.04
ATOM   2592  O   ALA A 334      23.156  -1.609 -20.293  1.00 93.04
ATOM   2593  CB  ALA A 334      20.729   0.242 -19.471  1.00 93.04
ATOM   2594  N   THR A 335      23.537  -1.053 -18.155  1.00 90.33
ATOM   2595  CA  THR A 335      24.998  -1.190 -18.239  1.00 90.33
ATOM   2596  C   THR A 335      25.490  -2.631 -18.091  1.00 90.33
ATOM   2597  O   THR A 335      26.672  -2.912 -18.306  1.00 90.33
ATOM   2598  CB  THR A 335      25.702  -0.334 -17.183  1.00 90.33
ATOM   2599  OG1 THR A 335      25.701  -1.003 -15.953  1.00 90.33
ATOM   2600  CG2 THR A 335      25.065   1.033 -16.945  1.00 90.33
ATOM   2601  N   LEU A 336      24.615  -3.547 -17.671  1.00 91.30
ATOM   2602  CA  LEU A 336      24.976  -4.934 -17.432  1.00 91.30
ATOM   2603  C   LEU A 336      25.068  -5.716 -18.750  1.00 91.30
ATOM   2604  O   LEU A 336      24.291  -5.475 -19.675  1.00 91.30
ATOM   2605  CB  LEU A 336      23.966  -5.593 -16.477  1.00 91.30
ATOM   2606  CG  LEU A 336      23.833  -4.935 -15.092  1.00 91.30
ATOM   2607  CD1 LEU A 336      22.927  -5.820 -14.234  1.00 91.30
ATOM   2608  CD2 LEU A 336      25.186  -4.799 -14.394  1.00 91.30
ATOM   2609  N   PRO A 337      25.946  -6.732 -18.831  1.00 90.80
ATOM   2610  CA  PRO A 337      25.857  -7.704 -19.911  1.00 90.80
ATOM   2611  C   PRO A 337      24.507  -8.429 -19.834  1.00 90.80
ATOM   2612  O   PRO A 337      24.051  -8.777 -18.742  1.00 90.80
ATOM   2613  CB  PRO A 337      27.041  -8.650 -19.708  1.00 90.80
ATOM   2614  CG  PRO A 337      27.274  -8.602 -18.197  1.00 90.80
ATOM   2615  CD  PRO A 337      26.908  -7.165 -17.828  1.00 90.80
ATOM   2616  N   LEU A 338      23.889  -8.673 -20.995  1.00 92.71
ATOM   2617  CA  LEU A 338      22.521  -9.202 -21.107  1.00 92.71
ATOM   2618  C   LEU A 338      21.497  -8.307 -20.377  1.00 92.71
ATOM   2619  O   LEU A 338      20.603  -8.802 -19.687  1.00 92.71
ATOM   2620  CB  LEU A 338      22.449 -10.688 -20.678  1.00 92.71
ATOM   2621  CG  LEU A 338      23.007 -11.730 -21.659  1.00 92.71
ATOM   2622  CD1 LEU A 338      24.502 -11.591 -21.951  1.00 92.71
ATOM   2623  CD2 LEU A 338      22.771 -13.121 -21.065  1.00 92.71
ATOM   2624  N   SER A 339      21.625  -6.986 -20.523  1.00 94.80
ATOM   2625  CA  SER A 339      20.760  -5.991 -19.877  1.00 94.80
ATOM   2626  C   SER A 339      19.265  -6.265 -20.072  1.00 94.80
ATOM   2627  O   SER A 339      18.514  -6.180 -19.103  1.00 94.80
ATOM   2628  CB  SER A 339      21.105  -4.593 -20.390  1.00 94.80
ATOM   2629  OG  SER A 339      21.066  -4.555 -21.804  1.00 94.80
ATOM   2630  N   SER A 340      18.827  -6.699 -21.259  1.00 96.18
ATOM   2631  CA  SER A 340      17.424  -7.069 -21.510  1.00 96.18
ATOM   2632  C   SER A 340      16.927  -8.203 -20.611  1.00 96.18
ATOM   2633  O   SER A 340      15.816  -8.136 -20.090  1.00 96.18
ATOM   2634  CB  SER A 340      17.215  -7.459 -22.977  1.00 96.18
ATOM   2635  OG  SER A 340      17.737  -6.457 -23.819  1.00 96.18
ATOM   2636  N   ALA A 341      17.750  -9.225 -20.353  1.00 95.75
ATOM   2637  CA  ALA A 341      17.370 -10.326 -19.465  1.00 95.75
ATOM   2638  C   ALA A 341      17.228  -9.849 -18.011  1.00 95.75
ATOM   2639  O   ALA A 341      16.268 -10.207 -17.328  1.00 95.75
ATOM   2640  CB  ALA A 341      18.399 -11.456 -19.591  1.00 95.75
ATOM   2641  N   TRP A 342      18.149  -8.997 -17.554  1.00 95.06
ATOM   2642  CA  TRP A 342      18.068  -8.379 -16.231  1.00 95.06
ATOM   2643  C   TRP A 342      16.845  -7.471 -16.091  1.00 95.06
ATOM   2644  O   TRP A 342      16.166  -7.533 -15.068  1.00 95.06
ATOM   2645  CB  TRP A 342      19.356  -7.603 -15.956  1.00 95.06
ATOM   2646  CG  TRP A 342      20.540  -8.460 -15.665  1.00 95.06
ATOM   2647  CD1 TRP A 342      21.612  -8.632 -16.467  1.00 95.06
ATOM   2648  CD2 TRP A 342      20.775  -9.289 -14.491  1.00 95.06
ATOM   2649  NE1 TRP A 342      22.494  -9.514 -15.877  1.00 95.06
ATOM   2650  CE2 TRP A 342      22.029  -9.950 -14.651  1.00 95.06
ATOM   2651  CE3 TRP A 342      20.046  -9.549 -13.310  1.00 95.06
ATOM   2652  CZ2 TRP A 342      22.536 -10.829 -13.681  1.00 95.06
ATOM   2653  CZ3 TRP A 342      20.547 -10.425 -12.329  1.00 95.06
ATOM   2654  CH2 TRP A 342      21.787 -11.063 -12.512  1.00 95.06
ATOM   2655  N   ALA A 343      16.527  -6.685 -17.122  1.00 96.93
ATOM   2656  CA  ALA A 343      15.355  -5.819 -17.144  1.00 96.93
ATOM   2657  C   ALA A 343      14.057  -6.636 -17.065  1.00 96.93
ATOM   2658  O   ALA A 343      13.218  -6.353 -16.212  1.00 96.93
ATOM   2659  CB  ALA A 343      15.419  -4.935 -18.394  1.00 96.93
ATOM   2660  N   VAL A 344      13.924  -7.709 -17.856  1.00 97.10
ATOM   2661  CA  VAL A 344      12.762  -8.615 -17.796  1.00 97.10
ATOM   2662  C   VAL A 344      12.563  -9.161 -16.381  1.00 97.10
ATOM   2663  O   VAL A 344      11.467  -9.068 -15.833  1.00 97.10
ATOM   2664  CB  VAL A 344      12.903  -9.766 -18.816  1.00 97.10
ATOM   2665  CG1 VAL A 344      11.881 -10.893 -18.604  1.00 97.10
ATOM   2666  CG2 VAL A 344      12.698  -9.255 -20.247  1.00 97.10
ATOM   2667  N   VAL A 345      13.613  -9.698 -15.758  1.00 95.21
ATOM   2668  CA  VAL A 345      13.513 -10.287 -14.414  1.00 95.21
ATOM   2669  C   VAL A 345      13.207  -9.216 -13.352  1.00 95.21
ATOM   2670  O   VAL A 345      12.384  -9.450 -12.467  1.00 95.21
ATOM   2671  CB  VAL A 345      14.784 -11.102 -14.108  1.00 95.21
ATOM   2672  CG1 VAL A 345      14.754 -11.713 -12.713  1.00 95.21
ATOM   2673  CG2 VAL A 345      14.936 -12.290 -15.071  1.00 95.21
ATOM   2674  N   PHE A 346      13.791  -8.019 -13.467  1.00 95.59
ATOM   2675  CA  PHE A 346      13.512  -6.882 -12.583  1.00 95.59
ATOM   2676  C   PHE A 346      12.059  -6.397 -12.684  1.00 95.59
ATOM   2677  O   PHE A 346      11.389  -6.241 -11.663  1.00 95.59
ATOM   2678  CB  PHE A 346      14.492  -5.747 -12.907  1.00 95.59
ATOM   2679  CG  PHE A 346      14.241  -4.471 -12.129  1.00 95.59
ATOM   2680  CD1 PHE A 346      13.629  -3.366 -12.752  1.00 95.59
ATOM   2681  CD2 PHE A 346      14.615  -4.386 -10.776  1.00 95.59
ATOM   2682  CE1 PHE A 346      13.410  -2.183 -12.026  1.00 95.59
ATOM   2683  CE2 PHE A 346      14.385  -3.207 -10.047  1.00 95.59
ATOM   2684  CZ  PHE A 346      13.785  -2.104 -10.674  1.00 95.59
ATOM   2685  N   PHE A 347      11.530  -6.211 -13.895  1.00 97.02
ATOM   2686  CA  PHE A 347      10.151  -5.757 -14.076  1.00 97.02
ATOM   2687  C   PHE A 347       9.117  -6.845 -13.777  1.00 97.02
ATOM   2688  O   PHE A 347       8.025  -6.511 -13.324  1.00 97.02
ATOM   2689  CB  PHE A 347       9.965  -5.139 -15.464  1.00 97.02
ATOM   2690  CG  PHE A 347      10.650  -3.796 -15.593  1.00 97.02
ATOM   2691  CD1 PHE A 347      10.195  -2.718 -14.813  1.00 97.02
ATOM   2692  CD2 PHE A 347      11.746  -3.622 -16.458  1.00 97.02
ATOM   2693  CE1 PHE A 347      10.860  -1.484 -14.857  1.00 97.02
ATOM   2694  CE2 PHE A 347      12.418  -2.390 -16.502  1.00 97.02
ATOM   2695  CZ  PHE A 347      11.971  -1.327 -15.699  1.00 97.02
ATOM   2696  N   ILE A 348       9.460  -8.133 -13.922  1.00 95.95
ATOM   2697  CA  ILE A 348       8.646  -9.232 -13.374  1.00 95.95
ATOM   2698  C   ILE A 348       8.552  -9.108 -11.851  1.00 95.95
ATOM   2699  O   ILE A 348       7.450  -9.192 -11.324  1.00 95.95
ATOM   2700  CB  ILE A 348       9.182 -10.616 -13.812  1.00 95.95
ATOM   2701  CG1 ILE A 348       8.847 -10.849 -15.302  1.00 95.95
ATOM   2702  CG2 ILE A 348       8.582 -11.762 -12.968  1.00 95.95
ATOM   2703  CD1 ILE A 348       9.572 -12.050 -15.923  1.00 95.95
ATOM   2704  N   MET A 349       9.661  -8.854 -11.147  1.00 95.62
ATOM   2705  CA  MET A 349       9.637  -8.639  -9.694  1.00 95.62
ATOM   2706  C   MET A 349       8.747  -7.452  -9.305  1.00 95.62
ATOM   2707  O   MET A 349       7.917  -7.594  -8.409  1.00 95.62
ATOM   2708  CB  MET A 349      11.068  -8.468  -9.170  1.00 95.62
ATOM   2709  CG  MET A 349      11.151  -7.957  -7.726  1.00 95.62
ATOM   2710  SD  MET A 349      12.830  -7.554  -7.187  1.00 95.62
ATOM   2711  CE  MET A 349      13.017  -5.940  -7.995  1.00 95.62
ATOM   2712  N   LEU A 350       8.888  -6.296  -9.965  1.00 95.74
ATOM   2713  CA  LEU A 350       8.037  -5.132  -9.678  1.00 95.74
ATOM   2714  C   LEU A 350       6.555  -5.435  -9.943  1.00 95.74
ATOM   2715  O   LEU A 350       5.698  -5.061  -9.143  1.00 95.74
ATOM   2716  CB  LEU A 350       8.478  -3.913 -10.508  1.00 95.74
ATOM   2717  CG  LEU A 350       9.872  -3.340 -10.194  1.00 95.74
ATOM   2718  CD1 LEU A 350      10.079  -2.089 -11.046  1.00 95.74
ATOM   2719  CD2 LEU A 350      10.062  -2.932  -8.733  1.00 95.74
ATOM   2720  N   LEU A 351       6.256  -6.149 -11.032  1.00 96.16
ATOM   2721  CA  LEU A 351       4.905  -6.585 -11.369  1.00 96.16
ATOM   2722  C   LEU A 351       4.336  -7.519 -10.293  1.00 96.16
ATOM   2723  O   LEU A 351       3.203  -7.322  -9.865  1.00 96.16
ATOM   2724  CB  LEU A 351       4.940  -7.250 -12.759  1.00 96.16
ATOM   2725  CG  LEU A 351       3.585  -7.756 -13.279  1.00 96.16
ATOM   2726  CD1 LEU A 351       2.603  -6.611 -13.500  1.00 96.16
ATOM   2727  CD2 LEU A 351       3.771  -8.491 -14.604  1.00 96.16
ATOM   2728  N   THR A 352       5.100  -8.512  -9.830  1.00 95.91
ATOM   2729  CA  THR A 352       4.621  -9.463  -8.820  1.00 95.91
ATOM   2730  C   THR A 352       4.431  -8.822  -7.447  1.00 95.91
ATOM   2731  O   THR A 352       3.399  -9.064  -6.829  1.00 95.91
ATOM   2732  CB  THR A 352       5.512 -10.706  -8.708  1.00 95.91
ATOM   2733  OG1 THR A 352       6.858 -10.393  -8.443  1.00 95.91
ATOM   2734  CG2 THR A 352       5.489 -11.567  -9.976  1.00 95.91
ATOM   2735  N   LEU A 353       5.360  -7.957  -7.015  1.00 95.98
ATOM   2736  CA  LEU A 353       5.218  -7.174  -5.779  1.00 95.98
ATOM   2737  C   LEU A 353       3.967  -6.295  -5.830  1.00 95.98
ATOM   2738  O   LEU A 353       3.169  -6.278  -4.900  1.00 95.98
ATOM   2739  CB  LEU A 353       6.459  -6.281  -5.582  1.00 95.98
ATOM   2740  CG  LEU A 353       7.740  -7.030  -5.189  1.00 95.98
ATOM   2741  CD1 LEU A 353       8.933  -6.081  -5.258  1.00 95.98
ATOM   2742  CD2 LEU A 353       7.673  -7.587  -3.771  1.00 95.98
ATOM   2743  N   GLY A 354       3.765  -5.595  -6.949  1.00 95.90
ATOM   2744  CA  GLY A 354       2.603  -4.736  -7.119  1.00 95.90
ATOM   2745  C   GLY A 354       1.280  -5.512  -7.151  1.00 95.90
ATOM   2746  O   GLY A 354       0.299  -5.097  -6.536  1.00 95.90
ATOM   2747  N   ILE A 355       1.232  -6.654  -7.844  1.00 96.19
ATOM   2748  CA  ILE A 355       0.013  -7.470  -7.939  1.00 96.19
ATOM   2749  C   ILE A 355      -0.422  -7.983  -6.564  1.00 96.19
ATOM   2750  O   ILE A 355      -1.610  -7.888  -6.258  1.00 96.19
ATOM   2751  CB  ILE A 355       0.186  -8.611  -8.970  1.00 96.19
ATOM   2752  CG1 ILE A 355       0.108  -8.025 -10.399  1.00 96.19
ATOM   2753  CG2 ILE A 355      -0.885  -9.709  -8.807  1.00 96.19
ATOM   2754  CD1 ILE A 355       0.493  -9.024 -11.498  1.00 96.19
ATOM   2755  N   ASP A 356       0.493  -8.485  -5.730  1.00 96.34
ATOM   2756  CA  ASP A 356       0.130  -9.003  -4.404  1.00 96.34
ATOM   2757  C   ASP A 356      -0.466  -7.914  -3.504  1.00 96.34
ATOM   2758  O   ASP A 356      -1.520  -8.120  -2.888  1.00 96.34
ATOM   2759  CB  ASP A 356       1.344  -9.651  -3.724  1.00 96.34
ATOM   2760  CG  ASP A 356       1.650 -11.055  -4.236  1.00 96.34
ATOM   2761  OD1 ASP A 356       0.731 -11.712  -4.779  1.00 96.34
ATOM   2762  OD2 ASP A 356       2.779 -11.544  -4.040  1.00 96.34
ATOM   2763  N   SER A 357       0.139  -6.725  -3.485  1.00 95.22
ATOM   2764  CA  SER A 357      -0.378  -5.596  -2.710  1.00 95.22
ATOM   2765  C   SER A 357      -1.732  -5.107  -3.224  1.00 95.22
ATOM   2766  O   SER A 357      -2.656  -4.895  -2.434  1.00 95.22
ATOM   2767  CB  SER A 357       0.629  -4.453  -2.689  1.00 95.22
ATOM   2768  OG  SER A 357       1.854  -4.941  -2.201  1.00 95.22
ATOM   2769  N   ALA A 358      -1.898  -4.994  -4.546  1.00 95.98
ATOM   2770  CA  ALA A 358      -3.167  -4.609  -5.163  1.00 95.98
ATOM   2771  C   ALA A 358      -4.272  -5.648  -4.914  1.00 95.98
ATOM   2772  O   ALA A 358      -5.417  -5.280  -4.636  1.00 95.98
ATOM   2773  CB  ALA A 358      -2.932  -4.380  -6.658  1.00 95.98
ATOM   2774  N   MET A 359      -3.940  -6.942  -4.960  1.00 95.88
ATOM   2775  CA  MET A 359      -4.859  -8.023  -4.604  1.00 95.88
ATOM   2776  C   MET A 359      -5.325  -7.901  -3.153  1.00 95.88
ATOM   2777  O   MET A 359      -6.525  -7.980  -2.897  1.00 95.88
ATOM   2778  CB  MET A 359      -4.201  -9.392  -4.828  1.00 95.88
ATOM   2779  CG  MET A 359      -4.194  -9.794  -6.305  1.00 95.88
ATOM   2780  SD  MET A 359      -3.274 -11.310  -6.695  1.00 95.88
ATOM   2781  CE  MET A 359      -3.956 -12.464  -5.484  1.00 95.88
ATOM   2782  N   GLY A 360      -4.405  -7.671  -2.212  1.00 96.16
ATOM   2783  CA  GLY A 360      -4.748  -7.467  -0.804  1.00 96.16
ATOM   2784  C   GLY A 360      -5.651  -6.257  -0.587  1.00 96.16
ATOM   2785  O   GLY A 360      -6.730  -6.397  -0.008  1.00 96.16
ATOM   2786  N   GLY A 361      -5.258  -5.094  -1.114  1.00 95.39
ATOM   2787  CA  GLY A 361      -6.021  -3.848  -0.992  1.00 95.39
ATOM   2788  C   GLY A 361      -7.433  -3.936  -1.578  1.00 95.39
ATOM   2789  O   GLY A 361      -8.384  -3.435  -0.987  1.00 95.39
ATOM   2790  N   MET A 362      -7.621  -4.619  -2.708  1.00 95.70
ATOM   2791  CA  MET A 362      -8.965  -4.804  -3.267  1.00 95.70
ATOM   2792  C   MET A 362      -9.778  -5.867  -2.535  1.00 95.70
ATOM   2793  O   MET A 362     -10.985  -5.693  -2.375  1.00 95.70
ATOM   2794  CB  MET A 362      -8.881  -5.133  -4.750  1.00 95.70
ATOM   2795  CG  MET A 362      -8.571  -3.866  -5.542  1.00 95.70
ATOM   2796  SD  MET A 362      -8.586  -4.131  -7.321  1.00 95.70
ATOM   2797  CE  MET A 362      -7.002  -4.969  -7.414  1.00 95.70
ATOM   2798  N   GLU A 363      -9.153  -6.943  -2.054  1.00 96.33
ATOM   2799  CA  GLU A 363      -9.848  -7.941  -1.239  1.00 96.33
ATOM   2800  C   GLU A 363     -10.376  -7.322   0.065  1.00 96.33
ATOM   2801  O   GLU A 363     -11.464  -7.705   0.498  1.00 96.33
ATOM   2802  CB  GLU A 363      -8.928  -9.143  -0.970  1.00 96.33
ATOM   2803  CG  GLU A 363      -9.603 -10.317  -0.234  1.00 96.33
ATOM   2804  CD  GLU A 363     -10.780 -10.974  -0.979  1.00 96.33
ATOM   2805  OE1 GLU A 363     -11.634 -11.586  -0.293  1.00 96.33
ATOM   2806  OE2 GLU A 363     -10.853 -10.930  -2.227  1.00 96.33
ATOM   2807  N   SER A 364      -9.685  -6.337   0.661  1.00 96.55
ATOM   2808  CA  SER A 364     -10.190  -5.627   1.849  1.00 96.55
ATOM   2809  C   SER A 364     -11.454  -4.822   1.558  1.00 96.55
ATOM   2810  O   SER A 364     -12.425  -4.919   2.313  1.00 96.55
ATOM   2811  CB  SER A 364      -9.122  -4.741   2.505  1.00 96.55
ATOM   2812  OG  SER A 364      -8.928  -3.518   1.832  1.00 96.55
ATOM   2813  N   VAL A 365     -11.487  -4.104   0.431  1.00 96.68
ATOM   2814  CA  VAL A 365     -12.662  -3.355  -0.036  1.00 96.68
ATOM   2815  C   VAL A 365     -13.821  -4.302  -0.333  1.00 96.68
ATOM   2816  O   VAL A 365     -14.926  -4.111   0.176  1.00 96.68
ATOM   2817  CB  VAL A 365     -12.316  -2.518  -1.285  1.00 96.68
ATOM   2818  CG1 VAL A 365     -13.546  -1.813  -1.876  1.00 96.68
ATOM   2819  CG2 VAL A 365     -11.273  -1.446  -0.957  1.00 96.68
ATOM   2820  N   ILE A 366     -13.568  -5.348  -1.126  1.00 96.02
ATOM   2821  CA  ILE A 366     -14.581  -6.329  -1.527  1.00 96.02
ATOM   2822  C   ILE A 366     -15.172  -7.000  -0.288  1.00 96.02
ATOM   2823  O   ILE A 366     -16.388  -7.021  -0.114  1.00 96.02
ATOM   2824  CB  ILE A 366     -13.975  -7.360  -2.508  1.00 96.02
ATOM   2825  CG1 ILE A 366     -13.662  -6.689  -3.864  1.00 96.02
ATOM   2826  CG2 ILE A 366     -14.925  -8.551  -2.734  1.00 96.02
ATOM   2827  CD1 ILE A 366     -12.685  -7.502  -4.723  1.00 96.02
ATOM   2828  N   THR A 367     -14.312  -7.500   0.597  1.00 95.66
ATOM   2829  CA  THR A 367     -14.719  -8.193   1.819  1.00 95.66
ATOM   2830  C   THR A 367     -15.490  -7.272   2.761  1.00 95.66
ATOM   2831  O   THR A 367     -16.556  -7.640   3.248  1.00 95.66
ATOM   2832  CB  THR A 367     -13.485  -8.747   2.537  1.00 95.66
ATOM   2833  OG1 THR A 367     -12.841  -9.712   1.745  1.00 95.66
ATOM   2834  CG2 THR A 367     -13.871  -9.459   3.813  1.00 95.66
ATOM   2835  N   GLY A 368     -14.979  -6.062   3.003  1.00 95.59
ATOM   2836  CA  GLY A 368     -15.608  -5.098   3.901  1.00 95.59
ATOM   2837  C   GLY A 368     -17.012  -4.687   3.454  1.00 95.59
ATOM   2838  O   GLY A 368     -17.885  -4.509   4.300  1.00 95.59
ATOM   2839  N   LEU A 369     -17.246  -4.580   2.143  1.00 95.68
ATOM   2840  CA  LEU A 369     -18.548  -4.213   1.582  1.00 95.68
ATOM   2841  C   LEU A 369     -19.503  -5.406   1.440  1.00 95.68
ATOM   2842  O   LEU A 369     -20.696  -5.244   1.689  1.00 95.68
ATOM   2843  CB  LEU A 369     -18.332  -3.504   0.234  1.00 95.68
ATOM   2844  CG  LEU A 369     -17.607  -2.146   0.336  1.00 95.68
ATOM   2845  CD1 LEU A 369     -17.343  -1.593  -1.065  1.00 95.68
ATOM   2846  CD2 LEU A 369     -18.425  -1.106   1.106  1.00 95.68
ATOM   2847  N   ILE A 370     -19.013  -6.597   1.073  1.00 93.83
ATOM   2848  CA  ILE A 370     -19.847  -7.810   0.986  1.00 93.83
ATOM   2849  C   ILE A 370     -20.421  -8.180   2.356  1.00 93.83
ATOM   2850  O   ILE A 370     -21.603  -8.517   2.442  1.00 93.83
ATOM   2851  CB  ILE A 370     -19.062  -8.991   0.362  1.00 93.83
ATOM   2852  CG1 ILE A 370     -18.932  -8.777  -1.163  1.00 93.83
ATOM   2853  CG2 ILE A 370     -19.741 -10.349   0.639  1.00 93.83
ATOM   2854  CD1 ILE A 370     -18.097  -9.849  -1.875  1.00 93.83
ATOM   2855  N   ASP A 371     -19.612  -8.094   3.414  1.00 91.87
ATOM   2856  CA  ASP A 371     -20.056  -8.441   4.767  1.00 91.87
ATOM   2857  C   ASP A 371     -21.132  -7.468   5.281  1.00 91.87
ATOM   2858  O   ASP A 371     -22.038  -7.871   6.012  1.00 91.87
ATOM   2859  CB  ASP A 371     -18.844  -8.501   5.713  1.00 91.87
ATOM   2860  CG  ASP A 371     -17.940  -9.724   5.488  1.00 91.87
ATOM   2861  OD1 ASP A 371     -18.333 -10.690   4.805  1.00 91.87
ATOM   2862  OD2 ASP A 371     -16.826  -9.745   6.062  1.00 91.87
ATOM   2863  N   GLU A 372     -21.093  -6.206   4.848  1.00 91.36
ATOM   2864  CA  GLU A 372     -22.112  -5.214   5.196  1.00 91.36
ATOM   2865  C   GLU A 372     -23.398  -5.379   4.377  1.00 91.36
ATOM   2866  O   GLU A 372     -24.510  -5.344   4.907  1.00 91.36
ATOM   2867  CB  GLU A 372     -21.526  -3.805   4.998  1.00 91.36
ATOM   2868  CG  GLU A 372     -22.458  -2.701   5.522  1.00 91.36
ATOM   2869  CD  GLU A 372     -22.689  -2.795   7.034  1.00 91.36
ATOM   2870  OE1 GLU A 372     -23.560  -2.077   7.583  1.00 91.36
ATOM   2871  OE2 GLU A 372     -21.939  -3.518   7.729  1.00 91.36
ATOM   2872  N   PHE A 373     -23.256  -5.576   3.067  1.00 90.85
ATOM   2873  CA  PHE A 373     -24.369  -5.650   2.133  1.00 90.85
ATOM   2874  C   PHE A 373     -24.544  -7.082   1.631  1.00 90.85
ATOM   2875  O   PHE A 373     -24.109  -7.441   0.539  1.00 90.85
ATOM   2876  CB  PHE A 373     -24.166  -4.637   1.002  1.00 90.85
ATOM   2877  CG  PHE A 373     -24.017  -3.199   1.457  1.00 90.85
ATOM   2878  CD1 PHE A 373     -25.122  -2.500   1.977  1.00 90.85
ATOM   2879  CD2 PHE A 373     -22.765  -2.561   1.367  1.00 90.85
ATOM   2880  CE1 PHE A 373     -24.975  -1.168   2.402  1.00 90.85
ATOM   2881  CE2 PHE A 373     -22.618  -1.231   1.795  1.00 90.85
ATOM   2882  CZ  PHE A 373     -23.724  -0.534   2.312  1.00 90.85
ATOM   2883  N   GLN A 374     -25.280  -7.886   2.400  1.00 82.53
ATOM   2884  CA  GLN A 374     -25.499  -9.324   2.164  1.00 82.53
ATOM   2885  C   GLN A 374     -26.007  -9.681   0.748  1.00 82.53
ATOM   2886  O   GLN A 374     -25.750 -10.774   0.242  1.00 82.53
ATOM   2887  CB  GLN A 374     -26.494  -9.828   3.225  1.00 82.53
ATOM   2888  CG  GLN A 374     -25.945  -9.724   4.662  1.00 82.53
ATOM   2889  CD  GLN A 374     -24.740 -10.633   4.882  1.00 82.53
ATOM   2890  OE1 GLN A 374     -24.759 -11.795   4.516  1.00 82.53
ATOM   2891  NE2 GLN A 374     -23.659 -10.165   5.461  1.00 82.53
ATOM   2892  N   LEU A 375     -26.685  -8.752   0.059  1.00 85.33
ATOM   2893  CA  LEU A 375     -27.119  -8.919  -1.337  1.00 85.33
ATOM   2894  C   LEU A 375     -25.945  -9.112  -2.319  1.00 85.33
ATOM   2895  O   LEU A 375     -26.114  -9.739  -3.370  1.00 85.33
ATOM   2896  CB  LEU A 375     -27.950  -7.691  -1.760  1.00 85.33
ATOM   2897  CG  LEU A 375     -29.247  -7.461  -0.963  1.00 85.33
ATOM   2898  CD1 LEU A 375     -29.927  -6.182  -1.453  1.00 85.33
ATOM   2899  CD2 LEU A 375     -30.237  -8.618  -1.116  1.00 85.33
ATOM   2900  N   LEU A 376     -24.762  -8.595  -1.976  1.00 86.87
ATOM   2901  CA  LEU A 376     -23.542  -8.697  -2.775  1.00 86.87
ATOM   2902  C   LEU A 376     -22.905 -10.087  -2.693  1.00 86.87
ATOM   2903  O   LEU A 376     -22.274 -10.506  -3.660  1.00 86.87
ATOM   2904  CB  LEU A 376     -22.533  -7.630  -2.319  1.00 86.87
ATOM   2905  CG  LEU A 376     -22.994  -6.169  -2.457  1.00 86.87
ATOM   2906  CD1 LEU A 376     -21.906  -5.253  -1.907  1.00 86.87
ATOM   2907  CD2 LEU A 376     -23.253  -5.795  -3.918  1.00 86.87
ATOM   2908  N   HIS A 377     -23.119 -10.840  -1.605  1.00 84.19
ATOM   2909  CA  HIS A 377     -22.532 -12.175  -1.428  1.00 84.19
ATOM   2910  C   HIS A 377     -22.941 -13.131  -2.560  1.00 84.19
ATOM   2911  O   HIS A 377     -22.123 -13.877  -3.097  1.00 84.19
ATOM   2912  CB  HIS A 377     -22.936 -12.737  -0.055  1.00 84.19
ATOM   2913  CG  HIS A 377     -22.087 -13.914   0.359  1.00 84.19
ATOM   2914  ND1 HIS A 377     -22.281 -15.239   0.029  1.00 84.19
ATOM   2915  CD2 HIS A 377     -20.948 -13.858   1.120  1.00 84.19
ATOM   2916  CE1 HIS A 377     -21.280 -15.952   0.568  1.00 84.19
ATOM   2917  NE2 HIS A 377     -20.432 -15.154   1.229  1.00 84.19
ATOM   2918  N   ARG A 378     -24.204 -13.045  -3.005  1.00 86.16
ATOM   2919  CA  ARG A 378     -24.732 -13.843  -4.124  1.00 86.16
ATOM   2920  C   ARG A 378     -24.090 -13.499  -5.473  1.00 86.16
ATOM   2921  O   ARG A 378     -24.090 -14.335  -6.371  1.00 86.16
ATOM   2922  CB  ARG A 378     -26.260 -13.684  -4.163  1.00 86.16
ATOM   2923  CG  ARG A 378     -26.907 -14.592  -5.218  1.00 86.16
ATOM   2924  CD  ARG A 378     -28.431 -14.544  -5.129  1.00 86.16
ATOM   2925  NE  ARG A 378     -29.036 -15.403  -6.163  1.00 86.16
ATOM   2926  CZ  ARG A 378     -30.325 -15.615  -6.348  1.00 86.16
ATOM   2927  NH1 ARG A 378     -31.228 -15.053  -5.593  1.00 86.16
ATOM   2928  NH2 ARG A 378     -30.732 -16.401  -7.304  1.00 86.16
ATOM   2929  N   HIS A 379     -23.554 -12.291  -5.616  1.00 90.72
ATOM   2930  CA  HIS A 379     -23.009 -11.764  -6.866  1.00 90.72
ATOM   2931  C   HIS A 379     -21.533 -11.381  -6.727  1.00 90.72
ATOM   2932  O   HIS A 379     -21.092 -10.454  -7.402  1.00 90.72
ATOM   2933  CB  HIS A 379     -23.876 -10.598  -7.365  1.00 90.72
ATOM   2934  CG  HIS A 379     -25.322 -10.962  -7.554  1.00 90.72
ATOM   2935  ND1 HIS A 379     -26.340 -10.678  -6.675  1.00 90.72
ATOM   2936  CD2 HIS A 379     -25.871 -11.633  -8.615  1.00 90.72
ATOM   2937  CE1 HIS A 379     -27.480 -11.147  -7.205  1.00 90.72
ATOM   2938  NE2 HIS A 379     -27.245 -11.760  -8.376  1.00 90.72
ATOM   2939  N   ARG A 380     -20.770 -12.084  -5.873  1.00 92.47
ATOM   2940  CA  ARG A 380     -19.360 -11.767  -5.587  1.00 92.47
ATOM   2941  C   ARG A 380     -18.549 -11.506  -6.854  1.00 92.47
ATOM   2942  O   ARG A 380     -17.917 -10.467  -6.937  1.00 92.47
ATOM   2943  CB  ARG A 380     -18.721 -12.879  -4.735  1.00 92.47
ATOM   2944  CG  ARG A 380     -17.233 -12.588  -4.466  1.00 92.47
ATOM   2945  CD  ARG A 380     -16.581 -13.628  -3.552  1.00 92.47
ATOM   2946  NE  ARG A 380     -15.176 -13.256  -3.304  1.00 92.47
ATOM   2947  CZ  ARG A 380     -14.566 -13.147  -2.134  1.00 92.47
ATOM   2948  NH1 ARG A 380     -15.070 -13.594  -1.021  1.00 92.47
ATOM   2949  NH2 ARG A 380     -13.414 -12.556  -2.067  1.00 92.47
ATOM   2950  N   GLU A 381     -18.614 -12.394  -7.847  1.00 94.93
ATOM   2951  CA  GLU A 381     -17.852 -12.251  -9.099  1.00 94.93
ATOM   2952  C   GLU A 381     -18.198 -10.946  -9.841  1.00 94.93
ATOM   2953  O   GLU A 381     -17.307 -10.195 -10.234  1.00 94.93
ATOM   2954  CB  GLU A 381     -18.109 -13.466 -10.013  1.00 94.93
ATOM   2955  CG  GLU A 381     -17.586 -14.791  -9.424  1.00 94.93
ATOM   2956  CD  GLU A 381     -17.815 -16.022 -10.323  1.00 94.93
ATOM   2957  OE1 GLU A 381     -17.431 -17.139  -9.892  1.00 94.93
ATOM   2958  OE2 GLU A 381     -18.357 -15.863 -11.440  1.00 94.93
ATOM   2959  N   LEU A 382     -19.491 -10.624  -9.967  1.00 95.08
ATOM   2960  CA  LEU A 382     -19.951  -9.386 -10.604  1.00 95.08
ATOM   2961  C   LEU A 382     -19.591  -8.147  -9.772  1.00 95.08
ATOM   2962  O   LEU A 382     -19.272  -7.099 -10.326  1.00 95.08
ATOM   2963  CB  LEU A 382     -21.471  -9.479 -10.832  1.00 95.08
ATOM   2964  CG  LEU A 382     -22.073  -8.286 -11.602  1.00 95.08
ATOM   2965  CD1 LEU A 382     -21.550  -8.213 -13.037  1.00 95.08
ATOM   2966  CD2 LEU A 382     -23.595  -8.421 -11.649  1.00 95.08
ATOM   2967  N   PHE A 383     -19.621  -8.262  -8.446  1.00 95.83
ATOM   2968  CA  PHE A 383     -19.228  -7.182  -7.550  1.00 95.83
ATOM   2969  C   PHE A 383     -17.718  -6.924  -7.597  1.00 95.83
ATOM   2970  O   PHE A 383     -17.302  -5.773  -7.687  1.00 95.83
ATOM   2971  CB  PHE A 383     -19.712  -7.492  -6.133  1.00 95.83
ATOM   2972  CG  PHE A 383     -19.371  -6.384  -5.161  1.00 95.83
ATOM   2973  CD1 PHE A 383     -18.485  -6.625  -4.097  1.00 95.83
ATOM   2974  CD2 PHE A 383     -19.904  -5.095  -5.352  1.00 95.83
ATOM   2975  CE1 PHE A 383     -18.154  -5.588  -3.210  1.00 95.83
ATOM   2976  CE2 PHE A 383     -19.555  -4.053  -4.478  1.00 95.83
ATOM   2977  CZ  PHE A 383     -18.683  -4.303  -3.406  1.00 95.83
ATOM   2978  N   THR A 384     -16.892  -7.973  -7.635  1.00 96.07
ATOM   2979  CA  THR A 384     -15.452  -7.859  -7.889  1.00 96.07
ATOM   2980  C   THR A 384     -15.203  -7.174  -9.229  1.00 96.07
ATOM   2981  O   THR A 384     -14.399  -6.247  -9.281  1.00 96.07
ATOM   2982  CB  THR A 384     -14.770  -9.238  -7.874  1.00 96.07
ATOM   2983  OG1 THR A 384     -14.924  -9.860  -6.620  1.00 96.07
ATOM   2984  CG2 THR A 384     -13.263  -9.157  -8.117  1.00 96.07
ATOM   2985  N   LEU A 385     -15.923  -7.559 -10.291  1.00 96.94
ATOM   2986  CA  LEU A 385     -15.832  -6.887 -11.590  1.00 96.94
ATOM   2987  C   LEU A 385     -16.186  -5.399 -11.479  1.00 96.94
ATOM   2988  O   LEU A 385     -15.464  -4.565 -12.010  1.00 96.94
ATOM   2989  CB  LEU A 385     -16.741  -7.595 -12.614  1.00 96.94
ATOM   2990  CG  LEU A 385     -16.655  -7.011 -14.035  1.00 96.94
ATOM   2991  CD1 LEU A 385     -15.259  -7.160 -14.644  1.00 96.94
ATOM   2992  CD2 LEU A 385     -17.657  -7.722 -14.943  1.00 96.94
ATOM   2993  N   PHE A 386     -17.260  -5.056 -10.765  1.00 95.85
ATOM   2994  CA  PHE A 386     -17.656  -3.667 -10.539  1.00 95.85
ATOM   2995  C   PHE A 386     -16.568  -2.860  -9.819  1.00 95.85
ATOM   2996  O   PHE A 386     -16.217  -1.784 -10.292  1.00 95.85
ATOM   2997  CB  PHE A 386     -18.982  -3.625  -9.768  1.00 95.85
ATOM   2998  CG  PHE A 386     -19.324  -2.246  -9.240  1.00 95.85
ATOM   2999  CD1 PHE A 386     -19.067  -1.922  -7.894  1.00 95.85
ATOM   3000  CD2 PHE A 386     -19.834  -1.265 -10.111  1.00 95.85
ATOM   3001  CE1 PHE A 386     -19.324  -0.624  -7.420  1.00 95.85
ATOM   3002  CE2 PHE A 386     -20.095   0.031  -9.635  1.00 95.85
ATOM   3003  CZ  PHE A 386     -19.840   0.352  -8.290  1.00 95.85
ATOM   3004  N   ILE A 387     -16.005  -3.375  -8.720  1.00 95.73
ATOM   3005  CA  ILE A 387     -14.944  -2.685  -7.969  1.00 95.73
ATOM   3006  C   ILE A 387     -13.701  -2.492  -8.840  1.00 95.73
ATOM   3007  O   ILE A 387     -13.158  -1.394  -8.890  1.00 95.73
ATOM   3008  CB  ILE A 387     -14.620  -3.442  -6.659  1.00 95.73
ATOM   3009  CG1 ILE A 387     -15.806  -3.433  -5.665  1.00 95.73
ATOM   3010  CG2 ILE A 387     -13.358  -2.889  -5.967  1.00 95.73
ATOM   3011  CD1 ILE A 387     -16.238  -2.050  -5.157  1.00 95.73
ATOM   3012  N   VAL A 388     -13.290  -3.529  -9.570  1.00 96.22
ATOM   3013  CA  VAL A 388     -12.120  -3.500 -10.457  1.00 96.22
ATOM   3014  C   VAL A 388     -12.331  -2.552 -11.652  1.00 96.22
ATOM   3015  O   VAL A 388     -11.412  -1.844 -12.056  1.00 96.22
ATOM   3016  CB  VAL A 388     -11.793  -4.950 -10.867  1.00 96.22
ATOM   3017  CG1 VAL A 388     -10.765  -5.044 -11.981  1.00 96.22
ATOM   3018  CG2 VAL A 388     -11.227  -5.752  -9.687  1.00 96.22
ATOM   3019  N   LEU A 389     -13.546  -2.465 -12.200  1.00 96.34
ATOM   3020  CA  LEU A 389     -13.883  -1.487 -13.242  1.00 96.34
ATOM   3021  C   LEU A 389     -13.976  -0.058 -12.691  1.00 96.34
ATOM   3022  O   LEU A 389     -13.550   0.881 -13.358  1.00 96.34
ATOM   3023  CB  LEU A 389     -15.201  -1.879 -13.929  1.00 96.34
ATOM   3024  CG  LEU A 389     -15.109  -3.102 -14.859  1.00 96.34
ATOM   3025  CD1 LEU A 389     -16.511  -3.437 -15.372  1.00 96.34
ATOM   3026  CD2 LEU A 389     -14.209  -2.853 -16.072  1.00 96.34
ATOM   3027  N   ALA A 390     -14.506   0.127 -11.481  1.00 95.92
ATOM   3028  CA  ALA A 390     -14.564   1.434 -10.837  1.00 95.92
ATOM   3029  C   ALA A 390     -13.155   1.964 -10.539  1.00 95.92
ATOM   3030  O   ALA A 390     -12.862   3.118 -10.849  1.00 95.92
ATOM   3031  CB  ALA A 390     -15.421   1.334  -9.570  1.00 95.92
ATOM   3032  N   THR A 391     -12.256   1.124 -10.013  1.00 95.67
ATOM   3033  CA  THR A 391     -10.855   1.512  -9.809  1.00 95.67
ATOM   3034  C   THR A 391     -10.169   1.810 -11.135  1.00 95.67
ATOM   3035  O   THR A 391      -9.527   2.847 -11.230  1.00 95.67
ATOM   3036  CB  THR A 391     -10.045   0.474  -9.019  1.00 95.67
ATOM   3037  OG1 THR A 391     -10.118  -0.793  -9.615  1.00 95.67
ATOM   3038  CG2 THR A 391     -10.523   0.328  -7.576  1.00 95.67
ATOM   3039  N   PHE A 392     -10.383   1.000 -12.179  1.00 96.46
ATOM   3040  CA  PHE A 392      -9.876   1.266 -13.530  1.00 96.46
ATOM   3041  C   PHE A 392     -10.272   2.652 -14.056  1.00 96.46
ATOM   3042  O   PHE A 392      -9.406   3.408 -14.492  1.00 96.46
ATOM   3043  CB  PHE A 392     -10.385   0.185 -14.494  1.00 96.46
ATOM   3044  CG  PHE A 392     -10.122   0.493 -15.957  1.00 96.46
ATOM   3045  CD1 PHE A 392     -11.173   0.897 -16.802  1.00 96.46
ATOM   3046  CD2 PHE A 392      -8.813   0.439 -16.459  1.00 96.46
ATOM   3047  CE1 PHE A 392     -10.911   1.230 -18.143  1.00 96.46
ATOM   3048  CE2 PHE A 392      -8.546   0.769 -17.798  1.00 96.46
ATOM   3049  CZ  PHE A 392      -9.598   1.162 -18.643  1.00 96.46
ATOM   3050  N   LEU A 393     -11.563   3.002 -14.003  1.00 96.47
ATOM   3051  CA  LEU A 393     -12.060   4.282 -14.519  1.00 96.47
ATOM   3052  C   LEU A 393     -11.432   5.478 -13.798  1.00 96.47
ATOM   3053  O   LEU A 393     -11.178   6.504 -14.423  1.00 96.47
ATOM   3054  CB  LEU A 393     -13.592   4.336 -14.385  1.00 96.47
ATOM   3055  CG  LEU A 393     -14.360   3.417 -15.350  1.00 96.47
ATOM   3056  CD1 LEU A 393     -15.851   3.465 -15.008  1.00 96.47
ATOM   3057  CD2 LEU A 393     -14.187   3.824 -16.814  1.00 96.47
ATOM   3058  N   LEU A 394     -11.156   5.348 -12.501  1.00 94.50
ATOM   3059  CA  LEU A 394     -10.534   6.407 -11.708  1.00 94.50
ATOM   3060  C   LEU A 394      -9.007   6.429 -11.890  1.00 94.50
ATOM   3061  O   LEU A 394      -8.414   7.504 -11.962  1.00 94.50
ATOM   3062  CB  LEU A 394     -10.993   6.261 -10.248  1.00 94.50
ATOM   3063  CG  LEU A 394     -12.355   6.942  -9.988  1.00 94.50
ATOM   3064  CD1 LEU A 394     -13.519   6.496 -10.876  1.00 94.50
ATOM   3065  CD2 LEU A 394     -12.801   6.706  -8.554  1.00 94.50
ATOM   3066  N   SER A 395      -8.375   5.270 -12.088  1.00 96.77
ATOM   3067  CA  SER A 395      -6.973   5.160 -12.504  1.00 96.77
ATOM   3068  C   SER A 395      -6.698   5.849 -13.848  1.00 96.77
ATOM   3069  O   SER A 395      -5.565   6.270 -14.082  1.00 96.77
ATOM   3070  CB  SER A 395      -6.563   3.688 -12.633  1.00 96.77
ATOM   3071  OG  SER A 395      -6.596   2.993 -11.408  1.00 96.77
ATOM   3072  N   LEU A 396      -7.705   6.026 -14.720  1.00 96.93
ATOM   3073  CA  LEU A 396      -7.529   6.716 -16.006  1.00 96.93
ATOM   3074  C   LEU A 396      -7.017   8.157 -15.854  1.00 96.93
ATOM   3075  O   LEU A 396      -6.251   8.614 -16.699  1.00 96.93
ATOM   3076  CB  LEU A 396      -8.810   6.702 -16.855  1.00 96.93
ATOM   3077  CG  LEU A 396      -9.203   5.327 -17.421  1.00 96.93
ATOM   3078  CD1 LEU A 396     -10.514   5.454 -18.198  1.00 96.93
ATOM   3079  CD2 LEU A 396      -8.147   4.750 -18.370  1.00 96.93
ATOM   3080  N   PHE A 397      -7.369   8.852 -14.766  1.00 95.57
ATOM   3081  CA  PHE A 397      -6.860  10.201 -14.483  1.00 95.57
ATOM   3082  C   PHE A 397      -5.355  10.228 -14.183  1.00 95.57
ATOM   3083  O   PHE A 397      -4.717  11.262 -14.344  1.00 95.57
ATOM   3084  CB  PHE A 397      -7.640  10.811 -13.311  1.00 95.57
ATOM   3085  CG  PHE A 397      -9.092  11.108 -13.627  1.00 95.57
ATOM   3086  CD1 PHE A 397      -9.420  12.236 -14.401  1.00 95.57
ATOM   3087  CD2 PHE A 397     -10.115  10.267 -13.152  1.00 95.57
ATOM   3088  CE1 PHE A 397     -10.764  12.518 -14.701  1.00 95.57
ATOM   3089  CE2 PHE A 397     -11.458  10.544 -13.457  1.00 95.57
ATOM   3090  CZ  PHE A 397     -11.783  11.672 -14.231  1.00 95.57
ATOM   3091  N   CYS A 398      -4.777   9.098 -13.772  1.00 96.28
ATOM   3092  CA  CYS A 398      -3.358   8.971 -13.446  1.00 96.28
ATOM   3093  C   CYS A 398      -2.500   8.475 -14.629  1.00 96.28
ATOM   3094  O   CYS A 398      -1.277   8.486 -14.528  1.00 96.28
ATOM   3095  CB  CYS A 398      -3.235   8.031 -12.248  1.00 96.28
ATOM   3096  SG  CYS A 398      -3.982   8.729 -10.749  1.00 96.28
ATOM   3097  N   VAL A 399      -3.108   8.051 -15.748  1.00 96.93
ATOM   3098  CA  VAL A 399      -2.395   7.605 -16.973  1.00 96.93
ATOM   3099  C   VAL A 399      -2.461   8.625 -18.119  1.00 96.93
ATOM   3100  O   VAL A 399      -2.144   8.302 -19.267  1.00 96.93
ATOM   3101  CB  VAL A 399      -2.834   6.204 -17.454  1.00 96.93
ATOM   3102  CG1 VAL A 399      -2.650   5.137 -16.375  1.00 96.93
ATOM   3103  CG2 VAL A 399      -4.290   6.177 -17.903  1.00 96.93
ATOM   3104  N   THR A 400      -2.911   9.848 -17.843  1.00 97.48
ATOM   3105  CA  THR A 400      -2.850  10.974 -18.786  1.00 97.48
ATOM   3106  C   THR A 400      -1.447  11.594 -18.821  1.00 97.48
ATOM   3107  O   THR A 400      -0.588  11.231 -18.019  1.00 97.48
ATOM   3108  CB  THR A 400      -3.901  12.035 -18.438  1.00 97.48
ATOM   3109  OG1 THR A 400      -3.540  12.670 -17.240  1.00 97.48
ATOM   3110  CG2 THR A 400      -5.315  11.495 -18.248  1.00 97.48
ATOM   3111  N   ASN A 401      -1.211  12.554 -19.723  1.00 96.27
ATOM   3112  CA  ASN A 401       0.068  13.276 -19.817  1.00 96.27
ATOM   3113  C   ASN A 401       0.451  13.958 -18.490  1.00 96.27
ATOM   3114  O   ASN A 401       1.586  13.854 -18.035  1.00 96.27
ATOM   3115  CB  ASN A 401      -0.022  14.335 -20.931  1.00 96.27
ATOM   3116  CG  ASN A 401      -0.115  13.767 -22.328  1.00 96.27
ATOM   3117  OD1 ASN A 401       0.030  12.585 -22.572  1.00 96.27
ATOM   3118  ND2 ASN A 401      -0.355  14.609 -23.308  1.00 96.27
ATOM   3119  N   GLY A 402      -0.516  14.621 -17.851  1.00 95.30
ATOM   3120  CA  GLY A 402      -0.381  15.226 -16.520  1.00 95.30
ATOM   3121  C   GLY A 402      -0.729  14.275 -15.369  1.00 95.30
ATOM   3122  O   GLY A 402      -0.848  14.707 -14.222  1.00 95.30
ATOM   3123  N   GLY A 403      -0.915  12.981 -15.643  1.00 96.09
ATOM   3124  CA  GLY A 403      -1.411  12.002 -14.674  1.00 96.09
ATOM   3125  C   GLY A 403      -0.481  11.793 -13.478  1.00 96.09
ATOM   3126  O   GLY A 403      -0.950  11.492 -12.382  1.00 96.09
ATOM   3127  N   ILE A 404       0.823  12.046 -13.644  1.00 94.78
ATOM   3128  CA  ILE A 404       1.804  12.002 -12.550  1.00 94.78
ATOM   3129  C   ILE A 404       1.516  13.043 -11.457  1.00 94.78
ATOM   3130  O   ILE A 404       1.786  12.794 -10.281  1.00 94.78
ATOM   3131  CB  ILE A 404       3.234  12.148 -13.111  1.00 94.78
ATOM   3132  CG1 ILE A 404       4.337  11.816 -12.088  1.00 94.78
ATOM   3133  CG2 ILE A 404       3.498  13.560 -13.659  1.00 94.78
ATOM   3134  CD1 ILE A 404       4.285  10.387 -11.539  1.00 94.78
ATOM   3135  N   TYR A 405       0.916  14.187 -11.805  1.00 95.20
ATOM   3136  CA  TYR A 405       0.522  15.195 -10.822  1.00 95.20
ATOM   3137  C   TYR A 405      -0.675  14.716  -9.996  1.00 95.20
ATOM   3138  O   TYR A 405      -0.668  14.850  -8.774  1.00 95.20
ATOM   3139  CB  TYR A 405       0.221  16.531 -11.512  1.00 95.20
ATOM   3140  CG  TYR A 405       1.369  17.089 -12.330  1.00 95.20
ATOM   3141  CD1 TYR A 405       2.586  17.409 -11.697  1.00 95.20
ATOM   3142  CD2 TYR A 405       1.224  17.293 -13.716  1.00 95.20
ATOM   3143  CE1 TYR A 405       3.655  17.935 -12.446  1.00 95.20
ATOM   3144  CE2 TYR A 405       2.292  17.818 -14.468  1.00 95.20
ATOM   3145  CZ  TYR A 405       3.504  18.155 -13.831  1.00 95.20
ATOM   3146  OH  TYR A 405       4.525  18.687 -14.549  1.00 95.20
ATOM   3147  N   VAL A 406      -1.663  14.083 -10.640  1.00 95.33
ATOM   3148  CA  VAL A 406      -2.808  13.455  -9.955  1.00 95.33
ATOM   3149  C   VAL A 406      -2.331  12.328  -9.040  1.00 95.33
ATOM   3150  O   VAL A 406      -2.716  12.281  -7.874  1.00 95.33
ATOM   3151  CB  VAL A 406      -3.845  12.913 -10.959  1.00 95.33
ATOM   3152  CG1 VAL A 406      -5.072  12.337 -10.240  1.00 95.33
ATOM   3153  CG2 VAL A 406      -4.330  14.015 -11.906  1.00 95.33
ATOM   3154  N   PHE A 407      -1.438  11.471  -9.541  1.00 94.28
ATOM   3155  CA  PHE A 407      -0.780  10.420  -8.767  1.00 94.28
ATOM   3156  C   PHE A 407      -0.110  10.988  -7.509  1.00 94.28
ATOM   3157  O   PHE A 407      -0.379  10.528  -6.403  1.00 94.28
ATOM   3158  CB  PHE A 407       0.245   9.719  -9.674  1.00 94.28
ATOM   3159  CG  PHE A 407       1.123   8.720  -8.953  1.00 94.28
ATOM   3160  CD1 PHE A 407       2.276   9.143  -8.260  1.00 94.28
ATOM   3161  CD2 PHE A 407       0.765   7.364  -8.945  1.00 94.28
ATOM   3162  CE1 PHE A 407       3.021   8.225  -7.502  1.00 94.28
ATOM   3163  CE2 PHE A 407       1.512   6.449  -8.191  1.00 94.28
ATOM   3164  CZ  PHE A 407       2.631   6.878  -7.456  1.00 94.28
ATOM   3165  N   THR A 408       0.717  12.025  -7.673  1.00 92.43
ATOM   3166  CA  THR A 408       1.479  12.638  -6.573  1.00 92.43
ATOM   3167  C   THR A 408       0.551  13.266  -5.531  1.00 92.43
ATOM   3168  O   THR A 408       0.797  13.148  -4.331  1.00 92.43
ATOM   3169  CB  THR A 408       2.448  13.695  -7.126  1.00 92.43
ATOM   3170  OG1 THR A 408       3.329  13.123  -8.067  1.00 92.43
ATOM   3171  CG2 THR A 408       3.320  14.339  -6.049  1.00 92.43
ATOM   3172  N   LEU A 409      -0.546  13.895  -5.967  1.00 92.88
ATOM   3173  CA  LEU A 409      -1.558  14.453  -5.070  1.00 92.88
ATOM   3174  C   LEU A 409      -2.252  13.351  -4.250  1.00 92.88
ATOM   3175  O   LEU A 409      -2.398  13.482  -3.034  1.00 92.88
ATOM   3176  CB  LEU A 409      -2.572  15.256  -5.911  1.00 92.88
ATOM   3177  CG  LEU A 409      -3.549  16.089  -5.062  1.00 92.88
ATOM   3178  CD1 LEU A 409      -2.860  17.336  -4.510  1.00 92.88
ATOM   3179  CD2 LEU A 409      -4.748  16.539  -5.896  1.00 92.88
ATOM   3180  N   LEU A 410      -2.666  12.259  -4.899  1.00 92.08
ATOM   3181  CA  LEU A 410      -3.345  11.145  -4.235  1.00 92.08
ATOM   3182  C   LEU A 410      -2.427  10.414  -3.248  1.00 92.08
ATOM   3183  O   LEU A 410      -2.842  10.171  -2.117  1.00 92.08
ATOM   3184  CB  LEU A 410      -3.896  10.165  -5.284  1.00 92.08
ATOM   3185  CG  LEU A 410      -5.090  10.685  -6.103  1.00 92.08
ATOM   3186  CD1 LEU A 410      -5.419   9.678  -7.205  1.00 92.08
ATOM   3187  CD2 LEU A 410      -6.340  10.870  -5.240  1.00 92.08
ATOM   3188  N   ASP A 411      -1.189  10.107  -3.635  1.00 88.15
ATOM   3189  CA  ASP A 411      -0.222   9.428  -2.762  1.00 88.15
ATOM   3190  C   ASP A 411       0.054  10.244  -1.488  1.00 88.15
ATOM   3191  O   ASP A 411      -0.014   9.728  -0.368  1.00 88.15
ATOM   3192  CB  ASP A 411       1.065   9.162  -3.558  1.00 88.15
ATOM   3193  CG  ASP A 411       2.094   8.376  -2.736  1.00 88.15
ATOM   3194  OD1 ASP A 411       1.744   7.272  -2.259  1.00 88.15
ATOM   3195  OD2 ASP A 411       3.230   8.879  -2.588  1.00 88.15
ATOM   3196  N   HIS A 412       0.252  11.557  -1.643  1.00 87.64
ATOM   3197  CA  HIS A 412       0.543  12.449  -0.526  1.00 87.64
ATOM   3198  C   HIS A 412      -0.632  12.582   0.460  1.00 87.64
ATOM   3199  O   HIS A 412      -0.455  12.408   1.668  1.00 87.64
ATOM   3200  CB  HIS A 412       0.971  13.809  -1.092  1.00 87.64
ATOM   3201  CG  HIS A 412       1.532  14.721  -0.037  1.00 87.64
ATOM   3202  ND1 HIS A 412       2.825  14.700   0.432  1.00 87.64
ATOM   3203  CD2 HIS A 412       0.864  15.698   0.649  1.00 87.64
ATOM   3204  CE1 HIS A 412       2.937  15.650   1.375  1.00 87.64
ATOM   3205  NE2 HIS A 412       1.766  16.280   1.542  1.00 87.64
ATOM   3206  N   PHE A 413      -1.839  12.876  -0.036  1.00 87.88
ATOM   3207  CA  PHE A 413      -2.990  13.206   0.814  1.00 87.88
ATOM   3208  C   PHE A 413      -3.867  12.000   1.172  1.00 87.88
ATOM   3209  O   PHE A 413      -4.271  11.829   2.327  1.00 87.88
ATOM   3210  CB  PHE A 413      -3.838  14.267   0.106  1.00 87.88
ATOM   3211  CG  PHE A 413      -3.251  15.662   0.119  1.00 87.88
ATOM   3212  CD1 PHE A 413      -3.425  16.472   1.255  1.00 87.88
ATOM   3213  CD2 PHE A 413      -2.588  16.179  -1.010  1.00 87.88
ATOM   3214  CE1 PHE A 413      -2.980  17.801   1.238  1.00 87.88
ATOM   3215  CE2 PHE A 413      -2.156  17.516  -1.026  1.00 87.88
ATOM   3216  CZ  PHE A 413      -2.381  18.334   0.086  1.00 87.88
ATOM   3217  N   ALA A 414      -4.202  11.171   0.183  1.00 84.35
ATOM   3218  CA  ALA A 414      -5.169  10.094   0.358  1.00 84.35
ATOM   3219  C   ALA A 414      -4.575   8.921   1.142  1.00 84.35
ATOM   3220  O   ALA A 414      -5.277   8.313   1.946  1.00 84.35
ATOM   3221  CB  ALA A 414      -5.696   9.654  -1.012  1.00 84.35
ATOM   3222  N   ALA A 415      -3.286   8.633   0.948  1.00 77.22
ATOM   3223  CA  ALA A 415      -2.604   7.564   1.659  1.00 77.22
ATOM   3224  C   ALA A 415      -1.924   8.087   2.939  1.00 77.22
ATOM   3225  O   ALA A 415      -2.276   7.659   4.035  1.00 77.22
ATOM   3226  CB  ALA A 415      -1.680   6.847   0.671  1.00 77.22
ATOM   3227  N   GLY A 416      -1.006   9.055   2.826  1.00 77.55
ATOM   3228  CA  GLY A 416      -0.113   9.486   3.916  1.00 77.55
ATOM   3229  C   GLY A 416      -0.802   9.777   5.257  1.00 77.55
ATOM   3230  O   GLY A 416      -0.703   9.001   6.210  1.00 77.55
ATOM   3231  N   THR A 417      -1.497  10.911   5.345  1.00 81.89
ATOM   3232  CA  THR A 417      -2.118  11.387   6.596  1.00 81.89
ATOM   3233  C   THR A 417      -3.345  10.562   6.995  1.00 81.89
ATOM   3234  O   THR A 417      -3.567  10.305   8.181  1.00 81.89
ATOM   3235  CB  THR A 417      -2.507  12.866   6.447  1.00 81.89
ATOM   3236  OG1 THR A 417      -1.396  13.605   6.001  1.00 81.89
ATOM   3237  CG2 THR A 417      -2.975  13.515   7.748  1.00 81.89
ATOM   3238  N   SER A 418      -4.132  10.117   6.013  1.00 86.93
ATOM   3239  CA  SER A 418      -5.394   9.407   6.254  1.00 86.93
ATOM   3240  C   SER A 418      -5.180   8.034   6.901  1.00 86.93
ATOM   3241  O   SER A 418      -5.921   7.674   7.817  1.00 86.93
ATOM   3242  CB  SER A 418      -6.175   9.241   4.949  1.00 86.93
ATOM   3243  OG  SER A 418      -6.391  10.493   4.318  1.00 86.93
ATOM   3244  N   ILE A 419      -4.140   7.291   6.491  1.00 88.04
ATOM   3245  CA  ILE A 419      -3.799   5.982   7.078  1.00 88.04
ATOM   3246  C   ILE A 419      -3.433   6.133   8.550  1.00 88.04
ATOM   3247  O   ILE A 419      -3.982   5.431   9.395  1.00 88.04
ATOM   3248  CB  ILE A 419      -2.655   5.301   6.290  1.00 88.04
ATOM   3249  CG1 ILE A 419      -3.186   4.831   4.924  1.00 88.04
ATOM   3250  CG2 ILE A 419      -2.069   4.088   7.045  1.00 88.04
ATOM   3251  CD1 ILE A 419      -2.085   4.522   3.914  1.00 88.04
ATOM   3252  N   LEU A 420      -2.544   7.074   8.881  1.00 87.25
ATOM   3253  CA  LEU A 420      -2.089   7.275  10.259  1.00 87.25
ATOM   3254  C   LEU A 420      -3.255   7.609  11.201  1.00 87.25
ATOM   3255  O   LEU A 420      -3.316   7.097  12.320  1.00 87.25
ATOM   3256  CB  LEU A 420      -1.037   8.393  10.281  1.00 87.25
ATOM   3257  CG  LEU A 420       0.266   8.070   9.530  1.00 87.25
ATOM   3258  CD1 LEU A 420       1.121   9.333   9.491  1.00 87.25
ATOM   3259  CD2 LEU A 420       1.055   6.950  10.215  1.00 87.25
ATOM   3260  N   PHE A 421      -4.209   8.415  10.728  1.00 90.13
ATOM   3261  CA  PHE A 421      -5.454   8.671  11.446  1.00 90.13
ATOM   3262  C   PHE A 421      -6.304   7.404  11.608  1.00 90.13
ATOM   3263  O   PHE A 421      -6.744   7.111  12.719  1.00 90.13
ATOM   3264  CB  PHE A 421      -6.236   9.768  10.720  1.00 90.13
ATOM   3265  CG  PHE A 421      -7.613  10.007  11.309  1.00 90.13
ATOM   3266  CD1 PHE A 421      -8.738   9.357  10.764  1.00 90.13
ATOM   3267  CD2 PHE A 421      -7.767  10.856  12.419  1.00 90.13
ATOM   3268  CE1 PHE A 421     -10.014   9.574  11.312  1.00 90.13
ATOM   3269  CE2 PHE A 421      -9.044  11.075  12.966  1.00 90.13
ATOM   3270  CZ  PHE A 421     -10.167  10.439  12.409  1.00 90.13
ATOM   3271  N   GLY A 422      -6.515   6.639  10.532  1.00 92.34
ATOM   3272  CA  GLY A 422      -7.285   5.391  10.565  1.00 92.34
ATOM   3273  C   GLY A 422      -6.739   4.400  11.596  1.00 92.34
ATOM   3274  O   GLY A 422      -7.484   3.946  12.464  1.00 92.34
ATOM   3275  N   VAL A 423      -5.425   4.162  11.575  1.00 93.15
ATOM   3276  CA  VAL A 423      -4.730   3.271  12.520  1.00 93.15
ATOM   3277  C   VAL A 423      -4.852   3.766  13.964  1.00 93.15
ATOM   3278  O   VAL A 423      -5.055   2.970  14.881  1.00 93.15
ATOM   3279  CB  VAL A 423      -3.240   3.140  12.145  1.00 93.15
ATOM   3280  CG1 VAL A 423      -2.508   2.182  13.086  1.00 93.15
ATOM   3281  CG2 VAL A 423      -3.036   2.549  10.753  1.00 93.15
ATOM   3282  N   LEU A 424      -4.746   5.079  14.192  1.00 94.76
ATOM   3283  CA  LEU A 424      -4.889   5.665  15.526  1.00 94.76
ATOM   3284  C   LEU A 424      -6.281   5.402  16.109  1.00 94.76
ATOM   3285  O   LEU A 424      -6.394   4.935  17.246  1.00 94.76
ATOM   3286  CB  LEU A 424      -4.587   7.172  15.446  1.00 94.76
ATOM   3287  CG  LEU A 424      -4.856   7.945  16.750  1.00 94.76
ATOM   3288  CD1 LEU A 424      -3.974   7.465  17.903  1.00 94.76
ATOM   3289  CD2 LEU A 424      -4.598   9.430  16.515  1.00 94.76
ATOM   3290  N   ILE A 425      -7.339   5.698  15.349  1.00 96.27
ATOM   3291  CA  ILE A 425      -8.710   5.492  15.826  1.00 96.27
ATOM   3292  C   ILE A 425      -9.010   4.000  15.973  1.00 96.27
ATOM   3293  O   ILE A 425      -9.684   3.618  16.929  1.00 96.27
ATOM   3294  CB  ILE A 425      -9.747   6.196  14.928  1.00 96.27
ATOM   3295  CG1 ILE A 425      -9.485   7.709  14.751  1.00 96.27
ATOM   3296  CG2 ILE A 425     -11.159   6.011  15.514  1.00 96.27
ATOM   3297  CD1 ILE A 425      -9.400   8.532  16.045  1.00 96.27
ATOM   3298  N   GLU A 426      -8.472   3.151  15.099  1.00 96.40
ATOM   3299  CA  GLU A 426      -8.588   1.704  15.237  1.00 96.40
ATOM   3300  C   GLU A 426      -7.984   1.210  16.559  1.00 96.40
ATOM   3301  O   GLU A 426      -8.665   0.547  17.348  1.00 96.40
ATOM   3302  CB  GLU A 426      -7.959   1.007  14.028  1.00 96.40
ATOM   3303  CG  GLU A 426      -8.150  -0.505  14.168  1.00 96.40
ATOM   3304  CD  GLU A 426      -7.647  -1.302  12.972  1.00 96.40
ATOM   3305  OE1 GLU A 426      -7.459  -2.513  13.209  1.00 96.40
ATOM   3306  OE2 GLU A 426      -7.527  -0.727  11.868  1.00 96.40
ATOM   3307  N   ALA A 427      -6.740   1.601  16.849  1.00 96.60
ATOM   3308  CA  ALA A 427      -6.051   1.233  18.080  1.00 96.60
ATOM   3309  C   ALA A 427      -6.807   1.722  19.325  1.00 96.60
ATOM   3310  O   ALA A 427      -6.991   0.965  20.280  1.00 96.60
ATOM   3311  CB  ALA A 427      -4.624   1.790  18.019  1.00 96.60
ATOM   3312  N   ILE A 428      -7.314   2.960  19.310  1.00 96.69
ATOM   3313  CA  ILE A 428      -8.151   3.497  20.393  1.00 96.69
ATOM   3314  C   ILE A 428      -9.457   2.698  20.520  1.00 96.69
ATOM   3315  O   ILE A 428      -9.858   2.331  21.627  1.00 96.69
ATOM   3316  CB  ILE A 428      -8.406   5.008  20.177  1.00 96.69
ATOM   3317  CG1 ILE A 428      -7.092   5.802  20.363  1.00 96.69
ATOM   3318  CG2 ILE A 428      -9.478   5.536  21.152  1.00 96.69
ATOM   3319  CD1 ILE A 428      -7.183   7.267  19.914  1.00 96.69
ATOM   3320  N   GLY A 429     -10.120   2.395  19.406  1.00 97.08
ATOM   3321  CA  GLY A 429     -11.382   1.664  19.373  1.00 97.08
ATOM   3322  C   GLY A 429     -11.273   0.264  19.969  1.00 97.08
ATOM   3323  O   GLY A 429     -12.060  -0.103  20.845  1.00 97.08
ATOM   3324  N   VAL A 430     -10.261  -0.500  19.561  1.00 97.48
ATOM   3325  CA  VAL A 430     -10.031  -1.858  20.069  1.00 97.48
ATOM   3326  C   VAL A 430      -9.519  -1.823  21.512  1.00 97.48
ATOM   3327  O   VAL A 430     -10.037  -2.529  22.379  1.00 97.48
ATOM   3328  CB  VAL A 430      -9.062  -2.625  19.149  1.00 97.48
ATOM   3329  CG1 VAL A 430      -8.802  -4.046  19.670  1.00 97.48
ATOM   3330  CG2 VAL A 430      -9.621  -2.755  17.727  1.00 97.48
ATOM   3331  N   ALA A 431      -8.523  -0.988  21.817  1.00 96.20
ATOM   3332  CA  ALA A 431      -7.857  -1.045  23.114  1.00 96.20
ATOM   3333  C   ALA A 431      -8.644  -0.372  24.249  1.00 96.20
ATOM   3334  O   ALA A 431      -8.616  -0.866  25.379  1.00 96.20
ATOM   3335  CB  ALA A 431      -6.451  -0.464  22.977  1.00 96.20
ATOM   3336  N   TRP A 432      -9.351   0.728  23.972  1.00 96.10
ATOM   3337  CA  TRP A 432     -10.043   1.523  24.992  1.00 96.10
ATOM   3338  C   TRP A 432     -11.556   1.293  25.004  1.00 96.10
ATOM   3339  O   TRP A 432     -12.110   1.009  26.066  1.00 96.10
ATOM   3340  CB  TRP A 432      -9.681   3.007  24.842  1.00 96.10
ATOM   3341  CG  TRP A 432      -8.281   3.370  25.202  1.00 96.10
ATOM   3342  CD1 TRP A 432      -7.188   3.210  24.425  1.00 96.10
ATOM   3343  CD2 TRP A 432      -7.804   3.945  26.456  1.00 96.10
ATOM   3344  NE1 TRP A 432      -6.074   3.635  25.120  1.00 96.10
ATOM   3345  CE2 TRP A 432      -6.392   4.074  26.384  1.00 96.10
ATOM   3346  CE3 TRP A 432      -8.417   4.394  27.644  1.00 96.10
ATOM   3347  CZ2 TRP A 432      -5.630   4.574  27.447  1.00 96.10
ATOM   3348  CZ3 TRP A 432      -7.665   4.863  28.737  1.00 96.10
ATOM   3349  CH2 TRP A 432      -6.267   4.951  28.641  1.00 96.10
ATOM   3350  N   PHE A 433     -12.234   1.366  23.853  1.00 96.01
ATOM   3351  CA  PHE A 433     -13.693   1.185  23.812  1.00 96.01
ATOM   3352  C   PHE A 433     -14.089  -0.282  23.986  1.00 96.01
ATOM   3353  O   PHE A 433     -14.834  -0.608  24.914  1.00 96.01
ATOM   3354  CB  PHE A 433     -14.300   1.778  22.536  1.00 96.01
ATOM   3355  CG  PHE A 433     -14.341   3.288  22.519  1.00 96.01
ATOM   3356  CD1 PHE A 433     -15.509   3.953  22.935  1.00 96.01
ATOM   3357  CD2 PHE A 433     -13.226   4.031  22.087  1.00 96.01
ATOM   3358  CE1 PHE A 433     -15.567   5.356  22.914  1.00 96.01
ATOM   3359  CE2 PHE A 433     -13.288   5.435  22.059  1.00 96.01
ATOM   3360  CZ  PHE A 433     -14.456   6.096  22.473  1.00 96.01
ATOM   3361  N   TYR A 434     -13.548  -1.176  23.154  1.00 96.31
ATOM   3362  CA  TYR A 434     -13.775  -2.613  23.314  1.00 96.31
ATOM   3363  C   TYR A 434     -13.044  -3.176  24.541  1.00 96.31
ATOM   3364  O   TYR A 434     -13.595  -3.981  25.293  1.00 96.31
ATOM   3365  CB  TYR A 434     -13.375  -3.346  22.030  1.00 96.31
ATOM   3366  CG  TYR A 434     -13.718  -4.817  22.073  1.00 96.31
ATOM   3367  CD1 TYR A 434     -12.734  -5.808  21.903  1.00 96.31
ATOM   3368  CD2 TYR A 434     -15.056  -5.181  22.279  1.00 96.31
ATOM   3369  CE1 TYR A 434     -13.107  -7.167  21.913  1.00 96.31
ATOM   3370  CE2 TYR A 434     -15.436  -6.531  22.279  1.00 96.31
ATOM   3371  CZ  TYR A 434     -14.464  -7.523  22.085  1.00 96.31
ATOM   3372  OH  TYR A 434     -14.863  -8.818  22.083  1.00 96.31
ATOM   3373  N   GLY A 435     -11.839  -2.667  24.800  1.00 95.80
ATOM   3374  CA  GLY A 435     -11.066  -2.934  26.005  1.00 95.80
ATOM   3375  C   GLY A 435     -10.079  -4.085  25.829  1.00 95.80
ATOM   3376  O   GLY A 435     -10.462  -5.226  25.559  1.00 95.80
ATOM   3377  N   VAL A 436      -8.797  -3.820  26.106  1.00 95.86
ATOM   3378  CA  VAL A 436      -7.710  -4.817  26.011  1.00 95.86
ATOM   3379  C   VAL A 436      -7.985  -6.085  26.821  1.00 95.86
ATOM   3380  O   VAL A 436      -7.598  -7.178  26.410  1.00 95.86
ATOM   3381  CB  VAL A 436      -6.365  -4.207  26.454  1.00 95.86
ATOM   3382  CG1 VAL A 436      -5.228  -5.227  26.408  1.00 95.86
ATOM   3383  CG2 VAL A 436      -5.967  -3.059  25.526  1.00 95.86
ATOM   3384  N   GLY A 437      -8.687  -5.969  27.951  1.00 94.20
ATOM   3385  CA  GLY A 437      -9.078  -7.123  28.754  1.00 94.20
ATOM   3386  C   GLY A 437      -9.985  -8.097  27.997  1.00 94.20
ATOM   3387  O   GLY A 437      -9.706  -9.289  28.008  1.00 94.20
ATOM   3388  N   GLN A 438     -11.033  -7.596  27.334  1.00 94.36
ATOM   3389  CA  GLN A 438     -11.953  -8.429  26.553  1.00 94.36
ATOM   3390  C   GLN A 438     -11.255  -8.975  25.305  1.00 94.36
ATOM   3391  O   GLN A 438     -11.344 -10.164  25.020  1.00 94.36
ATOM   3392  CB  GLN A 438     -13.194  -7.598  26.182  1.00 94.36
ATOM   3393  CG  GLN A 438     -14.231  -8.401  25.383  1.00 94.36
ATOM   3394  CD  GLN A 438     -14.817  -9.582  26.150  1.00 94.36
ATOM   3395  OE1 GLN A 438     -15.213  -9.476  27.306  1.00 94.36
ATOM   3396  NE2 GLN A 438     -14.900 -10.750  25.546  1.00 94.36
ATOM   3397  N   PHE A 439     -10.488  -8.133  24.616  1.00 97.22
ATOM   3398  CA  PHE A 439      -9.731  -8.547  23.438  1.00 97.22
ATOM   3399  C   PHE A 439      -8.689  -9.638  23.751  1.00 97.22
ATOM   3400  O   PHE A 439      -8.494 -10.577  22.985  1.00 97.22
ATOM   3401  CB  PHE A 439      -9.075  -7.294  22.853  1.00 97.22
ATOM   3402  CG  PHE A 439      -8.469  -7.523  21.491  1.00 97.22
ATOM   3403  CD1 PHE A 439      -7.083  -7.377  21.293  1.00 97.22
ATOM   3404  CD2 PHE A 439      -9.301  -7.885  20.415  1.00 97.22
ATOM   3405  CE1 PHE A 439      -6.535  -7.580  20.017  1.00 97.22
ATOM   3406  CE2 PHE A 439      -8.750  -8.095  19.143  1.00 97.22
ATOM   3407  CZ  PHE A 439      -7.370  -7.936  18.944  1.00 97.22
ATOM   3408  N   SER A 440      -8.053  -9.572  24.923  1.00 97.45
ATOM   3409  CA  SER A 440      -7.131 -10.614  25.395  1.00 97.45
ATOM   3410  C   SER A 440      -7.828 -11.950  25.661  1.00 97.45
ATOM   3411  O   SER A 440      -7.220 -13.003  25.459  1.00 97.45
ATOM   3412  CB  SER A 440      -6.456 -10.177  26.695  1.00 97.45
ATOM   3413  OG  SER A 440      -5.645  -9.040  26.490  1.00 97.45
ATOM   3414  N   ASP A 441      -9.076 -11.907  26.128  1.00 96.82
ATOM   3415  CA  ASP A 441      -9.899 -13.092  26.381  1.00 96.82
ATOM   3416  C   ASP A 441     -10.319 -13.742  25.054  1.00 96.82
ATOM   3417  O   ASP A 441     -10.214 -14.959  24.902  1.00 96.82
ATOM   3418  CB  ASP A 441     -11.116 -12.719  27.261  1.00 96.82
ATOM   3419  CG  ASP A 441     -10.747 -12.195  28.661  1.00 96.82
ATOM   3420  OD1 ASP A 441      -9.568 -12.303  29.065  1.00 96.82
ATOM   3421  OD2 ASP A 441     -11.628 -11.760  29.434  1.00 96.82
ATOM   3422  N   ASP A 442     -10.675 -12.927  24.059  1.00 97.33
ATOM   3423  CA  ASP A 442     -10.981 -13.371  22.696  1.00 97.33
ATOM   3424  C   ASP A 442      -9.765 -14.060  22.037  1.00 97.33
ATOM   3425  O   ASP A 442      -9.876 -15.141  21.452  1.00 97.33
ATOM   3426  CB  ASP A 442     -11.411 -12.155  21.866  1.00 97.33
ATOM   3427  CG  ASP A 442     -12.696 -11.434  22.303  1.00 97.33
ATOM   3428  OD1 ASP A 442     -13.505 -11.893  23.149  1.00 97.33
ATOM   3429  OD2 ASP A 442     -12.893 -10.325  21.768  1.00 97.33
ATOM   3430  N   ILE A 443      -8.562 -13.492  22.196  1.00 97.92
ATOM   3431  CA  ILE A 443      -7.306 -14.105  21.729  1.00 97.92
ATOM   3432  C   ILE A 443      -7.025 -15.433  22.438  1.00 97.92
ATOM   3433  O   ILE A 443      -6.600 -16.399  21.793  1.00 97.92
ATOM   3434  CB  ILE A 443      -6.133 -13.115  21.896  1.00 97.92
ATOM   3435  CG1 ILE A 443      -6.256 -12.000  20.838  1.00 97.92
ATOM   3436  CG2 ILE A 443      -4.766 -13.815  21.757  1.00 97.92
ATOM   3437  CD1 ILE A 443      -5.268 -10.845  21.025  1.00 97.92
ATOM   3438  N   GLN A 444      -7.267 -15.506  23.749  1.00 97.61
ATOM   3439  CA  GLN A 444      -7.119 -16.748  24.505  1.00 97.61
ATOM   3440  C   GLN A 444      -8.092 -17.821  24.012  1.00 97.61
ATOM   3441  O   GLN A 444      -7.713 -18.988  23.942  1.00 97.61
ATOM   3442  CB  GLN A 444      -7.319 -16.469  25.998  1.00 97.61
ATOM   3443  CG  GLN A 444      -7.059 -17.716  26.858  1.00 97.61
ATOM   3444  CD  GLN A 444      -7.255 -17.487  28.352  1.00 97.61
ATOM   3445  OE1 GLN A 444      -7.866 -16.538  28.826  1.00 97.61
ATOM   3446  NE2 GLN A 444      -6.701 -18.348  29.176  1.00 97.61
ATOM   3447  N   GLN A 445      -9.311 -17.443  23.631  1.00 97.27
ATOM   3448  CA  GLN A 445     -10.292 -18.366  23.067  1.00 97.27
ATOM   3449  C   GLN A 445      -9.832 -18.944  21.717  1.00 97.27
ATOM   3450  O   GLN A 445     -10.055 -20.124  21.455  1.00 97.27
ATOM   3451  CB  GLN A 445     -11.635 -17.632  22.948  1.00 97.27
ATOM   3452  CG  GLN A 445     -12.786 -18.582  22.592  1.00 97.27
ATOM   3453  CD  GLN A 445     -14.103 -17.849  22.367  1.00 97.27
ATOM   3454  OE1 GLN A 445     -14.319 -16.726  22.782  1.00 97.27
ATOM   3455  NE2 GLN A 445     -15.049 -18.461  21.690  1.00 97.27
ATOM   3456  N   MET A 446      -9.167 -18.148  20.874  1.00 96.63
ATOM   3457  CA  MET A 446      -8.642 -18.608  19.580  1.00 96.63
ATOM   3458  C   MET A 446      -7.365 -19.446  19.705  1.00 96.63
ATOM   3459  O   MET A 446      -7.236 -20.493  19.073  1.00 96.63
ATOM   3460  CB  MET A 446      -8.335 -17.405  18.685  1.00 96.63
ATOM   3461  CG  MET A 446      -9.593 -16.686  18.217  1.00 96.63
ATOM   3462  SD  MET A 446      -9.236 -15.354  17.047  1.00 96.63
ATOM   3463  CE  MET A 446      -8.428 -14.152  18.138  1.00 96.63
ATOM   3464  N   THR A 447      -6.392 -18.967  20.482  1.00 95.03
ATOM   3465  CA  THR A 447      -5.010 -19.486  20.473  1.00 95.03
ATOM   3466  C   THR A 447      -4.654 -20.313  21.710  1.00 95.03
ATOM   3467  O   THR A 447      -3.589 -20.925  21.760  1.00 95.03
ATOM   3468  CB  THR A 447      -3.992 -18.348  20.306  1.00 95.03
ATOM   3469  OG1 THR A 447      -4.013 -17.515  21.441  1.00 95.03
ATOM   3470  CG2 THR A 447      -4.234 -17.486  19.065  1.00 95.03
ATOM   3471  N   GLY A 448      -5.524 -20.333  22.722  1.00 94.55
ATOM   3472  CA  GLY A 448      -5.294 -20.979  24.015  1.00 94.55
ATOM   3473  C   GLY A 448      -4.430 -20.167  24.985  1.00 94.55
ATOM   3474  O   GLY A 448      -4.335 -20.526  26.158  1.00 94.55
ATOM   3475  N   GLN A 449      -3.817 -19.064  24.543  1.00 93.63
ATOM   3476  CA  GLN A 449      -2.920 -18.249  25.362  1.00 93.63
ATOM   3477  C   GLN A 449      -3.362 -16.790  25.374  1.00 93.63
ATOM   3478  O   GLN A 449      -3.705 -16.217  24.344  1.00 93.63
ATOM   3479  CB  GLN A 449      -1.472 -18.374  24.869  1.00 93.63
ATOM   3480  CG  GLN A 449      -0.941 -19.812  24.985  1.00 93.63
ATOM   3481  CD  GLN A 449       0.539 -19.934  24.642  1.00 93.63
ATOM   3482  OE1 GLN A 449       1.244 -18.978  24.375  1.00 93.63
ATOM   3483  NE2 GLN A 449       1.083 -21.131  24.657  1.00 93.63
ATOM   3484  N   ARG A 450      -3.327 -16.160  26.553  1.00 95.29
ATOM   3485  CA  ARG A 450      -3.520 -14.710  26.633  1.00 95.29
ATOM   3486  C   ARG A 450      -2.281 -13.988  26.107  1.00 95.29
ATOM   3487  O   ARG A 450      -1.168 -14.406  26.433  1.00 95.29
ATOM   3488  CB  ARG A 450      -3.829 -14.236  28.053  1.00 95.29
ATOM   3489  CG  ARG A 450      -5.268 -14.550  28.440  1.00 95.29
ATOM   3490  CD  ARG A 450      -5.647 -13.879  29.755  1.00 95.29
ATOM   3491  NE  ARG A 450      -7.034 -14.207  30.092  1.00 95.29
ATOM   3492  CZ  ARG A 450      -7.845 -13.557  30.891  1.00 95.29
ATOM   3493  NH1 ARG A 450      -7.483 -12.500  31.556  1.00 95.29
ATOM   3494  NH2 ARG A 450      -9.073 -13.935  31.034  1.00 95.29
ATOM   3495  N   PRO A 451      -2.446 -12.854  25.408  1.00 96.62
ATOM   3496  CA  PRO A 451      -1.317 -12.015  25.036  1.00 96.62
ATOM   3497  C   PRO A 451      -0.573 -11.556  26.297  1.00 96.62
ATOM   3498  O   PRO A 451      -1.195 -11.263  27.327  1.00 96.62
ATOM   3499  CB  PRO A 451      -1.918 -10.855  24.236  1.00 96.62
ATOM   3500  CG  PRO A 451      -3.345 -10.751  24.767  1.00 96.62
ATOM   3501  CD  PRO A 451      -3.706 -12.197  25.086  1.00 96.62
ATOM   3502  N   SER A 452       0.757 -11.515  26.227  1.00 96.16
ATOM   3503  CA  SER A 452       1.610 -11.027  27.315  1.00 96.16
ATOM   3504  C   SER A 452       1.383  -9.537  27.598  1.00 96.16
ATOM   3505  O   SER A 452       0.763  -8.820  26.810  1.00 96.16
ATOM   3506  CB  SER A 452       3.087 -11.310  27.009  1.00 96.16
ATOM   3507  OG  SER A 452       3.550 -10.484  25.961  1.00 96.16
ATOM   3508  N   LEU A 453       1.912  -9.058  28.728  1.00 95.56
ATOM   3509  CA  LEU A 453       1.784  -7.657  29.141  1.00 95.56
ATOM   3510  C   LEU A 453       2.341  -6.677  28.095  1.00 95.56
ATOM   3511  O   LEU A 453       1.785  -5.600  27.918  1.00 95.56
ATOM   3512  CB  LEU A 453       2.493  -7.495  30.498  1.00 95.56
ATOM   3513  CG  LEU A 453       2.386  -6.081  31.100  1.00 95.56
ATOM   3514  CD1 LEU A 453       0.937  -5.679  31.384  1.00 95.56
ATOM   3515  CD2 LEU A 453       3.175  -6.021  32.406  1.00 95.56
ATOM   3516  N   TYR A 454       3.389  -7.075  27.373  1.00 97.12
ATOM   3517  CA  TYR A 454       3.986  -6.288  26.296  1.00 97.12
ATOM   3518  C   TYR A 454       2.955  -5.868  25.236  1.00 97.12
ATOM   3519  O   TYR A 454       2.788  -4.676  24.985  1.00 97.12
ATOM   3520  CB  TYR A 454       5.119  -7.115  25.680  1.00 97.12
ATOM   3521  CG  TYR A 454       5.560  -6.616  24.327  1.00 97.12
ATOM   3522  CD1 TYR A 454       5.099  -7.261  23.162  1.00 97.12
ATOM   3523  CD2 TYR A 454       6.392  -5.486  24.237  1.00 97.12
ATOM   3524  CE1 TYR A 454       5.491  -6.793  21.899  1.00 97.12
ATOM   3525  CE2 TYR A 454       6.804  -5.031  22.975  1.00 97.12
ATOM   3526  CZ  TYR A 454       6.364  -5.694  21.814  1.00 97.12
ATOM   3527  OH  TYR A 454       6.840  -5.301  20.620  1.00 97.12
ATOM   3528  N   TRP A 455       2.210  -6.827  24.673  1.00 97.28
ATOM   3529  CA  TRP A 455       1.211  -6.554  23.632  1.00 97.28
ATOM   3530  C   TRP A 455       0.110  -5.633  24.148  1.00 97.28
ATOM   3531  O   TRP A 455      -0.257  -4.659  23.498  1.00 97.28
ATOM   3532  CB  TRP A 455       0.598  -7.874  23.162  1.00 97.28
ATOM   3533  CG  TRP A 455       1.587  -8.837  22.601  1.00 97.28
ATOM   3534  CD1 TRP A 455       2.065  -9.936  23.220  1.00 97.28
ATOM   3535  CD2 TRP A 455       2.296  -8.748  21.334  1.00 97.28
ATOM   3536  NE1 TRP A 455       3.032 -10.530  22.435  1.00 97.28
ATOM   3537  CE2 TRP A 455       3.232  -9.821  21.270  1.00 97.28
ATOM   3538  CE3 TRP A 455       2.265  -7.844  20.254  1.00 97.28
ATOM   3539  CZ2 TRP A 455       4.119  -9.973  20.199  1.00 97.28
ATOM   3540  CZ3 TRP A 455       3.117  -8.026  19.149  1.00 97.28
ATOM   3541  CH2 TRP A 455       4.038  -9.083  19.122  1.00 97.28
ATOM   3542  N   ARG A 456      -0.359  -5.905  25.368  1.00 97.63
ATOM   3543  CA  ARG A 456      -1.430  -5.144  26.016  1.00 97.63
ATOM   3544  C   ARG A 456      -1.037  -3.694  26.287  1.00 97.63
ATOM   3545  O   ARG A 456      -1.839  -2.795  26.050  1.00 97.63
ATOM   3546  CB  ARG A 456      -1.832  -5.853  27.311  1.00 97.63
ATOM   3547  CG  ARG A 456      -2.391  -7.255  27.037  1.00 97.63
ATOM   3548  CD  ARG A 456      -3.031  -7.788  28.313  1.00 97.63
ATOM   3549  NE  ARG A 456      -2.917  -9.243  28.427  1.00 97.63
ATOM   3550  CZ  ARG A 456      -3.199  -9.920  29.513  1.00 97.63
ATOM   3551  NH1 ARG A 456      -3.680  -9.342  30.582  1.00 97.63
ATOM   3552  NH2 ARG A 456      -2.935 -11.192  29.542  1.00 97.63
ATOM   3553  N   LEU A 457       0.194  -3.460  26.747  1.00 97.27
ATOM   3554  CA  LEU A 457       0.733  -2.114  26.951  1.00 97.27
ATOM   3555  C   LEU A 457       0.926  -1.369  25.629  1.00 97.27
ATOM   3556  O   LEU A 457       0.626  -0.175  25.569  1.00 97.27
ATOM   3557  CB  LEU A 457       2.069  -2.190  27.710  1.00 97.27
ATOM   3558  CG  LEU A 457       1.943  -2.517  29.207  1.00 97.27
ATOM   3559  CD1 LEU A 457       3.342  -2.705  29.795  1.00 97.27
ATOM   3560  CD2 LEU A 457       1.254  -1.398  29.992  1.00 97.27
ATOM   3561  N   CYS A 458       1.379  -2.059  24.579  1.00 97.53
ATOM   3562  CA  CYS A 458       1.521  -1.459  23.256  1.00 97.53
ATOM   3563  C   CYS A 458       0.167  -0.986  22.725  1.00 97.53
ATOM   3564  O   CYS A 458      -0.004   0.208  22.497  1.00 97.53
ATOM   3565  CB  CYS A 458       2.230  -2.415  22.291  1.00 97.53
ATOM   3566  SG  CYS A 458       3.953  -2.655  22.812  1.00 97.53
ATOM   3567  N   TRP A 459      -0.826  -1.878  22.655  1.00 97.49
ATOM   3568  CA  TRP A 459      -2.163  -1.543  22.154  1.00 97.49
ATOM   3569  C   TRP A 459      -2.845  -0.440  22.951  1.00 97.49
ATOM   3570  O   TRP A 459      -3.485   0.429  22.372  1.00 97.49
ATOM   3571  CB  TRP A 459      -3.043  -2.793  22.184  1.00 97.49
ATOM   3572  CG  TRP A 459      -2.548  -3.936  21.367  1.00 97.49
ATOM   3573  CD1 TRP A 459      -1.858  -3.827  20.210  1.00 97.49
ATOM   3574  CD2 TRP A 459      -2.744  -5.366  21.588  1.00 97.49
ATOM   3575  NE1 TRP A 459      -1.605  -5.084  19.718  1.00 97.49
ATOM   3576  CE2 TRP A 459      -2.153  -6.065  20.500  1.00 97.49
ATOM   3577  CE3 TRP A 459      -3.398  -6.145  22.567  1.00 97.49
ATOM   3578  CZ2 TRP A 459      -2.232  -7.451  20.356  1.00 97.49
ATOM   3579  CZ3 TRP A 459      -3.459  -7.548  22.454  1.00 97.49
ATOM   3580  CH2 TRP A 459      -2.881  -8.200  21.348  1.00 97.49
ATOM   3581  N   LYS A 460      -2.719  -0.465  24.282  1.00 96.31
ATOM   3582  CA  LYS A 460      -3.419   0.496  25.132  1.00 96.31
ATOM   3583  C   LYS A 460      -2.750   1.862  25.176  1.00 96.31
ATOM   3584  O   LYS A 460      -3.447   2.870  25.184  1.00 96.31
ATOM   3585  CB  LYS A 460      -3.587  -0.090  26.532  1.00 96.31
ATOM   3586  CG  LYS A 460      -4.652   0.701  27.290  1.00 96.31
ATOM   3587  CD  LYS A 460      -4.879   0.084  28.659  1.00 96.31
ATOM   3588  CE  LYS A 460      -5.979   0.887  29.337  1.00 96.31
ATOM   3589  NZ  LYS A 460      -6.359   0.287  30.624  1.00 96.31
ATOM   3590  N   LEU A 461      -1.426   1.910  25.280  1.00 95.91
ATOM   3591  CA  LEU A 461      -0.710   3.140  25.617  1.00 95.91
ATOM   3592  C   LEU A 461       0.335   3.488  24.568  1.00 95.91
ATOM   3593  O   LEU A 461       0.256   4.555  23.969  1.00 95.91
ATOM   3594  CB  LEU A 461      -0.095   3.023  27.029  1.00 95.91
ATOM   3595  CG  LEU A 461      -1.108   2.832  28.173  1.00 95.91
ATOM   3596  CD1 LEU A 461      -0.375   2.618  29.497  1.00 95.91
ATOM   3597  CD2 LEU A 461      -2.026   4.039  28.344  1.00 95.91
ATOM   3598  N   VAL A 462       1.307   2.604  24.336  1.00 95.78
ATOM   3599  CA  VAL A 462       2.511   2.982  23.583  1.00 95.78
ATOM   3600  C   VAL A 462       2.185   3.303  22.124  1.00 95.78
ATOM   3601  O   VAL A 462       2.546   4.380  21.651  1.00 95.78
ATOM   3602  CB  VAL A 462       3.626   1.926  23.685  1.00 95.78
ATOM   3603  CG1 VAL A 462       4.931   2.471  23.105  1.00 95.78
ATOM   3604  CG2 VAL A 462       3.904   1.509  25.138  1.00 95.78
ATOM   3605  N   SER A 463       1.465   2.421  21.424  1.00 95.25
ATOM   3606  CA  SER A 463       1.144   2.619  20.008  1.00 95.25
ATOM   3607  C   SER A 463       0.193   3.807  19.796  1.00 95.25
ATOM   3608  O   SER A 463       0.543   4.670  18.994  1.00 95.25
ATOM   3609  CB  SER A 463       0.624   1.345  19.319  1.00 95.25
ATOM   3610  OG  SER A 463       1.232   0.158  19.797  1.00 95.25
ATOM   3611  N   PRO A 464      -0.943   3.948  20.519  1.00 95.03
ATOM   3612  CA  PRO A 464      -1.822   5.109  20.353  1.00 95.03
ATOM   3613  C   PRO A 464      -1.148   6.446  20.678  1.00 95.03
ATOM   3614  O   PRO A 464      -1.334   7.407  19.939  1.00 95.03
ATOM   3615  CB  PRO A 464      -3.024   4.875  21.272  1.00 95.03
ATOM   3616  CG  PRO A 464      -3.060   3.361  21.428  1.00 95.03
ATOM   3617  CD  PRO A 464      -1.583   2.977  21.400  1.00 95.03
ATOM   3618  N   CYS A 465      -0.342   6.527  21.745  1.00 94.49
ATOM   3619  CA  CYS A 465       0.371   7.762  22.087  1.00 94.49
ATOM   3620  C   CYS A 465       1.372   8.154  20.998  1.00 94.49
ATOM   3621  O   CYS A 465       1.447   9.323  20.621  1.00 94.49
ATOM   3622  CB  CYS A 465       1.102   7.591  23.425  1.00 94.49
ATOM   3623  SG  CYS A 465      -0.083   7.608  24.800  1.00 94.49
ATOM   3624  N   PHE A 466       2.123   7.183  20.477  1.00 89.69
ATOM   3625  CA  PHE A 466       3.080   7.449  19.412  1.00 89.69
ATOM   3626  C   PHE A 466       2.374   7.823  18.103  1.00 89.69
ATOM   3627  O   PHE A 466       2.756   8.795  17.461  1.00 89.69
ATOM   3628  CB  PHE A 466       4.010   6.245  19.252  1.00 89.69
ATOM   3629  CG  PHE A 466       5.198   6.546  18.365  1.00 89.69
ATOM   3630  CD1 PHE A 466       5.033   6.620  16.976  1.00 89.69
ATOM   3631  CD2 PHE A 466       6.465   6.804  18.920  1.00 89.69
ATOM   3632  CE1 PHE A 466       6.135   6.851  16.142  1.00 89.69
ATOM   3633  CE2 PHE A 466       7.563   7.075  18.082  1.00 89.69
ATOM   3634  CZ  PHE A 466       7.404   7.070  16.687  1.00 89.69
ATOM   3635  N   LEU A 467       1.316   7.105  17.716  1.00 91.07
ATOM   3636  CA  LEU A 467       0.524   7.436  16.529  1.00 91.07
ATOM   3637  C   LEU A 467      -0.111   8.824  16.638  1.00 91.07
ATOM   3638  O   LEU A 467      -0.067   9.581  15.676  1.00 91.07
ATOM   3639  CB  LEU A 467      -0.571   6.384  16.332  1.00 91.07
ATOM   3640  CG  LEU A 467      -0.074   5.035  15.800  1.00 91.07
ATOM   3641  CD1 LEU A 467      -1.225   4.047  15.932  1.00 91.07
ATOM   3642  CD2 LEU A 467       0.348   5.108  14.331  1.00 91.07
ATOM   3643  N   LEU A 468      -0.642   9.192  17.808  1.00 92.83
ATOM   3644  CA  LEU A 468      -1.168  10.533  18.055  1.00 92.83
ATOM   3645  C   LEU A 468      -0.080  11.594  17.866  1.00 92.83
ATOM   3646  O   LEU A 468      -0.322  12.594  17.196  1.00 92.83
ATOM   3647  CB  LEU A 468      -1.774  10.591  19.468  1.00 92.83
ATOM   3648  CG  LEU A 468      -2.331  11.974  19.856  1.00 92.83
ATOM   3649  CD1 LEU A 468      -3.517  12.390  18.983  1.00 92.83
ATOM   3650  CD2 LEU A 468      -2.795  11.947  21.311  1.00 92.83
ATOM   3651  N   PHE A 469       1.116  11.363  18.412  1.00 89.93
ATOM   3652  CA  PHE A 469       2.260  12.248  18.205  1.00 89.93
ATOM   3653  C   PHE A 469       2.589  12.398  16.713  1.00 89.93
ATOM   3654  O   PHE A 469       2.658  13.521  16.222  1.00 89.93
ATOM   3655  CB  PHE A 469       3.458  11.738  19.018  1.00 89.93
ATOM   3656  CG  PHE A 469       4.748  12.478  18.731  1.00 89.93
ATOM   3657  CD1 PHE A 469       5.717  11.908  17.882  1.00 89.93
ATOM   3658  CD2 PHE A 469       4.968  13.749  19.291  1.00 89.93
ATOM   3659  CE1 PHE A 469       6.905  12.606  17.601  1.00 89.93
ATOM   3660  CE2 PHE A 469       6.158  14.445  19.012  1.00 89.93
ATOM   3661  CZ  PHE A 469       7.127  13.872  18.170  1.00 89.93
ATOM   3662  N   VAL A 470       2.711  11.294  15.969  1.00 85.57
ATOM   3663  CA  VAL A 470       3.017  11.332  14.528  1.00 85.57
ATOM   3664  C   VAL A 470       1.922  12.049  13.740  1.00 85.57
ATOM   3665  O   VAL A 470       2.244  12.890  12.906  1.00 85.57
ATOM   3666  CB  VAL A 470       3.246   9.918  13.967  1.00 85.57
ATOM   3667  CG1 VAL A 470       3.502   9.914  12.455  1.00 85.57
ATOM   3668  CG2 VAL A 470       4.484   9.274  14.592  1.00 85.57
ATOM   3669  N   VAL A 471       0.642  11.779  14.013  1.00 87.32
ATOM   3670  CA  VAL A 471      -0.485  12.443  13.337  1.00 87.32
ATOM   3671  C   VAL A 471      -0.449  13.948  13.592  1.00 87.32
ATOM   3672  O   VAL A 471      -0.478  14.724  12.638  1.00 87.32
ATOM   3673  CB  VAL A 471      -1.835  11.833  13.768  1.00 87.32
ATOM   3674  CG1 VAL A 471      -3.040  12.657  13.290  1.00 87.32
ATOM   3675  CG2 VAL A 471      -2.008  10.428  13.180  1.00 87.32
ATOM   3676  N   VAL A 472      -0.320  14.377  14.852  1.00 89.86
ATOM   3677  CA  VAL A 472      -0.271  15.803  15.210  1.00 89.86
ATOM   3678  C   VAL A 472       0.916  16.489  14.545  1.00 89.86
ATOM   3679  O   VAL A 472       0.738  17.536  13.925  1.00 89.86
ATOM   3680  CB  VAL A 472      -0.230  15.990  16.739  1.00 89.86
ATOM   3681  CG1 VAL A 472       0.052  17.442  17.153  1.00 89.86
ATOM   3682  CG2 VAL A 472      -1.578  15.598  17.359  1.00 89.86
ATOM   3683  N   VAL A 473       2.111  15.898  14.618  1.00 86.60
ATOM   3684  CA  VAL A 473       3.293  16.494  13.991  1.00 86.60
ATOM   3685  C   VAL A 473       3.137  16.524  12.472  1.00 86.60
ATOM   3686  O   VAL A 473       3.407  17.567  11.896  1.00 86.60
ATOM   3687  CB  VAL A 473       4.600  15.815  14.434  1.00 86.60
ATOM   3688  CG1 VAL A 473       5.811  16.513  13.806  1.00 86.60
ATOM   3689  CG2 VAL A 473       4.817  15.938  15.950  1.00 86.60
ATOM   3690  N   SER A 474       2.621  15.469  11.830  1.00 82.03
ATOM   3691  CA  SER A 474       2.412  15.434  10.371  1.00 82.03
ATOM   3692  C   SER A 474       1.471  16.532   9.863  1.00 82.03
ATOM   3693  O   SER A 474       1.682  17.068   8.778  1.00 82.03
ATOM   3694  CB  SER A 474       1.897  14.058   9.920  1.00 82.03
ATOM   3695  OG  SER A 474       0.527  13.852  10.228  1.00 82.03
ATOM   3696  N   ILE A 475       0.460  16.902  10.658  1.00 84.65
ATOM   3697  CA  ILE A 475      -0.468  17.992  10.335  1.00 84.65
ATOM   3698  C   ILE A 475       0.207  19.350  10.566  1.00 84.65
ATOM   3699  O   ILE A 475       0.083  20.248   9.738  1.00 84.65
ATOM   3700  CB  ILE A 475      -1.776  17.835  11.149  1.00 84.65
ATOM   3701  CG1 ILE A 475      -2.538  16.560  10.709  1.00 84.65
ATOM   3702  CG2 ILE A 475      -2.687  19.068  10.985  1.00 84.65
ATOM   3703  CD1 ILE A 475      -3.690  16.167  11.644  1.00 84.65
ATOM   3704  N   VAL A 476       0.939  19.510  11.672  1.00 86.74
ATOM   3705  CA  VAL A 476       1.610  20.775  12.024  1.00 86.74
ATOM   3706  C   VAL A 476       2.776  21.091  11.083  1.00 86.74
ATOM   3707  O   VAL A 476       2.995  22.252  10.751  1.00 86.74
ATOM   3708  CB  VAL A 476       2.075  20.739  13.494  1.00 86.74
ATOM   3709  CG1 VAL A 476       2.972  21.924  13.881  1.00 86.74
ATOM   3710  CG2 VAL A 476       0.867  20.771  14.443  1.00 86.74
ATOM   3711  N   THR A 477       3.527  20.080  10.642  1.00 84.26
ATOM   3712  CA  THR A 477       4.683  20.229   9.744  1.00 84.26
ATOM   3713  C   THR A 477       4.337  19.985   8.277  1.00 84.26
ATOM   3714  O   THR A 477       5.242  19.776   7.464  1.00 84.26
ATOM   3715  CB  THR A 477       5.876  19.362  10.181  1.00 84.26
ATOM   3716  OG1 THR A 477       5.580  17.991  10.087  1.00 84.26
ATOM   3717  CG2 THR A 477       6.309  19.650  11.619  1.00 84.26
ATOM   3718  N   PHE A 478       3.046  20.033   7.928  1.00 83.46
ATOM   3719  CA  PHE A 478       2.565  19.814   6.570  1.00 83.46
ATOM   3720  C   PHE A 478       3.293  20.715   5.563  1.00 83.46
ATOM   3721  O   PHE A 478       3.388  21.933   5.734  1.00 83.46
ATOM   3722  CB  PHE A 478       1.047  20.032   6.513  1.00 83.46
ATOM   3723  CG  PHE A 478       0.497  19.913   5.107  1.00 83.46
ATOM   3724  CD1 PHE A 478       0.278  21.070   4.333  1.00 83.46
ATOM   3725  CD2 PHE A 478       0.290  18.641   4.543  1.00 83.46
ATOM   3726  CE1 PHE A 478      -0.106  20.955   2.987  1.00 83.46
ATOM   3727  CE2 PHE A 478      -0.103  18.529   3.200  1.00 83.46
ATOM   3728  CZ  PHE A 478      -0.269  19.683   2.419  1.00 83.46
ATOM   3729  N   ARG A 479       3.789  20.104   4.484  1.00 83.89
ATOM   3730  CA  ARG A 479       4.374  20.804   3.339  1.00 83.89
ATOM   3731  C   ARG A 479       3.609  20.409   2.082  1.00 83.89
ATOM   3732  O   ARG A 479       3.440  19.209   1.874  1.00 83.89
ATOM   3733  CB  ARG A 479       5.863  20.478   3.184  1.00 83.89
ATOM   3734  CG  ARG A 479       6.689  21.054   4.338  1.00 83.89
ATOM   3735  CD  ARG A 479       8.181  20.941   4.018  1.00 83.89
ATOM   3736  NE  ARG A 479       9.001  21.506   5.104  1.00 83.89
ATOM   3737  CZ  ARG A 479      10.311  21.674   5.083  1.00 83.89
ATOM   3738  NH1 ARG A 479      11.031  21.350   4.044  1.00 83.89
ATOM   3739  NH2 ARG A 479      10.928  22.173   6.117  1.00 83.89
ATOM   3740  N   PRO A 480       3.198  21.375   1.240  1.00 88.00
ATOM   3741  CA  PRO A 480       2.582  21.067  -0.041  1.00 88.00
ATOM   3742  C   PRO A 480       3.436  20.084  -0.858  1.00 88.00
ATOM   3743  O   PRO A 480       4.670  20.202  -0.850  1.00 88.00
ATOM   3744  CB  PRO A 480       2.424  22.408  -0.763  1.00 88.00
ATOM   3745  CG  PRO A 480       2.320  23.409   0.385  1.00 88.00
ATOM   3746  CD  PRO A 480       3.254  22.817   1.439  1.00 88.00
ATOM   3747  N   PRO A 481       2.814  19.120  -1.559  1.00 88.19
ATOM   3748  CA  PRO A 481       3.538  18.232  -2.452  1.00 88.19
ATOM   3749  C   PRO A 481       4.200  19.022  -3.586  1.00 88.19
ATOM   3750  O   PRO A 481       3.761  20.106  -3.972  1.00 88.19
ATOM   3751  CB  PRO A 481       2.506  17.223  -2.963  1.00 88.19
ATOM   3752  CG  PRO A 481       1.190  17.991  -2.881  1.00 88.19
ATOM   3753  CD  PRO A 481       1.383  18.864  -1.642  1.00 88.19
ATOM   3754  N   HIS A 482       5.267  18.449  -4.133  1.00 88.19
ATOM   3755  CA  HIS A 482       5.976  18.950  -5.306  1.00 88.19
ATOM   3756  C   HIS A 482       6.410  17.756  -6.154  1.00 88.19
ATOM   3757  O   HIS A 482       6.624  16.662  -5.628  1.00 88.19
ATOM   3758  CB  HIS A 482       7.169  19.836  -4.900  1.00 88.19
ATOM   3759  CG  HIS A 482       8.261  19.121  -4.138  1.00 88.19
ATOM   3760  ND1 HIS A 482       8.115  18.471  -2.935  1.00 88.19
ATOM   3761  CD2 HIS A 482       9.575  18.993  -4.506  1.00 88.19
ATOM   3762  CE1 HIS A 482       9.300  17.937  -2.601  1.00 88.19
ATOM   3763  NE2 HIS A 482      10.228  18.248  -3.516  1.00 88.19
ATOM   3764  N   TYR A 483       6.524  17.960  -7.463  1.00 87.65
ATOM   3765  CA  TYR A 483       7.064  16.961  -8.382  1.00 87.65
ATOM   3766  C   TYR A 483       8.185  17.599  -9.200  1.00 87.65
ATOM   3767  O   TYR A 483       7.932  18.423 -10.082  1.00 87.65
ATOM   3768  CB  TYR A 483       5.951  16.372  -9.259  1.00 87.65
ATOM   3769  CG  TYR A 483       6.464  15.262 -10.155  1.00 87.65
ATOM   3770  CD1 TYR A 483       6.964  15.560 -11.439  1.00 87.65
ATOM   3771  CD2 TYR A 483       6.516  13.939  -9.674  1.00 87.65
ATOM   3772  CE1 TYR A 483       7.534  14.545 -12.231  1.00 87.65
ATOM   3773  CE2 TYR A 483       7.075  12.920 -10.469  1.00 87.65
ATOM   3774  CZ  TYR A 483       7.591  13.222 -11.747  1.00 87.65
ATOM   3775  OH  TYR A 483       8.150  12.239 -12.502  1.00 87.65
ATOM   3776  N   GLY A 484       9.436  17.271  -8.872  1.00 83.40
ATOM   3777  CA  GLY A 484      10.593  17.982  -9.413  1.00 83.40
ATOM   3778  C   GLY A 484      10.504  19.481  -9.104  1.00 83.40
ATOM   3779  O   GLY A 484      10.388  19.871  -7.945  1.00 83.40
ATOM   3780  N   ALA A 485      10.517  20.317 -10.145  1.00 85.17
ATOM   3781  CA  ALA A 485      10.363  21.769 -10.021  1.00 85.17
ATOM   3782  C   ALA A 485       8.896  22.251  -9.973  1.00 85.17
ATOM   3783  O   ALA A 485       8.650  23.439  -9.768  1.00 85.17
ATOM   3784  CB  ALA A 485      11.137  22.424 -11.173  1.00 85.17
ATOM   3785  N   TYR A 486       7.916  21.365 -10.181  1.00 90.44
ATOM   3786  CA  TYR A 486       6.502  21.736 -10.206  1.00 90.44
ATOM   3787  C   TYR A 486       5.931  21.876  -8.791  1.00 90.44
ATOM   3788  O   TYR A 486       5.996  20.942  -7.986  1.00 90.44
ATOM   3789  CB  TYR A 486       5.700  20.722 -11.025  1.00 90.44
ATOM   3790  CG  TYR A 486       4.237  21.091 -11.156  1.00 90.44
ATOM   3791  CD1 TYR A 486       3.284  20.523 -10.287  1.00 90.44
ATOM   3792  CD2 TYR A 486       3.834  22.018 -12.135  1.00 90.44
ATOM   3793  CE1 TYR A 486       1.925  20.868 -10.410  1.00 90.44
ATOM   3794  CE2 TYR A 486       2.480  22.382 -12.247  1.00 90.44
ATOM   3795  CZ  TYR A 486       1.524  21.804 -11.385  1.00 90.44
ATOM   3796  OH  TYR A 486       0.214  22.140 -11.504  1.00 90.44
ATOM   3797  N   ILE A 487       5.321  23.032  -8.523  1.00 92.55
ATOM   3798  CA  ILE A 487       4.641  23.356  -7.266  1.00 92.55
ATOM   3799  C   ILE A 487       3.134  23.304  -7.509  1.00 92.55
ATOM   3800  O   ILE A 487       2.628  23.926  -8.443  1.00 92.55
ATOM   3801  CB  ILE A 487       5.093  24.734  -6.731  1.00 92.55
ATOM   3802  CG1 ILE A 487       6.625  24.759  -6.505  1.00 92.55
ATOM   3803  CG2 ILE A 487       4.346  25.070  -5.424  1.00 92.55
ATOM   3804  CD1 ILE A 487       7.183  26.143  -6.154  1.00 92.55
ATOM   3805  N   PHE A 488       2.417  22.571  -6.660  1.00 94.14
ATOM   3806  CA  PHE A 488       0.974  22.408  -6.800  1.00 94.14
ATOM   3807  C   PHE A 488       0.226  23.703  -6.452  1.00 94.14
ATOM   3808  O   PHE A 488       0.532  24.317  -5.424  1.00 94.14
ATOM   3809  CB  PHE A 488       0.487  21.241  -5.935  1.00 94.14
ATOM   3810  CG  PHE A 488       0.777  19.889  -6.553  1.00 94.14
ATOM   3811  CD1 PHE A 488      -0.268  19.136  -7.116  1.00 94.14
ATOM   3812  CD2 PHE A 488       2.095  19.395  -6.600  1.00 94.14
ATOM   3813  CE1 PHE A 488       0.006  17.891  -7.704  1.00 94.14
ATOM   3814  CE2 PHE A 488       2.368  18.147  -7.180  1.00 94.14
ATOM   3815  CZ  PHE A 488       1.320  17.399  -7.735  1.00 94.14
ATOM   3816  N   PRO A 489      -0.776  24.102  -7.257  1.00 95.07
ATOM   3817  CA  PRO A 489      -1.586  25.279  -6.972  1.00 95.07
ATOM   3818  C   PRO A 489      -2.447  25.077  -5.716  1.00 95.07
ATOM   3819  O   PRO A 489      -2.807  23.953  -5.355  1.00 95.07
ATOM   3820  CB  PRO A 489      -2.428  25.502  -8.233  1.00 95.07
ATOM   3821  CG  PRO A 489      -2.580  24.096  -8.813  1.00 95.07
ATOM   3822  CD  PRO A 489      -1.244  23.443  -8.473  1.00 95.07
ATOM   3823  N   ASP A 490      -2.842  26.175  -5.069  1.00 94.35
ATOM   3824  CA  ASP A 490      -3.598  26.140  -3.807  1.00 94.35
ATOM   3825  C   ASP A 490      -4.919  25.370  -3.912  1.00 94.35
ATOM   3826  O   ASP A 490      -5.307  24.666  -2.977  1.00 94.35
ATOM   3827  CB  ASP A 490      -3.886  27.573  -3.336  1.00 94.35
ATOM   3828  CG  ASP A 490      -2.626  28.330  -2.916  1.00 94.35
ATOM   3829  OD1 ASP A 490      -1.677  27.660  -2.451  1.00 94.35
ATOM   3830  OD2 ASP A 490      -2.637  29.569  -3.067  1.00 94.35
ATOM   3831  N   TRP A 491      -5.594  25.440  -5.064  1.00 95.79
ATOM   3832  CA  TRP A 491      -6.827  24.690  -5.298  1.00 95.79
ATOM   3833  C   TRP A 491      -6.582  23.172  -5.298  1.00 95.79
ATOM   3834  O   TRP A 491      -7.421  22.421  -4.799  1.00 95.79
ATOM   3835  CB  TRP A 491      -7.480  25.163  -6.605  1.00 95.79
ATOM   3836  CG  TRP A 491      -6.832  24.683  -7.869  1.00 95.79
ATOM   3837  CD1 TRP A 491      -6.051  25.404  -8.711  1.00 95.79
ATOM   3838  CD2 TRP A 491      -6.938  23.352  -8.468  1.00 95.79
ATOM   3839  NE1 TRP A 491      -5.658  24.603  -9.771  1.00 95.79
ATOM   3840  CE2 TRP A 491      -6.143  23.325  -9.645  1.00 95.79
ATOM   3841  CE3 TRP A 491      -7.626  22.161  -8.135  1.00 95.79
ATOM   3842  CZ2 TRP A 491      -6.023  22.179 -10.435  1.00 95.79
ATOM   3843  CZ3 TRP A 491      -7.492  20.998  -8.918  1.00 95.79
ATOM   3844  CH2 TRP A 491      -6.688  21.005 -10.068  1.00 95.79
ATOM   3845  N   ALA A 492      -5.429  22.714  -5.801  1.00 95.34
ATOM   3846  CA  ALA A 492      -5.067  21.300  -5.816  1.00 95.34
ATOM   3847  C   ALA A 492      -4.739  20.817  -4.400  1.00 95.34
ATOM   3848  O   ALA A 492      -5.179  19.741  -4.002  1.00 95.34
ATOM   3849  CB  ALA A 492      -3.905  21.075  -6.788  1.00 95.34
ATOM   3850  N   ASN A 493      -4.062  21.646  -3.600  1.00 93.59
ATOM   3851  CA  ASN A 493      -3.848  21.374  -2.177  1.00 93.59
ATOM   3852  C   ASN A 493      -5.176  21.293  -1.408  1.00 93.59
ATOM   3853  O   ASN A 493      -5.368  20.386  -0.598  1.00 93.59
ATOM   3854  CB  ASN A 493      -2.925  22.456  -1.589  1.00 93.59
ATOM   3855  CG  ASN A 493      -1.519  22.364  -2.147  1.00 93.59
ATOM   3856  OD1 ASN A 493      -0.952  21.290  -2.234  1.00 93.59
ATOM   3857  ND2 ASN A 493      -0.917  23.467  -2.529  1.00 93.59
ATOM   3858  N   ALA A 494      -6.118  22.200  -1.686  1.00 94.85
ATOM   3859  CA  ALA A 494      -7.456  22.157  -1.102  1.00 94.85
ATOM   3860  C   ALA A 494      -8.207  20.877  -1.506  1.00 94.85
ATOM   3861  O   ALA A 494      -8.798  20.218  -0.652  1.00 94.85
ATOM   3862  CB  ALA A 494      -8.219  23.423  -1.507  1.00 94.85
ATOM   3863  N   LEU A 495      -8.130  20.479  -2.780  1.00 94.64
ATOM   3864  CA  LEU A 495      -8.698  19.222  -3.269  1.00 94.64
ATOM   3865  C   LEU A 495      -8.076  18.005  -2.566  1.00 94.64
ATOM   3866  O   LEU A 495      -8.804  17.115  -2.134  1.00 94.64
ATOM   3867  CB  LEU A 495      -8.519  19.155  -4.797  1.00 94.64
ATOM   3868  CG  LEU A 495      -9.053  17.860  -5.434  1.00 94.64
ATOM   3869  CD1 LEU A 495     -10.559  17.689  -5.218  1.00 94.64
ATOM   3870  CD2 LEU A 495      -8.782  17.873  -6.936  1.00 94.64
ATOM   3871  N   GLY A 496      -6.753  17.987  -2.392  1.00 93.47
ATOM   3872  CA  GLY A 496      -6.044  16.950  -1.642  1.00 93.47
ATOM   3873  C   GLY A 496      -6.562  16.810  -0.209  1.00 93.47
ATOM   3874  O   GLY A 496      -6.907  15.710   0.224  1.00 93.47
ATOM   3875  N   TRP A 497      -6.729  17.925   0.506  1.00 93.05
ATOM   3876  CA  TRP A 497      -7.323  17.924   1.846  1.00 93.05
ATOM   3877  C   TRP A 497      -8.784  17.468   1.860  1.00 93.05
ATOM   3878  O   TRP A 497      -9.179  16.757   2.783  1.00 93.05
ATOM   3879  CB  TRP A 497      -7.187  19.308   2.485  1.00 93.05
ATOM   3880  CG  TRP A 497      -5.856  19.558   3.115  1.00 93.05
ATOM   3881  CD1 TRP A 497      -4.930  20.450   2.699  1.00 93.05
ATOM   3882  CD2 TRP A 497      -5.277  18.887   4.276  1.00 93.05
ATOM   3883  NE1 TRP A 497      -3.828  20.396   3.533  1.00 93.05
ATOM   3884  CE2 TRP A 497      -3.984  19.441   4.514  1.00 93.05
ATOM   3885  CE3 TRP A 497      -5.708  17.857   5.142  1.00 93.05
ATOM   3886  CZ2 TRP A 497      -3.158  18.994   5.553  1.00 93.05
ATOM   3887  CZ3 TRP A 497      -4.884  17.399   6.188  1.00 93.05
ATOM   3888  CH2 TRP A 497      -3.611  17.963   6.392  1.00 93.05
ATOM   3889  N   VAL A 498      -9.588  17.810   0.850  1.00 95.29
ATOM   3890  CA  VAL A 498     -10.960  17.289   0.711  1.00 95.29
ATOM   3891  C   VAL A 498     -10.944  15.767   0.549  1.00 95.29
ATOM   3892  O   VAL A 498     -11.721  15.074   1.204  1.00 95.29
ATOM   3893  CB  VAL A 498     -11.705  17.980  -0.450  1.00 95.29
ATOM   3894  CG1 VAL A 498     -13.044  17.304  -0.780  1.00 95.29
ATOM   3895  CG2 VAL A 498     -12.019  19.439  -0.092  1.00 95.29
ATOM   3896  N   ILE A 499     -10.024  15.220  -0.249  1.00 93.59
ATOM   3897  CA  ILE A 499      -9.871  13.769  -0.423  1.00 93.59
ATOM   3898  C   ILE A 499      -9.435  13.113   0.894  1.00 93.59
ATOM   3899  O   ILE A 499     -10.073  12.155   1.332  1.00 93.59
ATOM   3900  CB  ILE A 499      -8.903  13.454  -1.585  1.00 93.59
ATOM   3901  CG1 ILE A 499      -9.505  13.932  -2.927  1.00 93.59
ATOM   3902  CG2 ILE A 499      -8.609  11.942  -1.657  1.00 93.59
ATOM   3903  CD1 ILE A 499      -8.489  13.984  -4.074  1.00 93.59
ATOM   3904  N   ALA A 500      -8.417  13.640   1.575  1.00 92.22
ATOM   3905  CA  ALA A 500      -7.960  13.100   2.856  1.00 92.22
ATOM   3906  C   ALA A 500      -9.082  13.116   3.910  1.00 92.22
ATOM   3907  O   ALA A 500      -9.439  12.088   4.492  1.00 92.22
ATOM   3908  CB  ALA A 500      -6.743  13.909   3.318  1.00 92.22
ATOM   3909  N   THR A 501      -9.721  14.274   4.089  1.00 93.66
ATOM   3910  CA  THR A 501     -10.798  14.447   5.069  1.00 93.66
ATOM   3911  C   THR A 501     -12.041  13.638   4.726  1.00 93.66
ATOM   3912  O   THR A 501     -12.730  13.218   5.649  1.00 93.66
ATOM   3913  CB  THR A 501     -11.188  15.915   5.276  1.00 93.66
ATOM   3914  OG1 THR A 501     -11.535  16.530   4.064  1.00 93.66
ATOM   3915  CG2 THR A 501     -10.069  16.727   5.928  1.00 93.66
ATOM   3916  N   SER A 502     -12.313  13.333   3.452  1.00 95.72
ATOM   3917  CA  SER A 502     -13.455  12.491   3.070  1.00 95.72
ATOM   3918  C   SER A 502     -13.398  11.085   3.680  1.00 95.72
ATOM   3919  O   SER A 502     -14.432  10.564   4.094  1.00 95.72
ATOM   3920  CB  SER A 502     -13.583  12.397   1.547  1.00 95.72
ATOM   3921  OG  SER A 502     -12.576  11.578   0.994  1.00 95.72
ATOM   3922  N   SER A 503     -12.205  10.489   3.808  1.00 94.91
ATOM   3923  CA  SER A 503     -12.039   9.179   4.452  1.00 94.91
ATOM   3924  C   SER A 503     -12.088   9.294   5.972  1.00 94.91
ATOM   3925  O   SER A 503     -12.800   8.533   6.630  1.00 94.91
ATOM   3926  CB  SER A 503     -10.763   8.482   3.963  1.00 94.91
ATOM   3927  OG  SER A 503      -9.605   9.103   4.482  1.00 94.91
ATOM   3928  N   MET A 504     -11.412  10.295   6.539  1.00 94.55
ATOM   3929  CA  MET A 504     -11.376  10.541   7.982  1.00 94.55
ATOM   3930  C   MET A 504     -12.760  10.902   8.542  1.00 94.55
ATOM   3931  O   MET A 504     -13.121  10.471   9.637  1.00 94.55
ATOM   3932  CB  MET A 504     -10.390  11.678   8.279  1.00 94.55
ATOM   3933  CG  MET A 504      -8.947  11.391   7.840  1.00 94.55
ATOM   3934  SD  MET A 504      -7.872  12.850   7.927  1.00 94.55
ATOM   3935  CE  MET A 504      -7.718  13.094   9.716  1.00 94.55
ATOM   3936  N   ALA A 505     -13.562  11.656   7.784  1.00 96.49
ATOM   3937  CA  ALA A 505     -14.894  12.108   8.174  1.00 96.49
ATOM   3938  C   ALA A 505     -15.908  10.961   8.302  1.00 96.49
ATOM   3939  O   ALA A 505     -16.915  11.131   8.992  1.00 96.49
ATOM   3940  CB  ALA A 505     -15.384  13.164   7.176  1.00 96.49
ATOM   3941  N   MET A 506     -15.641   9.780   7.728  1.00 97.25
ATOM   3942  CA  MET A 506     -16.504   8.605   7.905  1.00 97.25
ATOM   3943  C   MET A 506     -16.655   8.221   9.381  1.00 97.25
ATOM   3944  O   MET A 506     -17.740   7.806   9.787  1.00 97.25
ATOM   3945  CB  MET A 506     -15.976   7.407   7.100  1.00 97.25
ATOM   3946  CG  MET A 506     -16.021   7.655   5.591  1.00 97.25
ATOM   3947  SD  MET A 506     -17.705   7.855   4.947  1.00 97.25
ATOM   3948  CE  MET A 506     -17.332   8.752   3.419  1.00 97.25
ATOM   3949  N   VAL A 507     -15.619   8.429  10.206  1.00 97.24
ATOM   3950  CA  VAL A 507     -15.675   8.186  11.656  1.00 97.24
ATOM   3951  C   VAL A 507     -16.727   9.077  12.342  1.00 97.24
ATOM   3952  O   VAL A 507     -17.694   8.523  12.872  1.00 97.24
ATOM   3953  CB  VAL A 507     -14.281   8.273  12.319  1.00 97.24
ATOM   3954  CG1 VAL A 507     -14.366   7.984  13.823  1.00 97.24
ATOM   3955  CG2 VAL A 507     -13.297   7.280  11.701  1.00 97.24
ATOM   3956  N   PRO A 508     -16.617  10.425  12.344  1.00 97.33
ATOM   3957  CA  PRO A 508     -17.600  11.282  13.007  1.00 97.33
ATOM   3958  C   PRO A 508     -18.982  11.255  12.341  1.00 97.33
ATOM   3959  O   PRO A 508     -19.982  11.291  13.058  1.00 97.33
ATOM   3960  CB  PRO A 508     -16.997  12.691  13.001  1.00 97.33
ATOM   3961  CG  PRO A 508     -16.045  12.675  11.809  1.00 97.33
ATOM   3962  CD  PRO A 508     -15.519  11.244  11.846  1.00 97.33
ATOM   3963  N   ILE A 509     -19.070  11.155  11.007  1.00 97.85
ATOM   3964  CA  ILE A 509     -20.359  11.091  10.296  1.00 97.85
ATOM   3965  C   ILE A 509     -21.128   9.838  10.716  1.00 97.85
ATOM   3966  O   ILE A 509     -22.300   9.931  11.091  1.00 97.85
ATOM   3967  CB  ILE A 509     -20.161  11.149   8.761  1.00 97.85
ATOM   3968  CG1 ILE A 509     -19.664  12.553   8.344  1.00 97.85
ATOM   3969  CG2 ILE A 509     -21.467  10.814   8.010  1.00 97.85
ATOM   3970  CD1 ILE A 509     -19.194  12.638   6.885  1.00 97.85
ATOM   3971  N   TYR A 510     -20.475   8.671  10.711  1.00 97.57
ATOM   3972  CA  TYR A 510     -21.126   7.433  11.125  1.00 97.57
ATOM   3973  C   TYR A 510     -21.460   7.445  12.620  1.00 97.57
ATOM   3974  O   TYR A 510     -22.550   7.020  13.004  1.00 97.57
ATOM   3975  CB  TYR A 510     -20.265   6.223  10.758  1.00 97.57
ATOM   3976  CG  TYR A 510     -21.032   4.928  10.914  1.00 97.57
ATOM   3977  CD1 TYR A 510     -21.185   4.355  12.191  1.00 97.57
ATOM   3978  CD2 TYR A 510     -21.677   4.354   9.801  1.00 97.57
ATOM   3979  CE1 TYR A 510     -22.021   3.241  12.362  1.00 97.57
ATOM   3980  CE2 TYR A 510     -22.480   3.208   9.963  1.00 97.57
ATOM   3981  CZ  TYR A 510     -22.653   2.655  11.247  1.00 97.57
ATOM   3982  OH  TYR A 510     -23.416   1.548  11.436  1.00 97.57
ATOM   3983  N   ALA A 511     -20.567   7.968  13.466  1.00 97.21
ATOM   3984  CA  ALA A 511     -20.820   8.099  14.898  1.00 97.21
ATOM   3985  C   ALA A 511     -22.076   8.944  15.176  1.00 97.21
ATOM   3986  O   ALA A 511     -22.945   8.521  15.942  1.00 97.21
ATOM   3987  CB  ALA A 511     -19.576   8.692  15.569  1.00 97.21
ATOM   3988  N   ALA A 512     -22.217  10.092  14.503  1.00 97.00
ATOM   3989  CA  ALA A 512     -23.396  10.949  14.600  1.00 97.00
ATOM   3990  C   ALA A 512     -24.658  10.247  14.076  1.00 97.00
ATOM   3991  O   ALA A 512     -25.678  10.223  14.765  1.00 97.00
ATOM   3992  CB  ALA A 512     -23.119  12.255  13.844  1.00 97.00
ATOM   3993  N   TYR A 513     -24.584   9.610  12.902  1.00 97.05
ATOM   3994  CA  TYR A 513     -25.686   8.825  12.338  1.00 97.05
ATOM   3995  C   TYR A 513     -26.160   7.730  13.302  1.00 97.05
ATOM   3996  O   TYR A 513     -27.355   7.637  13.597  1.00 97.05
ATOM   3997  CB  TYR A 513     -25.250   8.215  10.998  1.00 97.05
ATOM   3998  CG  TYR A 513     -26.131   7.068  10.539  1.00 97.05
ATOM   3999  CD1 TYR A 513     -25.666   5.740  10.638  1.00 97.05
ATOM   4000  CD2 TYR A 513     -27.434   7.325  10.072  1.00 97.05
ATOM   4001  CE1 TYR A 513     -26.498   4.670  10.257  1.00 97.05
ATOM   4002  CE2 TYR A 513     -28.271   6.257   9.699  1.00 97.05
ATOM   4003  CZ  TYR A 513     -27.805   4.929   9.786  1.00 97.05
ATOM   4004  OH  TYR A 513     -28.610   3.904   9.404  1.00 97.05
ATOM   4005  N   LYS A 514     -25.237   6.921  13.837  1.00 95.93
ATOM   4006  CA  LYS A 514     -25.558   5.818  14.747  1.00 95.93
ATOM   4007  C   LYS A 514     -26.180   6.337  16.038  1.00 95.93
ATOM   4008  O   LYS A 514     -27.192   5.797  16.474  1.00 95.93
ATOM   4009  CB  LYS A 514     -24.289   4.988  15.016  1.00 95.93
ATOM   4010  CG  LYS A 514     -24.528   3.732  15.873  1.00 95.93
ATOM   4011  CD  LYS A 514     -25.463   2.714  15.200  1.00 95.93
ATOM   4012  CE  LYS A 514     -25.529   1.435  16.045  1.00 95.93
ATOM   4013  NZ  LYS A 514     -26.282   0.347  15.368  1.00 95.93
ATOM   4014  N   PHE A 515     -25.616   7.394  16.618  1.00 94.46
ATOM   4015  CA  PHE A 515     -26.127   7.989  17.849  1.00 94.46
ATOM   4016  C   PHE A 515     -27.532   8.590  17.671  1.00 94.46
ATOM   4017  O   PHE A 515     -28.409   8.387  18.512  1.00 94.46
ATOM   4018  CB  PHE A 515     -25.121   9.036  18.338  1.00 94.46
ATOM   4019  CG  PHE A 515     -25.405   9.488  19.750  1.00 94.46
ATOM   4020  CD1 PHE A 515     -26.151  10.658  19.992  1.00 94.46
ATOM   4021  CD2 PHE A 515     -24.959   8.700  20.826  1.00 94.46
ATOM   4022  CE1 PHE A 515     -26.462  11.027  21.313  1.00 94.46
ATOM   4023  CE2 PHE A 515     -25.269   9.070  22.142  1.00 94.46
ATOM   4024  CZ  PHE A 515     -26.030  10.223  22.383  1.00 94.46
ATOM   4025  N   CYS A 516     -27.781   9.279  16.553  1.00 95.04
ATOM   4026  CA  CYS A 516     -29.092   9.848  16.235  1.00 95.04
ATOM   4027  C   CYS A 516     -30.145   8.777  15.914  1.00 95.04
ATOM   4028  O   CYS A 516     -31.308   8.957  16.267  1.00 95.04
ATOM   4029  CB  CYS A 516     -28.932  10.839  15.077  1.00 95.04
ATOM   4030  SG  CYS A 516     -28.054  12.313  15.673  1.00 95.04
ATOM   4031  N   SER A 517     -29.740   7.662  15.300  1.00 94.51
ATOM   4032  CA  SER A 517     -30.643   6.570  14.904  1.00 94.51
ATOM   4033  C   SER A 517     -31.086   5.680  16.067  1.00 94.51
ATOM   4034  O   SER A 517     -32.090   4.979  15.954  1.00 94.51
ATOM   4035  CB  SER A 517     -29.975   5.690  13.845  1.00 94.51
ATOM   4036  OG  SER A 517     -29.622   6.452  12.711  1.00 94.51
ATOM   4037  N   LEU A 518     -30.350   5.671  17.183  1.00 93.61
ATOM   4038  CA  LEU A 518     -30.715   4.878  18.357  1.00 93.61
ATOM   4039  C   LEU A 518     -31.872   5.543  19.132  1.00 93.61
ATOM   4040  O   LEU A 518     -31.821   6.755  19.379  1.00 93.61
ATOM   4041  CB  LEU A 518     -29.478   4.651  19.244  1.00 93.61
ATOM   4042  CG  LEU A 518     -28.477   3.638  18.656  1.00 93.61
ATOM   4043  CD1 LEU A 518     -27.155   3.718  19.415  1.00 93.61
ATOM   4044  CD2 LEU A 518     -28.985   2.196  18.734  1.00 93.61
ATOM   4045  N   PRO A 519     -32.908   4.785  19.537  1.00 90.94
ATOM   4046  CA  PRO A 519     -33.964   5.283  20.414  1.00 90.94
ATOM   4047  C   PRO A 519     -33.477   5.385  21.870  1.00 90.94
ATOM   4048  O   PRO A 519     -32.426   4.853  22.224  1.00 90.94
ATOM   4049  CB  PRO A 519     -35.112   4.283  20.246  1.00 90.94
ATOM   4050  CG  PRO A 519     -34.382   2.962  20.008  1.00 90.94
ATOM   4051  CD  PRO A 519     -33.148   3.382  19.211  1.00 90.94
ATOM   4052  N   GLY A 520     -34.256   6.062  22.715  1.00 91.58
ATOM   4053  CA  GLY A 520     -34.010   6.127  24.160  1.00 91.58
ATOM   4054  C   GLY A 520     -33.323   7.404  24.647  1.00 91.58
ATOM   4055  O   GLY A 520     -33.107   8.364  23.896  1.00 91.58
ATOM   4056  N   SER A 521     -33.010   7.424  25.941  1.00 92.90
ATOM   4057  CA  SER A 521     -32.308   8.524  26.608  1.00 92.90
ATOM   4058  C   SER A 521     -30.857   8.655  26.126  1.00 92.90
ATOM   4059  O   SER A 521     -30.285   7.720  25.571  1.00 92.90
ATOM   4060  CB  SER A 521     -32.382   8.346  28.131  1.00 92.90
ATOM   4061  OG  SER A 521     -31.592   7.262  28.582  1.00 92.90
ATOM   4062  N   PHE A 522     -30.209   9.804  26.365  1.00 93.31
ATOM   4063  CA  PHE A 522     -28.796  10.003  25.993  1.00 93.31
ATOM   4064  C   PHE A 522     -27.888   8.878  26.525  1.00 93.31
ATOM   4065  O   PHE A 522     -27.004   8.398  25.818  1.00 93.31
ATOM   4066  CB  PHE A 522     -28.319  11.369  26.516  1.00 93.31
ATOM   4067  CG  PHE A 522     -26.882  11.703  26.151  1.00 93.31
ATOM   4068  CD1 PHE A 522     -25.816  11.257  26.959  1.00 93.31
ATOM   4069  CD2 PHE A 522     -26.604  12.444  24.987  1.00 93.31
ATOM   4070  CE1 PHE A 522     -24.486  11.521  26.588  1.00 93.31
ATOM   4071  CE2 PHE A 522     -25.273  12.704  24.614  1.00 93.31
ATOM   4072  CZ  PHE A 522     -24.214  12.236  25.410  1.00 93.31
ATOM   4073  N   ARG A 523     -28.136   8.426  27.763  1.00 92.18
ATOM   4074  CA  ARG A 523     -27.365   7.358  28.409  1.00 92.18
ATOM   4075  C   ARG A 523     -27.616   5.990  27.773  1.00 92.18
ATOM   4076  O   ARG A 523     -26.658   5.248  27.585  1.00 92.18
ATOM   4077  CB  ARG A 523     -27.677   7.360  29.912  1.00 92.18
ATOM   4078  CG  ARG A 523     -26.777   6.387  30.685  1.00 92.18
ATOM   4079  CD  ARG A 523     -27.096   6.449  32.180  1.00 92.18
ATOM   4080  NE  ARG A 523     -26.260   5.506  32.945  1.00 92.18
ATOM   4081  CZ  ARG A 523     -26.397   5.210  34.226  1.00 92.18
ATOM   4082  NH1 ARG A 523     -27.297   5.786  34.975  1.00 92.18
ATOM   4083  NH2 ARG A 523     -25.628   4.317  34.781  1.00 92.18
ATOM   4084  N   GLU A 524     -28.863   5.671  27.429  1.00 92.63
ATOM   4085  CA  GLU A 524     -29.217   4.432  26.717  1.00 92.63
ATOM   4086  C   GLU A 524     -28.591   4.406  25.324  1.00 92.63
ATOM   4087  O   GLU A 524     -27.898   3.451  24.978  1.00 92.63
ATOM   4088  CB  GLU A 524     -30.739   4.326  26.583  1.00 92.63
ATOM   4089  CG  GLU A 524     -31.427   3.957  27.903  1.00 92.63
ATOM   4090  CD  GLU A 524     -32.859   4.498  27.969  1.00 92.63
ATOM   4091  OE1 GLU A 524     -33.245   4.881  29.092  1.00 92.63
ATOM   4092  OE2 GLU A 524     -33.471   4.779  26.915  1.00 92.63
ATOM   4093  N   LYS A 525     -28.740   5.495  24.558  1.00 94.17
ATOM   4094  CA  LYS A 525     -28.112   5.645  23.239  1.00 94.17
ATOM   4095  C   LYS A 525     -26.609   5.423  23.319  1.00 94.17
ATOM   4096  O   LYS A 525     -26.065   4.650  22.538  1.00 94.17
ATOM   4097  CB  LYS A 525     -28.386   7.040  22.666  1.00 94.17
ATOM   4098  CG  LYS A 525     -29.853   7.250  22.282  1.00 94.17
ATOM   4099  CD  LYS A 525     -30.022   8.681  21.767  1.00 94.17
ATOM   4100  CE  LYS A 525     -31.492   8.972  21.460  1.00 94.17
ATOM   4101  NZ  LYS A 525     -31.668   9.437  20.067  1.00 94.17
ATOM   4102  N   LEU A 526     -25.943   6.063  24.283  1.00 94.69
ATOM   4103  CA  LEU A 526     -24.507   5.901  24.481  1.00 94.69
ATOM   4104  C   LEU A 526     -24.142   4.450  24.816  1.00 94.69
ATOM   4105  O   LEU A 526     -23.193   3.932  24.237  1.00 94.69
ATOM   4106  CB  LEU A 526     -24.029   6.888  25.561  1.00 94.69
ATOM   4107  CG  LEU A 526     -22.508   6.859  25.794  1.00 94.69
ATOM   4108  CD1 LEU A 526     -21.713   7.258  24.549  1.00 94.69
ATOM   4109  CD2 LEU A 526     -22.146   7.826  26.922  1.00 94.69
ATOM   4110  N   ALA A 527     -24.904   3.786  25.691  1.00 94.10
ATOM   4111  CA  ALA A 527     -24.674   2.393  26.065  1.00 94.10
ATOM   4112  C   ALA A 527     -24.738   1.448  24.856  1.00 94.10
ATOM   4113  O   ALA A 527     -23.786   0.709  24.619  1.00 94.10
ATOM   4114  CB  ALA A 527     -25.688   1.989  27.136  1.00 94.10
ATOM   4115  N   TYR A 528     -25.800   1.521  24.046  1.00 94.24
ATOM   4116  CA  TYR A 528     -25.932   0.698  22.835  1.00 94.24
ATOM   4117  C   TYR A 528     -24.922   1.058  21.739  1.00 94.24
ATOM   4118  O   TYR A 528     -24.625   0.230  20.880  1.00 94.24
ATOM   4119  CB  TYR A 528     -27.345   0.835  22.257  1.00 94.24
ATOM   4120  CG  TYR A 528     -28.433   0.177  23.075  1.00 94.24
ATOM   4121  CD1 TYR A 528     -28.504  -1.229  23.171  1.00 94.24
ATOM   4122  CD2 TYR A 528     -29.396   0.975  23.714  1.00 94.24
ATOM   4123  CE1 TYR A 528     -29.536  -1.833  23.920  1.00 94.24
ATOM   4124  CE2 TYR A 528     -30.417   0.379  24.465  1.00 94.24
ATOM   4125  CZ  TYR A 528     -30.493  -1.020  24.568  1.00 94.24
ATOM   4126  OH  TYR A 528     -31.511  -1.533  25.292  1.00 94.24
ATOM   4127  N   ALA A 529     -24.419   2.294  21.726  1.00 95.06
ATOM   4128  CA  ALA A 529     -23.470   2.751  20.721  1.00 95.06
ATOM   4129  C   ALA A 529     -22.036   2.264  20.998  1.00 95.06
ATOM   4130  O   ALA A 529     -21.318   1.954  20.050  1.00 95.06
ATOM   4131  CB  ALA A 529     -23.576   4.278  20.624  1.00 95.06
ATOM   4132  N   ILE A 530     -21.613   2.189  22.265  1.00 95.55
ATOM   4133  CA  ILE A 530     -20.235   1.809  22.641  1.00 95.55
ATOM   4134  C   ILE A 530     -20.087   0.345  23.065  1.00 95.55
ATOM   4135  O   ILE A 530     -18.971  -0.172  23.061  1.00 95.55
ATOM   4136  CB  ILE A 530     -19.670   2.741  23.734  1.00 95.55
ATOM   4137  CG1 ILE A 530     -20.351   2.500  25.103  1.00 95.55
ATOM   4138  CG2 ILE A 530     -19.713   4.204  23.259  1.00 95.55
ATOM   4139  CD1 ILE A 530     -19.979   3.515  26.187  1.00 95.55
ATOM   4140  N   ALA A 531     -21.173  -0.314  23.475  1.00 94.84
ATOM   4141  CA  ALA A 531     -21.128  -1.712  23.880  1.00 94.84
ATOM   4142  C   ALA A 531     -21.109  -2.646  22.655  1.00 94.84
ATOM   4143  O   ALA A 531     -21.783  -2.363  21.660  1.00 94.84
ATOM   4144  CB  ALA A 531     -22.301  -2.024  24.813  1.00 94.84
ATOM   4145  N   PRO A 532     -20.389  -3.781  22.724  1.00 94.86
ATOM   4146  CA  PRO A 532     -20.437  -4.810  21.694  1.00 94.86
ATOM   4147  C   PRO A 532     -21.867  -5.287  21.446  1.00 94.86
ATOM   4148  O   PRO A 532     -22.641  -5.454  22.386  1.00 94.86
ATOM   4149  CB  PRO A 532     -19.583  -5.969  22.220  1.00 94.86
ATOM   4150  CG  PRO A 532     -18.655  -5.307  23.227  1.00 94.86
ATOM   4151  CD  PRO A 532     -19.482  -4.166  23.790  1.00 94.86
ATOM   4152  N   GLU A 533     -22.214  -5.616  20.203  1.00 93.70
ATOM   4153  CA  GLU A 533     -23.564  -6.101  19.888  1.00 93.70
ATOM   4154  C   GLU A 533     -23.903  -7.421  20.593  1.00 93.70
ATOM   4155  O   GLU A 533     -25.057  -7.644  20.955  1.00 93.70
ATOM   4156  CB  GLU A 533     -23.762  -6.246  18.376  1.00 93.70
ATOM   4157  CG  GLU A 533     -23.629  -4.893  17.669  1.00 93.70
ATOM   4158  CD  GLU A 533     -24.247  -4.881  16.271  1.00 93.70
ATOM   4159  OE1 GLU A 533     -24.755  -3.787  15.912  1.00 93.70
ATOM   4160  OE2 GLU A 533     -24.342  -5.949  15.639  1.00 93.70
ATOM   4161  N   LYS A 534     -22.891  -8.255  20.864  1.00 92.58
ATOM   4162  CA  LYS A 534     -23.034  -9.480  21.667  1.00 92.58
ATOM   4163  C   LYS A 534     -23.421  -9.217  23.129  1.00 92.58
ATOM   4164  O   LYS A 534     -23.977 -10.100  23.768  1.00 92.58
ATOM   4165  CB  LYS A 534     -21.759 -10.340  21.571  1.00 92.58
ATOM   4166  CG  LYS A 534     -20.502  -9.671  22.160  1.00 92.58
ATOM   4167  CD  LYS A 534     -19.292 -10.619  22.174  1.00 92.58
ATOM   4168  CE  LYS A 534     -18.077  -9.913  22.794  1.00 92.58
ATOM   4169  NZ  LYS A 534     -16.840 -10.742  22.747  1.00 92.58
ATOM   4170  N   ASP A 535     -23.162  -8.013  23.638  1.00 92.84
ATOM   4171  CA  ASP A 535     -23.442  -7.618  25.021  1.00 92.84
ATOM   4172  C   ASP A 535     -24.782  -6.860  25.145  1.00 92.84
ATOM   4173  O   ASP A 535     -25.091  -6.343  26.217  1.00 92.84
ATOM   4174  CB  ASP A 535     -22.255  -6.812  25.599  1.00 92.84
ATOM   4175  CG  ASP A 535     -20.946  -7.596  25.810  1.00 92.84
ATOM   4176  OD1 ASP A 535     -20.934  -8.843  25.705  1.00 92.84
ATOM   4177  OD2 ASP A 535     -19.921  -6.939  26.113  1.00 92.84
ATOM   4178  N   ARG A 536     -25.611  -6.788  24.087  1.00 90.02
ATOM   4179  CA  ARG A 536     -26.901  -6.061  24.116  1.00 90.02
ATOM   4180  C   ARG A 536     -27.823  -6.517  25.246  1.00 90.02
ATOM   4181  O   ARG A 536     -28.386  -5.674  25.930  1.00 90.02
ATOM   4182  CB  ARG A 536     -27.627  -6.176  22.768  1.00 90.02
ATOM   4183  CG  ARG A 536     -27.062  -5.201  21.726  1.00 90.02
ATOM   4184  CD  ARG A 536     -27.807  -5.389  20.401  1.00 90.02
ATOM   4185  NE  ARG A 536     -27.272  -4.546  19.307  1.00 90.02
ATOM   4186  CZ  ARG A 536     -27.835  -4.408  18.118  1.00 90.02
ATOM   4187  NH1 ARG A 536     -29.025  -4.886  17.872  1.00 90.02
ATOM   4188  NH2 ARG A 536     -27.235  -3.813  17.125  1.00 90.02
ATOM   4189  N   GLU A 537     -27.890  -7.818  25.518  1.00 90.87
ATOM   4190  CA  GLU A 537     -28.684  -8.345  26.636  1.00 90.87
ATOM   4191  C   GLU A 537     -28.190  -7.854  28.009  1.00 90.87
ATOM   4192  O   GLU A 537     -28.980  -7.723  28.942  1.00 90.87
ATOM   4193  CB  GLU A 537     -28.629  -9.878  26.641  1.00 90.87
ATOM   4194  CG  GLU A 537     -29.235 -10.541  25.395  1.00 90.87
ATOM   4195  CD  GLU A 537     -29.237 -12.077  25.493  1.00 90.87
ATOM   4196  OE1 GLU A 537     -29.716 -12.711  24.528  1.00 90.87
ATOM   4197  OE2 GLU A 537     -28.788 -12.616  26.536  1.00 90.87
ATOM   4198  N   LEU A 538     -26.887  -7.579  28.156  1.00 91.01
ATOM   4199  CA  LEU A 538     -26.323  -6.990  29.375  1.00 91.01
ATOM   4200  C   LEU A 538     -26.689  -5.506  29.472  1.00 91.01
ATOM   4201  O   LEU A 538     -27.070  -5.039  30.544  1.00 91.01
ATOM   4202  CB  LEU A 538     -24.793  -7.174  29.417  1.00 91.01
ATOM   4203  CG  LEU A 538     -24.304  -8.631  29.421  1.00 91.01
ATOM   4204  CD1 LEU A 538     -22.775  -8.663  29.357  1.00 91.01
ATOM   4205  CD2 LEU A 538     -24.743  -9.374  30.686  1.00 91.01
ATOM   4206  N   VAL A 539     -26.651  -4.784  28.347  1.00 91.31
ATOM   4207  CA  VAL A 539     -27.094  -3.384  28.270  1.00 91.31
ATOM   4208  C   VAL A 539     -28.570  -3.254  28.654  1.00 91.31
ATOM   4209  O   VAL A 539     -28.903  -2.376  29.448  1.00 91.31
ATOM   4210  CB  VAL A 539     -26.841  -2.782  26.873  1.00 91.31
ATOM   4211  CG1 VAL A 539     -27.325  -1.329  26.797  1.00 91.31
ATOM   4212  CG2 VAL A 539     -25.348  -2.795  26.518  1.00 91.31
ATOM   4213  N   ASP A 540     -29.426  -4.164  28.184  1.00 90.14
ATOM   4214  CA  ASP A 540     -30.855  -4.208  28.530  1.00 90.14
ATOM   4215  C   ASP A 540     -31.081  -4.433  30.036  1.00 90.14
ATOM   4216  O   ASP A 540     -32.040  -3.926  30.617  1.00 90.14
ATOM   4217  CB  ASP A 540     -31.550  -5.330  27.735  1.00 90.14
ATOM   4218  CG  ASP A 540     -31.543  -5.146  26.212  1.00 90.14
ATOM   4219  OD1 ASP A 540     -31.379  -3.998  25.744  1.00 90.14
ATOM   4220  OD2 ASP A 540     -31.723  -6.159  25.504  1.00 90.14
ATOM   4221  N   ARG A 541     -30.164  -5.151  30.700  1.00 90.66
ATOM   4222  CA  ARG A 541     -30.143  -5.341  32.164  1.00 90.66
ATOM   4223  C   ARG A 541     -29.509  -4.167  32.922  1.00 90.66
ATOM   4224  O   ARG A 541     -29.424  -4.208  34.147  1.00 90.66
ATOM   4225  CB  ARG A 541     -29.439  -6.665  32.504  1.00 90.66
ATOM   4226  CG  ARG A 541     -30.217  -7.887  31.999  1.00 90.66
ATOM   4227  CD  ARG A 541     -29.377  -9.149  32.208  1.00 90.66
ATOM   4228  NE  ARG A 541     -29.948 -10.298  31.483  1.00 90.66
ATOM   4229  CZ  ARG A 541     -29.554 -11.553  31.584  1.00 90.66
ATOM   4230  NH1 ARG A 541     -28.659 -11.920  32.462  1.00 90.66
ATOM   4231  NH2 ARG A 541     -30.038 -12.461  30.785  1.00 90.66
ATOM   4232  N   GLY A 542     -29.056  -3.125  32.223  1.00 87.55
ATOM   4233  CA  GLY A 542     -28.365  -1.966  32.796  1.00 87.55
ATOM   4234  C   GLY A 542     -26.875  -2.192  33.089  1.00 87.55
ATOM   4235  O   GLY A 542     -26.223  -1.323  33.675  1.00 87.55
ATOM   4236  N   GLU A 543     -26.310  -3.326  32.674  1.00 89.61
ATOM   4237  CA  GLU A 543     -24.910  -3.692  32.883  1.00 89.61
ATOM   4238  C   GLU A 543     -24.042  -3.260  31.694  1.00 89.61
ATOM   4239  O   GLU A 543     -23.829  -3.997  30.733  1.00 89.61
ATOM   4240  CB  GLU A 543     -24.767  -5.196  33.151  1.00 89.61
ATOM   4241  CG  GLU A 543     -25.376  -5.635  34.490  1.00 89.61
ATOM   4242  CD  GLU A 543     -25.127  -7.125  34.785  1.00 89.61
ATOM   4243  OE1 GLU A 543     -25.838  -7.668  35.659  1.00 89.61
ATOM   4244  OE2 GLU A 543     -24.206  -7.716  34.172  1.00 89.61
ATOM   4245  N   VAL A 544     -23.483  -2.052  31.778  1.00 91.25
ATOM   4246  CA  VAL A 544     -22.600  -1.498  30.740  1.00 91.25
ATOM   4247  C   VAL A 544     -21.175  -1.413  31.274  1.00 91.25
ATOM   4248  O   VAL A 544     -20.842  -0.530  32.070  1.00 91.25
ATOM   4249  CB  VAL A 544     -23.099  -0.129  30.255  1.00 91.25
ATOM   4250  CG1 VAL A 544     -22.289   0.350  29.041  1.00 91.25
ATOM   4251  CG2 VAL A 544     -24.583  -0.152  29.875  1.00 91.25
ATOM   4252  N   ARG A 545     -20.297  -2.316  30.826  1.00 90.11
ATOM   4253  CA  ARG A 545     -18.897  -2.382  31.290  1.00 90.11
ATOM   4254  C   ARG A 545     -18.147  -1.074  31.040  1.00 90.11
ATOM   4255  O   ARG A 545     -17.403  -0.625  31.909  1.00 90.11
ATOM   4256  CB  ARG A 545     -18.166  -3.538  30.599  1.00 90.11
ATOM   4257  CG  ARG A 545     -18.755  -4.907  30.967  1.00 90.11
ATOM   4258  CD  ARG A 545     -17.999  -5.994  30.203  1.00 90.11
ATOM   4259  NE  ARG A 545     -18.580  -7.331  30.421  1.00 90.11
ATOM   4260  CZ  ARG A 545     -18.134  -8.441  29.860  1.00 90.11
ATOM   4261  NH1 ARG A 545     -17.056  -8.431  29.128  1.00 90.11
ATOM   4262  NH2 ARG A 545     -18.763  -9.568  30.027  1.00 90.11
ATOM   4263  N   GLN A 546     -18.408  -0.429  29.907  1.00 92.25
ATOM   4264  CA  GLN A 546     -17.810   0.837  29.482  1.00 92.25
ATOM   4265  C   GLN A 546     -18.186   2.015  30.394  1.00 92.25
ATOM   4266  O   GLN A 546     -17.500   3.032  30.389  1.00 92.25
ATOM   4267  CB  GLN A 546     -18.225   1.154  28.034  1.00 92.25
ATOM   4268  CG  GLN A 546     -17.699   0.180  26.964  1.00 92.25
ATOM   4269  CD  GLN A 546     -18.429  -1.160  26.880  1.00 92.25
ATOM   4270  OE1 GLN A 546     -19.411  -1.433  27.558  1.00 92.25
ATOM   4271  NE2 GLN A 546     -17.939  -2.065  26.070  1.00 92.25
ATOM   4272  N   PHE A 547     -19.228   1.899  31.223  1.00 92.07
ATOM   4273  CA  PHE A 547     -19.539   2.905  32.247  1.00 92.07
ATOM   4274  C   PHE A 547     -18.758   2.695  33.549  1.00 92.07
ATOM   4275  O   PHE A 547     -18.829   3.526  34.452  1.00 92.07
ATOM   4276  CB  PHE A 547     -21.056   2.961  32.477  1.00 92.07
ATOM   4277  CG  PHE A 547     -21.905   3.437  31.307  1.00 92.07
ATOM   4278  CD1 PHE A 547     -21.346   4.116  30.201  1.00 92.07
ATOM   4279  CD2 PHE A 547     -23.296   3.221  31.345  1.00 92.07
ATOM   4280  CE1 PHE A 547     -22.166   4.562  29.153  1.00 92.07
ATOM   4281  CE2 PHE A 547     -24.117   3.668  30.294  1.00 92.07
ATOM   4282  CZ  PHE A 547     -23.551   4.341  29.199  1.00 92.07
ATOM   4283  N   THR A 548     -17.986   1.612  33.665  1.00 91.08
ATOM   4284  CA  THR A 548     -17.180   1.325  34.854  1.00 91.08
ATOM   4285  C   THR A 548     -15.746   1.814  34.682  1.00 91.08
ATOM   4286  O   THR A 548     -15.092   1.557  33.674  1.00 91.08
ATOM   4287  CB  THR A 548     -17.212  -0.160  35.253  1.00 91.08
ATOM   4288  OG1 THR A 548     -16.448  -0.968  34.390  1.00 91.08
ATOM   4289  CG2 THR A 548     -18.626  -0.733  35.329  1.00 91.08
ATOM   4290  N   LEU A 549     -15.198   2.455  35.714  1.00 88.90
ATOM   4291  CA  LEU A 549     -13.807   2.928  35.714  1.00 88.90
ATOM   4292  C   LEU A 549     -12.799   1.764  35.596  1.00 88.90
ATOM   4293  O   LEU A 549     -11.728   1.904  35.007  1.00 88.90
ATOM   4294  CB  LEU A 549     -13.644   3.789  36.978  1.00 88.90
ATOM   4295  CG  LEU A 549     -12.380   4.666  36.995  1.00 88.90
ATOM   4296  CD1 LEU A 549     -12.667   6.001  37.680  1.00 88.90
ATOM   4297  CD2 LEU A 549     -11.266   3.992  37.781  1.00 88.90
ATOM   4298  N   ARG A 550     -13.183   0.574  36.080  1.00 90.39
ATOM   4299  CA  ARG A 550     -12.398  -0.663  35.962  1.00 90.39
ATOM   4300  C   ARG A 550     -12.134  -1.053  34.506  1.00 90.39
ATOM   4301  O   ARG A 550     -11.042  -1.538  34.225  1.00 90.39
ATOM   4302  CB  ARG A 550     -13.121  -1.790  36.716  1.00 90.39
ATOM   4303  CG  ARG A 550     -12.268  -3.066  36.818  1.00 90.39
ATOM   4304  CD  ARG A 550     -13.019  -4.149  37.601  1.00 90.39
ATOM   4305  NE  ARG A 550     -12.197  -5.363  37.776  1.00 90.39
ATOM   4306  CZ  ARG A 550     -12.605  -6.507  38.302  1.00 90.39
ATOM   4307  NH1 ARG A 550     -13.833  -6.686  38.702  1.00 90.39
ATOM   4308  NH2 ARG A 550     -11.775  -7.503  38.442  1.00 90.39
ATOM   4309  N   HIS A 551     -13.096  -0.849  33.603  1.00 91.38
ATOM   4310  CA  HIS A 551     -12.937  -1.136  32.172  1.00 91.38
ATOM   4311  C   HIS A 551     -11.783  -0.333  31.573  1.00 91.38
ATOM   4312  O   HIS A 551     -10.847  -0.903  31.019  1.00 91.38
ATOM   4313  CB  HIS A 551     -14.257  -0.839  31.454  1.00 91.38
ATOM   4314  CG  HIS A 551     -14.174  -1.011  29.966  1.00 91.38
ATOM   4315  ND1 HIS A 551     -14.166  -2.242  29.315  1.00 91.38
ATOM   4316  CD2 HIS A 551     -14.051  -0.009  29.049  1.00 91.38
ATOM   4317  CE1 HIS A 551     -14.051  -1.950  28.008  1.00 91.38
ATOM   4318  NE2 HIS A 551     -13.967  -0.623  27.822  1.00 91.38
ATOM   4319  N   TRP A 552     -11.794   0.979  31.798  1.00 90.80
ATOM   4320  CA  TRP A 552     -10.800   1.896  31.246  1.00 90.80
ATOM   4321  C   TRP A 552      -9.416   1.751  31.889  1.00 90.80
ATOM   4322  O   TRP A 552      -8.410   1.993  31.229  1.00 90.80
ATOM   4323  CB  TRP A 552     -11.336   3.320  31.379  1.00 90.80
ATOM   4324  CG  TRP A 552     -12.662   3.538  30.716  1.00 90.80
ATOM   4325  CD1 TRP A 552     -13.862   3.565  31.338  1.00 90.80
ATOM   4326  CD2 TRP A 552     -12.951   3.758  29.299  1.00 90.80
ATOM   4327  NE1 TRP A 552     -14.854   3.801  30.411  1.00 90.80
ATOM   4328  CE2 TRP A 552     -14.349   3.973  29.147  1.00 90.80
ATOM   4329  CE3 TRP A 552     -12.185   3.775  28.120  1.00 90.80
ATOM   4330  CZ2 TRP A 552     -14.951   4.254  27.913  1.00 90.80
ATOM   4331  CZ3 TRP A 552     -12.766   4.111  26.879  1.00 90.80
ATOM   4332  CH2 TRP A 552     -14.142   4.350  26.773  1.00 90.80
ATOM   4333  N   LEU A 553      -9.318   1.300  33.146  1.00 88.88
ATOM   4334  CA  LEU A 553      -8.027   1.091  33.817  1.00 88.88
ATOM   4335  C   LEU A 553      -7.393  -0.288  33.572  1.00 88.88
ATOM   4336  O   LEU A 553      -6.170  -0.397  33.627  1.00 88.88
ATOM   4337  CB  LEU A 553      -8.159   1.365  35.322  1.00 88.88
ATOM   4338  CG  LEU A 553      -8.393   2.835  35.723  1.00 88.88
ATOM   4339  CD1 LEU A 553      -8.220   2.923  37.240  1.00 88.88
ATOM   4340  CD2 LEU A 553      -7.399   3.816  35.098  1.00 88.88
ATOM   4341  N   LYS A 554      -8.167  -1.330  33.243  1.00 86.43
ATOM   4342  CA  LYS A 554      -7.657  -2.707  33.075  1.00 86.43
ATOM   4343  C   LYS A 554      -6.661  -2.825  31.910  1.00 86.43
ATOM   4344  O   LYS A 554      -6.958  -2.357  30.812  1.00 86.43
ATOM   4345  CB  LYS A 554      -8.860  -3.650  32.903  1.00 86.43
ATOM   4346  CG  LYS A 554      -8.496  -5.142  32.921  1.00 86.43
ATOM   4347  CD  LYS A 554      -9.767  -5.997  32.785  1.00 86.43
ATOM   4348  CE  LYS A 554      -9.428  -7.496  32.774  1.00 86.43
ATOM   4349  NZ  LYS A 554     -10.605  -8.336  32.408  1.00 86.43
ATOM   4350  N   VAL A 555      -5.501  -3.446  32.147  1.00 83.85
ATOM   4351  CA  VAL A 555      -4.473  -3.763  31.131  1.00 83.85
ATOM   4352  C   VAL A 555      -4.404  -5.263  30.902  1.00 83.85
ATOM   4353  O   VAL A 555      -4.322  -6.035  31.886  1.00 83.85
ATOM   4354  CB  VAL A 555      -3.095  -3.173  31.477  1.00 83.85
ATOM   4355  CG1 VAL A 555      -2.092  -3.412  30.340  1.00 83.85
ATOM   4356  CG2 VAL A 555      -3.191  -1.660  31.704  1.00 83.85
ATOM   4357  OXT VAL A 556      -4.495  -5.629  29.718  1.00 83.85
TER    4358      VAL A 556                                        
SPDBVT        1.0000000000         0.0000000000         0.0000000000 
SPDBVT        0.0000000000         1.0000000000         0.0000000000 
SPDBVT        0.0000000000         0.0000000000         1.0000000000 
SPDBVT        0.0000000000         0.0000000000         0.0000000000 
SPDBVT        0.0000000000         0.0000000000         0.0000000000 
SPDBVV default;
SPDBVV      3.838868499155    1701.384545885313      20.000000000000
SPDBVV        0.5806471330         0.7512275168         0.3138568542 
SPDBVV       -0.8070907181         0.4804446156         0.3431873308 
SPDBVV        0.1070209305        -0.4525816936         0.8852775447 
SPDBVV      -14.2880001068       -25.0025005341         2.2639999390 
SPDBVV        0.0000000000         0.0000000000         0.0000000000 
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48
SPDBVf 48 48 48 48 48 48 48 48 48 48 48 48 48 48 48 16
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVb 0.00 0.00 0.00
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64
SPDBVi        1 1 1 0 1 0 1 1 0 1 0 1 1 0  0
SPDBVp     9606
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: April 25th, 2023.