HEADER    MEMBRANE PROTEIN                        21-FEB-24   8S4D              
TITLE     CRYSTAL STRUCTURE OF A PEPTIDERGIC GPCR IN COMPLEX WITH A SMALL       
TITLE    2 SYNTHETIC G PROTEIN-BIASED AGONIST                                   
KEYWDS    RECEPTOR, GPCR, STABILISED, MEMBRANE PROTEIN                          
EXPDTA    X-RAY DIFFRACTION                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.58 ANGSTROMS.                                       
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
DBREF  8S4D A    7  1001  UNP    P35414   APJ_HUMAN        7    229             
DBREF  8S4D A 1002  1101  UNP    A7ZVB5   A7ZVB5_ECO24    24    123             
DBREF  8S4D A  235   324  UNP    P35414   APJ_HUMAN      235    324             
SEQRES   1 A  497  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 A  497  VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP LYS PHE ASP          
SEQRES   3 A  497  ASN TYR TYR GLY ALA ASP ASN GLN SER GLU CYS GLU TYR          
SEQRES   4 A  497  THR ASP TRP LYS SER SER GLY ALA LEU ILE PRO ALA ILE          
SEQRES   5 A  497  TYR MET LEU VAL PHE LEU LEU GLY THR THR GLY ASN GLY          
SEQRES   6 A  497  LEU VAL LEU TRP THR VAL PHE ARG SER SER ARG GLU LYS          
SEQRES   7 A  497  ARG ARG SER ALA ASP ILE PHE ILE ALA SER LEU ALA VAL          
SEQRES   8 A  497  ALA ASP LEU THR PHE VAL VAL THR LEU PRO LEU TRP ALA          
SEQRES   9 A  497  VAL TYR THR TYR ARG ASP TYR ASP TRP PRO PHE GLY THR          
SEQRES  10 A  497  PHE PHE CYS LYS LEU SER SER TYR LEU ILE PHE VAL ALA          
SEQRES  11 A  497  MET TYR ALA SER VAL PHE CYS LEU THR GLY LEU SER PHE          
SEQRES  12 A  497  ASP ARG TYR LEU ALA ILE VAL ARG PRO VAL ALA ASN ALA          
SEQRES  13 A  497  ARG LEU ARG LEU ARG VAL SER GLY ALA VAL ALA THR ALA          
SEQRES  14 A  497  VAL LEU TRP VAL LEU ALA ALA LEU LEU ALA MET PRO VAL          
SEQRES  15 A  497  MET VAL LEU ARG THR THR GLY ASP LEU GLU ASN THR ASN          
SEQRES  16 A  497  LYS VAL GLN CYS TYR MET ASP TYR SER MET VAL ALA THR          
SEQRES  17 A  497  VAL SER SER GLU TRP ALA TRP GLU VAL GLY LEU GLY VAL          
SEQRES  18 A  497  SER SER THR MET VAL GLY PHE VAL VAL PRO LEU THR ILE          
SEQRES  19 A  497  MET LEU THR CYS TYR PHE PHE ALA ALA GLN THR ILE ALA          
SEQRES  20 A  497  ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU          
SEQRES  21 A  497  LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS          
SEQRES  22 A  497  ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA          
SEQRES  23 A  497  GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO          
SEQRES  24 A  497  ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP          
SEQRES  25 A  497  ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA          
SEQRES  26 A  497  ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU          
SEQRES  27 A  497  GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR          
SEQRES  28 A  497  LEU GLU ARG ILE GLU GLY LEU ARG LYS ARG ARG ARG LEU          
SEQRES  29 A  497  LEU SER ILE ILE VAL VAL LEU VAL VAL THR PHE ALA LEU          
SEQRES  30 A  497  CYS TRP MET PRO TYR HIS LEU VAL LYS THR LEU TYR MET          
SEQRES  31 A  497  LEU GLY SER LEU LEU HIS TRP PRO CYS ASP PHE ASP LEU          
SEQRES  32 A  497  PHE LEU MET ASN ILE PHE PRO TYR CYS THR CYS ILE ALA          
SEQRES  33 A  497  TYR VAL ASN SER CYS LEU ASN PRO PHE LEU TYR ALA PHE          
SEQRES  34 A  497  PHE ASP PRO ARG PHE ARG GLN ALA CYS THR SER MET LEU          
SEQRES  35 A  497  LEU MET GLY GLN SER ARG LEU GLU VAL LEU PHE GLN GLY          
SEQRES  36 A  497  PRO ALA SER ALA TRP SER HIS PRO GLN PHE GLU LYS GLY          
SEQRES  37 A  497  SER ALA GLY SER ALA ALA GLY SER ALA SER ALA TRP SER          
SEQRES  38 A  497  HIS PRO GLN PHE GLU LYS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  39 A  497  HIS HIS HIS                                                  
HET    A1D5N  A1201      32                                                     
HET    OLA  A1202      20                                                       
HET    OLA  A1203      16                                                       
HET    OLA  A1204       8                                                       
HET    OLA  A1205       8                                                       
HET    OLA  A1206       8                                                       
HET    OLA  A1207       7                                                       
HET    1PE  A1208       6                                                       
HELIX    1   1 ALA A   29  PHE A   54  1                                  26    
HELIX    2   2 ALA A   64  THR A   81  1                                  18    
HELIX    3   3 THR A   81  ARG A   91  1                                  11    
HELIX    4   4 PHE A   97  ARG A  133  1                                  37    
HELIX    5   5 ARG A  141  ALA A  161  1                                  21    
HELIX    6   6 ALA A  161  LEU A  167  1                                   7    
HELIX    7   7 TYR A  185  VAL A  188  5                                   4    
HELIX    8   8 THR A  190  SER A  192  5                                   3    
HELIX    9   9 SER A  193  PHE A  210  1                                  18    
HELIX   10  10 PHE A  210  ALA A 1020  1                                  39    
HELIX   11  11 ASN A 1022  ALA A 1043  1                                  22    
HELIX   12  12 SER A 1055  GLU A 1081  1                                  27    
HELIX   13  13 LYS A 1083  GLU A 1092  1                                  10    
HELIX   14  14 GLN A 1093  LYS A 1095  5                                   3    
HELIX   15  15 THR A 1096  GLU A  238  1                                  15    
HELIX   16  16 GLY A  239  LEU A  277  1                                  39    
HELIX   17  17 PRO A  280  ASP A  313  1                                  34    
HELIX   18  18 ASP A  313  LEU A  324  1                                  12    
SHEET    1 AA1 2 ARG A 168  GLY A 171  0                                        
SHEET    2 AA1 2 GLN A 180  MET A 183 -1  O  TYR A 182   N  THR A 169           
SSBOND   1 CYS A  102    CYS A  181                          1555   1555  2.05  
CRYST1   65.823  153.948  111.646  90.00  90.00  90.00 C 2 2 21      8          
ATOM      1  N   ALA A  29     -17.300 -26.385  15.207  1.00 61.60           N  
ANISOU    1  N   ALA A  29     6351   7905   9149   -168    902   -792       N  
ATOM      2  CA  ALA A  29     -18.111 -27.254  16.070  1.00 61.72           C  
ANISOU    2  CA  ALA A  29     6335   8023   9091   -253   1008   -831       C  
ATOM      3  C   ALA A  29     -18.543 -28.576  15.382  1.00 61.02           C  
ANISOU    3  C   ALA A  29     6306   7890   8988   -253    996   -713       C  
ATOM      4  O   ALA A  29     -18.690 -29.605  16.060  1.00 61.00           O  
ANISOU    4  O   ALA A  29     6335   7975   8868   -328   1080   -668       O  
ATOM      5  CB  ALA A  29     -19.324 -26.499  16.595  1.00 62.01           C  
ANISOU    5  CB  ALA A  29     6224   8078   9260   -286   1067  -1042       C  
ATOM      6  N   LEU A  30     -18.717 -28.552  14.035  1.00 59.79           N  
ANISOU    6  N   LEU A  30     6172   7601   8947   -172    891   -657       N  
ATOM      7  CA  LEU A  30     -19.085 -29.758  13.296  1.00 58.76           C  
ANISOU    7  CA  LEU A  30     6090   7424   8813   -165    871   -557       C  
ATOM      8  C   LEU A  30     -17.846 -30.578  12.992  1.00 57.45           C  
ANISOU    8  C   LEU A  30     6054   7266   8509   -154    840   -377       C  
ATOM      9  O   LEU A  30     -17.834 -31.777  13.261  1.00 57.63           O  
ANISOU    9  O   LEU A  30     6124   7328   8446   -200    887   -296       O  
ATOM     10  CB  LEU A  30     -19.830 -29.423  11.992  1.00 59.14           C  
ANISOU   10  CB  LEU A  30     6099   7337   9032    -86    769   -587       C  
ATOM     11  CG  LEU A  30     -20.173 -30.635  11.113  1.00 61.14           C  
ANISOU   11  CG  LEU A  30     6400   7542   9288    -71    736   -491       C  
ATOM     12  CD1 LEU A  30     -21.028 -31.653  11.863  1.00 61.88           C  
ANISOU   12  CD1 LEU A  30     6458   7703   9352   -155    848   -522       C  
ATOM     13  CD2 LEU A  30     -20.878 -30.220   9.855  1.00 62.08           C  
ANISOU   13  CD2 LEU A  30     6480   7542   9564      9    626   -530       C  
ATOM     14  N   ILE A  31     -16.813 -29.925  12.418  1.00 55.88           N  
ANISOU   14  N   ILE A  31     5908   7021   8303    -96    761   -321       N  
ATOM     15  CA  ILE A  31     -15.543 -30.529  12.033  1.00 54.58           C  
ANISOU   15  CA  ILE A  31     5853   6855   8031    -77    721   -174       C  
ATOM     16  C   ILE A  31     -14.838 -31.235  13.204  1.00 53.12           C  
ANISOU   16  C   ILE A  31     5714   6788   7682   -138    791   -118       C  
ATOM     17  O   ILE A  31     -14.462 -32.391  13.016  1.00 53.02           O  
ANISOU   17  O   ILE A  31     5771   6777   7600   -147    786     -3       O  
ATOM     18  CB  ILE A  31     -14.646 -29.486  11.314  1.00 54.97           C  
ANISOU   18  CB  ILE A  31     5932   6837   8116    -17    640   -159       C  
ATOM     19  CG1 ILE A  31     -15.165 -29.206   9.902  1.00 55.69           C  
ANISOU   19  CG1 ILE A  31     6027   6804   8329     45    550   -144       C  
ATOM     20  CG2 ILE A  31     -13.174 -29.882  11.285  1.00 55.48           C  
ANISOU   20  CG2 ILE A  31     6087   6934   8060    -14    625    -51       C  
ATOM     21  CD1 ILE A  31     -15.189 -30.352   9.026  1.00 56.61           C  
ANISOU   21  CD1 ILE A  31     6198   6891   8421     55    521    -47       C  
ATOM     22  N   PRO A  32     -14.694 -30.648  14.420  1.00 51.90           N  
ANISOU   22  N   PRO A  32     5523   6733   7462   -183    853   -196       N  
ATOM     23  CA  PRO A  32     -14.041 -31.399  15.510  1.00 51.37           C  
ANISOU   23  CA  PRO A  32     5512   6782   7223   -240    906   -128       C  
ATOM     24  C   PRO A  32     -14.688 -32.765  15.777  1.00 51.16           C  
ANISOU   24  C   PRO A  32     5518   6776   7144   -296    960    -56       C  
ATOM     25  O   PRO A  32     -13.979 -33.734  16.029  1.00 51.50           O  
ANISOU   25  O   PRO A  32     5645   6846   7076   -309    953     69       O  
ATOM     26  CB  PRO A  32     -14.170 -30.472  16.723  1.00 51.82           C  
ANISOU   26  CB  PRO A  32     5503   6949   7239   -288    975   -259       C  
ATOM     27  CG  PRO A  32     -14.408 -29.139  16.174  1.00 52.33           C  
ANISOU   27  CG  PRO A  32     5483   6941   7458   -243    942   -383       C  
ATOM     28  CD  PRO A  32     -15.091 -29.296  14.861  1.00 51.00           C  
ANISOU   28  CD  PRO A  32     5315   6632   7429   -183    872   -351       C  
ATOM     29  N   ALA A  33     -16.024 -32.859  15.672  1.00 50.30           N  
ANISOU   29  N   ALA A  33     5340   6642   7131   -325   1009   -135       N  
ATOM     30  CA  ALA A  33     -16.722 -34.121  15.902  1.00 49.76           C  
ANISOU   30  CA  ALA A  33     5292   6583   7030   -387   1073    -79       C  
ATOM     31  C   ALA A  33     -16.312 -35.154  14.857  1.00 48.86           C  
ANISOU   31  C   ALA A  33     5253   6378   6934   -340   1003     61       C  
ATOM     32  O   ALA A  33     -16.008 -36.291  15.206  1.00 48.93           O  
ANISOU   32  O   ALA A  33     5333   6407   6852   -378   1027    175       O  
ATOM     33  CB  ALA A  33     -18.233 -33.908  15.893  1.00 49.72           C  
ANISOU   33  CB  ALA A  33     5181   6560   7152   -421   1135   -218       C  
ATOM     34  N   ILE A  34     -16.230 -34.742  13.598  1.00 47.93           N  
ANISOU   34  N   ILE A  34     5123   6161   6927   -259    913     55       N  
ATOM     35  CA  ILE A  34     -15.829 -35.628  12.522  1.00 47.64           C  
ANISOU   35  CA  ILE A  34     5146   6043   6914   -215    846    165       C  
ATOM     36  C   ILE A  34     -14.384 -36.034  12.693  1.00 47.54           C  
ANISOU   36  C   ILE A  34     5222   6055   6786   -198    807    281       C  
ATOM     37  O   ILE A  34     -14.074 -37.210  12.547  1.00 47.63           O  
ANISOU   37  O   ILE A  34     5289   6043   6765   -203    796    385       O  
ATOM     38  CB  ILE A  34     -16.057 -34.945  11.185  1.00 48.03           C  
ANISOU   38  CB  ILE A  34     5162   5995   7091   -139    760    121       C  
ATOM     39  CG1 ILE A  34     -17.535 -34.563  11.021  1.00 49.15           C  
ANISOU   39  CG1 ILE A  34     5205   6108   7362   -146    784     -6       C  
ATOM     40  CG2 ILE A  34     -15.584 -35.833  10.070  1.00 48.32           C  
ANISOU   40  CG2 ILE A  34     5257   5963   7140   -100    696    221       C  
ATOM     41  CD1 ILE A  34     -17.749 -33.334  10.140  1.00 50.66           C  
ANISOU   41  CD1 ILE A  34     5353   6232   7664    -77    703    -83       C  
ATOM     42  N   TYR A  35     -13.510 -35.083  13.058  1.00 47.23           N  
ANISOU   42  N   TYR A  35     5189   6061   6696   -179    786    253       N  
ATOM     43  CA  TYR A  35     -12.095 -35.352  13.319  1.00 47.62           C  
ANISOU   43  CA  TYR A  35     5309   6143   6640   -163    747    341       C  
ATOM     44  C   TYR A  35     -11.908 -36.361  14.457  1.00 48.69           C  
ANISOU   44  C   TYR A  35     5495   6356   6648   -222    795    420       C  
ATOM     45  O   TYR A  35     -10.974 -37.158  14.441  1.00 48.94           O  
ANISOU   45  O   TYR A  35     5593   6382   6619   -205    752    525       O  
ATOM     46  CB  TYR A  35     -11.318 -34.048  13.609  1.00 47.16           C  
ANISOU   46  CB  TYR A  35     5234   6124   6562   -138    726    274       C  
ATOM     47  CG  TYR A  35     -10.889 -33.264  12.383  1.00 47.31           C  
ANISOU   47  CG  TYR A  35     5249   6053   6674    -74    655    255       C  
ATOM     48  CD1 TYR A  35     -11.074 -33.774  11.105  1.00 48.01           C  
ANISOU   48  CD1 TYR A  35     5359   6048   6834    -40    607    306       C  
ATOM     49  CD2 TYR A  35     -10.271 -32.027  12.504  1.00 48.01           C  
ANISOU   49  CD2 TYR A  35     5314   6150   6776    -54    640    186       C  
ATOM     50  CE1 TYR A  35     -10.694 -33.060   9.979  1.00 48.81           C  
ANISOU   50  CE1 TYR A  35     5468   6074   7003      7    546    296       C  
ATOM     51  CE2 TYR A  35      -9.877 -31.306  11.383  1.00 48.82           C  
ANISOU   51  CE2 TYR A  35     5425   6165   6959     -7    582    180       C  
ATOM     52  CZ  TYR A  35     -10.095 -31.828  10.119  1.00 49.87           C  
ANISOU   52  CZ  TYR A  35     5589   6212   7146     22    535    240       C  
ATOM     53  OH  TYR A  35      -9.709 -31.160   8.981  1.00 51.66           O  
ANISOU   53  OH  TYR A  35     5838   6359   7432     59    479    246       O  
ATOM     54  N   MET A  36     -12.799 -36.327  15.438  1.00 49.16           N  
ANISOU   54  N   MET A  36     5523   6485   6670   -293    883    370       N  
ATOM     55  CA  MET A  36     -12.754 -37.248  16.551  1.00 49.95           C  
ANISOU   55  CA  MET A  36     5679   6661   6638   -362    936    450       C  
ATOM     56  C   MET A  36     -13.251 -38.607  16.154  1.00 50.47           C  
ANISOU   56  C   MET A  36     5784   6656   6736   -383    947    548       C  
ATOM     57  O   MET A  36     -12.639 -39.603  16.516  1.00 50.88           O  
ANISOU   57  O   MET A  36     5915   6711   6706   -394    925    674       O  
ATOM     58  CB  MET A  36     -13.527 -36.686  17.748  1.00 50.68           C  
ANISOU   58  CB  MET A  36     5723   6863   6668   -445   1039    349       C  
ATOM     59  CG  MET A  36     -12.774 -35.593  18.464  1.00 52.85           C  
ANISOU   59  CG  MET A  36     5983   7237   6861   -438   1030    279       C  
ATOM     60  SD  MET A  36     -11.115 -36.119  18.955  1.00 57.96           S  
ANISOU   60  SD  MET A  36     6735   7932   7355   -408    950    416       S  
ATOM     61  CE  MET A  36     -10.641 -34.761  19.934  1.00 59.64           C  
ANISOU   61  CE  MET A  36     6896   8254   7512   -402    953    286       C  
ATOM     62  N   LEU A  37     -14.335 -38.651  15.384  1.00 50.31           N  
ANISOU   62  N   LEU A  37     5704   6566   6846   -385    973    488       N  
ATOM     63  CA  LEU A  37     -14.921 -39.881  14.893  1.00 50.57           C  
ANISOU   63  CA  LEU A  37     5751   6520   6944   -403    988    552       C  
ATOM     64  C   LEU A  37     -13.926 -40.653  14.028  1.00 50.35           C  
ANISOU   64  C   LEU A  37     5784   6414   6931   -339    894    667       C  
ATOM     65  O   LEU A  37     -13.760 -41.853  14.251  1.00 50.31           O  
ANISOU   65  O   LEU A  37     5839   6386   6890   -368    902    779       O  
ATOM     66  CB  LEU A  37     -16.186 -39.552  14.096  1.00 51.09           C  
ANISOU   66  CB  LEU A  37     5723   6525   7164   -388   1002    433       C  
ATOM     67  CG  LEU A  37     -16.948 -40.736  13.538  1.00 53.19           C  
ANISOU   67  CG  LEU A  37     5975   6715   7519   -412   1031    458       C  
ATOM     68  CD1 LEU A  37     -17.365 -41.703  14.648  1.00 53.85           C  
ANISOU   68  CD1 LEU A  37     6087   6846   7529   -520   1142    501       C  
ATOM     69  CD2 LEU A  37     -18.168 -40.267  12.771  1.00 54.12           C  
ANISOU   69  CD2 LEU A  37     5991   6782   7788   -387   1028    322       C  
ATOM     70  N   VAL A  38     -13.232 -39.958  13.075  1.00 49.98           N  
ANISOU   70  N   VAL A  38     5726   6328   6937   -257    808    639       N  
ATOM     71  CA  VAL A  38     -12.220 -40.565  12.180  1.00 49.88           C  
ANISOU   71  CA  VAL A  38     5756   6249   6947   -196    720    718       C  
ATOM     72  C   VAL A  38     -10.969 -40.993  12.952  1.00 49.29           C  
ANISOU   72  C   VAL A  38     5752   6219   6758   -194    688    812       C  
ATOM     73  O   VAL A  38     -10.316 -41.951  12.562  1.00 49.09           O  
ANISOU   73  O   VAL A  38     5766   6139   6745   -171    639    897       O  
ATOM     74  CB  VAL A  38     -11.867 -39.714  10.923  1.00 50.70           C  
ANISOU   74  CB  VAL A  38     5832   6304   7127   -125    650    659       C  
ATOM     75  CG1 VAL A  38     -11.364 -38.341  11.301  1.00 51.35           C  
ANISOU   75  CG1 VAL A  38     5899   6444   7169   -110    643    590       C  
ATOM     76  CG2 VAL A  38     -10.832 -40.408  10.050  1.00 51.29           C  
ANISOU   76  CG2 VAL A  38     5948   6325   7215    -79    577    728       C  
ATOM     77  N   PHE A  39     -10.666 -40.315  14.064  1.00 48.87           N  
ANISOU   77  N   PHE A  39     5708   6264   6597   -218    712    789       N  
ATOM     78  CA  PHE A  39      -9.553 -40.674  14.924  1.00 49.08           C  
ANISOU   78  CA  PHE A  39     5799   6347   6502   -217    675    870       C  
ATOM     79  C   PHE A  39      -9.816 -42.062  15.570  1.00 50.53           C  
ANISOU   79  C   PHE A  39     6047   6516   6637   -268    698    995       C  
ATOM     80  O   PHE A  39      -8.960 -42.948  15.485  1.00 50.87           O  
ANISOU   80  O   PHE A  39     6142   6514   6672   -236    629   1094       O  
ATOM     81  CB  PHE A  39      -9.323 -39.580  15.991  1.00 47.92           C  
ANISOU   81  CB  PHE A  39     5639   6322   6248   -242    706    800       C  
ATOM     82  CG  PHE A  39      -8.343 -40.006  17.043  1.00 47.17           C  
ANISOU   82  CG  PHE A  39     5612   6299   6011   -248    668    885       C  
ATOM     83  CD1 PHE A  39      -7.018 -40.209  16.729  1.00 47.41           C  
ANISOU   83  CD1 PHE A  39     5670   6302   6041   -181    570    929       C  
ATOM     84  CD2 PHE A  39      -8.766 -40.313  18.315  1.00 47.53           C  
ANISOU   84  CD2 PHE A  39     5699   6434   5928   -323    726    927       C  
ATOM     85  CE1 PHE A  39      -6.129 -40.656  17.675  1.00 47.84           C  
ANISOU   85  CE1 PHE A  39     5785   6415   5977   -177    518   1007       C  
ATOM     86  CE2 PHE A  39      -7.876 -40.769  19.259  1.00 48.08           C  
ANISOU   86  CE2 PHE A  39     5842   6565   5862   -325    675   1020       C  
ATOM     87  CZ  PHE A  39      -6.561 -40.941  18.932  1.00 47.77           C  
ANISOU   87  CZ  PHE A  39     5824   6493   5833   -246    564   1060       C  
ATOM     88  N   LEU A  40     -11.002 -42.249  16.191  1.00 50.99           N  
ANISOU   88  N   LEU A  40     6097   6603   6675   -350    797    985       N  
ATOM     89  CA  LEU A  40     -11.377 -43.508  16.836  1.00 51.84           C  
ANISOU   89  CA  LEU A  40     6269   6690   6737   -415    837   1103       C  
ATOM     90  C   LEU A  40     -11.475 -44.635  15.828  1.00 52.69           C  
ANISOU   90  C   LEU A  40     6379   6663   6977   -384    801   1163       C  
ATOM     91  O   LEU A  40     -10.813 -45.650  16.017  1.00 53.12           O  
ANISOU   91  O   LEU A  40     6500   6671   7013   -370    745   1285       O  
ATOM     92  CB  LEU A  40     -12.682 -43.359  17.617  1.00 52.26           C  
ANISOU   92  CB  LEU A  40     6301   6805   6752   -518    967   1053       C  
ATOM     93  CG  LEU A  40     -12.676 -42.221  18.630  1.00 54.08           C  
ANISOU   93  CG  LEU A  40     6512   7176   6860   -557   1013    968       C  
ATOM     94  CD1 LEU A  40     -14.068 -41.970  19.197  1.00 54.37           C  
ANISOU   94  CD1 LEU A  40     6497   7266   6896   -657   1149    874       C  
ATOM     95  CD2 LEU A  40     -11.613 -42.445  19.714  1.00 54.90           C  
ANISOU   95  CD2 LEU A  40     6709   7365   6784   -567    969   1072       C  
ATOM     96  N   LEU A  41     -12.228 -44.431  14.721  1.00 52.80           N  
ANISOU   96  N   LEU A  41     6317   6614   7131   -366    821   1072       N  
ATOM     97  CA  LEU A  41     -12.398 -45.393  13.615  1.00 53.10           C  
ANISOU   97  CA  LEU A  41     6338   6532   7307   -335    789   1097       C  
ATOM     98  C   LEU A  41     -11.060 -45.741  12.956  1.00 53.55           C  
ANISOU   98  C   LEU A  41     6422   6537   7388   -255    678   1150       C  
ATOM     99  O   LEU A  41     -10.812 -46.894  12.602  1.00 53.56           O  
ANISOU   99  O   LEU A  41     6445   6452   7454   -245    646   1225       O  
ATOM    100  CB  LEU A  41     -13.318 -44.792  12.540  1.00 52.92           C  
ANISOU  100  CB  LEU A  41     6225   6478   7405   -313    806    967       C  
ATOM    101  CG  LEU A  41     -14.651 -45.452  12.385  1.00 54.02           C  
ANISOU  101  CG  LEU A  41     6323   6569   7635   -369    884    938       C  
ATOM    102  CD1 LEU A  41     -15.590 -45.027  13.506  1.00 54.79           C  
ANISOU  102  CD1 LEU A  41     6406   6748   7665   -458    995    893       C  
ATOM    103  CD2 LEU A  41     -15.234 -45.152  11.026  1.00 54.39           C  
ANISOU  103  CD2 LEU A  41     6290   6559   7817   -318    852    833       C  
ATOM    104  N   GLY A  42     -10.232 -44.724  12.779  1.00 53.68           N  
ANISOU  104  N   GLY A  42     6428   6602   7364   -203    625   1099       N  
ATOM    105  CA  GLY A  42      -8.934 -44.851  12.151  1.00 54.58           C  
ANISOU  105  CA  GLY A  42     6555   6680   7502   -132    528   1120       C  
ATOM    106  C   GLY A  42      -7.952 -45.662  12.962  1.00 55.25           C  
ANISOU  106  C   GLY A  42     6708   6770   7514   -124    474   1233       C  
ATOM    107  O   GLY A  42      -7.349 -46.599  12.427  1.00 55.77           O  
ANISOU  107  O   GLY A  42     6785   6755   7650    -87    410   1283       O  
ATOM    108  N   THR A  43      -7.783 -45.331  14.254  1.00 54.87           N  
ANISOU  108  N   THR A  43     6705   6815   7330   -159    493   1268       N  
ATOM    109  CA  THR A  43      -6.810 -46.051  15.071  1.00 54.97           C  
ANISOU  109  CA  THR A  43     6789   6838   7261   -145    424   1379       C  
ATOM    110  C   THR A  43      -7.308 -47.414  15.526  1.00 54.82           C  
ANISOU  110  C   THR A  43     6830   6749   7250   -192    439   1511       C  
ATOM    111  O   THR A  43      -6.480 -48.313  15.689  1.00 55.05           O  
ANISOU  111  O   THR A  43     6907   6724   7287   -157    354   1609       O  
ATOM    112  CB  THR A  43      -6.285 -45.215  16.213  1.00 56.38           C  
ANISOU  112  CB  THR A  43     6993   7145   7284   -158    422   1366       C  
ATOM    113  OG1 THR A  43      -7.384 -44.592  16.875  1.00 57.75           O  
ANISOU  113  OG1 THR A  43     7159   7392   7390   -238    532   1327       O  
ATOM    114  CG2 THR A  43      -5.281 -44.179  15.743  1.00 56.79           C  
ANISOU  114  CG2 THR A  43     6995   7237   7346    -96    375   1258       C  
ATOM    115  N   THR A  44      -8.632 -47.599  15.698  1.00 54.16           N  
ANISOU  115  N   THR A  44     6740   6657   7180   -269    545   1510       N  
ATOM    116  CA  THR A  44      -9.139 -48.909  16.120  1.00 54.00           C  
ANISOU  116  CA  THR A  44     6780   6563   7175   -326    575   1636       C  
ATOM    117  C   THR A  44      -9.159 -49.877  14.938  1.00 52.47           C  
ANISOU  117  C   THR A  44     6549   6224   7163   -287    538   1644       C  
ATOM    118  O   THR A  44      -8.703 -51.010  15.065  1.00 52.13           O  
ANISOU  118  O   THR A  44     6557   6093   7158   -274    481   1758       O  
ATOM    119  CB  THR A  44     -10.473 -48.793  16.872  1.00 56.36           C  
ANISOU  119  CB  THR A  44     7086   6917   7410   -437    712   1626       C  
ATOM    120  OG1 THR A  44     -11.381 -48.017  16.090  1.00 58.42           O  
ANISOU  120  OG1 THR A  44     7249   7187   7762   -438    776   1476       O  
ATOM    121  CG2 THR A  44     -10.316 -48.161  18.266  1.00 56.56           C  
ANISOU  121  CG2 THR A  44     7168   7088   7233   -489    742   1648       C  
ATOM    122  N   GLY A  45      -9.622 -49.400  13.793  1.00 51.68           N  
ANISOU  122  N   GLY A  45     6361   6100   7173   -262    562   1521       N  
ATOM    123  CA  GLY A  45      -9.660 -50.191  12.570  1.00 51.85           C  
ANISOU  123  CA  GLY A  45     6335   6004   7363   -224    531   1499       C  
ATOM    124  C   GLY A  45      -8.276 -50.570  12.065  1.00 51.84           C  
ANISOU  124  C   GLY A  45     6336   5952   7408   -141    411   1521       C  
ATOM    125  O   GLY A  45      -7.995 -51.753  11.862  1.00 52.02           O  
ANISOU  125  O   GLY A  45     6370   5869   7528   -127    369   1587       O  
ATOM    126  N   ASN A  46      -7.383 -49.576  11.877  1.00 51.18           N  
ANISOU  126  N   ASN A  46     6238   5940   7269    -87    358   1457       N  
ATOM    127  CA  ASN A  46      -6.021 -49.852  11.430  1.00 51.07           C  
ANISOU  127  CA  ASN A  46     6217   5890   7298    -13    251   1457       C  
ATOM    128  C   ASN A  46      -5.146 -50.482  12.507  1.00 52.47           C  
ANISOU  128  C   ASN A  46     6467   6059   7409      0    177   1580       C  
ATOM    129  O   ASN A  46      -4.158 -51.117  12.174  1.00 52.41           O  
ANISOU  129  O   ASN A  46     6453   5979   7483     55     86   1603       O  
ATOM    130  CB  ASN A  46      -5.375 -48.637  10.839  1.00 50.56           C  
ANISOU  130  CB  ASN A  46     6109   5895   7205     30    228   1344       C  
ATOM    131  CG  ASN A  46      -6.016 -48.262   9.543  1.00 51.87           C  
ANISOU  131  CG  ASN A  46     6211   6041   7457     31    268   1240       C  
ATOM    132  OD1 ASN A  46      -5.825 -48.920   8.510  1.00 52.70           O  
ANISOU  132  OD1 ASN A  46     6276   6070   7677     56    240   1209       O  
ATOM    133  ND2 ASN A  46      -6.796 -47.195   9.564  1.00 51.88           N  
ANISOU  133  ND2 ASN A  46     6197   6110   7407      5    329   1177       N  
ATOM    134  N   GLY A  47      -5.528 -50.341  13.774  1.00 53.66           N  
ANISOU  134  N   GLY A  47     6686   6283   7419    -52    214   1656       N  
ATOM    135  CA  GLY A  47      -4.850 -50.999  14.879  1.00 55.34           C  
ANISOU  135  CA  GLY A  47     6986   6492   7549    -49    143   1793       C  
ATOM    136  C   GLY A  47      -5.150 -52.487  14.863  1.00 57.25           C  
ANISOU  136  C   GLY A  47     7263   6595   7894    -67    128   1910       C  
ATOM    137  O   GLY A  47      -4.269 -53.302  15.141  1.00 57.44           O  
ANISOU  137  O   GLY A  47     7322   6546   7956    -18     19   1995       O  
ATOM    138  N   LEU A  48      -6.391 -52.853  14.499  1.00 58.59           N  
ANISOU  138  N   LEU A  48     7415   6717   8130   -133    234   1904       N  
ATOM    139  CA  LEU A  48      -6.829 -54.242  14.372  1.00 60.44           C  
ANISOU  139  CA  LEU A  48     7670   6808   8485   -161    240   1998       C  
ATOM    140  C   LEU A  48      -6.117 -54.936  13.185  1.00 62.22           C  
ANISOU  140  C   LEU A  48     7824   6913   8902    -81    154   1947       C  
ATOM    141  O   LEU A  48      -5.832 -56.133  13.255  1.00 62.51           O  
ANISOU  141  O   LEU A  48     7887   6823   9041    -71    101   2042       O  
ATOM    142  CB  LEU A  48      -8.346 -54.266  14.143  1.00 60.76           C  
ANISOU  142  CB  LEU A  48     7682   6841   8561   -248    382   1959       C  
ATOM    143  CG  LEU A  48      -9.176 -55.145  15.071  1.00 62.51           C  
ANISOU  143  CG  LEU A  48     7989   7020   8741   -347    456   2098       C  
ATOM    144  CD1 LEU A  48      -8.780 -56.608  14.957  1.00 63.19           C  
ANISOU  144  CD1 LEU A  48     8116   6943   8952   -328    383   2224       C  
ATOM    145  CD2 LEU A  48      -9.110 -54.651  16.502  1.00 63.33           C  
ANISOU  145  CD2 LEU A  48     8189   7251   8624   -399    477   2179       C  
ATOM    146  N   VAL A  49      -5.844 -54.189  12.100  1.00 63.14           N  
ANISOU  146  N   VAL A  49     7852   7069   9071    -31    145   1796       N  
ATOM    147  CA  VAL A  49      -5.170 -54.724  10.923  1.00 64.67           C  
ANISOU  147  CA  VAL A  49     7969   7173   9429     34     77   1722       C  
ATOM    148  C   VAL A  49      -3.719 -55.077  11.230  1.00 66.63           C  
ANISOU  148  C   VAL A  49     8236   7387   9692    108    -58   1766       C  
ATOM    149  O   VAL A  49      -3.260 -56.142  10.829  1.00 66.54           O  
ANISOU  149  O   VAL A  49     8197   7254   9832    144   -124   1782       O  
ATOM    150  CB  VAL A  49      -5.293 -53.768   9.719  1.00 65.29           C  
ANISOU  150  CB  VAL A  49     7961   7312   9534     54    111   1556       C  
ATOM    151  CG1 VAL A  49      -4.458 -54.248   8.537  1.00 65.86           C  
ANISOU  151  CG1 VAL A  49     7958   7317   9750    116     41   1469       C  
ATOM    152  CG2 VAL A  49      -6.745 -53.610   9.309  1.00 65.72           C  
ANISOU  152  CG2 VAL A  49     7985   7370   9616     -6    221   1510       C  
ATOM    153  N   LEU A  50      -3.008 -54.217  11.978  1.00 68.38           N  
ANISOU  153  N   LEU A  50     8499   7712   9769    131   -102   1781       N  
ATOM    154  CA  LEU A  50      -1.617 -54.493  12.351  1.00 70.60           C  
ANISOU  154  CA  LEU A  50     8794   7970  10063    205   -239   1814       C  
ATOM    155  C   LEU A  50      -1.497 -55.660  13.321  1.00 74.02           C  
ANISOU  155  C   LEU A  50     9313   8305  10508    203   -309   1989       C  
ATOM    156  O   LEU A  50      -0.526 -56.420  13.258  1.00 74.11           O  
ANISOU  156  O   LEU A  50     9308   8217  10635    269   -428   2012       O  
ATOM    157  CB  LEU A  50      -0.925 -53.263  12.935  1.00 70.12           C  
ANISOU  157  CB  LEU A  50     8750   8048   9843    227   -266   1776       C  
ATOM    158  CG  LEU A  50      -0.351 -52.281  11.942  1.00 71.09           C  
ANISOU  158  CG  LEU A  50     8790   8243   9979    251   -238   1608       C  
ATOM    159  CD1 LEU A  50       0.387 -51.201  12.653  1.00 71.62           C  
ANISOU  159  CD1 LEU A  50     8878   8439   9897    264   -258   1580       C  
ATOM    160  CD2 LEU A  50       0.595 -52.954  10.962  1.00 71.76           C  
ANISOU  160  CD2 LEU A  50     8792   8249  10225    315   -312   1516       C  
ATOM    161  N   TRP A  51      -2.496 -55.817  14.212  1.00 76.56           N  
ANISOU  161  N   TRP A  51     9725   8650  10713    122   -235   2111       N  
ATOM    162  CA  TRP A  51      -2.558 -56.920  15.164  1.00 79.51           C  
ANISOU  162  CA  TRP A  51    10202   8931  11078     99   -283   2300       C  
ATOM    163  C   TRP A  51      -2.629 -58.235  14.383  1.00 81.21           C  
ANISOU  163  C   TRP A  51    10374   8960  11523    116   -310   2319       C  
ATOM    164  O   TRP A  51      -1.912 -59.170  14.709  1.00 81.32           O  
ANISOU  164  O   TRP A  51    10424   8858  11616    162   -430   2420       O  
ATOM    165  CB  TRP A  51      -3.790 -56.771  16.079  1.00 80.69           C  
ANISOU  165  CB  TRP A  51    10441   9144  11073    -15   -158   2397       C  
ATOM    166  CG  TRP A  51      -3.839 -57.744  17.225  1.00 82.89           C  
ANISOU  166  CG  TRP A  51    10853   9358  11284    -54   -203   2610       C  
ATOM    167  CD1 TRP A  51      -4.001 -59.098  17.150  1.00 84.23           C  
ANISOU  167  CD1 TRP A  51    11059   9351  11594    -63   -237   2731       C  
ATOM    168  CD2 TRP A  51      -3.792 -57.424  18.626  1.00 83.81           C  
ANISOU  168  CD2 TRP A  51    11090   9585  11168    -98   -213   2730       C  
ATOM    169  NE1 TRP A  51      -4.004 -59.647  18.411  1.00 84.86           N  
ANISOU  169  NE1 TRP A  51    11284   9417  11543   -106   -277   2932       N  
ATOM    170  CE2 TRP A  51      -3.878 -58.641  19.337  1.00 84.84           C  
ANISOU  170  CE2 TRP A  51    11337   9597  11301   -131   -262   2936       C  
ATOM    171  CE3 TRP A  51      -3.665 -56.227  19.349  1.00 84.66           C  
ANISOU  171  CE3 TRP A  51    11218   9882  11067   -115   -187   2682       C  
ATOM    172  CZ2 TRP A  51      -3.830 -58.695  20.736  1.00 85.74           C  
ANISOU  172  CZ2 TRP A  51    11596   9784  11197   -181   -290   3100       C  
ATOM    173  CZ3 TRP A  51      -3.613 -56.284  20.732  1.00 85.69           C  
ANISOU  173  CZ3 TRP A  51    11480  10091  10988   -162   -212   2829       C  
ATOM    174  CH2 TRP A  51      -3.697 -57.505  21.411  1.00 85.90           C  
ANISOU  174  CH2 TRP A  51    11630  10005  11004   -197   -263   3039       C  
ATOM    175  N   THR A  52      -3.444 -58.279  13.318  1.00 82.54           N  
ANISOU  175  N   THR A  52    10454   9098  11808     88   -212   2204       N  
ATOM    176  CA  THR A  52      -3.604 -59.460  12.470  1.00 84.36           C  
ANISOU  176  CA  THR A  52    10624   9165  12265    100   -223   2187       C  
ATOM    177  C   THR A  52      -2.334 -59.795  11.658  1.00 86.20           C  
ANISOU  177  C   THR A  52    10769   9332  12651    204   -352   2093       C  
ATOM    178  O   THR A  52      -1.827 -60.918  11.774  1.00 86.23           O  
ANISOU  178  O   THR A  52    10782   9190  12791    242   -449   2170       O  
ATOM    179  CB  THR A  52      -4.853 -59.309  11.589  1.00 85.46           C  
ANISOU  179  CB  THR A  52    10692   9315  12464     39    -83   2079       C  
ATOM    180  OG1 THR A  52      -6.006 -59.459  12.418  1.00 86.12           O  
ANISOU  180  OG1 THR A  52    10855   9407  12459    -60     24   2186       O  
ATOM    181  CG2 THR A  52      -4.896 -60.319  10.441  1.00 85.87           C  
ANISOU  181  CG2 THR A  52    10646   9225  12755     64    -96   2001       C  
ATOM    182  N   VAL A  53      -1.819 -58.834  10.849  1.00 87.42           N  
ANISOU  182  N   VAL A  53    10840   9588  12788    245   -352   1925       N  
ATOM    183  CA  VAL A  53      -0.620 -59.057  10.027  1.00 88.98           C  
ANISOU  183  CA  VAL A  53    10943   9740  13123    330   -455   1809       C  
ATOM    184  C   VAL A  53       0.633 -59.366  10.872  1.00 90.74           C  
ANISOU  184  C   VAL A  53    11210   9931  13335    402   -609   1891       C  
ATOM    185  O   VAL A  53       1.605 -59.895  10.335  1.00 90.94           O  
ANISOU  185  O   VAL A  53    11158   9878  13515    473   -709   1816       O  
ATOM    186  CB  VAL A  53      -0.357 -57.933   8.999  1.00 89.41           C  
ANISOU  186  CB  VAL A  53    10910   9913  13151    345   -411   1619       C  
ATOM    187  CG1 VAL A  53      -1.588 -57.689   8.134  1.00 89.81           C  
ANISOU  187  CG1 VAL A  53    10913   9980  13229    286   -285   1537       C  
ATOM    188  CG2 VAL A  53       0.090 -56.652   9.687  1.00 89.86           C  
ANISOU  188  CG2 VAL A  53    11013  10122  13007    348   -410   1615       C  
ATOM    189  N   PHE A  54       0.596 -59.077  12.188  1.00 91.80           N  
ANISOU  189  N   PHE A  54    11462  10124  13293    384   -631   2038       N  
ATOM    190  CA  PHE A  54       1.674 -59.407  13.107  1.00 93.32           C  
ANISOU  190  CA  PHE A  54    11710  10288  13458    451   -788   2135       C  
ATOM    191  C   PHE A  54       1.175 -60.429  14.142  1.00 94.26           C  
ANISOU  191  C   PHE A  54    11956  10301  13558    414   -820   2361       C  
ATOM    192  O   PHE A  54       1.401 -60.272  15.341  1.00 94.37           O  
ANISOU  192  O   PHE A  54    12081  10367  13407    412   -879   2498       O  
ATOM    193  CB  PHE A  54       2.259 -58.150  13.759  1.00 93.79           C  
ANISOU  193  CB  PHE A  54    11794  10521  13320    471   -810   2096       C  
ATOM    194  CG  PHE A  54       3.318 -57.493  12.905  1.00 95.15           C  
ANISOU  194  CG  PHE A  54    11846  10742  13565    538   -851   1899       C  
ATOM    195  CD1 PHE A  54       2.968 -56.614  11.893  1.00 96.12           C  
ANISOU  195  CD1 PHE A  54    11881  10921  13719    508   -738   1737       C  
ATOM    196  CD2 PHE A  54       4.662 -57.773  13.098  1.00 96.34           C  
ANISOU  196  CD2 PHE A  54    11972  10881  13753    627  -1005   1873       C  
ATOM    197  CE1 PHE A  54       3.945 -56.017  11.098  1.00 96.94           C  
ANISOU  197  CE1 PHE A  54    11883  11070  13881    556   -764   1560       C  
ATOM    198  CE2 PHE A  54       5.638 -57.172  12.304  1.00 97.18           C  
ANISOU  198  CE2 PHE A  54    11962  11033  13928    677  -1028   1679       C  
ATOM    199  CZ  PHE A  54       5.273 -56.297  11.310  1.00 96.95           C  
ANISOU  199  CZ  PHE A  54    11855  11061  13920    636   -901   1527       C  
ATOM    200  N   ARG A  55       0.463 -61.465  13.659  1.00 94.80           N  
ANISOU  200  N   ARG A  55    12006  10222  13790    379   -773   2397       N  
ATOM    201  CA  ARG A  55      -0.070 -62.574  14.458  1.00 95.65           C  
ANISOU  201  CA  ARG A  55    12224  10194  13926    333   -787   2603       C  
ATOM    202  C   ARG A  55      -0.343 -63.802  13.566  1.00 95.88           C  
ANISOU  202  C   ARG A  55    12171  10030  14227    337   -779   2569       C  
ATOM    203  O   ARG A  55      -0.492 -63.686  12.346  1.00 95.83           O  
ANISOU  203  O   ARG A  55    12036  10031  14345    345   -717   2386       O  
ATOM    204  CB  ARG A  55      -1.342 -62.172  15.230  1.00 97.55           C  
ANISOU  204  CB  ARG A  55    12570  10526  13968    213   -636   2707       C  
ATOM    205  CG  ARG A  55      -1.591 -63.025  16.474  1.00101.80           C  
ANISOU  205  CG  ARG A  55    13268  10983  14429    163   -675   2956       C  
ATOM    206  CD  ARG A  55      -2.998 -62.855  17.045  1.00106.18           C  
ANISOU  206  CD  ARG A  55    13905  11595  14843     24   -496   3037       C  
ATOM    207  NE  ARG A  55      -3.990 -63.738  16.414  1.00110.04           N  
ANISOU  207  NE  ARG A  55    14356  11939  15516    -39   -394   3038       N  
ATOM    208  CZ  ARG A  55      -4.595 -64.756  17.029  1.00112.46           C  
ANISOU  208  CZ  ARG A  55    14766  12113  15853   -114   -368   3221       C  
ATOM    209  NH1 ARG A  55      -4.325 -65.027  18.301  1.00112.10           N  
ANISOU  209  NH1 ARG A  55    14878  12063  15653   -136   -440   3431       N  
ATOM    210  NH2 ARG A  55      -5.489 -65.495  16.382  1.00112.34           N  
ANISOU  210  NH2 ARG A  55    14697  11969  16017   -171   -267   3195       N  
ATOM    211  N   ARG A  62       2.761 -63.459   2.565  1.00 79.28           N  
ANISOU  211  N   ARG A  62     8874   7980  13268    542   -649    812       N  
ATOM    212  CA  ARG A  62       2.366 -63.188   1.181  1.00 79.50           C  
ANISOU  212  CA  ARG A  62     8812   8093  13302    496   -550    630       C  
ATOM    213  C   ARG A  62       3.174 -62.020   0.546  1.00 79.13           C  
ANISOU  213  C   ARG A  62     8732   8206  13126    497   -530    487       C  
ATOM    214  O   ARG A  62       3.929 -61.323   1.236  1.00 79.15           O  
ANISOU  214  O   ARG A  62     8784   8262  13029    530   -583    530       O  
ATOM    215  CB  ARG A  62       0.829 -62.999   1.020  1.00 80.97           C  
ANISOU  215  CB  ARG A  62     9048   8315  13401    425   -432    686       C  
ATOM    216  CG  ARG A  62       0.003 -62.870   2.303  1.00 84.13           C  
ANISOU  216  CG  ARG A  62     9589   8722  13653    400   -409    898       C  
ATOM    217  CD  ARG A  62      -1.480 -62.723   1.982  1.00 87.55           C  
ANISOU  217  CD  ARG A  62    10043   9188  14034    331   -291    912       C  
ATOM    218  NE  ARG A  62      -2.264 -62.235   3.122  1.00 90.34           N  
ANISOU  218  NE  ARG A  62    10523   9570  14234    295   -252   1088       N  
ATOM    219  CZ  ARG A  62      -2.907 -63.021   3.983  1.00 92.13           C  
ANISOU  219  CZ  ARG A  62    10808   9681  14515    268   -244   1236       C  
ATOM    220  NH1 ARG A  62      -2.866 -64.341   3.846  1.00 91.22           N  
ANISOU  220  NH1 ARG A  62    10639   9402  14617    279   -281   1238       N  
ATOM    221  NH2 ARG A  62      -3.592 -62.493   4.990  1.00 92.14           N  
ANISOU  221  NH2 ARG A  62    10922   9729  14358    225   -197   1380       N  
ATOM    222  N   SER A  63       3.044 -61.852  -0.789  1.00 78.51           N  
ANISOU  222  N   SER A  63     8570   8201  13060    458   -455    312       N  
ATOM    223  CA  SER A  63       3.749 -60.825  -1.564  1.00 78.00           C  
ANISOU  223  CA  SER A  63     8471   8279  12885    442   -420    166       C  
ATOM    224  C   SER A  63       3.202 -59.411  -1.296  1.00 76.43           C  
ANISOU  224  C   SER A  63     8380   8222  12437    404   -350    243       C  
ATOM    225  O   SER A  63       3.972 -58.501  -0.948  1.00 76.76           O  
ANISOU  225  O   SER A  63     8458   8341  12367    419   -369    245       O  
ATOM    226  CB  SER A  63       3.709 -61.154  -3.061  1.00 79.49           C  
ANISOU  226  CB  SER A  63     8540   8498  13166    405   -366    -40       C  
ATOM    227  OG  SER A  63       2.382 -61.224  -3.565  1.00 81.43           O  
ANISOU  227  OG  SER A  63     8786   8729  13423    363   -300    -26       O  
ATOM    228  N   ALA A  64       1.870 -59.237  -1.444  1.00 74.16           N  
ANISOU  228  N   ALA A  64     8138   7962  12077    358   -273    296       N  
ATOM    229  CA  ALA A  64       1.213 -57.956  -1.223  1.00 72.47           C  
ANISOU  229  CA  ALA A  64     8017   7867  11653    324   -209    361       C  
ATOM    230  C   ALA A  64       0.873 -57.699   0.232  1.00 70.36           C  
ANISOU  230  C   ALA A  64     7856   7580  11297    337   -229    548       C  
ATOM    231  O   ALA A  64       0.054 -56.824   0.487  1.00 70.43           O  
ANISOU  231  O   ALA A  64     7934   7654  11174    304   -169    616       O  
ATOM    232  CB  ALA A  64      -0.051 -57.868  -2.054  1.00 72.73           C  
ANISOU  232  CB  ALA A  64     8039   7933  11661    275   -130    322       C  
ATOM    233  N   ASP A  65       1.453 -58.451   1.186  1.00 68.45           N  
ANISOU  233  N   ASP A  65     7629   7252  11127    385   -316    630       N  
ATOM    234  CA  ASP A  65       1.169 -58.204   2.598  1.00 67.06           C  
ANISOU  234  CA  ASP A  65     7561   7070  10847    392   -339    809       C  
ATOM    235  C   ASP A  65       2.105 -57.168   3.236  1.00 63.99           C  
ANISOU  235  C   ASP A  65     7215   6775  10324    421   -379    819       C  
ATOM    236  O   ASP A  65       1.837 -56.707   4.347  1.00 64.10           O  
ANISOU  236  O   ASP A  65     7321   6822  10210    418   -385    949       O  
ATOM    237  CB  ASP A  65       1.106 -59.481   3.427  1.00 70.23           C  
ANISOU  237  CB  ASP A  65     7982   7320  11381    418   -407    932       C  
ATOM    238  CG  ASP A  65       0.021 -59.365   4.482  1.00 77.72           C  
ANISOU  238  CG  ASP A  65     9045   8270  12217    378   -364   1109       C  
ATOM    239  OD1 ASP A  65       0.295 -58.765   5.554  1.00 79.09           O  
ANISOU  239  OD1 ASP A  65     9303   8502  12245    388   -392   1209       O  
ATOM    240  OD2 ASP A  65      -1.123 -59.826   4.218  1.00 80.81           O  
ANISOU  240  OD2 ASP A  65     9435   8613  12656    331   -293   1135       O  
ATOM    241  N   ILE A  66       3.165 -56.743   2.518  1.00 61.00           N  
ANISOU  241  N   ILE A  66     6766   6449   9963    438   -395    670       N  
ATOM    242  CA  ILE A  66       4.030 -55.675   2.998  1.00 58.47           C  
ANISOU  242  CA  ILE A  66     6471   6226   9521    456   -417    650       C  
ATOM    243  C   ILE A  66       3.184 -54.394   2.911  1.00 56.46           C  
ANISOU  243  C   ILE A  66     6280   6086   9085    402   -317    672       C  
ATOM    244  O   ILE A  66       2.944 -53.755   3.928  1.00 56.25           O  
ANISOU  244  O   ILE A  66     6335   6103   8934    399   -313    782       O  
ATOM    245  CB  ILE A  66       5.344 -55.564   2.167  1.00 58.28           C  
ANISOU  245  CB  ILE A  66     6344   6224   9575    475   -442    466       C  
ATOM    246  CG1 ILE A  66       5.973 -56.937   1.851  1.00 58.95           C  
ANISOU  246  CG1 ILE A  66     6333   6184   9883    516   -519    397       C  
ATOM    247  CG2 ILE A  66       6.332 -54.636   2.837  1.00 58.46           C  
ANISOU  247  CG2 ILE A  66     6384   6322   9505    502   -481    448       C  
ATOM    248  CD1 ILE A  66       6.675 -57.654   3.016  1.00 59.82           C  
ANISOU  248  CD1 ILE A  66     6453   6194  10083    592   -656    489       C  
ATOM    249  N   PHE A  67       2.589 -54.144   1.729  1.00 55.02           N  
ANISOU  249  N   PHE A  67     6063   5938   8903    358   -239    581       N  
ATOM    250  CA  PHE A  67       1.738 -52.999   1.432  1.00 54.22           C  
ANISOU  250  CA  PHE A  67     6008   5929   8663    312   -155    582       C  
ATOM    251  C   PHE A  67       0.586 -52.851   2.378  1.00 53.68           C  
ANISOU  251  C   PHE A  67     6019   5862   8515    296   -126    721       C  
ATOM    252  O   PHE A  67       0.223 -51.722   2.690  1.00 54.30           O  
ANISOU  252  O   PHE A  67     6148   6024   8460    275    -84    741       O  
ATOM    253  CB  PHE A  67       1.186 -53.098   0.018  1.00 53.88           C  
ANISOU  253  CB  PHE A  67     5914   5892   8665    275   -100    481       C  
ATOM    254  CG  PHE A  67       2.259 -53.220  -1.025  1.00 54.41           C  
ANISOU  254  CG  PHE A  67     5903   5977   8794    274   -110    327       C  
ATOM    255  CD1 PHE A  67       3.179 -52.205  -1.215  1.00 54.97           C  
ANISOU  255  CD1 PHE A  67     5979   6132   8774    262    -94    259       C  
ATOM    256  CD2 PHE A  67       2.340 -54.343  -1.829  1.00 55.17           C  
ANISOU  256  CD2 PHE A  67     5913   6006   9044    277   -125    239       C  
ATOM    257  CE1 PHE A  67       4.155 -52.309  -2.186  1.00 55.67           C  
ANISOU  257  CE1 PHE A  67     5994   6243   8915    247    -87    107       C  
ATOM    258  CE2 PHE A  67       3.314 -54.443  -2.804  1.00 55.88           C  
ANISOU  258  CE2 PHE A  67     5923   6123   9187    265   -123     80       C  
ATOM    259  CZ  PHE A  67       4.213 -53.424  -2.979  1.00 55.63           C  
ANISOU  259  CZ  PHE A  67     5902   6181   9054    247   -100     15       C  
ATOM    260  N   ILE A  68      -0.014 -53.974   2.817  1.00 52.33           N  
ANISOU  260  N   ILE A  68     5856   5596   8430    299   -143    809       N  
ATOM    261  CA  ILE A  68      -1.149 -53.963   3.735  1.00 51.14           C  
ANISOU  261  CA  ILE A  68     5778   5442   8211    271   -104    937       C  
ATOM    262  C   ILE A  68      -0.686 -53.406   5.068  1.00 50.05           C  
ANISOU  262  C   ILE A  68     5712   5354   7952    286   -137   1029       C  
ATOM    263  O   ILE A  68      -1.297 -52.471   5.580  1.00 50.07           O  
ANISOU  263  O   ILE A  68     5764   5438   7824    257    -85   1060       O  
ATOM    264  CB  ILE A  68      -1.755 -55.383   3.893  1.00 51.34           C  
ANISOU  264  CB  ILE A  68     5795   5343   8368    262   -111   1008       C  
ATOM    265  CG1 ILE A  68      -2.377 -55.898   2.588  1.00 52.13           C  
ANISOU  265  CG1 ILE A  68     5821   5410   8575    239    -65    908       C  
ATOM    266  CG2 ILE A  68      -2.732 -55.444   5.057  1.00 51.74           C  
ANISOU  266  CG2 ILE A  68     5931   5387   8340    228    -75   1156       C  
ATOM    267  CD1 ILE A  68      -3.468 -55.083   2.068  1.00 53.52           C  
ANISOU  267  CD1 ILE A  68     6008   5667   8660    200     14    872       C  
ATOM    268  N   ALA A  69       0.419 -53.940   5.602  1.00 48.94           N  
ANISOU  268  N   ALA A  69     5570   5167   7858    333   -229   1062       N  
ATOM    269  CA  ALA A  69       0.930 -53.485   6.875  1.00 48.72           C  
ANISOU  269  CA  ALA A  69     5609   5189   7713    352   -275   1147       C  
ATOM    270  C   ALA A  69       1.491 -52.073   6.803  1.00 48.56           C  
ANISOU  270  C   ALA A  69     5583   5290   7576    355   -256   1062       C  
ATOM    271  O   ALA A  69       1.438 -51.363   7.807  1.00 49.26           O  
ANISOU  271  O   ALA A  69     5732   5452   7532    348   -253   1124       O  
ATOM    272  CB  ALA A  69       1.970 -54.442   7.386  1.00 49.10           C  
ANISOU  272  CB  ALA A  69     5651   5153   7851    411   -395   1192       C  
ATOM    273  N   SER A  70       2.007 -51.644   5.636  1.00 47.44           N  
ANISOU  273  N   SER A  70     5373   5173   7479    357   -237    921       N  
ATOM    274  CA  SER A  70       2.485 -50.272   5.486  1.00 47.02           C  
ANISOU  274  CA  SER A  70     5319   5225   7320    350   -207    843       C  
ATOM    275  C   SER A  70       1.288 -49.331   5.479  1.00 46.71           C  
ANISOU  275  C   SER A  70     5323   5248   7176    300   -116    866       C  
ATOM    276  O   SER A  70       1.356 -48.277   6.094  1.00 46.97           O  
ANISOU  276  O   SER A  70     5390   5360   7095    293    -97    874       O  
ATOM    277  CB  SER A  70       3.238 -50.106   4.184  1.00 48.12           C  
ANISOU  277  CB  SER A  70     5384   5374   7525    350   -198    692       C  
ATOM    278  OG  SER A  70       4.303 -51.027   4.129  1.00 51.25           O  
ANISOU  278  OG  SER A  70     5715   5689   8069    383   -262    644       O  
ATOM    279  N   LEU A  71       0.186 -49.716   4.789  1.00 45.66           N  
ANISOU  279  N   LEU A  71     5181   5078   7091    269    -64    867       N  
ATOM    280  CA  LEU A  71      -1.053 -48.950   4.730  1.00 44.91           C  
ANISOU  280  CA  LEU A  71     5115   5027   6923    228     12    882       C  
ATOM    281  C   LEU A  71      -1.622 -48.822   6.125  1.00 44.09           C  
ANISOU  281  C   LEU A  71     5072   4947   6733    214     25    991       C  
ATOM    282  O   LEU A  71      -2.071 -47.749   6.494  1.00 44.29           O  
ANISOU  282  O   LEU A  71     5123   5044   6662    193     70    986       O  
ATOM    283  CB  LEU A  71      -2.091 -49.678   3.872  1.00 45.40           C  
ANISOU  283  CB  LEU A  71     5148   5029   7074    207     45    869       C  
ATOM    284  CG  LEU A  71      -2.206 -49.340   2.400  1.00 47.56           C  
ANISOU  284  CG  LEU A  71     5380   5320   7369    192     75    763       C  
ATOM    285  CD1 LEU A  71      -3.411 -50.056   1.802  1.00 48.32           C  
ANISOU  285  CD1 LEU A  71     5452   5366   7541    171    105    763       C  
ATOM    286  CD2 LEU A  71      -2.383 -47.858   2.191  1.00 48.45           C  
ANISOU  286  CD2 LEU A  71     5523   5514   7371    176    112    735       C  
ATOM    287  N   ALA A  72      -1.606 -49.909   6.911  1.00 43.03           N  
ANISOU  287  N   ALA A  72     4963   4752   6633    223    -14   1088       N  
ATOM    288  CA  ALA A  72      -2.133 -49.898   8.268  1.00 42.51           C  
ANISOU  288  CA  ALA A  72     4965   4714   6472    198      2   1200       C  
ATOM    289  C   ALA A  72      -1.379 -48.906   9.136  1.00 42.04           C  
ANISOU  289  C   ALA A  72     4936   4752   6287    213    -23   1197       C  
ATOM    290  O   ALA A  72      -2.012 -48.155   9.875  1.00 42.09           O  
ANISOU  290  O   ALA A  72     4979   4832   6183    178     29   1223       O  
ATOM    291  CB  ALA A  72      -2.053 -51.290   8.872  1.00 42.36           C  
ANISOU  291  CB  ALA A  72     4977   4602   6516    206    -49   1313       C  
ATOM    292  N   VAL A  73      -0.034 -48.851   8.990  1.00 41.32           N  
ANISOU  292  N   VAL A  73     4816   4665   6218    263    -98   1144       N  
ATOM    293  CA  VAL A  73       0.803 -47.959   9.780  1.00 40.89           C  
ANISOU  293  CA  VAL A  73     4777   4701   6058    283   -129   1124       C  
ATOM    294  C   VAL A  73       0.820 -46.518   9.227  1.00 41.63           C  
ANISOU  294  C   VAL A  73     4842   4872   6105    266    -68   1013       C  
ATOM    295  O   VAL A  73       1.038 -45.588   9.999  1.00 41.60           O  
ANISOU  295  O   VAL A  73     4855   4952   5998    262    -60    999       O  
ATOM    296  CB  VAL A  73       2.209 -48.532  10.001  1.00 40.50           C  
ANISOU  296  CB  VAL A  73     4707   4621   6059    344   -240   1115       C  
ATOM    297  CG1 VAL A  73       3.088 -48.311   8.789  1.00 40.92           C  
ANISOU  297  CG1 VAL A  73     4682   4652   6215    367   -250    980       C  
ATOM    298  CG2 VAL A  73       2.840 -47.930  11.243  1.00 40.74           C  
ANISOU  298  CG2 VAL A  73     4768   4744   5966    363   -284   1128       C  
ATOM    299  N   ALA A  74       0.528 -46.316   7.921  1.00 42.00           N  
ANISOU  299  N   ALA A  74     4849   4889   6221    253    -25    937       N  
ATOM    300  CA  ALA A  74       0.455 -44.970   7.338  1.00 42.60           C  
ANISOU  300  CA  ALA A  74     4910   5021   6257    233     29    848       C  
ATOM    301  C   ALA A  74      -0.881 -44.355   7.760  1.00 43.57           C  
ANISOU  301  C   ALA A  74     5062   5176   6316    195     97    885       C  
ATOM    302  O   ALA A  74      -0.884 -43.243   8.279  1.00 44.05           O  
ANISOU  302  O   ALA A  74     5131   5305   6300    184    124    856       O  
ATOM    303  CB  ALA A  74       0.567 -45.021   5.814  1.00 42.47           C  
ANISOU  303  CB  ALA A  74     4851   4962   6322    227     45    768       C  
ATOM    304  N   ASP A  75      -2.007 -45.116   7.624  1.00 43.47           N  
ANISOU  304  N   ASP A  75     5057   5113   6344    173    124    940       N  
ATOM    305  CA  ASP A  75      -3.345 -44.699   8.023  1.00 43.98           C  
ANISOU  305  CA  ASP A  75     5139   5204   6369    133    190    962       C  
ATOM    306  C   ASP A  75      -3.335 -44.358   9.512  1.00 44.18           C  
ANISOU  306  C   ASP A  75     5203   5300   6284    118    199   1013       C  
ATOM    307  O   ASP A  75      -3.907 -43.358   9.923  1.00 44.27           O  
ANISOU  307  O   ASP A  75     5214   5372   6234     93    248    981       O  
ATOM    308  CB  ASP A  75      -4.345 -45.843   7.796  1.00 46.67           C  
ANISOU  308  CB  ASP A  75     5478   5474   6782    112    213   1014       C  
ATOM    309  CG  ASP A  75      -4.756 -46.192   6.371  1.00 53.03           C  
ANISOU  309  CG  ASP A  75     6240   6219   7690    116    218    958       C  
ATOM    310  OD1 ASP A  75      -4.661 -45.310   5.488  1.00 54.65           O  
ANISOU  310  OD1 ASP A  75     6426   6446   7893    123    222    881       O  
ATOM    311  OD2 ASP A  75      -5.212 -47.348   6.148  1.00 55.11           O  
ANISOU  311  OD2 ASP A  75     6493   6413   8034    108    218    994       O  
ATOM    312  N   LEU A  76      -2.661 -45.187  10.310  1.00 44.36           N  
ANISOU  312  N   LEU A  76     5257   5315   6284    135    144   1088       N  
ATOM    313  CA  LEU A  76      -2.512 -45.028  11.748  1.00 45.33           C  
ANISOU  313  CA  LEU A  76     5425   5513   6287    121    137   1144       C  
ATOM    314  C   LEU A  76      -1.781 -43.730  12.160  1.00 46.72           C  
ANISOU  314  C   LEU A  76     5586   5782   6383    137    128   1066       C  
ATOM    315  O   LEU A  76      -2.240 -43.066  13.093  1.00 47.48           O  
ANISOU  315  O   LEU A  76     5698   5961   6382    104    173   1062       O  
ATOM    316  CB  LEU A  76      -1.753 -46.244  12.276  1.00 45.05           C  
ANISOU  316  CB  LEU A  76     5428   5433   6258    147     56   1244       C  
ATOM    317  CG  LEU A  76      -2.175 -46.894  13.568  1.00 45.58           C  
ANISOU  317  CG  LEU A  76     5567   5526   6226    110     62   1363       C  
ATOM    318  CD1 LEU A  76      -3.672 -46.907  13.745  1.00 45.95           C  
ANISOU  318  CD1 LEU A  76     5625   5575   6257     38    169   1385       C  
ATOM    319  CD2 LEU A  76      -1.691 -48.302  13.574  1.00 45.81           C  
ANISOU  319  CD2 LEU A  76     5629   5462   6316    138    -20   1467       C  
ATOM    320  N   THR A  77      -0.647 -43.377  11.504  1.00 46.60           N  
ANISOU  320  N   THR A  77     5536   5758   6413    181     78    993       N  
ATOM    321  CA  THR A  77       0.040 -42.121  11.838  1.00 47.02           C  
ANISOU  321  CA  THR A  77     5568   5893   6404    190     79    909       C  
ATOM    322  C   THR A  77      -0.742 -40.903  11.326  1.00 48.20           C  
ANISOU  322  C   THR A  77     5696   6067   6551    157    160    838       C  
ATOM    323  O   THR A  77      -0.677 -39.836  11.940  1.00 48.56           O  
ANISOU  323  O   THR A  77     5736   6189   6525    142    188    795       O  
ATOM    324  CB  THR A  77       1.510 -42.088  11.358  1.00 47.01           C  
ANISOU  324  CB  THR A  77     5529   5877   6457    236     17    838       C  
ATOM    325  OG1 THR A  77       1.578 -41.905   9.951  1.00 47.03           O  
ANISOU  325  OG1 THR A  77     5498   5822   6548    231     46    774       O  
ATOM    326  CG2 THR A  77       2.292 -43.305  11.778  1.00 47.28           C  
ANISOU  326  CG2 THR A  77     5572   5872   6519    278    -77    895       C  
ATOM    327  N   PHE A  78      -1.472 -41.072  10.205  1.00 48.48           N  
ANISOU  327  N   PHE A  78     5717   6033   6669    147    192    826       N  
ATOM    328  CA  PHE A  78      -2.274 -40.053   9.536  1.00 49.37           C  
ANISOU  328  CA  PHE A  78     5811   6143   6805    124    250    768       C  
ATOM    329  C   PHE A  78      -3.352 -39.481  10.456  1.00 49.84           C  
ANISOU  329  C   PHE A  78     5874   6257   6805     89    306    770       C  
ATOM    330  O   PHE A  78      -3.531 -38.261  10.513  1.00 50.02           O  
ANISOU  330  O   PHE A  78     5876   6321   6810     81    335    700       O  
ATOM    331  CB  PHE A  78      -2.911 -40.664   8.263  1.00 49.52           C  
ANISOU  331  CB  PHE A  78     5821   6080   6914    123    256    775       C  
ATOM    332  CG  PHE A  78      -3.488 -39.718   7.234  1.00 50.24           C  
ANISOU  332  CG  PHE A  78     5896   6150   7042    116    282    712       C  
ATOM    333  CD1 PHE A  78      -2.863 -38.516   6.942  1.00 51.07           C  
ANISOU  333  CD1 PHE A  78     5996   6274   7134    120    283    649       C  
ATOM    334  CD2 PHE A  78      -4.603 -40.072   6.493  1.00 51.00           C  
ANISOU  334  CD2 PHE A  78     5984   6199   7193    106    300    718       C  
ATOM    335  CE1 PHE A  78      -3.383 -37.657   5.981  1.00 51.72           C  
ANISOU  335  CE1 PHE A  78     6077   6326   7249    113    298    608       C  
ATOM    336  CE2 PHE A  78      -5.121 -39.212   5.534  1.00 51.70           C  
ANISOU  336  CE2 PHE A  78     6066   6266   7312    105    307    669       C  
ATOM    337  CZ  PHE A  78      -4.512 -38.006   5.290  1.00 51.53           C  
ANISOU  337  CZ  PHE A  78     6050   6259   7270    109    304    622       C  
ATOM    338  N   VAL A  79      -4.032 -40.346  11.209  1.00 49.78           N  
ANISOU  338  N   VAL A  79     5890   6252   6773     63    324    842       N  
ATOM    339  CA  VAL A  79      -5.108 -39.897  12.079  1.00 50.13           C  
ANISOU  339  CA  VAL A  79     5930   6351   6764     18    390    833       C  
ATOM    340  C   VAL A  79      -4.655 -39.622  13.523  1.00 50.61           C  
ANISOU  340  C   VAL A  79     6013   6516   6702      1    392    842       C  
ATOM    341  O   VAL A  79      -5.311 -38.852  14.209  1.00 50.79           O  
ANISOU  341  O   VAL A  79     6015   6605   6678    -34    448    787       O  
ATOM    342  CB  VAL A  79      -6.306 -40.876  12.017  1.00 50.41           C  
ANISOU  342  CB  VAL A  79     5977   6342   6836    -18    430    893       C  
ATOM    343  CG1 VAL A  79      -6.764 -41.066  10.580  1.00 50.83           C  
ANISOU  343  CG1 VAL A  79     6001   6304   7007      1    422    869       C  
ATOM    344  CG2 VAL A  79      -5.960 -42.220  12.641  1.00 50.68           C  
ANISOU  344  CG2 VAL A  79     6063   6364   6828    -26    401   1006       C  
ATOM    345  N   VAL A  80      -3.517 -40.182  13.956  1.00 50.62           N  
ANISOU  345  N   VAL A  80     6046   6533   6654     29    325    895       N  
ATOM    346  CA  VAL A  80      -3.011 -40.103  15.330  1.00 51.10           C  
ANISOU  346  CA  VAL A  80     6136   6695   6584     18    307    916       C  
ATOM    347  C   VAL A  80      -2.875 -38.648  15.922  1.00 51.31           C  
ANISOU  347  C   VAL A  80     6121   6820   6553      7    342    803       C  
ATOM    348  O   VAL A  80      -3.089 -38.486  17.132  1.00 51.32           O  
ANISOU  348  O   VAL A  80     6139   6922   6439    -32    371    805       O  
ATOM    349  CB  VAL A  80      -1.714 -40.940  15.465  1.00 51.83           C  
ANISOU  349  CB  VAL A  80     6259   6769   6666     69    205    978       C  
ATOM    350  CG1 VAL A  80      -0.475 -40.116  15.832  1.00 52.32           C  
ANISOU  350  CG1 VAL A  80     6308   6921   6651     98    155    918       C  
ATOM    351  CG2 VAL A  80      -1.931 -42.098  16.431  1.00 52.43           C  
ANISOU  351  CG2 VAL A  80     6402   6824   6693     48    183   1116       C  
ATOM    352  N   THR A  81      -2.533 -37.627  15.109  1.00 51.16           N  
ANISOU  352  N   THR A  81     6053   6775   6611     34    344    704       N  
ATOM    353  CA  THR A  81      -2.450 -36.260  15.641  1.00 51.52           C  
ANISOU  353  CA  THR A  81     6055   6899   6623     22    378    595       C  
ATOM    354  C   THR A  81      -3.718 -35.453  15.408  1.00 51.69           C  
ANISOU  354  C   THR A  81     6037   6910   6692    -15    457    531       C  
ATOM    355  O   THR A  81      -3.697 -34.251  15.648  1.00 51.86           O  
ANISOU  355  O   THR A  81     6014   6981   6711    -24    487    430       O  
ATOM    356  CB  THR A  81      -1.252 -35.501  15.108  1.00 53.10           C  
ANISOU  356  CB  THR A  81     6223   7080   6874     62    341    518       C  
ATOM    357  OG1 THR A  81      -1.429 -35.304  13.706  1.00 54.37           O  
ANISOU  357  OG1 THR A  81     6374   7135   7150     75    349    509       O  
ATOM    358  CG2 THR A  81       0.056 -36.212  15.385  1.00 53.68           C  
ANISOU  358  CG2 THR A  81     6315   7172   6909    102    260    550       C  
ATOM    359  N   LEU A  82      -4.814 -36.086  14.938  1.00 51.42           N  
ANISOU  359  N   LEU A  82     6011   6809   6716    -32    486    576       N  
ATOM    360  CA  LEU A  82      -6.061 -35.372  14.725  1.00 51.43           C  
ANISOU  360  CA  LEU A  82     5967   6796   6778    -61    550    507       C  
ATOM    361  C   LEU A  82      -6.655 -34.767  15.970  1.00 51.90           C  
ANISOU  361  C   LEU A  82     5998   6962   6760   -112    615    444       C  
ATOM    362  O   LEU A  82      -7.100 -33.635  15.849  1.00 52.37           O  
ANISOU  362  O   LEU A  82     5998   7023   6876   -116    646    337       O  
ATOM    363  CB  LEU A  82      -7.122 -36.166  13.988  1.00 51.18           C  
ANISOU  363  CB  LEU A  82     5941   6684   6822    -71    568    555       C  
ATOM    364  CG  LEU A  82      -7.265 -35.887  12.499  1.00 52.36           C  
ANISOU  364  CG  LEU A  82     6076   6728   7092    -31    535    537       C  
ATOM    365  CD1 LEU A  82      -8.619 -36.302  12.043  1.00 53.07           C  
ANISOU  365  CD1 LEU A  82     6145   6765   7255    -49    567    537       C  
ATOM    366  CD2 LEU A  82      -7.052 -34.395  12.130  1.00 52.86           C  
ANISOU  366  CD2 LEU A  82     6102   6779   7203     -9    527    443       C  
ATOM    367  N   PRO A  83      -6.624 -35.381  17.182  1.00 51.54           N  
ANISOU  367  N   PRO A  83     5990   7008   6583   -153    633    497       N  
ATOM    368  CA  PRO A  83      -7.150 -34.670  18.361  1.00 51.25           C  
ANISOU  368  CA  PRO A  83     5921   7091   6462   -210    701    414       C  
ATOM    369  C   PRO A  83      -6.565 -33.253  18.547  1.00 50.74           C  
ANISOU  369  C   PRO A  83     5793   7073   6413   -190    698    282       C  
ATOM    370  O   PRO A  83      -7.268 -32.383  19.045  1.00 51.15           O  
ANISOU  370  O   PRO A  83     5781   7173   6480   -226    763    170       O  
ATOM    371  CB  PRO A  83      -6.809 -35.615  19.521  1.00 51.93           C  
ANISOU  371  CB  PRO A  83     6081   7267   6383   -245    691    516       C  
ATOM    372  CG  PRO A  83      -6.789 -36.963  18.897  1.00 52.42           C  
ANISOU  372  CG  PRO A  83     6204   7228   6485   -229    654    652       C  
ATOM    373  CD  PRO A  83      -6.154 -36.732  17.554  1.00 51.01           C  
ANISOU  373  CD  PRO A  83     6001   6941   6439   -155    592    633       C  
ATOM    374  N   LEU A  84      -5.333 -32.994  18.055  1.00 49.68           N  
ANISOU  374  N   LEU A  84     5664   6911   6299   -132    628    280       N  
ATOM    375  CA  LEU A  84      -4.690 -31.674  18.130  1.00 49.18           C  
ANISOU  375  CA  LEU A  84     5542   6875   6268   -113    626    156       C  
ATOM    376  C   LEU A  84      -5.419 -30.674  17.214  1.00 49.30           C  
ANISOU  376  C   LEU A  84     5498   6793   6439   -102    653     73       C  
ATOM    377  O   LEU A  84      -5.689 -29.548  17.622  1.00 49.27           O  
ANISOU  377  O   LEU A  84     5427   6820   6472   -116    690    -49       O  
ATOM    378  CB  LEU A  84      -3.212 -31.776  17.719  1.00 48.77           C  
ANISOU  378  CB  LEU A  84     5513   6804   6213    -60    548    179       C  
ATOM    379  CG  LEU A  84      -2.185 -32.166  18.773  1.00 49.44           C  
ANISOU  379  CG  LEU A  84     5626   7001   6158    -56    503    202       C  
ATOM    380  CD1 LEU A  84      -2.585 -33.424  19.524  1.00 49.95           C  
ANISOU  380  CD1 LEU A  84     5761   7111   6107    -84    497    326       C  
ATOM    381  CD2 LEU A  84      -0.817 -32.349  18.141  1.00 49.59           C  
ANISOU  381  CD2 LEU A  84     5655   6977   6212      2    426    214       C  
ATOM    382  N   TRP A  85      -5.737 -31.096  15.981  1.00 49.26           N  
ANISOU  382  N   TRP A  85     5519   6669   6528    -75    628    138       N  
ATOM    383  CA  TRP A  85      -6.476 -30.288  15.009  1.00 49.84           C  
ANISOU  383  CA  TRP A  85     5554   6638   6743    -59    634     86       C  
ATOM    384  C   TRP A  85      -7.992 -30.247  15.329  1.00 50.80           C  
ANISOU  384  C   TRP A  85     5630   6766   6905    -95    691     39       C  
ATOM    385  O   TRP A  85      -8.706 -29.369  14.847  1.00 51.51           O  
ANISOU  385  O   TRP A  85     5668   6789   7113    -84    697    -36       O  
ATOM    386  CB  TRP A  85      -6.236 -30.803  13.592  1.00 49.63           C  
ANISOU  386  CB  TRP A  85     5577   6501   6781    -21    581    173       C  
ATOM    387  CG  TRP A  85      -4.787 -30.905  13.246  1.00 50.30           C  
ANISOU  387  CG  TRP A  85     5694   6578   6838      7    534    202       C  
ATOM    388  CD1 TRP A  85      -3.974 -31.984  13.424  1.00 51.23           C  
ANISOU  388  CD1 TRP A  85     5857   6724   6882     17    498    279       C  
ATOM    389  CD2 TRP A  85      -3.964 -29.867  12.699  1.00 50.46           C  
ANISOU  389  CD2 TRP A  85     5700   6559   6916     26    519    142       C  
ATOM    390  NE1 TRP A  85      -2.694 -31.684  13.019  1.00 51.52           N  
ANISOU  390  NE1 TRP A  85     5898   6746   6929     43    463    259       N  
ATOM    391  CE2 TRP A  85      -2.662 -30.391  12.563  1.00 51.22           C  
ANISOU  391  CE2 TRP A  85     5827   6667   6967     43    481    177       C  
ATOM    392  CE3 TRP A  85      -4.205 -28.551  12.290  1.00 50.95           C  
ANISOU  392  CE3 TRP A  85     5724   6565   7071     28    534     62       C  
ATOM    393  CZ2 TRP A  85      -1.613 -29.648  12.029  1.00 51.76           C  
ANISOU  393  CZ2 TRP A  85     5888   6702   7076     54    470    129       C  
ATOM    394  CZ3 TRP A  85      -3.164 -27.820  11.757  1.00 51.73           C  
ANISOU  394  CZ3 TRP A  85     5826   6621   7206     39    519     31       C  
ATOM    395  CH2 TRP A  85      -1.885 -28.366  11.635  1.00 51.86           C  
ANISOU  395  CH2 TRP A  85     5872   6660   7172     48    494     60       C  
ATOM    396  N   ALA A  86      -8.484 -31.204  16.111  1.00 50.46           N  
ANISOU  396  N   ALA A  86     5607   6794   6772   -140    731     84       N  
ATOM    397  CA  ALA A  86      -9.852 -31.215  16.562  1.00 50.92           C  
ANISOU  397  CA  ALA A  86     5616   6873   6857   -188    800     25       C  
ATOM    398  C   ALA A  86      -9.968 -30.160  17.688  1.00 51.14           C  
ANISOU  398  C   ALA A  86     5573   7006   6850   -226    856   -113       C  
ATOM    399  O   ALA A  86     -10.930 -29.401  17.717  1.00 51.38           O  
ANISOU  399  O   ALA A  86     5523   7018   6982   -237    893   -231       O  
ATOM    400  CB  ALA A  86     -10.209 -32.594  17.076  1.00 51.19           C  
ANISOU  400  CB  ALA A  86     5704   6949   6796   -235    832    125       C  
ATOM    401  N   VAL A  87      -8.972 -30.083  18.584  1.00 51.02           N  
ANISOU  401  N   VAL A  87     5581   7100   6703   -240    854   -110       N  
ATOM    402  CA  VAL A  87      -8.932 -29.082  19.647  1.00 51.37           C  
ANISOU  402  CA  VAL A  87     5557   7255   6705   -274    901   -249       C  
ATOM    403  C   VAL A  87      -8.729 -27.674  19.036  1.00 52.36           C  
ANISOU  403  C   VAL A  87     5610   7303   6980   -228    877   -365       C  
ATOM    404  O   VAL A  87      -9.402 -26.728  19.455  1.00 52.89           O  
ANISOU  404  O   VAL A  87     5586   7396   7113   -252    926   -510       O  
ATOM    405  CB  VAL A  87      -7.845 -29.454  20.683  1.00 51.29           C  
ANISOU  405  CB  VAL A  87     5599   7378   6512   -291    885   -207       C  
ATOM    406  CG1 VAL A  87      -7.388 -28.244  21.490  1.00 51.68           C  
ANISOU  406  CG1 VAL A  87     5572   7530   6532   -306    911   -361       C  
ATOM    407  CG2 VAL A  87      -8.340 -30.563  21.595  1.00 51.34           C  
ANISOU  407  CG2 VAL A  87     5666   7474   6368   -357    927   -118       C  
ATOM    408  N   TYR A  88      -7.837 -27.562  18.021  1.00 52.11           N  
ANISOU  408  N   TYR A  88     5619   7171   7010   -166    804   -302       N  
ATOM    409  CA  TYR A  88      -7.511 -26.343  17.267  1.00 52.26           C  
ANISOU  409  CA  TYR A  88     5595   7092   7167   -125    775   -375       C  
ATOM    410  C   TYR A  88      -8.739 -25.768  16.546  1.00 52.99           C  
ANISOU  410  C   TYR A  88     5637   7075   7421   -113    781   -427       C  
ATOM    411  O   TYR A  88      -8.988 -24.570  16.637  1.00 52.87           O  
ANISOU  411  O   TYR A  88     5547   7025   7515   -106    790   -547       O  
ATOM    412  CB  TYR A  88      -6.418 -26.691  16.259  1.00 52.02           C  
ANISOU  412  CB  TYR A  88     5639   6982   7144    -78    707   -270       C  
ATOM    413  CG  TYR A  88      -6.043 -25.616  15.270  1.00 52.49           C  
ANISOU  413  CG  TYR A  88     5683   6922   7338    -43    676   -308       C  
ATOM    414  CD1 TYR A  88      -5.576 -24.386  15.700  1.00 53.28           C  
ANISOU  414  CD1 TYR A  88     5721   7037   7485    -46    694   -428       C  
ATOM    415  CD2 TYR A  88      -5.989 -25.888  13.913  1.00 53.36           C  
ANISOU  415  CD2 TYR A  88     5849   6910   7516    -10    629   -217       C  
ATOM    416  CE1 TYR A  88      -5.125 -23.426  14.802  1.00 54.24           C  
ANISOU  416  CE1 TYR A  88     5840   7041   7726    -20    668   -449       C  
ATOM    417  CE2 TYR A  88      -5.529 -24.944  13.005  1.00 54.44           C  
ANISOU  417  CE2 TYR A  88     5990   6940   7754     12    602   -235       C  
ATOM    418  CZ  TYR A  88      -5.116 -23.702  13.449  1.00 55.34           C  
ANISOU  418  CZ  TYR A  88     6047   7058   7922      6    623   -346       C  
ATOM    419  OH  TYR A  88      -4.679 -22.756  12.543  1.00 56.82           O  
ANISOU  419  OH  TYR A  88     6246   7127   8215     21    602   -354       O  
ATOM    420  N   THR A  89      -9.520 -26.623  15.855  1.00 53.68           N  
ANISOU  420  N   THR A  89     5759   7105   7533   -108    770   -344       N  
ATOM    421  CA  THR A  89     -10.735 -26.204  15.150  1.00 54.79           C  
ANISOU  421  CA  THR A  89     5848   7143   7824    -92    762   -393       C  
ATOM    422  C   THR A  89     -11.832 -25.804  16.159  1.00 56.68           C  
ANISOU  422  C   THR A  89     5988   7459   8088   -142    839   -535       C  
ATOM    423  O   THR A  89     -12.579 -24.854  15.917  1.00 56.80           O  
ANISOU  423  O   THR A  89     5923   7405   8254   -126    834   -643       O  
ATOM    424  CB  THR A  89     -11.190 -27.297  14.168  1.00 55.10           C  
ANISOU  424  CB  THR A  89     5948   7110   7878    -73    726   -274       C  
ATOM    425  OG1 THR A  89     -10.108 -27.656  13.315  1.00 55.76           O  
ANISOU  425  OG1 THR A  89     6117   7143   7928    -37    667   -159       O  
ATOM    426  CG2 THR A  89     -12.344 -26.860  13.316  1.00 55.23           C  
ANISOU  426  CG2 THR A  89     5918   7014   8054    -42    695   -319       C  
ATOM    427  N   TYR A  90     -11.904 -26.505  17.305  1.00 57.87           N  
ANISOU  427  N   TYR A  90     6145   7754   8091   -206    908   -537       N  
ATOM    428  CA  TYR A  90     -12.872 -26.188  18.346  1.00 59.59           C  
ANISOU  428  CA  TYR A  90     6272   8065   8306   -270    996   -678       C  
ATOM    429  C   TYR A  90     -12.564 -24.816  18.925  1.00 60.39           C  
ANISOU  429  C   TYR A  90     6283   8198   8465   -269   1011   -837       C  
ATOM    430  O   TYR A  90     -13.487 -24.036  19.147  1.00 60.66           O  
ANISOU  430  O   TYR A  90     6208   8220   8618   -285   1049   -989       O  
ATOM    431  CB  TYR A  90     -12.844 -27.236  19.470  1.00 60.58           C  
ANISOU  431  CB  TYR A  90     6442   8343   8232   -347   1066   -628       C  
ATOM    432  CG  TYR A  90     -14.024 -27.139  20.419  1.00 62.58           C  
ANISOU  432  CG  TYR A  90     6610   8686   8481   -430   1171   -760       C  
ATOM    433  CD1 TYR A  90     -15.273 -27.627  20.060  1.00 64.06           C  
ANISOU  433  CD1 TYR A  90     6767   8815   8759   -449   1203   -772       C  
ATOM    434  CD2 TYR A  90     -13.886 -26.571  21.679  1.00 63.95           C  
ANISOU  434  CD2 TYR A  90     6726   9006   8565   -492   1243   -887       C  
ATOM    435  CE1 TYR A  90     -16.360 -27.543  20.925  1.00 65.27           C  
ANISOU  435  CE1 TYR A  90     6832   9052   8917   -532   1309   -910       C  
ATOM    436  CE2 TYR A  90     -14.969 -26.471  22.550  1.00 65.19           C  
ANISOU  436  CE2 TYR A  90     6798   9254   8718   -578   1350  -1025       C  
ATOM    437  CZ  TYR A  90     -16.205 -26.969  22.174  1.00 66.45           C  
ANISOU  437  CZ  TYR A  90     6927   9351   8971   -601   1388  -1036       C  
ATOM    438  OH  TYR A  90     -17.290 -26.892  23.028  1.00 68.38           O  
ANISOU  438  OH  TYR A  90     7080   9686   9215   -695   1505  -1185       O  
ATOM    439  N   ARG A  91     -11.271 -24.500  19.141  1.00 60.63           N  
ANISOU  439  N   ARG A  91     6347   8263   8426   -250    981   -816       N  
ATOM    440  CA  ARG A  91     -10.858 -23.209  19.700  1.00 61.34           C  
ANISOU  440  CA  ARG A  91     6350   8382   8574   -250    996   -971       C  
ATOM    441  C   ARG A  91     -10.881 -22.070  18.681  1.00 61.74           C  
ANISOU  441  C   ARG A  91     6363   8261   8835   -185    936  -1013       C  
ATOM    442  O   ARG A  91     -10.171 -21.078  18.882  1.00 61.91           O  
ANISOU  442  O   ARG A  91     6342   8275   8907   -172    929  -1097       O  
ATOM    443  CB  ARG A  91      -9.466 -23.303  20.330  1.00 62.85           C  
ANISOU  443  CB  ARG A  91     6585   8681   8615   -256    988   -947       C  
ATOM    444  CG  ARG A  91      -9.405 -24.204  21.533  1.00 66.63           C  
ANISOU  444  CG  ARG A  91     7105   9335   8878   -320   1037   -908       C  
ATOM    445  CD  ARG A  91      -7.969 -24.402  21.944  1.00 71.35           C  
ANISOU  445  CD  ARG A  91     7762  10007   9341   -303    993   -850       C  
ATOM    446  NE  ARG A  91      -7.733 -23.938  23.312  1.00 75.78           N  
ANISOU  446  NE  ARG A  91     8269  10744   9782   -354   1042   -976       N  
ATOM    447  CZ  ARG A  91      -7.319 -22.716  23.633  1.00 78.22           C  
ANISOU  447  CZ  ARG A  91     8487  11074  10159   -347   1052  -1133       C  
ATOM    448  NH1 ARG A  91      -7.101 -21.811  22.686  1.00 77.34           N  
ANISOU  448  NH1 ARG A  91     8334  10810  10241   -293   1017  -1176       N  
ATOM    449  NH2 ARG A  91      -7.131 -22.386  24.906  1.00 78.46           N  
ANISOU  449  NH2 ARG A  91     8467  11280  10063   -398   1096  -1251       N  
ATOM    450  N   ASP A  92     -11.699 -22.202  17.601  1.00 61.58           N  
ANISOU  450  N   ASP A  92     6359   8103   8936   -146    890   -953       N  
ATOM    451  CA  ASP A  92     -11.853 -21.203  16.534  1.00 61.91           C  
ANISOU  451  CA  ASP A  92     6384   7970   9171    -84    819   -967       C  
ATOM    452  C   ASP A  92     -10.496 -20.900  15.925  1.00 59.99           C  
ANISOU  452  C   ASP A  92     6211   7671   8910    -52    771   -889       C  
ATOM    453  O   ASP A  92     -10.110 -19.736  15.789  1.00 59.87           O  
ANISOU  453  O   ASP A  92     6151   7589   9007    -34    757   -969       O  
ATOM    454  CB  ASP A  92     -12.540 -19.921  17.069  1.00 66.32           C  
ANISOU  454  CB  ASP A  92     6803   8499   9897    -88    843  -1164       C  
ATOM    455  CG  ASP A  92     -12.955 -18.875  16.034  1.00 75.37           C  
ANISOU  455  CG  ASP A  92     7925   9448  11264    -22    760  -1181       C  
ATOM    456  OD1 ASP A  92     -12.492 -18.971  14.864  1.00 77.34           O  
ANISOU  456  OD1 ASP A  92     8276   9585  11526     24    684  -1031       O  
ATOM    457  OD2 ASP A  92     -13.730 -17.945  16.399  1.00 78.62           O  
ANISOU  457  OD2 ASP A  92     8217   9818  11837    -17    769  -1345       O  
ATOM    458  N   TYR A  93      -9.758 -21.955  15.617  1.00 58.41           N  
ANISOU  458  N   TYR A  93     6115   7505   8575    -51    753   -744       N  
ATOM    459  CA  TYR A  93      -8.438 -21.820  15.049  1.00 57.70           C  
ANISOU  459  CA  TYR A  93     6092   7373   8457    -28    715   -672       C  
ATOM    460  C   TYR A  93      -7.475 -21.047  15.967  1.00 56.61           C  
ANISOU  460  C   TYR A  93     5903   7319   8286    -49    750   -780       C  
ATOM    461  O   TYR A  93      -7.094 -19.925  15.648  1.00 56.53           O  
ANISOU  461  O   TYR A  93     5861   7225   8393    -33    738   -843       O  
ATOM    462  CB  TYR A  93      -8.523 -21.248  13.629  1.00 57.72           C  
ANISOU  462  CB  TYR A  93     6130   7197   8602     17    649   -619       C  
ATOM    463  CG  TYR A  93      -9.155 -22.252  12.693  1.00 58.41           C  
ANISOU  463  CG  TYR A  93     6284   7230   8678     38    607   -496       C  
ATOM    464  CD1 TYR A  93      -8.464 -23.382  12.290  1.00 59.40           C  
ANISOU  464  CD1 TYR A  93     6503   7380   8687     38    589   -366       C  
ATOM    465  CD2 TYR A  93     -10.475 -22.128  12.298  1.00 59.32           C  
ANISOU  465  CD2 TYR A  93     6357   7284   8900     54    588   -528       C  
ATOM    466  CE1 TYR A  93      -9.052 -24.342  11.480  1.00 60.28           C  
ANISOU  466  CE1 TYR A  93     6666   7450   8789     53    556   -267       C  
ATOM    467  CE2 TYR A  93     -11.073 -23.076  11.474  1.00 60.29           C  
ANISOU  467  CE2 TYR A  93     6532   7367   9011     71    551   -429       C  
ATOM    468  CZ  TYR A  93     -10.358 -24.188  11.071  1.00 61.17           C  
ANISOU  468  CZ  TYR A  93     6737   7502   9003     69    538   -298       C  
ATOM    469  OH  TYR A  93     -10.928 -25.141  10.261  1.00 62.62           O  
ANISOU  469  OH  TYR A  93     6965   7648   9181     85    503   -211       O  
ATOM    470  N   ASP A  94      -7.116 -21.664  17.124  1.00 55.65           N  
ANISOU  470  N   ASP A  94     5777   7364   8004    -86    792   -798       N  
ATOM    471  CA  ASP A  94      -6.154 -21.182  18.133  1.00 55.20           C  
ANISOU  471  CA  ASP A  94     5677   7424   7871   -108    821   -895       C  
ATOM    472  C   ASP A  94      -5.308 -22.368  18.604  1.00 53.88           C  
ANISOU  472  C   ASP A  94     5588   7375   7510   -118    808   -792       C  
ATOM    473  O   ASP A  94      -5.764 -23.161  19.425  1.00 53.75           O  
ANISOU  473  O   ASP A  94     5584   7472   7367   -152    837   -769       O  
ATOM    474  CB  ASP A  94      -6.855 -20.537  19.342  1.00 57.40           C  
ANISOU  474  CB  ASP A  94     5845   7811   8155   -152    888  -1067       C  
ATOM    475  CG  ASP A  94      -5.938 -19.768  20.291  1.00 62.20           C  
ANISOU  475  CG  ASP A  94     6385   8517   8732   -169    914  -1203       C  
ATOM    476  OD1 ASP A  94      -4.714 -19.724  20.040  1.00 62.22           O  
ANISOU  476  OD1 ASP A  94     6432   8524   8687   -149    880  -1159       O  
ATOM    477  OD2 ASP A  94      -6.448 -19.219  21.289  1.00 65.14           O  
ANISOU  477  OD2 ASP A  94     6653   8967   9131   -205    969  -1367       O  
ATOM    478  N   TRP A  95      -4.077 -22.473  18.085  1.00 52.72           N  
ANISOU  478  N   TRP A  95     5491   7194   7345    -89    764   -734       N  
ATOM    479  CA  TRP A  95      -3.156 -23.559  18.379  1.00 52.23           C  
ANISOU  479  CA  TRP A  95     5498   7217   7130    -84    732   -640       C  
ATOM    480  C   TRP A  95      -2.466 -23.408  19.743  1.00 52.73           C  
ANISOU  480  C   TRP A  95     5520   7450   7065   -107    747   -732       C  
ATOM    481  O   TRP A  95      -1.542 -22.605  19.896  1.00 53.42           O  
ANISOU  481  O   TRP A  95     5563   7551   7184    -97    741   -825       O  
ATOM    482  CB  TRP A  95      -2.130 -23.698  17.235  1.00 51.50           C  
ANISOU  482  CB  TRP A  95     5462   7018   7086    -47    681   -562       C  
ATOM    483  CG  TRP A  95      -1.277 -24.930  17.319  1.00 51.12           C  
ANISOU  483  CG  TRP A  95     5483   7027   6913    -32    636   -458       C  
ATOM    484  CD1 TRP A  95      -0.076 -25.049  17.947  1.00 51.66           C  
ANISOU  484  CD1 TRP A  95     5545   7187   6898    -23    609   -491       C  
ATOM    485  CD2 TRP A  95      -1.565 -26.220  16.757  1.00 50.89           C  
ANISOU  485  CD2 TRP A  95     5532   6965   6839    -21    604   -312       C  
ATOM    486  NE1 TRP A  95       0.390 -26.337  17.837  1.00 51.83           N  
ANISOU  486  NE1 TRP A  95     5636   7229   6828     -4    557   -371       N  
ATOM    487  CE2 TRP A  95      -0.502 -27.076  17.106  1.00 51.43           C  
ANISOU  487  CE2 TRP A  95     5638   7100   6801     -4    557   -260       C  
ATOM    488  CE3 TRP A  95      -2.627 -26.740  16.007  1.00 51.33           C  
ANISOU  488  CE3 TRP A  95     5623   6938   6941    -21    608   -228       C  
ATOM    489  CZ2 TRP A  95      -0.465 -28.416  16.725  1.00 51.79           C  
ANISOU  489  CZ2 TRP A  95     5755   7126   6798     11    515   -126       C  
ATOM    490  CZ3 TRP A  95      -2.585 -28.067  15.624  1.00 51.98           C  
ANISOU  490  CZ3 TRP A  95     5775   7008   6968     -9    573   -100       C  
ATOM    491  CH2 TRP A  95      -1.511 -28.887  15.977  1.00 51.97           C  
ANISOU  491  CH2 TRP A  95     5810   7066   6871      6    529    -49       C  
ATOM    492  N   PRO A  96      -2.844 -24.238  20.732  1.00 52.09           N  
ANISOU  492  N   PRO A  96     5460   7503   6829   -139    762   -701       N  
ATOM    493  CA  PRO A  96      -2.209 -24.140  22.053  1.00 51.80           C  
ANISOU  493  CA  PRO A  96     5395   7639   6648   -162    766   -779       C  
ATOM    494  C   PRO A  96      -0.965 -25.018  22.262  1.00 51.88           C  
ANISOU  494  C   PRO A  96     5474   7706   6532   -131    690   -687       C  
ATOM    495  O   PRO A  96      -0.323 -24.915  23.305  1.00 52.48           O  
ANISOU  495  O   PRO A  96     5525   7919   6494   -138    675   -756       O  
ATOM    496  CB  PRO A  96      -3.312 -24.643  22.961  1.00 52.41           C  
ANISOU  496  CB  PRO A  96     5478   7825   6610   -220    819   -771       C  
ATOM    497  CG  PRO A  96      -3.968 -25.716  22.147  1.00 52.76           C  
ANISOU  497  CG  PRO A  96     5605   7770   6671   -210    803   -607       C  
ATOM    498  CD  PRO A  96      -3.921 -25.247  20.726  1.00 51.33           C  
ANISOU  498  CD  PRO A  96     5414   7409   6681   -164    781   -599       C  
ATOM    499  N   PHE A  97      -0.621 -25.885  21.303  1.00 50.95           N  
ANISOU  499  N   PHE A  97     5435   7487   6436    -94    638   -543       N  
ATOM    500  CA  PHE A  97       0.462 -26.852  21.481  1.00 50.17           C  
ANISOU  500  CA  PHE A  97     5398   7431   6233    -61    558   -452       C  
ATOM    501  C   PHE A  97       1.842 -26.428  20.979  1.00 49.76           C  
ANISOU  501  C   PHE A  97     5322   7331   6253    -16    510   -502       C  
ATOM    502  O   PHE A  97       2.707 -27.285  20.837  1.00 49.83           O  
ANISOU  502  O   PHE A  97     5377   7341   6214     20    438   -426       O  
ATOM    503  CB  PHE A  97       0.085 -28.207  20.856  1.00 49.78           C  
ANISOU  503  CB  PHE A  97     5441   7309   6163    -50    527   -275       C  
ATOM    504  CG  PHE A  97      -1.347 -28.642  21.072  1.00 50.10           C  
ANISOU  504  CG  PHE A  97     5503   7352   6180    -96    586   -223       C  
ATOM    505  CD1 PHE A  97      -1.732 -29.254  22.246  1.00 50.67           C  
ANISOU  505  CD1 PHE A  97     5610   7549   6091   -140    600   -181       C  
ATOM    506  CD2 PHE A  97      -2.307 -28.429  20.100  1.00 50.93           C  
ANISOU  506  CD2 PHE A  97     5594   7335   6423   -100    625   -219       C  
ATOM    507  CE1 PHE A  97      -3.046 -29.651  22.442  1.00 51.19           C  
ANISOU  507  CE1 PHE A  97     5692   7616   6142   -192    666   -142       C  
ATOM    508  CE2 PHE A  97      -3.620 -28.828  20.299  1.00 51.43           C  
ANISOU  508  CE2 PHE A  97     5666   7400   6477   -142    679   -187       C  
ATOM    509  CZ  PHE A  97      -3.980 -29.433  21.471  1.00 51.07           C  
ANISOU  509  CZ  PHE A  97     5648   7477   6277   -192    706   -154       C  
ATOM    510  N   GLY A  98       2.057 -25.145  20.717  1.00 49.49           N  
ANISOU  510  N   GLY A  98     5213   7252   6340    -19    549   -633       N  
ATOM    511  CA  GLY A  98       3.382 -24.654  20.320  1.00 49.79           C  
ANISOU  511  CA  GLY A  98     5218   7252   6447      9    520   -702       C  
ATOM    512  C   GLY A  98       3.892 -24.939  18.920  1.00 49.77           C  
ANISOU  512  C   GLY A  98     5260   7106   6545     35    497   -625       C  
ATOM    513  O   GLY A  98       3.268 -25.674  18.158  1.00 50.04           O  
ANISOU  513  O   GLY A  98     5361   7065   6589     40    487   -498       O  
ATOM    514  N   THR A  99       5.049 -24.362  18.567  1.00 49.49           N  
ANISOU  514  N   THR A  99     5183   7037   6584     45    492   -713       N  
ATOM    515  CA  THR A  99       5.606 -24.515  17.217  1.00 49.68           C  
ANISOU  515  CA  THR A  99     5241   6931   6704     55    485   -663       C  
ATOM    516  C   THR A  99       6.155 -25.917  16.922  1.00 50.42           C  
ANISOU  516  C   THR A  99     5394   7031   6733     89    413   -554       C  
ATOM    517  O   THR A  99       6.080 -26.352  15.771  1.00 50.76           O  
ANISOU  517  O   THR A  99     5485   6969   6834     90    413   -473       O  
ATOM    518  CB  THR A  99       6.655 -23.438  16.879  1.00 49.95           C  
ANISOU  518  CB  THR A  99     5213   6926   6839     44    514   -796       C  
ATOM    519  OG1 THR A  99       6.331 -22.193  17.502  1.00 50.64           O  
ANISOU  519  OG1 THR A  99     5230   7032   6980     19    568   -919       O  
ATOM    520  CG2 THR A  99       6.787 -23.218  15.386  1.00 50.04           C  
ANISOU  520  CG2 THR A  99     5264   6786   6962     28    541   -749       C  
ATOM    521  N   PHE A 100       6.687 -26.635  17.934  1.00 50.45           N  
ANISOU  521  N   PHE A 100     5394   7155   6619    116    347   -551       N  
ATOM    522  CA  PHE A 100       7.225 -27.981  17.686  1.00 50.69           C  
ANISOU  522  CA  PHE A 100     5476   7178   6608    154    268   -449       C  
ATOM    523  C   PHE A 100       6.113 -29.006  17.395  1.00 50.10           C  
ANISOU  523  C   PHE A 100     5481   7063   6493    151    263   -290       C  
ATOM    524  O   PHE A 100       6.290 -29.859  16.522  1.00 49.78           O  
ANISOU  524  O   PHE A 100     5480   6940   6494    168    234   -208       O  
ATOM    525  CB  PHE A 100       8.192 -28.458  18.792  1.00 50.91           C  
ANISOU  525  CB  PHE A 100     5480   7328   6535    193    180   -489       C  
ATOM    526  CG  PHE A 100       8.720 -29.855  18.545  1.00 51.76           C  
ANISOU  526  CG  PHE A 100     5636   7412   6620    239     88   -386       C  
ATOM    527  CD1 PHE A 100       9.584 -30.110  17.494  1.00 52.62           C  
ANISOU  527  CD1 PHE A 100     5729   7427   6837    256     72   -405       C  
ATOM    528  CD2 PHE A 100       8.301 -30.921  19.324  1.00 52.68           C  
ANISOU  528  CD2 PHE A 100     5813   7589   6613    258     21   -267       C  
ATOM    529  CE1 PHE A 100      10.024 -31.402  17.234  1.00 53.36           C  
ANISOU  529  CE1 PHE A 100     5855   7489   6930    299    -13   -321       C  
ATOM    530  CE2 PHE A 100       8.741 -32.209  19.061  1.00 53.38           C  
ANISOU  530  CE2 PHE A 100     5945   7636   6703    302    -68   -168       C  
ATOM    531  CZ  PHE A 100       9.599 -32.442  18.019  1.00 53.18           C  
ANISOU  531  CZ  PHE A 100     5891   7515   6799    325    -87   -201       C  
ATOM    532  N   PHE A 101       4.971 -28.906  18.091  1.00 49.85           N  
ANISOU  532  N   PHE A 101     5463   7086   6391    124    297   -262       N  
ATOM    533  CA  PHE A 101       3.861 -29.809  17.796  1.00 50.22           C  
ANISOU  533  CA  PHE A 101     5576   7088   6416    112    306   -126       C  
ATOM    534  C   PHE A 101       3.116 -29.381  16.515  1.00 49.93           C  
ANISOU  534  C   PHE A 101     5547   6919   6507     95    362   -110       C  
ATOM    535  O   PHE A 101       2.552 -30.233  15.841  1.00 50.16           O  
ANISOU  535  O   PHE A 101     5626   6876   6557    100    352     -5       O  
ATOM    536  CB  PHE A 101       2.948 -30.035  19.001  1.00 50.51           C  
ANISOU  536  CB  PHE A 101     5629   7232   6329     82    326    -99       C  
ATOM    537  CG  PHE A 101       3.641 -31.071  19.829  1.00 51.88           C  
ANISOU  537  CG  PHE A 101     5843   7492   6377    108    240    -33       C  
ATOM    538  CD1 PHE A 101       3.813 -32.353  19.348  1.00 53.17           C  
ANISOU  538  CD1 PHE A 101     6067   7590   6544    139    177     94       C  
ATOM    539  CD2 PHE A 101       4.320 -30.716  20.973  1.00 53.16           C  
ANISOU  539  CD2 PHE A 101     5974   7789   6436    113    209   -113       C  
ATOM    540  CE1 PHE A 101       4.562 -33.287  20.050  1.00 54.01           C  
ANISOU  540  CE1 PHE A 101     6209   7756   6555    174     79    154       C  
ATOM    541  CE2 PHE A 101       5.061 -31.656  21.683  1.00 54.06           C  
ANISOU  541  CE2 PHE A 101     6128   7974   6437    147    109    -49       C  
ATOM    542  CZ  PHE A 101       5.181 -32.934  21.214  1.00 53.79           C  
ANISOU  542  CZ  PHE A 101     6159   7864   6415    180     41     88       C  
ATOM    543  N   CYS A 102       3.187 -28.097  16.130  1.00 49.19           N  
ANISOU  543  N   CYS A 102     5404   6785   6502     79    412   -213       N  
ATOM    544  CA  CYS A 102       2.599 -27.630  14.884  1.00 49.01           C  
ANISOU  544  CA  CYS A 102     5395   6633   6594     66    450   -194       C  
ATOM    545  C   CYS A 102       3.409 -28.235  13.717  1.00 48.24           C  
ANISOU  545  C   CYS A 102     5335   6453   6543     83    418   -141       C  
ATOM    546  O   CYS A 102       2.814 -28.846  12.825  1.00 48.48           O  
ANISOU  546  O   CYS A 102     5412   6409   6598     83    413    -50       O  
ATOM    547  CB  CYS A 102       2.594 -26.104  14.845  1.00 50.31           C  
ANISOU  547  CB  CYS A 102     5502   6769   6845     46    501   -313       C  
ATOM    548  SG  CYS A 102       2.150 -25.384  13.240  1.00 56.42           S  
ANISOU  548  SG  CYS A 102     6303   7373   7760     32    531   -287       S  
ATOM    549  N   LYS A 103       4.767 -28.132  13.773  1.00 46.90           N  
ANISOU  549  N   LYS A 103     5135   6304   6380     94    396   -209       N  
ATOM    550  CA  LYS A 103       5.688 -28.651  12.754  1.00 46.02           C  
ANISOU  550  CA  LYS A 103     5042   6129   6316    102    375   -192       C  
ATOM    551  C   LYS A 103       5.663 -30.172  12.663  1.00 45.48           C  
ANISOU  551  C   LYS A 103     5014   6062   6203    131    315    -88       C  
ATOM    552  O   LYS A 103       5.616 -30.712  11.562  1.00 45.40           O  
ANISOU  552  O   LYS A 103     5036   5973   6239    127    315    -35       O  
ATOM    553  CB  LYS A 103       7.132 -28.190  13.036  1.00 46.93           C  
ANISOU  553  CB  LYS A 103     5098   6284   6449    108    365   -311       C  
ATOM    554  CG  LYS A 103       7.442 -26.767  12.616  1.00 49.19           C  
ANISOU  554  CG  LYS A 103     5347   6527   6817     70    433   -416       C  
ATOM    555  CD  LYS A 103       8.889 -26.401  12.922  1.00 51.69           C  
ANISOU  555  CD  LYS A 103     5599   6885   7158     73    426   -544       C  
ATOM    556  CE  LYS A 103       9.232 -24.946  12.679  1.00 54.07           C  
ANISOU  556  CE  LYS A 103     5856   7142   7545     30    500   -656       C  
ATOM    557  NZ  LYS A 103       9.404 -24.619  11.235  1.00 55.24           N  
ANISOU  557  NZ  LYS A 103     6044   7166   7777    -16    555   -633       N  
ATOM    558  N   LEU A 104       5.727 -30.853  13.823  1.00 45.01           N  
ANISOU  558  N   LEU A 104     4955   6093   6054    158    262    -61       N  
ATOM    559  CA  LEU A 104       5.748 -32.309  13.939  1.00 44.99           C  
ANISOU  559  CA  LEU A 104     4991   6094   6010    189    194     40       C  
ATOM    560  C   LEU A 104       4.432 -32.949  13.522  1.00 44.41           C  
ANISOU  560  C   LEU A 104     4971   5969   5933    174    214    155       C  
ATOM    561  O   LEU A 104       4.458 -33.915  12.764  1.00 44.59           O  
ANISOU  561  O   LEU A 104     5021   5930   5991    189    184    224       O  
ATOM    562  CB  LEU A 104       6.105 -32.729  15.371  1.00 45.51           C  
ANISOU  562  CB  LEU A 104     5052   6273   5968    216    130     43       C  
ATOM    563  CG  LEU A 104       6.196 -34.222  15.600  1.00 47.31           C  
ANISOU  563  CG  LEU A 104     5329   6501   6147    248     50    161       C  
ATOM    564  CD1 LEU A 104       7.360 -34.804  14.854  1.00 47.69           C  
ANISOU  564  CD1 LEU A 104     5359   6482   6278    286     -9    150       C  
ATOM    565  CD2 LEU A 104       6.281 -34.533  17.067  1.00 48.32           C  
ANISOU  565  CD2 LEU A 104     5467   6745   6146    265     -8    178       C  
ATOM    566  N   SER A 105       3.289 -32.430  14.026  1.00 43.53           N  
ANISOU  566  N   SER A 105     4866   5886   5789    146    264    165       N  
ATOM    567  CA  SER A 105       1.955 -32.921  13.696  1.00 42.95           C  
ANISOU  567  CA  SER A 105     4830   5767   5720    128    291    254       C  
ATOM    568  C   SER A 105       1.696 -32.788  12.198  1.00 42.17           C  
ANISOU  568  C   SER A 105     4742   5558   5724    122    314    262       C  
ATOM    569  O   SER A 105       1.250 -33.754  11.583  1.00 42.47           O  
ANISOU  569  O   SER A 105     4812   5541   5784    127    300    341       O  
ATOM    570  CB  SER A 105       0.897 -32.165  14.494  1.00 44.44           C  
ANISOU  570  CB  SER A 105     5004   6014   5867     96    346    225       C  
ATOM    571  OG  SER A 105      -0.393 -32.177  13.906  1.00 47.19           O  
ANISOU  571  OG  SER A 105     5357   6295   6278     75    392    244       O  
ATOM    572  N   SER A 106       1.988 -31.618  11.606  1.00 40.99           N  
ANISOU  572  N   SER A 106     4567   5374   5634    109    349    182       N  
ATOM    573  CA  SER A 106       1.787 -31.428  10.173  1.00 40.67           C  
ANISOU  573  CA  SER A 106     4548   5234   5673     98    366    197       C  
ATOM    574  C   SER A 106       2.693 -32.332   9.361  1.00 40.32           C  
ANISOU  574  C   SER A 106     4519   5154   5648    110    333    219       C  
ATOM    575  O   SER A 106       2.243 -32.876   8.358  1.00 40.41           O  
ANISOU  575  O   SER A 106     4559   5101   5694    105    331    270       O  
ATOM    576  CB  SER A 106       2.054 -29.987   9.771  1.00 41.97           C  
ANISOU  576  CB  SER A 106     4692   5364   5892     77    406    115       C  
ATOM    577  OG  SER A 106       1.386 -29.092  10.637  1.00 44.70           O  
ANISOU  577  OG  SER A 106     5002   5753   6229     69    434     61       O  
ATOM    578  N   TYR A 107       3.971 -32.479   9.776  1.00 39.87           N  
ANISOU  578  N   TYR A 107     4434   5141   5576    125    304    168       N  
ATOM    579  CA  TYR A 107       4.942 -33.330   9.094  1.00 39.96           C  
ANISOU  579  CA  TYR A 107     4441   5124   5618    138    270    164       C  
ATOM    580  C   TYR A 107       4.501 -34.776   9.093  1.00 39.95           C  
ANISOU  580  C   TYR A 107     4465   5107   5609    163    223    257       C  
ATOM    581  O   TYR A 107       4.451 -35.357   8.024  1.00 40.09           O  
ANISOU  581  O   TYR A 107     4492   5066   5674    158    220    275       O  
ATOM    582  CB  TYR A 107       6.350 -33.176   9.683  1.00 40.20           C  
ANISOU  582  CB  TYR A 107     4423   5209   5643    156    240     75       C  
ATOM    583  CG  TYR A 107       7.377 -34.109   9.080  1.00 41.16           C  
ANISOU  583  CG  TYR A 107     4525   5304   5811    174    198     54       C  
ATOM    584  CD1 TYR A 107       7.821 -33.939   7.777  1.00 42.19           C  
ANISOU  584  CD1 TYR A 107     4651   5376   6003    140    238      8       C  
ATOM    585  CD2 TYR A 107       7.911 -35.156   9.816  1.00 42.08           C  
ANISOU  585  CD2 TYR A 107     4628   5452   5909    223    115     79       C  
ATOM    586  CE1 TYR A 107       8.768 -34.789   7.220  1.00 43.16           C  
ANISOU  586  CE1 TYR A 107     4742   5479   6176    151    206    -33       C  
ATOM    587  CE2 TYR A 107       8.857 -36.014   9.272  1.00 42.97           C  
ANISOU  587  CE2 TYR A 107     4709   5532   6084    244     70     45       C  
ATOM    588  CZ  TYR A 107       9.286 -35.827   7.973  1.00 44.20           C  
ANISOU  588  CZ  TYR A 107     4847   5637   6309    207    120    -20       C  
ATOM    589  OH  TYR A 107      10.237 -36.670   7.444  1.00 46.26           O  
ANISOU  589  OH  TYR A 107     5065   5872   6640    223     81    -75       O  
ATOM    590  N   LEU A 108       4.133 -35.348  10.257  1.00 39.79           N  
ANISOU  590  N   LEU A 108     4456   5137   5526    183    190    316       N  
ATOM    591  CA  LEU A 108       3.649 -36.731  10.337  1.00 40.12           C  
ANISOU  591  CA  LEU A 108     4527   5151   5564    201    149    416       C  
ATOM    592  C   LEU A 108       2.417 -36.954   9.471  1.00 40.35           C  
ANISOU  592  C   LEU A 108     4582   5118   5630    177    189    470       C  
ATOM    593  O   LEU A 108       2.297 -38.006   8.847  1.00 40.69           O  
ANISOU  593  O   LEU A 108     4636   5107   5717    186    166    518       O  
ATOM    594  CB  LEU A 108       3.317 -37.124  11.775  1.00 40.29           C  
ANISOU  594  CB  LEU A 108     4569   5242   5498    212    118    477       C  
ATOM    595  CG  LEU A 108       4.473 -37.192  12.745  1.00 41.61           C  
ANISOU  595  CG  LEU A 108     4717   5475   5618    246     51    443       C  
ATOM    596  CD1 LEU A 108       3.968 -37.547  14.141  1.00 42.17           C  
ANISOU  596  CD1 LEU A 108     4823   5624   5575    244     29    513       C  
ATOM    597  CD2 LEU A 108       5.540 -38.166  12.264  1.00 42.02           C  
ANISOU  597  CD2 LEU A 108     4752   5476   5736    286    -22    443       C  
ATOM    598  N   ILE A 109       1.501 -35.973   9.429  1.00 39.96           N  
ANISOU  598  N   ILE A 109     4537   5072   5573    151    244    452       N  
ATOM    599  CA  ILE A 109       0.316 -36.086   8.578  1.00 40.23           C  
ANISOU  599  CA  ILE A 109     4589   5047   5649    134    273    490       C  
ATOM    600  C   ILE A 109       0.745 -36.110   7.104  1.00 40.00           C  
ANISOU  600  C   ILE A 109     4563   4953   5680    129    271    466       C  
ATOM    601  O   ILE A 109       0.430 -37.061   6.408  1.00 40.29           O  
ANISOU  601  O   ILE A 109     4610   4946   5752    133    256    506       O  
ATOM    602  CB  ILE A 109      -0.782 -35.002   8.883  1.00 40.63           C  
ANISOU  602  CB  ILE A 109     4635   5110   5694    113    321    466       C  
ATOM    603  CG1 ILE A 109      -1.527 -35.304  10.218  1.00 41.22           C  
ANISOU  603  CG1 ILE A 109     4707   5246   5707    103    336    498       C  
ATOM    604  CG2 ILE A 109      -1.779 -34.863   7.718  1.00 40.81           C  
ANISOU  604  CG2 ILE A 109     4669   5060   5778    104    336    479       C  
ATOM    605  CD1 ILE A 109      -2.555 -34.278  10.650  1.00 41.99           C  
ANISOU  605  CD1 ILE A 109     4782   5366   5805     81    384    451       C  
ATOM    606  N   PHE A 110       1.517 -35.120   6.661  1.00 39.40           N  
ANISOU  606  N   PHE A 110     4479   4877   5616    117    289    396       N  
ATOM    607  CA  PHE A 110       1.969 -35.054   5.282  1.00 39.56           C  
ANISOU  607  CA  PHE A 110     4508   4847   5675     97    298    370       C  
ATOM    608  C   PHE A 110       2.768 -36.265   4.814  1.00 39.79           C  
ANISOU  608  C   PHE A 110     4523   4865   5732    109    265    367       C  
ATOM    609  O   PHE A 110       2.626 -36.623   3.646  1.00 39.97           O  
ANISOU  609  O   PHE A 110     4557   4846   5783     92    272    368       O  
ATOM    610  CB  PHE A 110       2.736 -33.768   5.011  1.00 39.50           C  
ANISOU  610  CB  PHE A 110     4495   4840   5671     71    333    295       C  
ATOM    611  CG  PHE A 110       1.851 -32.759   4.341  1.00 40.42           C  
ANISOU  611  CG  PHE A 110     4646   4910   5801     47    362    310       C  
ATOM    612  CD1 PHE A 110       1.044 -31.917   5.090  1.00 41.27           C  
ANISOU  612  CD1 PHE A 110     4748   5025   5907     53    373    313       C  
ATOM    613  CD2 PHE A 110       1.780 -32.686   2.960  1.00 41.32           C  
ANISOU  613  CD2 PHE A 110     4798   4972   5930     19    372    321       C  
ATOM    614  CE1 PHE A 110       0.213 -30.995   4.470  1.00 41.97           C  
ANISOU  614  CE1 PHE A 110     4863   5058   6025     40    386    324       C  
ATOM    615  CE2 PHE A 110       0.953 -31.762   2.340  1.00 42.06           C  
ANISOU  615  CE2 PHE A 110     4931   5016   6035      3    382    346       C  
ATOM    616  CZ  PHE A 110       0.169 -30.927   3.098  1.00 41.95           C  
ANISOU  616  CZ  PHE A 110     4906   4997   6035     18    383    348       C  
ATOM    617  N   VAL A 111       3.599 -36.905   5.685  1.00 39.49           N  
ANISOU  617  N   VAL A 111     4456   4861   5687    140    223    359       N  
ATOM    618  CA  VAL A 111       4.332 -38.093   5.225  1.00 39.25           C  
ANISOU  618  CA  VAL A 111     4402   4806   5706    157    183    349       C  
ATOM    619  C   VAL A 111       3.301 -39.229   5.081  1.00 38.82           C  
ANISOU  619  C   VAL A 111     4366   4713   5672    169    163    435       C  
ATOM    620  O   VAL A 111       3.273 -39.858   4.034  1.00 38.86           O  
ANISOU  620  O   VAL A 111     4363   4675   5728    161    162    425       O  
ATOM    621  CB  VAL A 111       5.680 -38.496   5.949  1.00 39.61           C  
ANISOU  621  CB  VAL A 111     4402   4882   5764    191    129    297       C  
ATOM    622  CG1 VAL A 111       6.128 -37.473   6.972  1.00 39.89           C  
ANISOU  622  CG1 VAL A 111     4427   4982   5747    196    133    256       C  
ATOM    623  CG2 VAL A 111       5.667 -39.907   6.548  1.00 39.92           C  
ANISOU  623  CG2 VAL A 111     4437   4904   5827    236     55    364       C  
ATOM    624  N   ALA A 112       2.385 -39.395   6.053  1.00 38.26           N  
ANISOU  624  N   ALA A 112     4319   4658   5562    179    159    510       N  
ATOM    625  CA  ALA A 112       1.362 -40.440   5.993  1.00 38.38           C  
ANISOU  625  CA  ALA A 112     4349   4634   5600    182    151    589       C  
ATOM    626  C   ALA A 112       0.496 -40.308   4.746  1.00 38.95           C  
ANISOU  626  C   ALA A 112     4428   4663   5708    158    185    580       C  
ATOM    627  O   ALA A 112       0.189 -41.306   4.100  1.00 39.21           O  
ANISOU  627  O   ALA A 112     4451   4650   5796    161    171    597       O  
ATOM    628  CB  ALA A 112       0.503 -40.391   7.233  1.00 38.21           C  
ANISOU  628  CB  ALA A 112     4352   4647   5519    180    162    653       C  
ATOM    629  N   MET A 113       0.162 -39.055   4.389  1.00 38.88           N  
ANISOU  629  N   MET A 113     4433   4666   5673    136    223    549       N  
ATOM    630  CA  MET A 113      -0.600 -38.612   3.230  1.00 38.86           C  
ANISOU  630  CA  MET A 113     4446   4630   5688    116    245    539       C  
ATOM    631  C   MET A 113      -0.001 -39.234   1.971  1.00 39.15           C  
ANISOU  631  C   MET A 113     4474   4640   5763    106    235    504       C  
ATOM    632  O   MET A 113      -0.711 -39.950   1.292  1.00 39.13           O  
ANISOU  632  O   MET A 113     4467   4607   5794    106    226    523       O  
ATOM    633  CB  MET A 113      -0.515 -37.083   3.155  1.00 39.51           C  
ANISOU  633  CB  MET A 113     4546   4726   5740     98    273    500       C  
ATOM    634  CG  MET A 113      -1.763 -36.424   2.742  1.00 42.56           C  
ANISOU  634  CG  MET A 113     4951   5087   6132     91    284    518       C  
ATOM    635  SD  MET A 113      -1.468 -35.329   1.346  1.00 48.02           S  
ANISOU  635  SD  MET A 113     5682   5747   6818     61    296    485       S  
ATOM    636  CE  MET A 113      -1.662 -36.517  -0.037  1.00 46.61           C  
ANISOU  636  CE  MET A 113     5513   5544   6653     49    277    490       C  
ATOM    637  N   TYR A 114       1.324 -39.045   1.712  1.00 39.35           N  
ANISOU  637  N   TYR A 114     4484   4681   5786     96    237    443       N  
ATOM    638  CA  TYR A 114       2.022 -39.618   0.554  1.00 39.86           C  
ANISOU  638  CA  TYR A 114     4529   4730   5885     77    237    386       C  
ATOM    639  C   TYR A 114       2.266 -41.111   0.708  1.00 39.58           C  
ANISOU  639  C   TYR A 114     4451   4672   5915    105    196    390       C  
ATOM    640  O   TYR A 114       1.955 -41.836  -0.224  1.00 40.13           O  
ANISOU  640  O   TYR A 114     4508   4716   6024     94    195    374       O  
ATOM    641  CB  TYR A 114       3.367 -38.923   0.269  1.00 40.47           C  
ANISOU  641  CB  TYR A 114     4595   4833   5950     50    262    303       C  
ATOM    642  CG  TYR A 114       3.265 -37.434   0.066  1.00 42.10           C  
ANISOU  642  CG  TYR A 114     4844   5048   6105     15    305    295       C  
ATOM    643  CD1 TYR A 114       2.495 -36.904  -0.957  1.00 43.71           C  
ANISOU  643  CD1 TYR A 114     5096   5228   6282    -14    322    324       C  
ATOM    644  CD2 TYR A 114       3.990 -36.557   0.851  1.00 43.31           C  
ANISOU  644  CD2 TYR A 114     4986   5226   6242     10    323    254       C  
ATOM    645  CE1 TYR A 114       2.395 -35.532  -1.149  1.00 44.97           C  
ANISOU  645  CE1 TYR A 114     5301   5380   6406    -44    353    327       C  
ATOM    646  CE2 TYR A 114       3.900 -35.184   0.672  1.00 44.63           C  
ANISOU  646  CE2 TYR A 114     5191   5387   6379    -24    364    246       C  
ATOM    647  CZ  TYR A 114       3.111 -34.672  -0.339  1.00 45.88           C  
ANISOU  647  CZ  TYR A 114     5404   5512   6516    -51    377    287       C  
ATOM    648  OH  TYR A 114       3.012 -33.309  -0.506  1.00 47.69           O  
ANISOU  648  OH  TYR A 114     5676   5720   6726    -81    408    290       O  
ATOM    649  N   ALA A 115       2.828 -41.578   1.848  1.00 38.56           N  
ANISOU  649  N   ALA A 115     4300   4550   5801    142    158    409       N  
ATOM    650  CA  ALA A 115       3.114 -42.988   2.088  1.00 38.40           C  
ANISOU  650  CA  ALA A 115     4243   4491   5855    174    107    423       C  
ATOM    651  C   ALA A 115       1.900 -43.894   1.843  1.00 38.93           C  
ANISOU  651  C   ALA A 115     4319   4512   5959    176    106    487       C  
ATOM    652  O   ALA A 115       2.032 -44.885   1.136  1.00 39.31           O  
ANISOU  652  O   ALA A 115     4332   4521   6084    176     92    455       O  
ATOM    653  CB  ALA A 115       3.647 -43.190   3.490  1.00 38.26           C  
ANISOU  653  CB  ALA A 115     4223   4489   5827    215     56    461       C  
ATOM    654  N   SER A 116       0.713 -43.535   2.355  1.00 38.68           N  
ANISOU  654  N   SER A 116     4326   4487   5882    171    127    559       N  
ATOM    655  CA  SER A 116      -0.498 -44.331   2.130  1.00 39.03           C  
ANISOU  655  CA  SER A 116     4373   4491   5966    166    134    608       C  
ATOM    656  C   SER A 116      -0.988 -44.300   0.664  1.00 39.50           C  
ANISOU  656  C   SER A 116     4420   4536   6050    143    155    555       C  
ATOM    657  O   SER A 116      -1.612 -45.255   0.210  1.00 40.11           O  
ANISOU  657  O   SER A 116     4476   4573   6189    143    151    564       O  
ATOM    658  CB  SER A 116      -1.620 -43.856   3.039  1.00 39.85           C  
ANISOU  658  CB  SER A 116     4511   4615   6015    160    161    672       C  
ATOM    659  OG  SER A 116      -1.829 -42.475   2.800  1.00 41.77           O  
ANISOU  659  OG  SER A 116     4774   4899   6199    144    190    637       O  
ATOM    660  N   VAL A 117      -0.744 -43.207  -0.058  1.00 39.03           N  
ANISOU  660  N   VAL A 117     4378   4510   5940    119    177    503       N  
ATOM    661  CA  VAL A 117      -1.129 -43.110  -1.463  1.00 38.97           C  
ANISOU  661  CA  VAL A 117     4372   4500   5933     93    190    459       C  
ATOM    662  C   VAL A 117      -0.208 -44.009  -2.270  1.00 39.11           C  
ANISOU  662  C   VAL A 117     4344   4509   6006     83    181    385       C  
ATOM    663  O   VAL A 117      -0.697 -44.781  -3.095  1.00 39.00           O  
ANISOU  663  O   VAL A 117     4306   4476   6037     76    176    360       O  
ATOM    664  CB  VAL A 117      -1.114 -41.651  -1.966  1.00 39.58           C  
ANISOU  664  CB  VAL A 117     4498   4609   5933     66    213    444       C  
ATOM    665  CG1 VAL A 117      -1.178 -41.586  -3.480  1.00 40.04           C  
ANISOU  665  CG1 VAL A 117     4567   4673   5973     33    218    398       C  
ATOM    666  CG2 VAL A 117      -2.261 -40.859  -1.359  1.00 40.26           C  
ANISOU  666  CG2 VAL A 117     4613   4692   5991     79    216    501       C  
ATOM    667  N   PHE A 118       1.117 -43.942  -1.998  1.00 39.28           N  
ANISOU  667  N   PHE A 118     4345   4545   6034     84    178    339       N  
ATOM    668  CA  PHE A 118       2.142 -44.744  -2.667  1.00 40.21           C  
ANISOU  668  CA  PHE A 118     4405   4656   6218     75    170    247       C  
ATOM    669  C   PHE A 118       1.959 -46.243  -2.358  1.00 41.83           C  
ANISOU  669  C   PHE A 118     4557   4800   6536    112    127    264       C  
ATOM    670  O   PHE A 118       2.247 -47.082  -3.213  1.00 41.65           O  
ANISOU  670  O   PHE A 118     4479   4758   6588    102    122    188       O  
ATOM    671  CB  PHE A 118       3.551 -44.319  -2.241  1.00 39.85           C  
ANISOU  671  CB  PHE A 118     4339   4635   6167     73    171    188       C  
ATOM    672  CG  PHE A 118       4.021 -42.909  -2.517  1.00 40.20           C  
ANISOU  672  CG  PHE A 118     4425   4728   6122     32    219    159       C  
ATOM    673  CD1 PHE A 118       3.288 -42.060  -3.324  1.00 40.94           C  
ANISOU  673  CD1 PHE A 118     4578   4839   6139     -7    255    183       C  
ATOM    674  CD2 PHE A 118       5.174 -42.416  -1.924  1.00 40.46           C  
ANISOU  674  CD2 PHE A 118     4438   4783   6153     35    221    110       C  
ATOM    675  CE1 PHE A 118       3.707 -40.748  -3.536  1.00 41.48           C  
ANISOU  675  CE1 PHE A 118     4690   4935   6133    -46    297    168       C  
ATOM    676  CE2 PHE A 118       5.588 -41.111  -2.141  1.00 40.82           C  
ANISOU  676  CE2 PHE A 118     4519   4863   6127     -7    270     83       C  
ATOM    677  CZ  PHE A 118       4.854 -40.285  -2.943  1.00 40.82           C  
ANISOU  677  CZ  PHE A 118     4584   4870   6055    -49    310    117       C  
ATOM    678  N   CYS A 119       1.479 -46.574  -1.137  1.00 43.08           N  
ANISOU  678  N   CYS A 119     4735   4928   6707    150     98    363       N  
ATOM    679  CA  CYS A 119       1.210 -47.953  -0.717  1.00 44.83           C  
ANISOU  679  CA  CYS A 119     4924   5079   7031    181     58    406       C  
ATOM    680  C   CYS A 119      -0.046 -48.498  -1.345  1.00 45.32           C  
ANISOU  680  C   CYS A 119     4978   5111   7130    165     78    418       C  
ATOM    681  O   CYS A 119      -0.110 -49.693  -1.609  1.00 46.06           O  
ANISOU  681  O   CYS A 119     5024   5143   7335    176     56    403       O  
ATOM    682  CB  CYS A 119       1.165 -48.078   0.798  1.00 47.50           C  
ANISOU  682  CB  CYS A 119     5299   5402   7347    212     28    515       C  
ATOM    683  SG  CYS A 119       2.800 -48.047   1.578  1.00 57.69           S  
ANISOU  683  SG  CYS A 119     6570   6701   8647    251    -33    493       S  
ATOM    684  N   LEU A 120      -1.057 -47.639  -1.577  1.00 44.57           N  
ANISOU  684  N   LEU A 120     4926   5051   6956    143    114    443       N  
ATOM    685  CA  LEU A 120      -2.268 -48.017  -2.283  1.00 44.01           C  
ANISOU  685  CA  LEU A 120     4845   4964   6912    129    130    438       C  
ATOM    686  C   LEU A 120      -1.889 -48.306  -3.732  1.00 43.94           C  
ANISOU  686  C   LEU A 120     4794   4972   6929    106    133    328       C  
ATOM    687  O   LEU A 120      -2.308 -49.315  -4.266  1.00 43.86           O  
ANISOU  687  O   LEU A 120     4733   4924   7008    106    126    291       O  
ATOM    688  CB  LEU A 120      -3.260 -46.865  -2.237  1.00 44.11           C  
ANISOU  688  CB  LEU A 120     4910   5017   6833    118    154    474       C  
ATOM    689  CG  LEU A 120      -4.363 -47.011  -1.223  1.00 45.45           C  
ANISOU  689  CG  LEU A 120     5094   5161   7014    126    165    553       C  
ATOM    690  CD1 LEU A 120      -5.095 -45.679  -1.007  1.00 45.67           C  
ANISOU  690  CD1 LEU A 120     5167   5232   6953    120    185    576       C  
ATOM    691  CD2 LEU A 120      -5.306 -48.116  -1.637  1.00 46.17           C  
ANISOU  691  CD2 LEU A 120     5143   5205   7195    122    168    538       C  
ATOM    692  N   THR A 121      -1.033 -47.459  -4.339  1.00 44.27           N  
ANISOU  692  N   THR A 121     4855   5071   6894     80    149    271       N  
ATOM    693  CA  THR A 121      -0.533 -47.596  -5.716  1.00 45.08           C  
ANISOU  693  CA  THR A 121     4927   5208   6993     42    164    160       C  
ATOM    694  C   THR A 121       0.355 -48.839  -5.886  1.00 46.06           C  
ANISOU  694  C   THR A 121     4966   5297   7237     49    148     76       C  
ATOM    695  O   THR A 121       0.334 -49.471  -6.940  1.00 46.32           O  
ANISOU  695  O   THR A 121     4949   5341   7309     23    158    -17       O  
ATOM    696  CB  THR A 121       0.214 -46.324  -6.189  1.00 45.71           C  
ANISOU  696  CB  THR A 121     5057   5354   6958      2    195    128       C  
ATOM    697  OG1 THR A 121      -0.368 -45.140  -5.632  1.00 46.51           O  
ANISOU  697  OG1 THR A 121     5232   5469   6973      8    200    214       O  
ATOM    698  CG2 THR A 121       0.256 -46.211  -7.702  1.00 45.67           C  
ANISOU  698  CG2 THR A 121     5051   5398   6904    -52    219     41       C  
ATOM    699  N   GLY A 122       1.139 -49.165  -4.864  1.00 46.34           N  
ANISOU  699  N   GLY A 122     4983   5293   7332     84    120    104       N  
ATOM    700  CA  GLY A 122       1.986 -50.354  -4.874  1.00 46.98           C  
ANISOU  700  CA  GLY A 122     4979   5322   7551    105     88     32       C  
ATOM    701  C   GLY A 122       1.158 -51.619  -4.728  1.00 47.48           C  
ANISOU  701  C   GLY A 122     5002   5303   7734    130     62     66       C  
ATOM    702  O   GLY A 122       1.471 -52.646  -5.323  1.00 47.59           O  
ANISOU  702  O   GLY A 122     4935   5278   7869    129     49    -26       O  
ATOM    703  N   LEU A 123       0.072 -51.546  -3.950  1.00 47.71           N  
ANISOU  703  N   LEU A 123     5084   5306   7739    146     60    187       N  
ATOM    704  CA  LEU A 123      -0.853 -52.658  -3.748  1.00 48.45           C  
ANISOU  704  CA  LEU A 123     5150   5318   7941    159     49    230       C  
ATOM    705  C   LEU A 123      -1.664 -52.899  -5.025  1.00 49.54           C  
ANISOU  705  C   LEU A 123     5251   5476   8098    128     78    149       C  
ATOM    706  O   LEU A 123      -1.946 -54.039  -5.372  1.00 49.53           O  
ANISOU  706  O   LEU A 123     5182   5410   8225    132     69    108       O  
ATOM    707  CB  LEU A 123      -1.785 -52.330  -2.573  1.00 48.37           C  
ANISOU  707  CB  LEU A 123     5211   5290   7877    171     54    373       C  
ATOM    708  CG  LEU A 123      -2.688 -53.440  -2.086  1.00 49.48           C  
ANISOU  708  CG  LEU A 123     5338   5342   8120    177     53    441       C  
ATOM    709  CD1 LEU A 123      -1.881 -54.617  -1.614  1.00 50.21           C  
ANISOU  709  CD1 LEU A 123     5379   5337   8360    205      4    439       C  
ATOM    710  CD2 LEU A 123      -3.562 -52.958  -0.963  1.00 49.88           C  
ANISOU  710  CD2 LEU A 123     5462   5394   8094    176     70    571       C  
ATOM    711  N   SER A 124      -2.035 -51.821  -5.719  1.00 50.53           N  
ANISOU  711  N   SER A 124     5418   5687   8095     99    107    125       N  
ATOM    712  CA  SER A 124      -2.745 -51.880  -6.985  1.00 52.06           C  
ANISOU  712  CA  SER A 124     5587   5919   8275     70    123     45       C  
ATOM    713  C   SER A 124      -1.817 -52.417  -8.087  1.00 53.62           C  
ANISOU  713  C   SER A 124     5712   6143   8519     43    128   -100       C  
ATOM    714  O   SER A 124      -2.282 -53.082  -9.009  1.00 53.87           O  
ANISOU  714  O   SER A 124     5690   6185   8593     25    133   -186       O  
ATOM    715  CB  SER A 124      -3.274 -50.497  -7.356  1.00 53.58           C  
ANISOU  715  CB  SER A 124     5857   6190   8310     50    139     74       C  
ATOM    716  OG  SER A 124      -4.057 -50.513  -8.538  1.00 56.14           O  
ANISOU  716  OG  SER A 124     6168   6552   8613     30    139     15       O  
ATOM    717  N   PHE A 125      -0.511 -52.141  -7.994  1.00 54.75           N  
ANISOU  717  N   PHE A 125     5845   6301   8656     39    128   -141       N  
ATOM    718  CA  PHE A 125       0.453 -52.639  -8.960  1.00 56.30           C  
ANISOU  718  CA  PHE A 125     5962   6523   8904      8    140   -294       C  
ATOM    719  C   PHE A 125       0.776 -54.117  -8.677  1.00 56.86           C  
ANISOU  719  C   PHE A 125     5933   6493   9179     43    105   -340       C  
ATOM    720  O   PHE A 125       0.948 -54.889  -9.619  1.00 56.55           O  
ANISOU  720  O   PHE A 125     5804   6455   9226     21    113   -476       O  
ATOM    721  CB  PHE A 125       1.711 -51.758  -8.985  1.00 57.11           C  
ANISOU  721  CB  PHE A 125     6091   6685   8923    -17    160   -332       C  
ATOM    722  CG  PHE A 125       2.761 -52.293  -9.923  1.00 58.95           C  
ANISOU  722  CG  PHE A 125     6234   6948   9216    -56    182   -506       C  
ATOM    723  CD1 PHE A 125       2.585 -52.228 -11.293  1.00 60.16           C  
ANISOU  723  CD1 PHE A 125     6383   7192   9285   -125    229   -612       C  
ATOM    724  CD2 PHE A 125       3.883 -52.939  -9.436  1.00 60.32           C  
ANISOU  724  CD2 PHE A 125     6324   7060   9534    -25    152   -569       C  
ATOM    725  CE1 PHE A 125       3.521 -52.780 -12.156  1.00 61.11           C  
ANISOU  725  CE1 PHE A 125     6411   7348   9459   -171    259   -787       C  
ATOM    726  CE2 PHE A 125       4.823 -53.479 -10.301  1.00 61.29           C  
ANISOU  726  CE2 PHE A 125     6348   7210   9729    -63    175   -750       C  
ATOM    727  CZ  PHE A 125       4.632 -53.406 -11.654  1.00 61.05           C  
ANISOU  727  CZ  PHE A 125     6310   7278   9610   -140    235   -863       C  
ATOM    728  N   ASP A 126       0.808 -54.523  -7.388  1.00 57.63           N  
ANISOU  728  N   ASP A 126     6046   6500   9352     96     63   -227       N  
ATOM    729  CA  ASP A 126       1.035 -55.926  -7.027  1.00 58.80           C  
ANISOU  729  CA  ASP A 126     6112   6531   9698    134     19   -244       C  
ATOM    730  C   ASP A 126      -0.157 -56.790  -7.436  1.00 59.77           C  
ANISOU  730  C   ASP A 126     6195   6604   9912    127     29   -252       C  
ATOM    731  O   ASP A 126       0.028 -57.948  -7.811  1.00 60.06           O  
ANISOU  731  O   ASP A 126     6134   6567  10119    135     11   -340       O  
ATOM    732  CB  ASP A 126       1.324 -56.114  -5.535  1.00 60.64           C  
ANISOU  732  CB  ASP A 126     6388   6681   9971    187    -34   -103       C  
ATOM    733  CG  ASP A 126       1.895 -57.496  -5.274  1.00 66.01           C  
ANISOU  733  CG  ASP A 126     6980   7237  10864    226    -92   -138       C  
ATOM    734  OD1 ASP A 126       1.098 -58.454  -5.147  1.00 65.95           O  
ANISOU  734  OD1 ASP A 126     6948   7139  10970    234    -99    -99       O  
ATOM    735  OD2 ASP A 126       3.147 -57.630  -5.256  1.00 69.43           O  
ANISOU  735  OD2 ASP A 126     7358   7660  11364    247   -131   -221       O  
ATOM    736  N   ARG A 127      -1.384 -56.237  -7.346  1.00 59.98           N  
ANISOU  736  N   ARG A 127     6289   6663   9839    114     57   -169       N  
ATOM    737  CA  ARG A 127      -2.597 -56.922  -7.794  1.00 60.40           C  
ANISOU  737  CA  ARG A 127     6302   6682   9965    104     72   -191       C  
ATOM    738  C   ARG A 127      -2.639 -57.008  -9.318  1.00 60.12           C  
ANISOU  738  C   ARG A 127     6201   6727   9916     64     95   -357       C  
ATOM    739  O   ARG A 127      -3.177 -57.967  -9.855  1.00 60.05           O  
ANISOU  739  O   ARG A 127     6109   6676  10030     58     97   -438       O  
ATOM    740  CB  ARG A 127      -3.857 -56.264  -7.214  1.00 62.30           C  
ANISOU  740  CB  ARG A 127     6624   6934  10113    104     92    -67       C  
ATOM    741  CG  ARG A 127      -4.394 -56.966  -5.963  1.00 66.32           C  
ANISOU  741  CG  ARG A 127     7153   7330  10716    128     82     65       C  
ATOM    742  CD  ARG A 127      -3.379 -57.094  -4.831  1.00 70.27           C  
ANISOU  742  CD  ARG A 127     7689   7781  11231    159     44    152       C  
ATOM    743  NE  ARG A 127      -3.379 -58.433  -4.239  1.00 74.41           N  
ANISOU  743  NE  ARG A 127     8180   8167  11927    180     16    207       N  
ATOM    744  CZ  ARG A 127      -2.517 -59.399  -4.556  1.00 77.89           C  
ANISOU  744  CZ  ARG A 127     8533   8529  12533    198    -22    125       C  
ATOM    745  NH1 ARG A 127      -2.590 -60.584  -3.963  1.00 78.51           N  
ANISOU  745  NH1 ARG A 127     8593   8468  12770    218    -53    194       N  
ATOM    746  NH2 ARG A 127      -1.569 -59.184  -5.458  1.00 77.74           N  
ANISOU  746  NH2 ARG A 127     8445   8568  12526    192    -27    -30       N  
ATOM    747  N   TYR A 128      -2.034 -56.031 -10.005  1.00 59.99           N  
ANISOU  747  N   TYR A 128     6220   6823   9751     32    113   -412       N  
ATOM    748  CA  TYR A 128      -1.894 -56.016 -11.436  1.00 60.81           C  
ANISOU  748  CA  TYR A 128     6277   7020   9810    -16    136   -566       C  
ATOM    749  C   TYR A 128      -0.959 -57.152 -11.838  1.00 61.48           C  
ANISOU  749  C   TYR A 128     6238   7061  10062    -20    132   -713       C  
ATOM    750  O   TYR A 128      -1.295 -57.880 -12.766  1.00 62.01           O  
ANISOU  750  O   TYR A 128     6221   7142  10199    -44    143   -841       O  
ATOM    751  CB  TYR A 128      -1.347 -54.659 -11.911  1.00 61.30           C  
ANISOU  751  CB  TYR A 128     6421   7199   9670    -56    161   -568       C  
ATOM    752  CG  TYR A 128      -0.772 -54.708 -13.308  1.00 62.80           C  
ANISOU  752  CG  TYR A 128     6563   7488   9811   -119    193   -737       C  
ATOM    753  CD1 TYR A 128      -1.577 -54.991 -14.401  1.00 64.26           C  
ANISOU  753  CD1 TYR A 128     6717   7730   9969   -148    198   -820       C  
ATOM    754  CD2 TYR A 128       0.588 -54.554 -13.526  1.00 64.15           C  
ANISOU  754  CD2 TYR A 128     6706   7696   9973   -152    219   -829       C  
ATOM    755  CE1 TYR A 128      -1.050 -55.088 -15.681  1.00 65.58           C  
ANISOU  755  CE1 TYR A 128     6838   7997  10081   -214    230   -982       C  
ATOM    756  CE2 TYR A 128       1.127 -54.638 -14.804  1.00 65.50           C  
ANISOU  756  CE2 TYR A 128     6828   7964  10096   -223    261   -995       C  
ATOM    757  CZ  TYR A 128       0.304 -54.911 -15.880  1.00 66.85           C  
ANISOU  757  CZ  TYR A 128     6978   8198  10225   -255    267  -1069       C  
ATOM    758  OH  TYR A 128       0.820 -55.011 -17.149  1.00 69.06           O  
ANISOU  758  OH  TYR A 128     7212   8586  10441   -333    311  -1237       O  
ATOM    759  N   LEU A 129       0.212 -57.300 -11.179  1.00 61.39           N  
ANISOU  759  N   LEU A 129     6206   6999  10121      3    112   -711       N  
ATOM    760  CA  LEU A 129       1.145 -58.370 -11.543  1.00 61.95           C  
ANISOU  760  CA  LEU A 129     6147   7020  10373      4    100   -865       C  
ATOM    761  C   LEU A 129       0.584 -59.748 -11.266  1.00 63.28           C  
ANISOU  761  C   LEU A 129     6231   7056  10758     41     68   -870       C  
ATOM    762  O   LEU A 129       0.844 -60.660 -12.030  1.00 63.43           O  
ANISOU  762  O   LEU A 129     6131   7061  10910     23     74  -1034       O  
ATOM    763  CB  LEU A 129       2.519 -58.214 -10.892  1.00 61.80           C  
ANISOU  763  CB  LEU A 129     6113   6971  10395     28     74   -875       C  
ATOM    764  CG  LEU A 129       3.359 -57.026 -11.341  1.00 62.77           C  
ANISOU  764  CG  LEU A 129     6285   7221  10344    -21    118   -925       C  
ATOM    765  CD1 LEU A 129       4.657 -56.987 -10.583  1.00 63.13           C  
ANISOU  765  CD1 LEU A 129     6303   7224  10459     12     84   -940       C  
ATOM    766  CD2 LEU A 129       3.612 -57.055 -12.837  1.00 63.27           C  
ANISOU  766  CD2 LEU A 129     6290   7397  10354   -100    178  -1113       C  
ATOM    767  N   ALA A 130      -0.228 -59.904 -10.221  1.00 64.40           N  
ANISOU  767  N   ALA A 130     6432   7103  10934     82     43   -702       N  
ATOM    768  CA  ALA A 130      -0.868 -61.191  -9.914  1.00 66.19           C  
ANISOU  768  CA  ALA A 130     6591   7194  11366    107     22   -690       C  
ATOM    769  C   ALA A 130      -1.870 -61.661 -11.015  1.00 67.77           C  
ANISOU  769  C   ALA A 130     6723   7431  11597     70     59   -807       C  
ATOM    770  O   ALA A 130      -2.254 -62.832 -11.050  1.00 67.86           O  
ANISOU  770  O   ALA A 130     6644   7335  11805     80     50   -856       O  
ATOM    771  CB  ALA A 130      -1.573 -61.106  -8.569  1.00 66.51           C  
ANISOU  771  CB  ALA A 130     6727   7147  11397    141      3   -477       C  
ATOM    772  N   ILE A 131      -2.286 -60.744 -11.900  1.00 68.78           N  
ANISOU  772  N   ILE A 131     6894   7705  11534     28     95   -850       N  
ATOM    773  CA  ILE A 131      -3.191 -61.027 -13.004  1.00 70.25           C  
ANISOU  773  CA  ILE A 131     7027   7954  11709     -6    120   -963       C  
ATOM    774  C   ILE A 131      -2.367 -61.361 -14.249  1.00 72.09           C  
ANISOU  774  C   ILE A 131     7159   8273  11960    -50    139  -1182       C  
ATOM    775  O   ILE A 131      -2.651 -62.354 -14.908  1.00 72.73           O  
ANISOU  775  O   ILE A 131     7133   8347  12153    -66    147  -1321       O  
ATOM    776  CB  ILE A 131      -4.161 -59.828 -13.242  1.00 70.49           C  
ANISOU  776  CB  ILE A 131     7171   8093  11519    -21    133   -875       C  
ATOM    777  CG1 ILE A 131      -5.213 -59.730 -12.137  1.00 70.78           C  
ANISOU  777  CG1 ILE A 131     7261   8044  11588     12    127   -719       C  
ATOM    778  CG2 ILE A 131      -4.827 -59.870 -14.619  1.00 71.04           C  
ANISOU  778  CG2 ILE A 131     7207   8289  11496    -64    148  -1016       C  
ATOM    779  CD1 ILE A 131      -5.930 -58.423 -12.121  1.00 71.65           C  
ANISOU  779  CD1 ILE A 131     7490   8241  11495      9    131   -614       C  
ATOM    780  N   VAL A 132      -1.343 -60.566 -14.561  1.00 72.91           N  
ANISOU  780  N   VAL A 132     7287   8456  11958    -74    151  -1224       N  
ATOM    781  CA  VAL A 132      -0.530 -60.799 -15.753  1.00 74.60           C  
ANISOU  781  CA  VAL A 132     7409   8767  12168   -131    183  -1440       C  
ATOM    782  C   VAL A 132       0.520 -61.940 -15.588  1.00 76.89           C  
ANISOU  782  C   VAL A 132     7558   8958  12699   -114    168  -1573       C  
ATOM    783  O   VAL A 132       0.490 -62.910 -16.343  1.00 77.07           O  
ANISOU  783  O   VAL A 132     7450   8984  12850   -139    181  -1760       O  
ATOM    784  CB  VAL A 132       0.111 -59.477 -16.223  1.00 74.98           C  
ANISOU  784  CB  VAL A 132     7553   8966  11969   -185    219  -1440       C  
ATOM    785  CG1 VAL A 132       1.086 -59.715 -17.368  1.00 75.56           C  
ANISOU  785  CG1 VAL A 132     7537   9153  12019   -261    266  -1668       C  
ATOM    786  CG2 VAL A 132      -0.959 -58.472 -16.616  1.00 75.12           C  
ANISOU  786  CG2 VAL A 132     7700   9067  11774   -196    220  -1317       C  
ATOM    787  N   ARG A 133       1.429 -61.820 -14.604  1.00 78.38           N  
ANISOU  787  N   ARG A 133     7771   9057  12955    -68    132  -1483       N  
ATOM    788  CA  ARG A 133       2.531 -62.742 -14.308  1.00 80.04           C  
ANISOU  788  CA  ARG A 133     7862   9159  13392    -36     97  -1584       C  
ATOM    789  C   ARG A 133       2.131 -63.955 -13.377  1.00 81.22           C  
ANISOU  789  C   ARG A 133     7961   9102  13796     37     32  -1497       C  
ATOM    790  O   ARG A 133       0.970 -64.061 -12.963  1.00 80.93           O  
ANISOU  790  O   ARG A 133     7989   9014  13749     55     27  -1355       O  
ATOM    791  CB  ARG A 133       3.707 -61.909 -13.734  1.00 82.01           C  
ANISOU  791  CB  ARG A 133     8168   9437  13556    -27     86  -1539       C  
ATOM    792  CG  ARG A 133       4.599 -61.322 -14.817  1.00 86.64           C  
ANISOU  792  CG  ARG A 133     8726  10183  14012   -107    153  -1717       C  
ATOM    793  CD  ARG A 133       5.708 -60.430 -14.273  1.00 91.53           C  
ANISOU  793  CD  ARG A 133     9392  10829  14555   -104    151  -1688       C  
ATOM    794  NE  ARG A 133       6.675 -60.069 -15.317  1.00 96.01           N  
ANISOU  794  NE  ARG A 133     9904  11531  15046   -191    224  -1892       N  
ATOM    795  CZ  ARG A 133       7.686 -59.217 -15.150  1.00 98.87           C  
ANISOU  795  CZ  ARG A 133    10299  11952  15315   -217    251  -1910       C  
ATOM    796  NH1 ARG A 133       7.871 -58.616 -13.980  1.00 99.24           N  
ANISOU  796  NH1 ARG A 133    10434  11941  15330   -157    204  -1740       N  
ATOM    797  NH2 ARG A 133       8.516 -58.956 -16.154  1.00 98.27           N  
ANISOU  797  NH2 ARG A 133    10167  11997  15173   -309    330  -2106       N  
ATOM    798  N   PRO A 134       3.052 -64.916 -13.094  1.00 82.39           N  
ANISOU  798  N   PRO A 134     7992   9127  14184     75    -18  -1588       N  
ATOM    799  CA  PRO A 134       2.678 -66.054 -12.236  1.00 83.11           C  
ANISOU  799  CA  PRO A 134     8052   9013  14511    141    -85  -1489       C  
ATOM    800  C   PRO A 134       2.774 -65.719 -10.751  1.00 83.66           C  
ANISOU  800  C   PRO A 134     8252   8998  14537    200   -144  -1243       C  
ATOM    801  O   PRO A 134       3.717 -66.139 -10.076  1.00 83.79           O  
ANISOU  801  O   PRO A 134     8292   9034  14512    224   -179  -1231       O  
ATOM    802  CB  PRO A 134       3.690 -67.140 -12.632  1.00 83.79           C  
ANISOU  802  CB  PRO A 134     7963   9007  14867    160   -124  -1692       C  
ATOM    803  CG  PRO A 134       4.893 -66.396 -13.140  1.00 83.93           C  
ANISOU  803  CG  PRO A 134     7945   9169  14775    120    -92  -1852       C  
ATOM    804  CD  PRO A 134       4.472 -64.997 -13.512  1.00 82.16           C  
ANISOU  804  CD  PRO A 134     7857   9134  14225     61    -19  -1782       C  
ATOM    805  N   LEU A 140       8.922 -67.092  -4.189  1.00 78.92           N  
ANISOU  805  N   LEU A 140     7713   7737  14534    677   -841   -761       N  
ATOM    806  CA  LEU A 140       8.357 -65.745  -4.124  1.00 79.77           C  
ANISOU  806  CA  LEU A 140     7963   8017  14330    625   -750   -652       C  
ATOM    807  C   LEU A 140       9.437 -64.659  -3.964  1.00 80.87           C  
ANISOU  807  C   LEU A 140     8110   8280  14338    634   -762   -718       C  
ATOM    808  O   LEU A 140       9.780 -64.275  -2.841  1.00 81.24           O  
ANISOU  808  O   LEU A 140     8238   8303  14328    691   -848   -579       O  
ATOM    809  CB  LEU A 140       7.320 -65.638  -2.992  1.00 80.01           C  
ANISOU  809  CB  LEU A 140     8159   7989  14252    640   -772   -365       C  
ATOM    810  CG  LEU A 140       6.122 -64.699  -3.236  1.00 81.39           C  
ANISOU  810  CG  LEU A 140     8448   8293  14185    566   -646   -269       C  
ATOM    811  CD1 LEU A 140       5.161 -65.286  -4.255  1.00 81.86           C  
ANISOU  811  CD1 LEU A 140     8431   8362  14311    506   -555   -388       C  
ATOM    812  CD2 LEU A 140       5.366 -64.423  -1.947  1.00 81.83           C  
ANISOU  812  CD2 LEU A 140     8654   8287  14150    579   -670     -3       C  
ATOM    813  N   ARG A 141       9.982 -64.179  -5.104  1.00 81.02           N  
ANISOU  813  N   ARG A 141     8043   8433  14309    573   -673   -938       N  
ATOM    814  CA  ARG A 141      10.976 -63.090  -5.205  1.00 81.13           C  
ANISOU  814  CA  ARG A 141     8049   8580  14196    557   -649  -1039       C  
ATOM    815  C   ARG A 141      10.290 -61.719  -4.928  1.00 80.12           C  
ANISOU  815  C   ARG A 141     8081   8598  13761    505   -562   -896       C  
ATOM    816  O   ARG A 141      10.939 -60.793  -4.444  1.00 80.11           O  
ANISOU  816  O   ARG A 141     8124   8676  13640    512   -569   -884       O  
ATOM    817  CB  ARG A 141      11.656 -63.131  -6.602  1.00 83.31           C  
ANISOU  817  CB  ARG A 141     8167   8932  14554    497   -577  -1336       C  
ATOM    818  CG  ARG A 141      12.343 -61.848  -7.086  1.00 87.84           C  
ANISOU  818  CG  ARG A 141     8749   9683  14943    430   -487  -1455       C  
ATOM    819  CD  ARG A 141      13.602 -61.544  -6.297  1.00 92.51           C  
ANISOU  819  CD  ARG A 141     9316  10257  15575    492   -575  -1478       C  
ATOM    820  NE  ARG A 141      14.377 -60.437  -6.864  1.00 96.48           N  
ANISOU  820  NE  ARG A 141     9799  10915  15946    421   -482  -1631       N  
ATOM    821  CZ  ARG A 141      15.416 -60.592  -7.681  1.00 99.82           C  
ANISOU  821  CZ  ARG A 141    10068  11376  16483    380   -442  -1899       C  
ATOM    822  NH1 ARG A 141      15.806 -61.808  -8.051  1.00 99.70           N  
ANISOU  822  NH1 ARG A 141     9899  11259  16723    407   -491  -2055       N  
ATOM    823  NH2 ARG A 141      16.071 -59.532  -8.141  1.00100.26           N  
ANISOU  823  NH2 ARG A 141    10120  11572  16404    305   -348  -2021       N  
ATOM    824  N   LEU A 142       8.967 -61.620  -5.195  1.00 79.06           N  
ANISOU  824  N   LEU A 142     8029   8493  13519    458   -487   -791       N  
ATOM    825  CA  LEU A 142       8.130 -60.451  -4.921  1.00 78.55           C  
ANISOU  825  CA  LEU A 142     8110   8543  13192    417   -415   -647       C  
ATOM    826  C   LEU A 142       8.079 -60.126  -3.415  1.00 77.30           C  
ANISOU  826  C   LEU A 142     8069   8340  12960    477   -491   -429       C  
ATOM    827  O   LEU A 142       7.788 -58.990  -3.058  1.00 77.35           O  
ANISOU  827  O   LEU A 142     8180   8447  12761    453   -447   -338       O  
ATOM    828  CB  LEU A 142       6.699 -60.706  -5.432  1.00 79.01           C  
ANISOU  828  CB  LEU A 142     8208   8611  13203    369   -342   -592       C  
ATOM    829  CG  LEU A 142       6.516 -60.724  -6.945  1.00 80.61           C  
ANISOU  829  CG  LEU A 142     8303   8860  13464    310   -271   -792       C  
ATOM    830  CD1 LEU A 142       5.557 -61.822  -7.363  1.00 81.11           C  
ANISOU  830  CD1 LEU A 142     8331   8821  13666    314   -274   -766       C  
ATOM    831  CD2 LEU A 142       6.057 -59.363  -7.456  1.00 81.35           C  
ANISOU  831  CD2 LEU A 142     8456   9125  13327    231   -166   -834       C  
ATOM    832  N   ARG A 143       8.328 -61.122  -2.538  1.00 76.10           N  
ANISOU  832  N   ARG A 143     7903   8038  12974    550   -606   -344       N  
ATOM    833  CA  ARG A 143       8.369 -60.931  -1.088  1.00 75.53           C  
ANISOU  833  CA  ARG A 143     7940   7921  12839    607   -691   -141       C  
ATOM    834  C   ARG A 143       9.571 -60.027  -0.724  1.00 73.30           C  
ANISOU  834  C   ARG A 143     7656   7719  12475    636   -734   -194       C  
ATOM    835  O   ARG A 143       9.464 -59.189   0.173  1.00 73.61           O  
ANISOU  835  O   ARG A 143     7804   7806  12357    651   -754    -51       O  
ATOM    836  CB  ARG A 143       8.475 -62.289  -0.377  1.00 78.50           C  
ANISOU  836  CB  ARG A 143     8290   8106  13430    676   -812    -58       C  
ATOM    837  CG  ARG A 143       7.842 -62.308   1.012  1.00 84.53           C  
ANISOU  837  CG  ARG A 143     9200   8811  14106    698   -859    204       C  
ATOM    838  CD  ARG A 143       8.496 -63.349   1.914  1.00 90.33           C  
ANISOU  838  CD  ARG A 143     9926   9388  15006    788  -1023    285       C  
ATOM    839  NE  ARG A 143       7.977 -63.317   3.287  1.00 95.17           N  
ANISOU  839  NE  ARG A 143    10693   9971  15497    806  -1074    538       N  
ATOM    840  CZ  ARG A 143       8.609 -62.761   4.320  1.00 98.23           C  
ANISOU  840  CZ  ARG A 143    11155  10423  15746    844  -1143    620       C  
ATOM    841  NH1 ARG A 143       9.791 -62.176   4.148  1.00 98.21           N  
ANISOU  841  NH1 ARG A 143    11085  10515  15716    869  -1165    467       N  
ATOM    842  NH2 ARG A 143       8.070 -62.792   5.531  1.00 98.30           N  
ANISOU  842  NH2 ARG A 143    11305  10408  15636    850  -1183    847       N  
ATOM    843  N   VAL A 144      10.707 -60.186  -1.445  1.00 70.69           N  
ANISOU  843  N   VAL A 144     7193   7409  12255    638   -742   -414       N  
ATOM    844  CA  VAL A 144      11.903 -59.362  -1.289  1.00 68.12           C  
ANISOU  844  CA  VAL A 144     6835   7166  11882    653   -763   -518       C  
ATOM    845  C   VAL A 144      11.631 -58.002  -1.947  1.00 65.18           C  
ANISOU  845  C   VAL A 144     6511   6962  11293    563   -620   -571       C  
ATOM    846  O   VAL A 144      11.760 -56.981  -1.289  1.00 64.92           O  
ANISOU  846  O   VAL A 144     6558   7008  11099    562   -611   -498       O  
ATOM    847  CB  VAL A 144      13.137 -60.060  -1.921  1.00 68.71           C  
ANISOU  847  CB  VAL A 144     6734   7183  12189    682   -818   -751       C  
ATOM    848  CG1 VAL A 144      14.379 -59.178  -1.849  1.00 69.10           C  
ANISOU  848  CG1 VAL A 144     6728   7339  12188    670   -800   -912       C  
ATOM    849  CG2 VAL A 144      13.385 -61.413  -1.278  1.00 69.31           C  
ANISOU  849  CG2 VAL A 144     6770   7080  12484    785   -983   -687       C  
ATOM    850  N   SER A 145      11.204 -58.003  -3.225  1.00 63.08           N  
ANISOU  850  N   SER A 145     6200   6747  11022    487   -512   -689       N  
ATOM    851  CA  SER A 145      10.913 -56.819  -4.026  1.00 61.85           C  
ANISOU  851  CA  SER A 145     6089   6737  10674    395   -379   -741       C  
ATOM    852  C   SER A 145       9.891 -55.855  -3.415  1.00 60.27           C  
ANISOU  852  C   SER A 145     6043   6598  10257    377   -337   -547       C  
ATOM    853  O   SER A 145      10.079 -54.644  -3.483  1.00 60.63           O  
ANISOU  853  O   SER A 145     6141   6752  10145    333   -273   -560       O  
ATOM    854  CB  SER A 145      10.486 -57.223  -5.430  1.00 63.49           C  
ANISOU  854  CB  SER A 145     6231   6968  10925    328   -297   -869       C  
ATOM    855  OG  SER A 145      11.580 -57.064  -6.318  1.00 66.56           O  
ANISOU  855  OG  SER A 145     6506   7414  11369    283   -254  -1100       O  
ATOM    856  N   GLY A 146       8.827 -56.382  -2.830  1.00 58.22           N  
ANISOU  856  N   GLY A 146     5852   6268  10000    404   -367   -377       N  
ATOM    857  CA  GLY A 146       7.816 -55.557  -2.186  1.00 56.52           C  
ANISOU  857  CA  GLY A 146     5771   6103   9601    390   -331   -202       C  
ATOM    858  C   GLY A 146       8.388 -54.842  -0.981  1.00 54.44           C  
ANISOU  858  C   GLY A 146     5566   5866   9253    431   -385   -120       C  
ATOM    859  O   GLY A 146       8.080 -53.676  -0.753  1.00 54.40           O  
ANISOU  859  O   GLY A 146     5640   5953   9077    401   -330    -68       O  
ATOM    860  N   ALA A 147       9.267 -55.521  -0.228  1.00 52.79           N  
ANISOU  860  N   ALA A 147     5313   5577   9168    504   -499   -117       N  
ATOM    861  CA  ALA A 147       9.919 -54.924   0.933  1.00 51.78           C  
ANISOU  861  CA  ALA A 147     5228   5477   8967    551   -567    -55       C  
ATOM    862  C   ALA A 147      10.771 -53.720   0.503  1.00 50.60           C  
ANISOU  862  C   ALA A 147     5049   5445   8731    513   -506   -196       C  
ATOM    863  O   ALA A 147      10.672 -52.653   1.106  1.00 50.77           O  
ANISOU  863  O   ALA A 147     5147   5546   8597    501   -479   -132       O  
ATOM    864  CB  ALA A 147      10.769 -55.960   1.653  1.00 51.73           C  
ANISOU  864  CB  ALA A 147     5167   5359   9130    639   -714    -49       C  
ATOM    865  N   VAL A 148      11.543 -53.872  -0.586  1.00 49.14           N  
ANISOU  865  N   VAL A 148     4753   5272   8644    483   -471   -394       N  
ATOM    866  CA  VAL A 148      12.353 -52.804  -1.165  1.00 47.94           C  
ANISOU  866  CA  VAL A 148     4569   5225   8419    428   -393   -542       C  
ATOM    867  C   VAL A 148      11.438 -51.638  -1.587  1.00 47.70           C  
ANISOU  867  C   VAL A 148     4642   5291   8190    349   -272   -477       C  
ATOM    868  O   VAL A 148      11.658 -50.517  -1.145  1.00 48.06           O  
ANISOU  868  O   VAL A 148     4743   5408   8112    335   -244   -451       O  
ATOM    869  CB  VAL A 148      13.173 -53.347  -2.351  1.00 47.60           C  
ANISOU  869  CB  VAL A 148     4389   5174   8522    395   -365   -765       C  
ATOM    870  CG1 VAL A 148      13.763 -52.223  -3.185  1.00 48.15           C  
ANISOU  870  CG1 VAL A 148     4444   5361   8489    304   -245   -909       C  
ATOM    871  CG2 VAL A 148      14.249 -54.293  -1.870  1.00 47.58           C  
ANISOU  871  CG2 VAL A 148     4274   5083   8719    478   -491   -854       C  
ATOM    872  N   ALA A 149      10.369 -51.919  -2.363  1.00 46.83           N  
ANISOU  872  N   ALA A 149     4558   5177   8058    304   -211   -445       N  
ATOM    873  CA  ALA A 149       9.401 -50.914  -2.830  1.00 46.08           C  
ANISOU  873  CA  ALA A 149     4557   5160   7791    238   -114   -382       C  
ATOM    874  C   ALA A 149       8.793 -50.138  -1.662  1.00 44.91           C  
ANISOU  874  C   ALA A 149     4518   5031   7513    263   -128   -213       C  
ATOM    875  O   ALA A 149       8.724 -48.916  -1.703  1.00 44.84           O  
ANISOU  875  O   ALA A 149     4564   5097   7374    224    -68   -206       O  
ATOM    876  CB  ALA A 149       8.302 -51.586  -3.652  1.00 46.14           C  
ANISOU  876  CB  ALA A 149     4568   5142   7822    210    -80   -364       C  
ATOM    877  N   THR A 150       8.424 -50.840  -0.598  1.00 43.81           N  
ANISOU  877  N   THR A 150     4406   4824   7415    325   -206    -85       N  
ATOM    878  CA  THR A 150       7.859 -50.224   0.580  1.00 43.30           C  
ANISOU  878  CA  THR A 150     4436   4781   7233    346   -221     66       C  
ATOM    879  C   THR A 150       8.914 -49.356   1.284  1.00 42.48           C  
ANISOU  879  C   THR A 150     4330   4734   7076    366   -247     27       C  
ATOM    880  O   THR A 150       8.587 -48.265   1.747  1.00 42.50           O  
ANISOU  880  O   THR A 150     4401   4801   6947    348   -209     85       O  
ATOM    881  CB  THR A 150       7.195 -51.313   1.432  1.00 44.38           C  
ANISOU  881  CB  THR A 150     4600   4829   7434    395   -293    203       C  
ATOM    882  OG1 THR A 150       5.787 -51.246   1.195  1.00 45.31           O  
ANISOU  882  OG1 THR A 150     4768   4943   7505    357   -230    280       O  
ATOM    883  CG2 THR A 150       7.511 -51.208   2.938  1.00 44.60           C  
ANISOU  883  CG2 THR A 150     4685   4860   7401    445   -365    321       C  
ATOM    884  N   ALA A 151      10.174 -49.823   1.334  1.00 41.41           N  
ANISOU  884  N   ALA A 151     4107   4572   7055    404   -313    -82       N  
ATOM    885  CA  ALA A 151      11.235 -49.067   1.974  1.00 40.76           C  
ANISOU  885  CA  ALA A 151     4005   4541   6942    427   -343   -143       C  
ATOM    886  C   ALA A 151      11.483 -47.756   1.211  1.00 40.37           C  
ANISOU  886  C   ALA A 151     3960   4581   6797    349   -229   -243       C  
ATOM    887  O   ALA A 151      11.548 -46.682   1.814  1.00 40.25           O  
ANISOU  887  O   ALA A 151     3992   4628   6674    341   -206   -216       O  
ATOM    888  CB  ALA A 151      12.504 -49.905   2.048  1.00 40.49           C  
ANISOU  888  CB  ALA A 151     3860   4452   7072    483   -438   -263       C  
ATOM    889  N   VAL A 152      11.516 -47.832  -0.120  1.00 39.91           N  
ANISOU  889  N   VAL A 152     3863   4530   6771    287   -152   -348       N  
ATOM    890  CA  VAL A 152      11.761 -46.671  -0.954  1.00 40.27           C  
ANISOU  890  CA  VAL A 152     3921   4651   6728    204    -42   -437       C  
ATOM    891  C   VAL A 152      10.661 -45.646  -0.775  1.00 41.25           C  
ANISOU  891  C   VAL A 152     4159   4815   6700    173     14   -307       C  
ATOM    892  O   VAL A 152      10.959 -44.502  -0.442  1.00 41.70           O  
ANISOU  892  O   VAL A 152     4247   4921   6676    153     49   -314       O  
ATOM    893  CB  VAL A 152      11.985 -47.072  -2.439  1.00 40.70           C  
ANISOU  893  CB  VAL A 152     3916   4711   6838    137     26   -572       C  
ATOM    894  CG1 VAL A 152      11.806 -45.887  -3.385  1.00 41.12           C  
ANISOU  894  CG1 VAL A 152     4025   4837   6761     38    146   -607       C  
ATOM    895  CG2 VAL A 152      13.359 -47.715  -2.634  1.00 41.13           C  
ANISOU  895  CG2 VAL A 152     3838   4744   7044    153    -10   -752       C  
ATOM    896  N   LEU A 153       9.392 -46.053  -0.956  1.00 41.32           N  
ANISOU  896  N   LEU A 153     4222   4795   6682    172     19   -195       N  
ATOM    897  CA ALEU A 153       8.282 -45.118  -0.815  0.50 41.80           C  
ANISOU  897  CA ALEU A 153     4380   4888   6616    147     67    -85       C  
ATOM    898  CA BLEU A 153       8.291 -45.116  -0.829  0.50 41.59           C  
ANISOU  898  CA BLEU A 153     4352   4860   6589    146     67    -86       C  
ATOM    899  C   LEU A 153       8.179 -44.547   0.587  1.00 42.34           C  
ANISOU  899  C   LEU A 153     4492   4972   6623    189     30      8       C  
ATOM    900  O   LEU A 153       7.640 -43.463   0.749  1.00 42.88           O  
ANISOU  900  O   LEU A 153     4623   5077   6593    163     76     58       O  
ATOM    901  CB ALEU A 153       6.942 -45.705  -1.293  0.50 41.99           C  
ANISOU  901  CB ALEU A 153     4439   4879   6637    139     76     -4       C  
ATOM    902  CB BLEU A 153       6.978 -45.731  -1.336  0.50 41.47           C  
ANISOU  902  CB BLEU A 153     4369   4812   6575    138     77    -10       C  
ATOM    903  CG ALEU A 153       6.176 -46.632  -0.354  0.50 43.56           C  
ANISOU  903  CG ALEU A 153     4649   5020   6882    196     12    112       C  
ATOM    904  CG BLEU A 153       7.052 -46.315  -2.766  0.50 42.54           C  
ANISOU  904  CG BLEU A 153     4456   4944   6765     93    112   -115       C  
ATOM    905  CD1ALEU A 153       5.334 -45.851   0.638  0.50 44.04           C  
ANISOU  905  CD1ALEU A 153     4789   5104   6842    207     17    236       C  
ATOM    906  CD1BLEU A 153       5.741 -46.930  -3.191  0.50 42.93           C  
ANISOU  906  CD1BLEU A 153     4530   4966   6816     89    116    -48       C  
ATOM    907  CD2ALEU A 153       5.232 -47.506  -1.142  0.50 44.37           C  
ANISOU  907  CD2ALEU A 153     4741   5081   7036    183     23    124       C  
ATOM    908  CD2BLEU A 153       7.507 -45.284  -3.788  0.50 43.09           C  
ANISOU  908  CD2BLEU A 153     4536   5077   6760     16    193   -212       C  
ATOM    909  N   TRP A 154       8.713 -45.253   1.607  1.00 42.42           N  
ANISOU  909  N   TRP A 154     4470   4956   6691    254    -58     28       N  
ATOM    910  CA  TRP A 154       8.671 -44.738   2.976  1.00 42.53           C  
ANISOU  910  CA  TRP A 154     4526   5001   6634    292    -97    109       C  
ATOM    911  C   TRP A 154       9.726 -43.665   3.180  1.00 41.77           C  
ANISOU  911  C   TRP A 154     4402   4963   6505    280    -78      8       C  
ATOM    912  O   TRP A 154       9.468 -42.718   3.910  1.00 42.13           O  
ANISOU  912  O   TRP A 154     4490   5056   6459    277    -61     49       O  
ATOM    913  CB  TRP A 154       8.742 -45.840   4.042  1.00 42.78           C  
ANISOU  913  CB  TRP A 154     4553   4985   6717    362   -204    191       C  
ATOM    914  CG  TRP A 154       7.387 -46.281   4.518  1.00 43.47           C  
ANISOU  914  CG  TRP A 154     4711   5046   6762    365   -204    343       C  
ATOM    915  CD1 TRP A 154       6.737 -47.434   4.191  1.00 44.53           C  
ANISOU  915  CD1 TRP A 154     4843   5104   6972    373   -223    401       C  
ATOM    916  CD2 TRP A 154       6.510 -45.560   5.396  1.00 43.53           C  
ANISOU  916  CD2 TRP A 154     4793   5101   6648    354   -176    443       C  
ATOM    917  NE1 TRP A 154       5.511 -47.480   4.816  1.00 44.88           N  
ANISOU  917  NE1 TRP A 154     4959   5146   6948    364   -205    533       N  
ATOM    918  CE2 TRP A 154       5.345 -46.339   5.560  1.00 44.44           C  
ANISOU  918  CE2 TRP A 154     4949   5168   6769    351   -175    558       C  
ATOM    919  CE3 TRP A 154       6.606 -44.344   6.082  1.00 43.80           C  
ANISOU  919  CE3 TRP A 154     4853   5213   6576    343   -150    436       C  
ATOM    920  CZ2 TRP A 154       4.281 -45.932   6.365  1.00 44.77           C  
ANISOU  920  CZ2 TRP A 154     5057   5243   6711    333   -143    659       C  
ATOM    921  CZ3 TRP A 154       5.545 -43.937   6.864  1.00 44.48           C  
ANISOU  921  CZ3 TRP A 154     5003   5332   6567    329   -122    534       C  
ATOM    922  CH2 TRP A 154       4.407 -44.734   7.013  1.00 44.66           C  
ANISOU  922  CH2 TRP A 154     5064   5310   6594    323   -118    643       C  
ATOM    923  N   VAL A 155      10.879 -43.764   2.501  1.00 40.74           N  
ANISOU  923  N   VAL A 155     4193   4831   6454    267    -73   -137       N  
ATOM    924  CA  VAL A 155      11.902 -42.723   2.591  1.00 40.16           C  
ANISOU  924  CA  VAL A 155     4085   4812   6362    244    -39   -252       C  
ATOM    925  C   VAL A 155      11.479 -41.534   1.718  1.00 40.89           C  
ANISOU  925  C   VAL A 155     4229   4936   6371    158     80   -267       C  
ATOM    926  O   VAL A 155      11.364 -40.413   2.214  1.00 41.16           O  
ANISOU  926  O   VAL A 155     4303   5008   6327    144    113   -243       O  
ATOM    927  CB  VAL A 155      13.299 -43.236   2.227  1.00 39.28           C  
ANISOU  927  CB  VAL A 155     3865   4687   6371    253    -68   -415       C  
ATOM    928  CG1 VAL A 155      14.308 -42.110   2.308  1.00 39.52           C  
ANISOU  928  CG1 VAL A 155     3860   4774   6383    214    -13   -544       C  
ATOM    929  CG2 VAL A 155      13.693 -44.380   3.135  1.00 39.17           C  
ANISOU  929  CG2 VAL A 155     3806   4632   6443    348   -205   -391       C  
ATOM    930  N   LEU A 156      11.137 -41.795   0.447  1.00 40.83           N  
ANISOU  930  N   LEU A 156     4226   4911   6376    102    140   -295       N  
ATOM    931  CA  LEU A 156      10.665 -40.792  -0.500  1.00 41.22           C  
ANISOU  931  CA  LEU A 156     4338   4982   6343     22    239   -290       C  
ATOM    932  C   LEU A 156       9.507 -39.949   0.098  1.00 40.94           C  
ANISOU  932  C   LEU A 156     4390   4953   6212     30    247   -156       C  
ATOM    933  O   LEU A 156       9.482 -38.738  -0.087  1.00 40.80           O  
ANISOU  933  O   LEU A 156     4413   4956   6134    -17    309   -164       O  
ATOM    934  CB  LEU A 156      10.236 -41.509  -1.791  1.00 42.02           C  
ANISOU  934  CB  LEU A 156     4441   5062   6464    -16    266   -300       C  
ATOM    935  CG  LEU A 156       9.423 -40.707  -2.806  1.00 44.28           C  
ANISOU  935  CG  LEU A 156     4807   5362   6654    -89    344   -262       C  
ATOM    936  CD1 LEU A 156      10.288 -39.686  -3.477  1.00 45.34           C  
ANISOU  936  CD1 LEU A 156     4941   5531   6754   -171    429   -365       C  
ATOM    937  CD2 LEU A 156       8.792 -41.612  -3.858  1.00 44.69           C  
ANISOU  937  CD2 LEU A 156     4860   5399   6720   -108    347   -255       C  
ATOM    938  N   ALA A 157       8.612 -40.578   0.887  1.00 40.78           N  
ANISOU  938  N   ALA A 157     4394   4913   6188     88    186    -43       N  
ATOM    939  CA  ALA A 157       7.503 -39.863   1.532  1.00 40.93           C  
ANISOU  939  CA  ALA A 157     4481   4941   6128     95    196     66       C  
ATOM    940  C   ALA A 157       8.033 -38.956   2.626  1.00 41.12           C  
ANISOU  940  C   ALA A 157     4500   5008   6116    110    192     45       C  
ATOM    941  O   ALA A 157       7.659 -37.780   2.651  1.00 41.96           O  
ANISOU  941  O   ALA A 157     4646   5130   6168     78    243     54       O  
ATOM    942  CB  ALA A 157       6.474 -40.835   2.108  1.00 40.87           C  
ANISOU  942  CB  ALA A 157     4494   4907   6128    141    144    178       C  
ATOM    943  N   ALA A 158       8.946 -39.467   3.495  1.00 39.91           N  
ANISOU  943  N   ALA A 158     4294   4871   5999    159    126      6       N  
ATOM    944  CA  ALA A 158       9.534 -38.663   4.565  1.00 38.94           C  
ANISOU  944  CA  ALA A 158     4156   4799   5842    178    113    -30       C  
ATOM    945  C   ALA A 158      10.403 -37.527   4.051  1.00 38.47           C  
ANISOU  945  C   ALA A 158     4072   4758   5784    122    186   -146       C  
ATOM    946  O   ALA A 158      10.682 -36.616   4.813  1.00 38.83           O  
ANISOU  946  O   ALA A 158     4122   4841   5791    118    206   -165       O  
ATOM    947  CB  ALA A 158      10.315 -39.532   5.528  1.00 38.58           C  
ANISOU  947  CB  ALA A 158     4058   4764   5836    245     14    -50       C  
ATOM    948  N   LEU A 159      10.815 -37.550   2.771  1.00 37.81           N  
ANISOU  948  N   LEU A 159     3968   4652   5745     71    237   -225       N  
ATOM    949  CA  LEU A 159      11.617 -36.466   2.206  1.00 37.89           C  
ANISOU  949  CA  LEU A 159     3966   4677   5755      2    321   -330       C  
ATOM    950  C   LEU A 159      10.735 -35.407   1.534  1.00 39.35           C  
ANISOU  950  C   LEU A 159     4235   4843   5875    -60    399   -266       C  
ATOM    951  O   LEU A 159      11.053 -34.218   1.603  1.00 40.28           O  
ANISOU  951  O   LEU A 159     4363   4967   5975   -103    458   -310       O  
ATOM    952  CB  LEU A 159      12.643 -37.000   1.213  1.00 36.82           C  
ANISOU  952  CB  LEU A 159     3770   4533   5688    -39    350   -456       C  
ATOM    953  CG  LEU A 159      13.657 -37.916   1.814  1.00 36.55           C  
ANISOU  953  CG  LEU A 159     3640   4507   5739     23    269   -543       C  
ATOM    954  CD1 LEU A 159      14.374 -38.675   0.756  1.00 36.46           C  
ANISOU  954  CD1 LEU A 159     3567   4479   5808    -10    289   -652       C  
ATOM    955  CD2 LEU A 159      14.584 -37.161   2.723  1.00 36.62           C  
ANISOU  955  CD2 LEU A 159     3599   4556   5759     38    260   -633       C  
ATOM    956  N   LEU A 160       9.643 -35.826   0.868  1.00 38.97           N  
ANISOU  956  N   LEU A 160     4243   4764   5798    -63    396   -168       N  
ATOM    957  CA  LEU A 160       8.732 -34.876   0.228  1.00 38.87           C  
ANISOU  957  CA  LEU A 160     4312   4728   5731   -111    448   -101       C  
ATOM    958  C   LEU A 160       7.950 -34.072   1.266  1.00 39.37           C  
ANISOU  958  C   LEU A 160     4402   4794   5761    -79    435    -35       C  
ATOM    959  O   LEU A 160       7.600 -32.925   1.021  1.00 39.38           O  
ANISOU  959  O   LEU A 160     4448   4775   5738   -117    481    -20       O  
ATOM    960  CB  LEU A 160       7.781 -35.606  -0.725  1.00 38.53           C  
ANISOU  960  CB  LEU A 160     4309   4657   5672   -116    437    -30       C  
ATOM    961  CG  LEU A 160       8.475 -36.239  -1.911  1.00 39.29           C  
ANISOU  961  CG  LEU A 160     4383   4756   5789   -167    468   -107       C  
ATOM    962  CD1 LEU A 160       7.567 -37.173  -2.649  1.00 39.19           C  
ANISOU  962  CD1 LEU A 160     4389   4726   5775   -158    441    -53       C  
ATOM    963  CD2 LEU A 160       9.056 -35.197  -2.817  1.00 40.03           C  
ANISOU  963  CD2 LEU A 160     4515   4852   5844   -257    554   -160       C  
ATOM    964  N   ALA A 161       7.685 -34.669   2.429  1.00 39.60           N  
ANISOU  964  N   ALA A 161     4406   4848   5792    -13    372      3       N  
ATOM    965  CA  ALA A 161       6.986 -33.996   3.506  1.00 40.37           C  
ANISOU  965  CA  ALA A 161     4518   4964   5855     13    363     49       C  
ATOM    966  C   ALA A 161       7.881 -32.988   4.269  1.00 41.43           C  
ANISOU  966  C   ALA A 161     4613   5136   5992      8    383    -39       C  
ATOM    967  O   ALA A 161       7.366 -32.206   5.065  1.00 41.34           O  
ANISOU  967  O   ALA A 161     4607   5145   5955     20    386    -23       O  
ATOM    968  CB  ALA A 161       6.421 -35.026   4.458  1.00 40.26           C  
ANISOU  968  CB  ALA A 161     4499   4971   5828     72    298    123       C  
ATOM    969  N   MET A 162       9.210 -32.992   4.013  1.00 42.08           N  
ANISOU  969  N   MET A 162     4648   5230   6112    -13    399   -145       N  
ATOM    970  CA  MET A 162      10.197 -32.104   4.636  1.00 42.88           C  
ANISOU  970  CA  MET A 162     4699   5365   6228    -22    421   -251       C  
ATOM    971  C   MET A 162       9.882 -30.594   4.514  1.00 43.00           C  
ANISOU  971  C   MET A 162     4745   5355   6237    -72    493   -262       C  
ATOM    972  O   MET A 162       9.968 -29.923   5.545  1.00 42.62           O  
ANISOU  972  O   MET A 162     4666   5344   6183    -51    486   -297       O  
ATOM    973  CB  MET A 162      11.609 -32.415   4.124  1.00 44.16           C  
ANISOU  973  CB  MET A 162     4799   5533   6446    -46    436   -374       C  
ATOM    974  CG  MET A 162      12.657 -32.327   5.193  1.00 47.41           C  
ANISOU  974  CG  MET A 162     5129   6000   6883     -6    393   -477       C  
ATOM    975  SD  MET A 162      12.402 -33.522   6.521  1.00 54.58           S  
ANISOU  975  SD  MET A 162     6022   6954   7762     97    263   -404       S  
ATOM    976  CE  MET A 162      13.065 -32.578   7.911  1.00 54.22           C  
ANISOU  976  CE  MET A 162     5924   6987   7693    124    242   -490       C  
ATOM    977  N   PRO A 163       9.447 -30.046   3.335  1.00 43.38           N  
ANISOU  977  N   PRO A 163     4857   5341   6285   -132    552   -224       N  
ATOM    978  CA  PRO A 163       9.077 -28.614   3.277  1.00 43.75           C  
ANISOU  978  CA  PRO A 163     4939   5346   6338   -172    606   -219       C  
ATOM    979  C   PRO A 163       7.986 -28.200   4.261  1.00 44.66           C  
ANISOU  979  C   PRO A 163     5059   5472   6439   -126    573   -164       C  
ATOM    980  O   PRO A 163       7.979 -27.047   4.681  1.00 44.93           O  
ANISOU  980  O   PRO A 163     5078   5494   6498   -140    605   -206       O  
ATOM    981  CB  PRO A 163       8.572 -28.419   1.839  1.00 44.20           C  
ANISOU  981  CB  PRO A 163     5080   5336   6379   -227    641   -147       C  
ATOM    982  CG  PRO A 163       9.161 -29.524   1.060  1.00 44.59           C  
ANISOU  982  CG  PRO A 163     5119   5403   6422   -244    640   -173       C  
ATOM    983  CD  PRO A 163       9.291 -30.685   2.011  1.00 43.02           C  
ANISOU  983  CD  PRO A 163     4854   5260   6231   -168    567   -186       C  
ATOM    984  N   VAL A 164       7.072 -29.116   4.640  1.00 45.14           N  
ANISOU  984  N   VAL A 164     5132   5552   6467    -76    517    -82       N  
ATOM    985  CA  VAL A 164       6.028 -28.760   5.612  1.00 46.15           C  
ANISOU  985  CA  VAL A 164     5257   5700   6579    -40    495    -44       C  
ATOM    986  C   VAL A 164       6.674 -28.686   7.030  1.00 47.68           C  
ANISOU  986  C   VAL A 164     5382   5979   6756     -8    474   -120       C  
ATOM    987  O   VAL A 164       6.397 -27.763   7.781  1.00 47.70           O  
ANISOU  987  O   VAL A 164     5360   6002   6764     -8    492   -161       O  
ATOM    988  CB  VAL A 164       4.688 -29.576   5.538  1.00 46.27           C  
ANISOU  988  CB  VAL A 164     5309   5704   6569    -10    456     63       C  
ATOM    989  CG1 VAL A 164       4.529 -30.334   4.226  1.00 46.40           C  
ANISOU  989  CG1 VAL A 164     5366   5678   6585    -23    447    116       C  
ATOM    990  CG2 VAL A 164       4.482 -30.496   6.729  1.00 46.88           C  
ANISOU  990  CG2 VAL A 164     5356   5853   6605     37    412     84       C  
ATOM    991  N   MET A 165       7.599 -29.599   7.345  1.00 48.81           N  
ANISOU  991  N   MET A 165     5490   6170   6885     17    434   -151       N  
ATOM    992  CA  MET A 165       8.320 -29.573   8.619  1.00 50.13           C  
ANISOU  992  CA  MET A 165     5596   6421   7030     51    400   -225       C  
ATOM    993  C   MET A 165       9.132 -28.255   8.754  1.00 50.21           C  
ANISOU  993  C   MET A 165     5559   6435   7083     16    454   -350       C  
ATOM    994  O   MET A 165       9.331 -27.769   9.867  1.00 50.87           O  
ANISOU  994  O   MET A 165     5593   6587   7147     37    440   -416       O  
ATOM    995  CB  MET A 165       9.227 -30.826   8.740  1.00 51.87           C  
ANISOU  995  CB  MET A 165     5788   6674   7248     89    333   -237       C  
ATOM    996  CG  MET A 165      10.301 -30.734   9.823  1.00 56.88           C  
ANISOU  996  CG  MET A 165     6353   7389   7870    123    287   -336       C  
ATOM    997  SD  MET A 165      10.325 -32.032  11.101  1.00 69.37           S  
ANISOU  997  SD  MET A 165     7928   9048   9381    201    166   -277       S  
ATOM    998  CE  MET A 165       9.216 -31.273  12.411  1.00 66.91           C  
ANISOU  998  CE  MET A 165     7638   8815   8970    201    180   -236       C  
ATOM    999  N   VAL A 166       9.554 -27.661   7.624  1.00 49.17           N  
ANISOU  999  N   VAL A 166     5445   6230   7006    -41    519   -381       N  
ATOM   1000  CA  VAL A 166      10.338 -26.431   7.589  1.00 48.43           C  
ANISOU 1000  CA  VAL A 166     5312   6121   6967    -86    583   -494       C  
ATOM   1001  C   VAL A 166       9.494 -25.138   7.663  1.00 47.78           C  
ANISOU 1001  C   VAL A 166     5255   5988   6913   -112    630   -479       C  
ATOM   1002  O   VAL A 166       9.775 -24.272   8.495  1.00 47.71           O  
ANISOU 1002  O   VAL A 166     5188   6010   6928   -111    647   -569       O  
ATOM   1003  CB  VAL A 166      11.250 -26.452   6.337  1.00 48.71           C  
ANISOU 1003  CB  VAL A 166     5355   6105   7047   -146    637   -543       C  
ATOM   1004  CG1 VAL A 166      11.921 -25.107   6.102  1.00 49.32           C  
ANISOU 1004  CG1 VAL A 166     5396   6156   7187   -204    715   -659       C  
ATOM   1005  CG2 VAL A 166      12.283 -27.563   6.439  1.00 48.82           C  
ANISOU 1005  CG2 VAL A 166     5322   6168   7058   -116    588   -589       C  
ATOM   1006  N   LEU A 167       8.477 -25.003   6.802  1.00 47.17           N  
ANISOU 1006  N   LEU A 167     5252   5831   6838   -131    643   -375       N  
ATOM   1007  CA  LEU A 167       7.712 -23.760   6.734  1.00 47.16           C  
ANISOU 1007  CA  LEU A 167     5272   5761   6885   -154    678   -363       C  
ATOM   1008  C   LEU A 167       6.570 -23.638   7.747  1.00 48.12           C  
ANISOU 1008  C   LEU A 167     5372   5920   6991   -107    643   -341       C  
ATOM   1009  O   LEU A 167       6.132 -22.522   8.014  1.00 48.50           O  
ANISOU 1009  O   LEU A 167     5401   5929   7096   -118    669   -379       O  
ATOM   1010  CB  LEU A 167       7.202 -23.502   5.314  1.00 46.66           C  
ANISOU 1010  CB  LEU A 167     5299   5589   6840   -197    701   -271       C  
ATOM   1011  CG  LEU A 167       8.229 -23.637   4.193  1.00 47.64           C  
ANISOU 1011  CG  LEU A 167     5456   5680   6967   -260    749   -289       C  
ATOM   1012  CD1 LEU A 167       7.613 -23.310   2.865  1.00 48.22           C  
ANISOU 1012  CD1 LEU A 167     5629   5655   7036   -303    764   -187       C  
ATOM   1013  CD2 LEU A 167       9.463 -22.772   4.434  1.00 47.97           C  
ANISOU 1013  CD2 LEU A 167     5442   5719   7064   -308    815   -418       C  
ATOM   1014  N   ARG A 168       6.102 -24.749   8.341  1.00 48.31           N  
ANISOU 1014  N   ARG A 168     5394   6016   6945    -60    589   -288       N  
ATOM   1015  CA  ARG A 168       5.033 -24.700   9.333  1.00 49.02           C  
ANISOU 1015  CA  ARG A 168     5463   6154   7010    -29    567   -274       C  
ATOM   1016  C   ARG A 168       5.474 -23.880  10.528  1.00 50.51           C  
ANISOU 1016  C   ARG A 168     5574   6411   7207    -27    586   -395       C  
ATOM   1017  O   ARG A 168       6.579 -24.071  11.002  1.00 50.50           O  
ANISOU 1017  O   ARG A 168     5530   6475   7182    -22    578   -468       O  
ATOM   1018  CB  ARG A 168       4.687 -26.111   9.812  1.00 50.08           C  
ANISOU 1018  CB  ARG A 168     5607   6361   7058     10    514   -205       C  
ATOM   1019  CG  ARG A 168       3.654 -26.805   8.965  1.00 53.54           C  
ANISOU 1019  CG  ARG A 168     6108   6743   7493     16    496    -89       C  
ATOM   1020  CD  ARG A 168       2.284 -26.181   9.121  1.00 57.64           C  
ANISOU 1020  CD  ARG A 168     6630   7229   8043     16    508    -69       C  
ATOM   1021  NE  ARG A 168       1.489 -26.282   7.895  1.00 61.39           N  
ANISOU 1021  NE  ARG A 168     7163   7607   8555     10    500     12       N  
ATOM   1022  CZ  ARG A 168       0.187 -26.014   7.820  1.00 64.45           C  
ANISOU 1022  CZ  ARG A 168     7556   7954   8978     19    493     41       C  
ATOM   1023  NH1 ARG A 168      -0.451 -26.115   6.663  1.00 64.60           N  
ANISOU 1023  NH1 ARG A 168     7628   7890   9028     18    474    110       N  
ATOM   1024  NH2 ARG A 168      -0.487 -25.647   8.903  1.00 64.36           N  
ANISOU 1024  NH2 ARG A 168     7492   7991   8970     28    504     -8       N  
ATOM   1025  N   THR A 169       4.658 -22.926  10.975  1.00 51.86           N  
ANISOU 1025  N   THR A 169     5717   6564   7423    -33    610   -432       N  
ATOM   1026  CA  THR A 169       4.989 -22.097  12.139  1.00 53.51           C  
ANISOU 1026  CA  THR A 169     5842   6845   7644    -34    631   -563       C  
ATOM   1027  C   THR A 169       3.716 -21.590  12.852  1.00 54.48           C  
ANISOU 1027  C   THR A 169     5933   6984   7783    -28    641   -584       C  
ATOM   1028  O   THR A 169       2.625 -21.654  12.288  1.00 54.39           O  
ANISOU 1028  O   THR A 169     5962   6898   7805    -25    635   -506       O  
ATOM   1029  CB  THR A 169       5.966 -20.956  11.754  1.00 55.06           C  
ANISOU 1029  CB  THR A 169     6007   6975   7937    -71    680   -661       C  
ATOM   1030  OG1 THR A 169       6.512 -20.361  12.941  1.00 55.98           O  
ANISOU 1030  OG1 THR A 169     6031   7182   8056    -69    695   -804       O  
ATOM   1031  CG2 THR A 169       5.315 -19.912  10.861  1.00 55.50           C  
ANISOU 1031  CG2 THR A 169     6099   6883   8104   -100    714   -629       C  
ATOM   1032  N   THR A 170       3.860 -21.096  14.093  1.00 55.08           N  
ANISOU 1032  N   THR A 170     5929   7162   7836    -27    654   -701       N  
ATOM   1033  CA  THR A 170       2.739 -20.563  14.856  1.00 55.99           C  
ANISOU 1033  CA  THR A 170     5995   7307   7970    -30    674   -753       C  
ATOM   1034  C   THR A 170       2.911 -19.083  15.183  1.00 57.32           C  
ANISOU 1034  C   THR A 170     6084   7437   8259    -51    719   -897       C  
ATOM   1035  O   THR A 170       3.885 -18.688  15.807  1.00 57.72           O  
ANISOU 1035  O   THR A 170     6078   7548   8306    -59    734  -1006       O  
ATOM   1036  CB  THR A 170       2.464 -21.387  16.124  1.00 56.83           C  
ANISOU 1036  CB  THR A 170     6079   7579   7935    -20    656   -765       C  
ATOM   1037  OG1 THR A 170       3.663 -21.542  16.877  1.00 57.74           O  
ANISOU 1037  OG1 THR A 170     6159   7803   7978    -14    639   -840       O  
ATOM   1038  CG2 THR A 170       1.876 -22.732  15.827  1.00 57.06           C  
ANISOU 1038  CG2 THR A 170     6184   7621   7873     -5    620   -618       C  
ATOM   1039  N   GLY A 171       1.932 -18.288  14.801  1.00 58.14           N  
ANISOU 1039  N   GLY A 171     6176   7439   8476    -56    736   -904       N  
ATOM   1040  CA  GLY A 171       1.904 -16.856  15.070  1.00 59.29           C  
ANISOU 1040  CA  GLY A 171     6241   7525   8761    -74    776  -1038       C  
ATOM   1041  C   GLY A 171       0.538 -16.259  14.791  1.00 60.33           C  
ANISOU 1041  C   GLY A 171     6360   7553   9009    -67    774  -1032       C  
ATOM   1042  O   GLY A 171      -0.290 -16.885  14.124  1.00 59.77           O  
ANISOU 1042  O   GLY A 171     6355   7431   8922    -51    741   -912       O  
ATOM   1043  N   ASP A 172       0.290 -15.046  15.296  1.00 61.78           N  
ANISOU 1043  N   ASP A 172     6450   7701   9322    -78    806  -1172       N  
ATOM   1044  CA  ASP A 172      -0.991 -14.383  15.069  1.00 63.92           C  
ANISOU 1044  CA  ASP A 172     6692   7864   9733    -66    796  -1189       C  
ATOM   1045  C   ASP A 172      -1.121 -13.903  13.623  1.00 65.78           C  
ANISOU 1045  C   ASP A 172     7010   7891  10094    -58    763  -1077       C  
ATOM   1046  O   ASP A 172      -0.789 -12.765  13.298  1.00 66.26           O  
ANISOU 1046  O   ASP A 172     7044   7822  10310    -69    775  -1131       O  
ATOM   1047  CB  ASP A 172      -1.228 -13.236  16.063  1.00 65.94           C  
ANISOU 1047  CB  ASP A 172     6810   8146  10100    -78    837  -1388       C  
ATOM   1048  CG  ASP A 172      -2.608 -12.601  15.966  1.00 71.09           C  
ANISOU 1048  CG  ASP A 172     7409   8702  10901    -62    823  -1430       C  
ATOM   1049  OD1 ASP A 172      -3.516 -13.221  15.355  1.00 71.28           O  
ANISOU 1049  OD1 ASP A 172     7497   8676  10912    -38    780  -1311       O  
ATOM   1050  OD2 ASP A 172      -2.793 -11.494  16.520  1.00 74.15           O  
ANISOU 1050  OD2 ASP A 172     7682   9065  11426    -70    852  -1595       O  
ATOM   1051  N   LEU A 173      -1.636 -14.775  12.764  1.00 66.62           N  
ANISOU 1051  N   LEU A 173     7216   7963  10134    -41    719   -920       N  
ATOM   1052  CA  LEU A 173      -1.830 -14.462  11.363  1.00 67.77           C  
ANISOU 1052  CA  LEU A 173     7454   7930  10363    -34    678   -797       C  
ATOM   1053  C   LEU A 173      -3.159 -13.746  11.132  1.00 69.57           C  
ANISOU 1053  C   LEU A 173     7650   8038  10745     -4    637   -814       C  
ATOM   1054  O   LEU A 173      -4.218 -14.192  11.593  1.00 69.54           O  
ANISOU 1054  O   LEU A 173     7603   8091  10728     20    619   -836       O  
ATOM   1055  CB  LEU A 173      -1.750 -15.747  10.542  1.00 67.46           C  
ANISOU 1055  CB  LEU A 173     7524   7920  10188    -26    646   -640       C  
ATOM   1056  CG  LEU A 173      -1.782 -15.576   9.051  1.00 68.27           C  
ANISOU 1056  CG  LEU A 173     7738   7871  10329    -28    605   -504       C  
ATOM   1057  CD1 LEU A 173      -0.584 -14.786   8.565  1.00 68.55           C  
ANISOU 1057  CD1 LEU A 173     7810   7827  10408    -72    642   -507       C  
ATOM   1058  CD2 LEU A 173      -1.872 -16.914   8.374  1.00 68.74           C  
ANISOU 1058  CD2 LEU A 173     7880   7982  10256    -18    574   -377       C  
ATOM   1059  N   GLU A 174      -3.085 -12.613  10.425  1.00 71.01           N  
ANISOU 1059  N   GLU A 174     7850   8047  11082     -9    621   -809       N  
ATOM   1060  CA  GLU A 174      -4.226 -11.754  10.073  1.00 72.84           C  
ANISOU 1060  CA  GLU A 174     8056   8126  11493     26    564   -820       C  
ATOM   1061  C   GLU A 174      -4.957 -11.173  11.322  1.00 73.06           C  
ANISOU 1061  C   GLU A 174     7925   8202  11633     39    587  -1012       C  
ATOM   1062  O   GLU A 174      -6.172 -10.960  11.315  1.00 73.17           O  
ANISOU 1062  O   GLU A 174     7892   8138  11772     76    538  -1044       O  
ATOM   1063  CB  GLU A 174      -5.194 -12.434   9.073  1.00 76.61           C  
ANISOU 1063  CB  GLU A 174     8621   8547  11941     64    483   -674       C  
ATOM   1064  CG  GLU A 174      -4.514 -13.176   7.914  1.00 83.82           C  
ANISOU 1064  CG  GLU A 174     9682   9441  12724     46    465   -499       C  
ATOM   1065  CD  GLU A 174      -3.731 -12.421   6.841  1.00 92.43           C  
ANISOU 1065  CD  GLU A 174    10876  10381  13864     14    458   -409       C  
ATOM   1066  OE1 GLU A 174      -3.269 -11.283   7.102  1.00 94.72           O  
ANISOU 1066  OE1 GLU A 174    11124  10577  14288     -5    484   -485       O  
ATOM   1067  OE2 GLU A 174      -3.558 -12.990   5.736  1.00 94.38           O  
ANISOU 1067  OE2 GLU A 174    11244  10604  14012      1    433   -266       O  
ATOM   1068  N   ASN A 175      -4.151 -10.927  12.377  1.00 72.71           N  
ANISOU 1068  N   ASN A 175     7795   8289  11543      7    663  -1149       N  
ATOM   1069  CA  ASN A 175      -4.371 -10.250  13.657  1.00 72.49           C  
ANISOU 1069  CA  ASN A 175     7611   8334  11598     -2    710  -1359       C  
ATOM   1070  C   ASN A 175      -5.742 -10.457  14.341  1.00 72.18           C  
ANISOU 1070  C   ASN A 175     7479   8358  11588     21    700  -1448       C  
ATOM   1071  O   ASN A 175      -6.458  -9.482  14.603  1.00 72.35           O  
ANISOU 1071  O   ASN A 175     7396   8296  11798     35    692  -1577       O  
ATOM   1072  CB  ASN A 175      -4.091  -8.747  13.490  1.00 73.43           C  
ANISOU 1072  CB  ASN A 175     7679   8282  11939     -7    713  -1444       C  
ATOM   1073  CG  ASN A 175      -2.956  -8.427  12.555  1.00 76.41           C  
ANISOU 1073  CG  ASN A 175     8159   8559  12313    -37    724  -1343       C  
ATOM   1074  OD1 ASN A 175      -3.162  -7.834  11.495  1.00 77.69           O  
ANISOU 1074  OD1 ASN A 175     8410   8531  12579    -29    675  -1226       O  
ATOM   1075  ND2 ASN A 175      -1.747  -8.844  12.911  1.00 76.68           N  
ANISOU 1075  ND2 ASN A 175     8188   8726  12223    -73    786  -1384       N  
ATOM   1076  N   THR A 176      -6.082 -11.706  14.701  1.00 71.59           N  
ANISOU 1076  N   THR A 176     7432   8436  11333     18    709  -1395       N  
ATOM   1077  CA  THR A 176      -7.337 -11.959  15.439  1.00 71.25           C  
ANISOU 1077  CA  THR A 176     7297   8473  11300     23    720  -1491       C  
ATOM   1078  C   THR A 176      -7.107 -12.125  16.971  1.00 70.19           C  
ANISOU 1078  C   THR A 176     7058   8556  11057    -22    804  -1656       C  
ATOM   1079  O   THR A 176      -8.080 -12.306  17.706  1.00 70.52           O  
ANISOU 1079  O   THR A 176     7014   8684  11098    -35    833  -1759       O  
ATOM   1080  CB  THR A 176      -8.159 -13.129  14.836  1.00 72.70           C  
ANISOU 1080  CB  THR A 176     7566   8669  11388     43    678  -1344       C  
ATOM   1081  OG1 THR A 176      -7.317 -14.251  14.531  1.00 73.99           O  
ANISOU 1081  OG1 THR A 176     7857   8885  11370     34    672  -1182       O  
ATOM   1082  CG2 THR A 176      -8.936 -12.714  13.606  1.00 73.00           C  
ANISOU 1082  CG2 THR A 176     7630   8510  11596     93    592  -1280       C  
ATOM   1083  N   ASN A 177      -5.829 -12.051  17.431  1.00 68.72           N  
ANISOU 1083  N   ASN A 177     6875   8457  10777    -49    842  -1687       N  
ATOM   1084  CA  ASN A 177      -5.349 -12.228  18.811  1.00 67.72           C  
ANISOU 1084  CA  ASN A 177     6671   8545  10516    -91    909  -1824       C  
ATOM   1085  C   ASN A 177      -5.211 -13.717  19.246  1.00 66.38           C  
ANISOU 1085  C   ASN A 177     6576   8558  10089   -109    919  -1722       C  
ATOM   1086  O   ASN A 177      -4.764 -14.002  20.359  1.00 66.29           O  
ANISOU 1086  O   ASN A 177     6521   8735   9933   -143    963  -1808       O  
ATOM   1087  CB  ASN A 177      -6.176 -11.426  19.794  1.00 68.61           C  
ANISOU 1087  CB  ASN A 177     6624   8702  10743   -110    955  -2045       C  
ATOM   1088  CG  ASN A 177      -6.008  -9.961  19.545  1.00 71.13           C  
ANISOU 1088  CG  ASN A 177     6861   8872  11292    -99    953  -2166       C  
ATOM   1089  OD1 ASN A 177      -4.889  -9.466  19.392  1.00 72.18           O  
ANISOU 1089  OD1 ASN A 177     7009   8988  11426   -107    963  -2173       O  
ATOM   1090  ND2 ASN A 177      -7.107  -9.235  19.496  1.00 71.71           N  
ANISOU 1090  ND2 ASN A 177     6843   8828  11577    -82    940  -2268       N  
ATOM   1091  N   LYS A 178      -5.564 -14.648  18.345  1.00 65.16           N  
ANISOU 1091  N   LYS A 178     6537   8340   9880    -85    873  -1534       N  
ATOM   1092  CA  LYS A 178      -5.449 -16.091  18.512  1.00 64.24           C  
ANISOU 1092  CA  LYS A 178     6507   8347   9553    -95    869  -1407       C  
ATOM   1093  C   LYS A 178      -4.287 -16.559  17.614  1.00 63.29           C  
ANISOU 1093  C   LYS A 178     6502   8171   9375    -74    826  -1255       C  
ATOM   1094  O   LYS A 178      -4.163 -16.091  16.482  1.00 63.60           O  
ANISOU 1094  O   LYS A 178     6586   8043   9535    -50    791  -1191       O  
ATOM   1095  CB  LYS A 178      -6.768 -16.772  18.105  1.00 65.44           C  
ANISOU 1095  CB  LYS A 178     6683   8461   9722    -86    854  -1335       C  
ATOM   1096  CG  LYS A 178      -7.972 -16.274  18.908  1.00 68.72           C  
ANISOU 1096  CG  LYS A 178     6973   8937  10201   -114    905  -1503       C  
ATOM   1097  CD  LYS A 178      -9.240 -17.093  18.697  1.00 72.11           C  
ANISOU 1097  CD  LYS A 178     7412   9338  10648   -110    898  -1453       C  
ATOM   1098  CE  LYS A 178     -10.083 -16.560  17.566  1.00 75.65           C  
ANISOU 1098  CE  LYS A 178     7857   9576  11311    -57    831  -1428       C  
ATOM   1099  NZ  LYS A 178      -9.606 -17.024  16.236  1.00 77.91           N  
ANISOU 1099  NZ  LYS A 178     8280   9761  11562    -20    762  -1223       N  
ATOM   1100  N   VAL A 179      -3.426 -17.439  18.119  1.00 61.98           N  
ANISOU 1100  N   VAL A 179     6382   8142   9028    -85    828  -1206       N  
ATOM   1101  CA  VAL A 179      -2.285 -17.904  17.347  1.00 61.63           C  
ANISOU 1101  CA  VAL A 179     6428   8057   8933    -68    792  -1091       C  
ATOM   1102  C   VAL A 179      -2.662 -19.088  16.437  1.00 61.60           C  
ANISOU 1102  C   VAL A 179     6533   8000   8873    -49    750   -908       C  
ATOM   1103  O   VAL A 179      -3.380 -19.981  16.867  1.00 62.01           O  
ANISOU 1103  O   VAL A 179     6599   8127   8834    -56    753   -862       O  
ATOM   1104  CB  VAL A 179      -1.082 -18.176  18.263  1.00 61.94           C  
ANISOU 1104  CB  VAL A 179     6448   8252   8835    -81    801  -1146       C  
ATOM   1105  CG1 VAL A 179      -0.745 -16.923  19.061  1.00 62.55           C  
ANISOU 1105  CG1 VAL A 179     6408   8373   8985   -100    843  -1342       C  
ATOM   1106  CG2 VAL A 179      -1.350 -19.341  19.197  1.00 62.06           C  
ANISOU 1106  CG2 VAL A 179     6489   8431   8660    -92    798  -1099       C  
ATOM   1107  N   GLN A 180      -2.243 -19.063  15.156  1.00 60.83           N  
ANISOU 1107  N   GLN A 180     6509   7768   8836    -32    717   -809       N  
ATOM   1108  CA  GLN A 180      -2.608 -20.128  14.208  1.00 60.30           C  
ANISOU 1108  CA  GLN A 180     6537   7646   8728    -14    677   -650       C  
ATOM   1109  C   GLN A 180      -1.427 -20.990  13.806  1.00 58.88           C  
ANISOU 1109  C   GLN A 180     6428   7498   8445    -11    656   -563       C  
ATOM   1110  O   GLN A 180      -0.304 -20.516  13.811  1.00 58.85           O  
ANISOU 1110  O   GLN A 180     6411   7500   8448    -20    666   -614       O  
ATOM   1111  CB  GLN A 180      -3.301 -19.579  12.929  1.00 62.38           C  
ANISOU 1111  CB  GLN A 180     6840   7731   9132      2    646   -592       C  
ATOM   1112  CG  GLN A 180      -3.511 -18.061  12.844  1.00 66.48           C  
ANISOU 1112  CG  GLN A 180     7296   8145   9818      1    657   -696       C  
ATOM   1113  CD  GLN A 180      -4.834 -17.594  13.420  1.00 71.91           C  
ANISOU 1113  CD  GLN A 180     7901   8827  10594     10    661   -782       C  
ATOM   1114  OE1 GLN A 180      -5.667 -18.389  13.876  1.00 73.79           O  
ANISOU 1114  OE1 GLN A 180     8133   9135  10769     12    662   -761       O  
ATOM   1115  NE2 GLN A 180      -5.063 -16.282  13.415  1.00 72.77           N  
ANISOU 1115  NE2 GLN A 180     7939   8848  10863     13    667   -890       N  
ATOM   1116  N   CYS A 181      -1.684 -22.245  13.423  1.00 57.71           N  
ANISOU 1116  N   CYS A 181     6347   7362   8219      0    627   -442       N  
ATOM   1117  CA  CYS A 181      -0.654 -23.171  12.946  1.00 57.00           C  
ANISOU 1117  CA  CYS A 181     6319   7289   8050      7    600   -361       C  
ATOM   1118  C   CYS A 181      -0.754 -23.167  11.412  1.00 57.18           C  
ANISOU 1118  C   CYS A 181     6412   7175   8139     12    578   -268       C  
ATOM   1119  O   CYS A 181      -1.578 -23.887  10.841  1.00 57.52           O  
ANISOU 1119  O   CYS A 181     6499   7188   8169     24    553   -178       O  
ATOM   1120  CB  CYS A 181      -0.867 -24.564  13.536  1.00 56.42           C  
ANISOU 1120  CB  CYS A 181     6270   7318   7848     14    582   -293       C  
ATOM   1121  SG  CYS A 181       0.193 -25.858  12.835  1.00 56.84           S  
ANISOU 1121  SG  CYS A 181     6395   7367   7834     31    536   -186       S  
ATOM   1122  N   TYR A 182       0.042 -22.280  10.759  1.00 56.64           N  
ANISOU 1122  N   TYR A 182     6353   7025   8142     -2    590   -297       N  
ATOM   1123  CA  TYR A 182       0.047 -22.018   9.311  1.00 56.15           C  
ANISOU 1123  CA  TYR A 182     6362   6833   8139    -11    576   -221       C  
ATOM   1124  C   TYR A 182       1.393 -22.282   8.646  1.00 56.35           C  
ANISOU 1124  C   TYR A 182     6426   6852   8134    -34    588   -208       C  
ATOM   1125  O   TYR A 182       2.424 -22.286   9.316  1.00 56.29           O  
ANISOU 1125  O   TYR A 182     6373   6917   8098    -42    609   -286       O  
ATOM   1126  CB  TYR A 182      -0.347 -20.543   9.055  1.00 55.53           C  
ANISOU 1126  CB  TYR A 182     6267   6642   8191    -20    588   -267       C  
ATOM   1127  CG  TYR A 182       0.657 -19.524   9.568  1.00 55.46           C  
ANISOU 1127  CG  TYR A 182     6204   6634   8233    -46    633   -380       C  
ATOM   1128  CD1 TYR A 182       0.517 -18.952  10.824  1.00 56.10           C  
ANISOU 1128  CD1 TYR A 182     6190   6789   8338    -42    657   -503       C  
ATOM   1129  CD2 TYR A 182       1.693 -19.070   8.765  1.00 55.91           C  
ANISOU 1129  CD2 TYR A 182     6302   6619   8322    -81    656   -372       C  
ATOM   1130  CE1 TYR A 182       1.423 -18.008  11.294  1.00 56.72           C  
ANISOU 1130  CE1 TYR A 182     6209   6870   8472    -65    698   -620       C  
ATOM   1131  CE2 TYR A 182       2.604 -18.128   9.225  1.00 56.59           C  
ANISOU 1131  CE2 TYR A 182     6333   6702   8468   -108    703   -485       C  
ATOM   1132  CZ  TYR A 182       2.470 -17.602  10.492  1.00 57.28           C  
ANISOU 1132  CZ  TYR A 182     6319   6862   8582    -97    721   -611       C  
ATOM   1133  OH  TYR A 182       3.374 -16.673  10.948  1.00 58.29           O  
ANISOU 1133  OH  TYR A 182     6384   6989   8777   -124    768   -735       O  
ATOM   1134  N   MET A 183       1.389 -22.415   7.311  1.00 56.48           N  
ANISOU 1134  N   MET A 183     6519   6779   8162    -49    576   -123       N  
ATOM   1135  CA  MET A 183       2.598 -22.602   6.519  1.00 56.91           C  
ANISOU 1135  CA  MET A 183     6611   6816   8195    -84    598   -115       C  
ATOM   1136  C   MET A 183       3.115 -21.234   6.086  1.00 58.58           C  
ANISOU 1136  C   MET A 183     6830   6935   8492   -127    641   -162       C  
ATOM   1137  O   MET A 183       2.489 -20.586   5.256  1.00 58.78           O  
ANISOU 1137  O   MET A 183     6911   6852   8572   -139    631   -103       O  
ATOM   1138  CB  MET A 183       2.280 -23.437   5.282  1.00 56.28           C  
ANISOU 1138  CB  MET A 183     6613   6692   8080    -88    570     -6       C  
ATOM   1139  CG  MET A 183       3.472 -23.642   4.403  1.00 56.76           C  
ANISOU 1139  CG  MET A 183     6712   6738   8117   -133    600     -6       C  
ATOM   1140  SD  MET A 183       4.078 -25.327   4.208  1.00 55.89           S  
ANISOU 1140  SD  MET A 183     6603   6708   7925   -121    578     18       S  
ATOM   1141  CE  MET A 183       3.335 -26.115   5.575  1.00 53.95           C  
ANISOU 1141  CE  MET A 183     6297   6557   7646    -59    536     13       C  
ATOM   1142  N   ASP A 184       4.245 -20.791   6.634  1.00 59.91           N  
ANISOU 1142  N   ASP A 184     6944   7142   8677   -150    685   -266       N  
ATOM   1143  CA  ASP A 184       4.800 -19.478   6.304  1.00 61.93           C  
ANISOU 1143  CA  ASP A 184     7199   7306   9024   -198    737   -320       C  
ATOM   1144  C   ASP A 184       5.710 -19.481   5.082  1.00 63.17           C  
ANISOU 1144  C   ASP A 184     7427   7403   9172   -261    777   -286       C  
ATOM   1145  O   ASP A 184       6.852 -19.920   5.179  1.00 63.12           O  
ANISOU 1145  O   ASP A 184     7388   7458   9136   -284    809   -353       O  
ATOM   1146  CB  ASP A 184       5.572 -18.912   7.503  1.00 64.69           C  
ANISOU 1146  CB  ASP A 184     7446   7726   9406   -199    771   -468       C  
ATOM   1147  CG  ASP A 184       6.020 -17.477   7.318  1.00 70.95           C  
ANISOU 1147  CG  ASP A 184     8223   8419  10314   -248    829   -539       C  
ATOM   1148  OD1 ASP A 184       5.256 -16.687   6.706  1.00 72.22           O  
ANISOU 1148  OD1 ASP A 184     8436   8452  10552   -262    826   -477       O  
ATOM   1149  OD2 ASP A 184       7.134 -17.142   7.776  1.00 73.44           O  
ANISOU 1149  OD2 ASP A 184     8474   8779  10651   -273    874   -658       O  
ATOM   1150  N   TYR A 185       5.243 -18.929   3.956  1.00 64.08           N  
ANISOU 1150  N   TYR A 185     7634   7397   9316   -293    776   -191       N  
ATOM   1151  CA  TYR A 185       6.076 -18.841   2.753  1.00 65.55           C  
ANISOU 1151  CA  TYR A 185     7897   7527   9480   -369    825   -155       C  
ATOM   1152  C   TYR A 185       7.048 -17.628   2.767  1.00 67.11           C  
ANISOU 1152  C   TYR A 185     8077   7661   9761   -438    907   -241       C  
ATOM   1153  O   TYR A 185       7.871 -17.495   1.864  1.00 67.02           O  
ANISOU 1153  O   TYR A 185     8118   7615   9732   -515    968   -236       O  
ATOM   1154  CB  TYR A 185       5.208 -18.847   1.490  1.00 65.50           C  
ANISOU 1154  CB  TYR A 185     8009   7429   9447   -381    786    -11       C  
ATOM   1155  CG  TYR A 185       4.328 -20.071   1.393  1.00 66.40           C  
ANISOU 1155  CG  TYR A 185     8135   7608   9486   -321    715     60       C  
ATOM   1156  CD1 TYR A 185       4.851 -21.299   1.021  1.00 67.46           C  
ANISOU 1156  CD1 TYR A 185     8274   7823   9533   -330    720     64       C  
ATOM   1157  CD2 TYR A 185       2.973 -20.004   1.686  1.00 67.42           C  
ANISOU 1157  CD2 TYR A 185     8259   7711   9644   -259    646    109       C  
ATOM   1158  CE1 TYR A 185       4.048 -22.434   0.937  1.00 68.38           C  
ANISOU 1158  CE1 TYR A 185     8397   7990   9593   -278    659    125       C  
ATOM   1159  CE2 TYR A 185       2.159 -21.131   1.606  1.00 68.35           C  
ANISOU 1159  CE2 TYR A 185     8383   7884   9701   -210    589    165       C  
ATOM   1160  CZ  TYR A 185       2.698 -22.344   1.217  1.00 69.15           C  
ANISOU 1160  CZ  TYR A 185     8496   8061   9717   -221    596    178       C  
ATOM   1161  OH  TYR A 185       1.905 -23.466   1.122  1.00 70.23           O  
ANISOU 1161  OH  TYR A 185     8636   8243   9807   -177    544    231       O  
ATOM   1162  N   SER A 186       6.949 -16.748   3.783  1.00 68.26           N  
ANISOU 1162  N   SER A 186     8144   7792  10000   -417    916   -330       N  
ATOM   1163  CA  SER A 186       7.826 -15.585   3.897  1.00 69.90           C  
ANISOU 1163  CA  SER A 186     8320   7934  10304   -480    995   -425       C  
ATOM   1164  C   SER A 186       9.267 -15.958   4.227  1.00 71.17           C  
ANISOU 1164  C   SER A 186     8411   8189  10442   -514   1056   -552       C  
ATOM   1165  O   SER A 186      10.184 -15.197   3.900  1.00 71.32           O  
ANISOU 1165  O   SER A 186     8427   8148  10523   -591   1138   -617       O  
ATOM   1166  CB  SER A 186       7.298 -14.593   4.926  1.00 71.48           C  
ANISOU 1166  CB  SER A 186     8439   8100  10618   -444    985   -503       C  
ATOM   1167  OG  SER A 186       8.117 -13.433   4.933  1.00 74.13           O  
ANISOU 1167  OG  SER A 186     8752   8352  11062   -511   1064   -588       O  
ATOM   1168  N   MET A 187       9.471 -17.112   4.876  1.00 71.81           N  
ANISOU 1168  N   MET A 187     8433   8410  10441   -459   1015   -591       N  
ATOM   1169  CA  MET A 187      10.814 -17.569   5.171  1.00 73.11           C  
ANISOU 1169  CA  MET A 187     8527   8665  10586   -479   1052   -712       C  
ATOM   1170  C   MET A 187      11.532 -18.113   3.915  1.00 74.09           C  
ANISOU 1170  C   MET A 187     8719   8768  10663   -547   1096   -673       C  
ATOM   1171  O   MET A 187      12.735 -18.346   3.980  1.00 74.19           O  
ANISOU 1171  O   MET A 187     8671   8837  10679   -576   1137   -786       O  
ATOM   1172  CB  MET A 187      10.848 -18.553   6.352  1.00 74.50           C  
ANISOU 1172  CB  MET A 187     8618   8989  10700   -395    983   -768       C  
ATOM   1173  CG  MET A 187       9.695 -19.528   6.381  1.00 78.48           C  
ANISOU 1173  CG  MET A 187     9171   9528  11119   -333    902   -640       C  
ATOM   1174  SD  MET A 187       9.723 -20.694   7.778  1.00 87.57           S  
ANISOU 1174  SD  MET A 187    10243  10844  12184   -245    822   -681       S  
ATOM   1175  CE  MET A 187       8.772 -19.789   8.988  1.00 86.89           C  
ANISOU 1175  CE  MET A 187    10103  10782  12129   -206    806   -719       C  
ATOM   1176  N   VAL A 188      10.826 -18.261   2.763  1.00 74.71           N  
ANISOU 1176  N   VAL A 188     8918   8768  10701   -577   1089   -527       N  
ATOM   1177  CA  VAL A 188      11.444 -18.705   1.507  1.00 75.78           C  
ANISOU 1177  CA  VAL A 188     9125   8887  10782   -655   1140   -493       C  
ATOM   1178  C   VAL A 188      11.356 -17.653   0.378  1.00 76.93           C  
ANISOU 1178  C   VAL A 188     9384   8893  10953   -753   1207   -414       C  
ATOM   1179  O   VAL A 188      12.029 -17.813  -0.645  1.00 77.10           O  
ANISOU 1179  O   VAL A 188     9465   8899  10929   -842   1274   -403       O  
ATOM   1180  CB  VAL A 188      10.959 -20.090   1.001  1.00 76.32           C  
ANISOU 1180  CB  VAL A 188     9234   9015  10748   -615   1076   -404       C  
ATOM   1181  CG1 VAL A 188      11.743 -21.225   1.644  1.00 76.77           C  
ANISOU 1181  CG1 VAL A 188     9194   9194  10781   -575   1056   -507       C  
ATOM   1182  CG2 VAL A 188       9.462 -20.272   1.194  1.00 76.77           C  
ANISOU 1182  CG2 VAL A 188     9327   9058  10782   -534    983   -286       C  
ATOM   1183  N   ALA A 189      10.541 -16.592   0.539  1.00 77.61           N  
ANISOU 1183  N   ALA A 189     9502   8876  11112   -742   1190   -361       N  
ATOM   1184  CA  ALA A 189      10.397 -15.595  -0.528  1.00 78.88           C  
ANISOU 1184  CA  ALA A 189     9782   8890  11298   -829   1237   -265       C  
ATOM   1185  C   ALA A 189       9.900 -14.212  -0.040  1.00 79.77           C  
ANISOU 1185  C   ALA A 189     9886   8881  11542   -818   1231   -264       C  
ATOM   1186  O   ALA A 189       9.409 -14.092   1.083  1.00 79.92           O  
ANISOU 1186  O   ALA A 189     9808   8936  11621   -734   1182   -329       O  
ATOM   1187  CB  ALA A 189       9.474 -16.148  -1.624  1.00 79.22           C  
ANISOU 1187  CB  ALA A 189     9955   8906  11239   -825   1176    -94       C  
ATOM   1188  N   THR A 190      10.044 -13.168  -0.890  1.00 80.19           N  
ANISOU 1188  N   THR A 190    10041   8787  11641   -909   1286   -193       N  
ATOM   1189  CA  THR A 190       9.565 -11.811  -0.631  1.00 81.03           C  
ANISOU 1189  CA  THR A 190    10158   8743  11885   -909   1279   -174       C  
ATOM   1190  C   THR A 190       8.003 -11.764  -0.773  1.00 81.75           C  
ANISOU 1190  C   THR A 190    10309   8770  11983   -819   1150    -34       C  
ATOM   1191  O   THR A 190       7.376 -12.797  -1.013  1.00 82.02           O  
ANISOU 1191  O   THR A 190    10350   8895  11917   -754   1075     19       O  
ATOM   1192  CB  THR A 190      10.312 -10.837  -1.584  1.00 82.20           C  
ANISOU 1192  CB  THR A 190    10406   8758  12070  -1048   1387   -139       C  
ATOM   1193  OG1 THR A 190       9.912 -11.082  -2.936  1.00 83.15           O  
ANISOU 1193  OG1 THR A 190    10693   8828  12074  -1101   1369     36       O  
ATOM   1194  CG2 THR A 190      11.818 -10.952  -1.465  1.00 82.46           C  
ANISOU 1194  CG2 THR A 190    10362   8865  12104  -1133   1516   -298       C  
ATOM   1195  N   VAL A 191       7.374 -10.585  -0.608  1.00 81.76           N  
ANISOU 1195  N   VAL A 191    10343   8612  12112   -814   1120     15       N  
ATOM   1196  CA  VAL A 191       5.924 -10.450  -0.762  1.00 82.00           C  
ANISOU 1196  CA  VAL A 191    10420   8568  12168   -730    994    132       C  
ATOM   1197  C   VAL A 191       5.511 -10.752  -2.221  1.00 81.53           C  
ANISOU 1197  C   VAL A 191    10535   8458  11987   -766    948    320       C  
ATOM   1198  O   VAL A 191       4.579 -11.524  -2.453  1.00 81.81           O  
ANISOU 1198  O   VAL A 191    10592   8547  11947   -694    853    392       O  
ATOM   1199  CB  VAL A 191       5.449  -9.058  -0.247  1.00 83.16           C  
ANISOU 1199  CB  VAL A 191    10529   8556  12513   -707    970    104       C  
ATOM   1200  CG1 VAL A 191       4.155  -8.589  -0.918  1.00 83.80           C  
ANISOU 1200  CG1 VAL A 191    10733   8468  12638   -682    864    274       C  
ATOM   1201  CG2 VAL A 191       5.309  -9.062   1.275  1.00 83.77           C  
ANISOU 1201  CG2 VAL A 191    10432   8723  12673   -614    943    -52       C  
ATOM   1202  N   SER A 192       6.262 -10.211  -3.194  1.00 80.64           N  
ANISOU 1202  N   SER A 192    10542   8256  11844   -884   1024    391       N  
ATOM   1203  CA  SER A 192       5.996 -10.404  -4.623  1.00 80.27           C  
ANISOU 1203  CA  SER A 192    10669   8166  11665   -935    989    568       C  
ATOM   1204  C   SER A 192       6.388 -11.787  -5.153  1.00 79.17           C  
ANISOU 1204  C   SER A 192    10541   8195  11344   -959   1019    559       C  
ATOM   1205  O   SER A 192       6.460 -11.960  -6.373  1.00 79.43           O  
ANISOU 1205  O   SER A 192    10713   8216  11252  -1037   1033    672       O  
ATOM   1206  CB  SER A 192       6.755  -9.359  -5.436  1.00 82.04           C  
ANISOU 1206  CB  SER A 192    11022   8242  11907  -1068   1074    644       C  
ATOM   1207  OG  SER A 192       8.158  -9.577  -5.373  1.00 84.69           O  
ANISOU 1207  OG  SER A 192    11316   8649  12213  -1176   1228    526       O  
ATOM   1208  N   SER A 193       6.681 -12.751  -4.267  1.00 77.70           N  
ANISOU 1208  N   SER A 193    10213   8166  11144   -898   1030    425       N  
ATOM   1209  CA  SER A 193       7.142 -14.067  -4.696  1.00 76.47           C  
ANISOU 1209  CA  SER A 193    10050   8161  10845   -918   1059    398       C  
ATOM   1210  C   SER A 193       6.523 -15.237  -3.926  1.00 74.75           C  
ANISOU 1210  C   SER A 193     9729   8073  10601   -799    978    351       C  
ATOM   1211  O   SER A 193       6.710 -16.376  -4.331  1.00 74.55           O  
ANISOU 1211  O   SER A 193     9709   8153  10463   -800    974    356       O  
ATOM   1212  CB  SER A 193       8.666 -14.128  -4.610  1.00 77.67           C  
ANISOU 1212  CB  SER A 193    10145   8371  10994  -1014   1199    263       C  
ATOM   1213  OG  SER A 193       9.222 -15.150  -5.420  1.00 79.86           O  
ANISOU 1213  OG  SER A 193    10440   8764  11141  -1063   1241    245       O  
ATOM   1214  N   GLU A 194       5.795 -14.976  -2.832  1.00 73.55           N  
ANISOU 1214  N   GLU A 194     9482   7912  10550   -703    917    305       N  
ATOM   1215  CA  GLU A 194       5.189 -16.039  -2.028  1.00 73.00           C  
ANISOU 1215  CA  GLU A 194     9318   7964  10455   -600    850    262       C  
ATOM   1216  C   GLU A 194       4.274 -16.961  -2.835  1.00 71.68           C  
ANISOU 1216  C   GLU A 194     9222   7827  10185   -563    768    376       C  
ATOM   1217  O   GLU A 194       4.152 -18.143  -2.504  1.00 71.86           O  
ANISOU 1217  O   GLU A 194     9188   7969  10147   -516    746    344       O  
ATOM   1218  CB  GLU A 194       4.462 -15.462  -0.807  1.00 75.98           C  
ANISOU 1218  CB  GLU A 194     9597   8316  10954   -518    804    202       C  
ATOM   1219  CG  GLU A 194       5.396 -15.124   0.343  1.00 82.78           C  
ANISOU 1219  CG  GLU A 194    10332   9240  11879   -524    875     40       C  
ATOM   1220  CD  GLU A 194       4.954 -13.942   1.187  1.00 91.84           C  
ANISOU 1220  CD  GLU A 194    11412  10307  13176   -494    866    -24       C  
ATOM   1221  OE1 GLU A 194       5.297 -13.903   2.390  1.00 92.96           O  
ANISOU 1221  OE1 GLU A 194    11429  10532  13359   -464    890   -161       O  
ATOM   1222  OE2 GLU A 194       4.260 -13.052   0.642  1.00 95.42           O  
ANISOU 1222  OE2 GLU A 194    11936  10612  13707   -500    831     59       O  
ATOM   1223  N   TRP A 195       3.666 -16.431  -3.914  1.00 70.03           N  
ANISOU 1223  N   TRP A 195     9141   7510   9958   -587    721    509       N  
ATOM   1224  CA  TRP A 195       2.800 -17.188  -4.812  1.00 68.76           C  
ANISOU 1224  CA  TRP A 195     9058   7370   9699   -559    639    617       C  
ATOM   1225  C   TRP A 195       3.567 -18.309  -5.539  1.00 67.52           C  
ANISOU 1225  C   TRP A 195     8934   7318   9402   -624    695    612       C  
ATOM   1226  O   TRP A 195       3.054 -19.408  -5.633  1.00 67.77           O  
ANISOU 1226  O   TRP A 195     8948   7433   9368   -577    645    624       O  
ATOM   1227  CB  TRP A 195       2.130 -16.252  -5.833  1.00 68.53           C  
ANISOU 1227  CB  TRP A 195     9163   7194   9681   -574    570    759       C  
ATOM   1228  CG  TRP A 195       3.043 -15.788  -6.931  1.00 68.97           C  
ANISOU 1228  CG  TRP A 195     9349   7192   9665   -699    644    826       C  
ATOM   1229  CD1 TRP A 195       3.927 -14.748  -6.884  1.00 69.95           C  
ANISOU 1229  CD1 TRP A 195     9496   7229   9854   -782    733    803       C  
ATOM   1230  CD2 TRP A 195       3.236 -16.423  -8.201  1.00 69.04           C  
ANISOU 1230  CD2 TRP A 195     9474   7244   9514   -769    652    909       C  
ATOM   1231  NE1 TRP A 195       4.636 -14.677  -8.064  1.00 70.23           N  
ANISOU 1231  NE1 TRP A 195     9663   7244   9777   -904    799    876       N  
ATOM   1232  CE2 TRP A 195       4.228 -15.694  -8.889  1.00 69.92           C  
ANISOU 1232  CE2 TRP A 195     9685   7290   9594   -899    750    941       C  
ATOM   1233  CE3 TRP A 195       2.669 -17.542  -8.822  1.00 69.49           C  
ANISOU 1233  CE3 TRP A 195     9557   7392   9454   -740    592    950       C  
ATOM   1234  CZ2 TRP A 195       4.639 -16.034 -10.177  1.00 70.52           C  
ANISOU 1234  CZ2 TRP A 195     9890   7392   9511  -1003    789   1018       C  
ATOM   1235  CZ3 TRP A 195       3.087 -17.883 -10.092  1.00 70.30           C  
ANISOU 1235  CZ3 TRP A 195     9781   7524   9407   -837    625   1019       C  
ATOM   1236  CH2 TRP A 195       4.050 -17.127 -10.761  1.00 70.51           C  
ANISOU 1236  CH2 TRP A 195     9910   7489   9391   -968    723   1054       C  
ATOM   1237  N   ALA A 196       4.782 -18.030  -6.065  1.00 66.00           N  
ANISOU 1237  N   ALA A 196     8784   7120   9172   -736    803    584       N  
ATOM   1238  CA  ALA A 196       5.599 -19.008  -6.796  1.00 64.68           C  
ANISOU 1238  CA  ALA A 196     8639   7052   8885   -808    868    556       C  
ATOM   1239  C   ALA A 196       6.021 -20.190  -5.939  1.00 63.38           C  
ANISOU 1239  C   ALA A 196     8340   7022   8720   -753    876    438       C  
ATOM   1240  O   ALA A 196       6.327 -21.248  -6.474  1.00 63.78           O  
ANISOU 1240  O   ALA A 196     8392   7157   8684   -774    888    422       O  
ATOM   1241  CB  ALA A 196       6.824 -18.336  -7.375  1.00 64.66           C  
ANISOU 1241  CB  ALA A 196     8684   7015   8868   -942    995    521       C  
ATOM   1242  N   TRP A 197       6.065 -20.010  -4.617  1.00 61.71           N  
ANISOU 1242  N   TRP A 197     8014   6828   8605   -686    869    352       N  
ATOM   1243  CA  TRP A 197       6.397 -21.076  -3.694  1.00 60.45           C  
ANISOU 1243  CA  TRP A 197     7733   6786   8450   -626    862    252       C  
ATOM   1244  C   TRP A 197       5.126 -21.825  -3.369  1.00 58.42           C  
ANISOU 1244  C   TRP A 197     7458   6556   8183   -525    758    312       C  
ATOM   1245  O   TRP A 197       5.110 -23.046  -3.482  1.00 58.32           O  
ANISOU 1245  O   TRP A 197     7420   6624   8114   -500    735    305       O  
ATOM   1246  CB  TRP A 197       7.042 -20.510  -2.428  1.00 60.64           C  
ANISOU 1246  CB  TRP A 197     7651   6821   8567   -608    901    135       C  
ATOM   1247  CG  TRP A 197       8.491 -20.221  -2.612  1.00 61.23           C  
ANISOU 1247  CG  TRP A 197     7706   6908   8652   -701   1009     36       C  
ATOM   1248  CD1 TRP A 197       9.046 -19.063  -3.064  1.00 62.20           C  
ANISOU 1248  CD1 TRP A 197     7886   6939   8809   -794   1087     36       C  
ATOM   1249  CD2 TRP A 197       9.568 -21.144  -2.437  1.00 61.51           C  
ANISOU 1249  CD2 TRP A 197     7658   7045   8667   -714   1051    -82       C  
ATOM   1250  NE1 TRP A 197      10.409 -19.194  -3.143  1.00 62.71           N  
ANISOU 1250  NE1 TRP A 197     7902   7050   8877   -869   1186    -85       N  
ATOM   1251  CE2 TRP A 197      10.758 -20.465  -2.759  1.00 62.40           C  
ANISOU 1251  CE2 TRP A 197     7771   7130   8808   -817   1160   -165       C  
ATOM   1252  CE3 TRP A 197       9.644 -22.479  -2.025  1.00 62.02           C  
ANISOU 1252  CE3 TRP A 197     7647   7215   8703   -649   1005   -127       C  
ATOM   1253  CZ2 TRP A 197      12.010 -21.076  -2.678  1.00 62.80           C  
ANISOU 1253  CZ2 TRP A 197     7737   7261   8864   -852   1221   -305       C  
ATOM   1254  CZ3 TRP A 197      10.886 -23.072  -1.926  1.00 62.83           C  
ANISOU 1254  CZ3 TRP A 197     7669   7389   8813   -677   1054   -256       C  
ATOM   1255  CH2 TRP A 197      12.050 -22.374  -2.257  1.00 62.82           C  
ANISOU 1255  CH2 TRP A 197     7660   7364   8844   -776   1160   -349       C  
ATOM   1256  N   GLU A 198       4.038 -21.088  -3.040  1.00 56.70           N  
ANISOU 1256  N   GLU A 198     7253   6262   8028   -471    696    367       N  
ATOM   1257  CA  GLU A 198       2.708 -21.627  -2.742  1.00 55.41           C  
ANISOU 1257  CA  GLU A 198     7071   6109   7871   -381    601    417       C  
ATOM   1258  C   GLU A 198       2.234 -22.531  -3.887  1.00 52.92           C  
ANISOU 1258  C   GLU A 198     6827   5818   7463   -386    558    498       C  
ATOM   1259  O   GLU A 198       1.755 -23.638  -3.646  1.00 53.19           O  
ANISOU 1259  O   GLU A 198     6814   5922   7473   -332    518    492       O  
ATOM   1260  CB  GLU A 198       1.719 -20.463  -2.506  1.00 58.63           C  
ANISOU 1260  CB  GLU A 198     7497   6407   8371   -345    549    460       C  
ATOM   1261  CG  GLU A 198       0.243 -20.830  -2.566  1.00 66.05           C  
ANISOU 1261  CG  GLU A 198     8451   7327   9319   -271    446    531       C  
ATOM   1262  CD  GLU A 198      -0.700 -19.671  -2.305  1.00 76.54           C  
ANISOU 1262  CD  GLU A 198     9762   8556  10766   -223    392    537       C  
ATOM   1263  OE1 GLU A 198      -1.809 -19.659  -2.888  1.00 78.69           O  
ANISOU 1263  OE1 GLU A 198    10076   8767  11055   -180    303    610       O  
ATOM   1264  OE2 GLU A 198      -0.327 -18.770  -1.520  1.00 80.58           O  
ANISOU 1264  OE2 GLU A 198    10208   9048  11360   -226    436    459       O  
ATOM   1265  N   VAL A 199       2.418 -22.070  -5.123  1.00 50.41           N  
ANISOU 1265  N   VAL A 199     6621   5443   7089   -457    570    570       N  
ATOM   1266  CA  VAL A 199       2.043 -22.781  -6.328  1.00 48.56           C  
ANISOU 1266  CA  VAL A 199     6464   5233   6754   -475    534    641       C  
ATOM   1267  C   VAL A 199       3.040 -23.880  -6.625  1.00 47.05           C  
ANISOU 1267  C   VAL A 199     6238   5146   6494   -522    600    570       C  
ATOM   1268  O   VAL A 199       2.642 -25.002  -6.883  1.00 47.16           O  
ANISOU 1268  O   VAL A 199     6223   5226   6471   -485    562    566       O  
ATOM   1269  CB  VAL A 199       1.840 -21.794  -7.495  1.00 48.71           C  
ANISOU 1269  CB  VAL A 199     6625   5154   6729   -536    516    750       C  
ATOM   1270  CG1 VAL A 199       1.840 -22.496  -8.845  1.00 49.02           C  
ANISOU 1270  CG1 VAL A 199     6748   5240   6635   -583    502    805       C  
ATOM   1271  CG2 VAL A 199       0.554 -21.007  -7.295  1.00 49.16           C  
ANISOU 1271  CG2 VAL A 199     6703   5108   6867   -461    414    822       C  
ATOM   1272  N   GLY A 200       4.324 -23.584  -6.516  1.00 45.63           N  
ANISOU 1272  N   GLY A 200     6043   4979   6314   -598    698    496       N  
ATOM   1273  CA  GLY A 200       5.374 -24.564  -6.759  1.00 45.00           C  
ANISOU 1273  CA  GLY A 200     5915   4993   6190   -644    764    405       C  
ATOM   1274  C   GLY A 200       5.224 -25.835  -5.952  1.00 44.38           C  
ANISOU 1274  C   GLY A 200     5728   4997   6138   -560    721    349       C  
ATOM   1275  O   GLY A 200       5.098 -26.915  -6.526  1.00 44.36           O  
ANISOU 1275  O   GLY A 200     5721   5048   6084   -557    702    348       O  
ATOM   1276  N   LEU A 201       5.141 -25.691  -4.618  1.00 43.89           N  
ANISOU 1276  N   LEU A 201     5583   4938   6153   -488    698    311       N  
ATOM   1277  CA  LEU A 201       4.973 -26.789  -3.662  1.00 43.91           C  
ANISOU 1277  CA  LEU A 201     5491   5010   6182   -408    656    271       C  
ATOM   1278  C   LEU A 201       3.568 -27.415  -3.738  1.00 44.22           C  
ANISOU 1278  C   LEU A 201     5546   5046   6211   -340    571    353       C  
ATOM   1279  O   LEU A 201       3.420 -28.615  -3.540  1.00 44.54           O  
ANISOU 1279  O   LEU A 201     5540   5141   6242   -303    544    340       O  
ATOM   1280  CB  LEU A 201       5.208 -26.286  -2.229  1.00 43.94           C  
ANISOU 1280  CB  LEU A 201     5417   5024   6256   -364    661    211       C  
ATOM   1281  CG  LEU A 201       6.517 -25.589  -1.925  1.00 45.54           C  
ANISOU 1281  CG  LEU A 201     5583   5231   6488   -419    737    114       C  
ATOM   1282  CD1 LEU A 201       6.355 -24.658  -0.757  1.00 46.06           C  
ANISOU 1282  CD1 LEU A 201     5600   5282   6620   -382    735     77       C  
ATOM   1283  CD2 LEU A 201       7.611 -26.590  -1.609  1.00 46.30           C  
ANISOU 1283  CD2 LEU A 201     5602   5409   6580   -418    756     18       C  
ATOM   1284  N   GLY A 202       2.553 -26.589  -3.959  1.00 44.06           N  
ANISOU 1284  N   GLY A 202     5579   4955   6206   -320    528    428       N  
ATOM   1285  CA  GLY A 202       1.175 -27.042  -4.058  1.00 44.36           C  
ANISOU 1285  CA  GLY A 202     5625   4981   6247   -257    448    493       C  
ATOM   1286  C   GLY A 202       0.951 -27.941  -5.259  1.00 44.69           C  
ANISOU 1286  C   GLY A 202     5713   5049   6218   -277    425    528       C  
ATOM   1287  O   GLY A 202       0.335 -28.999  -5.121  1.00 45.16           O  
ANISOU 1287  O   GLY A 202     5730   5148   6282   -229    385    529       O  
ATOM   1288  N   VAL A 203       1.475 -27.550  -6.443  1.00 44.28           N  
ANISOU 1288  N   VAL A 203     5745   4980   6098   -356    457    551       N  
ATOM   1289  CA  VAL A 203       1.384 -28.332  -7.688  1.00 44.35           C  
ANISOU 1289  CA  VAL A 203     5803   5025   6023   -392    445    572       C  
ATOM   1290  C   VAL A 203       2.190 -29.641  -7.580  1.00 44.83           C  
ANISOU 1290  C   VAL A 203     5784   5172   6079   -401    485    484       C  
ATOM   1291  O   VAL A 203       1.766 -30.690  -8.071  1.00 45.17           O  
ANISOU 1291  O   VAL A 203     5812   5254   6098   -384    453    481       O  
ATOM   1292  CB  VAL A 203       1.810 -27.495  -8.916  1.00 44.35           C  
ANISOU 1292  CB  VAL A 203     5919   4991   5939   -489    482    616       C  
ATOM   1293  CG1 VAL A 203       1.953 -28.361 -10.162  1.00 44.69           C  
ANISOU 1293  CG1 VAL A 203     6003   5097   5879   -544    491    612       C  
ATOM   1294  CG2 VAL A 203       0.821 -26.377  -9.168  1.00 44.55           C  
ANISOU 1294  CG2 VAL A 203     6032   4922   5975   -468    414    720       C  
ATOM   1295  N   SER A 204       3.335 -29.576  -6.914  1.00 44.62           N  
ANISOU 1295  N   SER A 204     5699   5167   6085   -424    550    404       N  
ATOM   1296  CA  SER A 204       4.164 -30.747  -6.677  1.00 45.02           C  
ANISOU 1296  CA  SER A 204     5664   5285   6155   -422    576    313       C  
ATOM   1297  C   SER A 204       3.425 -31.732  -5.748  1.00 45.44           C  
ANISOU 1297  C   SER A 204     5643   5356   6265   -326    511    322       C  
ATOM   1298  O   SER A 204       3.516 -32.942  -5.942  1.00 46.13           O  
ANISOU 1298  O   SER A 204     5683   5482   6361   -312    499    287       O  
ATOM   1299  CB  SER A 204       5.475 -30.331  -6.018  1.00 46.13           C  
ANISOU 1299  CB  SER A 204     5753   5439   6334   -453    644    223       C  
ATOM   1300  OG  SER A 204       6.062 -29.208  -6.654  1.00 48.31           O  
ANISOU 1300  OG  SER A 204     6098   5685   6574   -544    713    219       O  
ATOM   1301  N   SER A 205       2.700 -31.214  -4.745  1.00 44.71           N  
ANISOU 1301  N   SER A 205     5540   5234   6215   -267    475    364       N  
ATOM   1302  CA  SER A 205       1.974 -32.026  -3.787  1.00 44.65           C  
ANISOU 1302  CA  SER A 205     5470   5242   6251   -190    426    377       C  
ATOM   1303  C   SER A 205       0.837 -32.802  -4.425  1.00 45.14           C  
ANISOU 1303  C   SER A 205     5547   5299   6303   -163    374    426       C  
ATOM   1304  O   SER A 205       0.548 -33.923  -4.015  1.00 45.08           O  
ANISOU 1304  O   SER A 205     5486   5315   6327   -123    350    419       O  
ATOM   1305  CB  SER A 205       1.428 -31.152  -2.672  1.00 45.63           C  
ANISOU 1305  CB  SER A 205     5580   5343   6413   -148    412    398       C  
ATOM   1306  OG  SER A 205       0.820 -31.978  -1.697  1.00 48.23           O  
ANISOU 1306  OG  SER A 205     5850   5701   6773    -89    381    402       O  
ATOM   1307  N   THR A 206       0.157 -32.181  -5.391  1.00 45.61           N  
ANISOU 1307  N   THR A 206     5681   5324   6325   -184    352    477       N  
ATOM   1308  CA  THR A 206      -0.977 -32.765  -6.127  1.00 46.12           C  
ANISOU 1308  CA  THR A 206     5763   5383   6375   -160    295    517       C  
ATOM   1309  C   THR A 206      -0.486 -33.707  -7.252  1.00 46.55           C  
ANISOU 1309  C   THR A 206     5824   5482   6380   -206    311    480       C  
ATOM   1310  O   THR A 206      -1.127 -34.717  -7.572  1.00 46.49           O  
ANISOU 1310  O   THR A 206     5788   5492   6383   -181    275    476       O  
ATOM   1311  CB  THR A 206      -1.879 -31.625  -6.654  1.00 46.69           C  
ANISOU 1311  CB  THR A 206     5913   5397   6429   -157    249    585       C  
ATOM   1312  OG1 THR A 206      -2.311 -30.822  -5.548  1.00 47.44           O  
ANISOU 1312  OG1 THR A 206     5983   5452   6588   -114    238    597       O  
ATOM   1313  CG2 THR A 206      -3.071 -32.133  -7.454  1.00 46.62           C  
ANISOU 1313  CG2 THR A 206     5925   5385   6404   -130    178    619       C  
ATOM   1314  N   MET A 207       0.668 -33.374  -7.828  1.00 46.61           N  
ANISOU 1314  N   MET A 207     5859   5509   6340   -279    372    440       N  
ATOM   1315  CA  MET A 207       1.265 -34.149  -8.880  1.00 47.13           C  
ANISOU 1315  CA  MET A 207     5925   5624   6357   -336    402    385       C  
ATOM   1316  C   MET A 207       1.728 -35.511  -8.390  1.00 47.28           C  
ANISOU 1316  C   MET A 207     5842   5679   6444   -306    406    312       C  
ATOM   1317  O   MET A 207       1.403 -36.531  -8.988  1.00 47.18           O  
ANISOU 1317  O   MET A 207     5803   5689   6433   -299    383    290       O  
ATOM   1318  CB  MET A 207       2.426 -33.362  -9.487  1.00 48.22           C  
ANISOU 1318  CB  MET A 207     6112   5772   6435   -430    480    351       C  
ATOM   1319  CG  MET A 207       2.772 -33.821 -10.840  1.00 51.89           C  
ANISOU 1319  CG  MET A 207     6617   6285   6812   -508    509    318       C  
ATOM   1320  SD  MET A 207       1.345 -33.721 -11.942  1.00 60.90           S  
ANISOU 1320  SD  MET A 207     7850   7418   7872   -495    424    414       S  
ATOM   1321  CE  MET A 207       1.703 -35.142 -13.028  1.00 61.48           C  
ANISOU 1321  CE  MET A 207     7880   7582   7896   -548    449    314       C  
ATOM   1322  N   VAL A 208       2.439 -35.521  -7.268  1.00 47.32           N  
ANISOU 1322  N   VAL A 208     5788   5683   6509   -282    428    275       N  
ATOM   1323  CA  VAL A 208       2.968 -36.711  -6.614  1.00 47.73           C  
ANISOU 1323  CA  VAL A 208     5745   5753   6636   -245    421    216       C  
ATOM   1324  C   VAL A 208       1.909 -37.392  -5.671  1.00 48.09           C  
ANISOU 1324  C   VAL A 208     5755   5775   6741   -161    360    275       C  
ATOM   1325  O   VAL A 208       1.888 -38.620  -5.536  1.00 48.25           O  
ANISOU 1325  O   VAL A 208     5716   5798   6818   -132    338    252       O  
ATOM   1326  CB  VAL A 208       4.299 -36.307  -5.911  1.00 48.10           C  
ANISOU 1326  CB  VAL A 208     5757   5810   6709   -260    464    154       C  
ATOM   1327  CG1 VAL A 208       4.435 -36.875  -4.490  1.00 48.46           C  
ANISOU 1327  CG1 VAL A 208     5731   5853   6829   -186    427    152       C  
ATOM   1328  CG2 VAL A 208       5.496 -36.660  -6.784  1.00 48.41           C  
ANISOU 1328  CG2 VAL A 208     5773   5885   6737   -334    523     47       C  
ATOM   1329  N   GLY A 209       1.043 -36.591  -5.056  1.00 47.70           N  
ANISOU 1329  N   GLY A 209     5741   5700   6685   -130    340    345       N  
ATOM   1330  CA  GLY A 209       0.029 -37.112  -4.154  1.00 47.70           C  
ANISOU 1330  CA  GLY A 209     5710   5683   6732    -67    299    393       C  
ATOM   1331  C   GLY A 209      -1.279 -37.500  -4.812  1.00 47.77           C  
ANISOU 1331  C   GLY A 209     5733   5675   6743    -52    260    429       C  
ATOM   1332  O   GLY A 209      -2.169 -38.020  -4.124  1.00 48.38           O  
ANISOU 1332  O   GLY A 209     5777   5738   6867     -8    235    457       O  
ATOM   1333  N   PHE A 210      -1.439 -37.237  -6.130  1.00 47.02           N  
ANISOU 1333  N   PHE A 210     5689   5584   6593    -90    255    426       N  
ATOM   1334  CA  PHE A 210      -2.698 -37.582  -6.786  1.00 47.08           C  
ANISOU 1334  CA  PHE A 210     5706   5581   6602    -69    207    451       C  
ATOM   1335  C   PHE A 210      -2.565 -37.937  -8.254  1.00 46.32           C  
ANISOU 1335  C   PHE A 210     5635   5515   6450   -114    204    417       C  
ATOM   1336  O   PHE A 210      -2.958 -39.040  -8.625  1.00 46.38           O  
ANISOU 1336  O   PHE A 210     5595   5536   6494   -101    186    384       O  
ATOM   1337  CB  PHE A 210      -3.772 -36.481  -6.587  1.00 47.52           C  
ANISOU 1337  CB  PHE A 210     5807   5598   6650    -42    169    511       C  
ATOM   1338  CG  PHE A 210      -5.197 -36.889  -6.921  1.00 48.58           C  
ANISOU 1338  CG  PHE A 210     5924   5717   6817     -2    112    526       C  
ATOM   1339  CD1 PHE A 210      -5.921 -37.704  -6.067  1.00 49.56           C  
ANISOU 1339  CD1 PHE A 210     5981   5832   7019     40    108    522       C  
ATOM   1340  CD2 PHE A 210      -5.821 -36.421  -8.065  1.00 49.51           C  
ANISOU 1340  CD2 PHE A 210     6096   5830   6887     -9     61    542       C  
ATOM   1341  CE1 PHE A 210      -7.218 -38.088  -6.377  1.00 50.52           C  
ANISOU 1341  CE1 PHE A 210     6076   5938   7181     72     63    520       C  
ATOM   1342  CE2 PHE A 210      -7.125 -36.796  -8.370  1.00 50.38           C  
ANISOU 1342  CE2 PHE A 210     6179   5927   7035     33      2    541       C  
ATOM   1343  CZ  PHE A 210      -7.816 -37.625  -7.524  1.00 50.42           C  
ANISOU 1343  CZ  PHE A 210     6105   5923   7130     72      8    523       C  
ATOM   1344  N   VAL A 211      -2.056 -37.020  -9.095  1.00 45.50           N  
ANISOU 1344  N   VAL A 211     5607   5423   6259   -170    222    424       N  
ATOM   1345  CA  VAL A 211      -2.019 -37.262 -10.538  1.00 45.23           C  
ANISOU 1345  CA  VAL A 211     5611   5429   6146   -222    217    397       C  
ATOM   1346  C   VAL A 211      -1.194 -38.497 -10.918  1.00 44.87           C  
ANISOU 1346  C   VAL A 211     5493   5431   6123   -252    257    300       C  
ATOM   1347  O   VAL A 211      -1.744 -39.408 -11.533  1.00 45.52           O  
ANISOU 1347  O   VAL A 211     5539   5535   6223   -241    228    266       O  
ATOM   1348  CB  VAL A 211      -1.609 -36.021 -11.365  1.00 45.51           C  
ANISOU 1348  CB  VAL A 211     5755   5468   6070   -289    235    434       C  
ATOM   1349  CG1 VAL A 211      -1.832 -36.266 -12.849  1.00 45.65           C  
ANISOU 1349  CG1 VAL A 211     5822   5535   5987   -342    218    418       C  
ATOM   1350  CG2 VAL A 211      -2.382 -34.791 -10.915  1.00 45.98           C  
ANISOU 1350  CG2 VAL A 211     5875   5463   6133   -250    186    525       C  
ATOM   1351  N   VAL A 212       0.082 -38.549 -10.538  1.00 43.43           N  
ANISOU 1351  N   VAL A 212     5280   5262   5958   -286    318    245       N  
ATOM   1352  CA  VAL A 212       0.934 -39.680 -10.858  1.00 42.81           C  
ANISOU 1352  CA  VAL A 212     5123   5219   5923   -311    352    140       C  
ATOM   1353  C   VAL A 212       0.393 -41.032 -10.297  1.00 42.03           C  
ANISOU 1353  C   VAL A 212     4932   5098   5940   -244    312    121       C  
ATOM   1354  O   VAL A 212       0.215 -41.941 -11.098  1.00 41.70           O  
ANISOU 1354  O   VAL A 212     4851   5082   5911   -258    306     60       O  
ATOM   1355  CB  VAL A 212       2.393 -39.379 -10.457  1.00 43.76           C  
ANISOU 1355  CB  VAL A 212     5222   5348   6057   -348    415     82       C  
ATOM   1356  CG1 VAL A 212       3.253 -40.644 -10.452  1.00 44.49           C  
ANISOU 1356  CG1 VAL A 212     5206   5458   6239   -349    434    -32       C  
ATOM   1357  CG2 VAL A 212       2.981 -38.321 -11.383  1.00 44.01           C  
ANISOU 1357  CG2 VAL A 212     5339   5410   5972   -442    472     75       C  
ATOM   1358  N   PRO A 213       0.050 -41.192  -9.001  1.00 42.01           N  
ANISOU 1358  N   PRO A 213     4897   5049   6018   -177    287    172       N  
ATOM   1359  CA  PRO A 213      -0.506 -42.479  -8.540  1.00 42.29           C  
ANISOU 1359  CA  PRO A 213     4857   5055   6157   -125    254    165       C  
ATOM   1360  C   PRO A 213      -1.813 -42.890  -9.243  1.00 42.62           C  
ANISOU 1360  C   PRO A 213     4901   5096   6196   -112    216    178       C  
ATOM   1361  O   PRO A 213      -1.972 -44.054  -9.595  1.00 42.53           O  
ANISOU 1361  O   PRO A 213     4825   5084   6249   -107    207    120       O  
ATOM   1362  CB  PRO A 213      -0.728 -42.248  -7.040  1.00 42.86           C  
ANISOU 1362  CB  PRO A 213     4924   5086   6275    -70    239    239       C  
ATOM   1363  CG  PRO A 213       0.171 -41.143  -6.688  1.00 43.22           C  
ANISOU 1363  CG  PRO A 213     5008   5146   6267    -92    270    243       C  
ATOM   1364  CD  PRO A 213       0.162 -40.247  -7.877  1.00 41.70           C  
ANISOU 1364  CD  PRO A 213     4885   4983   5976   -150    290    235       C  
ATOM   1365  N   LEU A 214      -2.734 -41.945  -9.474  1.00 42.56           N  
ANISOU 1365  N   LEU A 214     4961   5086   6124   -103    188    243       N  
ATOM   1366  CA  LEU A 214      -3.990 -42.246 -10.170  1.00 42.78           C  
ANISOU 1366  CA  LEU A 214     4989   5116   6149    -86    142    247       C  
ATOM   1367  C   LEU A 214      -3.747 -42.649 -11.643  1.00 43.54           C  
ANISOU 1367  C   LEU A 214     5086   5270   6186   -138    144    169       C  
ATOM   1368  O   LEU A 214      -4.448 -43.495 -12.183  1.00 43.79           O  
ANISOU 1368  O   LEU A 214     5069   5312   6259   -126    117    123       O  
ATOM   1369  CB  LEU A 214      -4.933 -41.047 -10.086  1.00 42.26           C  
ANISOU 1369  CB  LEU A 214     4995   5032   6030    -65    102    325       C  
ATOM   1370  CG  LEU A 214      -6.370 -41.316 -10.409  1.00 42.88           C  
ANISOU 1370  CG  LEU A 214     5059   5098   6136    -27     43    332       C  
ATOM   1371  CD1 LEU A 214      -6.957 -42.369  -9.484  1.00 43.34           C  
ANISOU 1371  CD1 LEU A 214     5030   5118   6318     17     48    322       C  
ATOM   1372  CD2 LEU A 214      -7.163 -40.054 -10.317  1.00 43.38           C  
ANISOU 1372  CD2 LEU A 214     5187   5136   6159     -3     -2    399       C  
ATOM   1373  N   THR A 215      -2.728 -42.072 -12.267  1.00 43.64           N  
ANISOU 1373  N   THR A 215     5149   5326   6105   -202    183    144       N  
ATOM   1374  CA  THR A 215      -2.327 -42.417 -13.623  1.00 44.26           C  
ANISOU 1374  CA  THR A 215     5232   5474   6109   -269    202     61       C  
ATOM   1375  C   THR A 215      -1.710 -43.839 -13.643  1.00 44.56           C  
ANISOU 1375  C   THR A 215     5155   5523   6253   -275    233    -54       C  
ATOM   1376  O   THR A 215      -1.896 -44.576 -14.611  1.00 45.11           O  
ANISOU 1376  O   THR A 215     5188   5641   6312   -305    231   -140       O  
ATOM   1377  CB  THR A 215      -1.319 -41.379 -14.109  1.00 45.68           C  
ANISOU 1377  CB  THR A 215     5494   5690   6172   -346    254     66       C  
ATOM   1378  OG1 THR A 215      -1.934 -40.092 -14.053  1.00 46.76           O  
ANISOU 1378  OG1 THR A 215     5735   5800   6232   -335    219    177       O  
ATOM   1379  CG2 THR A 215      -0.807 -41.666 -15.506  1.00 46.05           C  
ANISOU 1379  CG2 THR A 215     5553   5821   6123   -433    290    -25       C  
ATOM   1380  N   ILE A 216      -0.982 -44.223 -12.579  1.00 43.73           N  
ANISOU 1380  N   ILE A 216     4991   5371   6252   -246    255    -61       N  
ATOM   1381  CA  ILE A 216      -0.399 -45.556 -12.471  1.00 43.18           C  
ANISOU 1381  CA  ILE A 216     4811   5289   6307   -239    269   -160       C  
ATOM   1382  C   ILE A 216      -1.512 -46.575 -12.138  1.00 43.57           C  
ANISOU 1382  C   ILE A 216     4801   5287   6466   -177    222   -142       C  
ATOM   1383  O   ILE A 216      -1.532 -47.657 -12.713  1.00 43.95           O  
ANISOU 1383  O   ILE A 216     4773   5344   6583   -185    220   -235       O  
ATOM   1384  CB  ILE A 216       0.770 -45.568 -11.447  1.00 42.85           C  
ANISOU 1384  CB  ILE A 216     4733   5212   6334   -225    295   -170       C  
ATOM   1385  CG1 ILE A 216       1.927 -44.670 -11.925  1.00 43.25           C  
ANISOU 1385  CG1 ILE A 216     4825   5317   6289   -299    354   -219       C  
ATOM   1386  CG2 ILE A 216       1.263 -46.982 -11.164  1.00 42.97           C  
ANISOU 1386  CG2 ILE A 216     4633   5188   6505   -198    286   -253       C  
ATOM   1387  CD1 ILE A 216       2.872 -44.230 -10.873  1.00 43.68           C  
ANISOU 1387  CD1 ILE A 216     4878   5345   6375   -284    373   -201       C  
ATOM   1388  N   MET A 217      -2.456 -46.220 -11.267  1.00 43.37           N  
ANISOU 1388  N   MET A 217     4806   5211   6460   -123    190    -35       N  
ATOM   1389  CA  MET A 217      -3.543 -47.125 -10.909  1.00 44.17           C  
ANISOU 1389  CA  MET A 217     4854   5262   6665    -75    158    -19       C  
ATOM   1390  C   MET A 217      -4.550 -47.302 -12.028  1.00 44.82           C  
ANISOU 1390  C   MET A 217     4932   5382   6717    -85    130    -62       C  
ATOM   1391  O   MET A 217      -5.193 -48.351 -12.098  1.00 44.98           O  
ANISOU 1391  O   MET A 217     4879   5372   6842    -63    116   -101       O  
ATOM   1392  CB  MET A 217      -4.239 -46.670  -9.637  1.00 45.18           C  
ANISOU 1392  CB  MET A 217     5015   5339   6814    -27    144     94       C  
ATOM   1393  CG  MET A 217      -3.380 -46.817  -8.417  1.00 47.88           C  
ANISOU 1393  CG  MET A 217     5341   5639   7212     -7    161    132       C  
ATOM   1394  SD  MET A 217      -4.347 -46.602  -6.914  1.00 52.55           S  
ANISOU 1394  SD  MET A 217     5954   6177   7837     41    151    249       S  
ATOM   1395  CE  MET A 217      -4.859 -44.915  -7.108  1.00 50.31           C  
ANISOU 1395  CE  MET A 217     5758   5933   7425     33    147    298       C  
ATOM   1396  N   LEU A 218      -4.709 -46.289 -12.897  1.00 45.01           N  
ANISOU 1396  N   LEU A 218     5034   5469   6600   -118    118    -54       N  
ATOM   1397  CA  LEU A 218      -5.629 -46.407 -14.020  1.00 45.54           C  
ANISOU 1397  CA  LEU A 218     5103   5583   6619   -126     77    -97       C  
ATOM   1398  C   LEU A 218      -5.021 -47.240 -15.116  1.00 46.60           C  
ANISOU 1398  C   LEU A 218     5181   5779   6745   -179    101   -227       C  
ATOM   1399  O   LEU A 218      -5.673 -48.143 -15.606  1.00 46.75           O  
ANISOU 1399  O   LEU A 218     5130   5807   6828   -169     80   -302       O  
ATOM   1400  CB  LEU A 218      -6.127 -45.059 -14.520  1.00 45.31           C  
ANISOU 1400  CB  LEU A 218     5185   5586   6446   -133     36    -24       C  
ATOM   1401  CG  LEU A 218      -7.212 -44.481 -13.631  1.00 46.29           C  
ANISOU 1401  CG  LEU A 218     5329   5649   6611    -70     -7     68       C  
ATOM   1402  CD1 LEU A 218      -7.462 -43.038 -13.951  1.00 47.00           C  
ANISOU 1402  CD1 LEU A 218     5529   5752   6579    -74    -47    146       C  
ATOM   1403  CD2 LEU A 218      -8.484 -45.295 -13.710  1.00 46.41           C  
ANISOU 1403  CD2 LEU A 218     5271   5645   6720    -27    -49     29       C  
ATOM   1404  N   THR A 219      -3.727 -47.061 -15.394  1.00 47.29           N  
ANISOU 1404  N   THR A 219     5282   5905   6781   -236    154   -272       N  
ATOM   1405  CA  THR A 219      -2.986 -47.876 -16.355  1.00 48.61           C  
ANISOU 1405  CA  THR A 219     5382   6133   6953   -295    192   -417       C  
ATOM   1406  C   THR A 219      -3.088 -49.371 -15.953  1.00 50.22           C  
ANISOU 1406  C   THR A 219     5449   6278   7353   -256    189   -498       C  
ATOM   1407  O   THR A 219      -3.471 -50.201 -16.771  1.00 50.38           O  
ANISOU 1407  O   THR A 219     5405   6332   7404   -267    176   -596       O  
ATOM   1408  CB  THR A 219      -1.521 -47.412 -16.371  1.00 49.78           C  
ANISOU 1408  CB  THR A 219     5554   6307   7053   -353    257   -445       C  
ATOM   1409  OG1 THR A 219      -1.442 -46.001 -16.591  1.00 50.38           O  
ANISOU 1409  OG1 THR A 219     5759   6429   6956   -396    264   -366       O  
ATOM   1410  CG2 THR A 219      -0.688 -48.155 -17.382  1.00 50.39           C  
ANISOU 1410  CG2 THR A 219     5543   6441   7160   -416    308   -612       C  
ATOM   1411  N   CYS A 220      -2.865 -49.671 -14.660  1.00 51.41           N  
ANISOU 1411  N   CYS A 220     5565   6334   7634   -205    191   -443       N  
ATOM   1412  CA  CYS A 220      -2.980 -51.012 -14.081  1.00 53.12           C  
ANISOU 1412  CA  CYS A 220     5671   6469   8044   -163    182   -484       C  
ATOM   1413  C   CYS A 220      -4.367 -51.584 -14.314  1.00 53.71           C  
ANISOU 1413  C   CYS A 220     5713   6525   8171   -133    147   -485       C  
ATOM   1414  O   CYS A 220      -4.483 -52.754 -14.656  1.00 53.36           O  
ANISOU 1414  O   CYS A 220     5568   6460   8246   -133    147   -588       O  
ATOM   1415  CB  CYS A 220      -2.640 -51.001 -12.591  1.00 54.86           C  
ANISOU 1415  CB  CYS A 220     5894   6595   8354   -113    179   -385       C  
ATOM   1416  SG  CYS A 220      -0.872 -50.857 -12.218  1.00 59.71           S  
ANISOU 1416  SG  CYS A 220     6505   7217   8967   -135    212   -420       S  
ATOM   1417  N   TYR A 221      -5.408 -50.776 -14.109  1.00 54.78           N  
ANISOU 1417  N   TYR A 221     5922   6658   8232   -106    116   -382       N  
ATOM   1418  CA  TYR A 221      -6.763 -51.246 -14.336  1.00 56.94           C  
ANISOU 1418  CA  TYR A 221     6159   6916   8559    -77     81   -394       C  
ATOM   1419  C   TYR A 221      -6.992 -51.532 -15.824  1.00 59.52           C  
ANISOU 1419  C   TYR A 221     6455   7334   8826   -114     63   -519       C  
ATOM   1420  O   TYR A 221      -7.448 -52.617 -16.162  1.00 59.83           O  
ANISOU 1420  O   TYR A 221     6400   7356   8975   -103     54   -606       O  
ATOM   1421  CB  TYR A 221      -7.817 -50.282 -13.770  1.00 56.76           C  
ANISOU 1421  CB  TYR A 221     6212   6875   8478    -40     48   -275       C  
ATOM   1422  CG  TYR A 221      -9.213 -50.583 -14.272  1.00 57.40           C  
ANISOU 1422  CG  TYR A 221     6255   6961   8596    -16      6   -313       C  
ATOM   1423  CD1 TYR A 221      -9.837 -51.783 -13.970  1.00 58.22           C  
ANISOU 1423  CD1 TYR A 221     6263   6993   8867      7     16   -350       C  
ATOM   1424  CD2 TYR A 221      -9.881 -49.695 -15.102  1.00 58.49           C  
ANISOU 1424  CD2 TYR A 221     6447   7175   8604    -21    -47   -325       C  
ATOM   1425  CE1 TYR A 221     -11.088 -52.098 -14.490  1.00 59.32           C  
ANISOU 1425  CE1 TYR A 221     6350   7141   9050     24    -18   -411       C  
ATOM   1426  CE2 TYR A 221     -11.148 -49.983 -15.601  1.00 59.51           C  
ANISOU 1426  CE2 TYR A 221     6528   7313   8770      5    -96   -379       C  
ATOM   1427  CZ  TYR A 221     -11.755 -51.185 -15.286  1.00 60.20           C  
ANISOU 1427  CZ  TYR A 221     6509   7332   9032     27    -78   -428       C  
ATOM   1428  OH  TYR A 221     -13.013 -51.475 -15.766  1.00 61.14           O  
ANISOU 1428  OH  TYR A 221     6571   7460   9200     51   -123   -495       O  
ATOM   1429  N   PHE A 222      -6.668 -50.578 -16.703  1.00 61.07           N  
ANISOU 1429  N   PHE A 222     6730   7627   8846   -161     61   -529       N  
ATOM   1430  CA  PHE A 222      -6.885 -50.712 -18.143  1.00 62.92           C  
ANISOU 1430  CA  PHE A 222     6953   7966   8989   -203     41   -638       C  
ATOM   1431  C   PHE A 222      -6.170 -51.897 -18.794  1.00 64.44           C  
ANISOU 1431  C   PHE A 222     7028   8187   9271   -244     82   -807       C  
ATOM   1432  O   PHE A 222      -6.714 -52.491 -19.725  1.00 64.74           O  
ANISOU 1432  O   PHE A 222     6996   8267   9334   -250     59   -915       O  
ATOM   1433  CB  PHE A 222      -6.544 -49.404 -18.863  1.00 63.08           C  
ANISOU 1433  CB  PHE A 222     7103   8078   8786   -253     33   -591       C  
ATOM   1434  CG  PHE A 222      -7.518 -48.310 -18.500  1.00 64.02           C  
ANISOU 1434  CG  PHE A 222     7320   8173   8832   -206    -32   -454       C  
ATOM   1435  CD1 PHE A 222      -8.879 -48.565 -18.431  1.00 64.85           C  
ANISOU 1435  CD1 PHE A 222     7389   8252   9000   -148    -96   -453       C  
ATOM   1436  CD2 PHE A 222      -7.077 -47.024 -18.241  1.00 65.04           C  
ANISOU 1436  CD2 PHE A 222     7569   8302   8841   -221    -28   -341       C  
ATOM   1437  CE1 PHE A 222      -9.773 -47.565 -18.079  1.00 65.62           C  
ANISOU 1437  CE1 PHE A 222     7562   8322   9048   -102   -159   -345       C  
ATOM   1438  CE2 PHE A 222      -7.974 -46.027 -17.879  1.00 65.81           C  
ANISOU 1438  CE2 PHE A 222     7746   8366   8893   -173    -91   -226       C  
ATOM   1439  CZ  PHE A 222      -9.316 -46.302 -17.809  1.00 65.54           C  
ANISOU 1439  CZ  PHE A 222     7669   8307   8927   -113   -159   -231       C  
ATOM   1440  N   PHE A 223      -4.995 -52.269 -18.291  1.00 65.18           N  
ANISOU 1440  N   PHE A 223     7085   8251   9429   -266    136   -838       N  
ATOM   1441  CA  PHE A 223      -4.264 -53.394 -18.848  1.00 66.55           C  
ANISOU 1441  CA  PHE A 223     7136   8441   9710   -302    174  -1009       C  
ATOM   1442  C   PHE A 223      -4.843 -54.711 -18.368  1.00 67.32           C  
ANISOU 1442  C   PHE A 223     7111   8434  10034   -249    158  -1052       C  
ATOM   1443  O   PHE A 223      -5.123 -55.577 -19.192  1.00 67.32           O  
ANISOU 1443  O   PHE A 223     7012   8466  10100   -268    159  -1197       O  
ATOM   1444  CB  PHE A 223      -2.780 -53.275 -18.519  1.00 67.14           C  
ANISOU 1444  CB  PHE A 223     7203   8508   9798   -336    228  -1037       C  
ATOM   1445  CG  PHE A 223      -2.055 -52.324 -19.437  1.00 68.79           C  
ANISOU 1445  CG  PHE A 223     7499   8843   9793   -421    265  -1065       C  
ATOM   1446  CD1 PHE A 223      -2.649 -51.143 -19.851  1.00 69.86           C  
ANISOU 1446  CD1 PHE A 223     7776   9033   9736   -432    238   -946       C  
ATOM   1447  CD2 PHE A 223      -0.784 -52.614 -19.897  1.00 70.15           C  
ANISOU 1447  CD2 PHE A 223     7612   9077   9964   -494    328  -1214       C  
ATOM   1448  CE1 PHE A 223      -1.986 -50.273 -20.698  1.00 70.76           C  
ANISOU 1448  CE1 PHE A 223     7980   9254   9650   -517    274   -959       C  
ATOM   1449  CE2 PHE A 223      -0.120 -51.741 -20.746  1.00 71.06           C  
ANISOU 1449  CE2 PHE A 223     7813   9311   9876   -586    376  -1240       C  
ATOM   1450  CZ  PHE A 223      -0.727 -50.577 -21.139  1.00 70.80           C  
ANISOU 1450  CZ  PHE A 223     7932   9325   9644   -599    348  -1104       C  
ATOM   1451  N   ALA A 224      -5.060 -54.845 -17.036  1.00 67.75           N  
ANISOU 1451  N   ALA A 224     7176   8365  10202   -187    147   -925       N  
ATOM   1452  CA  ALA A 224      -5.596 -56.056 -16.396  1.00 68.18           C  
ANISOU 1452  CA  ALA A 224     7132   8298  10474   -141    138   -933       C  
ATOM   1453  C   ALA A 224      -7.014 -56.363 -16.832  1.00 68.24           C  
ANISOU 1453  C   ALA A 224     7108   8314  10504   -124    108   -960       C  
ATOM   1454  O   ALA A 224      -7.327 -57.524 -17.085  1.00 68.24           O  
ANISOU 1454  O   ALA A 224     6994   8268  10668   -119    112  -1064       O  
ATOM   1455  CB  ALA A 224      -5.525 -55.942 -14.876  1.00 68.26           C  
ANISOU 1455  CB  ALA A 224     7186   8193  10556    -92    136   -775       C  
ATOM   1456  N   ALA A 225      -7.869 -55.334 -16.935  1.00 68.20           N  
ANISOU 1456  N   ALA A 225     7199   8365  10350   -113     75   -877       N  
ATOM   1457  CA  ALA A 225      -9.252 -55.518 -17.379  1.00 68.70           C  
ANISOU 1457  CA  ALA A 225     7230   8445  10428    -93     36   -914       C  
ATOM   1458  C   ALA A 225      -9.289 -56.053 -18.798  1.00 69.54           C  
ANISOU 1458  C   ALA A 225     7261   8651  10509   -132     27  -1092       C  
ATOM   1459  O   ALA A 225     -10.115 -56.904 -19.093  1.00 69.17           O  
ANISOU 1459  O   ALA A 225     7117   8585  10580   -119     14  -1185       O  
ATOM   1460  CB  ALA A 225     -10.018 -54.212 -17.295  1.00 68.57           C  
ANISOU 1460  CB  ALA A 225     7329   8471  10253    -71     -9   -800       C  
ATOM   1461  N   GLN A 226      -8.360 -55.591 -19.657  1.00 70.56           N  
ANISOU 1461  N   GLN A 226     7430   8889  10491   -188     42  -1149       N  
ATOM   1462  CA  GLN A 226      -8.236 -56.039 -21.038  1.00 71.88           C  
ANISOU 1462  CA  GLN A 226     7534   9174  10605   -242     43  -1326       C  
ATOM   1463  C   GLN A 226      -7.893 -57.518 -21.057  1.00 72.41           C  
ANISOU 1463  C   GLN A 226     7438   9175  10898   -246     81  -1476       C  
ATOM   1464  O   GLN A 226      -8.624 -58.277 -21.681  1.00 72.72           O  
ANISOU 1464  O   GLN A 226     7382   9232  11016   -242     62  -1597       O  
ATOM   1465  CB  GLN A 226      -7.185 -55.201 -21.789  1.00 74.26           C  
ANISOU 1465  CB  GLN A 226     7921   9594  10699   -313     70  -1341       C  
ATOM   1466  CG  GLN A 226      -6.709 -55.787 -23.114  1.00 79.26           C  
ANISOU 1466  CG  GLN A 226     8480  10353  11284   -387     97  -1541       C  
ATOM   1467  CD  GLN A 226      -5.240 -55.490 -23.301  1.00 86.01           C  
ANISOU 1467  CD  GLN A 226     9373  11263  12044   -460    164  -1569       C  
ATOM   1468  OE1 GLN A 226      -4.815 -54.322 -23.333  1.00 88.02           O  
ANISOU 1468  OE1 GLN A 226     9768  11578  12098   -494    167  -1465       O  
ATOM   1469  NE2 GLN A 226      -4.424 -56.541 -23.410  1.00 87.17           N  
ANISOU 1469  NE2 GLN A 226     9391  11382  12347   -486    220  -1715       N  
ATOM   1470  N   THR A 227      -6.835 -57.929 -20.323  1.00 72.43           N  
ANISOU 1470  N   THR A 227     7406   9092  11022   -247    126  -1466       N  
ATOM   1471  CA  THR A 227      -6.359 -59.317 -20.211  1.00 73.05           C  
ANISOU 1471  CA  THR A 227     7331   9082  11342   -245    154  -1597       C  
ATOM   1472  C   THR A 227      -7.442 -60.290 -19.718  1.00 73.27           C  
ANISOU 1472  C   THR A 227     7274   8985  11579   -194    137  -1592       C  
ATOM   1473  O   THR A 227      -7.618 -61.378 -20.285  1.00 73.59           O  
ANISOU 1473  O   THR A 227     7180   9012  11769   -205    144  -1754       O  
ATOM   1474  CB  THR A 227      -5.132 -59.360 -19.301  1.00 74.68           C  
ANISOU 1474  CB  THR A 227     7541   9204  11629   -238    183  -1546       C  
ATOM   1475  OG1 THR A 227      -4.082 -58.610 -19.915  1.00 76.20           O  
ANISOU 1475  OG1 THR A 227     7783   9517  11652   -300    214  -1597       O  
ATOM   1476  CG2 THR A 227      -4.664 -60.778 -19.014  1.00 75.05           C  
ANISOU 1476  CG2 THR A 227     7436   9131  11949   -222    196  -1658       C  
ATOM   1477  N   ILE A 228      -8.182 -59.886 -18.675  1.00 72.67           N  
ANISOU 1477  N   ILE A 228     7275   8823  11514   -145    119  -1414       N  
ATOM   1478  CA  ILE A 228      -9.257 -60.699 -18.130  1.00 72.35           C  
ANISOU 1478  CA  ILE A 228     7172   8666  11654   -107    114  -1391       C  
ATOM   1479  C   ILE A 228     -10.373 -60.793 -19.156  1.00 72.79           C  
ANISOU 1479  C   ILE A 228     7171   8804  11682   -115     88  -1512       C  
ATOM   1480  O   ILE A 228     -10.836 -61.893 -19.442  1.00 73.30           O  
ANISOU 1480  O   ILE A 228     7112   8807  11933   -111     98  -1622       O  
ATOM   1481  CB  ILE A 228      -9.696 -60.148 -16.755  1.00 72.23           C  
ANISOU 1481  CB  ILE A 228     7262   8565  11618    -67    110  -1179       C  
ATOM   1482  CG1 ILE A 228      -8.770 -60.667 -15.670  1.00 72.63           C  
ANISOU 1482  CG1 ILE A 228     7289   8463  11846    -47    134  -1102       C  
ATOM   1483  CG2 ILE A 228     -11.144 -60.475 -16.415  1.00 72.78           C  
ANISOU 1483  CG2 ILE A 228     7338   8619  11696    -43     93  -1138       C  
ATOM   1484  CD1 ILE A 228      -8.558 -59.727 -14.683  1.00 73.72           C  
ANISOU 1484  CD1 ILE A 228     7535   8596  11878    -36    133   -959       C  
ATOM   1485  N   ALA A1001     -10.734 -59.665 -19.784  1.00 72.51           N  
ANISOU 1485  N   ALA A1001     9953   6628  10971     -8  -2332  -1554       N  
ATOM   1486  CA  ALA A1001     -11.760 -59.669 -20.812  1.00 72.83           C  
ANISOU 1486  CA  ALA A1001    10208   6433  11032    116  -2312  -1386       C  
ATOM   1487  C   ALA A1001     -11.348 -60.398 -22.097  1.00 73.49           C  
ANISOU 1487  C   ALA A1001    10412   6487  11023    -38  -2065   -855       C  
ATOM   1488  O   ALA A1001     -12.103 -60.365 -23.056  1.00 73.86           O  
ANISOU 1488  O   ALA A1001    10616   6404  11044     63  -2031   -706       O  
ATOM   1489  CB  ALA A1001     -12.200 -58.259 -21.127  1.00 72.87           C  
ANISOU 1489  CB  ALA A1001    10387   5864  11437    149  -2624  -1550       C  
ATOM   1490  N   ASP A1002     -10.176 -61.052 -22.135  1.00 73.52           N  
ANISOU 1490  N   ASP A1002    10326   6646  10962   -257  -1902   -596       N  
ATOM   1491  CA  ASP A1002      -9.778 -61.844 -23.295  1.00 74.08           C  
ANISOU 1491  CA  ASP A1002    10468   6772  10907   -357  -1667   -159       C  
ATOM   1492  C   ASP A1002     -10.249 -63.280 -23.077  1.00 74.03           C  
ANISOU 1492  C   ASP A1002    10382   7160  10585   -186  -1450   -139       C  
ATOM   1493  O   ASP A1002     -10.846 -63.876 -23.976  1.00 74.26           O  
ANISOU 1493  O   ASP A1002    10522   7175  10517   -109  -1338     32       O  
ATOM   1494  CB  ASP A1002      -8.262 -61.780 -23.528  1.00 76.44           C  
ANISOU 1494  CB  ASP A1002    10671   7118  11253   -634  -1590     87       C  
ATOM   1495  CG  ASP A1002      -7.779 -60.432 -24.046  1.00 82.40           C  
ANISOU 1495  CG  ASP A1002    11512   7447  12350   -872  -1797    198       C  
ATOM   1496  OD1 ASP A1002      -8.624 -59.654 -24.567  1.00 83.29           O  
ANISOU 1496  OD1 ASP A1002    11805   7175  12666   -817  -1972    192       O  
ATOM   1497  OD2 ASP A1002      -6.556 -60.147 -23.925  1.00 84.84           O  
ANISOU 1497  OD2 ASP A1002    11697   7801  12738  -1123  -1797    311       O  
ATOM   1498  N   LEU A1003     -10.023 -63.823 -21.868  1.00 73.48           N  
ANISOU 1498  N   LEU A1003    10106   7447  10366   -130  -1411   -311       N  
ATOM   1499  CA  LEU A1003     -10.453 -65.177 -21.531  1.00 73.40           C  
ANISOU 1499  CA  LEU A1003     9991   7796  10101      3  -1236   -248       C  
ATOM   1500  C   LEU A1003     -11.980 -65.261 -21.532  1.00 73.29           C  
ANISOU 1500  C   LEU A1003    10048   7786  10013    201  -1284   -388       C  
ATOM   1501  O   LEU A1003     -12.551 -66.185 -22.104  1.00 73.38           O  
ANISOU 1501  O   LEU A1003    10112   7849   9919    258  -1150   -219       O  
ATOM   1502  CB  LEU A1003      -9.902 -65.567 -20.147  1.00 73.47           C  
ANISOU 1502  CB  LEU A1003     9733   8210   9971     14  -1227   -380       C  
ATOM   1503  CG  LEU A1003      -8.389 -65.466 -19.969  1.00 74.74           C  
ANISOU 1503  CG  LEU A1003     9781   8431  10186   -173  -1197   -284       C  
ATOM   1504  CD1 LEU A1003      -8.026 -64.457 -18.901  1.00 75.14           C  
ANISOU 1504  CD1 LEU A1003     9693   8542  10315   -214  -1398   -625       C  
ATOM   1505  CD2 LEU A1003      -7.794 -66.812 -19.642  1.00 75.35           C  
ANISOU 1505  CD2 LEU A1003     9689   8866  10076   -157  -1003    -59       C  
ATOM   1506  N   GLU A1004     -12.632 -64.271 -20.914  1.00 73.06           N  
ANISOU 1506  N   GLU A1004    10008   7697  10054    311  -1490   -722       N  
ATOM   1507  CA  GLU A1004     -14.079 -64.219 -20.813  1.00 73.52           C  
ANISOU 1507  CA  GLU A1004    10090   7816  10027    522  -1562   -907       C  
ATOM   1508  C   GLU A1004     -14.745 -64.048 -22.151  1.00 73.79           C  
ANISOU 1508  C   GLU A1004    10365   7521  10153    548  -1555   -741       C  
ATOM   1509  O   GLU A1004     -15.855 -64.523 -22.312  1.00 73.74           O  
ANISOU 1509  O   GLU A1004    10364   7648  10006    683  -1513   -753       O  
ATOM   1510  CB  GLU A1004     -14.520 -63.082 -19.896  1.00 76.03           C  
ANISOU 1510  CB  GLU A1004    10330   8130  10426    666  -1815  -1359       C  
ATOM   1511  CG  GLU A1004     -13.867 -63.086 -18.534  1.00 81.45           C  
ANISOU 1511  CG  GLU A1004    10747   9199  11002    654  -1852  -1587       C  
ATOM   1512  CD  GLU A1004     -14.376 -61.985 -17.628  1.00 88.88           C  
ANISOU 1512  CD  GLU A1004    11564  10231  11976    850  -2110  -2123       C  
ATOM   1513  OE1 GLU A1004     -14.323 -62.174 -16.393  1.00 90.73           O  
ANISOU 1513  OE1 GLU A1004    11511  10966  11994    913  -2125  -2355       O  
ATOM   1514  OE2 GLU A1004     -14.836 -60.940 -18.145  1.00 91.18           O  
ANISOU 1514  OE2 GLU A1004    12025  10119  12500    962  -2308  -2322       O  
ATOM   1515  N   ASP A1005     -14.103 -63.368 -23.107  1.00 74.04           N  
ANISOU 1515  N   ASP A1005    10567   7166  10400    409  -1602   -567       N  
ATOM   1516  CA  ASP A1005     -14.702 -63.162 -24.424  1.00 74.81           C  
ANISOU 1516  CA  ASP A1005    10867   7003  10554    435  -1603   -376       C  
ATOM   1517  C   ASP A1005     -14.932 -64.483 -25.134  1.00 74.66           C  
ANISOU 1517  C   ASP A1005    10854   7190  10325    434  -1372   -144       C  
ATOM   1518  O   ASP A1005     -15.982 -64.678 -25.741  1.00 74.95           O  
ANISOU 1518  O   ASP A1005    10975   7213  10291    552  -1367   -131       O  
ATOM   1519  CB  ASP A1005     -13.837 -62.234 -25.296  1.00 77.56           C  
ANISOU 1519  CB  ASP A1005    11352   6968  11150    247  -1688   -149       C  
ATOM   1520  CG  ASP A1005     -14.096 -60.749 -25.099  1.00 83.52           C  
ANISOU 1520  CG  ASP A1005    12188   7328  12216    281  -1989   -349       C  
ATOM   1521  OD1 ASP A1005     -15.096 -60.399 -24.425  1.00 84.40           O  
ANISOU 1521  OD1 ASP A1005    12258   7475  12335    504  -2139   -724       O  
ATOM   1522  OD2 ASP A1005     -13.287 -59.933 -25.606  1.00 86.19           O  
ANISOU 1522  OD2 ASP A1005    12615   7328  12804     86  -2090   -132       O  
ATOM   1523  N   ASN A1006     -13.963 -65.399 -25.037  1.00 74.07           N  
ANISOU 1523  N   ASN A1006    10678   7301  10165    314  -1197     15       N  
ATOM   1524  CA  ASN A1006     -14.077 -66.695 -25.691  1.00 73.87           C  
ANISOU 1524  CA  ASN A1006    10647   7425   9993    323  -1003    194       C  
ATOM   1525  C   ASN A1006     -15.132 -67.567 -25.029  1.00 73.32           C  
ANISOU 1525  C   ASN A1006    10482   7593   9784    452   -968     78       C  
ATOM   1526  O   ASN A1006     -15.831 -68.299 -25.729  1.00 73.44           O  
ANISOU 1526  O   ASN A1006    10544   7632   9729    500   -892    147       O  
ATOM   1527  CB  ASN A1006     -12.718 -67.397 -25.751  1.00 75.04           C  
ANISOU 1527  CB  ASN A1006    10709   7678  10126    190   -855    379       C  
ATOM   1528  CG  ASN A1006     -11.631 -66.570 -26.404  1.00 77.94           C  
ANISOU 1528  CG  ASN A1006    11123   7883  10608     24   -886    529       C  
ATOM   1529  OD1 ASN A1006     -11.895 -65.672 -27.203  1.00 79.20           O  
ANISOU 1529  OD1 ASN A1006    11413   7806  10875    -10  -1002    577       O  
ATOM   1530  ND2 ASN A1006     -10.379 -66.855 -26.082  1.00 78.36           N  
ANISOU 1530  ND2 ASN A1006    11054   8071  10648    -92   -792    638       N  
ATOM   1531  N   TRP A1007     -15.277 -67.473 -23.697  1.00 72.74           N  
ANISOU 1531  N   TRP A1007    10250   7728   9661    501  -1034    -97       N  
ATOM   1532  CA  TRP A1007     -16.294 -68.268 -23.016  1.00 72.90           C  
ANISOU 1532  CA  TRP A1007    10134   8039   9526    596  -1008   -154       C  
ATOM   1533  C   TRP A1007     -17.691 -67.655 -23.231  1.00 72.27           C  
ANISOU 1533  C   TRP A1007    10118   7934   9409    746  -1129   -342       C  
ATOM   1534  O   TRP A1007     -18.652 -68.408 -23.352  1.00 72.30           O  
ANISOU 1534  O   TRP A1007    10079   8090   9302    792  -1081   -307       O  
ATOM   1535  CB  TRP A1007     -15.959 -68.555 -21.534  1.00 73.32           C  
ANISOU 1535  CB  TRP A1007     9934   8455   9469    592  -1008   -210       C  
ATOM   1536  CG  TRP A1007     -14.759 -69.454 -21.332  1.00 74.39           C  
ANISOU 1536  CG  TRP A1007     9982   8664   9619    473   -877     19       C  
ATOM   1537  CD1 TRP A1007     -13.508 -69.072 -20.943  1.00 75.45           C  
ANISOU 1537  CD1 TRP A1007    10057   8805   9804    392   -884     15       C  
ATOM   1538  CD2 TRP A1007     -14.695 -70.881 -21.537  1.00 74.67           C  
ANISOU 1538  CD2 TRP A1007     9970   8757   9645    435   -739    274       C  
ATOM   1539  NE1 TRP A1007     -12.669 -70.163 -20.904  1.00 75.78           N  
ANISOU 1539  NE1 TRP A1007    10015   8937   9840    326   -749    258       N  
ATOM   1540  CE2 TRP A1007     -13.374 -71.286 -21.262  1.00 75.39           C  
ANISOU 1540  CE2 TRP A1007     9978   8892   9775    361   -667    415       C  
ATOM   1541  CE3 TRP A1007     -15.620 -71.852 -21.938  1.00 75.28           C  
ANISOU 1541  CE3 TRP A1007    10062   8828   9713    454   -690    386       C  
ATOM   1542  CZ2 TRP A1007     -12.964 -72.614 -21.369  1.00 75.83           C  
ANISOU 1542  CZ2 TRP A1007     9974   8963   9874    341   -557    655       C  
ATOM   1543  CZ3 TRP A1007     -15.206 -73.166 -22.043  1.00 75.86           C  
ANISOU 1543  CZ3 TRP A1007    10082   8881   9859    406   -591    617       C  
ATOM   1544  CH2 TRP A1007     -13.895 -73.535 -21.755  1.00 75.82           C  
ANISOU 1544  CH2 TRP A1007    10002   8899   9905    367   -530    747       C  
ATOM   1545  N   GLU A1008     -17.802 -66.309 -23.353  1.00 71.63           N  
ANISOU 1545  N   GLU A1008    10139   7632   9445    820  -1300   -531       N  
ATOM   1546  CA  GLU A1008     -19.086 -65.653 -23.633  1.00 71.62           C  
ANISOU 1546  CA  GLU A1008    10206   7572   9435   1001  -1439   -715       C  
ATOM   1547  C   GLU A1008     -19.534 -66.063 -25.026  1.00 70.85           C  
ANISOU 1547  C   GLU A1008    10267   7326   9326    985  -1356   -509       C  
ATOM   1548  O   GLU A1008     -20.693 -66.398 -25.206  1.00 71.12           O  
ANISOU 1548  O   GLU A1008    10271   7513   9238   1093  -1360   -569       O  
ATOM   1549  CB  GLU A1008     -18.966 -64.117 -23.650  1.00 74.78           C  
ANISOU 1549  CB  GLU A1008    10725   7631  10057   1075  -1661   -901       C  
ATOM   1550  CG  GLU A1008     -18.851 -63.390 -22.327  1.00 81.80           C  
ANISOU 1550  CG  GLU A1008    11472   8613  10997   1167  -1833  -1255       C  
ATOM   1551  CD  GLU A1008     -18.581 -61.899 -22.499  1.00 90.47           C  
ANISOU 1551  CD  GLU A1008    12725   9234  12413   1213  -2082  -1408       C  
ATOM   1552  OE1 GLU A1008     -18.938 -61.345 -23.568  1.00 91.50           O  
ANISOU 1552  OE1 GLU A1008    13050   9042  12674   1259  -2152  -1278       O  
ATOM   1553  OE2 GLU A1008     -18.009 -61.283 -21.567  1.00 93.45           O  
ANISOU 1553  OE2 GLU A1008    13023   9558  12927   1197  -2221  -1649       O  
ATOM   1554  N   THR A1009     -18.616 -66.023 -26.016  1.00 69.73           N  
ANISOU 1554  N   THR A1009    10267   6937   9289    852  -1289   -278       N  
ATOM   1555  CA  THR A1009     -18.890 -66.382 -27.403  1.00 69.07           C  
ANISOU 1555  CA  THR A1009    10308   6771   9165    839  -1211    -95       C  
ATOM   1556  C   THR A1009     -19.453 -67.801 -27.491  1.00 68.61           C  
ANISOU 1556  C   THR A1009    10160   6954   8954    842  -1073    -72       C  
ATOM   1557  O   THR A1009     -20.431 -68.033 -28.200  1.00 68.66           O  
ANISOU 1557  O   THR A1009    10207   7002   8880    921  -1083    -95       O  
ATOM   1558  CB  THR A1009     -17.617 -66.235 -28.240  1.00 69.86           C  
ANISOU 1558  CB  THR A1009    10487   6709   9346    681  -1136    147       C  
ATOM   1559  OG1 THR A1009     -17.254 -64.856 -28.309  1.00 70.55           O  
ANISOU 1559  OG1 THR A1009    10669   6522   9616    654  -1300    170       O  
ATOM   1560  CG2 THR A1009     -17.781 -66.786 -29.638  1.00 70.23           C  
ANISOU 1560  CG2 THR A1009    10601   6798   9287    671  -1026    314       C  
ATOM   1561  N   LEU A1010     -18.867 -68.734 -26.724  1.00 67.87           N  
ANISOU 1561  N   LEU A1010     9935   7012   8842    753   -966    -23       N  
ATOM   1562  CA  LEU A1010     -19.313 -70.122 -26.686  1.00 67.33           C  
ANISOU 1562  CA  LEU A1010     9768   7109   8704    725   -865     30       C  
ATOM   1563  C   LEU A1010     -20.733 -70.228 -26.173  1.00 67.01           C  
ANISOU 1563  C   LEU A1010     9629   7278   8555    814   -939   -102       C  
ATOM   1564  O   LEU A1010     -21.552 -70.867 -26.819  1.00 67.04           O  
ANISOU 1564  O   LEU A1010     9644   7316   8513    823   -918    -95       O  
ATOM   1565  CB  LEU A1010     -18.391 -70.961 -25.806  1.00 67.28           C  
ANISOU 1565  CB  LEU A1010     9621   7212   8731    630   -780    138       C  
ATOM   1566  CG  LEU A1010     -17.721 -72.117 -26.492  1.00 68.47           C  
ANISOU 1566  CG  LEU A1010     9796   7261   8958    557   -655    289       C  
ATOM   1567  CD1 LEU A1010     -16.486 -71.655 -27.229  1.00 68.95           C  
ANISOU 1567  CD1 LEU A1010     9970   7171   9056    528   -626    341       C  
ATOM   1568  CD2 LEU A1010     -17.342 -73.160 -25.493  1.00 69.10           C  
ANISOU 1568  CD2 LEU A1010     9716   7458   9081    498   -601    407       C  
ATOM   1569  N   ASN A1011     -21.043 -69.586 -25.040  1.00 66.76           N  
ANISOU 1569  N   ASN A1011     9480   7422   8465    888  -1034   -249       N  
ATOM   1570  CA  ASN A1011     -22.381 -69.645 -24.455  1.00 67.00           C  
ANISOU 1570  CA  ASN A1011     9359   7753   8343    990  -1105   -390       C  
ATOM   1571  C   ASN A1011     -23.444 -68.917 -25.286  1.00 66.38           C  
ANISOU 1571  C   ASN A1011     9396   7592   8235   1142  -1207   -531       C  
ATOM   1572  O   ASN A1011     -24.541 -69.445 -25.450  1.00 66.48           O  
ANISOU 1572  O   ASN A1011     9326   7801   8132   1167  -1204   -549       O  
ATOM   1573  CB  ASN A1011     -22.367 -69.147 -23.003  1.00 68.70           C  
ANISOU 1573  CB  ASN A1011     9371   8270   8461   1061  -1182   -553       C  
ATOM   1574  CG  ASN A1011     -23.733 -69.124 -22.352  1.00 72.96           C  
ANISOU 1574  CG  ASN A1011     9704   9221   8794   1185  -1254   -712       C  
ATOM   1575  OD1 ASN A1011     -24.312 -68.055 -22.093  1.00 74.55           O  
ANISOU 1575  OD1 ASN A1011     9884   9500   8944   1386  -1399  -1000       O  
ATOM   1576  ND2 ASN A1011     -24.298 -70.304 -22.115  1.00 73.79           N  
ANISOU 1576  ND2 ASN A1011     9648   9591   8796   1070  -1169   -526       N  
ATOM   1577  N   ASP A1012     -23.126 -67.723 -25.804  1.00 65.63           N  
ANISOU 1577  N   ASP A1012     9473   7210   8253   1231  -1308   -604       N  
ATOM   1578  CA  ASP A1012     -24.054 -66.935 -26.612  1.00 65.50           C  
ANISOU 1578  CA  ASP A1012     9570   7083   8234   1396  -1428   -698       C  
ATOM   1579  C   ASP A1012     -24.455 -67.701 -27.860  1.00 64.98           C  
ANISOU 1579  C   ASP A1012     9580   7003   8106   1341  -1336   -547       C  
ATOM   1580  O   ASP A1012     -25.646 -67.808 -28.174  1.00 65.09           O  
ANISOU 1580  O   ASP A1012     9547   7185   8000   1446  -1380   -634       O  
ATOM   1581  CB  ASP A1012     -23.415 -65.598 -27.025  1.00 67.58           C  
ANISOU 1581  CB  ASP A1012    10017   6961   8699   1446  -1559   -699       C  
ATOM   1582  CG  ASP A1012     -23.147 -64.632 -25.891  1.00 73.09           C  
ANISOU 1582  CG  ASP A1012    10650   7618   9504   1534  -1711   -937       C  
ATOM   1583  OD1 ASP A1012     -23.744 -64.810 -24.804  1.00 74.40           O  
ANISOU 1583  OD1 ASP A1012    10612   8131   9527   1640  -1744  -1168       O  
ATOM   1584  OD2 ASP A1012     -22.341 -63.695 -26.089  1.00 75.19           O  
ANISOU 1584  OD2 ASP A1012    11045   7532   9990   1489  -1805   -898       O  
ATOM   1585  N   ASN A1013     -23.457 -68.273 -28.550  1.00 64.24           N  
ANISOU 1585  N   ASN A1013     9573   6758   8077   1184  -1208   -350       N  
ATOM   1586  CA  ASN A1013     -23.705 -69.010 -29.776  1.00 63.94           C  
ANISOU 1586  CA  ASN A1013     9590   6725   7979   1141  -1126   -256       C  
ATOM   1587  C   ASN A1013     -24.395 -70.341 -29.549  1.00 62.85           C  
ANISOU 1587  C   ASN A1013     9309   6801   7770   1068  -1054   -288       C  
ATOM   1588  O   ASN A1013     -25.092 -70.796 -30.454  1.00 62.93           O  
ANISOU 1588  O   ASN A1013     9331   6870   7711   1080  -1045   -313       O  
ATOM   1589  CB  ASN A1013     -22.448 -69.160 -30.591  1.00 65.51           C  
ANISOU 1589  CB  ASN A1013     9891   6753   8245   1034  -1031    -82       C  
ATOM   1590  CG  ASN A1013     -22.137 -67.932 -31.412  1.00 69.31           C  
ANISOU 1590  CG  ASN A1013    10517   7048   8771   1085  -1116     24       C  
ATOM   1591  OD1 ASN A1013     -23.012 -67.328 -32.054  1.00 70.49           O  
ANISOU 1591  OD1 ASN A1013    10725   7197   8863   1207  -1211     15       O  
ATOM   1592  ND2 ASN A1013     -20.878 -67.535 -31.415  1.00 70.25           N  
ANISOU 1592  ND2 ASN A1013    10678   7009   9003    982  -1096    156       N  
ATOM   1593  N   LEU A1014     -24.260 -70.943 -28.354  1.00 61.91           N  
ANISOU 1593  N   LEU A1014     9038   6816   7671    987  -1022   -277       N  
ATOM   1594  CA  LEU A1014     -25.023 -72.152 -28.072  1.00 61.73           C  
ANISOU 1594  CA  LEU A1014     8858   6985   7613    892   -987   -255       C  
ATOM   1595  C   LEU A1014     -26.502 -71.803 -27.948  1.00 61.91           C  
ANISOU 1595  C   LEU A1014     8775   7269   7476    997  -1083   -393       C  
ATOM   1596  O   LEU A1014     -27.338 -72.584 -28.389  1.00 62.22           O  
ANISOU 1596  O   LEU A1014     8744   7417   7478    933  -1078   -397       O  
ATOM   1597  CB  LEU A1014     -24.551 -72.944 -26.867  1.00 61.65           C  
ANISOU 1597  CB  LEU A1014     8684   7082   7659    760   -935   -125       C  
ATOM   1598  CG  LEU A1014     -25.312 -74.277 -26.699  1.00 62.84           C  
ANISOU 1598  CG  LEU A1014     8672   7369   7836    615   -920    -27       C  
ATOM   1599  CD1 LEU A1014     -25.149 -75.202 -27.907  1.00 62.99           C  
ANISOU 1599  CD1 LEU A1014     8797   7146   7990    545   -886    -31       C  
ATOM   1600  CD2 LEU A1014     -24.892 -74.992 -25.462  1.00 63.86           C  
ANISOU 1600  CD2 LEU A1014     8631   7599   8034    483   -882    176       C  
ATOM   1601  N   LYS A1015     -26.836 -70.618 -27.408  1.00 61.69           N  
ANISOU 1601  N   LYS A1015     8731   7339   7367   1171  -1186   -534       N  
ATOM   1602  CA  LYS A1015     -28.224 -70.181 -27.329  1.00 62.05           C  
ANISOU 1602  CA  LYS A1015     8667   7659   7250   1324  -1289   -699       C  
ATOM   1603  C   LYS A1015     -28.782 -69.980 -28.743  1.00 62.89           C  
ANISOU 1603  C   LYS A1015     8918   7645   7333   1402  -1320   -723       C  
ATOM   1604  O   LYS A1015     -29.928 -70.345 -29.008  1.00 63.12           O  
ANISOU 1604  O   LYS A1015     8834   7915   7233   1424  -1350   -789       O  
ATOM   1605  CB  LYS A1015     -28.346 -68.892 -26.506  1.00 63.24           C  
ANISOU 1605  CB  LYS A1015     8778   7894   7357   1542  -1420   -902       C  
ATOM   1606  CG  LYS A1015     -27.876 -69.014 -25.062  1.00 66.99           C  
ANISOU 1606  CG  LYS A1015     9055   8613   7786   1497  -1403   -928       C  
ATOM   1607  CD  LYS A1015     -28.606 -70.103 -24.275  1.00 71.98           C  
ANISOU 1607  CD  LYS A1015     9389   9718   8241   1372  -1346   -842       C  
ATOM   1608  CE  LYS A1015     -27.824 -70.535 -23.052  1.00 76.39           C  
ANISOU 1608  CE  LYS A1015     9773  10470   8782   1240  -1281   -713       C  
ATOM   1609  NZ  LYS A1015     -28.281 -71.854 -22.532  1.00 78.83           N  
ANISOU 1609  NZ  LYS A1015     9874  11032   9047   1001  -1193   -438       N  
ATOM   1610  N   VAL A1016     -27.957 -69.433 -29.655  1.00 63.05           N  
ANISOU 1610  N   VAL A1016     9157   7341   7458   1427  -1313   -647       N  
ATOM   1611  CA  VAL A1016     -28.312 -69.226 -31.058  1.00 63.52           C  
ANISOU 1611  CA  VAL A1016     9336   7330   7466   1495  -1334   -621       C  
ATOM   1612  C   VAL A1016     -28.631 -70.562 -31.764  1.00 63.59           C  
ANISOU 1612  C   VAL A1016     9284   7451   7427   1346  -1241   -604       C  
ATOM   1613  O   VAL A1016     -29.611 -70.634 -32.497  1.00 63.97           O  
ANISOU 1613  O   VAL A1016     9298   7657   7350   1412  -1286   -680       O  
ATOM   1614  CB  VAL A1016     -27.207 -68.428 -31.786  1.00 64.29           C  
ANISOU 1614  CB  VAL A1016     9636   7117   7672   1512  -1338   -477       C  
ATOM   1615  CG1 VAL A1016     -27.399 -68.458 -33.298  1.00 64.76           C  
ANISOU 1615  CG1 VAL A1016     9779   7190   7637   1541  -1325   -392       C  
ATOM   1616  CG2 VAL A1016     -27.145 -66.996 -31.268  1.00 64.80           C  
ANISOU 1616  CG2 VAL A1016     9768   7019   7832   1678  -1492   -526       C  
ATOM   1617  N   ILE A1017     -27.831 -71.611 -31.532  1.00 63.18           N  
ANISOU 1617  N   ILE A1017     9206   7309   7489   1158  -1132   -526       N  
ATOM   1618  CA  ILE A1017     -28.073 -72.920 -32.133  1.00 63.39           C  
ANISOU 1618  CA  ILE A1017     9173   7371   7543   1021  -1079   -553       C  
ATOM   1619  C   ILE A1017     -29.391 -73.504 -31.638  1.00 64.27           C  
ANISOU 1619  C   ILE A1017     9088   7745   7586    961  -1134   -627       C  
ATOM   1620  O   ILE A1017     -30.164 -74.045 -32.428  1.00 64.62           O  
ANISOU 1620  O   ILE A1017     9084   7892   7574    932  -1161   -723       O  
ATOM   1621  CB  ILE A1017     -26.898 -73.870 -31.839  1.00 63.44           C  
ANISOU 1621  CB  ILE A1017     9186   7183   7737    865   -982   -457       C  
ATOM   1622  CG1 ILE A1017     -25.653 -73.397 -32.560  1.00 64.49           C  
ANISOU 1622  CG1 ILE A1017     9475   7135   7893    915   -922   -397       C  
ATOM   1623  CG2 ILE A1017     -27.221 -75.305 -32.225  1.00 63.69           C  
ANISOU 1623  CG2 ILE A1017     9131   7195   7874    723   -971   -517       C  
ATOM   1624  CD1 ILE A1017     -24.425 -74.035 -32.066  1.00 65.93           C  
ANISOU 1624  CD1 ILE A1017     9654   7159   8239    814   -838   -300       C  
ATOM   1625  N   GLU A1018     -29.663 -73.376 -30.338  1.00 64.42           N  
ANISOU 1625  N   GLU A1018     8965   7926   7586    939  -1155   -585       N  
ATOM   1626  CA  GLU A1018     -30.889 -73.897 -29.753  1.00 64.92           C  
ANISOU 1626  CA  GLU A1018     8792   8320   7554    860  -1203   -607       C  
ATOM   1627  C   GLU A1018     -32.135 -73.284 -30.398  1.00 65.34           C  
ANISOU 1627  C   GLU A1018     8810   8611   7406   1027  -1292   -772       C  
ATOM   1628  O   GLU A1018     -33.047 -74.021 -30.747  1.00 65.64           O  
ANISOU 1628  O   GLU A1018     8717   8823   7400    919  -1317   -814       O  
ATOM   1629  CB  GLU A1018     -30.872 -73.709 -28.227  1.00 67.40           C  
ANISOU 1629  CB  GLU A1018     8926   8867   7817    842  -1207   -528       C  
ATOM   1630  CG  GLU A1018     -29.813 -74.567 -27.534  1.00 72.82           C  
ANISOU 1630  CG  GLU A1018     9589   9390   8689    650  -1126   -320       C  
ATOM   1631  CD  GLU A1018     -29.479 -74.283 -26.074  1.00 79.17           C  
ANISOU 1631  CD  GLU A1018    10229  10431   9420    655  -1119   -231       C  
ATOM   1632  OE1 GLU A1018     -28.601 -73.426 -25.822  1.00 79.73           O  
ANISOU 1632  OE1 GLU A1018    10412  10394   9487    798  -1119   -304       O  
ATOM   1633  OE2 GLU A1018     -30.065 -74.940 -25.182  1.00 81.43           O  
ANISOU 1633  OE2 GLU A1018    10256  11029   9656    500  -1121    -74       O  
ATOM   1634  N   LYS A1019     -32.140 -71.966 -30.648  1.00 65.39           N  
ANISOU 1634  N   LYS A1019     8938   8587   7321   1284  -1354   -859       N  
ATOM   1635  CA  LYS A1019     -33.286 -71.300 -31.266  1.00 66.23           C  
ANISOU 1635  CA  LYS A1019     9015   8902   7247   1490  -1457   -999       C  
ATOM   1636  C   LYS A1019     -33.201 -71.119 -32.788  1.00 67.21           C  
ANISOU 1636  C   LYS A1019     9303   8887   7346   1553  -1463  -1003       C  
ATOM   1637  O   LYS A1019     -34.059 -70.436 -33.343  1.00 67.30           O  
ANISOU 1637  O   LYS A1019     9291   9076   7203   1741  -1556  -1089       O  
ATOM   1638  CB  LYS A1019     -33.556 -69.943 -30.595  1.00 67.84           C  
ANISOU 1638  CB  LYS A1019     9228   9159   7388   1772  -1567  -1103       C  
ATOM   1639  CG  LYS A1019     -32.366 -68.967 -30.583  1.00 71.48           C  
ANISOU 1639  CG  LYS A1019     9939   9207   8012   1876  -1587  -1039       C  
ATOM   1640  CD  LYS A1019     -32.194 -68.099 -31.870  1.00 75.13           C  
ANISOU 1640  CD  LYS A1019    10600   9467   8478   2047  -1663   -989       C  
ATOM   1641  CE  LYS A1019     -33.299 -67.081 -32.070  1.00 78.28           C  
ANISOU 1641  CE  LYS A1019    10963   9995   8786   2361  -1840  -1130       C  
ATOM   1642  NZ  LYS A1019     -33.379 -66.581 -33.470  1.00 79.91           N  
ANISOU 1642  NZ  LYS A1019    11291  10132   8940   2489  -1904  -1029       N  
ATOM   1643  N   ALA A1020     -32.181 -71.682 -33.461  1.00 67.87           N  
ANISOU 1643  N   ALA A1020     9527   8706   7553   1427  -1372   -913       N  
ATOM   1644  CA  ALA A1020     -32.045 -71.533 -34.917  1.00 68.92           C  
ANISOU 1644  CA  ALA A1020     9776   8800   7612   1491  -1369   -913       C  
ATOM   1645  C   ALA A1020     -33.187 -72.210 -35.665  1.00 69.77           C  
ANISOU 1645  C   ALA A1020     9745   9191   7575   1463  -1407  -1061       C  
ATOM   1646  O   ALA A1020     -33.774 -73.177 -35.167  1.00 69.83           O  
ANISOU 1646  O   ALA A1020     9584   9328   7620   1294  -1406  -1138       O  
ATOM   1647  CB  ALA A1020     -30.706 -72.074 -35.402  1.00 69.20           C  
ANISOU 1647  CB  ALA A1020     9927   8591   7776   1364  -1258   -830       C  
ATOM   1648  N   ASP A1021     -33.501 -71.683 -36.868  1.00 70.16           N  
ANISOU 1648  N   ASP A1021     9847   9356   7456   1615  -1450  -1077       N  
ATOM   1649  CA  ASP A1021     -34.592 -72.159 -37.721  1.00 70.80           C  
ANISOU 1649  CA  ASP A1021     9789   9755   7358   1623  -1501  -1238       C  
ATOM   1650  C   ASP A1021     -34.112 -72.968 -38.942  1.00 71.03           C  
ANISOU 1650  C   ASP A1021     9831   9799   7360   1530  -1444  -1330       C  
ATOM   1651  O   ASP A1021     -34.936 -73.594 -39.606  1.00 71.42           O  
ANISOU 1651  O   ASP A1021     9739  10091   7304   1479  -1486  -1524       O  
ATOM   1652  CB  ASP A1021     -35.485 -70.979 -38.180  1.00 72.49           C  
ANISOU 1652  CB  ASP A1021     9995  10194   7353   1903  -1618  -1214       C  
ATOM   1653  CG  ASP A1021     -36.127 -70.168 -37.063  1.00 77.14           C  
ANISOU 1653  CG  ASP A1021    10535  10829   7946   2063  -1708  -1214       C  
ATOM   1654  OD1 ASP A1021     -36.650 -70.781 -36.104  1.00 77.77           O  
ANISOU 1654  OD1 ASP A1021    10452  11041   8057   1940  -1700  -1310       O  
ATOM   1655  OD2 ASP A1021     -36.123 -68.919 -37.158  1.00 79.39           O  
ANISOU 1655  OD2 ASP A1021    10924  11036   8206   2316  -1802  -1119       O  
ATOM   1656  N   ASN A1022     -32.813 -72.942 -39.259  1.00 70.77           N  
ANISOU 1656  N   ASN A1022     9937   9551   7400   1519  -1360  -1222       N  
ATOM   1657  CA  ASN A1022     -32.288 -73.686 -40.408  1.00 71.30           C  
ANISOU 1657  CA  ASN A1022     9984   9697   7411   1472  -1308  -1354       C  
ATOM   1658  C   ASN A1022     -30.847 -74.151 -40.177  1.00 70.64           C  
ANISOU 1658  C   ASN A1022     9992   9323   7525   1370  -1201  -1298       C  
ATOM   1659  O   ASN A1022     -30.210 -73.698 -39.224  1.00 70.90           O  
ANISOU 1659  O   ASN A1022    10121   9106   7714   1342  -1165  -1113       O  
ATOM   1660  CB  ASN A1022     -32.413 -72.868 -41.707  1.00 73.47           C  
ANISOU 1660  CB  ASN A1022    10265  10272   7380   1665  -1337  -1284       C  
ATOM   1661  CG  ASN A1022     -31.688 -71.551 -41.656  1.00 78.07           C  
ANISOU 1661  CG  ASN A1022    11001  10720   7941   1791  -1330   -944       C  
ATOM   1662  OD1 ASN A1022     -30.454 -71.494 -41.656  1.00 79.77           O  
ANISOU 1662  OD1 ASN A1022    11306  10757   8245   1736  -1244   -806       O  
ATOM   1663  ND2 ASN A1022     -32.446 -70.460 -41.614  1.00 78.89           N  
ANISOU 1663  ND2 ASN A1022    11128  10895   7952   1963  -1438   -802       N  
ATOM   1664  N   ALA A1023     -30.334 -75.044 -41.055  1.00 69.51           N  
ANISOU 1664  N   ALA A1023     9799   9244   7369   1334  -1160  -1491       N  
ATOM   1665  CA  ALA A1023     -28.986 -75.598 -40.972  1.00 68.82           C  
ANISOU 1665  CA  ALA A1023     9762   8937   7448   1273  -1067  -1491       C  
ATOM   1666  C   ALA A1023     -27.894 -74.555 -41.171  1.00 68.20           C  
ANISOU 1666  C   ALA A1023     9797   8853   7264   1363   -989  -1203       C  
ATOM   1667  O   ALA A1023     -26.813 -74.688 -40.588  1.00 68.35           O  
ANISOU 1667  O   ALA A1023     9878   8636   7455   1300   -913  -1103       O  
ATOM   1668  CB  ALA A1023     -28.817 -76.714 -41.987  1.00 68.83           C  
ANISOU 1668  CB  ALA A1023     9652   9076   7426   1272  -1072  -1835       C  
ATOM   1669  N   ALA A1024     -28.152 -73.528 -41.995  1.00 67.26           N  
ANISOU 1669  N   ALA A1024     9688   8995   6871   1498  -1016  -1045       N  
ATOM   1670  CA  ALA A1024     -27.149 -72.488 -42.240  1.00 66.66           C  
ANISOU 1670  CA  ALA A1024     9703   8906   6719   1546   -967   -710       C  
ATOM   1671  C   ALA A1024     -26.892 -71.637 -40.987  1.00 65.77           C  
ANISOU 1671  C   ALA A1024     9730   8426   6832   1504   -990   -470       C  
ATOM   1672  O   ALA A1024     -25.753 -71.241 -40.727  1.00 65.65           O  
ANISOU 1672  O   ALA A1024     9788   8248   6909   1452   -931   -266       O  
ATOM   1673  CB  ALA A1024     -27.566 -71.616 -43.412  1.00 66.75           C  
ANISOU 1673  CB  ALA A1024     9674   9279   6409   1686  -1018   -543       C  
ATOM   1674  N   GLN A1025     -27.941 -71.397 -40.193  1.00 64.91           N  
ANISOU 1674  N   GLN A1025     9632   8230   6801   1530  -1080   -525       N  
ATOM   1675  CA  GLN A1025     -27.814 -70.656 -38.952  1.00 64.59           C  
ANISOU 1675  CA  GLN A1025     9683   7904   6953   1522  -1121   -393       C  
ATOM   1676  C   GLN A1025     -27.033 -71.461 -37.932  1.00 64.36           C  
ANISOU 1676  C   GLN A1025     9648   7660   7146   1368  -1037   -455       C  
ATOM   1677  O   GLN A1025     -26.179 -70.909 -37.248  1.00 64.49           O  
ANISOU 1677  O   GLN A1025     9743   7464   7295   1332  -1017   -301       O  
ATOM   1678  CB  GLN A1025     -29.189 -70.302 -38.405  1.00 65.84           C  
ANISOU 1678  CB  GLN A1025     9797   8134   7086   1619  -1239   -491       C  
ATOM   1679  CG  GLN A1025     -29.871 -69.254 -39.251  1.00 69.30           C  
ANISOU 1679  CG  GLN A1025    10257   8731   7342   1810  -1347   -377       C  
ATOM   1680  CD  GLN A1025     -31.248 -68.897 -38.778  1.00 74.58           C  
ANISOU 1680  CD  GLN A1025    10864   9497   7975   1948  -1473   -492       C  
ATOM   1681  OE1 GLN A1025     -31.821 -69.529 -37.879  1.00 77.11           O  
ANISOU 1681  OE1 GLN A1025    11084   9865   8350   1881  -1469   -680       O  
ATOM   1682  NE2 GLN A1025     -31.819 -67.873 -39.391  1.00 74.79           N  
ANISOU 1682  NE2 GLN A1025    10928   9585   7903   2151  -1596   -361       N  
ATOM   1683  N   VAL A1026     -27.301 -72.769 -37.838  1.00 64.00           N  
ANISOU 1683  N   VAL A1026     9503   7655   7161   1270  -1003   -666       N  
ATOM   1684  CA  VAL A1026     -26.572 -73.644 -36.925  1.00 64.11           C  
ANISOU 1684  CA  VAL A1026     9496   7457   7404   1129   -938   -686       C  
ATOM   1685  C   VAL A1026     -25.092 -73.699 -37.331  1.00 64.25           C  
ANISOU 1685  C   VAL A1026     9568   7385   7458   1112   -838   -595       C  
ATOM   1686  O   VAL A1026     -24.218 -73.579 -36.469  1.00 64.23           O  
ANISOU 1686  O   VAL A1026     9603   7196   7605   1049   -793   -471       O  
ATOM   1687  CB  VAL A1026     -27.200 -75.052 -36.882  1.00 64.59           C  
ANISOU 1687  CB  VAL A1026     9435   7537   7569   1020   -958   -902       C  
ATOM   1688  CG1 VAL A1026     -26.365 -75.996 -36.026  1.00 65.22           C  
ANISOU 1688  CG1 VAL A1026     9494   7371   7918    884   -906   -873       C  
ATOM   1689  CG2 VAL A1026     -28.640 -74.996 -36.382  1.00 64.78           C  
ANISOU 1689  CG2 VAL A1026     9366   7701   7546   1002  -1051   -954       C  
ATOM   1690  N   LYS A1027     -24.816 -73.822 -38.652  1.00 64.04           N  
ANISOU 1690  N   LYS A1027     9519   7557   7256   1179   -804   -655       N  
ATOM   1691  CA  LYS A1027     -23.446 -73.863 -39.167  1.00 64.02           C  
ANISOU 1691  CA  LYS A1027     9520   7582   7224   1180   -706   -574       C  
ATOM   1692  C   LYS A1027     -22.696 -72.584 -38.820  1.00 64.35           C  
ANISOU 1692  C   LYS A1027     9659   7525   7267   1164   -693   -250       C  
ATOM   1693  O   LYS A1027     -21.574 -72.646 -38.326  1.00 64.54           O  
ANISOU 1693  O   LYS A1027     9696   7416   7411   1094   -624   -154       O  
ATOM   1694  CB  LYS A1027     -23.428 -74.087 -40.683  1.00 64.97           C  
ANISOU 1694  CB  LYS A1027     9549   8056   7080   1276   -682   -701       C  
ATOM   1695  CG  LYS A1027     -22.016 -74.140 -41.254  1.00 68.21           C  
ANISOU 1695  CG  LYS A1027     9921   8614   7383   1292   -578   -580       C  
ATOM   1696  CD  LYS A1027     -22.029 -73.980 -42.760  1.00 72.25           C  
ANISOU 1696  CD  LYS A1027    10280   9538   7634   1400   -548   -811       C  
ATOM   1697  CE  LYS A1027     -20.671 -73.959 -43.404  1.00 75.16           C  
ANISOU 1697  CE  LYS A1027    10574  10260   7725   1434   -467   -562       C  
ATOM   1698  NZ  LYS A1027     -20.792 -74.144 -44.875  1.00 76.60           N  
ANISOU 1698  NZ  LYS A1027    10583  10984   7536   1564   -467   -728       N  
ATOM   1699  N   ASP A1028     -23.323 -71.429 -39.044  1.00 64.32           N  
ANISOU 1699  N   ASP A1028     9717   7564   7159   1227   -778    -87       N  
ATOM   1700  CA  ASP A1028     -22.708 -70.150 -38.746  1.00 64.73           C  
ANISOU 1700  CA  ASP A1028     9865   7454   7275   1203   -813    211       C  
ATOM   1701  C   ASP A1028     -22.299 -70.021 -37.283  1.00 64.65           C  
ANISOU 1701  C   ASP A1028     9905   7145   7517   1123   -822    213       C  
ATOM   1702  O   ASP A1028     -21.176 -69.604 -37.012  1.00 64.97           O  
ANISOU 1702  O   ASP A1028     9973   7065   7647   1039   -784    379       O  
ATOM   1703  CB  ASP A1028     -23.649 -69.013 -39.131  1.00 67.05           C  
ANISOU 1703  CB  ASP A1028    10218   7771   7485   1314   -948    351       C  
ATOM   1704  CG  ASP A1028     -22.977 -67.670 -39.035  1.00 72.77           C  
ANISOU 1704  CG  ASP A1028    11046   8273   8331   1281  -1024    672       C  
ATOM   1705  OD1 ASP A1028     -22.317 -67.270 -40.018  1.00 74.08           O  
ANISOU 1705  OD1 ASP A1028    11199   8573   8373   1255  -1013    950       O  
ATOM   1706  OD2 ASP A1028     -23.095 -67.019 -37.967  1.00 74.97           O  
ANISOU 1706  OD2 ASP A1028    11397   8258   8831   1275  -1106    645       O  
ATOM   1707  N   ALA A1029     -23.188 -70.385 -36.344  1.00 64.19           N  
ANISOU 1707  N   ALA A1029     9825   7020   7545   1142   -873     35       N  
ATOM   1708  CA  ALA A1029     -22.874 -70.276 -34.923  1.00 64.29           C  
ANISOU 1708  CA  ALA A1029     9839   6848   7740   1082   -886     27       C  
ATOM   1709  C   ALA A1029     -21.787 -71.267 -34.500  1.00 64.35           C  
ANISOU 1709  C   ALA A1029     9792   6806   7854    966   -767     23       C  
ATOM   1710  O   ALA A1029     -20.932 -70.914 -33.692  1.00 64.36           O  
ANISOU 1710  O   ALA A1029     9805   6681   7968    904   -752    117       O  
ATOM   1711  CB  ALA A1029     -24.129 -70.457 -34.082  1.00 64.23           C  
ANISOU 1711  CB  ALA A1029     9766   6899   7739   1130   -962   -136       C  
ATOM   1712  N   LEU A1030     -21.787 -72.485 -35.078  1.00 64.17           N  
ANISOU 1712  N   LEU A1030     9701   6874   7805    951   -698   -102       N  
ATOM   1713  CA  LEU A1030     -20.775 -73.503 -34.769  1.00 64.32           C  
ANISOU 1713  CA  LEU A1030     9662   6824   7952    882   -606   -124       C  
ATOM   1714  C   LEU A1030     -19.395 -73.070 -35.210  1.00 64.49           C  
ANISOU 1714  C   LEU A1030     9701   6870   7933    868   -528     20       C  
ATOM   1715  O   LEU A1030     -18.426 -73.342 -34.511  1.00 64.30           O  
ANISOU 1715  O   LEU A1030     9642   6760   8029    811   -472     77       O  
ATOM   1716  CB  LEU A1030     -21.115 -74.842 -35.425  1.00 64.38           C  
ANISOU 1716  CB  LEU A1030     9596   6886   7981    899   -591   -337       C  
ATOM   1717  CG  LEU A1030     -22.223 -75.620 -34.761  1.00 65.74           C  
ANISOU 1717  CG  LEU A1030     9707   6996   8274    843   -660   -445       C  
ATOM   1718  CD1 LEU A1030     -22.753 -76.684 -35.677  1.00 66.17           C  
ANISOU 1718  CD1 LEU A1030     9701   7100   8341    861   -689   -688       C  
ATOM   1719  CD2 LEU A1030     -21.753 -76.216 -33.462  1.00 66.35           C  
ANISOU 1719  CD2 LEU A1030     9731   6909   8570    746   -646   -347       C  
ATOM   1720  N   THR A1031     -19.305 -72.388 -36.357  1.00 64.82           N  
ANISOU 1720  N   THR A1031     9770   7067   7792    911   -526    110       N  
ATOM   1721  CA  THR A1031     -18.043 -71.885 -36.884  1.00 65.87           C  
ANISOU 1721  CA  THR A1031     9884   7293   7850    869   -456    303       C  
ATOM   1722  C   THR A1031     -17.454 -70.858 -35.919  1.00 66.85           C  
ANISOU 1722  C   THR A1031    10071   7210   8120    768   -496    503       C  
ATOM   1723  O   THR A1031     -16.263 -70.920 -35.602  1.00 67.16           O  
ANISOU 1723  O   THR A1031    10062   7237   8221    690   -427    589       O  
ATOM   1724  CB  THR A1031     -18.236 -71.375 -38.326  1.00 67.17           C  
ANISOU 1724  CB  THR A1031    10031   7730   7761    922   -460    411       C  
ATOM   1725  OG1 THR A1031     -18.117 -72.481 -39.228  1.00 68.08           O  
ANISOU 1725  OG1 THR A1031    10027   8114   7725   1008   -387    188       O  
ATOM   1726  CG2 THR A1031     -17.242 -70.275 -38.717  1.00 67.57           C  
ANISOU 1726  CG2 THR A1031    10076   7848   7750    826   -439    752       C  
ATOM   1727  N   LYS A1032     -18.300 -69.951 -35.412  1.00 67.18           N  
ANISOU 1727  N   LYS A1032    10204   7099   8225    786   -620    535       N  
ATOM   1728  CA  LYS A1032     -17.862 -68.932 -34.463  1.00 67.86           C  
ANISOU 1728  CA  LYS A1032    10343   6968   8474    712   -698    647       C  
ATOM   1729  C   LYS A1032     -17.503 -69.547 -33.090  1.00 68.65           C  
ANISOU 1729  C   LYS A1032    10379   6997   8708    669   -663    526       C  
ATOM   1730  O   LYS A1032     -16.608 -69.043 -32.411  1.00 68.86           O  
ANISOU 1730  O   LYS A1032    10393   6931   8841    578   -671    609       O  
ATOM   1731  CB  LYS A1032     -18.918 -67.828 -34.331  1.00 69.04           C  
ANISOU 1731  CB  LYS A1032    10587   6977   8667    795   -866    650       C  
ATOM   1732  CG  LYS A1032     -19.115 -66.986 -35.583  1.00 71.84           C  
ANISOU 1732  CG  LYS A1032    10999   7379   8918    826   -923    864       C  
ATOM   1733  CD  LYS A1032     -20.305 -66.060 -35.398  1.00 75.81           C  
ANISOU 1733  CD  LYS A1032    11591   7727   9488    957  -1108    832       C  
ATOM   1734  CE  LYS A1032     -20.460 -65.041 -36.500  1.00 79.97           C  
ANISOU 1734  CE  LYS A1032    12180   8225   9980    974  -1205   1132       C  
ATOM   1735  NZ  LYS A1032     -21.719 -64.254 -36.353  1.00 82.50           N  
ANISOU 1735  NZ  LYS A1032    12594   8316  10436   1128  -1421   1101       N  
ATOM   1736  N   MET A1033     -18.178 -70.643 -32.699  1.00 68.78           N  
ANISOU 1736  N   MET A1033    10336   7077   8721    716   -631    356       N  
ATOM   1737  CA  MET A1033     -17.877 -71.350 -31.450  1.00 69.27           C  
ANISOU 1737  CA  MET A1033    10308   7119   8892    671   -599    306       C  
ATOM   1738  C   MET A1033     -16.553 -72.096 -31.555  1.00 69.73           C  
ANISOU 1738  C   MET A1033    10300   7204   8990    618   -482    373       C  
ATOM   1739  O   MET A1033     -15.795 -72.157 -30.587  1.00 70.01           O  
ANISOU 1739  O   MET A1033    10271   7220   9111    561   -461    427       O  
ATOM   1740  CB  MET A1033     -18.966 -72.375 -31.138  1.00 69.88           C  
ANISOU 1740  CB  MET A1033    10322   7253   8975    704   -611    176       C  
ATOM   1741  CG  MET A1033     -20.196 -71.776 -30.586  1.00 72.12           C  
ANISOU 1741  CG  MET A1033    10603   7581   9216    757   -720     96       C  
ATOM   1742  SD  MET A1033     -21.439 -73.026 -30.218  1.00 76.17           S  
ANISOU 1742  SD  MET A1033    10999   8215   9727    741   -731     -2       S  
ATOM   1743  CE  MET A1033     -20.610 -73.924 -28.911  1.00 73.13           C  
ANISOU 1743  CE  MET A1033    10476   7829   9483    632   -675    115       C  
ATOM   1744  N   ARG A1034     -16.291 -72.691 -32.721  1.00 69.67           N  
ANISOU 1744  N   ARG A1034    10283   7284   8905    659   -411    344       N  
ATOM   1745  CA  ARG A1034     -15.087 -73.464 -32.968  1.00 70.12           C  
ANISOU 1745  CA  ARG A1034    10252   7406   8983    660   -308    355       C  
ATOM   1746  C   ARG A1034     -13.871 -72.555 -32.933  1.00 70.32           C  
ANISOU 1746  C   ARG A1034    10260   7484   8974    574   -271    540       C  
ATOM   1747  O   ARG A1034     -12.871 -72.903 -32.311  1.00 70.37           O  
ANISOU 1747  O   ARG A1034    10181   7504   9053    541   -216    584       O  
ATOM   1748  CB  ARG A1034     -15.200 -74.173 -34.319  1.00 71.35           C  
ANISOU 1748  CB  ARG A1034    10378   7704   9029    758   -264    213       C  
ATOM   1749  CG  ARG A1034     -14.224 -75.299 -34.499  1.00 74.05           C  
ANISOU 1749  CG  ARG A1034    10608   8095   9432    824   -187    116       C  
ATOM   1750  CD  ARG A1034     -14.323 -75.849 -35.901  1.00 77.07           C  
ANISOU 1750  CD  ARG A1034    10935   8682   9666    947   -158    -81       C  
ATOM   1751  NE  ARG A1034     -13.246 -76.799 -36.163  1.00 79.82           N  
ANISOU 1751  NE  ARG A1034    11156   9116  10058   1051    -92   -207       N  
ATOM   1752  CZ  ARG A1034     -12.049 -76.462 -36.632  1.00 81.96           C  
ANISOU 1752  CZ  ARG A1034    11325   9649  10168   1067     -1   -112       C  
ATOM   1753  NH1 ARG A1034     -11.772 -75.193 -36.920  1.00 81.60           N  
ANISOU 1753  NH1 ARG A1034    11297   9774   9932    949     28    147       N  
ATOM   1754  NH2 ARG A1034     -11.122 -77.390 -36.826  1.00 81.81           N  
ANISOU 1754  NH2 ARG A1034    11169   9723  10191   1200     47   -267       N  
ATOM   1755  N   ALA A1035     -13.967 -71.376 -33.559  1.00 70.24           N  
ANISOU 1755  N   ALA A1035    10320   7496   8873    526   -316    673       N  
ATOM   1756  CA  ALA A1035     -12.867 -70.424 -33.550  1.00 70.70           C  
ANISOU 1756  CA  ALA A1035    10354   7577   8933    397   -308    889       C  
ATOM   1757  C   ALA A1035     -12.614 -69.897 -32.141  1.00 70.99           C  
ANISOU 1757  C   ALA A1035    10396   7433   9142    311   -377    897       C  
ATOM   1758  O   ALA A1035     -11.471 -69.627 -31.813  1.00 71.21           O  
ANISOU 1758  O   ALA A1035    10347   7504   9207    204   -342   1006       O  
ATOM   1759  CB  ALA A1035     -13.149 -69.279 -34.505  1.00 71.00           C  
ANISOU 1759  CB  ALA A1035    10464   7627   8884    349   -377   1078       C  
ATOM   1760  N   ALA A1036     -13.658 -69.774 -31.302  1.00 70.86           N  
ANISOU 1760  N   ALA A1036    10440   7278   9206    363   -475    764       N  
ATOM   1761  CA  ALA A1036     -13.510 -69.315 -29.921  1.00 71.40           C  
ANISOU 1761  CA  ALA A1036    10475   7259   9395    314   -549    713       C  
ATOM   1762  C   ALA A1036     -12.897 -70.391 -29.041  1.00 71.98           C  
ANISOU 1762  C   ALA A1036    10413   7447   9491    316   -461    679       C  
ATOM   1763  O   ALA A1036     -12.129 -70.067 -28.139  1.00 72.10           O  
ANISOU 1763  O   ALA A1036    10348   7484   9562    243   -479    699       O  
ATOM   1764  CB  ALA A1036     -14.851 -68.903 -29.356  1.00 71.56           C  
ANISOU 1764  CB  ALA A1036    10553   7195   9442    402   -678    558       C  
ATOM   1765  N   ALA A1037     -13.217 -71.663 -29.294  1.00 72.26           N  
ANISOU 1765  N   ALA A1037    10412   7544   9501    399   -385    630       N  
ATOM   1766  CA  ALA A1037     -12.648 -72.760 -28.520  1.00 73.15           C  
ANISOU 1766  CA  ALA A1037    10396   7721   9676    414   -322    645       C  
ATOM   1767  C   ALA A1037     -11.144 -72.845 -28.765  1.00 74.26           C  
ANISOU 1767  C   ALA A1037    10455   7950   9809    375   -233    744       C  
ATOM   1768  O   ALA A1037     -10.378 -72.953 -27.813  1.00 74.46           O  
ANISOU 1768  O   ALA A1037    10370   8043   9878    336   -222    801       O  
ATOM   1769  CB  ALA A1037     -13.326 -74.069 -28.883  1.00 73.23           C  
ANISOU 1769  CB  ALA A1037    10398   7699   9728    501   -297    573       C  
ATOM   1770  N   LEU A1038     -10.712 -72.728 -30.026  1.00 75.02           N  
ANISOU 1770  N   LEU A1038    10576   8110   9818    384   -175    773       N  
ATOM   1771  CA  LEU A1038      -9.286 -72.735 -30.353  1.00 76.19           C  
ANISOU 1771  CA  LEU A1038    10610   8423   9916    346    -86    872       C  
ATOM   1772  C   LEU A1038      -8.585 -71.490 -29.821  1.00 77.44           C  
ANISOU 1772  C   LEU A1038    10746   8589  10090    171   -130   1008       C  
ATOM   1773  O   LEU A1038      -7.409 -71.561 -29.476  1.00 77.44           O  
ANISOU 1773  O   LEU A1038    10611   8726  10087    117    -77   1083       O  
ATOM   1774  CB  LEU A1038      -9.062 -72.826 -31.866  1.00 76.34           C  
ANISOU 1774  CB  LEU A1038    10617   8607   9780    397    -16    874       C  
ATOM   1775  CG  LEU A1038      -9.742 -73.955 -32.604  1.00 77.70           C  
ANISOU 1775  CG  LEU A1038    10804   8784   9936    571      5    678       C  
ATOM   1776  CD1 LEU A1038      -9.358 -73.936 -34.059  1.00 78.27           C  
ANISOU 1776  CD1 LEU A1038    10814   9127   9797    629     73    658       C  
ATOM   1777  CD2 LEU A1038      -9.390 -75.287 -32.001  1.00 78.51           C  
ANISOU 1777  CD2 LEU A1038    10816   8824  10189    689     28    568       C  
ATOM   1778  N   ASP A1039      -9.292 -70.356 -29.758  1.00 78.37           N  
ANISOU 1778  N   ASP A1039    10984   8546  10245     90   -245   1023       N  
ATOM   1779  CA  ASP A1039      -8.740 -69.117 -29.226  1.00 79.92           C  
ANISOU 1779  CA  ASP A1039    11175   8663  10528    -82   -339   1107       C  
ATOM   1780  C   ASP A1039      -8.449 -69.260 -27.738  1.00 80.79           C  
ANISOU 1780  C   ASP A1039    11186   8796  10714    -91   -375   1004       C  
ATOM   1781  O   ASP A1039      -7.448 -68.730 -27.260  1.00 80.94           O  
ANISOU 1781  O   ASP A1039    11111   8860  10781   -229   -401   1057       O  
ATOM   1782  CB  ASP A1039      -9.690 -67.934 -29.479  1.00 82.28           C  
ANISOU 1782  CB  ASP A1039    11636   8725  10904   -114   -492   1102       C  
ATOM   1783  CG  ASP A1039      -9.624 -67.371 -30.890  1.00 87.80           C  
ANISOU 1783  CG  ASP A1039    12401   9426  11533   -170   -488   1304       C  
ATOM   1784  OD1 ASP A1039      -8.638 -67.674 -31.609  1.00 88.65           O  
ANISOU 1784  OD1 ASP A1039    12405   9776  11503   -205   -359   1445       O  
ATOM   1785  OD2 ASP A1039     -10.566 -66.638 -31.282  1.00 90.09           O  
ANISOU 1785  OD2 ASP A1039    12827   9514  11890   -160   -620   1326       O  
ATOM   1786  N   ALA A1040      -9.315 -69.969 -27.001  1.00 81.15           N  
ANISOU 1786  N   ALA A1040    11226   8847  10760     39   -385    871       N  
ATOM   1787  CA  ALA A1040      -9.087 -70.203 -25.581  1.00 82.07           C  
ANISOU 1787  CA  ALA A1040    11206   9080  10895     44   -412    807       C  
ATOM   1788  C   ALA A1040      -8.024 -71.288 -25.336  1.00 83.37           C  
ANISOU 1788  C   ALA A1040    11210   9430  11035     74   -291    911       C  
ATOM   1789  O   ALA A1040      -7.446 -71.336 -24.255  1.00 83.54           O  
ANISOU 1789  O   ALA A1040    11082   9606  11052     52   -305    916       O  
ATOM   1790  CB  ALA A1040     -10.389 -70.560 -24.887  1.00 82.03           C  
ANISOU 1790  CB  ALA A1040    11213   9081  10872    152   -471    685       C  
ATOM   1791  N   GLN A1041      -7.748 -72.142 -26.334  1.00 84.28           N  
ANISOU 1791  N   GLN A1041    11338   9557  11128    147   -185    975       N  
ATOM   1792  CA  GLN A1041      -6.739 -73.199 -26.243  1.00 85.81           C  
ANISOU 1792  CA  GLN A1041    11383   9896  11324    224    -87   1045       C  
ATOM   1793  C   GLN A1041      -5.318 -72.647 -26.433  1.00 86.65           C  
ANISOU 1793  C   GLN A1041    11371  10179  11372    115    -38   1136       C  
ATOM   1794  O   GLN A1041      -4.371 -73.156 -25.836  1.00 86.54           O  
ANISOU 1794  O   GLN A1041    11188  10337  11356    145      6   1191       O  
ATOM   1795  CB  GLN A1041      -7.029 -74.291 -27.286  1.00 88.16           C  
ANISOU 1795  CB  GLN A1041    11727  10134  11635    377    -23    997       C  
ATOM   1796  CG  GLN A1041      -6.232 -75.577 -27.090  1.00 92.89           C  
ANISOU 1796  CG  GLN A1041    12189  10786  12318    525     28   1020       C  
ATOM   1797  CD  GLN A1041      -6.624 -76.661 -28.076  1.00 98.46           C  
ANISOU 1797  CD  GLN A1041    12941  11378  13090    693     49    895       C  
ATOM   1798  OE1 GLN A1041      -7.146 -76.398 -29.166  1.00100.16           O  
ANISOU 1798  OE1 GLN A1041    13261  11568  13228    700     57    789       O  
ATOM   1799  NE2 GLN A1041      -6.379 -77.912 -27.717  1.00 99.35           N  
ANISOU 1799  NE2 GLN A1041    12964  11419  13364    840     41    896       N  
ATOM   1800  N   LYS A1042      -5.173 -71.612 -27.269  1.00 87.43           N  
ANISOU 1800  N   LYS A1042    11540  10252  11426    -21    -53   1183       N  
ATOM   1801  CA  LYS A1042      -3.884 -70.977 -27.544  1.00 88.70           C  
ANISOU 1801  CA  LYS A1042    11575  10592  11536   -182    -20   1313       C  
ATOM   1802  C   LYS A1042      -3.380 -70.127 -26.366  1.00 90.11           C  
ANISOU 1802  C   LYS A1042    11674  10772  11791   -352   -119   1307       C  
ATOM   1803  O   LYS A1042      -2.174 -69.935 -26.215  1.00 90.25           O  
ANISOU 1803  O   LYS A1042    11533  10977  11781   -487    -94   1403       O  
ATOM   1804  CB  LYS A1042      -3.974 -70.112 -28.811  1.00 90.27           C  
ANISOU 1804  CB  LYS A1042    11862  10759  11679   -306    -29   1430       C  
ATOM   1805  CG  LYS A1042      -4.204 -70.907 -30.087  1.00 94.07           C  
ANISOU 1805  CG  LYS A1042    12364  11353  12025   -144     72   1414       C  
ATOM   1806  CD  LYS A1042      -4.428 -69.995 -31.287  1.00 98.55           C  
ANISOU 1806  CD  LYS A1042    13019  11912  12514   -262     43   1562       C  
ATOM   1807  CE  LYS A1042      -5.785 -69.324 -31.277  1.00102.21           C  
ANISOU 1807  CE  LYS A1042    13702  12040  13095   -275    -94   1512       C  
ATOM   1808  NZ  LYS A1042      -5.723 -67.895 -30.853  1.00104.23           N  
ANISOU 1808  NZ  LYS A1042    14012  12097  13494   -508   -236   1655       N  
ATOM   1809  N   ALA A1043      -4.298 -69.586 -25.558  1.00 90.98           N  
ANISOU 1809  N   ALA A1043    11872  10711  11985   -346   -241   1171       N  
ATOM   1810  CA  ALA A1043      -3.930 -68.758 -24.418  1.00 92.26           C  
ANISOU 1810  CA  ALA A1043    11946  10894  12214   -476   -360   1082       C  
ATOM   1811  C   ALA A1043      -3.424 -69.649 -23.298  1.00 93.49           C  
ANISOU 1811  C   ALA A1043    11901  11321  12300   -382   -311   1060       C  
ATOM   1812  O   ALA A1043      -4.211 -70.387 -22.705  1.00 93.68           O  
ANISOU 1812  O   ALA A1043    11925  11372  12297   -228   -311   1005       O  
ATOM   1813  CB  ALA A1043      -5.133 -67.960 -23.943  1.00 92.44           C  
ANISOU 1813  CB  ALA A1043    12110  10688  12325   -456   -518    896       C  
ATOM   1814  N   THR A1044      -2.108 -69.598 -23.030  1.00 94.13           N  
ANISOU 1814  N   THR A1044    11789  11628  12346   -484   -275   1136       N  
ATOM   1815  CA  THR A1044      -1.458 -70.398 -21.992  1.00 95.15           C  
ANISOU 1815  CA  THR A1044    11696  12059  12397   -394   -233   1156       C  
ATOM   1816  C   THR A1044      -1.919 -69.979 -20.592  1.00 96.49           C  
ANISOU 1816  C   THR A1044    11784  12328  12551   -397   -359    989       C  
ATOM   1817  O   THR A1044      -1.844 -68.804 -20.236  1.00 96.84           O  
ANISOU 1817  O   THR A1044    11821  12320  12653   -554   -491    827       O  
ATOM   1818  CB  THR A1044       0.060 -70.313 -22.156  1.00 95.97           C  
ANISOU 1818  CB  THR A1044    11602  12414  12449   -505   -169   1269       C  
ATOM   1819  OG1 THR A1044       0.397 -70.726 -23.480  1.00 96.73           O  
ANISOU 1819  OG1 THR A1044    11742  12502  12511   -453    -47   1396       O  
ATOM   1820  CG2 THR A1044       0.809 -71.155 -21.139  1.00 96.30           C  
ANISOU 1820  CG2 THR A1044    11393  12794  12402   -394   -131   1312       C  
ATOM   1821  N   PRO A1045      -2.416 -70.931 -19.785  1.00 97.04           N  
ANISOU 1821  N   PRO A1045    11770  12555  12547   -223   -333   1024       N  
ATOM   1822  CA  PRO A1045      -2.873 -70.589 -18.424  1.00 97.64           C  
ANISOU 1822  CA  PRO A1045    11709  12851  12537   -206   -442    876       C  
ATOM   1823  C   PRO A1045      -1.721 -70.158 -17.480  1.00 98.69           C  
ANISOU 1823  C   PRO A1045    11573  13340  12584   -297   -484    824       C  
ATOM   1824  O   PRO A1045      -0.586 -70.051 -17.951  1.00 98.94           O  
ANISOU 1824  O   PRO A1045    11540  13412  12640   -393   -429    916       O  
ATOM   1825  CB  PRO A1045      -3.556 -71.893 -17.988  1.00 98.11           C  
ANISOU 1825  CB  PRO A1045    11727  13012  12541    -21   -382   1043       C  
ATOM   1826  CG  PRO A1045      -2.790 -72.949 -18.689  1.00 98.38           C  
ANISOU 1826  CG  PRO A1045    11752  12993  12634     57   -255   1269       C  
ATOM   1827  CD  PRO A1045      -2.561 -72.374 -20.053  1.00 96.64           C  
ANISOU 1827  CD  PRO A1045    11717  12505  12497    -36   -220   1210       C  
ATOM   1828  N   PRO A1046      -1.940 -69.882 -16.164  1.00 99.20           N  
ANISOU 1828  N   PRO A1046    11444  13726  12519   -270   -584    666       N  
ATOM   1829  CA  PRO A1046      -0.805 -69.504 -15.296  1.00 99.66           C  
ANISOU 1829  CA  PRO A1046    11222  14167  12476   -354   -630    594       C  
ATOM   1830  C   PRO A1046       0.096 -70.684 -14.897  1.00100.25           C  
ANISOU 1830  C   PRO A1046    11070  14593  12427   -246   -510    893       C  
ATOM   1831  O   PRO A1046       0.505 -70.782 -13.742  1.00100.31           O  
ANISOU 1831  O   PRO A1046    10794  15059  12261   -217   -551    875       O  
ATOM   1832  CB  PRO A1046      -1.492 -68.898 -14.074  1.00100.34           C  
ANISOU 1832  CB  PRO A1046    11162  14534  12427   -311   -776    303       C  
ATOM   1833  CG  PRO A1046      -2.785 -69.634 -13.987  1.00100.65           C  
ANISOU 1833  CG  PRO A1046    11284  14556  12401   -140   -731    423       C  
ATOM   1834  CD  PRO A1046      -3.209 -69.896 -15.408  1.00 98.86           C  
ANISOU 1834  CD  PRO A1046    11391  13788  12382   -160   -662    528       C  
ATOM   1835  N   LYS A1047       0.390 -71.586 -15.851  1.00100.53           N  
ANISOU 1835  N   LYS A1047    11213  14433  12550   -164   -376   1151       N  
ATOM   1836  CA  LYS A1047       1.237 -72.767 -15.703  1.00101.22           C  
ANISOU 1836  CA  LYS A1047    11116  14758  12587    -22   -279   1430       C  
ATOM   1837  C   LYS A1047       2.144 -72.896 -16.949  1.00101.46           C  
ANISOU 1837  C   LYS A1047    11225  14607  12718    -42   -176   1510       C  
ATOM   1838  O   LYS A1047       1.677 -72.730 -18.076  1.00101.49           O  
ANISOU 1838  O   LYS A1047    11467  14255  12839    -17   -127   1515       O  
ATOM   1839  CB  LYS A1047       0.371 -74.032 -15.536  1.00103.36           C  
ANISOU 1839  CB  LYS A1047    11416  14973  12882    180   -247   1665       C  
ATOM   1840  CG  LYS A1047      -0.620 -73.961 -14.370  1.00107.85           C  
ANISOU 1840  CG  LYS A1047    11858  15819  13300    201   -336   1642       C  
ATOM   1841  CD  LYS A1047      -1.225 -75.323 -14.034  1.00112.52           C  
ANISOU 1841  CD  LYS A1047    12426  16393  13932    357   -311   1975       C  
ATOM   1842  CE  LYS A1047      -2.167 -75.281 -12.848  1.00116.11           C  
ANISOU 1842  CE  LYS A1047    12681  17255  14182    368   -386   2026       C  
ATOM   1843  NZ  LYS A1047      -2.598 -76.648 -12.433  1.00118.21           N  
ANISOU 1843  NZ  LYS A1047    12888  17510  14517    475   -373   2444       N  
ATOM   1844  N   LEU A1048       3.441 -73.176 -16.744  1.00101.47           N  
ANISOU 1844  N   LEU A1048    10995  14915  12642    -87   -146   1558       N  
ATOM   1845  CA  LEU A1048       4.412 -73.319 -17.837  1.00101.74           C  
ANISOU 1845  CA  LEU A1048    11023  14923  12711   -102    -46   1632       C  
ATOM   1846  C   LEU A1048       4.973 -74.745 -17.920  1.00101.83           C  
ANISOU 1846  C   LEU A1048    10879  15102  12709    173     44   1845       C  
ATOM   1847  O   LEU A1048       6.127 -74.933 -18.302  1.00101.79           O  
ANISOU 1847  O   LEU A1048    10728  15288  12658    195    115   1891       O  
ATOM   1848  CB  LEU A1048       5.562 -72.313 -17.664  1.00101.86           C  
ANISOU 1848  CB  LEU A1048    10868  15174  12662   -369    -85   1533       C  
ATOM   1849  CG  LEU A1048       5.534 -71.092 -18.577  1.00103.08           C  
ANISOU 1849  CG  LEU A1048    11206  15039  12922   -635   -117   1436       C  
ATOM   1850  CD1 LEU A1048       4.253 -70.286 -18.398  1.00103.52           C  
ANISOU 1850  CD1 LEU A1048    11517  14726  13090   -698   -231   1264       C  
ATOM   1851  CD2 LEU A1048       6.741 -70.218 -18.333  1.00103.60           C  
ANISOU 1851  CD2 LEU A1048    11061  15341  12961   -926   -177   1384       C  
ATOM   1852  N   PRO A1053       5.843 -76.846 -21.670  1.00 94.46           N  
ANISOU 1852  N   PRO A1053    10193  13710  11989    738    333   1856       N  
ATOM   1853  CA  PRO A1053       6.118 -77.545 -22.934  1.00 94.70           C  
ANISOU 1853  CA  PRO A1053    10226  13715  12040    966    409   1776       C  
ATOM   1854  C   PRO A1053       5.032 -78.595 -23.232  1.00 95.16           C  
ANISOU 1854  C   PRO A1053    10487  13346  12323   1209    364   1726       C  
ATOM   1855  O   PRO A1053       3.934 -78.229 -23.652  1.00 94.97           O  
ANISOU 1855  O   PRO A1053    10707  13026  12352   1102    343   1654       O  
ATOM   1856  CB  PRO A1053       7.542 -78.103 -22.727  1.00 95.18           C  
ANISOU 1856  CB  PRO A1053     9958  14196  12009   1140    451   1835       C  
ATOM   1857  CG  PRO A1053       7.680 -78.245 -21.261  1.00 95.49           C  
ANISOU 1857  CG  PRO A1053     9871  14348  12061   1111    377   1988       C  
ATOM   1858  CD  PRO A1053       6.828 -77.180 -20.624  1.00 93.86           C  
ANISOU 1858  CD  PRO A1053     9823  14009  11831    786    318   1972       C  
ATOM   1859  N   ASP A1054       5.330 -79.887 -23.028  1.00 95.53           N  
ANISOU 1859  N   ASP A1054    10429  13345  12524   1533    334   1764       N  
ATOM   1860  CA  ASP A1054       4.406 -80.997 -23.165  1.00 96.27           C  
ANISOU 1860  CA  ASP A1054    10675  13001  12901   1757    253   1748       C  
ATOM   1861  C   ASP A1054       4.537 -81.783 -21.876  1.00 96.31           C  
ANISOU 1861  C   ASP A1054    10550  12998  13046   1863    164   2011       C  
ATOM   1862  O   ASP A1054       4.969 -82.934 -21.865  1.00 96.29           O  
ANISOU 1862  O   ASP A1054    10442  12903  13243   2166    107   2065       O  
ATOM   1863  CB  ASP A1054       4.721 -81.858 -24.399  1.00 98.62           C  
ANISOU 1863  CB  ASP A1054    10948  13221  13301   2079    269   1522       C  
ATOM   1864  CG  ASP A1054       3.920 -81.478 -25.642  1.00103.99           C  
ANISOU 1864  CG  ASP A1054    11839  13718  13955   2029    302   1282       C  
ATOM   1865  OD1 ASP A1054       3.284 -80.390 -25.637  1.00104.84           O  
ANISOU 1865  OD1 ASP A1054    12100  13804  13930   1727    330   1311       O  
ATOM   1866  OD2 ASP A1054       3.935 -82.264 -26.625  1.00106.23           O  
ANISOU 1866  OD2 ASP A1054    12120  13894  14350   2311    285   1045       O  
ATOM   1867  N   SER A1055       4.235 -81.093 -20.774  1.00 96.30           N  
ANISOU 1867  N   SER A1055    10527  13141  12923   1619    142   2170       N  
ATOM   1868  CA  SER A1055       4.266 -81.605 -19.410  1.00 96.84           C  
ANISOU 1868  CA  SER A1055    10438  13320  13035   1659     62   2458       C  
ATOM   1869  C   SER A1055       2.974 -82.389 -19.104  1.00 97.03           C  
ANISOU 1869  C   SER A1055    10622  12935  13309   1691    -38   2610       C  
ATOM   1870  O   SER A1055       1.967 -82.199 -19.792  1.00 97.07           O  
ANISOU 1870  O   SER A1055    10866  12631  13385   1602    -36   2455       O  
ATOM   1871  CB  SER A1055       4.467 -80.452 -18.424  1.00 98.27           C  
ANISOU 1871  CB  SER A1055    10496  13902  12939   1386     75   2496       C  
ATOM   1872  OG  SER A1055       3.732 -79.283 -18.754  1.00100.42           O  
ANISOU 1872  OG  SER A1055    10961  14087  13108   1118     96   2303       O  
ATOM   1873  N   PRO A1056       2.968 -83.288 -18.095  1.00 96.93           N  
ANISOU 1873  N   PRO A1056    10464  12930  13435   1808   -132   2942       N  
ATOM   1874  CA  PRO A1056       1.751 -84.067 -17.818  1.00 96.97           C  
ANISOU 1874  CA  PRO A1056    10589  12558  13696   1802   -238   3145       C  
ATOM   1875  C   PRO A1056       0.486 -83.227 -17.638  1.00 97.18           C  
ANISOU 1875  C   PRO A1056    10762  12592  13570   1520   -226   3084       C  
ATOM   1876  O   PRO A1056      -0.542 -83.544 -18.232  1.00 97.58           O  
ANISOU 1876  O   PRO A1056    11015  12259  13802   1486   -264   3027       O  
ATOM   1877  CB  PRO A1056       2.111 -84.859 -16.549  1.00 97.66           C  
ANISOU 1877  CB  PRO A1056    10423  12824  13859   1911   -333   3592       C  
ATOM   1878  CG  PRO A1056       3.315 -84.166 -15.973  1.00 98.08           C  
ANISOU 1878  CG  PRO A1056    10228  13452  13587   1899   -262   3582       C  
ATOM   1879  CD  PRO A1056       4.057 -83.662 -17.174  1.00 96.49           C  
ANISOU 1879  CD  PRO A1056    10107  13243  13312   1943   -157   3188       C  
ATOM   1880  N   GLU A1057       0.574 -82.133 -16.865  1.00 96.69           N  
ANISOU 1880  N   GLU A1057    10590  12969  13177   1331   -183   3050       N  
ATOM   1881  CA  GLU A1057      -0.558 -81.242 -16.588  1.00 96.40           C  
ANISOU 1881  CA  GLU A1057    10650  13007  12971   1100   -189   2950       C  
ATOM   1882  C   GLU A1057      -0.954 -80.386 -17.810  1.00 95.12           C  
ANISOU 1882  C   GLU A1057    10758  12593  12791    995   -130   2582       C  
ATOM   1883  O   GLU A1057      -2.116 -80.007 -17.952  1.00 94.93           O  
ANISOU 1883  O   GLU A1057    10889  12422  12757    879   -154   2496       O  
ATOM   1884  CB  GLU A1057      -0.248 -80.365 -15.351  1.00 99.36           C  
ANISOU 1884  CB  GLU A1057    10782  13946  13024    976   -194   2980       C  
ATOM   1885  CG  GLU A1057       0.203 -81.155 -14.120  1.00104.85           C  
ANISOU 1885  CG  GLU A1057    11172  14983  13684   1082   -252   3378       C  
ATOM   1886  CD  GLU A1057       1.583 -80.831 -13.562  1.00111.20           C  
ANISOU 1886  CD  GLU A1057    11706  16248  14297   1132   -228   3398       C  
ATOM   1887  OE1 GLU A1057       2.517 -81.642 -13.765  1.00112.21           O  
ANISOU 1887  OE1 GLU A1057    11736  16325  14572   1334   -228   3568       O  
ATOM   1888  OE2 GLU A1057       1.727 -79.773 -12.906  1.00113.13           O  
ANISOU 1888  OE2 GLU A1057    11819  16912  14254    980   -226   3225       O  
ATOM   1889  N   MET A1058       0.008 -80.109 -18.694  1.00 94.16           N  
ANISOU 1889  N   MET A1058    10665  12456  12654   1046    -56   2397       N  
ATOM   1890  CA  MET A1058      -0.210 -79.315 -19.893  1.00 93.77           C  
ANISOU 1890  CA  MET A1058    10825  12236  12566    952      1   2116       C  
ATOM   1891  C   MET A1058      -1.024 -80.068 -20.926  1.00 92.80           C  
ANISOU 1891  C   MET A1058    10907  11693  12659   1068    -10   2037       C  
ATOM   1892  O   MET A1058      -1.843 -79.459 -21.611  1.00 92.93           O  
ANISOU 1892  O   MET A1058    11118  11546  12644    961      0   1869       O  
ATOM   1893  CB  MET A1058       1.135 -78.861 -20.481  1.00 94.83           C  
ANISOU 1893  CB  MET A1058    10856  12595  12581    955     83   2007       C  
ATOM   1894  CG  MET A1058       1.020 -78.031 -21.744  1.00 97.99           C  
ANISOU 1894  CG  MET A1058    11428  12879  12925    857    144   1792       C  
ATOM   1895  SD  MET A1058      -0.016 -76.547 -21.583  1.00104.42           S  
ANISOU 1895  SD  MET A1058    12434  13596  13645    568    100   1671       S  
ATOM   1896  CE  MET A1058       0.941 -75.599 -20.395  1.00102.95           C  
ANISOU 1896  CE  MET A1058    12025  13795  13297    380     66   1692       C  
ATOM   1897  N   LYS A1059      -0.820 -81.384 -21.037  1.00 91.83           N  
ANISOU 1897  N   LYS A1059    10734  11384  12773   1293    -49   2142       N  
ATOM   1898  CA  LYS A1059      -1.568 -82.186 -21.997  1.00 91.57           C  
ANISOU 1898  CA  LYS A1059    10877  10932  12985   1410    -90   2020       C  
ATOM   1899  C   LYS A1059      -3.029 -82.323 -21.601  1.00 91.57           C  
ANISOU 1899  C   LYS A1059    10998  10708  13085   1279   -168   2121       C  
ATOM   1900  O   LYS A1059      -3.886 -82.378 -22.476  1.00 92.04           O  
ANISOU 1900  O   LYS A1059    11242  10505  13225   1261   -180   1938       O  
ATOM   1901  CB  LYS A1059      -0.933 -83.561 -22.185  1.00 92.76           C  
ANISOU 1901  CB  LYS A1059    10935  10890  13420   1699   -150   2067       C  
ATOM   1902  CG  LYS A1059       0.523 -83.485 -22.583  1.00 96.09           C  
ANISOU 1902  CG  LYS A1059    11244  11536  13731   1870    -66   1873       C  
ATOM   1903  CD  LYS A1059       1.015 -84.791 -23.164  1.00 99.97           C  
ANISOU 1903  CD  LYS A1059    11679  11769  14536   2216   -146   1789       C  
ATOM   1904  CE  LYS A1059       2.510 -84.771 -23.352  1.00103.22           C  
ANISOU 1904  CE  LYS A1059    11835  12507  14876   2414   -115   1850       C  
ATOM   1905  NZ  LYS A1059       3.010 -86.002 -24.014  1.00105.09           N  
ANISOU 1905  NZ  LYS A1059    12009  12584  15336   2793   -168   1607       N  
ATOM   1906  N   ASP A1060      -3.322 -82.372 -20.298  1.00 90.86           N  
ANISOU 1906  N   ASP A1060    10778  10784  12959   1187   -221   2411       N  
ATOM   1907  CA  ASP A1060      -4.697 -82.474 -19.821  1.00 90.70           C  
ANISOU 1907  CA  ASP A1060    10815  10662  12982   1048   -291   2540       C  
ATOM   1908  C   ASP A1060      -5.497 -81.207 -20.146  1.00 89.98           C  
ANISOU 1908  C   ASP A1060    10870  10663  12654    875   -246   2295       C  
ATOM   1909  O   ASP A1060      -6.709 -81.294 -20.373  1.00 90.33           O  
ANISOU 1909  O   ASP A1060    11036  10526  12759    801   -288   2258       O  
ATOM   1910  CB  ASP A1060      -4.728 -82.746 -18.312  1.00 92.81           C  
ANISOU 1910  CB  ASP A1060    10846  11230  13186    993   -349   2924       C  
ATOM   1911  CG  ASP A1060      -4.039 -84.020 -17.867  1.00 98.00           C  
ANISOU 1911  CG  ASP A1060    11350  11774  14113   1159   -426   3256       C  
ATOM   1912  OD1 ASP A1060      -3.413 -84.693 -18.723  1.00 98.76           O  
ANISOU 1912  OD1 ASP A1060    11512  11564  14448   1354   -435   3131       O  
ATOM   1913  OD2 ASP A1060      -4.125 -84.350 -16.660  1.00100.39           O  
ANISOU 1913  OD2 ASP A1060    11445  12316  14383   1110   -488   3645       O  
ATOM   1914  N   PHE A1061      -4.836 -80.039 -20.175  1.00 88.74           N  
ANISOU 1914  N   PHE A1061    10692  10773  12252    808   -178   2135       N  
ATOM   1915  CA  PHE A1061      -5.519 -78.806 -20.527  1.00 88.12           C  
ANISOU 1915  CA  PHE A1061    10756  10719  12004    665   -164   1908       C  
ATOM   1916  C   PHE A1061      -5.925 -78.859 -22.007  1.00 87.31           C  
ANISOU 1916  C   PHE A1061    10880  10302  11993    701   -134   1697       C  
ATOM   1917  O   PHE A1061      -7.088 -78.616 -22.338  1.00 87.64           O  
ANISOU 1917  O   PHE A1061    11062  10203  12034    641   -166   1604       O  
ATOM   1918  CB  PHE A1061      -4.630 -77.591 -20.217  1.00 88.03           C  
ANISOU 1918  CB  PHE A1061    10662  11004  11784    569   -134   1804       C  
ATOM   1919  CG  PHE A1061      -5.044 -76.303 -20.894  1.00 88.73           C  
ANISOU 1919  CG  PHE A1061    10921  11016  11775    441   -138   1563       C  
ATOM   1920  CD1 PHE A1061      -6.052 -75.514 -20.366  1.00 89.33           C  
ANISOU 1920  CD1 PHE A1061    11037  11140  11767    359   -211   1469       C  
ATOM   1921  CD2 PHE A1061      -4.413 -75.874 -22.049  1.00 89.54           C  
ANISOU 1921  CD2 PHE A1061    11123  11026  11873    414    -80   1448       C  
ATOM   1922  CE1 PHE A1061      -6.405 -74.316 -20.969  1.00 89.94           C  
ANISOU 1922  CE1 PHE A1061    11270  11103  11800    267   -244   1258       C  
ATOM   1923  CE2 PHE A1061      -4.794 -74.695 -22.668  1.00 90.16           C  
ANISOU 1923  CE2 PHE A1061    11352  11008  11895    289   -106   1295       C  
ATOM   1924  CZ  PHE A1061      -5.784 -73.922 -22.123  1.00 89.83           C  
ANISOU 1924  CZ  PHE A1061    11370  10945  11816    224   -196   1198       C  
ATOM   1925  N   ARG A1062      -4.980 -79.206 -22.885  1.00 86.18           N  
ANISOU 1925  N   ARG A1062    10740  10104  11900    815    -74   1616       N  
ATOM   1926  CA  ARG A1062      -5.268 -79.257 -24.307  1.00 85.87           C  
ANISOU 1926  CA  ARG A1062    10865   9871  11891    866    -42   1403       C  
ATOM   1927  C   ARG A1062      -6.232 -80.391 -24.648  1.00 85.28           C  
ANISOU 1927  C   ARG A1062    10876   9476  12049    961   -110   1376       C  
ATOM   1928  O   ARG A1062      -7.028 -80.229 -25.565  1.00 85.43           O  
ANISOU 1928  O   ARG A1062    11047   9359  12056    942   -113   1201       O  
ATOM   1929  CB  ARG A1062      -3.986 -79.259 -25.153  1.00 87.50           C  
ANISOU 1929  CB  ARG A1062    11002  10217  12027    965     43   1306       C  
ATOM   1930  CG  ARG A1062      -3.615 -80.552 -25.881  1.00 91.28           C  
ANISOU 1930  CG  ARG A1062    11451  10548  12681   1211     41   1193       C  
ATOM   1931  CD  ARG A1062      -2.362 -80.384 -26.730  1.00 95.05           C  
ANISOU 1931  CD  ARG A1062    11823  11289  13003   1306    137   1068       C  
ATOM   1932  NE  ARG A1062      -1.205 -79.950 -25.943  1.00 98.27           N  
ANISOU 1932  NE  ARG A1062    12045  12009  13287   1252    184   1220       N  
ATOM   1933  CZ  ARG A1062      -0.341 -80.774 -25.355  1.00100.54           C  
ANISOU 1933  CZ  ARG A1062    12151  12375  13673   1422    170   1313       C  
ATOM   1934  NH1 ARG A1062       0.675 -80.289 -24.653  1.00100.25           N  
ANISOU 1934  NH1 ARG A1062    11932  12669  13490   1353    213   1439       N  
ATOM   1935  NH2 ARG A1062      -0.487 -82.091 -25.465  1.00100.23           N  
ANISOU 1935  NH2 ARG A1062    12108  12072  13904   1662     95   1281       N  
ATOM   1936  N   HIS A1063      -6.221 -81.489 -23.888  1.00 84.63           N  
ANISOU 1936  N   HIS A1063    10694   9273  12191   1041   -181   1567       N  
ATOM   1937  CA  HIS A1063      -7.144 -82.592 -24.141  1.00 84.63           C  
ANISOU 1937  CA  HIS A1063    10764   8917  12476   1089   -279   1568       C  
ATOM   1938  C   HIS A1063      -8.587 -82.241 -23.783  1.00 83.84           C  
ANISOU 1938  C   HIS A1063    10741   8788  12327    906   -327   1623       C  
ATOM   1939  O   HIS A1063      -9.509 -82.636 -24.498  1.00 83.75           O  
ANISOU 1939  O   HIS A1063    10846   8533  12442    898   -377   1485       O  
ATOM   1940  CB  HIS A1063      -6.667 -83.880 -23.482  1.00 85.95           C  
ANISOU 1940  CB  HIS A1063    10794   8914  12949   1214   -370   1806       C  
ATOM   1941  CG  HIS A1063      -5.669 -84.595 -24.339  1.00 89.02           C  
ANISOU 1941  CG  HIS A1063    11163   9157  13505   1469   -371   1607       C  
ATOM   1942  ND1 HIS A1063      -5.713 -85.963 -24.504  1.00 91.18           N  
ANISOU 1942  ND1 HIS A1063    11423   9031  14191   1633   -507   1618       N  
ATOM   1943  CD2 HIS A1063      -4.678 -84.093 -25.116  1.00 90.41           C  
ANISOU 1943  CD2 HIS A1063    11315   9550  13485   1584   -265   1371       C  
ATOM   1944  CE1 HIS A1063      -4.726 -86.257 -25.337  1.00 91.78           C  
ANISOU 1944  CE1 HIS A1063    11462   9111  14299   1881   -480   1346       C  
ATOM   1945  NE2 HIS A1063      -4.077 -85.161 -25.734  1.00 91.64           N  
ANISOU 1945  NE2 HIS A1063    11425   9500  13895   1854   -325   1206       N  
ATOM   1946  N   GLY A1064      -8.774 -81.407 -22.768  1.00 83.18           N  
ANISOU 1946  N   GLY A1064    10579   8996  12030    772   -311   1770       N  
ATOM   1947  CA  GLY A1064     -10.102 -80.937 -22.399  1.00 83.20           C  
ANISOU 1947  CA  GLY A1064    10618   9068  11928    626   -352   1787       C  
ATOM   1948  C   GLY A1064     -10.731 -80.141 -23.524  1.00 83.07           C  
ANISOU 1948  C   GLY A1064    10795   8971  11796    605   -322   1489       C  
ATOM   1949  O   GLY A1064     -11.888 -80.356 -23.881  1.00 83.34           O  
ANISOU 1949  O   GLY A1064    10908   8871  11885    559   -372   1428       O  
ATOM   1950  N   PHE A1065      -9.935 -79.287 -24.154  1.00 82.61           N  
ANISOU 1950  N   PHE A1065    10799   8995  11593    636   -248   1328       N  
ATOM   1951  CA  PHE A1065     -10.390 -78.488 -25.281  1.00 82.77           C  
ANISOU 1951  CA  PHE A1065    10987   8965  11498    620   -222   1103       C  
ATOM   1952  C   PHE A1065     -10.638 -79.336 -26.526  1.00 83.10           C  
ANISOU 1952  C   PHE A1065    11118   8780  11674    722   -227    943       C  
ATOM   1953  O   PHE A1065     -11.547 -79.044 -27.297  1.00 82.84           O  
ANISOU 1953  O   PHE A1065    11203   8685  11587    700   -247    799       O  
ATOM   1954  CB  PHE A1065      -9.358 -77.403 -25.575  1.00 82.55           C  
ANISOU 1954  CB  PHE A1065    10961   9096  11307    597   -154   1052       C  
ATOM   1955  CG  PHE A1065      -9.622 -76.161 -24.780  1.00 83.11           C  
ANISOU 1955  CG  PHE A1065    11031   9314  11233    476   -191   1056       C  
ATOM   1956  CD1 PHE A1065     -10.606 -75.275 -25.167  1.00 83.88           C  
ANISOU 1956  CD1 PHE A1065    11263   9352  11256    431   -238    936       C  
ATOM   1957  CD2 PHE A1065      -8.920 -75.899 -23.622  1.00 83.93           C  
ANISOU 1957  CD2 PHE A1065    10984   9621  11285    429   -198   1153       C  
ATOM   1958  CE1 PHE A1065     -10.861 -74.132 -24.430  1.00 84.57           C  
ANISOU 1958  CE1 PHE A1065    11344   9539  11249    357   -303    886       C  
ATOM   1959  CE2 PHE A1065      -9.192 -74.763 -22.876  1.00 84.71           C  
ANISOU 1959  CE2 PHE A1065    11066   9851  11269    340   -260   1082       C  
ATOM   1960  CZ  PHE A1065     -10.151 -73.880 -23.292  1.00 84.40           C  
ANISOU 1960  CZ  PHE A1065    11172   9708  11189    313   -318    936       C  
ATOM   1961  N   ASP A1066      -9.822 -80.384 -26.724  1.00 83.30           N  
ANISOU 1961  N   ASP A1066    11074   8701  11876    855   -221    940       N  
ATOM   1962  CA  ASP A1066      -9.955 -81.296 -27.862  1.00 83.69           C  
ANISOU 1962  CA  ASP A1066    11175   8542  12080    991   -249    718       C  
ATOM   1963  C   ASP A1066     -11.293 -82.033 -27.842  1.00 83.34           C  
ANISOU 1963  C   ASP A1066    11185   8243  12238    936   -360    699       C  
ATOM   1964  O   ASP A1066     -11.862 -82.298 -28.900  1.00 83.27           O  
ANISOU 1964  O   ASP A1066    11255   8120  12264    989   -390    450       O  
ATOM   1965  CB  ASP A1066      -8.793 -82.292 -27.911  1.00 85.81           C  
ANISOU 1965  CB  ASP A1066    11331   8738  12535   1180   -252    697       C  
ATOM   1966  CG  ASP A1066      -7.485 -81.678 -28.364  1.00 91.04           C  
ANISOU 1966  CG  ASP A1066    11917   9700  12975   1249   -137    658       C  
ATOM   1967  OD1 ASP A1066      -7.530 -80.655 -29.096  1.00 92.08           O  
ANISOU 1967  OD1 ASP A1066    12108  10036  12841   1171    -62    577       O  
ATOM   1968  OD2 ASP A1066      -6.411 -82.210 -27.975  1.00 93.11           O  
ANISOU 1968  OD2 ASP A1066    12042  10002  13332   1370   -129    739       O  
ATOM   1969  N   ILE A1067     -11.810 -82.341 -26.649  1.00 82.93           N  
ANISOU 1969  N   ILE A1067    11063   8152  12294    818   -424    967       N  
ATOM   1970  CA  ILE A1067     -13.112 -82.983 -26.533  1.00 83.06           C  
ANISOU 1970  CA  ILE A1067    11094   7975  12490    715   -533   1010       C  
ATOM   1971  C   ILE A1067     -14.203 -82.020 -27.034  1.00 83.03           C  
ANISOU 1971  C   ILE A1067    11195   8113  12242    625   -513    856       C  
ATOM   1972  O   ILE A1067     -15.053 -82.395 -27.848  1.00 83.22           O  
ANISOU 1972  O   ILE A1067    11284   7986  12349    615   -572    676       O  
ATOM   1973  CB  ILE A1067     -13.350 -83.420 -25.074  1.00 83.58           C  
ANISOU 1973  CB  ILE A1067    11009   8081  12668    591   -596   1403       C  
ATOM   1974  CG1 ILE A1067     -12.212 -84.329 -24.578  1.00 84.47           C  
ANISOU 1974  CG1 ILE A1067    11008   8078  13008    701   -621   1599       C  
ATOM   1975  CG2 ILE A1067     -14.704 -84.096 -24.933  1.00 84.15           C  
ANISOU 1975  CG2 ILE A1067    11061   7977  12936    446   -715   1500       C  
ATOM   1976  CD1 ILE A1067     -11.987 -85.590 -25.409  1.00 85.87           C  
ANISOU 1976  CD1 ILE A1067    11227   7835  13565    868   -709   1419       C  
ATOM   1977  N   LEU A1068     -14.118 -80.760 -26.591  1.00 82.56           N  
ANISOU 1977  N   LEU A1068    11142   8334  11894    575   -445    904       N  
ATOM   1978  CA  LEU A1068     -15.054 -79.700 -26.953  1.00 82.45           C  
ANISOU 1978  CA  LEU A1068    11220   8453  11656    522   -443    776       C  
ATOM   1979  C   LEU A1068     -15.018 -79.363 -28.448  1.00 81.98           C  
ANISOU 1979  C   LEU A1068    11294   8354  11500    611   -404    515       C  
ATOM   1980  O   LEU A1068     -16.066 -79.277 -29.086  1.00 82.17           O  
ANISOU 1980  O   LEU A1068    11386   8361  11476    598   -444    377       O  
ATOM   1981  CB  LEU A1068     -14.783 -78.456 -26.096  1.00 82.68           C  
ANISOU 1981  CB  LEU A1068    11213   8740  11462    474   -414    860       C  
ATOM   1982  CG  LEU A1068     -14.888 -78.678 -24.584  1.00 84.16           C  
ANISOU 1982  CG  LEU A1068    11220   9098  11659    403   -443   1104       C  
ATOM   1983  CD1 LEU A1068     -14.489 -77.444 -23.822  1.00 84.85           C  
ANISOU 1983  CD1 LEU A1068    11264   9454  11521    385   -433   1082       C  
ATOM   1984  CD2 LEU A1068     -16.281 -79.095 -24.179  1.00 84.66           C  
ANISOU 1984  CD2 LEU A1068    11194   9187  11784    311   -521   1221       C  
ATOM   1985  N   VAL A1069     -13.817 -79.208 -29.011  1.00 81.13           N  
ANISOU 1985  N   VAL A1069    11193   8288  11344    700   -329    463       N  
ATOM   1986  CA  VAL A1069     -13.646 -78.925 -30.433  1.00 80.71           C  
ANISOU 1986  CA  VAL A1069    11214   8296  11157    786   -284    258       C  
ATOM   1987  C   VAL A1069     -14.175 -80.084 -31.287  1.00 80.44           C  
ANISOU 1987  C   VAL A1069    11182   8102  11281    876   -342     30       C  
ATOM   1988  O   VAL A1069     -14.811 -79.854 -32.317  1.00 80.50           O  
ANISOU 1988  O   VAL A1069    11246   8183  11156    912   -348   -159       O  
ATOM   1989  CB  VAL A1069     -12.171 -78.601 -30.737  1.00 81.10           C  
ANISOU 1989  CB  VAL A1069    11209   8494  11111    846   -190    291       C  
ATOM   1990  CG1 VAL A1069     -11.919 -78.509 -32.235  1.00 81.70           C  
ANISOU 1990  CG1 VAL A1069    11298   8720  11024    947   -138    104       C  
ATOM   1991  CG2 VAL A1069     -11.754 -77.319 -30.040  1.00 81.36           C  
ANISOU 1991  CG2 VAL A1069    11248   8662  11005    729   -161    471       C  
ATOM   1992  N   GLY A1070     -13.957 -81.312 -30.827  1.00 80.01           N  
ANISOU 1992  N   GLY A1070    11056   7821  11523    909   -404     51       N  
ATOM   1993  CA  GLY A1070     -14.438 -82.497 -31.519  1.00 80.07           C  
ANISOU 1993  CA  GLY A1070    11057   7597  11767    984   -501   -188       C  
ATOM   1994  C   GLY A1070     -15.949 -82.532 -31.588  1.00 79.68           C  
ANISOU 1994  C   GLY A1070    11055   7486  11736    856   -585   -232       C  
ATOM   1995  O   GLY A1070     -16.519 -82.838 -32.637  1.00 79.83           O  
ANISOU 1995  O   GLY A1070    11101   7486  11746    911   -631   -520       O  
ATOM   1996  N   GLN A1071     -16.609 -82.175 -30.482  1.00 79.12           N  
ANISOU 1996  N   GLN A1071    10965   7446  11650    692   -605     36       N  
ATOM   1997  CA  GLN A1071     -18.069 -82.149 -30.441  1.00 79.21           C  
ANISOU 1997  CA  GLN A1071    10983   7466  11645    563   -682     23       C  
ATOM   1998  C   GLN A1071     -18.657 -81.053 -31.324  1.00 79.11           C  
ANISOU 1998  C   GLN A1071    11060   7686  11312    601   -639   -154       C  
ATOM   1999  O   GLN A1071     -19.746 -81.220 -31.866  1.00 79.11           O  
ANISOU 1999  O   GLN A1071    11069   7687  11303    566   -706   -310       O  
ATOM   2000  CB  GLN A1071     -18.566 -82.039 -29.000  1.00 80.77           C  
ANISOU 2000  CB  GLN A1071    11090   7749  11850    403   -706    352       C  
ATOM   2001  CG  GLN A1071     -18.323 -83.314 -28.203  1.00 84.10           C  
ANISOU 2001  CG  GLN A1071    11397   7922  12637    314   -800    575       C  
ATOM   2002  CD  GLN A1071     -18.669 -83.133 -26.755  1.00 88.03           C  
ANISOU 2002  CD  GLN A1071    11756   8625  13065    175   -801    944       C  
ATOM   2003  OE1 GLN A1071     -18.469 -82.061 -26.186  1.00 89.70           O  
ANISOU 2003  OE1 GLN A1071    11955   9112  13012    210   -715   1014       O  
ATOM   2004  NE2 GLN A1071     -19.191 -84.173 -26.123  1.00 88.11           N  
ANISOU 2004  NE2 GLN A1071    11637   8532  13310      8   -910   1189       N  
ATOM   2005  N   ILE A1072     -17.929 -79.945 -31.488  1.00 78.94           N  
ANISOU 2005  N   ILE A1072    11094   7856  11043    665   -541   -113       N  
ATOM   2006  CA  ILE A1072     -18.336 -78.862 -32.366  1.00 79.14           C  
ANISOU 2006  CA  ILE A1072    11204   8081  10786    710   -512   -214       C  
ATOM   2007  C   ILE A1072     -18.205 -79.342 -33.815  1.00 79.84           C  
ANISOU 2007  C   ILE A1072    11299   8209  10828    828   -506   -487       C  
ATOM   2008  O   ILE A1072     -19.116 -79.125 -34.602  1.00 79.91           O  
ANISOU 2008  O   ILE A1072    11333   8329  10700    845   -544   -632       O  
ATOM   2009  CB  ILE A1072     -17.499 -77.597 -32.076  1.00 79.33           C  
ANISOU 2009  CB  ILE A1072    11269   8237  10637    717   -435    -55       C  
ATOM   2010  CG1 ILE A1072     -17.854 -77.009 -30.700  1.00 80.00           C  
ANISOU 2010  CG1 ILE A1072    11328   8344  10724    626   -466    126       C  
ATOM   2011  CG2 ILE A1072     -17.681 -76.564 -33.168  1.00 79.81           C  
ANISOU 2011  CG2 ILE A1072    11411   8462  10453    770   -416   -109       C  
ATOM   2012  CD1 ILE A1072     -16.924 -75.935 -30.225  1.00 81.04           C  
ANISOU 2012  CD1 ILE A1072    11477   8547  10768    614   -422    251       C  
ATOM   2013  N   ASP A1073     -17.110 -80.049 -34.155  1.00 80.32           N  
ANISOU 2013  N   ASP A1073    11310   8218  10991    928   -469   -582       N  
ATOM   2014  CA  ASP A1073     -16.899 -80.598 -35.501  1.00 81.31           C  
ANISOU 2014  CA  ASP A1073    11395   8445  11055   1077   -470   -901       C  
ATOM   2015  C   ASP A1073     -17.977 -81.627 -35.860  1.00 81.62           C  
ANISOU 2015  C   ASP A1073    11410   8310  11294   1068   -601  -1168       C  
ATOM   2016  O   ASP A1073     -18.426 -81.675 -37.004  1.00 81.39           O  
ANISOU 2016  O   ASP A1073    11358   8455  11110   1153   -624  -1448       O  
ATOM   2017  CB  ASP A1073     -15.500 -81.237 -35.615  1.00 83.71           C  
ANISOU 2017  CB  ASP A1073    11617   8734  11455   1212   -420   -970       C  
ATOM   2018  CG  ASP A1073     -14.511 -80.480 -36.493  1.00 89.43           C  
ANISOU 2018  CG  ASP A1073    12281   9842  11855   1345   -317  -1075       C  
ATOM   2019  OD1 ASP A1073     -14.715 -80.446 -37.731  1.00 90.61           O  
ANISOU 2019  OD1 ASP A1073    12401  10214  11813   1426   -332  -1315       O  
ATOM   2020  OD2 ASP A1073     -13.513 -79.955 -35.949  1.00 91.72           O  
ANISOU 2020  OD2 ASP A1073    12525  10256  12067   1362   -225   -908       O  
ATOM   2021  N   ASP A1074     -18.397 -82.433 -34.880  1.00 82.10           N  
ANISOU 2021  N   ASP A1074    11454   8050  11689    951   -694  -1065       N  
ATOM   2022  CA  ASP A1074     -19.436 -83.436 -35.084  1.00 83.05           C  
ANISOU 2022  CA  ASP A1074    11539   7951  12066    885   -843  -1267       C  
ATOM   2023  C   ASP A1074     -20.757 -82.762 -35.471  1.00 83.69           C  
ANISOU 2023  C   ASP A1074    11644   8248  11909    799   -865  -1311       C  
ATOM   2024  O   ASP A1074     -21.430 -83.203 -36.403  1.00 84.11           O  
ANISOU 2024  O   ASP A1074    11663   8332  11962    829   -947  -1628       O  
ATOM   2025  CB  ASP A1074     -19.619 -84.294 -33.816  1.00 84.89           C  
ANISOU 2025  CB  ASP A1074    11728   7826  12698    726   -939  -1013       C  
ATOM   2026  CG  ASP A1074     -18.452 -85.212 -33.497  1.00 89.57           C  
ANISOU 2026  CG  ASP A1074    12282   8139  13613    832   -968  -1001       C  
ATOM   2027  OD1 ASP A1074     -17.562 -85.368 -34.362  1.00 90.28           O  
ANISOU 2027  OD1 ASP A1074    12364   8307  13631   1048   -923  -1266       O  
ATOM   2028  OD2 ASP A1074     -18.424 -85.769 -32.379  1.00 91.87           O  
ANISOU 2028  OD2 ASP A1074    12526   8168  14211    711  -1040   -711       O  
ATOM   2029  N   ALA A1075     -21.121 -81.688 -34.765  1.00 83.57           N  
ANISOU 2029  N   ALA A1075    11670   8395  11687    712   -805  -1025       N  
ATOM   2030  CA  ALA A1075     -22.347 -80.953 -35.069  1.00 83.95           C  
ANISOU 2030  CA  ALA A1075    11733   8667  11497    669   -830  -1051       C  
ATOM   2031  C   ALA A1075     -22.219 -80.175 -36.381  1.00 84.41           C  
ANISOU 2031  C   ALA A1075    11833   9021  11219    824   -773  -1220       C  
ATOM   2032  O   ALA A1075     -23.204 -80.028 -37.103  1.00 84.59           O  
ANISOU 2032  O   ALA A1075    11837   9217  11085    837   -825  -1375       O  
ATOM   2033  CB  ALA A1075     -22.673 -80.002 -33.939  1.00 84.09           C  
ANISOU 2033  CB  ALA A1075    11768   8779  11402    585   -798   -745       C  
ATOM   2034  N   LEU A1076     -21.007 -79.678 -36.683  1.00 84.50           N  
ANISOU 2034  N   LEU A1076    11876   9128  11102    931   -669  -1157       N  
ATOM   2035  CA  LEU A1076     -20.694 -78.936 -37.897  1.00 84.98           C  
ANISOU 2035  CA  LEU A1076    11942   9514  10833   1060   -605  -1229       C  
ATOM   2036  C   LEU A1076     -20.865 -79.809 -39.137  1.00 85.52           C  
ANISOU 2036  C   LEU A1076    11914   9722  10856   1173   -654  -1628       C  
ATOM   2037  O   LEU A1076     -21.331 -79.313 -40.165  1.00 85.70           O  
ANISOU 2037  O   LEU A1076    11910  10070  10584   1243   -657  -1725       O  
ATOM   2038  CB  LEU A1076     -19.271 -78.387 -37.824  1.00 85.06           C  
ANISOU 2038  CB  LEU A1076    11959   9589  10771   1108   -492  -1056       C  
ATOM   2039  CG  LEU A1076     -19.171 -76.880 -37.806  1.00 86.53           C  
ANISOU 2039  CG  LEU A1076    12217   9935  10725   1078   -438   -757       C  
ATOM   2040  CD1 LEU A1076     -18.046 -76.429 -36.910  1.00 87.17           C  
ANISOU 2040  CD1 LEU A1076    12305   9947  10870   1039   -359   -540       C  
ATOM   2041  CD2 LEU A1076     -19.009 -76.330 -39.216  1.00 87.19           C  
ANISOU 2041  CD2 LEU A1076    12264  10390  10476   1172   -413   -793       C  
ATOM   2042  N   LYS A1077     -20.519 -81.107 -39.043  1.00 85.46           N  
ANISOU 2042  N   LYS A1077    11844   9475  11151   1204   -711  -1872       N  
ATOM   2043  CA  LYS A1077     -20.692 -81.996 -40.181  1.00 85.87           C  
ANISOU 2043  CA  LYS A1077    11790   9636  11201   1331   -788  -2334       C  
ATOM   2044  C   LYS A1077     -22.169 -82.330 -40.399  1.00 86.44           C  
ANISOU 2044  C   LYS A1077    11840   9676  11326   1232   -917  -2512       C  
ATOM   2045  O   LYS A1077     -22.598 -82.430 -41.546  1.00 86.54           O  
ANISOU 2045  O   LYS A1077    11767   9985  11128   1334   -958  -2836       O  
ATOM   2046  CB  LYS A1077     -19.786 -83.231 -40.128  1.00 87.52           C  
ANISOU 2046  CB  LYS A1077    11931   9580  11742   1437   -838  -2593       C  
ATOM   2047  CG  LYS A1077     -19.915 -84.140 -38.925  1.00 91.31           C  
ANISOU 2047  CG  LYS A1077    12449   9517  12729   1295   -944  -2477       C  
ATOM   2048  CD  LYS A1077     -18.828 -85.218 -38.966  1.00 95.42           C  
ANISOU 2048  CD  LYS A1077    12902   9787  13567   1458  -1001  -2723       C  
ATOM   2049  CE  LYS A1077     -19.277 -86.535 -38.377  1.00 98.79           C  
ANISOU 2049  CE  LYS A1077    13338   9634  14564   1329  -1167  -2670       C  
ATOM   2050  NZ  LYS A1077     -18.763 -87.703 -39.149  1.00100.39           N  
ANISOU 2050  NZ  LYS A1077    13455   9558  15129   1512  -1328  -3153       N  
ATOM   2051  N   LEU A1078     -22.967 -82.410 -39.325  1.00 86.96           N  
ANISOU 2051  N   LEU A1078    11957   9470  11614   1034   -977  -2287       N  
ATOM   2052  CA  LEU A1078     -24.414 -82.632 -39.458  1.00 88.04           C  
ANISOU 2052  CA  LEU A1078    12048   9632  11770    912  -1094  -2405       C  
ATOM   2053  C   LEU A1078     -25.084 -81.400 -40.062  1.00 88.79           C  
ANISOU 2053  C   LEU A1078    12159  10163  11412    971  -1040  -2323       C  
ATOM   2054  O   LEU A1078     -25.985 -81.522 -40.889  1.00 88.68           O  
ANISOU 2054  O   LEU A1078    12069  10374  11251    991  -1115  -2572       O  
ATOM   2055  CB  LEU A1078     -25.046 -82.929 -38.097  1.00 88.50           C  
ANISOU 2055  CB  LEU A1078    12114   9390  12121    680  -1155  -2118       C  
ATOM   2056  CG  LEU A1078     -24.629 -84.237 -37.477  1.00 90.40           C  
ANISOU 2056  CG  LEU A1078    12318   9169  12860    582  -1256  -2146       C  
ATOM   2057  CD1 LEU A1078     -25.075 -84.315 -36.043  1.00 91.05           C  
ANISOU 2057  CD1 LEU A1078    12384   9072  13138    356  -1279  -1734       C  
ATOM   2058  CD2 LEU A1078     -25.174 -85.398 -38.270  1.00 91.29           C  
ANISOU 2058  CD2 LEU A1078    12340   9126  13221    552  -1432  -2577       C  
ATOM   2059  N   ALA A1079     -24.637 -80.205 -39.657  1.00 89.36           N  
ANISOU 2059  N   ALA A1079    12325  10344  11283   1003   -927  -1973       N  
ATOM   2060  CA  ALA A1079     -25.165 -78.960 -40.188  1.00 90.33           C  
ANISOU 2060  CA  ALA A1079    12478  10810  11032   1076   -896  -1838       C  
ATOM   2061  C   ALA A1079     -24.889 -78.872 -41.690  1.00 91.37           C  
ANISOU 2061  C   ALA A1079    12535  11328  10853   1243   -870  -2055       C  
ATOM   2062  O   ALA A1079     -25.808 -78.570 -42.449  1.00 91.58           O  
ANISOU 2062  O   ALA A1079    12505  11656  10637   1294   -922  -2157       O  
ATOM   2063  CB  ALA A1079     -24.544 -77.776 -39.465  1.00 90.44           C  
ANISOU 2063  CB  ALA A1079    12606  10777  10980   1075   -810  -1450       C  
ATOM   2064  N   ASN A1080     -23.662 -79.223 -42.129  1.00 91.83           N  
ANISOU 2064  N   ASN A1080    12556  11429  10905   1338   -799  -2152       N  
ATOM   2065  CA  ASN A1080     -23.301 -79.196 -43.548  1.00 92.72           C  
ANISOU 2065  CA  ASN A1080    12544  12007  10679   1509   -765  -2366       C  
ATOM   2066  C   ASN A1080     -24.136 -80.146 -44.390  1.00 93.72           C  
ANISOU 2066  C   ASN A1080    12532  12298  10781   1565   -883  -2857       C  
ATOM   2067  O   ASN A1080     -24.412 -79.852 -45.555  1.00 94.02           O  
ANISOU 2067  O   ASN A1080    12453  12835  10436   1687   -883  -2988       O  
ATOM   2068  CB  ASN A1080     -21.817 -79.437 -43.740  1.00 93.63           C  
ANISOU 2068  CB  ASN A1080    12610  12164  10801   1604   -669  -2396       C  
ATOM   2069  CG  ASN A1080     -21.005 -78.236 -43.361  1.00 96.75           C  
ANISOU 2069  CG  ASN A1080    13071  12679  11009   1581   -546  -1931       C  
ATOM   2070  OD1 ASN A1080     -21.298 -77.114 -43.772  1.00 97.86           O  
ANISOU 2070  OD1 ASN A1080    13173  13221  10787   1627   -506  -1737       O  
ATOM   2071  ND2 ASN A1080     -19.970 -78.439 -42.563  1.00 97.52           N  
ANISOU 2071  ND2 ASN A1080    13254  12439  11359   1501   -496  -1724       N  
ATOM   2072  N   GLU A1081     -24.582 -81.260 -43.795  1.00 94.04           N  
ANISOU 2072  N   GLU A1081    12571  11929  11233   1460   -999  -3104       N  
ATOM   2073  CA  GLU A1081     -25.458 -82.192 -44.496  1.00 94.76           C  
ANISOU 2073  CA  GLU A1081    12528  12097  11378   1470  -1146  -3592       C  
ATOM   2074  C   GLU A1081     -26.955 -81.811 -44.416  1.00 95.14           C  
ANISOU 2074  C   GLU A1081    12569  12253  11325   1348  -1224  -3522       C  
ATOM   2075  O   GLU A1081     -27.807 -82.577 -44.861  1.00 95.33           O  
ANISOU 2075  O   GLU A1081    12477  12329  11417   1312  -1360  -3905       O  
ATOM   2076  CB  GLU A1081     -25.217 -83.634 -44.030  1.00 97.12           C  
ANISOU 2076  CB  GLU A1081    12807  11884  12212   1404  -1271  -3903       C  
ATOM   2077  CG  GLU A1081     -25.649 -83.931 -42.609  1.00101.56           C  
ANISOU 2077  CG  GLU A1081    13469  11923  13196   1151  -1331  -3608       C  
ATOM   2078  CD  GLU A1081     -25.204 -85.285 -42.095  1.00106.63           C  
ANISOU 2078  CD  GLU A1081    14104  12014  14397   1090  -1447  -3774       C  
ATOM   2079  OE1 GLU A1081     -26.078 -86.065 -41.652  1.00107.68           O  
ANISOU 2079  OE1 GLU A1081    14202  11811  14899    889  -1609  -3847       O  
ATOM   2080  OE2 GLU A1081     -23.984 -85.570 -42.140  1.00107.84           O  
ANISOU 2080  OE2 GLU A1081    14271  12072  14629   1242  -1388  -3814       O  
ATOM   2081  N   GLY A1082     -27.257 -80.633 -43.879  1.00 95.00           N  
ANISOU 2081  N   GLY A1082    12660  12288  11148   1301  -1151  -3068       N  
ATOM   2082  CA  GLY A1082     -28.613 -80.123 -43.764  1.00 95.29           C  
ANISOU 2082  CA  GLY A1082    12680  12475  11051   1232  -1217  -2973       C  
ATOM   2083  C   GLY A1082     -29.451 -80.788 -42.697  1.00 95.26           C  
ANISOU 2083  C   GLY A1082    12672  12112  11411   1006  -1315  -2959       C  
ATOM   2084  O   GLY A1082     -30.676 -80.663 -42.724  1.00 95.50           O  
ANISOU 2084  O   GLY A1082    12629  12311  11346    940  -1394  -2985       O  
ATOM   2085  N   LYS A1083     -28.815 -81.489 -41.746  1.00 94.92           N  
ANISOU 2085  N   LYS A1083    12681  11613  11772    882  -1316  -2886       N  
ATOM   2086  CA  LYS A1083     -29.553 -82.162 -40.678  1.00 95.07           C  
ANISOU 2086  CA  LYS A1083    12664  11316  12142    637  -1413  -2795       C  
ATOM   2087  C   LYS A1083     -29.594 -81.270 -39.444  1.00 94.56           C  
ANISOU 2087  C   LYS A1083    12683  11207  12039    578  -1331  -2335       C  
ATOM   2088  O   LYS A1083     -28.800 -81.440 -38.523  1.00 94.54           O  
ANISOU 2088  O   LYS A1083    12743  10916  12261    519  -1282  -2116       O  
ATOM   2089  CB  LYS A1083     -28.951 -83.551 -40.380  1.00 97.20           C  
ANISOU 2089  CB  LYS A1083    12911  11116  12903    529  -1499  -2966       C  
ATOM   2090  CG  LYS A1083     -29.882 -84.509 -39.616  1.00101.13           C  
ANISOU 2090  CG  LYS A1083    13314  11312  13797    234  -1652  -2920       C  
ATOM   2091  CD  LYS A1083     -31.309 -84.632 -40.167  1.00105.06           C  
ANISOU 2091  CD  LYS A1083    13668  12061  14187    122  -1775  -3141       C  
ATOM   2092  CE  LYS A1083     -32.294 -85.008 -39.084  1.00108.53           C  
ANISOU 2092  CE  LYS A1083    14006  12350  14882   -195  -1869  -2877       C  
ATOM   2093  NZ  LYS A1083     -33.690 -84.626 -39.441  1.00110.60           N  
ANISOU 2093  NZ  LYS A1083    14121  12998  14906   -279  -1942  -2989       N  
ATOM   2094  N   VAL A1084     -30.526 -80.309 -39.453  1.00 93.93           N  
ANISOU 2094  N   VAL A1084    12585  11444  11662    619  -1329  -2218       N  
ATOM   2095  CA  VAL A1084     -30.696 -79.291 -38.428  1.00 93.70           C  
ANISOU 2095  CA  VAL A1084    12612  11455  11536    625  -1276  -1870       C  
ATOM   2096  C   VAL A1084     -31.033 -79.876 -37.052  1.00 93.86           C  
ANISOU 2096  C   VAL A1084    12552  11277  11834    397  -1315  -1688       C  
ATOM   2097  O   VAL A1084     -30.307 -79.600 -36.101  1.00 94.06           O  
ANISOU 2097  O   VAL A1084    12641  11150  11949    384  -1247  -1440       O  
ATOM   2098  CB  VAL A1084     -31.706 -78.216 -38.891  1.00 93.84           C  
ANISOU 2098  CB  VAL A1084    12604  11858  11191    765  -1301  -1854       C  
ATOM   2099  CG1 VAL A1084     -33.061 -78.816 -39.254  1.00 94.17           C  
ANISOU 2099  CG1 VAL A1084    12472  12116  11192    666  -1418  -2076       C  
ATOM   2100  CG2 VAL A1084     -31.836 -77.094 -37.878  1.00 94.17           C  
ANISOU 2100  CG2 VAL A1084    12704  11929  11149    827  -1271  -1563       C  
ATOM   2101  N   LYS A1085     -32.067 -80.723 -36.946  1.00 93.57           N  
ANISOU 2101  N   LYS A1085    12357  11256  11939    201  -1429  -1795       N  
ATOM   2102  CA  LYS A1085     -32.456 -81.334 -35.671  1.00 93.74           C  
ANISOU 2102  CA  LYS A1085    12255  11151  12210    -52  -1477  -1563       C  
ATOM   2103  C   LYS A1085     -31.308 -82.129 -35.055  1.00 93.62           C  
ANISOU 2103  C   LYS A1085    12300  10716  12554   -142  -1453  -1414       C  
ATOM   2104  O   LYS A1085     -31.038 -82.013 -33.854  1.00 93.58           O  
ANISOU 2104  O   LYS A1085    12268  10676  12611   -219  -1410  -1096       O  
ATOM   2105  CB  LYS A1085     -33.694 -82.237 -35.851  1.00 95.43           C  
ANISOU 2105  CB  LYS A1085    12274  11422  12563   -288  -1624  -1707       C  
ATOM   2106  CG  LYS A1085     -35.024 -81.505 -35.722  1.00 99.29           C  
ANISOU 2106  CG  LYS A1085    12611  12378  12737   -294  -1652  -1663       C  
ATOM   2107  CD  LYS A1085     -35.559 -81.011 -37.065  1.00103.41           C  
ANISOU 2107  CD  LYS A1085    13159  13214  12919    -71  -1663  -1953       C  
ATOM   2108  CE  LYS A1085     -36.901 -80.330 -36.925  1.00106.35           C  
ANISOU 2108  CE  LYS A1085    13364  14053  12989    -48  -1706  -1922       C  
ATOM   2109  NZ  LYS A1085     -37.422 -79.885 -38.241  1.00108.06           N  
ANISOU 2109  NZ  LYS A1085    13588  14580  12892    167  -1734  -2180       N  
ATOM   2110  N   GLU A1086     -30.626 -82.923 -35.885  1.00 93.43           N  
ANISOU 2110  N   GLU A1086    12337  10413  12750   -106  -1488  -1666       N  
ATOM   2111  CA  GLU A1086     -29.512 -83.721 -35.407  1.00 93.85           C  
ANISOU 2111  CA  GLU A1086    12442  10053  13163   -149  -1484  -1560       C  
ATOM   2112  C   GLU A1086     -28.327 -82.848 -35.030  1.00 93.74           C  
ANISOU 2112  C   GLU A1086    12565  10067  12984     35  -1328  -1373       C  
ATOM   2113  O   GLU A1086     -27.628 -83.169 -34.072  1.00 93.98           O  
ANISOU 2113  O   GLU A1086    12600   9879  13228    -32  -1303  -1120       O  
ATOM   2114  CB  GLU A1086     -29.116 -84.802 -36.413  1.00 96.35           C  
ANISOU 2114  CB  GLU A1086    12761  10064  13782   -125  -1591  -1940       C  
ATOM   2115  CG  GLU A1086     -28.252 -85.904 -35.818  1.00101.38           C  
ANISOU 2115  CG  GLU A1086    13409  10207  14903   -210  -1650  -1814       C  
ATOM   2116  CD  GLU A1086     -28.811 -87.313 -35.914  1.00108.11           C  
ANISOU 2116  CD  GLU A1086    14168  10648  16260   -385  -1869  -2039       C  
ATOM   2117  OE1 GLU A1086     -29.919 -87.479 -36.474  1.00109.84           O  
ANISOU 2117  OE1 GLU A1086    14294  10987  16455   -490  -1981  -2291       O  
ATOM   2118  OE2 GLU A1086     -28.135 -88.252 -35.432  1.00109.79           O  
ANISOU 2118  OE2 GLU A1086    14396  10404  16916   -416  -1947  -1966       O  
ATOM   2119  N   ALA A1087     -28.120 -81.727 -35.739  1.00 93.11           N  
ANISOU 2119  N   ALA A1087    12580  10266  12533    248  -1234  -1460       N  
ATOM   2120  CA  ALA A1087     -27.035 -80.807 -35.409  1.00 92.91           C  
ANISOU 2120  CA  ALA A1087    12673  10265  12362    389  -1104  -1270       C  
ATOM   2121  C   ALA A1087     -27.309 -80.084 -34.091  1.00 92.26           C  
ANISOU 2121  C   ALA A1087    12568  10282  12206    324  -1073   -953       C  
ATOM   2122  O   ALA A1087     -26.390 -79.904 -33.296  1.00 92.31           O  
ANISOU 2122  O   ALA A1087    12611  10177  12286    327  -1008   -752       O  
ATOM   2123  CB  ALA A1087     -26.828 -79.798 -36.524  1.00 93.09           C  
ANISOU 2123  CB  ALA A1087    12782  10548  12040    596  -1040  -1391       C  
ATOM   2124  N   GLN A1088     -28.565 -79.694 -33.846  1.00 91.47           N  
ANISOU 2124  N   GLN A1088    12378  10428  11948    276  -1127   -935       N  
ATOM   2125  CA  GLN A1088     -28.925 -79.027 -32.599  1.00 91.24           C  
ANISOU 2125  CA  GLN A1088    12280  10573  11813    246  -1114   -700       C  
ATOM   2126  C   GLN A1088     -28.765 -79.983 -31.424  1.00 91.08           C  
ANISOU 2126  C   GLN A1088    12133  10418  12056     36  -1133   -465       C  
ATOM   2127  O   GLN A1088     -28.281 -79.570 -30.374  1.00 91.19           O  
ANISOU 2127  O   GLN A1088    12125  10490  12034     46  -1083   -257       O  
ATOM   2128  CB  GLN A1088     -30.361 -78.490 -32.657  1.00 92.24           C  
ANISOU 2128  CB  GLN A1088    12295  11043  11707    263  -1180   -769       C  
ATOM   2129  CG  GLN A1088     -30.556 -77.345 -33.639  1.00 94.04           C  
ANISOU 2129  CG  GLN A1088    12639  11437  11654    499  -1173   -917       C  
ATOM   2130  CD  GLN A1088     -31.966 -76.805 -33.627  1.00 96.70           C  
ANISOU 2130  CD  GLN A1088    12853  12126  11762    556  -1247   -974       C  
ATOM   2131  OE1 GLN A1088     -32.766 -77.059 -32.719  1.00 97.89           O  
ANISOU 2131  OE1 GLN A1088    12820  12464  11909    435  -1288   -893       O  
ATOM   2132  NE2 GLN A1088     -32.290 -75.997 -34.613  1.00 96.79           N  
ANISOU 2132  NE2 GLN A1088    12942  12279  11556    754  -1270  -1092       N  
ATOM   2133  N   ALA A1089     -29.141 -81.263 -31.607  1.00 90.68           N  
ANISOU 2133  N   ALA A1089    11988  10183  12285   -158  -1222   -492       N  
ATOM   2134  CA  ALA A1089     -28.998 -82.275 -30.564  1.00 90.63           C  
ANISOU 2134  CA  ALA A1089    11847  10004  12583   -385  -1270   -206       C  
ATOM   2135  C   ALA A1089     -27.518 -82.545 -30.290  1.00 90.51           C  
ANISOU 2135  C   ALA A1089    11939   9690  12762   -315  -1208    -97       C  
ATOM   2136  O   ALA A1089     -27.128 -82.679 -29.129  1.00 90.58           O  
ANISOU 2136  O   ALA A1089    11858   9718  12841   -399  -1188    219       O  
ATOM   2137  CB  ALA A1089     -29.704 -83.555 -30.974  1.00 90.71           C  
ANISOU 2137  CB  ALA A1089    11756   9797  12915   -607  -1414   -285       C  
ATOM   2138  N   ALA A1090     -26.689 -82.588 -31.351  1.00 90.02           N  
ANISOU 2138  N   ALA A1090    12037   9417  12749   -148  -1176   -357       N  
ATOM   2139  CA  ALA A1090     -25.243 -82.785 -31.210  1.00 89.99           C  
ANISOU 2139  CA  ALA A1090    12121   9179  12891    -47  -1111   -295       C  
ATOM   2140  C   ALA A1090     -24.601 -81.596 -30.498  1.00 89.32           C  
ANISOU 2140  C   ALA A1090    12085   9314  12537     62   -989   -125       C  
ATOM   2141  O   ALA A1090     -23.681 -81.784 -29.705  1.00 89.57           O  
ANISOU 2141  O   ALA A1090    12100   9251  12682     56   -949     80       O  
ATOM   2142  CB  ALA A1090     -24.593 -82.976 -32.571  1.00 90.21           C  
ANISOU 2142  CB  ALA A1090    12263   9057  12954    125  -1102   -644       C  
ATOM   2143  N   ALA A1091     -25.074 -80.379 -30.780  1.00 88.29           N  
ANISOU 2143  N   ALA A1091    12009   9462  12075    166   -949   -216       N  
ATOM   2144  CA  ALA A1091     -24.544 -79.186 -30.134  1.00 87.90           C  
ANISOU 2144  CA  ALA A1091    12006   9576  11815    265   -871   -100       C  
ATOM   2145  C   ALA A1091     -24.849 -79.191 -28.637  1.00 87.45           C  
ANISOU 2145  C   ALA A1091    11789   9686  11751    154   -886    154       C  
ATOM   2146  O   ALA A1091     -24.005 -78.799 -27.833  1.00 87.50           O  
ANISOU 2146  O   ALA A1091    11787   9709  11749    181   -834    298       O  
ATOM   2147  CB  ALA A1091     -25.120 -77.943 -30.783  1.00 87.97           C  
ANISOU 2147  CB  ALA A1091    12097   9792  11537    400   -871   -247       C  
ATOM   2148  N   GLU A1092     -26.032 -79.688 -28.263  1.00 86.88           N  
ANISOU 2148  N   GLU A1092    11557   9779  11676     17   -960    218       N  
ATOM   2149  CA  GLU A1092     -26.440 -79.769 -26.869  1.00 86.73           C  
ANISOU 2149  CA  GLU A1092    11322  10033  11598   -102   -978    479       C  
ATOM   2150  C   GLU A1092     -25.611 -80.755 -26.046  1.00 85.65           C  
ANISOU 2150  C   GLU A1092    11090   9727  11724   -241   -978    781       C  
ATOM   2151  O   GLU A1092     -25.771 -80.776 -24.830  1.00 85.72           O  
ANISOU 2151  O   GLU A1092    10891  10019  11658   -342   -987   1046       O  
ATOM   2152  CB  GLU A1092     -27.943 -80.052 -26.736  1.00 89.71           C  
ANISOU 2152  CB  GLU A1092    11513  10692  11882   -230  -1057    494       C  
ATOM   2153  CG  GLU A1092     -28.805 -78.809 -26.912  1.00 95.48           C  
ANISOU 2153  CG  GLU A1092    12257  11743  12276    -55  -1063    269       C  
ATOM   2154  CD  GLU A1092     -30.075 -79.042 -27.709  1.00103.68           C  
ANISOU 2154  CD  GLU A1092    13221  12903  13271   -126  -1138    139       C  
ATOM   2155  OE1 GLU A1092     -30.683 -80.126 -27.554  1.00106.07           O  
ANISOU 2155  OE1 GLU A1092    13335  13247  13719   -372  -1198    309       O  
ATOM   2156  OE2 GLU A1092     -30.454 -78.150 -28.503  1.00105.88           O  
ANISOU 2156  OE2 GLU A1092    13617  13232  13381     49  -1147   -109       O  
ATOM   2157  N   GLN A1093     -24.708 -81.534 -26.672  1.00 84.44           N  
ANISOU 2157  N   GLN A1093    11063   9160  11861   -229   -977    745       N  
ATOM   2158  CA  GLN A1093     -23.823 -82.419 -25.923  1.00 83.83           C  
ANISOU 2158  CA  GLN A1093    10908   8885  12058   -315   -990   1033       C  
ATOM   2159  C   GLN A1093     -22.908 -81.614 -24.986  1.00 83.15           C  
ANISOU 2159  C   GLN A1093    10785   9028  11780   -223   -901   1180       C  
ATOM   2160  O   GLN A1093     -22.586 -82.081 -23.891  1.00 83.23           O  
ANISOU 2160  O   GLN A1093    10626   9135  11865   -323   -916   1512       O  
ATOM   2161  CB  GLN A1093     -23.005 -83.315 -26.865  1.00 84.88           C  
ANISOU 2161  CB  GLN A1093    11187   8546  12516   -245  -1014    873       C  
ATOM   2162  CG  GLN A1093     -23.849 -84.306 -27.654  1.00 87.27           C  
ANISOU 2162  CG  GLN A1093    11482   8588  13088   -362  -1140    733       C  
ATOM   2163  CD  GLN A1093     -24.633 -85.232 -26.766  1.00 90.72           C  
ANISOU 2163  CD  GLN A1093    11734   8883  13854   -613  -1264   1100       C  
ATOM   2164  OE1 GLN A1093     -24.098 -86.176 -26.175  1.00 91.54           O  
ANISOU 2164  OE1 GLN A1093    11832   8610  14340   -634  -1335   1240       O  
ATOM   2165  NE2 GLN A1093     -25.926 -84.977 -26.658  1.00 91.54           N  
ANISOU 2165  NE2 GLN A1093    11661   9300  13819   -805  -1302   1288       N  
ATOM   2166  N   LEU A1094     -22.543 -80.385 -25.381  1.00 82.25           N  
ANISOU 2166  N   LEU A1094    10810   9023  11419    -47   -825    950       N  
ATOM   2167  CA  LEU A1094     -21.713 -79.501 -24.572  1.00 81.71           C  
ANISOU 2167  CA  LEU A1094    10714   9158  11176     37   -762   1014       C  
ATOM   2168  C   LEU A1094     -22.339 -79.161 -23.203  1.00 81.91           C  
ANISOU 2168  C   LEU A1094    10501   9643  10978    -24   -786   1178       C  
ATOM   2169  O   LEU A1094     -21.619 -78.752 -22.295  1.00 81.83           O  
ANISOU 2169  O   LEU A1094    10403   9834  10855     17   -754   1265       O  
ATOM   2170  CB  LEU A1094     -21.390 -78.234 -25.373  1.00 81.31           C  
ANISOU 2170  CB  LEU A1094    10861   9071  10961    202   -712    738       C  
ATOM   2171  CG  LEU A1094     -20.638 -78.467 -26.690  1.00 81.98           C  
ANISOU 2171  CG  LEU A1094    11125   8830  11192    275   -668    603       C  
ATOM   2172  CD1 LEU A1094     -20.847 -77.337 -27.655  1.00 82.42           C  
ANISOU 2172  CD1 LEU A1094    11343   8895  11076    387   -651    375       C  
ATOM   2173  CD2 LEU A1094     -19.173 -78.667 -26.452  1.00 82.30           C  
ANISOU 2173  CD2 LEU A1094    11163   8783  11324    310   -607    714       C  
ATOM   2174  N   LYS A1095     -23.665 -79.358 -23.046  1.00 82.17           N  
ANISOU 2174  N   LYS A1095    10398   9893  10931   -121   -846   1211       N  
ATOM   2175  CA  LYS A1095     -24.414 -79.107 -21.806  1.00 82.99           C  
ANISOU 2175  CA  LYS A1095    10217  10534  10781   -177   -873   1358       C  
ATOM   2176  C   LYS A1095     -24.404 -80.287 -20.812  1.00 84.18           C  
ANISOU 2176  C   LYS A1095    10104  10824  11056   -391   -902   1816       C  
ATOM   2177  O   LYS A1095     -24.819 -80.118 -19.662  1.00 84.25           O  
ANISOU 2177  O   LYS A1095     9826  11369  10817   -438   -911   1998       O  
ATOM   2178  CB  LYS A1095     -25.872 -78.770 -22.131  1.00 84.07           C  
ANISOU 2178  CB  LYS A1095    10292  10905  10747   -180   -925   1194       C  
ATOM   2179  CG  LYS A1095     -26.065 -77.425 -22.798  1.00 87.21           C  
ANISOU 2179  CG  LYS A1095    10893  11261  10982     46   -922    801       C  
ATOM   2180  CD  LYS A1095     -26.943 -76.523 -21.956  1.00 91.11           C  
ANISOU 2180  CD  LYS A1095    11221  12255  11142    191   -955    652       C  
ATOM   2181  CE  LYS A1095     -27.993 -75.844 -22.789  1.00 94.60           C  
ANISOU 2181  CE  LYS A1095    11624  12897  11422    260  -1016    452       C  
ATOM   2182  NZ  LYS A1095     -28.562 -74.661 -22.094  1.00 96.87           N  
ANISOU 2182  NZ  LYS A1095    11827  13550  11427    499  -1069    182       N  
ATOM   2183  N   THR A1096     -23.965 -81.476 -21.252  1.00 84.82           N  
ANISOU 2183  N   THR A1096    10261  10444  11523   -511   -932   2006       N  
ATOM   2184  CA  THR A1096     -23.919 -82.686 -20.418  1.00 85.73           C  
ANISOU 2184  CA  THR A1096    10152  10565  11854   -724   -991   2496       C  
ATOM   2185  C   THR A1096     -23.046 -82.496 -19.170  1.00 86.71           C  
ANISOU 2185  C   THR A1096    10101  11022  11823   -681   -945   2756       C  
ATOM   2186  O   THR A1096     -22.198 -81.611 -19.152  1.00 86.81           O  
ANISOU 2186  O   THR A1096    10232  11070  11683   -488   -870   2520       O  
ATOM   2187  CB  THR A1096     -23.393 -83.897 -21.225  1.00 86.76           C  
ANISOU 2187  CB  THR A1096    10448  10026  12492   -789  -1058   2557       C  
ATOM   2188  OG1 THR A1096     -23.831 -83.842 -22.584  1.00 87.51           O  
ANISOU 2188  OG1 THR A1096    10751   9809  12690   -750  -1084   2178       O  
ATOM   2189  CG2 THR A1096     -23.813 -85.225 -20.615  1.00 87.27           C  
ANISOU 2189  CG2 THR A1096    10289  10001  12870  -1058  -1178   3065       C  
ATOM   2190  N   THR A1097     -23.231 -83.337 -18.135  1.00 87.21           N  
ANISOU 2190  N   THR A1097     9865  11340  11930   -875   -998   3264       N  
ATOM   2191  CA  THR A1097     -22.404 -83.292 -16.929  1.00 88.05           C  
ANISOU 2191  CA  THR A1097     9761  11815  11878   -844   -964   3560       C  
ATOM   2192  C   THR A1097     -20.930 -83.559 -17.271  1.00 88.97           C  
ANISOU 2192  C   THR A1097    10084  11454  12265   -710   -934   3533       C  
ATOM   2193  O   THR A1097     -20.047 -82.957 -16.658  1.00 89.33           O  
ANISOU 2193  O   THR A1097    10063  11778  12101   -584   -873   3522       O  
ATOM   2194  CB  THR A1097     -22.890 -84.329 -15.932  1.00 88.99           C  
ANISOU 2194  CB  THR A1097     9523  12235  12055  -1103  -1043   4190       C  
ATOM   2195  OG1 THR A1097     -22.875 -85.610 -16.569  1.00 89.82           O  
ANISOU 2195  OG1 THR A1097     9743  11672  12713  -1265  -1149   4434       O  
ATOM   2196  CG2 THR A1097     -24.270 -84.005 -15.390  1.00 89.22           C  
ANISOU 2196  CG2 THR A1097     9254  12927  11718  -1232  -1057   4259       C  
ATOM   2197  N   ARG A1098     -20.669 -84.432 -18.268  1.00 89.13           N  
ANISOU 2197  N   ARG A1098    10337  10793  12734   -720   -985   3479       N  
ATOM   2198  CA  ARG A1098     -19.315 -84.770 -18.726  1.00 89.64           C  
ANISOU 2198  CA  ARG A1098    10584  10417  13060   -564   -964   3411       C  
ATOM   2199  C   ARG A1098     -18.616 -83.505 -19.229  1.00 89.17           C  
ANISOU 2199  C   ARG A1098    10708  10449  12722   -345   -844   2954       C  
ATOM   2200  O   ARG A1098     -17.492 -83.212 -18.817  1.00 89.17           O  
ANISOU 2200  O   ARG A1098    10668  10590  12620   -238   -787   2992       O  
ATOM   2201  CB  ARG A1098     -19.355 -85.833 -19.850  1.00 91.76           C  
ANISOU 2201  CB  ARG A1098    11055   9983  13826   -578  -1056   3309       C  
ATOM   2202  CG  ARG A1098     -20.504 -86.850 -19.749  1.00 95.95           C  
ANISOU 2202  CG  ARG A1098    11462  10349  14645   -838  -1202   3602       C  
ATOM   2203  CD  ARG A1098     -20.842 -87.480 -21.092  1.00 99.63           C  
ANISOU 2203  CD  ARG A1098    12152  10180  15523   -828  -1296   3292       C  
ATOM   2204  NE  ARG A1098     -21.116 -86.473 -22.122  1.00102.65           N  
ANISOU 2204  NE  ARG A1098    12740  10612  15649   -694  -1207   2739       N  
ATOM   2205  CZ  ARG A1098     -21.758 -86.718 -23.260  1.00104.97           C  
ANISOU 2205  CZ  ARG A1098    13141  10653  16089   -748  -1276   2457       C  
ATOM   2206  NH1 ARG A1098     -21.960 -85.745 -24.138  1.00104.44           N  
ANISOU 2206  NH1 ARG A1098    13239  10692  15750   -610  -1192   2006       N  
ATOM   2207  NH2 ARG A1098     -22.221 -87.935 -23.520  1.00105.32           N  
ANISOU 2207  NH2 ARG A1098    13115  10339  16564   -951  -1445   2638       N  
ATOM   2208  N   ASN A1099     -19.309 -82.727 -20.076  1.00 88.55           N  
ANISOU 2208  N   ASN A1099    10805  10330  12511   -296   -816   2554       N  
ATOM   2209  CA  ASN A1099     -18.760 -81.490 -20.625  1.00 88.35           C  
ANISOU 2209  CA  ASN A1099    10958  10347  12264   -120   -728   2161       C  
ATOM   2210  C   ASN A1099     -18.850 -80.293 -19.681  1.00 88.26           C  
ANISOU 2210  C   ASN A1099    10800  10874  11859    -78   -697   2097       C  
ATOM   2211  O   ASN A1099     -18.150 -79.310 -19.879  1.00 88.31           O  
ANISOU 2211  O   ASN A1099    10915  10907  11733     46   -648   1849       O  
ATOM   2212  CB  ASN A1099     -19.383 -81.190 -21.958  1.00 88.95           C  
ANISOU 2212  CB  ASN A1099    11268  10158  12371    -69   -727   1803       C  
ATOM   2213  CG  ASN A1099     -18.961 -82.228 -22.946  1.00 91.23           C  
ANISOU 2213  CG  ASN A1099    11675   9954  13035    -78   -770   1791       C  
ATOM   2214  OD1 ASN A1099     -19.686 -83.175 -23.239  1.00 92.23           O  
ANISOU 2214  OD1 ASN A1099    11762   9922  13357   -204   -858   1869       O  
ATOM   2215  ND2 ASN A1099     -17.742 -82.108 -23.430  1.00 91.68           N  
ANISOU 2215  ND2 ASN A1099    11843   9777  13214     53   -724   1700       N  
ATOM   2216  N   ALA A1100     -19.679 -80.375 -18.650  1.00 88.07           N  
ANISOU 2216  N   ALA A1100    10508  11298  11658   -182   -738   2316       N  
ATOM   2217  CA  ALA A1100     -19.777 -79.340 -17.636  1.00 88.55           C  
ANISOU 2217  CA  ALA A1100    10366  11943  11337   -118   -728   2235       C  
ATOM   2218  C   ALA A1100     -18.531 -79.408 -16.770  1.00 88.78           C  
ANISOU 2218  C   ALA A1100    10268  12127  11337    -84   -697   2420       C  
ATOM   2219  O   ALA A1100     -17.998 -78.352 -16.432  1.00 89.02           O  
ANISOU 2219  O   ALA A1100    10291  12375  11157     33   -675   2164       O  
ATOM   2220  CB  ALA A1100     -21.011 -79.556 -16.777  1.00 88.88           C  
ANISOU 2220  CB  ALA A1100    10093  12508  11171   -240   -777   2457       C  
ATOM   2221  N   TYR A1101     -18.044 -80.635 -16.416  1.00 88.66           N  
ANISOU 2221  N   TYR A1101    10151  11977  11558   -181   -712   2856       N  
ATOM   2222  CA  TYR A1101     -16.811 -80.714 -15.631  1.00 89.06           C  
ANISOU 2222  CA  TYR A1101    10074  12192  11573   -126   -684   3036       C  
ATOM   2223  C   TYR A1101     -15.562 -80.414 -16.490  1.00 87.83           C  
ANISOU 2223  C   TYR A1101    10191  11581  11601      4   -629   2788       C  
ATOM   2224  O   TYR A1101     -14.570 -79.913 -15.957  1.00 87.77           O  
ANISOU 2224  O   TYR A1101    10108  11777  11463     79   -594   2751       O  
ATOM   2225  CB  TYR A1101     -16.645 -81.986 -14.797  1.00 90.14           C  
ANISOU 2225  CB  TYR A1101     9946  12464  11837   -246   -733   3627       C  
ATOM   2226  CG  TYR A1101     -15.507 -81.790 -13.814  1.00 92.23           C  
ANISOU 2226  CG  TYR A1101    10022  13101  11920   -160   -702   3749       C  
ATOM   2227  CD1 TYR A1101     -15.548 -80.768 -12.871  1.00 93.68           C  
ANISOU 2227  CD1 TYR A1101     9991  13946  11658   -104   -681   3564       C  
ATOM   2228  CD2 TYR A1101     -14.323 -82.504 -13.941  1.00 93.62           C  
ANISOU 2228  CD2 TYR A1101    10256  12948  12370    -98   -699   3943       C  
ATOM   2229  CE1 TYR A1101     -14.463 -80.503 -12.042  1.00 94.93           C  
ANISOU 2229  CE1 TYR A1101     9985  14443  11642    -19   -658   3590       C  
ATOM   2230  CE2 TYR A1101     -13.232 -82.248 -13.117  1.00 94.93           C  
ANISOU 2230  CE2 TYR A1101    10256  13460  12353     -7   -667   4003       C  
ATOM   2231  CZ  TYR A1101     -13.307 -81.251 -12.162  1.00 96.10           C  
ANISOU 2231  CZ  TYR A1101    10183  14280  12050     18   -646   3832       C  
ATOM   2232  OH  TYR A1101     -12.235 -81.017 -11.330  1.00 97.97           O  
ANISOU 2232  OH  TYR A1101    10228  14895  12101     96   -627   3879       O  
ATOM   2233  N   ILE A1102     -15.642 -80.588 -17.824  1.00 86.64           N  
ANISOU 2233  N   ILE A1102    10329  10900  11692     32   -620   2573       N  
ATOM   2234  CA  ILE A1102     -14.550 -80.174 -18.708  1.00 85.84           C  
ANISOU 2234  CA  ILE A1102    10450  10483  11681    154   -558   2312       C  
ATOM   2235  C   ILE A1102     -14.437 -78.635 -18.643  1.00 84.91           C  
ANISOU 2235  C   ILE A1102    10381  10608  11272    210   -526   1971       C  
ATOM   2236  O   ILE A1102     -13.342 -78.116 -18.465  1.00 85.25           O  
ANISOU 2236  O   ILE A1102    10415  10721  11254    263   -489   1898       O  
ATOM   2237  CB  ILE A1102     -14.772 -80.688 -20.145  1.00 86.23           C  
ANISOU 2237  CB  ILE A1102    10751  10017  11996    183   -561   2140       C  
ATOM   2238  CG1 ILE A1102     -14.577 -82.204 -20.189  1.00 87.13           C  
ANISOU 2238  CG1 ILE A1102    10819   9812  12473    157   -624   2423       C  
ATOM   2239  CG2 ILE A1102     -13.847 -79.989 -21.132  1.00 86.66           C  
ANISOU 2239  CG2 ILE A1102    10999   9894  12034    300   -487   1845       C  
ATOM   2240  CD1 ILE A1102     -14.855 -82.834 -21.520  1.00 88.44           C  
ANISOU 2240  CD1 ILE A1102    11190   9504  12909    195   -654   2209       C  
ATOM   2241  N   GLN A1103     -15.578 -77.925 -18.678  1.00 83.51           N  
ANISOU 2241  N   GLN A1103    10223  10579  10927    196   -561   1779       N  
ATOM   2242  CA  GLN A1103     -15.628 -76.469 -18.570  1.00 82.56           C  
ANISOU 2242  CA  GLN A1103    10146  10635  10590    263   -577   1446       C  
ATOM   2243  C   GLN A1103     -15.077 -76.012 -17.233  1.00 81.59           C  
ANISOU 2243  C   GLN A1103     9768  10982  10249    279   -596   1471       C  
ATOM   2244  O   GLN A1103     -14.303 -75.073 -17.195  1.00 81.58           O  
ANISOU 2244  O   GLN A1103     9813  10992  10192    325   -601   1247       O  
ATOM   2245  CB  GLN A1103     -17.073 -75.980 -18.707  1.00 83.77           C  
ANISOU 2245  CB  GLN A1103    10313  10897  10616    274   -633   1272       C  
ATOM   2246  CG  GLN A1103     -17.341 -75.123 -19.917  1.00 86.21           C  
ANISOU 2246  CG  GLN A1103    10866  10966  10923    357   -655    925       C  
ATOM   2247  CD  GLN A1103     -18.805 -74.824 -19.954  1.00 89.35           C  
ANISOU 2247  CD  GLN A1103    11254  11471  11223    379   -711    817       C  
ATOM   2248  OE1 GLN A1103     -19.356 -74.255 -19.009  1.00 90.38           O  
ANISOU 2248  OE1 GLN A1103    11188  12016  11134    424   -770    725       O  
ATOM   2249  NE2 GLN A1103     -19.473 -75.235 -21.028  1.00 89.59           N  
ANISOU 2249  NE2 GLN A1103    11459  11187  11393    356   -696    816       N  
ATOM   2250  N   LYS A1104     -15.462 -76.677 -16.140  1.00 80.78           N  
ANISOU 2250  N   LYS A1104     9377  11296  10021    228   -615   1752       N  
ATOM   2251  CA  LYS A1104     -14.985 -76.329 -14.809  1.00 80.75           C  
ANISOU 2251  CA  LYS A1104     9073  11852   9757    252   -636   1790       C  
ATOM   2252  C   LYS A1104     -13.484 -76.547 -14.696  1.00 80.50           C  
ANISOU 2252  C   LYS A1104     9029  11734   9823    262   -591   1916       C  
ATOM   2253  O   LYS A1104     -12.799 -75.732 -14.093  1.00 80.76           O  
ANISOU 2253  O   LYS A1104     8939  12064   9682    305   -609   1738       O  
ATOM   2254  CB  LYS A1104     -15.723 -77.140 -13.734  1.00 82.71           C  
ANISOU 2254  CB  LYS A1104     8980  12617   9831    178   -661   2156       C  
ATOM   2255  CG  LYS A1104     -17.136 -76.637 -13.442  1.00 86.86           C  
ANISOU 2255  CG  LYS A1104     9359  13563  10078    203   -716   1956       C  
ATOM   2256  CD  LYS A1104     -17.740 -77.294 -12.175  1.00 91.07           C  
ANISOU 2256  CD  LYS A1104     9462  14789  10353    116   -736   2359       C  
ATOM   2257  CE  LYS A1104     -18.858 -76.479 -11.538  1.00 94.05           C  
ANISOU 2257  CE  LYS A1104     9572  15851  10313    206   -791   2069       C  
ATOM   2258  NZ  LYS A1104     -19.344 -77.067 -10.256  1.00 95.23           N  
ANISOU 2258  NZ  LYS A1104     9248  16785  10149    111   -802   2492       N  
ATOM   2259  N   TYR A1105     -12.971 -77.631 -15.284  1.00 79.76           N  
ANISOU 2259  N   TYR A1105     9045  11247  10013    234   -547   2190       N  
ATOM   2260  CA  TYR A1105     -11.550 -77.918 -15.252  1.00 79.48           C  
ANISOU 2260  CA  TYR A1105     8991  11131  10079    272   -505   2307       C  
ATOM   2261  C   TYR A1105     -10.780 -76.859 -16.022  1.00 78.61           C  
ANISOU 2261  C   TYR A1105     9088  10793   9987    311   -473   1937       C  
ATOM   2262  O   TYR A1105      -9.770 -76.372 -15.529  1.00 78.74           O  
ANISOU 2262  O   TYR A1105     8994  11020   9903    325   -466   1875       O  
ATOM   2263  CB  TYR A1105     -11.256 -79.317 -15.813  1.00 80.02           C  
ANISOU 2263  CB  TYR A1105     9131  10793  10480    275   -491   2632       C  
ATOM   2264  CG  TYR A1105      -9.775 -79.608 -15.911  1.00 81.78           C  
ANISOU 2264  CG  TYR A1105     9344  10911  10817    357   -449   2703       C  
ATOM   2265  CD1 TYR A1105      -8.975 -79.635 -14.777  1.00 83.19           C  
ANISOU 2265  CD1 TYR A1105     9252  11526  10832    378   -453   2896       C  
ATOM   2266  CD2 TYR A1105      -9.166 -79.810 -17.141  1.00 83.05           C  
ANISOU 2266  CD2 TYR A1105     9739  10609  11209    428   -405   2554       C  
ATOM   2267  CE1 TYR A1105      -7.611 -79.892 -14.859  1.00 84.31           C  
ANISOU 2267  CE1 TYR A1105     9361  11611  11061    464   -417   2958       C  
ATOM   2268  CE2 TYR A1105      -7.798 -80.051 -17.240  1.00 84.21           C  
ANISOU 2268  CE2 TYR A1105     9844  10724  11428    521   -364   2598       C  
ATOM   2269  CZ  TYR A1105      -7.022 -80.092 -16.094  1.00 85.36           C  
ANISOU 2269  CZ  TYR A1105     9726  11278  11429    538   -371   2803       C  
ATOM   2270  OH  TYR A1105      -5.666 -80.336 -16.173  1.00 86.97           O  
ANISOU 2270  OH  TYR A1105     9866  11489  11691    640   -333   2848       O  
ATOM   2271  N   LEU A1106     -11.256 -76.492 -17.215  1.00 77.63           N  
ANISOU 2271  N   LEU A1106     9242  10269   9984    314   -462   1714       N  
ATOM   2272  CA  LEU A1106     -10.573 -75.512 -18.055  1.00 77.01           C  
ANISOU 2272  CA  LEU A1106     9356   9965   9940    321   -440   1440       C  
ATOM   2273  C   LEU A1106     -10.671 -74.093 -17.522  1.00 77.33           C  
ANISOU 2273  C   LEU A1106     9356  10223   9804    306   -513   1140       C  
ATOM   2274  O   LEU A1106      -9.680 -73.376 -17.559  1.00 77.41           O  
ANISOU 2274  O   LEU A1106     9374  10219   9818    276   -515   1020       O  
ATOM   2275  CB  LEU A1106     -11.042 -75.602 -19.503  1.00 76.37           C  
ANISOU 2275  CB  LEU A1106     9551   9449  10019    332   -412   1338       C  
ATOM   2276  CG  LEU A1106     -10.942 -76.987 -20.110  1.00 76.76           C  
ANISOU 2276  CG  LEU A1106     9645   9243  10277    367   -370   1537       C  
ATOM   2277  CD1 LEU A1106     -11.672 -77.059 -21.414  1.00 77.31           C  
ANISOU 2277  CD1 LEU A1106     9943   8989  10444    383   -364   1383       C  
ATOM   2278  CD2 LEU A1106      -9.521 -77.451 -20.203  1.00 76.87           C  
ANISOU 2278  CD2 LEU A1106     9600   9222  10386    419   -314   1654       C  
ATOM   2279  N   GLU A 235     -11.837 -73.686 -17.005  1.00 77.45           N  
ANISOU 2279  N   GLU A 235     6526   7910  14992   -107    310  -2242       N  
ATOM   2280  CA  GLU A 235     -11.992 -72.357 -16.407  1.00 78.08           C  
ANISOU 2280  CA  GLU A 235     6791   8094  14784    -94    298  -2040       C  
ATOM   2281  C   GLU A 235     -11.251 -72.269 -15.061  1.00 78.67           C  
ANISOU 2281  C   GLU A 235     6988   8032  14873    -68    283  -1800       C  
ATOM   2282  O   GLU A 235     -10.883 -71.177 -14.643  1.00 78.71           O  
ANISOU 2282  O   GLU A 235     7130   8129  14646    -54    263  -1663       O  
ATOM   2283  CB  GLU A 235     -13.471 -71.979 -16.251  1.00 80.33           C  
ANISOU 2283  CB  GLU A 235     7112   8415  14993   -107    328  -1993       C  
ATOM   2284  CG  GLU A 235     -14.194 -71.791 -17.574  1.00 85.85           C  
ANISOU 2284  CG  GLU A 235     7720   9290  15609   -123    321  -2211       C  
ATOM   2285  CD  GLU A 235     -15.685 -72.076 -17.547  1.00 94.23           C  
ANISOU 2285  CD  GLU A 235     8733  10326  16745   -136    354  -2248       C  
ATOM   2286  OE1 GLU A 235     -16.238 -72.302 -16.445  1.00 95.94           O  
ANISOU 2286  OE1 GLU A 235     8969  10370  17116   -144    399  -2121       O  
ATOM   2287  OE2 GLU A 235     -16.302 -72.090 -18.636  1.00 97.07           O  
ANISOU 2287  OE2 GLU A 235     9034  10841  17008   -141    334  -2408       O  
ATOM   2288  N   ARG A 236     -11.030 -73.416 -14.388  1.00 79.12           N  
ANISOU 2288  N   ARG A 236     6996   7866  15202    -61    287  -1750       N  
ATOM   2289  CA  ARG A 236     -10.267 -73.504 -13.147  1.00 80.00           C  
ANISOU 2289  CA  ARG A 236     7211   7831  15355    -33    258  -1533       C  
ATOM   2290  C   ARG A 236      -8.794 -73.378 -13.497  1.00 79.85           C  
ANISOU 2290  C   ARG A 236     7165   7852  15323     -4    201  -1607       C  
ATOM   2291  O   ARG A 236      -8.092 -72.597 -12.867  1.00 80.03           O  
ANISOU 2291  O   ARG A 236     7309   7908  15191     20    168  -1460       O  
ATOM   2292  CB  ARG A 236     -10.528 -74.840 -12.431  1.00 82.32           C  
ANISOU 2292  CB  ARG A 236     7456   7866  15956    -39    273  -1467       C  
ATOM   2293  CG  ARG A 236      -9.690 -75.045 -11.186  1.00 87.13           C  
ANISOU 2293  CG  ARG A 236     8167   8314  16625     -6    225  -1250       C  
ATOM   2294  CD  ARG A 236     -10.077 -76.323 -10.478  1.00 92.27           C  
ANISOU 2294  CD  ARG A 236     8787   8705  17567    -18    240  -1167       C  
ATOM   2295  NE  ARG A 236      -9.296 -77.467 -10.955  1.00 96.77           N  
ANISOU 2295  NE  ARG A 236     9204   9135  18429      5    195  -1320       N  
ATOM   2296  CZ  ARG A 236      -9.819 -78.549 -11.523  1.00 99.39           C  
ANISOU 2296  CZ  ARG A 236     9381   9359  19026    -20    230  -1484       C  
ATOM   2297  NH1 ARG A 236     -11.134 -78.645 -11.700  1.00 98.95           N  
ANISOU 2297  NH1 ARG A 236     9301   9319  18977    -70    311  -1518       N  
ATOM   2298  NH2 ARG A 236      -9.035 -79.545 -11.917  1.00 99.16           N  
ANISOU 2298  NH2 ARG A 236     9210   9199  19269      4    184  -1626       N  
ATOM   2299  N   ILE A 237      -8.337 -74.100 -14.532  1.00 79.59           N  
ANISOU 2299  N   ILE A 237     6964   7827  15447    -12    195  -1850       N  
ATOM   2300  CA  ILE A 237      -6.963 -74.051 -15.010  1.00 79.91           C  
ANISOU 2300  CA  ILE A 237     6953   7919  15492      6    153  -1965       C  
ATOM   2301  C   ILE A 237      -6.572 -72.622 -15.412  1.00 80.06           C  
ANISOU 2301  C   ILE A 237     7074   8176  15170     -5    152  -1957       C  
ATOM   2302  O   ILE A 237      -5.454 -72.204 -15.124  1.00 80.34           O  
ANISOU 2302  O   ILE A 237     7158   8232  15137     17    117  -1912       O  
ATOM   2303  CB  ILE A 237      -6.731 -75.107 -16.127  1.00 80.50           C  
ANISOU 2303  CB  ILE A 237     6812   7966  15808    -11    159  -2256       C  
ATOM   2304  CG1 ILE A 237      -6.657 -76.519 -15.534  1.00 81.33           C  
ANISOU 2304  CG1 ILE A 237     6829   7796  16279     11    140  -2235       C  
ATOM   2305  CG2 ILE A 237      -5.480 -74.821 -16.944  1.00 81.07           C  
ANISOU 2305  CG2 ILE A 237     6819   8154  15831    -11    134  -2425       C  
ATOM   2306  CD1 ILE A 237      -5.518 -76.747 -14.550  1.00 82.57           C  
ANISOU 2306  CD1 ILE A 237     7031   7784  16557     65     68  -2093       C  
ATOM   2307  N   GLU A 238      -7.504 -71.846 -15.988  1.00 79.85           N  
ANISOU 2307  N   GLU A 238     7092   8316  14931    -35    186  -1979       N  
ATOM   2308  CA  GLU A 238      -7.221 -70.456 -16.363  1.00 80.32           C  
ANISOU 2308  CA  GLU A 238     7261   8590  14669    -47    184  -1955       C  
ATOM   2309  C   GLU A 238      -7.198 -69.460 -15.185  1.00 80.88           C  
ANISOU 2309  C   GLU A 238     7518   8655  14558    -22    169  -1690       C  
ATOM   2310  O   GLU A 238      -6.673 -68.350 -15.323  1.00 80.91           O  
ANISOU 2310  O   GLU A 238     7612   8800  14330    -26    161  -1655       O  
ATOM   2311  CB  GLU A 238      -8.204 -69.975 -17.431  1.00 82.05           C  
ANISOU 2311  CB  GLU A 238     7460   8984  14732    -83    208  -2075       C  
ATOM   2312  CG  GLU A 238      -7.972 -70.626 -18.776  1.00 86.60           C  
ANISOU 2312  CG  GLU A 238     7866   9635  15403   -116    220  -2361       C  
ATOM   2313  CD  GLU A 238      -9.152 -70.551 -19.722  1.00 93.41           C  
ANISOU 2313  CD  GLU A 238     8682  10634  16175   -145    234  -2493       C  
ATOM   2314  OE1 GLU A 238     -10.052 -69.707 -19.499  1.00 94.49           O  
ANISOU 2314  OE1 GLU A 238     8922  10818  16160   -136    230  -2366       O  
ATOM   2315  OE2 GLU A 238      -9.178 -71.344 -20.690  1.00 95.99           O  
ANISOU 2315  OE2 GLU A 238     8861  11024  16587   -176    245  -2737       O  
ATOM   2316  N   GLY A 239      -7.752 -69.865 -14.045  1.00 80.97           N  
ANISOU 2316  N   GLY A 239     7583   8505  14677     -1    171  -1511       N  
ATOM   2317  CA  GLY A 239      -7.844 -69.023 -12.863  1.00 81.58           C  
ANISOU 2317  CA  GLY A 239     7828   8571  14599     18    163  -1267       C  
ATOM   2318  C   GLY A 239      -8.809 -67.893 -13.139  1.00 82.27           C  
ANISOU 2318  C   GLY A 239     7998   8815  14445      0    188  -1233       C  
ATOM   2319  O   GLY A 239      -8.508 -66.737 -12.861  1.00 82.65           O  
ANISOU 2319  O   GLY A 239     8158   8977  14269      5    176  -1148       O  
ATOM   2320  N   LEU A 240      -9.961 -68.215 -13.740  1.00 82.27           N  
ANISOU 2320  N   LEU A 240     7933   8825  14502    -22    218  -1319       N  
ATOM   2321  CA  LEU A 240     -10.935 -67.207 -14.121  1.00 82.66           C  
ANISOU 2321  CA  LEU A 240     8041   9019  14346    -33    228  -1313       C  
ATOM   2322  C   LEU A 240     -11.564 -66.477 -12.935  1.00 82.96           C  
ANISOU 2322  C   LEU A 240     8214   9023  14283    -23    242  -1095       C  
ATOM   2323  O   LEU A 240     -11.384 -65.264 -12.849  1.00 83.19           O  
ANISOU 2323  O   LEU A 240     8355   9161  14094    -14    225  -1009       O  
ATOM   2324  CB  LEU A 240     -12.005 -67.780 -15.065  1.00 82.90           C  
ANISOU 2324  CB  LEU A 240     7950   9085  14463    -54    246  -1493       C  
ATOM   2325  CG  LEU A 240     -11.666 -67.680 -16.550  1.00 84.26           C  
ANISOU 2325  CG  LEU A 240     8048   9426  14541    -71    224  -1704       C  
ATOM   2326  CD1 LEU A 240     -12.701 -68.390 -17.398  1.00 84.51           C  
ANISOU 2326  CD1 LEU A 240     7945   9480  14685    -88    236  -1893       C  
ATOM   2327  CD2 LEU A 240     -11.517 -66.226 -16.978  1.00 85.01           C  
ANISOU 2327  CD2 LEU A 240     8269   9702  14327    -70    196  -1647       C  
ATOM   2328  N   ARG A 241     -12.268 -67.177 -12.016  1.00 82.79           N  
ANISOU 2328  N   ARG A 241     8187   8855  14415    -32    279  -1007       N  
ATOM   2329  CA  ARG A 241     -12.893 -66.491 -10.873  1.00 83.12           C  
ANISOU 2329  CA  ARG A 241     8353   8878  14350    -34    304   -813       C  
ATOM   2330  C   ARG A 241     -11.853 -65.812  -9.971  1.00 82.27           C  
ANISOU 2330  C   ARG A 241     8372   8772  14114    -11    276   -644       C  
ATOM   2331  O   ARG A 241     -12.132 -64.754  -9.399  1.00 82.46           O  
ANISOU 2331  O   ARG A 241     8506   8866  13959     -9    281   -527       O  
ATOM   2332  CB  ARG A 241     -13.806 -67.434 -10.057  1.00 85.43           C  
ANISOU 2332  CB  ARG A 241     8621   9009  14829    -62    361   -747       C  
ATOM   2333  CG  ARG A 241     -14.870 -66.703  -9.210  1.00 90.15           C  
ANISOU 2333  CG  ARG A 241     9316   9629  15308    -80    404   -613       C  
ATOM   2334  CD  ARG A 241     -14.703 -66.884  -7.699  1.00 95.05           C  
ANISOU 2334  CD  ARG A 241    10034  10115  15965    -97    437   -403       C  
ATOM   2335  NE  ARG A 241     -14.763 -68.290  -7.277  1.00 99.78           N  
ANISOU 2335  NE  ARG A 241    10568  10526  16817   -123    467   -395       N  
ATOM   2336  CZ  ARG A 241     -15.858 -68.890  -6.810  1.00103.21           C  
ANISOU 2336  CZ  ARG A 241    10974  10860  17381   -172    542   -379       C  
ATOM   2337  NH1 ARG A 241     -16.997 -68.216  -6.697  1.00103.26           N  
ANISOU 2337  NH1 ARG A 241    11001  10942  17292   -200    593   -380       N  
ATOM   2338  NH2 ARG A 241     -15.820 -70.167  -6.448  1.00103.31           N  
ANISOU 2338  NH2 ARG A 241    10932  10690  17630   -197    566   -366       N  
ATOM   2339  N   LYS A 242     -10.649 -66.405  -9.873  1.00 81.08           N  
ANISOU 2339  N   LYS A 242     8197   8551  14060      7    243   -649       N  
ATOM   2340  CA  LYS A 242      -9.564 -65.877  -9.047  1.00 80.45           C  
ANISOU 2340  CA  LYS A 242     8219   8468  13881     33    207   -511       C  
ATOM   2341  C   LYS A 242      -8.949 -64.598  -9.633  1.00 78.89           C  
ANISOU 2341  C   LYS A 242     8077   8448  13450     41    184   -545       C  
ATOM   2342  O   LYS A 242      -8.491 -63.735  -8.880  1.00 79.11           O  
ANISOU 2342  O   LYS A 242     8218   8514  13328     55    173   -409       O  
ATOM   2343  CB  LYS A 242      -8.512 -66.965  -8.769  1.00 82.97           C  
ANISOU 2343  CB  LYS A 242     8482   8647  14397     55    167   -519       C  
ATOM   2344  CG  LYS A 242      -9.137 -68.227  -8.164  1.00 87.85           C  
ANISOU 2344  CG  LYS A 242     9068   9069  15242     43    188   -449       C  
ATOM   2345  CD  LYS A 242      -8.108 -69.297  -7.829  1.00 92.91           C  
ANISOU 2345  CD  LYS A 242     9662   9550  16088     74    132   -438       C  
ATOM   2346  CE  LYS A 242      -8.768 -70.560  -7.328  1.00 96.67           C  
ANISOU 2346  CE  LYS A 242    10110   9822  16797     56    154   -367       C  
ATOM   2347  NZ  LYS A 242      -7.770 -71.557  -6.855  1.00 98.71           N  
ANISOU 2347  NZ  LYS A 242    10339   9907  17259     93     84   -328       N  
ATOM   2348  N   ARG A 243      -8.972 -64.455 -10.965  1.00 76.98           N  
ANISOU 2348  N   ARG A 243     7760   8318  13171     29    180   -724       N  
ATOM   2349  CA  ARG A 243      -8.473 -63.243 -11.602  1.00 75.71           C  
ANISOU 2349  CA  ARG A 243     7658   8323  12783     26    165   -754       C  
ATOM   2350  C   ARG A 243      -9.543 -62.153 -11.664  1.00 73.96           C  
ANISOU 2350  C   ARG A 243     7513   8202  12386     19    176   -703       C  
ATOM   2351  O   ARG A 243      -9.209 -60.979 -11.628  1.00 73.80           O  
ANISOU 2351  O   ARG A 243     7585   8282  12172     22    163   -646       O  
ATOM   2352  CB  ARG A 243      -7.832 -63.539 -12.958  1.00 77.26           C  
ANISOU 2352  CB  ARG A 243     7759   8604  12995      7    155   -956       C  
ATOM   2353  CG  ARG A 243      -6.384 -64.001 -12.769  1.00 80.90           C  
ANISOU 2353  CG  ARG A 243     8194   9013  13532     20    134   -975       C  
ATOM   2354  CD  ARG A 243      -5.895 -64.975 -13.814  1.00 84.10           C  
ANISOU 2354  CD  ARG A 243     8449   9405  14099      5    133  -1185       C  
ATOM   2355  NE  ARG A 243      -5.595 -64.302 -15.074  1.00 87.30           N  
ANISOU 2355  NE  ARG A 243     8833   9989  14348    -36    147  -1341       N  
ATOM   2356  CZ  ARG A 243      -4.657 -64.697 -15.928  1.00 90.24           C  
ANISOU 2356  CZ  ARG A 243     9105  10410  14773    -62    153  -1527       C  
ATOM   2357  NH1 ARG A 243      -3.901 -65.755 -15.653  1.00 90.55           N  
ANISOU 2357  NH1 ARG A 243     9047  10324  15035    -42    137  -1587       N  
ATOM   2358  NH2 ARG A 243      -4.446 -64.021 -17.050  1.00 90.17           N  
ANISOU 2358  NH2 ARG A 243     9094  10575  14591   -110    172  -1653       N  
ATOM   2359  N   ARG A 244     -10.826 -62.527 -11.661  1.00 72.73           N  
ANISOU 2359  N   ARG A 244     7320   8007  12308     11    199   -715       N  
ATOM   2360  CA  ARG A 244     -11.916 -61.569 -11.626  1.00 72.08           C  
ANISOU 2360  CA  ARG A 244     7296   8002  12089     11    202   -673       C  
ATOM   2361  C   ARG A 244     -11.886 -60.863 -10.270  1.00 71.10           C  
ANISOU 2361  C   ARG A 244     7290   7843  11881     22    215   -481       C  
ATOM   2362  O   ARG A 244     -11.978 -59.642 -10.236  1.00 71.08           O  
ANISOU 2362  O   ARG A 244     7373   7936  11697     30    199   -428       O  
ATOM   2363  CB  ARG A 244     -13.247 -62.287 -11.818  1.00 73.78           C  
ANISOU 2363  CB  ARG A 244     7423   8170  12440     -1    228   -752       C  
ATOM   2364  CG  ARG A 244     -14.045 -61.788 -13.005  1.00 77.94           C  
ANISOU 2364  CG  ARG A 244     7923   8829  12862      1    198   -871       C  
ATOM   2365  CD  ARG A 244     -15.298 -62.624 -13.196  1.00 82.60           C  
ANISOU 2365  CD  ARG A 244     8403   9367  13613    -10    222   -974       C  
ATOM   2366  NE  ARG A 244     -14.981 -64.019 -13.523  1.00 87.07           N  
ANISOU 2366  NE  ARG A 244     8845   9868  14371    -25    235  -1109       N  
ATOM   2367  CZ  ARG A 244     -15.875 -65.007 -13.555  1.00 90.42           C  
ANISOU 2367  CZ  ARG A 244     9165  10183  15006    -42    275  -1175       C  
ATOM   2368  NH1 ARG A 244     -15.497 -66.243 -13.862  1.00 90.45           N  
ANISOU 2368  NH1 ARG A 244     9050  10127  15188    -54    283  -1308       N  
ATOM   2369  NH2 ARG A 244     -17.153 -64.767 -13.279  1.00 90.78           N  
ANISOU 2369  NH2 ARG A 244     9219  10177  15095    -51    312  -1119       N  
ATOM   2370  N   ARG A 245     -11.683 -61.621  -9.162  1.00 70.19           N  
ANISOU 2370  N   ARG A 245     7183   7591  11895     19    241   -376       N  
ATOM   2371  CA  ARG A 245     -11.584 -61.095  -7.785  1.00 69.56           C  
ANISOU 2371  CA  ARG A 245     7214   7475  11740     23    255   -192       C  
ATOM   2372  C   ARG A 245     -10.411 -60.126  -7.653  1.00 67.38           C  
ANISOU 2372  C   ARG A 245     7018   7276  11306     44    219   -139       C  
ATOM   2373  O   ARG A 245     -10.531 -59.105  -6.985  1.00 67.58           O  
ANISOU 2373  O   ARG A 245     7136   7350  11189     49    223    -35       O  
ATOM   2374  CB  ARG A 245     -11.440 -62.243  -6.761  1.00 72.06           C  
ANISOU 2374  CB  ARG A 245     7524   7630  12226     13    278    -97       C  
ATOM   2375  CG  ARG A 245     -11.233 -61.789  -5.306  1.00 76.77           C  
ANISOU 2375  CG  ARG A 245     8239   8193  12738     15    284     95       C  
ATOM   2376  CD  ARG A 245     -11.010 -62.958  -4.346  1.00 81.92           C  
ANISOU 2376  CD  ARG A 245     8896   8681  13550      5    292    198       C  
ATOM   2377  NE  ARG A 245      -9.729 -63.649  -4.561  1.00 86.45           N  
ANISOU 2377  NE  ARG A 245     9431   9189  14228     38    231    170       N  
ATOM   2378  CZ  ARG A 245      -9.610 -64.956  -4.798  1.00 89.31           C  
ANISOU 2378  CZ  ARG A 245     9705   9419  14809     36    224    115       C  
ATOM   2379  NH1 ARG A 245     -10.690 -65.731  -4.854  1.00 89.32           N  
ANISOU 2379  NH1 ARG A 245     9650   9342  14945      0    278     84       N  
ATOM   2380  NH2 ARG A 245      -8.411 -65.497  -4.981  1.00 88.85           N  
ANISOU 2380  NH2 ARG A 245     9605   9304  14849     71    162     80       N  
ATOM   2381  N   LEU A 246      -9.293 -60.444  -8.316  1.00 65.24           N  
ANISOU 2381  N   LEU A 246     6702   7017  11069     54    187   -225       N  
ATOM   2382  CA  LEU A 246      -8.080 -59.633  -8.359  1.00 63.49           C  
ANISOU 2382  CA  LEU A 246     6535   6869  10721     67    158   -211       C  
ATOM   2383  C   LEU A 246      -8.323 -58.303  -9.102  1.00 61.43           C  
ANISOU 2383  C   LEU A 246     6324   6756  10260     58    154   -248       C  
ATOM   2384  O   LEU A 246      -7.840 -57.266  -8.662  1.00 61.65           O  
ANISOU 2384  O   LEU A 246     6439   6837  10146     65    147   -168       O  
ATOM   2385  CB  LEU A 246      -6.989 -60.423  -9.081  1.00 63.55           C  
ANISOU 2385  CB  LEU A 246     6452   6853  10841     69    135   -337       C  
ATOM   2386  CG  LEU A 246      -5.982 -61.131  -8.228  1.00 64.70           C  
ANISOU 2386  CG  LEU A 246     6592   6890  11103     95    106   -278       C  
ATOM   2387  CD1 LEU A 246      -5.086 -61.975  -9.088  1.00 65.31           C  
ANISOU 2387  CD1 LEU A 246     6560   6958  11298     95     86   -442       C  
ATOM   2388  CD2 LEU A 246      -5.144 -60.143  -7.487  1.00 65.30           C  
ANISOU 2388  CD2 LEU A 246     6771   7010  11031    112     88   -164       C  
ATOM   2389  N   LEU A 247      -9.053 -58.332 -10.229  1.00 59.37           N  
ANISOU 2389  N   LEU A 247     6010   6559   9989     43    154   -368       N  
ATOM   2390  CA  LEU A 247      -9.364 -57.108 -10.969  1.00 57.83           C  
ANISOU 2390  CA  LEU A 247     5873   6495   9606     36    138   -389       C  
ATOM   2391  C   LEU A 247     -10.280 -56.218 -10.136  1.00 56.39           C  
ANISOU 2391  C   LEU A 247     5770   6314   9343     50    143   -269       C  
ATOM   2392  O   LEU A 247     -10.051 -55.012 -10.052  1.00 56.85           O  
ANISOU 2392  O   LEU A 247     5913   6441   9246     54    130   -210       O  
ATOM   2393  CB  LEU A 247     -10.028 -57.425 -12.310  1.00 57.63           C  
ANISOU 2393  CB  LEU A 247     5775   6537   9583     21    124   -540       C  
ATOM   2394  CG  LEU A 247     -10.408 -56.219 -13.149  1.00 58.71           C  
ANISOU 2394  CG  LEU A 247     5982   6805   9522     15     93   -553       C  
ATOM   2395  CD1 LEU A 247      -9.200 -55.441 -13.551  1.00 59.39           C  
ANISOU 2395  CD1 LEU A 247     6131   6963   9472     -5     91   -546       C  
ATOM   2396  CD2 LEU A 247     -11.147 -56.636 -14.375  1.00 59.46           C  
ANISOU 2396  CD2 LEU A 247     6006   6967   9618      2     69   -697       C  
ATOM   2397  N   SER A 248     -11.274 -56.831  -9.470  1.00 54.44           N  
ANISOU 2397  N   SER A 248     5491   5984   9211     52    169   -234       N  
ATOM   2398  CA  SER A 248     -12.241 -56.175  -8.589  1.00 53.05           C  
ANISOU 2398  CA  SER A 248     5368   5798   8992     56    187   -137       C  
ATOM   2399  C   SER A 248     -11.529 -55.428  -7.476  1.00 50.96           C  
ANISOU 2399  C   SER A 248     5200   5532   8632     64    195     -2       C  
ATOM   2400  O   SER A 248     -11.929 -54.315  -7.142  1.00 51.19           O  
ANISOU 2400  O   SER A 248     5292   5612   8547     70    192     50       O  
ATOM   2401  CB  SER A 248     -13.169 -57.201  -7.952  1.00 54.63           C  
ANISOU 2401  CB  SER A 248     5511   5892   9355     42    232   -125       C  
ATOM   2402  OG  SER A 248     -13.442 -58.291  -8.814  1.00 57.46           O  
ANISOU 2402  OG  SER A 248     5763   6226   9844     34    230   -257       O  
ATOM   2403  N   ILE A 249     -10.458 -56.029  -6.912  1.00 48.64           N  
ANISOU 2403  N   ILE A 249     4912   5179   8391     65    197     47       N  
ATOM   2404  CA  ILE A 249      -9.667 -55.421  -5.857  1.00 47.18           C  
ANISOU 2404  CA  ILE A 249     4811   4995   8120     75    196    164       C  
ATOM   2405  C   ILE A 249      -9.075 -54.122  -6.358  1.00 46.88           C  
ANISOU 2405  C   ILE A 249     4828   5064   7921     81    172    148       C  
ATOM   2406  O   ILE A 249      -9.176 -53.120  -5.667  1.00 47.49           O  
ANISOU 2406  O   ILE A 249     4976   5173   7894     86    178    228       O  
ATOM   2407  CB  ILE A 249      -8.571 -56.384  -5.362  1.00 47.03           C  
ANISOU 2407  CB  ILE A 249     4776   4895   8199     84    182    197       C  
ATOM   2408  CG1 ILE A 249      -9.176 -57.606  -4.668  1.00 47.21           C  
ANISOU 2408  CG1 ILE A 249     4760   4792   8384     73    206    242       C  
ATOM   2409  CG2 ILE A 249      -7.554 -55.670  -4.457  1.00 47.37           C  
ANISOU 2409  CG2 ILE A 249     4901   4961   8138    100    166    296       C  
ATOM   2410  CD1 ILE A 249      -8.233 -58.779  -4.543  1.00 48.00           C  
ANISOU 2410  CD1 ILE A 249     4813   4791   8635     87    176    234       C  
ATOM   2411  N   ILE A 250      -8.549 -54.111  -7.589  1.00 46.04           N  
ANISOU 2411  N   ILE A 250     4689   5012   7791     75    151     40       N  
ATOM   2412  CA  ILE A 250      -7.980 -52.906  -8.179  1.00 45.94           C  
ANISOU 2412  CA  ILE A 250     4734   5097   7622     69    135     24       C  
ATOM   2413  C   ILE A 250      -9.019 -51.805  -8.294  1.00 45.26           C  
ANISOU 2413  C   ILE A 250     4701   5063   7433     74    126     55       C  
ATOM   2414  O   ILE A 250      -8.800 -50.717  -7.777  1.00 45.23           O  
ANISOU 2414  O   ILE A 250     4770   5088   7325     79    125    126       O  
ATOM   2415  CB  ILE A 250      -7.299 -53.187  -9.537  1.00 46.92           C  
ANISOU 2415  CB  ILE A 250     4814   5277   7735     47    124   -105       C  
ATOM   2416  CG1 ILE A 250      -6.173 -54.222  -9.395  1.00 48.38           C  
ANISOU 2416  CG1 ILE A 250     4944   5412   8028     46    128   -144       C  
ATOM   2417  CG2 ILE A 250      -6.781 -51.887 -10.153  1.00 47.50           C  
ANISOU 2417  CG2 ILE A 250     4963   5451   7633     28    115   -110       C  
ATOM   2418  CD1 ILE A 250      -5.557 -54.659 -10.719  1.00 49.99           C  
ANISOU 2418  CD1 ILE A 250     5085   5671   8238     16    128   -295       C  
ATOM   2419  N   VAL A 251     -10.173 -52.105  -8.891  1.00 44.76           N  
ANISOU 2419  N   VAL A 251     4593   5003   7411     75    115     -4       N  
ATOM   2420  CA  VAL A 251     -11.237 -51.125  -9.079  1.00 44.88           C  
ANISOU 2420  CA  VAL A 251     4643   5059   7349     88     91     10       C  
ATOM   2421  C   VAL A 251     -11.686 -50.464  -7.786  1.00 45.37           C  
ANISOU 2421  C   VAL A 251     4753   5091   7393    100    113    113       C  
ATOM   2422  O   VAL A 251     -11.770 -49.239  -7.732  1.00 45.91           O  
ANISOU 2422  O   VAL A 251     4885   5203   7357    109     93    151       O  
ATOM   2423  CB  VAL A 251     -12.424 -51.711  -9.843  1.00 45.22           C  
ANISOU 2423  CB  VAL A 251     4614   5103   7463     93     72    -81       C  
ATOM   2424  CG1 VAL A 251     -13.457 -50.636 -10.130  1.00 45.69           C  
ANISOU 2424  CG1 VAL A 251     4711   5211   7437    113     26    -79       C  
ATOM   2425  CG2 VAL A 251     -11.956 -52.351 -11.134  1.00 45.70           C  
ANISOU 2425  CG2 VAL A 251     4621   5202   7542     76     54   -196       C  
ATOM   2426  N   VAL A 252     -11.921 -51.249  -6.735  1.00 44.95           N  
ANISOU 2426  N   VAL A 252     4673   4967   7438     94    156    160       N  
ATOM   2427  CA  VAL A 252     -12.333 -50.695  -5.451  1.00 44.88           C  
ANISOU 2427  CA  VAL A 252     4707   4941   7405     95    186    252       C  
ATOM   2428  C   VAL A 252     -11.208 -49.811  -4.827  1.00 44.19           C  
ANISOU 2428  C   VAL A 252     4697   4884   7208     99    184    327       C  
ATOM   2429  O   VAL A 252     -11.525 -48.799  -4.214  1.00 44.25           O  
ANISOU 2429  O   VAL A 252     4749   4916   7147    103    191    373       O  
ATOM   2430  CB  VAL A 252     -12.876 -51.801  -4.513  1.00 45.85           C  
ANISOU 2430  CB  VAL A 252     4790   4981   7648     75    238    287       C  
ATOM   2431  CG1 VAL A 252     -13.289 -51.231  -3.164  1.00 46.56           C  
ANISOU 2431  CG1 VAL A 252     4923   5067   7699     63    280    371       C  
ATOM   2432  CG2 VAL A 252     -14.060 -52.516  -5.163  1.00 46.14           C  
ANISOU 2432  CG2 VAL A 252     4742   4990   7798     68    244    195       C  
ATOM   2433  N   LEU A 253      -9.924 -50.108  -5.076  1.00 43.81           N  
ANISOU 2433  N   LEU A 253     4656   4840   7149     97    173    321       N  
ATOM   2434  CA  LEU A 253      -8.836 -49.250  -4.569  1.00 44.28           C  
ANISOU 2434  CA  LEU A 253     4780   4934   7112    101    169    371       C  
ATOM   2435  C   LEU A 253      -8.808 -47.907  -5.324  1.00 44.46           C  
ANISOU 2435  C   LEU A 253     4850   5026   7018    101    146    348       C  
ATOM   2436  O   LEU A 253      -8.831 -46.838  -4.704  1.00 44.45           O  
ANISOU 2436  O   LEU A 253     4901   5045   6943    106    150    399       O  
ATOM   2437  CB  LEU A 253      -7.461 -49.938  -4.659  1.00 44.51           C  
ANISOU 2437  CB  LEU A 253     4790   4945   7175    100    161    353       C  
ATOM   2438  CG  LEU A 253      -7.265 -51.205  -3.836  1.00 46.31           C  
ANISOU 2438  CG  LEU A 253     4985   5092   7520    105    169    394       C  
ATOM   2439  CD1 LEU A 253      -5.855 -51.742  -4.006  1.00 47.17           C  
ANISOU 2439  CD1 LEU A 253     5070   5185   7668    113    145    361       C  
ATOM   2440  CD2 LEU A 253      -7.555 -50.968  -2.365  1.00 46.93           C  
ANISOU 2440  CD2 LEU A 253     5112   5151   7569    108    188    505       C  
ATOM   2441  N   VAL A 254      -8.802 -47.988  -6.670  1.00 44.28           N  
ANISOU 2441  N   VAL A 254     4810   5036   6980     92    120    270       N  
ATOM   2442  CA  VAL A 254      -8.788 -46.867  -7.601  1.00 44.40           C  
ANISOU 2442  CA  VAL A 254     4876   5110   6883     85     91    249       C  
ATOM   2443  C   VAL A 254      -9.928 -45.906  -7.297  1.00 44.43           C  
ANISOU 2443  C   VAL A 254     4910   5113   6858    107     71    287       C  
ATOM   2444  O   VAL A 254      -9.670 -44.730  -7.079  1.00 44.88           O  
ANISOU 2444  O   VAL A 254     5029   5189   6835    108     65    330       O  
ATOM   2445  CB  VAL A 254      -8.859 -47.383  -9.062  1.00 45.31           C  
ANISOU 2445  CB  VAL A 254     4957   5261   6998     70     66    155       C  
ATOM   2446  CG1 VAL A 254      -9.075 -46.236 -10.037  1.00 45.95           C  
ANISOU 2446  CG1 VAL A 254     5103   5400   6954     61     25    150       C  
ATOM   2447  CG2 VAL A 254      -7.611 -48.175  -9.431  1.00 46.22           C  
ANISOU 2447  CG2 VAL A 254     5037   5384   7141     44     88     96       C  
ATOM   2448  N   VAL A 255     -11.178 -46.422  -7.235  1.00 43.70           N  
ANISOU 2448  N   VAL A 255     4765   4993   6847    122     64    264       N  
ATOM   2449  CA  VAL A 255     -12.397 -45.668  -6.991  1.00 43.12           C  
ANISOU 2449  CA  VAL A 255     4693   4913   6778    145     42    272       C  
ATOM   2450  C   VAL A 255     -12.458 -45.099  -5.591  1.00 43.12           C  
ANISOU 2450  C   VAL A 255     4714   4892   6778    148     81    338       C  
ATOM   2451  O   VAL A 255     -12.643 -43.900  -5.493  1.00 43.16           O  
ANISOU 2451  O   VAL A 255     4758   4910   6729    161     58    357       O  
ATOM   2452  CB  VAL A 255     -13.629 -46.507  -7.351  1.00 43.44           C  
ANISOU 2452  CB  VAL A 255     4655   4932   6919    154     32    204       C  
ATOM   2453  CG1 VAL A 255     -14.923 -45.903  -6.793  1.00 44.04           C  
ANISOU 2453  CG1 VAL A 255     4708   4989   7035    175     24    199       C  
ATOM   2454  CG2 VAL A 255     -13.707 -46.681  -8.859  1.00 43.61           C  
ANISOU 2454  CG2 VAL A 255     4666   4994   6908    156    -25    130       C  
ATOM   2455  N   THR A 256     -12.242 -45.895  -4.510  1.00 43.22           N  
ANISOU 2455  N   THR A 256     4704   4873   6843    133    137    375       N  
ATOM   2456  CA  THR A 256     -12.253 -45.369  -3.125  1.00 43.99           C  
ANISOU 2456  CA  THR A 256     4827   4968   6921    128    177    436       C  
ATOM   2457  C   THR A 256     -11.272 -44.202  -2.991  1.00 44.71           C  
ANISOU 2457  C   THR A 256     4983   5094   6911    132    164    470       C  
ATOM   2458  O   THR A 256     -11.613 -43.175  -2.396  1.00 45.31           O  
ANISOU 2458  O   THR A 256     5080   5182   6955    139    168    486       O  
ATOM   2459  CB  THR A 256     -11.874 -46.448  -2.095  1.00 45.30           C  
ANISOU 2459  CB  THR A 256     4980   5100   7131    107    228    488       C  
ATOM   2460  OG1 THR A 256     -12.738 -47.566  -2.248  1.00 46.93           O  
ANISOU 2460  OG1 THR A 256     5127   5261   7442     95    248    459       O  
ATOM   2461  CG2 THR A 256     -11.962 -45.951  -0.664  1.00 45.18           C  
ANISOU 2461  CG2 THR A 256     4992   5096   7077     94    270    546       C  
ATOM   2462  N   PHE A 257     -10.088 -44.337  -3.626  1.00 44.03           N  
ANISOU 2462  N   PHE A 257     4921   5023   6785    126    150    467       N  
ATOM   2463  CA  PHE A 257      -9.094 -43.284  -3.619  1.00 43.89           C  
ANISOU 2463  CA  PHE A 257     4960   5036   6679    122    145    487       C  
ATOM   2464  C   PHE A 257      -9.541 -42.049  -4.440  1.00 43.33           C  
ANISOU 2464  C   PHE A 257     4929   4982   6553    130    104    472       C  
ATOM   2465  O   PHE A 257      -9.406 -40.923  -3.962  1.00 44.02           O  
ANISOU 2465  O   PHE A 257     5053   5074   6597    134    106    498       O  
ATOM   2466  CB  PHE A 257      -7.758 -43.830  -4.118  1.00 44.23           C  
ANISOU 2466  CB  PHE A 257     5008   5092   6707    106    149    470       C  
ATOM   2467  CG  PHE A 257      -6.707 -42.773  -4.353  1.00 45.28           C  
ANISOU 2467  CG  PHE A 257     5194   5258   6752     92    148    470       C  
ATOM   2468  CD1 PHE A 257      -5.959 -42.274  -3.303  1.00 46.22           C  
ANISOU 2468  CD1 PHE A 257     5333   5386   6843     92    170    502       C  
ATOM   2469  CD2 PHE A 257      -6.488 -42.260  -5.623  1.00 46.01           C  
ANISOU 2469  CD2 PHE A 257     5319   5375   6787     74    126    437       C  
ATOM   2470  CE1 PHE A 257      -5.016 -41.287  -3.518  1.00 47.10           C  
ANISOU 2470  CE1 PHE A 257     5487   5523   6884     74    177    492       C  
ATOM   2471  CE2 PHE A 257      -5.540 -41.283  -5.838  1.00 46.89           C  
ANISOU 2471  CE2 PHE A 257     5484   5510   6820     49    136    439       C  
ATOM   2472  CZ  PHE A 257      -4.801 -40.808  -4.787  1.00 46.98           C  
ANISOU 2472  CZ  PHE A 257     5507   5524   6820     50    165    463       C  
ATOM   2473  N   ALA A 258     -10.035 -42.244  -5.672  1.00 41.97           N  
ANISOU 2473  N   ALA A 258     4750   4815   6383    133     63    431       N  
ATOM   2474  CA  ALA A 258     -10.473 -41.133  -6.514  1.00 41.09           C  
ANISOU 2474  CA  ALA A 258     4686   4712   6215    143      8    429       C  
ATOM   2475  C   ALA A 258     -11.610 -40.369  -5.874  1.00 40.66           C  
ANISOU 2475  C   ALA A 258     4618   4630   6200    174    -11    439       C  
ATOM   2476  O   ALA A 258     -11.653 -39.156  -5.968  1.00 40.87           O  
ANISOU 2476  O   ALA A 258     4692   4649   6187    185    -41    461       O  
ATOM   2477  CB  ALA A 258     -10.905 -41.642  -7.871  1.00 40.85           C  
ANISOU 2477  CB  ALA A 258     4646   4701   6176    143    -40    381       C  
ATOM   2478  N   LEU A 259     -12.510 -41.063  -5.200  1.00 40.23           N  
ANISOU 2478  N   LEU A 259     4498   4557   6232    185     13    417       N  
ATOM   2479  CA  LEU A 259     -13.653 -40.442  -4.550  1.00 40.59           C  
ANISOU 2479  CA  LEU A 259     4511   4580   6330    208      5    403       C  
ATOM   2480  C   LEU A 259     -13.261 -39.718  -3.281  1.00 41.65           C  
ANISOU 2480  C   LEU A 259     4663   4716   6445    199     53    439       C  
ATOM   2481  O   LEU A 259     -13.867 -38.706  -2.961  1.00 41.88           O  
ANISOU 2481  O   LEU A 259     4691   4733   6490    217     33    427       O  
ATOM   2482  CB  LEU A 259     -14.727 -41.494  -4.233  1.00 40.19           C  
ANISOU 2482  CB  LEU A 259     4379   4513   6380    208     30    357       C  
ATOM   2483  CG  LEU A 259     -15.875 -41.622  -5.218  1.00 40.76           C  
ANISOU 2483  CG  LEU A 259     4408   4574   6506    237    -36    289       C  
ATOM   2484  CD1 LEU A 259     -15.401 -42.110  -6.539  1.00 41.20           C  
ANISOU 2484  CD1 LEU A 259     4483   4651   6521    236    -81    274       C  
ATOM   2485  CD2 LEU A 259     -16.894 -42.579  -4.716  1.00 41.35           C  
ANISOU 2485  CD2 LEU A 259     4395   4627   6688    228      6    237       C  
ATOM   2486  N   CYS A 260     -12.276 -40.227  -2.549  1.00 42.43           N  
ANISOU 2486  N   CYS A 260     4773   4833   6517    173    110    475       N  
ATOM   2487  CA  CYS A 260     -11.867 -39.620  -1.287  1.00 44.09           C  
ANISOU 2487  CA  CYS A 260     4996   5058   6700    162    154    503       C  
ATOM   2488  C   CYS A 260     -10.981 -38.408  -1.445  1.00 44.59           C  
ANISOU 2488  C   CYS A 260     5115   5131   6697    165    137    520       C  
ATOM   2489  O   CYS A 260     -11.137 -37.438  -0.709  1.00 44.58           O  
ANISOU 2489  O   CYS A 260     5114   5131   6693    168    150    516       O  
ATOM   2490  CB  CYS A 260     -11.212 -40.656  -0.379  1.00 46.20           C  
ANISOU 2490  CB  CYS A 260     5255   5338   6962    139    208    539       C  
ATOM   2491  SG  CYS A 260     -12.358 -41.900   0.272  1.00 53.61           S  
ANISOU 2491  SG  CYS A 260     6132   6257   7981    121    255    533       S  
ATOM   2492  N   TRP A 261     -10.022 -38.469  -2.372  1.00 44.78           N  
ANISOU 2492  N   TRP A 261     5182   5162   6670    155    117    531       N  
ATOM   2493  CA  TRP A 261      -9.046 -37.408  -2.523  1.00 45.34           C  
ANISOU 2493  CA  TRP A 261     5309   5240   6679    144    115    547       C  
ATOM   2494  C   TRP A 261      -9.382 -36.321  -3.544  1.00 45.79           C  
ANISOU 2494  C   TRP A 261     5414   5271   6715    153     59    549       C  
ATOM   2495  O   TRP A 261      -8.861 -35.217  -3.397  1.00 46.06           O  
ANISOU 2495  O   TRP A 261     5486   5293   6722    147     63    563       O  
ATOM   2496  CB  TRP A 261      -7.678 -38.007  -2.805  1.00 45.54           C  
ANISOU 2496  CB  TRP A 261     5353   5290   6662    118    138    551       C  
ATOM   2497  CG  TRP A 261      -7.073 -38.605  -1.569  1.00 46.58           C  
ANISOU 2497  CG  TRP A 261     5455   5441   6803    115    181    562       C  
ATOM   2498  CD1 TRP A 261      -7.127 -39.911  -1.178  1.00 47.69           C  
ANISOU 2498  CD1 TRP A 261     5557   5579   6982    116    194    569       C  
ATOM   2499  CD2 TRP A 261      -6.414 -37.895  -0.507  1.00 46.71           C  
ANISOU 2499  CD2 TRP A 261     5480   5478   6791    111    210    571       C  
ATOM   2500  NE1 TRP A 261      -6.464 -40.073   0.018  1.00 48.10           N  
ANISOU 2500  NE1 TRP A 261     5604   5650   7022    114    221    592       N  
ATOM   2501  CE2 TRP A 261      -6.036 -38.845   0.462  1.00 47.61           C  
ANISOU 2501  CE2 TRP A 261     5567   5609   6915    112    231    589       C  
ATOM   2502  CE3 TRP A 261      -6.085 -36.552  -0.293  1.00 46.99           C  
ANISOU 2502  CE3 TRP A 261     5541   5516   6796    107    216    564       C  
ATOM   2503  CZ2 TRP A 261      -5.354 -38.491   1.625  1.00 47.85           C  
ANISOU 2503  CZ2 TRP A 261     5597   5671   6912    111    253    598       C  
ATOM   2504  CZ3 TRP A 261      -5.420 -36.205   0.865  1.00 47.61           C  
ANISOU 2504  CZ3 TRP A 261     5610   5626   6854    104    246    561       C  
ATOM   2505  CH2 TRP A 261      -5.078 -37.166   1.814  1.00 47.69           C  
ANISOU 2505  CH2 TRP A 261     5594   5664   6861    107    262    577       C  
ATOM   2506  N   MET A 262     -10.252 -36.578  -4.544  1.00 45.75           N  
ANISOU 2506  N   MET A 262     5408   5251   6723    169      3    537       N  
ATOM   2507  CA  MET A 262     -10.606 -35.538  -5.525  1.00 46.03           C  
ANISOU 2507  CA  MET A 262     5501   5257   6730    181    -67    552       C  
ATOM   2508  C   MET A 262     -11.045 -34.205  -4.896  1.00 45.01           C  
ANISOU 2508  C   MET A 262     5378   5084   6639    205    -86    560       C  
ATOM   2509  O   MET A 262     -10.433 -33.210  -5.246  1.00 45.00           O  
ANISOU 2509  O   MET A 262     5443   5063   6594    190    -96    593       O  
ATOM   2510  CB  MET A 262     -11.634 -36.017  -6.548  1.00 48.10           C  
ANISOU 2510  CB  MET A 262     5751   5515   7011    206   -138    530       C  
ATOM   2511  CG  MET A 262     -11.073 -36.126  -7.944  1.00 53.88           C  
ANISOU 2511  CG  MET A 262     6549   6273   7651    178   -170    545       C  
ATOM   2512  SD  MET A 262     -12.095 -37.203  -9.016  1.00 69.44           S  
ANISOU 2512  SD  MET A 262     8479   8266   9639    199   -236    494       S  
ATOM   2513  CE  MET A 262     -10.975 -37.420 -10.465  1.00 70.01           C  
ANISOU 2513  CE  MET A 262     8625   8398   9576    137   -228    499       C  
ATOM   2514  N   PRO A 263     -11.997 -34.137  -3.926  1.00 44.03           N  
ANISOU 2514  N   PRO A 263     5184   4946   6598    233    -77    524       N  
ATOM   2515  CA  PRO A 263     -12.353 -32.835  -3.349  1.00 43.35           C  
ANISOU 2515  CA  PRO A 263     5092   4820   6559    253    -92    514       C  
ATOM   2516  C   PRO A 263     -11.165 -32.067  -2.775  1.00 42.90           C  
ANISOU 2516  C   PRO A 263     5074   4769   6458    224    -41    537       C  
ATOM   2517  O   PRO A 263     -11.019 -30.887  -3.076  1.00 43.36           O  
ANISOU 2517  O   PRO A 263     5175   4778   6521    230    -75    554       O  
ATOM   2518  CB  PRO A 263     -13.379 -33.199  -2.267  1.00 43.77           C  
ANISOU 2518  CB  PRO A 263     5050   4883   6696    268    -57    456       C  
ATOM   2519  CG  PRO A 263     -13.978 -34.429  -2.734  1.00 44.30           C  
ANISOU 2519  CG  PRO A 263     5084   4968   6780    271    -66    439       C  
ATOM   2520  CD  PRO A 263     -12.846 -35.197  -3.349  1.00 43.33           C  
ANISOU 2520  CD  PRO A 263     5015   4876   6574    242    -52    483       C  
ATOM   2521  N   TYR A 264     -10.289 -32.729  -2.000  1.00 41.87           N  
ANISOU 2521  N   TYR A 264     4928   4691   6289    193     35    537       N  
ATOM   2522  CA  TYR A 264      -9.110 -32.087  -1.411  1.00 41.12           C  
ANISOU 2522  CA  TYR A 264     4858   4610   6156    167     83    543       C  
ATOM   2523  C   TYR A 264      -8.229 -31.491  -2.496  1.00 40.38           C  
ANISOU 2523  C   TYR A 264     4846   4492   6005    142     64    579       C  
ATOM   2524  O   TYR A 264      -7.923 -30.305  -2.428  1.00 40.43           O  
ANISOU 2524  O   TYR A 264     4882   4459   6020    136     62    584       O  
ATOM   2525  CB  TYR A 264      -8.309 -33.093  -0.537  1.00 40.96           C  
ANISOU 2525  CB  TYR A 264     4808   4653   6102    145    148    538       C  
ATOM   2526  CG  TYR A 264      -6.953 -32.605  -0.055  1.00 41.45           C  
ANISOU 2526  CG  TYR A 264     4891   4740   6120    119    191    535       C  
ATOM   2527  CD1 TYR A 264      -6.841 -31.800   1.068  1.00 42.26           C  
ANISOU 2527  CD1 TYR A 264     4965   4854   6238    120    221    505       C  
ATOM   2528  CD2 TYR A 264      -5.782 -32.996  -0.691  1.00 42.02           C  
ANISOU 2528  CD2 TYR A 264     4995   4831   6139     92    205    546       C  
ATOM   2529  CE1 TYR A 264      -5.604 -31.371   1.528  1.00 42.95           C  
ANISOU 2529  CE1 TYR A 264     5061   4970   6290     99    258    489       C  
ATOM   2530  CE2 TYR A 264      -4.540 -32.557  -0.249  1.00 42.81           C  
ANISOU 2530  CE2 TYR A 264     5102   4954   6208     69    244    528       C  
ATOM   2531  CZ  TYR A 264      -4.457 -31.731   0.856  1.00 43.68           C  
ANISOU 2531  CZ  TYR A 264     5187   5075   6336     74    268    500       C  
ATOM   2532  OH  TYR A 264      -3.243 -31.275   1.312  1.00 44.99           O  
ANISOU 2532  OH  TYR A 264     5350   5266   6478     54    304    470       O  
ATOM   2533  N   HIS A 265      -7.904 -32.289  -3.534  1.00 39.77           N  
ANISOU 2533  N   HIS A 265     4803   4433   5874    123     51    599       N  
ATOM   2534  CA  HIS A 265      -7.008 -31.879  -4.612  1.00 39.92           C  
ANISOU 2534  CA  HIS A 265     4903   4445   5821     82     49    629       C  
ATOM   2535  C   HIS A 265      -7.625 -30.890  -5.597  1.00 39.77           C  
ANISOU 2535  C   HIS A 265     4952   4363   5795     91    -23    670       C  
ATOM   2536  O   HIS A 265      -6.908 -30.097  -6.178  1.00 39.72           O  
ANISOU 2536  O   HIS A 265     5015   4328   5748     55    -14    700       O  
ATOM   2537  CB  HIS A 265      -6.413 -33.098  -5.331  1.00 40.79           C  
ANISOU 2537  CB  HIS A 265     5017   4605   5876     53     66    619       C  
ATOM   2538  CG  HIS A 265      -5.340 -33.777  -4.526  1.00 43.45           C  
ANISOU 2538  CG  HIS A 265     5311   4987   6212     34    134    588       C  
ATOM   2539  ND1 HIS A 265      -5.560 -34.996  -3.900  1.00 45.35           N  
ANISOU 2539  ND1 HIS A 265     5486   5256   6490     55    145    569       N  
ATOM   2540  CD2 HIS A 265      -4.086 -33.357  -4.226  1.00 44.56           C  
ANISOU 2540  CD2 HIS A 265     5463   5142   6326      0    185    572       C  
ATOM   2541  CE1 HIS A 265      -4.432 -35.286  -3.264  1.00 45.73           C  
ANISOU 2541  CE1 HIS A 265     5513   5334   6529     38    192    549       C  
ATOM   2542  NE2 HIS A 265      -3.518 -34.330  -3.430  1.00 45.55           N  
ANISOU 2542  NE2 HIS A 265     5529   5308   6470      7    217    543       N  
ATOM   2543  N   LEU A 266      -8.934 -30.892  -5.742  1.00 39.70           N  
ANISOU 2543  N   LEU A 266     4923   4328   5834    138    -96    670       N  
ATOM   2544  CA  LEU A 266      -9.637 -29.965  -6.614  1.00 40.11           C  
ANISOU 2544  CA  LEU A 266     5035   4312   5894    162   -188    710       C  
ATOM   2545  C   LEU A 266      -9.678 -28.582  -5.952  1.00 40.60           C  
ANISOU 2545  C   LEU A 266     5101   4301   6022    176   -193    716       C  
ATOM   2546  O   LEU A 266      -9.409 -27.585  -6.610  1.00 40.47           O  
ANISOU 2546  O   LEU A 266     5171   4225   5981    160   -229    771       O  
ATOM   2547  CB  LEU A 266     -11.061 -30.492  -6.832  1.00 40.43           C  
ANISOU 2547  CB  LEU A 266     5021   4346   5997    220   -264    682       C  
ATOM   2548  CG  LEU A 266     -12.058 -29.551  -7.485  1.00 42.10           C  
ANISOU 2548  CG  LEU A 266     5264   4479   6254    269   -380    706       C  
ATOM   2549  CD1 LEU A 266     -11.636 -29.216  -8.907  1.00 42.81           C  
ANISOU 2549  CD1 LEU A 266     5477   4552   6236    240   -440    784       C  
ATOM   2550  CD2 LEU A 266     -13.470 -30.130  -7.438  1.00 42.60           C  
ANISOU 2550  CD2 LEU A 266     5242   4542   6401    329   -443    648       C  
ATOM   2551  N   VAL A 267     -10.026 -28.528  -4.656  1.00 40.98           N  
ANISOU 2551  N   VAL A 267     5059   4355   6157    203   -157    658       N  
ATOM   2552  CA  VAL A 267     -10.140 -27.286  -3.902  1.00 41.84           C  
ANISOU 2552  CA  VAL A 267     5146   4403   6346    218   -155    637       C  
ATOM   2553  C   VAL A 267      -8.790 -26.680  -3.584  1.00 43.67           C  
ANISOU 2553  C   VAL A 267     5415   4639   6536    166    -81    647       C  
ATOM   2554  O   VAL A 267      -8.702 -25.454  -3.496  1.00 44.24           O  
ANISOU 2554  O   VAL A 267     5511   4638   6658    167    -95    655       O  
ATOM   2555  CB  VAL A 267     -11.011 -27.479  -2.651  1.00 41.93           C  
ANISOU 2555  CB  VAL A 267     5043   4435   6452    254   -132    557       C  
ATOM   2556  CG1 VAL A 267     -10.862 -26.321  -1.664  1.00 42.11           C  
ANISOU 2556  CG1 VAL A 267     5029   4424   6546    254   -100    512       C  
ATOM   2557  CG2 VAL A 267     -12.474 -27.679  -3.049  1.00 42.29           C  
ANISOU 2557  CG2 VAL A 267     5048   4447   6572    308   -219    533       C  
ATOM   2558  N   LYS A 268      -7.740 -27.505  -3.408  1.00 44.46           N  
ANISOU 2558  N   LYS A 268     5515   4819   6561    124     -4    640       N  
ATOM   2559  CA  LYS A 268      -6.410 -26.947  -3.160  1.00 45.59           C  
ANISOU 2559  CA  LYS A 268     5686   4968   6669     73     65    636       C  
ATOM   2560  C   LYS A 268      -5.906 -26.317  -4.468  1.00 47.44           C  
ANISOU 2560  C   LYS A 268     6032   5150   6844     30     43    702       C  
ATOM   2561  O   LYS A 268      -5.414 -25.192  -4.445  1.00 47.78           O  
ANISOU 2561  O   LYS A 268     6115   5133   6907      4     59    715       O  
ATOM   2562  CB  LYS A 268      -5.438 -28.004  -2.637  1.00 46.47           C  
ANISOU 2562  CB  LYS A 268     5760   5171   6725     47    138    602       C  
ATOM   2563  CG  LYS A 268      -4.142 -27.432  -2.100  1.00 49.19           C  
ANISOU 2563  CG  LYS A 268     6097   5534   7060      9    209    566       C  
ATOM   2564  CD  LYS A 268      -3.293 -28.551  -1.552  1.00 53.86           C  
ANISOU 2564  CD  LYS A 268     6673   6202   7590    -19    256    546       C  
ATOM   2565  CE  LYS A 268      -1.825 -28.214  -1.427  1.00 58.09           C  
ANISOU 2565  CE  LYS A 268     7183   6771   8118    -49    321    493       C  
ATOM   2566  NZ  LYS A 268      -1.037 -29.369  -0.897  1.00 60.04           N  
ANISOU 2566  NZ  LYS A 268     7390   7093   8329    -53    346    463       N  
ATOM   2567  N   THR A 269      -6.109 -27.001  -5.618  1.00 48.43           N  
ANISOU 2567  N   THR A 269     6210   5294   6898     20      3    744       N  
ATOM   2568  CA  THR A 269      -5.701 -26.508  -6.939  1.00 49.88           C  
ANISOU 2568  CA  THR A 269     6510   5441   7000    -30    -19    813       C  
ATOM   2569  C   THR A 269      -6.526 -25.280  -7.367  1.00 51.71           C  
ANISOU 2569  C   THR A 269     6805   5563   7279     -1   -110    876       C  
ATOM   2570  O   THR A 269      -5.983 -24.371  -7.997  1.00 52.33           O  
ANISOU 2570  O   THR A 269     6982   5583   7317    -52   -107    936       O  
ATOM   2571  CB  THR A 269      -5.714 -27.662  -7.956  1.00 50.85           C  
ANISOU 2571  CB  THR A 269     6658   5632   7032    -49    -34    823       C  
ATOM   2572  OG1 THR A 269      -4.493 -28.385  -7.817  1.00 51.96           O  
ANISOU 2572  OG1 THR A 269     6775   5846   7120   -104     61    777       O  
ATOM   2573  CG2 THR A 269      -5.872 -27.205  -9.404  1.00 51.10           C  
ANISOU 2573  CG2 THR A 269     6810   5629   6975    -80    -97    902       C  
ATOM   2574  N   LEU A 270      -7.816 -25.243  -7.010  1.00 52.25           N  
ANISOU 2574  N   LEU A 270     6817   5598   7439     77   -191    860       N  
ATOM   2575  CA  LEU A 270      -8.681 -24.121  -7.326  1.00 53.37           C  
ANISOU 2575  CA  LEU A 270     6998   5627   7653    120   -294    905       C  
ATOM   2576  C   LEU A 270      -8.287 -22.896  -6.501  1.00 54.97           C  
ANISOU 2576  C   LEU A 270     7186   5753   7948    114   -258    887       C  
ATOM   2577  O   LEU A 270      -8.285 -21.789  -7.026  1.00 54.72           O  
ANISOU 2577  O   LEU A 270     7235   5615   7941    107   -310    953       O  
ATOM   2578  CB  LEU A 270     -10.119 -24.504  -7.023  1.00 53.62           C  
ANISOU 2578  CB  LEU A 270     6942   5656   7777    204   -374    857       C  
ATOM   2579  CG  LEU A 270     -11.050 -24.541  -8.209  1.00 55.51           C  
ANISOU 2579  CG  LEU A 270     7239   5854   7999    245   -507    913       C  
ATOM   2580  CD1 LEU A 270     -10.619 -25.585  -9.216  1.00 56.03           C  
ANISOU 2580  CD1 LEU A 270     7369   6003   7917    200   -499    949       C  
ATOM   2581  CD2 LEU A 270     -12.467 -24.829  -7.759  1.00 56.51           C  
ANISOU 2581  CD2 LEU A 270     7255   5973   8243    329   -577    839       C  
ATOM   2582  N   TYR A 271      -7.946 -23.091  -5.210  1.00 56.46           N  
ANISOU 2582  N   TYR A 271     7271   5993   8187    114   -171    799       N  
ATOM   2583  CA  TYR A 271      -7.518 -22.000  -4.324  1.00 58.46           C  
ANISOU 2583  CA  TYR A 271     7491   6193   8529    105   -125    758       C  
ATOM   2584  C   TYR A 271      -6.151 -21.447  -4.766  1.00 60.14           C  
ANISOU 2584  C   TYR A 271     7791   6385   8676     23    -55    799       C  
ATOM   2585  O   TYR A 271      -5.911 -20.237  -4.691  1.00 60.15           O  
ANISOU 2585  O   TYR A 271     7819   6289   8747      9    -54    810       O  
ATOM   2586  CB  TYR A 271      -7.484 -22.452  -2.849  1.00 58.82           C  
ANISOU 2586  CB  TYR A 271     7408   6322   8619    122    -51    651       C  
ATOM   2587  CG  TYR A 271      -6.958 -21.382  -1.920  1.00 60.17           C  
ANISOU 2587  CG  TYR A 271     7537   6457   8870    107      3    592       C  
ATOM   2588  CD1 TYR A 271      -7.749 -20.301  -1.556  1.00 61.34           C  
ANISOU 2588  CD1 TYR A 271     7649   6504   9153    148    -50    563       C  
ATOM   2589  CD2 TYR A 271      -5.643 -21.407  -1.471  1.00 61.45           C  
ANISOU 2589  CD2 TYR A 271     7693   6676   8980     51    102    559       C  
ATOM   2590  CE1 TYR A 271      -7.259 -19.291  -0.735  1.00 62.60           C  
ANISOU 2590  CE1 TYR A 271     7763   6626   9395    132      1    498       C  
ATOM   2591  CE2 TYR A 271      -5.136 -20.397  -0.659  1.00 62.60           C  
ANISOU 2591  CE2 TYR A 271     7795   6789   9200     36    151    495       C  
ATOM   2592  CZ  TYR A 271      -5.949 -19.340  -0.289  1.00 63.66           C  
ANISOU 2592  CZ  TYR A 271     7892   6826   9469     75    103    465       C  
ATOM   2593  OH  TYR A 271      -5.454 -18.337   0.516  1.00 65.12           O  
ANISOU 2593  OH  TYR A 271     8026   6977   9738     58    154    389       O  
ATOM   2594  N   MET A 272      -5.272 -22.340  -5.254  1.00 61.24           N  
ANISOU 2594  N   MET A 272     7969   6610   8690    -33      4    814       N  
ATOM   2595  CA  MET A 272      -3.958 -22.030  -5.797  1.00 62.92           C  
ANISOU 2595  CA  MET A 272     8259   6821   8826   -122     81    840       C  
ATOM   2596  C   MET A 272      -4.108 -21.016  -6.938  1.00 64.71           C  
ANISOU 2596  C   MET A 272     8618   6932   9037   -152     23    946       C  
ATOM   2597  O   MET A 272      -3.345 -20.065  -7.000  1.00 64.86           O  
ANISOU 2597  O   MET A 272     8681   6884   9078   -207     72    960       O  
ATOM   2598  CB  MET A 272      -3.348 -23.320  -6.345  1.00 63.75           C  
ANISOU 2598  CB  MET A 272     8378   7036   8809   -164    125    834       C  
ATOM   2599  CG  MET A 272      -1.931 -23.568  -5.926  1.00 66.44           C  
ANISOU 2599  CG  MET A 272     8682   7443   9119   -224    239    764       C  
ATOM   2600  SD  MET A 272      -1.488 -25.341  -5.884  1.00 71.87           S  
ANISOU 2600  SD  MET A 272     9296   8270   9743   -218    275    702       S  
ATOM   2601  CE  MET A 272      -2.126 -25.918  -7.449  1.00 69.86           C  
ANISOU 2601  CE  MET A 272     9128   8028   9387   -234    215    774       C  
ATOM   2602  N   LEU A 273      -5.146 -21.188  -7.788  1.00 66.06           N  
ANISOU 2602  N   LEU A 273     8846   7072   9180   -112    -90   1020       N  
ATOM   2603  CA  LEU A 273      -5.493 -20.336  -8.935  1.00 67.69           C  
ANISOU 2603  CA  LEU A 273     9190   7169   9359   -128   -177   1140       C  
ATOM   2604  C   LEU A 273      -6.315 -19.096  -8.577  1.00 70.73           C  
ANISOU 2604  C   LEU A 273     9566   7411   9897    -62   -269   1161       C  
ATOM   2605  O   LEU A 273      -6.233 -18.100  -9.286  1.00 70.75           O  
ANISOU 2605  O   LEU A 273     9684   7298   9901    -89   -319   1260       O  
ATOM   2606  CB  LEU A 273      -6.266 -21.151  -9.965  1.00 66.84           C  
ANISOU 2606  CB  LEU A 273     9139   7104   9152   -105   -271   1198       C  
ATOM   2607  CG  LEU A 273      -5.528 -21.520 -11.212  1.00 67.15           C  
ANISOU 2607  CG  LEU A 273     9266   7230   9016   -194   -218   1234       C  
ATOM   2608  CD1 LEU A 273      -4.267 -22.316 -10.902  1.00 67.53           C  
ANISOU 2608  CD1 LEU A 273     9239   7390   9030   -251    -72   1137       C  
ATOM   2609  CD2 LEU A 273      -6.420 -22.307 -12.105  1.00 67.57           C  
ANISOU 2609  CD2 LEU A 273     9327   7345   9003   -151   -310   1250       C  
ATOM   2610  N   GLY A 274      -7.130 -19.180  -7.525  1.00 72.99           N  
ANISOU 2610  N   GLY A 274     9718   7704  10311     21   -296   1070       N  
ATOM   2611  CA  GLY A 274      -7.947 -18.065  -7.052  1.00 75.46           C  
ANISOU 2611  CA  GLY A 274     9990   7889  10794     90   -380   1056       C  
ATOM   2612  C   GLY A 274      -7.101 -16.932  -6.508  1.00 77.93           C  
ANISOU 2612  C   GLY A 274    10304   8115  11191     47   -310   1038       C  
ATOM   2613  O   GLY A 274      -7.418 -15.753  -6.695  1.00 78.15           O  
ANISOU 2613  O   GLY A 274    10380   7993  11321     64   -382   1091       O  
ATOM   2614  N   SER A 275      -5.997 -17.289  -5.850  1.00 79.50           N  
ANISOU 2614  N   SER A 275    10449   8406  11352    -10   -172    963       N  
ATOM   2615  CA  SER A 275      -5.071 -16.309  -5.318  1.00 81.55           C  
ANISOU 2615  CA  SER A 275    10697   8604  11685    -59    -89    925       C  
ATOM   2616  C   SER A 275      -4.140 -15.818  -6.442  1.00 83.14           C  
ANISOU 2616  C   SER A 275    11051   8744  11795   -157    -51   1033       C  
ATOM   2617  O   SER A 275      -3.929 -14.610  -6.546  1.00 83.28           O  
ANISOU 2617  O   SER A 275    11114   8628  11900   -185    -49   1065       O  
ATOM   2618  CB  SER A 275      -4.281 -16.907  -4.158  1.00 83.44           C  
ANISOU 2618  CB  SER A 275    10817   8973  11913    -78     33    797       C  
ATOM   2619  OG  SER A 275      -5.161 -17.388  -3.154  1.00 85.85           O  
ANISOU 2619  OG  SER A 275    10997   9344  12279     -1      5    709       O  
ATOM   2620  N   LEU A 276      -3.615 -16.749  -7.297  1.00 83.98           N  
ANISOU 2620  N   LEU A 276    11234   8947  11728   -215    -16   1083       N  
ATOM   2621  CA  LEU A 276      -2.747 -16.448  -8.456  1.00 85.22           C  
ANISOU 2621  CA  LEU A 276    11542   9073  11765   -324     30   1182       C  
ATOM   2622  C   LEU A 276      -3.513 -15.589  -9.506  1.00 86.45           C  
ANISOU 2622  C   LEU A 276    11839   9083  11923   -311   -100   1333       C  
ATOM   2623  O   LEU A 276      -3.340 -14.371  -9.492  1.00 87.10           O  
ANISOU 2623  O   LEU A 276    11957   9020  12116   -321   -113   1369       O  
ATOM   2624  CB  LEU A 276      -2.108 -17.740  -9.044  1.00 85.41           C  
ANISOU 2624  CB  LEU A 276    11586   9250  11616   -382     98   1170       C  
ATOM   2625  CG  LEU A 276      -1.651 -17.738 -10.515  1.00 86.80           C  
ANISOU 2625  CG  LEU A 276    11924   9421  11637   -493    131   1272       C  
ATOM   2626  CD1 LEU A 276      -0.414 -16.908 -10.708  1.00 87.59           C  
ANISOU 2626  CD1 LEU A 276    12074   9451  11756   -598    243   1273       C  
ATOM   2627  CD2 LEU A 276      -1.427 -19.148 -11.027  1.00 87.12           C  
ANISOU 2627  CD2 LEU A 276    11952   9618  11531   -533    184   1232       C  
ATOM   2628  N   LEU A 277      -4.383 -16.172 -10.358  1.00 86.66           N  
ANISOU 2628  N   LEU A 277    11939   9139  11850   -280   -207   1415       N  
ATOM   2629  CA  LEU A 277      -5.199 -15.368 -11.271  1.00 87.52           C  
ANISOU 2629  CA  LEU A 277    12175   9107  11973   -251   -354   1556       C  
ATOM   2630  C   LEU A 277      -6.341 -14.958 -10.370  1.00 88.37           C  
ANISOU 2630  C   LEU A 277    12164   9132  12282   -123   -461   1496       C  
ATOM   2631  O   LEU A 277      -7.126 -15.818  -9.981  1.00 88.54           O  
ANISOU 2631  O   LEU A 277    12079   9238  12325    -43   -508   1421       O  
ATOM   2632  CB  LEU A 277      -5.726 -16.159 -12.485  1.00 87.79           C  
ANISOU 2632  CB  LEU A 277    12315   9205  11838   -253   -445   1649       C  
ATOM   2633  CG  LEU A 277      -5.630 -17.678 -12.464  1.00 89.34           C  
ANISOU 2633  CG  LEU A 277    12429   9582  11934   -240   -407   1564       C  
ATOM   2634  CD1 LEU A 277      -6.915 -18.303 -12.982  1.00 89.93           C  
ANISOU 2634  CD1 LEU A 277    12497   9669  12002   -142   -567   1591       C  
ATOM   2635  CD2 LEU A 277      -4.390 -18.160 -13.232  1.00 89.93           C  
ANISOU 2635  CD2 LEU A 277    12587   9763  11818   -369   -285   1582       C  
ATOM   2636  N   HIS A 278      -6.360 -13.694  -9.923  1.00 88.74           N  
ANISOU 2636  N   HIS A 278    12208   9023  12487   -114   -476   1503       N  
ATOM   2637  CA  HIS A 278      -7.326 -13.243  -8.923  1.00 89.47           C  
ANISOU 2637  CA  HIS A 278    12163   9040  12793     -5   -550   1411       C  
ATOM   2638  C   HIS A 278      -8.806 -13.410  -9.285  1.00 88.76           C  
ANISOU 2638  C   HIS A 278    12052   8915  12757    110   -728   1432       C  
ATOM   2639  O   HIS A 278      -9.291 -12.963 -10.330  1.00 88.95           O  
ANISOU 2639  O   HIS A 278    12207   8851  12740    128   -863   1566       O  
ATOM   2640  CB  HIS A 278      -7.056 -11.812  -8.458  1.00 91.38           C  
ANISOU 2640  CB  HIS A 278    12409   9106  13204    -18   -543   1416       C  
ATOM   2641  CG  HIS A 278      -6.352 -11.797  -7.136  1.00 95.42           C  
ANISOU 2641  CG  HIS A 278    12773   9681  13802    -38   -398   1255       C  
ATOM   2642  ND1 HIS A 278      -5.002 -11.490  -7.035  1.00 97.71           N  
ANISOU 2642  ND1 HIS A 278    13094  10001  14032   -148   -246   1241       N  
ATOM   2643  CD2 HIS A 278      -6.811 -12.153  -5.913  1.00 97.02           C  
ANISOU 2643  CD2 HIS A 278    12796   9947  14121     33   -383   1099       C  
ATOM   2644  CE1 HIS A 278      -4.700 -11.617  -5.753  1.00 98.42           C  
ANISOU 2644  CE1 HIS A 278    13024  10160  14211   -131   -157   1081       C  
ATOM   2645  NE2 HIS A 278      -5.753 -12.023  -5.039  1.00 98.39           N  
ANISOU 2645  NE2 HIS A 278    12894  10183  14306    -28   -232    995       N  
ATOM   2646  N   TRP A 279      -9.504 -14.092  -8.366  1.00 87.66           N  
ANISOU 2646  N   TRP A 279    11743   8859  12704    184   -722   1289       N  
ATOM   2647  CA  TRP A 279     -10.930 -14.392  -8.405  1.00 87.03           C  
ANISOU 2647  CA  TRP A 279    11590   8775  12703    295   -861   1252       C  
ATOM   2648  C   TRP A 279     -11.657 -13.581  -7.308  1.00 85.43           C  
ANISOU 2648  C   TRP A 279    11239   8480  12740    373   -897   1130       C  
ATOM   2649  O   TRP A 279     -10.997 -13.024  -6.423  1.00 85.54           O  
ANISOU 2649  O   TRP A 279    11189   8474  12837    338   -793   1055       O  
ATOM   2650  CB  TRP A 279     -11.149 -15.920  -8.244  1.00 87.38           C  
ANISOU 2650  CB  TRP A 279    11563   9010  12629    300   -809   1183       C  
ATOM   2651  CG  TRP A 279     -10.959 -16.727  -9.505  1.00 88.18           C  
ANISOU 2651  CG  TRP A 279    11792   9182  12530    263   -843   1291       C  
ATOM   2652  CD1 TRP A 279     -10.999 -16.272 -10.794  1.00 89.21           C  
ANISOU 2652  CD1 TRP A 279    12090   9232  12575    243   -945   1442       C  
ATOM   2653  CD2 TRP A 279     -10.754 -18.144  -9.587  1.00 88.18           C  
ANISOU 2653  CD2 TRP A 279    11758   9351  12394    241   -780   1250       C  
ATOM   2654  NE1 TRP A 279     -10.783 -17.312 -11.669  1.00 89.45           N  
ANISOU 2654  NE1 TRP A 279    12189   9383  12413    203   -938   1487       N  
ATOM   2655  CE2 TRP A 279     -10.648 -18.475 -10.955  1.00 88.99           C  
ANISOU 2655  CE2 TRP A 279    12004   9475  12334    206   -840   1367       C  
ATOM   2656  CE3 TRP A 279     -10.640 -19.163  -8.638  1.00 88.57           C  
ANISOU 2656  CE3 TRP A 279    11673   9533  12445    246   -680   1128       C  
ATOM   2657  CZ2 TRP A 279     -10.424 -19.777 -11.390  1.00 89.44           C  
ANISOU 2657  CZ2 TRP A 279    12060   9679  12243    177   -799   1350       C  
ATOM   2658  CZ3 TRP A 279     -10.429 -20.452  -9.074  1.00 89.37           C  
ANISOU 2658  CZ3 TRP A 279    11783   9767  12408    220   -645   1125       C  
ATOM   2659  CH2 TRP A 279     -10.323 -20.749 -10.434  1.00 89.53           C  
ANISOU 2659  CH2 TRP A 279    11932   9803  12281    188   -704   1227       C  
ATOM   2660  N   PRO A 280     -12.998 -13.449  -7.365  1.00 83.84           N  
ANISOU 2660  N   PRO A 280    10978   8216  12661    477  -1048   1099       N  
ATOM   2661  CA  PRO A 280     -13.693 -12.650  -6.340  1.00 83.02           C  
ANISOU 2661  CA  PRO A 280    10722   8022  12799    549  -1081    965       C  
ATOM   2662  C   PRO A 280     -13.582 -13.239  -4.941  1.00 82.15           C  
ANISOU 2662  C   PRO A 280    10441   8053  12720    535   -934    789       C  
ATOM   2663  O   PRO A 280     -13.445 -14.448  -4.813  1.00 82.28           O  
ANISOU 2663  O   PRO A 280    10433   8232  12599    510   -859    762       O  
ATOM   2664  CB  PRO A 280     -15.155 -12.653  -6.803  1.00 83.84           C  
ANISOU 2664  CB  PRO A 280    10789   8068  12997    659  -1266    954       C  
ATOM   2665  CG  PRO A 280     -15.148 -13.185  -8.185  1.00 84.43           C  
ANISOU 2665  CG  PRO A 280    11020   8175  12884    646  -1347   1107       C  
ATOM   2666  CD  PRO A 280     -13.942 -14.029  -8.337  1.00 83.07           C  
ANISOU 2666  CD  PRO A 280    10935   8136  12493    534  -1191   1165       C  
ATOM   2667  N   CYS A 281     -13.673 -12.404  -3.890  1.00 81.26           N  
ANISOU 2667  N   CYS A 281    10208   7877  12790    552   -899    666       N  
ATOM   2668  CA  CYS A 281     -13.626 -12.910  -2.512  1.00 80.96           C  
ANISOU 2668  CA  CYS A 281    10006   7977  12777    538   -766    494       C  
ATOM   2669  C   CYS A 281     -14.819 -13.836  -2.205  1.00 79.90           C  
ANISOU 2669  C   CYS A 281     9763   7940  12657    598   -804    402       C  
ATOM   2670  O   CYS A 281     -14.711 -14.672  -1.315  1.00 80.02           O  
ANISOU 2670  O   CYS A 281     9690   8110  12604    569   -688    309       O  
ATOM   2671  CB  CYS A 281     -13.505 -11.780  -1.490  1.00 82.27           C  
ANISOU 2671  CB  CYS A 281    10060   8056  13142    546   -732    369       C  
ATOM   2672  SG  CYS A 281     -15.031 -10.826  -1.238  1.00 87.63           S  
ANISOU 2672  SG  CYS A 281    10627   8562  14107    661   -901    275       S  
ATOM   2673  N   ASP A 282     -15.934 -13.722  -2.972  1.00 78.54           N  
ANISOU 2673  N   ASP A 282     9601   7675  12565    679   -968    433       N  
ATOM   2674  CA  ASP A 282     -17.107 -14.595  -2.868  1.00 77.48           C  
ANISOU 2674  CA  ASP A 282     9372   7618  12450    735  -1016    350       C  
ATOM   2675  C   ASP A 282     -16.647 -16.047  -3.159  1.00 75.06           C  
ANISOU 2675  C   ASP A 282     9123   7481  11916    681   -933    409       C  
ATOM   2676  O   ASP A 282     -17.008 -16.977  -2.439  1.00 75.32           O  
ANISOU 2676  O   ASP A 282     9052   7643  11923    674   -854    308       O  
ATOM   2677  CB  ASP A 282     -18.192 -14.177  -3.899  1.00 80.42           C  
ANISOU 2677  CB  ASP A 282     9780   7851  12924    829  -1226    404       C  
ATOM   2678  CG  ASP A 282     -18.599 -12.703  -3.898  1.00 87.15           C  
ANISOU 2678  CG  ASP A 282    10620   8497  13996    887  -1346    395       C  
ATOM   2679  OD1 ASP A 282     -19.697 -12.385  -3.362  1.00 88.28           O  
ANISOU 2679  OD1 ASP A 282    10605   8586  14350    957  -1404    240       O  
ATOM   2680  OD2 ASP A 282     -17.838 -11.868  -4.465  1.00 89.85           O  
ANISOU 2680  OD2 ASP A 282    11107   8723  14308    860  -1384    540       O  
ATOM   2681  N   PHE A 283     -15.808 -16.221  -4.190  1.00 72.52           N  
ANISOU 2681  N   PHE A 283     8967   7157  11431    636   -942    569       N  
ATOM   2682  CA  PHE A 283     -15.287 -17.518  -4.563  1.00 70.51           C  
ANISOU 2682  CA  PHE A 283     8767   7050  10975    584   -868    620       C  
ATOM   2683  C   PHE A 283     -14.019 -17.893  -3.801  1.00 68.60           C  
ANISOU 2683  C   PHE A 283     8518   6919  10630    499   -692    598       C  
ATOM   2684  O   PHE A 283     -13.762 -19.079  -3.618  1.00 68.96           O  
ANISOU 2684  O   PHE A 283     8545   7100  10557    468   -615    583       O  
ATOM   2685  CB  PHE A 283     -15.059 -17.593  -6.066  1.00 70.20           C  
ANISOU 2685  CB  PHE A 283     8895   6974  10804    575   -962    781       C  
ATOM   2686  CG  PHE A 283     -14.920 -19.015  -6.529  1.00 70.81           C  
ANISOU 2686  CG  PHE A 283     8995   7197  10712    546   -920    802       C  
ATOM   2687  CD1 PHE A 283     -15.804 -19.988  -6.104  1.00 71.56           C  
ANISOU 2687  CD1 PHE A 283     8967   7384  10840    582   -906    695       C  
ATOM   2688  CD2 PHE A 283     -13.900 -19.384  -7.379  1.00 71.59           C  
ANISOU 2688  CD2 PHE A 283     9234   7338  10630    479   -893    920       C  
ATOM   2689  CE1 PHE A 283     -15.666 -21.304  -6.519  1.00 72.23           C  
ANISOU 2689  CE1 PHE A 283     9067   7590  10785    555   -867    711       C  
ATOM   2690  CE2 PHE A 283     -13.774 -20.699  -7.804  1.00 72.33           C  
ANISOU 2690  CE2 PHE A 283     9338   7561  10584    455   -858    925       C  
ATOM   2691  CZ  PHE A 283     -14.655 -21.650  -7.368  1.00 72.04           C  
ANISOU 2691  CZ  PHE A 283     9176   7605  10591    495   -848    822       C  
ATOM   2692  N   ASP A 284     -13.226 -16.909  -3.353  1.00 66.51           N  
ANISOU 2692  N   ASP A 284     8262   6594  10416    463   -634    591       N  
ATOM   2693  CA  ASP A 284     -12.017 -17.196  -2.576  1.00 65.18           C  
ANISOU 2693  CA  ASP A 284     8075   6531  10161    388   -476    554       C  
ATOM   2694  C   ASP A 284     -12.434 -17.706  -1.193  1.00 63.06           C  
ANISOU 2694  C   ASP A 284     7645   6368   9947    403   -399    402       C  
ATOM   2695  O   ASP A 284     -11.894 -18.699  -0.705  1.00 63.21           O  
ANISOU 2695  O   ASP A 284     7641   6525   9852    363   -300    378       O  
ATOM   2696  CB  ASP A 284     -11.122 -15.944  -2.420  1.00 67.29           C  
ANISOU 2696  CB  ASP A 284     8382   6701  10482    345   -434    571       C  
ATOM   2697  CG  ASP A 284     -10.359 -15.510  -3.657  1.00 71.90           C  
ANISOU 2697  CG  ASP A 284     9137   7200  10982    299   -467    725       C  
ATOM   2698  OD1 ASP A 284      -9.962 -14.320  -3.723  1.00 72.36           O  
ANISOU 2698  OD1 ASP A 284     9236   7131  11126    279   -472    752       O  
ATOM   2699  OD2 ASP A 284     -10.163 -16.354  -4.563  1.00 74.31           O  
ANISOU 2699  OD2 ASP A 284     9535   7564  11134    277   -485    816       O  
ATOM   2700  N   LEU A 285     -13.414 -17.036  -0.576  1.00 61.00           N  
ANISOU 2700  N   LEU A 285     7276   6040   9862    458   -447    298       N  
ATOM   2701  CA  LEU A 285     -13.916 -17.409   0.733  1.00 59.63           C  
ANISOU 2701  CA  LEU A 285     6951   5963   9744    463   -374    146       C  
ATOM   2702  C   LEU A 285     -14.761 -18.674   0.710  1.00 57.39           C  
ANISOU 2702  C   LEU A 285     6624   5774   9409    484   -382    123       C  
ATOM   2703  O   LEU A 285     -14.796 -19.389   1.710  1.00 57.60           O  
ANISOU 2703  O   LEU A 285     6573   5928   9383    453   -281     47       O  
ATOM   2704  CB  LEU A 285     -14.637 -16.251   1.392  1.00 60.27           C  
ANISOU 2704  CB  LEU A 285     6921   5943  10035    506   -412     25       C  
ATOM   2705  CG  LEU A 285     -13.680 -15.412   2.205  1.00 62.82           C  
ANISOU 2705  CG  LEU A 285     7222   6260  10386    459   -321    -25       C  
ATOM   2706  CD1 LEU A 285     -13.790 -13.933   1.862  1.00 63.83           C  
ANISOU 2706  CD1 LEU A 285     7363   6198  10692    491   -406    -21       C  
ATOM   2707  CD2 LEU A 285     -13.811 -15.712   3.692  1.00 63.79           C  
ANISOU 2707  CD2 LEU A 285     7204   6521  10511    432   -203   -185       C  
ATOM   2708  N   PHE A 286     -15.370 -19.019  -0.448  1.00 54.82           N  
ANISOU 2708  N   PHE A 286     6360   5396   9075    527   -498    201       N  
ATOM   2709  CA  PHE A 286     -16.080 -20.284  -0.575  1.00 52.66           C  
ANISOU 2709  CA  PHE A 286     6051   5212   8744    540   -501    185       C  
ATOM   2710  C   PHE A 286     -15.037 -21.419  -0.445  1.00 50.77           C  
ANISOU 2710  C   PHE A 286     5868   5107   8317    472   -388    243       C  
ATOM   2711  O   PHE A 286     -15.071 -22.143   0.540  1.00 50.91           O  
ANISOU 2711  O   PHE A 286     5807   5232   8305    445   -292    171       O  
ATOM   2712  CB  PHE A 286     -16.849 -20.379  -1.911  1.00 52.26           C  
ANISOU 2712  CB  PHE A 286     6064   5084   8709    598   -652    258       C  
ATOM   2713  CG  PHE A 286     -17.204 -21.797  -2.319  1.00 52.74           C  
ANISOU 2713  CG  PHE A 286     6127   5244   8669    595   -646    273       C  
ATOM   2714  CD1 PHE A 286     -18.256 -22.465  -1.721  1.00 53.41           C  
ANISOU 2714  CD1 PHE A 286     6087   5377   8831    621   -637    158       C  
ATOM   2715  CD2 PHE A 286     -16.471 -22.465  -3.287  1.00 53.30           C  
ANISOU 2715  CD2 PHE A 286     6317   5360   8573    558   -639    392       C  
ATOM   2716  CE1 PHE A 286     -18.567 -23.767  -2.084  1.00 53.96           C  
ANISOU 2716  CE1 PHE A 286     6154   5528   8819    614   -625    169       C  
ATOM   2717  CE2 PHE A 286     -16.778 -23.772  -3.637  1.00 53.80           C  
ANISOU 2717  CE2 PHE A 286     6372   5511   8558    554   -630    394       C  
ATOM   2718  CZ  PHE A 286     -17.827 -24.410  -3.041  1.00 53.62           C  
ANISOU 2718  CZ  PHE A 286     6228   5526   8620    583   -625    286       C  
ATOM   2719  N   LEU A 287     -14.037 -21.474  -1.352  1.00 48.88           N  
ANISOU 2719  N   LEU A 287     5758   4855   7957    439   -394    366       N  
ATOM   2720  CA  LEU A 287     -13.004 -22.500  -1.360  1.00 47.71           C  
ANISOU 2720  CA  LEU A 287     5659   4820   7650    380   -302    414       C  
ATOM   2721  C   LEU A 287     -12.337 -22.677  -0.012  1.00 47.55           C  
ANISOU 2721  C   LEU A 287     5568   4892   7605    338   -176    341       C  
ATOM   2722  O   LEU A 287     -12.082 -23.802   0.410  1.00 47.58           O  
ANISOU 2722  O   LEU A 287     5550   5003   7525    314   -109    332       O  
ATOM   2723  CB  LEU A 287     -11.965 -22.191  -2.426  1.00 47.09           C  
ANISOU 2723  CB  LEU A 287     5718   4701   7472    342   -317    531       C  
ATOM   2724  CG  LEU A 287     -12.438 -22.338  -3.850  1.00 47.70           C  
ANISOU 2724  CG  LEU A 287     5889   4731   7505    364   -427    623       C  
ATOM   2725  CD1 LEU A 287     -11.386 -21.862  -4.794  1.00 48.28           C  
ANISOU 2725  CD1 LEU A 287     6099   4771   7474    309   -420    730       C  
ATOM   2726  CD2 LEU A 287     -12.755 -23.768  -4.169  1.00 48.02           C  
ANISOU 2726  CD2 LEU A 287     5911   4869   7466    366   -421    618       C  
ATOM   2727  N   MET A 288     -12.127 -21.572   0.692  1.00 47.29           N  
ANISOU 2727  N   MET A 288     5497   4818   7655    334   -149    284       N  
ATOM   2728  CA  MET A 288     -11.510 -21.586   2.007  1.00 47.70           C  
ANISOU 2728  CA  MET A 288     5481   4959   7683    296    -39    206       C  
ATOM   2729  C   MET A 288     -12.341 -22.304   3.067  1.00 46.78           C  
ANISOU 2729  C   MET A 288     5254   4933   7587    303      6    110       C  
ATOM   2730  O   MET A 288     -11.777 -22.987   3.919  1.00 46.89           O  
ANISOU 2730  O   MET A 288     5241   5058   7515    265     95     85       O  
ATOM   2731  CB  MET A 288     -11.291 -20.154   2.471  1.00 49.83           C  
ANISOU 2731  CB  MET A 288     5719   5152   8062    296    -33    147       C  
ATOM   2732  CG  MET A 288     -10.160 -19.457   1.788  1.00 55.04           C  
ANISOU 2732  CG  MET A 288     6478   5748   8686    262    -28    225       C  
ATOM   2733  SD  MET A 288      -9.279 -18.384   2.957  1.00 68.33           S  
ANISOU 2733  SD  MET A 288     8090   7411  10459    236     44    118       S  
ATOM   2734  CE  MET A 288     -10.703 -17.606   3.905  1.00 67.87           C  
ANISOU 2734  CE  MET A 288     7866   7358  10565    286     30    -45       C  
ATOM   2735  N   ASN A 289     -13.672 -22.102   3.057  1.00 45.56           N  
ANISOU 2735  N   ASN A 289     5031   4728   7550    348    -54     50       N  
ATOM   2736  CA  ASN A 289     -14.565 -22.676   4.060  1.00 44.60           C  
ANISOU 2736  CA  ASN A 289     4796   4684   7465    346     -5    -57       C  
ATOM   2737  C   ASN A 289     -15.026 -24.080   3.737  1.00 43.02           C  
ANISOU 2737  C   ASN A 289     4605   4550   7191    341      3    -20       C  
ATOM   2738  O   ASN A 289     -15.391 -24.816   4.646  1.00 43.03           O  
ANISOU 2738  O   ASN A 289     4542   4646   7163    311     81    -77       O  
ATOM   2739  CB  ASN A 289     -15.730 -21.751   4.307  1.00 46.32           C  
ANISOU 2739  CB  ASN A 289     4920   4818   7863    392    -64   -165       C  
ATOM   2740  CG  ASN A 289     -15.278 -20.438   4.881  1.00 50.46           C  
ANISOU 2740  CG  ASN A 289     5401   5301   8470    385    -39   -239       C  
ATOM   2741  OD1 ASN A 289     -14.428 -20.400   5.776  1.00 52.48           O  
ANISOU 2741  OD1 ASN A 289     5634   5651   8657    337     61   -278       O  
ATOM   2742  ND2 ASN A 289     -15.825 -19.333   4.383  1.00 50.98           N  
ANISOU 2742  ND2 ASN A 289     5454   5226   8689    435   -134   -260       N  
ATOM   2743  N   ILE A 290     -15.025 -24.458   2.455  1.00 41.70           N  
ANISOU 2743  N   ILE A 290     4519   4333   6993    366    -77     75       N  
ATOM   2744  CA  ILE A 290     -15.345 -25.825   2.071  1.00 40.94           C  
ANISOU 2744  CA  ILE A 290     4433   4294   6827    360    -70    112       C  
ATOM   2745  C   ILE A 290     -14.096 -26.724   2.233  1.00 41.35           C  
ANISOU 2745  C   ILE A 290     4551   4432   6729    309      6    187       C  
ATOM   2746  O   ILE A 290     -14.254 -27.935   2.343  1.00 42.21           O  
ANISOU 2746  O   ILE A 290     4651   4603   6783    292     40    202       O  
ATOM   2747  CB  ILE A 290     -15.971 -25.953   0.662  1.00 40.30           C  
ANISOU 2747  CB  ILE A 290     4398   4140   6774    408   -189    163       C  
ATOM   2748  CG1 ILE A 290     -16.917 -27.181   0.620  1.00 40.85           C  
ANISOU 2748  CG1 ILE A 290     4408   4258   6855    414   -181    124       C  
ATOM   2749  CG2 ILE A 290     -14.893 -25.955  -0.434  1.00 40.28           C  
ANISOU 2749  CG2 ILE A 290     4526   4116   6663    395   -224    286       C  
ATOM   2750  CD1 ILE A 290     -17.090 -27.958  -0.720  1.00 42.10           C  
ANISOU 2750  CD1 ILE A 290     4630   4412   6955    430   -248    197       C  
ATOM   2751  N   PHE A 291     -12.865 -26.148   2.272  1.00 40.47           N  
ANISOU 2751  N   PHE A 291     4497   4317   6561    285     31    227       N  
ATOM   2752  CA  PHE A 291     -11.632 -26.909   2.421  1.00 40.05           C  
ANISOU 2752  CA  PHE A 291     4495   4340   6383    243     93    282       C  
ATOM   2753  C   PHE A 291     -11.556 -27.806   3.675  1.00 39.44           C  
ANISOU 2753  C   PHE A 291     4361   4369   6255    213    180    245       C  
ATOM   2754  O   PHE A 291     -11.095 -28.934   3.519  1.00 39.38           O  
ANISOU 2754  O   PHE A 291     4385   4409   6167    196    200    298       O  
ATOM   2755  CB  PHE A 291     -10.421 -26.002   2.340  1.00 40.40           C  
ANISOU 2755  CB  PHE A 291     4592   4359   6398    221    109    306       C  
ATOM   2756  CG  PHE A 291      -9.145 -26.796   2.257  1.00 41.83           C  
ANISOU 2756  CG  PHE A 291     4821   4610   6464    184    159    353       C  
ATOM   2757  CD1 PHE A 291      -8.833 -27.519   1.116  1.00 42.94           C  
ANISOU 2757  CD1 PHE A 291     5027   4747   6540    177    133    424       C  
ATOM   2758  CD2 PHE A 291      -8.277 -26.860   3.333  1.00 42.67           C  
ANISOU 2758  CD2 PHE A 291     4897   4788   6527    157    230    315       C  
ATOM   2759  CE1 PHE A 291      -7.656 -28.253   1.040  1.00 43.35           C  
ANISOU 2759  CE1 PHE A 291     5110   4858   6505    144    177    451       C  
ATOM   2760  CE2 PHE A 291      -7.119 -27.616   3.262  1.00 43.29           C  
ANISOU 2760  CE2 PHE A 291     5009   4924   6514    130    264    350       C  
ATOM   2761  CZ  PHE A 291      -6.812 -28.294   2.114  1.00 43.05           C  
ANISOU 2761  CZ  PHE A 291     5039   4881   6438    124    238    414       C  
ATOM   2762  N   PRO A 292     -12.001 -27.410   4.897  1.00 39.10           N  
ANISOU 2762  N   PRO A 292     4237   4365   6252    203    229    158       N  
ATOM   2763  CA  PRO A 292     -11.934 -28.341   6.035  1.00 39.47           C  
ANISOU 2763  CA  PRO A 292     4251   4518   6228    166    308    142       C  
ATOM   2764  C   PRO A 292     -12.895 -29.533   5.909  1.00 40.41           C  
ANISOU 2764  C   PRO A 292     4348   4654   6351    163    314    154       C  
ATOM   2765  O   PRO A 292     -12.688 -30.550   6.567  1.00 40.66           O  
ANISOU 2765  O   PRO A 292     4382   4759   6309    130    370    180       O  
ATOM   2766  CB  PRO A 292     -12.267 -27.458   7.240  1.00 39.90           C  
ANISOU 2766  CB  PRO A 292     4225   4607   6326    152    356     35       C  
ATOM   2767  CG  PRO A 292     -12.160 -26.074   6.753  1.00 40.10           C  
ANISOU 2767  CG  PRO A 292     4251   4544   6443    181    306      4       C  
ATOM   2768  CD  PRO A 292     -12.566 -26.127   5.331  1.00 38.47           C  
ANISOU 2768  CD  PRO A 292     4094   4240   6282    219    219     67       C  
ATOM   2769  N   TYR A 293     -13.932 -29.424   5.061  1.00 40.56           N  
ANISOU 2769  N   TYR A 293     4348   4604   6461    198    253    137       N  
ATOM   2770  CA  TYR A 293     -14.827 -30.541   4.777  1.00 41.27           C  
ANISOU 2770  CA  TYR A 293     4414   4699   6568    197    253    142       C  
ATOM   2771  C   TYR A 293     -14.157 -31.527   3.816  1.00 41.33           C  
ANISOU 2771  C   TYR A 293     4497   4703   6505    199    226    239       C  
ATOM   2772  O   TYR A 293     -14.373 -32.729   3.947  1.00 41.71           O  
ANISOU 2772  O   TYR A 293     4538   4787   6524    177    262    261       O  
ATOM   2773  CB  TYR A 293     -16.169 -30.049   4.251  1.00 42.01           C  
ANISOU 2773  CB  TYR A 293     4451   4722   6789    239    188     74       C  
ATOM   2774  CG  TYR A 293     -16.979 -29.456   5.377  1.00 44.21           C  
ANISOU 2774  CG  TYR A 293     4629   5023   7145    224    238    -46       C  
ATOM   2775  CD1 TYR A 293     -17.593 -30.269   6.318  1.00 45.85           C  
ANISOU 2775  CD1 TYR A 293     4779   5304   7340    175    328    -95       C  
ATOM   2776  CD2 TYR A 293     -17.034 -28.082   5.572  1.00 45.58           C  
ANISOU 2776  CD2 TYR A 293     4770   5151   7398    248    208   -112       C  
ATOM   2777  CE1 TYR A 293     -18.306 -29.732   7.386  1.00 47.03           C  
ANISOU 2777  CE1 TYR A 293     4833   5488   7549    148    389   -217       C  
ATOM   2778  CE2 TYR A 293     -17.727 -27.533   6.648  1.00 46.71           C  
ANISOU 2778  CE2 TYR A 293     4810   5324   7614    229    263   -240       C  
ATOM   2779  CZ  TYR A 293     -18.356 -28.363   7.558  1.00 48.01           C  
ANISOU 2779  CZ  TYR A 293     4914   5572   7755    176    357   -296       C  
ATOM   2780  OH  TYR A 293     -19.033 -27.841   8.638  1.00 50.05           O  
ANISOU 2780  OH  TYR A 293     5068   5873   8074    144    425   -433       O  
ATOM   2781  N   CYS A 294     -13.293 -31.023   2.900  1.00 40.92           N  
ANISOU 2781  N   CYS A 294     4516   4609   6424    217    171    292       N  
ATOM   2782  CA  CYS A 294     -12.482 -31.783   1.940  1.00 41.15           C  
ANISOU 2782  CA  CYS A 294     4615   4638   6381    212    149    370       C  
ATOM   2783  C   CYS A 294     -11.457 -32.672   2.632  1.00 40.80           C  
ANISOU 2783  C   CYS A 294     4587   4663   6254    177    215    405       C  
ATOM   2784  O   CYS A 294     -11.064 -33.693   2.073  1.00 40.97           O  
ANISOU 2784  O   CYS A 294     4637   4693   6238    170    209    450       O  
ATOM   2785  CB  CYS A 294     -11.797 -30.850   0.944  1.00 42.29           C  
ANISOU 2785  CB  CYS A 294     4830   4730   6507    224     94    407       C  
ATOM   2786  SG  CYS A 294     -12.937 -29.928  -0.116  1.00 47.15           S  
ANISOU 2786  SG  CYS A 294     5451   5252   7213    274    -13    393       S  
ATOM   2787  N   THR A 295     -10.953 -32.236   3.799  1.00 40.11           N  
ANISOU 2787  N   THR A 295     4481   4622   6138    157    268    381       N  
ATOM   2788  CA  THR A 295      -9.980 -32.991   4.577  1.00 39.64           C  
ANISOU 2788  CA  THR A 295     4436   4628   5998    130    316    414       C  
ATOM   2789  C   THR A 295     -10.665 -34.173   5.331  1.00 40.20           C  
ANISOU 2789  C   THR A 295     4474   4740   6062    109    359    422       C  
ATOM   2790  O   THR A 295     -10.016 -35.177   5.596  1.00 39.93           O  
ANISOU 2790  O   THR A 295     4462   4735   5973     94    375    473       O  
ATOM   2791  CB  THR A 295      -9.167 -32.038   5.457  1.00 39.39           C  
ANISOU 2791  CB  THR A 295     4401   4634   5933    119    345    382       C  
ATOM   2792  OG1 THR A 295     -10.023 -31.415   6.405  1.00 39.59           O  
ANISOU 2792  OG1 THR A 295     4366   4686   5991    110    380    314       O  
ATOM   2793  CG2 THR A 295      -8.450 -30.975   4.641  1.00 39.34           C  
ANISOU 2793  CG2 THR A 295     4430   4574   5944    130    310    377       C  
ATOM   2794  N   CYS A 296     -11.980 -34.082   5.604  1.00 40.77           N  
ANISOU 2794  N   CYS A 296     4492   4803   6197    106    374    372       N  
ATOM   2795  CA  CYS A 296     -12.736 -35.152   6.253  1.00 41.85           C  
ANISOU 2795  CA  CYS A 296     4598   4969   6333     74    426    377       C  
ATOM   2796  C   CYS A 296     -13.010 -36.261   5.269  1.00 43.52           C  
ANISOU 2796  C   CYS A 296     4821   5137   6578     85    396    416       C  
ATOM   2797  O   CYS A 296     -12.777 -37.426   5.587  1.00 44.22           O  
ANISOU 2797  O   CYS A 296     4924   5241   6637     61    426    467       O  
ATOM   2798  CB  CYS A 296     -14.036 -34.623   6.842  1.00 41.79           C  
ANISOU 2798  CB  CYS A 296     4516   4969   6391     60    463    288       C  
ATOM   2799  SG  CYS A 296     -13.804 -33.323   8.064  1.00 44.16           S  
ANISOU 2799  SG  CYS A 296     4785   5324   6669     44    501    214       S  
ATOM   2800  N   ILE A 297     -13.506 -35.913   4.071  1.00 43.80           N  
ANISOU 2800  N   ILE A 297     4851   5114   6675    122    333    392       N  
ATOM   2801  CA  ILE A 297     -13.806 -36.900   3.038  1.00 44.47           C  
ANISOU 2801  CA  ILE A 297     4940   5165   6793    133    300    413       C  
ATOM   2802  C   ILE A 297     -12.505 -37.617   2.565  1.00 45.09           C  
ANISOU 2802  C   ILE A 297     5075   5249   6807    130    287    482       C  
ATOM   2803  O   ILE A 297     -12.558 -38.796   2.218  1.00 45.42           O  
ANISOU 2803  O   ILE A 297     5112   5280   6864    122    293    506       O  
ATOM   2804  CB  ILE A 297     -14.665 -36.293   1.895  1.00 45.11           C  
ANISOU 2804  CB  ILE A 297     5001   5193   6945    174    225    367       C  
ATOM   2805  CG1 ILE A 297     -14.752 -37.234   0.681  1.00 46.74           C  
ANISOU 2805  CG1 ILE A 297     5217   5375   7167    187    183    384       C  
ATOM   2806  CG2 ILE A 297     -14.204 -34.906   1.502  1.00 45.53           C  
ANISOU 2806  CG2 ILE A 297     5095   5223   6982    200    173    369       C  
ATOM   2807  CD1 ILE A 297     -15.381 -36.656  -0.614  1.00 48.55           C  
ANISOU 2807  CD1 ILE A 297     5459   5562   7425    230     87    363       C  
ATOM   2808  N   ALA A 298     -11.339 -36.935   2.625  1.00 44.95           N  
ANISOU 2808  N   ALA A 298     5102   5247   6728    133    277    504       N  
ATOM   2809  CA  ALA A 298     -10.046 -37.534   2.288  1.00 45.12           C  
ANISOU 2809  CA  ALA A 298     5167   5280   6698    128    270    549       C  
ATOM   2810  C   ALA A 298      -9.611 -38.459   3.409  1.00 45.47           C  
ANISOU 2810  C   ALA A 298     5206   5359   6712    107    314    586       C  
ATOM   2811  O   ALA A 298      -9.110 -39.546   3.132  1.00 45.48           O  
ANISOU 2811  O   ALA A 298     5214   5349   6716    104    308    619       O  
ATOM   2812  CB  ALA A 298      -9.002 -36.457   2.070  1.00 45.29           C  
ANISOU 2812  CB  ALA A 298     5227   5307   6673    132    255    546       C  
ATOM   2813  N   TYR A 299      -9.809 -38.033   4.682  1.00 45.76           N  
ANISOU 2813  N   TYR A 299     5230   5438   6720     90    356    578       N  
ATOM   2814  CA  TYR A 299      -9.526 -38.842   5.879  1.00 46.50           C  
ANISOU 2814  CA  TYR A 299     5329   5571   6768     64    396    621       C  
ATOM   2815  C   TYR A 299     -10.366 -40.103   5.918  1.00 47.02           C  
ANISOU 2815  C   TYR A 299     5377   5611   6877     44    419    650       C  
ATOM   2816  O   TYR A 299      -9.960 -41.104   6.492  1.00 47.23           O  
ANISOU 2816  O   TYR A 299     5424   5645   6877     27    434    711       O  
ATOM   2817  CB  TYR A 299      -9.824 -38.061   7.153  1.00 46.64           C  
ANISOU 2817  CB  TYR A 299     5330   5648   6742     42    441    592       C  
ATOM   2818  CG  TYR A 299      -8.574 -37.574   7.830  1.00 47.78           C  
ANISOU 2818  CG  TYR A 299     5502   5844   6807     44    435    604       C  
ATOM   2819  CD1 TYR A 299      -7.516 -38.433   8.079  1.00 49.06           C  
ANISOU 2819  CD1 TYR A 299     5697   6022   6923     46    418    667       C  
ATOM   2820  CD2 TYR A 299      -8.453 -36.258   8.241  1.00 48.81           C  
ANISOU 2820  CD2 TYR A 299     5620   6002   6922     49    440    545       C  
ATOM   2821  CE1 TYR A 299      -6.355 -37.986   8.696  1.00 50.20           C  
ANISOU 2821  CE1 TYR A 299     5858   6214   7000     54    403    667       C  
ATOM   2822  CE2 TYR A 299      -7.296 -35.796   8.849  1.00 49.92           C  
ANISOU 2822  CE2 TYR A 299     5777   6192   6998     52    433    542       C  
ATOM   2823  CZ  TYR A 299      -6.242 -36.660   9.066  1.00 51.16           C  
ANISOU 2823  CZ  TYR A 299     5964   6371   7104     56    413    600       C  
ATOM   2824  OH  TYR A 299      -5.102 -36.202   9.680  1.00 52.96           O  
ANISOU 2824  OH  TYR A 299     6200   6651   7273     64    398    586       O  
ATOM   2825  N   VAL A 300     -11.552 -40.046   5.334  1.00 47.24           N  
ANISOU 2825  N   VAL A 300     5368   5604   6977     47    420    606       N  
ATOM   2826  CA  VAL A 300     -12.484 -41.138   5.242  1.00 48.34           C  
ANISOU 2826  CA  VAL A 300     5479   5712   7176     25    448    614       C  
ATOM   2827  C   VAL A 300     -11.828 -42.360   4.580  1.00 49.20           C  
ANISOU 2827  C   VAL A 300     5606   5780   7308     36    417    662       C  
ATOM   2828  O   VAL A 300     -12.050 -43.473   5.039  1.00 49.41           O  
ANISOU 2828  O   VAL A 300     5629   5786   7360      9    449    703       O  
ATOM   2829  CB  VAL A 300     -13.780 -40.614   4.566  1.00 49.24           C  
ANISOU 2829  CB  VAL A 300     5537   5801   7370     35    442    533       C  
ATOM   2830  CG1 VAL A 300     -14.314 -41.538   3.465  1.00 49.88           C  
ANISOU 2830  CG1 VAL A 300     5591   5829   7532     47    416    518       C  
ATOM   2831  CG2 VAL A 300     -14.842 -40.282   5.615  1.00 49.52           C  
ANISOU 2831  CG2 VAL A 300     5531   5869   7416     -6    513    490       C  
ATOM   2832  N   ASN A 301     -10.919 -42.147   3.620  1.00 49.81           N  
ANISOU 2832  N   ASN A 301     5704   5846   7375     68    362    658       N  
ATOM   2833  CA  ASN A 301     -10.194 -43.251   2.999  1.00 51.35           C  
ANISOU 2833  CA  ASN A 301     5906   6008   7599     76    336    685       C  
ATOM   2834  C   ASN A 301      -9.430 -44.095   4.047  1.00 52.18           C  
ANISOU 2834  C   ASN A 301     6036   6115   7676     61    351    759       C  
ATOM   2835  O   ASN A 301      -9.610 -45.312   4.080  1.00 52.78           O  
ANISOU 2835  O   ASN A 301     6101   6147   7808     49    360    793       O  
ATOM   2836  CB  ASN A 301      -9.224 -42.735   1.926  1.00 53.22           C  
ANISOU 2836  CB  ASN A 301     6161   6248   7811    100    287    659       C  
ATOM   2837  CG  ASN A 301      -8.726 -43.794   0.964  1.00 57.35           C  
ANISOU 2837  CG  ASN A 301     6670   6737   8385    106    260    648       C  
ATOM   2838  OD1 ASN A 301      -9.055 -44.981   1.063  1.00 58.44           O  
ANISOU 2838  OD1 ASN A 301     6782   6837   8585     98    271    666       O  
ATOM   2839  ND2 ASN A 301      -7.915 -43.385  -0.004  1.00 58.87           N  
ANISOU 2839  ND2 ASN A 301     6875   6939   8554    115    228    611       N  
ATOM   2840  N   SER A 302      -8.649 -43.450   4.936  1.00 51.81           N  
ANISOU 2840  N   SER A 302     6020   6117   7547     62    352    782       N  
ATOM   2841  CA  SER A 302      -7.858 -44.165   5.940  1.00 51.85           C  
ANISOU 2841  CA  SER A 302     6056   6130   7515     56    348    855       C  
ATOM   2842  C   SER A 302      -8.659 -45.202   6.769  1.00 51.36           C  
ANISOU 2842  C   SER A 302     6000   6044   7471     18    391    919       C  
ATOM   2843  O   SER A 302      -8.262 -46.365   6.837  1.00 51.44           O  
ANISOU 2843  O   SER A 302     6022   6004   7518     19    370    978       O  
ATOM   2844  CB  SER A 302      -7.102 -43.190   6.847  1.00 53.42           C  
ANISOU 2844  CB  SER A 302     6281   6400   7617     60    346    856       C  
ATOM   2845  OG  SER A 302      -7.827 -42.784   7.998  1.00 55.84           O  
ANISOU 2845  OG  SER A 302     6594   6757   7868     25    398    866       O  
ATOM   2846  N   CYS A 303      -9.787 -44.801   7.358  1.00 50.75           N  
ANISOU 2846  N   CYS A 303     5911   5995   7378    -19    451    901       N  
ATOM   2847  CA  CYS A 303     -10.584 -45.714   8.189  1.00 50.36           C  
ANISOU 2847  CA  CYS A 303     5870   5929   7335    -72    509    957       C  
ATOM   2848  C   CYS A 303     -11.529 -46.609   7.409  1.00 49.02           C  
ANISOU 2848  C   CYS A 303     5659   5684   7284    -85    530    937       C  
ATOM   2849  O   CYS A 303     -12.116 -47.496   8.007  1.00 48.91           O  
ANISOU 2849  O   CYS A 303     5653   5639   7290   -133    580    989       O  
ATOM   2850  CB  CYS A 303     -11.324 -44.962   9.287  1.00 51.15           C  
ANISOU 2850  CB  CYS A 303     5970   6102   7363   -118    578    935       C  
ATOM   2851  SG  CYS A 303     -11.988 -43.373   8.757  1.00 53.68           S  
ANISOU 2851  SG  CYS A 303     6233   6458   7704    -96    582    807       S  
ATOM   2852  N   LEU A 304     -11.662 -46.412   6.106  1.00 48.03           N  
ANISOU 2852  N   LEU A 304     5491   5529   7229    -48    493    866       N  
ATOM   2853  CA  LEU A 304     -12.484 -47.280   5.279  1.00 47.96           C  
ANISOU 2853  CA  LEU A 304     5435   5455   7335    -55    502    833       C  
ATOM   2854  C   LEU A 304     -11.723 -48.546   4.892  1.00 47.33           C  
ANISOU 2854  C   LEU A 304     5362   5306   7315    -42    466    882       C  
ATOM   2855  O   LEU A 304     -12.326 -49.613   4.785  1.00 47.11           O  
ANISOU 2855  O   LEU A 304     5309   5213   7376    -68    495    894       O  
ATOM   2856  CB  LEU A 304     -12.902 -46.539   4.016  1.00 48.65           C  
ANISOU 2856  CB  LEU A 304     5477   5546   7460    -18    465    735       C  
ATOM   2857  CG  LEU A 304     -13.930 -47.236   3.151  1.00 50.80           C  
ANISOU 2857  CG  LEU A 304     5688   5767   7844    -23    472    675       C  
ATOM   2858  CD1 LEU A 304     -15.188 -47.617   3.956  1.00 51.39           C  
ANISOU 2858  CD1 LEU A 304     5732   5832   7963    -78    554    666       C  
ATOM   2859  CD2 LEU A 304     -14.314 -46.360   2.005  1.00 51.83           C  
ANISOU 2859  CD2 LEU A 304     5789   5916   7990     16    421    588       C  
ATOM   2860  N   ASN A 305     -10.398 -48.409   4.659  1.00 46.79           N  
ANISOU 2860  N   ASN A 305     5319   5247   7211     -2    405    898       N  
ATOM   2861  CA  ASN A 305      -9.474 -49.473   4.295  1.00 46.79           C  
ANISOU 2861  CA  ASN A 305     5318   5187   7272     20    358    928       C  
ATOM   2862  C   ASN A 305      -9.567 -50.719   5.161  1.00 47.17           C  
ANISOU 2862  C   ASN A 305     5390   5170   7364     -9    376   1024       C  
ATOM   2863  O   ASN A 305      -9.696 -51.785   4.565  1.00 47.64           O  
ANISOU 2863  O   ASN A 305     5412   5149   7538     -8    367   1014       O  
ATOM   2864  CB  ASN A 305      -8.045 -48.972   4.248  1.00 47.40           C  
ANISOU 2864  CB  ASN A 305     5421   5300   7288     58    300    930       C  
ATOM   2865  CG  ASN A 305      -7.794 -48.051   3.102  1.00 50.30           C  
ANISOU 2865  CG  ASN A 305     5768   5709   7636     82    278    840       C  
ATOM   2866  OD1 ASN A 305      -8.289 -48.256   1.988  1.00 51.12           O  
ANISOU 2866  OD1 ASN A 305     5831   5792   7798     84    274    774       O  
ATOM   2867  ND2 ASN A 305      -7.016 -47.006   3.354  1.00 51.27           N  
ANISOU 2867  ND2 ASN A 305     5920   5890   7670     96    261    835       N  
ATOM   2868  N   PRO A 306      -9.560 -50.671   6.524  1.00 46.82           N  
ANISOU 2868  N   PRO A 306     5404   5151   7233    -40    403   1117       N  
ATOM   2869  CA  PRO A 306      -9.663 -51.928   7.292  1.00 46.71           C  
ANISOU 2869  CA  PRO A 306     5426   5062   7260    -72    415   1225       C  
ATOM   2870  C   PRO A 306     -10.864 -52.821   6.927  1.00 46.86           C  
ANISOU 2870  C   PRO A 306     5403   5001   7401   -115    475   1209       C  
ATOM   2871  O   PRO A 306     -10.746 -54.045   7.020  1.00 46.58           O  
ANISOU 2871  O   PRO A 306     5372   4866   7460   -122    460   1270       O  
ATOM   2872  CB  PRO A 306      -9.694 -51.461   8.758  1.00 47.31           C  
ANISOU 2872  CB  PRO A 306     5575   5207   7194   -112    450   1309       C  
ATOM   2873  CG  PRO A 306      -9.960 -49.991   8.722  1.00 47.66           C  
ANISOU 2873  CG  PRO A 306     5600   5357   7150   -109    477   1223       C  
ATOM   2874  CD  PRO A 306      -9.396 -49.511   7.426  1.00 46.20           C  
ANISOU 2874  CD  PRO A 306     5367   5170   7016    -48    419   1129       C  
ATOM   2875  N   PHE A 307     -11.998 -52.210   6.475  1.00 47.12           N  
ANISOU 2875  N   PHE A 307     5385   5069   7447   -139    535   1118       N  
ATOM   2876  CA  PHE A 307     -13.215 -52.909   6.037  1.00 47.69           C  
ANISOU 2876  CA  PHE A 307     5401   5080   7641   -178    594   1071       C  
ATOM   2877  C   PHE A 307     -13.073 -53.467   4.621  1.00 49.11           C  
ANISOU 2877  C   PHE A 307     5510   5203   7949   -135    544    986       C  
ATOM   2878  O   PHE A 307     -13.674 -54.487   4.323  1.00 49.42           O  
ANISOU 2878  O   PHE A 307     5507   5159   8112   -161    573    975       O  
ATOM   2879  CB  PHE A 307     -14.411 -51.981   6.031  1.00 47.09           C  
ANISOU 2879  CB  PHE A 307     5285   5066   7541   -209    659    984       C  
ATOM   2880  CG  PHE A 307     -14.720 -51.294   7.324  1.00 47.51           C  
ANISOU 2880  CG  PHE A 307     5386   5194   7471   -257    719   1026       C  
ATOM   2881  CD1 PHE A 307     -15.552 -51.880   8.252  1.00 48.32           C  
ANISOU 2881  CD1 PHE A 307     5503   5280   7575   -340    815   1069       C  
ATOM   2882  CD2 PHE A 307     -14.281 -50.007   7.561  1.00 48.33           C  
ANISOU 2882  CD2 PHE A 307     5510   5391   7464   -225    690   1002       C  
ATOM   2883  CE1 PHE A 307     -15.897 -51.212   9.419  1.00 49.05           C  
ANISOU 2883  CE1 PHE A 307     5631   5457   7549   -394    881   1086       C  
ATOM   2884  CE2 PHE A 307     -14.624 -49.342   8.730  1.00 49.01           C  
ANISOU 2884  CE2 PHE A 307     5626   5554   7442   -272    750   1016       C  
ATOM   2885  CZ  PHE A 307     -15.421 -49.950   9.654  1.00 48.80           C  
ANISOU 2885  CZ  PHE A 307     5614   5520   7408   -357    845   1056       C  
ATOM   2886  N   LEU A 308     -12.335 -52.790   3.737  1.00 49.78           N  
ANISOU 2886  N   LEU A 308     5577   5335   8004    -78    478    918       N  
ATOM   2887  CA  LEU A 308     -12.098 -53.287   2.383  1.00 51.12           C  
ANISOU 2887  CA  LEU A 308     5683   5466   8274    -43    433    832       C  
ATOM   2888  C   LEU A 308     -11.175 -54.513   2.427  1.00 53.02           C  
ANISOU 2888  C   LEU A 308     5927   5621   8598    -30    393    886       C  
ATOM   2889  O   LEU A 308     -11.313 -55.396   1.596  1.00 53.44           O  
ANISOU 2889  O   LEU A 308     5917   5611   8778    -24    381    825       O  
ATOM   2890  CB  LEU A 308     -11.484 -52.189   1.518  1.00 51.36           C  
ANISOU 2890  CB  LEU A 308     5709   5576   8231      1    380    757       C  
ATOM   2891  CG  LEU A 308     -12.346 -50.949   1.368  1.00 52.75           C  
ANISOU 2891  CG  LEU A 308     5879   5822   8340     -1    400    703       C  
ATOM   2892  CD1 LEU A 308     -11.549 -49.777   0.831  1.00 53.32           C  
ANISOU 2892  CD1 LEU A 308     5971   5962   8326     37    347    660       C  
ATOM   2893  CD2 LEU A 308     -13.505 -51.227   0.494  1.00 53.21           C  
ANISOU 2893  CD2 LEU A 308     5868   5857   8492    -13    420    617       C  
ATOM   2894  N   TYR A 309     -10.252 -54.581   3.401  1.00 54.17           N  
ANISOU 2894  N   TYR A 309     6139   5760   8682    -22    366    991       N  
ATOM   2895  CA  TYR A 309      -9.365 -55.719   3.631  1.00 55.85           C  
ANISOU 2895  CA  TYR A 309     6359   5880   8980     -4    315   1054       C  
ATOM   2896  C   TYR A 309     -10.235 -56.867   4.177  1.00 57.24           C  
ANISOU 2896  C   TYR A 309     6538   5951   9261    -55    367   1124       C  
ATOM   2897  O   TYR A 309     -10.161 -57.992   3.687  1.00 57.11           O  
ANISOU 2897  O   TYR A 309     6470   5831   9396    -49    350   1102       O  
ATOM   2898  CB  TYR A 309      -8.288 -55.297   4.642  1.00 56.35           C  
ANISOU 2898  CB  TYR A 309     6501   5980   8931     18    268   1149       C  
ATOM   2899  CG  TYR A 309      -7.252 -56.338   4.995  1.00 57.90           C  
ANISOU 2899  CG  TYR A 309     6710   6082   9206     50    194   1219       C  
ATOM   2900  CD1 TYR A 309      -6.977 -57.396   4.140  1.00 59.23           C  
ANISOU 2900  CD1 TYR A 309     6807   6155   9542     73    159   1159       C  
ATOM   2901  CD2 TYR A 309      -6.481 -56.215   6.140  1.00 59.31           C  
ANISOU 2901  CD2 TYR A 309     6966   6273   9295     63    148   1332       C  
ATOM   2902  CE1 TYR A 309      -6.012 -58.350   4.454  1.00 60.56           C  
ANISOU 2902  CE1 TYR A 309     6979   6226   9805    108     80   1215       C  
ATOM   2903  CE2 TYR A 309      -5.500 -57.150   6.457  1.00 60.65           C  
ANISOU 2903  CE2 TYR A 309     7147   6351   9547    102     61   1395       C  
ATOM   2904  CZ  TYR A 309      -5.273 -58.227   5.618  1.00 61.70           C  
ANISOU 2904  CZ  TYR A 309     7205   6374   9864    126     26   1337       C  
ATOM   2905  OH  TYR A 309      -4.317 -59.169   5.948  1.00 63.25           O  
ANISOU 2905  OH  TYR A 309     7405   6466  10161    170    -69   1395       O  
ATOM   2906  N   ALA A 310     -11.106 -56.561   5.153  1.00 58.48           N  
ANISOU 2906  N   ALA A 310     6747   6134   9340   -111    440   1195       N  
ATOM   2907  CA  ALA A 310     -12.059 -57.509   5.722  1.00 60.06           C  
ANISOU 2907  CA  ALA A 310     6956   6246   9619   -179    514   1259       C  
ATOM   2908  C   ALA A 310     -13.039 -58.033   4.669  1.00 62.28           C  
ANISOU 2908  C   ALA A 310     7136   6480  10049   -195    557   1137       C  
ATOM   2909  O   ALA A 310     -13.527 -59.139   4.810  1.00 62.90           O  
ANISOU 2909  O   ALA A 310     7198   6450  10250   -239    599   1169       O  
ATOM   2910  CB  ALA A 310     -12.823 -56.863   6.869  1.00 59.88           C  
ANISOU 2910  CB  ALA A 310     6997   6293   9462   -245    596   1323       C  
ATOM   2911  N   PHE A 311     -13.327 -57.259   3.623  1.00 63.38           N  
ANISOU 2911  N   PHE A 311     7209   6694  10179   -162    544    999       N  
ATOM   2912  CA  PHE A 311     -14.234 -57.687   2.573  1.00 65.10           C  
ANISOU 2912  CA  PHE A 311     7329   6883  10524   -170    571    873       C  
ATOM   2913  C   PHE A 311     -13.531 -58.664   1.645  1.00 67.93           C  
ANISOU 2913  C   PHE A 311     7629   7159  11023   -134    513    825       C  
ATOM   2914  O   PHE A 311     -13.935 -59.820   1.551  1.00 68.16           O  
ANISOU 2914  O   PHE A 311     7613   7081  11204   -164    545    819       O  
ATOM   2915  CB  PHE A 311     -14.775 -56.469   1.790  1.00 64.49           C  
ANISOU 2915  CB  PHE A 311     7211   6918  10374   -143    560    751       C  
ATOM   2916  CG  PHE A 311     -15.725 -56.804   0.664  1.00 64.60           C  
ANISOU 2916  CG  PHE A 311     7124   6916  10505   -146    576    613       C  
ATOM   2917  CD1 PHE A 311     -17.052 -57.097   0.919  1.00 65.07           C  
ANISOU 2917  CD1 PHE A 311     7143   6948  10633   -200    657    581       C  
ATOM   2918  CD2 PHE A 311     -15.299 -56.797  -0.649  1.00 65.13           C  
ANISOU 2918  CD2 PHE A 311     7133   7003  10611    -98    511    507       C  
ATOM   2919  CE1 PHE A 311     -17.926 -57.394  -0.115  1.00 65.48           C  
ANISOU 2919  CE1 PHE A 311     7093   6989  10797   -199    664    442       C  
ATOM   2920  CE2 PHE A 311     -16.180 -57.097  -1.682  1.00 65.70           C  
ANISOU 2920  CE2 PHE A 311     7111   7071  10782    -99    517    375       C  
ATOM   2921  CZ  PHE A 311     -17.485 -57.392  -1.407  1.00 65.28           C  
ANISOU 2921  CZ  PHE A 311     7014   6986  10802   -145    589    342       C  
ATOM   2922  N   PHE A 312     -12.454 -58.216   1.000  1.00 70.15           N  
ANISOU 2922  N   PHE A 312     7908   7487  11260    -76    435    787       N  
ATOM   2923  CA  PHE A 312     -11.746 -58.964  -0.022  1.00 72.99           C  
ANISOU 2923  CA  PHE A 312     8198   7795  11741    -41    380    705       C  
ATOM   2924  C   PHE A 312     -10.873 -60.108   0.466  1.00 76.16           C  
ANISOU 2924  C   PHE A 312     8613   8075  12248    -30    341    790       C  
ATOM   2925  O   PHE A 312     -10.681 -61.055  -0.300  1.00 76.10           O  
ANISOU 2925  O   PHE A 312     8526   7992  12396    -17    317    713       O  
ATOM   2926  CB  PHE A 312     -10.927 -58.012  -0.896  1.00 72.93           C  
ANISOU 2926  CB  PHE A 312     8179   7892  11637      6    323    617       C  
ATOM   2927  CG  PHE A 312     -11.796 -57.187  -1.816  1.00 73.58           C  
ANISOU 2927  CG  PHE A 312     8224   8067  11667      3    340    507       C  
ATOM   2928  CD1 PHE A 312     -12.464 -57.774  -2.876  1.00 74.37           C  
ANISOU 2928  CD1 PHE A 312     8232   8147  11877     -2    347    384       C  
ATOM   2929  CD2 PHE A 312     -11.937 -55.823  -1.625  1.00 74.36           C  
ANISOU 2929  CD2 PHE A 312     8376   8267  11608     10    340    521       C  
ATOM   2930  CE1 PHE A 312     -13.251 -57.015  -3.728  1.00 75.10           C  
ANISOU 2930  CE1 PHE A 312     8294   8325  11915      3    344    286       C  
ATOM   2931  CE2 PHE A 312     -12.724 -55.065  -2.478  1.00 75.07           C  
ANISOU 2931  CE2 PHE A 312     8436   8431  11657     16    338    426       C  
ATOM   2932  CZ  PHE A 312     -13.383 -55.667  -3.519  1.00 74.97           C  
ANISOU 2932  CZ  PHE A 312     8338   8401  11745     14    336    312       C  
ATOM   2933  N   ASP A 313     -10.328 -60.039   1.695  1.00 78.86           N  
ANISOU 2933  N   ASP A 313     9050   8398  12514    -34    328    940       N  
ATOM   2934  CA  ASP A 313      -9.483 -61.127   2.184  1.00 82.05           C  
ANISOU 2934  CA  ASP A 313     9475   8678  13023    -16    273   1032       C  
ATOM   2935  C   ASP A 313     -10.167 -61.940   3.239  1.00 85.13           C  
ANISOU 2935  C   ASP A 313     9919   8961  13467    -74    324   1168       C  
ATOM   2936  O   ASP A 313     -10.238 -61.500   4.385  1.00 85.01           O  
ANISOU 2936  O   ASP A 313    10004   8980  13317   -103    347   1297       O  
ATOM   2937  CB  ASP A 313      -8.119 -60.644   2.691  1.00 84.36           C  
ANISOU 2937  CB  ASP A 313     9830   9014  13208     33    192   1098       C  
ATOM   2938  CG  ASP A 313      -7.022 -61.710   2.644  1.00 90.11           C  
ANISOU 2938  CG  ASP A 313    10526   9629  14082     82    100   1104       C  
ATOM   2939  OD1 ASP A 313      -7.349 -62.903   2.404  1.00 90.86           O  
ANISOU 2939  OD1 ASP A 313    10585   9584  14354     68    102   1122       O  
ATOM   2940  OD2 ASP A 313      -5.838 -61.352   2.832  1.00 92.78           O  
ANISOU 2940  OD2 ASP A 313    10867  10014  14371    134     26   1079       O  
ATOM   2941  N   PRO A 314     -10.615 -63.167   2.874  1.00 87.77           N  
ANISOU 2941  N   PRO A 314    10189   9160  14000    -95    344   1141       N  
ATOM   2942  CA  PRO A 314     -11.246 -64.049   3.871  1.00 89.85           C  
ANISOU 2942  CA  PRO A 314    10509   9299  14330   -160    399   1282       C  
ATOM   2943  C   PRO A 314     -10.266 -64.582   4.922  1.00 92.70           C  
ANISOU 2943  C   PRO A 314    10968   9570  14684   -139    321   1459       C  
ATOM   2944  O   PRO A 314     -10.700 -65.140   5.930  1.00 92.92           O  
ANISOU 2944  O   PRO A 314    11077   9510  14720   -198    361   1609       O  
ATOM   2945  CB  PRO A 314     -11.852 -65.174   3.023  1.00 90.14           C  
ANISOU 2945  CB  PRO A 314    10434   9216  14598   -179    432   1178       C  
ATOM   2946  CG  PRO A 314     -11.007 -65.227   1.807  1.00 90.04           C  
ANISOU 2946  CG  PRO A 314    10321   9228  14664   -107    354   1023       C  
ATOM   2947  CD  PRO A 314     -10.535 -63.818   1.549  1.00 87.88           C  
ANISOU 2947  CD  PRO A 314    10076   9128  14188    -65    319    980       C  
ATOM   2948  N   ARG A 315      -8.952 -64.387   4.709  1.00 94.66           N  
ANISOU 2948  N   ARG A 315    11212   9843  14910    -59    209   1442       N  
ATOM   2949  CA  ARG A 315      -7.942 -64.753   5.684  1.00 97.06           C  
ANISOU 2949  CA  ARG A 315    11606  10082  15191    -25    114   1597       C  
ATOM   2950  C   ARG A 315      -7.953 -63.713   6.817  1.00 98.27           C  
ANISOU 2950  C   ARG A 315    11880  10366  15093    -48    133   1709       C  
ATOM   2951  O   ARG A 315      -7.798 -64.095   7.969  1.00 98.28           O  
ANISOU 2951  O   ARG A 315    11990  10314  15038    -70    110   1885       O  
ATOM   2952  CB  ARG A 315      -6.568 -64.898   5.022  1.00 99.98           C  
ANISOU 2952  CB  ARG A 315    11907  10430  15649     68     -9   1509       C  
ATOM   2953  CG  ARG A 315      -6.572 -65.925   3.887  1.00105.43           C  
ANISOU 2953  CG  ARG A 315    12469  10994  16595     86    -25   1383       C  
ATOM   2954  CD  ARG A 315      -5.308 -66.765   3.890  1.00110.76           C  
ANISOU 2954  CD  ARG A 315    13108  11573  17404    166   -159   1373       C  
ATOM   2955  NE  ARG A 315      -5.191 -67.606   2.696  1.00115.64           N  
ANISOU 2955  NE  ARG A 315    13583  12088  18266    187   -177   1217       N  
ATOM   2956  CZ  ARG A 315      -4.042 -67.891   2.086  1.00119.08           C  
ANISOU 2956  CZ  ARG A 315    13930  12499  18816    256   -270   1100       C  
ATOM   2957  NH1 ARG A 315      -2.896 -67.398   2.546  1.00119.23           N  
ANISOU 2957  NH1 ARG A 315    13985  12588  18728    312   -354   1118       N  
ATOM   2958  NH2 ARG A 315      -4.029 -68.669   1.010  1.00119.28           N  
ANISOU 2958  NH2 ARG A 315    13821  12435  19066    266   -275    948       N  
ATOM   2959  N   PHE A 316      -8.197 -62.415   6.509  1.00 99.21           N  
ANISOU 2959  N   PHE A 316    11981  10652  15061    -48    177   1611       N  
ATOM   2960  CA  PHE A 316      -8.357 -61.394   7.552  1.00100.74           C  
ANISOU 2960  CA  PHE A 316    12274  10971  15032    -79    212   1696       C  
ATOM   2961  C   PHE A 316      -9.734 -61.569   8.229  1.00102.25           C  
ANISOU 2961  C   PHE A 316    12510  11150  15192   -181    338   1765       C  
ATOM   2962  O   PHE A 316      -9.862 -61.300   9.422  1.00102.28           O  
ANISOU 2962  O   PHE A 316    12618  11196  15048   -227    366   1893       O  
ATOM   2963  CB  PHE A 316      -8.205 -59.959   7.003  1.00100.76           C  
ANISOU 2963  CB  PHE A 316    12242  11139  14904    -49    220   1569       C  
ATOM   2964  CG  PHE A 316      -8.383 -58.863   8.042  1.00101.45           C  
ANISOU 2964  CG  PHE A 316    12417  11355  14775    -79    255   1637       C  
ATOM   2965  CD1 PHE A 316      -7.370 -58.551   8.929  1.00102.18           C  
ANISOU 2965  CD1 PHE A 316    12581  11491  14752    -41    175   1721       C  
ATOM   2966  CD2 PHE A 316      -9.571 -58.158   8.136  1.00102.19           C  
ANISOU 2966  CD2 PHE A 316    12510  11526  14790   -143    364   1603       C  
ATOM   2967  CE1 PHE A 316      -7.534 -57.542   9.873  1.00102.80           C  
ANISOU 2967  CE1 PHE A 316    12731  11695  14634    -70    209   1767       C  
ATOM   2968  CE2 PHE A 316      -9.737 -57.161   9.090  1.00102.76           C  
ANISOU 2968  CE2 PHE A 316    12651  11718  14676   -173    400   1648       C  
ATOM   2969  CZ  PHE A 316      -8.719 -56.861   9.952  1.00102.54           C  
ANISOU 2969  CZ  PHE A 316    12695  11737  14529   -138    324   1730       C  
ATOM   2970  N   ARG A 317     -10.758 -62.038   7.479  1.00103.37           N  
ANISOU 2970  N   ARG A 317    12569  11236  15472   -220    416   1672       N  
ATOM   2971  CA  ARG A 317     -12.082 -62.312   8.030  1.00105.04           C  
ANISOU 2971  CA  ARG A 317    12804  11421  15685   -321    543   1716       C  
ATOM   2972  C   ARG A 317     -11.952 -63.438   9.060  1.00106.87           C  
ANISOU 2972  C   ARG A 317    13137  11516  15954   -369    538   1911       C  
ATOM   2973  O   ARG A 317     -12.499 -63.323  10.151  1.00107.07           O  
ANISOU 2973  O   ARG A 317    13257  11570  15854   -451    614   2026       O  
ATOM   2974  CB  ARG A 317     -13.095 -62.751   6.944  1.00106.15           C  
ANISOU 2974  CB  ARG A 317    12823  11508  16001   -345    610   1568       C  
ATOM   2975  CG  ARG A 317     -12.958 -62.097   5.579  1.00108.37           C  
ANISOU 2975  CG  ARG A 317    12997  11889  16290   -287    588   1375       C  
ATOM   2976  CD  ARG A 317     -14.252 -62.104   4.773  1.00110.69           C  
ANISOU 2976  CD  ARG A 317    13197  12191  16669   -333    682   1241       C  
ATOM   2977  NE  ARG A 317     -14.786 -63.450   4.578  1.00113.15           N  
ANISOU 2977  NE  ARG A 317    13456  12348  17187   -373    721   1236       N  
ATOM   2978  CZ  ARG A 317     -15.961 -63.868   5.039  1.00115.12           C  
ANISOU 2978  CZ  ARG A 317    13699  12545  17495   -463    835   1249       C  
ATOM   2979  NH1 ARG A 317     -16.749 -63.041   5.718  1.00114.90           N  
ANISOU 2979  NH1 ARG A 317    13707  12614  17335   -522    922   1257       N  
ATOM   2980  NH2 ARG A 317     -16.360 -65.115   4.823  1.00114.77           N  
ANISOU 2980  NH2 ARG A 317    13604  12350  17652   -497    867   1242       N  
ATOM   2981  N   GLN A 318     -11.198 -64.507   8.727  1.00108.00           N  
ANISOU 2981  N   GLN A 318    13261  11510  16264   -319    445   1948       N  
ATOM   2982  CA  GLN A 318     -11.010 -65.639   9.634  1.00109.60           C  
ANISOU 2982  CA  GLN A 318    13561  11559  16524   -353    419   2142       C  
ATOM   2983  C   GLN A 318     -10.042 -65.327  10.781  1.00110.57           C  
ANISOU 2983  C   GLN A 318    13817  11727  16466   -327    329   2308       C  
ATOM   2984  O   GLN A 318     -10.177 -65.900  11.863  1.00110.77           O  
ANISOU 2984  O   GLN A 318    13965  11683  16440   -387    341   2496       O  
ATOM   2985  CB  GLN A 318     -10.606 -66.917   8.881  1.00111.84           C  
ANISOU 2985  CB  GLN A 318    13769  11655  17072   -305    345   2115       C  
ATOM   2986  CG  GLN A 318     -11.060 -68.191   9.601  1.00116.44           C  
ANISOU 2986  CG  GLN A 318    14429  12045  17769   -372    366   2291       C  
ATOM   2987  CD  GLN A 318     -10.694 -69.464   8.875  1.00122.01           C  
ANISOU 2987  CD  GLN A 318    15049  12552  18755   -321    288   2256       C  
ATOM   2988  OE1 GLN A 318     -10.282 -69.452   7.705  1.00124.12           O  
ANISOU 2988  OE1 GLN A 318    15178  12831  19150   -251    246   2069       O  
ATOM   2989  NE2 GLN A 318     -10.842 -70.596   9.558  1.00122.53           N  
ANISOU 2989  NE2 GLN A 318    15198  12431  18927   -359    268   2435       N  
ATOM   2990  N   ALA A 319      -9.079 -64.418  10.558  1.00110.94           N  
ANISOU 2990  N   ALA A 319    13845  11894  16413   -240    240   2238       N  
ATOM   2991  CA  ALA A 319      -8.148 -64.015  11.615  1.00111.71           C  
ANISOU 2991  CA  ALA A 319    14054  12055  16334   -207    147   2368       C  
ATOM   2992  C   ALA A 319      -8.847 -63.112  12.630  1.00112.38           C  
ANISOU 2992  C   ALA A 319    14232  12287  16180   -290    247   2431       C  
ATOM   2993  O   ALA A 319      -8.554 -63.189  13.820  1.00112.45           O  
ANISOU 2993  O   ALA A 319    14369  12306  16050   -319    217   2600       O  
ATOM   2994  CB  ALA A 319      -6.951 -63.292  11.024  1.00111.83           C  
ANISOU 2994  CB  ALA A 319    14005  12155  16331    -98     37   2249       C  
ATOM   2995  N   CYS A 320      -9.776 -62.265  12.166  1.00112.77           N  
ANISOU 2995  N   CYS A 320    14215  12452  16182   -330    361   2291       N  
ATOM   2996  CA  CYS A 320     -10.514 -61.379  13.050  1.00113.72           C  
ANISOU 2996  CA  CYS A 320    14399  12714  16097   -410    465   2317       C  
ATOM   2997  C   CYS A 320     -11.678 -62.103  13.726  1.00114.58           C  
ANISOU 2997  C   CYS A 320    14570  12756  16209   -537    592   2422       C  
ATOM   2998  O   CYS A 320     -11.964 -61.814  14.886  1.00114.83           O  
ANISOU 2998  O   CYS A 320    14708  12865  16057   -612    645   2530       O  
ATOM   2999  CB  CYS A 320     -10.983 -60.130  12.310  1.00114.41           C  
ANISOU 2999  CB  CYS A 320    14388  12941  16143   -398    526   2126       C  
ATOM   3000  SG  CYS A 320     -11.631 -58.832  13.393  1.00117.68           S  
ANISOU 3000  SG  CYS A 320    14863  13543  16309   -476    631   2128       S  
ATOM   3001  N   THR A 321     -12.339 -63.053  13.024  1.00114.85           N  
ANISOU 3001  N   THR A 321    14540  12649  16449   -569    644   2387       N  
ATOM   3002  CA  THR A 321     -13.469 -63.792  13.602  1.00115.63           C  
ANISOU 3002  CA  THR A 321    14690  12673  16572   -699    778   2475       C  
ATOM   3003  C   THR A 321     -13.024 -64.822  14.656  1.00116.16           C  
ANISOU 3003  C   THR A 321    14907  12621  16607   -741    734   2718       C  
ATOM   3004  O   THR A 321     -13.839 -65.203  15.494  1.00116.31           O  
ANISOU 3004  O   THR A 321    15016  12632  16544   -866    849   2827       O  
ATOM   3005  CB  THR A 321     -14.376 -64.406  12.521  1.00117.06           C  
ANISOU 3005  CB  THR A 321    14746  12746  16986   -723    854   2347       C  
ATOM   3006  OG1 THR A 321     -15.717 -64.443  13.004  1.00118.14           O  
ANISOU 3006  OG1 THR A 321    14907  12879  17101   -861   1021   2368       O  
ATOM   3007  CG2 THR A 321     -13.940 -65.803  12.091  1.00117.51           C  
ANISOU 3007  CG2 THR A 321    14784  12598  17266   -679    769   2404       C  
ATOM   3008  N   SER A 322     -11.746 -65.260  14.631  1.00116.29           N  
ANISOU 3008  N   SER A 322    14953  12545  16688   -640    568   2800       N  
ATOM   3009  CA  SER A 322     -11.208 -66.186  15.635  1.00116.97           C  
ANISOU 3009  CA  SER A 322    15187  12512  16746   -661    492   3040       C  
ATOM   3010  C   SER A 322     -10.941 -65.417  16.945  1.00117.56           C  
ANISOU 3010  C   SER A 322    15398  12745  16525   -684    470   3158       C  
ATOM   3011  O   SER A 322     -11.233 -65.909  18.036  1.00117.60           O  
ANISOU 3011  O   SER A 322    15547  12731  16404   -783    514   3345       O  
ATOM   3012  CB  SER A 322      -9.926 -66.851  15.133  1.00118.34           C  
ANISOU 3012  CB  SER A 322    15326  12536  17101   -534    309   3062       C  
ATOM   3013  OG  SER A 322      -8.808 -65.976  15.135  1.00120.56           O  
ANISOU 3013  OG  SER A 322    15603  12922  17282   -420    168   3028       O  
ATOM   3014  N   MET A 323     -10.398 -64.197  16.816  1.00117.91           N  
ANISOU 3014  N   MET A 323    15392  12951  16457   -600    408   3041       N  
ATOM   3015  CA  MET A 323     -10.118 -63.289  17.926  1.00118.62           C  
ANISOU 3015  CA  MET A 323    15578  13216  16278   -608    384   3101       C  
ATOM   3016  C   MET A 323     -11.408 -62.646  18.489  1.00119.00           C  
ANISOU 3016  C   MET A 323    15663  13400  16153   -748    570   3085       C  
ATOM   3017  O   MET A 323     -11.420 -62.204  19.637  1.00119.24           O  
ANISOU 3017  O   MET A 323    15817  13532  15958   -808    583   3204       O  
ATOM   3018  CB  MET A 323      -9.135 -62.199  17.468  1.00119.41           C  
ANISOU 3018  CB  MET A 323    15582  13439  16348   -487    293   2938       C  
ATOM   3019  CG  MET A 323      -7.754 -62.733  17.127  1.00121.51           C  
ANISOU 3019  CG  MET A 323    15848  13621  16699   -358     96   2981       C  
ATOM   3020  SD  MET A 323      -6.650 -61.480  16.411  1.00125.41           S  
ANISOU 3020  SD  MET A 323    16250  14272  17126   -234     -1   2804       S  
ATOM   3021  CE  MET A 323      -6.691 -60.231  17.687  1.00123.12           C  
ANISOU 3021  CE  MET A 323    16049  14208  16524   -310     81   2831       C  
ATOM   3022  N   LEU A 324     -12.481 -62.586  17.682  1.00118.92           N  
ANISOU 3022  N   LEU A 324    15540  13394  16249   -798    708   2929       N  
ATOM   3023  CA  LEU A 324     -13.775 -62.027  18.066  1.00119.35           C  
ANISOU 3023  CA  LEU A 324    15593  13566  16190   -927    892   2868       C  
ATOM   3024  C   LEU A 324     -14.416 -62.850  19.190  1.00119.41           C  
ANISOU 3024  C   LEU A 324    15748  13534  16090  -1073    987   3061       C  
ATOM   3025  O   LEU A 324     -14.186 -64.057  19.295  1.00119.52           O  
ANISOU 3025  O   LEU A 324    15799  13369  16243  -1113    997   3172       O  
ATOM   3026  CB  LEU A 324     -14.700 -62.012  16.836  1.00119.73           C  
ANISOU 3026  CB  LEU A 324    15489  13567  16437   -941    994   2682       C  
ATOM   3027  CG  LEU A 324     -15.500 -60.740  16.582  1.00121.06           C  
ANISOU 3027  CG  LEU A 324    15589  13878  16529  -1022   1150   2529       C  
ATOM   3028  CD1 LEU A 324     -14.591 -59.536  16.432  1.00121.67           C  
ANISOU 3028  CD1 LEU A 324    15633  14134  16460   -950   1099   2422       C  
ATOM   3029  CD2 LEU A 324     -16.347 -60.888  15.341  1.00121.64           C  
ANISOU 3029  CD2 LEU A 324    15515  13882  16820  -1023   1222   2358       C  
TER    3030      LEU A 324                                                      
HETATM 3031  C08 A1D A1201      -3.695 -30.951   7.375  1.00 41.10           C  
ANISOU 3031  C08 A1D A1201     4661   5028   5925     80    403    336       C  
HETATM 3032  C09 A1D A1201      -2.596 -30.293   8.224  1.00 41.07           C  
ANISOU 3032  C09 A1D A1201     4637   5080   5888     73    421    276       C  
HETATM 3033  C10 A1D A1201      -5.112 -30.730   7.935  1.00 40.81           C  
ANISOU 3033  C10 A1D A1201     4587   4999   5918     78    423    310       C  
HETATM 3034  C11 A1D A1201      -3.562 -29.350   5.355  1.00 41.74           C  
ANISOU 3034  C11 A1D A1201     4793   4967   6098     74    380    327       C  
HETATM 3035  C12 A1D A1201      -3.278 -31.469   4.905  1.00 42.63           C  
ANISOU 3035  C12 A1D A1201     4931   5111   6154     81    357    404       C  
HETATM 3036  C13 A1D A1201      -4.209 -23.640   1.871  1.00 47.02           C  
ANISOU 3036  C13 A1D A1201     5627   5195   7042     42    298    347       C  
HETATM 3037  C14 A1D A1201      -5.613 -23.040   1.775  1.00 46.53           C  
ANISOU 3037  C14 A1D A1201     5551   5054   7075     84    234    351       C  
HETATM 3038  C15 A1D A1201      -6.710 -24.024   1.312  1.00 45.97           C  
ANISOU 3038  C15 A1D A1201     5484   4994   6988    119    178    393       C  
HETATM 3039  C16 A1D A1201      -3.352 -29.517   3.993  1.00 41.98           C  
ANISOU 3039  C16 A1D A1201     4877   4939   6133     68    356    370       C  
HETATM 3040  C17 A1D A1201      -3.091 -33.011   4.974  1.00 43.68           C  
ANISOU 3040  C17 A1D A1201     5067   5273   6258     88    344    450       C  
HETATM 3041  C18 A1D A1201      -3.784 -28.054   5.872  1.00 41.64           C  
ANISOU 3041  C18 A1D A1201     4750   4939   6132     72    397    266       C  
HETATM 3042  C19 A1D A1201      -3.221 -22.557   2.289  1.00 48.56           C  
ANISOU 3042  C19 A1D A1201     5807   5371   7272     10    350    289       C  
HETATM 3043  C20 A1D A1201      -3.532 -27.164   3.616  1.00 42.64           C  
ANISOU 3043  C20 A1D A1201     4975   4920   6307     57    357    325       C  
HETATM 3044  C21 A1D A1201      -3.346 -28.431   3.105  1.00 42.03           C  
ANISOU 3044  C21 A1D A1201     4921   4871   6177     56    346    372       C  
HETATM 3045  C22 A1D A1201      -1.208 -30.886   7.884  1.00 41.10           C  
ANISOU 3045  C22 A1D A1201     4661   5093   5860     75    402    290       C  
HETATM 3046  C23 A1D A1201      -5.532 -31.836   8.940  1.00 40.67           C  
ANISOU 3046  C23 A1D A1201     4559   5047   5846     67    441    343       C  
HETATM 3047  C24 A1D A1201      -3.752 -26.967   4.987  1.00 42.11           C  
ANISOU 3047  C24 A1D A1201     4841   4911   6249     66    384    264       C  
HETATM 3048  C25 A1D A1201      -3.550 -25.982   2.569  1.00 44.13           C  
ANISOU 3048  C25 A1D A1201     5219   5006   6543     42    338    345       C  
HETATM 3049  C26 A1D A1201      -8.070 -23.277   1.228  1.00 45.65           C  
ANISOU 3049  C26 A1D A1201     5417   4867   7063    166    107    378       C  
HETATM 3050  C27 A1D A1201      -6.364 -24.705  -0.024  1.00 45.86           C  
ANISOU 3050  C27 A1D A1201     5562   4973   6891     98    153    479       C  
HETATM 3051  C28 A1D A1201      -4.445 -33.658   5.241  1.00 45.09           C  
ANISOU 3051  C28 A1D A1201     5231   5445   6456     96    342    480       C  
HETATM 3052  C29 A1D A1201      -1.743 -22.982   2.422  1.00 49.68           C  
ANISOU 3052  C29 A1D A1201     5950   5583   7344    -33    413    260       C  
HETATM 3053  C30 A1D A1201      -5.000 -33.900   6.499  1.00 45.32           C  
ANISOU 3053  C30 A1D A1201     5227   5515   6477     93    368    464       C  
HETATM 3054  C31 A1D A1201      -6.287 -34.494   6.402  1.00 45.56           C  
ANISOU 3054  C31 A1D A1201     5245   5525   6542     93    369    485       C  
HETATM 3055  C32 A1D A1201      -6.782 -34.745   5.121  1.00 45.92           C  
ANISOU 3055  C32 A1D A1201     5309   5517   6622    103    339    518       C  
HETATM 3056  N05 A1D A1201      -3.552 -30.604   5.902  1.00 41.80           N  
ANISOU 3056  N05 A1D A1201     4790   5033   6058     80    380    356       N  
HETATM 3057  N06 A1D A1201      -3.184 -30.829   3.747  1.00 42.33           N  
ANISOU 3057  N06 A1D A1201     4930   5010   6142     71    345    409       N  
HETATM 3058  N07 A1D A1201      -4.220 -24.711   2.883  1.00 45.69           N  
ANISOU 3058  N07 A1D A1201     5393   5137   6829     56    325    310       N  
HETATM 3059  O02 A1D A1201      -3.061 -26.139   1.502  1.00 44.20           O  
ANISOU 3059  O02 A1D A1201     5290   4987   6516     18    331    390       O  
HETATM 3060  O03 A1D A1201      -1.060 -23.246   1.374  1.00 50.09           O  
ANISOU 3060  O03 A1D A1201     6072   5619   7343    -72    424    308       O  
HETATM 3061  O04 A1D A1201      -1.215 -23.051   3.582  1.00 49.95           O1-
ANISOU 3061  O04 A1D A1201     5911   5692   7376    -31    453    179       O1-
HETATM 3062  S01 A1D A1201      -5.577 -34.168   4.094  1.00 46.28           S  
ANISOU 3062  S01 A1D A1201     5392   5543   6647    104    316    519       S  
HETATM 3063  C1  OLA A1202       0.106 -26.875   3.429  1.00 47.21           C  
HETATM 3064  O1  OLA A1202      -0.327 -25.718   3.645  1.00 47.46           O  
HETATM 3065  O2  OLA A1202       0.584 -27.577   4.356  1.00 47.72           O  
HETATM 3066  C2  OLA A1202       0.038 -27.449   2.023  1.00 45.97           C  
HETATM 3067  C3  OLA A1202       1.046 -26.752   1.122  1.00 44.89           C  
HETATM 3068  C4  OLA A1202       1.647 -27.724   0.118  1.00 44.01           C  
HETATM 3069  C5  OLA A1202       2.499 -28.777   0.816  1.00 43.22           C  
HETATM 3070  C6  OLA A1202       3.887 -28.865   0.199  1.00 42.55           C  
HETATM 3071  C7  OLA A1202       4.589 -30.113   0.691  1.00 42.19           C  
HETATM 3072  C8  OLA A1202       5.772 -30.462  -0.187  1.00 42.18           C  
HETATM 3073  C9  OLA A1202       5.278 -31.117  -1.451  1.00 42.50           C  
HETATM 3074  C10 OLA A1202       6.010 -31.190  -2.561  1.00 43.15           C  
HETATM 3075  C11 OLA A1202       7.419 -30.645  -2.665  1.00 43.97           C  
HETATM 3076  C12 OLA A1202       8.287 -31.536  -3.549  1.00 44.76           C  
HETATM 3077  C13 OLA A1202       9.758 -31.124  -3.495  1.00 45.66           C  
HETATM 3078  C14 OLA A1202      10.320 -31.339  -2.090  1.00 46.55           C  
HETATM 3079  C15 OLA A1202      11.838 -31.514  -2.078  1.00 47.38           C  
HETATM 3080  C16 OLA A1202      12.268 -32.490  -0.975  1.00 47.88           C  
HETATM 3081  C17 OLA A1202      13.212 -31.877   0.062  1.00 47.94           C  
HETATM 3082  C18 OLA A1202      14.624 -32.402  -0.115  1.00 48.05           C  
HETATM 3083  C1  OLA A1203       6.240 -55.386  -6.438  1.00 51.71           C  
HETATM 3084  O1  OLA A1203       5.945 -56.325  -5.638  1.00 52.19           O  
HETATM 3085  O2  OLA A1203       7.146 -55.483  -7.316  1.00 51.94           O  
HETATM 3086  C2  OLA A1203       5.453 -54.084  -6.354  1.00 50.20           C  
HETATM 3087  C3  OLA A1203       6.371 -52.880  -6.558  1.00 48.63           C  
HETATM 3088  C4  OLA A1203       5.575 -51.583  -6.553  1.00 47.43           C  
HETATM 3089  C5  OLA A1203       6.112 -50.638  -7.619  1.00 46.50           C  
HETATM 3090  C6  OLA A1203       5.121 -49.536  -7.989  1.00 45.78           C  
HETATM 3091  C7  OLA A1203       4.982 -48.478  -6.893  1.00 45.07           C  
HETATM 3092  C8  OLA A1203       4.563 -47.120  -7.476  1.00 44.43           C  
HETATM 3093  C9  OLA A1203       4.500 -46.121  -6.341  1.00 43.81           C  
HETATM 3094  C10 OLA A1203       4.550 -44.786  -6.452  1.00 42.75           C  
HETATM 3095  C11 OLA A1203       4.636 -44.028  -7.748  1.00 41.60           C  
HETATM 3096  C12 OLA A1203       4.456 -42.545  -7.446  1.00 40.72           C  
HETATM 3097  C13 OLA A1203       5.657 -42.017  -6.675  1.00 40.29           C  
HETATM 3098  C14 OLA A1203       6.195 -40.730  -7.291  1.00 40.10           C  
HETATM 3099  C10 OLA A1204     -16.648 -54.127  -8.692  1.00 45.70           C  
HETATM 3100  C11 OLA A1204     -17.081 -52.682  -8.829  1.00 45.78           C  
HETATM 3101  C12 OLA A1204     -16.402 -51.813  -7.766  1.00 45.88           C  
HETATM 3102  C13 OLA A1204     -16.679 -50.319  -7.959  1.00 45.76           C  
HETATM 3103  C14 OLA A1204     -16.024 -49.443  -6.891  1.00 45.72           C  
HETATM 3104  C15 OLA A1204     -16.586 -49.730  -5.502  1.00 45.85           C  
HETATM 3105  C16 OLA A1204     -16.501 -48.523  -4.563  1.00 45.99           C  
HETATM 3106  C17 OLA A1204     -17.367 -48.711  -3.307  1.00 45.96           C  
HETATM 3107  C10 OLA A1205     -17.317 -56.175  -6.046  1.00 36.18           C  
HETATM 3108  C11 OLA A1205     -16.664 -55.146  -5.144  1.00 36.02           C  
HETATM 3109  C12 OLA A1205     -17.686 -54.093  -4.705  1.00 35.77           C  
HETATM 3110  C13 OLA A1205     -18.110 -54.269  -3.237  1.00 35.36           C  
HETATM 3111  C14 OLA A1205     -17.224 -53.477  -2.266  1.00 34.82           C  
HETATM 3112  C15 OLA A1205     -17.522 -53.729  -0.787  1.00 34.11           C  
HETATM 3113  C16 OLA A1205     -16.495 -53.008   0.089  1.00 33.74           C  
HETATM 3114  C17 OLA A1205     -17.019 -52.585   1.463  1.00 33.47           C  
HETATM 3115  C11 OLA A1206      11.065 -19.543  -7.529  1.00 40.50           C  
HETATM 3116  C12 OLA A1206      10.221 -20.340  -6.541  1.00 40.63           C  
HETATM 3117  C13 OLA A1206      10.362 -21.847  -6.755  1.00 40.66           C  
HETATM 3118  C14 OLA A1206       9.438 -22.618  -5.809  1.00 40.79           C  
HETATM 3119  C15 OLA A1206       9.522 -24.124  -6.045  1.00 40.79           C  
HETATM 3120  C16 OLA A1206       8.897 -24.931  -4.904  1.00 40.72           C  
HETATM 3121  C17 OLA A1206       9.425 -26.370  -4.847  1.00 40.59           C  
HETATM 3122  C18 OLA A1206       9.125 -27.178  -6.094  1.00 40.40           C  
HETATM 3123  C11 OLA A1207       6.254 -43.661  11.604  1.00 23.62           C  
HETATM 3124  C12 OLA A1207       6.531 -44.356  10.273  1.00 24.26           C  
HETATM 3125  C13 OLA A1207       7.825 -45.188  10.271  1.00 24.82           C  
HETATM 3126  C14 OLA A1207       8.077 -46.007   8.994  1.00 25.22           C  
HETATM 3127  C15 OLA A1207       7.337 -47.355   8.998  1.00 25.81           C  
HETATM 3128  C16 OLA A1207       7.541 -48.212   7.733  1.00 26.07           C  
HETATM 3129  C17 OLA A1207       6.434 -49.260   7.515  1.00 25.97           C  
HETATM 3130  OH2 1PE A1208      -5.650 -51.392   5.810  1.00 47.00           O  
HETATM 3131  C12 1PE A1208      -5.359 -52.213   4.682  1.00 47.66           C  
HETATM 3132  C22 1PE A1208      -6.461 -52.210   3.643  1.00 48.36           C  
HETATM 3133  OH3 1PE A1208      -6.173 -53.114   2.573  1.00 48.58           O  
HETATM 3134  C13 1PE A1208      -6.858 -54.214   0.546  1.00 47.71           C  
HETATM 3135  C23 1PE A1208      -7.235 -53.240   1.628  1.00 48.11           C  
HETATM 3136  O   HOH A1301      -1.349 -37.732  12.460  1.00 63.22           O  
HETATM 3137  O   HOH A1302     -11.085 -34.883  -0.110  1.00 30.92           O  
END